data_9EDO
# 
_entry.id   9EDO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9EDO         pdb_00009edo 10.2210/pdb9edo/pdb 
WWPDB D_1000290173 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-03-19 ? 
3 'Structure model' 1 2 2025-04-23 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
12 3 'Structure model' '_citation.journal_volume'          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EDO 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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              g.hansman@griffith.edu.au 
_pdbx_contact_author.name_first         Grant 
_pdbx_contact_author.name_last          Hansman 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8735-4618 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Holroyd, D.L.' 1 0009-0002-2830-6020 
'Kumar, A.'     2 0000-0001-7540-6177 
'Bruning, J.B.' 3 0000-0002-6919-1824 
'Hansman, G.S.' 4 0000-0001-8735-4618 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Virol. 
_citation.journal_id_ASTM           JOVIAM 
_citation.journal_id_CSD            0825 
_citation.journal_id_ISSN           1098-5514 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            99 
_citation.language                  ? 
_citation.page_first                e0197124 
_citation.page_last                 e0197124 
_citation.title                     'Antigenic structural analysis of bat and human norovirus protruding (P) domains.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1128/jvi.01971-24 
_citation.pdbx_database_id_PubMed   40062838 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Holroyd, D.L.'    1 0009-0002-2830-6020 
primary 'Kumar, A.'        2 0000-0001-7540-6177 
primary 'Vasquez, E.'      3 ?                   
primary 'Masic, V.'        4 ?                   
primary 'von Itzstein, M.' 5 0000-0001-6302-7524 
primary 'Bruning, J.B.'    6 0000-0002-6919-1824 
primary 'Hansman, G.S.'    7 0000-0001-8735-4618 
# 
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 VP1            34333.137 2   ? ? 'P domain' ? 
2 non-polymer syn 'CHLORIDE ION' 35.453    1   ? ? ?          ? 
3 water       nat water          18.015    931 ? ? ?          ? 
# 
_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       
;SKPFTIPILTIGEMTNSRFPVAIDMLHTSPTDNFIVQPQNGRCTLDGELQGTTQLVASNICAFRGSISGHENNGDQHQWH
FSITNPNGTPFDPTEDVPAPLGTPDFKGQLYGVISQRNREGSSGNGNQKANRSHEGVISTVAPRFTPKLGSVMIGTWTTD
DIQDQPSRFTPVGLNDDDNYKQWELPNYSGALTLNMGLAPSVFPTYPGEQLLFFRSYIPMKGGYGSPYIDCLIPQEWISH
FYQESAPSQTDVALIRYVNPDTGRVLFEAKLHRQGYITVAKTGDSPINVPANGYFRFDSWVSQFYSLAPM
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SKPFTIPILTIGEMTNSRFPVAIDMLHTSPTDNFIVQPQNGRCTLDGELQGTTQLVASNICAFRGSISGHENNGDQHQWH
FSITNPNGTPFDPTEDVPAPLGTPDFKGQLYGVISQRNREGSSGNGNQKANRSHEGVISTVAPRFTPKLGSVMIGTWTTD
DIQDQPSRFTPVGLNDDDNYKQWELPNYSGALTLNMGLAPSVFPTYPGEQLLFFRSYIPMKGGYGSPYIDCLIPQEWISH
FYQESAPSQTDVALIRYVNPDTGRVLFEAKLHRQGYITVAKTGDSPINVPANGYFRFDSWVSQFYSLAPM
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CHLORIDE ION' CL  
3 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   LYS n 
1 3   PRO n 
1 4   PHE n 
1 5   THR n 
1 6   ILE n 
1 7   PRO n 
1 8   ILE n 
1 9   LEU n 
1 10  THR n 
1 11  ILE n 
1 12  GLY n 
1 13  GLU n 
1 14  MET n 
1 15  THR n 
1 16  ASN n 
1 17  SER n 
1 18  ARG n 
1 19  PHE n 
1 20  PRO n 
1 21  VAL n 
1 22  ALA n 
1 23  ILE n 
1 24  ASP n 
1 25  MET n 
1 26  LEU n 
1 27  HIS n 
1 28  THR n 
1 29  SER n 
1 30  PRO n 
1 31  THR n 
1 32  ASP n 
1 33  ASN n 
1 34  PHE n 
1 35  ILE n 
1 36  VAL n 
1 37  GLN n 
1 38  PRO n 
1 39  GLN n 
1 40  ASN n 
1 41  GLY n 
1 42  ARG n 
1 43  CYS n 
1 44  THR n 
1 45  LEU n 
1 46  ASP n 
1 47  GLY n 
1 48  GLU n 
1 49  LEU n 
1 50  GLN n 
1 51  GLY n 
1 52  THR n 
1 53  THR n 
1 54  GLN n 
1 55  LEU n 
1 56  VAL n 
1 57  ALA n 
1 58  SER n 
1 59  ASN n 
1 60  ILE n 
1 61  CYS n 
1 62  ALA n 
1 63  PHE n 
1 64  ARG n 
1 65  GLY n 
1 66  SER n 
1 67  ILE n 
1 68  SER n 
1 69  GLY n 
1 70  HIS n 
1 71  GLU n 
1 72  ASN n 
1 73  ASN n 
1 74  GLY n 
1 75  ASP n 
1 76  GLN n 
1 77  HIS n 
1 78  GLN n 
1 79  TRP n 
1 80  HIS n 
1 81  PHE n 
1 82  SER n 
1 83  ILE n 
1 84  THR n 
1 85  ASN n 
1 86  PRO n 
1 87  ASN n 
1 88  GLY n 
1 89  THR n 
1 90  PRO n 
1 91  PHE n 
1 92  ASP n 
1 93  PRO n 
1 94  THR n 
1 95  GLU n 
1 96  ASP n 
1 97  VAL n 
1 98  PRO n 
1 99  ALA n 
1 100 PRO n 
1 101 LEU n 
1 102 GLY n 
1 103 THR n 
1 104 PRO n 
1 105 ASP n 
1 106 PHE n 
1 107 LYS n 
1 108 GLY n 
1 109 GLN n 
1 110 LEU n 
1 111 TYR n 
1 112 GLY n 
1 113 VAL n 
1 114 ILE n 
1 115 SER n 
1 116 GLN n 
1 117 ARG n 
1 118 ASN n 
1 119 ARG n 
1 120 GLU n 
1 121 GLY n 
1 122 SER n 
1 123 SER n 
1 124 GLY n 
1 125 ASN n 
1 126 GLY n 
1 127 ASN n 
1 128 GLN n 
1 129 LYS n 
1 130 ALA n 
1 131 ASN n 
1 132 ARG n 
1 133 SER n 
1 134 HIS n 
1 135 GLU n 
1 136 GLY n 
1 137 VAL n 
1 138 ILE n 
1 139 SER n 
1 140 THR n 
1 141 VAL n 
1 142 ALA n 
1 143 PRO n 
1 144 ARG n 
1 145 PHE n 
1 146 THR n 
1 147 PRO n 
1 148 LYS n 
1 149 LEU n 
1 150 GLY n 
1 151 SER n 
1 152 VAL n 
1 153 MET n 
1 154 ILE n 
1 155 GLY n 
1 156 THR n 
1 157 TRP n 
1 158 THR n 
1 159 THR n 
1 160 ASP n 
1 161 ASP n 
1 162 ILE n 
1 163 GLN n 
1 164 ASP n 
1 165 GLN n 
1 166 PRO n 
1 167 SER n 
1 168 ARG n 
1 169 PHE n 
1 170 THR n 
1 171 PRO n 
1 172 VAL n 
1 173 GLY n 
1 174 LEU n 
1 175 ASN n 
1 176 ASP n 
1 177 ASP n 
1 178 ASP n 
1 179 ASN n 
1 180 TYR n 
1 181 LYS n 
1 182 GLN n 
1 183 TRP n 
1 184 GLU n 
1 185 LEU n 
1 186 PRO n 
1 187 ASN n 
1 188 TYR n 
1 189 SER n 
1 190 GLY n 
1 191 ALA n 
1 192 LEU n 
1 193 THR n 
1 194 LEU n 
1 195 ASN n 
1 196 MET n 
1 197 GLY n 
1 198 LEU n 
1 199 ALA n 
1 200 PRO n 
1 201 SER n 
1 202 VAL n 
1 203 PHE n 
1 204 PRO n 
1 205 THR n 
1 206 TYR n 
1 207 PRO n 
1 208 GLY n 
1 209 GLU n 
1 210 GLN n 
1 211 LEU n 
1 212 LEU n 
1 213 PHE n 
1 214 PHE n 
1 215 ARG n 
1 216 SER n 
1 217 TYR n 
1 218 ILE n 
1 219 PRO n 
1 220 MET n 
1 221 LYS n 
1 222 GLY n 
1 223 GLY n 
1 224 TYR n 
1 225 GLY n 
1 226 SER n 
1 227 PRO n 
1 228 TYR n 
1 229 ILE n 
1 230 ASP n 
1 231 CYS n 
1 232 LEU n 
1 233 ILE n 
1 234 PRO n 
1 235 GLN n 
1 236 GLU n 
1 237 TRP n 
1 238 ILE n 
1 239 SER n 
1 240 HIS n 
1 241 PHE n 
1 242 TYR n 
1 243 GLN n 
1 244 GLU n 
1 245 SER n 
1 246 ALA n 
1 247 PRO n 
1 248 SER n 
1 249 GLN n 
1 250 THR n 
1 251 ASP n 
1 252 VAL n 
1 253 ALA n 
1 254 LEU n 
1 255 ILE n 
1 256 ARG n 
1 257 TYR n 
1 258 VAL n 
1 259 ASN n 
1 260 PRO n 
1 261 ASP n 
1 262 THR n 
1 263 GLY n 
1 264 ARG n 
1 265 VAL n 
1 266 LEU n 
1 267 PHE n 
1 268 GLU n 
1 269 ALA n 
1 270 LYS n 
1 271 LEU n 
1 272 HIS n 
1 273 ARG n 
1 274 GLN n 
1 275 GLY n 
1 276 TYR n 
1 277 ILE n 
1 278 THR n 
1 279 VAL n 
1 280 ALA n 
1 281 LYS n 
1 282 THR n 
1 283 GLY n 
1 284 ASP n 
1 285 SER n 
1 286 PRO n 
1 287 ILE n 
1 288 ASN n 
1 289 VAL n 
1 290 PRO n 
1 291 ALA n 
1 292 ASN n 
1 293 GLY n 
1 294 TYR n 
1 295 PHE n 
1 296 ARG n 
1 297 PHE n 
1 298 ASP n 
1 299 SER n 
1 300 TRP n 
1 301 VAL n 
1 302 SER n 
1 303 GLN n 
1 304 PHE n 
1 305 TYR n 
1 306 SER n 
1 307 LEU n 
1 308 ALA n 
1 309 PRO n 
1 310 MET 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                   310 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Norovirus GII' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     122929 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
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  
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 
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_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   SER 1   224 ?   ?   ?   A . n 
A 1 2   LYS 2   225 225 LYS LYS A . n 
A 1 3   PRO 3   226 226 PRO PRO A . n 
A 1 4   PHE 4   227 227 PHE PHE A . n 
A 1 5   THR 5   228 228 THR THR A . n 
A 1 6   ILE 6   229 229 ILE ILE A . n 
A 1 7   PRO 7   230 230 PRO PRO A . n 
A 1 8   ILE 8   231 231 ILE ILE A . n 
A 1 9   LEU 9   232 232 LEU LEU A . n 
A 1 10  THR 10  233 233 THR THR A . n 
A 1 11  ILE 11  234 234 ILE ILE A . n 
A 1 12  GLY 12  235 235 GLY GLY A . n 
A 1 13  GLU 13  236 236 GLU GLU A . n 
A 1 14  MET 14  237 237 MET MET A . n 
A 1 15  THR 15  238 238 THR THR A . n 
A 1 16  ASN 16  239 239 ASN ASN A . n 
A 1 17  SER 17  240 240 SER SER A . n 
A 1 18  ARG 18  241 241 ARG ARG A . n 
A 1 19  PHE 19  242 242 PHE PHE A . n 
A 1 20  PRO 20  243 243 PRO PRO A . n 
A 1 21  VAL 21  244 244 VAL VAL A . n 
A 1 22  ALA 22  245 245 ALA ALA A . n 
A 1 23  ILE 23  246 246 ILE ILE A . n 
A 1 24  ASP 24  247 247 ASP ASP A . n 
A 1 25  MET 25  248 248 MET MET A . n 
A 1 26  LEU 26  249 249 LEU LEU A . n 
A 1 27  HIS 27  250 250 HIS HIS A . n 
A 1 28  THR 28  251 251 THR THR A . n 
A 1 29  SER 29  252 252 SER SER A . n 
A 1 30  PRO 30  253 253 PRO PRO A . n 
A 1 31  THR 31  254 254 THR THR A . n 
A 1 32  ASP 32  255 255 ASP ASP A . n 
A 1 33  ASN 33  256 256 ASN ASN A . n 
A 1 34  PHE 34  257 257 PHE PHE A . n 
A 1 35  ILE 35  258 258 ILE ILE A . n 
A 1 36  VAL 36  259 259 VAL VAL A . n 
A 1 37  GLN 37  260 260 GLN GLN A . n 
A 1 38  PRO 38  261 261 PRO PRO A . n 
A 1 39  GLN 39  262 262 GLN GLN A . n 
A 1 40  ASN 40  263 263 ASN ASN A . n 
A 1 41  GLY 41  264 264 GLY GLY A . n 
A 1 42  ARG 42  265 265 ARG ARG A . n 
A 1 43  CYS 43  266 266 CYS CYS A . n 
A 1 44  THR 44  267 267 THR THR A . n 
A 1 45  LEU 45  268 268 LEU LEU A . n 
A 1 46  ASP 46  269 269 ASP ASP A . n 
A 1 47  GLY 47  270 270 GLY GLY A . n 
A 1 48  GLU 48  271 271 GLU GLU A . n 
A 1 49  LEU 49  272 272 LEU LEU A . n 
A 1 50  GLN 50  273 273 GLN GLN A . n 
A 1 51  GLY 51  274 274 GLY GLY A . n 
A 1 52  THR 52  275 275 THR THR A . n 
A 1 53  THR 53  276 276 THR THR A . n 
A 1 54  GLN 54  277 277 GLN GLN A . n 
A 1 55  LEU 55  278 278 LEU LEU A . n 
A 1 56  VAL 56  279 279 VAL VAL A . n 
A 1 57  ALA 57  280 280 ALA ALA A . n 
A 1 58  SER 58  281 281 SER SER A . n 
A 1 59  ASN 59  282 282 ASN ASN A . n 
A 1 60  ILE 60  283 283 ILE ILE A . n 
A 1 61  CYS 61  284 284 CYS CYS A . n 
A 1 62  ALA 62  285 285 ALA ALA A . n 
A 1 63  PHE 63  286 286 PHE PHE A . n 
A 1 64  ARG 64  287 287 ARG ARG A . n 
A 1 65  GLY 65  288 288 GLY GLY A . n 
A 1 66  SER 66  289 289 SER SER A . n 
A 1 67  ILE 67  290 290 ILE ILE A . n 
A 1 68  SER 68  291 291 SER SER A . n 
A 1 69  GLY 69  292 292 GLY GLY A . n 
A 1 70  HIS 70  293 293 HIS HIS A . n 
A 1 71  GLU 71  294 294 GLU GLU A . n 
A 1 72  ASN 72  295 295 ASN ASN A . n 
A 1 73  ASN 73  296 296 ASN ASN A . n 
A 1 74  GLY 74  297 297 GLY GLY A . n 
A 1 75  ASP 75  298 298 ASP ASP A . n 
A 1 76  GLN 76  299 299 GLN GLN A . n 
A 1 77  HIS 77  300 300 HIS HIS A . n 
A 1 78  GLN 78  301 301 GLN GLN A . n 
A 1 79  TRP 79  302 302 TRP TRP A . n 
A 1 80  HIS 80  303 303 HIS HIS A . n 
A 1 81  PHE 81  304 304 PHE PHE A . n 
A 1 82  SER 82  305 305 SER SER A . n 
A 1 83  ILE 83  306 306 ILE ILE A . n 
A 1 84  THR 84  307 307 THR THR A . n 
A 1 85  ASN 85  308 308 ASN ASN A . n 
A 1 86  PRO 86  309 309 PRO PRO A . n 
A 1 87  ASN 87  310 310 ASN ASN A . n 
A 1 88  GLY 88  311 311 GLY GLY A . n 
A 1 89  THR 89  312 312 THR THR A . n 
A 1 90  PRO 90  313 313 PRO PRO A . n 
A 1 91  PHE 91  314 314 PHE PHE A . n 
A 1 92  ASP 92  315 315 ASP ASP A . n 
A 1 93  PRO 93  316 316 PRO PRO A . n 
A 1 94  THR 94  317 317 THR THR A . n 
A 1 95  GLU 95  318 318 GLU GLU A . n 
A 1 96  ASP 96  319 319 ASP ASP A . n 
A 1 97  VAL 97  320 320 VAL VAL A . n 
A 1 98  PRO 98  321 321 PRO PRO A . n 
A 1 99  ALA 99  322 322 ALA ALA A . n 
A 1 100 PRO 100 323 323 PRO PRO A . n 
A 1 101 LEU 101 324 324 LEU LEU A . n 
A 1 102 GLY 102 325 325 GLY GLY A . n 
A 1 103 THR 103 326 326 THR THR A . n 
A 1 104 PRO 104 327 327 PRO PRO A . n 
A 1 105 ASP 105 328 328 ASP ASP A . n 
A 1 106 PHE 106 329 329 PHE PHE A . n 
A 1 107 LYS 107 330 330 LYS LYS A . n 
A 1 108 GLY 108 331 331 GLY GLY A . n 
A 1 109 GLN 109 332 332 GLN GLN A . n 
A 1 110 LEU 110 333 333 LEU LEU A . n 
A 1 111 TYR 111 334 334 TYR TYR A . n 
A 1 112 GLY 112 335 335 GLY GLY A . n 
A 1 113 VAL 113 336 336 VAL VAL A . n 
A 1 114 ILE 114 337 337 ILE ILE A . n 
A 1 115 SER 115 338 338 SER SER A . n 
A 1 116 GLN 116 339 339 GLN GLN A . n 
A 1 117 ARG 117 340 340 ARG ARG A . n 
A 1 118 ASN 118 341 341 ASN ASN A . n 
A 1 119 ARG 119 342 342 ARG ARG A . n 
A 1 120 GLU 120 343 343 GLU GLU A . n 
A 1 121 GLY 121 344 344 GLY GLY A . n 
A 1 122 SER 122 345 345 SER SER A . n 
A 1 123 SER 123 346 346 SER SER A . n 
A 1 124 GLY 124 347 347 GLY GLY A . n 
A 1 125 ASN 125 348 348 ASN ASN A . n 
A 1 126 GLY 126 349 349 GLY GLY A . n 
A 1 127 ASN 127 350 350 ASN ASN A . n 
A 1 128 GLN 128 351 351 GLN GLN A . n 
A 1 129 LYS 129 352 352 LYS LYS A . n 
A 1 130 ALA 130 353 353 ALA ALA A . n 
A 1 131 ASN 131 354 354 ASN ASN A . n 
A 1 132 ARG 132 355 355 ARG ARG A . n 
A 1 133 SER 133 356 356 SER SER A . n 
A 1 134 HIS 134 357 357 HIS HIS A . n 
A 1 135 GLU 135 358 358 GLU GLU A . n 
A 1 136 GLY 136 359 359 GLY GLY A . n 
A 1 137 VAL 137 360 360 VAL VAL A . n 
A 1 138 ILE 138 361 361 ILE ILE A . n 
A 1 139 SER 139 362 362 SER SER A . n 
A 1 140 THR 140 363 363 THR THR A . n 
A 1 141 VAL 141 364 364 VAL VAL A . n 
A 1 142 ALA 142 365 365 ALA ALA A . n 
A 1 143 PRO 143 366 366 PRO PRO A . n 
A 1 144 ARG 144 367 367 ARG ARG A . n 
A 1 145 PHE 145 368 368 PHE PHE A . n 
A 1 146 THR 146 369 369 THR THR A . n 
A 1 147 PRO 147 370 370 PRO PRO A . n 
A 1 148 LYS 148 371 371 LYS LYS A . n 
A 1 149 LEU 149 372 372 LEU LEU A . n 
A 1 150 GLY 150 373 373 GLY GLY A . n 
A 1 151 SER 151 374 374 SER SER A . n 
A 1 152 VAL 152 375 375 VAL VAL A . n 
A 1 153 MET 153 376 376 MET MET A . n 
A 1 154 ILE 154 377 377 ILE ILE A . n 
A 1 155 GLY 155 378 378 GLY GLY A . n 
A 1 156 THR 156 379 379 THR THR A . n 
A 1 157 TRP 157 380 380 TRP TRP A . n 
A 1 158 THR 158 381 381 THR THR A . n 
A 1 159 THR 159 382 382 THR THR A . n 
A 1 160 ASP 160 383 383 ASP ASP A . n 
A 1 161 ASP 161 384 384 ASP ASP A . n 
A 1 162 ILE 162 385 385 ILE ILE A . n 
A 1 163 GLN 163 386 386 GLN GLN A . n 
A 1 164 ASP 164 387 387 ASP ASP A . n 
A 1 165 GLN 165 388 388 GLN GLN A . n 
A 1 166 PRO 166 389 389 PRO PRO A . n 
A 1 167 SER 167 390 390 SER SER A . n 
A 1 168 ARG 168 391 391 ARG ARG A . n 
A 1 169 PHE 169 392 392 PHE PHE A . n 
A 1 170 THR 170 393 393 THR THR A . n 
A 1 171 PRO 171 394 394 PRO PRO A . n 
A 1 172 VAL 172 395 395 VAL VAL A . n 
A 1 173 GLY 173 396 396 GLY GLY A . n 
A 1 174 LEU 174 397 397 LEU LEU A . n 
A 1 175 ASN 175 398 398 ASN ASN A . n 
A 1 176 ASP 176 399 399 ASP ASP A . n 
A 1 177 ASP 177 400 400 ASP ASP A . n 
A 1 178 ASP 178 401 401 ASP ASP A . n 
A 1 179 ASN 179 402 402 ASN ASN A . n 
A 1 180 TYR 180 403 403 TYR TYR A . n 
A 1 181 LYS 181 404 404 LYS LYS A . n 
A 1 182 GLN 182 405 405 GLN GLN A . n 
A 1 183 TRP 183 406 406 TRP TRP A . n 
A 1 184 GLU 184 407 407 GLU GLU A . n 
A 1 185 LEU 185 408 408 LEU LEU A . n 
A 1 186 PRO 186 409 409 PRO PRO A . n 
A 1 187 ASN 187 410 410 ASN ASN A . n 
A 1 188 TYR 188 411 411 TYR TYR A . n 
A 1 189 SER 189 412 412 SER SER A . n 
A 1 190 GLY 190 413 413 GLY GLY A . n 
A 1 191 ALA 191 414 414 ALA ALA A . n 
A 1 192 LEU 192 415 ?   ?   ?   A . n 
A 1 193 THR 193 416 416 THR THR A . n 
A 1 194 LEU 194 417 417 LEU LEU A . n 
A 1 195 ASN 195 418 418 ASN ASN A . n 
A 1 196 MET 196 419 419 MET MET A . n 
A 1 197 GLY 197 420 420 GLY GLY A . n 
A 1 198 LEU 198 421 421 LEU LEU A . n 
A 1 199 ALA 199 422 422 ALA ALA A . n 
A 1 200 PRO 200 423 423 PRO PRO A . n 
A 1 201 SER 201 424 424 SER SER A . n 
A 1 202 VAL 202 425 425 VAL VAL A . n 
A 1 203 PHE 203 426 426 PHE PHE A . n 
A 1 204 PRO 204 427 427 PRO PRO A . n 
A 1 205 THR 205 428 428 THR THR A . n 
A 1 206 TYR 206 429 429 TYR TYR A . n 
A 1 207 PRO 207 430 430 PRO PRO A . n 
A 1 208 GLY 208 431 431 GLY GLY A . n 
A 1 209 GLU 209 432 432 GLU GLU A . n 
A 1 210 GLN 210 433 433 GLN GLN A . n 
A 1 211 LEU 211 434 434 LEU LEU A . n 
A 1 212 LEU 212 435 435 LEU LEU A . n 
A 1 213 PHE 213 436 436 PHE PHE A . n 
A 1 214 PHE 214 437 437 PHE PHE A . n 
A 1 215 ARG 215 438 438 ARG ARG A . n 
A 1 216 SER 216 439 439 SER SER A . n 
A 1 217 TYR 217 440 440 TYR TYR A . n 
A 1 218 ILE 218 441 441 ILE ILE A . n 
A 1 219 PRO 219 442 442 PRO PRO A . n 
A 1 220 MET 220 443 443 MET MET A . n 
A 1 221 LYS 221 444 444 LYS LYS A . n 
A 1 222 GLY 222 445 445 GLY GLY A . n 
A 1 223 GLY 223 446 446 GLY GLY A . n 
A 1 224 TYR 224 447 447 TYR TYR A . n 
A 1 225 GLY 225 448 448 GLY GLY A . n 
A 1 226 SER 226 449 449 SER SER A . n 
A 1 227 PRO 227 450 450 PRO PRO A . n 
A 1 228 TYR 228 451 451 TYR TYR A . n 
A 1 229 ILE 229 452 452 ILE ILE A . n 
A 1 230 ASP 230 453 453 ASP ASP A . n 
A 1 231 CYS 231 454 454 CYS CYS A . n 
A 1 232 LEU 232 455 455 LEU LEU A . n 
A 1 233 ILE 233 456 456 ILE ILE A . n 
A 1 234 PRO 234 457 457 PRO PRO A . n 
A 1 235 GLN 235 458 458 GLN GLN A . n 
A 1 236 GLU 236 459 459 GLU GLU A . n 
A 1 237 TRP 237 460 460 TRP TRP A . n 
A 1 238 ILE 238 461 461 ILE ILE A . n 
A 1 239 SER 239 462 462 SER SER A . n 
A 1 240 HIS 240 463 463 HIS HIS A . n 
A 1 241 PHE 241 464 464 PHE PHE A . n 
A 1 242 TYR 242 465 465 TYR TYR A . n 
A 1 243 GLN 243 466 466 GLN GLN A . n 
A 1 244 GLU 244 467 467 GLU GLU A . n 
A 1 245 SER 245 468 468 SER SER A . n 
A 1 246 ALA 246 469 469 ALA ALA A . n 
A 1 247 PRO 247 470 470 PRO PRO A . n 
A 1 248 SER 248 471 471 SER SER A . n 
A 1 249 GLN 249 472 472 GLN GLN A . n 
A 1 250 THR 250 473 473 THR THR A . n 
A 1 251 ASP 251 474 474 ASP ASP A . n 
A 1 252 VAL 252 475 475 VAL VAL A . n 
A 1 253 ALA 253 476 476 ALA ALA A . n 
A 1 254 LEU 254 477 477 LEU LEU A . n 
A 1 255 ILE 255 478 478 ILE ILE A . n 
A 1 256 ARG 256 479 479 ARG ARG A . n 
A 1 257 TYR 257 480 480 TYR TYR A . n 
A 1 258 VAL 258 481 481 VAL VAL A . n 
A 1 259 ASN 259 482 482 ASN ASN A . n 
A 1 260 PRO 260 483 483 PRO PRO A . n 
A 1 261 ASP 261 484 484 ASP ASP A . n 
A 1 262 THR 262 485 485 THR THR A . n 
A 1 263 GLY 263 486 486 GLY GLY A . n 
A 1 264 ARG 264 487 487 ARG ARG A . n 
A 1 265 VAL 265 488 488 VAL VAL A . n 
A 1 266 LEU 266 489 489 LEU LEU A . n 
A 1 267 PHE 267 490 490 PHE PHE A . n 
A 1 268 GLU 268 491 491 GLU GLU A . n 
A 1 269 ALA 269 492 492 ALA ALA A . n 
A 1 270 LYS 270 493 493 LYS LYS A . n 
A 1 271 LEU 271 494 494 LEU LEU A . n 
A 1 272 HIS 272 495 495 HIS HIS A . n 
A 1 273 ARG 273 496 496 ARG ARG A . n 
A 1 274 GLN 274 497 497 GLN GLN A . n 
A 1 275 GLY 275 498 498 GLY GLY A . n 
A 1 276 TYR 276 499 499 TYR TYR A . n 
A 1 277 ILE 277 500 500 ILE ILE A . n 
A 1 278 THR 278 501 501 THR THR A . n 
A 1 279 VAL 279 502 502 VAL VAL A . n 
A 1 280 ALA 280 503 503 ALA ALA A . n 
A 1 281 LYS 281 504 504 LYS LYS A . n 
A 1 282 THR 282 505 505 THR THR A . n 
A 1 283 GLY 283 506 506 GLY GLY A . n 
A 1 284 ASP 284 507 507 ASP ASP A . n 
A 1 285 SER 285 508 508 SER SER A . n 
A 1 286 PRO 286 509 509 PRO PRO A . n 
A 1 287 ILE 287 510 510 ILE ILE A . n 
A 1 288 ASN 288 511 511 ASN ASN A . n 
A 1 289 VAL 289 512 512 VAL VAL A . n 
A 1 290 PRO 290 513 513 PRO PRO A . n 
A 1 291 ALA 291 514 514 ALA ALA A . n 
A 1 292 ASN 292 515 515 ASN ASN A . n 
A 1 293 GLY 293 516 516 GLY GLY A . n 
A 1 294 TYR 294 517 517 TYR TYR A . n 
A 1 295 PHE 295 518 518 PHE PHE A . n 
A 1 296 ARG 296 519 519 ARG ARG A . n 
A 1 297 PHE 297 520 520 PHE PHE A . n 
A 1 298 ASP 298 521 521 ASP ASP A . n 
A 1 299 SER 299 522 522 SER SER A . n 
A 1 300 TRP 300 523 523 TRP TRP A . n 
A 1 301 VAL 301 524 524 VAL VAL A . n 
A 1 302 SER 302 525 525 SER SER A . n 
A 1 303 GLN 303 526 526 GLN GLN A . n 
A 1 304 PHE 304 527 527 PHE PHE A . n 
A 1 305 TYR 305 528 528 TYR TYR A . n 
A 1 306 SER 306 529 529 SER SER A . n 
A 1 307 LEU 307 530 530 LEU LEU A . n 
A 1 308 ALA 308 531 531 ALA ALA A . n 
A 1 309 PRO 309 532 532 PRO PRO A . n 
A 1 310 MET 310 533 533 MET MET A . n 
B 1 1   SER 1   224 224 SER SER B . n 
B 1 2   LYS 2   225 225 LYS LYS B . n 
B 1 3   PRO 3   226 226 PRO PRO B . n 
B 1 4   PHE 4   227 227 PHE PHE B . n 
B 1 5   THR 5   228 228 THR THR B . n 
B 1 6   ILE 6   229 229 ILE ILE B . n 
B 1 7   PRO 7   230 230 PRO PRO B . n 
B 1 8   ILE 8   231 231 ILE ILE B . n 
B 1 9   LEU 9   232 232 LEU LEU B . n 
B 1 10  THR 10  233 233 THR THR B . n 
B 1 11  ILE 11  234 234 ILE ILE B . n 
B 1 12  GLY 12  235 235 GLY GLY B . n 
B 1 13  GLU 13  236 236 GLU GLU B . n 
B 1 14  MET 14  237 237 MET MET B . n 
B 1 15  THR 15  238 238 THR THR B . n 
B 1 16  ASN 16  239 239 ASN ASN B . n 
B 1 17  SER 17  240 240 SER SER B . n 
B 1 18  ARG 18  241 241 ARG ARG B . n 
B 1 19  PHE 19  242 242 PHE PHE B . n 
B 1 20  PRO 20  243 243 PRO PRO B . n 
B 1 21  VAL 21  244 244 VAL VAL B . n 
B 1 22  ALA 22  245 245 ALA ALA B . n 
B 1 23  ILE 23  246 246 ILE ILE B . n 
B 1 24  ASP 24  247 247 ASP ASP B . n 
B 1 25  MET 25  248 248 MET MET B . n 
B 1 26  LEU 26  249 249 LEU LEU B . n 
B 1 27  HIS 27  250 250 HIS HIS B . n 
B 1 28  THR 28  251 251 THR THR B . n 
B 1 29  SER 29  252 252 SER SER B . n 
B 1 30  PRO 30  253 253 PRO PRO B . n 
B 1 31  THR 31  254 254 THR THR B . n 
B 1 32  ASP 32  255 255 ASP ASP B . n 
B 1 33  ASN 33  256 256 ASN ASN B . n 
B 1 34  PHE 34  257 257 PHE PHE B . n 
B 1 35  ILE 35  258 258 ILE ILE B . n 
B 1 36  VAL 36  259 259 VAL VAL B . n 
B 1 37  GLN 37  260 260 GLN GLN B . n 
B 1 38  PRO 38  261 261 PRO PRO B . n 
B 1 39  GLN 39  262 262 GLN GLN B . n 
B 1 40  ASN 40  263 263 ASN ASN B . n 
B 1 41  GLY 41  264 264 GLY GLY B . n 
B 1 42  ARG 42  265 265 ARG ARG B . n 
B 1 43  CYS 43  266 266 CYS CYS B . n 
B 1 44  THR 44  267 267 THR THR B . n 
B 1 45  LEU 45  268 268 LEU LEU B . n 
B 1 46  ASP 46  269 269 ASP ASP B . n 
B 1 47  GLY 47  270 270 GLY GLY B . n 
B 1 48  GLU 48  271 271 GLU GLU B . n 
B 1 49  LEU 49  272 272 LEU LEU B . n 
B 1 50  GLN 50  273 273 GLN GLN B . n 
B 1 51  GLY 51  274 274 GLY GLY B . n 
B 1 52  THR 52  275 275 THR THR B . n 
B 1 53  THR 53  276 276 THR THR B . n 
B 1 54  GLN 54  277 277 GLN GLN B . n 
B 1 55  LEU 55  278 278 LEU LEU B . n 
B 1 56  VAL 56  279 279 VAL VAL B . n 
B 1 57  ALA 57  280 280 ALA ALA B . n 
B 1 58  SER 58  281 281 SER SER B . n 
B 1 59  ASN 59  282 282 ASN ASN B . n 
B 1 60  ILE 60  283 283 ILE ILE B . n 
B 1 61  CYS 61  284 284 CYS CYS B . n 
B 1 62  ALA 62  285 285 ALA ALA B . n 
B 1 63  PHE 63  286 286 PHE PHE B . n 
B 1 64  ARG 64  287 287 ARG ARG B . n 
B 1 65  GLY 65  288 288 GLY GLY B . n 
B 1 66  SER 66  289 289 SER SER B . n 
B 1 67  ILE 67  290 290 ILE ILE B . n 
B 1 68  SER 68  291 291 SER SER B . n 
B 1 69  GLY 69  292 292 GLY GLY B . n 
B 1 70  HIS 70  293 293 HIS HIS B . n 
B 1 71  GLU 71  294 294 GLU GLU B . n 
B 1 72  ASN 72  295 295 ASN ASN B . n 
B 1 73  ASN 73  296 296 ASN ASN B . n 
B 1 74  GLY 74  297 297 GLY GLY B . n 
B 1 75  ASP 75  298 298 ASP ASP B . n 
B 1 76  GLN 76  299 299 GLN GLN B . n 
B 1 77  HIS 77  300 300 HIS HIS B . n 
B 1 78  GLN 78  301 301 GLN GLN B . n 
B 1 79  TRP 79  302 302 TRP TRP B . n 
B 1 80  HIS 80  303 303 HIS HIS B . n 
B 1 81  PHE 81  304 304 PHE PHE B . n 
B 1 82  SER 82  305 305 SER SER B . n 
B 1 83  ILE 83  306 306 ILE ILE B . n 
B 1 84  THR 84  307 307 THR THR B . n 
B 1 85  ASN 85  308 308 ASN ASN B . n 
B 1 86  PRO 86  309 309 PRO PRO B . n 
B 1 87  ASN 87  310 310 ASN ASN B . n 
B 1 88  GLY 88  311 311 GLY GLY B . n 
B 1 89  THR 89  312 312 THR THR B . n 
B 1 90  PRO 90  313 313 PRO PRO B . n 
B 1 91  PHE 91  314 314 PHE PHE B . n 
B 1 92  ASP 92  315 315 ASP ASP B . n 
B 1 93  PRO 93  316 316 PRO PRO B . n 
B 1 94  THR 94  317 317 THR THR B . n 
B 1 95  GLU 95  318 318 GLU GLU B . n 
B 1 96  ASP 96  319 319 ASP ASP B . n 
B 1 97  VAL 97  320 320 VAL VAL B . n 
B 1 98  PRO 98  321 321 PRO PRO B . n 
B 1 99  ALA 99  322 322 ALA ALA B . n 
B 1 100 PRO 100 323 323 PRO PRO B . n 
B 1 101 LEU 101 324 324 LEU LEU B . n 
B 1 102 GLY 102 325 325 GLY GLY B . n 
B 1 103 THR 103 326 326 THR THR B . n 
B 1 104 PRO 104 327 327 PRO PRO B . n 
B 1 105 ASP 105 328 328 ASP ASP B . n 
B 1 106 PHE 106 329 329 PHE PHE B . n 
B 1 107 LYS 107 330 330 LYS LYS B . n 
B 1 108 GLY 108 331 331 GLY GLY B . n 
B 1 109 GLN 109 332 332 GLN GLN B . n 
B 1 110 LEU 110 333 333 LEU LEU B . n 
B 1 111 TYR 111 334 334 TYR TYR B . n 
B 1 112 GLY 112 335 335 GLY GLY B . n 
B 1 113 VAL 113 336 336 VAL VAL B . n 
B 1 114 ILE 114 337 337 ILE ILE B . n 
B 1 115 SER 115 338 338 SER SER B . n 
B 1 116 GLN 116 339 339 GLN GLN B . n 
B 1 117 ARG 117 340 340 ARG ARG B . n 
B 1 118 ASN 118 341 341 ASN ASN B . n 
B 1 119 ARG 119 342 342 ARG ARG B . n 
B 1 120 GLU 120 343 343 GLU GLU B . n 
B 1 121 GLY 121 344 344 GLY GLY B . n 
B 1 122 SER 122 345 345 SER SER B . n 
B 1 123 SER 123 346 346 SER SER B . n 
B 1 124 GLY 124 347 ?   ?   ?   B . n 
B 1 125 ASN 125 348 ?   ?   ?   B . n 
B 1 126 GLY 126 349 ?   ?   ?   B . n 
B 1 127 ASN 127 350 350 ASN ASN B . n 
B 1 128 GLN 128 351 351 GLN GLN B . n 
B 1 129 LYS 129 352 352 LYS LYS B . n 
B 1 130 ALA 130 353 353 ALA ALA B . n 
B 1 131 ASN 131 354 354 ASN ASN B . n 
B 1 132 ARG 132 355 355 ARG ARG B . n 
B 1 133 SER 133 356 356 SER SER B . n 
B 1 134 HIS 134 357 357 HIS HIS B . n 
B 1 135 GLU 135 358 358 GLU GLU B . n 
B 1 136 GLY 136 359 359 GLY GLY B . n 
B 1 137 VAL 137 360 360 VAL VAL B . n 
B 1 138 ILE 138 361 361 ILE ILE B . n 
B 1 139 SER 139 362 362 SER SER B . n 
B 1 140 THR 140 363 363 THR THR B . n 
B 1 141 VAL 141 364 364 VAL VAL B . n 
B 1 142 ALA 142 365 365 ALA ALA B . n 
B 1 143 PRO 143 366 366 PRO PRO B . n 
B 1 144 ARG 144 367 367 ARG ARG B . n 
B 1 145 PHE 145 368 368 PHE PHE B . n 
B 1 146 THR 146 369 369 THR THR B . n 
B 1 147 PRO 147 370 370 PRO PRO B . n 
B 1 148 LYS 148 371 371 LYS LYS B . n 
B 1 149 LEU 149 372 372 LEU LEU B . n 
B 1 150 GLY 150 373 373 GLY GLY B . n 
B 1 151 SER 151 374 374 SER SER B . n 
B 1 152 VAL 152 375 375 VAL VAL B . n 
B 1 153 MET 153 376 376 MET MET B . n 
B 1 154 ILE 154 377 377 ILE ILE B . n 
B 1 155 GLY 155 378 378 GLY GLY B . n 
B 1 156 THR 156 379 379 THR THR B . n 
B 1 157 TRP 157 380 380 TRP TRP B . n 
B 1 158 THR 158 381 381 THR THR B . n 
B 1 159 THR 159 382 382 THR THR B . n 
B 1 160 ASP 160 383 383 ASP ASP B . n 
B 1 161 ASP 161 384 384 ASP ASP B . n 
B 1 162 ILE 162 385 385 ILE ILE B . n 
B 1 163 GLN 163 386 386 GLN GLN B . n 
B 1 164 ASP 164 387 387 ASP ASP B . n 
B 1 165 GLN 165 388 388 GLN GLN B . n 
B 1 166 PRO 166 389 389 PRO PRO B . n 
B 1 167 SER 167 390 390 SER SER B . n 
B 1 168 ARG 168 391 391 ARG ARG B . n 
B 1 169 PHE 169 392 392 PHE PHE B . n 
B 1 170 THR 170 393 393 THR THR B . n 
B 1 171 PRO 171 394 394 PRO PRO B . n 
B 1 172 VAL 172 395 395 VAL VAL B . n 
B 1 173 GLY 173 396 396 GLY GLY B . n 
B 1 174 LEU 174 397 397 LEU LEU B . n 
B 1 175 ASN 175 398 398 ASN ASN B . n 
B 1 176 ASP 176 399 399 ASP ASP B . n 
B 1 177 ASP 177 400 400 ASP ASP B . n 
B 1 178 ASP 178 401 401 ASP ASP B . n 
B 1 179 ASN 179 402 402 ASN ASN B . n 
B 1 180 TYR 180 403 403 TYR TYR B . n 
B 1 181 LYS 181 404 404 LYS LYS B . n 
B 1 182 GLN 182 405 405 GLN GLN B . n 
B 1 183 TRP 183 406 406 TRP TRP B . n 
B 1 184 GLU 184 407 407 GLU GLU B . n 
B 1 185 LEU 185 408 408 LEU LEU B . n 
B 1 186 PRO 186 409 409 PRO PRO B . n 
B 1 187 ASN 187 410 410 ASN ASN B . n 
B 1 188 TYR 188 411 411 TYR TYR B . n 
B 1 189 SER 189 412 412 SER SER B . n 
B 1 190 GLY 190 413 413 GLY GLY B . n 
B 1 191 ALA 191 414 414 ALA ALA B . n 
B 1 192 LEU 192 415 415 LEU LEU B . n 
B 1 193 THR 193 416 416 THR THR B . n 
B 1 194 LEU 194 417 417 LEU LEU B . n 
B 1 195 ASN 195 418 418 ASN ASN B . n 
B 1 196 MET 196 419 419 MET MET B . n 
B 1 197 GLY 197 420 420 GLY GLY B . n 
B 1 198 LEU 198 421 421 LEU LEU B . n 
B 1 199 ALA 199 422 422 ALA ALA B . n 
B 1 200 PRO 200 423 423 PRO PRO B . n 
B 1 201 SER 201 424 424 SER SER B . n 
B 1 202 VAL 202 425 425 VAL VAL B . n 
B 1 203 PHE 203 426 426 PHE PHE B . n 
B 1 204 PRO 204 427 427 PRO PRO B . n 
B 1 205 THR 205 428 428 THR THR B . n 
B 1 206 TYR 206 429 429 TYR TYR B . n 
B 1 207 PRO 207 430 430 PRO PRO B . n 
B 1 208 GLY 208 431 431 GLY GLY B . n 
B 1 209 GLU 209 432 432 GLU GLU B . n 
B 1 210 GLN 210 433 433 GLN GLN B . n 
B 1 211 LEU 211 434 434 LEU LEU B . n 
B 1 212 LEU 212 435 435 LEU LEU B . n 
B 1 213 PHE 213 436 436 PHE PHE B . n 
B 1 214 PHE 214 437 437 PHE PHE B . n 
B 1 215 ARG 215 438 438 ARG ARG B . n 
B 1 216 SER 216 439 439 SER SER B . n 
B 1 217 TYR 217 440 440 TYR TYR B . n 
B 1 218 ILE 218 441 441 ILE ILE B . n 
B 1 219 PRO 219 442 442 PRO PRO B . n 
B 1 220 MET 220 443 443 MET MET B . n 
B 1 221 LYS 221 444 444 LYS LYS B . n 
B 1 222 GLY 222 445 445 GLY GLY B . n 
B 1 223 GLY 223 446 446 GLY GLY B . n 
B 1 224 TYR 224 447 447 TYR TYR B . n 
B 1 225 GLY 225 448 448 GLY GLY B . n 
B 1 226 SER 226 449 449 SER SER B . n 
B 1 227 PRO 227 450 450 PRO PRO B . n 
B 1 228 TYR 228 451 451 TYR TYR B . n 
B 1 229 ILE 229 452 452 ILE ILE B . n 
B 1 230 ASP 230 453 453 ASP ASP B . n 
B 1 231 CYS 231 454 454 CYS CYS B . n 
B 1 232 LEU 232 455 455 LEU LEU B . n 
B 1 233 ILE 233 456 456 ILE ILE B . n 
B 1 234 PRO 234 457 457 PRO PRO B . n 
B 1 235 GLN 235 458 458 GLN GLN B . n 
B 1 236 GLU 236 459 459 GLU GLU B . n 
B 1 237 TRP 237 460 460 TRP TRP B . n 
B 1 238 ILE 238 461 461 ILE ILE B . n 
B 1 239 SER 239 462 462 SER SER B . n 
B 1 240 HIS 240 463 463 HIS HIS B . n 
B 1 241 PHE 241 464 464 PHE PHE B . n 
B 1 242 TYR 242 465 465 TYR TYR B . n 
B 1 243 GLN 243 466 466 GLN GLN B . n 
B 1 244 GLU 244 467 467 GLU GLU B . n 
B 1 245 SER 245 468 468 SER SER B . n 
B 1 246 ALA 246 469 469 ALA ALA B . n 
B 1 247 PRO 247 470 470 PRO PRO B . n 
B 1 248 SER 248 471 471 SER SER B . n 
B 1 249 GLN 249 472 472 GLN GLN B . n 
B 1 250 THR 250 473 473 THR THR B . n 
B 1 251 ASP 251 474 474 ASP ASP B . n 
B 1 252 VAL 252 475 475 VAL VAL B . n 
B 1 253 ALA 253 476 476 ALA ALA B . n 
B 1 254 LEU 254 477 477 LEU LEU B . n 
B 1 255 ILE 255 478 478 ILE ILE B . n 
B 1 256 ARG 256 479 479 ARG ARG B . n 
B 1 257 TYR 257 480 480 TYR TYR B . n 
B 1 258 VAL 258 481 481 VAL VAL B . n 
B 1 259 ASN 259 482 482 ASN ASN B . n 
B 1 260 PRO 260 483 483 PRO PRO B . n 
B 1 261 ASP 261 484 484 ASP ASP B . n 
B 1 262 THR 262 485 485 THR THR B . n 
B 1 263 GLY 263 486 486 GLY GLY B . n 
B 1 264 ARG 264 487 487 ARG ARG B . n 
B 1 265 VAL 265 488 488 VAL VAL B . n 
B 1 266 LEU 266 489 489 LEU LEU B . n 
B 1 267 PHE 267 490 490 PHE PHE B . n 
B 1 268 GLU 268 491 491 GLU GLU B . n 
B 1 269 ALA 269 492 492 ALA ALA B . n 
B 1 270 LYS 270 493 493 LYS LYS B . n 
B 1 271 LEU 271 494 494 LEU LEU B . n 
B 1 272 HIS 272 495 495 HIS HIS B . n 
B 1 273 ARG 273 496 496 ARG ARG B . n 
B 1 274 GLN 274 497 497 GLN GLN B . n 
B 1 275 GLY 275 498 498 GLY GLY B . n 
B 1 276 TYR 276 499 499 TYR TYR B . n 
B 1 277 ILE 277 500 500 ILE ILE B . n 
B 1 278 THR 278 501 501 THR THR B . n 
B 1 279 VAL 279 502 502 VAL VAL B . n 
B 1 280 ALA 280 503 503 ALA ALA B . n 
B 1 281 LYS 281 504 504 LYS LYS B . n 
B 1 282 THR 282 505 505 THR THR B . n 
B 1 283 GLY 283 506 506 GLY GLY B . n 
B 1 284 ASP 284 507 507 ASP ASP B . n 
B 1 285 SER 285 508 508 SER SER B . n 
B 1 286 PRO 286 509 509 PRO PRO B . n 
B 1 287 ILE 287 510 510 ILE ILE B . n 
B 1 288 ASN 288 511 511 ASN ASN B . n 
B 1 289 VAL 289 512 512 VAL VAL B . n 
B 1 290 PRO 290 513 513 PRO PRO B . n 
B 1 291 ALA 291 514 514 ALA ALA B . n 
B 1 292 ASN 292 515 515 ASN ASN B . n 
B 1 293 GLY 293 516 516 GLY GLY B . n 
B 1 294 TYR 294 517 517 TYR TYR B . n 
B 1 295 PHE 295 518 518 PHE PHE B . n 
B 1 296 ARG 296 519 519 ARG ARG B . n 
B 1 297 PHE 297 520 520 PHE PHE B . n 
B 1 298 ASP 298 521 521 ASP ASP B . n 
B 1 299 SER 299 522 522 SER SER B . n 
B 1 300 TRP 300 523 523 TRP TRP B . n 
B 1 301 VAL 301 524 524 VAL VAL B . n 
B 1 302 SER 302 525 525 SER SER B . n 
B 1 303 GLN 303 526 526 GLN GLN B . n 
B 1 304 PHE 304 527 527 PHE PHE B . n 
B 1 305 TYR 305 528 528 TYR TYR B . n 
B 1 306 SER 306 529 529 SER SER B . n 
B 1 307 LEU 307 530 530 LEU LEU B . n 
B 1 308 ALA 308 531 531 ALA ALA B . n 
B 1 309 PRO 309 532 532 PRO PRO B . n 
B 1 310 MET 310 533 533 MET MET B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 CL  1   601  1    CL  CL  A . 
D 3 HOH 1   701  1297 HOH HOH A . 
D 3 HOH 2   702  1519 HOH HOH A . 
D 3 HOH 3   703  1117 HOH HOH A . 
D 3 HOH 4   704  1522 HOH HOH A . 
D 3 HOH 5   705  1233 HOH HOH A . 
D 3 HOH 6   706  1067 HOH HOH A . 
D 3 HOH 7   707  1055 HOH HOH A . 
D 3 HOH 8   708  941  HOH HOH A . 
D 3 HOH 9   709  1187 HOH HOH A . 
D 3 HOH 10  710  1220 HOH HOH A . 
D 3 HOH 11  711  1356 HOH HOH A . 
D 3 HOH 12  712  1184 HOH HOH A . 
D 3 HOH 13  713  944  HOH HOH A . 
D 3 HOH 14  714  1353 HOH HOH A . 
D 3 HOH 15  715  1023 HOH HOH A . 
D 3 HOH 16  716  1035 HOH HOH A . 
D 3 HOH 17  717  1332 HOH HOH A . 
D 3 HOH 18  718  678  HOH HOH A . 
D 3 HOH 19  719  724  HOH HOH A . 
D 3 HOH 20  720  943  HOH HOH A . 
D 3 HOH 21  721  834  HOH HOH A . 
D 3 HOH 22  722  804  HOH HOH A . 
D 3 HOH 23  723  1182 HOH HOH A . 
D 3 HOH 24  724  1330 HOH HOH A . 
D 3 HOH 25  725  1295 HOH HOH A . 
D 3 HOH 26  726  928  HOH HOH A . 
D 3 HOH 27  727  1382 HOH HOH A . 
D 3 HOH 28  728  1215 HOH HOH A . 
D 3 HOH 29  729  890  HOH HOH A . 
D 3 HOH 30  730  1207 HOH HOH A . 
D 3 HOH 31  731  913  HOH HOH A . 
D 3 HOH 32  732  929  HOH HOH A . 
D 3 HOH 33  733  186  HOH HOH A . 
D 3 HOH 34  734  806  HOH HOH A . 
D 3 HOH 35  735  118  HOH HOH A . 
D 3 HOH 36  736  922  HOH HOH A . 
D 3 HOH 37  737  698  HOH HOH A . 
D 3 HOH 38  738  1068 HOH HOH A . 
D 3 HOH 39  739  1208 HOH HOH A . 
D 3 HOH 40  740  906  HOH HOH A . 
D 3 HOH 41  741  1043 HOH HOH A . 
D 3 HOH 42  742  679  HOH HOH A . 
D 3 HOH 43  743  50   HOH HOH A . 
D 3 HOH 44  744  808  HOH HOH A . 
D 3 HOH 45  745  151  HOH HOH A . 
D 3 HOH 46  746  756  HOH HOH A . 
D 3 HOH 47  747  1071 HOH HOH A . 
D 3 HOH 48  748  1376 HOH HOH A . 
D 3 HOH 49  749  1028 HOH HOH A . 
D 3 HOH 50  750  130  HOH HOH A . 
D 3 HOH 51  751  931  HOH HOH A . 
D 3 HOH 52  752  305  HOH HOH A . 
D 3 HOH 53  753  681  HOH HOH A . 
D 3 HOH 54  754  251  HOH HOH A . 
D 3 HOH 55  755  171  HOH HOH A . 
D 3 HOH 56  756  905  HOH HOH A . 
D 3 HOH 57  757  810  HOH HOH A . 
D 3 HOH 58  758  370  HOH HOH A . 
D 3 HOH 59  759  282  HOH HOH A . 
D 3 HOH 60  760  982  HOH HOH A . 
D 3 HOH 61  761  188  HOH HOH A . 
D 3 HOH 62  762  1489 HOH HOH A . 
D 3 HOH 63  763  909  HOH HOH A . 
D 3 HOH 64  764  694  HOH HOH A . 
D 3 HOH 65  765  887  HOH HOH A . 
D 3 HOH 66  766  232  HOH HOH A . 
D 3 HOH 67  767  1031 HOH HOH A . 
D 3 HOH 68  768  40   HOH HOH A . 
D 3 HOH 69  769  821  HOH HOH A . 
D 3 HOH 70  770  105  HOH HOH A . 
D 3 HOH 71  771  854  HOH HOH A . 
D 3 HOH 72  772  269  HOH HOH A . 
D 3 HOH 73  773  923  HOH HOH A . 
D 3 HOH 74  774  405  HOH HOH A . 
D 3 HOH 75  775  1120 HOH HOH A . 
D 3 HOH 76  776  3    HOH HOH A . 
D 3 HOH 77  777  1032 HOH HOH A . 
D 3 HOH 78  778  937  HOH HOH A . 
D 3 HOH 79  779  157  HOH HOH A . 
D 3 HOH 80  780  758  HOH HOH A . 
D 3 HOH 81  781  914  HOH HOH A . 
D 3 HOH 82  782  414  HOH HOH A . 
D 3 HOH 83  783  1123 HOH HOH A . 
D 3 HOH 84  784  75   HOH HOH A . 
D 3 HOH 85  785  1469 HOH HOH A . 
D 3 HOH 86  786  896  HOH HOH A . 
D 3 HOH 87  787  1087 HOH HOH A . 
D 3 HOH 88  788  551  HOH HOH A . 
D 3 HOH 89  789  24   HOH HOH A . 
D 3 HOH 90  790  99   HOH HOH A . 
D 3 HOH 91  791  95   HOH HOH A . 
D 3 HOH 92  792  14   HOH HOH A . 
D 3 HOH 93  793  61   HOH HOH A . 
D 3 HOH 94  794  827  HOH HOH A . 
D 3 HOH 95  795  22   HOH HOH A . 
D 3 HOH 96  796  797  HOH HOH A . 
D 3 HOH 97  797  1125 HOH HOH A . 
D 3 HOH 98  798  16   HOH HOH A . 
D 3 HOH 99  799  725  HOH HOH A . 
D 3 HOH 100 800  271  HOH HOH A . 
D 3 HOH 101 801  1110 HOH HOH A . 
D 3 HOH 102 802  1147 HOH HOH A . 
D 3 HOH 103 803  842  HOH HOH A . 
D 3 HOH 104 804  30   HOH HOH A . 
D 3 HOH 105 805  259  HOH HOH A . 
D 3 HOH 106 806  736  HOH HOH A . 
D 3 HOH 107 807  826  HOH HOH A . 
D 3 HOH 108 808  1209 HOH HOH A . 
D 3 HOH 109 809  17   HOH HOH A . 
D 3 HOH 110 810  686  HOH HOH A . 
D 3 HOH 111 811  126  HOH HOH A . 
D 3 HOH 112 812  891  HOH HOH A . 
D 3 HOH 113 813  801  HOH HOH A . 
D 3 HOH 114 814  811  HOH HOH A . 
D 3 HOH 115 815  250  HOH HOH A . 
D 3 HOH 116 816  404  HOH HOH A . 
D 3 HOH 117 817  1341 HOH HOH A . 
D 3 HOH 118 818  1313 HOH HOH A . 
D 3 HOH 119 819  224  HOH HOH A . 
D 3 HOH 120 820  67   HOH HOH A . 
D 3 HOH 121 821  723  HOH HOH A . 
D 3 HOH 122 822  1264 HOH HOH A . 
D 3 HOH 123 823  103  HOH HOH A . 
D 3 HOH 124 824  820  HOH HOH A . 
D 3 HOH 125 825  193  HOH HOH A . 
D 3 HOH 126 826  1316 HOH HOH A . 
D 3 HOH 127 827  180  HOH HOH A . 
D 3 HOH 128 828  755  HOH HOH A . 
D 3 HOH 129 829  828  HOH HOH A . 
D 3 HOH 130 830  1334 HOH HOH A . 
D 3 HOH 131 831  945  HOH HOH A . 
D 3 HOH 132 832  267  HOH HOH A . 
D 3 HOH 133 833  1022 HOH HOH A . 
D 3 HOH 134 834  1389 HOH HOH A . 
D 3 HOH 135 835  114  HOH HOH A . 
D 3 HOH 136 836  247  HOH HOH A . 
D 3 HOH 137 837  380  HOH HOH A . 
D 3 HOH 138 838  823  HOH HOH A . 
D 3 HOH 139 839  822  HOH HOH A . 
D 3 HOH 140 840  1338 HOH HOH A . 
D 3 HOH 141 841  888  HOH HOH A . 
D 3 HOH 142 842  172  HOH HOH A . 
D 3 HOH 143 843  691  HOH HOH A . 
D 3 HOH 144 844  29   HOH HOH A . 
D 3 HOH 145 845  766  HOH HOH A . 
D 3 HOH 146 846  18   HOH HOH A . 
D 3 HOH 147 847  889  HOH HOH A . 
D 3 HOH 148 848  304  HOH HOH A . 
D 3 HOH 149 849  1021 HOH HOH A . 
D 3 HOH 150 850  899  HOH HOH A . 
D 3 HOH 151 851  1099 HOH HOH A . 
D 3 HOH 152 852  189  HOH HOH A . 
D 3 HOH 153 853  284  HOH HOH A . 
D 3 HOH 154 854  849  HOH HOH A . 
D 3 HOH 155 855  120  HOH HOH A . 
D 3 HOH 156 856  23   HOH HOH A . 
D 3 HOH 157 857  1062 HOH HOH A . 
D 3 HOH 158 858  802  HOH HOH A . 
D 3 HOH 159 859  781  HOH HOH A . 
D 3 HOH 160 860  815  HOH HOH A . 
D 3 HOH 161 861  1229 HOH HOH A . 
D 3 HOH 162 862  1451 HOH HOH A . 
D 3 HOH 163 863  735  HOH HOH A . 
D 3 HOH 164 864  1234 HOH HOH A . 
D 3 HOH 165 865  1436 HOH HOH A . 
D 3 HOH 166 866  476  HOH HOH A . 
D 3 HOH 167 867  115  HOH HOH A . 
D 3 HOH 168 868  799  HOH HOH A . 
D 3 HOH 169 869  76   HOH HOH A . 
D 3 HOH 170 870  204  HOH HOH A . 
D 3 HOH 171 871  78   HOH HOH A . 
D 3 HOH 172 872  825  HOH HOH A . 
D 3 HOH 173 873  272  HOH HOH A . 
D 3 HOH 174 874  998  HOH HOH A . 
D 3 HOH 175 875  824  HOH HOH A . 
D 3 HOH 176 876  925  HOH HOH A . 
D 3 HOH 177 877  940  HOH HOH A . 
D 3 HOH 178 878  166  HOH HOH A . 
D 3 HOH 179 879  1494 HOH HOH A . 
D 3 HOH 180 880  902  HOH HOH A . 
D 3 HOH 181 881  64   HOH HOH A . 
D 3 HOH 182 882  73   HOH HOH A . 
D 3 HOH 183 883  1320 HOH HOH A . 
D 3 HOH 184 884  321  HOH HOH A . 
D 3 HOH 185 885  1054 HOH HOH A . 
D 3 HOH 186 886  223  HOH HOH A . 
D 3 HOH 187 887  837  HOH HOH A . 
D 3 HOH 188 888  938  HOH HOH A . 
D 3 HOH 189 889  818  HOH HOH A . 
D 3 HOH 190 890  935  HOH HOH A . 
D 3 HOH 191 891  844  HOH HOH A . 
D 3 HOH 192 892  800  HOH HOH A . 
D 3 HOH 193 893  1073 HOH HOH A . 
D 3 HOH 194 894  71   HOH HOH A . 
D 3 HOH 195 895  676  HOH HOH A . 
D 3 HOH 196 896  54   HOH HOH A . 
D 3 HOH 197 897  727  HOH HOH A . 
D 3 HOH 198 898  12   HOH HOH A . 
D 3 HOH 199 899  1196 HOH HOH A . 
D 3 HOH 200 900  762  HOH HOH A . 
D 3 HOH 201 901  1027 HOH HOH A . 
D 3 HOH 202 902  59   HOH HOH A . 
D 3 HOH 203 903  1181 HOH HOH A . 
D 3 HOH 204 904  1111 HOH HOH A . 
D 3 HOH 205 905  207  HOH HOH A . 
D 3 HOH 206 906  496  HOH HOH A . 
D 3 HOH 207 907  792  HOH HOH A . 
D 3 HOH 208 908  904  HOH HOH A . 
D 3 HOH 209 909  685  HOH HOH A . 
D 3 HOH 210 910  1423 HOH HOH A . 
D 3 HOH 211 911  696  HOH HOH A . 
D 3 HOH 212 912  831  HOH HOH A . 
D 3 HOH 213 913  814  HOH HOH A . 
D 3 HOH 214 914  1372 HOH HOH A . 
D 3 HOH 215 915  942  HOH HOH A . 
D 3 HOH 216 916  816  HOH HOH A . 
D 3 HOH 217 917  1041 HOH HOH A . 
D 3 HOH 218 918  407  HOH HOH A . 
D 3 HOH 219 919  893  HOH HOH A . 
D 3 HOH 220 920  817  HOH HOH A . 
D 3 HOH 221 921  697  HOH HOH A . 
D 3 HOH 222 922  138  HOH HOH A . 
D 3 HOH 223 923  36   HOH HOH A . 
D 3 HOH 224 924  333  HOH HOH A . 
D 3 HOH 225 925  1197 HOH HOH A . 
D 3 HOH 226 926  930  HOH HOH A . 
D 3 HOH 227 927  1333 HOH HOH A . 
D 3 HOH 228 928  1528 HOH HOH A . 
D 3 HOH 229 929  932  HOH HOH A . 
D 3 HOH 230 930  49   HOH HOH A . 
D 3 HOH 231 931  1086 HOH HOH A . 
D 3 HOH 232 932  1222 HOH HOH A . 
D 3 HOH 233 933  1088 HOH HOH A . 
D 3 HOH 234 934  1202 HOH HOH A . 
D 3 HOH 235 935  1391 HOH HOH A . 
D 3 HOH 236 936  687  HOH HOH A . 
D 3 HOH 237 937  1377 HOH HOH A . 
D 3 HOH 238 938  722  HOH HOH A . 
D 3 HOH 239 939  1079 HOH HOH A . 
D 3 HOH 240 940  1520 HOH HOH A . 
D 3 HOH 241 941  382  HOH HOH A . 
D 3 HOH 242 942  839  HOH HOH A . 
D 3 HOH 243 943  1053 HOH HOH A . 
D 3 HOH 244 944  803  HOH HOH A . 
D 3 HOH 245 945  892  HOH HOH A . 
D 3 HOH 246 946  946  HOH HOH A . 
D 3 HOH 247 947  783  HOH HOH A . 
D 3 HOH 248 948  42   HOH HOH A . 
D 3 HOH 249 949  340  HOH HOH A . 
D 3 HOH 250 950  1056 HOH HOH A . 
D 3 HOH 251 951  677  HOH HOH A . 
D 3 HOH 252 952  1392 HOH HOH A . 
D 3 HOH 253 953  288  HOH HOH A . 
D 3 HOH 254 954  791  HOH HOH A . 
D 3 HOH 255 955  63   HOH HOH A . 
D 3 HOH 256 956  277  HOH HOH A . 
D 3 HOH 257 957  109  HOH HOH A . 
D 3 HOH 258 958  1072 HOH HOH A . 
D 3 HOH 259 959  1169 HOH HOH A . 
D 3 HOH 260 960  1170 HOH HOH A . 
D 3 HOH 261 961  129  HOH HOH A . 
D 3 HOH 262 962  1025 HOH HOH A . 
D 3 HOH 263 963  20   HOH HOH A . 
D 3 HOH 264 964  903  HOH HOH A . 
D 3 HOH 265 965  237  HOH HOH A . 
D 3 HOH 266 966  764  HOH HOH A . 
D 3 HOH 267 967  558  HOH HOH A . 
D 3 HOH 268 968  836  HOH HOH A . 
D 3 HOH 269 969  838  HOH HOH A . 
D 3 HOH 270 970  314  HOH HOH A . 
D 3 HOH 271 971  637  HOH HOH A . 
D 3 HOH 272 972  238  HOH HOH A . 
D 3 HOH 273 973  227  HOH HOH A . 
D 3 HOH 274 974  143  HOH HOH A . 
D 3 HOH 275 975  939  HOH HOH A . 
D 3 HOH 276 976  1509 HOH HOH A . 
D 3 HOH 277 977  504  HOH HOH A . 
D 3 HOH 278 978  611  HOH HOH A . 
D 3 HOH 279 979  805  HOH HOH A . 
D 3 HOH 280 980  1127 HOH HOH A . 
D 3 HOH 281 981  1465 HOH HOH A . 
D 3 HOH 282 982  1128 HOH HOH A . 
D 3 HOH 283 983  847  HOH HOH A . 
D 3 HOH 284 984  1390 HOH HOH A . 
D 3 HOH 285 985  819  HOH HOH A . 
D 3 HOH 286 986  1375 HOH HOH A . 
D 3 HOH 287 987  440  HOH HOH A . 
D 3 HOH 288 988  200  HOH HOH A . 
D 3 HOH 289 989  1325 HOH HOH A . 
D 3 HOH 290 990  437  HOH HOH A . 
D 3 HOH 291 991  1373 HOH HOH A . 
D 3 HOH 292 992  1228 HOH HOH A . 
D 3 HOH 293 993  682  HOH HOH A . 
D 3 HOH 294 994  812  HOH HOH A . 
D 3 HOH 295 995  169  HOH HOH A . 
D 3 HOH 296 996  1102 HOH HOH A . 
D 3 HOH 297 997  1431 HOH HOH A . 
D 3 HOH 298 998  1223 HOH HOH A . 
D 3 HOH 299 999  80   HOH HOH A . 
D 3 HOH 300 1000 1124 HOH HOH A . 
D 3 HOH 301 1001 1085 HOH HOH A . 
D 3 HOH 302 1002 763  HOH HOH A . 
D 3 HOH 303 1003 1044 HOH HOH A . 
D 3 HOH 304 1004 1199 HOH HOH A . 
D 3 HOH 305 1005 1089 HOH HOH A . 
D 3 HOH 306 1006 1046 HOH HOH A . 
D 3 HOH 307 1007 898  HOH HOH A . 
D 3 HOH 308 1008 921  HOH HOH A . 
D 3 HOH 309 1009 712  HOH HOH A . 
D 3 HOH 310 1010 216  HOH HOH A . 
D 3 HOH 311 1011 1232 HOH HOH A . 
D 3 HOH 312 1012 294  HOH HOH A . 
D 3 HOH 313 1013 155  HOH HOH A . 
D 3 HOH 314 1014 1474 HOH HOH A . 
D 3 HOH 315 1015 1016 HOH HOH A . 
D 3 HOH 316 1016 701  HOH HOH A . 
D 3 HOH 317 1017 1461 HOH HOH A . 
D 3 HOH 318 1018 989  HOH HOH A . 
D 3 HOH 319 1019 1118 HOH HOH A . 
D 3 HOH 320 1020 1459 HOH HOH A . 
D 3 HOH 321 1021 1471 HOH HOH A . 
D 3 HOH 322 1022 1212 HOH HOH A . 
D 3 HOH 323 1023 1206 HOH HOH A . 
D 3 HOH 324 1024 239  HOH HOH A . 
D 3 HOH 325 1025 936  HOH HOH A . 
D 3 HOH 326 1026 761  HOH HOH A . 
D 3 HOH 327 1027 1042 HOH HOH A . 
D 3 HOH 328 1028 996  HOH HOH A . 
D 3 HOH 329 1029 1475 HOH HOH A . 
D 3 HOH 330 1030 1237 HOH HOH A . 
D 3 HOH 331 1031 1114 HOH HOH A . 
D 3 HOH 332 1032 1026 HOH HOH A . 
D 3 HOH 333 1033 1060 HOH HOH A . 
D 3 HOH 334 1034 1104 HOH HOH A . 
D 3 HOH 335 1035 1116 HOH HOH A . 
D 3 HOH 336 1036 1263 HOH HOH A . 
D 3 HOH 337 1037 1226 HOH HOH A . 
D 3 HOH 338 1038 798  HOH HOH A . 
D 3 HOH 339 1039 1064 HOH HOH A . 
D 3 HOH 340 1040 1521 HOH HOH A . 
D 3 HOH 341 1041 353  HOH HOH A . 
D 3 HOH 342 1042 1224 HOH HOH A . 
D 3 HOH 343 1043 1354 HOH HOH A . 
D 3 HOH 344 1044 767  HOH HOH A . 
D 3 HOH 345 1045 778  HOH HOH A . 
D 3 HOH 346 1046 1058 HOH HOH A . 
D 3 HOH 347 1047 1037 HOH HOH A . 
D 3 HOH 348 1048 1428 HOH HOH A . 
D 3 HOH 349 1049 1014 HOH HOH A . 
D 3 HOH 350 1050 1235 HOH HOH A . 
D 3 HOH 351 1051 924  HOH HOH A . 
D 3 HOH 352 1052 1529 HOH HOH A . 
D 3 HOH 353 1053 1414 HOH HOH A . 
D 3 HOH 354 1054 1285 HOH HOH A . 
D 3 HOH 355 1055 91   HOH HOH A . 
D 3 HOH 356 1056 1444 HOH HOH A . 
D 3 HOH 357 1057 1386 HOH HOH A . 
D 3 HOH 358 1058 1385 HOH HOH A . 
D 3 HOH 359 1059 1066 HOH HOH A . 
D 3 HOH 360 1060 757  HOH HOH A . 
D 3 HOH 361 1061 1034 HOH HOH A . 
D 3 HOH 362 1062 1213 HOH HOH A . 
D 3 HOH 363 1063 995  HOH HOH A . 
D 3 HOH 364 1064 520  HOH HOH A . 
D 3 HOH 365 1065 580  HOH HOH A . 
D 3 HOH 366 1066 794  HOH HOH A . 
D 3 HOH 367 1067 1425 HOH HOH A . 
D 3 HOH 368 1068 1457 HOH HOH A . 
D 3 HOH 369 1069 1100 HOH HOH A . 
D 3 HOH 370 1070 1019 HOH HOH A . 
D 3 HOH 371 1071 1472 HOH HOH A . 
D 3 HOH 372 1072 1383 HOH HOH A . 
D 3 HOH 373 1073 680  HOH HOH A . 
D 3 HOH 374 1074 1294 HOH HOH A . 
D 3 HOH 375 1075 1036 HOH HOH A . 
D 3 HOH 376 1076 1413 HOH HOH A . 
D 3 HOH 377 1077 910  HOH HOH A . 
D 3 HOH 378 1078 911  HOH HOH A . 
D 3 HOH 379 1079 1346 HOH HOH A . 
D 3 HOH 380 1080 1109 HOH HOH A . 
D 3 HOH 381 1081 567  HOH HOH A . 
D 3 HOH 382 1082 1065 HOH HOH A . 
D 3 HOH 383 1083 1388 HOH HOH A . 
D 3 HOH 384 1084 1195 HOH HOH A . 
D 3 HOH 385 1085 777  HOH HOH A . 
D 3 HOH 386 1086 813  HOH HOH A . 
D 3 HOH 387 1087 1203 HOH HOH A . 
D 3 HOH 388 1088 428  HOH HOH A . 
D 3 HOH 389 1089 926  HOH HOH A . 
D 3 HOH 390 1090 1467 HOH HOH A . 
D 3 HOH 391 1091 540  HOH HOH A . 
D 3 HOH 392 1092 779  HOH HOH A . 
D 3 HOH 393 1093 840  HOH HOH A . 
D 3 HOH 394 1094 1315 HOH HOH A . 
D 3 HOH 395 1095 1433 HOH HOH A . 
D 3 HOH 396 1096 1490 HOH HOH A . 
D 3 HOH 397 1097 521  HOH HOH A . 
D 3 HOH 398 1098 1188 HOH HOH A . 
D 3 HOH 399 1099 807  HOH HOH A . 
D 3 HOH 400 1100 1238 HOH HOH A . 
D 3 HOH 401 1101 1450 HOH HOH A . 
D 3 HOH 402 1102 217  HOH HOH A . 
D 3 HOH 403 1103 1198 HOH HOH A . 
D 3 HOH 404 1104 1310 HOH HOH A . 
D 3 HOH 405 1105 1122 HOH HOH A . 
D 3 HOH 406 1106 124  HOH HOH A . 
D 3 HOH 407 1107 894  HOH HOH A . 
D 3 HOH 408 1108 1018 HOH HOH A . 
D 3 HOH 409 1109 1335 HOH HOH A . 
D 3 HOH 410 1110 1171 HOH HOH A . 
D 3 HOH 411 1111 846  HOH HOH A . 
D 3 HOH 412 1112 1200 HOH HOH A . 
D 3 HOH 413 1113 1005 HOH HOH A . 
D 3 HOH 414 1114 1096 HOH HOH A . 
D 3 HOH 415 1115 927  HOH HOH A . 
D 3 HOH 416 1116 874  HOH HOH A . 
D 3 HOH 417 1117 519  HOH HOH A . 
D 3 HOH 418 1118 1438 HOH HOH A . 
D 3 HOH 419 1119 1352 HOH HOH A . 
D 3 HOH 420 1120 1090 HOH HOH A . 
D 3 HOH 421 1121 1183 HOH HOH A . 
D 3 HOH 422 1122 1119 HOH HOH A . 
D 3 HOH 423 1123 1476 HOH HOH A . 
D 3 HOH 424 1124 1437 HOH HOH A . 
D 3 HOH 425 1125 886  HOH HOH A . 
D 3 HOH 426 1126 565  HOH HOH A . 
D 3 HOH 427 1127 1378 HOH HOH A . 
D 3 HOH 428 1128 1322 HOH HOH A . 
D 3 HOH 429 1129 1115 HOH HOH A . 
D 3 HOH 430 1130 1460 HOH HOH A . 
D 3 HOH 431 1131 1284 HOH HOH A . 
D 3 HOH 432 1132 1463 HOH HOH A . 
D 3 HOH 433 1133 1462 HOH HOH A . 
D 3 HOH 434 1134 1449 HOH HOH A . 
D 3 HOH 435 1135 738  HOH HOH A . 
D 3 HOH 436 1136 1084 HOH HOH A . 
D 3 HOH 437 1137 630  HOH HOH A . 
D 3 HOH 438 1138 1029 HOH HOH A . 
D 3 HOH 439 1139 1205 HOH HOH A . 
D 3 HOH 440 1140 1061 HOH HOH A . 
D 3 HOH 441 1141 1045 HOH HOH A . 
D 3 HOH 442 1142 400  HOH HOH A . 
D 3 HOH 443 1143 1179 HOH HOH A . 
D 3 HOH 444 1144 531  HOH HOH A . 
D 3 HOH 445 1145 1379 HOH HOH A . 
D 3 HOH 446 1146 848  HOH HOH A . 
D 3 HOH 447 1147 1145 HOH HOH A . 
D 3 HOH 448 1148 1180 HOH HOH A . 
D 3 HOH 449 1149 1323 HOH HOH A . 
D 3 HOH 450 1150 830  HOH HOH A . 
D 3 HOH 451 1151 760  HOH HOH A . 
D 3 HOH 452 1152 1452 HOH HOH A . 
D 3 HOH 453 1153 1365 HOH HOH A . 
D 3 HOH 454 1154 1296 HOH HOH A . 
D 3 HOH 455 1155 1321 HOH HOH A . 
D 3 HOH 456 1156 1501 HOH HOH A . 
D 3 HOH 457 1157 1470 HOH HOH A . 
D 3 HOH 458 1158 1291 HOH HOH A . 
D 3 HOH 459 1159 907  HOH HOH A . 
D 3 HOH 460 1160 897  HOH HOH A . 
D 3 HOH 461 1161 1318 HOH HOH A . 
D 3 HOH 462 1162 915  HOH HOH A . 
D 3 HOH 463 1163 850  HOH HOH A . 
D 3 HOH 464 1164 901  HOH HOH A . 
D 3 HOH 465 1165 1108 HOH HOH A . 
D 3 HOH 466 1166 1069 HOH HOH A . 
D 3 HOH 467 1167 845  HOH HOH A . 
D 3 HOH 468 1168 1454 HOH HOH A . 
D 3 HOH 469 1169 1020 HOH HOH A . 
D 3 HOH 470 1170 1370 HOH HOH A . 
D 3 HOH 471 1171 1422 HOH HOH A . 
D 3 HOH 472 1172 895  HOH HOH A . 
D 3 HOH 473 1173 1210 HOH HOH A . 
D 3 HOH 474 1174 1311 HOH HOH A . 
D 3 HOH 475 1175 1328 HOH HOH A . 
D 3 HOH 476 1176 1121 HOH HOH A . 
D 3 HOH 477 1177 702  HOH HOH A . 
D 3 HOH 478 1178 1012 HOH HOH A . 
D 3 HOH 479 1179 1076 HOH HOH A . 
D 3 HOH 480 1180 1314 HOH HOH A . 
D 3 HOH 481 1181 1455 HOH HOH A . 
D 3 HOH 482 1182 908  HOH HOH A . 
D 3 HOH 483 1183 1075 HOH HOH A . 
D 3 HOH 484 1184 1317 HOH HOH A . 
D 3 HOH 485 1185 1482 HOH HOH A . 
D 3 HOH 486 1186 997  HOH HOH A . 
D 3 HOH 487 1187 1219 HOH HOH A . 
D 3 HOH 488 1188 1369 HOH HOH A . 
E 3 HOH 1   601  1185 HOH HOH B . 
E 3 HOH 2   602  1038 HOH HOH B . 
E 3 HOH 3   603  695  HOH HOH B . 
E 3 HOH 4   604  1426 HOH HOH B . 
E 3 HOH 5   605  343  HOH HOH B . 
E 3 HOH 6   606  1091 HOH HOH B . 
E 3 HOH 7   607  1400 HOH HOH B . 
E 3 HOH 8   608  674  HOH HOH B . 
E 3 HOH 9   609  969  HOH HOH B . 
E 3 HOH 10  610  98   HOH HOH B . 
E 3 HOH 11  611  1244 HOH HOH B . 
E 3 HOH 12  612  954  HOH HOH B . 
E 3 HOH 13  613  1135 HOH HOH B . 
E 3 HOH 14  614  971  HOH HOH B . 
E 3 HOH 15  615  1290 HOH HOH B . 
E 3 HOH 16  616  918  HOH HOH B . 
E 3 HOH 17  617  160  HOH HOH B . 
E 3 HOH 18  618  795  HOH HOH B . 
E 3 HOH 19  619  734  HOH HOH B . 
E 3 HOH 20  620  693  HOH HOH B . 
E 3 HOH 21  621  690  HOH HOH B . 
E 3 HOH 22  622  869  HOH HOH B . 
E 3 HOH 23  623  1130 HOH HOH B . 
E 3 HOH 24  624  1257 HOH HOH B . 
E 3 HOH 25  625  344  HOH HOH B . 
E 3 HOH 26  626  970  HOH HOH B . 
E 3 HOH 27  627  1409 HOH HOH B . 
E 3 HOH 28  628  832  HOH HOH B . 
E 3 HOH 29  629  1218 HOH HOH B . 
E 3 HOH 30  630  972  HOH HOH B . 
E 3 HOH 31  631  563  HOH HOH B . 
E 3 HOH 32  632  789  HOH HOH B . 
E 3 HOH 33  633  661  HOH HOH B . 
E 3 HOH 34  634  879  HOH HOH B . 
E 3 HOH 35  635  348  HOH HOH B . 
E 3 HOH 36  636  1483 HOH HOH B . 
E 3 HOH 37  637  1112 HOH HOH B . 
E 3 HOH 38  638  952  HOH HOH B . 
E 3 HOH 39  639  1094 HOH HOH B . 
E 3 HOH 40  640  1059 HOH HOH B . 
E 3 HOH 41  641  853  HOH HOH B . 
E 3 HOH 42  642  1308 HOH HOH B . 
E 3 HOH 43  643  347  HOH HOH B . 
E 3 HOH 44  644  782  HOH HOH B . 
E 3 HOH 45  645  730  HOH HOH B . 
E 3 HOH 46  646  714  HOH HOH B . 
E 3 HOH 47  647  634  HOH HOH B . 
E 3 HOH 48  648  1360 HOH HOH B . 
E 3 HOH 49  649  86   HOH HOH B . 
E 3 HOH 50  650  707  HOH HOH B . 
E 3 HOH 51  651  176  HOH HOH B . 
E 3 HOH 52  652  741  HOH HOH B . 
E 3 HOH 53  653  852  HOH HOH B . 
E 3 HOH 54  654  744  HOH HOH B . 
E 3 HOH 55  655  962  HOH HOH B . 
E 3 HOH 56  656  6    HOH HOH B . 
E 3 HOH 57  657  1270 HOH HOH B . 
E 3 HOH 58  658  56   HOH HOH B . 
E 3 HOH 59  659  268  HOH HOH B . 
E 3 HOH 60  660  958  HOH HOH B . 
E 3 HOH 61  661  746  HOH HOH B . 
E 3 HOH 62  662  994  HOH HOH B . 
E 3 HOH 63  663  219  HOH HOH B . 
E 3 HOH 64  664  1420 HOH HOH B . 
E 3 HOH 65  665  131  HOH HOH B . 
E 3 HOH 66  666  1276 HOH HOH B . 
E 3 HOH 67  667  83   HOH HOH B . 
E 3 HOH 68  668  1394 HOH HOH B . 
E 3 HOH 69  669  2    HOH HOH B . 
E 3 HOH 70  670  769  HOH HOH B . 
E 3 HOH 71  671  753  HOH HOH B . 
E 3 HOH 72  672  875  HOH HOH B . 
E 3 HOH 73  673  860  HOH HOH B . 
E 3 HOH 74  674  190  HOH HOH B . 
E 3 HOH 75  675  254  HOH HOH B . 
E 3 HOH 76  676  220  HOH HOH B . 
E 3 HOH 77  677  43   HOH HOH B . 
E 3 HOH 78  678  199  HOH HOH B . 
E 3 HOH 79  679  672  HOH HOH B . 
E 3 HOH 80  680  13   HOH HOH B . 
E 3 HOH 81  681  146  HOH HOH B . 
E 3 HOH 82  682  128  HOH HOH B . 
E 3 HOH 83  683  933  HOH HOH B . 
E 3 HOH 84  684  731  HOH HOH B . 
E 3 HOH 85  685  709  HOH HOH B . 
E 3 HOH 86  686  427  HOH HOH B . 
E 3 HOH 87  687  865  HOH HOH B . 
E 3 HOH 88  688  10   HOH HOH B . 
E 3 HOH 89  689  1078 HOH HOH B . 
E 3 HOH 90  690  1144 HOH HOH B . 
E 3 HOH 91  691  1134 HOH HOH B . 
E 3 HOH 92  692  458  HOH HOH B . 
E 3 HOH 93  693  33   HOH HOH B . 
E 3 HOH 94  694  363  HOH HOH B . 
E 3 HOH 95  695  1265 HOH HOH B . 
E 3 HOH 96  696  711  HOH HOH B . 
E 3 HOH 97  697  776  HOH HOH B . 
E 3 HOH 98  698  745  HOH HOH B . 
E 3 HOH 99  699  963  HOH HOH B . 
E 3 HOH 100 700  178  HOH HOH B . 
E 3 HOH 101 701  1396 HOH HOH B . 
E 3 HOH 102 702  57   HOH HOH B . 
E 3 HOH 103 703  867  HOH HOH B . 
E 3 HOH 104 704  876  HOH HOH B . 
E 3 HOH 105 705  533  HOH HOH B . 
E 3 HOH 106 706  863  HOH HOH B . 
E 3 HOH 107 707  116  HOH HOH B . 
E 3 HOH 108 708  66   HOH HOH B . 
E 3 HOH 109 709  742  HOH HOH B . 
E 3 HOH 110 710  19   HOH HOH B . 
E 3 HOH 111 711  1030 HOH HOH B . 
E 3 HOH 112 712  107  HOH HOH B . 
E 3 HOH 113 713  624  HOH HOH B . 
E 3 HOH 114 714  32   HOH HOH B . 
E 3 HOH 115 715  97   HOH HOH B . 
E 3 HOH 116 716  84   HOH HOH B . 
E 3 HOH 117 717  26   HOH HOH B . 
E 3 HOH 118 718  1131 HOH HOH B . 
E 3 HOH 119 719  48   HOH HOH B . 
E 3 HOH 120 720  884  HOH HOH B . 
E 3 HOH 121 721  870  HOH HOH B . 
E 3 HOH 122 722  881  HOH HOH B . 
E 3 HOH 123 723  729  HOH HOH B . 
E 3 HOH 124 724  981  HOH HOH B . 
E 3 HOH 125 725  265  HOH HOH B . 
E 3 HOH 126 726  718  HOH HOH B . 
E 3 HOH 127 727  1186 HOH HOH B . 
E 3 HOH 128 728  728  HOH HOH B . 
E 3 HOH 129 729  1227 HOH HOH B . 
E 3 HOH 130 730  1178 HOH HOH B . 
E 3 HOH 131 731  1260 HOH HOH B . 
E 3 HOH 132 732  192  HOH HOH B . 
E 3 HOH 133 733  1154 HOH HOH B . 
E 3 HOH 134 734  101  HOH HOH B . 
E 3 HOH 135 735  44   HOH HOH B . 
E 3 HOH 136 736  959  HOH HOH B . 
E 3 HOH 137 737  1149 HOH HOH B . 
E 3 HOH 138 738  135  HOH HOH B . 
E 3 HOH 139 739  11   HOH HOH B . 
E 3 HOH 140 740  740  HOH HOH B . 
E 3 HOH 141 741  699  HOH HOH B . 
E 3 HOH 142 742  148  HOH HOH B . 
E 3 HOH 143 743  4    HOH HOH B . 
E 3 HOH 144 744  39   HOH HOH B . 
E 3 HOH 145 745  772  HOH HOH B . 
E 3 HOH 146 746  264  HOH HOH B . 
E 3 HOH 147 747  721  HOH HOH B . 
E 3 HOH 148 748  704  HOH HOH B . 
E 3 HOH 149 749  546  HOH HOH B . 
E 3 HOH 150 750  673  HOH HOH B . 
E 3 HOH 151 751  65   HOH HOH B . 
E 3 HOH 152 752  77   HOH HOH B . 
E 3 HOH 153 753  5    HOH HOH B . 
E 3 HOH 154 754  415  HOH HOH B . 
E 3 HOH 155 755  1282 HOH HOH B . 
E 3 HOH 156 756  751  HOH HOH B . 
E 3 HOH 157 757  851  HOH HOH B . 
E 3 HOH 158 758  70   HOH HOH B . 
E 3 HOH 159 759  214  HOH HOH B . 
E 3 HOH 160 760  992  HOH HOH B . 
E 3 HOH 161 761  878  HOH HOH B . 
E 3 HOH 162 762  285  HOH HOH B . 
E 3 HOH 163 763  862  HOH HOH B . 
E 3 HOH 164 764  775  HOH HOH B . 
E 3 HOH 165 765  15   HOH HOH B . 
E 3 HOH 166 766  35   HOH HOH B . 
E 3 HOH 167 767  1267 HOH HOH B . 
E 3 HOH 168 768  732  HOH HOH B . 
E 3 HOH 169 769  1468 HOH HOH B . 
E 3 HOH 170 770  108  HOH HOH B . 
E 3 HOH 171 771  92   HOH HOH B . 
E 3 HOH 172 772  856  HOH HOH B . 
E 3 HOH 173 773  866  HOH HOH B . 
E 3 HOH 174 774  858  HOH HOH B . 
E 3 HOH 175 775  253  HOH HOH B . 
E 3 HOH 176 776  203  HOH HOH B . 
E 3 HOH 177 777  194  HOH HOH B . 
E 3 HOH 178 778  286  HOH HOH B . 
E 3 HOH 179 779  957  HOH HOH B . 
E 3 HOH 180 780  974  HOH HOH B . 
E 3 HOH 181 781  717  HOH HOH B . 
E 3 HOH 182 782  1239 HOH HOH B . 
E 3 HOH 183 783  89   HOH HOH B . 
E 3 HOH 184 784  1138 HOH HOH B . 
E 3 HOH 185 785  700  HOH HOH B . 
E 3 HOH 186 786  614  HOH HOH B . 
E 3 HOH 187 787  106  HOH HOH B . 
E 3 HOH 188 788  1518 HOH HOH B . 
E 3 HOH 189 789  868  HOH HOH B . 
E 3 HOH 190 790  1272 HOH HOH B . 
E 3 HOH 191 791  31   HOH HOH B . 
E 3 HOH 192 792  46   HOH HOH B . 
E 3 HOH 193 793  52   HOH HOH B . 
E 3 HOH 194 794  835  HOH HOH B . 
E 3 HOH 195 795  986  HOH HOH B . 
E 3 HOH 196 796  27   HOH HOH B . 
E 3 HOH 197 797  833  HOH HOH B . 
E 3 HOH 198 798  770  HOH HOH B . 
E 3 HOH 199 799  871  HOH HOH B . 
E 3 HOH 200 800  880  HOH HOH B . 
E 3 HOH 201 801  961  HOH HOH B . 
E 3 HOH 202 802  747  HOH HOH B . 
E 3 HOH 203 803  788  HOH HOH B . 
E 3 HOH 204 804  183  HOH HOH B . 
E 3 HOH 205 805  864  HOH HOH B . 
E 3 HOH 206 806  716  HOH HOH B . 
E 3 HOH 207 807  956  HOH HOH B . 
E 3 HOH 208 808  492  HOH HOH B . 
E 3 HOH 209 809  950  HOH HOH B . 
E 3 HOH 210 810  768  HOH HOH B . 
E 3 HOH 211 811  38   HOH HOH B . 
E 3 HOH 212 812  705  HOH HOH B . 
E 3 HOH 213 813  719  HOH HOH B . 
E 3 HOH 214 814  920  HOH HOH B . 
E 3 HOH 215 815  1245 HOH HOH B . 
E 3 HOH 216 816  257  HOH HOH B . 
E 3 HOH 217 817  1249 HOH HOH B . 
E 3 HOH 218 818  423  HOH HOH B . 
E 3 HOH 219 819  771  HOH HOH B . 
E 3 HOH 220 820  34   HOH HOH B . 
E 3 HOH 221 821  51   HOH HOH B . 
E 3 HOH 222 822  110  HOH HOH B . 
E 3 HOH 223 823  965  HOH HOH B . 
E 3 HOH 224 824  861  HOH HOH B . 
E 3 HOH 225 825  1530 HOH HOH B . 
E 3 HOH 226 826  743  HOH HOH B . 
E 3 HOH 227 827  1093 HOH HOH B . 
E 3 HOH 228 828  917  HOH HOH B . 
E 3 HOH 229 829  1410 HOH HOH B . 
E 3 HOH 230 830  261  HOH HOH B . 
E 3 HOH 231 831  671  HOH HOH B . 
E 3 HOH 232 832  1148 HOH HOH B . 
E 3 HOH 233 833  334  HOH HOH B . 
E 3 HOH 234 834  145  HOH HOH B . 
E 3 HOH 235 835  973  HOH HOH B . 
E 3 HOH 236 836  978  HOH HOH B . 
E 3 HOH 237 837  1499 HOH HOH B . 
E 3 HOH 238 838  141  HOH HOH B . 
E 3 HOH 239 839  919  HOH HOH B . 
E 3 HOH 240 840  955  HOH HOH B . 
E 3 HOH 241 841  1439 HOH HOH B . 
E 3 HOH 242 842  1273 HOH HOH B . 
E 3 HOH 243 843  1048 HOH HOH B . 
E 3 HOH 244 844  1081 HOH HOH B . 
E 3 HOH 245 845  1496 HOH HOH B . 
E 3 HOH 246 846  1299 HOH HOH B . 
E 3 HOH 247 847  1271 HOH HOH B . 
E 3 HOH 248 848  809  HOH HOH B . 
E 3 HOH 249 849  102  HOH HOH B . 
E 3 HOH 250 850  559  HOH HOH B . 
E 3 HOH 251 851  934  HOH HOH B . 
E 3 HOH 252 852  1211 HOH HOH B . 
E 3 HOH 253 853  242  HOH HOH B . 
E 3 HOH 254 854  752  HOH HOH B . 
E 3 HOH 255 855  1478 HOH HOH B . 
E 3 HOH 256 856  1168 HOH HOH B . 
E 3 HOH 257 857  255  HOH HOH B . 
E 3 HOH 258 858  94   HOH HOH B . 
E 3 HOH 259 859  1166 HOH HOH B . 
E 3 HOH 260 860  121  HOH HOH B . 
E 3 HOH 261 861  979  HOH HOH B . 
E 3 HOH 262 862  748  HOH HOH B . 
E 3 HOH 263 863  1255 HOH HOH B . 
E 3 HOH 264 864  1512 HOH HOH B . 
E 3 HOH 265 865  215  HOH HOH B . 
E 3 HOH 266 866  739  HOH HOH B . 
E 3 HOH 267 867  308  HOH HOH B . 
E 3 HOH 268 868  1277 HOH HOH B . 
E 3 HOH 269 869  8    HOH HOH B . 
E 3 HOH 270 870  164  HOH HOH B . 
E 3 HOH 271 871  303  HOH HOH B . 
E 3 HOH 272 872  184  HOH HOH B . 
E 3 HOH 273 873  883  HOH HOH B . 
E 3 HOH 274 874  684  HOH HOH B . 
E 3 HOH 275 875  137  HOH HOH B . 
E 3 HOH 276 876  733  HOH HOH B . 
E 3 HOH 277 877  1283 HOH HOH B . 
E 3 HOH 278 878  1140 HOH HOH B . 
E 3 HOH 279 879  1077 HOH HOH B . 
E 3 HOH 280 880  948  HOH HOH B . 
E 3 HOH 281 881  951  HOH HOH B . 
E 3 HOH 282 882  55   HOH HOH B . 
E 3 HOH 283 883  1517 HOH HOH B . 
E 3 HOH 284 884  401  HOH HOH B . 
E 3 HOH 285 885  161  HOH HOH B . 
E 3 HOH 286 886  787  HOH HOH B . 
E 3 HOH 287 887  993  HOH HOH B . 
E 3 HOH 288 888  966  HOH HOH B . 
E 3 HOH 289 889  749  HOH HOH B . 
E 3 HOH 290 890  653  HOH HOH B . 
E 3 HOH 291 891  1010 HOH HOH B . 
E 3 HOH 292 892  1156 HOH HOH B . 
E 3 HOH 293 893  243  HOH HOH B . 
E 3 HOH 294 894  1279 HOH HOH B . 
E 3 HOH 295 895  1256 HOH HOH B . 
E 3 HOH 296 896  1440 HOH HOH B . 
E 3 HOH 297 897  1152 HOH HOH B . 
E 3 HOH 298 898  179  HOH HOH B . 
E 3 HOH 299 899  368  HOH HOH B . 
E 3 HOH 300 900  1136 HOH HOH B . 
E 3 HOH 301 901  1083 HOH HOH B . 
E 3 HOH 302 902  1481 HOH HOH B . 
E 3 HOH 303 903  1395 HOH HOH B . 
E 3 HOH 304 904  1399 HOH HOH B . 
E 3 HOH 305 905  784  HOH HOH B . 
E 3 HOH 306 906  706  HOH HOH B . 
E 3 HOH 307 907  1524 HOH HOH B . 
E 3 HOH 308 908  1159 HOH HOH B . 
E 3 HOH 309 909  843  HOH HOH B . 
E 3 HOH 310 910  765  HOH HOH B . 
E 3 HOH 311 911  1407 HOH HOH B . 
E 3 HOH 312 912  1348 HOH HOH B . 
E 3 HOH 313 913  1448 HOH HOH B . 
E 3 HOH 314 914  1039 HOH HOH B . 
E 3 HOH 315 915  829  HOH HOH B . 
E 3 HOH 316 916  1498 HOH HOH B . 
E 3 HOH 317 917  1464 HOH HOH B . 
E 3 HOH 318 918  977  HOH HOH B . 
E 3 HOH 319 919  1261 HOH HOH B . 
E 3 HOH 320 920  1398 HOH HOH B . 
E 3 HOH 321 921  1040 HOH HOH B . 
E 3 HOH 322 922  62   HOH HOH B . 
E 3 HOH 323 923  1504 HOH HOH B . 
E 3 HOH 324 924  754  HOH HOH B . 
E 3 HOH 325 925  1262 HOH HOH B . 
E 3 HOH 326 926  1009 HOH HOH B . 
E 3 HOH 327 927  1473 HOH HOH B . 
E 3 HOH 328 928  1505 HOH HOH B . 
E 3 HOH 329 929  390  HOH HOH B . 
E 3 HOH 330 930  1137 HOH HOH B . 
E 3 HOH 331 931  715  HOH HOH B . 
E 3 HOH 332 932  1515 HOH HOH B . 
E 3 HOH 333 933  726  HOH HOH B . 
E 3 HOH 334 934  1493 HOH HOH B . 
E 3 HOH 335 935  1242 HOH HOH B . 
E 3 HOH 336 936  1441 HOH HOH B . 
E 3 HOH 337 937  713  HOH HOH B . 
E 3 HOH 338 938  1268 HOH HOH B . 
E 3 HOH 339 939  1479 HOH HOH B . 
E 3 HOH 340 940  916  HOH HOH B . 
E 3 HOH 341 941  1172 HOH HOH B . 
E 3 HOH 342 942  859  HOH HOH B . 
E 3 HOH 343 943  1252 HOH HOH B . 
E 3 HOH 344 944  1526 HOH HOH B . 
E 3 HOH 345 945  451  HOH HOH B . 
E 3 HOH 346 946  413  HOH HOH B . 
E 3 HOH 347 947  1405 HOH HOH B . 
E 3 HOH 348 948  750  HOH HOH B . 
E 3 HOH 349 949  857  HOH HOH B . 
E 3 HOH 350 950  988  HOH HOH B . 
E 3 HOH 351 951  786  HOH HOH B . 
E 3 HOH 352 952  1442 HOH HOH B . 
E 3 HOH 353 953  692  HOH HOH B . 
E 3 HOH 354 954  1155 HOH HOH B . 
E 3 HOH 355 955  1456 HOH HOH B . 
E 3 HOH 356 956  968  HOH HOH B . 
E 3 HOH 357 957  885  HOH HOH B . 
E 3 HOH 358 958  1113 HOH HOH B . 
E 3 HOH 359 959  623  HOH HOH B . 
E 3 HOH 360 960  1298 HOH HOH B . 
E 3 HOH 361 961  1253 HOH HOH B . 
E 3 HOH 362 962  1485 HOH HOH B . 
E 3 HOH 363 963  1017 HOH HOH B . 
E 3 HOH 364 964  1251 HOH HOH B . 
E 3 HOH 365 965  1161 HOH HOH B . 
E 3 HOH 366 966  1443 HOH HOH B . 
E 3 HOH 367 967  1133 HOH HOH B . 
E 3 HOH 368 968  1139 HOH HOH B . 
E 3 HOH 369 969  1269 HOH HOH B . 
E 3 HOH 370 970  720  HOH HOH B . 
E 3 HOH 371 971  1307 HOH HOH B . 
E 3 HOH 372 972  1162 HOH HOH B . 
E 3 HOH 373 973  985  HOH HOH B . 
E 3 HOH 374 974  1082 HOH HOH B . 
E 3 HOH 375 975  1000 HOH HOH B . 
E 3 HOH 376 976  364  HOH HOH B . 
E 3 HOH 377 977  1447 HOH HOH B . 
E 3 HOH 378 978  256  HOH HOH B . 
E 3 HOH 379 979  855  HOH HOH B . 
E 3 HOH 380 980  1371 HOH HOH B . 
E 3 HOH 381 981  1527 HOH HOH B . 
E 3 HOH 382 982  1403 HOH HOH B . 
E 3 HOH 383 983  1286 HOH HOH B . 
E 3 HOH 384 984  1216 HOH HOH B . 
E 3 HOH 385 985  975  HOH HOH B . 
E 3 HOH 386 986  737  HOH HOH B . 
E 3 HOH 387 987  1516 HOH HOH B . 
E 3 HOH 388 988  1052 HOH HOH B . 
E 3 HOH 389 989  1380 HOH HOH B . 
E 3 HOH 390 990  1176 HOH HOH B . 
E 3 HOH 391 991  1324 HOH HOH B . 
E 3 HOH 392 992  999  HOH HOH B . 
E 3 HOH 393 993  785  HOH HOH B . 
E 3 HOH 394 994  1001 HOH HOH B . 
E 3 HOH 395 995  1404 HOH HOH B . 
E 3 HOH 396 996  1477 HOH HOH B . 
E 3 HOH 397 997  873  HOH HOH B . 
E 3 HOH 398 998  302  HOH HOH B . 
E 3 HOH 399 999  1434 HOH HOH B . 
E 3 HOH 400 1000 1175 HOH HOH B . 
E 3 HOH 401 1001 964  HOH HOH B . 
E 3 HOH 402 1002 1435 HOH HOH B . 
E 3 HOH 403 1003 1243 HOH HOH B . 
E 3 HOH 404 1004 703  HOH HOH B . 
E 3 HOH 405 1005 1095 HOH HOH B . 
E 3 HOH 406 1006 1143 HOH HOH B . 
E 3 HOH 407 1007 872  HOH HOH B . 
E 3 HOH 408 1008 289  HOH HOH B . 
E 3 HOH 409 1009 1525 HOH HOH B . 
E 3 HOH 410 1010 1254 HOH HOH B . 
E 3 HOH 411 1011 1097 HOH HOH B . 
E 3 HOH 412 1012 1011 HOH HOH B . 
E 3 HOH 413 1013 1146 HOH HOH B . 
E 3 HOH 414 1014 987  HOH HOH B . 
E 3 HOH 415 1015 1047 HOH HOH B . 
E 3 HOH 416 1016 710  HOH HOH B . 
E 3 HOH 417 1017 1453 HOH HOH B . 
E 3 HOH 418 1018 416  HOH HOH B . 
E 3 HOH 419 1019 1004 HOH HOH B . 
E 3 HOH 420 1020 1412 HOH HOH B . 
E 3 HOH 421 1021 1280 HOH HOH B . 
E 3 HOH 422 1022 669  HOH HOH B . 
E 3 HOH 423 1023 708  HOH HOH B . 
E 3 HOH 424 1024 319  HOH HOH B . 
E 3 HOH 425 1025 379  HOH HOH B . 
E 3 HOH 426 1026 774  HOH HOH B . 
E 3 HOH 427 1027 418  HOH HOH B . 
E 3 HOH 428 1028 1408 HOH HOH B . 
E 3 HOH 429 1029 983  HOH HOH B . 
E 3 HOH 430 1030 1484 HOH HOH B . 
E 3 HOH 431 1031 1150 HOH HOH B . 
E 3 HOH 432 1032 976  HOH HOH B . 
E 3 HOH 433 1033 1241 HOH HOH B . 
E 3 HOH 434 1034 1401 HOH HOH B . 
E 3 HOH 435 1035 984  HOH HOH B . 
E 3 HOH 436 1036 295  HOH HOH B . 
E 3 HOH 437 1037 1006 HOH HOH B . 
E 3 HOH 438 1038 877  HOH HOH B . 
E 3 HOH 439 1039 1225 HOH HOH B . 
E 3 HOH 440 1040 1157 HOH HOH B . 
E 3 HOH 441 1041 569  HOH HOH B . 
E 3 HOH 442 1042 1098 HOH HOH B . 
E 3 HOH 443 1043 588  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 225 ? CD  ? A LYS 2   CD  
2  1 Y 1 A LYS 225 ? CE  ? A LYS 2   CE  
3  1 Y 1 A LYS 225 ? NZ  ? A LYS 2   NZ  
4  1 Y 1 A ASP 255 ? OD1 ? A ASP 32  OD1 
5  1 Y 1 A ASP 255 ? OD2 ? A ASP 32  OD2 
6  1 Y 1 A ASN 295 ? CG  ? A ASN 72  CG  
7  1 Y 1 A ASN 295 ? OD1 ? A ASN 72  OD1 
8  1 Y 1 A ASN 295 ? ND2 ? A ASN 72  ND2 
9  1 Y 1 A SER 346 ? OG  ? A SER 123 OG  
10 1 Y 1 B SER 224 ? OG  ? B SER 1   OG  
11 1 Y 1 B THR 312 ? OG1 ? B THR 89  OG1 
12 1 Y 1 B THR 312 ? CG2 ? B THR 89  CG2 
13 1 Y 1 B GLU 343 ? OE1 ? B GLU 120 OE1 
14 1 Y 1 B GLU 343 ? OE2 ? B GLU 120 OE2 
15 1 Y 1 B THR 382 ? CB  ? B THR 159 CB  
16 1 Y 1 B THR 382 ? OG1 ? B THR 159 OG1 
17 1 Y 1 B THR 382 ? CG2 ? B THR 159 CG2 
18 1 Y 1 B ASP 383 ? CG  ? B ASP 160 CG  
19 1 Y 1 B ASP 383 ? OD1 ? B ASP 160 OD1 
20 1 Y 1 B ASP 383 ? OD2 ? B ASP 160 OD2 
21 1 Y 1 B LEU 415 ? CG  ? B LEU 192 CG  
22 1 Y 1 B LEU 415 ? CD1 ? B LEU 192 CD1 
23 1 Y 1 B LEU 415 ? CD2 ? B LEU 192 CD2 
# 
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  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.34 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EDO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.150 
_cell.length_a_esd                 ? 
_cell.length_b                     90.560 
_cell.length_b_esd                 ? 
_cell.length_c                     67.120 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9EDO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EDO 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.97 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    
;0.17 M ammonium sulfate, 
25.5% w/v PEG 4000
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-07-20 
_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   0.95374 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95374 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EDO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.42 
_reflns.d_resolution_low                               49.09 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     109595 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.49 
_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                                0.093 
_reflns.pdbx_Rpim_I_all                                0.038 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       623429 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.085 
_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                                    1.42 
_reflns_shell.d_res_low                                     1.44 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           26748 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4837 
_reflns_shell.percent_possible_obs                          88.0 
_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                               5.5 
_reflns_shell.pdbx_chi_squared                              0.33 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.7 
_reflns_shell.pdbx_Rrim_I_all                               0.763 
_reflns_shell.pdbx_Rpim_I_all                               0.311 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.861 
_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                                  0.695 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EDO 
_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                            1.42 
_refine.ls_d_res_low                             49.08 
_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                     109563 
_refine.ls_number_reflns_R_free                  5479 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.51 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1354 
_refine.ls_R_factor_R_free                       0.1746 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1334 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.35 
_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       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 16.57 
_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                            0.13 
_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                       1.42 
_refine_hist.d_res_low                        49.08 
_refine_hist.number_atoms_solvent             931 
_refine_hist.number_atoms_total               5723 
_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        4791 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         1 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005  ? 5217 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.774  ? 7179 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.774 ? 1937 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.080  ? 761  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 973  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 1.42 1.44  . . 157 2970 86.00  . . . . 0.1923 . . . . . . . . . . . . . . . 0.2591 
'X-RAY DIFFRACTION' 1.44 1.45  . . 183 3492 100.00 . . . . 0.1753 . . . . . . . . . . . . . . . 0.1938 
'X-RAY DIFFRACTION' 1.45 1.47  . . 183 3469 100.00 . . . . 0.1589 . . . . . . . . . . . . . . . 0.2077 
'X-RAY DIFFRACTION' 1.47 1.49  . . 182 3463 100.00 . . . . 0.1575 . . . . . . . . . . . . . . . 0.2082 
'X-RAY DIFFRACTION' 1.49 1.51  . . 184 3496 100.00 . . . . 0.1513 . . . . . . . . . . . . . . . 0.1872 
'X-RAY DIFFRACTION' 1.51 1.53  . . 182 3460 100.00 . . . . 0.1548 . . . . . . . . . . . . . . . 0.2035 
'X-RAY DIFFRACTION' 1.53 1.55  . . 184 3482 100.00 . . . . 0.1581 . . . . . . . . . . . . . . . 0.2169 
'X-RAY DIFFRACTION' 1.55 1.58  . . 181 3454 100.00 . . . . 0.1469 . . . . . . . . . . . . . . . 0.1851 
'X-RAY DIFFRACTION' 1.58 1.60  . . 187 3546 100.00 . . . . 0.1460 . . . . . . . . . . . . . . . 0.2033 
'X-RAY DIFFRACTION' 1.60 1.63  . . 180 3427 100.00 . . . . 0.1447 . . . . . . . . . . . . . . . 0.2002 
'X-RAY DIFFRACTION' 1.63 1.65  . . 183 3465 100.00 . . . . 0.1344 . . . . . . . . . . . . . . . 0.1843 
'X-RAY DIFFRACTION' 1.65 1.69  . . 184 3495 100.00 . . . . 0.1291 . . . . . . . . . . . . . . . 0.1738 
'X-RAY DIFFRACTION' 1.69 1.72  . . 182 3459 100.00 . . . . 0.1279 . . . . . . . . . . . . . . . 0.1757 
'X-RAY DIFFRACTION' 1.72 1.75  . . 184 3502 100.00 . . . . 0.1232 . . . . . . . . . . . . . . . 0.1778 
'X-RAY DIFFRACTION' 1.75 1.79  . . 182 3461 100.00 . . . . 0.1255 . . . . . . . . . . . . . . . 0.1458 
'X-RAY DIFFRACTION' 1.79 1.83  . . 184 3486 100.00 . . . . 0.1315 . . . . . . . . . . . . . . . 0.1805 
'X-RAY DIFFRACTION' 1.83 1.88  . . 183 3484 100.00 . . . . 0.1392 . . . . . . . . . . . . . . . 0.1858 
'X-RAY DIFFRACTION' 1.88 1.93  . . 184 3499 100.00 . . . . 0.1427 . . . . . . . . . . . . . . . 0.1852 
'X-RAY DIFFRACTION' 1.93 1.99  . . 183 3471 100.00 . . . . 0.1333 . . . . . . . . . . . . . . . 0.1574 
'X-RAY DIFFRACTION' 1.99 2.05  . . 185 3506 100.00 . . . . 0.1321 . . . . . . . . . . . . . . . 0.1637 
'X-RAY DIFFRACTION' 2.05 2.12  . . 182 3471 100.00 . . . . 0.1343 . . . . . . . . . . . . . . . 0.1684 
'X-RAY DIFFRACTION' 2.12 2.21  . . 184 3482 100.00 . . . . 0.1321 . . . . . . . . . . . . . . . 0.1673 
'X-RAY DIFFRACTION' 2.21 2.31  . . 183 3481 100.00 . . . . 0.1384 . . . . . . . . . . . . . . . 0.1875 
'X-RAY DIFFRACTION' 2.31 2.43  . . 183 3481 100.00 . . . . 0.1395 . . . . . . . . . . . . . . . 0.1722 
'X-RAY DIFFRACTION' 2.43 2.58  . . 185 3523 100.00 . . . . 0.1477 . . . . . . . . . . . . . . . 0.2026 
'X-RAY DIFFRACTION' 2.58 2.78  . . 183 3463 100.00 . . . . 0.1463 . . . . . . . . . . . . . . . 0.1717 
'X-RAY DIFFRACTION' 2.78 3.06  . . 184 3504 100.00 . . . . 0.1385 . . . . . . . . . . . . . . . 0.1877 
'X-RAY DIFFRACTION' 3.06 3.50  . . 185 3510 100.00 . . . . 0.1239 . . . . . . . . . . . . . . . 0.1791 
'X-RAY DIFFRACTION' 3.50 4.41  . . 184 3504 100.00 . . . . 0.1059 . . . . . . . . . . . . . . . 0.1369 
'X-RAY DIFFRACTION' 4.42 49.08 . . 189 3578 100.00 . . . . 0.1260 . . . . . . . . . . . . . . . 0.1693 
# 
_struct.entry_id                     9EDO 
_struct.title                        'GII.27: Loreto0959 norovirus protruding domain' 
_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        9EDO 
_struct_keywords.text            'norovirus, P domain, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A2H4Y8Z8_9CALI 
_struct_ref.pdbx_db_accession          A0A2H4Y8Z8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;KPFTIPILTIGEMTNSRFPVAIDMLHTSPTDNFIVQPQNGRCTLDGELQGTTQLVASNICAFRGSISGHENNGDQHQWHF
SITNPNGTPFDPTEDVPAPLGTPDFKGQLYGVISQRNREGSSGNGNQKANRSHEGVISTVAPRFTPKLGSVMIGTWTTDD
IQDQPSRFTPVGLNDDDNYKQWELPNYSGALTLNMGLAPSVFPTYPGEQLLFFRSYIPMKGGYGSPYIDCLIPQEWISHF
YQESAPSQTDVALIRYVNPDTGRVLFEAKLHRQGYITVAKTGDSPINVPANGYFRFDSWVSQFYSLAPM
;
_struct_ref.pdbx_align_begin           225 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9EDO A 2 ? 310 ? A0A2H4Y8Z8 225 ? 533 ? 225 533 
2 1 9EDO B 2 ? 310 ? A0A2H4Y8Z8 225 ? 533 ? 225 533 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9EDO SER A 1 ? UNP A0A2H4Y8Z8 ? ? 'expression tag' 224 1 
2 9EDO SER B 1 ? UNP A0A2H4Y8Z8 ? ? 'expression tag' 224 2 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 3710  ? 
1 MORE         -19   ? 
1 'SSA (A^2)'  24050 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 THR A 10  ? MET A 14  ? THR A 233 MET A 237 5 ? 5  
HELX_P HELX_P2  AA2 VAL A 56  ? ILE A 60  ? VAL A 279 ILE A 283 5 ? 5  
HELX_P HELX_P3  AA3 SER A 122 ? GLY A 126 ? SER A 345 GLY A 349 5 ? 5  
HELX_P HELX_P4  AA4 THR A 146 ? LEU A 149 ? THR A 369 LEU A 372 5 ? 4  
HELX_P HELX_P5  AA5 PRO A 234 ? SER A 245 ? PRO A 457 SER A 468 1 ? 12 
HELX_P HELX_P6  AA6 THR B 10  ? MET B 14  ? THR B 233 MET B 237 5 ? 5  
HELX_P HELX_P7  AA7 VAL B 56  ? ILE B 60  ? VAL B 279 ILE B 283 5 ? 5  
HELX_P HELX_P8  AA8 THR B 146 ? LEU B 149 ? THR B 369 LEU B 372 5 ? 4  
HELX_P HELX_P9  AA9 SER B 189 ? THR B 193 ? SER B 412 THR B 416 5 ? 5  
HELX_P HELX_P10 AB1 PRO B 234 ? SER B 245 ? PRO B 457 SER B 468 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ASN 
_struct_mon_prot_cis.label_seq_id           73 
_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            296 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   GLY 
_struct_mon_prot_cis.pdbx_label_seq_id_2    74 
_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    GLY 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     297 
_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       -2.74 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 7 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? 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 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 228 ? CYS A 231 ? TYR A 451 CYS A 454 
AA1 2 GLU A 209 ? TYR A 217 ? GLU A 432 TYR A 440 
AA1 3 MET A 25  ? THR A 28  ? MET A 248 THR A 251 
AA1 4 SER A 285 ? PRO A 286 ? SER A 508 PRO A 509 
AA2 1 TYR A 228 ? CYS A 231 ? TYR A 451 CYS A 454 
AA2 2 GLU A 209 ? TYR A 217 ? GLU A 432 TYR A 440 
AA2 3 TYR A 276 ? ALA A 280 ? TYR A 499 ALA A 503 
AA2 4 VAL A 265 ? HIS A 272 ? VAL A 488 HIS A 495 
AA2 5 VAL A 252 ? VAL A 258 ? VAL A 475 VAL A 481 
AA2 6 TYR A 294 ? VAL A 301 ? TYR A 517 VAL A 524 
AA3 1 PHE A 63  ? HIS A 70  ? PHE A 286 HIS A 293 
AA3 2 GLN A 78  ? ILE A 83  ? GLN A 301 ILE A 306 
AA3 3 SER A 151 ? THR A 156 ? SER A 374 THR A 379 
AA3 4 ASN A 131 ? SER A 139 ? ASN A 354 SER A 362 
AA3 5 GLN A 109 ? ARG A 117 ? GLN A 332 ARG A 340 
AA3 6 PRO A 166 ? LEU A 174 ? PRO A 389 LEU A 397 
AA3 7 PHE A 63  ? HIS A 70  ? PHE A 286 HIS A 293 
AA4 1 TYR B 228 ? CYS B 231 ? TYR B 451 CYS B 454 
AA4 2 GLN B 210 ? TYR B 217 ? GLN B 433 TYR B 440 
AA4 3 MET B 25  ? THR B 28  ? MET B 248 THR B 251 
AA4 4 SER B 285 ? ILE B 287 ? SER B 508 ILE B 510 
AA5 1 TYR B 228 ? CYS B 231 ? TYR B 451 CYS B 454 
AA5 2 GLN B 210 ? TYR B 217 ? GLN B 433 TYR B 440 
AA5 3 TYR B 276 ? VAL B 279 ? TYR B 499 VAL B 502 
AA5 4 VAL B 265 ? HIS B 272 ? VAL B 488 HIS B 495 
AA5 5 VAL B 252 ? VAL B 258 ? VAL B 475 VAL B 481 
AA5 6 TYR B 294 ? VAL B 301 ? TYR B 517 VAL B 524 
AA6 1 PHE B 63  ? ILE B 67  ? PHE B 286 ILE B 290 
AA6 2 GLN B 78  ? ILE B 83  ? GLN B 301 ILE B 306 
AA6 3 SER B 151 ? THR B 156 ? SER B 374 THR B 379 
AA6 4 ASN B 131 ? SER B 139 ? ASN B 354 SER B 362 
AA6 5 GLN B 109 ? ARG B 117 ? GLN B 332 ARG B 340 
AA6 6 PRO B 166 ? LEU B 174 ? PRO B 389 LEU B 397 
AA6 7 PHE B 63  ? ILE B 67  ? PHE B 286 ILE B 290 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O CYS A 231 ? O CYS A 454 N PHE A 214 ? N PHE A 437 
AA1 2 3 O PHE A 213 ? O PHE A 436 N HIS A 27  ? N HIS A 250 
AA1 3 4 N THR A 28  ? N THR A 251 O SER A 285 ? O SER A 508 
AA2 1 2 O CYS A 231 ? O CYS A 454 N PHE A 214 ? N PHE A 437 
AA2 2 3 N GLN A 210 ? N GLN A 433 O VAL A 279 ? O VAL A 502 
AA2 3 4 O TYR A 276 ? O TYR A 499 N HIS A 272 ? N HIS A 495 
AA2 4 5 O LEU A 271 ? O LEU A 494 N ALA A 253 ? N ALA A 476 
AA2 5 6 N LEU A 254 ? N LEU A 477 O SER A 299 ? O SER A 522 
AA3 1 2 N GLY A 69  ? N GLY A 292 O HIS A 80  ? O HIS A 303 
AA3 2 3 N PHE A 81  ? N PHE A 304 O VAL A 152 ? O VAL A 375 
AA3 3 4 O GLY A 155 ? O GLY A 378 N VAL A 137 ? N VAL A 360 
AA3 4 5 O ILE A 138 ? O ILE A 361 N LEU A 110 ? N LEU A 333 
AA3 5 6 N SER A 115 ? N SER A 338 O ARG A 168 ? O ARG A 391 
AA3 6 7 O PHE A 169 ? O PHE A 392 N PHE A 63  ? N PHE A 286 
AA4 1 2 O CYS B 231 ? O CYS B 454 N PHE B 214 ? N PHE B 437 
AA4 2 3 O PHE B 213 ? O PHE B 436 N HIS B 27  ? N HIS B 250 
AA4 3 4 N THR B 28  ? N THR B 251 O SER B 285 ? O SER B 508 
AA5 1 2 O CYS B 231 ? O CYS B 454 N PHE B 214 ? N PHE B 437 
AA5 2 3 N LEU B 212 ? N LEU B 435 O ILE B 277 ? O ILE B 500 
AA5 3 4 O TYR B 276 ? O TYR B 499 N HIS B 272 ? N HIS B 495 
AA5 4 5 O LEU B 271 ? O LEU B 494 N ALA B 253 ? N ALA B 476 
AA5 5 6 N LEU B 254 ? N LEU B 477 O SER B 299 ? O SER B 522 
AA6 1 2 N SER B 66  ? N SER B 289 O SER B 82  ? O SER B 305 
AA6 2 3 N PHE B 81  ? N PHE B 304 O VAL B 152 ? O VAL B 375 
AA6 3 4 O GLY B 155 ? O GLY B 378 N VAL B 137 ? N VAL B 360 
AA6 4 5 O ILE B 138 ? O ILE B 361 N LEU B 110 ? N LEU B 333 
AA6 5 6 N SER B 115 ? N SER B 338 O ARG B 168 ? O ARG B 391 
AA6 6 7 O PHE B 169 ? O PHE B 392 N PHE B 63  ? N PHE B 286 
# 
_pdbx_entry_details.entry_id                   9EDO 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    907 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    964 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
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 ASN A 296 ? ? -168.63 104.52 
2 1 THR A 428 ? ? -130.33 -39.41 
3 1 GLN B 351 ? ? 61.61   65.38  
4 1 ASP B 383 ? ? -132.26 -57.24 
5 1 ASP B 384 ? ? -80.42  47.57  
# 
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 SER 224 ? A SER 1   
2 1 Y 1 A LEU 415 ? A LEU 192 
3 1 Y 1 B GLY 347 ? B GLY 124 
4 1 Y 1 B ASN 348 ? B ASN 125 
5 1 Y 1 B GLY 349 ? B GLY 126 
# 
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  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4OOS 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EDO 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.019550 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005732 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011042 
_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]   0.015526 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LYS A 1 2   ? 10.226  5.503   40.960  1.00 53.56  ? 225  LYS A N   1 
ATOM   2    C  CA  . LYS A 1 2   ? 9.917   4.632   42.094  1.00 52.66  ? 225  LYS A CA  1 
ATOM   3    C  C   . LYS A 1 2   ? 8.502   4.020   42.044  1.00 49.65  ? 225  LYS A C   1 
ATOM   4    O  O   . LYS A 1 2   ? 8.375   2.797   42.072  1.00 50.17  ? 225  LYS A O   1 
ATOM   5    C  CB  . LYS A 1 2   ? 10.204  5.334   43.434  1.00 53.81  ? 225  LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 2   ? 9.971   4.472   44.664  1.00 47.27  ? 225  LYS A CG  1 
ATOM   7    N  N   . PRO A 1 3   ? 7.447   4.840   41.956  1.00 45.87  ? 226  PRO A N   1 
ATOM   8    C  CA  . PRO A 1 3   ? 6.094   4.268   41.909  1.00 43.63  ? 226  PRO A CA  1 
ATOM   9    C  C   . PRO A 1 3   ? 5.852   3.533   40.598  1.00 41.23  ? 226  PRO A C   1 
ATOM   10   O  O   . PRO A 1 3   ? 6.293   3.964   39.529  1.00 42.27  ? 226  PRO A O   1 
ATOM   11   C  CB  . PRO A 1 3   ? 5.179   5.495   42.027  1.00 43.47  ? 226  PRO A CB  1 
ATOM   12   C  CG  . PRO A 1 3   ? 6.059   6.598   42.519  1.00 44.62  ? 226  PRO A CG  1 
ATOM   13   C  CD  . PRO A 1 3   ? 7.394   6.312   41.921  1.00 45.40  ? 226  PRO A CD  1 
ATOM   14   N  N   . PHE A 1 4   ? 5.128   2.420   40.692  1.00 37.88  ? 227  PHE A N   1 
ATOM   15   C  CA  . PHE A 1 4   ? 4.911   1.531   39.557  1.00 35.08  ? 227  PHE A CA  1 
ATOM   16   C  C   . PHE A 1 4   ? 3.662   1.938   38.779  1.00 34.70  ? 227  PHE A C   1 
ATOM   17   O  O   . PHE A 1 4   ? 2.626   2.264   39.365  1.00 36.26  ? 227  PHE A O   1 
ATOM   18   C  CB  . PHE A 1 4   ? 4.771   0.093   40.062  1.00 33.22  ? 227  PHE A CB  1 
ATOM   19   C  CG  . PHE A 1 4   ? 4.595   -0.920  38.968  1.00 30.07  ? 227  PHE A CG  1 
ATOM   20   C  CD1 . PHE A 1 4   ? 5.663   -1.286  38.167  1.00 30.08  ? 227  PHE A CD1 1 
ATOM   21   C  CD2 . PHE A 1 4   ? 3.363   -1.508  38.740  1.00 30.72  ? 227  PHE A CD2 1 
ATOM   22   C  CE1 . PHE A 1 4   ? 5.499   -2.209  37.148  1.00 29.29  ? 227  PHE A CE1 1 
ATOM   23   C  CE2 . PHE A 1 4   ? 3.196   -2.437  37.728  1.00 30.02  ? 227  PHE A CE2 1 
ATOM   24   C  CZ  . PHE A 1 4   ? 4.265   -2.788  36.932  1.00 28.61  ? 227  PHE A CZ  1 
ATOM   25   N  N   . THR A 1 5   ? 3.763   1.905   37.446  1.00 32.49  ? 228  THR A N   1 
ATOM   26   C  CA  . THR A 1 5   ? 2.652   2.268   36.574  1.00 30.49  ? 228  THR A CA  1 
ATOM   27   C  C   . THR A 1 5   ? 2.577   1.331   35.374  1.00 28.07  ? 228  THR A C   1 
ATOM   28   O  O   . THR A 1 5   ? 3.574   0.752   34.938  1.00 28.47  ? 228  THR A O   1 
ATOM   29   C  CB  . THR A 1 5   ? 2.768   3.707   36.045  1.00 31.41  ? 228  THR A CB  1 
ATOM   30   O  OG1 . THR A 1 5   ? 4.009   3.864   35.346  1.00 32.47  ? 228  THR A OG1 1 
ATOM   31   C  CG2 . THR A 1 5   ? 2.693   4.713   37.182  1.00 31.32  ? 228  THR A CG2 1 
ATOM   32   N  N   . ILE A 1 6   ? 1.367   1.210   34.839  1.00 26.72  ? 229  ILE A N   1 
ATOM   33   C  CA  . ILE A 1 6   ? 1.089   0.491   33.599  1.00 25.63  ? 229  ILE A CA  1 
ATOM   34   C  C   . ILE A 1 6   ? 0.614   1.496   32.553  1.00 24.70  ? 229  ILE A C   1 
ATOM   35   O  O   . ILE A 1 6   ? -0.200  2.373   32.873  1.00 25.93  ? 229  ILE A O   1 
ATOM   36   C  CB  . ILE A 1 6   ? 0.032   -0.592  33.839  1.00 27.58  ? 229  ILE A CB  1 
ATOM   37   C  CG1 . ILE A 1 6   ? 0.562   -1.619  34.841  1.00 30.05  ? 229  ILE A CG1 1 
ATOM   38   C  CG2 . ILE A 1 6   ? -0.367  -1.257  32.534  1.00 28.75  ? 229  ILE A CG2 1 
ATOM   39   C  CD1 . ILE A 1 6   ? -0.387  -2.719  35.076  1.00 32.00  ? 229  ILE A CD1 1 
ATOM   40   N  N   . PRO A 1 7   ? 1.085   1.412   31.306  1.00 22.18  ? 230  PRO A N   1 
ATOM   41   C  CA  . PRO A 1 7   ? 0.672   2.390   30.290  1.00 22.18  ? 230  PRO A CA  1 
ATOM   42   C  C   . PRO A 1 7   ? -0.834  2.383   30.070  1.00 24.55  ? 230  PRO A C   1 
ATOM   43   O  O   . PRO A 1 7   ? -1.494  1.345   30.156  1.00 24.93  ? 230  PRO A O   1 
ATOM   44   C  CB  . PRO A 1 7   ? 1.411   1.919   29.030  1.00 22.81  ? 230  PRO A CB  1 
ATOM   45   C  CG  . PRO A 1 7   ? 2.568   1.131   29.546  1.00 23.46  ? 230  PRO A CG  1 
ATOM   46   C  CD  . PRO A 1 7   ? 2.087   0.463   30.789  1.00 22.19  ? 230  PRO A CD  1 
ATOM   47   N  N   . ILE A 1 8   ? -1.381  3.565   29.791  1.00 23.87  ? 231  ILE A N   1 
ATOM   48   C  CA  . ILE A 1 8   ? -2.802  3.701   29.468  1.00 24.16  ? 231  ILE A CA  1 
ATOM   49   C  C   . ILE A 1 8   ? -2.927  3.524   27.959  1.00 23.74  ? 231  ILE A C   1 
ATOM   50   O  O   . ILE A 1 8   ? -2.870  4.477   27.182  1.00 25.49  ? 231  ILE A O   1 
ATOM   51   C  CB  . ILE A 1 8   ? -3.386  5.019   29.963  1.00 27.33  ? 231  ILE A CB  1 
ATOM   52   C  CG1 . ILE A 1 8   ? -3.203  5.139   31.480  1.00 29.91  ? 231  ILE A CG1 1 
ATOM   53   C  CG2 . ILE A 1 8   ? -4.864  5.107   29.607  1.00 31.04  ? 231  ILE A CG2 1 
ATOM   54   C  CD1 . ILE A 1 8   ? -3.894  6.349   32.086  1.00 32.76  ? 231  ILE A CD1 1 
ATOM   55   N  N   . LEU A 1 9   ? -3.080  2.273   27.542  1.00 21.32  ? 232  LEU A N   1 
ATOM   56   C  CA  . LEU A 1 9   ? -3.183  1.901   26.140  1.00 19.32  ? 232  LEU A CA  1 
ATOM   57   C  C   . LEU A 1 9   ? -4.193  0.770   26.046  1.00 19.66  ? 232  LEU A C   1 
ATOM   58   O  O   . LEU A 1 9   ? -4.121  -0.188  26.822  1.00 19.75  ? 232  LEU A O   1 
ATOM   59   C  CB  . LEU A 1 9   ? -1.826  1.414   25.607  1.00 20.28  ? 232  LEU A CB  1 
ATOM   60   C  CG  . LEU A 1 9   ? -0.673  2.418   25.499  1.00 19.54  ? 232  LEU A CG  1 
ATOM   61   C  CD1 . LEU A 1 9   ? 0.645   1.698   25.225  1.00 21.81  ? 232  LEU A CD1 1 
ATOM   62   C  CD2 . LEU A 1 9   ? -0.974  3.457   24.415  1.00 22.62  ? 232  LEU A CD2 1 
ATOM   63   N  N   . THR A 1 10  ? -5.130  0.888   25.108  1.00 17.85  ? 233  THR A N   1 
ATOM   64   C  CA  . THR A 1 10  ? -6.060  -0.193  24.821  1.00 19.51  ? 233  THR A CA  1 
ATOM   65   C  C   . THR A 1 10  ? -5.312  -1.312  24.108  1.00 19.07  ? 233  THR A C   1 
ATOM   66   O  O   . THR A 1 10  ? -4.183  -1.134  23.642  1.00 19.79  ? 233  THR A O   1 
ATOM   67   C  CB  . THR A 1 10  ? -7.200  0.307   23.936  1.00 20.43  ? 233  THR A CB  1 
ATOM   68   O  OG1 . THR A 1 10  ? -6.677  0.631   22.644  1.00 20.87  ? 233  THR A OG1 1 
ATOM   69   C  CG2 . THR A 1 10  ? -7.853  1.557   24.529  1.00 21.66  ? 233  THR A CG2 1 
ATOM   70   N  N   . ILE A 1 11  ? -5.940  -2.488  24.025  1.00 20.46  ? 234  ILE A N   1 
ATOM   71   C  CA  . ILE A 1 11  ? -5.239  -3.613  23.408  1.00 21.79  ? 234  ILE A CA  1 
ATOM   72   C  C   . ILE A 1 11  ? -5.000  -3.355  21.925  1.00 19.15  ? 234  ILE A C   1 
ATOM   73   O  O   . ILE A 1 11  ? -3.975  -3.769  21.371  1.00 18.84  ? 234  ILE A O   1 
ATOM   74   C  CB  . ILE A 1 11  ? -5.933  -4.963  23.676  1.00 27.11  ? 234  ILE A CB  1 
ATOM   75   C  CG1 . ILE A 1 11  ? -7.363  -4.976  23.144  1.00 27.54  ? 234  ILE A CG1 1 
ATOM   76   C  CG2 . ILE A 1 11  ? -5.890  -5.311  25.154  1.00 29.55  ? 234  ILE A CG2 1 
ATOM   77   C  CD1 . ILE A 1 11  ? -8.012  -6.333  23.225  1.00 28.60  ? 234  ILE A CD1 1 
ATOM   78   N  N   . GLY A 1 12  ? -5.922  -2.648  21.264  1.00 18.42  ? 235  GLY A N   1 
ATOM   79   C  CA  . GLY A 1 12  ? -5.710  -2.286  19.874  1.00 16.95  ? 235  GLY A CA  1 
ATOM   80   C  C   . GLY A 1 12  ? -4.623  -1.254  19.660  1.00 15.70  ? 235  GLY A C   1 
ATOM   81   O  O   . GLY A 1 12  ? -4.202  -1.053  18.512  1.00 17.29  ? 235  GLY A O   1 
ATOM   82   N  N   . GLU A 1 13  ? -4.169  -0.605  20.736  1.00 15.74  ? 236  GLU A N   1 
ATOM   83   C  CA  . GLU A 1 13  ? -3.050  0.325   20.730  1.00 15.80  ? 236  GLU A CA  1 
ATOM   84   C  C   . GLU A 1 13  ? -1.728  -0.326  21.138  1.00 15.87  ? 236  GLU A C   1 
ATOM   85   O  O   . GLU A 1 13  ? -0.745  0.384   21.376  1.00 18.55  ? 236  GLU A O   1 
ATOM   86   C  CB  . GLU A 1 13  ? -3.366  1.498   21.657  1.00 16.97  ? 236  GLU A CB  1 
ATOM   87   C  CG  . GLU A 1 13  ? -4.508  2.355   21.148  1.00 17.67  ? 236  GLU A CG  1 
ATOM   88   C  CD  . GLU A 1 13  ? -4.976  3.394   22.150  1.00 20.17  ? 236  GLU A CD  1 
ATOM   89   O  OE1 . GLU A 1 13  ? -4.688  3.254   23.353  1.00 20.75  ? 236  GLU A OE1 1 
ATOM   90   O  OE2 . GLU A 1 13  ? -5.638  4.365   21.726  1.00 22.02  ? 236  GLU A OE2 1 
ATOM   91   N  N   . MET A 1 14  ? -1.671  -1.651  21.211  1.00 14.50  ? 237  MET A N   1 
ATOM   92   C  CA  . MET A 1 14  ? -0.475  -2.330  21.689  1.00 14.40  ? 237  MET A CA  1 
ATOM   93   C  C   . MET A 1 14  ? -0.096  -3.470  20.761  1.00 13.75  ? 237  MET A C   1 
ATOM   94   O  O   . MET A 1 14  ? -0.908  -3.946  19.957  1.00 13.96  ? 237  MET A O   1 
ATOM   95   C  CB  . MET A 1 14  ? -0.644  -2.823  23.122  1.00 17.45  ? 237  MET A CB  1 
ATOM   96   C  CG  . MET A 1 14  ? -0.734  -1.676  24.105  1.00 17.51  ? 237  MET A CG  1 
ATOM   97   S  SD  . MET A 1 14  ? -0.611  -2.231  25.816  1.00 18.91  ? 237  MET A SD  1 
ATOM   98   C  CE  . MET A 1 14  ? -2.103  -3.224  25.965  1.00 19.17  ? 237  MET A CE  1 
ATOM   99   N  N   . THR A 1 15  ? 1.158   -3.894  20.884  1.00 12.59  ? 238  THR A N   1 
ATOM   100  C  CA  . THR A 1 15  ? 1.767   -4.854  19.975  1.00 11.75  ? 238  THR A CA  1 
ATOM   101  C  C   . THR A 1 15  ? 2.067   -6.149  20.710  1.00 12.24  ? 238  THR A C   1 
ATOM   102  O  O   . THR A 1 15  ? 2.550   -6.133  21.846  1.00 12.65  ? 238  THR A O   1 
ATOM   103  C  CB  . THR A 1 15  ? 3.075   -4.291  19.400  1.00 12.31  ? 238  THR A CB  1 
ATOM   104  O  OG1 . THR A 1 15  ? 2.813   -2.991  18.867  1.00 13.36  ? 238  THR A OG1 1 
ATOM   105  C  CG2 . THR A 1 15  ? 3.625   -5.169  18.279  1.00 13.80  ? 238  THR A CG2 1 
ATOM   106  N  N   . ASN A 1 16  ? 1.787   -7.265  20.050  1.00 11.49  ? 239  ASN A N   1 
ATOM   107  C  CA  . ASN A 1 16  ? 2.202   -8.560  20.570  1.00 11.29  ? 239  ASN A CA  1 
ATOM   108  C  C   . ASN A 1 16  ? 3.722   -8.591  20.685  1.00 10.51  ? 239  ASN A C   1 
ATOM   109  O  O   . ASN A 1 16  ? 4.432   -8.137  19.785  1.00 12.35  ? 239  ASN A O   1 
ATOM   110  C  CB  . ASN A 1 16  ? 1.727   -9.637  19.590  1.00 12.46  ? 239  ASN A CB  1 
ATOM   111  C  CG  . ASN A 1 16  ? 1.676   -11.016 20.219  1.00 12.63  ? 239  ASN A CG  1 
ATOM   112  O  OD1 . ASN A 1 16  ? 2.699   -11.592 20.581  1.00 12.13  ? 239  ASN A OD1 1 
ATOM   113  N  ND2 . ASN A 1 16  ? 0.474   -11.564 20.330  1.00 12.40  ? 239  ASN A ND2 1 
ATOM   114  N  N   . SER A 1 17  ? 4.224   -9.092  21.810  1.00 10.70  ? 240  SER A N   1 
ATOM   115  C  CA  . SER A 1 17  ? 5.669   -9.132  22.023  1.00 9.74   ? 240  SER A CA  1 
ATOM   116  C  C   . SER A 1 17  ? 6.330   -10.387 21.466  1.00 10.04  ? 240  SER A C   1 
ATOM   117  O  O   . SER A 1 17  ? 7.547   -10.552 21.605  1.00 10.87  ? 240  SER A O   1 
ATOM   118  C  CB  . SER A 1 17  ? 5.995   -8.935  23.498  1.00 11.62  ? 240  SER A CB  1 
ATOM   119  O  OG  . SER A 1 17  ? 5.313   -9.895  24.292  1.00 11.72  ? 240  SER A OG  1 
ATOM   120  N  N   . ARG A 1 18  ? 5.565   -11.263 20.818  1.00 10.85  ? 241  ARG A N   1 
ATOM   121  C  CA  . ARG A 1 18  ? 6.122   -12.454 20.190  1.00 10.85  ? 241  ARG A CA  1 
ATOM   122  C  C   . ARG A 1 18  ? 5.945   -12.478 18.680  1.00 11.34  ? 241  ARG A C   1 
ATOM   123  O  O   . ARG A 1 18  ? 6.468   -13.384 18.021  1.00 11.92  ? 241  ARG A O   1 
ATOM   124  C  CB  . ARG A 1 18  ? 5.529   -13.724 20.814  1.00 11.06  ? 241  ARG A CB  1 
ATOM   125  C  CG  . ARG A 1 18  ? 5.902   -13.888 22.279  1.00 10.88  ? 241  ARG A CG  1 
ATOM   126  C  CD  . ARG A 1 18  ? 5.300   -15.172 22.836  1.00 11.23  ? 241  ARG A CD  1 
ATOM   127  N  NE  . ARG A 1 18  ? 5.881   -16.357 22.209  1.00 11.15  ? 241  ARG A NE  1 
ATOM   128  C  CZ  . ARG A 1 18  ? 5.210   -17.471 21.947  1.00 10.79  ? 241  ARG A CZ  1 
ATOM   129  N  NH1 . ARG A 1 18  ? 3.947   -17.615 22.303  1.00 12.89  ? 241  ARG A NH1 1 
ATOM   130  N  NH2 . ARG A 1 18  ? 5.812   -18.451 21.273  1.00 12.97  ? 241  ARG A NH2 1 
ATOM   131  N  N   . PHE A 1 19  ? 5.243   -11.497 18.108  1.00 11.92  ? 242  PHE A N   1 
ATOM   132  C  CA  . PHE A 1 19  ? 5.130   -11.377 16.661  1.00 11.70  ? 242  PHE A CA  1 
ATOM   133  C  C   . PHE A 1 19  ? 4.716   -9.945  16.374  1.00 11.01  ? 242  PHE A C   1 
ATOM   134  O  O   . PHE A 1 19  ? 3.887   -9.404  17.117  1.00 12.65  ? 242  PHE A O   1 
ATOM   135  C  CB  . PHE A 1 19  ? 4.115   -12.358 16.053  1.00 11.15  ? 242  PHE A CB  1 
ATOM   136  C  CG  . PHE A 1 19  ? 4.284   -12.531 14.571  1.00 11.02  ? 242  PHE A CG  1 
ATOM   137  C  CD1 . PHE A 1 19  ? 5.268   -13.378 14.064  1.00 13.44  ? 242  PHE A CD1 1 
ATOM   138  C  CD2 . PHE A 1 19  ? 3.510   -11.792 13.681  1.00 11.61  ? 242  PHE A CD2 1 
ATOM   139  C  CE1 . PHE A 1 19  ? 5.445   -13.502 12.696  1.00 14.01  ? 242  PHE A CE1 1 
ATOM   140  C  CE2 . PHE A 1 19  ? 3.692   -11.922 12.317  1.00 13.39  ? 242  PHE A CE2 1 
ATOM   141  C  CZ  . PHE A 1 19  ? 4.660   -12.766 11.825  1.00 14.17  ? 242  PHE A CZ  1 
ATOM   142  N  N   . PRO A 1 20  ? 5.252   -9.296  15.321  1.00 11.78  ? 243  PRO A N   1 
ATOM   143  C  CA  . PRO A 1 20  ? 4.991   -7.842  15.146  1.00 12.26  ? 243  PRO A CA  1 
ATOM   144  C  C   . PRO A 1 20  ? 3.628   -7.529  14.541  1.00 13.71  ? 243  PRO A C   1 
ATOM   145  O  O   . PRO A 1 20  ? 3.500   -7.170  13.369  1.00 15.90  ? 243  PRO A O   1 
ATOM   146  C  CB  . PRO A 1 20  ? 6.157   -7.403  14.254  1.00 12.85  ? 243  PRO A CB  1 
ATOM   147  C  CG  . PRO A 1 20  ? 6.503   -8.631  13.463  1.00 11.80  ? 243  PRO A CG  1 
ATOM   148  C  CD  . PRO A 1 20  ? 6.313   -9.781  14.423  1.00 11.62  ? 243  PRO A CD  1 
ATOM   149  N  N   A VAL A 1 21  ? 2.596   -7.667  15.372  0.70 12.85  ? 244  VAL A N   1 
ATOM   150  N  N   B VAL A 1 21  ? 2.590   -7.658  15.373  0.30 12.66  ? 244  VAL A N   1 
ATOM   151  C  CA  A VAL A 1 21  ? 1.216   -7.380  15.014  0.70 13.57  ? 244  VAL A CA  1 
ATOM   152  C  CA  B VAL A 1 21  ? 1.197   -7.440  14.993  0.30 12.31  ? 244  VAL A CA  1 
ATOM   153  C  C   A VAL A 1 21  ? 0.522   -6.838  16.255  0.70 12.87  ? 244  VAL A C   1 
ATOM   154  C  C   B VAL A 1 21  ? 0.458   -6.938  16.231  0.30 12.00  ? 244  VAL A C   1 
ATOM   155  O  O   A VAL A 1 21  ? 0.916   -7.120  17.389  0.70 13.33  ? 244  VAL A O   1 
ATOM   156  O  O   B VAL A 1 21  ? 0.767   -7.345  17.356  0.30 12.19  ? 244  VAL A O   1 
ATOM   157  C  CB  A VAL A 1 21  ? 0.458   -8.621  14.484  0.70 14.90  ? 244  VAL A CB  1 
ATOM   158  C  CB  B VAL A 1 21  ? 0.554   -8.744  14.442  0.30 12.42  ? 244  VAL A CB  1 
ATOM   159  C  CG1 A VAL A 1 21  ? 0.915   -8.970  13.075  0.70 18.56  ? 244  VAL A CG1 1 
ATOM   160  C  CG1 B VAL A 1 21  ? -0.938  -8.581  14.232  0.30 9.64   ? 244  VAL A CG1 1 
ATOM   161  C  CG2 A VAL A 1 21  ? 0.632   -9.802  15.434  0.70 13.04  ? 244  VAL A CG2 1 
ATOM   162  C  CG2 B VAL A 1 21  ? 1.194   -9.174  13.129  0.30 15.47  ? 244  VAL A CG2 1 
ATOM   163  N  N   . ALA A 1 22  ? -0.513  -6.039  16.025  1.00 12.64  ? 245  ALA A N   1 
ATOM   164  C  CA  . ALA A 1 22  ? -1.327  -5.551  17.130  1.00 12.54  ? 245  ALA A CA  1 
ATOM   165  C  C   . ALA A 1 22  ? -2.009  -6.696  17.885  1.00 13.45  ? 245  ALA A C   1 
ATOM   166  O  O   . ALA A 1 22  ? -2.268  -7.772  17.344  1.00 13.72  ? 245  ALA A O   1 
ATOM   167  C  CB  . ALA A 1 22  ? -2.374  -4.558  16.624  1.00 13.70  ? 245  ALA A CB  1 
ATOM   168  N  N   . ILE A 1 23  ? -2.289  -6.457  19.170  1.00 12.94  ? 246  ILE A N   1 
ATOM   169  C  CA  . ILE A 1 23  ? -3.023  -7.432  19.968  1.00 13.34  ? 246  ILE A CA  1 
ATOM   170  C  C   . ILE A 1 23  ? -4.489  -7.429  19.544  1.00 15.12  ? 246  ILE A C   1 
ATOM   171  O  O   . ILE A 1 23  ? -5.103  -6.367  19.387  1.00 17.14  ? 246  ILE A O   1 
ATOM   172  C  CB  . ILE A 1 23  ? -2.861  -7.123  21.463  1.00 14.48  ? 246  ILE A CB  1 
ATOM   173  C  CG1 . ILE A 1 23  ? -1.396  -7.335  21.870  1.00 16.30  ? 246  ILE A CG1 1 
ATOM   174  C  CG2 . ILE A 1 23  ? -3.777  -8.030  22.302  1.00 14.53  ? 246  ILE A CG2 1 
ATOM   175  C  CD1 . ILE A 1 23  ? -0.993  -6.761  23.201  1.00 17.38  ? 246  ILE A CD1 1 
ATOM   176  N  N   . ASP A 1 24  ? -5.061  -8.621  19.361  1.00 14.36  ? 247  ASP A N   1 
ATOM   177  C  CA  . ASP A 1 24  ? -6.459  -8.742  18.960  1.00 15.41  ? 247  ASP A CA  1 
ATOM   178  C  C   . ASP A 1 24  ? -7.412  -8.909  20.138  1.00 15.67  ? 247  ASP A C   1 
ATOM   179  O  O   . ASP A 1 24  ? -8.517  -8.356  20.116  1.00 18.60  ? 247  ASP A O   1 
ATOM   180  C  CB  . ASP A 1 24  ? -6.632  -9.915  17.995  1.00 15.40  ? 247  ASP A CB  1 
ATOM   181  C  CG  . ASP A 1 24  ? -6.007  -9.650  16.649  1.00 16.63  ? 247  ASP A CG  1 
ATOM   182  O  OD1 . ASP A 1 24  ? -6.170  -8.521  16.133  1.00 19.63  ? 247  ASP A OD1 1 
ATOM   183  O  OD2 . ASP A 1 24  ? -5.355  -10.558 16.110  1.00 17.27  ? 247  ASP A OD2 1 
ATOM   184  N  N   . MET A 1 25  ? -7.034  -9.671  21.167  1.00 16.16  ? 248  MET A N   1 
ATOM   185  C  CA  A MET A 1 25  ? -7.940  -9.957  22.275  0.75 16.93  ? 248  MET A CA  1 
ATOM   186  C  CA  B MET A 1 25  ? -7.914  -9.832  22.321  0.25 17.47  ? 248  MET A CA  1 
ATOM   187  C  C   . MET A 1 25  ? -7.136  -10.458 23.469  1.00 16.87  ? 248  MET A C   1 
ATOM   188  O  O   . MET A 1 25  ? -5.965  -10.825 23.343  1.00 17.67  ? 248  MET A O   1 
ATOM   189  C  CB  A MET A 1 25  ? -8.960  -11.025 21.871  0.75 18.64  ? 248  MET A CB  1 
ATOM   190  C  CB  B MET A 1 25  ? -9.211  -10.603 22.031  0.25 20.09  ? 248  MET A CB  1 
ATOM   191  C  CG  A MET A 1 25  ? -8.351  -12.415 21.765  0.75 23.73  ? 248  MET A CG  1 
ATOM   192  C  CG  B MET A 1 25  ? -9.238  -11.477 20.789  0.25 22.68  ? 248  MET A CG  1 
ATOM   193  S  SD  A MET A 1 25  ? -9.357  -13.615 20.872  0.75 30.42  ? 248  MET A SD  1 
ATOM   194  S  SD  B MET A 1 25  ? -7.850  -12.603 20.661  0.25 23.80  ? 248  MET A SD  1 
ATOM   195  C  CE  A MET A 1 25  ? -9.440  -12.831 19.267  0.75 30.57  ? 248  MET A CE  1 
ATOM   196  C  CE  B MET A 1 25  ? -8.585  -13.895 19.673  0.25 23.51  ? 248  MET A CE  1 
ATOM   197  N  N   . LEU A 1 26  ? -7.800  -10.516 24.621  1.00 17.47  ? 249  LEU A N   1 
ATOM   198  C  CA  . LEU A 1 26  ? -7.293  -11.201 25.798  1.00 18.04  ? 249  LEU A CA  1 
ATOM   199  C  C   . LEU A 1 26  ? -7.896  -12.600 25.816  1.00 18.98  ? 249  LEU A C   1 
ATOM   200  O  O   . LEU A 1 26  ? -9.013  -12.818 25.341  1.00 20.34  ? 249  LEU A O   1 
ATOM   201  C  CB  . LEU A 1 26  ? -7.697  -10.458 27.072  1.00 18.96  ? 249  LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 26  ? -7.284  -8.990  27.140  1.00 20.43  ? 249  LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 26  ? -7.792  -8.345  28.417  1.00 21.50  ? 249  LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 26  ? -5.774  -8.874  27.041  1.00 22.16  ? 249  LEU A CD2 1 
ATOM   205  N  N   . HIS A 1 27  ? -7.145  -13.557 26.347  1.00 18.21  ? 250  HIS A N   1 
ATOM   206  C  CA  . HIS A 1 27  ? -7.642  -14.918 26.376  1.00 19.33  ? 250  HIS A CA  1 
ATOM   207  C  C   . HIS A 1 27  ? -7.028  -15.634 27.566  1.00 19.45  ? 250  HIS A C   1 
ATOM   208  O  O   . HIS A 1 27  ? -5.906  -15.332 27.976  1.00 21.14  ? 250  HIS A O   1 
ATOM   209  C  CB  . HIS A 1 27  ? -7.312  -15.647 25.070  1.00 20.35  ? 250  HIS A CB  1 
ATOM   210  C  CG  . HIS A 1 27  ? -8.113  -16.892 24.860  1.00 22.73  ? 250  HIS A CG  1 
ATOM   211  N  ND1 . HIS A 1 27  ? -9.288  -16.908 24.136  1.00 24.55  ? 250  HIS A ND1 1 
ATOM   212  C  CD2 . HIS A 1 27  ? -7.917  -18.161 25.287  1.00 23.82  ? 250  HIS A CD2 1 
ATOM   213  C  CE1 . HIS A 1 27  ? -9.775  -18.135 24.121  1.00 25.23  ? 250  HIS A CE1 1 
ATOM   214  N  NE2 . HIS A 1 27  ? -8.965  -18.914 24.816  1.00 25.48  ? 250  HIS A NE2 1 
ATOM   215  N  N   . THR A 1 28  ? -7.779  -16.570 28.135  1.00 20.88  ? 251  THR A N   1 
ATOM   216  C  CA  . THR A 1 28  ? -7.260  -17.416 29.200  1.00 21.54  ? 251  THR A CA  1 
ATOM   217  C  C   . THR A 1 28  ? -7.629  -18.865 28.924  1.00 23.80  ? 251  THR A C   1 
ATOM   218  O  O   . THR A 1 28  ? -8.671  -19.156 28.333  1.00 24.22  ? 251  THR A O   1 
ATOM   219  C  CB  . THR A 1 28  ? -7.757  -16.987 30.595  1.00 22.61  ? 251  THR A CB  1 
ATOM   220  O  OG1 . THR A 1 28  ? -7.169  -17.832 31.595  1.00 21.98  ? 251  THR A OG1 1 
ATOM   221  C  CG2 . THR A 1 28  ? -9.279  -17.076 30.687  1.00 23.49  ? 251  THR A CG2 1 
ATOM   222  N  N   . SER A 1 29  ? -6.765  -19.775 29.355  1.00 25.21  ? 252  SER A N   1 
ATOM   223  C  CA  . SER A 1 29  ? -7.020  -21.195 29.173  1.00 29.78  ? 252  SER A CA  1 
ATOM   224  C  C   . SER A 1 29  ? -6.096  -21.969 30.097  1.00 27.42  ? 252  SER A C   1 
ATOM   225  O  O   . SER A 1 29  ? -5.058  -21.445 30.526  1.00 25.59  ? 252  SER A O   1 
ATOM   226  C  CB  . SER A 1 29  ? -6.803  -21.618 27.709  1.00 34.60  ? 252  SER A CB  1 
ATOM   227  O  OG  . SER A 1 29  ? -5.494  -21.318 27.262  1.00 37.39  ? 252  SER A OG  1 
ATOM   228  N  N   . PRO A 1 30  ? -6.452  -23.203 30.444  1.00 28.30  ? 253  PRO A N   1 
ATOM   229  C  CA  . PRO A 1 30  ? -5.516  -24.039 31.195  1.00 28.08  ? 253  PRO A CA  1 
ATOM   230  C  C   . PRO A 1 30  ? -4.296  -24.335 30.341  1.00 28.09  ? 253  PRO A C   1 
ATOM   231  O  O   . PRO A 1 30  ? -4.373  -24.429 29.114  1.00 30.03  ? 253  PRO A O   1 
ATOM   232  C  CB  . PRO A 1 30  ? -6.321  -25.311 31.479  1.00 28.85  ? 253  PRO A CB  1 
ATOM   233  C  CG  . PRO A 1 30  ? -7.342  -25.360 30.406  1.00 30.08  ? 253  PRO A CG  1 
ATOM   234  C  CD  . PRO A 1 30  ? -7.696  -23.924 30.117  1.00 28.73  ? 253  PRO A CD  1 
ATOM   235  N  N   . THR A 1 31  ? -3.149  -24.452 31.006  1.00 26.30  ? 254  THR A N   1 
ATOM   236  C  CA  . THR A 1 31  ? -1.882  -24.664 30.316  1.00 27.26  ? 254  THR A CA  1 
ATOM   237  C  C   . THR A 1 31  ? -1.134  -25.862 30.881  1.00 28.55  ? 254  THR A C   1 
ATOM   238  O  O   . THR A 1 31  ? 0.064   -26.015 30.627  1.00 27.48  ? 254  THR A O   1 
ATOM   239  C  CB  . THR A 1 31  ? -1.008  -23.406 30.355  1.00 27.77  ? 254  THR A CB  1 
ATOM   240  O  OG1 . THR A 1 31  ? -0.911  -22.927 31.704  1.00 27.24  ? 254  THR A OG1 1 
ATOM   241  C  CG2 . THR A 1 31  ? -1.604  -22.316 29.484  1.00 28.69  ? 254  THR A CG2 1 
ATOM   242  N  N   . ASP A 1 32  ? -1.829  -26.718 31.632  1.00 32.37  ? 255  ASP A N   1 
ATOM   243  C  CA  . ASP A 1 32  ? -1.187  -27.865 32.263  1.00 35.42  ? 255  ASP A CA  1 
ATOM   244  C  C   . ASP A 1 32  ? -0.539  -28.807 31.256  1.00 36.36  ? 255  ASP A C   1 
ATOM   245  O  O   . ASP A 1 32  ? 0.383   -29.546 31.622  1.00 37.60  ? 255  ASP A O   1 
ATOM   246  C  CB  . ASP A 1 32  ? -2.212  -28.619 33.106  1.00 37.67  ? 255  ASP A CB  1 
ATOM   247  C  CG  . ASP A 1 32  ? -2.939  -27.712 34.084  1.00 39.51  ? 255  ASP A CG  1 
ATOM   248  N  N   . ASN A 1 33  ? -0.993  -28.803 30.006  1.00 35.22  ? 256  ASN A N   1 
ATOM   249  C  CA  . ASN A 1 33  ? -0.411  -29.653 28.977  1.00 34.56  ? 256  ASN A CA  1 
ATOM   250  C  C   . ASN A 1 33  ? 0.680   -28.959 28.173  1.00 30.50  ? 256  ASN A C   1 
ATOM   251  O  O   . ASN A 1 33  ? 1.180   -29.539 27.204  1.00 30.19  ? 256  ASN A O   1 
ATOM   252  C  CB  . ASN A 1 33  ? -1.500  -30.187 28.040  1.00 36.95  ? 256  ASN A CB  1 
ATOM   253  C  CG  . ASN A 1 33  ? -2.477  -31.107 28.748  1.00 158.38 ? 256  ASN A CG  1 
ATOM   254  O  OD1 . ASN A 1 33  ? -2.109  -31.823 29.680  1.00 90.11  ? 256  ASN A OD1 1 
ATOM   255  N  ND2 . ASN A 1 33  ? -3.729  -31.092 28.308  1.00 57.35  ? 256  ASN A ND2 1 
ATOM   256  N  N   . PHE A 1 34  ? 1.062   -27.743 28.549  1.00 25.97  ? 257  PHE A N   1 
ATOM   257  C  CA  . PHE A 1 34  ? 2.127   -27.010 27.889  1.00 23.79  ? 257  PHE A CA  1 
ATOM   258  C  C   . PHE A 1 34  ? 3.233   -26.692 28.886  1.00 23.24  ? 257  PHE A C   1 
ATOM   259  O  O   . PHE A 1 34  ? 2.999   -26.602 30.098  1.00 23.86  ? 257  PHE A O   1 
ATOM   260  C  CB  . PHE A 1 34  ? 1.622   -25.670 27.333  1.00 23.37  ? 257  PHE A CB  1 
ATOM   261  C  CG  . PHE A 1 34  ? 0.583   -25.800 26.257  1.00 25.22  ? 257  PHE A CG  1 
ATOM   262  C  CD1 . PHE A 1 34  ? 0.845   -26.514 25.095  1.00 24.81  ? 257  PHE A CD1 1 
ATOM   263  C  CD2 . PHE A 1 34  ? -0.649  -25.173 26.388  1.00 27.98  ? 257  PHE A CD2 1 
ATOM   264  C  CE1 . PHE A 1 34  ? -0.110  -26.620 24.093  1.00 26.65  ? 257  PHE A CE1 1 
ATOM   265  C  CE2 . PHE A 1 34  ? -1.604  -25.271 25.388  1.00 28.67  ? 257  PHE A CE2 1 
ATOM   266  C  CZ  . PHE A 1 34  ? -1.334  -25.998 24.241  1.00 27.70  ? 257  PHE A CZ  1 
ATOM   267  N  N   . ILE A 1 35  ? 4.440   -26.522 28.363  1.00 22.54  ? 258  ILE A N   1 
ATOM   268  C  CA  . ILE A 1 35  ? 5.511   -25.830 29.068  1.00 21.59  ? 258  ILE A CA  1 
ATOM   269  C  C   . ILE A 1 35  ? 5.541   -24.425 28.494  1.00 20.08  ? 258  ILE A C   1 
ATOM   270  O  O   . ILE A 1 35  ? 5.880   -24.230 27.322  1.00 21.83  ? 258  ILE A O   1 
ATOM   271  C  CB  . ILE A 1 35  ? 6.861   -26.536 28.900  1.00 22.80  ? 258  ILE A CB  1 
ATOM   272  C  CG1 . ILE A 1 35  ? 6.807   -27.932 29.524  1.00 27.23  ? 258  ILE A CG1 1 
ATOM   273  C  CG2 . ILE A 1 35  ? 7.982   -25.707 29.541  1.00 23.84  ? 258  ILE A CG2 1 
ATOM   274  C  CD1 . ILE A 1 35  ? 8.075   -28.712 29.338  1.00 30.27  ? 258  ILE A CD1 1 
ATOM   275  N  N   . VAL A 1 36  ? 5.163   -23.443 29.306  1.00 17.56  ? 259  VAL A N   1 
ATOM   276  C  CA  . VAL A 1 36  ? 5.002   -22.069 28.833  1.00 15.92  ? 259  VAL A CA  1 
ATOM   277  C  C   . VAL A 1 36  ? 6.323   -21.358 29.104  1.00 14.96  ? 259  VAL A C   1 
ATOM   278  O  O   . VAL A 1 36  ? 6.540   -20.772 30.163  1.00 15.60  ? 259  VAL A O   1 
ATOM   279  C  CB  . VAL A 1 36  ? 3.807   -21.380 29.480  1.00 15.81  ? 259  VAL A CB  1 
ATOM   280  C  CG1 . VAL A 1 36  ? 3.648   -19.963 28.945  1.00 16.36  ? 259  VAL A CG1 1 
ATOM   281  C  CG2 . VAL A 1 36  ? 2.541   -22.198 29.222  1.00 17.20  ? 259  VAL A CG2 1 
ATOM   282  N  N   . GLN A 1 37  ? 7.221   -21.412 28.122  1.00 14.14  ? 260  GLN A N   1 
ATOM   283  C  CA  . GLN A 1 37  ? 8.564   -20.850 28.264  1.00 12.63  ? 260  GLN A CA  1 
ATOM   284  C  C   . GLN A 1 37  ? 8.932   -19.980 27.059  1.00 13.59  ? 260  GLN A C   1 
ATOM   285  O  O   . GLN A 1 37  ? 9.994   -20.151 26.458  1.00 13.06  ? 260  GLN A O   1 
ATOM   286  C  CB  . GLN A 1 37  ? 9.568   -21.983 28.480  1.00 14.11  ? 260  GLN A CB  1 
ATOM   287  C  CG  . GLN A 1 37  ? 10.936  -21.536 28.981  1.00 14.90  ? 260  GLN A CG  1 
ATOM   288  C  CD  . GLN A 1 37  ? 11.727  -22.640 29.681  1.00 16.12  ? 260  GLN A CD  1 
ATOM   289  O  OE1 . GLN A 1 37  ? 11.535  -23.838 29.438  1.00 17.81  ? 260  GLN A OE1 1 
ATOM   290  N  NE2 . GLN A 1 37  ? 12.628  -22.227 30.570  1.00 15.86  ? 260  GLN A NE2 1 
ATOM   291  N  N   . PRO A 1 38  ? 8.068   -19.034 26.666  1.00 12.57  ? 261  PRO A N   1 
ATOM   292  C  CA  . PRO A 1 38  ? 8.427   -18.158 25.543  1.00 12.24  ? 261  PRO A CA  1 
ATOM   293  C  C   . PRO A 1 38  ? 9.695   -17.394 25.878  1.00 11.40  ? 261  PRO A C   1 
ATOM   294  O  O   . PRO A 1 38  ? 9.993   -17.118 27.046  1.00 12.64  ? 261  PRO A O   1 
ATOM   295  C  CB  . PRO A 1 38  ? 7.220   -17.219 25.410  1.00 13.17  ? 261  PRO A CB  1 
ATOM   296  C  CG  . PRO A 1 38  ? 6.637   -17.168 26.821  1.00 12.37  ? 261  PRO A CG  1 
ATOM   297  C  CD  . PRO A 1 38  ? 6.855   -18.557 27.363  1.00 13.30  ? 261  PRO A CD  1 
ATOM   298  N  N   . GLN A 1 39  ? 10.455  -17.053 24.836  1.00 11.19  ? 262  GLN A N   1 
ATOM   299  C  CA  . GLN A 1 39  ? 11.703  -16.321 24.996  1.00 11.73  ? 262  GLN A CA  1 
ATOM   300  C  C   . GLN A 1 39  ? 11.637  -14.891 24.485  1.00 10.83  ? 262  GLN A C   1 
ATOM   301  O  O   . GLN A 1 39  ? 12.433  -14.058 24.929  1.00 11.85  ? 262  GLN A O   1 
ATOM   302  C  CB  . GLN A 1 39  ? 12.873  -17.072 24.341  1.00 12.88  ? 262  GLN A CB  1 
ATOM   303  C  CG  . GLN A 1 39  ? 13.088  -18.453 24.961  1.00 13.56  ? 262  GLN A CG  1 
ATOM   304  C  CD  . GLN A 1 39  ? 13.404  -18.368 26.432  1.00 13.44  ? 262  GLN A CD  1 
ATOM   305  O  OE1 . GLN A 1 39  ? 14.349  -17.681 26.833  1.00 14.24  ? 262  GLN A OE1 1 
ATOM   306  N  NE2 . GLN A 1 39  ? 12.621  -19.070 27.250  1.00 13.08  ? 262  GLN A NE2 1 
ATOM   307  N  N   . ASN A 1 40  ? 10.711  -14.577 23.578  1.00 10.32  ? 263  ASN A N   1 
ATOM   308  C  CA  . ASN A 1 40  ? 10.380  -13.191 23.284  1.00 10.93  ? 263  ASN A CA  1 
ATOM   309  C  C   . ASN A 1 40  ? 9.244   -12.733 24.186  1.00 12.14  ? 263  ASN A C   1 
ATOM   310  O  O   . ASN A 1 40  ? 8.447   -13.536 24.686  1.00 12.99  ? 263  ASN A O   1 
ATOM   311  C  CB  . ASN A 1 40  ? 9.980   -13.027 21.819  1.00 11.64  ? 263  ASN A CB  1 
ATOM   312  C  CG  . ASN A 1 40  ? 11.164  -13.144 20.879  1.00 11.34  ? 263  ASN A CG  1 
ATOM   313  O  OD1 . ASN A 1 40  ? 12.229  -12.596 21.154  1.00 12.27  ? 263  ASN A OD1 1 
ATOM   314  N  ND2 . ASN A 1 40  ? 10.987  -13.858 19.764  1.00 12.59  ? 263  ASN A ND2 1 
ATOM   315  N  N   . GLY A 1 41  ? 9.172   -11.419 24.388  1.00 11.38  ? 264  GLY A N   1 
ATOM   316  C  CA  . GLY A 1 41  ? 8.180   -10.874 25.287  1.00 11.14  ? 264  GLY A CA  1 
ATOM   317  C  C   . GLY A 1 41  ? 8.434   -11.160 26.754  1.00 11.66  ? 264  GLY A C   1 
ATOM   318  O  O   . GLY A 1 41  ? 7.475   -11.330 27.513  1.00 13.01  ? 264  GLY A O   1 
ATOM   319  N  N   . ARG A 1 42  ? 9.697   -11.203 27.181  1.00 11.88  ? 265  ARG A N   1 
ATOM   320  C  CA  . ARG A 1 42  ? 10.051  -11.536 28.561  1.00 12.05  ? 265  ARG A CA  1 
ATOM   321  C  C   . ARG A 1 42  ? 10.732  -10.343 29.212  1.00 12.73  ? 265  ARG A C   1 
ATOM   322  O  O   . ARG A 1 42  ? 11.818  -9.933  28.784  1.00 13.46  ? 265  ARG A O   1 
ATOM   323  C  CB  . ARG A 1 42  ? 10.974  -12.755 28.612  1.00 12.19  ? 265  ARG A CB  1 
ATOM   324  C  CG  . ARG A 1 42  ? 10.369  -14.002 27.977  1.00 12.73  ? 265  ARG A CG  1 
ATOM   325  C  CD  . ARG A 1 42  ? 9.035   -14.403 28.592  1.00 12.98  ? 265  ARG A CD  1 
ATOM   326  N  NE  . ARG A 1 42  ? 9.154   -14.639 30.030  1.00 13.07  ? 265  ARG A NE  1 
ATOM   327  C  CZ  . ARG A 1 42  ? 9.346   -15.834 30.578  1.00 12.44  ? 265  ARG A CZ  1 
ATOM   328  N  NH1 . ARG A 1 42  ? 9.432   -16.930 29.831  1.00 13.54  ? 265  ARG A NH1 1 
ATOM   329  N  NH2 . ARG A 1 42  ? 9.474   -15.928 31.904  1.00 13.83  ? 265  ARG A NH2 1 
ATOM   330  N  N   . CYS A 1 43  ? 10.101  -9.795  30.251  1.00 13.26  ? 266  CYS A N   1 
ATOM   331  C  CA  . CYS A 1 43  ? 10.685  -8.677  30.984  1.00 13.98  ? 266  CYS A CA  1 
ATOM   332  C  C   . CYS A 1 43  ? 10.104  -8.677  32.387  1.00 14.47  ? 266  CYS A C   1 
ATOM   333  O  O   . CYS A 1 43  ? 8.889   -8.800  32.545  1.00 15.80  ? 266  CYS A O   1 
ATOM   334  C  CB  . CYS A 1 43  ? 10.340  -7.352  30.287  1.00 14.15  ? 266  CYS A CB  1 
ATOM   335  S  SG  . CYS A 1 43  ? 11.155  -5.896  31.036  1.00 15.97  ? 266  CYS A SG  1 
ATOM   336  N  N   . THR A 1 44  ? 10.959  -8.535  33.403  1.00 13.71  ? 267  THR A N   1 
ATOM   337  C  CA  . THR A 1 44  ? 10.439  -8.429  34.755  1.00 15.12  ? 267  THR A CA  1 
ATOM   338  C  C   . THR A 1 44  ? 9.853   -7.043  34.985  1.00 16.23  ? 267  THR A C   1 
ATOM   339  O  O   . THR A 1 44  ? 10.098  -6.100  34.227  1.00 15.93  ? 267  THR A O   1 
ATOM   340  C  CB  . THR A 1 44  ? 11.537  -8.659  35.790  1.00 15.24  ? 267  THR A CB  1 
ATOM   341  O  OG1 . THR A 1 44  ? 12.474  -7.574  35.716  1.00 16.13  ? 267  THR A OG1 1 
ATOM   342  C  CG2 . THR A 1 44  ? 12.245  -10.012 35.562  1.00 16.76  ? 267  THR A CG2 1 
ATOM   343  N  N   . LEU A 1 45  ? 9.074   -6.927  36.059  1.00 16.38  ? 268  LEU A N   1 
ATOM   344  C  CA  . LEU A 1 45  ? 8.439   -5.648  36.357  1.00 16.73  ? 268  LEU A CA  1 
ATOM   345  C  C   . LEU A 1 45  ? 9.450   -4.559  36.670  1.00 19.09  ? 268  LEU A C   1 
ATOM   346  O  O   . LEU A 1 45  ? 9.147   -3.377  36.477  1.00 21.99  ? 268  LEU A O   1 
ATOM   347  C  CB  . LEU A 1 45  ? 7.422   -5.793  37.489  1.00 17.16  ? 268  LEU A CB  1 
ATOM   348  C  CG  . LEU A 1 45  ? 6.273   -6.773  37.233  1.00 17.54  ? 268  LEU A CG  1 
ATOM   349  C  CD1 . LEU A 1 45  ? 5.242   -6.675  38.357  1.00 18.58  ? 268  LEU A CD1 1 
ATOM   350  C  CD2 . LEU A 1 45  ? 5.628   -6.577  35.853  1.00 17.45  ? 268  LEU A CD2 1 
ATOM   351  N  N   . ASP A 1 46  ? 10.643  -4.908  37.143  0.87 19.65  ? 269  ASP A N   1 
ATOM   352  C  CA  . ASP A 1 46  ? 11.643  -3.874  37.361  0.87 22.14  ? 269  ASP A CA  1 
ATOM   353  C  C   . ASP A 1 46  ? 12.577  -3.683  36.175  0.87 19.77  ? 269  ASP A C   1 
ATOM   354  O  O   . ASP A 1 46  ? 13.617  -3.028  36.316  0.87 21.07  ? 269  ASP A O   1 
ATOM   355  C  CB  . ASP A 1 46  ? 12.390  -4.068  38.682  0.87 26.12  ? 269  ASP A CB  1 
ATOM   356  C  CG  . ASP A 1 46  ? 13.143  -5.362  38.743  0.87 28.80  ? 269  ASP A CG  1 
ATOM   357  O  OD1 . ASP A 1 46  ? 13.402  -5.966  37.684  0.87 31.10  ? 269  ASP A OD1 1 
ATOM   358  O  OD2 . ASP A 1 46  ? 13.478  -5.777  39.868  0.87 32.42  ? 269  ASP A OD2 1 
ATOM   359  N  N   . GLY A 1 47  ? 12.228  -4.236  35.018  1.00 18.06  ? 270  GLY A N   1 
ATOM   360  C  CA  . GLY A 1 47  ? 12.838  -3.843  33.768  1.00 16.42  ? 270  GLY A CA  1 
ATOM   361  C  C   . GLY A 1 47  ? 13.976  -4.692  33.253  1.00 16.58  ? 270  GLY A C   1 
ATOM   362  O  O   . GLY A 1 47  ? 14.731  -4.214  32.397  1.00 18.08  ? 270  GLY A O   1 
ATOM   363  N  N   . GLU A 1 48  ? 14.110  -5.935  33.713  1.00 16.44  ? 271  GLU A N   1 
ATOM   364  C  CA  . GLU A 1 48  ? 15.158  -6.833  33.229  1.00 18.09  ? 271  GLU A CA  1 
ATOM   365  C  C   . GLU A 1 48  ? 14.632  -7.642  32.040  1.00 16.08  ? 271  GLU A C   1 
ATOM   366  O  O   . GLU A 1 48  ? 13.762  -8.511  32.201  1.00 14.81  ? 271  GLU A O   1 
ATOM   367  C  CB  . GLU A 1 48  ? 15.620  -7.757  34.354  1.00 20.97  ? 271  GLU A CB  1 
ATOM   368  C  CG  . GLU A 1 48  ? 16.558  -8.867  33.918  1.00 26.32  ? 271  GLU A CG  1 
ATOM   369  C  CD  . GLU A 1 48  ? 16.868  -9.832  35.047  1.00 31.92  ? 271  GLU A CD  1 
ATOM   370  O  OE1 . GLU A 1 48  ? 17.325  -9.370  36.109  1.00 35.96  ? 271  GLU A OE1 1 
ATOM   371  O  OE2 . GLU A 1 48  ? 16.650  -11.047 34.876  1.00 34.96  ? 271  GLU A OE2 1 
ATOM   372  N  N   . LEU A 1 49  ? 15.181  -7.385  30.855  1.00 14.92  ? 272  LEU A N   1 
ATOM   373  C  CA  . LEU A 1 49  ? 14.844  -8.188  29.683  1.00 15.45  ? 272  LEU A CA  1 
ATOM   374  C  C   . LEU A 1 49  ? 15.441  -9.580  29.834  1.00 14.94  ? 272  LEU A C   1 
ATOM   375  O  O   . LEU A 1 49  ? 16.527  -9.754  30.396  1.00 17.20  ? 272  LEU A O   1 
ATOM   376  C  CB  . LEU A 1 49  ? 15.422  -7.558  28.419  1.00 17.12  ? 272  LEU A CB  1 
ATOM   377  C  CG  . LEU A 1 49  ? 15.065  -6.095  28.154  1.00 18.18  ? 272  LEU A CG  1 
ATOM   378  C  CD1 . LEU A 1 49  ? 15.791  -5.605  26.922  1.00 19.49  ? 272  LEU A CD1 1 
ATOM   379  C  CD2 . LEU A 1 49  ? 13.559  -5.940  27.998  1.00 18.29  ? 272  LEU A CD2 1 
ATOM   380  N  N   . GLN A 1 50  ? 14.727  -10.584 29.319  1.00 13.93  ? 273  GLN A N   1 
ATOM   381  C  CA  . GLN A 1 50  ? 15.185  -11.960 29.444  1.00 13.82  ? 273  GLN A CA  1 
ATOM   382  C  C   . GLN A 1 50  ? 15.027  -12.689 28.119  1.00 13.07  ? 273  GLN A C   1 
ATOM   383  O  O   . GLN A 1 50  ? 14.358  -12.216 27.191  1.00 13.91  ? 273  GLN A O   1 
ATOM   384  C  CB  . GLN A 1 50  ? 14.446  -12.703 30.566  1.00 14.78  ? 273  GLN A CB  1 
ATOM   385  C  CG  . GLN A 1 50  ? 14.574  -12.029 31.928  1.00 16.88  ? 273  GLN A CG  1 
ATOM   386  C  CD  . GLN A 1 50  ? 13.731  -12.708 32.973  1.00 18.64  ? 273  GLN A CD  1 
ATOM   387  O  OE1 . GLN A 1 50  ? 12.746  -13.367 32.649  1.00 21.62  ? 273  GLN A OE1 1 
ATOM   388  N  NE2 . GLN A 1 50  ? 14.107  -12.553 34.234  1.00 22.02  ? 273  GLN A NE2 1 
ATOM   389  N  N   . GLY A 1 51  ? 15.634  -13.868 28.046  1.00 13.38  ? 274  GLY A N   1 
ATOM   390  C  CA  . GLY A 1 51  ? 15.482  -14.694 26.858  1.00 13.79  ? 274  GLY A CA  1 
ATOM   391  C  C   . GLY A 1 51  ? 16.109  -14.044 25.641  1.00 13.36  ? 274  GLY A C   1 
ATOM   392  O  O   . GLY A 1 51  ? 17.261  -13.595 25.672  1.00 15.03  ? 274  GLY A O   1 
ATOM   393  N  N   . THR A 1 52  ? 15.344  -13.993 24.546  1.00 12.18  ? 275  THR A N   1 
ATOM   394  C  CA  . THR A 1 52  ? 15.763  -13.311 23.327  1.00 11.98  ? 275  THR A CA  1 
ATOM   395  C  C   . THR A 1 52  ? 15.085  -11.956 23.170  1.00 11.88  ? 275  THR A C   1 
ATOM   396  O  O   . THR A 1 52  ? 15.038  -11.414 22.061  1.00 12.92  ? 275  THR A O   1 
ATOM   397  C  CB  . THR A 1 52  ? 15.488  -14.179 22.092  1.00 12.62  ? 275  THR A CB  1 
ATOM   398  O  OG1 . THR A 1 52  ? 14.099  -14.540 22.045  1.00 12.69  ? 275  THR A OG1 1 
ATOM   399  C  CG2 . THR A 1 52  ? 16.341  -15.449 22.112  1.00 14.26  ? 275  THR A CG2 1 
ATOM   400  N  N   . THR A 1 53  ? 14.573  -11.388 24.258  1.00 12.54  ? 276  THR A N   1 
ATOM   401  C  CA  . THR A 1 53  ? 13.734  -10.199 24.161  1.00 11.57  ? 276  THR A CA  1 
ATOM   402  C  C   . THR A 1 53  ? 14.567  -8.944  23.907  1.00 11.75  ? 276  THR A C   1 
ATOM   403  O  O   . THR A 1 53  ? 15.565  -8.686  24.589  1.00 13.79  ? 276  THR A O   1 
ATOM   404  C  CB  . THR A 1 53  ? 12.894  -10.038 25.433  1.00 11.56  ? 276  THR A CB  1 
ATOM   405  O  OG1 . THR A 1 53  ? 12.003  -11.147 25.568  1.00 12.60  ? 276  THR A OG1 1 
ATOM   406  C  CG2 . THR A 1 53  ? 12.067  -8.754  25.407  1.00 13.36  ? 276  THR A CG2 1 
ATOM   407  N  N   . GLN A 1 54  ? 14.149  -8.166  22.910  1.00 12.09  ? 277  GLN A N   1 
ATOM   408  C  CA  . GLN A 1 54  ? 14.730  -6.864  22.634  1.00 12.77  ? 277  GLN A CA  1 
ATOM   409  C  C   . GLN A 1 54  ? 13.586  -5.860  22.520  1.00 12.40  ? 277  GLN A C   1 
ATOM   410  O  O   . GLN A 1 54  ? 12.420  -6.224  22.677  1.00 13.66  ? 277  GLN A O   1 
ATOM   411  C  CB  . GLN A 1 54  ? 15.641  -6.926  21.398  1.00 12.74  ? 277  GLN A CB  1 
ATOM   412  C  CG  . GLN A 1 54  ? 15.028  -7.627  20.200  1.00 12.54  ? 277  GLN A CG  1 
ATOM   413  C  CD  . GLN A 1 54  ? 14.040  -6.738  19.492  1.00 12.35  ? 277  GLN A CD  1 
ATOM   414  O  OE1 . GLN A 1 54  ? 14.358  -5.600  19.155  1.00 12.42  ? 277  GLN A OE1 1 
ATOM   415  N  NE2 . GLN A 1 54  ? 12.834  -7.243  19.271  1.00 12.06  ? 277  GLN A NE2 1 
ATOM   416  N  N   . LEU A 1 55  ? 13.914  -4.586  22.255  1.00 12.20  ? 278  LEU A N   1 
ATOM   417  C  CA  . LEU A 1 55  ? 12.967  -3.501  22.483  1.00 12.95  ? 278  LEU A CA  1 
ATOM   418  C  C   . LEU A 1 55  ? 12.201  -3.052  21.243  1.00 13.44  ? 278  LEU A C   1 
ATOM   419  O  O   . LEU A 1 55  ? 11.178  -2.367  21.383  1.00 15.64  ? 278  LEU A O   1 
ATOM   420  C  CB  . LEU A 1 55  ? 13.698  -2.299  23.092  1.00 13.62  ? 278  LEU A CB  1 
ATOM   421  C  CG  . LEU A 1 55  ? 14.104  -2.538  24.551  1.00 16.85  ? 278  LEU A CG  1 
ATOM   422  C  CD1 . LEU A 1 55  ? 15.092  -1.501  25.005  1.00 19.35  ? 278  LEU A CD1 1 
ATOM   423  C  CD2 . LEU A 1 55  ? 12.877  -2.549  25.462  1.00 18.39  ? 278  LEU A CD2 1 
ATOM   424  N  N   . VAL A 1 56  ? 12.663  -3.400  20.047  1.00 12.44  ? 279  VAL A N   1 
ATOM   425  C  CA  . VAL A 1 56  ? 12.068  -2.926  18.800  1.00 12.68  ? 279  VAL A CA  1 
ATOM   426  C  C   . VAL A 1 56  ? 11.053  -3.970  18.335  1.00 11.64  ? 279  VAL A C   1 
ATOM   427  O  O   . VAL A 1 56  ? 11.426  -5.084  17.961  1.00 12.13  ? 279  VAL A O   1 
ATOM   428  C  CB  . VAL A 1 56  ? 13.156  -2.690  17.744  1.00 12.88  ? 279  VAL A CB  1 
ATOM   429  C  CG1 . VAL A 1 56  ? 12.554  -2.232  16.422  1.00 13.17  ? 279  VAL A CG1 1 
ATOM   430  C  CG2 . VAL A 1 56  ? 14.160  -1.646  18.230  1.00 14.43  ? 279  VAL A CG2 1 
ATOM   431  N  N   . ALA A 1 57  ? 9.762   -3.626  18.363  1.00 12.88  ? 280  ALA A N   1 
ATOM   432  C  CA  . ALA A 1 57  ? 8.747   -4.596  17.953  1.00 12.30  ? 280  ALA A CA  1 
ATOM   433  C  C   . ALA A 1 57  ? 8.994   -5.090  16.533  1.00 11.41  ? 280  ALA A C   1 
ATOM   434  O  O   . ALA A 1 57  ? 8.796   -6.277  16.235  1.00 12.51  ? 280  ALA A O   1 
ATOM   435  C  CB  . ALA A 1 57  ? 7.334   -4.026  18.061  1.00 13.40  ? 280  ALA A CB  1 
ATOM   436  N  N   . SER A 1 58  ? 9.438   -4.192  15.644  1.00 11.99  ? 281  SER A N   1 
ATOM   437  C  CA  . SER A 1 58  ? 9.652   -4.551  14.251  1.00 12.44  ? 281  SER A CA  1 
ATOM   438  C  C   . SER A 1 58  ? 10.809  -5.526  14.060  1.00 14.01  ? 281  SER A C   1 
ATOM   439  O  O   . SER A 1 58  ? 10.982  -6.035  12.946  1.00 16.45  ? 281  SER A O   1 
ATOM   440  C  CB  . SER A 1 58  ? 9.872   -3.281  13.431  1.00 13.14  ? 281  SER A CB  1 
ATOM   441  O  OG  . SER A 1 58  ? 8.763   -2.404  13.574  1.00 14.19  ? 281  SER A OG  1 
ATOM   442  N  N   . ASN A 1 59  ? 11.598  -5.807  15.105  1.00 10.92  ? 282  ASN A N   1 
ATOM   443  C  CA  . ASN A 1 59  ? 12.672  -6.792  15.032  1.00 11.40  ? 282  ASN A CA  1 
ATOM   444  C  C   . ASN A 1 59  ? 12.270  -8.155  15.584  1.00 11.45  ? 282  ASN A C   1 
ATOM   445  O  O   . ASN A 1 59  ? 13.072  -9.101  15.533  1.00 12.68  ? 282  ASN A O   1 
ATOM   446  C  CB  . ASN A 1 59  ? 13.944  -6.280  15.727  1.00 11.99  ? 282  ASN A CB  1 
ATOM   447  C  CG  . ASN A 1 59  ? 14.707  -5.280  14.874  1.00 13.58  ? 282  ASN A CG  1 
ATOM   448  O  OD1 . ASN A 1 59  ? 14.430  -5.139  13.677  1.00 14.91  ? 282  ASN A OD1 1 
ATOM   449  N  ND2 . ASN A 1 59  ? 15.676  -4.592  15.471  1.00 13.31  ? 282  ASN A ND2 1 
ATOM   450  N  N   . ILE A 1 60  ? 11.055  -8.287  16.105  1.00 10.84  ? 283  ILE A N   1 
ATOM   451  C  CA  . ILE A 1 60  ? 10.585  -9.586  16.583  1.00 10.86  ? 283  ILE A CA  1 
ATOM   452  C  C   . ILE A 1 60  ? 10.376  -10.500 15.387  1.00 10.26  ? 283  ILE A C   1 
ATOM   453  O  O   . ILE A 1 60  ? 9.677   -10.143 14.431  1.00 11.64  ? 283  ILE A O   1 
ATOM   454  C  CB  . ILE A 1 60  ? 9.282   -9.424  17.375  1.00 10.89  ? 283  ILE A CB  1 
ATOM   455  C  CG1 . ILE A 1 60  ? 9.469   -8.487  18.575  1.00 11.96  ? 283  ILE A CG1 1 
ATOM   456  C  CG2 . ILE A 1 60  ? 8.802   -10.778 17.847  1.00 11.33  ? 283  ILE A CG2 1 
ATOM   457  C  CD1 . ILE A 1 60  ? 8.151   -8.029  19.174  1.00 14.17  ? 283  ILE A CD1 1 
ATOM   458  N  N   . CYS A 1 61  ? 10.989  -11.681 15.421  1.00 10.48  ? 284  CYS A N   1 
ATOM   459  C  CA  . CYS A 1 61  ? 10.928  -12.635 14.310  1.00 11.24  ? 284  CYS A CA  1 
ATOM   460  C  C   . CYS A 1 61  ? 11.606  -12.112 13.049  1.00 11.49  ? 284  CYS A C   1 
ATOM   461  O  O   . CYS A 1 61  ? 11.335  -12.592 11.935  1.00 13.39  ? 284  CYS A O   1 
ATOM   462  C  CB  . CYS A 1 61  ? 9.509   -13.154 14.025  1.00 11.51  ? 284  CYS A CB  1 
ATOM   463  S  SG  . CYS A 1 61  ? 8.930   -14.323 15.287  1.00 12.89  ? 284  CYS A SG  1 
ATOM   464  N  N   . ALA A 1 62  ? 12.492  -11.140 13.199  1.00 11.71  ? 285  ALA A N   1 
ATOM   465  C  CA  . ALA A 1 62  ? 13.306  -10.650 12.100  1.00 12.62  ? 285  ALA A CA  1 
ATOM   466  C  C   . ALA A 1 62  ? 14.722  -11.207 12.220  1.00 12.79  ? 285  ALA A C   1 
ATOM   467  O  O   . ALA A 1 62  ? 15.162  -11.640 13.294  1.00 14.08  ? 285  ALA A O   1 
ATOM   468  C  CB  . ALA A 1 62  ? 13.340  -9.122  12.093  1.00 13.20  ? 285  ALA A CB  1 
ATOM   469  N  N   . PHE A 1 63  ? 15.429  -11.209 11.091  1.00 13.51  ? 286  PHE A N   1 
ATOM   470  C  CA  . PHE A 1 63  ? 16.843  -11.542 11.052  1.00 13.56  ? 286  PHE A CA  1 
ATOM   471  C  C   . PHE A 1 63  ? 17.567  -10.534 10.177  1.00 14.36  ? 286  PHE A C   1 
ATOM   472  O  O   . PHE A 1 63  ? 17.012  -10.020 9.199   1.00 14.70  ? 286  PHE A O   1 
ATOM   473  C  CB  . PHE A 1 63  ? 17.113  -12.936 10.471  1.00 15.10  ? 286  PHE A CB  1 
ATOM   474  C  CG  . PHE A 1 63  ? 16.643  -14.066 11.338  1.00 15.92  ? 286  PHE A CG  1 
ATOM   475  C  CD1 . PHE A 1 63  ? 17.334  -14.417 12.482  1.00 16.72  ? 286  PHE A CD1 1 
ATOM   476  C  CD2 . PHE A 1 63  ? 15.529  -14.812 10.980  1.00 16.57  ? 286  PHE A CD2 1 
ATOM   477  C  CE1 . PHE A 1 63  ? 16.909  -15.480 13.275  1.00 17.54  ? 286  PHE A CE1 1 
ATOM   478  C  CE2 . PHE A 1 63  ? 15.102  -15.873 11.763  1.00 17.92  ? 286  PHE A CE2 1 
ATOM   479  C  CZ  . PHE A 1 63  ? 15.797  -16.208 12.913  1.00 17.63  ? 286  PHE A CZ  1 
ATOM   480  N  N   . ARG A 1 64  ? 18.828  -10.284 10.523  1.00 15.50  ? 287  ARG A N   1 
ATOM   481  C  CA  . ARG A 1 64  ? 19.727  -9.457  9.741   1.00 16.22  ? 287  ARG A CA  1 
ATOM   482  C  C   . ARG A 1 64  ? 21.034  -10.217 9.582   1.00 15.02  ? 287  ARG A C   1 
ATOM   483  O  O   . ARG A 1 64  ? 21.455  -10.942 10.493  1.00 16.05  ? 287  ARG A O   1 
ATOM   484  C  CB  . ARG A 1 64  ? 19.994  -8.151  10.477  1.00 20.33  ? 287  ARG A CB  1 
ATOM   485  C  CG  . ARG A 1 64  ? 20.805  -7.140  9.722   1.00 27.50  ? 287  ARG A CG  1 
ATOM   486  C  CD  . ARG A 1 64  ? 20.957  -5.893  10.578  1.00 32.30  ? 287  ARG A CD  1 
ATOM   487  N  NE  . ARG A 1 64  ? 21.780  -4.867  9.950   1.00 35.27  ? 287  ARG A NE  1 
ATOM   488  C  CZ  . ARG A 1 64  ? 21.884  -3.621  10.391  1.00 35.87  ? 287  ARG A CZ  1 
ATOM   489  N  NH1 . ARG A 1 64  ? 21.224  -3.210  11.464  1.00 31.86  ? 287  ARG A NH1 1 
ATOM   490  N  NH2 . ARG A 1 64  ? 22.665  -2.765  9.739   1.00 38.57  ? 287  ARG A NH2 1 
ATOM   491  N  N   . GLY A 1 65  ? 21.670  -10.063 8.422   1.00 14.84  ? 288  GLY A N   1 
ATOM   492  C  CA  . GLY A 1 65  ? 22.936  -10.727 8.168   1.00 15.76  ? 288  GLY A CA  1 
ATOM   493  C  C   . GLY A 1 65  ? 23.296  -10.768 6.696   1.00 15.66  ? 288  GLY A C   1 
ATOM   494  O  O   . GLY A 1 65  ? 23.267  -9.734  6.024   1.00 17.17  ? 288  GLY A O   1 
ATOM   495  N  N   . SER A 1 66  ? 23.616  -11.955 6.177   1.00 15.48  ? 289  SER A N   1 
ATOM   496  C  CA  . SER A 1 66  ? 24.025  -12.094 4.786   1.00 15.02  ? 289  SER A CA  1 
ATOM   497  C  C   . SER A 1 66  ? 23.780  -13.531 4.365   1.00 14.69  ? 289  SER A C   1 
ATOM   498  O  O   . SER A 1 66  ? 23.698  -14.434 5.202   1.00 17.92  ? 289  SER A O   1 
ATOM   499  C  CB  . SER A 1 66  ? 25.502  -11.733 4.594   1.00 17.05  ? 289  SER A CB  1 
ATOM   500  O  OG  . SER A 1 66  ? 26.336  -12.537 5.406   1.00 21.07  ? 289  SER A OG  1 
ATOM   501  N  N   . ILE A 1 67  ? 23.658  -13.731 3.059   1.00 15.68  ? 290  ILE A N   1 
ATOM   502  C  CA  . ILE A 1 67  ? 23.547  -15.066 2.485   1.00 16.18  ? 290  ILE A CA  1 
ATOM   503  C  C   . ILE A 1 67  ? 24.934  -15.512 2.058   1.00 17.72  ? 290  ILE A C   1 
ATOM   504  O  O   . ILE A 1 67  ? 25.682  -14.743 1.441   1.00 19.78  ? 290  ILE A O   1 
ATOM   505  C  CB  . ILE A 1 67  ? 22.574  -15.082 1.293   1.00 15.66  ? 290  ILE A CB  1 
ATOM   506  C  CG1 . ILE A 1 67  ? 21.138  -14.835 1.763   1.00 16.44  ? 290  ILE A CG1 1 
ATOM   507  C  CG2 . ILE A 1 67  ? 22.681  -16.397 0.525   1.00 17.58  ? 290  ILE A CG2 1 
ATOM   508  C  CD1 . ILE A 1 67  ? 20.573  -15.958 2.636   1.00 17.17  ? 290  ILE A CD1 1 
ATOM   509  N  N   . SER A 1 68  ? 25.292  -16.745 2.405   1.00 18.97  ? 291  SER A N   1 
ATOM   510  C  CA  . SER A 1 68  ? 26.567  -17.335 2.022   1.00 21.74  ? 291  SER A CA  1 
ATOM   511  C  C   . SER A 1 68  ? 26.262  -18.642 1.288   1.00 22.95  ? 291  SER A C   1 
ATOM   512  O  O   . SER A 1 68  ? 26.458  -19.739 1.820   1.00 25.65  ? 291  SER A O   1 
ATOM   513  C  CB  . SER A 1 68  ? 27.467  -17.561 3.234   1.00 26.08  ? 291  SER A CB  1 
ATOM   514  O  OG  . SER A 1 68  ? 28.739  -18.026 2.822   1.00 30.87  ? 291  SER A OG  1 
ATOM   515  N  N   . GLY A 1 69  ? 25.746  -18.509 0.068   1.00 20.47  ? 292  GLY A N   1 
ATOM   516  C  CA  . GLY A 1 69  ? 25.498  -19.644 -0.799  1.00 20.83  ? 292  GLY A CA  1 
ATOM   517  C  C   . GLY A 1 69  ? 24.334  -20.509 -0.338  1.00 20.48  ? 292  GLY A C   1 
ATOM   518  O  O   . GLY A 1 69  ? 23.546  -20.161 0.545   1.00 20.81  ? 292  GLY A O   1 
ATOM   519  N  N   . HIS A 1 70  ? 24.238  -21.666 -0.980  1.00 20.28  ? 293  HIS A N   1 
ATOM   520  C  CA  . HIS A 1 70  ? 23.281  -22.679 -0.576  1.00 21.25  ? 293  HIS A CA  1 
ATOM   521  C  C   . HIS A 1 70  ? 23.788  -23.395 0.674   1.00 25.71  ? 293  HIS A C   1 
ATOM   522  O  O   . HIS A 1 70  ? 24.941  -23.243 1.080   1.00 24.99  ? 293  HIS A O   1 
ATOM   523  C  CB  . HIS A 1 70  ? 23.074  -23.675 -1.717  1.00 20.04  ? 293  HIS A CB  1 
ATOM   524  C  CG  . HIS A 1 70  ? 22.429  -23.082 -2.930  1.00 20.00  ? 293  HIS A CG  1 
ATOM   525  N  ND1 . HIS A 1 70  ? 21.094  -22.744 -2.968  1.00 19.54  ? 293  HIS A ND1 1 
ATOM   526  C  CD2 . HIS A 1 70  ? 22.933  -22.767 -4.148  1.00 21.24  ? 293  HIS A CD2 1 
ATOM   527  C  CE1 . HIS A 1 70  ? 20.800  -22.251 -4.158  1.00 21.64  ? 293  HIS A CE1 1 
ATOM   528  N  NE2 . HIS A 1 70  ? 21.899  -22.248 -4.891  1.00 21.81  ? 293  HIS A NE2 1 
ATOM   529  N  N   . GLU A 1 71  ? 22.908  -24.168 1.307   1.00 31.59  ? 294  GLU A N   1 
ATOM   530  C  CA  . GLU A 1 71  ? 23.367  -25.013 2.401   1.00 37.06  ? 294  GLU A CA  1 
ATOM   531  C  C   . GLU A 1 71  ? 24.134  -26.216 1.851   1.00 46.29  ? 294  GLU A C   1 
ATOM   532  O  O   . GLU A 1 71  ? 24.222  -26.424 0.637   1.00 45.85  ? 294  GLU A O   1 
ATOM   533  C  CB  . GLU A 1 71  ? 22.197  -25.467 3.273   1.00 34.34  ? 294  GLU A CB  1 
ATOM   534  C  CG  . GLU A 1 71  ? 21.508  -24.349 4.054   1.00 30.19  ? 294  GLU A CG  1 
ATOM   535  C  CD  . GLU A 1 71  ? 22.274  -23.885 5.297   1.00 28.06  ? 294  GLU A CD  1 
ATOM   536  O  OE1 . GLU A 1 71  ? 23.447  -24.280 5.482   1.00 28.89  ? 294  GLU A OE1 1 
ATOM   537  O  OE2 . GLU A 1 71  ? 21.688  -23.115 6.095   1.00 26.57  ? 294  GLU A OE2 1 
ATOM   538  N  N   . ASN A 1 72  ? 24.698  -27.013 2.771   1.00 55.56  ? 295  ASN A N   1 
ATOM   539  C  CA  . ASN A 1 72  ? 25.505  -28.186 2.433   1.00 95.90  ? 295  ASN A CA  1 
ATOM   540  C  C   . ASN A 1 72  ? 24.842  -28.994 1.328   1.00 79.07  ? 295  ASN A C   1 
ATOM   541  O  O   . ASN A 1 72  ? 25.349  -29.042 0.203   1.00 77.51  ? 295  ASN A O   1 
ATOM   542  C  CB  . ASN A 1 72  ? 25.731  -29.064 3.669   1.00 47.81  ? 295  ASN A CB  1 
ATOM   543  N  N   . ASN A 1 73  ? 23.718  -29.634 1.650   1.00 98.28  ? 296  ASN A N   1 
ATOM   544  C  CA  . ASN A 1 73  ? 22.733  -30.038 0.653   1.00 40.97  ? 296  ASN A CA  1 
ATOM   545  C  C   . ASN A 1 73  ? 21.437  -30.492 1.312   1.00 48.84  ? 296  ASN A C   1 
ATOM   546  O  O   . ASN A 1 73  ? 21.365  -31.591 1.871   1.00 168.18 ? 296  ASN A O   1 
ATOM   547  C  CB  . ASN A 1 73  ? 23.250  -31.101 -0.318  1.00 126.56 ? 296  ASN A CB  1 
ATOM   548  C  CG  . ASN A 1 73  ? 22.611  -30.977 -1.689  1.00 101.10 ? 296  ASN A CG  1 
ATOM   549  O  OD1 . ASN A 1 73  ? 23.071  -30.206 -2.529  1.00 74.63  ? 296  ASN A OD1 1 
ATOM   550  N  ND2 . ASN A 1 73  ? 21.530  -31.713 -1.910  1.00 134.01 ? 296  ASN A ND2 1 
ATOM   551  N  N   . GLY A 1 74  ? 20.414  -29.644 1.258   1.00 47.63  ? 297  GLY A N   1 
ATOM   552  C  CA  . GLY A 1 74  ? 20.535  -28.327 0.658   1.00 30.45  ? 297  GLY A CA  1 
ATOM   553  C  C   . GLY A 1 74  ? 20.327  -28.257 -0.844  1.00 108.05 ? 297  GLY A C   1 
ATOM   554  O  O   . GLY A 1 74  ? 21.280  -28.305 -1.619  1.00 72.58  ? 297  GLY A O   1 
ATOM   555  N  N   . ASP A 1 75  ? 19.076  -28.111 -1.255  1.00 84.04  ? 298  ASP A N   1 
ATOM   556  C  CA  . ASP A 1 75  ? 18.726  -28.063 -2.665  1.00 60.08  ? 298  ASP A CA  1 
ATOM   557  C  C   . ASP A 1 75  ? 18.858  -26.630 -3.187  1.00 44.49  ? 298  ASP A C   1 
ATOM   558  O  O   . ASP A 1 75  ? 19.310  -25.723 -2.483  1.00 39.91  ? 298  ASP A O   1 
ATOM   559  C  CB  . ASP A 1 75  ? 17.325  -28.635 -2.850  1.00 52.24  ? 298  ASP A CB  1 
ATOM   560  C  CG  . ASP A 1 75  ? 16.294  -27.888 -2.040  1.00 32.68  ? 298  ASP A CG  1 
ATOM   561  O  OD1 . ASP A 1 75  ? 16.009  -26.734 -2.400  1.00 33.09  ? 298  ASP A OD1 1 
ATOM   562  O  OD2 . ASP A 1 75  ? 15.778  -28.443 -1.047  1.00 29.26  ? 298  ASP A OD2 1 
ATOM   563  N  N   . GLN A 1 76  ? 18.440  -26.410 -4.434  1.00 34.82  ? 299  GLN A N   1 
ATOM   564  C  CA  . GLN A 1 76  ? 18.578  -25.106 -5.072  1.00 28.68  ? 299  GLN A CA  1 
ATOM   565  C  C   . GLN A 1 76  ? 17.598  -24.068 -4.538  1.00 25.02  ? 299  GLN A C   1 
ATOM   566  O  O   . GLN A 1 76  ? 17.730  -22.889 -4.883  1.00 23.94  ? 299  GLN A O   1 
ATOM   567  C  CB  . GLN A 1 76  ? 18.435  -25.243 -6.591  1.00 28.95  ? 299  GLN A CB  1 
ATOM   568  C  CG  . GLN A 1 76  ? 19.576  -26.001 -7.251  1.00 31.54  ? 299  GLN A CG  1 
ATOM   569  C  CD  . GLN A 1 76  ? 20.874  -25.212 -7.255  1.00 35.00  ? 299  GLN A CD  1 
ATOM   570  O  OE1 . GLN A 1 76  ? 21.779  -25.476 -6.464  1.00 36.33  ? 299  GLN A OE1 1 
ATOM   571  N  NE2 . GLN A 1 76  ? 20.969  -24.238 -8.150  1.00 36.58  ? 299  GLN A NE2 1 
ATOM   572  N  N   . HIS A 1 77  ? 16.633  -24.467 -3.712  1.00 21.46  ? 300  HIS A N   1 
ATOM   573  C  CA  . HIS A 1 77  ? 15.692  -23.542 -3.096  1.00 19.70  ? 300  HIS A CA  1 
ATOM   574  C  C   . HIS A 1 77  ? 16.098  -23.136 -1.686  1.00 18.48  ? 300  HIS A C   1 
ATOM   575  O  O   . HIS A 1 77  ? 15.378  -22.362 -1.051  1.00 19.83  ? 300  HIS A O   1 
ATOM   576  C  CB  . HIS A 1 77  ? 14.291  -24.163 -3.037  1.00 21.30  ? 300  HIS A CB  1 
ATOM   577  C  CG  . HIS A 1 77  ? 13.638  -24.340 -4.371  1.00 23.89  ? 300  HIS A CG  1 
ATOM   578  N  ND1 . HIS A 1 77  ? 12.802  -23.392 -4.921  1.00 25.09  ? 300  HIS A ND1 1 
ATOM   579  C  CD2 . HIS A 1 77  ? 13.672  -25.369 -5.251  1.00 25.05  ? 300  HIS A CD2 1 
ATOM   580  C  CE1 . HIS A 1 77  ? 12.357  -23.825 -6.087  1.00 25.91  ? 300  HIS A CE1 1 
ATOM   581  N  NE2 . HIS A 1 77  ? 12.872  -25.020 -6.312  1.00 26.59  ? 300  HIS A NE2 1 
ATOM   582  N  N   . GLN A 1 78  ? 17.221  -23.626 -1.174  1.00 18.35  ? 301  GLN A N   1 
ATOM   583  C  CA  . GLN A 1 78  ? 17.606  -23.376 0.210   1.00 17.03  ? 301  GLN A CA  1 
ATOM   584  C  C   . GLN A 1 78  ? 18.922  -22.613 0.273   1.00 16.90  ? 301  GLN A C   1 
ATOM   585  O  O   . GLN A 1 78  ? 19.841  -22.880 -0.510  1.00 19.34  ? 301  GLN A O   1 
ATOM   586  C  CB  . GLN A 1 78  ? 17.721  -24.691 0.984   1.00 18.04  ? 301  GLN A CB  1 
ATOM   587  C  CG  . GLN A 1 78  ? 16.401  -25.437 1.072   1.00 18.57  ? 301  GLN A CG  1 
ATOM   588  C  CD  . GLN A 1 78  ? 16.527  -26.717 1.844   1.00 23.66  ? 301  GLN A CD  1 
ATOM   589  O  OE1 . GLN A 1 78  ? 17.615  -27.274 1.945   1.00 26.32  ? 301  GLN A OE1 1 
ATOM   590  N  NE2 . GLN A 1 78  ? 15.415  -27.199 2.391   1.00 25.21  ? 301  GLN A NE2 1 
ATOM   591  N  N   . TRP A 1 79  ? 19.018  -21.682 1.226   1.00 16.23  ? 302  TRP A N   1 
ATOM   592  C  CA  . TRP A 1 79  ? 20.155  -20.782 1.305   1.00 15.38  ? 302  TRP A CA  1 
ATOM   593  C  C   . TRP A 1 79  ? 20.627  -20.673 2.747   1.00 16.31  ? 302  TRP A C   1 
ATOM   594  O  O   . TRP A 1 79  ? 19.828  -20.732 3.685   1.00 16.60  ? 302  TRP A O   1 
ATOM   595  C  CB  . TRP A 1 79  ? 19.775  -19.384 0.791   1.00 15.45  ? 302  TRP A CB  1 
ATOM   596  C  CG  . TRP A 1 79  ? 19.039  -19.415 -0.524  1.00 16.16  ? 302  TRP A CG  1 
ATOM   597  C  CD1 . TRP A 1 79  ? 17.690  -19.561 -0.701  1.00 16.03  ? 302  TRP A CD1 1 
ATOM   598  C  CD2 . TRP A 1 79  ? 19.606  -19.292 -1.837  1.00 17.15  ? 302  TRP A CD2 1 
ATOM   599  N  NE1 . TRP A 1 79  ? 17.389  -19.555 -2.044  1.00 16.69  ? 302  TRP A NE1 1 
ATOM   600  C  CE2 . TRP A 1 79  ? 18.545  -19.395 -2.761  1.00 17.67  ? 302  TRP A CE2 1 
ATOM   601  C  CE3 . TRP A 1 79  ? 20.909  -19.133 -2.323  1.00 19.56  ? 302  TRP A CE3 1 
ATOM   602  C  CZ2 . TRP A 1 79  ? 18.742  -19.300 -4.140  1.00 19.03  ? 302  TRP A CZ2 1 
ATOM   603  C  CZ3 . TRP A 1 79  ? 21.104  -19.044 -3.691  1.00 20.35  ? 302  TRP A CZ3 1 
ATOM   604  C  CH2 . TRP A 1 79  ? 20.027  -19.136 -4.584  1.00 20.56  ? 302  TRP A CH2 1 
ATOM   605  N  N   . HIS A 1 80  ? 21.940  -20.495 2.908   1.00 16.00  ? 303  HIS A N   1 
ATOM   606  C  CA  . HIS A 1 80  ? 22.570  -20.351 4.216   1.00 16.63  ? 303  HIS A CA  1 
ATOM   607  C  C   . HIS A 1 80  ? 22.542  -18.876 4.604   1.00 16.77  ? 303  HIS A C   1 
ATOM   608  O  O   . HIS A 1 80  ? 23.235  -18.053 3.993   1.00 17.93  ? 303  HIS A O   1 
ATOM   609  C  CB  . HIS A 1 80  ? 24.006  -20.861 4.145   1.00 18.18  ? 303  HIS A CB  1 
ATOM   610  C  CG  . HIS A 1 80  ? 24.743  -20.801 5.448   1.00 19.55  ? 303  HIS A CG  1 
ATOM   611  N  ND1 . HIS A 1 80  ? 24.885  -21.895 6.277   1.00 21.69  ? 303  HIS A ND1 1 
ATOM   612  C  CD2 . HIS A 1 80  ? 25.398  -19.782 6.056   1.00 21.21  ? 303  HIS A CD2 1 
ATOM   613  C  CE1 . HIS A 1 80  ? 25.582  -21.547 7.345   1.00 22.71  ? 303  HIS A CE1 1 
ATOM   614  N  NE2 . HIS A 1 80  ? 25.910  -20.273 7.234   1.00 21.83  ? 303  HIS A NE2 1 
ATOM   615  N  N   . PHE A 1 81  ? 21.762  -18.550 5.635   1.00 15.00  ? 304  PHE A N   1 
ATOM   616  C  CA  . PHE A 1 81  ? 21.562  -17.174 6.091   1.00 16.39  ? 304  PHE A CA  1 
ATOM   617  C  C   . PHE A 1 81  ? 22.397  -16.996 7.356   1.00 16.12  ? 304  PHE A C   1 
ATOM   618  O  O   . PHE A 1 81  ? 21.994  -17.419 8.445   1.00 16.31  ? 304  PHE A O   1 
ATOM   619  C  CB  . PHE A 1 81  ? 20.074  -16.954 6.358   1.00 16.22  ? 304  PHE A CB  1 
ATOM   620  C  CG  . PHE A 1 81  ? 19.659  -15.508 6.528   1.00 16.42  ? 304  PHE A CG  1 
ATOM   621  C  CD1 . PHE A 1 81  ? 20.573  -14.493 6.746   1.00 18.09  ? 304  PHE A CD1 1 
ATOM   622  C  CD2 . PHE A 1 81  ? 18.320  -15.178 6.472   1.00 21.11  ? 304  PHE A CD2 1 
ATOM   623  C  CE1 . PHE A 1 81  ? 20.149  -13.170 6.902   1.00 18.71  ? 304  PHE A CE1 1 
ATOM   624  C  CE2 . PHE A 1 81  ? 17.904  -13.865 6.632   1.00 22.59  ? 304  PHE A CE2 1 
ATOM   625  C  CZ  . PHE A 1 81  ? 18.823  -12.860 6.838   1.00 20.52  ? 304  PHE A CZ  1 
ATOM   626  N  N   . SER A 1 82  ? 23.573  -16.380 7.204   1.00 16.79  ? 305  SER A N   1 
ATOM   627  C  CA  . SER A 1 82  ? 24.395  -16.010 8.351   1.00 17.89  ? 305  SER A CA  1 
ATOM   628  C  C   . SER A 1 82  ? 23.777  -14.803 9.033   1.00 18.11  ? 305  SER A C   1 
ATOM   629  O  O   . SER A 1 82  ? 23.425  -13.820 8.374   1.00 20.47  ? 305  SER A O   1 
ATOM   630  C  CB  . SER A 1 82  ? 25.800  -15.654 7.881   1.00 19.37  ? 305  SER A CB  1 
ATOM   631  O  OG  . SER A 1 82  ? 26.423  -16.769 7.275   1.00 22.25  ? 305  SER A OG  1 
ATOM   632  N  N   . ILE A 1 83  ? 23.651  -14.863 10.352  1.00 16.68  ? 306  ILE A N   1 
ATOM   633  C  CA  . ILE A 1 83  ? 22.917  -13.839 11.085  1.00 18.03  ? 306  ILE A CA  1 
ATOM   634  C  C   . ILE A 1 83  ? 23.832  -13.092 12.049  1.00 19.72  ? 306  ILE A C   1 
ATOM   635  O  O   . ILE A 1 83  ? 24.777  -13.656 12.624  1.00 22.30  ? 306  ILE A O   1 
ATOM   636  C  CB  . ILE A 1 83  ? 21.629  -14.364 11.759  1.00 19.88  ? 306  ILE A CB  1 
ATOM   637  C  CG1 . ILE A 1 83  ? 21.922  -15.446 12.797  1.00 21.99  ? 306  ILE A CG1 1 
ATOM   638  C  CG2 . ILE A 1 83  ? 20.654  -14.889 10.693  1.00 21.96  ? 306  ILE A CG2 1 
ATOM   639  C  CD1 . ILE A 1 83  ? 20.667  -15.995 13.419  1.00 22.50  ? 306  ILE A CD1 1 
ATOM   640  N  N   . THR A 1 84  ? 23.548  -11.799 12.200  1.00 21.10  ? 307  THR A N   1 
ATOM   641  C  CA  . THR A 1 84  ? 24.222  -10.899 13.122  1.00 21.95  ? 307  THR A CA  1 
ATOM   642  C  C   . THR A 1 84  ? 23.248  -10.483 14.216  1.00 21.34  ? 307  THR A C   1 
ATOM   643  O  O   . THR A 1 84  ? 22.077  -10.879 14.229  1.00 21.78  ? 307  THR A O   1 
ATOM   644  C  CB  . THR A 1 84  ? 24.737  -9.652  12.390  1.00 23.87  ? 307  THR A CB  1 
ATOM   645  O  OG1 . THR A 1 84  ? 23.630  -8.843  11.960  1.00 23.68  ? 307  THR A OG1 1 
ATOM   646  C  CG2 . THR A 1 84  ? 25.594  -10.028 11.191  1.00 24.99  ? 307  THR A CG2 1 
ATOM   647  N  N   . ASN A 1 85  ? 23.737  -9.653  15.138  1.00 21.59  ? 308  ASN A N   1 
ATOM   648  C  CA  . ASN A 1 85  ? 22.839  -8.969  16.051  1.00 21.57  ? 308  ASN A CA  1 
ATOM   649  C  C   . ASN A 1 85  ? 21.936  -8.033  15.253  1.00 19.41  ? 308  ASN A C   1 
ATOM   650  O  O   . ASN A 1 85  ? 22.271  -7.640  14.133  1.00 19.68  ? 308  ASN A O   1 
ATOM   651  C  CB  . ASN A 1 85  ? 23.637  -8.170  17.085  1.00 22.29  ? 308  ASN A CB  1 
ATOM   652  C  CG  . ASN A 1 85  ? 24.387  -9.064  18.049  1.00 24.36  ? 308  ASN A CG  1 
ATOM   653  O  OD1 . ASN A 1 85  ? 23.896  -10.123 18.439  1.00 24.86  ? 308  ASN A OD1 1 
ATOM   654  N  ND2 . ASN A 1 85  ? 25.591  -8.650  18.428  1.00 25.48  ? 308  ASN A ND2 1 
ATOM   655  N  N   . PRO A 1 86  ? 20.774  -7.673  15.802  1.00 18.89  ? 309  PRO A N   1 
ATOM   656  C  CA  . PRO A 1 86  ? 19.876  -6.760  15.067  1.00 19.59  ? 309  PRO A CA  1 
ATOM   657  C  C   . PRO A 1 86  ? 20.500  -5.420  14.716  1.00 20.54  ? 309  PRO A C   1 
ATOM   658  O  O   . PRO A 1 86  ? 20.147  -4.845  13.678  1.00 21.39  ? 309  PRO A O   1 
ATOM   659  C  CB  . PRO A 1 86  ? 18.673  -6.618  16.008  1.00 19.66  ? 309  PRO A CB  1 
ATOM   660  C  CG  . PRO A 1 86  ? 18.673  -7.902  16.784  1.00 20.23  ? 309  PRO A CG  1 
ATOM   661  C  CD  . PRO A 1 86  ? 20.126  -8.241  16.999  1.00 19.69  ? 309  PRO A CD  1 
ATOM   662  N  N   . ASN A 1 87  ? 21.430  -4.908  15.523  1.00 23.82  ? 310  ASN A N   1 
ATOM   663  C  CA  . ASN A 1 87  ? 22.056  -3.628  15.206  1.00 26.46  ? 310  ASN A CA  1 
ATOM   664  C  C   . ASN A 1 87  ? 23.195  -3.748  14.200  1.00 28.39  ? 310  ASN A C   1 
ATOM   665  O  O   . ASN A 1 87  ? 23.859  -2.744  13.916  1.00 30.23  ? 310  ASN A O   1 
ATOM   666  C  CB  . ASN A 1 87  ? 22.529  -2.914  16.478  1.00 28.48  ? 310  ASN A CB  1 
ATOM   667  C  CG  . ASN A 1 87  ? 23.660  -3.646  17.191  1.00 29.94  ? 310  ASN A CG  1 
ATOM   668  O  OD1 . ASN A 1 87  ? 24.128  -4.695  16.748  1.00 30.89  ? 310  ASN A OD1 1 
ATOM   669  N  ND2 . ASN A 1 87  ? 24.106  -3.083  18.306  1.00 31.97  ? 310  ASN A ND2 1 
ATOM   670  N  N   . GLY A 1 88  ? 23.435  -4.944  13.659  1.00 28.49  ? 311  GLY A N   1 
ATOM   671  C  CA  . GLY A 1 88  ? 24.477  -5.157  12.680  1.00 29.54  ? 311  GLY A CA  1 
ATOM   672  C  C   . GLY A 1 88  ? 25.793  -5.651  13.239  1.00 30.72  ? 311  GLY A C   1 
ATOM   673  O  O   . GLY A 1 88  ? 26.647  -6.096  12.462  1.00 31.56  ? 311  GLY A O   1 
ATOM   674  N  N   . THR A 1 89  ? 25.990  -5.579  14.552  1.00 30.81  ? 312  THR A N   1 
ATOM   675  C  CA  . THR A 1 89  ? 27.222  -6.066  15.152  1.00 30.83  ? 312  THR A CA  1 
ATOM   676  C  C   . THR A 1 89  ? 27.241  -7.598  15.162  1.00 31.97  ? 312  THR A C   1 
ATOM   677  O  O   . THR A 1 89  ? 26.191  -8.242  15.111  1.00 31.67  ? 312  THR A O   1 
ATOM   678  C  CB  . THR A 1 89  ? 27.380  -5.498  16.566  1.00 31.98  ? 312  THR A CB  1 
ATOM   679  O  OG1 . THR A 1 89  ? 26.247  -5.849  17.373  1.00 31.66  ? 312  THR A OG1 1 
ATOM   680  C  CG2 . THR A 1 89  ? 27.513  -3.974  16.525  1.00 33.53  ? 312  THR A CG2 1 
ATOM   681  N  N   . PRO A 1 90  ? 28.428  -8.206  15.205  1.00 33.03  ? 313  PRO A N   1 
ATOM   682  C  CA  . PRO A 1 90  ? 28.502  -9.675  15.171  1.00 32.21  ? 313  PRO A CA  1 
ATOM   683  C  C   . PRO A 1 90  ? 27.875  -10.315 16.404  1.00 33.01  ? 313  PRO A C   1 
ATOM   684  O  O   . PRO A 1 90  ? 28.031  -9.829  17.527  1.00 34.57  ? 313  PRO A O   1 
ATOM   685  C  CB  . PRO A 1 90  ? 30.010  -9.955  15.112  1.00 33.44  ? 313  PRO A CB  1 
ATOM   686  C  CG  . PRO A 1 90  ? 30.617  -8.697  14.612  1.00 34.47  ? 313  PRO A CG  1 
ATOM   687  C  CD  . PRO A 1 90  ? 29.762  -7.586  15.137  1.00 34.53  ? 313  PRO A CD  1 
ATOM   688  N  N   . PHE A 1 91  ? 27.156  -11.418 16.182  1.00 33.40  ? 314  PHE A N   1 
ATOM   689  C  CA  . PHE A 1 91  ? 26.579  -12.185 17.281  1.00 34.34  ? 314  PHE A CA  1 
ATOM   690  C  C   . PHE A 1 91  ? 27.657  -13.046 17.929  1.00 36.28  ? 314  PHE A C   1 
ATOM   691  O  O   . PHE A 1 91  ? 28.411  -13.736 17.236  1.00 37.60  ? 314  PHE A O   1 
ATOM   692  C  CB  . PHE A 1 91  ? 25.446  -13.078 16.772  1.00 34.21  ? 314  PHE A CB  1 
ATOM   693  C  CG  . PHE A 1 91  ? 24.893  -14.015 17.816  1.00 33.64  ? 314  PHE A CG  1 
ATOM   694  C  CD1 . PHE A 1 91  ? 24.131  -13.530 18.871  1.00 33.13  ? 314  PHE A CD1 1 
ATOM   695  C  CD2 . PHE A 1 91  ? 25.121  -15.383 17.735  1.00 32.60  ? 314  PHE A CD2 1 
ATOM   696  C  CE1 . PHE A 1 91  ? 23.621  -14.387 19.833  1.00 32.48  ? 314  PHE A CE1 1 
ATOM   697  C  CE2 . PHE A 1 91  ? 24.616  -16.244 18.696  1.00 32.71  ? 314  PHE A CE2 1 
ATOM   698  C  CZ  . PHE A 1 91  ? 23.864  -15.749 19.745  1.00 32.49  ? 314  PHE A CZ  1 
ATOM   699  N  N   . ASP A 1 92  ? 27.720  -13.013 19.261  1.00 38.82  ? 315  ASP A N   1 
ATOM   700  C  CA  . ASP A 1 92  ? 28.700  -13.793 20.003  1.00 41.19  ? 315  ASP A CA  1 
ATOM   701  C  C   . ASP A 1 92  ? 28.012  -15.014 20.589  1.00 40.91  ? 315  ASP A C   1 
ATOM   702  O  O   . ASP A 1 92  ? 27.196  -14.869 21.512  1.00 40.36  ? 315  ASP A O   1 
ATOM   703  C  CB  . ASP A 1 92  ? 29.309  -12.946 21.119  1.00 43.70  ? 315  ASP A CB  1 
ATOM   704  C  CG  . ASP A 1 92  ? 30.375  -13.691 21.909  1.00 46.53  ? 315  ASP A CG  1 
ATOM   705  O  OD1 . ASP A 1 92  ? 30.753  -14.812 21.509  1.00 47.47  ? 315  ASP A OD1 1 
ATOM   706  O  OD2 . ASP A 1 92  ? 30.837  -13.150 22.935  1.00 47.86  ? 315  ASP A OD2 1 
ATOM   707  N  N   . PRO A 1 93  ? 28.310  -16.226 20.112  1.00 41.65  ? 316  PRO A N   1 
ATOM   708  C  CA  . PRO A 1 93  ? 27.622  -17.417 20.634  1.00 42.02  ? 316  PRO A CA  1 
ATOM   709  C  C   . PRO A 1 93  ? 28.008  -17.792 22.058  1.00 42.48  ? 316  PRO A C   1 
ATOM   710  O  O   . PRO A 1 93  ? 27.338  -18.647 22.650  1.00 41.80  ? 316  PRO A O   1 
ATOM   711  C  CB  . PRO A 1 93  ? 28.025  -18.524 19.647  1.00 43.65  ? 316  PRO A CB  1 
ATOM   712  C  CG  . PRO A 1 93  ? 28.592  -17.807 18.447  1.00 44.05  ? 316  PRO A CG  1 
ATOM   713  C  CD  . PRO A 1 93  ? 29.192  -16.545 18.979  1.00 42.65  ? 316  PRO A CD  1 
ATOM   714  N  N   . THR A 1 94  ? 29.055  -17.197 22.629  1.00 42.60  ? 317  THR A N   1 
ATOM   715  C  CA  . THR A 1 94  ? 29.512  -17.617 23.949  1.00 42.07  ? 317  THR A CA  1 
ATOM   716  C  C   . THR A 1 94  ? 28.720  -16.999 25.097  1.00 41.39  ? 317  THR A C   1 
ATOM   717  O  O   . THR A 1 94  ? 28.889  -17.433 26.242  1.00 41.94  ? 317  THR A O   1 
ATOM   718  C  CB  . THR A 1 94  ? 31.014  -17.353 24.121  1.00 42.11  ? 317  THR A CB  1 
ATOM   719  O  OG1 . THR A 1 94  ? 31.276  -15.947 24.025  1.00 42.83  ? 317  THR A OG1 1 
ATOM   720  C  CG2 . THR A 1 94  ? 31.811  -18.089 23.050  1.00 42.36  ? 317  THR A CG2 1 
ATOM   721  N  N   . GLU A 1 95  ? 27.861  -16.018 24.830  1.00 39.04  ? 318  GLU A N   1 
ATOM   722  C  CA  . GLU A 1 95  ? 27.048  -15.438 25.890  1.00 36.33  ? 318  GLU A CA  1 
ATOM   723  C  C   . GLU A 1 95  ? 25.949  -16.408 26.306  1.00 33.83  ? 318  GLU A C   1 
ATOM   724  O  O   . GLU A 1 95  ? 25.465  -17.216 25.506  1.00 34.00  ? 318  GLU A O   1 
ATOM   725  C  CB  . GLU A 1 95  ? 26.410  -14.131 25.421  1.00 36.12  ? 318  GLU A CB  1 
ATOM   726  C  CG  . GLU A 1 95  ? 27.394  -13.106 24.875  1.00 64.87  ? 318  GLU A CG  1 
ATOM   727  C  CD  . GLU A 1 95  ? 26.711  -11.827 24.425  1.00 140.05 ? 318  GLU A CD  1 
ATOM   728  O  OE1 . GLU A 1 95  ? 25.613  -11.526 24.938  1.00 55.94  ? 318  GLU A OE1 1 
ATOM   729  O  OE2 . GLU A 1 95  ? 27.270  -11.126 23.555  1.00 133.52 ? 318  GLU A OE2 1 
ATOM   730  N  N   . ASP A 1 96  ? 25.552  -16.321 27.578  0.83 30.75  ? 319  ASP A N   1 
ATOM   731  C  CA  . ASP A 1 96  ? 24.462  -17.134 28.118  0.83 28.54  ? 319  ASP A CA  1 
ATOM   732  C  C   . ASP A 1 96  ? 23.109  -16.555 27.690  0.83 27.24  ? 319  ASP A C   1 
ATOM   733  O  O   . ASP A 1 96  ? 22.298  -16.100 28.497  0.83 26.30  ? 319  ASP A O   1 
ATOM   734  C  CB  . ASP A 1 96  ? 24.588  -17.261 29.632  0.83 29.93  ? 319  ASP A CB  1 
ATOM   735  C  CG  . ASP A 1 96  ? 23.646  -18.305 30.216  0.83 31.27  ? 319  ASP A CG  1 
ATOM   736  O  OD1 . ASP A 1 96  ? 23.575  -19.424 29.669  0.83 31.53  ? 319  ASP A OD1 1 
ATOM   737  O  OD2 . ASP A 1 96  ? 22.991  -18.013 31.238  0.83 31.41  ? 319  ASP A OD2 1 
ATOM   738  N  N   . VAL A 1 97  ? 22.905  -16.559 26.374  1.00 26.28  ? 320  VAL A N   1 
ATOM   739  C  CA  A VAL A 1 97  ? 21.696  -16.069 25.709  0.54 24.96  ? 320  VAL A CA  1 
ATOM   740  C  CA  B VAL A 1 97  ? 21.663  -16.103 25.757  0.46 25.21  ? 320  VAL A CA  1 
ATOM   741  C  C   . VAL A 1 97  ? 21.222  -17.203 24.799  1.00 22.60  ? 320  VAL A C   1 
ATOM   742  O  O   . VAL A 1 97  ? 22.060  -17.967 24.302  1.00 23.36  ? 320  VAL A O   1 
ATOM   743  C  CB  A VAL A 1 97  ? 22.010  -14.783 24.922  0.54 26.27  ? 320  VAL A CB  1 
ATOM   744  C  CB  B VAL A 1 97  ? 21.837  -14.753 25.042  0.46 27.08  ? 320  VAL A CB  1 
ATOM   745  C  CG1 A VAL A 1 97  ? 20.760  -14.134 24.344  0.54 26.60  ? 320  VAL A CG1 1 
ATOM   746  C  CG1 B VAL A 1 97  ? 22.316  -13.684 26.020  0.46 28.30  ? 320  VAL A CG1 1 
ATOM   747  C  CG2 A VAL A 1 97  ? 22.748  -13.788 25.807  0.54 27.68  ? 320  VAL A CG2 1 
ATOM   748  C  CG2 B VAL A 1 97  ? 22.791  -14.886 23.860  0.46 28.04  ? 320  VAL A CG2 1 
ATOM   749  N  N   . PRO A 1 98  ? 19.922  -17.360 24.540  1.00 17.91  ? 321  PRO A N   1 
ATOM   750  C  CA  . PRO A 1 98  ? 19.507  -18.520 23.738  1.00 16.32  ? 321  PRO A CA  1 
ATOM   751  C  C   . PRO A 1 98  ? 19.874  -18.427 22.272  1.00 16.07  ? 321  PRO A C   1 
ATOM   752  O  O   . PRO A 1 98  ? 20.142  -19.462 21.653  1.00 17.84  ? 321  PRO A O   1 
ATOM   753  C  CB  . PRO A 1 98  ? 17.986  -18.560 23.931  1.00 16.01  ? 321  PRO A CB  1 
ATOM   754  C  CG  . PRO A 1 98  ? 17.739  -17.770 25.176  1.00 16.12  ? 321  PRO A CG  1 
ATOM   755  C  CD  . PRO A 1 98  ? 18.759  -16.689 25.145  1.00 17.41  ? 321  PRO A CD  1 
ATOM   756  N  N   . ALA A 1 99  ? 19.892  -17.227 21.704  1.00 14.61  ? 322  ALA A N   1 
ATOM   757  C  CA  . ALA A 1 99  ? 19.977  -17.025 20.268  1.00 14.77  ? 322  ALA A CA  1 
ATOM   758  C  C   . ALA A 1 99  ? 20.048  -15.520 20.055  1.00 14.70  ? 322  ALA A C   1 
ATOM   759  O  O   . ALA A 1 99  ? 19.862  -14.758 21.012  1.00 15.69  ? 322  ALA A O   1 
ATOM   760  C  CB  . ALA A 1 99  ? 18.716  -17.594 19.608  1.00 14.86  ? 322  ALA A CB  1 
ATOM   761  N  N   . PRO A 1 100 ? 20.324  -15.050 18.838  1.00 13.17  ? 323  PRO A N   1 
ATOM   762  C  CA  . PRO A 1 100 ? 20.254  -13.603 18.583  1.00 13.91  ? 323  PRO A CA  1 
ATOM   763  C  C   . PRO A 1 100 ? 18.899  -13.038 18.983  1.00 14.08  ? 323  PRO A C   1 
ATOM   764  O  O   . PRO A 1 100 ? 17.861  -13.700 18.870  1.00 14.66  ? 323  PRO A O   1 
ATOM   765  C  CB  . PRO A 1 100 ? 20.483  -13.504 17.071  1.00 14.59  ? 323  PRO A CB  1 
ATOM   766  C  CG  . PRO A 1 100 ? 21.316  -14.718 16.767  1.00 15.47  ? 323  PRO A CG  1 
ATOM   767  C  CD  . PRO A 1 100 ? 20.781  -15.797 17.651  1.00 14.56  ? 323  PRO A CD  1 
ATOM   768  N  N   . LEU A 1 101 ? 18.922  -11.803 19.476  1.00 13.82  ? 324  LEU A N   1 
ATOM   769  C  CA  . LEU A 1 101 ? 17.693  -11.180 19.951  1.00 14.13  ? 324  LEU A CA  1 
ATOM   770  C  C   . LEU A 1 101 ? 16.636  -11.129 18.849  1.00 13.22  ? 324  LEU A C   1 
ATOM   771  O  O   . LEU A 1 101 ? 16.934  -10.861 17.679  1.00 13.95  ? 324  LEU A O   1 
ATOM   772  C  CB  . LEU A 1 101 ? 17.990  -9.783  20.491  1.00 17.92  ? 324  LEU A CB  1 
ATOM   773  C  CG  . LEU A 1 101 ? 18.976  -9.805  21.675  1.00 20.34  ? 324  LEU A CG  1 
ATOM   774  C  CD1 . LEU A 1 101 ? 19.113  -8.432  22.310  1.00 23.75  ? 324  LEU A CD1 1 
ATOM   775  C  CD2 . LEU A 1 101 ? 18.566  -10.840 22.731  1.00 23.43  ? 324  LEU A CD2 1 
ATOM   776  N  N   . GLY A 1 102 ? 15.397  -11.455 19.218  1.00 11.11  ? 325  GLY A N   1 
ATOM   777  C  CA  . GLY A 1 102 ? 14.294  -11.462 18.286  1.00 12.04  ? 325  GLY A CA  1 
ATOM   778  C  C   . GLY A 1 102 ? 14.076  -12.765 17.545  1.00 11.99  ? 325  GLY A C   1 
ATOM   779  O  O   . GLY A 1 102 ? 13.051  -12.899 16.864  1.00 12.91  ? 325  GLY A O   1 
ATOM   780  N  N   . THR A 1 103 ? 14.983  -13.733 17.658  1.00 12.67  ? 326  THR A N   1 
ATOM   781  C  CA  . THR A 1 103 ? 14.785  -15.025 17.010  1.00 12.36  ? 326  THR A CA  1 
ATOM   782  C  C   . THR A 1 103 ? 13.422  -15.597 17.405  1.00 11.79  ? 326  THR A C   1 
ATOM   783  O  O   . THR A 1 103 ? 13.020  -15.484 18.569  1.00 12.36  ? 326  THR A O   1 
ATOM   784  C  CB  . THR A 1 103 ? 15.886  -15.992 17.476  1.00 12.90  ? 326  THR A CB  1 
ATOM   785  O  OG1 . THR A 1 103 ? 17.167  -15.517 17.037  1.00 14.06  ? 326  THR A OG1 1 
ATOM   786  C  CG2 . THR A 1 103 ? 15.692  -17.419 16.942  1.00 13.02  ? 326  THR A CG2 1 
ATOM   787  N  N   . PRO A 1 104 ? 12.685  -16.209 16.476  1.00 10.81  ? 327  PRO A N   1 
ATOM   788  C  CA  . PRO A 1 104 ? 11.413  -16.840 16.851  1.00 11.63  ? 327  PRO A CA  1 
ATOM   789  C  C   . PRO A 1 104 ? 11.593  -17.875 17.952  1.00 12.07  ? 327  PRO A C   1 
ATOM   790  O  O   . PRO A 1 104 ? 12.615  -18.568 18.032  1.00 13.18  ? 327  PRO A O   1 
ATOM   791  C  CB  . PRO A 1 104 ? 10.953  -17.498 15.550  1.00 11.52  ? 327  PRO A CB  1 
ATOM   792  C  CG  . PRO A 1 104 ? 12.169  -17.612 14.734  1.00 14.86  ? 327  PRO A CG  1 
ATOM   793  C  CD  . PRO A 1 104 ? 13.004  -16.429 15.057  1.00 11.99  ? 327  PRO A CD  1 
ATOM   794  N  N   . ASP A 1 105 ? 10.577  -17.961 18.815  1.00 12.01  ? 328  ASP A N   1 
ATOM   795  C  CA  . ASP A 1 105 ? 10.592  -18.838 19.983  1.00 11.86  ? 328  ASP A CA  1 
ATOM   796  C  C   . ASP A 1 105 ? 9.525   -19.929 19.901  1.00 13.02  ? 328  ASP A C   1 
ATOM   797  O  O   . ASP A 1 105 ? 8.950   -20.324 20.920  1.00 14.83  ? 328  ASP A O   1 
ATOM   798  C  CB  . ASP A 1 105 ? 10.449  -18.010 21.258  1.00 12.44  ? 328  ASP A CB  1 
ATOM   799  C  CG  . ASP A 1 105 ? 9.124   -17.288 21.345  1.00 11.73  ? 328  ASP A CG  1 
ATOM   800  O  OD1 . ASP A 1 105 ? 8.325   -17.331 20.373  1.00 12.50  ? 328  ASP A OD1 1 
ATOM   801  O  OD2 . ASP A 1 105 ? 8.872   -16.677 22.400  1.00 12.67  ? 328  ASP A OD2 1 
ATOM   802  N  N   . PHE A 1 106 ? 9.264   -20.440 18.697  1.00 11.41  ? 329  PHE A N   1 
ATOM   803  C  CA  . PHE A 1 106 ? 8.237   -21.447 18.497  1.00 12.49  ? 329  PHE A CA  1 
ATOM   804  C  C   . PHE A 1 106 ? 8.674   -22.361 17.369  1.00 12.03  ? 329  PHE A C   1 
ATOM   805  O  O   . PHE A 1 106 ? 9.525   -21.998 16.555  1.00 13.59  ? 329  PHE A O   1 
ATOM   806  C  CB  . PHE A 1 106 ? 6.875   -20.825 18.150  1.00 13.17  ? 329  PHE A CB  1 
ATOM   807  C  CG  . PHE A 1 106 ? 6.926   -19.857 16.997  1.00 13.00  ? 329  PHE A CG  1 
ATOM   808  C  CD1 . PHE A 1 106 ? 6.809   -20.301 15.669  1.00 13.12  ? 329  PHE A CD1 1 
ATOM   809  C  CD2 . PHE A 1 106 ? 7.063   -18.495 17.228  1.00 12.64  ? 329  PHE A CD2 1 
ATOM   810  C  CE1 . PHE A 1 106 ? 6.859   -19.410 14.604  1.00 13.88  ? 329  PHE A CE1 1 
ATOM   811  C  CE2 . PHE A 1 106 ? 7.111   -17.592 16.167  1.00 13.28  ? 329  PHE A CE2 1 
ATOM   812  C  CZ  . PHE A 1 106 ? 7.015   -18.037 14.863  1.00 13.02  ? 329  PHE A CZ  1 
ATOM   813  N  N   . LYS A 1 107 ? 8.078   -23.555 17.331  1.00 12.54  ? 330  LYS A N   1 
ATOM   814  C  CA  . LYS A 1 107 ? 8.245   -24.479 16.213  1.00 12.85  ? 330  LYS A CA  1 
ATOM   815  C  C   . LYS A 1 107 ? 7.248   -24.110 15.118  1.00 13.08  ? 330  LYS A C   1 
ATOM   816  O  O   . LYS A 1 107 ? 6.036   -24.090 15.357  1.00 14.30  ? 330  LYS A O   1 
ATOM   817  C  CB  . LYS A 1 107 ? 8.011   -25.915 16.666  1.00 14.60  ? 330  LYS A CB  1 
ATOM   818  C  CG  . LYS A 1 107 ? 9.093   -26.439 17.580  1.00 15.01  ? 330  LYS A CG  1 
ATOM   819  C  CD  . LYS A 1 107 ? 8.816   -27.898 17.926  1.00 16.99  ? 330  LYS A CD  1 
ATOM   820  C  CE  . LYS A 1 107 ? 9.857   -28.461 18.864  1.00 20.18  ? 330  LYS A CE  1 
ATOM   821  N  NZ  . LYS A 1 107 ? 9.496   -29.858 19.269  1.00 23.19  ? 330  LYS A NZ  1 
ATOM   822  N  N   . GLY A 1 108 ? 7.749   -23.819 13.923  1.00 13.49  ? 331  GLY A N   1 
ATOM   823  C  CA  . GLY A 1 108 ? 6.853   -23.490 12.830  1.00 14.38  ? 331  GLY A CA  1 
ATOM   824  C  C   . GLY A 1 108 ? 7.609   -23.037 11.601  1.00 14.00  ? 331  GLY A C   1 
ATOM   825  O  O   . GLY A 1 108 ? 8.843   -22.991 11.576  1.00 15.74  ? 331  GLY A O   1 
ATOM   826  N  N   A GLN A 1 109 ? 6.837   -22.681 10.577  0.42 12.84  ? 332  GLN A N   1 
ATOM   827  N  N   B GLN A 1 109 ? 6.839   -22.743 10.557  0.58 12.16  ? 332  GLN A N   1 
ATOM   828  C  CA  A GLN A 1 109 ? 7.354   -22.260 9.275   0.42 13.13  ? 332  GLN A CA  1 
ATOM   829  C  CA  B GLN A 1 109 ? 7.375   -22.261 9.286   0.58 12.69  ? 332  GLN A CA  1 
ATOM   830  C  C   A GLN A 1 109 ? 7.171   -20.748 9.169   0.42 12.23  ? 332  GLN A C   1 
ATOM   831  C  C   B GLN A 1 109 ? 7.155   -20.757 9.251   0.58 11.25  ? 332  GLN A C   1 
ATOM   832  O  O   A GLN A 1 109 ? 6.127   -20.269 8.727   0.42 13.42  ? 332  GLN A O   1 
ATOM   833  O  O   B GLN A 1 109 ? 6.059   -20.291 8.935   0.58 12.00  ? 332  GLN A O   1 
ATOM   834  C  CB  A GLN A 1 109 ? 6.595   -22.986 8.164   0.42 13.68  ? 332  GLN A CB  1 
ATOM   835  C  CB  B GLN A 1 109 ? 6.645   -22.915 8.120   0.58 13.92  ? 332  GLN A CB  1 
ATOM   836  C  CG  A GLN A 1 109 ? 6.654   -24.492 8.292   0.42 15.62  ? 332  GLN A CG  1 
ATOM   837  C  CG  B GLN A 1 109 ? 6.902   -24.385 7.936   0.58 16.77  ? 332  GLN A CG  1 
ATOM   838  C  CD  A GLN A 1 109 ? 8.060   -25.016 8.135   0.42 16.38  ? 332  GLN A CD  1 
ATOM   839  C  CD  B GLN A 1 109 ? 6.288   -24.865 6.654   0.58 19.03  ? 332  GLN A CD  1 
ATOM   840  O  OE1 A GLN A 1 109 ? 8.726   -24.748 7.133   0.42 18.85  ? 332  GLN A OE1 1 
ATOM   841  O  OE1 B GLN A 1 109 ? 6.890   -24.743 5.590   0.58 20.87  ? 332  GLN A OE1 1 
ATOM   842  N  NE2 A GLN A 1 109 ? 8.525   -25.778 9.124   0.42 15.85  ? 332  GLN A NE2 1 
ATOM   843  N  NE2 B GLN A 1 109 ? 5.067   -25.379 6.736   0.58 21.65  ? 332  GLN A NE2 1 
ATOM   844  N  N   . LEU A 1 110 ? 8.202   -19.998 9.561   1.00 11.60  ? 333  LEU A N   1 
ATOM   845  C  CA  . LEU A 1 110 ? 8.124   -18.537 9.566   1.00 11.81  ? 333  LEU A CA  1 
ATOM   846  C  C   . LEU A 1 110 ? 8.199   -17.997 8.137   1.00 11.47  ? 333  LEU A C   1 
ATOM   847  O  O   . LEU A 1 110 ? 9.199   -18.199 7.437   1.00 13.39  ? 333  LEU A O   1 
ATOM   848  C  CB  . LEU A 1 110 ? 9.266   -17.988 10.421  1.00 12.69  ? 333  LEU A CB  1 
ATOM   849  C  CG  . LEU A 1 110 ? 9.369   -16.464 10.531  1.00 12.99  ? 333  LEU A CG  1 
ATOM   850  C  CD1 . LEU A 1 110 ? 8.111   -15.846 11.133  1.00 13.68  ? 333  LEU A CD1 1 
ATOM   851  C  CD2 . LEU A 1 110 ? 10.583  -16.060 11.347  1.00 14.60  ? 333  LEU A CD2 1 
ATOM   852  N  N   . TYR A 1 111 ? 7.143   -17.308 7.707   1.00 10.63  ? 334  TYR A N   1 
ATOM   853  C  CA  . TYR A 1 111 ? 7.018   -16.832 6.337   1.00 10.47  ? 334  TYR A CA  1 
ATOM   854  C  C   . TYR A 1 111 ? 7.238   -15.327 6.301   1.00 10.76  ? 334  TYR A C   1 
ATOM   855  O  O   . TYR A 1 111 ? 6.748   -14.600 7.167   1.00 11.64  ? 334  TYR A O   1 
ATOM   856  C  CB  . TYR A 1 111 ? 5.623   -17.168 5.789   1.00 10.92  ? 334  TYR A CB  1 
ATOM   857  C  CG  . TYR A 1 111 ? 5.167   -16.348 4.603   1.00 10.68  ? 334  TYR A CG  1 
ATOM   858  C  CD1 . TYR A 1 111 ? 5.781   -16.467 3.360   1.00 11.67  ? 334  TYR A CD1 1 
ATOM   859  C  CD2 . TYR A 1 111 ? 4.094   -15.472 4.721   1.00 12.73  ? 334  TYR A CD2 1 
ATOM   860  C  CE1 . TYR A 1 111 ? 5.349   -15.703 2.265   1.00 11.66  ? 334  TYR A CE1 1 
ATOM   861  C  CE2 . TYR A 1 111 ? 3.645   -14.706 3.636   1.00 12.44  ? 334  TYR A CE2 1 
ATOM   862  C  CZ  . TYR A 1 111 ? 4.278   -14.825 2.405   1.00 11.83  ? 334  TYR A CZ  1 
ATOM   863  O  OH  . TYR A 1 111 ? 3.843   -14.068 1.326   1.00 13.86  ? 334  TYR A OH  1 
ATOM   864  N  N   . GLY A 1 112 ? 7.995   -14.866 5.309   1.00 11.28  ? 335  GLY A N   1 
ATOM   865  C  CA  . GLY A 1 112 ? 8.186   -13.437 5.151   1.00 10.79  ? 335  GLY A CA  1 
ATOM   866  C  C   . GLY A 1 112 ? 8.955   -13.119 3.893   1.00 9.95   ? 335  GLY A C   1 
ATOM   867  O  O   . GLY A 1 112 ? 8.854   -13.870 2.922   1.00 11.26  ? 335  GLY A O   1 
ATOM   868  N  N   . VAL A 1 113 ? 9.712   -12.018 3.882   1.00 10.34  ? 336  VAL A N   1 
ATOM   869  C  CA  . VAL A 1 113 ? 10.425  -11.561 2.696   1.00 11.02  ? 336  VAL A CA  1 
ATOM   870  C  C   . VAL A 1 113 ? 11.889  -11.367 3.061   1.00 10.28  ? 336  VAL A C   1 
ATOM   871  O  O   . VAL A 1 113 ? 12.206  -10.696 4.056   1.00 11.83  ? 336  VAL A O   1 
ATOM   872  C  CB  . VAL A 1 113 ? 9.819   -10.251 2.155   1.00 11.17  ? 336  VAL A CB  1 
ATOM   873  C  CG1 . VAL A 1 113 ? 10.694  -9.629  1.054   1.00 12.34  ? 336  VAL A CG1 1 
ATOM   874  C  CG2 . VAL A 1 113 ? 8.398   -10.507 1.646   1.00 12.29  ? 336  VAL A CG2 1 
ATOM   875  N  N   . ILE A 1 114 ? 12.776  -11.978 2.282   1.00 10.48  ? 337  ILE A N   1 
ATOM   876  C  CA  . ILE A 1 114 ? 14.202  -11.688 2.374   1.00 11.35  ? 337  ILE A CA  1 
ATOM   877  C  C   . ILE A 1 114 ? 14.536  -10.590 1.373   1.00 11.23  ? 337  ILE A C   1 
ATOM   878  O  O   . ILE A 1 114 ? 14.213  -10.699 0.183   1.00 12.10  ? 337  ILE A O   1 
ATOM   879  C  CB  . ILE A 1 114 ? 15.066  -12.953 2.180   1.00 12.58  ? 337  ILE A CB  1 
ATOM   880  C  CG1 . ILE A 1 114 ? 16.545  -12.572 2.237   1.00 14.65  ? 337  ILE A CG1 1 
ATOM   881  C  CG2 . ILE A 1 114 ? 14.770  -13.668 0.869   1.00 12.92  ? 337  ILE A CG2 1 
ATOM   882  C  CD1 . ILE A 1 114 ? 17.489  -13.746 2.343   1.00 17.29  ? 337  ILE A CD1 1 
ATOM   883  N  N   A SER A 1 115 ? 15.149  -9.517  1.864   0.77 11.00  ? 338  SER A N   1 
ATOM   884  N  N   B SER A 1 115 ? 15.177  -9.529  1.849   0.23 10.98  ? 338  SER A N   1 
ATOM   885  C  CA  A SER A 1 115 ? 15.590  -8.398  1.050   0.77 10.93  ? 338  SER A CA  1 
ATOM   886  C  CA  B SER A 1 115 ? 15.569  -8.410  1.006   0.23 10.75  ? 338  SER A CA  1 
ATOM   887  C  C   A SER A 1 115 ? 17.110  -8.324  1.060   0.77 12.04  ? 338  SER A C   1 
ATOM   888  C  C   B SER A 1 115 ? 17.076  -8.213  1.081   0.23 11.95  ? 338  SER A C   1 
ATOM   889  O  O   A SER A 1 115 ? 17.757  -8.633  2.063   0.77 13.20  ? 338  SER A O   1 
ATOM   890  O  O   B SER A 1 115 ? 17.674  -8.331  2.155   0.23 11.91  ? 338  SER A O   1 
ATOM   891  C  CB  A SER A 1 115 ? 15.026  -7.080  1.592   0.77 12.17  ? 338  SER A CB  1 
ATOM   892  C  CB  B SER A 1 115 ? 14.852  -7.129  1.427   0.23 9.94   ? 338  SER A CB  1 
ATOM   893  O  OG  A SER A 1 115 ? 13.617  -7.080  1.578   0.77 12.89  ? 338  SER A OG  1 
ATOM   894  O  OG  B SER A 1 115 ? 15.030  -6.885  2.806   0.23 9.35   ? 338  SER A OG  1 
ATOM   895  N  N   . GLN A 1 116 ? 17.681  -7.908  -0.066  1.00 13.62  ? 339  GLN A N   1 
ATOM   896  C  CA  . GLN A 1 116 ? 19.122  -7.772  -0.192  1.00 13.33  ? 339  GLN A CA  1 
ATOM   897  C  C   . GLN A 1 116 ? 19.481  -6.433  -0.817  1.00 14.18  ? 339  GLN A C   1 
ATOM   898  O  O   . GLN A 1 116 ? 18.772  -5.941  -1.698  1.00 14.09  ? 339  GLN A O   1 
ATOM   899  C  CB  . GLN A 1 116 ? 19.687  -8.857  -1.092  1.00 14.49  ? 339  GLN A CB  1 
ATOM   900  C  CG  . GLN A 1 116 ? 19.306  -10.268 -0.684  1.00 14.78  ? 339  GLN A CG  1 
ATOM   901  C  CD  . GLN A 1 116 ? 20.162  -11.319 -1.374  1.00 15.48  ? 339  GLN A CD  1 
ATOM   902  O  OE1 . GLN A 1 116 ? 20.299  -11.309 -2.596  1.00 15.62  ? 339  GLN A OE1 1 
ATOM   903  N  NE2 . GLN A 1 116 ? 20.769  -12.206 -0.591  1.00 15.41  ? 339  GLN A NE2 1 
ATOM   904  N  N   A ARG A 1 117 ? 20.604  -5.869  -0.369  0.42 13.96  ? 340  ARG A N   1 
ATOM   905  N  N   B ARG A 1 117 ? 20.571  -5.833  -0.335  0.58 14.23  ? 340  ARG A N   1 
ATOM   906  C  CA  A ARG A 1 117 ? 21.191  -4.666  -0.951  0.42 14.36  ? 340  ARG A CA  1 
ATOM   907  C  CA  B ARG A 1 117 ? 21.191  -4.672  -0.968  0.58 15.16  ? 340  ARG A CA  1 
ATOM   908  C  C   A ARG A 1 117 ? 22.689  -4.915  -1.045  0.42 15.60  ? 340  ARG A C   1 
ATOM   909  C  C   B ARG A 1 117 ? 22.680  -4.962  -1.055  0.58 15.32  ? 340  ARG A C   1 
ATOM   910  O  O   A ARG A 1 117 ? 23.340  -5.137  -0.020  0.42 17.85  ? 340  ARG A O   1 
ATOM   911  O  O   B ARG A 1 117 ? 23.312  -5.262  -0.038  0.58 16.51  ? 340  ARG A O   1 
ATOM   912  C  CB  A ARG A 1 117 ? 20.899  -3.441  -0.078  0.42 13.63  ? 340  ARG A CB  1 
ATOM   913  C  CB  B ARG A 1 117 ? 20.931  -3.377  -0.189  0.58 15.43  ? 340  ARG A CB  1 
ATOM   914  C  CG  A ARG A 1 117 ? 21.291  -2.107  -0.706  0.42 14.03  ? 340  ARG A CG  1 
ATOM   915  C  CG  B ARG A 1 117 ? 21.718  -2.169  -0.724  0.58 16.73  ? 340  ARG A CG  1 
ATOM   916  C  CD  A ARG A 1 117 ? 21.173  -0.946  0.288   0.42 14.91  ? 340  ARG A CD  1 
ATOM   917  C  CD  B ARG A 1 117 ? 21.212  -0.837  -0.172  0.58 17.02  ? 340  ARG A CD  1 
ATOM   918  N  NE  A ARG A 1 117 ? 22.282  -0.898  1.235   0.42 16.22  ? 340  ARG A NE  1 
ATOM   919  N  NE  B ARG A 1 117 ? 19.805  -0.652  -0.504  0.58 17.08  ? 340  ARG A NE  1 
ATOM   920  C  CZ  A ARG A 1 117 ? 22.430  0.027   2.174   0.42 16.43  ? 340  ARG A CZ  1 
ATOM   921  C  CZ  B ARG A 1 117 ? 18.823  -0.551  0.383   0.58 16.37  ? 340  ARG A CZ  1 
ATOM   922  N  NH1 A ARG A 1 117 ? 21.536  0.988   2.349   0.42 16.94  ? 340  ARG A NH1 1 
ATOM   923  N  NH1 B ARG A 1 117 ? 19.067  -0.476  1.683   0.58 18.58  ? 340  ARG A NH1 1 
ATOM   924  N  NH2 A ARG A 1 117 ? 23.505  -0.010  2.956   0.42 15.63  ? 340  ARG A NH2 1 
ATOM   925  N  NH2 B ARG A 1 117 ? 17.564  -0.541  -0.046  0.58 11.24  ? 340  ARG A NH2 1 
ATOM   926  N  N   . ASN A 1 118 ? 23.227  -4.909  -2.265  1.00 16.23  ? 341  ASN A N   1 
ATOM   927  C  CA  . ASN A 1 118 ? 24.606  -5.334  -2.479  1.00 16.70  ? 341  ASN A CA  1 
ATOM   928  C  C   . ASN A 1 118 ? 25.616  -4.415  -1.789  1.00 18.65  ? 341  ASN A C   1 
ATOM   929  O  O   . ASN A 1 118 ? 25.372  -3.222  -1.579  1.00 18.72  ? 341  ASN A O   1 
ATOM   930  C  CB  . ASN A 1 118 ? 24.899  -5.405  -3.978  1.00 17.71  ? 341  ASN A CB  1 
ATOM   931  C  CG  . ASN A 1 118 ? 24.240  -6.605  -4.642  1.00 19.21  ? 341  ASN A CG  1 
ATOM   932  O  OD1 . ASN A 1 118 ? 23.285  -7.169  -4.105  1.00 19.36  ? 341  ASN A OD1 1 
ATOM   933  N  ND2 . ASN A 1 118 ? 24.749  -7.008  -5.806  1.00 20.68  ? 341  ASN A ND2 1 
ATOM   934  N  N   . ARG A 1 119 ? 26.780  -4.997  -1.473  1.00 21.54  ? 342  ARG A N   1 
ATOM   935  C  CA  . ARG A 1 119 ? 27.838  -4.305  -0.737  1.00 25.40  ? 342  ARG A CA  1 
ATOM   936  C  C   . ARG A 1 119 ? 28.479  -3.194  -1.553  1.00 31.04  ? 342  ARG A C   1 
ATOM   937  O  O   . ARG A 1 119 ? 28.851  -2.152  -1.001  1.00 31.32  ? 342  ARG A O   1 
ATOM   938  C  CB  . ARG A 1 119 ? 28.931  -5.297  -0.358  1.00 27.39  ? 342  ARG A CB  1 
ATOM   939  C  CG  . ARG A 1 119 ? 28.593  -6.191  0.773   1.00 29.22  ? 342  ARG A CG  1 
ATOM   940  C  CD  . ARG A 1 119 ? 29.727  -7.142  1.066   1.00 30.47  ? 342  ARG A CD  1 
ATOM   941  N  NE  . ARG A 1 119 ? 29.183  -8.306  1.740   1.00 32.45  ? 342  ARG A NE  1 
ATOM   942  C  CZ  . ARG A 1 119 ? 28.734  -9.381  1.112   1.00 32.75  ? 342  ARG A CZ  1 
ATOM   943  N  NH1 . ARG A 1 119 ? 28.876  -9.527  -0.195  1.00 32.54  ? 342  ARG A NH1 1 
ATOM   944  N  NH2 . ARG A 1 119 ? 28.114  -10.325 1.811   1.00 34.72  ? 342  ARG A NH2 1 
ATOM   945  N  N   A GLU A 1 120 ? 28.651  -3.399  -2.854  0.50 33.75  ? 343  GLU A N   1 
ATOM   946  N  N   B GLU A 1 120 ? 28.651  -3.399  -2.854  0.50 33.75  ? 343  GLU A N   1 
ATOM   947  C  CA  A GLU A 1 120 ? 29.290  -2.403  -3.699  0.50 38.63  ? 343  GLU A CA  1 
ATOM   948  C  CA  B GLU A 1 120 ? 29.290  -2.403  -3.699  0.50 38.63  ? 343  GLU A CA  1 
ATOM   949  C  C   A GLU A 1 120 ? 28.341  -1.941  -4.795  0.50 40.32  ? 343  GLU A C   1 
ATOM   950  C  C   B GLU A 1 120 ? 28.341  -1.941  -4.795  0.50 40.32  ? 343  GLU A C   1 
ATOM   951  O  O   A GLU A 1 120 ? 27.502  -2.705  -5.279  0.50 39.65  ? 343  GLU A O   1 
ATOM   952  O  O   B GLU A 1 120 ? 27.502  -2.705  -5.279  0.50 39.65  ? 343  GLU A O   1 
ATOM   953  C  CB  A GLU A 1 120 ? 30.601  -2.916  -4.309  0.50 41.87  ? 343  GLU A CB  1 
ATOM   954  C  CB  B GLU A 1 120 ? 30.601  -2.916  -4.309  0.50 41.87  ? 343  GLU A CB  1 
ATOM   955  C  CG  A GLU A 1 120 ? 31.811  -2.718  -3.410  0.50 44.54  ? 343  GLU A CG  1 
ATOM   956  C  CG  B GLU A 1 120 ? 31.811  -2.718  -3.410  0.50 44.54  ? 343  GLU A CG  1 
ATOM   957  C  CD  A GLU A 1 120 ? 33.105  -2.597  -4.191  0.50 47.07  ? 343  GLU A CD  1 
ATOM   958  C  CD  B GLU A 1 120 ? 33.105  -2.597  -4.191  0.50 47.07  ? 343  GLU A CD  1 
ATOM   959  O  OE1 . GLU A 1 120 ? 33.180  -3.150  -5.309  1.00 48.02  ? 343  GLU A OE1 1 
ATOM   960  O  OE2 . GLU A 1 120 ? 34.045  -1.940  -3.693  1.00 47.81  ? 343  GLU A OE2 1 
ATOM   961  N  N   . GLY A 1 121 ? 28.482  -0.675  -5.174  1.00 42.52  ? 344  GLY A N   1 
ATOM   962  C  CA  . GLY A 1 121 ? 27.664  -0.117  -6.225  1.00 46.44  ? 344  GLY A CA  1 
ATOM   963  C  C   . GLY A 1 121 ? 28.080  -0.613  -7.595  1.00 50.68  ? 344  GLY A C   1 
ATOM   964  O  O   . GLY A 1 121 ? 29.081  -1.308  -7.776  1.00 50.92  ? 344  GLY A O   1 
ATOM   965  N  N   . SER A 1 122 ? 27.275  -0.242  -8.585  1.00 54.31  ? 345  SER A N   1 
ATOM   966  C  CA  . SER A 1 122 ? 27.521  -0.599  -9.974  1.00 58.17  ? 345  SER A CA  1 
ATOM   967  C  C   . SER A 1 122 ? 28.087  0.609   -10.708 1.00 61.13  ? 345  SER A C   1 
ATOM   968  O  O   . SER A 1 122 ? 27.493  1.692   -10.677 1.00 62.04  ? 345  SER A O   1 
ATOM   969  C  CB  . SER A 1 122 ? 26.224  -1.051  -10.645 1.00 58.63  ? 345  SER A CB  1 
ATOM   970  O  OG  . SER A 1 122 ? 26.416  -1.262  -12.032 1.00 58.87  ? 345  SER A OG  1 
ATOM   971  N  N   . SER A 1 123 ? 29.234  0.418   -11.366 1.00 62.35  ? 346  SER A N   1 
ATOM   972  C  CA  . SER A 1 123 ? 29.858  1.513   -12.102 1.00 63.39  ? 346  SER A CA  1 
ATOM   973  C  C   . SER A 1 123 ? 28.953  2.036   -13.210 1.00 64.77  ? 346  SER A C   1 
ATOM   974  O  O   . SER A 1 123 ? 28.997  3.228   -13.536 1.00 65.11  ? 346  SER A O   1 
ATOM   975  C  CB  . SER A 1 123 ? 31.202  1.064   -12.676 1.00 62.95  ? 346  SER A CB  1 
ATOM   976  N  N   . GLY A 1 124 ? 28.128  1.168   -13.797 1.00 65.74  ? 347  GLY A N   1 
ATOM   977  C  CA  . GLY A 1 124 ? 27.216  1.589   -14.843 1.00 66.47  ? 347  GLY A CA  1 
ATOM   978  C  C   . GLY A 1 124 ? 25.922  2.209   -14.364 1.00 66.71  ? 347  GLY A C   1 
ATOM   979  O  O   . GLY A 1 124 ? 25.151  2.706   -15.190 1.00 67.21  ? 347  GLY A O   1 
ATOM   980  N  N   . ASN A 1 125 ? 25.666  2.200   -13.058 1.00 65.67  ? 348  ASN A N   1 
ATOM   981  C  CA  . ASN A 1 125 ? 24.432  2.731   -12.491 1.00 64.08  ? 348  ASN A CA  1 
ATOM   982  C  C   . ASN A 1 125 ? 24.710  3.797   -11.435 1.00 61.97  ? 348  ASN A C   1 
ATOM   983  O  O   . ASN A 1 125 ? 24.044  3.861   -10.400 1.00 61.92  ? 348  ASN A O   1 
ATOM   984  C  CB  . ASN A 1 125 ? 23.549  1.614   -11.938 1.00 64.24  ? 348  ASN A CB  1 
ATOM   985  C  CG  . ASN A 1 125 ? 23.148  0.610   -13.003 1.00 64.51  ? 348  ASN A CG  1 
ATOM   986  O  OD1 . ASN A 1 125 ? 23.860  -0.362  -13.255 1.00 64.85  ? 348  ASN A OD1 1 
ATOM   987  N  ND2 . ASN A 1 125 ? 22.003  0.841   -13.635 1.00 64.33  ? 348  ASN A ND2 1 
ATOM   988  N  N   . GLY A 1 126 ? 25.697  4.651   -11.691 1.00 59.52  ? 349  GLY A N   1 
ATOM   989  C  CA  . GLY A 1 126 ? 26.001  5.744   -10.778 1.00 56.81  ? 349  GLY A CA  1 
ATOM   990  C  C   . GLY A 1 126 ? 26.504  5.296   -9.424  1.00 54.16  ? 349  GLY A C   1 
ATOM   991  O  O   . GLY A 1 126 ? 26.206  5.941   -8.409  1.00 53.92  ? 349  GLY A O   1 
ATOM   992  N  N   . ASN A 1 127 ? 27.271  4.202   -9.388  1.00 51.16  ? 350  ASN A N   1 
ATOM   993  C  CA  A ASN A 1 127 ? 27.797  3.641   -8.142  0.59 49.87  ? 350  ASN A CA  1 
ATOM   994  C  CA  B ASN A 1 127 ? 27.797  3.648   -8.140  0.41 49.39  ? 350  ASN A CA  1 
ATOM   995  C  C   . ASN A 1 127 ? 26.680  3.344   -7.143  1.00 47.72  ? 350  ASN A C   1 
ATOM   996  O  O   . ASN A 1 127 ? 26.835  3.524   -5.933  1.00 48.82  ? 350  ASN A O   1 
ATOM   997  C  CB  A ASN A 1 127 ? 28.894  4.517   -7.526  0.59 50.38  ? 350  ASN A CB  1 
ATOM   998  C  CB  B ASN A 1 127 ? 28.882  4.536   -7.524  0.41 48.95  ? 350  ASN A CB  1 
ATOM   999  C  CG  A ASN A 1 127 ? 29.727  3.772   -6.494  0.59 50.70  ? 350  ASN A CG  1 
ATOM   1000 C  CG  B ASN A 1 127 ? 30.151  4.564   -8.353  0.41 48.43  ? 350  ASN A CG  1 
ATOM   1001 O  OD1 A ASN A 1 127 ? 30.122  2.626   -6.708  0.59 50.86  ? 350  ASN A OD1 1 
ATOM   1002 O  OD1 B ASN A 1 127 ? 30.560  3.548   -8.915  0.41 48.50  ? 350  ASN A OD1 1 
ATOM   1003 N  ND2 A ASN A 1 127 ? 29.988  4.420   -5.365  0.59 50.50  ? 350  ASN A ND2 1 
ATOM   1004 N  ND2 B ASN A 1 127 ? 30.779  5.731   -8.435  0.41 47.88  ? 350  ASN A ND2 1 
ATOM   1005 N  N   . GLN A 1 128 ? 25.542  2.884   -7.653  1.00 42.12  ? 351  GLN A N   1 
ATOM   1006 C  CA  . GLN A 1 128 ? 24.410  2.530   -6.813  1.00 35.53  ? 351  GLN A CA  1 
ATOM   1007 C  C   . GLN A 1 128 ? 24.352  1.021   -6.606  1.00 29.98  ? 351  GLN A C   1 
ATOM   1008 O  O   . GLN A 1 128 ? 24.771  0.232   -7.458  1.00 30.83  ? 351  GLN A O   1 
ATOM   1009 C  CB  . GLN A 1 128 ? 23.087  3.030   -7.404  1.00 37.07  ? 351  GLN A CB  1 
ATOM   1010 C  CG  . GLN A 1 128 ? 22.855  4.525   -7.250  1.00 41.65  ? 351  GLN A CG  1 
ATOM   1011 C  CD  . GLN A 1 128 ? 21.424  4.927   -7.558  1.00 46.01  ? 351  GLN A CD  1 
ATOM   1012 O  OE1 . GLN A 1 128 ? 20.860  4.528   -8.575  1.00 46.97  ? 351  GLN A OE1 1 
ATOM   1013 N  NE2 . GLN A 1 128 ? 20.828  5.718   -6.673  1.00 47.92  ? 351  GLN A NE2 1 
ATOM   1014 N  N   . LYS A 1 129 ? 23.817  0.629   -5.461  1.00 23.53  ? 352  LYS A N   1 
ATOM   1015 C  CA  . LYS A 1 129 ? 23.786  -0.768  -5.058  1.00 20.73  ? 352  LYS A CA  1 
ATOM   1016 C  C   . LYS A 1 129 ? 22.545  -1.458  -5.602  1.00 18.09  ? 352  LYS A C   1 
ATOM   1017 O  O   . LYS A 1 129 ? 21.442  -0.911  -5.562  1.00 18.32  ? 352  LYS A O   1 
ATOM   1018 C  CB  . LYS A 1 129 ? 23.812  -0.862  -3.534  1.00 19.71  ? 352  LYS A CB  1 
ATOM   1019 C  CG  . LYS A 1 129 ? 25.081  -0.268  -2.931  1.00 21.20  ? 352  LYS A CG  1 
ATOM   1020 C  CD  . LYS A 1 129 ? 24.980  -0.104  -1.427  1.00 23.03  ? 352  LYS A CD  1 
ATOM   1021 C  CE  . LYS A 1 129 ? 26.333  0.282   -0.842  1.00 26.61  ? 352  LYS A CE  1 
ATOM   1022 N  NZ  . LYS A 1 129 ? 26.265  0.579   0.613   1.00 29.18  ? 352  LYS A NZ  1 
ATOM   1023 N  N   . ALA A 1 130 ? 22.736  -2.668  -6.110  1.00 17.67  ? 353  ALA A N   1 
ATOM   1024 C  CA  . ALA A 1 130 ? 21.613  -3.457  -6.586  1.00 16.81  ? 353  ALA A CA  1 
ATOM   1025 C  C   . ALA A 1 130 ? 20.809  -4.014  -5.412  1.00 17.02  ? 353  ALA A C   1 
ATOM   1026 O  O   . ALA A 1 130 ? 21.351  -4.304  -4.341  1.00 19.21  ? 353  ALA A O   1 
ATOM   1027 C  CB  . ALA A 1 130 ? 22.129  -4.606  -7.449  1.00 17.04  ? 353  ALA A CB  1 
ATOM   1028 N  N   . ASN A 1 131 ? 19.500  -4.169  -5.629  1.00 15.67  ? 354  ASN A N   1 
ATOM   1029 C  CA  . ASN A 1 131 ? 18.566  -4.664  -4.621  1.00 13.50  ? 354  ASN A CA  1 
ATOM   1030 C  C   . ASN A 1 131 ? 17.737  -5.807  -5.196  1.00 13.96  ? 354  ASN A C   1 
ATOM   1031 O  O   . ASN A 1 131 ? 17.475  -5.860  -6.400  1.00 16.12  ? 354  ASN A O   1 
ATOM   1032 C  CB  . ASN A 1 131 ? 17.556  -3.580  -4.195  1.00 13.34  ? 354  ASN A CB  1 
ATOM   1033 C  CG  . ASN A 1 131 ? 18.203  -2.406  -3.465  1.00 13.75  ? 354  ASN A CG  1 
ATOM   1034 O  OD1 . ASN A 1 131 ? 18.066  -2.261  -2.241  1.00 14.50  ? 354  ASN A OD1 1 
ATOM   1035 N  ND2 . ASN A 1 131 ? 18.882  -1.541  -4.211  1.00 16.02  ? 354  ASN A ND2 1 
ATOM   1036 N  N   . ARG A 1 132 ? 17.302  -6.715  -4.320  1.00 13.86  ? 355  ARG A N   1 
ATOM   1037 C  CA  . ARG A 1 132 ? 16.282  -7.700  -4.679  1.00 14.26  ? 355  ARG A CA  1 
ATOM   1038 C  C   . ARG A 1 132 ? 15.594  -8.183  -3.409  1.00 12.53  ? 355  ARG A C   1 
ATOM   1039 O  O   . ARG A 1 132 ? 16.209  -8.246  -2.340  1.00 14.63  ? 355  ARG A O   1 
ATOM   1040 C  CB  . ARG A 1 132 ? 16.858  -8.895  -5.458  1.00 14.78  ? 355  ARG A CB  1 
ATOM   1041 C  CG  . ARG A 1 132 ? 17.796  -9.799  -4.652  1.00 15.05  ? 355  ARG A CG  1 
ATOM   1042 C  CD  . ARG A 1 132 ? 18.840  -10.457 -5.552  1.00 16.19  ? 355  ARG A CD  1 
ATOM   1043 N  NE  . ARG A 1 132 ? 19.651  -9.445  -6.222  1.00 17.01  ? 355  ARG A NE  1 
ATOM   1044 C  CZ  . ARG A 1 132 ? 20.624  -8.753  -5.633  1.00 17.77  ? 355  ARG A CZ  1 
ATOM   1045 N  NH1 . ARG A 1 132 ? 20.996  -9.001  -4.384  1.00 17.98  ? 355  ARG A NH1 1 
ATOM   1046 N  NH2 . ARG A 1 132 ? 21.232  -7.781  -6.310  1.00 18.63  ? 355  ARG A NH2 1 
ATOM   1047 N  N   . SER A 1 133 ? 14.309  -8.514  -3.532  1.00 12.38  ? 356  SER A N   1 
ATOM   1048 C  CA  . SER A 1 133 ? 13.558  -9.115  -2.437  1.00 12.14  ? 356  SER A CA  1 
ATOM   1049 C  C   . SER A 1 133 ? 12.733  -10.261 -2.991  1.00 13.19  ? 356  SER A C   1 
ATOM   1050 O  O   . SER A 1 133 ? 12.270  -10.209 -4.133  1.00 13.74  ? 356  SER A O   1 
ATOM   1051 C  CB  . SER A 1 133 ? 12.568  -8.149  -1.798  1.00 12.41  ? 356  SER A CB  1 
ATOM   1052 O  OG  . SER A 1 133 ? 13.218  -7.049  -1.185  1.00 13.32  ? 356  SER A OG  1 
ATOM   1053 N  N   . HIS A 1 134 ? 12.538  -11.289 -2.165  1.00 12.75  ? 357  HIS A N   1 
ATOM   1054 C  CA  . HIS A 1 134 ? 11.732  -12.453 -2.524  1.00 13.22  ? 357  HIS A CA  1 
ATOM   1055 C  C   . HIS A 1 134 ? 11.070  -13.022 -1.281  1.00 11.74  ? 357  HIS A C   1 
ATOM   1056 O  O   . HIS A 1 134 ? 11.576  -12.888 -0.163  1.00 13.34  ? 357  HIS A O   1 
ATOM   1057 C  CB  . HIS A 1 134 ? 12.571  -13.544 -3.201  1.00 13.69  ? 357  HIS A CB  1 
ATOM   1058 C  CG  . HIS A 1 134 ? 13.041  -13.157 -4.564  1.00 15.31  ? 357  HIS A CG  1 
ATOM   1059 N  ND1 . HIS A 1 134 ? 12.195  -13.120 -5.652  1.00 18.38  ? 357  HIS A ND1 1 
ATOM   1060 C  CD2 . HIS A 1 134 ? 14.254  -12.760 -5.014  1.00 17.12  ? 357  HIS A CD2 1 
ATOM   1061 C  CE1 . HIS A 1 134 ? 12.870  -12.723 -6.716  1.00 19.25  ? 357  HIS A CE1 1 
ATOM   1062 N  NE2 . HIS A 1 134 ? 14.122  -12.498 -6.357  1.00 18.56  ? 357  HIS A NE2 1 
ATOM   1063 N  N   . GLU A 1 135 ? 9.933   -13.673 -1.487  1.00 12.10  ? 358  GLU A N   1 
ATOM   1064 C  CA  . GLU A 1 135 ? 9.320   -14.431 -0.407  1.00 11.55  ? 358  GLU A CA  1 
ATOM   1065 C  C   . GLU A 1 135 ? 10.218  -15.580 0.029   1.00 11.85  ? 358  GLU A C   1 
ATOM   1066 O  O   . GLU A 1 135 ? 10.898  -16.214 -0.785  1.00 13.71  ? 358  GLU A O   1 
ATOM   1067 C  CB  . GLU A 1 135 ? 7.984   -14.999 -0.857  1.00 14.33  ? 358  GLU A CB  1 
ATOM   1068 C  CG  . GLU A 1 135 ? 6.923   -13.949 -1.055  1.00 15.27  ? 358  GLU A CG  1 
ATOM   1069 C  CD  . GLU A 1 135 ? 5.694   -14.523 -1.713  1.00 17.33  ? 358  GLU A CD  1 
ATOM   1070 O  OE1 . GLU A 1 135 ? 5.772   -14.859 -2.912  1.00 20.99  ? 358  GLU A OE1 1 
ATOM   1071 O  OE2 . GLU A 1 135 ? 4.660   -14.656 -1.034  1.00 17.00  ? 358  GLU A OE2 1 
ATOM   1072 N  N   . GLY A 1 136 ? 10.189  -15.871 1.323   1.00 11.42  ? 359  GLY A N   1 
ATOM   1073 C  CA  . GLY A 1 136 ? 10.948  -16.991 1.834   1.00 13.12  ? 359  GLY A CA  1 
ATOM   1074 C  C   . GLY A 1 136 ? 10.333  -17.532 3.105   1.00 11.97  ? 359  GLY A C   1 
ATOM   1075 O  O   . GLY A 1 136 ? 9.490   -16.895 3.740   1.00 12.72  ? 359  GLY A O   1 
ATOM   1076 N  N   . VAL A 1 137 ? 10.781  -18.727 3.482   1.00 11.88  ? 360  VAL A N   1 
ATOM   1077 C  CA  . VAL A 1 137 ? 10.280  -19.424 4.660   1.00 11.40  ? 360  VAL A CA  1 
ATOM   1078 C  C   . VAL A 1 137 ? 11.470  -19.915 5.461   1.00 11.68  ? 360  VAL A C   1 
ATOM   1079 O  O   . VAL A 1 137 ? 12.367  -20.569 4.911   1.00 13.32  ? 360  VAL A O   1 
ATOM   1080 C  CB  . VAL A 1 137 ? 9.362   -20.604 4.280   1.00 12.41  ? 360  VAL A CB  1 
ATOM   1081 C  CG1 . VAL A 1 137 ? 8.909   -21.342 5.532   1.00 14.40  ? 360  VAL A CG1 1 
ATOM   1082 C  CG2 . VAL A 1 137 ? 8.146   -20.099 3.493   1.00 14.31  ? 360  VAL A CG2 1 
ATOM   1083 N  N   . ILE A 1 138 ? 11.475  -19.608 6.754   1.00 11.69  ? 361  ILE A N   1 
ATOM   1084 C  CA  . ILE A 1 138 ? 12.490  -20.089 7.689   1.00 12.40  ? 361  ILE A CA  1 
ATOM   1085 C  C   . ILE A 1 138 ? 11.812  -21.095 8.614   1.00 12.38  ? 361  ILE A C   1 
ATOM   1086 O  O   . ILE A 1 138 ? 11.025  -20.718 9.493   1.00 12.98  ? 361  ILE A O   1 
ATOM   1087 C  CB  . ILE A 1 138 ? 13.141  -18.933 8.476   1.00 12.11  ? 361  ILE A CB  1 
ATOM   1088 C  CG1 . ILE A 1 138 ? 13.896  -18.009 7.516   1.00 13.02  ? 361  ILE A CG1 1 
ATOM   1089 C  CG2 . ILE A 1 138 ? 14.087  -19.469 9.554   1.00 13.50  ? 361  ILE A CG2 1 
ATOM   1090 C  CD1 . ILE A 1 138 ? 14.351  -16.712 8.134   1.00 13.28  ? 361  ILE A CD1 1 
ATOM   1091 N  N   . SER A 1 139 ? 12.109  -22.381 8.418   1.00 12.61  ? 362  SER A N   1 
ATOM   1092 C  CA  . SER A 1 139 ? 11.567  -23.423 9.281   1.00 13.83  ? 362  SER A CA  1 
ATOM   1093 C  C   . SER A 1 139 ? 12.382  -23.478 10.563  1.00 13.72  ? 362  SER A C   1 
ATOM   1094 O  O   . SER A 1 139 ? 13.599  -23.678 10.515  1.00 14.79  ? 362  SER A O   1 
ATOM   1095 C  CB  . SER A 1 139 ? 11.669  -24.776 8.588   1.00 15.28  ? 362  SER A CB  1 
ATOM   1096 O  OG  . SER A 1 139 ? 11.414  -25.797 9.531   1.00 18.98  ? 362  SER A OG  1 
ATOM   1097 N  N   . THR A 1 140 ? 11.729  -23.301 11.708  1.00 14.38  ? 363  THR A N   1 
ATOM   1098 C  CA  . THR A 1 140 ? 12.467  -23.324 12.967  1.00 13.95  ? 363  THR A CA  1 
ATOM   1099 C  C   . THR A 1 140 ? 12.738  -24.735 13.464  1.00 13.47  ? 363  THR A C   1 
ATOM   1100 O  O   . THR A 1 140 ? 13.365  -24.893 14.522  1.00 15.41  ? 363  THR A O   1 
ATOM   1101 C  CB  . THR A 1 140 ? 11.752  -22.496 14.045  1.00 13.45  ? 363  THR A CB  1 
ATOM   1102 O  OG1 . THR A 1 140 ? 10.555  -23.167 14.441  1.00 13.04  ? 363  THR A OG1 1 
ATOM   1103 C  CG2 . THR A 1 140 ? 11.420  -21.088 13.538  1.00 13.68  ? 363  THR A CG2 1 
ATOM   1104 N  N   . VAL A 1 141 ? 12.293  -25.756 12.732  1.00 14.46  ? 364  VAL A N   1 
ATOM   1105 C  CA  . VAL A 1 141 ? 12.593  -27.145 13.062  1.00 15.88  ? 364  VAL A CA  1 
ATOM   1106 C  C   . VAL A 1 141 ? 13.573  -27.777 12.094  1.00 18.04  ? 364  VAL A C   1 
ATOM   1107 O  O   . VAL A 1 141 ? 13.919  -28.956 12.268  1.00 21.04  ? 364  VAL A O   1 
ATOM   1108 C  CB  . VAL A 1 141 ? 11.322  -28.005 13.202  1.00 16.74  ? 364  VAL A CB  1 
ATOM   1109 C  CG1 . VAL A 1 141 ? 10.446  -27.490 14.332  1.00 16.33  ? 364  VAL A CG1 1 
ATOM   1110 C  CG2 . VAL A 1 141 ? 10.552  -28.074 11.880  1.00 19.56  ? 364  VAL A CG2 1 
ATOM   1111 N  N   . ALA A 1 142 ? 14.031  -27.043 11.080  1.00 16.71  ? 365  ALA A N   1 
ATOM   1112 C  CA  . ALA A 1 142 ? 14.986  -27.606 10.139  1.00 16.52  ? 365  ALA A CA  1 
ATOM   1113 C  C   . ALA A 1 142 ? 16.295  -27.945 10.853  1.00 16.99  ? 365  ALA A C   1 
ATOM   1114 O  O   . ALA A 1 142 ? 16.706  -27.244 11.782  1.00 17.42  ? 365  ALA A O   1 
ATOM   1115 C  CB  . ALA A 1 142 ? 15.258  -26.618 9.007   1.00 16.54  ? 365  ALA A CB  1 
ATOM   1116 N  N   . PRO A 1 143 ? 16.967  -29.028 10.451  1.00 17.33  ? 366  PRO A N   1 
ATOM   1117 C  CA  . PRO A 1 143 ? 18.294  -29.307 11.026  1.00 19.15  ? 366  PRO A CA  1 
ATOM   1118 C  C   . PRO A 1 143 ? 19.245  -28.120 10.936  1.00 17.64  ? 366  PRO A C   1 
ATOM   1119 O  O   . PRO A 1 143 ? 20.084  -27.932 11.828  1.00 19.68  ? 366  PRO A O   1 
ATOM   1120 C  CB  . PRO A 1 143 ? 18.787  -30.507 10.207  1.00 20.22  ? 366  PRO A CB  1 
ATOM   1121 C  CG  . PRO A 1 143 ? 17.538  -31.194 9.758   1.00 19.50  ? 366  PRO A CG  1 
ATOM   1122 C  CD  . PRO A 1 143 ? 16.512  -30.101 9.547   1.00 17.79  ? 366  PRO A CD  1 
ATOM   1123 N  N   . ARG A 1 144 ? 19.121  -27.292 9.900   1.00 17.82  ? 367  ARG A N   1 
ATOM   1124 C  CA  . ARG A 1 144 ? 19.994  -26.143 9.719   1.00 19.03  ? 367  ARG A CA  1 
ATOM   1125 C  C   . ARG A 1 144 ? 19.443  -24.867 10.351  1.00 17.14  ? 367  ARG A C   1 
ATOM   1126 O  O   . ARG A 1 144 ? 19.999  -23.789 10.126  1.00 16.48  ? 367  ARG A O   1 
ATOM   1127 C  CB  . ARG A 1 144 ? 20.295  -25.930 8.230   1.00 22.78  ? 367  ARG A CB  1 
ATOM   1128 C  CG  . ARG A 1 144 ? 21.001  -27.106 7.557   1.00 27.56  ? 367  ARG A CG  1 
ATOM   1129 C  CD  . ARG A 1 144 ? 22.504  -27.057 7.764   1.00 34.99  ? 367  ARG A CD  1 
ATOM   1130 N  NE  . ARG A 1 144 ? 22.889  -27.362 9.137   1.00 41.72  ? 367  ARG A NE  1 
ATOM   1131 C  CZ  . ARG A 1 144 ? 23.183  -28.576 9.584   1.00 46.85  ? 367  ARG A CZ  1 
ATOM   1132 N  NH1 . ARG A 1 144 ? 23.160  -29.632 8.787   1.00 48.93  ? 367  ARG A NH1 1 
ATOM   1133 N  NH2 . ARG A 1 144 ? 23.506  -28.733 10.864  1.00 49.21  ? 367  ARG A NH2 1 
ATOM   1134 N  N   . PHE A 1 145 ? 18.369  -24.954 11.132  1.00 15.44  ? 368  PHE A N   1 
ATOM   1135 C  CA  . PHE A 1 145 ? 17.971  -23.832 11.981  1.00 14.27  ? 368  PHE A CA  1 
ATOM   1136 C  C   . PHE A 1 145 ? 18.875  -23.859 13.203  1.00 14.36  ? 368  PHE A C   1 
ATOM   1137 O  O   . PHE A 1 145 ? 18.616  -24.552 14.185  1.00 16.33  ? 368  PHE A O   1 
ATOM   1138 C  CB  . PHE A 1 145 ? 16.507  -23.934 12.382  1.00 14.95  ? 368  PHE A CB  1 
ATOM   1139 C  CG  . PHE A 1 145 ? 16.017  -22.751 13.184  1.00 13.56  ? 368  PHE A CG  1 
ATOM   1140 C  CD1 . PHE A 1 145 ? 15.659  -21.566 12.545  1.00 13.97  ? 368  PHE A CD1 1 
ATOM   1141 C  CD2 . PHE A 1 145 ? 15.917  -22.814 14.574  1.00 13.82  ? 368  PHE A CD2 1 
ATOM   1142 C  CE1 . PHE A 1 145 ? 15.199  -20.471 13.274  1.00 14.71  ? 368  PHE A CE1 1 
ATOM   1143 C  CE2 . PHE A 1 145 ? 15.467  -21.725 15.312  1.00 14.18  ? 368  PHE A CE2 1 
ATOM   1144 C  CZ  . PHE A 1 145 ? 15.103  -20.548 14.665  1.00 14.30  ? 368  PHE A CZ  1 
ATOM   1145 N  N   . THR A 1 146 ? 19.964  -23.100 13.145  1.00 14.75  ? 369  THR A N   1 
ATOM   1146 C  CA  . THR A 1 146 ? 20.953  -23.073 14.221  1.00 15.90  ? 369  THR A CA  1 
ATOM   1147 C  C   . THR A 1 146 ? 21.332  -21.634 14.550  1.00 15.95  ? 369  THR A C   1 
ATOM   1148 O  O   . THR A 1 146 ? 22.506  -21.255 14.484  1.00 16.69  ? 369  THR A O   1 
ATOM   1149 C  CB  . THR A 1 146 ? 22.188  -23.900 13.848  1.00 17.75  ? 369  THR A CB  1 
ATOM   1150 O  OG1 . THR A 1 146 ? 22.775  -23.403 12.634  1.00 19.31  ? 369  THR A OG1 1 
ATOM   1151 C  CG2 . THR A 1 146 ? 21.828  -25.364 13.662  1.00 17.94  ? 369  THR A CG2 1 
ATOM   1152 N  N   . PRO A 1 147 ? 20.354  -20.798 14.914  1.00 15.57  ? 370  PRO A N   1 
ATOM   1153 C  CA  . PRO A 1 147 ? 20.660  -19.371 15.139  1.00 15.18  ? 370  PRO A CA  1 
ATOM   1154 C  C   . PRO A 1 147 ? 21.689  -19.128 16.232  1.00 16.62  ? 370  PRO A C   1 
ATOM   1155 O  O   . PRO A 1 147 ? 22.466  -18.168 16.130  1.00 17.54  ? 370  PRO A O   1 
ATOM   1156 C  CB  . PRO A 1 147 ? 19.290  -18.772 15.489  1.00 14.98  ? 370  PRO A CB  1 
ATOM   1157 C  CG  . PRO A 1 147 ? 18.506  -19.929 16.057  1.00 14.30  ? 370  PRO A CG  1 
ATOM   1158 C  CD  . PRO A 1 147 ? 18.940  -21.107 15.221  1.00 14.55  ? 370  PRO A CD  1 
ATOM   1159 N  N   A LYS A 1 148 ? 21.720  -19.967 17.272  0.52 17.16  ? 371  LYS A N   1 
ATOM   1160 N  N   B LYS A 1 148 ? 21.726  -19.974 17.266  0.48 17.04  ? 371  LYS A N   1 
ATOM   1161 C  CA  A LYS A 1 148 ? 22.743  -19.827 18.304  0.52 18.18  ? 371  LYS A CA  1 
ATOM   1162 C  CA  B LYS A 1 148 ? 22.735  -19.838 18.310  0.48 17.87  ? 371  LYS A CA  1 
ATOM   1163 C  C   A LYS A 1 148 ? 24.136  -20.034 17.726  0.52 18.77  ? 371  LYS A C   1 
ATOM   1164 C  C   B LYS A 1 148 ? 24.135  -20.118 17.782  0.48 18.05  ? 371  LYS A C   1 
ATOM   1165 O  O   A LYS A 1 148 ? 25.112  -19.465 18.230  0.52 20.43  ? 371  LYS A O   1 
ATOM   1166 O  O   B LYS A 1 148 ? 25.117  -19.684 18.393  0.48 18.50  ? 371  LYS A O   1 
ATOM   1167 C  CB  A LYS A 1 148 ? 22.466  -20.819 19.436  0.52 19.15  ? 371  LYS A CB  1 
ATOM   1168 C  CB  B LYS A 1 148 ? 22.394  -20.770 19.474  0.48 19.06  ? 371  LYS A CB  1 
ATOM   1169 C  CG  A LYS A 1 148 ? 23.579  -20.963 20.473  0.52 19.51  ? 371  LYS A CG  1 
ATOM   1170 C  CG  B LYS A 1 148 ? 23.304  -20.639 20.683  0.48 19.95  ? 371  LYS A CG  1 
ATOM   1171 C  CD  A LYS A 1 148 ? 23.645  -19.797 21.451  0.52 20.24  ? 371  LYS A CD  1 
ATOM   1172 C  CD  B LYS A 1 148 ? 23.342  -19.213 21.207  0.48 21.11  ? 371  LYS A CD  1 
ATOM   1173 C  CE  A LYS A 1 148 ? 24.546  -20.147 22.624  0.52 21.76  ? 371  LYS A CE  1 
ATOM   1174 C  CE  B LYS A 1 148 ? 24.296  -19.092 22.378  0.48 22.46  ? 371  LYS A CE  1 
ATOM   1175 N  NZ  A LYS A 1 148 ? 24.716  -19.022 23.575  0.52 22.46  ? 371  LYS A NZ  1 
ATOM   1176 N  NZ  B LYS A 1 148 ? 23.884  -19.942 23.526  0.48 22.54  ? 371  LYS A NZ  1 
ATOM   1177 N  N   . LEU A 1 149 ? 24.248  -20.825 16.663  1.00 17.83  ? 372  LEU A N   1 
ATOM   1178 C  CA  . LEU A 1 149 ? 25.522  -21.038 15.993  1.00 18.97  ? 372  LEU A CA  1 
ATOM   1179 C  C   . LEU A 1 149 ? 25.779  -20.003 14.911  1.00 19.12  ? 372  LEU A C   1 
ATOM   1180 O  O   . LEU A 1 149 ? 26.809  -20.075 14.230  1.00 22.37  ? 372  LEU A O   1 
ATOM   1181 C  CB  . LEU A 1 149 ? 25.594  -22.449 15.399  1.00 20.89  ? 372  LEU A CB  1 
ATOM   1182 C  CG  . LEU A 1 149 ? 25.392  -23.596 16.390  1.00 23.14  ? 372  LEU A CG  1 
ATOM   1183 C  CD1 . LEU A 1 149 ? 25.523  -24.951 15.716  1.00 23.25  ? 372  LEU A CD1 1 
ATOM   1184 C  CD2 . LEU A 1 149 ? 26.382  -23.473 17.536  1.00 24.05  ? 372  LEU A CD2 1 
ATOM   1185 N  N   . GLY A 1 150 ? 24.857  -19.063 14.727  1.00 17.59  ? 373  GLY A N   1 
ATOM   1186 C  CA  . GLY A 1 150 ? 25.042  -17.956 13.817  1.00 17.46  ? 373  GLY A CA  1 
ATOM   1187 C  C   . GLY A 1 150 ? 24.429  -18.098 12.443  1.00 16.50  ? 373  GLY A C   1 
ATOM   1188 O  O   . GLY A 1 150 ? 24.748  -17.286 11.568  1.00 18.41  ? 373  GLY A O   1 
ATOM   1189 N  N   . SER A 1 151 ? 23.554  -19.080 12.216  1.00 15.12  ? 374  SER A N   1 
ATOM   1190 C  CA  . SER A 1 151 ? 22.960  -19.199 10.890  1.00 15.45  ? 374  SER A CA  1 
ATOM   1191 C  C   . SER A 1 151 ? 21.611  -19.909 10.937  1.00 14.82  ? 374  SER A C   1 
ATOM   1192 O  O   . SER A 1 151 ? 21.344  -20.725 11.822  1.00 15.35  ? 374  SER A O   1 
ATOM   1193 C  CB  . SER A 1 151 ? 23.883  -19.927 9.908   1.00 17.35  ? 374  SER A CB  1 
ATOM   1194 O  OG  . SER A 1 151 ? 24.061  -21.275 10.302  1.00 20.18  ? 374  SER A OG  1 
ATOM   1195 N  N   . VAL A 1 152 ? 20.775  -19.604 9.945   1.00 14.41  ? 375  VAL A N   1 
ATOM   1196 C  CA  . VAL A 1 152 ? 19.534  -20.331 9.714   1.00 13.23  ? 375  VAL A CA  1 
ATOM   1197 C  C   . VAL A 1 152 ? 19.430  -20.613 8.222   1.00 13.81  ? 375  VAL A C   1 
ATOM   1198 O  O   . VAL A 1 152 ? 20.080  -19.967 7.400   1.00 16.07  ? 375  VAL A O   1 
ATOM   1199 C  CB  . VAL A 1 152 ? 18.274  -19.565 10.198  1.00 14.31  ? 375  VAL A CB  1 
ATOM   1200 C  CG1 . VAL A 1 152 ? 18.339  -19.299 11.703  1.00 14.94  ? 375  VAL A CG1 1 
ATOM   1201 C  CG2 . VAL A 1 152 ? 18.083  -18.257 9.410   1.00 15.07  ? 375  VAL A CG2 1 
ATOM   1202 N  N   . MET A 1 153 ? 18.608  -21.595 7.875   1.00 13.88  ? 376  MET A N   1 
ATOM   1203 C  CA  . MET A 1 153 ? 18.329  -21.909 6.480   1.00 14.29  ? 376  MET A CA  1 
ATOM   1204 C  C   . MET A 1 153 ? 17.025  -21.238 6.067   1.00 13.95  ? 376  MET A C   1 
ATOM   1205 O  O   . MET A 1 153 ? 16.021  -21.317 6.786   1.00 15.08  ? 376  MET A O   1 
ATOM   1206 C  CB  . MET A 1 153 ? 18.240  -23.426 6.276   1.00 15.95  ? 376  MET A CB  1 
ATOM   1207 C  CG  . MET A 1 153 ? 18.014  -23.856 4.826   1.00 16.14  ? 376  MET A CG  1 
ATOM   1208 S  SD  . MET A 1 153 ? 16.261  -23.945 4.381   1.00 16.82  ? 376  MET A SD  1 
ATOM   1209 C  CE  . MET A 1 153 ? 15.737  -25.402 5.310   1.00 17.69  ? 376  MET A CE  1 
ATOM   1210 N  N   . ILE A 1 154 ? 17.037  -20.581 4.909   1.00 13.51  ? 377  ILE A N   1 
ATOM   1211 C  CA  . ILE A 1 154 ? 15.833  -19.989 4.345   1.00 13.44  ? 377  ILE A CA  1 
ATOM   1212 C  C   . ILE A 1 154 ? 15.518  -20.671 3.015   1.00 13.74  ? 377  ILE A C   1 
ATOM   1213 O  O   . ILE A 1 154 ? 16.416  -20.906 2.196   1.00 14.82  ? 377  ILE A O   1 
ATOM   1214 C  CB  . ILE A 1 154 ? 15.962  -18.461 4.204   1.00 13.66  ? 377  ILE A CB  1 
ATOM   1215 C  CG1 . ILE A 1 154 ? 14.642  -17.844 3.720   1.00 12.99  ? 377  ILE A CG1 1 
ATOM   1216 C  CG2 . ILE A 1 154 ? 17.130  -18.094 3.308   1.00 15.27  ? 377  ILE A CG2 1 
ATOM   1217 C  CD1 . ILE A 1 154 ? 14.590  -16.327 3.907   1.00 13.53  ? 377  ILE A CD1 1 
ATOM   1218 N  N   . GLY A 1 155 ? 14.251  -21.015 2.817   1.00 12.91  ? 378  GLY A N   1 
ATOM   1219 C  CA  . GLY A 1 155 ? 13.781  -21.597 1.571   1.00 13.07  ? 378  GLY A CA  1 
ATOM   1220 C  C   . GLY A 1 155 ? 13.015  -20.570 0.759   1.00 13.19  ? 378  GLY A C   1 
ATOM   1221 O  O   . GLY A 1 155 ? 12.235  -19.790 1.308   1.00 14.34  ? 378  GLY A O   1 
ATOM   1222 N  N   . THR A 1 156 ? 13.241  -20.568 -0.552  1.00 13.72  ? 379  THR A N   1 
ATOM   1223 C  CA  . THR A 1 156 ? 12.590  -19.616 -1.433  1.00 14.84  ? 379  THR A CA  1 
ATOM   1224 C  C   . THR A 1 156 ? 11.968  -20.352 -2.608  1.00 16.29  ? 379  THR A C   1 
ATOM   1225 O  O   . THR A 1 156 ? 12.366  -21.466 -2.949  1.00 17.30  ? 379  THR A O   1 
ATOM   1226 C  CB  . THR A 1 156 ? 13.583  -18.566 -1.973  1.00 14.92  ? 379  THR A CB  1 
ATOM   1227 O  OG1 . THR A 1 156 ? 14.626  -19.224 -2.712  1.00 16.74  ? 379  THR A OG1 1 
ATOM   1228 C  CG2 . THR A 1 156 ? 14.186  -17.750 -0.838  1.00 15.91  ? 379  THR A CG2 1 
ATOM   1229 N  N   . TRP A 1 157 ? 10.982  -19.706 -3.231  1.00 16.07  ? 380  TRP A N   1 
ATOM   1230 C  CA  . TRP A 1 157 ? 10.441  -20.224 -4.481  1.00 17.99  ? 380  TRP A CA  1 
ATOM   1231 C  C   . TRP A 1 157 ? 11.368  -19.953 -5.659  1.00 20.42  ? 380  TRP A C   1 
ATOM   1232 O  O   . TRP A 1 157 ? 11.405  -20.749 -6.609  1.00 22.22  ? 380  TRP A O   1 
ATOM   1233 C  CB  . TRP A 1 157 ? 9.028   -19.676 -4.702  1.00 18.08  ? 380  TRP A CB  1 
ATOM   1234 C  CG  . TRP A 1 157 ? 8.034   -20.298 -3.752  1.00 19.44  ? 380  TRP A CG  1 
ATOM   1235 C  CD1 . TRP A 1 157 ? 7.291   -21.415 -3.976  1.00 21.92  ? 380  TRP A CD1 1 
ATOM   1236 C  CD2 . TRP A 1 157 ? 7.712   -19.868 -2.415  1.00 18.78  ? 380  TRP A CD2 1 
ATOM   1237 N  NE1 . TRP A 1 157 ? 6.512   -21.700 -2.881  1.00 21.80  ? 380  TRP A NE1 1 
ATOM   1238 C  CE2 . TRP A 1 157 ? 6.749   -20.765 -1.910  1.00 19.15  ? 380  TRP A CE2 1 
ATOM   1239 C  CE3 . TRP A 1 157 ? 8.132   -18.805 -1.607  1.00 18.04  ? 380  TRP A CE3 1 
ATOM   1240 C  CZ2 . TRP A 1 157 ? 6.207   -20.643 -0.633  1.00 19.99  ? 380  TRP A CZ2 1 
ATOM   1241 C  CZ3 . TRP A 1 157 ? 7.586   -18.683 -0.332  1.00 17.94  ? 380  TRP A CZ3 1 
ATOM   1242 C  CH2 . TRP A 1 157 ? 6.630   -19.597 0.137   1.00 18.06  ? 380  TRP A CH2 1 
ATOM   1243 N  N   . THR A 1 158 ? 12.127  -18.860 -5.619  1.00 21.07  ? 381  THR A N   1 
ATOM   1244 C  CA  . THR A 1 158 ? 13.151  -18.624 -6.627  1.00 23.59  ? 381  THR A CA  1 
ATOM   1245 C  C   . THR A 1 158 ? 14.336  -19.556 -6.393  1.00 24.19  ? 381  THR A C   1 
ATOM   1246 O  O   . THR A 1 158 ? 14.638  -19.938 -5.259  1.00 22.40  ? 381  THR A O   1 
ATOM   1247 C  CB  . THR A 1 158 ? 13.614  -17.160 -6.606  1.00 23.91  ? 381  THR A CB  1 
ATOM   1248 O  OG1 . THR A 1 158 ? 14.581  -16.949 -7.643  1.00 25.77  ? 381  THR A OG1 1 
ATOM   1249 C  CG2 . THR A 1 158 ? 14.247  -16.794 -5.270  1.00 23.91  ? 381  THR A CG2 1 
ATOM   1250 N  N   . THR A 1 159 ? 14.996  -19.945 -7.485  1.00 27.00  ? 382  THR A N   1 
ATOM   1251 C  CA  . THR A 1 159 ? 16.219  -20.734 -7.408  1.00 30.65  ? 382  THR A CA  1 
ATOM   1252 C  C   . THR A 1 159 ? 17.450  -19.972 -7.870  1.00 31.86  ? 382  THR A C   1 
ATOM   1253 O  O   . THR A 1 159 ? 18.555  -20.527 -7.832  1.00 34.00  ? 382  THR A O   1 
ATOM   1254 C  CB  . THR A 1 159 ? 16.103  -22.026 -8.232  1.00 32.37  ? 382  THR A CB  1 
ATOM   1255 O  OG1 . THR A 1 159 ? 15.747  -21.711 -9.584  1.00 33.40  ? 382  THR A OG1 1 
ATOM   1256 C  CG2 . THR A 1 159 ? 15.077  -22.956 -7.643  1.00 32.97  ? 382  THR A CG2 1 
ATOM   1257 N  N   . ASP A 1 160 ? 17.298  -18.723 -8.305  0.88 29.72  ? 383  ASP A N   1 
ATOM   1258 C  CA  . ASP A 1 160 ? 18.365  -18.063 -9.039  0.88 30.78  ? 383  ASP A CA  1 
ATOM   1259 C  C   . ASP A 1 160 ? 18.512  -16.580 -8.750  0.88 29.22  ? 383  ASP A C   1 
ATOM   1260 O  O   . ASP A 1 160 ? 19.340  -15.930 -9.399  0.88 32.16  ? 383  ASP A O   1 
ATOM   1261 C  CB  . ASP A 1 160 ? 18.152  -18.257 -10.549 0.88 35.84  ? 383  ASP A CB  1 
ATOM   1262 C  CG  . ASP A 1 160 ? 16.745  -17.879 -10.997 0.88 40.98  ? 383  ASP A CG  1 
ATOM   1263 O  OD1 . ASP A 1 160 ? 16.069  -17.109 -10.285 0.88 42.87  ? 383  ASP A OD1 1 
ATOM   1264 O  OD2 . ASP A 1 160 ? 16.307  -18.366 -12.062 0.88 43.81  ? 383  ASP A OD2 1 
ATOM   1265 N  N   . ASP A 1 161 ? 17.745  -16.015 -7.826  1.00 22.79  ? 384  ASP A N   1 
ATOM   1266 C  CA  . ASP A 1 161 ? 17.784  -14.572 -7.612  1.00 19.51  ? 384  ASP A CA  1 
ATOM   1267 C  C   . ASP A 1 161 ? 18.043  -14.238 -6.148  1.00 17.66  ? 384  ASP A C   1 
ATOM   1268 O  O   . ASP A 1 161 ? 17.430  -13.334 -5.572  1.00 17.64  ? 384  ASP A O   1 
ATOM   1269 C  CB  . ASP A 1 161 ? 16.539  -13.869 -8.143  1.00 20.21  ? 384  ASP A CB  1 
ATOM   1270 C  CG  . ASP A 1 161 ? 16.752  -12.381 -8.333  1.00 20.86  ? 384  ASP A CG  1 
ATOM   1271 O  OD1 . ASP A 1 161 ? 17.851  -11.992 -8.781  1.00 22.14  ? 384  ASP A OD1 1 
ATOM   1272 O  OD2 . ASP A 1 161 ? 15.821  -11.602 -8.054  1.00 20.75  ? 384  ASP A OD2 1 
ATOM   1273 N  N   . ILE A 1 162 ? 18.975  -14.968 -5.537  1.00 18.71  ? 385  ILE A N   1 
ATOM   1274 C  CA  . ILE A 1 162 ? 19.482  -14.688 -4.197  1.00 18.31  ? 385  ILE A CA  1 
ATOM   1275 C  C   . ILE A 1 162 ? 21.002  -14.671 -4.295  1.00 19.24  ? 385  ILE A C   1 
ATOM   1276 O  O   . ILE A 1 162 ? 21.606  -15.653 -4.741  1.00 20.68  ? 385  ILE A O   1 
ATOM   1277 C  CB  . ILE A 1 162 ? 19.024  -15.748 -3.180  1.00 17.24  ? 385  ILE A CB  1 
ATOM   1278 C  CG1 . ILE A 1 162 ? 17.491  -15.794 -3.079  1.00 18.33  ? 385  ILE A CG1 1 
ATOM   1279 C  CG2 . ILE A 1 162 ? 19.650  -15.488 -1.822  1.00 16.66  ? 385  ILE A CG2 1 
ATOM   1280 C  CD1 . ILE A 1 162 ? 16.855  -14.571 -2.414  1.00 18.84  ? 385  ILE A CD1 1 
ATOM   1281 N  N   . GLN A 1 163 ? 21.621  -13.561 -3.899  1.00 18.38  ? 386  GLN A N   1 
ATOM   1282 C  CA  . GLN A 1 163 ? 23.066  -13.389 -4.022  1.00 18.67  ? 386  GLN A CA  1 
ATOM   1283 C  C   . GLN A 1 163 ? 23.736  -13.478 -2.655  1.00 18.61  ? 386  GLN A C   1 
ATOM   1284 O  O   . GLN A 1 163 ? 23.080  -13.440 -1.612  1.00 17.91  ? 386  GLN A O   1 
ATOM   1285 C  CB  . GLN A 1 163 ? 23.394  -12.057 -4.711  1.00 19.23  ? 386  GLN A CB  1 
ATOM   1286 C  CG  . GLN A 1 163 ? 22.825  -11.942 -6.122  1.00 19.93  ? 386  GLN A CG  1 
ATOM   1287 C  CD  . GLN A 1 163 ? 23.185  -10.635 -6.808  1.00 22.37  ? 386  GLN A CD  1 
ATOM   1288 O  OE1 . GLN A 1 163 ? 24.061  -9.893  -6.357  1.00 23.07  ? 386  GLN A OE1 1 
ATOM   1289 N  NE2 . GLN A 1 163 ? 22.509  -10.353 -7.915  1.00 21.63  ? 386  GLN A NE2 1 
ATOM   1290 N  N   . ASP A 1 164 ? 25.068  -13.597 -2.665  1.00 18.99  ? 387  ASP A N   1 
ATOM   1291 C  CA  . ASP A 1 164 ? 25.832  -13.638 -1.417  1.00 18.49  ? 387  ASP A CA  1 
ATOM   1292 C  C   . ASP A 1 164 ? 26.084  -12.205 -0.962  1.00 19.12  ? 387  ASP A C   1 
ATOM   1293 O  O   . ASP A 1 164 ? 27.159  -11.633 -1.157  1.00 20.91  ? 387  ASP A O   1 
ATOM   1294 C  CB  . ASP A 1 164 ? 27.136  -14.400 -1.599  1.00 21.13  ? 387  ASP A CB  1 
ATOM   1295 C  CG  . ASP A 1 164 ? 26.921  -15.880 -1.840  1.00 24.49  ? 387  ASP A CG  1 
ATOM   1296 O  OD1 . ASP A 1 164 ? 25.760  -16.342 -1.760  1.00 24.81  ? 387  ASP A OD1 1 
ATOM   1297 O  OD2 . ASP A 1 164 ? 27.922  -16.580 -2.114  1.00 29.95  ? 387  ASP A OD2 1 
ATOM   1298 N  N   . GLN A 1 165 ? 25.064  -11.620 -0.344  1.00 16.66  ? 388  GLN A N   1 
ATOM   1299 C  CA  . GLN A 1 165 ? 25.024  -10.183 -0.135  1.00 16.96  ? 388  GLN A CA  1 
ATOM   1300 C  C   . GLN A 1 165 ? 24.310  -9.899  1.173   1.00 16.56  ? 388  GLN A C   1 
ATOM   1301 O  O   . GLN A 1 165 ? 23.596  -10.765 1.696   1.00 17.18  ? 388  GLN A O   1 
ATOM   1302 C  CB  . GLN A 1 165 ? 24.274  -9.504  -1.291  1.00 17.21  ? 388  GLN A CB  1 
ATOM   1303 C  CG  . GLN A 1 165 ? 25.008  -9.548  -2.623  1.00 18.06  ? 388  GLN A CG  1 
ATOM   1304 C  CD  . GLN A 1 165 ? 26.247  -8.659  -2.638  1.00 19.07  ? 388  GLN A CD  1 
ATOM   1305 O  OE1 . GLN A 1 165 ? 26.472  -7.863  -1.729  1.00 18.78  ? 388  GLN A OE1 1 
ATOM   1306 N  NE2 . GLN A 1 165 ? 27.048  -8.789  -3.680  1.00 21.13  ? 388  GLN A NE2 1 
ATOM   1307 N  N   . PRO A 1 166 ? 24.472  -8.693  1.726   1.00 16.88  ? 389  PRO A N   1 
ATOM   1308 C  CA  . PRO A 1 166 ? 23.757  -8.337  2.958   1.00 16.74  ? 389  PRO A CA  1 
ATOM   1309 C  C   . PRO A 1 166 ? 22.252  -8.490  2.790   1.00 16.49  ? 389  PRO A C   1 
ATOM   1310 O  O   . PRO A 1 166 ? 21.677  -8.089  1.773   1.00 17.07  ? 389  PRO A O   1 
ATOM   1311 C  CB  . PRO A 1 166 ? 24.154  -6.874  3.182   1.00 16.22  ? 389  PRO A CB  1 
ATOM   1312 C  CG  . PRO A 1 166 ? 25.488  -6.757  2.537   1.00 16.79  ? 389  PRO A CG  1 
ATOM   1313 C  CD  . PRO A 1 166 ? 25.407  -7.628  1.312   1.00 17.38  ? 389  PRO A CD  1 
ATOM   1314 N  N   . SER A 1 167 ? 21.618  -9.073  3.809   1.00 14.38  ? 390  SER A N   1 
ATOM   1315 C  CA  . SER A 1 167 ? 20.244  -9.536  3.720   1.00 14.97  ? 390  SER A CA  1 
ATOM   1316 C  C   . SER A 1 167 ? 19.507  -9.249  5.017   1.00 14.04  ? 390  SER A C   1 
ATOM   1317 O  O   . SER A 1 167 ? 20.094  -9.258  6.105   1.00 15.09  ? 390  SER A O   1 
ATOM   1318 C  CB  . SER A 1 167 ? 20.189  -11.047 3.460   1.00 15.47  ? 390  SER A CB  1 
ATOM   1319 O  OG  . SER A 1 167 ? 20.833  -11.370 2.242   1.00 15.35  ? 390  SER A OG  1 
ATOM   1320 N  N   . ARG A 1 168 ? 18.206  -9.035  4.891   1.00 14.27  ? 391  ARG A N   1 
ATOM   1321 C  CA  . ARG A 1 168 ? 17.329  -8.863  6.037   1.00 14.94  ? 391  ARG A CA  1 
ATOM   1322 C  C   . ARG A 1 168 ? 16.051  -9.637  5.772   1.00 14.29  ? 391  ARG A C   1 
ATOM   1323 O  O   . ARG A 1 168 ? 15.579  -9.696  4.633   1.00 15.94  ? 391  ARG A O   1 
ATOM   1324 C  CB  . ARG A 1 168 ? 16.996  -7.388  6.292   1.00 17.25  ? 391  ARG A CB  1 
ATOM   1325 C  CG  . ARG A 1 168 ? 17.091  -6.497  5.073   1.00 56.69  ? 391  ARG A CG  1 
ATOM   1326 C  CD  . ARG A 1 168 ? 17.128  -5.024  5.456   1.00 125.35 ? 391  ARG A CD  1 
ATOM   1327 N  NE  . ARG A 1 168 ? 16.033  -4.655  6.345   1.00 60.35  ? 391  ARG A NE  1 
ATOM   1328 C  CZ  . ARG A 1 168 ? 15.688  -3.406  6.628   1.00 46.61  ? 391  ARG A CZ  1 
ATOM   1329 N  NH1 . ARG A 1 168 ? 16.320  -2.376  6.090   1.00 32.44  ? 391  ARG A NH1 1 
ATOM   1330 N  NH2 . ARG A 1 168 ? 14.679  -3.186  7.466   1.00 57.04  ? 391  ARG A NH2 1 
ATOM   1331 N  N   . PHE A 1 169 ? 15.500  -10.227 6.821   1.00 12.79  ? 392  PHE A N   1 
ATOM   1332 C  CA  . PHE A 1 169 ? 14.245  -10.969 6.741   1.00 11.41  ? 392  PHE A CA  1 
ATOM   1333 C  C   . PHE A 1 169 ? 13.175  -10.187 7.488   1.00 11.27  ? 392  PHE A C   1 
ATOM   1334 O  O   . PHE A 1 169 ? 13.304  -9.970  8.701   1.00 13.39  ? 392  PHE A O   1 
ATOM   1335 C  CB  . PHE A 1 169 ? 14.396  -12.370 7.343   1.00 12.29  ? 392  PHE A CB  1 
ATOM   1336 C  CG  . PHE A 1 169 ? 13.129  -13.183 7.322   1.00 11.59  ? 392  PHE A CG  1 
ATOM   1337 C  CD1 . PHE A 1 169 ? 12.737  -13.859 6.165   1.00 11.77  ? 392  PHE A CD1 1 
ATOM   1338 C  CD2 . PHE A 1 169 ? 12.321  -13.270 8.451   1.00 12.44  ? 392  PHE A CD2 1 
ATOM   1339 C  CE1 . PHE A 1 169 ? 11.567  -14.613 6.139   1.00 13.44  ? 392  PHE A CE1 1 
ATOM   1340 C  CE2 . PHE A 1 169 ? 11.152  -14.006 8.438   1.00 12.51  ? 392  PHE A CE2 1 
ATOM   1341 C  CZ  . PHE A 1 169 ? 10.776  -14.696 7.278   1.00 13.61  ? 392  PHE A CZ  1 
ATOM   1342 N  N   . THR A 1 170 ? 12.115  -9.793  6.772   1.00 10.89  ? 393  THR A N   1 
ATOM   1343 C  CA  . THR A 1 170 ? 10.949  -9.135  7.369   1.00 10.49  ? 393  THR A CA  1 
ATOM   1344 C  C   . THR A 1 170 ? 9.854   -10.174 7.547   1.00 10.41  ? 393  THR A C   1 
ATOM   1345 O  O   . THR A 1 170 ? 9.388   -10.741 6.546   1.00 10.86  ? 393  THR A O   1 
ATOM   1346 C  CB  . THR A 1 170 ? 10.447  -8.021  6.449   1.00 10.93  ? 393  THR A CB  1 
ATOM   1347 O  OG1 . THR A 1 170 ? 11.484  -7.049  6.250   1.00 12.39  ? 393  THR A OG1 1 
ATOM   1348 C  CG2 . THR A 1 170 ? 9.213   -7.333  7.044   1.00 12.02  ? 393  THR A CG2 1 
ATOM   1349 N  N   . PRO A 1 171 ? 9.432   -10.486 8.770   1.00 10.41  ? 394  PRO A N   1 
ATOM   1350 C  CA  . PRO A 1 171 ? 8.381   -11.493 8.945   1.00 10.12  ? 394  PRO A CA  1 
ATOM   1351 C  C   . PRO A 1 171 ? 7.017   -10.986 8.501   1.00 10.20  ? 394  PRO A C   1 
ATOM   1352 O  O   . PRO A 1 171 ? 6.688   -9.798  8.621   1.00 11.21  ? 394  PRO A O   1 
ATOM   1353 C  CB  . PRO A 1 171 ? 8.397   -11.747 10.457  1.00 10.90  ? 394  PRO A CB  1 
ATOM   1354 C  CG  . PRO A 1 171 ? 8.842   -10.424 11.016  1.00 11.11  ? 394  PRO A CG  1 
ATOM   1355 C  CD  . PRO A 1 171 ? 9.876   -9.918  10.056  1.00 10.97  ? 394  PRO A CD  1 
ATOM   1356 N  N   . VAL A 1 172 ? 6.206   -11.927 7.998   1.00 9.78   ? 395  VAL A N   1 
ATOM   1357 C  CA  . VAL A 1 172 ? 4.821   -11.656 7.634   1.00 10.08  ? 395  VAL A CA  1 
ATOM   1358 C  C   . VAL A 1 172 ? 3.849   -12.561 8.382   1.00 11.49  ? 395  VAL A C   1 
ATOM   1359 O  O   . VAL A 1 172 ? 2.824   -12.094 8.890   1.00 11.67  ? 395  VAL A O   1 
ATOM   1360 C  CB  . VAL A 1 172 ? 4.592   -11.731 6.104   1.00 10.82  ? 395  VAL A CB  1 
ATOM   1361 C  CG1 . VAL A 1 172 ? 3.107   -11.553 5.761   1.00 11.94  ? 395  VAL A CG1 1 
ATOM   1362 C  CG2 . VAL A 1 172 ? 5.425   -10.666 5.398   1.00 11.60  ? 395  VAL A CG2 1 
ATOM   1363 N  N   . GLY A 1 173 ? 4.151   -13.860 8.478   1.00 11.12  ? 396  GLY A N   1 
ATOM   1364 C  CA  . GLY A 1 173 ? 3.278   -14.784 9.163   1.00 11.52  ? 396  GLY A CA  1 
ATOM   1365 C  C   . GLY A 1 173 ? 3.857   -16.170 9.136   1.00 10.13  ? 396  GLY A C   1 
ATOM   1366 O  O   . GLY A 1 173 ? 5.066   -16.337 9.328   1.00 11.41  ? 396  GLY A O   1 
ATOM   1367 N  N   . LEU A 1 174 ? 3.007   -17.164 8.921   1.00 10.97  ? 397  LEU A N   1 
ATOM   1368 C  CA  . LEU A 1 174 ? 3.425   -18.554 8.816   1.00 11.25  ? 397  LEU A CA  1 
ATOM   1369 C  C   . LEU A 1 174 ? 3.177   -19.049 7.399   1.00 11.11  ? 397  LEU A C   1 
ATOM   1370 O  O   . LEU A 1 174 ? 2.266   -18.583 6.712   1.00 12.33  ? 397  LEU A O   1 
ATOM   1371 C  CB  . LEU A 1 174 ? 2.617   -19.448 9.761   1.00 11.46  ? 397  LEU A CB  1 
ATOM   1372 C  CG  . LEU A 1 174 ? 2.734   -19.112 11.245  1.00 13.50  ? 397  LEU A CG  1 
ATOM   1373 C  CD1 . LEU A 1 174 ? 1.811   -19.974 12.063  1.00 14.06  ? 397  LEU A CD1 1 
ATOM   1374 C  CD2 . LEU A 1 174 ? 4.164   -19.256 11.746  1.00 15.42  ? 397  LEU A CD2 1 
ATOM   1375 N  N   . ASN A 1 175 ? 3.968   -20.031 6.968   1.00 11.20  ? 398  ASN A N   1 
ATOM   1376 C  CA  . ASN A 1 175 ? 3.716   -20.620 5.656   1.00 12.65  ? 398  ASN A CA  1 
ATOM   1377 C  C   . ASN A 1 175 ? 2.420   -21.420 5.670   1.00 14.33  ? 398  ASN A C   1 
ATOM   1378 O  O   . ASN A 1 175 ? 1.593   -21.307 4.758   1.00 15.62  ? 398  ASN A O   1 
ATOM   1379 C  CB  . ASN A 1 175 ? 4.893   -21.498 5.232   1.00 13.66  ? 398  ASN A CB  1 
ATOM   1380 C  CG  . ASN A 1 175 ? 4.749   -22.001 3.817   1.00 15.64  ? 398  ASN A CG  1 
ATOM   1381 O  OD1 . ASN A 1 175 ? 4.450   -21.239 2.898   1.00 16.35  ? 398  ASN A OD1 1 
ATOM   1382 N  ND2 . ASN A 1 175 ? 4.952   -23.296 3.631   1.00 21.25  ? 398  ASN A ND2 1 
ATOM   1383 N  N   . ASP A 1 176 ? 2.237   -22.222 6.710   1.00 15.29  ? 399  ASP A N   1 
ATOM   1384 C  CA  . ASP A 1 176 ? 1.025   -22.963 7.030   1.00 15.14  ? 399  ASP A CA  1 
ATOM   1385 C  C   . ASP A 1 176 ? 1.134   -23.218 8.527   1.00 15.22  ? 399  ASP A C   1 
ATOM   1386 O  O   . ASP A 1 176 ? 2.105   -22.802 9.168   1.00 17.71  ? 399  ASP A O   1 
ATOM   1387 C  CB  . ASP A 1 176 ? 0.939   -24.253 6.195   1.00 17.18  ? 399  ASP A CB  1 
ATOM   1388 C  CG  . ASP A 1 176 ? -0.484  -24.858 6.135   1.00 20.36  ? 399  ASP A CG  1 
ATOM   1389 O  OD1 . ASP A 1 176 ? -1.293  -24.641 7.060   1.00 20.20  ? 399  ASP A OD1 1 
ATOM   1390 O  OD2 . ASP A 1 176 ? -0.791  -25.575 5.151   1.00 22.61  ? 399  ASP A OD2 1 
ATOM   1391 N  N   . ASP A 1 177 ? 0.151   -23.896 9.103   1.00 15.53  ? 400  ASP A N   1 
ATOM   1392 C  CA  . ASP A 1 177 ? 0.170   -24.063 10.551  1.00 16.41  ? 400  ASP A CA  1 
ATOM   1393 C  C   . ASP A 1 177 ? 0.072   -25.521 10.978  1.00 16.19  ? 400  ASP A C   1 
ATOM   1394 O  O   . ASP A 1 177 ? -0.167  -25.790 12.161  1.00 17.17  ? 400  ASP A O   1 
ATOM   1395 C  CB  . ASP A 1 177 ? -0.941  -23.244 11.208  1.00 16.13  ? 400  ASP A CB  1 
ATOM   1396 C  CG  . ASP A 1 177 ? -2.316  -23.754 10.853  1.00 17.99  ? 400  ASP A CG  1 
ATOM   1397 O  OD1 . ASP A 1 177 ? -2.433  -24.563 9.902   1.00 18.06  ? 400  ASP A OD1 1 
ATOM   1398 O  OD2 . ASP A 1 177 ? -3.280  -23.354 11.533  1.00 22.23  ? 400  ASP A OD2 1 
ATOM   1399 N  N   . ASP A 1 178 ? 0.280   -26.462 10.051  1.00 17.46  ? 401  ASP A N   1 
ATOM   1400 C  CA  . ASP A 1 178 ? 0.013   -27.867 10.355  1.00 19.49  ? 401  ASP A CA  1 
ATOM   1401 C  C   . ASP A 1 178 ? 0.810   -28.367 11.549  1.00 20.77  ? 401  ASP A C   1 
ATOM   1402 O  O   . ASP A 1 178 ? 0.317   -29.204 12.319  1.00 22.88  ? 401  ASP A O   1 
ATOM   1403 C  CB  . ASP A 1 178 ? 0.282   -28.737 9.130   1.00 22.31  ? 401  ASP A CB  1 
ATOM   1404 C  CG  . ASP A 1 178 ? -0.777  -28.567 8.067   1.00 25.34  ? 401  ASP A CG  1 
ATOM   1405 O  OD1 . ASP A 1 178 ? -1.703  -27.755 8.290   1.00 26.72  ? 401  ASP A OD1 1 
ATOM   1406 O  OD2 . ASP A 1 178 ? -0.693  -29.249 7.024   1.00 27.87  ? 401  ASP A OD2 1 
ATOM   1407 N  N   . ASN A 1 179 ? 2.037   -27.890 11.714  1.00 19.59  ? 402  ASN A N   1 
ATOM   1408 C  CA  . ASN A 1 179 ? 2.877   -28.335 12.815  1.00 20.59  ? 402  ASN A CA  1 
ATOM   1409 C  C   . ASN A 1 179 ? 3.374   -27.155 13.634  1.00 17.92  ? 402  ASN A C   1 
ATOM   1410 O  O   . ASN A 1 179 ? 4.407   -27.234 14.289  1.00 19.87  ? 402  ASN A O   1 
ATOM   1411 C  CB  . ASN A 1 179 ? 4.008   -29.223 12.303  1.00 24.18  ? 402  ASN A CB  1 
ATOM   1412 C  CG  . ASN A 1 179 ? 3.484   -30.526 11.705  1.00 29.44  ? 402  ASN A CG  1 
ATOM   1413 O  OD1 . ASN A 1 179 ? 3.068   -31.416 12.437  1.00 31.11  ? 402  ASN A OD1 1 
ATOM   1414 N  ND2 . ASN A 1 179 ? 3.472   -30.625 10.378  1.00 31.53  ? 402  ASN A ND2 1 
ATOM   1415 N  N   . TYR A 1 180 ? 2.605   -26.072 13.634  1.00 15.20  ? 403  TYR A N   1 
ATOM   1416 C  CA  . TYR A 1 180 ? 2.944   -24.871 14.396  1.00 13.43  ? 403  TYR A CA  1 
ATOM   1417 C  C   . TYR A 1 180 ? 2.635   -25.110 15.873  1.00 13.63  ? 403  TYR A C   1 
ATOM   1418 O  O   . TYR A 1 180 ? 1.482   -25.363 16.234  1.00 16.11  ? 403  TYR A O   1 
ATOM   1419 C  CB  . TYR A 1 180 ? 2.116   -23.705 13.856  1.00 12.90  ? 403  TYR A CB  1 
ATOM   1420 C  CG  . TYR A 1 180 ? 2.038   -22.487 14.749  1.00 11.85  ? 403  TYR A CG  1 
ATOM   1421 C  CD1 . TYR A 1 180 ? 3.186   -21.825 15.178  1.00 12.51  ? 403  TYR A CD1 1 
ATOM   1422 C  CD2 . TYR A 1 180 ? 0.805   -21.973 15.120  1.00 12.65  ? 403  TYR A CD2 1 
ATOM   1423 C  CE1 . TYR A 1 180 ? 3.097   -20.704 15.988  1.00 12.92  ? 403  TYR A CE1 1 
ATOM   1424 C  CE2 . TYR A 1 180 ? 0.704   -20.861 15.923  1.00 12.75  ? 403  TYR A CE2 1 
ATOM   1425 C  CZ  . TYR A 1 180 ? 1.856   -20.218 16.353  1.00 13.08  ? 403  TYR A CZ  1 
ATOM   1426 O  OH  . TYR A 1 180 ? 1.770   -19.102 17.156  1.00 12.97  ? 403  TYR A OH  1 
ATOM   1427 N  N   . LYS A 1 181 ? 3.653   -25.012 16.729  1.00 13.27  ? 404  LYS A N   1 
ATOM   1428 C  CA  . LYS A 1 181 ? 3.508   -25.270 18.164  1.00 14.01  ? 404  LYS A CA  1 
ATOM   1429 C  C   . LYS A 1 181 ? 4.098   -24.075 18.907  1.00 13.49  ? 404  LYS A C   1 
ATOM   1430 O  O   . LYS A 1 181 ? 5.317   -23.982 19.086  1.00 13.72  ? 404  LYS A O   1 
ATOM   1431 C  CB  . LYS A 1 181 ? 4.200   -26.572 18.562  1.00 16.74  ? 404  LYS A CB  1 
ATOM   1432 C  CG  . LYS A 1 181 ? 3.556   -27.821 17.955  1.00 21.45  ? 404  LYS A CG  1 
ATOM   1433 C  CD  . LYS A 1 181 ? 2.103   -27.975 18.405  1.00 26.82  ? 404  LYS A CD  1 
ATOM   1434 C  CE  . LYS A 1 181 ? 1.660   -29.430 18.433  1.00 32.07  ? 404  LYS A CE  1 
ATOM   1435 N  NZ  . LYS A 1 181 ? 1.883   -30.109 17.138  1.00 34.63  ? 404  LYS A NZ  1 
ATOM   1436 N  N   . GLN A 1 182 ? 3.234   -23.137 19.310  1.00 12.10  ? 405  GLN A N   1 
ATOM   1437 C  CA  . GLN A 1 182 ? 3.711   -21.880 19.888  1.00 12.28  ? 405  GLN A CA  1 
ATOM   1438 C  C   . GLN A 1 182 ? 4.383   -22.067 21.235  1.00 12.59  ? 405  GLN A C   1 
ATOM   1439 O  O   . GLN A 1 182 ? 5.155   -21.191 21.636  1.00 13.70  ? 405  GLN A O   1 
ATOM   1440 C  CB  . GLN A 1 182 ? 2.571   -20.861 20.017  1.00 12.88  ? 405  GLN A CB  1 
ATOM   1441 C  CG  . GLN A 1 182 ? 1.581   -21.154 21.133  1.00 13.22  ? 405  GLN A CG  1 
ATOM   1442 C  CD  . GLN A 1 182 ? 0.790   -19.917 21.520  1.00 12.37  ? 405  GLN A CD  1 
ATOM   1443 O  OE1 . GLN A 1 182 ? 1.333   -18.810 21.532  1.00 13.71  ? 405  GLN A OE1 1 
ATOM   1444 N  NE2 . GLN A 1 182 ? -0.493  -20.092 21.821  1.00 13.82  ? 405  GLN A NE2 1 
ATOM   1445 N  N   . TRP A 1 183 ? 4.106   -23.165 21.943  1.00 12.59  ? 406  TRP A N   1 
ATOM   1446 C  CA  . TRP A 1 183 ? 4.691   -23.408 23.259  1.00 14.02  ? 406  TRP A CA  1 
ATOM   1447 C  C   . TRP A 1 183 ? 5.820   -24.433 23.235  1.00 15.23  ? 406  TRP A C   1 
ATOM   1448 O  O   . TRP A 1 183 ? 6.187   -24.956 24.288  1.00 16.74  ? 406  TRP A O   1 
ATOM   1449 C  CB  . TRP A 1 183 ? 3.628   -23.825 24.282  1.00 14.26  ? 406  TRP A CB  1 
ATOM   1450 C  CG  . TRP A 1 183 ? 2.546   -22.804 24.502  1.00 15.20  ? 406  TRP A CG  1 
ATOM   1451 C  CD1 . TRP A 1 183 ? 1.200   -23.013 24.414  1.00 16.62  ? 406  TRP A CD1 1 
ATOM   1452 C  CD2 . TRP A 1 183 ? 2.710   -21.413 24.830  1.00 14.35  ? 406  TRP A CD2 1 
ATOM   1453 N  NE1 . TRP A 1 183 ? 0.516   -21.855 24.685  1.00 16.31  ? 406  TRP A NE1 1 
ATOM   1454 C  CE2 . TRP A 1 183 ? 1.416   -20.850 24.922  1.00 14.82  ? 406  TRP A CE2 1 
ATOM   1455 C  CE3 . TRP A 1 183 ? 3.821   -20.586 25.042  1.00 15.21  ? 406  TRP A CE3 1 
ATOM   1456 C  CZ2 . TRP A 1 183 ? 1.205   -19.511 25.241  1.00 14.84  ? 406  TRP A CZ2 1 
ATOM   1457 C  CZ3 . TRP A 1 183 ? 3.606   -19.256 25.350  1.00 15.85  ? 406  TRP A CZ3 1 
ATOM   1458 C  CH2 . TRP A 1 183 ? 2.307   -18.730 25.445  1.00 16.07  ? 406  TRP A CH2 1 
ATOM   1459 N  N   . GLU A 1 184 ? 6.375   -24.733 22.069  1.00 14.49  ? 407  GLU A N   1 
ATOM   1460 C  CA  . GLU A 1 184 ? 7.538   -25.604 21.960  1.00 13.55  ? 407  GLU A CA  1 
ATOM   1461 C  C   . GLU A 1 184 ? 8.685   -24.788 21.385  1.00 13.63  ? 407  GLU A C   1 
ATOM   1462 O  O   . GLU A 1 184 ? 8.589   -24.274 20.264  1.00 14.05  ? 407  GLU A O   1 
ATOM   1463 C  CB  . GLU A 1 184 ? 7.219   -26.833 21.103  1.00 15.53  ? 407  GLU A CB  1 
ATOM   1464 C  CG  . GLU A 1 184 ? 6.133   -27.707 21.731  1.00 17.46  ? 407  GLU A CG  1 
ATOM   1465 C  CD  . GLU A 1 184 ? 5.777   -28.931 20.911  1.00 20.73  ? 407  GLU A CD  1 
ATOM   1466 O  OE1 . GLU A 1 184 ? 6.637   -29.394 20.133  1.00 23.47  ? 407  GLU A OE1 1 
ATOM   1467 O  OE2 . GLU A 1 184 ? 4.639   -29.433 21.057  1.00 23.92  ? 407  GLU A OE2 1 
ATOM   1468 N  N   . LEU A 1 185 ? 9.750   -24.638 22.162  1.00 14.25  ? 408  LEU A N   1 
ATOM   1469 C  CA  . LEU A 1 185 ? 10.906  -23.899 21.690  1.00 15.36  ? 408  LEU A CA  1 
ATOM   1470 C  C   . LEU A 1 185 ? 11.612  -24.688 20.593  1.00 15.93  ? 408  LEU A C   1 
ATOM   1471 O  O   . LEU A 1 185 ? 11.659  -25.925 20.646  1.00 16.93  ? 408  LEU A O   1 
ATOM   1472 C  CB  . LEU A 1 185 ? 11.890  -23.646 22.834  1.00 15.27  ? 408  LEU A CB  1 
ATOM   1473 C  CG  . LEU A 1 185 ? 11.415  -22.699 23.944  1.00 15.70  ? 408  LEU A CG  1 
ATOM   1474 C  CD1 . LEU A 1 185 ? 12.447  -22.550 25.040  1.00 16.92  ? 408  LEU A CD1 1 
ATOM   1475 C  CD2 . LEU A 1 185 ? 11.081  -21.329 23.375  1.00 15.61  ? 408  LEU A CD2 1 
ATOM   1476 N  N   . PRO A 1 186 ? 12.173  -24.014 19.595  1.00 14.39  ? 409  PRO A N   1 
ATOM   1477 C  CA  . PRO A 1 186 ? 13.053  -24.706 18.650  1.00 15.37  ? 409  PRO A CA  1 
ATOM   1478 C  C   . PRO A 1 186 ? 14.370  -25.028 19.333  1.00 15.85  ? 409  PRO A C   1 
ATOM   1479 O  O   . PRO A 1 186 ? 14.650  -24.580 20.447  1.00 16.84  ? 409  PRO A O   1 
ATOM   1480 C  CB  . PRO A 1 186 ? 13.237  -23.687 17.524  1.00 18.86  ? 409  PRO A CB  1 
ATOM   1481 C  CG  . PRO A 1 186 ? 13.059  -22.366 18.193  1.00 17.56  ? 409  PRO A CG  1 
ATOM   1482 C  CD  . PRO A 1 186 ? 12.133  -22.555 19.367  1.00 14.83  ? 409  PRO A CD  1 
ATOM   1483 N  N   . ASN A 1 187 ? 15.180  -25.831 18.651  1.00 16.95  ? 410  ASN A N   1 
ATOM   1484 C  CA  . ASN A 1 187 ? 16.535  -26.122 19.119  1.00 18.21  ? 410  ASN A CA  1 
ATOM   1485 C  C   . ASN A 1 187 ? 17.436  -25.052 18.528  1.00 17.39  ? 410  ASN A C   1 
ATOM   1486 O  O   . ASN A 1 187 ? 17.821  -25.126 17.359  1.00 18.73  ? 410  ASN A O   1 
ATOM   1487 C  CB  . ASN A 1 187 ? 16.982  -27.504 18.660  1.00 20.11  ? 410  ASN A CB  1 
ATOM   1488 C  CG  . ASN A 1 187 ? 16.128  -28.608 19.225  1.00 23.55  ? 410  ASN A CG  1 
ATOM   1489 O  OD1 . ASN A 1 187 ? 15.698  -28.547 20.373  1.00 26.16  ? 410  ASN A OD1 1 
ATOM   1490 N  ND2 . ASN A 1 187 ? 15.894  -29.642 18.423  1.00 26.07  ? 410  ASN A ND2 1 
ATOM   1491 N  N   . TYR A 1 188 ? 17.769  -24.042 19.334  1.00 16.51  ? 411  TYR A N   1 
ATOM   1492 C  CA  . TYR A 1 188 ? 18.514  -22.907 18.807  1.00 16.42  ? 411  TYR A CA  1 
ATOM   1493 C  C   . TYR A 1 188 ? 19.895  -23.304 18.293  1.00 16.72  ? 411  TYR A C   1 
ATOM   1494 O  O   . TYR A 1 188 ? 20.471  -22.588 17.468  1.00 17.15  ? 411  TYR A O   1 
ATOM   1495 C  CB  . TYR A 1 188 ? 18.638  -21.825 19.870  1.00 16.09  ? 411  TYR A CB  1 
ATOM   1496 C  CG  . TYR A 1 188 ? 17.337  -21.210 20.342  1.00 15.09  ? 411  TYR A CG  1 
ATOM   1497 C  CD1 . TYR A 1 188 ? 16.569  -20.403 19.498  1.00 14.62  ? 411  TYR A CD1 1 
ATOM   1498 C  CD2 . TYR A 1 188 ? 16.894  -21.398 21.649  1.00 15.80  ? 411  TYR A CD2 1 
ATOM   1499 C  CE1 . TYR A 1 188 ? 15.391  -19.814 19.944  1.00 13.51  ? 411  TYR A CE1 1 
ATOM   1500 C  CE2 . TYR A 1 188 ? 15.720  -20.816 22.098  1.00 14.82  ? 411  TYR A CE2 1 
ATOM   1501 C  CZ  . TYR A 1 188 ? 14.975  -20.022 21.244  1.00 13.60  ? 411  TYR A CZ  1 
ATOM   1502 O  OH  . TYR A 1 188 ? 13.810  -19.432 21.685  1.00 14.14  ? 411  TYR A OH  1 
ATOM   1503 N  N   . SER A 1 189 ? 20.458  -24.410 18.788  1.00 18.03  ? 412  SER A N   1 
ATOM   1504 C  CA  . SER A 1 189 ? 21.750  -24.911 18.322  1.00 19.43  ? 412  SER A CA  1 
ATOM   1505 C  C   . SER A 1 189 ? 21.639  -26.159 17.457  1.00 20.69  ? 412  SER A C   1 
ATOM   1506 O  O   . SER A 1 189 ? 22.660  -26.810 17.201  1.00 22.05  ? 412  SER A O   1 
ATOM   1507 C  CB  . SER A 1 189 ? 22.678  -25.195 19.506  1.00 20.75  ? 412  SER A CB  1 
ATOM   1508 O  OG  . SER A 1 189 ? 23.050  -23.998 20.151  1.00 22.96  ? 412  SER A OG  1 
ATOM   1509 N  N   . GLY A 1 190 ? 20.440  -26.514 16.997  1.00 21.67  ? 413  GLY A N   1 
ATOM   1510 C  CA  . GLY A 1 190 ? 20.285  -27.745 16.255  1.00 23.54  ? 413  GLY A CA  1 
ATOM   1511 C  C   . GLY A 1 190 ? 20.218  -28.966 17.157  1.00 25.58  ? 413  GLY A C   1 
ATOM   1512 O  O   . GLY A 1 190 ? 20.101  -28.889 18.383  1.00 24.19  ? 413  GLY A O   1 
ATOM   1513 N  N   . ALA A 1 191 ? 20.319  -30.123 16.516  1.00 28.78  ? 414  ALA A N   1 
ATOM   1514 C  CA  . ALA A 1 191 ? 20.055  -31.395 17.183  1.00 34.35  ? 414  ALA A CA  1 
ATOM   1515 C  C   . ALA A 1 191 ? 21.126  -31.778 18.206  1.00 36.14  ? 414  ALA A C   1 
ATOM   1516 O  O   . ALA A 1 191 ? 22.235  -31.243 18.198  1.00 38.40  ? 414  ALA A O   1 
ATOM   1517 C  CB  . ALA A 1 191 ? 19.887  -32.493 16.156  1.00 36.80  ? 414  ALA A CB  1 
ATOM   1518 N  N   . THR A 1 193 ? 21.870  -30.721 21.048  1.00 47.20  ? 416  THR A N   1 
ATOM   1519 C  CA  . THR A 1 193 ? 22.408  -29.635 21.857  1.00 45.89  ? 416  THR A CA  1 
ATOM   1520 C  C   . THR A 1 193 ? 21.272  -28.921 22.571  1.00 40.52  ? 416  THR A C   1 
ATOM   1521 O  O   . THR A 1 193 ? 20.325  -28.470 21.934  1.00 41.04  ? 416  THR A O   1 
ATOM   1522 C  CB  . THR A 1 193 ? 23.173  -28.618 20.995  1.00 48.42  ? 416  THR A CB  1 
ATOM   1523 O  OG1 . THR A 1 193 ? 24.022  -29.313 20.076  1.00 49.04  ? 416  THR A OG1 1 
ATOM   1524 C  CG2 . THR A 1 193 ? 24.021  -27.704 21.872  1.00 50.53  ? 416  THR A CG2 1 
ATOM   1525 N  N   . LEU A 1 194 ? 21.375  -28.809 23.891  1.00 34.47  ? 417  LEU A N   1 
ATOM   1526 C  CA  . LEU A 1 194 ? 20.311  -28.221 24.689  1.00 29.58  ? 417  LEU A CA  1 
ATOM   1527 C  C   . LEU A 1 194 ? 20.314  -26.703 24.553  1.00 25.18  ? 417  LEU A C   1 
ATOM   1528 O  O   . LEU A 1 194 ? 21.359  -26.076 24.354  1.00 24.93  ? 417  LEU A O   1 
ATOM   1529 C  CB  . LEU A 1 194 ? 20.492  -28.596 26.162  1.00 30.51  ? 417  LEU A CB  1 
ATOM   1530 C  CG  . LEU A 1 194 ? 20.437  -30.094 26.478  1.00 32.08  ? 417  LEU A CG  1 
ATOM   1531 C  CD1 . LEU A 1 194 ? 20.572  -30.323 27.976  1.00 33.51  ? 417  LEU A CD1 1 
ATOM   1532 C  CD2 . LEU A 1 194 ? 19.156  -30.710 25.949  1.00 34.24  ? 417  LEU A CD2 1 
ATOM   1533 N  N   . ASN A 1 195 ? 19.126  -26.113 24.665  1.00 21.59  ? 418  ASN A N   1 
ATOM   1534 C  CA  . ASN A 1 195 ? 19.031  -24.661 24.705  1.00 19.19  ? 418  ASN A CA  1 
ATOM   1535 C  C   . ASN A 1 195 ? 19.650  -24.122 25.993  1.00 19.03  ? 418  ASN A C   1 
ATOM   1536 O  O   . ASN A 1 195 ? 19.662  -24.788 27.032  1.00 20.84  ? 418  ASN A O   1 
ATOM   1537 C  CB  . ASN A 1 195 ? 17.570  -24.232 24.633  1.00 17.89  ? 418  ASN A CB  1 
ATOM   1538 C  CG  . ASN A 1 195 ? 16.950  -24.504 23.275  1.00 18.03  ? 418  ASN A CG  1 
ATOM   1539 O  OD1 . ASN A 1 195 ? 17.651  -24.576 22.264  1.00 18.91  ? 418  ASN A OD1 1 
ATOM   1540 N  ND2 . ASN A 1 195 ? 15.634  -24.675 23.253  1.00 18.28  ? 418  ASN A ND2 1 
ATOM   1541 N  N   A MET A 1 196 ? 20.145  -22.888 25.913  0.58 19.04  ? 419  MET A N   1 
ATOM   1542 N  N   B MET A 1 196 ? 20.176  -22.901 25.918  0.42 18.85  ? 419  MET A N   1 
ATOM   1543 C  CA  A MET A 1 196 ? 20.824  -22.233 27.019  0.58 19.28  ? 419  MET A CA  1 
ATOM   1544 C  CA  B MET A 1 196 ? 20.806  -22.272 27.072  0.42 19.04  ? 419  MET A CA  1 
ATOM   1545 C  C   A MET A 1 196 ? 20.256  -20.834 27.217  0.58 17.03  ? 419  MET A C   1 
ATOM   1546 C  C   B MET A 1 196 ? 20.336  -20.829 27.195  0.42 17.70  ? 419  MET A C   1 
ATOM   1547 O  O   A MET A 1 196 ? 19.556  -20.295 26.355  0.58 16.87  ? 419  MET A O   1 
ATOM   1548 O  O   B MET A 1 196 ? 19.778  -20.254 26.260  0.42 18.08  ? 419  MET A O   1 
ATOM   1549 C  CB  A MET A 1 196 ? 22.329  -22.131 26.749  0.58 21.68  ? 419  MET A CB  1 
ATOM   1550 C  CB  B MET A 1 196 ? 22.341  -22.340 27.000  0.42 21.20  ? 419  MET A CB  1 
ATOM   1551 C  CG  A MET A 1 196 ? 23.008  -23.476 26.579  0.58 24.08  ? 419  MET A CG  1 
ATOM   1552 C  CG  B MET A 1 196 ? 22.886  -23.760 26.940  0.42 23.16  ? 419  MET A CG  1 
ATOM   1553 S  SD  A MET A 1 196 ? 23.140  -24.384 28.133  0.58 28.72  ? 419  MET A SD  1 
ATOM   1554 S  SD  B MET A 1 196 ? 24.663  -23.882 27.221  0.42 26.03  ? 419  MET A SD  1 
ATOM   1555 C  CE  A MET A 1 196 ? 24.481  -23.499 28.931  0.58 29.96  ? 419  MET A CE  1 
ATOM   1556 C  CE  B MET A 1 196 ? 24.774  -23.431 28.951  0.42 25.62  ? 419  MET A CE  1 
ATOM   1557 N  N   . GLY A 1 197 ? 20.563  -20.253 28.375  1.00 17.10  ? 420  GLY A N   1 
ATOM   1558 C  CA  . GLY A 1 197 ? 20.217  -18.866 28.638  1.00 16.86  ? 420  GLY A CA  1 
ATOM   1559 C  C   . GLY A 1 197 ? 18.736  -18.573 28.703  1.00 15.27  ? 420  GLY A C   1 
ATOM   1560 O  O   . GLY A 1 197 ? 18.339  -17.416 28.541  1.00 17.77  ? 420  GLY A O   1 
ATOM   1561 N  N   . LEU A 1 198 ? 17.897  -19.583 28.936  1.00 14.59  ? 421  LEU A N   1 
ATOM   1562 C  CA  . LEU A 1 198 ? 16.453  -19.411 28.801  1.00 14.80  ? 421  LEU A CA  1 
ATOM   1563 C  C   . LEU A 1 198 ? 15.857  -18.592 29.941  1.00 14.14  ? 421  LEU A C   1 
ATOM   1564 O  O   . LEU A 1 198 ? 16.235  -18.746 31.108  1.00 16.13  ? 421  LEU A O   1 
ATOM   1565 C  CB  . LEU A 1 198 ? 15.758  -20.776 28.756  1.00 15.40  ? 421  LEU A CB  1 
ATOM   1566 C  CG  . LEU A 1 198 ? 16.113  -21.689 27.588  1.00 16.62  ? 421  LEU A CG  1 
ATOM   1567 C  CD1 . LEU A 1 198 ? 15.230  -22.922 27.633  1.00 18.53  ? 421  LEU A CD1 1 
ATOM   1568 C  CD2 . LEU A 1 198 ? 15.951  -20.950 26.260  1.00 16.93  ? 421  LEU A CD2 1 
ATOM   1569 N  N   . ALA A 1 199 ? 14.903  -17.727 29.594  1.00 13.53  ? 422  ALA A N   1 
ATOM   1570 C  CA  . ALA A 1 199 ? 13.988  -17.175 30.581  1.00 13.97  ? 422  ALA A CA  1 
ATOM   1571 C  C   . ALA A 1 199 ? 13.173  -18.318 31.197  1.00 14.43  ? 422  ALA A C   1 
ATOM   1572 O  O   . ALA A 1 199 ? 12.870  -19.309 30.520  1.00 14.65  ? 422  ALA A O   1 
ATOM   1573 C  CB  . ALA A 1 199 ? 13.051  -16.161 29.915  1.00 13.93  ? 422  ALA A CB  1 
ATOM   1574 N  N   . PRO A 1 200 ? 12.793  -18.203 32.470  1.00 14.21  ? 423  PRO A N   1 
ATOM   1575 C  CA  A PRO A 1 200 ? 12.090  -19.309 33.130  0.32 14.96  ? 423  PRO A CA  1 
ATOM   1576 C  CA  B PRO A 1 200 ? 12.086  -19.305 33.136  0.68 14.92  ? 423  PRO A CA  1 
ATOM   1577 C  C   . PRO A 1 200 ? 10.710  -19.556 32.544  1.00 14.89  ? 423  PRO A C   1 
ATOM   1578 O  O   . PRO A 1 200 ? 10.045  -18.648 32.034  1.00 14.72  ? 423  PRO A O   1 
ATOM   1579 C  CB  A PRO A 1 200 ? 11.979  -18.835 34.584  0.32 15.41  ? 423  PRO A CB  1 
ATOM   1580 C  CB  B PRO A 1 200 ? 11.959  -18.810 34.581  0.68 15.02  ? 423  PRO A CB  1 
ATOM   1581 C  CG  A PRO A 1 200 ? 12.034  -17.348 34.501  0.32 15.73  ? 423  PRO A CG  1 
ATOM   1582 C  CG  B PRO A 1 200 ? 13.066  -17.791 34.744  0.68 15.94  ? 423  PRO A CG  1 
ATOM   1583 C  CD  A PRO A 1 200 ? 12.978  -17.051 33.369  0.32 14.99  ? 423  PRO A CD  1 
ATOM   1584 C  CD  B PRO A 1 200 ? 13.128  -17.116 33.406  0.68 15.76  ? 423  PRO A CD  1 
ATOM   1585 N  N   . SER A 1 201 ? 10.274  -20.808 32.642  1.00 14.47  ? 424  SER A N   1 
ATOM   1586 C  CA  . SER A 1 201 ? 8.901   -21.136 32.294  1.00 14.48  ? 424  SER A CA  1 
ATOM   1587 C  C   . SER A 1 201 ? 7.964   -20.697 33.424  1.00 15.53  ? 424  SER A C   1 
ATOM   1588 O  O   . SER A 1 201 ? 8.368   -20.567 34.587  1.00 15.46  ? 424  SER A O   1 
ATOM   1589 C  CB  . SER A 1 201 ? 8.763   -22.636 32.006  1.00 14.92  ? 424  SER A CB  1 
ATOM   1590 O  OG  . SER A 1 201 ? 8.933   -23.420 33.184  1.00 15.29  ? 424  SER A OG  1 
ATOM   1591 N  N   . VAL A 1 202 ? 6.703   -20.456 33.070  1.00 15.48  ? 425  VAL A N   1 
ATOM   1592 C  CA  . VAL A 1 202 ? 5.722   -19.887 33.987  1.00 15.77  ? 425  VAL A CA  1 
ATOM   1593 C  C   . VAL A 1 202 ? 4.461   -20.747 34.007  1.00 18.30  ? 425  VAL A C   1 
ATOM   1594 O  O   . VAL A 1 202 ? 4.121   -21.417 33.027  1.00 18.89  ? 425  VAL A O   1 
ATOM   1595 C  CB  . VAL A 1 202 ? 5.384   -18.417 33.624  1.00 18.41  ? 425  VAL A CB  1 
ATOM   1596 C  CG1 . VAL A 1 202 ? 6.631   -17.551 33.722  1.00 20.21  ? 425  VAL A CG1 1 
ATOM   1597 C  CG2 . VAL A 1 202 ? 4.782   -18.315 32.219  1.00 17.49  ? 425  VAL A CG2 1 
ATOM   1598 N  N   . PHE A 1 203 ? 3.756   -20.720 35.135  1.00 19.99  ? 426  PHE A N   1 
ATOM   1599 C  CA  . PHE A 1 203 ? 2.508   -21.462 35.257  1.00 23.38  ? 426  PHE A CA  1 
ATOM   1600 C  C   . PHE A 1 203 ? 1.734   -20.903 36.436  1.00 23.72  ? 426  PHE A C   1 
ATOM   1601 O  O   . PHE A 1 203 ? 2.339   -20.336 37.352  1.00 24.23  ? 426  PHE A O   1 
ATOM   1602 C  CB  . PHE A 1 203 ? 2.764   -22.964 35.464  1.00 24.06  ? 426  PHE A CB  1 
ATOM   1603 C  CG  . PHE A 1 203 ? 3.809   -23.265 36.494  1.00 23.99  ? 426  PHE A CG  1 
ATOM   1604 C  CD1 . PHE A 1 203 ? 3.487   -23.314 37.840  1.00 24.38  ? 426  PHE A CD1 1 
ATOM   1605 C  CD2 . PHE A 1 203 ? 5.120   -23.492 36.118  1.00 26.96  ? 426  PHE A CD2 1 
ATOM   1606 C  CE1 . PHE A 1 203 ? 4.461   -23.594 38.795  1.00 27.39  ? 426  PHE A CE1 1 
ATOM   1607 C  CE2 . PHE A 1 203 ? 6.094   -23.767 37.067  1.00 27.19  ? 426  PHE A CE2 1 
ATOM   1608 C  CZ  . PHE A 1 203 ? 5.764   -23.814 38.403  1.00 27.56  ? 426  PHE A CZ  1 
ATOM   1609 N  N   . PRO A 1 204 ? 0.412   -21.037 36.445  1.00 25.22  ? 427  PRO A N   1 
ATOM   1610 C  CA  . PRO A 1 204 ? -0.359  -20.633 37.623  1.00 26.91  ? 427  PRO A CA  1 
ATOM   1611 C  C   . PRO A 1 204 ? -0.206  -21.651 38.740  1.00 29.08  ? 427  PRO A C   1 
ATOM   1612 O  O   . PRO A 1 204 ? 0.045   -22.836 38.509  1.00 29.08  ? 427  PRO A O   1 
ATOM   1613 C  CB  . PRO A 1 204 ? -1.801  -20.612 37.102  1.00 27.06  ? 427  PRO A CB  1 
ATOM   1614 C  CG  . PRO A 1 204 ? -1.809  -21.626 36.006  1.00 26.17  ? 427  PRO A CG  1 
ATOM   1615 C  CD  . PRO A 1 204 ? -0.449  -21.551 35.364  1.00 24.30  ? 427  PRO A CD  1 
ATOM   1616 N  N   . THR A 1 205 ? -0.339  -21.167 39.961  1.00 31.08  ? 428  THR A N   1 
ATOM   1617 C  CA  . THR A 1 205 ? -0.218  -22.036 41.130  1.00 34.42  ? 428  THR A CA  1 
ATOM   1618 C  C   . THR A 1 205 ? -1.365  -21.881 42.116  1.00 35.83  ? 428  THR A C   1 
ATOM   1619 O  O   . THR A 1 205 ? -1.811  -22.879 42.690  1.00 35.84  ? 428  THR A O   1 
ATOM   1620 C  CB  . THR A 1 205 ? 1.117   -21.805 41.865  1.00 36.18  ? 428  THR A CB  1 
ATOM   1621 O  OG1 . THR A 1 205 ? 1.195   -20.442 42.302  1.00 37.01  ? 428  THR A OG1 1 
ATOM   1622 C  CG2 . THR A 1 205 ? 2.293   -22.113 40.958  1.00 36.24  ? 428  THR A CG2 1 
ATOM   1623 N  N   . TYR A 1 206 ? -1.836  -20.659 42.344  1.00 36.76  ? 429  TYR A N   1 
ATOM   1624 C  CA  . TYR A 1 206 ? -2.929  -20.452 43.280  1.00 37.91  ? 429  TYR A CA  1 
ATOM   1625 C  C   . TYR A 1 206 ? -4.170  -21.183 42.773  1.00 37.75  ? 429  TYR A C   1 
ATOM   1626 O  O   . TYR A 1 206 ? -4.443  -21.175 41.567  1.00 37.14  ? 429  TYR A O   1 
ATOM   1627 C  CB  . TYR A 1 206 ? -3.220  -18.956 43.413  1.00 39.57  ? 429  TYR A CB  1 
ATOM   1628 C  CG  . TYR A 1 206 ? -4.047  -18.588 44.624  1.00 41.25  ? 429  TYR A CG  1 
ATOM   1629 C  CD1 . TYR A 1 206 ? -3.447  -18.363 45.856  1.00 42.80  ? 429  TYR A CD1 1 
ATOM   1630 C  CD2 . TYR A 1 206 ? -5.428  -18.466 44.536  1.00 42.76  ? 429  TYR A CD2 1 
ATOM   1631 C  CE1 . TYR A 1 206 ? -4.197  -18.028 46.967  1.00 43.94  ? 429  TYR A CE1 1 
ATOM   1632 C  CE2 . TYR A 1 206 ? -6.188  -18.129 45.644  1.00 43.95  ? 429  TYR A CE2 1 
ATOM   1633 C  CZ  . TYR A 1 206 ? -5.566  -17.914 46.856  1.00 44.91  ? 429  TYR A CZ  1 
ATOM   1634 O  OH  . TYR A 1 206 ? -6.316  -17.580 47.959  1.00 46.80  ? 429  TYR A OH  1 
ATOM   1635 N  N   . PRO A 1 207 ? -4.922  -21.845 43.652  1.00 37.65  ? 430  PRO A N   1 
ATOM   1636 C  CA  . PRO A 1 207 ? -6.069  -22.641 43.193  1.00 37.27  ? 430  PRO A CA  1 
ATOM   1637 C  C   . PRO A 1 207 ? -7.066  -21.788 42.424  1.00 35.87  ? 430  PRO A C   1 
ATOM   1638 O  O   . PRO A 1 207 ? -7.425  -20.687 42.845  1.00 37.32  ? 430  PRO A O   1 
ATOM   1639 C  CB  . PRO A 1 207 ? -6.678  -23.167 44.496  1.00 37.65  ? 430  PRO A CB  1 
ATOM   1640 C  CG  . PRO A 1 207 ? -5.571  -23.128 45.476  1.00 37.68  ? 430  PRO A CG  1 
ATOM   1641 C  CD  . PRO A 1 207 ? -4.726  -21.950 45.107  1.00 37.95  ? 430  PRO A CD  1 
ATOM   1642 N  N   . GLY A 1 208 ? -7.506  -22.305 41.280  1.00 33.12  ? 431  GLY A N   1 
ATOM   1643 C  CA  . GLY A 1 208 ? -8.466  -21.606 40.460  1.00 31.08  ? 431  GLY A CA  1 
ATOM   1644 C  C   . GLY A 1 208 ? -7.886  -20.564 39.530  1.00 29.41  ? 431  GLY A C   1 
ATOM   1645 O  O   . GLY A 1 208 ? -8.655  -19.882 38.842  1.00 30.17  ? 431  GLY A O   1 
ATOM   1646 N  N   . GLU A 1 209 ? -6.563  -20.414 39.478  1.00 27.90  ? 432  GLU A N   1 
ATOM   1647 C  CA  . GLU A 1 209 ? -5.937  -19.421 38.615  1.00 26.09  ? 432  GLU A CA  1 
ATOM   1648 C  C   . GLU A 1 209 ? -5.443  -20.021 37.301  1.00 24.76  ? 432  GLU A C   1 
ATOM   1649 O  O   . GLU A 1 209 ? -5.039  -21.184 37.233  1.00 25.25  ? 432  GLU A O   1 
ATOM   1650 C  CB  . GLU A 1 209 ? -4.798  -18.684 39.332  1.00 27.07  ? 432  GLU A CB  1 
ATOM   1651 C  CG  . GLU A 1 209 ? -5.298  -17.650 40.340  1.00 26.56  ? 432  GLU A CG  1 
ATOM   1652 C  CD  . GLU A 1 209 ? -4.201  -16.774 40.927  1.00 26.88  ? 432  GLU A CD  1 
ATOM   1653 O  OE1 . GLU A 1 209 ? -3.096  -16.711 40.345  1.00 26.38  ? 432  GLU A OE1 1 
ATOM   1654 O  OE2 . GLU A 1 209 ? -4.455  -16.135 41.976  1.00 27.81  ? 432  GLU A OE2 1 
ATOM   1655 N  N   . GLN A 1 210 ? -5.505  -19.202 36.248  1.00 22.84  ? 433  GLN A N   1 
ATOM   1656 C  CA  . GLN A 1 210 ? -4.965  -19.513 34.931  1.00 20.73  ? 433  GLN A CA  1 
ATOM   1657 C  C   . GLN A 1 210 ? -4.151  -18.326 34.437  1.00 19.33  ? 433  GLN A C   1 
ATOM   1658 O  O   . GLN A 1 210 ? -4.349  -17.190 34.869  1.00 20.39  ? 433  GLN A O   1 
ATOM   1659 C  CB  . GLN A 1 210 ? -6.082  -19.812 33.915  1.00 22.14  ? 433  GLN A CB  1 
ATOM   1660 C  CG  . GLN A 1 210 ? -6.649  -21.200 34.055  1.00 23.87  ? 433  GLN A CG  1 
ATOM   1661 C  CD  . GLN A 1 210 ? -7.804  -21.487 33.118  1.00 25.87  ? 433  GLN A CD  1 
ATOM   1662 O  OE1 . GLN A 1 210 ? -8.354  -22.584 33.132  1.00 28.12  ? 433  GLN A OE1 1 
ATOM   1663 N  NE2 . GLN A 1 210 ? -8.176  -20.510 32.300  1.00 25.21  ? 433  GLN A NE2 1 
ATOM   1664 N  N   . LEU A 1 211 ? -3.224  -18.599 33.526  1.00 18.24  ? 434  LEU A N   1 
ATOM   1665 C  CA  . LEU A 1 211 ? -2.539  -17.515 32.839  1.00 17.10  ? 434  LEU A CA  1 
ATOM   1666 C  C   . LEU A 1 211 ? -3.512  -16.733 31.967  1.00 17.64  ? 434  LEU A C   1 
ATOM   1667 O  O   . LEU A 1 211 ? -4.464  -17.283 31.404  1.00 17.94  ? 434  LEU A O   1 
ATOM   1668 C  CB  . LEU A 1 211 ? -1.431  -18.071 31.944  1.00 18.01  ? 434  LEU A CB  1 
ATOM   1669 C  CG  . LEU A 1 211 ? -0.232  -18.732 32.639  1.00 19.44  ? 434  LEU A CG  1 
ATOM   1670 C  CD1 . LEU A 1 211 ? 0.659   -19.477 31.647  1.00 20.16  ? 434  LEU A CD1 1 
ATOM   1671 C  CD2 . LEU A 1 211 ? 0.582   -17.709 33.413  1.00 21.87  ? 434  LEU A CD2 1 
ATOM   1672 N  N   . LEU A 1 212 ? -3.264  -15.432 31.876  1.00 16.62  ? 435  LEU A N   1 
ATOM   1673 C  CA  A LEU A 1 212 ? -3.945  -14.556 30.935  0.78 16.68  ? 435  LEU A CA  1 
ATOM   1674 C  CA  B LEU A 1 212 ? -3.944  -14.550 30.940  0.22 16.40  ? 435  LEU A CA  1 
ATOM   1675 C  C   . LEU A 1 212 ? -2.968  -14.187 29.830  1.00 15.95  ? 435  LEU A C   1 
ATOM   1676 O  O   . LEU A 1 212 ? -1.811  -13.848 30.103  1.00 17.99  ? 435  LEU A O   1 
ATOM   1677 C  CB  A LEU A 1 212 ? -4.447  -13.282 31.630  0.78 18.78  ? 435  LEU A CB  1 
ATOM   1678 C  CB  B LEU A 1 212 ? -4.422  -13.281 31.650  0.22 17.30  ? 435  LEU A CB  1 
ATOM   1679 C  CG  A LEU A 1 212 ? -5.186  -12.249 30.765  0.78 19.97  ? 435  LEU A CG  1 
ATOM   1680 C  CG  B LEU A 1 212 ? -4.816  -12.101 30.757  0.22 17.99  ? 435  LEU A CG  1 
ATOM   1681 C  CD1 A LEU A 1 212 ? -6.179  -11.471 31.598  0.78 21.82  ? 435  LEU A CD1 1 
ATOM   1682 C  CD1 B LEU A 1 212 ? -5.906  -12.494 29.783  0.22 19.07  ? 435  LEU A CD1 1 
ATOM   1683 C  CD2 A LEU A 1 212 ? -4.230  -11.267 30.072  0.78 21.42  ? 435  LEU A CD2 1 
ATOM   1684 C  CD2 B LEU A 1 212 ? -5.252  -10.912 31.598  0.22 17.71  ? 435  LEU A CD2 1 
ATOM   1685 N  N   . PHE A 1 213 ? -3.437  -14.245 28.586  1.00 14.12  ? 436  PHE A N   1 
ATOM   1686 C  CA  . PHE A 1 213 ? -2.598  -13.971 27.432  1.00 14.25  ? 436  PHE A CA  1 
ATOM   1687 C  C   . PHE A 1 213 ? -3.137  -12.798 26.628  1.00 14.32  ? 436  PHE A C   1 
ATOM   1688 O  O   . PHE A 1 213 ? -4.349  -12.546 26.579  1.00 15.81  ? 436  PHE A O   1 
ATOM   1689 C  CB  . PHE A 1 213 ? -2.525  -15.178 26.490  1.00 15.63  ? 436  PHE A CB  1 
ATOM   1690 C  CG  . PHE A 1 213 ? -1.943  -16.410 27.121  1.00 17.45  ? 436  PHE A CG  1 
ATOM   1691 C  CD1 . PHE A 1 213 ? -0.604  -16.462 27.464  1.00 17.72  ? 436  PHE A CD1 1 
ATOM   1692 C  CD2 . PHE A 1 213 ? -2.730  -17.528 27.350  1.00 19.78  ? 436  PHE A CD2 1 
ATOM   1693 C  CE1 . PHE A 1 213 ? -0.074  -17.590 28.053  1.00 18.22  ? 436  PHE A CE1 1 
ATOM   1694 C  CE2 . PHE A 1 213 ? -2.197  -18.657 27.928  1.00 21.00  ? 436  PHE A CE2 1 
ATOM   1695 C  CZ  . PHE A 1 213 ? -0.870  -18.692 28.268  1.00 19.27  ? 436  PHE A CZ  1 
ATOM   1696 N  N   . PHE A 1 214 ? -2.217  -12.102 25.973  1.00 12.45  ? 437  PHE A N   1 
ATOM   1697 C  CA  . PHE A 1 214 ? -2.549  -11.138 24.934  1.00 13.05  ? 437  PHE A CA  1 
ATOM   1698 C  C   . PHE A 1 214 ? -2.358  -11.851 23.601  1.00 13.30  ? 437  PHE A C   1 
ATOM   1699 O  O   . PHE A 1 214 ? -1.237  -12.251 23.265  1.00 13.45  ? 437  PHE A O   1 
ATOM   1700 C  CB  . PHE A 1 214 ? -1.637  -9.912  25.038  1.00 13.56  ? 437  PHE A CB  1 
ATOM   1701 C  CG  . PHE A 1 214 ? -1.727  -9.194  26.364  1.00 13.33  ? 437  PHE A CG  1 
ATOM   1702 C  CD1 . PHE A 1 214 ? -1.021  -9.655  27.472  1.00 13.36  ? 437  PHE A CD1 1 
ATOM   1703 C  CD2 . PHE A 1 214 ? -2.519  -8.067  26.512  1.00 14.49  ? 437  PHE A CD2 1 
ATOM   1704 C  CE1 . PHE A 1 214 ? -1.094  -9.004  28.694  1.00 14.33  ? 437  PHE A CE1 1 
ATOM   1705 C  CE2 . PHE A 1 214 ? -2.594  -7.405  27.735  1.00 16.07  ? 437  PHE A CE2 1 
ATOM   1706 C  CZ  . PHE A 1 214 ? -1.890  -7.882  28.830  1.00 15.57  ? 437  PHE A CZ  1 
ATOM   1707 N  N   . ARG A 1 215 ? -3.453  -12.034 22.861  1.00 13.02  ? 438  ARG A N   1 
ATOM   1708 C  CA  . ARG A 1 215 ? -3.495  -12.935 21.717  1.00 12.90  ? 438  ARG A CA  1 
ATOM   1709 C  C   . ARG A 1 215 ? -3.615  -12.153 20.416  1.00 13.24  ? 438  ARG A C   1 
ATOM   1710 O  O   . ARG A 1 215 ? -4.389  -11.194 20.327  1.00 13.86  ? 438  ARG A O   1 
ATOM   1711 C  CB  . ARG A 1 215 ? -4.693  -13.882 21.847  1.00 13.72  ? 438  ARG A CB  1 
ATOM   1712 C  CG  . ARG A 1 215 ? -4.880  -14.826 20.671  1.00 14.27  ? 438  ARG A CG  1 
ATOM   1713 C  CD  . ARG A 1 215 ? -5.874  -15.934 20.997  1.00 15.35  ? 438  ARG A CD  1 
ATOM   1714 N  NE  . ARG A 1 215 ? -5.329  -16.839 22.002  1.00 17.20  ? 438  ARG A NE  1 
ATOM   1715 C  CZ  . ARG A 1 215 ? -5.889  -17.981 22.378  1.00 17.56  ? 438  ARG A CZ  1 
ATOM   1716 N  NH1 . ARG A 1 215 ? -7.060  -18.371 21.896  1.00 19.27  ? 438  ARG A NH1 1 
ATOM   1717 N  NH2 . ARG A 1 215 ? -5.245  -18.767 23.233  1.00 17.36  ? 438  ARG A NH2 1 
ATOM   1718 N  N   . SER A 1 216 ? -2.865  -12.590 19.396  1.00 12.67  ? 439  SER A N   1 
ATOM   1719 C  CA  . SER A 1 216 ? -3.001  -12.067 18.041  1.00 11.97  ? 439  SER A CA  1 
ATOM   1720 C  C   . SER A 1 216 ? -3.095  -13.203 17.032  1.00 12.54  ? 439  SER A C   1 
ATOM   1721 O  O   . SER A 1 216 ? -2.348  -14.183 17.118  1.00 12.98  ? 439  SER A O   1 
ATOM   1722 C  CB  . SER A 1 216 ? -1.794  -11.244 17.638  1.00 11.73  ? 439  SER A CB  1 
ATOM   1723 O  OG  . SER A 1 216 ? -1.576  -10.179 18.538  1.00 12.09  ? 439  SER A OG  1 
ATOM   1724 N  N   . TYR A 1 217 ? -3.969  -13.047 16.040  1.00 12.44  ? 440  TYR A N   1 
ATOM   1725 C  CA  . TYR A 1 217 ? -3.953  -13.925 14.876  1.00 12.89  ? 440  TYR A CA  1 
ATOM   1726 C  C   . TYR A 1 217 ? -2.813  -13.544 13.932  1.00 14.15  ? 440  TYR A C   1 
ATOM   1727 O  O   . TYR A 1 217 ? -2.390  -12.383 13.870  1.00 17.67  ? 440  TYR A O   1 
ATOM   1728 C  CB  . TYR A 1 217 ? -5.296  -13.875 14.149  1.00 14.33  ? 440  TYR A CB  1 
ATOM   1729 C  CG  . TYR A 1 217 ? -6.399  -14.519 14.934  1.00 18.15  ? 440  TYR A CG  1 
ATOM   1730 C  CD1 . TYR A 1 217 ? -6.513  -15.903 14.989  1.00 20.14  ? 440  TYR A CD1 1 
ATOM   1731 C  CD2 . TYR A 1 217 ? -7.333  -13.756 15.622  1.00 24.86  ? 440  TYR A CD2 1 
ATOM   1732 C  CE1 . TYR A 1 217 ? -7.516  -16.517 15.717  1.00 24.11  ? 440  TYR A CE1 1 
ATOM   1733 C  CE2 . TYR A 1 217 ? -8.349  -14.363 16.339  1.00 28.19  ? 440  TYR A CE2 1 
ATOM   1734 C  CZ  . TYR A 1 217 ? -8.434  -15.742 16.386  1.00 29.32  ? 440  TYR A CZ  1 
ATOM   1735 O  OH  . TYR A 1 217 ? -9.444  -16.346 17.104  1.00 34.24  ? 440  TYR A OH  1 
ATOM   1736 N  N   A ILE A 1 218 ? -2.336  -14.527 13.178  0.58 13.26  ? 441  ILE A N   1 
ATOM   1737 N  N   B ILE A 1 218 ? -2.317  -14.547 13.203  0.42 13.21  ? 441  ILE A N   1 
ATOM   1738 C  CA  A ILE A 1 218 ? -1.154  -14.374 12.333  0.58 14.45  ? 441  ILE A CA  1 
ATOM   1739 C  CA  B ILE A 1 218 ? -1.139  -14.484 12.332  0.42 14.46  ? 441  ILE A CA  1 
ATOM   1740 C  C   A ILE A 1 218 ? -1.506  -14.745 10.897  0.58 11.74  ? 441  ILE A C   1 
ATOM   1741 C  C   B ILE A 1 218 ? -1.598  -14.700 10.892  0.42 12.53  ? 441  ILE A C   1 
ATOM   1742 O  O   A ILE A 1 218 ? -2.166  -15.768 10.673  0.58 11.09  ? 441  ILE A O   1 
ATOM   1743 O  O   B ILE A 1 218 ? -2.433  -15.581 10.659  0.42 14.03  ? 441  ILE A O   1 
ATOM   1744 C  CB  A ILE A 1 218 ? 0.006   -15.233 12.872  0.58 15.95  ? 441  ILE A CB  1 
ATOM   1745 C  CB  B ILE A 1 218 ? -0.135  -15.597 12.707  0.42 14.59  ? 441  ILE A CB  1 
ATOM   1746 C  CG1 A ILE A 1 218 ? 0.304   -14.864 14.325  0.58 19.73  ? 441  ILE A CG1 1 
ATOM   1747 C  CG1 B ILE A 1 218 ? 0.255   -15.552 14.187  0.42 15.19  ? 441  ILE A CG1 1 
ATOM   1748 C  CG2 A ILE A 1 218 ? 1.261   -15.035 12.057  0.58 19.37  ? 441  ILE A CG2 1 
ATOM   1749 C  CG2 B ILE A 1 218 ? 1.105   -15.539 11.821  0.42 16.05  ? 441  ILE A CG2 1 
ATOM   1750 C  CD1 A ILE A 1 218 ? 0.588   -13.415 14.472  0.58 21.11  ? 441  ILE A CD1 1 
ATOM   1751 C  CD1 B ILE A 1 218 ? 1.386   -16.498 14.524  0.42 15.40  ? 441  ILE A CD1 1 
ATOM   1752 N  N   . PRO A 1 219 ? -1.097  -13.955 9.901   1.00 10.81  ? 442  PRO A N   1 
ATOM   1753 C  CA  . PRO A 1 219 ? -1.375  -14.313 8.498   1.00 11.27  ? 442  PRO A CA  1 
ATOM   1754 C  C   . PRO A 1 219 ? -0.673  -15.598 8.070   1.00 10.69  ? 442  PRO A C   1 
ATOM   1755 O  O   . PRO A 1 219 ? 0.306   -16.029 8.675   1.00 11.93  ? 442  PRO A O   1 
ATOM   1756 C  CB  . PRO A 1 219 ? -0.789  -13.130 7.715   1.00 14.16  ? 442  PRO A CB  1 
ATOM   1757 C  CG  . PRO A 1 219 ? -0.682  -12.018 8.679   1.00 14.70  ? 442  PRO A CG  1 
ATOM   1758 C  CD  . PRO A 1 219 ? -0.396  -12.660 10.010  1.00 12.14  ? 442  PRO A CD  1 
ATOM   1759 N  N   . MET A 1 220 ? -1.178  -16.202 6.985   1.00 11.50  ? 443  MET A N   1 
ATOM   1760 C  CA  . MET A 1 220 ? -0.528  -17.363 6.387   1.00 11.55  ? 443  MET A CA  1 
ATOM   1761 C  C   . MET A 1 220 ? -0.342  -17.193 4.881   1.00 10.24  ? 443  MET A C   1 
ATOM   1762 O  O   . MET A 1 220 ? -1.150  -16.549 4.200   1.00 11.28  ? 443  MET A O   1 
ATOM   1763 C  CB  . MET A 1 220 ? -1.286  -18.675 6.657   1.00 11.86  ? 443  MET A CB  1 
ATOM   1764 C  CG  . MET A 1 220 ? -1.460  -18.960 8.137   1.00 12.62  ? 443  MET A CG  1 
ATOM   1765 S  SD  . MET A 1 220 ? -1.368  -20.726 8.536   1.00 13.04  ? 443  MET A SD  1 
ATOM   1766 C  CE  . MET A 1 220 ? -2.865  -21.337 7.741   1.00 14.74  ? 443  MET A CE  1 
ATOM   1767 N  N   . LYS A 1 221 ? 0.735   -17.803 4.372   1.00 9.79   ? 444  LYS A N   1 
ATOM   1768 C  CA  . LYS A 1 221 ? 0.996   -17.827 2.933   1.00 10.98  ? 444  LYS A CA  1 
ATOM   1769 C  C   . LYS A 1 221 ? -0.051  -18.646 2.189   1.00 11.70  ? 444  LYS A C   1 
ATOM   1770 O  O   . LYS A 1 221 ? -0.427  -18.293 1.064   1.00 12.37  ? 444  LYS A O   1 
ATOM   1771 C  CB  . LYS A 1 221 ? 2.405   -18.380 2.678   1.00 11.28  ? 444  LYS A CB  1 
ATOM   1772 C  CG  . LYS A 1 221 ? 2.768   -18.683 1.223   1.00 12.27  ? 444  LYS A CG  1 
ATOM   1773 C  CD  . LYS A 1 221 ? 2.679   -17.457 0.312   1.00 13.11  ? 444  LYS A CD  1 
ATOM   1774 C  CE  . LYS A 1 221 ? 3.139   -17.793 -1.102  1.00 14.37  ? 444  LYS A CE  1 
ATOM   1775 N  NZ  . LYS A 1 221 ? 2.984   -16.619 -1.998  1.00 15.82  ? 444  LYS A NZ  1 
ATOM   1776 N  N   . GLY A 1 222 ? -0.526  -19.730 2.797   1.00 12.13  ? 445  GLY A N   1 
ATOM   1777 C  CA  . GLY A 1 222 ? -1.507  -20.599 2.179   1.00 11.87  ? 445  GLY A CA  1 
ATOM   1778 C  C   . GLY A 1 222 ? -2.063  -21.563 3.202   1.00 13.03  ? 445  GLY A C   1 
ATOM   1779 O  O   . GLY A 1 222 ? -1.821  -21.437 4.404   1.00 13.47  ? 445  GLY A O   1 
ATOM   1780 N  N   . GLY A 1 223 ? -2.799  -22.549 2.710   1.00 12.98  ? 446  GLY A N   1 
ATOM   1781 C  CA  . GLY A 1 223 ? -3.347  -23.557 3.596   1.00 11.84  ? 446  GLY A CA  1 
ATOM   1782 C  C   . GLY A 1 223 ? -4.552  -23.056 4.380   1.00 11.47  ? 446  GLY A C   1 
ATOM   1783 O  O   . GLY A 1 223 ? -5.078  -21.945 4.182   1.00 12.02  ? 446  GLY A O   1 
ATOM   1784 N  N   . TYR A 1 224 ? -4.980  -23.908 5.303   1.00 13.17  ? 447  TYR A N   1 
ATOM   1785 C  CA  . TYR A 1 224 ? -6.196  -23.694 6.069   1.00 12.38  ? 447  TYR A CA  1 
ATOM   1786 C  C   . TYR A 1 224 ? -5.855  -23.477 7.532   1.00 13.48  ? 447  TYR A C   1 
ATOM   1787 O  O   . TYR A 1 224 ? -4.995  -24.172 8.088   1.00 15.75  ? 447  TYR A O   1 
ATOM   1788 C  CB  . TYR A 1 224 ? -7.112  -24.907 5.963   1.00 12.44  ? 447  TYR A CB  1 
ATOM   1789 C  CG  . TYR A 1 224 ? -7.554  -25.275 4.573   1.00 10.81  ? 447  TYR A CG  1 
ATOM   1790 C  CD1 . TYR A 1 224 ? -6.793  -26.129 3.794   1.00 11.88  ? 447  TYR A CD1 1 
ATOM   1791 C  CD2 . TYR A 1 224 ? -8.753  -24.797 4.050   1.00 11.87  ? 447  TYR A CD2 1 
ATOM   1792 C  CE1 . TYR A 1 224 ? -7.209  -26.504 2.531   1.00 12.37  ? 447  TYR A CE1 1 
ATOM   1793 C  CE2 . TYR A 1 224 ? -9.186  -25.171 2.796   1.00 12.45  ? 447  TYR A CE2 1 
ATOM   1794 C  CZ  . TYR A 1 224 ? -8.408  -26.028 2.041   1.00 11.88  ? 447  TYR A CZ  1 
ATOM   1795 O  OH  . TYR A 1 224 ? -8.863  -26.393 0.789   1.00 12.70  ? 447  TYR A OH  1 
ATOM   1796 N  N   . GLY A 1 225 ? -6.549  -22.531 8.159   1.00 13.30  ? 448  GLY A N   1 
ATOM   1797 C  CA  . GLY A 1 225 ? -6.379  -22.316 9.583   1.00 14.46  ? 448  GLY A CA  1 
ATOM   1798 C  C   . GLY A 1 225 ? -6.415  -20.861 9.991   1.00 13.92  ? 448  GLY A C   1 
ATOM   1799 O  O   . GLY A 1 225 ? -6.315  -19.966 9.146   1.00 14.29  ? 448  GLY A O   1 
ATOM   1800 N  N   . SER A 1 226 ? -6.554  -20.625 11.296  1.00 14.20  ? 449  SER A N   1 
ATOM   1801 C  CA  . SER A 1 226 ? -6.507  -19.292 11.892  1.00 13.71  ? 449  SER A CA  1 
ATOM   1802 C  C   . SER A 1 226 ? -5.510  -19.324 13.043  1.00 13.60  ? 449  SER A C   1 
ATOM   1803 O  O   . SER A 1 226 ? -5.897  -19.266 14.220  1.00 14.51  ? 449  SER A O   1 
ATOM   1804 C  CB  . SER A 1 226 ? -7.883  -18.884 12.413  1.00 15.09  ? 449  SER A CB  1 
ATOM   1805 O  OG  . SER A 1 226 ? -8.802  -18.749 11.347  1.00 17.20  ? 449  SER A OG  1 
ATOM   1806 N  N   . PRO A 1 227 ? -4.214  -19.426 12.740  1.00 12.36  ? 450  PRO A N   1 
ATOM   1807 C  CA  . PRO A 1 227 ? -3.212  -19.509 13.808  1.00 12.91  ? 450  PRO A CA  1 
ATOM   1808 C  C   . PRO A 1 227 ? -3.150  -18.224 14.616  1.00 13.11  ? 450  PRO A C   1 
ATOM   1809 O  O   . PRO A 1 227 ? -3.346  -17.121 14.096  1.00 13.43  ? 450  PRO A O   1 
ATOM   1810 C  CB  . PRO A 1 227 ? -1.901  -19.714 13.040  1.00 13.65  ? 450  PRO A CB  1 
ATOM   1811 C  CG  . PRO A 1 227 ? -2.161  -19.058 11.703  1.00 13.62  ? 450  PRO A CG  1 
ATOM   1812 C  CD  . PRO A 1 227 ? -3.588  -19.431 11.404  1.00 12.82  ? 450  PRO A CD  1 
ATOM   1813 N  N   . TYR A 1 228 ? -2.866  -18.378 15.903  1.00 11.84  ? 451  TYR A N   1 
ATOM   1814 C  CA  . TYR A 1 228 ? -2.662  -17.248 16.797  1.00 12.58  ? 451  TYR A CA  1 
ATOM   1815 C  C   . TYR A 1 228 ? -1.404  -17.464 17.629  1.00 12.12  ? 451  TYR A C   1 
ATOM   1816 O  O   . TYR A 1 228 ? -0.881  -18.581 17.741  1.00 12.68  ? 451  TYR A O   1 
ATOM   1817 C  CB  . TYR A 1 228 ? -3.870  -17.034 17.717  1.00 14.22  ? 451  TYR A CB  1 
ATOM   1818 C  CG  . TYR A 1 228 ? -4.273  -18.268 18.482  1.00 14.62  ? 451  TYR A CG  1 
ATOM   1819 C  CD1 . TYR A 1 228 ? -3.597  -18.645 19.633  1.00 15.58  ? 451  TYR A CD1 1 
ATOM   1820 C  CD2 . TYR A 1 228 ? -5.333  -19.070 18.058  1.00 16.44  ? 451  TYR A CD2 1 
ATOM   1821 C  CE1 . TYR A 1 228 ? -3.959  -19.768 20.339  1.00 18.84  ? 451  TYR A CE1 1 
ATOM   1822 C  CE2 . TYR A 1 228 ? -5.701  -20.204 18.768  1.00 18.84  ? 451  TYR A CE2 1 
ATOM   1823 C  CZ  . TYR A 1 228 ? -5.008  -20.547 19.908  1.00 20.17  ? 451  TYR A CZ  1 
ATOM   1824 O  OH  . TYR A 1 228 ? -5.373  -21.665 20.622  1.00 22.83  ? 451  TYR A OH  1 
ATOM   1825 N  N   . ILE A 1 229 ? -0.919  -16.376 18.212  1.00 12.56  ? 452  ILE A N   1 
ATOM   1826 C  CA  . ILE A 1 229 ? 0.224   -16.420 19.110  1.00 11.86  ? 452  ILE A CA  1 
ATOM   1827 C  C   . ILE A 1 229 ? -0.105  -15.601 20.354  1.00 11.68  ? 452  ILE A C   1 
ATOM   1828 O  O   . ILE A 1 229 ? -0.687  -14.511 20.262  1.00 12.10  ? 452  ILE A O   1 
ATOM   1829 C  CB  . ILE A 1 229 ? 1.527   -15.966 18.407  1.00 11.24  ? 452  ILE A CB  1 
ATOM   1830 C  CG1 . ILE A 1 229 ? 2.761   -16.307 19.259  1.00 10.79  ? 452  ILE A CG1 1 
ATOM   1831 C  CG2 . ILE A 1 229 ? 1.474   -14.488 18.029  1.00 13.47  ? 452  ILE A CG2 1 
ATOM   1832 C  CD1 . ILE A 1 229 ? 4.067   -16.265 18.484  1.00 12.83  ? 452  ILE A CD1 1 
ATOM   1833 N  N   . ASP A 1 230 ? 0.235   -16.159 21.518  1.00 11.52  ? 453  ASP A N   1 
ATOM   1834 C  CA  . ASP A 1 230 ? -0.064  -15.593 22.825  1.00 11.88  ? 453  ASP A CA  1 
ATOM   1835 C  C   . ASP A 1 230 ? 1.210   -15.052 23.464  1.00 12.41  ? 453  ASP A C   1 
ATOM   1836 O  O   . ASP A 1 230 ? 2.200   -15.778 23.600  1.00 13.67  ? 453  ASP A O   1 
ATOM   1837 C  CB  . ASP A 1 230 ? -0.622  -16.695 23.731  1.00 12.14  ? 453  ASP A CB  1 
ATOM   1838 C  CG  . ASP A 1 230 ? -2.033  -17.097 23.353  1.00 14.53  ? 453  ASP A CG  1 
ATOM   1839 O  OD1 . ASP A 1 230 ? -2.848  -16.192 23.047  1.00 15.38  ? 453  ASP A OD1 1 
ATOM   1840 O  OD2 . ASP A 1 230 ? -2.328  -18.314 23.377  1.00 15.43  ? 453  ASP A OD2 1 
ATOM   1841 N  N   . CYS A 1 231 ? 1.174   -13.805 23.914  1.00 11.81  ? 454  CYS A N   1 
ATOM   1842 C  CA  . CYS A 1 231 ? 2.313   -13.246 24.624  1.00 11.82  ? 454  CYS A CA  1 
ATOM   1843 C  C   . CYS A 1 231 ? 1.930   -12.953 26.071  1.00 11.75  ? 454  CYS A C   1 
ATOM   1844 O  O   . CYS A 1 231 ? 0.751   -12.828 26.415  1.00 12.94  ? 454  CYS A O   1 
ATOM   1845 C  CB  . CYS A 1 231 ? 2.901   -12.010 23.903  1.00 12.49  ? 454  CYS A CB  1 
ATOM   1846 S  SG  . CYS A 1 231 ? 1.912   -10.519 23.984  1.00 12.60  ? 454  CYS A SG  1 
ATOM   1847 N  N   . LEU A 1 232 ? 2.951   -12.877 26.928  1.00 12.21  ? 455  LEU A N   1 
ATOM   1848 C  CA  . LEU A 1 232 ? 2.714   -12.729 28.360  1.00 13.31  ? 455  LEU A CA  1 
ATOM   1849 C  C   . LEU A 1 232 ? 2.383   -11.288 28.738  1.00 13.23  ? 455  LEU A C   1 
ATOM   1850 O  O   . LEU A 1 232 ? 1.531   -11.059 29.606  1.00 13.74  ? 455  LEU A O   1 
ATOM   1851 C  CB  . LEU A 1 232 ? 3.923   -13.228 29.154  1.00 13.36  ? 455  LEU A CB  1 
ATOM   1852 C  CG  . LEU A 1 232 ? 4.311   -14.694 28.946  1.00 13.97  ? 455  LEU A CG  1 
ATOM   1853 C  CD1 . LEU A 1 232 ? 5.519   -15.052 29.804  1.00 13.43  ? 455  LEU A CD1 1 
ATOM   1854 C  CD2 . LEU A 1 232 ? 3.115   -15.622 29.229  1.00 15.15  ? 455  LEU A CD2 1 
ATOM   1855 N  N   . ILE A 1 233 ? 3.062   -10.314 28.131  1.00 12.76  ? 456  ILE A N   1 
ATOM   1856 C  CA  . ILE A 1 233 ? 2.787   -8.888  28.338  1.00 12.72  ? 456  ILE A CA  1 
ATOM   1857 C  C   . ILE A 1 233 ? 3.067   -8.177  27.018  1.00 12.31  ? 456  ILE A C   1 
ATOM   1858 O  O   . ILE A 1 233 ? 3.900   -8.656  26.231  1.00 13.13  ? 456  ILE A O   1 
ATOM   1859 C  CB  . ILE A 1 233 ? 3.613   -8.279  29.493  1.00 14.06  ? 456  ILE A CB  1 
ATOM   1860 C  CG1 . ILE A 1 233 ? 5.105   -8.575  29.325  1.00 14.33  ? 456  ILE A CG1 1 
ATOM   1861 C  CG2 . ILE A 1 233 ? 3.087   -8.712  30.859  1.00 14.69  ? 456  ILE A CG2 1 
ATOM   1862 C  CD1 . ILE A 1 233 ? 6.000   -7.923  30.385  1.00 15.64  ? 456  ILE A CD1 1 
ATOM   1863 N  N   . PRO A 1 234 ? 2.396   -7.061  26.730  1.00 13.21  ? 457  PRO A N   1 
ATOM   1864 C  CA  . PRO A 1 234 ? 2.594   -6.369  25.446  1.00 13.55  ? 457  PRO A CA  1 
ATOM   1865 C  C   . PRO A 1 234 ? 3.989   -5.778  25.326  1.00 12.60  ? 457  PRO A C   1 
ATOM   1866 O  O   . PRO A 1 234 ? 4.645   -5.465  26.321  1.00 12.99  ? 457  PRO A O   1 
ATOM   1867 C  CB  . PRO A 1 234 ? 1.550   -5.242  25.494  1.00 15.78  ? 457  PRO A CB  1 
ATOM   1868 C  CG  . PRO A 1 234 ? 0.516   -5.708  26.484  1.00 17.09  ? 457  PRO A CG  1 
ATOM   1869 C  CD  . PRO A 1 234 ? 1.297   -6.461  27.512  1.00 15.52  ? 457  PRO A CD  1 
ATOM   1870 N  N   . GLN A 1 235 ? 4.419   -5.575  24.074  1.00 11.87  ? 458  GLN A N   1 
ATOM   1871 C  CA  . GLN A 1 235 ? 5.736   -4.981  23.839  1.00 12.45  ? 458  GLN A CA  1 
ATOM   1872 C  C   . GLN A 1 235 ? 5.846   -3.595  24.471  1.00 13.05  ? 458  GLN A C   1 
ATOM   1873 O  O   . GLN A 1 235 ? 6.909   -3.222  24.992  1.00 13.55  ? 458  GLN A O   1 
ATOM   1874 C  CB  . GLN A 1 235 ? 6.055   -4.939  22.343  1.00 12.22  ? 458  GLN A CB  1 
ATOM   1875 C  CG  . GLN A 1 235 ? 7.461   -4.452  22.031  1.00 11.90  ? 458  GLN A CG  1 
ATOM   1876 C  CD  . GLN A 1 235 ? 8.550   -5.449  22.405  1.00 13.85  ? 458  GLN A CD  1 
ATOM   1877 O  OE1 . GLN A 1 235 ? 8.286   -6.632  22.661  1.00 13.05  ? 458  GLN A OE1 1 
ATOM   1878 N  NE2 . GLN A 1 235 ? 9.788   -4.976  22.418  1.00 16.83  ? 458  GLN A NE2 1 
ATOM   1879 N  N   . GLU A 1 236 ? 4.751   -2.830  24.467  1.00 13.12  ? 459  GLU A N   1 
ATOM   1880 C  CA  . GLU A 1 236 ? 4.785   -1.480  25.027  1.00 14.07  ? 459  GLU A CA  1 
ATOM   1881 C  C   . GLU A 1 236 ? 4.914   -1.510  26.544  1.00 14.07  ? 459  GLU A C   1 
ATOM   1882 O  O   . GLU A 1 236 ? 5.486   -0.584  27.130  1.00 16.78  ? 459  GLU A O   1 
ATOM   1883 C  CB  . GLU A 1 236 ? 3.554   -0.680  24.586  1.00 15.19  ? 459  GLU A CB  1 
ATOM   1884 C  CG  . GLU A 1 236 ? 3.555   -0.290  23.106  1.00 15.30  ? 459  GLU A CG  1 
ATOM   1885 C  CD  . GLU A 1 236 ? 3.135   -1.425  22.174  1.00 15.84  ? 459  GLU A CD  1 
ATOM   1886 O  OE1 . GLU A 1 236 ? 2.705   -2.491  22.677  1.00 15.08  ? 459  GLU A OE1 1 
ATOM   1887 O  OE2 . GLU A 1 236 ? 3.231   -1.251  20.940  1.00 17.88  ? 459  GLU A OE2 1 
ATOM   1888 N  N   . TRP A 1 237 ? 4.405   -2.559  27.204  1.00 14.51  ? 460  TRP A N   1 
ATOM   1889 C  CA  . TRP A 1 237 ? 4.655   -2.683  28.638  1.00 14.52  ? 460  TRP A CA  1 
ATOM   1890 C  C   . TRP A 1 237 ? 6.124   -2.982  28.900  1.00 14.17  ? 460  TRP A C   1 
ATOM   1891 O  O   . TRP A 1 237 ? 6.705   -2.466  29.862  1.00 14.99  ? 460  TRP A O   1 
ATOM   1892 C  CB  . TRP A 1 237 ? 3.820   -3.810  29.243  1.00 14.70  ? 460  TRP A CB  1 
ATOM   1893 C  CG  . TRP A 1 237 ? 2.343   -3.574  29.377  1.00 14.95  ? 460  TRP A CG  1 
ATOM   1894 C  CD1 . TRP A 1 237 ? 1.560   -2.690  28.677  1.00 14.91  ? 460  TRP A CD1 1 
ATOM   1895 C  CD2 . TRP A 1 237 ? 1.467   -4.258  30.278  1.00 15.10  ? 460  TRP A CD2 1 
ATOM   1896 N  NE1 . TRP A 1 237 ? 0.253   -2.799  29.091  1.00 15.67  ? 460  TRP A NE1 1 
ATOM   1897 C  CE2 . TRP A 1 237 ? 0.172   -3.751  30.074  1.00 15.55  ? 460  TRP A CE2 1 
ATOM   1898 C  CE3 . TRP A 1 237 ? 1.659   -5.256  31.241  1.00 14.75  ? 460  TRP A CE3 1 
ATOM   1899 C  CZ2 . TRP A 1 237 ? -0.928  -4.211  30.790  1.00 16.07  ? 460  TRP A CZ2 1 
ATOM   1900 C  CZ3 . TRP A 1 237 ? 0.575   -5.707  31.954  1.00 15.04  ? 460  TRP A CZ3 1 
ATOM   1901 C  CH2 . TRP A 1 237 ? -0.710  -5.181  31.728  1.00 16.22  ? 460  TRP A CH2 1 
ATOM   1902 N  N   . ILE A 1 238 ? 6.731   -3.827  28.064  1.00 13.71  ? 461  ILE A N   1 
ATOM   1903 C  CA  . ILE A 1 238 ? 8.155   -4.134  28.197  1.00 14.15  ? 461  ILE A CA  1 
ATOM   1904 C  C   . ILE A 1 238 ? 8.995   -2.870  28.048  1.00 15.49  ? 461  ILE A C   1 
ATOM   1905 O  O   . ILE A 1 238 ? 9.894   -2.600  28.856  1.00 15.74  ? 461  ILE A O   1 
ATOM   1906 C  CB  . ILE A 1 238 ? 8.555   -5.214  27.175  1.00 13.50  ? 461  ILE A CB  1 
ATOM   1907 C  CG1 . ILE A 1 238 ? 7.822   -6.513  27.489  1.00 13.12  ? 461  ILE A CG1 1 
ATOM   1908 C  CG2 . ILE A 1 238 ? 10.063  -5.380  27.116  1.00 13.69  ? 461  ILE A CG2 1 
ATOM   1909 C  CD1 . ILE A 1 238 ? 8.109   -7.642  26.527  1.00 14.49  ? 461  ILE A CD1 1 
ATOM   1910 N  N   A SER A 1 239 ? 8.716   -2.077  27.008  0.18 16.15  ? 462  SER A N   1 
ATOM   1911 N  N   B SER A 1 239 ? 8.717   -2.076  27.013  0.82 16.04  ? 462  SER A N   1 
ATOM   1912 C  CA  A SER A 1 239 ? 9.426   -0.815  26.823  0.18 16.93  ? 462  SER A CA  1 
ATOM   1913 C  CA  B SER A 1 239 ? 9.456   -0.832  26.841  0.82 17.03  ? 462  SER A CA  1 
ATOM   1914 C  C   A SER A 1 239 ? 9.290   0.074   28.050  0.18 17.93  ? 462  SER A C   1 
ATOM   1915 C  C   B SER A 1 239 ? 9.300   0.067   28.060  0.82 18.80  ? 462  SER A C   1 
ATOM   1916 O  O   A SER A 1 239 ? 10.255  0.722   28.471  0.18 18.26  ? 462  SER A O   1 
ATOM   1917 O  O   B SER A 1 239 ? 10.268  0.697   28.498  0.82 19.87  ? 462  SER A O   1 
ATOM   1918 C  CB  A SER A 1 239 ? 8.881   -0.091  25.593  0.18 17.41  ? 462  SER A CB  1 
ATOM   1919 C  CB  B SER A 1 239 ? 9.003   -0.117  25.564  0.82 19.76  ? 462  SER A CB  1 
ATOM   1920 O  OG  A SER A 1 239 ? 9.135   -0.824  24.413  0.18 18.15  ? 462  SER A OG  1 
ATOM   1921 O  OG  B SER A 1 239 ? 9.882   0.955   25.240  0.82 23.13  ? 462  SER A OG  1 
ATOM   1922 N  N   . HIS A 1 240 ? 8.097   0.107   28.641  1.00 18.37  ? 463  HIS A N   1 
ATOM   1923 C  CA  . HIS A 1 240 ? 7.856   0.937   29.814  1.00 19.90  ? 463  HIS A CA  1 
ATOM   1924 C  C   . HIS A 1 240 ? 8.623   0.424   31.032  1.00 19.59  ? 463  HIS A C   1 
ATOM   1925 O  O   . HIS A 1 240 ? 9.292   1.201   31.729  1.00 20.16  ? 463  HIS A O   1 
ATOM   1926 C  CB  . HIS A 1 240 ? 6.355   0.962   30.090  1.00 20.92  ? 463  HIS A CB  1 
ATOM   1927 C  CG  . HIS A 1 240 ? 5.971   1.800   31.264  1.00 24.37  ? 463  HIS A CG  1 
ATOM   1928 N  ND1 . HIS A 1 240 ? 6.216   3.155   31.319  1.00 27.64  ? 463  HIS A ND1 1 
ATOM   1929 C  CD2 . HIS A 1 240 ? 5.367   1.477   32.431  1.00 26.09  ? 463  HIS A CD2 1 
ATOM   1930 C  CE1 . HIS A 1 240 ? 5.769   3.632   32.465  1.00 27.62  ? 463  HIS A CE1 1 
ATOM   1931 N  NE2 . HIS A 1 240 ? 5.257   2.634   33.162  1.00 27.99  ? 463  HIS A NE2 1 
ATOM   1932 N  N   . PHE A 1 241 ? 8.528   -0.875  31.323  1.00 18.98  ? 464  PHE A N   1 
ATOM   1933 C  CA  . PHE A 1 241 ? 9.211   -1.392  32.505  1.00 18.04  ? 464  PHE A CA  1 
ATOM   1934 C  C   . PHE A 1 241 ? 10.719  -1.251  32.359  1.00 17.78  ? 464  PHE A C   1 
ATOM   1935 O  O   . PHE A 1 241 ? 11.419  -0.916  33.325  1.00 18.28  ? 464  PHE A O   1 
ATOM   1936 C  CB  . PHE A 1 241 ? 8.854   -2.864  32.746  1.00 17.77  ? 464  PHE A CB  1 
ATOM   1937 C  CG  . PHE A 1 241 ? 7.384   -3.133  32.925  1.00 17.70  ? 464  PHE A CG  1 
ATOM   1938 C  CD1 . PHE A 1 241 ? 6.518   -2.149  33.386  1.00 18.94  ? 464  PHE A CD1 1 
ATOM   1939 C  CD2 . PHE A 1 241 ? 6.865   -4.386  32.619  1.00 16.88  ? 464  PHE A CD2 1 
ATOM   1940 C  CE1 . PHE A 1 241 ? 5.161   -2.419  33.549  1.00 19.60  ? 464  PHE A CE1 1 
ATOM   1941 C  CE2 . PHE A 1 241 ? 5.513   -4.660  32.770  1.00 17.12  ? 464  PHE A CE2 1 
ATOM   1942 C  CZ  . PHE A 1 241 ? 4.659   -3.678  33.236  1.00 18.03  ? 464  PHE A CZ  1 
ATOM   1943 N  N   . TYR A 1 242 ? 11.239  -1.495  31.155  1.00 17.81  ? 465  TYR A N   1 
ATOM   1944 C  CA  . TYR A 1 242 ? 12.670  -1.357  30.913  1.00 18.66  ? 465  TYR A CA  1 
ATOM   1945 C  C   . TYR A 1 242 ? 13.145  0.067   31.180  1.00 20.57  ? 465  TYR A C   1 
ATOM   1946 O  O   . TYR A 1 242 ? 14.200  0.278   31.799  1.00 21.67  ? 465  TYR A O   1 
ATOM   1947 C  CB  . TYR A 1 242 ? 12.982  -1.768  29.472  1.00 18.23  ? 465  TYR A CB  1 
ATOM   1948 C  CG  . TYR A 1 242 ? 14.415  -1.516  29.090  1.00 19.36  ? 465  TYR A CG  1 
ATOM   1949 C  CD1 . TYR A 1 242 ? 15.410  -2.424  29.416  1.00 20.96  ? 465  TYR A CD1 1 
ATOM   1950 C  CD2 . TYR A 1 242 ? 14.781  -0.357  28.416  1.00 20.64  ? 465  TYR A CD2 1 
ATOM   1951 C  CE1 . TYR A 1 242 ? 16.731  -2.188  29.077  1.00 22.29  ? 465  TYR A CE1 1 
ATOM   1952 C  CE2 . TYR A 1 242 ? 16.097  -0.106  28.092  1.00 21.67  ? 465  TYR A CE2 1 
ATOM   1953 C  CZ  . TYR A 1 242 ? 17.064  -1.028  28.411  1.00 22.98  ? 465  TYR A CZ  1 
ATOM   1954 O  OH  . TYR A 1 242 ? 18.372  -0.774  28.068  1.00 25.87  ? 465  TYR A OH  1 
ATOM   1955 N  N   . GLN A 1 243 ? 12.378  1.059   30.728  1.00 21.46  ? 466  GLN A N   1 
ATOM   1956 C  CA  . GLN A 1 243 ? 12.792  2.446   30.923  1.00 23.91  ? 466  GLN A CA  1 
ATOM   1957 C  C   . GLN A 1 243 ? 12.646  2.885   32.376  1.00 24.73  ? 466  GLN A C   1 
ATOM   1958 O  O   . GLN A 1 243 ? 13.494  3.622   32.889  1.00 25.91  ? 466  GLN A O   1 
ATOM   1959 C  CB  . GLN A 1 243 ? 11.995  3.363   30.003  1.00 26.57  ? 466  GLN A CB  1 
ATOM   1960 C  CG  . GLN A 1 243 ? 12.333  3.208   28.542  1.00 28.97  ? 466  GLN A CG  1 
ATOM   1961 C  CD  . GLN A 1 243 ? 11.484  4.110   27.680  1.00 31.62  ? 466  GLN A CD  1 
ATOM   1962 O  OE1 . GLN A 1 243 ? 11.561  5.332   27.786  1.00 34.67  ? 466  GLN A OE1 1 
ATOM   1963 N  NE2 . GLN A 1 243 ? 10.652  3.515   26.837  1.00 32.71  ? 466  GLN A NE2 1 
ATOM   1964 N  N   . GLU A 1 244 ? 11.574  2.466   33.048  1.00 23.95  ? 467  GLU A N   1 
ATOM   1965 C  CA  . GLU A 1 244 ? 11.327  2.935   34.411  1.00 26.91  ? 467  GLU A CA  1 
ATOM   1966 C  C   . GLU A 1 244 ? 12.287  2.304   35.414  1.00 27.17  ? 467  GLU A C   1 
ATOM   1967 O  O   . GLU A 1 244 ? 12.777  2.989   36.326  1.00 27.81  ? 467  GLU A O   1 
ATOM   1968 C  CB  . GLU A 1 244 ? 9.875   2.657   34.797  1.00 30.05  ? 467  GLU A CB  1 
ATOM   1969 C  CG  . GLU A 1 244 ? 8.871   3.483   34.017  1.00 33.70  ? 467  GLU A CG  1 
ATOM   1970 C  CD  . GLU A 1 244 ? 9.001   4.968   34.295  1.00 37.42  ? 467  GLU A CD  1 
ATOM   1971 O  OE1 . GLU A 1 244 ? 9.025   5.353   35.482  1.00 38.73  ? 467  GLU A OE1 1 
ATOM   1972 O  OE2 . GLU A 1 244 ? 9.086   5.751   33.326  1.00 39.52  ? 467  GLU A OE2 1 
ATOM   1973 N  N   . SER A 1 245 ? 12.553  1.004   35.282  1.00 28.96  ? 468  SER A N   1 
ATOM   1974 C  CA  . SER A 1 245 ? 13.381  0.275   36.249  1.00 32.63  ? 468  SER A CA  1 
ATOM   1975 C  C   . SER A 1 245 ? 12.891  0.495   37.680  1.00 33.93  ? 468  SER A C   1 
ATOM   1976 O  O   . SER A 1 245 ? 13.677  0.711   38.607  1.00 35.17  ? 468  SER A O   1 
ATOM   1977 C  CB  . SER A 1 245 ? 14.860  0.637   36.114  1.00 35.85  ? 468  SER A CB  1 
ATOM   1978 O  OG  . SER A 1 245 ? 15.400  0.154   34.905  1.00 37.60  ? 468  SER A OG  1 
ATOM   1979 N  N   . ALA A 1 246 ? 11.577  0.487   37.853  1.00 35.04  ? 469  ALA A N   1 
ATOM   1980 C  CA  . ALA A 1 246 ? 11.007  0.720   39.176  1.00 35.22  ? 469  ALA A CA  1 
ATOM   1981 C  C   . ALA A 1 246 ? 11.104  -0.555  40.002  1.00 34.29  ? 469  ALA A C   1 
ATOM   1982 O  O   . ALA A 1 246 ? 10.682  -1.618  39.538  1.00 32.70  ? 469  ALA A O   1 
ATOM   1983 C  CB  . ALA A 1 246 ? 9.543   1.131   39.057  1.00 36.57  ? 469  ALA A CB  1 
ATOM   1984 N  N   . PRO A 1 247 ? 11.646  -0.489  41.215  1.00 36.23  ? 470  PRO A N   1 
ATOM   1985 C  CA  . PRO A 1 247 ? 11.736  -1.689  42.055  1.00 36.27  ? 470  PRO A CA  1 
ATOM   1986 C  C   . PRO A 1 247 ? 10.350  -2.228  42.370  1.00 34.60  ? 470  PRO A C   1 
ATOM   1987 O  O   . PRO A 1 247 ? 9.437   -1.480  42.725  1.00 36.72  ? 470  PRO A O   1 
ATOM   1988 C  CB  . PRO A 1 247 ? 12.442  -1.187  43.323  1.00 37.64  ? 470  PRO A CB  1 
ATOM   1989 C  CG  . PRO A 1 247 ? 13.044  0.130   42.958  1.00 38.22  ? 470  PRO A CG  1 
ATOM   1990 C  CD  . PRO A 1 247 ? 12.181  0.708   41.883  1.00 37.26  ? 470  PRO A CD  1 
ATOM   1991 N  N   . SER A 1 248 ? 10.194  -3.536  42.210  1.00 30.53  ? 471  SER A N   1 
ATOM   1992 C  CA  . SER A 1 248 ? 8.957   -4.212  42.570  1.00 29.50  ? 471  SER A CA  1 
ATOM   1993 C  C   . SER A 1 248 ? 8.899   -4.326  44.086  1.00 28.45  ? 471  SER A C   1 
ATOM   1994 O  O   . SER A 1 248 ? 9.811   -4.882  44.705  1.00 28.71  ? 471  SER A O   1 
ATOM   1995 C  CB  . SER A 1 248 ? 8.934   -5.598  41.928  1.00 30.18  ? 471  SER A CB  1 
ATOM   1996 O  OG  . SER A 1 248 ? 9.238   -5.498  40.547  1.00 32.28  ? 471  SER A OG  1 
ATOM   1997 N  N   . GLN A 1 249 ? 7.842   -3.784  44.689  0.96 27.02  ? 472  GLN A N   1 
ATOM   1998 C  CA  . GLN A 1 249 ? 7.785   -3.750  46.148  0.96 27.12  ? 472  GLN A CA  1 
ATOM   1999 C  C   . GLN A 1 249 ? 7.451   -5.116  46.735  0.96 24.78  ? 472  GLN A C   1 
ATOM   2000 O  O   . GLN A 1 249 ? 7.915   -5.449  47.835  0.96 26.11  ? 472  GLN A O   1 
ATOM   2001 C  CB  . GLN A 1 249 ? 6.810   -2.673  46.616  0.96 31.19  ? 472  GLN A CB  1 
ATOM   2002 C  CG  . GLN A 1 249 ? 7.331   -1.271  46.365  0.96 36.45  ? 472  GLN A CG  1 
ATOM   2003 C  CD  . GLN A 1 249 ? 6.499   -0.206  47.042  0.96 40.75  ? 472  GLN A CD  1 
ATOM   2004 O  OE1 . GLN A 1 249 ? 5.698   -0.494  47.931  0.96 41.58  ? 472  GLN A OE1 1 
ATOM   2005 N  NE2 . GLN A 1 249 ? 6.683   1.039   46.619  0.96 42.44  ? 472  GLN A NE2 1 
ATOM   2006 N  N   . THR A 1 250 ? 6.634   -5.899  46.033  1.00 23.55  ? 473  THR A N   1 
ATOM   2007 C  CA  . THR A 1 250 ? 6.371   -7.298  46.340  1.00 23.37  ? 473  THR A CA  1 
ATOM   2008 C  C   . THR A 1 250 ? 6.469   -8.098  45.045  1.00 23.44  ? 473  THR A C   1 
ATOM   2009 O  O   . THR A 1 250 ? 6.792   -7.564  43.978  1.00 23.96  ? 473  THR A O   1 
ATOM   2010 C  CB  . THR A 1 250 ? 4.986   -7.498  46.974  1.00 24.31  ? 473  THR A CB  1 
ATOM   2011 O  OG1 . THR A 1 250 ? 3.978   -7.291  45.976  1.00 24.45  ? 473  THR A OG1 1 
ATOM   2012 C  CG2 . THR A 1 250 ? 4.752   -6.531  48.137  1.00 25.38  ? 473  THR A CG2 1 
ATOM   2013 N  N   . ASP A 1 251 ? 6.174   -9.392  45.134  1.00 23.29  ? 474  ASP A N   1 
ATOM   2014 C  CA  . ASP A 1 251 ? 6.237   -10.248 43.954  1.00 22.72  ? 474  ASP A CA  1 
ATOM   2015 C  C   . ASP A 1 251 ? 4.980   -10.193 43.086  1.00 21.45  ? 474  ASP A C   1 
ATOM   2016 O  O   . ASP A 1 251 ? 4.967   -10.819 42.023  1.00 21.48  ? 474  ASP A O   1 
ATOM   2017 C  CB  . ASP A 1 251 ? 6.581   -11.695 44.340  1.00 26.56  ? 474  ASP A CB  1 
ATOM   2018 C  CG  . ASP A 1 251 ? 5.771   -12.193 45.517  1.00 30.83  ? 474  ASP A CG  1 
ATOM   2019 O  OD1 . ASP A 1 251 ? 4.796   -11.505 45.900  1.00 32.74  ? 474  ASP A OD1 1 
ATOM   2020 O  OD2 . ASP A 1 251 ? 6.114   -13.260 46.071  1.00 32.03  ? 474  ASP A OD2 1 
ATOM   2021 N  N   . VAL A 1 252 ? 3.931   -9.475  43.491  1.00 21.13  ? 475  VAL A N   1 
ATOM   2022 C  CA  . VAL A 1 252 ? 2.677   -9.451  42.737  1.00 21.01  ? 475  VAL A CA  1 
ATOM   2023 C  C   . VAL A 1 252 ? 2.088   -8.047  42.777  1.00 19.35  ? 475  VAL A C   1 
ATOM   2024 O  O   . VAL A 1 252 ? 1.884   -7.487  43.859  1.00 21.28  ? 475  VAL A O   1 
ATOM   2025 C  CB  . VAL A 1 252 ? 1.648   -10.459 43.292  1.00 21.54  ? 475  VAL A CB  1 
ATOM   2026 C  CG1 . VAL A 1 252 ? 0.341   -10.350 42.512  1.00 22.43  ? 475  VAL A CG1 1 
ATOM   2027 C  CG2 . VAL A 1 252 ? 2.186   -11.885 43.237  1.00 21.67  ? 475  VAL A CG2 1 
ATOM   2028 N  N   . ALA A 1 253 ? 1.798   -7.485  41.604  1.00 19.09  ? 476  ALA A N   1 
ATOM   2029 C  CA  . ALA A 1 253 ? 1.032   -6.250  41.495  1.00 20.34  ? 476  ALA A CA  1 
ATOM   2030 C  C   . ALA A 1 253 ? -0.418  -6.601  41.197  1.00 20.66  ? 476  ALA A C   1 
ATOM   2031 O  O   . ALA A 1 253 ? -0.703  -7.328  40.237  1.00 21.92  ? 476  ALA A O   1 
ATOM   2032 C  CB  . ALA A 1 253 ? 1.583   -5.353  40.384  1.00 20.88  ? 476  ALA A CB  1 
ATOM   2033 N  N   . LEU A 1 254 ? -1.328  -6.087  42.020  1.00 21.38  ? 477  LEU A N   1 
ATOM   2034 C  CA  . LEU A 1 254 ? -2.759  -6.241  41.784  1.00 21.62  ? 477  LEU A CA  1 
ATOM   2035 C  C   . LEU A 1 254 ? -3.198  -5.210  40.748  1.00 21.87  ? 477  LEU A C   1 
ATOM   2036 O  O   . LEU A 1 254 ? -3.031  -4.003  40.957  1.00 23.82  ? 477  LEU A O   1 
ATOM   2037 C  CB  . LEU A 1 254 ? -3.511  -6.043  43.101  1.00 23.66  ? 477  LEU A CB  1 
ATOM   2038 C  CG  . LEU A 1 254 ? -5.039  -6.054  43.042  1.00 24.64  ? 477  LEU A CG  1 
ATOM   2039 C  CD1 . LEU A 1 254 ? -5.547  -7.404  42.548  1.00 24.96  ? 477  LEU A CD1 1 
ATOM   2040 C  CD2 . LEU A 1 254 ? -5.617  -5.710  44.414  1.00 25.14  ? 477  LEU A CD2 1 
ATOM   2041 N  N   . ILE A 1 255 ? -3.742  -5.678  39.627  1.00 20.88  ? 478  ILE A N   1 
ATOM   2042 C  CA  . ILE A 1 255 ? -4.146  -4.804  38.532  1.00 20.89  ? 478  ILE A CA  1 
ATOM   2043 C  C   . ILE A 1 255 ? -5.619  -5.033  38.226  1.00 22.70  ? 478  ILE A C   1 
ATOM   2044 O  O   . ILE A 1 255 ? -6.114  -6.162  38.314  1.00 23.11  ? 478  ILE A O   1 
ATOM   2045 C  CB  . ILE A 1 255 ? -3.258  -4.999  37.283  1.00 19.33  ? 478  ILE A CB  1 
ATOM   2046 C  CG1 . ILE A 1 255 ? -3.320  -6.445  36.770  1.00 18.93  ? 478  ILE A CG1 1 
ATOM   2047 C  CG2 . ILE A 1 255 ? -1.827  -4.607  37.602  1.00 20.51  ? 478  ILE A CG2 1 
ATOM   2048 C  CD1 . ILE A 1 255 ? -2.605  -6.665  35.425  1.00 18.80  ? 478  ILE A CD1 1 
ATOM   2049 N  N   . ARG A 1 256 ? -6.324  -3.953  37.888  1.00 24.24  ? 479  ARG A N   1 
ATOM   2050 C  CA  . ARG A 1 256 ? -7.752  -3.988  37.608  1.00 25.76  ? 479  ARG A CA  1 
ATOM   2051 C  C   . ARG A 1 256 ? -7.983  -3.528  36.176  1.00 24.79  ? 479  ARG A C   1 
ATOM   2052 O  O   . ARG A 1 256 ? -7.450  -2.493  35.762  1.00 25.02  ? 479  ARG A O   1 
ATOM   2053 C  CB  . ARG A 1 256 ? -8.521  -3.067  38.568  1.00 29.40  ? 479  ARG A CB  1 
ATOM   2054 C  CG  . ARG A 1 256 ? -9.102  -3.759  39.801  1.00 33.69  ? 479  ARG A CG  1 
ATOM   2055 C  CD  . ARG A 1 256 ? -8.036  -4.185  40.789  1.00 36.73  ? 479  ARG A CD  1 
ATOM   2056 N  NE  . ARG A 1 256 ? -8.621  -4.831  41.960  1.00 37.41  ? 479  ARG A NE  1 
ATOM   2057 C  CZ  . ARG A 1 256 ? -8.891  -4.217  43.105  1.00 38.04  ? 479  ARG A CZ  1 
ATOM   2058 N  NH1 . ARG A 1 256 ? -8.632  -2.931  43.278  1.00 38.64  ? 479  ARG A NH1 1 
ATOM   2059 N  NH2 . ARG A 1 256 ? -9.429  -4.913  44.103  1.00 37.64  ? 479  ARG A NH2 1 
ATOM   2060 N  N   . TYR A 1 257 ? -8.769  -4.293  35.421  1.00 24.42  ? 480  TYR A N   1 
ATOM   2061 C  CA  . TYR A 1 257 ? -9.144  -3.909  34.064  1.00 24.97  ? 480  TYR A CA  1 
ATOM   2062 C  C   . TYR A 1 257 ? -10.390 -3.039  34.154  1.00 26.38  ? 480  TYR A C   1 
ATOM   2063 O  O   . TYR A 1 257 ? -11.440 -3.494  34.623  1.00 27.00  ? 480  TYR A O   1 
ATOM   2064 C  CB  . TYR A 1 257 ? -9.411  -5.141  33.204  1.00 25.93  ? 480  TYR A CB  1 
ATOM   2065 C  CG  . TYR A 1 257 ? -9.134  -4.939  31.723  1.00 26.66  ? 480  TYR A CG  1 
ATOM   2066 C  CD1 . TYR A 1 257 ? -7.849  -5.077  31.218  1.00 27.00  ? 480  TYR A CD1 1 
ATOM   2067 C  CD2 . TYR A 1 257 ? -10.155 -4.631  30.833  1.00 28.81  ? 480  TYR A CD2 1 
ATOM   2068 C  CE1 . TYR A 1 257 ? -7.581  -4.905  29.872  1.00 26.25  ? 480  TYR A CE1 1 
ATOM   2069 C  CE2 . TYR A 1 257 ? -9.896  -4.459  29.485  1.00 28.70  ? 480  TYR A CE2 1 
ATOM   2070 C  CZ  . TYR A 1 257 ? -8.608  -4.596  29.009  1.00 27.60  ? 480  TYR A CZ  1 
ATOM   2071 O  OH  . TYR A 1 257 ? -8.338  -4.428  27.664  1.00 29.64  ? 480  TYR A OH  1 
ATOM   2072 N  N   A VAL A 1 258 ? -10.272 -1.791  33.717  0.54 26.84  ? 481  VAL A N   1 
ATOM   2073 N  N   B VAL A 1 258 ? -10.277 -1.792  33.699  0.46 26.96  ? 481  VAL A N   1 
ATOM   2074 C  CA  A VAL A 1 258 ? -11.321 -0.806  33.937  0.54 27.04  ? 481  VAL A CA  1 
ATOM   2075 C  CA  B VAL A 1 258 ? -11.283 -0.765  33.945  0.46 27.24  ? 481  VAL A CA  1 
ATOM   2076 C  C   A VAL A 1 258 ? -11.869 -0.311  32.607  0.54 27.50  ? 481  VAL A C   1 
ATOM   2077 C  C   B VAL A 1 258 ? -11.854 -0.273  32.622  0.46 27.51  ? 481  VAL A C   1 
ATOM   2078 O  O   A VAL A 1 258 ? -11.156 -0.221  31.602  0.54 28.12  ? 481  VAL A O   1 
ATOM   2079 O  O   B VAL A 1 258 ? -11.129 -0.145  31.628  0.46 28.04  ? 481  VAL A O   1 
ATOM   2080 C  CB  A VAL A 1 258 ? -10.827 0.374   34.801  0.54 27.80  ? 481  VAL A CB  1 
ATOM   2081 C  CB  B VAL A 1 258 ? -10.673 0.408   34.742  0.46 28.21  ? 481  VAL A CB  1 
ATOM   2082 C  CG1 A VAL A 1 258 ? -10.456 -0.116  36.191  0.54 28.39  ? 481  VAL A CG1 1 
ATOM   2083 C  CG1 B VAL A 1 258 ? -11.747 1.408   35.145  0.46 28.03  ? 481  VAL A CG1 1 
ATOM   2084 C  CG2 A VAL A 1 258 ? -9.644  1.056   34.136  0.54 27.25  ? 481  VAL A CG2 1 
ATOM   2085 C  CG2 B VAL A 1 258 ? -9.934  -0.114  35.965  0.46 28.97  ? 481  VAL A CG2 1 
ATOM   2086 N  N   . ASN A 1 259 ? -13.162 0.002   32.613  1.00 26.89  ? 482  ASN A N   1 
ATOM   2087 C  CA  . ASN A 1 259 ? -13.791 0.707   31.508  1.00 27.96  ? 482  ASN A CA  1 
ATOM   2088 C  C   . ASN A 1 259 ? -13.691 2.179   31.875  1.00 27.58  ? 482  ASN A C   1 
ATOM   2089 O  O   . ASN A 1 259 ? -14.359 2.612   32.829  1.00 29.22  ? 482  ASN A O   1 
ATOM   2090 C  CB  . ASN A 1 259 ? -15.252 0.295   31.386  1.00 30.23  ? 482  ASN A CB  1 
ATOM   2091 C  CG  . ASN A 1 259 ? -15.961 0.954   30.215  1.00 31.92  ? 482  ASN A CG  1 
ATOM   2092 O  OD1 . ASN A 1 259 ? -15.669 2.094   29.843  1.00 31.48  ? 482  ASN A OD1 1 
ATOM   2093 N  ND2 . ASN A 1 259 ? -16.911 0.234   29.630  1.00 32.52  ? 482  ASN A ND2 1 
ATOM   2094 N  N   . PRO A 1 260 ? -12.868 2.972   31.189  1.00 29.45  ? 483  PRO A N   1 
ATOM   2095 C  CA  . PRO A 1 260 ? -12.701 4.375   31.597  1.00 32.50  ? 483  PRO A CA  1 
ATOM   2096 C  C   . PRO A 1 260 ? -13.959 5.214   31.434  1.00 34.94  ? 483  PRO A C   1 
ATOM   2097 O  O   . PRO A 1 260 ? -14.054 6.279   32.056  1.00 37.89  ? 483  PRO A O   1 
ATOM   2098 C  CB  . PRO A 1 260 ? -11.560 4.874   30.701  1.00 31.65  ? 483  PRO A CB  1 
ATOM   2099 C  CG  . PRO A 1 260 ? -11.604 3.979   29.500  1.00 30.69  ? 483  PRO A CG  1 
ATOM   2100 C  CD  . PRO A 1 260 ? -12.092 2.641   29.980  1.00 29.73  ? 483  PRO A CD  1 
ATOM   2101 N  N   . ASP A 1 261 ? -14.931 4.763   30.637  1.00 36.14  ? 484  ASP A N   1 
ATOM   2102 C  CA  . ASP A 1 261 ? -16.163 5.530   30.465  1.00 38.13  ? 484  ASP A CA  1 
ATOM   2103 C  C   . ASP A 1 261 ? -17.023 5.494   31.720  1.00 39.40  ? 484  ASP A C   1 
ATOM   2104 O  O   . ASP A 1 261 ? -17.660 6.493   32.074  1.00 41.13  ? 484  ASP A O   1 
ATOM   2105 C  CB  . ASP A 1 261 ? -16.959 4.990   29.277  1.00 40.05  ? 484  ASP A CB  1 
ATOM   2106 C  CG  . ASP A 1 261 ? -16.373 5.401   27.947  1.00 41.71  ? 484  ASP A CG  1 
ATOM   2107 O  OD1 . ASP A 1 261 ? -15.374 6.149   27.944  1.00 43.41  ? 484  ASP A OD1 1 
ATOM   2108 O  OD2 . ASP A 1 261 ? -16.915 4.978   26.904  1.00 42.44  ? 484  ASP A OD2 1 
ATOM   2109 N  N   . THR A 1 262 ? -17.067 4.350   32.398  1.00 38.88  ? 485  THR A N   1 
ATOM   2110 C  CA  . THR A 1 262 ? -17.925 4.168   33.555  1.00 38.69  ? 485  THR A CA  1 
ATOM   2111 C  C   . THR A 1 262 ? -17.160 4.067   34.864  1.00 39.50  ? 485  THR A C   1 
ATOM   2112 O  O   . THR A 1 262 ? -17.776 4.192   35.929  1.00 40.07  ? 485  THR A O   1 
ATOM   2113 C  CB  . THR A 1 262 ? -18.776 2.900   33.382  1.00 38.07  ? 485  THR A CB  1 
ATOM   2114 O  OG1 . THR A 1 262 ? -17.914 1.766   33.224  1.00 38.19  ? 485  THR A OG1 1 
ATOM   2115 C  CG2 . THR A 1 262 ? -19.676 3.025   32.158  1.00 38.26  ? 485  THR A CG2 1 
ATOM   2116 N  N   . GLY A 1 263 ? -15.846 3.852   34.816  1.00 39.41  ? 486  GLY A N   1 
ATOM   2117 C  CA  . GLY A 1 263 ? -15.081 3.520   35.998  1.00 39.98  ? 486  GLY A CA  1 
ATOM   2118 C  C   . GLY A 1 263 ? -15.280 2.108   36.496  1.00 39.70  ? 486  GLY A C   1 
ATOM   2119 O  O   . GLY A 1 263 ? -14.675 1.734   37.509  1.00 41.17  ? 486  GLY A O   1 
ATOM   2120 N  N   . ARG A 1 264 ? -16.100 1.313   35.816  1.00 38.86  ? 487  ARG A N   1 
ATOM   2121 C  CA  . ARG A 1 264 ? -16.395 -0.040  36.260  1.00 39.69  ? 487  ARG A CA  1 
ATOM   2122 C  C   . ARG A 1 264 ? -15.174 -0.940  36.110  1.00 36.64  ? 487  ARG A C   1 
ATOM   2123 O  O   . ARG A 1 264 ? -14.464 -0.896  35.101  1.00 35.72  ? 487  ARG A O   1 
ATOM   2124 C  CB  . ARG A 1 264 ? -17.560 -0.602  35.445  1.00 43.45  ? 487  ARG A CB  1 
ATOM   2125 C  CG  . ARG A 1 264 ? -17.750 -2.106  35.549  1.00 182.86 ? 487  ARG A CG  1 
ATOM   2126 C  CD  . ARG A 1 264 ? -19.194 -2.503  35.274  1.00 71.43  ? 487  ARG A CD  1 
ATOM   2127 N  NE  . ARG A 1 264 ? -20.048 -2.279  36.435  1.00 175.61 ? 487  ARG A NE  1 
ATOM   2128 C  CZ  . ARG A 1 264 ? -20.755 -1.177  36.652  1.00 194.81 ? 487  ARG A CZ  1 
ATOM   2129 N  NH1 . ARG A 1 264 ? -20.753 -0.172  35.792  1.00 70.52  ? 487  ARG A NH1 1 
ATOM   2130 N  NH2 . ARG A 1 264 ? -21.481 -1.081  37.762  1.00 157.94 ? 487  ARG A NH2 1 
ATOM   2131 N  N   . VAL A 1 265 ? -14.927 -1.753  37.131  1.00 34.96  ? 488  VAL A N   1 
ATOM   2132 C  CA  . VAL A 1 265 ? -13.881 -2.764  37.071  1.00 33.52  ? 488  VAL A CA  1 
ATOM   2133 C  C   . VAL A 1 265 ? -14.470 -4.006  36.417  1.00 33.36  ? 488  VAL A C   1 
ATOM   2134 O  O   . VAL A 1 265 ? -15.389 -4.627  36.960  1.00 35.34  ? 488  VAL A O   1 
ATOM   2135 C  CB  . VAL A 1 265 ? -13.347 -3.080  38.476  1.00 32.28  ? 488  VAL A CB  1 
ATOM   2136 C  CG1 . VAL A 1 265 ? -12.405 -4.275  38.432  1.00 32.64  ? 488  VAL A CG1 1 
ATOM   2137 C  CG2 . VAL A 1 265 ? -12.655 -1.859  39.058  1.00 33.12  ? 488  VAL A CG2 1 
ATOM   2138 N  N   . LEU A 1 266 ? -13.954 -4.360  35.238  1.00 32.58  ? 489  LEU A N   1 
ATOM   2139 C  CA  . LEU A 1 266 ? -14.428 -5.565  34.563  1.00 33.44  ? 489  LEU A CA  1 
ATOM   2140 C  C   . LEU A 1 266 ? -13.926 -6.821  35.267  1.00 32.31  ? 489  LEU A C   1 
ATOM   2141 O  O   . LEU A 1 266 ? -14.695 -7.762  35.497  1.00 33.41  ? 489  LEU A O   1 
ATOM   2142 C  CB  . LEU A 1 266 ? -14.009 -5.555  33.087  1.00 35.67  ? 489  LEU A CB  1 
ATOM   2143 C  CG  . LEU A 1 266 ? -14.664 -4.591  32.081  1.00 38.01  ? 489  LEU A CG  1 
ATOM   2144 C  CD1 . LEU A 1 266 ? -16.186 -4.685  32.107  1.00 39.19  ? 489  LEU A CD1 1 
ATOM   2145 C  CD2 . LEU A 1 266 ? -14.207 -3.151  32.274  1.00 38.75  ? 489  LEU A CD2 1 
ATOM   2146 N  N   . PHE A 1 267 ? -12.645 -6.845  35.632  1.00 29.45  ? 490  PHE A N   1 
ATOM   2147 C  CA  . PHE A 1 267 ? -12.055 -7.949  36.379  1.00 28.64  ? 490  PHE A CA  1 
ATOM   2148 C  C   . PHE A 1 267 ? -10.737 -7.468  36.964  1.00 27.35  ? 490  PHE A C   1 
ATOM   2149 O  O   . PHE A 1 267 ? -10.233 -6.397  36.612  1.00 27.06  ? 490  PHE A O   1 
ATOM   2150 C  CB  . PHE A 1 267 ? -11.861 -9.200  35.507  1.00 27.86  ? 490  PHE A CB  1 
ATOM   2151 C  CG  . PHE A 1 267 ? -10.831 -9.042  34.416  1.00 26.18  ? 490  PHE A CG  1 
ATOM   2152 C  CD1 . PHE A 1 267 ? -11.184 -8.517  33.181  1.00 25.94  ? 490  PHE A CD1 1 
ATOM   2153 C  CD2 . PHE A 1 267 ? -9.518  -9.446  34.615  1.00 25.17  ? 490  PHE A CD2 1 
ATOM   2154 C  CE1 . PHE A 1 267 ? -10.245 -8.379  32.172  1.00 26.12  ? 490  PHE A CE1 1 
ATOM   2155 C  CE2 . PHE A 1 267 ? -8.572  -9.314  33.614  1.00 25.26  ? 490  PHE A CE2 1 
ATOM   2156 C  CZ  . PHE A 1 267 ? -8.934  -8.779  32.386  1.00 25.48  ? 490  PHE A CZ  1 
ATOM   2157 N  N   . GLU A 1 268 ? -10.181 -8.276  37.862  1.00 25.45  ? 491  GLU A N   1 
ATOM   2158 C  CA  . GLU A 1 268 ? -8.873  -8.015  38.439  1.00 24.45  ? 491  GLU A CA  1 
ATOM   2159 C  C   . GLU A 1 268 ? -7.957  -9.201  38.179  1.00 23.45  ? 491  GLU A C   1 
ATOM   2160 O  O   . GLU A 1 268 ? -8.409  -10.309 37.881  1.00 23.47  ? 491  GLU A O   1 
ATOM   2161 C  CB  . GLU A 1 268 ? -8.953  -7.704  39.941  1.00 25.22  ? 491  GLU A CB  1 
ATOM   2162 C  CG  . GLU A 1 268 ? -9.499  -8.824  40.802  1.00 27.84  ? 491  GLU A CG  1 
ATOM   2163 C  CD  . GLU A 1 268 ? -9.674  -8.404  42.258  1.00 31.21  ? 491  GLU A CD  1 
ATOM   2164 O  OE1 . GLU A 1 268 ? -9.809  -7.183  42.515  1.00 33.35  ? 491  GLU A OE1 1 
ATOM   2165 O  OE2 . GLU A 1 268 ? -9.680  -9.286  43.149  1.00 30.20  ? 491  GLU A OE2 1 
ATOM   2166 N  N   . ALA A 1 269 ? -6.655  -8.949  38.291  1.00 22.42  ? 492  ALA A N   1 
ATOM   2167 C  CA  . ALA A 1 269 ? -5.655  -9.934  37.917  1.00 19.87  ? 492  ALA A CA  1 
ATOM   2168 C  C   . ALA A 1 269 ? -4.400  -9.702  38.739  1.00 19.45  ? 492  ALA A C   1 
ATOM   2169 O  O   . ALA A 1 269 ? -4.211  -8.635  39.331  1.00 18.71  ? 492  ALA A O   1 
ATOM   2170 C  CB  . ALA A 1 269 ? -5.319  -9.837  36.425  1.00 20.18  ? 492  ALA A CB  1 
ATOM   2171 N  N   . LYS A 1 270 ? -3.543  -10.726 38.771  1.00 18.79  ? 493  LYS A N   1 
ATOM   2172 C  CA  . LYS A 1 270 ? -2.243  -10.660 39.423  1.00 19.06  ? 493  LYS A CA  1 
ATOM   2173 C  C   . LYS A 1 270 ? -1.170  -10.490 38.357  1.00 17.73  ? 493  LYS A C   1 
ATOM   2174 O  O   . LYS A 1 270 ? -1.034  -11.339 37.471  1.00 18.74  ? 493  LYS A O   1 
ATOM   2175 C  CB  . LYS A 1 270 ? -1.974  -11.963 40.168  1.00 20.54  ? 493  LYS A CB  1 
ATOM   2176 C  CG  . LYS A 1 270 ? -2.720  -12.144 41.462  1.00 23.21  ? 493  LYS A CG  1 
ATOM   2177 C  CD  . LYS A 1 270 ? -2.392  -13.532 42.005  1.00 25.84  ? 493  LYS A CD  1 
ATOM   2178 C  CE  . LYS A 1 270 ? -2.781  -13.696 43.436  1.00 26.44  ? 493  LYS A CE  1 
ATOM   2179 N  NZ  . LYS A 1 270 ? -2.818  -15.137 43.777  1.00 25.66  ? 493  LYS A NZ  1 
ATOM   2180 N  N   . LEU A 1 271 ? -0.397  -9.409  38.447  1.00 17.03  ? 494  LEU A N   1 
ATOM   2181 C  CA  . LEU A 1 271 ? 0.748   -9.192  37.569  1.00 16.77  ? 494  LEU A CA  1 
ATOM   2182 C  C   . LEU A 1 271 ? 1.999   -9.595  38.348  1.00 16.20  ? 494  LEU A C   1 
ATOM   2183 O  O   . LEU A 1 271 ? 2.413   -8.896  39.280  1.00 16.90  ? 494  LEU A O   1 
ATOM   2184 C  CB  . LEU A 1 271 ? 0.815   -7.741  37.097  1.00 16.98  ? 494  LEU A CB  1 
ATOM   2185 C  CG  . LEU A 1 271 ? 2.007   -7.351  36.218  1.00 16.46  ? 494  LEU A CG  1 
ATOM   2186 C  CD1 . LEU A 1 271 ? 2.108   -8.223  34.968  1.00 17.10  ? 494  LEU A CD1 1 
ATOM   2187 C  CD2 . LEU A 1 271 ? 1.916   -5.875  35.848  1.00 17.53  ? 494  LEU A CD2 1 
ATOM   2188 N  N   . HIS A 1 272 ? 2.587   -10.728 37.973  1.00 15.81  ? 495  HIS A N   1 
ATOM   2189 C  CA  . HIS A 1 272 ? 3.701   -11.283 38.726  1.00 15.10  ? 495  HIS A CA  1 
ATOM   2190 C  C   . HIS A 1 272 ? 5.007   -10.581 38.365  1.00 16.54  ? 495  HIS A C   1 
ATOM   2191 O  O   . HIS A 1 272 ? 5.186   -10.100 37.239  1.00 16.41  ? 495  HIS A O   1 
ATOM   2192 C  CB  . HIS A 1 272 ? 3.811   -12.784 38.460  1.00 14.59  ? 495  HIS A CB  1 
ATOM   2193 C  CG  . HIS A 1 272 ? 2.590   -13.546 38.855  1.00 15.50  ? 495  HIS A CG  1 
ATOM   2194 N  ND1 . HIS A 1 272 ? 2.496   -14.234 40.047  1.00 16.83  ? 495  HIS A ND1 1 
ATOM   2195 C  CD2 . HIS A 1 272 ? 1.394   -13.691 38.237  1.00 17.03  ? 495  HIS A CD2 1 
ATOM   2196 C  CE1 . HIS A 1 272 ? 1.299   -14.794 40.130  1.00 17.10  ? 495  HIS A CE1 1 
ATOM   2197 N  NE2 . HIS A 1 272 ? 0.611   -14.475 39.046  1.00 18.48  ? 495  HIS A NE2 1 
ATOM   2198 N  N   . ARG A 1 273 ? 5.919   -10.528 39.345  1.00 16.62  ? 496  ARG A N   1 
ATOM   2199 C  CA  . ARG A 1 273 ? 7.215   -9.872  39.178  1.00 18.82  ? 496  ARG A CA  1 
ATOM   2200 C  C   . ARG A 1 273 ? 7.943   -10.364 37.933  1.00 17.08  ? 496  ARG A C   1 
ATOM   2201 O  O   . ARG A 1 273 ? 8.622   -9.585  37.253  1.00 16.74  ? 496  ARG A O   1 
ATOM   2202 C  CB  . ARG A 1 273 ? 8.060   -10.122 40.433  1.00 23.98  ? 496  ARG A CB  1 
ATOM   2203 C  CG  . ARG A 1 273 ? 9.495   -9.690  40.315  1.00 29.64  ? 496  ARG A CG  1 
ATOM   2204 C  CD  . ARG A 1 273 ? 10.219  -9.922  41.626  1.00 33.95  ? 496  ARG A CD  1 
ATOM   2205 N  NE  . ARG A 1 273 ? 9.902   -8.901  42.615  1.00 39.37  ? 496  ARG A NE  1 
ATOM   2206 C  CZ  . ARG A 1 273 ? 10.040  -9.063  43.925  1.00 43.10  ? 496  ARG A CZ  1 
ATOM   2207 N  NH1 . ARG A 1 273 ? 10.398  -10.226 44.443  1.00 44.14  ? 496  ARG A NH1 1 
ATOM   2208 N  NH2 . ARG A 1 273 ? 9.805   -8.035  44.736  1.00 44.69  ? 496  ARG A NH2 1 
ATOM   2209 N  N   . GLN A 1 274 ? 7.796   -11.647 37.610  0.93 15.20  ? 497  GLN A N   1 
ATOM   2210 C  CA  . GLN A 1 274 ? 8.480   -12.227 36.464  0.93 16.25  ? 497  GLN A CA  1 
ATOM   2211 C  C   . GLN A 1 274 ? 7.988   -11.663 35.132  0.93 15.05  ? 497  GLN A C   1 
ATOM   2212 O  O   . GLN A 1 274 ? 8.672   -11.840 34.122  0.93 16.49  ? 497  GLN A O   1 
ATOM   2213 C  CB  . GLN A 1 274 ? 8.334   -13.753 36.496  0.93 19.78  ? 497  GLN A CB  1 
ATOM   2214 C  CG  . GLN A 1 274 ? 8.811   -14.403 37.793  0.93 23.05  ? 497  GLN A CG  1 
ATOM   2215 C  CD  . GLN A 1 274 ? 7.678   -14.679 38.765  0.93 25.37  ? 497  GLN A CD  1 
ATOM   2216 O  OE1 . GLN A 1 274 ? 6.976   -13.765 39.197  0.93 22.60  ? 497  GLN A OE1 1 
ATOM   2217 N  NE2 . GLN A 1 274 ? 7.491   -15.947 39.108  0.93 29.22  ? 497  GLN A NE2 1 
ATOM   2218 N  N   . GLY A 1 275 ? 6.836   -10.990 35.106  1.00 13.78  ? 498  GLY A N   1 
ATOM   2219 C  CA  . GLY A 1 275 ? 6.304   -10.413 33.878  1.00 13.38  ? 498  GLY A CA  1 
ATOM   2220 C  C   . GLY A 1 275 ? 5.229   -11.255 33.215  1.00 13.56  ? 498  GLY A C   1 
ATOM   2221 O  O   . GLY A 1 275 ? 5.315   -11.521 32.013  1.00 15.19  ? 498  GLY A O   1 
ATOM   2222 N  N   . TYR A 1 276 ? 4.223   -11.698 33.969  1.00 14.07  ? 499  TYR A N   1 
ATOM   2223 C  CA  . TYR A 1 276 ? 3.089   -12.425 33.399  1.00 13.59  ? 499  TYR A CA  1 
ATOM   2224 C  C   . TYR A 1 276 ? 1.884   -12.237 34.315  1.00 14.48  ? 499  TYR A C   1 
ATOM   2225 O  O   . TYR A 1 276 ? 2.023   -11.813 35.468  1.00 15.36  ? 499  TYR A O   1 
ATOM   2226 C  CB  . TYR A 1 276 ? 3.398   -13.917 33.170  1.00 14.83  ? 499  TYR A CB  1 
ATOM   2227 C  CG  . TYR A 1 276 ? 3.589   -14.711 34.447  1.00 16.19  ? 499  TYR A CG  1 
ATOM   2228 C  CD1 . TYR A 1 276 ? 4.832   -14.792 35.064  1.00 15.85  ? 499  TYR A CD1 1 
ATOM   2229 C  CD2 . TYR A 1 276 ? 2.519   -15.357 35.053  1.00 17.36  ? 499  TYR A CD2 1 
ATOM   2230 C  CE1 . TYR A 1 276 ? 5.009   -15.510 36.237  1.00 15.75  ? 499  TYR A CE1 1 
ATOM   2231 C  CE2 . TYR A 1 276 ? 2.689   -16.083 36.225  1.00 18.54  ? 499  TYR A CE2 1 
ATOM   2232 C  CZ  . TYR A 1 276 ? 3.933   -16.147 36.812  1.00 17.72  ? 499  TYR A CZ  1 
ATOM   2233 O  OH  . TYR A 1 276 ? 4.118   -16.852 37.980  1.00 19.71  ? 499  TYR A OH  1 
ATOM   2234 N  N   . ILE A 1 277 ? 0.699   -12.570 33.800  1.00 14.67  ? 500  ILE A N   1 
ATOM   2235 C  CA  . ILE A 1 277 ? -0.564  -12.272 34.466  1.00 14.33  ? 500  ILE A CA  1 
ATOM   2236 C  C   . ILE A 1 277 ? -1.320  -13.565 34.742  1.00 16.02  ? 500  ILE A C   1 
ATOM   2237 O  O   . ILE A 1 277 ? -1.385  -14.452 33.883  1.00 15.74  ? 500  ILE A O   1 
ATOM   2238 C  CB  . ILE A 1 277 ? -1.430  -11.315 33.616  1.00 15.36  ? 500  ILE A CB  1 
ATOM   2239 C  CG1 . ILE A 1 277 ? -0.696  -9.992  33.381  1.00 16.26  ? 500  ILE A CG1 1 
ATOM   2240 C  CG2 . ILE A 1 277 ? -2.780  -11.072 34.285  1.00 17.12  ? 500  ILE A CG2 1 
ATOM   2241 C  CD1 . ILE A 1 277 ? -1.400  -9.051  32.405  1.00 16.17  ? 500  ILE A CD1 1 
ATOM   2242 N  N   . THR A 1 278 ? -1.911  -13.668 35.934  1.00 16.61  ? 501  THR A N   1 
ATOM   2243 C  CA  . THR A 1 278 ? -2.875  -14.723 36.207  1.00 16.93  ? 501  THR A CA  1 
ATOM   2244 C  C   . THR A 1 278 ? -4.221  -14.135 36.618  1.00 18.82  ? 501  THR A C   1 
ATOM   2245 O  O   . THR A 1 278 ? -4.298  -13.031 37.162  1.00 19.57  ? 501  THR A O   1 
ATOM   2246 C  CB  . THR A 1 278 ? -2.383  -15.728 37.267  1.00 17.80  ? 501  THR A CB  1 
ATOM   2247 O  OG1 . THR A 1 278 ? -2.120  -15.053 38.505  1.00 19.14  ? 501  THR A OG1 1 
ATOM   2248 C  CG2 . THR A 1 278 ? -1.130  -16.447 36.791  1.00 18.81  ? 501  THR A CG2 1 
ATOM   2249 N  N   . VAL A 1 279 ? -5.289  -14.894 36.350  1.00 19.23  ? 502  VAL A N   1 
ATOM   2250 C  CA  . VAL A 1 279 ? -6.654  -14.515 36.689  1.00 21.24  ? 502  VAL A CA  1 
ATOM   2251 C  C   . VAL A 1 279 ? -7.344  -15.713 37.321  1.00 22.87  ? 502  VAL A C   1 
ATOM   2252 O  O   . VAL A 1 279 ? -6.967  -16.864 37.098  1.00 24.43  ? 502  VAL A O   1 
ATOM   2253 C  CB  . VAL A 1 279 ? -7.466  -14.048 35.462  1.00 22.40  ? 502  VAL A CB  1 
ATOM   2254 C  CG1 . VAL A 1 279 ? -6.945  -12.730 34.942  1.00 23.25  ? 502  VAL A CG1 1 
ATOM   2255 C  CG2 . VAL A 1 279 ? -7.434  -15.113 34.376  1.00 23.03  ? 502  VAL A CG2 1 
ATOM   2256 N  N   . ALA A 1 280 ? -8.377  -15.428 38.113  1.00 24.72  ? 503  ALA A N   1 
ATOM   2257 C  CA  . ALA A 1 280 ? -9.185  -16.472 38.747  1.00 27.06  ? 503  ALA A CA  1 
ATOM   2258 C  C   . ALA A 1 280 ? -10.283 -16.866 37.768  1.00 29.51  ? 503  ALA A C   1 
ATOM   2259 O  O   . ALA A 1 280 ? -11.376 -16.299 37.759  1.00 30.60  ? 503  ALA A O   1 
ATOM   2260 C  CB  . ALA A 1 280 ? -9.754  -15.993 40.079  1.00 28.00  ? 503  ALA A CB  1 
ATOM   2261 N  N   . LYS A 1 281 ? -9.978  -17.848 36.924  1.00 30.96  ? 504  LYS A N   1 
ATOM   2262 C  CA  . LYS A 1 281 ? -10.914 -18.340 35.927  1.00 34.09  ? 504  LYS A CA  1 
ATOM   2263 C  C   . LYS A 1 281 ? -10.531 -19.773 35.592  1.00 36.71  ? 504  LYS A C   1 
ATOM   2264 O  O   . LYS A 1 281 ? -9.345  -20.105 35.533  1.00 36.76  ? 504  LYS A O   1 
ATOM   2265 C  CB  . LYS A 1 281 ? -10.869 -17.474 34.662  1.00 35.15  ? 504  LYS A CB  1 
ATOM   2266 C  CG  . LYS A 1 281 ? -11.708 -18.004 33.504  1.00 37.24  ? 504  LYS A CG  1 
ATOM   2267 C  CD  . LYS A 1 281 ? -13.181 -18.054 33.862  1.00 39.13  ? 504  LYS A CD  1 
ATOM   2268 C  CE  . LYS A 1 281 ? -14.017 -18.505 32.671  1.00 40.72  ? 504  LYS A CE  1 
ATOM   2269 N  NZ  . LYS A 1 281 ? -15.471 -18.544 32.992  1.00 41.63  ? 504  LYS A NZ  1 
ATOM   2270 N  N   . THR A 1 282 ? -11.538 -20.615 35.387  1.00 39.50  ? 505  THR A N   1 
ATOM   2271 C  CA  . THR A 1 282 ? -11.330 -22.010 35.023  1.00 42.62  ? 505  THR A CA  1 
ATOM   2272 C  C   . THR A 1 282 ? -11.940 -22.250 33.652  1.00 42.56  ? 505  THR A C   1 
ATOM   2273 O  O   . THR A 1 282 ? -13.152 -22.085 33.472  1.00 44.00  ? 505  THR A O   1 
ATOM   2274 C  CB  . THR A 1 282 ? -11.974 -22.937 36.054  1.00 44.99  ? 505  THR A CB  1 
ATOM   2275 O  OG1 . THR A 1 282 ? -11.374 -22.717 37.337  1.00 45.85  ? 505  THR A OG1 1 
ATOM   2276 C  CG2 . THR A 1 282 ? -11.783 -24.389 35.648  1.00 45.88  ? 505  THR A CG2 1 
ATOM   2277 N  N   . GLY A 1 283 ? -11.106 -22.642 32.692  1.00 41.47  ? 506  GLY A N   1 
ATOM   2278 C  CA  . GLY A 1 283 ? -11.590 -22.995 31.371  1.00 41.63  ? 506  GLY A CA  1 
ATOM   2279 C  C   . GLY A 1 283 ? -10.969 -22.204 30.237  1.00 42.15  ? 506  GLY A C   1 
ATOM   2280 O  O   . GLY A 1 283 ? -10.456 -21.100 30.443  1.00 40.93  ? 506  GLY A O   1 
ATOM   2281 N  N   . ASP A 1 284 ? -11.008 -22.766 29.030  1.00 43.10  ? 507  ASP A N   1 
ATOM   2282 C  CA  . ASP A 1 284 ? -10.508 -22.089 27.834  1.00 44.24  ? 507  ASP A CA  1 
ATOM   2283 C  C   . ASP A 1 284 ? -11.552 -21.067 27.409  1.00 43.31  ? 507  ASP A C   1 
ATOM   2284 O  O   . ASP A 1 284 ? -12.572 -21.415 26.814  1.00 44.12  ? 507  ASP A O   1 
ATOM   2285 C  CB  . ASP A 1 284 ? -10.255 -23.097 26.721  1.00 45.32  ? 507  ASP A CB  1 
ATOM   2286 C  CG  . ASP A 1 284 ? -9.918  -22.432 25.402  1.00 48.00  ? 507  ASP A CG  1 
ATOM   2287 O  OD1 . ASP A 1 284 ? -8.952  -21.645 25.364  1.00 48.70  ? 507  ASP A OD1 1 
ATOM   2288 O  OD2 . ASP A 1 284 ? -10.619 -22.694 24.404  1.00 50.20  ? 507  ASP A OD2 1 
ATOM   2289 N  N   . SER A 1 285 ? -11.298 -19.796 27.695  1.00 41.67  ? 508  SER A N   1 
ATOM   2290 C  CA  . SER A 1 285 ? -12.340 -18.794 27.554  1.00 40.62  ? 508  SER A CA  1 
ATOM   2291 C  C   . SER A 1 285 ? -11.810 -17.516 26.918  1.00 37.05  ? 508  SER A C   1 
ATOM   2292 O  O   . SER A 1 285 ? -10.682 -17.097 27.193  1.00 34.16  ? 508  SER A O   1 
ATOM   2293 C  CB  . SER A 1 285 ? -12.955 -18.449 28.918  1.00 42.31  ? 508  SER A CB  1 
ATOM   2294 O  OG  . SER A 1 285 ? -13.939 -17.439 28.791  1.00 43.60  ? 508  SER A OG  1 
ATOM   2295 N  N   . PRO A 1 286 ? -12.613 -16.882 26.075  1.00 37.18  ? 509  PRO A N   1 
ATOM   2296 C  CA  . PRO A 1 286 ? -12.344 -15.493 25.702  1.00 36.23  ? 509  PRO A CA  1 
ATOM   2297 C  C   . PRO A 1 286 ? -12.696 -14.578 26.864  1.00 36.47  ? 509  PRO A C   1 
ATOM   2298 O  O   . PRO A 1 286 ? -13.441 -14.943 27.774  1.00 38.75  ? 509  PRO A O   1 
ATOM   2299 C  CB  . PRO A 1 286 ? -13.308 -15.266 24.532  1.00 37.53  ? 509  PRO A CB  1 
ATOM   2300 C  CG  . PRO A 1 286 ? -14.451 -16.174 24.827  1.00 39.08  ? 509  PRO A CG  1 
ATOM   2301 C  CD  . PRO A 1 286 ? -13.854 -17.393 25.471  1.00 37.95  ? 509  PRO A CD  1 
ATOM   2302 N  N   . ILE A 1 287 ? -12.135 -13.376 26.834  1.00 34.80  ? 510  ILE A N   1 
ATOM   2303 C  CA  . ILE A 1 287 ? -12.378 -12.384 27.878  1.00 35.42  ? 510  ILE A CA  1 
ATOM   2304 C  C   . ILE A 1 287 ? -13.086 -11.205 27.226  1.00 38.84  ? 510  ILE A C   1 
ATOM   2305 O  O   . ILE A 1 287 ? -12.452 -10.364 26.579  1.00 38.67  ? 510  ILE A O   1 
ATOM   2306 C  CB  . ILE A 1 287 ? -11.093 -11.963 28.594  1.00 33.60  ? 510  ILE A CB  1 
ATOM   2307 C  CG1 . ILE A 1 287 ? -10.433 -13.197 29.211  1.00 32.68  ? 510  ILE A CG1 1 
ATOM   2308 C  CG2 . ILE A 1 287 ? -11.394 -10.918 29.660  1.00 32.76  ? 510  ILE A CG2 1 
ATOM   2309 C  CD1 . ILE A 1 287 ? -9.307  -12.886 30.152  1.00 33.88  ? 510  ILE A CD1 1 
ATOM   2310 N  N   . ASN A 1 288 ? -14.406 -11.141 27.396  1.00 43.14  ? 511  ASN A N   1 
ATOM   2311 C  CA  . ASN A 1 288 ? -15.226 -10.109 26.772  1.00 49.02  ? 511  ASN A CA  1 
ATOM   2312 C  C   . ASN A 1 288 ? -15.074 -8.811  27.555  1.00 46.32  ? 511  ASN A C   1 
ATOM   2313 O  O   . ASN A 1 288 ? -15.529 -8.709  28.699  1.00 47.08  ? 511  ASN A O   1 
ATOM   2314 C  CB  . ASN A 1 288 ? -16.685 -10.554 26.734  1.00 57.13  ? 511  ASN A CB  1 
ATOM   2315 C  CG  . ASN A 1 288 ? -16.871 -11.876 26.016  1.00 85.54  ? 511  ASN A CG  1 
ATOM   2316 O  OD1 . ASN A 1 288 ? -16.137 -12.197 25.081  1.00 61.76  ? 511  ASN A OD1 1 
ATOM   2317 N  ND2 . ASN A 1 288 ? -17.857 -12.652 26.452  1.00 114.39 ? 511  ASN A ND2 1 
ATOM   2318 N  N   . VAL A 1 289 ? -14.443 -7.819  26.937  1.00 42.95  ? 512  VAL A N   1 
ATOM   2319 C  CA  . VAL A 1 289 ? -14.197 -6.523  27.569  1.00 40.97  ? 512  VAL A CA  1 
ATOM   2320 C  C   . VAL A 1 289 ? -14.378 -5.428  26.530  1.00 37.83  ? 512  VAL A C   1 
ATOM   2321 O  O   . VAL A 1 289 ? -14.253 -5.668  25.321  1.00 36.61  ? 512  VAL A O   1 
ATOM   2322 C  CB  . VAL A 1 289 ? -12.781 -6.445  28.173  1.00 43.05  ? 512  VAL A CB  1 
ATOM   2323 C  CG1 . VAL A 1 289 ? -12.680 -7.310  29.424  1.00 44.39  ? 512  VAL A CG1 1 
ATOM   2324 C  CG2 . VAL A 1 289 ? -11.751 -6.864  27.141  1.00 43.78  ? 512  VAL A CG2 1 
ATOM   2325 N  N   . PRO A 1 290 ? -14.681 -4.210  26.975  1.00 35.71  ? 513  PRO A N   1 
ATOM   2326 C  CA  . PRO A 1 290 ? -14.820 -3.105  26.023  1.00 34.70  ? 513  PRO A CA  1 
ATOM   2327 C  C   . PRO A 1 290 ? -13.489 -2.775  25.370  1.00 32.05  ? 513  PRO A C   1 
ATOM   2328 O  O   . PRO A 1 290 ? -12.421 -2.907  25.972  1.00 31.00  ? 513  PRO A O   1 
ATOM   2329 C  CB  . PRO A 1 290 ? -15.314 -1.944  26.896  1.00 35.58  ? 513  PRO A CB  1 
ATOM   2330 C  CG  . PRO A 1 290 ? -14.856 -2.284  28.269  1.00 36.73  ? 513  PRO A CG  1 
ATOM   2331 C  CD  . PRO A 1 290 ? -14.959 -3.779  28.356  1.00 36.87  ? 513  PRO A CD  1 
ATOM   2332 N  N   . ALA A 1 291 ? -13.568 -2.352  24.107  1.00 31.14  ? 514  ALA A N   1 
ATOM   2333 C  CA  . ALA A 1 291 ? -12.363 -2.018  23.358  1.00 30.48  ? 514  ALA A CA  1 
ATOM   2334 C  C   . ALA A 1 291 ? -11.568 -0.890  24.003  1.00 30.19  ? 514  ALA A C   1 
ATOM   2335 O  O   . ALA A 1 291 ? -10.355 -0.808  23.793  1.00 30.80  ? 514  ALA A O   1 
ATOM   2336 C  CB  . ALA A 1 291 ? -12.721 -1.660  21.916  1.00 31.06  ? 514  ALA A CB  1 
ATOM   2337 N  N   . ASN A 1 292 ? -12.216 -0.033  24.792  1.00 28.95  ? 515  ASN A N   1 
ATOM   2338 C  CA  . ASN A 1 292 ? -11.555 1.094   25.438  1.00 28.57  ? 515  ASN A CA  1 
ATOM   2339 C  C   . ASN A 1 292 ? -10.899 0.733   26.768  1.00 26.97  ? 515  ASN A C   1 
ATOM   2340 O  O   . ASN A 1 292 ? -10.335 1.617   27.420  1.00 27.73  ? 515  ASN A O   1 
ATOM   2341 C  CB  . ASN A 1 292 ? -12.554 2.240   25.645  1.00 29.20  ? 515  ASN A CB  1 
ATOM   2342 C  CG  . ASN A 1 292 ? -13.616 1.920   26.697  1.00 30.85  ? 515  ASN A CG  1 
ATOM   2343 O  OD1 . ASN A 1 292 ? -13.736 0.785   27.170  1.00 31.22  ? 515  ASN A OD1 1 
ATOM   2344 N  ND2 . ASN A 1 292 ? -14.395 2.929   27.064  1.00 30.54  ? 515  ASN A ND2 1 
ATOM   2345 N  N   . GLY A 1 293 ? -10.955 -0.530  27.185  1.00 24.98  ? 516  GLY A N   1 
ATOM   2346 C  CA  . GLY A 1 293 ? -10.496 -0.890  28.512  1.00 25.13  ? 516  GLY A CA  1 
ATOM   2347 C  C   . GLY A 1 293 ? -8.987  -1.055  28.615  1.00 24.30  ? 516  GLY A C   1 
ATOM   2348 O  O   . GLY A 1 293 ? -8.275  -1.267  27.632  1.00 24.11  ? 516  GLY A O   1 
ATOM   2349 N  N   . TYR A 1 294 ? -8.491  -0.952  29.845  1.00 23.51  ? 517  TYR A N   1 
ATOM   2350 C  CA  . TYR A 1 294 ? -7.067  -1.132  30.090  1.00 22.54  ? 517  TYR A CA  1 
ATOM   2351 C  C   . TYR A 1 294 ? -6.843  -1.460  31.557  1.00 21.92  ? 517  TYR A C   1 
ATOM   2352 O  O   . TYR A 1 294 ? -7.692  -1.190  32.411  1.00 22.88  ? 517  TYR A O   1 
ATOM   2353 C  CB  . TYR A 1 294 ? -6.249  0.099   29.681  1.00 22.73  ? 517  TYR A CB  1 
ATOM   2354 C  CG  . TYR A 1 294 ? -6.681  1.376   30.358  1.00 25.42  ? 517  TYR A CG  1 
ATOM   2355 C  CD1 . TYR A 1 294 ? -6.117  1.767   31.565  1.00 27.89  ? 517  TYR A CD1 1 
ATOM   2356 C  CD2 . TYR A 1 294 ? -7.649  2.197   29.788  1.00 27.21  ? 517  TYR A CD2 1 
ATOM   2357 C  CE1 . TYR A 1 294 ? -6.508  2.933   32.188  1.00 30.30  ? 517  TYR A CE1 1 
ATOM   2358 C  CE2 . TYR A 1 294 ? -8.044  3.365   30.407  1.00 29.61  ? 517  TYR A CE2 1 
ATOM   2359 C  CZ  . TYR A 1 294 ? -7.470  3.725   31.607  1.00 31.23  ? 517  TYR A CZ  1 
ATOM   2360 O  OH  . TYR A 1 294 ? -7.861  4.889   32.227  1.00 33.74  ? 517  TYR A OH  1 
ATOM   2361 N  N   . PHE A 1 295 ? -5.678  -2.041  31.833  1.00 21.44  ? 518  PHE A N   1 
ATOM   2362 C  CA  . PHE A 1 295 ? -5.308  -2.392  33.192  1.00 21.51  ? 518  PHE A CA  1 
ATOM   2363 C  C   . PHE A 1 295 ? -4.781  -1.177  33.940  1.00 22.25  ? 518  PHE A C   1 
ATOM   2364 O  O   . PHE A 1 295 ? -4.044  -0.356  33.387  1.00 23.27  ? 518  PHE A O   1 
ATOM   2365 C  CB  . PHE A 1 295 ? -4.210  -3.452  33.174  1.00 19.91  ? 518  PHE A CB  1 
ATOM   2366 C  CG  . PHE A 1 295 ? -4.712  -4.849  32.977  1.00 19.70  ? 518  PHE A CG  1 
ATOM   2367 C  CD1 . PHE A 1 295 ? -5.483  -5.466  33.954  1.00 20.03  ? 518  PHE A CD1 1 
ATOM   2368 C  CD2 . PHE A 1 295 ? -4.381  -5.565  31.834  1.00 19.86  ? 518  PHE A CD2 1 
ATOM   2369 C  CE1 . PHE A 1 295 ? -5.934  -6.762  33.783  1.00 20.69  ? 518  PHE A CE1 1 
ATOM   2370 C  CE2 . PHE A 1 295 ? -4.831  -6.858  31.655  1.00 20.92  ? 518  PHE A CE2 1 
ATOM   2371 C  CZ  . PHE A 1 295 ? -5.604  -7.460  32.637  1.00 21.11  ? 518  PHE A CZ  1 
ATOM   2372 N  N   . ARG A 1 296 ? -5.131  -1.095  35.220  1.00 23.93  ? 519  ARG A N   1 
ATOM   2373 C  CA  . ARG A 1 296 ? -4.665  -0.049  36.117  1.00 26.26  ? 519  ARG A CA  1 
ATOM   2374 C  C   . ARG A 1 296 ? -4.013  -0.724  37.314  1.00 25.85  ? 519  ARG A C   1 
ATOM   2375 O  O   . ARG A 1 296 ? -4.585  -1.659  37.881  1.00 26.21  ? 519  ARG A O   1 
ATOM   2376 C  CB  . ARG A 1 296 ? -5.863  0.784   36.580  1.00 28.88  ? 519  ARG A CB  1 
ATOM   2377 C  CG  . ARG A 1 296 ? -5.546  1.920   37.523  1.00 32.88  ? 519  ARG A CG  1 
ATOM   2378 C  CD  . ARG A 1 296 ? -6.837  2.525   38.053  1.00 36.67  ? 519  ARG A CD  1 
ATOM   2379 N  NE  . ARG A 1 296 ? -7.597  1.567   38.849  1.00 39.78  ? 519  ARG A NE  1 
ATOM   2380 C  CZ  . ARG A 1 296 ? -8.884  1.689   39.145  1.00 43.95  ? 519  ARG A CZ  1 
ATOM   2381 N  NH1 . ARG A 1 296 ? -9.601  2.710   38.702  1.00 44.99  ? 519  ARG A NH1 1 
ATOM   2382 N  NH2 . ARG A 1 296 ? -9.467  0.762   39.899  1.00 45.77  ? 519  ARG A NH2 1 
ATOM   2383 N  N   . PHE A 1 297 ? -2.810  -0.277  37.675  1.00 25.46  ? 520  PHE A N   1 
ATOM   2384 C  CA  . PHE A 1 297 ? -2.154  -0.771  38.883  1.00 25.66  ? 520  PHE A CA  1 
ATOM   2385 C  C   . PHE A 1 297 ? -2.856  -0.219  40.113  1.00 27.89  ? 520  PHE A C   1 
ATOM   2386 O  O   . PHE A 1 297 ? -3.060  0.992   40.229  1.00 29.52  ? 520  PHE A O   1 
ATOM   2387 C  CB  . PHE A 1 297 ? -0.695  -0.324  38.909  1.00 26.73  ? 520  PHE A CB  1 
ATOM   2388 C  CG  . PHE A 1 297 ? -0.021  -0.533  40.243  1.00 27.60  ? 520  PHE A CG  1 
ATOM   2389 C  CD1 . PHE A 1 297 ? 0.322   -1.808  40.668  1.00 27.44  ? 520  PHE A CD1 1 
ATOM   2390 C  CD2 . PHE A 1 297 ? 0.269   0.540   41.071  1.00 28.18  ? 520  PHE A CD2 1 
ATOM   2391 C  CE1 . PHE A 1 297 ? 0.941   -2.008  41.893  1.00 28.17  ? 520  PHE A CE1 1 
ATOM   2392 C  CE2 . PHE A 1 297 ? 0.892   0.342   42.298  1.00 30.21  ? 520  PHE A CE2 1 
ATOM   2393 C  CZ  . PHE A 1 297 ? 1.222   -0.933  42.704  1.00 29.88  ? 520  PHE A CZ  1 
ATOM   2394 N  N   . ASP A 1 298 ? -3.201  -1.101  41.045  1.00 26.79  ? 521  ASP A N   1 
ATOM   2395 C  CA  A ASP A 1 298 ? -3.879  -0.666  42.255  0.59 27.41  ? 521  ASP A CA  1 
ATOM   2396 C  CA  B ASP A 1 298 ? -3.916  -0.742  42.270  0.41 27.80  ? 521  ASP A CA  1 
ATOM   2397 C  C   . ASP A 1 298 ? -3.048  -0.814  43.519  1.00 27.65  ? 521  ASP A C   1 
ATOM   2398 O  O   . ASP A 1 298 ? -3.033  0.116   44.331  1.00 29.49  ? 521  ASP A O   1 
ATOM   2399 C  CB  A ASP A 1 298 ? -5.252  -1.335  42.391  0.59 29.30  ? 521  ASP A CB  1 
ATOM   2400 C  CB  B ASP A 1 298 ? -5.134  -1.663  42.449  0.41 29.67  ? 521  ASP A CB  1 
ATOM   2401 C  CG  A ASP A 1 298 ? -6.294  -0.704  41.468  0.59 31.02  ? 521  ASP A CG  1 
ATOM   2402 C  CG  B ASP A 1 298 ? -5.831  -1.460  43.784  0.41 31.49  ? 521  ASP A CG  1 
ATOM   2403 O  OD1 A ASP A 1 298 ? -5.960  0.280   40.775  0.59 32.18  ? 521  ASP A OD1 1 
ATOM   2404 O  OD1 B ASP A 1 298 ? -6.616  -0.496  43.903  0.41 32.74  ? 521  ASP A OD1 1 
ATOM   2405 O  OD2 A ASP A 1 298 ? -7.445  -1.182  41.430  0.59 32.09  ? 521  ASP A OD2 1 
ATOM   2406 O  OD2 B ASP A 1 298 ? -5.596  -2.262  44.715  0.41 31.98  ? 521  ASP A OD2 1 
ATOM   2407 N  N   . SER A 1 299 ? -2.328  -1.918  43.706  1.00 25.50  ? 522  SER A N   1 
ATOM   2408 C  CA  . SER A 1 299 ? -1.518  -2.070  44.908  1.00 25.48  ? 522  SER A CA  1 
ATOM   2409 C  C   . SER A 1 299 ? -0.595  -3.273  44.769  1.00 24.55  ? 522  SER A C   1 
ATOM   2410 O  O   . SER A 1 299 ? -0.793  -4.145  43.917  1.00 24.78  ? 522  SER A O   1 
ATOM   2411 C  CB  . SER A 1 299 ? -2.396  -2.241  46.151  1.00 27.29  ? 522  SER A CB  1 
ATOM   2412 O  OG  . SER A 1 299 ? -3.291  -3.323  45.987  1.00 29.05  ? 522  SER A OG  1 
ATOM   2413 N  N   . TRP A 1 300 ? 0.410   -3.314  45.638  1.00 23.79  ? 523  TRP A N   1 
ATOM   2414 C  CA  . TRP A 1 300 ? 1.290   -4.471  45.742  1.00 23.12  ? 523  TRP A CA  1 
ATOM   2415 C  C   . TRP A 1 300 ? 0.696   -5.466  46.732  1.00 23.84  ? 523  TRP A C   1 
ATOM   2416 O  O   . TRP A 1 300 ? 0.331   -5.096  47.855  1.00 26.87  ? 523  TRP A O   1 
ATOM   2417 C  CB  . TRP A 1 300 ? 2.694   -4.049  46.183  1.00 23.91  ? 523  TRP A CB  1 
ATOM   2418 C  CG  . TRP A 1 300 ? 3.428   -3.248  45.149  1.00 24.44  ? 523  TRP A CG  1 
ATOM   2419 C  CD1 . TRP A 1 300 ? 3.608   -1.890  45.126  1.00 25.74  ? 523  TRP A CD1 1 
ATOM   2420 C  CD2 . TRP A 1 300 ? 4.070   -3.758  43.977  1.00 24.17  ? 523  TRP A CD2 1 
ATOM   2421 N  NE1 . TRP A 1 300 ? 4.323   -1.530  44.006  1.00 25.59  ? 523  TRP A NE1 1 
ATOM   2422 C  CE2 . TRP A 1 300 ? 4.619   -2.659  43.287  1.00 24.83  ? 523  TRP A CE2 1 
ATOM   2423 C  CE3 . TRP A 1 300 ? 4.234   -5.040  43.443  1.00 24.18  ? 523  TRP A CE3 1 
ATOM   2424 C  CZ2 . TRP A 1 300 ? 5.327   -2.804  42.099  1.00 25.29  ? 523  TRP A CZ2 1 
ATOM   2425 C  CZ3 . TRP A 1 300 ? 4.931   -5.181  42.256  1.00 24.76  ? 523  TRP A CZ3 1 
ATOM   2426 C  CH2 . TRP A 1 300 ? 5.464   -4.067  41.593  1.00 24.77  ? 523  TRP A CH2 1 
ATOM   2427 N  N   . VAL A 1 301 ? 0.602   -6.729  46.315  1.00 23.29  ? 524  VAL A N   1 
ATOM   2428 C  CA  . VAL A 1 301 ? 0.026   -7.785  47.141  1.00 24.06  ? 524  VAL A CA  1 
ATOM   2429 C  C   . VAL A 1 301 ? 0.980   -8.973  47.142  1.00 25.68  ? 524  VAL A C   1 
ATOM   2430 O  O   . VAL A 1 301 ? 2.160   -8.834  46.802  1.00 27.35  ? 524  VAL A O   1 
ATOM   2431 C  CB  . VAL A 1 301 ? -1.385  -8.172  46.652  1.00 23.54  ? 524  VAL A CB  1 
ATOM   2432 C  CG1 . VAL A 1 301 ? -2.327  -6.979  46.734  1.00 24.12  ? 524  VAL A CG1 1 
ATOM   2433 C  CG2 . VAL A 1 301 ? -1.344  -8.705  45.216  1.00 24.07  ? 524  VAL A CG2 1 
ATOM   2434 N  N   . SER A 1 302 ? 0.493   -10.144 47.529  1.00 28.29  ? 525  SER A N   1 
ATOM   2435 C  CA  . SER A 1 302 ? 1.327   -11.336 47.581  1.00 28.14  ? 525  SER A CA  1 
ATOM   2436 C  C   . SER A 1 302 ? 0.738   -12.423 46.694  1.00 26.18  ? 525  SER A C   1 
ATOM   2437 O  O   . SER A 1 302 ? -0.354  -12.285 46.138  1.00 25.31  ? 525  SER A O   1 
ATOM   2438 C  CB  . SER A 1 302 ? 1.453   -11.859 49.014  1.00 30.45  ? 525  SER A CB  1 
ATOM   2439 O  OG  . SER A 1 302 ? 0.248   -12.478 49.424  1.00 31.89  ? 525  SER A OG  1 
ATOM   2440 N  N   . GLN A 1 303 ? 1.476   -13.530 46.575  1.00 26.91  ? 526  GLN A N   1 
ATOM   2441 C  CA  . GLN A 1 303 ? 0.971   -14.665 45.814  1.00 28.76  ? 526  GLN A CA  1 
ATOM   2442 C  C   . GLN A 1 303 ? -0.228  -15.316 46.490  1.00 30.84  ? 526  GLN A C   1 
ATOM   2443 O  O   . GLN A 1 303 ? -0.950  -16.081 45.841  1.00 31.02  ? 526  GLN A O   1 
ATOM   2444 C  CB  . GLN A 1 303 ? 2.092   -15.677 45.555  1.00 29.83  ? 526  GLN A CB  1 
ATOM   2445 C  CG  . GLN A 1 303 ? 3.269   -15.068 44.799  1.00 31.61  ? 526  GLN A CG  1 
ATOM   2446 C  CD  . GLN A 1 303 ? 4.319   -16.081 44.404  1.00 32.33  ? 526  GLN A CD  1 
ATOM   2447 O  OE1 . GLN A 1 303 ? 4.034   -17.047 43.694  1.00 33.37  ? 526  GLN A OE1 1 
ATOM   2448 N  NE2 . GLN A 1 303 ? 5.547   -15.865 44.861  1.00 30.79  ? 526  GLN A NE2 1 
ATOM   2449 N  N   . PHE A 1 304 ? -0.463  -15.012 47.770  1.00 30.92  ? 527  PHE A N   1 
ATOM   2450 C  CA  . PHE A 1 304 ? -1.611  -15.530 48.501  1.00 32.95  ? 527  PHE A CA  1 
ATOM   2451 C  C   . PHE A 1 304 ? -2.886  -14.729 48.274  1.00 32.24  ? 527  PHE A C   1 
ATOM   2452 O  O   . PHE A 1 304 ? -3.946  -15.150 48.748  1.00 33.35  ? 527  PHE A O   1 
ATOM   2453 C  CB  . PHE A 1 304 ? -1.316  -15.562 50.006  1.00 35.61  ? 527  PHE A CB  1 
ATOM   2454 C  CG  . PHE A 1 304 ? -0.143  -16.412 50.380  1.00 39.96  ? 527  PHE A CG  1 
ATOM   2455 C  CD1 . PHE A 1 304 ? -0.242  -17.793 50.370  1.00 41.49  ? 527  PHE A CD1 1 
ATOM   2456 C  CD2 . PHE A 1 304 ? 1.057   -15.831 50.756  1.00 41.79  ? 527  PHE A CD2 1 
ATOM   2457 C  CE1 . PHE A 1 304 ? 0.837   -18.582 50.720  1.00 42.62  ? 527  PHE A CE1 1 
ATOM   2458 C  CE2 . PHE A 1 304 ? 2.142   -16.615 51.108  1.00 43.73  ? 527  PHE A CE2 1 
ATOM   2459 C  CZ  . PHE A 1 304 ? 2.030   -17.990 51.093  1.00 43.60  ? 527  PHE A CZ  1 
ATOM   2460 N  N   . TYR A 1 305 ? -2.820  -13.596 47.577  1.00 30.57  ? 528  TYR A N   1 
ATOM   2461 C  CA  . TYR A 1 305 ? -4.015  -12.785 47.375  1.00 30.55  ? 528  TYR A CA  1 
ATOM   2462 C  C   . TYR A 1 305 ? -5.071  -13.587 46.623  1.00 31.04  ? 528  TYR A C   1 
ATOM   2463 O  O   . TYR A 1 305 ? -4.765  -14.282 45.651  1.00 31.12  ? 528  TYR A O   1 
ATOM   2464 C  CB  . TYR A 1 305 ? -3.665  -11.513 46.603  1.00 31.20  ? 528  TYR A CB  1 
ATOM   2465 C  CG  . TYR A 1 305 ? -4.776  -10.489 46.585  1.00 32.16  ? 528  TYR A CG  1 
ATOM   2466 C  CD1 . TYR A 1 305 ? -4.877  -9.526  47.583  1.00 32.55  ? 528  TYR A CD1 1 
ATOM   2467 C  CD2 . TYR A 1 305 ? -5.728  -10.489 45.575  1.00 32.27  ? 528  TYR A CD2 1 
ATOM   2468 C  CE1 . TYR A 1 305 ? -5.892  -8.588  47.569  1.00 33.91  ? 528  TYR A CE1 1 
ATOM   2469 C  CE2 . TYR A 1 305 ? -6.747  -9.557  45.556  1.00 33.02  ? 528  TYR A CE2 1 
ATOM   2470 C  CZ  . TYR A 1 305 ? -6.825  -8.611  46.555  1.00 34.44  ? 528  TYR A CZ  1 
ATOM   2471 O  OH  . TYR A 1 305 ? -7.838  -7.682  46.535  1.00 36.54  ? 528  TYR A OH  1 
ATOM   2472 N  N   . SER A 1 306 ? -6.313  -13.512 47.091  1.00 32.06  ? 529  SER A N   1 
ATOM   2473 C  CA  . SER A 1 306 ? -7.415  -14.265 46.502  1.00 32.60  ? 529  SER A CA  1 
ATOM   2474 C  C   . SER A 1 306 ? -8.181  -13.337 45.568  1.00 31.24  ? 529  SER A C   1 
ATOM   2475 O  O   . SER A 1 306 ? -8.937  -12.475 46.026  1.00 32.51  ? 529  SER A O   1 
ATOM   2476 C  CB  . SER A 1 306 ? -8.329  -14.816 47.593  1.00 34.12  ? 529  SER A CB  1 
ATOM   2477 O  OG  . SER A 1 306 ? -9.303  -15.686 47.043  1.00 35.67  ? 529  SER A OG  1 
ATOM   2478 N  N   . LEU A 1 307 ? -7.989  -13.522 44.263  1.00 29.65  ? 530  LEU A N   1 
ATOM   2479 C  CA  . LEU A 1 307 ? -8.638  -12.677 43.272  1.00 28.86  ? 530  LEU A CA  1 
ATOM   2480 C  C   . LEU A 1 307 ? -10.133 -12.960 43.216  1.00 30.75  ? 530  LEU A C   1 
ATOM   2481 O  O   . LEU A 1 307 ? -10.580 -14.099 43.373  1.00 30.61  ? 530  LEU A O   1 
ATOM   2482 C  CB  . LEU A 1 307 ? -8.054  -12.947 41.885  1.00 26.94  ? 530  LEU A CB  1 
ATOM   2483 C  CG  . LEU A 1 307 ? -6.603  -12.561 41.597  1.00 26.60  ? 530  LEU A CG  1 
ATOM   2484 C  CD1 . LEU A 1 307 ? -6.159  -13.142 40.257  1.00 25.27  ? 530  LEU A CD1 1 
ATOM   2485 C  CD2 . LEU A 1 307 ? -6.430  -11.045 41.599  1.00 26.60  ? 530  LEU A CD2 1 
ATOM   2486 N  N   . ALA A 1 308 ? -10.906 -11.907 42.977  1.00 31.68  ? 531  ALA A N   1 
ATOM   2487 C  CA  . ALA A 1 308 ? -12.311 -12.085 42.654  1.00 33.59  ? 531  ALA A CA  1 
ATOM   2488 C  C   . ALA A 1 308 ? -12.444 -12.886 41.360  1.00 34.35  ? 531  ALA A C   1 
ATOM   2489 O  O   . ALA A 1 308 ? -11.734 -12.617 40.382  1.00 33.08  ? 531  ALA A O   1 
ATOM   2490 C  CB  . ALA A 1 308 ? -12.990 -10.724 42.489  1.00 34.26  ? 531  ALA A CB  1 
ATOM   2491 N  N   . PRO A 1 309 ? -13.330 -13.879 41.320  1.00 36.74  ? 532  PRO A N   1 
ATOM   2492 C  CA  . PRO A 1 309 ? -13.501 -14.673 40.099  1.00 39.63  ? 532  PRO A CA  1 
ATOM   2493 C  C   . PRO A 1 309 ? -14.029 -13.833 38.945  1.00 44.08  ? 532  PRO A C   1 
ATOM   2494 O  O   . PRO A 1 309 ? -14.577 -12.744 39.124  1.00 45.53  ? 532  PRO A O   1 
ATOM   2495 C  CB  . PRO A 1 309 ? -14.520 -15.745 40.511  1.00 38.94  ? 532  PRO A CB  1 
ATOM   2496 C  CG  . PRO A 1 309 ? -15.169 -15.215 41.757  1.00 38.54  ? 532  PRO A CG  1 
ATOM   2497 C  CD  . PRO A 1 309 ? -14.122 -14.404 42.445  1.00 37.57  ? 532  PRO A CD  1 
ATOM   2498 N  N   . MET A 1 310 ? -13.850 -14.360 37.738  1.00 46.22  ? 533  MET A N   1 
ATOM   2499 C  CA  . MET A 1 310 ? -14.408 -13.741 36.540  1.00 48.40  ? 533  MET A CA  1 
ATOM   2500 C  C   . MET A 1 310 ? -15.023 -14.802 35.637  1.00 48.92  ? 533  MET A C   1 
ATOM   2501 O  O   . MET A 1 310 ? -15.446 -15.858 36.110  1.00 49.13  ? 533  MET A O   1 
ATOM   2502 C  CB  . MET A 1 310 ? -13.342 -12.942 35.787  1.00 48.99  ? 533  MET A CB  1 
ATOM   2503 C  CG  . MET A 1 310 ? -12.003 -13.641 35.663  1.00 48.55  ? 533  MET A CG  1 
ATOM   2504 S  SD  . MET A 1 310 ? -10.912 -12.805 34.497  1.00 47.67  ? 533  MET A SD  1 
ATOM   2505 C  CE  . MET A 1 310 ? -11.518 -13.459 32.942  1.00 47.41  ? 533  MET A CE  1 
ATOM   2506 N  N   . SER B 1 1   ? 2.945   21.832  35.472  1.00 42.46  ? 224  SER B N   1 
ATOM   2507 C  CA  . SER B 1 1   ? 3.481   21.326  36.729  1.00 111.45 ? 224  SER B CA  1 
ATOM   2508 C  C   . SER B 1 1   ? 4.110   19.947  36.557  1.00 37.73  ? 224  SER B C   1 
ATOM   2509 O  O   . SER B 1 1   ? 5.047   19.595  37.273  1.00 74.41  ? 224  SER B O   1 
ATOM   2510 C  CB  . SER B 1 1   ? 2.391   21.278  37.803  1.00 43.44  ? 224  SER B CB  1 
ATOM   2511 N  N   . LYS B 1 2   ? 3.593   19.162  35.618  1.00 35.87  ? 225  LYS B N   1 
ATOM   2512 C  CA  . LYS B 1 2   ? 4.173   17.855  35.348  1.00 34.27  ? 225  LYS B CA  1 
ATOM   2513 C  C   . LYS B 1 2   ? 5.467   18.027  34.563  1.00 31.33  ? 225  LYS B C   1 
ATOM   2514 O  O   . LYS B 1 2   ? 5.453   18.646  33.492  1.00 31.37  ? 225  LYS B O   1 
ATOM   2515 C  CB  . LYS B 1 2   ? 3.205   16.986  34.559  1.00 35.59  ? 225  LYS B CB  1 
ATOM   2516 C  CG  . LYS B 1 2   ? 3.661   15.547  34.434  1.00 37.30  ? 225  LYS B CG  1 
ATOM   2517 C  CD  . LYS B 1 2   ? 2.550   14.661  33.890  1.00 38.65  ? 225  LYS B CD  1 
ATOM   2518 C  CE  . LYS B 1 2   ? 2.941   13.195  33.941  1.00 40.05  ? 225  LYS B CE  1 
ATOM   2519 N  NZ  . LYS B 1 2   ? 1.826   12.296  33.524  1.00 41.15  ? 225  LYS B NZ  1 
ATOM   2520 N  N   . PRO B 1 3   ? 6.592   17.509  35.048  1.00 29.89  ? 226  PRO B N   1 
ATOM   2521 C  CA  . PRO B 1 3   ? 7.859   17.700  34.336  1.00 28.70  ? 226  PRO B CA  1 
ATOM   2522 C  C   . PRO B 1 3   ? 7.889   16.948  33.014  1.00 25.99  ? 226  PRO B C   1 
ATOM   2523 O  O   . PRO B 1 3   ? 7.346   15.849  32.875  1.00 26.37  ? 226  PRO B O   1 
ATOM   2524 C  CB  . PRO B 1 3   ? 8.902   17.131  35.305  1.00 30.41  ? 226  PRO B CB  1 
ATOM   2525 C  CG  . PRO B 1 3   ? 8.224   17.109  36.640  1.00 32.78  ? 226  PRO B CG  1 
ATOM   2526 C  CD  . PRO B 1 3   ? 6.781   16.853  36.352  1.00 31.30  ? 226  PRO B CD  1 
ATOM   2527 N  N   . PHE B 1 4   ? 8.549   17.561  32.040  1.00 22.48  ? 227  PHE B N   1 
ATOM   2528 C  CA  . PHE B 1 4   ? 8.726   16.969  30.724  1.00 20.78  ? 227  PHE B CA  1 
ATOM   2529 C  C   . PHE B 1 4   ? 10.001  16.135  30.714  1.00 22.44  ? 227  PHE B C   1 
ATOM   2530 O  O   . PHE B 1 4   ? 11.038  16.569  31.227  1.00 24.78  ? 227  PHE B O   1 
ATOM   2531 C  CB  . PHE B 1 4   ? 8.823   18.086  29.690  1.00 19.78  ? 227  PHE B CB  1 
ATOM   2532 C  CG  . PHE B 1 4   ? 9.144   17.608  28.309  1.00 18.60  ? 227  PHE B CG  1 
ATOM   2533 C  CD1 . PHE B 1 4   ? 8.199   16.935  27.549  1.00 18.29  ? 227  PHE B CD1 1 
ATOM   2534 C  CD2 . PHE B 1 4   ? 10.392  17.842  27.762  1.00 19.27  ? 227  PHE B CD2 1 
ATOM   2535 C  CE1 . PHE B 1 4   ? 8.499   16.506  26.276  1.00 19.70  ? 227  PHE B CE1 1 
ATOM   2536 C  CE2 . PHE B 1 4   ? 10.696  17.412  26.484  1.00 19.01  ? 227  PHE B CE2 1 
ATOM   2537 C  CZ  . PHE B 1 4   ? 9.747   16.736  25.739  1.00 18.68  ? 227  PHE B CZ  1 
ATOM   2538 N  N   . THR B 1 5   ? 9.919   14.938  30.133  1.00 21.58  ? 228  THR B N   1 
ATOM   2539 C  CA  . THR B 1 5   ? 11.049  14.020  30.074  1.00 22.00  ? 228  THR B CA  1 
ATOM   2540 C  C   . THR B 1 5   ? 11.122  13.381  28.696  1.00 20.45  ? 228  THR B C   1 
ATOM   2541 O  O   . THR B 1 5   ? 10.143  13.345  27.947  1.00 21.14  ? 228  THR B O   1 
ATOM   2542 C  CB  . THR B 1 5   ? 10.947  12.907  31.126  1.00 24.41  ? 228  THR B CB  1 
ATOM   2543 O  OG1 . THR B 1 5   ? 9.737   12.163  30.921  1.00 26.19  ? 228  THR B OG1 1 
ATOM   2544 C  CG2 . THR B 1 5   ? 10.959  13.488  32.534  1.00 25.26  ? 228  THR B CG2 1 
ATOM   2545 N  N   . ILE B 1 6   ? 12.302  12.851  28.387  1.00 19.83  ? 229  ILE B N   1 
ATOM   2546 C  CA  . ILE B 1 6   ? 12.577  12.175  27.123  1.00 20.70  ? 229  ILE B CA  1 
ATOM   2547 C  C   . ILE B 1 6   ? 12.994  10.741  27.433  1.00 19.20  ? 229  ILE B C   1 
ATOM   2548 O  O   . ILE B 1 6   ? 13.735  10.513  28.397  1.00 18.59  ? 229  ILE B O   1 
ATOM   2549 C  CB  . ILE B 1 6   ? 13.655  12.934  26.337  1.00 23.43  ? 229  ILE B CB  1 
ATOM   2550 C  CG1 . ILE B 1 6   ? 13.144  14.338  26.012  1.00 26.51  ? 229  ILE B CG1 1 
ATOM   2551 C  CG2 . ILE B 1 6   ? 14.074  12.178  25.076  1.00 24.09  ? 229  ILE B CG2 1 
ATOM   2552 C  CD1 . ILE B 1 6   ? 14.125  15.144  25.311  1.00 29.91  ? 229  ILE B CD1 1 
ATOM   2553 N  N   . PRO B 1 7   ? 12.537  9.750   26.673  1.00 17.17  ? 230  PRO B N   1 
ATOM   2554 C  CA  . PRO B 1 7   ? 12.970  8.372   26.925  1.00 17.73  ? 230  PRO B CA  1 
ATOM   2555 C  C   . PRO B 1 7   ? 14.484  8.240   26.866  1.00 19.69  ? 230  PRO B C   1 
ATOM   2556 O  O   . PRO B 1 7   ? 15.175  9.021   26.205  1.00 20.21  ? 230  PRO B O   1 
ATOM   2557 C  CB  . PRO B 1 7   ? 12.306  7.584   25.794  1.00 17.46  ? 230  PRO B CB  1 
ATOM   2558 C  CG  . PRO B 1 7   ? 11.121  8.395   25.441  1.00 17.06  ? 230  PRO B CG  1 
ATOM   2559 C  CD  . PRO B 1 7   ? 11.576  9.822   25.560  1.00 17.10  ? 230  PRO B CD  1 
ATOM   2560 N  N   A ILE B 1 8   ? 14.999  7.229   27.564  0.51 19.36  ? 231  ILE B N   1 
ATOM   2561 N  N   B ILE B 1 8   ? 14.989  7.254   27.602  0.49 18.95  ? 231  ILE B N   1 
ATOM   2562 C  CA  A ILE B 1 8   ? 16.439  7.003   27.645  0.51 20.03  ? 231  ILE B CA  1 
ATOM   2563 C  CA  B ILE B 1 8   ? 16.418  6.984   27.680  0.49 19.49  ? 231  ILE B CA  1 
ATOM   2564 C  C   A ILE B 1 8   ? 16.922  6.025   26.576  0.51 18.68  ? 231  ILE B C   1 
ATOM   2565 C  C   B ILE B 1 8   ? 16.851  5.905   26.681  0.49 19.74  ? 231  ILE B C   1 
ATOM   2566 O  O   A ILE B 1 8   ? 18.097  5.642   26.559  0.51 19.02  ? 231  ILE B O   1 
ATOM   2567 O  O   B ILE B 1 8   ? 17.935  5.338   26.812  0.49 22.33  ? 231  ILE B O   1 
ATOM   2568 C  CB  A ILE B 1 8   ? 16.853  6.560   29.064  0.51 22.65  ? 231  ILE B CB  1 
ATOM   2569 C  CB  B ILE B 1 8   ? 16.867  6.665   29.116  0.49 20.88  ? 231  ILE B CB  1 
ATOM   2570 C  CG1 A ILE B 1 8   ? 15.932  5.449   29.580  0.51 23.55  ? 231  ILE B CG1 1 
ATOM   2571 C  CG1 B ILE B 1 8   ? 16.271  5.336   29.584  0.49 21.32  ? 231  ILE B CG1 1 
ATOM   2572 C  CG2 A ILE B 1 8   ? 16.825  7.744   30.020  0.51 23.05  ? 231  ILE B CG2 1 
ATOM   2573 C  CG2 B ILE B 1 8   ? 16.434  7.779   30.052  0.49 20.35  ? 231  ILE B CG2 1 
ATOM   2574 C  CD1 A ILE B 1 8   ? 16.322  4.049   29.147  0.51 24.19  ? 231  ILE B CD1 1 
ATOM   2575 C  CD1 B ILE B 1 8   ? 16.643  4.953   31.006  0.49 21.99  ? 231  ILE B CD1 1 
ATOM   2576 N  N   . LEU B 1 9   ? 16.026  5.626   25.674  1.00 16.82  ? 232  LEU B N   1 
ATOM   2577 C  CA  . LEU B 1 9   ? 16.337  4.591   24.687  1.00 16.10  ? 232  LEU B CA  1 
ATOM   2578 C  C   . LEU B 1 9   ? 17.423  5.046   23.714  1.00 14.60  ? 232  LEU B C   1 
ATOM   2579 O  O   . LEU B 1 9   ? 17.445  6.197   23.271  1.00 15.29  ? 232  LEU B O   1 
ATOM   2580 C  CB  . LEU B 1 9   ? 15.065  4.244   23.901  1.00 16.63  ? 232  LEU B CB  1 
ATOM   2581 C  CG  . LEU B 1 9   ? 13.918  3.659   24.733  1.00 17.35  ? 232  LEU B CG  1 
ATOM   2582 C  CD1 . LEU B 1 9   ? 12.633  3.586   23.927  1.00 19.44  ? 232  LEU B CD1 1 
ATOM   2583 C  CD2 . LEU B 1 9   ? 14.292  2.279   25.271  1.00 19.78  ? 232  LEU B CD2 1 
ATOM   2584 N  N   . THR B 1 10  ? 18.323  4.129   23.366  1.00 15.72  ? 233  THR B N   1 
ATOM   2585 C  CA  . THR B 1 10  ? 19.343  4.419   22.368  1.00 16.82  ? 233  THR B CA  1 
ATOM   2586 C  C   . THR B 1 10  ? 18.748  4.337   20.962  1.00 16.70  ? 233  THR B C   1 
ATOM   2587 O  O   . THR B 1 10  ? 17.625  3.864   20.755  1.00 16.39  ? 233  THR B O   1 
ATOM   2588 C  CB  . THR B 1 10  ? 20.507  3.436   22.488  1.00 19.18  ? 233  THR B CB  1 
ATOM   2589 O  OG1 . THR B 1 10  ? 20.077  2.143   22.046  1.00 20.62  ? 233  THR B OG1 1 
ATOM   2590 C  CG2 . THR B 1 10  ? 20.986  3.343   23.931  1.00 19.50  ? 233  THR B CG2 1 
ATOM   2591 N  N   . ILE B 1 11  ? 19.532  4.800   19.984  1.00 18.44  ? 234  ILE B N   1 
ATOM   2592 C  CA  . ILE B 1 11  ? 19.083  4.810   18.589  1.00 21.71  ? 234  ILE B CA  1 
ATOM   2593 C  C   . ILE B 1 11  ? 18.647  3.418   18.151  1.00 21.10  ? 234  ILE B C   1 
ATOM   2594 O  O   . ILE B 1 11  ? 17.575  3.236   17.555  1.00 21.76  ? 234  ILE B O   1 
ATOM   2595 C  CB  . ILE B 1 11  ? 20.191  5.370   17.678  1.00 25.15  ? 234  ILE B CB  1 
ATOM   2596 C  CG1 . ILE B 1 11  ? 20.352  6.869   17.906  1.00 26.38  ? 234  ILE B CG1 1 
ATOM   2597 C  CG2 . ILE B 1 11  ? 19.885  5.097   16.222  1.00 28.40  ? 234  ILE B CG2 1 
ATOM   2598 C  CD1 . ILE B 1 11  ? 19.103  7.658   17.571  1.00 25.98  ? 234  ILE B CD1 1 
ATOM   2599 N  N   . GLY B 1 12  ? 19.472  2.413   18.430  1.00 21.31  ? 235  GLY B N   1 
ATOM   2600 C  CA  . GLY B 1 12  ? 19.150  1.060   18.008  1.00 21.74  ? 235  GLY B CA  1 
ATOM   2601 C  C   . GLY B 1 12  ? 17.998  0.428   18.750  1.00 21.22  ? 235  GLY B C   1 
ATOM   2602 O  O   . GLY B 1 12  ? 17.558  -0.655  18.353  1.00 24.03  ? 235  GLY B O   1 
ATOM   2603 N  N   . GLU B 1 13  ? 17.499  1.071   19.802  1.00 18.06  ? 236  GLU B N   1 
ATOM   2604 C  CA  . GLU B 1 13  ? 16.358  0.593   20.568  1.00 16.60  ? 236  GLU B CA  1 
ATOM   2605 C  C   . GLU B 1 13  ? 15.062  1.283   20.172  1.00 14.72  ? 236  GLU B C   1 
ATOM   2606 O  O   . GLU B 1 13  ? 14.063  1.157   20.888  1.00 17.38  ? 236  GLU B O   1 
ATOM   2607 C  CB  . GLU B 1 13  ? 16.615  0.810   22.063  1.00 17.94  ? 236  GLU B CB  1 
ATOM   2608 C  CG  . GLU B 1 13  ? 17.781  -0.008  22.588  1.00 18.81  ? 236  GLU B CG  1 
ATOM   2609 C  CD  . GLU B 1 13  ? 18.221  0.376   23.998  1.00 20.48  ? 236  GLU B CD  1 
ATOM   2610 O  OE1 . GLU B 1 13  ? 17.887  1.472   24.493  1.00 20.48  ? 236  GLU B OE1 1 
ATOM   2611 O  OE2 . GLU B 1 13  ? 18.938  -0.437  24.613  1.00 22.91  ? 236  GLU B OE2 1 
ATOM   2612 N  N   . MET B 1 14  ? 15.046  2.004   19.054  1.00 13.38  ? 237  MET B N   1 
ATOM   2613 C  CA  . MET B 1 14  ? 13.875  2.775   18.667  1.00 11.98  ? 237  MET B CA  1 
ATOM   2614 C  C   . MET B 1 14  ? 13.493  2.528   17.210  1.00 11.16  ? 237  MET B C   1 
ATOM   2615 O  O   . MET B 1 14  ? 14.273  1.995   16.413  1.00 12.31  ? 237  MET B O   1 
ATOM   2616 C  CB  . MET B 1 14  ? 14.078  4.265   18.943  1.00 13.19  ? 237  MET B CB  1 
ATOM   2617 C  CG  . MET B 1 14  ? 14.138  4.554   20.432  1.00 14.21  ? 237  MET B CG  1 
ATOM   2618 S  SD  . MET B 1 14  ? 14.079  6.319   20.834  1.00 15.32  ? 237  MET B SD  1 
ATOM   2619 C  CE  . MET B 1 14  ? 15.636  6.894   20.161  1.00 15.08  ? 237  MET B CE  1 
ATOM   2620 N  N   . THR B 1 15  ? 12.263  2.921   16.881  1.00 11.15  ? 238  THR B N   1 
ATOM   2621 C  CA  . THR B 1 15  ? 11.623  2.585   15.621  1.00 10.21  ? 238  THR B CA  1 
ATOM   2622 C  C   . THR B 1 15  ? 11.328  3.859   14.855  1.00 10.34  ? 238  THR B C   1 
ATOM   2623 O  O   . THR B 1 15  ? 10.878  4.856   15.433  1.00 11.07  ? 238  THR B O   1 
ATOM   2624 C  CB  . THR B 1 15  ? 10.297  1.847   15.876  1.00 11.59  ? 238  THR B CB  1 
ATOM   2625 O  OG1 . THR B 1 15  ? 10.531  0.751   16.773  1.00 13.21  ? 238  THR B OG1 1 
ATOM   2626 C  CG2 . THR B 1 15  ? 9.675   1.353   14.572  1.00 12.23  ? 238  THR B CG2 1 
ATOM   2627 N  N   . ASN B 1 16  ? 11.568  3.821   13.550  1.00 9.73   ? 239  ASN B N   1 
ATOM   2628 C  CA  . ASN B 1 16  ? 11.172  4.925   12.688  1.00 10.22  ? 239  ASN B CA  1 
ATOM   2629 C  C   . ASN B 1 16  ? 9.655   5.099   12.742  1.00 10.74  ? 239  ASN B C   1 
ATOM   2630 O  O   . ASN B 1 16  ? 8.904   4.125   12.698  1.00 12.12  ? 239  ASN B O   1 
ATOM   2631 C  CB  . ASN B 1 16  ? 11.621  4.611   11.258  1.00 10.30  ? 239  ASN B CB  1 
ATOM   2632 C  CG  . ASN B 1 16  ? 11.687  5.844   10.387  1.00 10.93  ? 239  ASN B CG  1 
ATOM   2633 O  OD1 . ASN B 1 16  ? 10.665  6.482   10.119  1.00 12.03  ? 239  ASN B OD1 1 
ATOM   2634 N  ND2 . ASN B 1 16  ? 12.896  6.209   9.965   1.00 11.53  ? 239  ASN B ND2 1 
ATOM   2635 N  N   . SER B 1 17  ? 9.202   6.343   12.875  1.00 10.32  ? 240  SER B N   1 
ATOM   2636 C  CA  . SER B 1 17  ? 7.773   6.616   12.970  1.00 9.88   ? 240  SER B CA  1 
ATOM   2637 C  C   . SER B 1 17  ? 7.110   6.818   11.609  1.00 9.36   ? 240  SER B C   1 
ATOM   2638 O  O   . SER B 1 17  ? 5.899   7.068   11.552  1.00 10.81  ? 240  SER B O   1 
ATOM   2639 C  CB  . SER B 1 17  ? 7.520   7.798   13.910  1.00 10.04  ? 240  SER B CB  1 
ATOM   2640 O  OG  . SER B 1 17  ? 8.211   8.946   13.442  1.00 11.00  ? 240  SER B OG  1 
ATOM   2641 N  N   . ARG B 1 18  ? 7.863   6.700   10.512  1.00 10.19  ? 241  ARG B N   1 
ATOM   2642 C  CA  . ARG B 1 18  ? 7.287   6.771   9.172   1.00 10.64  ? 241  ARG B CA  1 
ATOM   2643 C  C   . ARG B 1 18  ? 7.369   5.455   8.411   1.00 11.05  ? 241  ARG B C   1 
ATOM   2644 O  O   . ARG B 1 18  ? 6.793   5.345   7.322   1.00 11.60  ? 241  ARG B O   1 
ATOM   2645 C  CB  . ARG B 1 18  ? 7.941   7.899   8.361   1.00 10.53  ? 241  ARG B CB  1 
ATOM   2646 C  CG  . ARG B 1 18  ? 7.606   9.276   8.920   1.00 10.02  ? 241  ARG B CG  1 
ATOM   2647 C  CD  . ARG B 1 18  ? 8.260   10.389  8.111   1.00 9.89   ? 241  ARG B CD  1 
ATOM   2648 N  NE  . ARG B 1 18  ? 7.685   10.444  6.770   1.00 11.13  ? 241  ARG B NE  1 
ATOM   2649 C  CZ  . ARG B 1 18  ? 8.357   10.783  5.677   1.00 10.65  ? 241  ARG B CZ  1 
ATOM   2650 N  NH1 . ARG B 1 18  ? 9.625   11.148  5.731   1.00 11.53  ? 241  ARG B NH1 1 
ATOM   2651 N  NH2 . ARG B 1 18  ? 7.749   10.736  4.494   1.00 11.66  ? 241  ARG B NH2 1 
ATOM   2652 N  N   . PHE B 1 19  ? 8.057   4.449   8.960   1.00 10.84  ? 242  PHE B N   1 
ATOM   2653 C  CA  . PHE B 1 19  ? 8.116   3.143   8.324   1.00 11.07  ? 242  PHE B CA  1 
ATOM   2654 C  C   . PHE B 1 19  ? 8.508   2.152   9.406   1.00 10.61  ? 242  PHE B C   1 
ATOM   2655 O  O   . PHE B 1 19  ? 9.352   2.485   10.247  1.00 11.81  ? 242  PHE B O   1 
ATOM   2656 C  CB  . PHE B 1 19  ? 9.122   3.121   7.164   1.00 11.16  ? 242  PHE B CB  1 
ATOM   2657 C  CG  . PHE B 1 19  ? 8.907   1.972   6.232   1.00 11.88  ? 242  PHE B CG  1 
ATOM   2658 C  CD1 . PHE B 1 19  ? 7.929   2.051   5.269   1.00 12.61  ? 242  PHE B CD1 1 
ATOM   2659 C  CD2 . PHE B 1 19  ? 9.648   0.794   6.348   1.00 11.80  ? 242  PHE B CD2 1 
ATOM   2660 C  CE1 . PHE B 1 19  ? 7.683   0.997   4.415   1.00 14.62  ? 242  PHE B CE1 1 
ATOM   2661 C  CE2 . PHE B 1 19  ? 9.406   -0.270  5.498   1.00 13.70  ? 242  PHE B CE2 1 
ATOM   2662 C  CZ  . PHE B 1 19  ? 8.418   -0.166  4.530   1.00 15.12  ? 242  PHE B CZ  1 
ATOM   2663 N  N   . PRO B 1 20  ? 7.913   0.951   9.443   1.00 9.88   ? 243  PRO B N   1 
ATOM   2664 C  CA  . PRO B 1 20  ? 8.119   0.050   10.609  1.00 10.80  ? 243  PRO B CA  1 
ATOM   2665 C  C   . PRO B 1 20  ? 9.442   -0.705  10.567  1.00 11.88  ? 243  PRO B C   1 
ATOM   2666 O  O   . PRO B 1 20  ? 9.518   -1.921  10.320  1.00 13.07  ? 243  PRO B O   1 
ATOM   2667 C  CB  . PRO B 1 20  ? 6.903   -0.876  10.520  1.00 11.45  ? 243  PRO B CB  1 
ATOM   2668 C  CG  . PRO B 1 20  ? 6.657   -1.003  9.040   1.00 11.99  ? 243  PRO B CG  1 
ATOM   2669 C  CD  . PRO B 1 20  ? 6.900   0.411   8.507   1.00 11.39  ? 243  PRO B CD  1 
ATOM   2670 N  N   . VAL B 1 21  ? 10.523  0.030   10.835  1.00 11.65  ? 244  VAL B N   1 
ATOM   2671 C  CA  . VAL B 1 21  ? 11.876  -0.505  10.890  1.00 11.54  ? 244  VAL B CA  1 
ATOM   2672 C  C   . VAL B 1 21  ? 12.639  0.257   11.967  1.00 10.25  ? 244  VAL B C   1 
ATOM   2673 O  O   . VAL B 1 21  ? 12.302  1.392   12.316  1.00 11.83  ? 244  VAL B O   1 
ATOM   2674 C  CB  . VAL B 1 21  ? 12.608  -0.389  9.539   1.00 12.50  ? 244  VAL B CB  1 
ATOM   2675 C  CG1 . VAL B 1 21  ? 11.988  -1.351  8.497   1.00 14.19  ? 244  VAL B CG1 1 
ATOM   2676 C  CG2 . VAL B 1 21  ? 12.615  1.063   9.056   1.00 13.58  ? 244  VAL B CG2 1 
ATOM   2677 N  N   . ALA B 1 22  ? 13.682  -0.372  12.498  1.00 10.61  ? 245  ALA B N   1 
ATOM   2678 C  CA  . ALA B 1 22  ? 14.522  0.301   13.479  1.00 10.85  ? 245  ALA B CA  1 
ATOM   2679 C  C   . ALA B 1 22  ? 15.177  1.531   12.864  1.00 11.32  ? 245  ALA B C   1 
ATOM   2680 O  O   . ALA B 1 22  ? 15.410  1.598   11.656  1.00 12.22  ? 245  ALA B O   1 
ATOM   2681 C  CB  . ALA B 1 22  ? 15.611  -0.640  13.976  1.00 13.17  ? 245  ALA B CB  1 
ATOM   2682 N  N   . ILE B 1 23  ? 15.467  2.518   13.710  1.00 11.19  ? 246  ILE B N   1 
ATOM   2683 C  CA  . ILE B 1 23  ? 16.257  3.671   13.284  1.00 11.30  ? 246  ILE B CA  1 
ATOM   2684 C  C   . ILE B 1 23  ? 17.695  3.226   13.063  1.00 12.02  ? 246  ILE B C   1 
ATOM   2685 O  O   . ILE B 1 23  ? 18.269  2.505   13.895  1.00 13.37  ? 246  ILE B O   1 
ATOM   2686 C  CB  . ILE B 1 23  ? 16.167  4.784   14.341  1.00 12.41  ? 246  ILE B CB  1 
ATOM   2687 C  CG1 . ILE B 1 23  ? 14.717  5.273   14.437  1.00 13.96  ? 246  ILE B CG1 1 
ATOM   2688 C  CG2 . ILE B 1 23  ? 17.131  5.943   14.031  1.00 12.20  ? 246  ILE B CG2 1 
ATOM   2689 C  CD1 . ILE B 1 23  ? 14.415  6.115   15.640  1.00 15.29  ? 246  ILE B CD1 1 
ATOM   2690 N  N   . ASP B 1 24  ? 18.283  3.638   11.938  1.00 12.02  ? 247  ASP B N   1 
ATOM   2691 C  CA  . ASP B 1 24  ? 19.678  3.310   11.655  1.00 13.65  ? 247  ASP B CA  1 
ATOM   2692 C  C   . ASP B 1 24  ? 20.672  4.369   12.134  1.00 15.02  ? 247  ASP B C   1 
ATOM   2693 O  O   . ASP B 1 24  ? 21.772  4.022   12.586  1.00 16.83  ? 247  ASP B O   1 
ATOM   2694 C  CB  . ASP B 1 24  ? 19.870  3.094   10.159  1.00 14.79  ? 247  ASP B CB  1 
ATOM   2695 C  CG  . ASP B 1 24  ? 19.153  1.857   9.653   1.00 16.22  ? 247  ASP B CG  1 
ATOM   2696 O  OD1 . ASP B 1 24  ? 19.184  0.816   10.341  1.00 20.74  ? 247  ASP B OD1 1 
ATOM   2697 O  OD2 . ASP B 1 24  ? 18.567  1.897   8.557   1.00 16.89  ? 247  ASP B OD2 1 
ATOM   2698 N  N   A MET B 1 25  ? 20.304  5.648   12.075  0.75 13.13  ? 248  MET B N   1 
ATOM   2699 N  N   B MET B 1 25  ? 20.339  5.651   12.033  0.25 14.41  ? 248  MET B N   1 
ATOM   2700 C  CA  A MET B 1 25  ? 21.264  6.711   12.346  0.75 12.74  ? 248  MET B CA  1 
ATOM   2701 C  CA  B MET B 1 25  ? 21.278  6.679   12.469  0.25 14.23  ? 248  MET B CA  1 
ATOM   2702 C  C   A MET B 1 25  ? 20.518  8.017   12.561  0.75 12.76  ? 248  MET B C   1 
ATOM   2703 C  C   B MET B 1 25  ? 20.564  8.019   12.516  0.25 13.26  ? 248  MET B C   1 
ATOM   2704 O  O   A MET B 1 25  ? 19.363  8.168   12.146  0.75 13.34  ? 248  MET B O   1 
ATOM   2705 O  O   B MET B 1 25  ? 19.476  8.191   11.959  0.25 13.10  ? 248  MET B O   1 
ATOM   2706 C  CB  A MET B 1 25  ? 22.227  6.896   11.171  0.75 14.95  ? 248  MET B CB  1 
ATOM   2707 C  CB  B MET B 1 25  ? 22.500  6.780   11.550  0.25 15.55  ? 248  MET B CB  1 
ATOM   2708 C  CG  A MET B 1 25  ? 21.555  7.471   9.929   0.75 17.15  ? 248  MET B CG  1 
ATOM   2709 C  CG  B MET B 1 25  ? 22.199  7.357   10.182  0.25 16.10  ? 248  MET B CG  1 
ATOM   2710 S  SD  A MET B 1 25  ? 22.661  7.647   8.513   0.75 20.95  ? 248  MET B SD  1 
ATOM   2711 S  SD  B MET B 1 25  ? 21.341  6.191   9.115   0.25 17.09  ? 248  MET B SD  1 
ATOM   2712 C  CE  A MET B 1 25  ? 23.089  5.934   8.237   0.75 22.54  ? 248  MET B CE  1 
ATOM   2713 C  CE  B MET B 1 25  ? 22.646  5.010   8.775   0.25 16.07  ? 248  MET B CE  1 
ATOM   2714 N  N   . LEU B 1 26  ? 21.207  8.968   13.188  1.00 12.34  ? 249  LEU B N   1 
ATOM   2715 C  CA  . LEU B 1 26  ? 20.798  10.366  13.141  1.00 11.93  ? 249  LEU B CA  1 
ATOM   2716 C  C   . LEU B 1 26  ? 21.391  10.990  11.884  1.00 13.24  ? 249  LEU B C   1 
ATOM   2717 O  O   . LEU B 1 26  ? 22.482  10.613  11.443  1.00 14.64  ? 249  LEU B O   1 
ATOM   2718 C  CB  . LEU B 1 26  ? 21.361  11.106  14.355  1.00 13.09  ? 249  LEU B CB  1 
ATOM   2719 C  CG  . LEU B 1 26  ? 20.876  10.666  15.733  1.00 15.06  ? 249  LEU B CG  1 
ATOM   2720 C  CD1 . LEU B 1 26  ? 21.665  11.373  16.829  1.00 15.87  ? 249  LEU B CD1 1 
ATOM   2721 C  CD2 . LEU B 1 26  ? 19.399  10.965  15.866  1.00 18.76  ? 249  LEU B CD2 1 
ATOM   2722 N  N   . HIS B 1 27  ? 20.664  11.940  11.288  1.00 13.71  ? 250  HIS B N   1 
ATOM   2723 C  CA  . HIS B 1 27  ? 21.149  12.549  10.054  1.00 15.12  ? 250  HIS B CA  1 
ATOM   2724 C  C   . HIS B 1 27  ? 20.607  13.965  9.944   1.00 14.27  ? 250  HIS B C   1 
ATOM   2725 O  O   . HIS B 1 27  ? 19.494  14.255  10.384  1.00 15.62  ? 250  HIS B O   1 
ATOM   2726 C  CB  . HIS B 1 27  ? 20.751  11.717  8.820   1.00 15.60  ? 250  HIS B CB  1 
ATOM   2727 C  CG  . HIS B 1 27  ? 21.585  11.986  7.609   1.00 17.94  ? 250  HIS B CG  1 
ATOM   2728 N  ND1 . HIS B 1 27  ? 21.345  13.044  6.758   1.00 19.46  ? 250  HIS B ND1 1 
ATOM   2729 C  CD2 . HIS B 1 27  ? 22.642  11.317  7.086   1.00 19.57  ? 250  HIS B CD2 1 
ATOM   2730 C  CE1 . HIS B 1 27  ? 22.230  13.029  5.780   1.00 20.97  ? 250  HIS B CE1 1 
ATOM   2731 N  NE2 . HIS B 1 27  ? 23.029  11.992  5.953   1.00 21.09  ? 250  HIS B NE2 1 
ATOM   2732 N  N   . THR B 1 28  ? 21.413  14.858  9.374   1.00 14.44  ? 251  THR B N   1 
ATOM   2733 C  CA  . THR B 1 28  ? 20.956  16.213  9.120   1.00 15.58  ? 251  THR B CA  1 
ATOM   2734 C  C   . THR B 1 28  ? 21.265  16.591  7.682   1.00 17.36  ? 251  THR B C   1 
ATOM   2735 O  O   . THR B 1 28  ? 22.242  16.120  7.098   1.00 19.16  ? 251  THR B O   1 
ATOM   2736 C  CB  . THR B 1 28  ? 21.555  17.227  10.125  1.00 16.79  ? 251  THR B CB  1 
ATOM   2737 O  OG1 . THR B 1 28  ? 20.938  18.509  9.946   1.00 17.10  ? 251  THR B OG1 1 
ATOM   2738 C  CG2 . THR B 1 28  ? 23.066  17.394  9.959   1.00 17.85  ? 251  THR B CG2 1 
ATOM   2739 N  N   A SER B 1 29  ? 20.411  17.433  7.107   0.32 19.08  ? 252  SER B N   1 
ATOM   2740 N  N   B SER B 1 29  ? 20.420  17.440  7.111   0.68 19.67  ? 252  SER B N   1 
ATOM   2741 C  CA  A SER B 1 29  ? 20.573  17.879  5.730   0.32 20.51  ? 252  SER B CA  1 
ATOM   2742 C  CA  B SER B 1 29  ? 20.644  17.908  5.753   0.68 21.71  ? 252  SER B CA  1 
ATOM   2743 C  C   A SER B 1 29  ? 19.899  19.234  5.585   0.32 21.00  ? 252  SER B C   1 
ATOM   2744 C  C   B SER B 1 29  ? 19.891  19.213  5.560   0.68 21.40  ? 252  SER B C   1 
ATOM   2745 O  O   A SER B 1 29  ? 18.989  19.564  6.355   0.32 19.87  ? 252  SER B O   1 
ATOM   2746 O  O   B SER B 1 29  ? 18.922  19.491  6.277   0.68 19.34  ? 252  SER B O   1 
ATOM   2747 C  CB  A SER B 1 29  ? 19.936  16.882  4.746   0.32 21.71  ? 252  SER B CB  1 
ATOM   2748 C  CB  B SER B 1 29  ? 20.182  16.866  4.722   0.68 24.94  ? 252  SER B CB  1 
ATOM   2749 O  OG  A SER B 1 29  ? 20.333  15.550  5.019   0.32 21.72  ? 252  SER B OG  1 
ATOM   2750 O  OG  B SER B 1 29  ? 18.842  16.475  4.944   0.68 25.15  ? 252  SER B OG  1 
ATOM   2751 N  N   . PRO B 1 30  ? 20.323  20.044  4.614   1.00 22.37  ? 253  PRO B N   1 
ATOM   2752 C  CA  . PRO B 1 30  ? 19.535  21.229  4.259   1.00 22.13  ? 253  PRO B CA  1 
ATOM   2753 C  C   . PRO B 1 30  ? 18.235  20.790  3.600   1.00 20.88  ? 253  PRO B C   1 
ATOM   2754 O  O   . PRO B 1 30  ? 18.220  19.904  2.742   1.00 22.01  ? 253  PRO B O   1 
ATOM   2755 C  CB  . PRO B 1 30  ? 20.440  21.978  3.270   1.00 25.09  ? 253  PRO B CB  1 
ATOM   2756 C  CG  . PRO B 1 30  ? 21.353  20.927  2.734   1.00 27.47  ? 253  PRO B CG  1 
ATOM   2757 C  CD  . PRO B 1 30  ? 21.576  19.955  3.846   1.00 26.05  ? 253  PRO B CD  1 
ATOM   2758 N  N   . THR B 1 31  ? 17.137  21.401  4.022   1.00 17.37  ? 254  THR B N   1 
ATOM   2759 C  CA  . THR B 1 31  ? 15.824  21.030  3.515   1.00 17.04  ? 254  THR B CA  1 
ATOM   2760 C  C   . THR B 1 31  ? 15.007  22.242  3.107   1.00 16.53  ? 254  THR B C   1 
ATOM   2761 O  O   . THR B 1 31  ? 13.809  22.102  2.844   1.00 16.97  ? 254  THR B O   1 
ATOM   2762 C  CB  . THR B 1 31  ? 15.044  20.185  4.532   1.00 19.96  ? 254  THR B CB  1 
ATOM   2763 O  OG1 . THR B 1 31  ? 14.925  20.900  5.771   1.00 20.08  ? 254  THR B OG1 1 
ATOM   2764 C  CG2 . THR B 1 31  ? 15.742  18.841  4.778   1.00 21.07  ? 254  THR B CG2 1 
ATOM   2765 N  N   . ASP B 1 32  ? 15.619  23.422  3.040   1.00 17.62  ? 255  ASP B N   1 
ATOM   2766 C  CA  . ASP B 1 32  ? 14.835  24.613  2.733   1.00 19.63  ? 255  ASP B CA  1 
ATOM   2767 C  C   . ASP B 1 32  ? 14.228  24.579  1.336   1.00 17.18  ? 255  ASP B C   1 
ATOM   2768 O  O   . ASP B 1 32  ? 13.288  25.330  1.070   1.00 18.29  ? 255  ASP B O   1 
ATOM   2769 C  CB  . ASP B 1 32  ? 15.640  25.883  3.001   1.00 25.68  ? 255  ASP B CB  1 
ATOM   2770 C  CG  . ASP B 1 32  ? 15.975  26.051  4.477   1.00 31.04  ? 255  ASP B CG  1 
ATOM   2771 O  OD1 . ASP B 1 32  ? 15.575  25.183  5.288   1.00 31.91  ? 255  ASP B OD1 1 
ATOM   2772 O  OD2 . ASP B 1 32  ? 16.640  27.047  4.831   1.00 34.80  ? 255  ASP B OD2 1 
ATOM   2773 N  N   . ASN B 1 33  ? 14.699  23.706  0.452   1.00 15.28  ? 256  ASN B N   1 
ATOM   2774 C  CA  . ASN B 1 33  ? 14.077  23.577  -0.857  1.00 17.14  ? 256  ASN B CA  1 
ATOM   2775 C  C   . ASN B 1 33  ? 13.007  22.488  -0.914  1.00 14.95  ? 256  ASN B C   1 
ATOM   2776 O  O   . ASN B 1 33  ? 12.378  22.315  -1.965  1.00 15.02  ? 256  ASN B O   1 
ATOM   2777 C  CB  . ASN B 1 33  ? 15.148  23.412  -1.935  1.00 21.82  ? 256  ASN B CB  1 
ATOM   2778 C  CG  . ASN B 1 33  ? 16.004  24.663  -2.083  1.00 26.63  ? 256  ASN B CG  1 
ATOM   2779 O  OD1 . ASN B 1 33  ? 15.543  25.776  -1.820  1.00 27.30  ? 256  ASN B OD1 1 
ATOM   2780 N  ND2 . ASN B 1 33  ? 17.246  24.487  -2.505  1.00 29.56  ? 256  ASN B ND2 1 
ATOM   2781 N  N   . PHE B 1 34  ? 12.762  21.791  0.197   1.00 14.36  ? 257  PHE B N   1 
ATOM   2782 C  CA  . PHE B 1 34  ? 11.645  20.867  0.330   1.00 12.90  ? 257  PHE B CA  1 
ATOM   2783 C  C   . PHE B 1 34  ? 10.537  21.492  1.176   1.00 13.46  ? 257  PHE B C   1 
ATOM   2784 O  O   . PHE B 1 34  ? 10.744  22.469  1.906   1.00 14.01  ? 257  PHE B O   1 
ATOM   2785 C  CB  . PHE B 1 34  ? 12.088  19.554  0.998   1.00 14.51  ? 257  PHE B CB  1 
ATOM   2786 C  CG  . PHE B 1 34  ? 13.036  18.726  0.175   1.00 14.39  ? 257  PHE B CG  1 
ATOM   2787 C  CD1 . PHE B 1 34  ? 12.599  18.070  -0.975  1.00 14.70  ? 257  PHE B CD1 1 
ATOM   2788 C  CD2 . PHE B 1 34  ? 14.354  18.559  0.574   1.00 18.13  ? 257  PHE B CD2 1 
ATOM   2789 C  CE1 . PHE B 1 34  ? 13.469  17.298  -1.727  1.00 17.34  ? 257  PHE B CE1 1 
ATOM   2790 C  CE2 . PHE B 1 34  ? 15.235  17.786  -0.174  1.00 20.79  ? 257  PHE B CE2 1 
ATOM   2791 C  CZ  . PHE B 1 34  ? 14.790  17.150  -1.324  1.00 19.33  ? 257  PHE B CZ  1 
ATOM   2792 N  N   . ILE B 1 35  ? 9.344   20.924  1.056   1.00 12.90  ? 258  ILE B N   1 
ATOM   2793 C  CA  . ILE B 1 35  ? 8.249   21.172  1.987   1.00 11.98  ? 258  ILE B CA  1 
ATOM   2794 C  C   . ILE B 1 35  ? 8.214   19.952  2.901   1.00 11.33  ? 258  ILE B C   1 
ATOM   2795 O  O   . ILE B 1 35  ? 7.762   18.878  2.501   1.00 13.51  ? 258  ILE B O   1 
ATOM   2796 C  CB  . ILE B 1 35  ? 6.920   21.386  1.259   1.00 13.74  ? 258  ILE B CB  1 
ATOM   2797 C  CG1 . ILE B 1 35  ? 7.064   22.502  0.215   1.00 14.67  ? 258  ILE B CG1 1 
ATOM   2798 C  CG2 . ILE B 1 35  ? 5.807   21.692  2.269   1.00 15.57  ? 258  ILE B CG2 1 
ATOM   2799 C  CD1 . ILE B 1 35  ? 6.023   22.436  -0.870  1.00 16.17  ? 258  ILE B CD1 1 
ATOM   2800 N  N   . VAL B 1 36  ? 8.728   20.100  4.122   1.00 11.16  ? 259  VAL B N   1 
ATOM   2801 C  CA  . VAL B 1 36  ? 8.879   18.975  5.053   1.00 11.11  ? 259  VAL B CA  1 
ATOM   2802 C  C   . VAL B 1 36  ? 7.588   18.903  5.861   1.00 10.94  ? 259  VAL B C   1 
ATOM   2803 O  O   . VAL B 1 36  ? 7.421   19.593  6.873   1.00 12.41  ? 259  VAL B O   1 
ATOM   2804 C  CB  . VAL B 1 36  ? 10.106  19.146  5.942   1.00 12.38  ? 259  VAL B CB  1 
ATOM   2805 C  CG1 . VAL B 1 36  ? 10.218  17.970  6.891   1.00 12.57  ? 259  VAL B CG1 1 
ATOM   2806 C  CG2 . VAL B 1 36  ? 11.351  19.277  5.091   1.00 13.60  ? 259  VAL B CG2 1 
ATOM   2807 N  N   . GLN B 1 37  ? 6.661   18.053  5.411   1.00 11.50  ? 260  GLN B N   1 
ATOM   2808 C  CA  . GLN B 1 37  ? 5.327   17.974  6.005   1.00 11.17  ? 260  GLN B CA  1 
ATOM   2809 C  C   . GLN B 1 37  ? 4.885   16.520  6.136   1.00 11.40  ? 260  GLN B C   1 
ATOM   2810 O  O   . GLN B 1 37  ? 3.798   16.149  5.689   1.00 11.69  ? 260  GLN B O   1 
ATOM   2811 C  CB  . GLN B 1 37  ? 4.336   18.790  5.170   1.00 11.88  ? 260  GLN B CB  1 
ATOM   2812 C  CG  . GLN B 1 37  ? 3.012   19.060  5.841   1.00 13.27  ? 260  GLN B CG  1 
ATOM   2813 C  CD  . GLN B 1 37  ? 2.208   20.170  5.188   1.00 15.49  ? 260  GLN B CD  1 
ATOM   2814 O  OE1 . GLN B 1 37  ? 2.545   20.674  4.103   1.00 17.42  ? 260  GLN B OE1 1 
ATOM   2815 N  NE2 . GLN B 1 37  ? 1.133   20.568  5.854   1.00 15.65  ? 260  GLN B NE2 1 
ATOM   2816 N  N   . PRO B 1 38  ? 5.695   15.663  6.775   1.00 10.98  ? 261  PRO B N   1 
ATOM   2817 C  CA  . PRO B 1 38  ? 5.260   14.271  6.967   1.00 11.05  ? 261  PRO B CA  1 
ATOM   2818 C  C   . PRO B 1 38  ? 3.992   14.208  7.808   1.00 10.61  ? 261  PRO B C   1 
ATOM   2819 O  O   . PRO B 1 38  ? 3.719   15.079  8.641   1.00 11.40  ? 261  PRO B O   1 
ATOM   2820 C  CB  . PRO B 1 38  ? 6.451   13.615  7.682   1.00 11.82  ? 261  PRO B CB  1 
ATOM   2821 C  CG  . PRO B 1 38  ? 7.110   14.770  8.440   1.00 11.66  ? 261  PRO B CG  1 
ATOM   2822 C  CD  . PRO B 1 38  ? 6.957   15.955  7.511   1.00 11.82  ? 261  PRO B CD  1 
ATOM   2823 N  N   . GLN B 1 39  ? 3.211   13.154  7.582   1.00 10.58  ? 262  GLN B N   1 
ATOM   2824 C  CA  . GLN B 1 39  ? 1.960   12.952  8.301   1.00 10.71  ? 262  GLN B CA  1 
ATOM   2825 C  C   . GLN B 1 39  ? 1.989   11.799  9.290   1.00 11.76  ? 262  GLN B C   1 
ATOM   2826 O  O   . GLN B 1 39  ? 1.192   11.805  10.230  1.00 11.75  ? 262  GLN B O   1 
ATOM   2827 C  CB  . GLN B 1 39  ? 0.797   12.777  7.315   1.00 11.25  ? 262  GLN B CB  1 
ATOM   2828 C  CG  . GLN B 1 39  ? 0.645   13.996  6.400   1.00 11.96  ? 262  GLN B CG  1 
ATOM   2829 C  CD  . GLN B 1 39  ? 0.330   15.248  7.181   1.00 13.58  ? 262  GLN B CD  1 
ATOM   2830 O  OE1 . GLN B 1 39  ? -0.623  15.267  7.960   1.00 13.49  ? 262  GLN B OE1 1 
ATOM   2831 N  NE2 . GLN B 1 39  ? 1.130   16.306  6.979   1.00 13.98  ? 262  GLN B NE2 1 
ATOM   2832 N  N   . ASN B 1 40  ? 2.870   10.821  9.104   1.00 11.03  ? 263  ASN B N   1 
ATOM   2833 C  CA  . ASN B 1 40  ? 3.173   9.861   10.160  1.00 10.60  ? 263  ASN B CA  1 
ATOM   2834 C  C   . ASN B 1 40  ? 4.329   10.386  10.998  1.00 10.79  ? 263  ASN B C   1 
ATOM   2835 O  O   . ASN B 1 40  ? 5.129   11.209  10.542  1.00 11.44  ? 263  ASN B O   1 
ATOM   2836 C  CB  . ASN B 1 40  ? 3.519   8.496   9.569   1.00 10.56  ? 263  ASN B CB  1 
ATOM   2837 C  CG  . ASN B 1 40  ? 2.305   7.802   9.001   1.00 11.60  ? 263  ASN B CG  1 
ATOM   2838 O  OD1 . ASN B 1 40  ? 1.243   7.785   9.619   1.00 12.56  ? 263  ASN B OD1 1 
ATOM   2839 N  ND2 . ASN B 1 40  ? 2.451   7.237   7.814   1.00 11.96  ? 263  ASN B ND2 1 
ATOM   2840 N  N   . GLY B 1 41  ? 4.388   9.941   12.249  1.00 11.08  ? 264  GLY B N   1 
ATOM   2841 C  CA  . GLY B 1 41  ? 5.432   10.409  13.138  1.00 11.62  ? 264  GLY B CA  1 
ATOM   2842 C  C   . GLY B 1 41  ? 5.256   11.837  13.623  1.00 10.39  ? 264  GLY B C   1 
ATOM   2843 O  O   . GLY B 1 41  ? 6.256   12.555  13.811  1.00 10.78  ? 264  GLY B O   1 
ATOM   2844 N  N   . ARG B 1 42  ? 4.010   12.270  13.835  1.00 11.19  ? 265  ARG B N   1 
ATOM   2845 C  CA  . ARG B 1 42  ? 3.690   13.643  14.214  1.00 10.66  ? 265  ARG B CA  1 
ATOM   2846 C  C   . ARG B 1 42  ? 3.023   13.649  15.585  1.00 11.65  ? 265  ARG B C   1 
ATOM   2847 O  O   . ARG B 1 42  ? 1.936   13.082  15.754  1.00 12.83  ? 265  ARG B O   1 
ATOM   2848 C  CB  . ARG B 1 42  ? 2.800   14.306  13.157  1.00 12.33  ? 265  ARG B CB  1 
ATOM   2849 C  CG  . ARG B 1 42  ? 3.425   14.332  11.763  1.00 12.10  ? 265  ARG B CG  1 
ATOM   2850 C  CD  . ARG B 1 42  ? 4.765   15.080  11.742  1.00 12.57  ? 265  ARG B CD  1 
ATOM   2851 N  NE  . ARG B 1 42  ? 4.622   16.456  12.206  1.00 12.46  ? 265  ARG B NE  1 
ATOM   2852 C  CZ  . ARG B 1 42  ? 4.456   17.526  11.433  1.00 13.08  ? 265  ARG B CZ  1 
ATOM   2853 N  NH1 . ARG B 1 42  ? 4.375   17.430  10.111  1.00 13.07  ? 265  ARG B NH1 1 
ATOM   2854 N  NH2 . ARG B 1 42  ? 4.358   18.723  12.009  1.00 14.71  ? 265  ARG B NH2 1 
ATOM   2855 N  N   . CYS B 1 43  ? 3.673   14.288  16.560  1.00 11.88  ? 266  CYS B N   1 
ATOM   2856 C  CA  . CYS B 1 43  ? 3.127   14.397  17.906  1.00 12.81  ? 266  CYS B CA  1 
ATOM   2857 C  C   . CYS B 1 43  ? 3.772   15.596  18.581  1.00 12.88  ? 266  CYS B C   1 
ATOM   2858 O  O   . CYS B 1 43  ? 4.995   15.749  18.526  1.00 13.73  ? 266  CYS B O   1 
ATOM   2859 C  CB  . CYS B 1 43  ? 3.440   13.123  18.701  1.00 13.24  ? 266  CYS B CB  1 
ATOM   2860 S  SG  . CYS B 1 43  ? 2.718   13.076  20.371  1.00 15.10  ? 266  CYS B SG  1 
ATOM   2861 N  N   . THR B 1 44  ? 2.955   16.438  19.212  1.00 14.15  ? 267  THR B N   1 
ATOM   2862 C  CA  . THR B 1 44  ? 3.513   17.548  19.972  1.00 13.28  ? 267  THR B CA  1 
ATOM   2863 C  C   . THR B 1 44  ? 4.161   17.028  21.252  1.00 14.07  ? 267  THR B C   1 
ATOM   2864 O  O   . THR B 1 44  ? 3.931   15.891  21.679  1.00 14.15  ? 267  THR B O   1 
ATOM   2865 C  CB  . THR B 1 44  ? 2.421   18.545  20.356  1.00 14.45  ? 267  THR B CB  1 
ATOM   2866 O  OG1 . THR B 1 44  ? 1.516   17.912  21.265  1.00 16.08  ? 267  THR B OG1 1 
ATOM   2867 C  CG2 . THR B 1 44  ? 1.649   19.045  19.125  1.00 15.41  ? 267  THR B CG2 1 
ATOM   2868 N  N   . LEU B 1 45  ? 4.994   17.878  21.860  1.00 13.70  ? 268  LEU B N   1 
ATOM   2869 C  CA  . LEU B 1 45  ? 5.683   17.483  23.087  1.00 15.06  ? 268  LEU B CA  1 
ATOM   2870 C  C   . LEU B 1 45  ? 4.711   17.234  24.229  1.00 16.30  ? 268  LEU B C   1 
ATOM   2871 O  O   . LEU B 1 45  ? 5.013   16.430  25.122  1.00 17.00  ? 268  LEU B O   1 
ATOM   2872 C  CB  . LEU B 1 45  ? 6.756   18.499  23.491  1.00 14.75  ? 268  LEU B CB  1 
ATOM   2873 C  CG  . LEU B 1 45  ? 7.818   18.815  22.432  1.00 14.36  ? 268  LEU B CG  1 
ATOM   2874 C  CD1 . LEU B 1 45  ? 8.884   19.724  23.033  1.00 14.86  ? 268  LEU B CD1 1 
ATOM   2875 C  CD2 . LEU B 1 45  ? 8.440   17.552  21.864  1.00 15.56  ? 268  LEU B CD2 1 
ATOM   2876 N  N   . ASP B 1 46  ? 3.553   17.897  24.224  1.00 17.09  ? 269  ASP B N   1 
ATOM   2877 C  CA  . ASP B 1 46  ? 2.537   17.644  25.239  1.00 18.98  ? 269  ASP B CA  1 
ATOM   2878 C  C   . ASP B 1 46  ? 1.584   16.503  24.880  1.00 18.44  ? 269  ASP B C   1 
ATOM   2879 O  O   . ASP B 1 46  ? 0.586   16.302  25.579  1.00 20.28  ? 269  ASP B O   1 
ATOM   2880 C  CB  . ASP B 1 46  ? 1.813   18.933  25.679  1.00 20.81  ? 269  ASP B CB  1 
ATOM   2881 C  CG  . ASP B 1 46  ? 0.920   19.539  24.608  1.00 22.56  ? 269  ASP B CG  1 
ATOM   2882 O  OD1 . ASP B 1 46  ? 0.667   18.912  23.562  1.00 22.77  ? 269  ASP B OD1 1 
ATOM   2883 O  OD2 . ASP B 1 46  ? 0.453   20.676  24.841  1.00 24.59  ? 269  ASP B OD2 1 
ATOM   2884 N  N   . GLY B 1 47  ? 1.871   15.753  23.822  1.00 17.01  ? 270  GLY B N   1 
ATOM   2885 C  CA  . GLY B 1 47  ? 1.199   14.493  23.582  1.00 16.05  ? 270  GLY B CA  1 
ATOM   2886 C  C   . GLY B 1 47  ? 0.035   14.488  22.613  1.00 17.55  ? 270  GLY B C   1 
ATOM   2887 O  O   . GLY B 1 47  ? -0.764  13.552  22.663  1.00 18.64  ? 270  GLY B O   1 
ATOM   2888 N  N   . GLU B 1 48  ? -0.075  15.474  21.725  1.00 16.80  ? 271  GLU B N   1 
ATOM   2889 C  CA  . GLU B 1 48  ? -1.171  15.530  20.756  1.00 16.72  ? 271  GLU B CA  1 
ATOM   2890 C  C   . GLU B 1 48  ? -0.712  14.889  19.450  1.00 15.60  ? 271  GLU B C   1 
ATOM   2891 O  O   . GLU B 1 48  ? 0.180   15.412  18.778  1.00 15.88  ? 271  GLU B O   1 
ATOM   2892 C  CB  . GLU B 1 48  ? -1.597  16.978  20.522  1.00 20.48  ? 271  GLU B CB  1 
ATOM   2893 C  CG  . GLU B 1 48  ? -2.580  17.177  19.372  1.00 27.68  ? 271  GLU B CG  1 
ATOM   2894 C  CD  . GLU B 1 48  ? -2.744  18.645  18.996  1.00 32.97  ? 271  GLU B CD  1 
ATOM   2895 O  OE1 . GLU B 1 48  ? -2.563  19.509  19.881  1.00 36.55  ? 271  GLU B OE1 1 
ATOM   2896 O  OE2 . GLU B 1 48  ? -3.050  18.944  17.820  1.00 35.37  ? 271  GLU B OE2 1 
ATOM   2897 N  N   . LEU B 1 49  ? -1.328  13.762  19.087  1.00 14.98  ? 272  LEU B N   1 
ATOM   2898 C  CA  . LEU B 1 49  ? -1.036  13.132  17.802  1.00 15.51  ? 272  LEU B CA  1 
ATOM   2899 C  C   . LEU B 1 49  ? -1.610  13.972  16.669  1.00 14.98  ? 272  LEU B C   1 
ATOM   2900 O  O   . LEU B 1 49  ? -2.683  14.565  16.804  1.00 17.69  ? 272  LEU B O   1 
ATOM   2901 C  CB  . LEU B 1 49  ? -1.668  11.743  17.744  1.00 15.99  ? 272  LEU B CB  1 
ATOM   2902 C  CG  . LEU B 1 49  ? -1.309  10.759  18.859  1.00 17.31  ? 272  LEU B CG  1 
ATOM   2903 C  CD1 . LEU B 1 49  ? -2.043  9.447   18.623  1.00 17.77  ? 272  LEU B CD1 1 
ATOM   2904 C  CD2 . LEU B 1 49  ? 0.192   10.529  18.965  1.00 17.37  ? 272  LEU B CD2 1 
ATOM   2905 N  N   . GLN B 1 50  ? -0.911  14.002  15.534  1.00 14.73  ? 273  GLN B N   1 
ATOM   2906 C  CA  . GLN B 1 50  ? -1.356  14.790  14.385  1.00 13.78  ? 273  GLN B CA  1 
ATOM   2907 C  C   . GLN B 1 50  ? -1.259  13.988  13.089  1.00 12.58  ? 273  GLN B C   1 
ATOM   2908 O  O   . GLN B 1 50  ? -0.674  12.905  13.032  1.00 13.69  ? 273  GLN B O   1 
ATOM   2909 C  CB  . GLN B 1 50  ? -0.562  16.095  14.261  1.00 14.89  ? 273  GLN B CB  1 
ATOM   2910 C  CG  . GLN B 1 50  ? -0.665  16.978  15.497  1.00 17.12  ? 273  GLN B CG  1 
ATOM   2911 C  CD  . GLN B 1 50  ? 0.161   18.239  15.374  1.00 20.56  ? 273  GLN B CD  1 
ATOM   2912 O  OE1 . GLN B 1 50  ? 1.130   18.293  14.618  1.00 22.71  ? 273  GLN B OE1 1 
ATOM   2913 N  NE2 . GLN B 1 50  ? -0.227  19.263  16.111  1.00 22.04  ? 273  GLN B NE2 1 
ATOM   2914 N  N   . GLY B 1 51  ? -1.835  14.548  12.026  1.00 13.15  ? 274  GLY B N   1 
ATOM   2915 C  CA  . GLY B 1 51  ? -1.724  13.927  10.714  1.00 13.30  ? 274  GLY B CA  1 
ATOM   2916 C  C   . GLY B 1 51  ? -2.422  12.581  10.685  1.00 12.86  ? 274  GLY B C   1 
ATOM   2917 O  O   . GLY B 1 51  ? -3.573  12.444  11.109  1.00 16.13  ? 274  GLY B O   1 
ATOM   2918 N  N   . THR B 1 52  ? -1.718  11.561  10.188  1.00 12.83  ? 275  THR B N   1 
ATOM   2919 C  CA  . THR B 1 52  ? -2.215  10.196  10.168  1.00 13.00  ? 275  THR B CA  1 
ATOM   2920 C  C   . THR B 1 52  ? -1.558  9.343   11.252  1.00 12.70  ? 275  THR B C   1 
ATOM   2921 O  O   . THR B 1 52  ? -1.535  8.112   11.142  1.00 13.71  ? 275  THR B O   1 
ATOM   2922 C  CB  . THR B 1 52  ? -2.008  9.569   8.782   1.00 13.45  ? 275  THR B CB  1 
ATOM   2923 O  OG1 . THR B 1 52  ? -0.617  9.618   8.433   1.00 14.07  ? 275  THR B OG1 1 
ATOM   2924 C  CG2 . THR B 1 52  ? -2.855  10.286  7.716   1.00 14.28  ? 275  THR B CG2 1 
ATOM   2925 N  N   . THR B 1 53  ? -1.012  9.974   12.291  1.00 12.55  ? 276  THR B N   1 
ATOM   2926 C  CA  . THR B 1 53  ? -0.178  9.266   13.255  1.00 11.82  ? 276  THR B CA  1 
ATOM   2927 C  C   . THR B 1 53  ? -1.017  8.464   14.233  1.00 12.81  ? 276  THR B C   1 
ATOM   2928 O  O   . THR B 1 53  ? -2.001  8.960   14.790  1.00 13.97  ? 276  THR B O   1 
ATOM   2929 C  CB  . THR B 1 53  ? 0.701   10.261  14.010  1.00 11.94  ? 276  THR B CB  1 
ATOM   2930 O  OG1 . THR B 1 53  ? 1.578   10.888  13.075  1.00 12.41  ? 276  THR B OG1 1 
ATOM   2931 C  CG2 . THR B 1 53  ? 1.554   9.567   15.065  1.00 12.41  ? 276  THR B CG2 1 
ATOM   2932 N  N   . GLN B 1 54  ? -0.635  7.207   14.413  1.00 12.22  ? 277  GLN B N   1 
ATOM   2933 C  CA  . GLN B 1 54  ? -1.223  6.320   15.406  1.00 11.88  ? 277  GLN B CA  1 
ATOM   2934 C  C   . GLN B 1 54  ? -0.089  5.696   16.222  1.00 13.22  ? 277  GLN B C   1 
ATOM   2935 O  O   . GLN B 1 54  ? 1.084   6.007   16.007  1.00 13.50  ? 277  GLN B O   1 
ATOM   2936 C  CB  . GLN B 1 54  ? -2.190  5.311   14.760  1.00 12.86  ? 277  GLN B CB  1 
ATOM   2937 C  CG  . GLN B 1 54  ? -1.625  4.609   13.538  1.00 12.39  ? 277  GLN B CG  1 
ATOM   2938 C  CD  . GLN B 1 54  ? -0.641  3.533   13.931  1.00 12.41  ? 277  GLN B CD  1 
ATOM   2939 O  OE1 . GLN B 1 54  ? -0.969  2.652   14.734  1.00 13.38  ? 277  GLN B OE1 1 
ATOM   2940 N  NE2 . GLN B 1 54  ? 0.563   3.596   13.381  1.00 12.67  ? 277  GLN B NE2 1 
ATOM   2941 N  N   . LEU B 1 55  ? -0.438  4.820   17.165  1.00 13.07  ? 278  LEU B N   1 
ATOM   2942 C  CA  . LEU B 1 55  ? 0.492   4.420   18.216  1.00 13.02  ? 278  LEU B CA  1 
ATOM   2943 C  C   . LEU B 1 55  ? 1.220   3.108   17.961  1.00 12.51  ? 278  LEU B C   1 
ATOM   2944 O  O   . LEU B 1 55  ? 2.216   2.839   18.644  1.00 14.76  ? 278  LEU B O   1 
ATOM   2945 C  CB  . LEU B 1 55  ? -0.237  4.330   19.563  1.00 14.38  ? 278  LEU B CB  1 
ATOM   2946 C  CG  . LEU B 1 55  ? -0.744  5.680   20.082  1.00 16.08  ? 278  LEU B CG  1 
ATOM   2947 C  CD1 . LEU B 1 55  ? -1.691  5.485   21.268  1.00 18.29  ? 278  LEU B CD1 1 
ATOM   2948 C  CD2 . LEU B 1 55  ? 0.435   6.573   20.468  1.00 17.84  ? 278  LEU B CD2 1 
ATOM   2949 N  N   . VAL B 1 56  ? 0.757   2.283   17.029  1.00 11.79  ? 279  VAL B N   1 
ATOM   2950 C  CA  . VAL B 1 56  ? 1.303   0.949   16.824  1.00 12.34  ? 279  VAL B CA  1 
ATOM   2951 C  C   . VAL B 1 56  ? 2.286   1.021   15.663  1.00 12.52  ? 279  VAL B C   1 
ATOM   2952 O  O   . VAL B 1 56  ? 1.888   1.260   14.514  1.00 12.21  ? 279  VAL B O   1 
ATOM   2953 C  CB  . VAL B 1 56  ? 0.184   -0.060  16.534  1.00 11.99  ? 279  VAL B CB  1 
ATOM   2954 C  CG1 . VAL B 1 56  ? 0.770   -1.445  16.200  1.00 11.76  ? 279  VAL B CG1 1 
ATOM   2955 C  CG2 . VAL B 1 56  ? -0.786  -0.143  17.713  1.00 14.22  ? 279  VAL B CG2 1 
ATOM   2956 N  N   . ALA B 1 57  ? 3.572   0.794   15.939  1.00 12.25  ? 280  ALA B N   1 
ATOM   2957 C  CA  . ALA B 1 57  ? 4.558   0.894   14.866  1.00 13.29  ? 280  ALA B CA  1 
ATOM   2958 C  C   . ALA B 1 57  ? 4.233   -0.081  13.747  1.00 12.26  ? 280  ALA B C   1 
ATOM   2959 O  O   . ALA B 1 57  ? 4.386   0.245   12.564  1.00 12.80  ? 280  ALA B O   1 
ATOM   2960 C  CB  . ALA B 1 57  ? 5.978   0.672   15.391  1.00 14.51  ? 280  ALA B CB  1 
ATOM   2961 N  N   . SER B 1 58  ? 3.757   -1.279  14.105  1.00 11.44  ? 281  SER B N   1 
ATOM   2962 C  CA  . SER B 1 58  ? 3.493   -2.309  13.107  1.00 12.86  ? 281  SER B CA  1 
ATOM   2963 C  C   . SER B 1 58  ? 2.300   -1.980  12.219  1.00 13.51  ? 281  SER B C   1 
ATOM   2964 O  O   . SER B 1 58  ? 2.037   -2.725  11.267  1.00 15.87  ? 281  SER B O   1 
ATOM   2965 C  CB  . SER B 1 58  ? 3.313   -3.677  13.776  1.00 14.49  ? 281  SER B CB  1 
ATOM   2966 O  OG  . SER B 1 58  ? 4.462   -4.012  14.541  1.00 14.58  ? 281  SER B OG  1 
ATOM   2967 N  N   . ASN B 1 59  ? 1.589   -0.883  12.490  1.00 12.96  ? 282  ASN B N   1 
ATOM   2968 C  CA  . ASN B 1 59  ? 0.524   -0.414  11.612  1.00 12.82  ? 282  ASN B CA  1 
ATOM   2969 C  C   . ASN B 1 59  ? 0.951   0.735   10.712  1.00 12.36  ? 282  ASN B C   1 
ATOM   2970 O  O   . ASN B 1 59  ? 0.153   1.186   9.887   1.00 12.88  ? 282  ASN B O   1 
ATOM   2971 C  CB  . ASN B 1 59  ? -0.718  -0.042  12.428  1.00 13.28  ? 282  ASN B CB  1 
ATOM   2972 C  CG  . ASN B 1 59  ? -1.439  -1.268  12.975  1.00 13.90  ? 282  ASN B CG  1 
ATOM   2973 O  OD1 . ASN B 1 59  ? -1.145  -2.395  12.582  1.00 15.96  ? 282  ASN B OD1 1 
ATOM   2974 N  ND2 . ASN B 1 59  ? -2.405  -1.045  13.862  1.00 13.26  ? 282  ASN B ND2 1 
ATOM   2975 N  N   . ILE B 1 60  ? 2.192   1.207   10.833  1.00 11.37  ? 283  ILE B N   1 
ATOM   2976 C  CA  . ILE B 1 60  ? 2.671   2.265   9.944   1.00 11.06  ? 283  ILE B CA  1 
ATOM   2977 C  C   . ILE B 1 60  ? 2.852   1.703   8.537   1.00 11.42  ? 283  ILE B C   1 
ATOM   2978 O  O   . ILE B 1 60  ? 3.538   0.691   8.335   1.00 11.52  ? 283  ILE B O   1 
ATOM   2979 C  CB  . ILE B 1 60  ? 3.989   2.856   10.458  1.00 11.12  ? 283  ILE B CB  1 
ATOM   2980 C  CG1 . ILE B 1 60  ? 3.854   3.430   11.872  1.00 11.94  ? 283  ILE B CG1 1 
ATOM   2981 C  CG2 . ILE B 1 60  ? 4.482   3.914   9.485   1.00 11.97  ? 283  ILE B CG2 1 
ATOM   2982 C  CD1 . ILE B 1 60  ? 5.204   3.727   12.530  1.00 12.74  ? 283  ILE B CD1 1 
ATOM   2983 N  N   . CYS B 1 61  ? 2.246   2.358   7.545   1.00 11.69  ? 284  CYS B N   1 
ATOM   2984 C  CA  . CYS B 1 61  ? 2.281   1.902   6.155   1.00 12.47  ? 284  CYS B CA  1 
ATOM   2985 C  C   . CYS B 1 61  ? 1.594   0.555   5.956   1.00 11.74  ? 284  CYS B C   1 
ATOM   2986 O  O   . CYS B 1 61  ? 1.835   -0.129  4.949   1.00 12.50  ? 284  CYS B O   1 
ATOM   2987 C  CB  . CYS B 1 61  ? 3.694   1.918   5.560   1.00 13.26  ? 284  CYS B CB  1 
ATOM   2988 S  SG  . CYS B 1 61  ? 4.309   3.564   5.184   1.00 12.92  ? 284  CYS B SG  1 
ATOM   2989 N  N   . ALA B 1 62  ? 0.740   0.165   6.895   1.00 12.30  ? 285  ALA B N   1 
ATOM   2990 C  CA  . ALA B 1 62  ? -0.087  -1.016  6.726   1.00 12.91  ? 285  ALA B CA  1 
ATOM   2991 C  C   . ALA B 1 62  ? -1.493  -0.609  6.299   1.00 12.96  ? 285  ALA B C   1 
ATOM   2992 O  O   . ALA B 1 62  ? -1.919  0.533   6.492   1.00 14.09  ? 285  ALA B O   1 
ATOM   2993 C  CB  . ALA B 1 62  ? -0.156  -1.812  8.031   1.00 13.86  ? 285  ALA B CB  1 
ATOM   2994 N  N   . PHE B 1 63  ? -2.215  -1.562  5.711   1.00 13.28  ? 286  PHE B N   1 
ATOM   2995 C  CA  . PHE B 1 63  ? -3.624  -1.382  5.402   1.00 14.11  ? 286  PHE B CA  1 
ATOM   2996 C  C   . PHE B 1 63  ? -4.381  -2.635  5.814   1.00 13.98  ? 286  PHE B C   1 
ATOM   2997 O  O   . PHE B 1 63  ? -3.850  -3.750  5.764   1.00 15.48  ? 286  PHE B O   1 
ATOM   2998 C  CB  . PHE B 1 63  ? -3.877  -1.162  3.911   1.00 14.62  ? 286  PHE B CB  1 
ATOM   2999 C  CG  . PHE B 1 63  ? -3.390  0.159   3.381   1.00 15.50  ? 286  PHE B CG  1 
ATOM   3000 C  CD1 . PHE B 1 63  ? -4.093  1.327   3.631   1.00 16.42  ? 286  PHE B CD1 1 
ATOM   3001 C  CD2 . PHE B 1 63  ? -2.258  0.222   2.583   1.00 16.93  ? 286  PHE B CD2 1 
ATOM   3002 C  CE1 . PHE B 1 63  ? -3.649  2.547   3.116   1.00 16.75  ? 286  PHE B CE1 1 
ATOM   3003 C  CE2 . PHE B 1 63  ? -1.828  1.429   2.045   1.00 16.82  ? 286  PHE B CE2 1 
ATOM   3004 C  CZ  . PHE B 1 63  ? -2.530  2.584   2.306   1.00 17.09  ? 286  PHE B CZ  1 
ATOM   3005 N  N   . ARG B 1 64  ? -5.628  -2.438  6.219   1.00 14.77  ? 287  ARG B N   1 
ATOM   3006 C  CA  . ARG B 1 64  ? -6.532  -3.517  6.587   1.00 15.65  ? 287  ARG B CA  1 
ATOM   3007 C  C   . ARG B 1 64  ? -7.871  -3.250  5.916   1.00 15.37  ? 287  ARG B C   1 
ATOM   3008 O  O   . ARG B 1 64  ? -8.300  -2.099  5.821   1.00 15.83  ? 287  ARG B O   1 
ATOM   3009 C  CB  . ARG B 1 64  ? -6.719  -3.521  8.107   1.00 20.62  ? 287  ARG B CB  1 
ATOM   3010 C  CG  . ARG B 1 64  ? -7.583  -4.630  8.657   1.00 27.13  ? 287  ARG B CG  1 
ATOM   3011 C  CD  . ARG B 1 64  ? -7.646  -4.510  10.176  1.00 34.42  ? 287  ARG B CD  1 
ATOM   3012 N  NE  . ARG B 1 64  ? -8.483  -5.527  10.801  1.00 40.25  ? 287  ARG B NE  1 
ATOM   3013 C  CZ  . ARG B 1 64  ? -8.618  -5.677  12.112  1.00 43.94  ? 287  ARG B CZ  1 
ATOM   3014 N  NH1 . ARG B 1 64  ? -7.986  -4.889  12.967  1.00 45.22  ? 287  ARG B NH1 1 
ATOM   3015 N  NH2 . ARG B 1 64  ? -9.402  -6.645  12.577  1.00 45.60  ? 287  ARG B NH2 1 
ATOM   3016 N  N   . GLY B 1 65  ? -8.527  -4.305  5.444   1.00 14.68  ? 288  GLY B N   1 
ATOM   3017 C  CA  . GLY B 1 65  ? -9.818  -4.159  4.802   1.00 15.06  ? 288  GLY B CA  1 
ATOM   3018 C  C   . GLY B 1 65  ? -10.193 -5.412  4.040   1.00 15.90  ? 288  GLY B C   1 
ATOM   3019 O  O   . GLY B 1 65  ? -10.162 -6.510  4.605   1.00 15.42  ? 288  GLY B O   1 
ATOM   3020 N  N   . SER B 1 66  ? -10.539 -5.265  2.761   1.00 16.39  ? 289  SER B N   1 
ATOM   3021 C  CA  . SER B 1 66  ? -10.984 -6.389  1.947   1.00 16.83  ? 289  SER B CA  1 
ATOM   3022 C  C   . SER B 1 66  ? -10.800 -6.030  0.480   1.00 17.88  ? 289  SER B C   1 
ATOM   3023 O  O   . SER B 1 66  ? -10.775 -4.853  0.109   1.00 19.16  ? 289  SER B O   1 
ATOM   3024 C  CB  . SER B 1 66  ? -12.448 -6.740  2.238   1.00 19.19  ? 289  SER B CB  1 
ATOM   3025 O  OG  . SER B 1 66  ? -13.275 -5.619  2.002   1.00 21.44  ? 289  SER B OG  1 
ATOM   3026 N  N   . ILE B 1 67  ? -10.671 -7.054  -0.354  1.00 16.95  ? 290  ILE B N   1 
ATOM   3027 C  CA  . ILE B 1 67  ? -10.594 -6.876  -1.802  1.00 17.31  ? 290  ILE B CA  1 
ATOM   3028 C  C   . ILE B 1 67  ? -11.989 -7.006  -2.381  1.00 18.84  ? 290  ILE B C   1 
ATOM   3029 O  O   . ILE B 1 67  ? -12.766 -7.877  -1.974  1.00 20.06  ? 290  ILE B O   1 
ATOM   3030 C  CB  . ILE B 1 67  ? -9.635  -7.901  -2.440  1.00 16.89  ? 290  ILE B CB  1 
ATOM   3031 C  CG1 . ILE B 1 67  ? -8.193  -7.661  -1.982  1.00 16.66  ? 290  ILE B CG1 1 
ATOM   3032 C  CG2 . ILE B 1 67  ? -9.749  -7.861  -3.965  1.00 17.84  ? 290  ILE B CG2 1 
ATOM   3033 C  CD1 . ILE B 1 67  ? -7.609  -6.352  -2.452  1.00 17.69  ? 290  ILE B CD1 1 
ATOM   3034 N  N   . SER B 1 68  ? -12.318 -6.126  -3.330  1.00 19.63  ? 291  SER B N   1 
ATOM   3035 C  CA  . SER B 1 68  ? -13.571 -6.209  -4.085  1.00 22.01  ? 291  SER B CA  1 
ATOM   3036 C  C   . SER B 1 68  ? -13.253 -6.113  -5.580  1.00 23.08  ? 291  SER B C   1 
ATOM   3037 O  O   . SER B 1 68  ? -13.407 -5.056  -6.200  1.00 25.00  ? 291  SER B O   1 
ATOM   3038 C  CB  . SER B 1 68  ? -14.547 -5.138  -3.633  1.00 24.74  ? 291  SER B CB  1 
ATOM   3039 O  OG  . SER B 1 68  ? -15.790 -5.286  -4.300  1.00 28.50  ? 291  SER B OG  1 
ATOM   3040 N  N   . GLY B 1 69  ? -12.795 -7.223  -6.153  1.00 24.16  ? 292  GLY B N   1 
ATOM   3041 C  CA  . GLY B 1 69  ? -12.558 -7.323  -7.576  1.00 25.06  ? 292  GLY B CA  1 
ATOM   3042 C  C   . GLY B 1 69  ? -11.455 -6.403  -8.073  1.00 24.34  ? 292  GLY B C   1 
ATOM   3043 O  O   . GLY B 1 69  ? -10.592 -5.933  -7.323  1.00 23.14  ? 292  GLY B O   1 
ATOM   3044 N  N   . HIS B 1 70  ? -11.497 -6.154  -9.373  1.00 26.01  ? 293  HIS B N   1 
ATOM   3045 C  CA  . HIS B 1 70  ? -10.561 -5.271  -10.048 1.00 27.61  ? 293  HIS B CA  1 
ATOM   3046 C  C   . HIS B 1 70  ? -11.093 -3.836  -10.057 1.00 32.78  ? 293  HIS B C   1 
ATOM   3047 O  O   . HIS B 1 70  ? -12.257 -3.574  -9.745  1.00 33.18  ? 293  HIS B O   1 
ATOM   3048 C  CB  . HIS B 1 70  ? -10.332 -5.779  -11.476 1.00 27.37  ? 293  HIS B CB  1 
ATOM   3049 C  CG  . HIS B 1 70  ? -9.774  -7.169  -11.534 1.00 27.08  ? 293  HIS B CG  1 
ATOM   3050 N  ND1 . HIS B 1 70  ? -8.462  -7.457  -11.222 1.00 27.49  ? 293  HIS B ND1 1 
ATOM   3051 C  CD2 . HIS B 1 70  ? -10.353 -8.352  -11.847 1.00 28.28  ? 293  HIS B CD2 1 
ATOM   3052 C  CE1 . HIS B 1 70  ? -8.254  -8.756  -11.352 1.00 26.77  ? 293  HIS B CE1 1 
ATOM   3053 N  NE2 . HIS B 1 70  ? -9.386  -9.322  -11.733 1.00 27.88  ? 293  HIS B NE2 1 
ATOM   3054 N  N   . GLU B 1 71  ? -10.219 -2.893  -10.416 1.00 35.23  ? 294  GLU B N   1 
ATOM   3055 C  CA  . GLU B 1 71  ? -10.636 -1.509  -10.614 1.00 36.87  ? 294  GLU B CA  1 
ATOM   3056 C  C   . GLU B 1 71  ? -11.353 -1.384  -11.961 1.00 41.34  ? 294  GLU B C   1 
ATOM   3057 O  O   . GLU B 1 71  ? -11.611 -2.374  -12.649 1.00 41.74  ? 294  GLU B O   1 
ATOM   3058 C  CB  . GLU B 1 71  ? -9.451  -0.551  -10.466 1.00 34.96  ? 294  GLU B CB  1 
ATOM   3059 C  CG  . GLU B 1 71  ? -8.694  -0.639  -9.133  1.00 33.69  ? 294  GLU B CG  1 
ATOM   3060 C  CD  . GLU B 1 71  ? -9.391  0.074   -7.980  1.00 31.87  ? 294  GLU B CD  1 
ATOM   3061 O  OE1 . GLU B 1 71  ? -10.573 0.455   -8.120  1.00 32.91  ? 294  GLU B OE1 1 
ATOM   3062 O  OE2 . GLU B 1 71  ? -8.753  0.254   -6.921  1.00 30.58  ? 294  GLU B OE2 1 
ATOM   3063 N  N   . ASN B 1 72  ? -11.670 -0.151  -12.363 1.00 44.95  ? 295  ASN B N   1 
ATOM   3064 C  CA  . ASN B 1 72  ? -12.492 0.060   -13.551 1.00 50.31  ? 295  ASN B CA  1 
ATOM   3065 C  C   . ASN B 1 72  ? -11.722 -0.057  -14.863 1.00 51.35  ? 295  ASN B C   1 
ATOM   3066 O  O   . ASN B 1 72  ? -12.352 -0.206  -15.914 1.00 50.74  ? 295  ASN B O   1 
ATOM   3067 C  CB  . ASN B 1 72  ? -13.218 1.405   -13.472 1.00 54.32  ? 295  ASN B CB  1 
ATOM   3068 C  CG  . ASN B 1 72  ? -14.415 1.365   -12.541 1.00 58.21  ? 295  ASN B CG  1 
ATOM   3069 O  OD1 . ASN B 1 72  ? -14.983 0.302   -12.291 1.00 59.28  ? 295  ASN B OD1 1 
ATOM   3070 N  ND2 . ASN B 1 72  ? -14.809 2.525   -12.029 1.00 59.84  ? 295  ASN B ND2 1 
ATOM   3071 N  N   . ASN B 1 73  ? -10.389 0.005   -14.838 1.00 52.34  ? 296  ASN B N   1 
ATOM   3072 C  CA  . ASN B 1 73  ? -9.630  -0.130  -16.079 1.00 52.99  ? 296  ASN B CA  1 
ATOM   3073 C  C   . ASN B 1 73  ? -9.566  -1.565  -16.588 1.00 53.41  ? 296  ASN B C   1 
ATOM   3074 O  O   . ASN B 1 73  ? -9.066  -1.789  -17.696 1.00 53.39  ? 296  ASN B O   1 
ATOM   3075 C  CB  . ASN B 1 73  ? -8.221  0.456   -15.934 1.00 53.35  ? 296  ASN B CB  1 
ATOM   3076 C  CG  . ASN B 1 73  ? -7.406  -0.220  -14.843 1.00 53.78  ? 296  ASN B CG  1 
ATOM   3077 O  OD1 . ASN B 1 73  ? -7.705  -1.337  -14.419 1.00 54.15  ? 296  ASN B OD1 1 
ATOM   3078 N  ND2 . ASN B 1 73  ? -6.361  0.459   -14.387 1.00 53.80  ? 296  ASN B ND2 1 
ATOM   3079 N  N   . GLY B 1 74  ? -10.043 -2.535  -15.811 1.00 53.03  ? 297  GLY B N   1 
ATOM   3080 C  CA  . GLY B 1 74  ? -10.030 -3.914  -16.255 1.00 52.28  ? 297  GLY B CA  1 
ATOM   3081 C  C   . GLY B 1 74  ? -8.673  -4.576  -16.266 1.00 50.20  ? 297  GLY B C   1 
ATOM   3082 O  O   . GLY B 1 74  ? -8.508  -5.613  -16.913 1.00 51.29  ? 297  GLY B O   1 
ATOM   3083 N  N   . ASP B 1 75  ? -7.690  -4.009  -15.569 1.00 46.32  ? 298  ASP B N   1 
ATOM   3084 C  CA  . ASP B 1 75  ? -6.371  -4.624  -15.483 1.00 42.22  ? 298  ASP B CA  1 
ATOM   3085 C  C   . ASP B 1 75  ? -6.439  -5.819  -14.540 1.00 38.73  ? 298  ASP B C   1 
ATOM   3086 O  O   . ASP B 1 75  ? -6.713  -5.663  -13.345 1.00 36.15  ? 298  ASP B O   1 
ATOM   3087 C  CB  . ASP B 1 75  ? -5.358  -3.598  -14.978 1.00 41.05  ? 298  ASP B CB  1 
ATOM   3088 C  CG  . ASP B 1 75  ? -3.917  -4.113  -14.999 1.00 40.68  ? 298  ASP B CG  1 
ATOM   3089 O  OD1 . ASP B 1 75  ? -3.686  -5.324  -14.797 1.00 39.52  ? 298  ASP B OD1 1 
ATOM   3090 O  OD2 . ASP B 1 75  ? -3.002  -3.289  -15.205 1.00 41.38  ? 298  ASP B OD2 1 
ATOM   3091 N  N   . GLN B 1 76  ? -6.168  -7.011  -15.074 1.00 36.73  ? 299  GLN B N   1 
ATOM   3092 C  CA  . GLN B 1 76  ? -6.297  -8.230  -14.285 1.00 35.28  ? 299  GLN B CA  1 
ATOM   3093 C  C   . GLN B 1 76  ? -5.237  -8.364  -13.200 1.00 32.87  ? 299  GLN B C   1 
ATOM   3094 O  O   . GLN B 1 76  ? -5.368  -9.249  -12.349 1.00 33.83  ? 299  GLN B O   1 
ATOM   3095 C  CB  . GLN B 1 76  ? -6.290  -9.461  -15.191 1.00 37.44  ? 299  GLN B CB  1 
ATOM   3096 C  CG  . GLN B 1 76  ? -7.446  -9.489  -16.184 1.00 40.26  ? 299  GLN B CG  1 
ATOM   3097 C  CD  . GLN B 1 76  ? -8.799  -9.480  -15.495 1.00 43.04  ? 299  GLN B CD  1 
ATOM   3098 O  OE1 . GLN B 1 76  ? -9.231  -10.489 -14.938 1.00 43.75  ? 299  GLN B OE1 1 
ATOM   3099 N  NE2 . GLN B 1 76  ? -9.472  -8.335  -15.525 1.00 43.97  ? 299  GLN B NE2 1 
ATOM   3100 N  N   . HIS B 1 77  ? -4.202  -7.525  -13.205 1.00 29.71  ? 300  HIS B N   1 
ATOM   3101 C  CA  A HIS B 1 77  ? -3.181  -7.555  -12.167 0.52 27.39  ? 300  HIS B CA  1 
ATOM   3102 C  CA  B HIS B 1 77  ? -3.171  -7.543  -12.176 0.48 29.24  ? 300  HIS B CA  1 
ATOM   3103 C  C   . HIS B 1 77  ? -3.393  -6.493  -11.097 1.00 25.04  ? 300  HIS B C   1 
ATOM   3104 O  O   . HIS B 1 77  ? -2.550  -6.356  -10.208 1.00 24.48  ? 300  HIS B O   1 
ATOM   3105 C  CB  A HIS B 1 77  ? -1.782  -7.411  -12.773 0.52 29.36  ? 300  HIS B CB  1 
ATOM   3106 C  CB  B HIS B 1 77  ? -1.787  -7.336  -12.804 0.48 34.56  ? 300  HIS B CB  1 
ATOM   3107 C  CG  A HIS B 1 77  ? -1.264  -8.663  -13.409 0.52 62.70  ? 300  HIS B CG  1 
ATOM   3108 C  CG  B HIS B 1 77  ? -1.369  -8.436  -13.728 0.48 101.77 ? 300  HIS B CG  1 
ATOM   3109 N  ND1 A HIS B 1 77  ? -2.092  -9.678  -13.838 0.52 87.42  ? 300  HIS B ND1 1 
ATOM   3110 N  ND1 B HIS B 1 77  ? -1.778  -9.742  -13.564 0.48 79.77  ? 300  HIS B ND1 1 
ATOM   3111 C  CD2 A HIS B 1 77  ? -0.001  -9.066  -13.685 0.52 58.14  ? 300  HIS B CD2 1 
ATOM   3112 C  CD2 B HIS B 1 77  ? -0.578  -8.426  -14.827 0.48 59.60  ? 300  HIS B CD2 1 
ATOM   3113 C  CE1 A HIS B 1 77  ? -1.361  -10.651 -14.353 0.52 96.47  ? 300  HIS B CE1 1 
ATOM   3114 C  CE1 B HIS B 1 77  ? -1.257  -10.488 -14.520 0.48 56.55  ? 300  HIS B CE1 1 
ATOM   3115 N  NE2 A HIS B 1 77  ? -0.089  -10.305 -14.271 0.52 96.55  ? 300  HIS B NE2 1 
ATOM   3116 N  NE2 B HIS B 1 77  ? -0.524  -9.714  -15.301 0.48 95.14  ? 300  HIS B NE2 1 
ATOM   3117 N  N   . GLN B 1 78  ? -4.496  -5.747  -11.156 1.00 21.98  ? 301  GLN B N   1 
ATOM   3118 C  CA  . GLN B 1 78  ? -4.766  -4.669  -10.213 1.00 20.89  ? 301  GLN B CA  1 
ATOM   3119 C  C   . GLN B 1 78  ? -6.088  -4.916  -9.501  1.00 19.62  ? 301  GLN B C   1 
ATOM   3120 O  O   . GLN B 1 78  ? -7.059  -5.362  -10.116 1.00 21.78  ? 301  GLN B O   1 
ATOM   3121 C  CB  . GLN B 1 78  ? -4.800  -3.319  -10.922 1.00 21.91  ? 301  GLN B CB  1 
ATOM   3122 C  CG  . GLN B 1 78  ? -3.488  -2.945  -11.596 1.00 23.86  ? 301  GLN B CG  1 
ATOM   3123 C  CD  . GLN B 1 78  ? -3.544  -1.582  -12.230 1.00 27.95  ? 301  GLN B CD  1 
ATOM   3124 O  OE1 . GLN B 1 78  ? -4.624  -1.040  -12.455 1.00 28.91  ? 301  GLN B OE1 1 
ATOM   3125 N  NE2 . GLN B 1 78  ? -2.379  -1.007  -12.506 1.00 30.13  ? 301  GLN B NE2 1 
ATOM   3126 N  N   . TRP B 1 79  ? -6.128  -4.611  -8.204  1.00 18.01  ? 302  TRP B N   1 
ATOM   3127 C  CA  . TRP B 1 79  ? -7.252  -4.985  -7.361  1.00 17.59  ? 302  TRP B CA  1 
ATOM   3128 C  C   . TRP B 1 79  ? -7.713  -3.800  -6.526  1.00 17.59  ? 302  TRP B C   1 
ATOM   3129 O  O   . TRP B 1 79  ? -6.898  -3.000  -6.051  1.00 17.48  ? 302  TRP B O   1 
ATOM   3130 C  CB  . TRP B 1 79  ? -6.883  -6.160  -6.441  1.00 18.01  ? 302  TRP B CB  1 
ATOM   3131 C  CG  . TRP B 1 79  ? -6.181  -7.296  -7.162  1.00 18.55  ? 302  TRP B CG  1 
ATOM   3132 C  CD1 . TRP B 1 79  ? -4.847  -7.390  -7.443  1.00 19.23  ? 302  TRP B CD1 1 
ATOM   3133 C  CD2 . TRP B 1 79  ? -6.789  -8.468  -7.723  1.00 18.50  ? 302  TRP B CD2 1 
ATOM   3134 N  NE1 . TRP B 1 79  ? -4.584  -8.551  -8.131  1.00 19.35  ? 302  TRP B NE1 1 
ATOM   3135 C  CE2 . TRP B 1 79  ? -5.758  -9.234  -8.310  1.00 19.64  ? 302  TRP B CE2 1 
ATOM   3136 C  CE3 . TRP B 1 79  ? -8.097  -8.963  -7.753  1.00 19.74  ? 302  TRP B CE3 1 
ATOM   3137 C  CZ2 . TRP B 1 79  ? -5.998  -10.455 -8.940  1.00 21.19  ? 302  TRP B CZ2 1 
ATOM   3138 C  CZ3 . TRP B 1 79  ? -8.336  -10.184 -8.393  1.00 21.52  ? 302  TRP B CZ3 1 
ATOM   3139 C  CH2 . TRP B 1 79  ? -7.286  -10.912 -8.967  1.00 21.39  ? 302  TRP B CH2 1 
ATOM   3140 N  N   . HIS B 1 80  ? -9.029  -3.707  -6.346  1.00 17.34  ? 303  HIS B N   1 
ATOM   3141 C  CA  . HIS B 1 80  ? -9.648  -2.676  -5.518  1.00 17.57  ? 303  HIS B CA  1 
ATOM   3142 C  C   . HIS B 1 80  ? -9.596  -3.112  -4.056  1.00 17.05  ? 303  HIS B C   1 
ATOM   3143 O  O   . HIS B 1 80  ? -10.311 -4.031  -3.649  1.00 18.31  ? 303  HIS B O   1 
ATOM   3144 C  CB  . HIS B 1 80  ? -11.090 -2.464  -5.969  1.00 19.67  ? 303  HIS B CB  1 
ATOM   3145 C  CG  . HIS B 1 80  ? -11.818 -1.399  -5.207  1.00 21.59  ? 303  HIS B CG  1 
ATOM   3146 N  ND1 . HIS B 1 80  ? -11.899 -0.094  -5.643  1.00 22.82  ? 303  HIS B ND1 1 
ATOM   3147 C  CD2 . HIS B 1 80  ? -12.502 -1.449  -4.039  1.00 23.53  ? 303  HIS B CD2 1 
ATOM   3148 C  CE1 . HIS B 1 80  ? -12.601 0.613   -4.776  1.00 23.14  ? 303  HIS B CE1 1 
ATOM   3149 N  NE2 . HIS B 1 80  ? -12.983 -0.185  -3.797  1.00 22.83  ? 303  HIS B NE2 1 
ATOM   3150 N  N   . PHE B 1 81  ? -8.761  -2.440  -3.261  1.00 17.98  ? 304  PHE B N   1 
ATOM   3151 C  CA  . PHE B 1 81  ? -8.530  -2.762  -1.851  1.00 17.75  ? 304  PHE B CA  1 
ATOM   3152 C  C   . PHE B 1 81  ? -9.325  -1.751  -1.016  1.00 17.28  ? 304  PHE B C   1 
ATOM   3153 O  O   . PHE B 1 81  ? -8.894  -0.607  -0.808  1.00 17.46  ? 304  PHE B O   1 
ATOM   3154 C  CB  . PHE B 1 81  ? -7.025  -2.690  -1.584  1.00 17.37  ? 304  PHE B CB  1 
ATOM   3155 C  CG  . PHE B 1 81  ? -6.573  -3.233  -0.248  1.00 17.37  ? 304  PHE B CG  1 
ATOM   3156 C  CD1 . PHE B 1 81  ? -7.457  -3.672  0.726   1.00 17.55  ? 304  PHE B CD1 1 
ATOM   3157 C  CD2 . PHE B 1 81  ? -5.221  -3.302  0.012   1.00 19.56  ? 304  PHE B CD2 1 
ATOM   3158 C  CE1 . PHE B 1 81  ? -6.982  -4.167  1.942   1.00 17.82  ? 304  PHE B CE1 1 
ATOM   3159 C  CE2 . PHE B 1 81  ? -4.747  -3.784  1.216   1.00 19.60  ? 304  PHE B CE2 1 
ATOM   3160 C  CZ  . PHE B 1 81  ? -5.629  -4.233  2.176   1.00 18.44  ? 304  PHE B CZ  1 
ATOM   3161 N  N   . SER B 1 82  ? -10.505 -2.164  -0.563  1.00 17.36  ? 305  SER B N   1 
ATOM   3162 C  CA  . SER B 1 82  ? -11.288 -1.362  0.370   1.00 18.85  ? 305  SER B CA  1 
ATOM   3163 C  C   . SER B 1 82  ? -10.621 -1.393  1.738   1.00 18.41  ? 305  SER B C   1 
ATOM   3164 O  O   . SER B 1 82  ? -10.251 -2.462  2.238   1.00 19.79  ? 305  SER B O   1 
ATOM   3165 C  CB  . SER B 1 82  ? -12.696 -1.935  0.485   1.00 20.68  ? 305  SER B CB  1 
ATOM   3166 O  OG  . SER B 1 82  ? -13.358 -1.892  -0.762  1.00 23.44  ? 305  SER B OG  1 
ATOM   3167 N  N   . ILE B 1 83  ? -10.465 -0.225  2.356   1.00 16.96  ? 306  ILE B N   1 
ATOM   3168 C  CA  . ILE B 1 83  ? -9.697  -0.123  3.588   1.00 17.63  ? 306  ILE B CA  1 
ATOM   3169 C  C   . ILE B 1 83  ? -10.555 0.437   4.712   1.00 17.96  ? 306  ILE B C   1 
ATOM   3170 O  O   . ILE B 1 83  ? -11.457 1.257   4.501   1.00 21.25  ? 306  ILE B O   1 
ATOM   3171 C  CB  . ILE B 1 83  ? -8.378  0.665   3.430   1.00 17.40  ? 306  ILE B CB  1 
ATOM   3172 C  CG1 . ILE B 1 83  ? -8.641  2.114   3.020   1.00 18.10  ? 306  ILE B CG1 1 
ATOM   3173 C  CG2 . ILE B 1 83  ? -7.458  -0.036  2.425   1.00 18.12  ? 306  ILE B CG2 1 
ATOM   3174 C  CD1 . ILE B 1 83  ? -7.366  2.945   2.965   1.00 19.60  ? 306  ILE B CD1 1 
ATOM   3175 N  N   . THR B 1 84  ? -10.274 -0.036  5.915   1.00 18.45  ? 307  THR B N   1 
ATOM   3176 C  CA  . THR B 1 84  ? -10.908 0.401   7.143   1.00 20.85  ? 307  THR B CA  1 
ATOM   3177 C  C   . THR B 1 84  ? -9.862  1.080   8.012   1.00 22.92  ? 307  THR B C   1 
ATOM   3178 O  O   . THR B 1 84  ? -8.697  1.221   7.629   1.00 21.22  ? 307  THR B O   1 
ATOM   3179 C  CB  . THR B 1 84  ? -11.491 -0.798  7.897   1.00 21.85  ? 307  THR B CB  1 
ATOM   3180 O  OG1 . THR B 1 84  ? -10.422 -1.613  8.402   1.00 22.77  ? 307  THR B OG1 1 
ATOM   3181 C  CG2 . THR B 1 84  ? -12.370 -1.636  6.981   1.00 22.91  ? 307  THR B CG2 1 
ATOM   3182 N  N   . ASN B 1 85  ? -10.299 1.505   9.194   1.00 24.63  ? 308  ASN B N   1 
ATOM   3183 C  CA  . ASN B 1 85  ? -9.374  1.887   10.238  1.00 27.04  ? 308  ASN B CA  1 
ATOM   3184 C  C   . ASN B 1 85  ? -8.556  0.666   10.654  1.00 27.55  ? 308  ASN B C   1 
ATOM   3185 O  O   . ASN B 1 85  ? -8.991  -0.474  10.474  1.00 27.28  ? 308  ASN B O   1 
ATOM   3186 C  CB  . ASN B 1 85  ? -10.150 2.414   11.443  1.00 27.83  ? 308  ASN B CB  1 
ATOM   3187 C  CG  . ASN B 1 85  ? -10.866 3.714   11.154  1.00 29.15  ? 308  ASN B CG  1 
ATOM   3188 O  OD1 . ASN B 1 85  ? -10.311 4.608   10.523  1.00 28.81  ? 308  ASN B OD1 1 
ATOM   3189 N  ND2 . ASN B 1 85  ? -12.108 3.827   11.618  1.00 31.30  ? 308  ASN B ND2 1 
ATOM   3190 N  N   . PRO B 1 86  ? -7.366  0.877   11.215  1.00 29.79  ? 309  PRO B N   1 
ATOM   3191 C  CA  . PRO B 1 86  ? -6.540  -0.262  11.652  1.00 33.68  ? 309  PRO B CA  1 
ATOM   3192 C  C   . PRO B 1 86  ? -7.236  -1.217  12.616  1.00 40.16  ? 309  PRO B C   1 
ATOM   3193 O  O   . PRO B 1 86  ? -6.851  -2.389  12.720  1.00 39.02  ? 309  PRO B O   1 
ATOM   3194 C  CB  . PRO B 1 86  ? -5.339  0.418   12.316  1.00 31.58  ? 309  PRO B CB  1 
ATOM   3195 C  CG  . PRO B 1 86  ? -5.236  1.741   11.636  1.00 30.36  ? 309  PRO B CG  1 
ATOM   3196 C  CD  . PRO B 1 86  ? -6.648  2.160   11.333  1.00 29.50  ? 309  PRO B CD  1 
ATOM   3197 N  N   . ASN B 1 87  ? -8.256  -0.736  13.324  1.00 46.58  ? 310  ASN B N   1 
ATOM   3198 C  CA  . ASN B 1 87  ? -9.008  -1.548  14.273  1.00 52.16  ? 310  ASN B CA  1 
ATOM   3199 C  C   . ASN B 1 87  ? -10.139 -2.333  13.622  1.00 52.44  ? 310  ASN B C   1 
ATOM   3200 O  O   . ASN B 1 87  ? -10.843 -3.072  14.320  1.00 53.18  ? 310  ASN B O   1 
ATOM   3201 C  CB  . ASN B 1 87  ? -9.586  -0.666  15.387  1.00 57.14  ? 310  ASN B CB  1 
ATOM   3202 C  CG  . ASN B 1 87  ? -10.739 0.201   14.908  1.00 35.07  ? 310  ASN B CG  1 
ATOM   3203 O  OD1 . ASN B 1 87  ? -10.878 0.470   13.717  1.00 76.59  ? 310  ASN B OD1 1 
ATOM   3204 N  ND2 . ASN B 1 87  ? -11.567 0.652   15.844  1.00 53.99  ? 310  ASN B ND2 1 
ATOM   3205 N  N   . GLY B 1 88  ? -10.341 -2.184  12.314  1.00 51.39  ? 311  GLY B N   1 
ATOM   3206 C  CA  . GLY B 1 88  ? -11.439 -2.828  11.632  1.00 50.74  ? 311  GLY B CA  1 
ATOM   3207 C  C   . GLY B 1 88  ? -12.715 -2.017  11.565  1.00 50.17  ? 311  GLY B C   1 
ATOM   3208 O  O   . GLY B 1 88  ? -13.601 -2.355  10.769  1.00 50.89  ? 311  GLY B O   1 
ATOM   3209 N  N   . THR B 1 89  ? -12.845 -0.969  12.375  1.00 48.58  ? 312  THR B N   1 
ATOM   3210 C  CA  . THR B 1 89  ? -14.011 -0.108  12.294  1.00 47.38  ? 312  THR B CA  1 
ATOM   3211 C  C   . THR B 1 89  ? -13.980 0.674   10.981  1.00 44.90  ? 312  THR B C   1 
ATOM   3212 O  O   . THR B 1 89  ? -12.905 0.939   10.435  1.00 42.87  ? 312  THR B O   1 
ATOM   3213 C  CB  . THR B 1 89  ? -14.028 0.867   13.469  1.00 48.48  ? 312  THR B CB  1 
ATOM   3214 N  N   . PRO B 1 90  ? -15.144 1.033   10.440  1.00 43.62  ? 313  PRO B N   1 
ATOM   3215 C  CA  A PRO B 1 90  ? -15.163 1.779   9.176   0.11 43.14  ? 313  PRO B CA  1 
ATOM   3216 C  CA  B PRO B 1 90  ? -15.168 1.780   9.177   0.89 43.15  ? 313  PRO B CA  1 
ATOM   3217 C  C   . PRO B 1 90  ? -14.524 3.151   9.327   1.00 42.27  ? 313  PRO B C   1 
ATOM   3218 O  O   . PRO B 1 90  ? -14.746 3.859   10.312  1.00 42.80  ? 313  PRO B O   1 
ATOM   3219 C  CB  A PRO B 1 90  ? -16.658 1.894   8.853   0.11 43.41  ? 313  PRO B CB  1 
ATOM   3220 C  CB  B PRO B 1 90  ? -16.665 1.901   8.865   0.89 43.89  ? 313  PRO B CB  1 
ATOM   3221 C  CG  A PRO B 1 90  ? -17.346 1.728   10.170  0.11 43.49  ? 313  PRO B CG  1 
ATOM   3222 C  CG  B PRO B 1 90  ? -17.307 0.793   9.631   0.89 43.71  ? 313  PRO B CG  1 
ATOM   3223 C  CD  A PRO B 1 90  ? -16.502 0.760   10.942  0.11 43.58  ? 313  PRO B CD  1 
ATOM   3224 C  CD  B PRO B 1 90  ? -16.497 0.655   10.883  0.89 43.83  ? 313  PRO B CD  1 
ATOM   3225 N  N   . PHE B 1 91  ? -13.718 3.520   8.334   1.00 39.23  ? 314  PHE B N   1 
ATOM   3226 C  CA  . PHE B 1 91  ? -13.079 4.829   8.332   1.00 37.04  ? 314  PHE B CA  1 
ATOM   3227 C  C   . PHE B 1 91  ? -14.103 5.901   7.985   1.00 40.73  ? 314  PHE B C   1 
ATOM   3228 O  O   . PHE B 1 91  ? -14.821 5.785   6.988   1.00 40.70  ? 314  PHE B O   1 
ATOM   3229 C  CB  . PHE B 1 91  ? -11.942 4.849   7.313   1.00 34.58  ? 314  PHE B CB  1 
ATOM   3230 C  CG  . PHE B 1 91  ? -11.361 6.212   7.089   1.00 31.81  ? 314  PHE B CG  1 
ATOM   3231 C  CD1 . PHE B 1 91  ? -10.605 6.822   8.075   1.00 30.52  ? 314  PHE B CD1 1 
ATOM   3232 C  CD2 . PHE B 1 91  ? -11.587 6.893   5.905   1.00 31.63  ? 314  PHE B CD2 1 
ATOM   3233 C  CE1 . PHE B 1 91  ? -10.072 8.077   7.883   1.00 29.97  ? 314  PHE B CE1 1 
ATOM   3234 C  CE2 . PHE B 1 91  ? -11.052 8.150   5.705   1.00 30.94  ? 314  PHE B CE2 1 
ATOM   3235 C  CZ  . PHE B 1 91  ? -10.292 8.745   6.696   1.00 30.65  ? 314  PHE B CZ  1 
ATOM   3236 N  N   . ASP B 1 92  ? -14.168 6.949   8.809   1.00 44.03  ? 315  ASP B N   1 
ATOM   3237 C  CA  . ASP B 1 92  ? -15.126 8.029   8.617   1.00 47.75  ? 315  ASP B CA  1 
ATOM   3238 C  C   . ASP B 1 92  ? -14.436 9.182   7.906   1.00 49.30  ? 315  ASP B C   1 
ATOM   3239 O  O   . ASP B 1 92  ? -13.626 9.885   8.530   1.00 48.96  ? 315  ASP B O   1 
ATOM   3240 C  CB  . ASP B 1 92  ? -15.667 8.490   9.970   1.00 49.97  ? 315  ASP B CB  1 
ATOM   3241 C  CG  . ASP B 1 92  ? -16.783 9.518   9.844   1.00 52.20  ? 315  ASP B CG  1 
ATOM   3242 O  OD1 . ASP B 1 92  ? -17.049 10.003  8.723   1.00 52.32  ? 315  ASP B OD1 1 
ATOM   3243 O  OD2 . ASP B 1 92  ? -17.405 9.838   10.879  1.00 53.54  ? 315  ASP B OD2 1 
ATOM   3244 N  N   . PRO B 1 93  ? -14.721 9.426   6.623   1.00 51.20  ? 316  PRO B N   1 
ATOM   3245 C  CA  . PRO B 1 93  ? -14.058 10.538  5.924   1.00 52.12  ? 316  PRO B CA  1 
ATOM   3246 C  C   . PRO B 1 93  ? -14.494 11.916  6.395   1.00 52.97  ? 316  PRO B C   1 
ATOM   3247 O  O   . PRO B 1 93  ? -13.771 12.889  6.148   1.00 52.87  ? 316  PRO B O   1 
ATOM   3248 C  CB  . PRO B 1 93  ? -14.430 10.307  4.451   1.00 52.53  ? 316  PRO B CB  1 
ATOM   3249 C  CG  . PRO B 1 93  ? -14.907 8.879   4.383   1.00 52.71  ? 316  PRO B CG  1 
ATOM   3250 C  CD  . PRO B 1 93  ? -15.543 8.616   5.711   1.00 52.24  ? 316  PRO B CD  1 
ATOM   3251 N  N   . THR B 1 94  ? -15.647 12.039  7.058   1.00 53.22  ? 317  THR B N   1 
ATOM   3252 C  CA  . THR B 1 94  ? -16.114 13.355  7.481   1.00 53.17  ? 317  THR B CA  1 
ATOM   3253 C  C   . THR B 1 94  ? -15.285 13.930  8.622   1.00 53.92  ? 317  THR B C   1 
ATOM   3254 O  O   . THR B 1 94  ? -15.371 15.132  8.890   1.00 54.26  ? 317  THR B O   1 
ATOM   3255 C  CB  . THR B 1 94  ? -17.596 13.314  7.858   1.00 51.73  ? 317  THR B CB  1 
ATOM   3256 O  OG1 . THR B 1 94  ? -17.758 12.625  9.104   1.00 51.43  ? 317  THR B OG1 1 
ATOM   3257 C  CG2 . THR B 1 94  ? -18.394 12.598  6.782   1.00 52.00  ? 317  THR B CG2 1 
ATOM   3258 N  N   . GLU B 1 95  ? -14.499 13.105  9.308   1.00 54.78  ? 318  GLU B N   1 
ATOM   3259 C  CA  . GLU B 1 95  ? -13.542 13.640  10.261  1.00 55.80  ? 318  GLU B CA  1 
ATOM   3260 C  C   . GLU B 1 95  ? -12.398 14.308  9.508   1.00 49.70  ? 318  GLU B C   1 
ATOM   3261 O  O   . GLU B 1 95  ? -12.012 13.882  8.417   1.00 48.50  ? 318  GLU B O   1 
ATOM   3262 C  CB  . GLU B 1 95  ? -13.003 12.524  11.156  1.00 63.31  ? 318  GLU B CB  1 
ATOM   3263 C  CG  . GLU B 1 95  ? -14.060 11.883  12.043  1.00 60.52  ? 318  GLU B CG  1 
ATOM   3264 C  CD  . GLU B 1 95  ? -13.472 10.891  13.026  1.00 115.99 ? 318  GLU B CD  1 
ATOM   3265 O  OE1 . GLU B 1 95  ? -12.359 10.384  12.769  1.00 94.14  ? 318  GLU B OE1 1 
ATOM   3266 O  OE2 . GLU B 1 95  ? -14.121 10.622  14.058  1.00 65.88  ? 318  GLU B OE2 1 
ATOM   3267 N  N   . ASP B 1 96  ? -11.863 15.382  10.091  0.77 45.74  ? 319  ASP B N   1 
ATOM   3268 C  CA  A ASP B 1 96  ? -10.776 16.137  9.464   0.50 43.72  ? 319  ASP B CA  1 
ATOM   3269 C  CA  B ASP B 1 96  ? -10.776 16.137  9.465   0.50 43.72  ? 319  ASP B CA  1 
ATOM   3270 C  C   . ASP B 1 96  ? -9.439  15.445  9.738   1.00 40.13  ? 319  ASP B C   1 
ATOM   3271 O  O   . ASP B 1 96  ? -8.569  15.933  10.464  0.91 40.64  ? 319  ASP B O   1 
ATOM   3272 C  CB  A ASP B 1 96  ? -10.790 17.593  9.905   0.50 45.30  ? 319  ASP B CB  1 
ATOM   3273 C  CB  B ASP B 1 96  ? -10.790 17.594  9.906   0.50 45.30  ? 319  ASP B CB  1 
ATOM   3274 C  CG  A ASP B 1 96  ? -11.764 18.432  9.099   0.50 46.98  ? 319  ASP B CG  1 
ATOM   3275 C  CG  B ASP B 1 96  ? -11.764 18.432  9.099   0.50 46.98  ? 319  ASP B CG  1 
ATOM   3276 O  OD1 . ASP B 1 96  ? -12.092 18.035  7.960   1.00 47.17  ? 319  ASP B OD1 1 
ATOM   3277 O  OD2 . ASP B 1 96  ? -12.200 19.489  9.600   1.00 47.49  ? 319  ASP B OD2 1 
ATOM   3278 N  N   A VAL B 1 97  ? -9.306  14.261  9.156   0.83 36.04  ? 320  VAL B N   1 
ATOM   3279 N  N   B VAL B 1 97  ? -9.287  14.283  9.112   0.17 36.32  ? 320  VAL B N   1 
ATOM   3280 C  CA  A VAL B 1 97  ? -8.053  13.516  9.164   0.83 32.79  ? 320  VAL B CA  1 
ATOM   3281 C  CA  B VAL B 1 97  ? -8.069  13.479  9.164   0.17 32.56  ? 320  VAL B CA  1 
ATOM   3282 C  C   A VAL B 1 97  ? -7.659  13.358  7.700   0.83 29.76  ? 320  VAL B C   1 
ATOM   3283 C  C   B VAL B 1 97  ? -7.656  13.223  7.717   0.17 29.46  ? 320  VAL B C   1 
ATOM   3284 O  O   A VAL B 1 97  ? -8.541  13.319  6.831   0.83 29.42  ? 320  VAL B O   1 
ATOM   3285 O  O   B VAL B 1 97  ? -8.527  12.965  6.874   0.17 29.45  ? 320  VAL B O   1 
ATOM   3286 C  CB  A VAL B 1 97  ? -8.211  12.170  9.888   0.83 33.57  ? 320  VAL B CB  1 
ATOM   3287 C  CB  B VAL B 1 97  ? -8.310  12.185  9.964   0.17 32.06  ? 320  VAL B CB  1 
ATOM   3288 C  CG1 A VAL B 1 97  ? -8.622  12.395  11.335  0.83 33.74  ? 320  VAL B CG1 1 
ATOM   3289 C  CG1 B VAL B 1 97  ? -9.508  11.420  9.411   0.17 31.99  ? 320  VAL B CG1 1 
ATOM   3290 C  CG2 A VAL B 1 97  ? -9.239  11.302  9.180   0.83 33.96  ? 320  VAL B CG2 1 
ATOM   3291 C  CG2 B VAL B 1 97  ? -7.070  11.304  9.992   0.17 31.62  ? 320  VAL B CG2 1 
ATOM   3292 N  N   . PRO B 1 98  ? -6.367  13.314  7.369   1.00 26.12  ? 321  PRO B N   1 
ATOM   3293 C  CA  . PRO B 1 98  ? -5.991  13.211  5.946   1.00 24.94  ? 321  PRO B CA  1 
ATOM   3294 C  C   . PRO B 1 98  ? -6.385  11.904  5.293   1.00 22.26  ? 321  PRO B C   1 
ATOM   3295 O  O   . PRO B 1 98  ? -6.706  11.896  4.098   1.00 23.35  ? 321  PRO B O   1 
ATOM   3296 C  CB  . PRO B 1 98  ? -4.467  13.374  5.965   1.00 24.49  ? 321  PRO B CB  1 
ATOM   3297 C  CG  . PRO B 1 98  ? -4.178  14.074  7.247   1.00 25.29  ? 321  PRO B CG  1 
ATOM   3298 C  CD  . PRO B 1 98  ? -5.202  13.598  8.225   1.00 25.34  ? 321  PRO B CD  1 
ATOM   3299 N  N   . ALA B 1 99  ? -6.377  10.806  6.046   1.00 20.86  ? 322  ALA B N   1 
ATOM   3300 C  CA  . ALA B 1 99  ? -6.534  9.451   5.536   1.00 19.47  ? 322  ALA B CA  1 
ATOM   3301 C  C   . ALA B 1 99  ? -6.609  8.511   6.732   1.00 18.78  ? 322  ALA B C   1 
ATOM   3302 O  O   . ALA B 1 99  ? -6.352  8.938   7.864   1.00 19.30  ? 322  ALA B O   1 
ATOM   3303 C  CB  . ALA B 1 99  ? -5.331  9.086   4.661   1.00 19.62  ? 322  ALA B CB  1 
ATOM   3304 N  N   . PRO B 1 100 ? -6.939  7.235   6.538   1.00 18.02  ? 323  PRO B N   1 
ATOM   3305 C  CA  . PRO B 1 100 ? -6.869  6.287   7.658   1.00 17.56  ? 323  PRO B CA  1 
ATOM   3306 C  C   . PRO B 1 100 ? -5.494  6.312   8.315   1.00 16.45  ? 323  PRO B C   1 
ATOM   3307 O  O   . PRO B 1 100 ? -4.471  6.519   7.657   1.00 18.21  ? 323  PRO B O   1 
ATOM   3308 C  CB  . PRO B 1 100 ? -7.155  4.938   6.994   1.00 18.53  ? 323  PRO B CB  1 
ATOM   3309 C  CG  . PRO B 1 100 ? -8.043  5.303   5.852   1.00 19.24  ? 323  PRO B CG  1 
ATOM   3310 C  CD  . PRO B 1 100 ? -7.503  6.605   5.331   1.00 18.79  ? 323  PRO B CD  1 
ATOM   3311 N  N   . LEU B 1 101 ? -5.478  6.131   9.632   1.00 15.40  ? 324  LEU B N   1 
ATOM   3312 C  CA  . LEU B 1 101 ? -4.229  6.273   10.364  1.00 14.78  ? 324  LEU B CA  1 
ATOM   3313 C  C   . LEU B 1 101 ? -3.217  5.253   9.862   1.00 15.51  ? 324  LEU B C   1 
ATOM   3314 O  O   . LEU B 1 101 ? -3.568  4.115   9.543   1.00 17.76  ? 324  LEU B O   1 
ATOM   3315 C  CB  . LEU B 1 101 ? -4.486  6.108   11.859  1.00 17.84  ? 324  LEU B CB  1 
ATOM   3316 C  CG  . LEU B 1 101 ? -5.428  7.188   12.425  1.00 20.25  ? 324  LEU B CG  1 
ATOM   3317 C  CD1 . LEU B 1 101 ? -5.508  7.124   13.939  1.00 23.74  ? 324  LEU B CD1 1 
ATOM   3318 C  CD2 . LEU B 1 101 ? -5.051  8.618   11.975  1.00 21.62  ? 324  LEU B CD2 1 
ATOM   3319 N  N   . GLY B 1 102 ? -1.965  5.683   9.742   1.00 13.24  ? 325  GLY B N   1 
ATOM   3320 C  CA  . GLY B 1 102 ? -0.908  4.841   9.240   1.00 13.41  ? 325  GLY B CA  1 
ATOM   3321 C  C   . GLY B 1 102 ? -0.716  4.847   7.737   1.00 12.29  ? 325  GLY B C   1 
ATOM   3322 O  O   . GLY B 1 102 ? 0.279   4.280   7.270   1.00 13.61  ? 325  GLY B O   1 
ATOM   3323 N  N   . THR B 1 103 ? -1.622  5.463   6.971   1.00 12.62  ? 326  THR B N   1 
ATOM   3324 C  CA  . THR B 1 103 ? -1.472  5.523   5.520   1.00 12.58  ? 326  THR B CA  1 
ATOM   3325 C  C   . THR B 1 103 ? -0.100  6.105   5.179   1.00 12.72  ? 326  THR B C   1 
ATOM   3326 O  O   . THR B 1 103 ? 0.349   7.043   5.849   1.00 13.10  ? 326  THR B O   1 
ATOM   3327 C  CB  . THR B 1 103 ? -2.564  6.436   4.932   1.00 13.77  ? 326  THR B CB  1 
ATOM   3328 O  OG1 . THR B 1 103 ? -3.848  5.837   5.121   1.00 15.27  ? 326  THR B OG1 1 
ATOM   3329 C  CG2 . THR B 1 103 ? -2.367  6.680   3.448   1.00 14.55  ? 326  THR B CG2 1 
ATOM   3330 N  N   . PRO B 1 104 ? 0.600   5.584   4.166   1.00 12.36  ? 327  PRO B N   1 
ATOM   3331 C  CA  . PRO B 1 104 ? 1.881   6.187   3.770   1.00 13.05  ? 327  PRO B CA  1 
ATOM   3332 C  C   . PRO B 1 104 ? 1.730   7.670   3.456   1.00 12.51  ? 327  PRO B C   1 
ATOM   3333 O  O   . PRO B 1 104 ? 0.712   8.115   2.920   1.00 13.63  ? 327  PRO B O   1 
ATOM   3334 C  CB  . PRO B 1 104 ? 2.269   5.401   2.507   1.00 14.39  ? 327  PRO B CB  1 
ATOM   3335 C  CG  . PRO B 1 104 ? 1.000   4.694   2.074   1.00 15.22  ? 327  PRO B CG  1 
ATOM   3336 C  CD  . PRO B 1 104 ? 0.245   4.421   3.324   1.00 14.70  ? 327  PRO B CD  1 
ATOM   3337 N  N   . ASP B 1 105 ? 2.784   8.432   3.768   1.00 12.08  ? 328  ASP B N   1 
ATOM   3338 C  CA  . ASP B 1 105 ? 2.791   9.886   3.641   1.00 11.68  ? 328  ASP B CA  1 
ATOM   3339 C  C   . ASP B 1 105 ? 3.810   10.373  2.614   1.00 12.47  ? 328  ASP B C   1 
ATOM   3340 O  O   . ASP B 1 105 ? 4.319   11.490  2.718   1.00 15.42  ? 328  ASP B O   1 
ATOM   3341 C  CB  . ASP B 1 105 ? 2.998   10.566  5.000   1.00 12.32  ? 328  ASP B CB  1 
ATOM   3342 C  CG  . ASP B 1 105 ? 4.366   10.261  5.616   1.00 11.67  ? 328  ASP B CG  1 
ATOM   3343 O  OD1 . ASP B 1 105 ? 5.118   9.453   5.023   1.00 12.30  ? 328  ASP B OD1 1 
ATOM   3344 O  OD2 . ASP B 1 105 ? 4.695   10.823  6.694   1.00 11.33  ? 328  ASP B OD2 1 
ATOM   3345 N  N   . PHE B 1 106 ? 4.121   9.545   1.620   1.00 11.63  ? 329  PHE B N   1 
ATOM   3346 C  CA  . PHE B 1 106 ? 5.119   9.869   0.608   1.00 11.57  ? 329  PHE B CA  1 
ATOM   3347 C  C   . PHE B 1 106 ? 4.618   9.382   -0.745  1.00 12.50  ? 329  PHE B C   1 
ATOM   3348 O  O   . PHE B 1 106 ? 3.770   8.482   -0.831  1.00 13.91  ? 329  PHE B O   1 
ATOM   3349 C  CB  . PHE B 1 106 ? 6.483   9.216   0.924   1.00 12.62  ? 329  PHE B CB  1 
ATOM   3350 C  CG  . PHE B 1 106 ? 6.400   7.731   1.150   1.00 12.33  ? 329  PHE B CG  1 
ATOM   3351 C  CD1 . PHE B 1 106 ? 6.429   6.843   0.083   1.00 12.87  ? 329  PHE B CD1 1 
ATOM   3352 C  CD2 . PHE B 1 106 ? 6.284   7.219   2.437   1.00 13.47  ? 329  PHE B CD2 1 
ATOM   3353 C  CE1 . PHE B 1 106 ? 6.337   5.470   0.295   1.00 14.13  ? 329  PHE B CE1 1 
ATOM   3354 C  CE2 . PHE B 1 106 ? 6.190   5.851   2.654   1.00 14.70  ? 329  PHE B CE2 1 
ATOM   3355 C  CZ  . PHE B 1 106 ? 6.218   4.980   1.573   1.00 14.55  ? 329  PHE B CZ  1 
ATOM   3356 N  N   . LYS B 1 107 ? 5.164   9.982   -1.804  1.00 13.42  ? 330  LYS B N   1 
ATOM   3357 C  CA  . LYS B 1 107 ? 4.933   9.519   -3.172  1.00 12.62  ? 330  LYS B CA  1 
ATOM   3358 C  C   . LYS B 1 107 ? 5.925   8.410   -3.488  1.00 12.66  ? 330  LYS B C   1 
ATOM   3359 O  O   . LYS B 1 107 ? 7.138   8.610   -3.390  1.00 13.87  ? 330  LYS B O   1 
ATOM   3360 C  CB  . LYS B 1 107 ? 5.088   10.667  -4.171  1.00 13.66  ? 330  LYS B CB  1 
ATOM   3361 C  CG  . LYS B 1 107 ? 3.918   11.628  -4.176  1.00 13.45  ? 330  LYS B CG  1 
ATOM   3362 C  CD  . LYS B 1 107 ? 4.035   12.613  -5.325  1.00 15.30  ? 330  LYS B CD  1 
ATOM   3363 C  CE  . LYS B 1 107 ? 2.848   13.565  -5.375  1.00 17.70  ? 330  LYS B CE  1 
ATOM   3364 N  NZ  . LYS B 1 107 ? 2.954   14.518  -6.533  1.00 20.57  ? 330  LYS B NZ  1 
ATOM   3365 N  N   . GLY B 1 108 ? 5.420   7.234   -3.841  1.00 13.07  ? 331  GLY B N   1 
ATOM   3366 C  CA  . GLY B 1 108 ? 6.310   6.145   -4.191  1.00 13.97  ? 331  GLY B CA  1 
ATOM   3367 C  C   . GLY B 1 108 ? 5.546   4.846   -4.344  1.00 13.61  ? 331  GLY B C   1 
ATOM   3368 O  O   . GLY B 1 108 ? 4.311   4.809   -4.300  1.00 14.32  ? 331  GLY B O   1 
ATOM   3369 N  N   . GLN B 1 109 ? 6.312   3.772   -4.529  1.00 13.49  ? 332  GLN B N   1 
ATOM   3370 C  CA  . GLN B 1 109 ? 5.762   2.446   -4.805  1.00 13.47  ? 332  GLN B CA  1 
ATOM   3371 C  C   . GLN B 1 109 ? 5.943   1.602   -3.544  1.00 12.69  ? 332  GLN B C   1 
ATOM   3372 O  O   . GLN B 1 109 ? 7.016   1.035   -3.308  1.00 13.45  ? 332  GLN B O   1 
ATOM   3373 C  CB  . GLN B 1 109 ? 6.474   1.820   -6.003  1.00 14.36  ? 332  GLN B CB  1 
ATOM   3374 C  CG  . GLN B 1 109 ? 6.346   2.653   -7.262  1.00 15.94  ? 332  GLN B CG  1 
ATOM   3375 C  CD  . GLN B 1 109 ? 4.906   2.820   -7.650  1.00 18.26  ? 332  GLN B CD  1 
ATOM   3376 O  OE1 . GLN B 1 109 ? 4.191   1.839   -7.833  1.00 21.28  ? 332  GLN B OE1 1 
ATOM   3377 N  NE2 . GLN B 1 109 ? 4.455   4.064   -7.754  1.00 18.85  ? 332  GLN B NE2 1 
ATOM   3378 N  N   . LEU B 1 110 ? 4.894   1.517   -2.731  1.00 12.67  ? 333  LEU B N   1 
ATOM   3379 C  CA  . LEU B 1 110 ? 4.972   0.789   -1.462  1.00 12.36  ? 333  LEU B CA  1 
ATOM   3380 C  C   . LEU B 1 110 ? 4.876   -0.711  -1.731  1.00 12.39  ? 333  LEU B C   1 
ATOM   3381 O  O   . LEU B 1 110 ? 3.882   -1.181  -2.291  1.00 13.52  ? 333  LEU B O   1 
ATOM   3382 C  CB  . LEU B 1 110 ? 3.852   1.256   -0.526  1.00 12.33  ? 333  LEU B CB  1 
ATOM   3383 C  CG  . LEU B 1 110 ? 3.734   0.593   0.852   1.00 11.59  ? 333  LEU B CG  1 
ATOM   3384 C  CD1 . LEU B 1 110 ? 4.997   0.792   1.680   1.00 13.25  ? 333  LEU B CD1 1 
ATOM   3385 C  CD2 . LEU B 1 110 ? 2.523   1.114   1.582   1.00 12.90  ? 333  LEU B CD2 1 
ATOM   3386 N  N   . TYR B 1 111 ? 5.905   -1.454  -1.338  1.00 12.05  ? 334  TYR B N   1 
ATOM   3387 C  CA  . TYR B 1 111 ? 6.016   -2.875  -1.620  1.00 11.24  ? 334  TYR B CA  1 
ATOM   3388 C  C   . TYR B 1 111 ? 5.821   -3.668  -0.340  1.00 10.98  ? 334  TYR B C   1 
ATOM   3389 O  O   . TYR B 1 111 ? 6.362   -3.317  0.712   1.00 12.35  ? 334  TYR B O   1 
ATOM   3390 C  CB  . TYR B 1 111 ? 7.392   -3.188  -2.224  1.00 11.36  ? 334  TYR B CB  1 
ATOM   3391 C  CG  . TYR B 1 111 ? 7.843   -4.633  -2.122  1.00 11.82  ? 334  TYR B CG  1 
ATOM   3392 C  CD1 . TYR B 1 111 ? 7.218   -5.642  -2.849  1.00 13.02  ? 334  TYR B CD1 1 
ATOM   3393 C  CD2 . TYR B 1 111 ? 8.905   -4.989  -1.300  1.00 12.53  ? 334  TYR B CD2 1 
ATOM   3394 C  CE1 . TYR B 1 111 ? 7.635   -6.955  -2.752  1.00 12.80  ? 334  TYR B CE1 1 
ATOM   3395 C  CE2 . TYR B 1 111 ? 9.335   -6.303  -1.208  1.00 12.29  ? 334  TYR B CE2 1 
ATOM   3396 C  CZ  . TYR B 1 111 ? 8.691   -7.283  -1.925  1.00 13.50  ? 334  TYR B CZ  1 
ATOM   3397 O  OH  . TYR B 1 111 ? 9.127   -8.589  -1.816  1.00 14.24  ? 334  TYR B OH  1 
ATOM   3398 N  N   . GLY B 1 112 ? 5.031   -4.729  -0.419  1.00 10.62  ? 335  GLY B N   1 
ATOM   3399 C  CA  . GLY B 1 112 ? 4.851   -5.604  0.724   1.00 11.63  ? 335  GLY B CA  1 
ATOM   3400 C  C   . GLY B 1 112 ? 4.072   -6.847  0.375   1.00 11.00  ? 335  GLY B C   1 
ATOM   3401 O  O   . GLY B 1 112 ? 4.101   -7.292  -0.776  1.00 11.82  ? 335  GLY B O   1 
ATOM   3402 N  N   . VAL B 1 113 ? 3.385   -7.431  1.350   1.00 10.98  ? 336  VAL B N   1 
ATOM   3403 C  CA  . VAL B 1 113 ? 2.621   -8.652  1.145   1.00 11.62  ? 336  VAL B CA  1 
ATOM   3404 C  C   . VAL B 1 113 ? 1.165   -8.398  1.517   1.00 11.24  ? 336  VAL B C   1 
ATOM   3405 O  O   . VAL B 1 113 ? 0.874   -7.883  2.605   1.00 12.11  ? 336  VAL B O   1 
ATOM   3406 C  CB  . VAL B 1 113 ? 3.219   -9.818  1.951   1.00 10.32  ? 336  VAL B CB  1 
ATOM   3407 C  CG1 . VAL B 1 113 ? 2.262   -11.016 1.948   1.00 11.20  ? 336  VAL B CG1 1 
ATOM   3408 C  CG2 . VAL B 1 113 ? 4.615   -10.183 1.400   1.00 11.93  ? 336  VAL B CG2 1 
ATOM   3409 N  N   . ILE B 1 114 ? 0.252   -8.772  0.626   1.00 10.34  ? 337  ILE B N   1 
ATOM   3410 C  CA  . ILE B 1 114 ? -1.170  -8.805  0.954   1.00 12.16  ? 337  ILE B CA  1 
ATOM   3411 C  C   . ILE B 1 114 ? -1.529  -10.222 1.384   1.00 11.53  ? 337  ILE B C   1 
ATOM   3412 O  O   . ILE B 1 114 ? -1.236  -11.193 0.676   1.00 12.40  ? 337  ILE B O   1 
ATOM   3413 C  CB  . ILE B 1 114 ? -2.047  -8.312  -0.216  1.00 12.91  ? 337  ILE B CB  1 
ATOM   3414 C  CG1 . ILE B 1 114 ? -3.537  -8.440  0.143   1.00 14.88  ? 337  ILE B CG1 1 
ATOM   3415 C  CG2 . ILE B 1 114 ? -1.750  -9.049  -1.527  1.00 14.05  ? 337  ILE B CG2 1 
ATOM   3416 C  CD1 . ILE B 1 114 ? -4.483  -7.726  -0.826  1.00 16.76  ? 337  ILE B CD1 1 
ATOM   3417 N  N   A SER B 1 115 ? -2.120  -10.342 2.567   0.81 11.36  ? 338  SER B N   1 
ATOM   3418 N  N   B SER B 1 115 ? -2.155  -10.341 2.551   0.19 11.09  ? 338  SER B N   1 
ATOM   3419 C  CA  A SER B 1 115 ? -2.566  -11.618 3.104   0.81 11.46  ? 338  SER B CA  1 
ATOM   3420 C  CA  B SER B 1 115 ? -2.555  -11.624 3.108   0.19 10.66  ? 338  SER B CA  1 
ATOM   3421 C  C   A SER B 1 115 ? -4.078  -11.612 3.219   0.81 11.43  ? 338  SER B C   1 
ATOM   3422 C  C   B SER B 1 115 ? -4.062  -11.645 3.317   0.19 10.96  ? 338  SER B C   1 
ATOM   3423 O  O   A SER B 1 115 ? -4.681  -10.590 3.564   0.81 13.19  ? 338  SER B O   1 
ATOM   3424 O  O   B SER B 1 115 ? -4.645  -10.671 3.805   0.19 11.37  ? 338  SER B O   1 
ATOM   3425 C  CB  A SER B 1 115 ? -1.986  -11.853 4.490   0.81 11.51  ? 338  SER B CB  1 
ATOM   3426 C  CB  B SER B 1 115 ? -1.852  -11.890 4.441   0.19 9.86   ? 338  SER B CB  1 
ATOM   3427 O  OG  A SER B 1 115 ? -0.569  -11.883 4.462   0.81 11.33  ? 338  SER B OG  1 
ATOM   3428 O  OG  B SER B 1 115 ? -2.133  -10.879 5.392   0.19 8.68   ? 338  SER B OG  1 
ATOM   3429 N  N   . GLN B 1 116 ? -4.686  -12.760 2.951   1.00 11.27  ? 339  GLN B N   1 
ATOM   3430 C  CA  . GLN B 1 116 ? -6.125  -12.920 3.066   1.00 12.48  ? 339  GLN B CA  1 
ATOM   3431 C  C   . GLN B 1 116 ? -6.451  -14.152 3.893   1.00 11.28  ? 339  GLN B C   1 
ATOM   3432 O  O   . GLN B 1 116 ? -5.727  -15.152 3.866   1.00 12.42  ? 339  GLN B O   1 
ATOM   3433 C  CB  . GLN B 1 116 ? -6.805  -13.079 1.699   1.00 13.02  ? 339  GLN B CB  1 
ATOM   3434 C  CG  . GLN B 1 116 ? -6.317  -12.135 0.631   1.00 13.51  ? 339  GLN B CG  1 
ATOM   3435 C  CD  . GLN B 1 116 ? -7.216  -12.159 -0.585  1.00 14.31  ? 339  GLN B CD  1 
ATOM   3436 O  OE1 . GLN B 1 116 ? -7.456  -13.217 -1.168  1.00 15.21  ? 339  GLN B OE1 1 
ATOM   3437 N  NE2 . GLN B 1 116 ? -7.755  -10.997 -0.949  1.00 15.38  ? 339  GLN B NE2 1 
ATOM   3438 N  N   . ARG B 1 117 ? -7.558  -14.064 4.624   1.00 12.28  ? 340  ARG B N   1 
ATOM   3439 C  CA  . ARG B 1 117 ? -8.161  -15.202 5.304   1.00 12.88  ? 340  ARG B CA  1 
ATOM   3440 C  C   . ARG B 1 117 ? -9.660  -15.132 5.061   1.00 14.13  ? 340  ARG B C   1 
ATOM   3441 O  O   . ARG B 1 117 ? -10.283 -14.098 5.317   1.00 15.06  ? 340  ARG B O   1 
ATOM   3442 C  CB  . ARG B 1 117 ? -7.843  -15.209 6.810   1.00 13.89  ? 340  ARG B CB  1 
ATOM   3443 C  CG  . ARG B 1 117 ? -8.555  -16.323 7.561   1.00 14.17  ? 340  ARG B CG  1 
ATOM   3444 C  CD  . ARG B 1 117 ? -8.132  -16.413 9.012   1.00 17.04  ? 340  ARG B CD  1 
ATOM   3445 N  NE  . ARG B 1 117 ? -6.739  -16.825 9.058   1.00 17.50  ? 340  ARG B NE  1 
ATOM   3446 C  CZ  . ARG B 1 117 ? -5.747  -16.126 9.595   1.00 16.01  ? 340  ARG B CZ  1 
ATOM   3447 N  NH1 . ARG B 1 117 ? -5.975  -15.042 10.320  1.00 18.65  ? 340  ARG B NH1 1 
ATOM   3448 N  NH2 . ARG B 1 117 ? -4.499  -16.541 9.416   1.00 14.57  ? 340  ARG B NH2 1 
ATOM   3449 N  N   . ASN B 1 118 ? -10.235 -16.207 4.529   1.00 13.17  ? 341  ASN B N   1 
ATOM   3450 C  CA  . ASN B 1 118 ? -11.628 -16.160 4.106   1.00 14.54  ? 341  ASN B CA  1 
ATOM   3451 C  C   . ASN B 1 118 ? -12.572 -15.955 5.291   1.00 14.90  ? 341  ASN B C   1 
ATOM   3452 O  O   . ASN B 1 118 ? -12.278 -16.346 6.424   1.00 16.21  ? 341  ASN B O   1 
ATOM   3453 C  CB  . ASN B 1 118 ? -11.993 -17.442 3.370   1.00 14.82  ? 341  ASN B CB  1 
ATOM   3454 C  CG  . ASN B 1 118 ? -11.532 -17.430 1.932   1.00 17.15  ? 341  ASN B CG  1 
ATOM   3455 O  OD1 . ASN B 1 118 ? -10.484 -16.874 1.611   1.00 16.28  ? 341  ASN B OD1 1 
ATOM   3456 N  ND2 . ASN B 1 118 ? -12.321 -18.039 1.053   1.00 19.80  ? 341  ASN B ND2 1 
ATOM   3457 N  N   . ARG B 1 119 ? -13.728 -15.336 5.004   1.00 17.10  ? 342  ARG B N   1 
ATOM   3458 C  CA  . ARG B 1 119 ? -14.746 -15.071 6.023   1.00 20.49  ? 342  ARG B CA  1 
ATOM   3459 C  C   . ARG B 1 119 ? -15.335 -16.351 6.599   1.00 23.37  ? 342  ARG B C   1 
ATOM   3460 O  O   . ARG B 1 119 ? -15.662 -16.406 7.790   1.00 24.79  ? 342  ARG B O   1 
ATOM   3461 C  CB  . ARG B 1 119 ? -15.882 -14.239 5.429   1.00 23.52  ? 342  ARG B CB  1 
ATOM   3462 C  CG  . ARG B 1 119 ? -15.455 -12.914 4.928   1.00 25.68  ? 342  ARG B CG  1 
ATOM   3463 C  CD  . ARG B 1 119 ? -16.616 -12.083 4.418   1.00 25.69  ? 342  ARG B CD  1 
ATOM   3464 N  NE  . ARG B 1 119 ? -16.079 -10.832 3.909   1.00 27.01  ? 342  ARG B NE  1 
ATOM   3465 C  CZ  . ARG B 1 119 ? -15.587 -10.682 2.689   1.00 27.60  ? 342  ARG B CZ  1 
ATOM   3466 N  NH1 . ARG B 1 119 ? -15.689 -11.640 1.784   1.00 26.82  ? 342  ARG B NH1 1 
ATOM   3467 N  NH2 . ARG B 1 119 ? -14.960 -9.552  2.378   1.00 28.59  ? 342  ARG B NH2 1 
ATOM   3468 N  N   . GLU B 1 120 ? -15.527 -17.370 5.771   1.00 23.23  ? 343  GLU B N   1 
ATOM   3469 C  CA  . GLU B 1 120 ? -16.201 -18.584 6.204   1.00 24.80  ? 343  GLU B CA  1 
ATOM   3470 C  C   . GLU B 1 120 ? -15.245 -19.759 6.108   1.00 24.40  ? 343  GLU B C   1 
ATOM   3471 O  O   . GLU B 1 120 ? -14.526 -19.911 5.114   1.00 23.72  ? 343  GLU B O   1 
ATOM   3472 C  CB  . GLU B 1 120 ? -17.459 -18.864 5.374   1.00 27.93  ? 343  GLU B CB  1 
ATOM   3473 C  CG  . GLU B 1 120 ? -18.452 -17.715 5.369   1.00 31.72  ? 343  GLU B CG  1 
ATOM   3474 C  CD  . GLU B 1 120 ? -18.913 -17.337 6.761   1.00 34.91  ? 343  GLU B CD  1 
ATOM   3475 N  N   . GLY B 1 121 ? -15.235 -20.580 7.153   1.00 25.73  ? 344  GLY B N   1 
ATOM   3476 C  CA  . GLY B 1 121 ? -14.400 -21.754 7.147   1.00 27.89  ? 344  GLY B CA  1 
ATOM   3477 C  C   . GLY B 1 121 ? -14.840 -22.765 6.107   1.00 31.30  ? 344  GLY B C   1 
ATOM   3478 O  O   . GLY B 1 121 ? -15.970 -22.762 5.615   1.00 31.05  ? 344  GLY B O   1 
ATOM   3479 N  N   . SER B 1 122 ? -13.908 -23.647 5.763   1.00 34.87  ? 345  SER B N   1 
ATOM   3480 C  CA  . SER B 1 122 ? -14.206 -24.742 4.854   1.00 38.86  ? 345  SER B CA  1 
ATOM   3481 C  C   . SER B 1 122 ? -14.875 -25.919 5.551   1.00 45.44  ? 345  SER B C   1 
ATOM   3482 O  O   . SER B 1 122 ? -15.442 -26.779 4.870   1.00 45.84  ? 345  SER B O   1 
ATOM   3483 C  CB  . SER B 1 122 ? -12.919 -25.213 4.179   1.00 36.78  ? 345  SER B CB  1 
ATOM   3484 O  OG  . SER B 1 122 ? -12.010 -25.711 5.145   1.00 36.02  ? 345  SER B OG  1 
ATOM   3485 N  N   . SER B 1 123 ? -14.827 -25.975 6.879   1.00 50.07  ? 346  SER B N   1 
ATOM   3486 C  CA  . SER B 1 123 ? -15.415 -27.084 7.624   1.00 54.74  ? 346  SER B CA  1 
ATOM   3487 C  C   . SER B 1 123 ? -16.578 -26.626 8.502   1.00 56.02  ? 346  SER B C   1 
ATOM   3488 O  O   . SER B 1 123 ? -16.458 -25.664 9.260   1.00 56.92  ? 346  SER B O   1 
ATOM   3489 C  CB  . SER B 1 123 ? -14.350 -27.779 8.477   1.00 57.08  ? 346  SER B CB  1 
ATOM   3490 O  OG  . SER B 1 123 ? -13.729 -26.866 9.364   1.00 58.26  ? 346  SER B OG  1 
ATOM   3491 N  N   . ASN B 1 127 ? -13.573 -25.151 11.756  1.00 49.86  ? 350  ASN B N   1 
ATOM   3492 C  CA  . ASN B 1 127 ? -13.492 -23.868 11.065  1.00 48.94  ? 350  ASN B CA  1 
ATOM   3493 C  C   . ASN B 1 127 ? -12.668 -23.987 9.777   1.00 42.21  ? 350  ASN B C   1 
ATOM   3494 O  O   . ASN B 1 127 ? -13.227 -24.211 8.702   1.00 43.27  ? 350  ASN B O   1 
ATOM   3495 C  CB  . ASN B 1 127 ? -12.915 -22.801 11.996  1.00 53.01  ? 350  ASN B CB  1 
ATOM   3496 C  CG  . ASN B 1 127 ? -13.229 -21.396 11.534  1.00 56.34  ? 350  ASN B CG  1 
ATOM   3497 O  OD1 . ASN B 1 127 ? -12.327 -20.594 11.295  1.00 57.32  ? 350  ASN B OD1 1 
ATOM   3498 N  ND2 . ASN B 1 127 ? -14.514 -21.089 11.398  1.00 57.65  ? 350  ASN B ND2 1 
ATOM   3499 N  N   . GLN B 1 128 ? -11.345 -23.840 9.891   1.00 32.81  ? 351  GLN B N   1 
ATOM   3500 C  CA  . GLN B 1 128 ? -10.408 -24.110 8.797   1.00 27.85  ? 351  GLN B CA  1 
ATOM   3501 C  C   . GLN B 1 128 ? -10.665 -23.194 7.594   1.00 22.54  ? 351  GLN B C   1 
ATOM   3502 O  O   . GLN B 1 128 ? -11.030 -23.618 6.497   1.00 21.80  ? 351  GLN B O   1 
ATOM   3503 C  CB  . GLN B 1 128 ? -10.390 -25.599 8.424   1.00 29.46  ? 351  GLN B CB  1 
ATOM   3504 C  CG  . GLN B 1 128 ? -9.824  -26.509 9.517   1.00 31.33  ? 351  GLN B CG  1 
ATOM   3505 C  CD  . GLN B 1 128 ? -8.302  -26.506 9.553   1.00 33.43  ? 351  GLN B CD  1 
ATOM   3506 O  OE1 . GLN B 1 128 ? -7.653  -27.129 8.712   1.00 34.50  ? 351  GLN B OE1 1 
ATOM   3507 N  NE2 . GLN B 1 128 ? -7.728  -25.800 10.524  1.00 33.12  ? 351  GLN B NE2 1 
ATOM   3508 N  N   . LYS B 1 129 ? -10.436 -21.910 7.837   1.00 17.76  ? 352  LYS B N   1 
ATOM   3509 C  CA  . LYS B 1 129 ? -10.544 -20.891 6.803   1.00 14.90  ? 352  LYS B CA  1 
ATOM   3510 C  C   . LYS B 1 129 ? -9.344  -20.957 5.860   1.00 13.89  ? 352  LYS B C   1 
ATOM   3511 O  O   . LYS B 1 129 ? -8.205  -21.159 6.290   1.00 14.17  ? 352  LYS B O   1 
ATOM   3512 C  CB  . LYS B 1 129 ? -10.604 -19.507 7.460   1.00 16.34  ? 352  LYS B CB  1 
ATOM   3513 C  CG  . LYS B 1 129 ? -11.894 -19.250 8.221   1.00 17.52  ? 352  LYS B CG  1 
ATOM   3514 C  CD  . LYS B 1 129 ? -11.786 -18.018 9.098   1.00 19.07  ? 352  LYS B CD  1 
ATOM   3515 C  CE  . LYS B 1 129 ? -13.097 -17.728 9.810   1.00 22.27  ? 352  LYS B CE  1 
ATOM   3516 N  NZ  . LYS B 1 129 ? -12.984 -16.528 10.680  1.00 25.11  ? 352  LYS B NZ  1 
ATOM   3517 N  N   . ALA B 1 130 ? -9.602  -20.769 4.573   1.00 12.04  ? 353  ALA B N   1 
ATOM   3518 C  CA  . ALA B 1 130 ? -8.528  -20.724 3.594   1.00 12.33  ? 353  ALA B CA  1 
ATOM   3519 C  C   . ALA B 1 130 ? -7.742  -19.420 3.708   1.00 11.94  ? 353  ALA B C   1 
ATOM   3520 O  O   . ALA B 1 130 ? -8.284  -18.361 4.066   1.00 12.40  ? 353  ALA B O   1 
ATOM   3521 C  CB  . ALA B 1 130 ? -9.107  -20.852 2.184   1.00 13.18  ? 353  ALA B CB  1 
ATOM   3522 N  N   . ASN B 1 131 ? -6.450  -19.508 3.407   1.00 11.41  ? 354  ASN B N   1 
ATOM   3523 C  CA  . ASN B 1 131 ? -5.522  -18.387 3.449   1.00 11.76  ? 354  ASN B CA  1 
ATOM   3524 C  C   . ASN B 1 131 ? -4.778  -18.296 2.125   1.00 11.76  ? 354  ASN B C   1 
ATOM   3525 O  O   . ASN B 1 131 ? -4.526  -19.309 1.467   1.00 12.41  ? 354  ASN B O   1 
ATOM   3526 C  CB  . ASN B 1 131 ? -4.440  -18.581 4.531   1.00 12.08  ? 354  ASN B CB  1 
ATOM   3527 C  CG  . ASN B 1 131 ? -5.005  -18.611 5.933   1.00 12.36  ? 354  ASN B CG  1 
ATOM   3528 O  OD1 . ASN B 1 131 ? -4.926  -17.633 6.680   1.00 13.84  ? 354  ASN B OD1 1 
ATOM   3529 N  ND2 . ASN B 1 131 ? -5.559  -19.746 6.314   1.00 13.08  ? 354  ASN B ND2 1 
ATOM   3530 N  N   . ARG B 1 132 ? -4.388  -17.072 1.758   1.00 11.44  ? 355  ARG B N   1 
ATOM   3531 C  CA  . ARG B 1 132 ? -3.407  -16.878 0.697   1.00 11.35  ? 355  ARG B CA  1 
ATOM   3532 C  C   . ARG B 1 132 ? -2.697  -15.547 0.905   1.00 11.54  ? 355  ARG B C   1 
ATOM   3533 O  O   . ARG B 1 132 ? -3.319  -14.563 1.315   1.00 13.22  ? 355  ARG B O   1 
ATOM   3534 C  CB  . ARG B 1 132 ? -4.060  -16.912 -0.695  1.00 13.16  ? 355  ARG B CB  1 
ATOM   3535 C  CG  . ARG B 1 132 ? -5.028  -15.761 -0.960  1.00 14.09  ? 355  ARG B CG  1 
ATOM   3536 C  CD  . ARG B 1 132 ? -6.100  -16.142 -2.002  1.00 13.95  ? 355  ARG B CD  1 
ATOM   3537 N  NE  . ARG B 1 132 ? -6.959  -17.214 -1.516  1.00 14.37  ? 355  ARG B NE  1 
ATOM   3538 C  CZ  . ARG B 1 132 ? -7.909  -17.058 -0.604  1.00 14.74  ? 355  ARG B CZ  1 
ATOM   3539 N  NH1 . ARG B 1 132 ? -8.239  -15.854 -0.142  1.00 14.74  ? 355  ARG B NH1 1 
ATOM   3540 N  NH2 . ARG B 1 132 ? -8.539  -18.139 -0.134  1.00 15.96  ? 355  ARG B NH2 1 
ATOM   3541 N  N   . SER B 1 133 ? -1.400  -15.519 0.608   1.00 11.78  ? 356  SER B N   1 
ATOM   3542 C  CA  . SER B 1 133 ? -0.631  -14.284 0.625   1.00 12.16  ? 356  SER B CA  1 
ATOM   3543 C  C   . SER B 1 133 ? 0.178   -14.169 -0.654  1.00 13.31  ? 356  SER B C   1 
ATOM   3544 O  O   . SER B 1 133 ? 0.644   -15.173 -1.199  1.00 13.15  ? 356  SER B O   1 
ATOM   3545 C  CB  . SER B 1 133 ? 0.346   -14.208 1.809   1.00 12.80  ? 356  SER B CB  1 
ATOM   3546 O  OG  . SER B 1 133 ? -0.321  -14.216 3.054   1.00 12.73  ? 356  SER B OG  1 
ATOM   3547 N  N   . HIS B 1 134 ? 0.372   -12.924 -1.100  1.00 12.59  ? 357  HIS B N   1 
ATOM   3548 C  CA  . HIS B 1 134 ? 1.171   -12.638 -2.282  1.00 12.81  ? 357  HIS B CA  1 
ATOM   3549 C  C   . HIS B 1 134 ? 1.844   -11.287 -2.136  1.00 10.97  ? 357  HIS B C   1 
ATOM   3550 O  O   . HIS B 1 134 ? 1.337   -10.387 -1.458  1.00 12.38  ? 357  HIS B O   1 
ATOM   3551 C  CB  . HIS B 1 134 ? 0.337   -12.643 -3.571  1.00 15.96  ? 357  HIS B CB  1 
ATOM   3552 C  CG  . HIS B 1 134 ? -0.211  -13.989 -3.905  1.00 19.98  ? 357  HIS B CG  1 
ATOM   3553 N  ND1 . HIS B 1 134 ? 0.579   -15.008 -4.396  1.00 21.88  ? 357  HIS B ND1 1 
ATOM   3554 C  CD2 . HIS B 1 134 ? -1.454  -14.507 -3.769  1.00 20.87  ? 357  HIS B CD2 1 
ATOM   3555 C  CE1 . HIS B 1 134 ? -0.160  -16.089 -4.567  1.00 22.32  ? 357  HIS B CE1 1 
ATOM   3556 N  NE2 . HIS B 1 134 ? -1.396  -15.812 -4.193  1.00 22.55  ? 357  HIS B NE2 1 
ATOM   3557 N  N   . GLU B 1 135 ? 2.992   -11.159 -2.787  1.00 11.83  ? 358  GLU B N   1 
ATOM   3558 C  CA  . GLU B 1 135 ? 3.625   -9.857  -2.918  1.00 13.31  ? 358  GLU B CA  1 
ATOM   3559 C  C   . GLU B 1 135 ? 2.722   -8.898  -3.684  1.00 13.25  ? 358  GLU B C   1 
ATOM   3560 O  O   . GLU B 1 135 ? 2.034   -9.286  -4.639  1.00 14.35  ? 358  GLU B O   1 
ATOM   3561 C  CB  . GLU B 1 135 ? 4.942   -10.005 -3.670  1.00 14.27  ? 358  GLU B CB  1 
ATOM   3562 C  CG  . GLU B 1 135 ? 6.036   -10.704 -2.908  1.00 14.77  ? 358  GLU B CG  1 
ATOM   3563 C  CD  . GLU B 1 135 ? 7.230   -10.965 -3.798  1.00 16.33  ? 358  GLU B CD  1 
ATOM   3564 O  OE1 . GLU B 1 135 ? 7.112   -11.821 -4.694  1.00 20.86  ? 358  GLU B OE1 1 
ATOM   3565 O  OE2 . GLU B 1 135 ? 8.271   -10.307 -3.630  1.00 15.66  ? 358  GLU B OE2 1 
ATOM   3566 N  N   . GLY B 1 136 ? 2.738   -7.636  -3.279  1.00 13.36  ? 359  GLY B N   1 
ATOM   3567 C  CA  . GLY B 1 136 ? 1.984   -6.622  -3.993  1.00 13.92  ? 359  GLY B CA  1 
ATOM   3568 C  C   . GLY B 1 136 ? 2.624   -5.256  -3.863  1.00 13.81  ? 359  GLY B C   1 
ATOM   3569 O  O   . GLY B 1 136 ? 3.478   -5.019  -2.996  1.00 14.02  ? 359  GLY B O   1 
ATOM   3570 N  N   . VAL B 1 137 ? 2.185   -4.344  -4.728  1.00 13.18  ? 360  VAL B N   1 
ATOM   3571 C  CA  . VAL B 1 137 ? 2.670   -2.969  -4.714  1.00 13.26  ? 360  VAL B CA  1 
ATOM   3572 C  C   . VAL B 1 137 ? 1.477   -2.025  -4.683  1.00 13.07  ? 360  VAL B C   1 
ATOM   3573 O  O   . VAL B 1 137 ? 0.545   -2.161  -5.489  1.00 14.53  ? 360  VAL B O   1 
ATOM   3574 C  CB  . VAL B 1 137 ? 3.572   -2.660  -5.924  1.00 14.73  ? 360  VAL B CB  1 
ATOM   3575 C  CG1 . VAL B 1 137 ? 3.981   -1.199  -5.915  1.00 15.82  ? 360  VAL B CG1 1 
ATOM   3576 C  CG2 . VAL B 1 137 ? 4.802   -3.529  -5.896  1.00 16.92  ? 360  VAL B CG2 1 
ATOM   3577 N  N   . ILE B 1 138 ? 1.511   -1.064  -3.763  1.00 13.09  ? 361  ILE B N   1 
ATOM   3578 C  CA  . ILE B 1 138 ? 0.496   -0.033  -3.650  1.00 13.41  ? 361  ILE B CA  1 
ATOM   3579 C  C   . ILE B 1 138 ? 1.163   1.268   -4.079  1.00 14.72  ? 361  ILE B C   1 
ATOM   3580 O  O   . ILE B 1 138 ? 2.007   1.825   -3.360  1.00 14.43  ? 361  ILE B O   1 
ATOM   3581 C  CB  . ILE B 1 138 ? -0.094  0.042   -2.236  1.00 12.86  ? 361  ILE B CB  1 
ATOM   3582 C  CG1 . ILE B 1 138 ? -0.833  -1.268  -1.908  1.00 13.85  ? 361  ILE B CG1 1 
ATOM   3583 C  CG2 . ILE B 1 138 ? -1.019  1.263   -2.097  1.00 14.58  ? 361  ILE B CG2 1 
ATOM   3584 C  CD1 . ILE B 1 138 ? -1.315  -1.372  -0.474  1.00 13.95  ? 361  ILE B CD1 1 
ATOM   3585 N  N   . SER B 1 139 ? 0.833   1.724   -5.282  1.00 15.97  ? 362  SER B N   1 
ATOM   3586 C  CA  . SER B 1 139 ? 1.369   2.981   -5.782  1.00 15.05  ? 362  SER B CA  1 
ATOM   3587 C  C   . SER B 1 139 ? 0.625   4.123   -5.108  1.00 15.49  ? 362  SER B C   1 
ATOM   3588 O  O   . SER B 1 139 ? -0.600  4.216   -5.215  1.00 15.26  ? 362  SER B O   1 
ATOM   3589 C  CB  . SER B 1 139 ? 1.147   3.068   -7.292  1.00 16.03  ? 362  SER B CB  1 
ATOM   3590 O  OG  . SER B 1 139 ? 1.539   4.364   -7.753  1.00 17.57  ? 362  SER B OG  1 
ATOM   3591 N  N   . THR B 1 140 ? 1.352   4.996   -4.413  1.00 14.57  ? 363  THR B N   1 
ATOM   3592 C  CA  . THR B 1 140 ? 0.678   6.111   -3.758  1.00 14.29  ? 363  THR B CA  1 
ATOM   3593 C  C   . THR B 1 140 ? 0.418   7.278   -4.700  1.00 15.11  ? 363  THR B C   1 
ATOM   3594 O  O   . THR B 1 140 ? -0.151  8.279   -4.257  1.00 16.58  ? 363  THR B O   1 
ATOM   3595 C  CB  . THR B 1 140 ? 1.457   6.595   -2.526  1.00 14.53  ? 363  THR B CB  1 
ATOM   3596 O  OG1 . THR B 1 140 ? 2.670   7.232   -2.941  1.00 14.43  ? 363  THR B OG1 1 
ATOM   3597 C  CG2 . THR B 1 140 ? 1.778   5.443   -1.584  1.00 15.28  ? 363  THR B CG2 1 
ATOM   3598 N  N   . VAL B 1 141 ? 0.835   7.175   -5.963  1.00 16.89  ? 364  VAL B N   1 
ATOM   3599 C  CA  . VAL B 1 141 ? 0.563   8.175   -6.994  1.00 17.67  ? 364  VAL B CA  1 
ATOM   3600 C  C   . VAL B 1 141 ? -0.455  7.701   -8.026  1.00 19.58  ? 364  VAL B C   1 
ATOM   3601 O  O   . VAL B 1 141 ? -0.755  8.449   -8.970  1.00 20.94  ? 364  VAL B O   1 
ATOM   3602 C  CB  . VAL B 1 141 ? 1.852   8.672   -7.683  1.00 19.05  ? 364  VAL B CB  1 
ATOM   3603 C  CG1 . VAL B 1 141 ? 2.767   9.361   -6.679  1.00 18.70  ? 364  VAL B CG1 1 
ATOM   3604 C  CG2 . VAL B 1 141 ? 2.585   7.521   -8.376  1.00 20.23  ? 364  VAL B CG2 1 
ATOM   3605 N  N   . ALA B 1 142 ? -0.990  6.486   -7.885  1.00 19.04  ? 365  ALA B N   1 
ATOM   3606 C  CA  . ALA B 1 142 ? -1.963  5.973   -8.841  1.00 19.51  ? 365  ALA B CA  1 
ATOM   3607 C  C   . ALA B 1 142 ? -3.268  6.763   -8.733  1.00 19.61  ? 365  ALA B C   1 
ATOM   3608 O  O   . ALA B 1 142 ? -3.635  7.228   -7.652  1.00 20.03  ? 365  ALA B O   1 
ATOM   3609 C  CB  . ALA B 1 142 ? -2.239  4.483   -8.588  1.00 19.43  ? 365  ALA B CB  1 
ATOM   3610 N  N   . PRO B 1 143 ? -3.973  6.961   -9.847  1.00 20.72  ? 366  PRO B N   1 
ATOM   3611 C  CA  . PRO B 1 143 ? -5.283  7.620   -9.760  1.00 20.66  ? 366  PRO B CA  1 
ATOM   3612 C  C   . PRO B 1 143 ? -6.230  6.964   -8.773  1.00 20.44  ? 366  PRO B C   1 
ATOM   3613 O  O   . PRO B 1 143 ? -7.070  7.643   -8.171  1.00 20.74  ? 366  PRO B O   1 
ATOM   3614 C  CB  . PRO B 1 143 ? -5.810  7.532   -11.198 1.00 22.38  ? 366  PRO B CB  1 
ATOM   3615 C  CG  . PRO B 1 143 ? -4.578  7.532   -12.031 1.00 22.51  ? 366  PRO B CG  1 
ATOM   3616 C  CD  . PRO B 1 143 ? -3.526  6.794   -11.240 1.00 21.28  ? 366  PRO B CD  1 
ATOM   3617 N  N   . ARG B 1 144 ? -6.111  5.653   -8.575  1.00 19.56  ? 367  ARG B N   1 
ATOM   3618 C  CA  . ARG B 1 144 ? -6.979  4.922   -7.666  1.00 19.10  ? 367  ARG B CA  1 
ATOM   3619 C  C   . ARG B 1 144 ? -6.407  4.803   -6.261  1.00 18.18  ? 367  ARG B C   1 
ATOM   3620 O  O   . ARG B 1 144 ? -6.959  4.066   -5.438  1.00 19.25  ? 367  ARG B O   1 
ATOM   3621 C  CB  . ARG B 1 144 ? -7.295  3.532   -8.232  1.00 18.05  ? 367  ARG B CB  1 
ATOM   3622 C  CG  . ARG B 1 144 ? -8.076  3.563   -9.541  1.00 22.36  ? 367  ARG B CG  1 
ATOM   3623 C  CD  . ARG B 1 144 ? -9.534  3.900   -9.298  1.00 31.35  ? 367  ARG B CD  1 
ATOM   3624 N  NE  . ARG B 1 144 ? -10.284 3.957   -10.547 1.00 122.60 ? 367  ARG B NE  1 
ATOM   3625 C  CZ  . ARG B 1 144 ? -11.603 4.063   -10.627 1.00 130.26 ? 367  ARG B CZ  1 
ATOM   3626 N  NH1 . ARG B 1 144 ? -12.360 4.114   -9.544  1.00 80.35  ? 367  ARG B NH1 1 
ATOM   3627 N  NH2 . ARG B 1 144 ? -12.177 4.115   -11.826 1.00 76.98  ? 367  ARG B NH2 1 
ATOM   3628 N  N   . PHE B 1 145 ? -5.326  5.527   -5.956  1.00 18.32  ? 368  PHE B N   1 
ATOM   3629 C  CA  . PHE B 1 145 ? -4.871  5.665   -4.570  1.00 16.90  ? 368  PHE B CA  1 
ATOM   3630 C  C   . PHE B 1 145 ? -5.737  6.745   -3.933  1.00 17.54  ? 368  PHE B C   1 
ATOM   3631 O  O   . PHE B 1 145 ? -5.458  7.947   -4.027  1.00 18.63  ? 368  PHE B O   1 
ATOM   3632 C  CB  . PHE B 1 145 ? -3.386  6.002   -4.488  1.00 16.34  ? 368  PHE B CB  1 
ATOM   3633 C  CG  . PHE B 1 145 ? -2.860  6.072   -3.071  1.00 16.05  ? 368  PHE B CG  1 
ATOM   3634 C  CD1 . PHE B 1 145 ? -2.569  4.912   -2.358  1.00 15.14  ? 368  PHE B CD1 1 
ATOM   3635 C  CD2 . PHE B 1 145 ? -2.650  7.296   -2.457  1.00 17.27  ? 368  PHE B CD2 1 
ATOM   3636 C  CE1 . PHE B 1 145 ? -2.093  4.984   -1.068  1.00 15.14  ? 368  PHE B CE1 1 
ATOM   3637 C  CE2 . PHE B 1 145 ? -2.173  7.355   -1.164  1.00 16.73  ? 368  PHE B CE2 1 
ATOM   3638 C  CZ  . PHE B 1 145 ? -1.890  6.202   -0.476  1.00 15.97  ? 368  PHE B CZ  1 
ATOM   3639 N  N   . THR B 1 146 ? -6.824  6.319   -3.292  1.00 17.99  ? 369  THR B N   1 
ATOM   3640 C  CA  . THR B 1 146 ? -7.796  7.236   -2.687  1.00 17.97  ? 369  THR B CA  1 
ATOM   3641 C  C   . THR B 1 146 ? -8.130  6.795   -1.268  1.00 18.18  ? 369  THR B C   1 
ATOM   3642 O  O   . THR B 1 146 ? -9.295  6.574   -0.931  1.00 18.48  ? 369  THR B O   1 
ATOM   3643 C  CB  . THR B 1 146 ? -9.063  7.343   -3.543  1.00 19.18  ? 369  THR B CB  1 
ATOM   3644 O  OG1 . THR B 1 146 ? -9.674  6.048   -3.693  1.00 21.40  ? 369  THR B OG1 1 
ATOM   3645 C  CG2 . THR B 1 146 ? -8.740  7.903   -4.922  1.00 19.52  ? 369  THR B CG2 1 
ATOM   3646 N  N   . PRO B 1 147 ? -7.119  6.666   -0.395  1.00 17.16  ? 370  PRO B N   1 
ATOM   3647 C  CA  . PRO B 1 147 ? -7.392  6.137   0.953   1.00 17.45  ? 370  PRO B CA  1 
ATOM   3648 C  C   . PRO B 1 147 ? -8.399  6.959   1.735   1.00 18.85  ? 370  PRO B C   1 
ATOM   3649 O  O   . PRO B 1 147 ? -9.154  6.398   2.538   1.00 19.38  ? 370  PRO B O   1 
ATOM   3650 C  CB  . PRO B 1 147 ? -6.007  6.135   1.622   1.00 16.23  ? 370  PRO B CB  1 
ATOM   3651 C  CG  . PRO B 1 147 ? -5.227  7.186   0.848   1.00 16.29  ? 370  PRO B CG  1 
ATOM   3652 C  CD  . PRO B 1 147 ? -5.694  6.996   -0.565  1.00 16.64  ? 370  PRO B CD  1 
ATOM   3653 N  N   . LYS B 1 148 ? -8.427  8.281   1.527   1.00 19.32  ? 371  LYS B N   1 
ATOM   3654 C  CA  . LYS B 1 148 ? -9.393  9.125   2.219   1.00 21.65  ? 371  LYS B CA  1 
ATOM   3655 C  C   . LYS B 1 148 ? -10.822 8.767   1.830   1.00 22.38  ? 371  LYS B C   1 
ATOM   3656 O  O   . LYS B 1 148 ? -11.744 8.932   2.637   1.00 23.25  ? 371  LYS B O   1 
ATOM   3657 C  CB  . LYS B 1 148 ? -9.073  10.595  1.926   1.00 24.22  ? 371  LYS B CB  1 
ATOM   3658 C  CG  . LYS B 1 148 ? -10.109 11.600  2.381   1.00 27.10  ? 371  LYS B CG  1 
ATOM   3659 C  CD  . LYS B 1 148 ? -10.084 11.844  3.866   1.00 29.87  ? 371  LYS B CD  1 
ATOM   3660 C  CE  . LYS B 1 148 ? -10.894 13.097  4.175   1.00 31.41  ? 371  LYS B CE  1 
ATOM   3661 N  NZ  . LYS B 1 148 ? -10.847 13.499  5.604   1.00 32.41  ? 371  LYS B NZ  1 
ATOM   3662 N  N   . LEU B 1 149 ? -11.018 8.240   0.620   1.00 21.01  ? 372  LEU B N   1 
ATOM   3663 C  CA  . LEU B 1 149 ? -12.321 7.792   0.154   1.00 22.01  ? 372  LEU B CA  1 
ATOM   3664 C  C   . LEU B 1 149 ? -12.568 6.318   0.447   1.00 22.66  ? 372  LEU B C   1 
ATOM   3665 O  O   . LEU B 1 149 ? -13.598 5.777   0.034   1.00 25.03  ? 372  LEU B O   1 
ATOM   3666 C  CB  . LEU B 1 149 ? -12.439 8.038   -1.351  1.00 23.42  ? 372  LEU B CB  1 
ATOM   3667 C  CG  . LEU B 1 149 ? -12.153 9.473   -1.795  1.00 25.11  ? 372  LEU B CG  1 
ATOM   3668 C  CD1 . LEU B 1 149 ? -12.325 9.599   -3.297  1.00 26.43  ? 372  LEU B CD1 1 
ATOM   3669 C  CD2 . LEU B 1 149 ? -13.065 10.444  -1.056  1.00 26.50  ? 372  LEU B CD2 1 
ATOM   3670 N  N   . GLY B 1 150 ? -11.635 5.648   1.113   1.00 20.99  ? 373  GLY B N   1 
ATOM   3671 C  CA  . GLY B 1 150 ? -11.838 4.299   1.581   1.00 21.20  ? 373  GLY B CA  1 
ATOM   3672 C  C   . GLY B 1 150 ? -11.262 3.194   0.725   1.00 19.84  ? 373  GLY B C   1 
ATOM   3673 O  O   . GLY B 1 150 ? -11.620 2.032   0.944   1.00 20.26  ? 373  GLY B O   1 
ATOM   3674 N  N   . SER B 1 151 ? -10.387 3.499   -0.234  1.00 20.07  ? 374  SER B N   1 
ATOM   3675 C  CA  . SER B 1 151 ? -9.830  2.422   -1.047  1.00 20.14  ? 374  SER B CA  1 
ATOM   3676 C  C   . SER B 1 151 ? -8.497  2.823   -1.663  1.00 18.04  ? 374  SER B C   1 
ATOM   3677 O  O   . SER B 1 151 ? -8.219  4.006   -1.884  1.00 17.93  ? 374  SER B O   1 
ATOM   3678 C  CB  . SER B 1 151 ? -10.793 1.987   -2.154  1.00 20.55  ? 374  SER B CB  1 
ATOM   3679 O  OG  . SER B 1 151 ? -10.989 3.035   -3.094  1.00 22.80  ? 374  SER B OG  1 
ATOM   3680 N  N   . VAL B 1 152 ? -7.669  1.810   -1.919  1.00 17.16  ? 375  VAL B N   1 
ATOM   3681 C  CA  . VAL B 1 152 ? -6.433  1.950   -2.671  1.00 16.68  ? 375  VAL B CA  1 
ATOM   3682 C  C   . VAL B 1 152 ? -6.390  0.814   -3.685  1.00 16.50  ? 375  VAL B C   1 
ATOM   3683 O  O   . VAL B 1 152 ? -7.108  -0.179  -3.564  1.00 17.30  ? 375  VAL B O   1 
ATOM   3684 C  CB  . VAL B 1 152 ? -5.177  1.943   -1.762  1.00 15.82  ? 375  VAL B CB  1 
ATOM   3685 C  CG1 . VAL B 1 152 ? -5.298  3.019   -0.700  1.00 17.02  ? 375  VAL B CG1 1 
ATOM   3686 C  CG2 . VAL B 1 152 ? -4.984  0.574   -1.111  1.00 17.42  ? 375  VAL B CG2 1 
ATOM   3687 N  N   . MET B 1 153 ? -5.555  0.976   -4.703  1.00 16.49  ? 376  MET B N   1 
ATOM   3688 C  CA  . MET B 1 153 ? -5.335  -0.066  -5.700  1.00 16.21  ? 376  MET B CA  1 
ATOM   3689 C  C   . MET B 1 153 ? -4.034  -0.793  -5.374  1.00 16.09  ? 376  MET B C   1 
ATOM   3690 O  O   . MET B 1 153 ? -3.015  -0.153  -5.085  1.00 16.46  ? 376  MET B O   1 
ATOM   3691 C  CB  . MET B 1 153 ? -5.277  0.537   -7.106  1.00 18.15  ? 376  MET B CB  1 
ATOM   3692 C  CG  . MET B 1 153 ? -5.088  -0.482  -8.218  1.00 19.22  ? 376  MET B CG  1 
ATOM   3693 S  SD  . MET B 1 153 ? -3.361  -0.813  -8.585  1.00 19.69  ? 376  MET B SD  1 
ATOM   3694 C  CE  . MET B 1 153 ? -2.921  0.716   -9.418  1.00 19.65  ? 376  MET B CE  1 
ATOM   3695 N  N   . ILE B 1 154 ? -4.067  -2.127  -5.422  1.00 15.16  ? 377  ILE B N   1 
ATOM   3696 C  CA  . ILE B 1 154 ? -2.878  -2.944  -5.225  1.00 15.28  ? 377  ILE B CA  1 
ATOM   3697 C  C   . ILE B 1 154 ? -2.617  -3.753  -6.489  1.00 16.02  ? 377  ILE B C   1 
ATOM   3698 O  O   . ILE B 1 154 ? -3.545  -4.331  -7.084  1.00 17.37  ? 377  ILE B O   1 
ATOM   3699 C  CB  . ILE B 1 154 ? -2.965  -3.826  -3.962  1.00 14.50  ? 377  ILE B CB  1 
ATOM   3700 C  CG1 . ILE B 1 154 ? -1.640  -4.565  -3.715  1.00 13.72  ? 377  ILE B CG1 1 
ATOM   3701 C  CG2 . ILE B 1 154 ? -4.155  -4.773  -4.024  1.00 15.40  ? 377  ILE B CG2 1 
ATOM   3702 C  CD1 . ILE B 1 154 ? -1.531  -5.165  -2.331  1.00 14.26  ? 377  ILE B CD1 1 
ATOM   3703 N  N   . GLY B 1 155 ? -1.361  -3.765  -6.915  1.00 15.62  ? 378  GLY B N   1 
ATOM   3704 C  CA  . GLY B 1 155 ? -0.926  -4.546  -8.064  1.00 16.43  ? 378  GLY B CA  1 
ATOM   3705 C  C   . GLY B 1 155 ? -0.182  -5.785  -7.617  1.00 16.64  ? 378  GLY B C   1 
ATOM   3706 O  O   . GLY B 1 155 ? 0.669   -5.733  -6.723  1.00 16.41  ? 378  GLY B O   1 
ATOM   3707 N  N   . THR B 1 156 ? -0.506  -6.907  -8.236  1.00 19.32  ? 379  THR B N   1 
ATOM   3708 C  CA  . THR B 1 156 ? 0.190   -8.147  -7.949  1.00 23.03  ? 379  THR B CA  1 
ATOM   3709 C  C   . THR B 1 156 ? 0.814   -8.663  -9.236  1.00 31.20  ? 379  THR B C   1 
ATOM   3710 O  O   . THR B 1 156 ? 0.501   -8.199  -10.333 1.00 32.14  ? 379  THR B O   1 
ATOM   3711 C  CB  . THR B 1 156 ? -0.751  -9.200  -7.343  1.00 21.70  ? 379  THR B CB  1 
ATOM   3712 O  OG1 . THR B 1 156 ? -1.815  -9.470  -8.263  1.00 22.68  ? 379  THR B OG1 1 
ATOM   3713 C  CG2 . THR B 1 156 ? -1.338  -8.699  -6.046  1.00 21.97  ? 379  THR B CG2 1 
ATOM   3714 N  N   . TRP B 1 157 ? 1.732   -9.607  -9.088  1.00 42.89  ? 380  TRP B N   1 
ATOM   3715 C  CA  . TRP B 1 157 ? 2.315   -10.257 -10.248 1.00 57.07  ? 380  TRP B CA  1 
ATOM   3716 C  C   . TRP B 1 157 ? 1.475   -11.434 -10.720 1.00 72.65  ? 380  TRP B C   1 
ATOM   3717 O  O   . TRP B 1 157 ? 1.548   -11.801 -11.898 1.00 72.20  ? 380  TRP B O   1 
ATOM   3718 C  CB  . TRP B 1 157 ? 3.764   -10.663 -9.952  1.00 56.38  ? 380  TRP B CB  1 
ATOM   3719 C  CG  . TRP B 1 157 ? 4.712   -9.481  -9.836  1.00 55.31  ? 380  TRP B CG  1 
ATOM   3720 C  CD1 . TRP B 1 157 ? 5.490   -8.960  -10.830 1.00 55.85  ? 380  TRP B CD1 1 
ATOM   3721 C  CD2 . TRP B 1 157 ? 4.970   -8.679  -8.668  1.00 53.41  ? 380  TRP B CD2 1 
ATOM   3722 N  NE1 . TRP B 1 157 ? 6.217   -7.893  -10.358 1.00 55.10  ? 380  TRP B NE1 1 
ATOM   3723 C  CE2 . TRP B 1 157 ? 5.916   -7.699  -9.034  1.00 53.29  ? 380  TRP B CE2 1 
ATOM   3724 C  CE3 . TRP B 1 157 ? 4.494   -8.697  -7.353  1.00 51.55  ? 380  TRP B CE3 1 
ATOM   3725 C  CZ2 . TRP B 1 157 ? 6.395   -6.746  -8.133  1.00 52.00  ? 380  TRP B CZ2 1 
ATOM   3726 C  CZ3 . TRP B 1 157 ? 4.974   -7.749  -6.460  1.00 50.62  ? 380  TRP B CZ3 1 
ATOM   3727 C  CH2 . TRP B 1 157 ? 5.914   -6.790  -6.854  1.00 50.47  ? 380  TRP B CH2 1 
ATOM   3728 N  N   . THR B 1 158 ? 0.665   -12.008 -9.833  1.00 88.55  ? 381  THR B N   1 
ATOM   3729 C  CA  . THR B 1 158 ? -0.349  -12.982 -10.207 1.00 34.86  ? 381  THR B CA  1 
ATOM   3730 C  C   . THR B 1 158 ? -1.636  -12.248 -10.563 1.00 61.14  ? 381  THR B C   1 
ATOM   3731 O  O   . THR B 1 158 ? -2.052  -11.327 -9.852  1.00 61.15  ? 381  THR B O   1 
ATOM   3732 C  CB  . THR B 1 158 ? -0.614  -13.943 -9.047  1.00 67.87  ? 381  THR B CB  1 
ATOM   3733 O  OG1 . THR B 1 158 ? -1.875  -14.596 -9.245  1.00 60.04  ? 381  THR B OG1 1 
ATOM   3734 C  CG2 . THR B 1 158 ? -0.632  -13.194 -7.715  1.00 40.59  ? 381  THR B CG2 1 
ATOM   3735 N  N   . THR B 1 159 ? -2.260  -12.650 -11.666 0.70 114.69 ? 382  THR B N   1 
ATOM   3736 C  CA  . THR B 1 159 ? -3.517  -12.059 -12.096 0.70 86.61  ? 382  THR B CA  1 
ATOM   3737 C  C   . THR B 1 159 ? -4.728  -12.853 -11.635 0.70 115.72 ? 382  THR B C   1 
ATOM   3738 O  O   . THR B 1 159 ? -5.839  -12.606 -12.116 0.70 35.15  ? 382  THR B O   1 
ATOM   3739 N  N   . ASP B 1 160 ? -4.547  -13.785 -10.701 1.00 52.69  ? 383  ASP B N   1 
ATOM   3740 C  CA  . ASP B 1 160 ? -5.615  -14.719 -10.382 1.00 57.11  ? 383  ASP B CA  1 
ATOM   3741 C  C   . ASP B 1 160 ? -5.864  -14.864 -8.884  1.00 28.53  ? 383  ASP B C   1 
ATOM   3742 O  O   . ASP B 1 160 ? -6.981  -14.628 -8.413  1.00 73.50  ? 383  ASP B O   1 
ATOM   3743 C  CB  . ASP B 1 160 ? -5.307  -16.082 -11.010 1.00 38.61  ? 383  ASP B CB  1 
ATOM   3744 N  N   . ASP B 1 161 ? -4.832  -15.244 -8.129  1.00 28.57  ? 384  ASP B N   1 
ATOM   3745 C  CA  . ASP B 1 161 ? -5.016  -15.829 -6.802  1.00 25.89  ? 384  ASP B CA  1 
ATOM   3746 C  C   . ASP B 1 161 ? -5.272  -14.795 -5.706  1.00 21.09  ? 384  ASP B C   1 
ATOM   3747 O  O   . ASP B 1 161 ? -4.665  -14.861 -4.632  1.00 20.60  ? 384  ASP B O   1 
ATOM   3748 C  CB  . ASP B 1 161 ? -3.808  -16.706 -6.453  1.00 28.31  ? 384  ASP B CB  1 
ATOM   3749 C  CG  . ASP B 1 161 ? -4.053  -17.605 -5.250  1.00 30.07  ? 384  ASP B CG  1 
ATOM   3750 O  OD1 . ASP B 1 161 ? -5.206  -18.050 -5.054  1.00 31.14  ? 384  ASP B OD1 1 
ATOM   3751 O  OD2 . ASP B 1 161 ? -3.086  -17.864 -4.502  1.00 30.10  ? 384  ASP B OD2 1 
ATOM   3752 N  N   . ILE B 1 162 ? -6.182  -13.858 -5.957  1.00 21.05  ? 385  ILE B N   1 
ATOM   3753 C  CA  . ILE B 1 162 ? -6.611  -12.853 -4.989  1.00 20.46  ? 385  ILE B CA  1 
ATOM   3754 C  C   . ILE B 1 162 ? -8.132  -12.884 -4.978  1.00 19.54  ? 385  ILE B C   1 
ATOM   3755 O  O   . ILE B 1 162 ? -8.762  -12.671 -6.020  1.00 21.66  ? 385  ILE B O   1 
ATOM   3756 C  CB  . ILE B 1 162 ? -6.127  -11.446 -5.381  1.00 19.63  ? 385  ILE B CB  1 
ATOM   3757 C  CG1 . ILE B 1 162 ? -4.602  -11.394 -5.478  1.00 21.08  ? 385  ILE B CG1 1 
ATOM   3758 C  CG2 . ILE B 1 162 ? -6.657  -10.409 -4.406  1.00 21.57  ? 385  ILE B CG2 1 
ATOM   3759 C  CD1 . ILE B 1 162 ? -3.893  -11.491 -4.147  1.00 21.96  ? 385  ILE B CD1 1 
ATOM   3760 N  N   . GLN B 1 163 ? -8.725  -13.127 -3.813  1.00 17.31  ? 386  GLN B N   1 
ATOM   3761 C  CA  A GLN B 1 163 ? -10.166 -13.306 -3.676  0.64 17.84  ? 386  GLN B CA  1 
ATOM   3762 C  CA  B GLN B 1 163 ? -10.169 -13.281 -3.723  0.36 17.30  ? 386  GLN B CA  1 
ATOM   3763 C  C   . GLN B 1 163 ? -10.808 -12.098 -3.004  1.00 17.10  ? 386  GLN B C   1 
ATOM   3764 O  O   . GLN B 1 163 ? -10.136 -11.245 -2.422  1.00 17.49  ? 386  GLN B O   1 
ATOM   3765 C  CB  A GLN B 1 163 ? -10.488 -14.580 -2.884  0.64 19.88  ? 386  GLN B CB  1 
ATOM   3766 C  CB  B GLN B 1 163 ? -10.538 -14.614 -3.063  0.36 18.05  ? 386  GLN B CB  1 
ATOM   3767 C  CG  A GLN B 1 163 ? -10.037 -15.857 -3.559  0.64 22.24  ? 386  GLN B CG  1 
ATOM   3768 C  CG  B GLN B 1 163 ? -9.896  -15.818 -3.742  0.36 18.72  ? 386  GLN B CG  1 
ATOM   3769 C  CD  A GLN B 1 163 ? -10.518 -17.103 -2.836  0.64 23.52  ? 386  GLN B CD  1 
ATOM   3770 C  CD  B GLN B 1 163 ? -10.195 -15.892 -5.232  0.36 19.35  ? 386  GLN B CD  1 
ATOM   3771 O  OE1 A GLN B 1 163 ? -11.457 -17.055 -2.039  0.64 25.54  ? 386  GLN B OE1 1 
ATOM   3772 O  OE1 B GLN B 1 163 ? -11.250 -15.455 -5.688  0.36 19.43  ? 386  GLN B OE1 1 
ATOM   3773 N  NE2 A GLN B 1 163 ? -9.875  -18.223 -3.112  0.64 24.99  ? 386  GLN B NE2 1 
ATOM   3774 N  NE2 B GLN B 1 163 ? -9.258  -16.441 -5.999  0.36 19.35  ? 386  GLN B NE2 1 
ATOM   3775 N  N   . ASP B 1 164 ? -12.139 -12.044 -3.082  1.00 17.36  ? 387  ASP B N   1 
ATOM   3776 C  CA  . ASP B 1 164 ? -12.916 -10.950 -2.498  1.00 18.43  ? 387  ASP B CA  1 
ATOM   3777 C  C   . ASP B 1 164 ? -13.140 -11.263 -1.020  1.00 18.89  ? 387  ASP B C   1 
ATOM   3778 O  O   . ASP B 1 164 ? -14.220 -11.675 -0.584  1.00 20.36  ? 387  ASP B O   1 
ATOM   3779 C  CB  . ASP B 1 164 ? -14.231 -10.774 -3.247  1.00 19.46  ? 387  ASP B CB  1 
ATOM   3780 C  CG  . ASP B 1 164 ? -14.043 -10.177 -4.637  1.00 21.74  ? 387  ASP B CG  1 
ATOM   3781 O  OD1 . ASP B 1 164 ? -12.905 -9.810  -4.993  1.00 21.23  ? 387  ASP B OD1 1 
ATOM   3782 O  OD2 . ASP B 1 164 ? -15.044 -10.078 -5.388  1.00 24.41  ? 387  ASP B OD2 1 
ATOM   3783 N  N   . GLN B 1 165 ? -12.086 -11.066 -0.239  1.00 17.67  ? 388  GLN B N   1 
ATOM   3784 C  CA  . GLN B 1 165 ? -11.996 -11.592 1.114   1.00 15.72  ? 388  GLN B CA  1 
ATOM   3785 C  C   . GLN B 1 165 ? -11.266 -10.600 2.010   1.00 15.65  ? 388  GLN B C   1 
ATOM   3786 O  O   . GLN B 1 165 ? -10.576 -9.701  1.518   1.00 15.21  ? 388  GLN B O   1 
ATOM   3787 C  CB  . GLN B 1 165 ? -11.237 -12.928 1.114   1.00 15.66  ? 388  GLN B CB  1 
ATOM   3788 C  CG  . GLN B 1 165 ? -12.004 -14.073 0.446   1.00 16.81  ? 388  GLN B CG  1 
ATOM   3789 C  CD  . GLN B 1 165 ? -13.261 -14.480 1.200   1.00 17.69  ? 388  GLN B CD  1 
ATOM   3790 O  OE1 . GLN B 1 165 ? -13.434 -14.155 2.375   1.00 17.67  ? 388  GLN B OE1 1 
ATOM   3791 N  NE2 . GLN B 1 165 ? -14.154 -15.185 0.515   1.00 20.39  ? 388  GLN B NE2 1 
ATOM   3792 N  N   . PRO B 1 166 ? -11.405 -10.741 3.331   1.00 16.03  ? 389  PRO B N   1 
ATOM   3793 C  CA  . PRO B 1 166 ? -10.655 -9.867  4.244   1.00 15.44  ? 389  PRO B CA  1 
ATOM   3794 C  C   . PRO B 1 166 ? -9.162  -9.950  3.975   1.00 14.64  ? 389  PRO B C   1 
ATOM   3795 O  O   . PRO B 1 166 ? -8.602  -11.034 3.790   1.00 15.94  ? 389  PRO B O   1 
ATOM   3796 C  CB  . PRO B 1 166 ? -11.006 -10.429 5.625   1.00 15.46  ? 389  PRO B CB  1 
ATOM   3797 C  CG  . PRO B 1 166 ? -12.365 -11.051 5.427   1.00 15.75  ? 389  PRO B CG  1 
ATOM   3798 C  CD  . PRO B 1 166 ? -12.299 -11.656 4.061   1.00 16.29  ? 389  PRO B CD  1 
ATOM   3799 N  N   . SER B 1 167 ? -8.515  -8.788  3.980   1.00 14.20  ? 390  SER B N   1 
ATOM   3800 C  CA  . SER B 1 167 ? -7.146  -8.659  3.516   1.00 14.39  ? 390  SER B CA  1 
ATOM   3801 C  C   . SER B 1 167 ? -6.394  -7.683  4.404   1.00 13.60  ? 390  SER B C   1 
ATOM   3802 O  O   . SER B 1 167 ? -6.966  -6.721  4.928   1.00 15.48  ? 390  SER B O   1 
ATOM   3803 C  CB  . SER B 1 167 ? -7.102  -8.130  2.080   1.00 15.21  ? 390  SER B CB  1 
ATOM   3804 O  OG  . SER B 1 167 ? -7.821  -8.993  1.217   1.00 14.65  ? 390  SER B OG  1 
ATOM   3805 N  N   . ARG B 1 168 ? -5.102  -7.939  4.569   1.00 12.39  ? 391  ARG B N   1 
ATOM   3806 C  CA  . ARG B 1 168 ? -4.222  -7.048  5.299   1.00 13.26  ? 391  ARG B CA  1 
ATOM   3807 C  C   . ARG B 1 168 ? -2.918  -6.941  4.530   1.00 12.59  ? 391  ARG B C   1 
ATOM   3808 O  O   . ARG B 1 168 ? -2.393  -7.943  4.031   1.00 14.95  ? 391  ARG B O   1 
ATOM   3809 C  CB  . ARG B 1 168 ? -3.950  -7.607  6.698   1.00 17.01  ? 391  ARG B CB  1 
ATOM   3810 C  CG  . ARG B 1 168 ? -3.612  -6.562  7.740   1.00 22.14  ? 391  ARG B CG  1 
ATOM   3811 C  CD  . ARG B 1 168 ? -2.122  -6.329  7.849   1.00 24.84  ? 391  ARG B CD  1 
ATOM   3812 N  NE  . ARG B 1 168 ? -1.818  -5.341  8.875   1.00 23.94  ? 391  ARG B NE  1 
ATOM   3813 C  CZ  . ARG B 1 168 ? -0.594  -5.078  9.306   1.00 23.41  ? 391  ARG B CZ  1 
ATOM   3814 N  NH1 . ARG B 1 168 ? 0.461   -5.689  8.793   1.00 22.81  ? 391  ARG B NH1 1 
ATOM   3815 N  NH2 . ARG B 1 168 ? -0.424  -4.180  10.274  1.00 24.07  ? 391  ARG B NH2 1 
ATOM   3816 N  N   . PHE B 1 169 ? -2.383  -5.728  4.457   1.00 12.21  ? 392  PHE B N   1 
ATOM   3817 C  CA  . PHE B 1 169 ? -1.126  -5.459  3.769   1.00 11.40  ? 392  PHE B CA  1 
ATOM   3818 C  C   . PHE B 1 169 ? -0.034  -5.195  4.798   1.00 10.46  ? 392  PHE B C   1 
ATOM   3819 O  O   . PHE B 1 169 ? -0.144  -4.252  5.592   1.00 11.88  ? 392  PHE B O   1 
ATOM   3820 C  CB  . PHE B 1 169 ? -1.275  -4.251  2.843   1.00 11.54  ? 392  PHE B CB  1 
ATOM   3821 C  CG  . PHE B 1 169 ? -0.015  -3.876  2.123   1.00 12.06  ? 392  PHE B CG  1 
ATOM   3822 C  CD1 . PHE B 1 169 ? 0.336   -4.522  0.941   1.00 12.55  ? 392  PHE B CD1 1 
ATOM   3823 C  CD2 . PHE B 1 169 ? 0.807   -2.852  2.599   1.00 11.61  ? 392  PHE B CD2 1 
ATOM   3824 C  CE1 . PHE B 1 169 ? 1.488   -4.167  0.248   1.00 13.56  ? 392  PHE B CE1 1 
ATOM   3825 C  CE2 . PHE B 1 169 ? 1.964   -2.495  1.919   1.00 13.72  ? 392  PHE B CE2 1 
ATOM   3826 C  CZ  . PHE B 1 169 ? 2.295   -3.133  0.735   1.00 13.24  ? 392  PHE B CZ  1 
ATOM   3827 N  N   . THR B 1 170 ? 1.009   -6.041  4.785   1.00 9.96   ? 393  THR B N   1 
ATOM   3828 C  CA  . THR B 1 170 ? 2.194   -5.856  5.615   1.00 10.05  ? 393  THR B CA  1 
ATOM   3829 C  C   . THR B 1 170 ? 3.279   -5.217  4.770   1.00 10.91  ? 393  THR B C   1 
ATOM   3830 O  O   . THR B 1 170 ? 3.695   -5.820  3.762   1.00 11.39  ? 393  THR B O   1 
ATOM   3831 C  CB  . THR B 1 170 ? 2.682   -7.208  6.138   1.00 11.29  ? 393  THR B CB  1 
ATOM   3832 O  OG1 . THR B 1 170 ? 1.657   -7.824  6.922   1.00 12.38  ? 393  THR B OG1 1 
ATOM   3833 C  CG2 . THR B 1 170 ? 3.957   -7.051  6.981   1.00 11.58  ? 393  THR B CG2 1 
ATOM   3834 N  N   . PRO B 1 171 ? 3.738   -4.011  5.103   1.00 10.07  ? 394  PRO B N   1 
ATOM   3835 C  CA  . PRO B 1 171 ? 4.756   -3.352  4.281   1.00 10.61  ? 394  PRO B CA  1 
ATOM   3836 C  C   . PRO B 1 171 ? 6.117   -3.981  4.484   1.00 11.20  ? 394  PRO B C   1 
ATOM   3837 O  O   . PRO B 1 171 ? 6.462   -4.456  5.568   1.00 12.11  ? 394  PRO B O   1 
ATOM   3838 C  CB  . PRO B 1 171 ? 4.753   -1.912  4.807   1.00 10.75  ? 394  PRO B CB  1 
ATOM   3839 C  CG  . PRO B 1 171 ? 4.344   -2.039  6.200   1.00 10.70  ? 394  PRO B CG  1 
ATOM   3840 C  CD  . PRO B 1 171 ? 3.326   -3.170  6.237   1.00 10.79  ? 394  PRO B CD  1 
ATOM   3841 N  N   . VAL B 1 172 ? 6.915   -3.960  3.418   1.00 10.44  ? 395  VAL B N   1 
ATOM   3842 C  CA  . VAL B 1 172 ? 8.297   -4.414  3.471   1.00 10.41  ? 395  VAL B CA  1 
ATOM   3843 C  C   . VAL B 1 172 ? 9.273   -3.319  3.064   1.00 10.70  ? 395  VAL B C   1 
ATOM   3844 O  O   . VAL B 1 172 ? 10.316  -3.137  3.704   1.00 11.39  ? 395  VAL B O   1 
ATOM   3845 C  CB  . VAL B 1 172 ? 8.498   -5.681  2.614   1.00 10.94  ? 395  VAL B CB  1 
ATOM   3846 C  CG1 . VAL B 1 172 ? 9.978   -6.108  2.582   1.00 11.54  ? 395  VAL B CG1 1 
ATOM   3847 C  CG2 . VAL B 1 172 ? 7.606   -6.818  3.130   1.00 12.32  ? 395  VAL B CG2 1 
ATOM   3848 N  N   . GLY B 1 173 ? 8.963   -2.578  2.006   1.00 10.67  ? 396  GLY B N   1 
ATOM   3849 C  CA  . GLY B 1 173 ? 9.848   -1.531  1.535   1.00 10.44  ? 396  GLY B CA  1 
ATOM   3850 C  C   . GLY B 1 173 ? 9.272   -0.846  0.324   1.00 10.64  ? 396  GLY B C   1 
ATOM   3851 O  O   . GLY B 1 173 ? 8.065   -0.584  0.270   1.00 11.28  ? 396  GLY B O   1 
ATOM   3852 N  N   . LEU B 1 174 ? 10.125  -0.562  -0.654  1.00 11.26  ? 397  LEU B N   1 
ATOM   3853 C  CA  . LEU B 1 174 ? 9.713   0.077   -1.895  1.00 11.33  ? 397  LEU B CA  1 
ATOM   3854 C  C   . LEU B 1 174 ? 9.872   -0.906  -3.047  1.00 12.29  ? 397  LEU B C   1 
ATOM   3855 O  O   . LEU B 1 174 ? 10.734  -1.787  -3.016  1.00 13.48  ? 397  LEU B O   1 
ATOM   3856 C  CB  . LEU B 1 174 ? 10.558  1.321   -2.192  1.00 12.40  ? 397  LEU B CB  1 
ATOM   3857 C  CG  . LEU B 1 174 ? 10.509  2.449   -1.167  1.00 12.84  ? 397  LEU B CG  1 
ATOM   3858 C  CD1 . LEU B 1 174 ? 11.511  3.520   -1.553  1.00 14.23  ? 397  LEU B CD1 1 
ATOM   3859 C  CD2 . LEU B 1 174 ? 9.114   3.047   -1.080  1.00 16.15  ? 397  LEU B CD2 1 
ATOM   3860 N  N   . ASN B 1 175 ? 9.053   -0.744  -4.085  1.00 13.43  ? 398  ASN B N   1 
ATOM   3861 C  CA  . ASN B 1 175 ? 9.247   -1.588  -5.258  1.00 15.18  ? 398  ASN B CA  1 
ATOM   3862 C  C   . ASN B 1 175 ? 10.521  -1.205  -5.993  1.00 15.46  ? 398  ASN B C   1 
ATOM   3863 O  O   . ASN B 1 175 ? 11.249  -2.069  -6.500  1.00 16.83  ? 398  ASN B O   1 
ATOM   3864 C  CB  . ASN B 1 175 ? 8.051   -1.494  -6.196  1.00 16.19  ? 398  ASN B CB  1 
ATOM   3865 C  CG  . ASN B 1 175 ? 8.202   -2.420  -7.375  1.00 20.41  ? 398  ASN B CG  1 
ATOM   3866 O  OD1 . ASN B 1 175 ? 8.262   -3.629  -7.198  1.00 21.52  ? 398  ASN B OD1 1 
ATOM   3867 N  ND2 . ASN B 1 175 ? 8.326   -1.861  -8.575  1.00 25.19  ? 398  ASN B ND2 1 
ATOM   3868 N  N   . ASP B 1 176 ? 10.793  0.088   -6.047  1.00 15.63  ? 399  ASP B N   1 
ATOM   3869 C  CA  . ASP B 1 176 ? 11.912  0.706   -6.734  1.00 17.66  ? 399  ASP B CA  1 
ATOM   3870 C  C   . ASP B 1 176 ? 11.974  2.104   -6.141  1.00 16.85  ? 399  ASP B C   1 
ATOM   3871 O  O   . ASP B 1 176 ? 11.079  2.510   -5.398  1.00 17.25  ? 399  ASP B O   1 
ATOM   3872 C  CB  . ASP B 1 176 ? 11.638  0.762   -8.239  1.00 20.69  ? 399  ASP B CB  1 
ATOM   3873 C  CG  . ASP B 1 176 ? 10.442  1.649   -8.582  1.00 23.46  ? 399  ASP B CG  1 
ATOM   3874 O  OD1 . ASP B 1 176 ? 10.587  2.883   -8.563  1.00 23.48  ? 399  ASP B OD1 1 
ATOM   3875 O  OD2 . ASP B 1 176 ? 9.351   1.115   -8.865  1.00 26.40  ? 399  ASP B OD2 1 
ATOM   3876 N  N   . ASP B 1 177 ? 13.020  2.853   -6.470  1.00 17.35  ? 400  ASP B N   1 
ATOM   3877 C  CA  . ASP B 1 177 ? 13.051  4.237   -6.012  1.00 19.13  ? 400  ASP B CA  1 
ATOM   3878 C  C   . ASP B 1 177 ? 13.182  5.221   -7.170  1.00 20.25  ? 400  ASP B C   1 
ATOM   3879 O  O   . ASP B 1 177 ? 13.793  6.278   -7.029  1.00 24.21  ? 400  ASP B O   1 
ATOM   3880 C  CB  . ASP B 1 177 ? 14.074  4.462   -4.896  1.00 22.66  ? 400  ASP B CB  1 
ATOM   3881 C  CG  . ASP B 1 177 ? 15.492  4.466   -5.394  1.00 26.92  ? 400  ASP B CG  1 
ATOM   3882 O  OD1 . ASP B 1 177 ? 15.739  3.933   -6.491  1.00 28.43  ? 400  ASP B OD1 1 
ATOM   3883 O  OD2 . ASP B 1 177 ? 16.359  5.024   -4.686  1.00 29.69  ? 400  ASP B OD2 1 
ATOM   3884 N  N   . ASP B 1 178 ? 12.580  4.881   -8.311  1.00 19.76  ? 401  ASP B N   1 
ATOM   3885 C  CA  . ASP B 1 178 ? 12.660  5.729   -9.497  1.00 20.90  ? 401  ASP B CA  1 
ATOM   3886 C  C   . ASP B 1 178 ? 12.066  7.107   -9.240  1.00 20.70  ? 401  ASP B C   1 
ATOM   3887 O  O   . ASP B 1 178 ? 12.613  8.124   -9.691  1.00 23.04  ? 401  ASP B O   1 
ATOM   3888 C  CB  . ASP B 1 178 ? 11.908  5.067   -10.647 1.00 23.31  ? 401  ASP B CB  1 
ATOM   3889 C  CG  . ASP B 1 178 ? 12.544  3.770   -11.103 1.00 29.94  ? 401  ASP B CG  1 
ATOM   3890 O  OD1 . ASP B 1 178 ? 13.650  3.437   -10.637 1.00 31.84  ? 401  ASP B OD1 1 
ATOM   3891 O  OD2 . ASP B 1 178 ? 11.927  3.088   -11.945 1.00 33.90  ? 401  ASP B OD2 1 
ATOM   3892 N  N   . ASN B 1 179 ? 10.939  7.165   -8.528  1.00 18.88  ? 402  ASN B N   1 
ATOM   3893 C  CA  . ASN B 1 179 ? 10.269  8.431   -8.256  1.00 20.12  ? 402  ASN B CA  1 
ATOM   3894 C  C   . ASN B 1 179 ? 9.840   8.532   -6.801  1.00 19.99  ? 402  ASN B C   1 
ATOM   3895 O  O   . ASN B 1 179 ? 8.814   9.138   -6.486  1.00 21.28  ? 402  ASN B O   1 
ATOM   3896 C  CB  . ASN B 1 179 ? 9.088   8.645   -9.195  1.00 24.57  ? 402  ASN B CB  1 
ATOM   3897 C  CG  . ASN B 1 179 ? 9.518   8.717   -10.640 1.00 30.06  ? 402  ASN B CG  1 
ATOM   3898 O  OD1 . ASN B 1 179 ? 10.179  9.668   -11.044 1.00 32.17  ? 402  ASN B OD1 1 
ATOM   3899 N  ND2 . ASN B 1 179 ? 9.162   7.705   -11.423 1.00 32.70  ? 402  ASN B ND2 1 
ATOM   3900 N  N   . TYR B 1 180 ? 10.634  7.950   -5.907  1.00 16.01  ? 403  TYR B N   1 
ATOM   3901 C  CA  . TYR B 1 180 ? 10.355  7.989   -4.479  1.00 14.58  ? 403  TYR B CA  1 
ATOM   3902 C  C   . TYR B 1 180 ? 10.665  9.387   -3.941  1.00 14.23  ? 403  TYR B C   1 
ATOM   3903 O  O   . TYR B 1 180 ? 11.813  9.843   -3.987  1.00 15.87  ? 403  TYR B O   1 
ATOM   3904 C  CB  . TYR B 1 180 ? 11.207  6.928   -3.783  1.00 13.00  ? 403  TYR B CB  1 
ATOM   3905 C  CG  . TYR B 1 180 ? 11.272  7.063   -2.286  1.00 12.33  ? 403  TYR B CG  1 
ATOM   3906 C  CD1 . TYR B 1 180 ? 10.115  7.110   -1.519  1.00 12.97  ? 403  TYR B CD1 1 
ATOM   3907 C  CD2 . TYR B 1 180 ? 12.496  7.121   -1.637  1.00 12.85  ? 403  TYR B CD2 1 
ATOM   3908 C  CE1 . TYR B 1 180 ? 10.174  7.226   -0.140  1.00 12.68  ? 403  TYR B CE1 1 
ATOM   3909 C  CE2 . TYR B 1 180 ? 12.574  7.228   -0.267  1.00 12.01  ? 403  TYR B CE2 1 
ATOM   3910 C  CZ  . TYR B 1 180 ? 11.413  7.281   0.489   1.00 12.32  ? 403  TYR B CZ  1 
ATOM   3911 O  OH  . TYR B 1 180 ? 11.496  7.395   1.871   1.00 12.70  ? 403  TYR B OH  1 
ATOM   3912 N  N   . LYS B 1 181 ? 9.642   10.074  -3.437  1.00 12.57  ? 404  LYS B N   1 
ATOM   3913 C  CA  . LYS B 1 181 ? 9.785   11.446  -2.946  1.00 12.04  ? 404  LYS B CA  1 
ATOM   3914 C  C   . LYS B 1 181 ? 9.232   11.510  -1.527  1.00 12.47  ? 404  LYS B C   1 
ATOM   3915 O  O   . LYS B 1 181 ? 8.020   11.666  -1.332  1.00 12.30  ? 404  LYS B O   1 
ATOM   3916 C  CB  . LYS B 1 181 ? 9.050   12.417  -3.865  1.00 13.14  ? 404  LYS B CB  1 
ATOM   3917 C  CG  . LYS B 1 181 ? 9.596   12.450  -5.279  1.00 16.84  ? 404  LYS B CG  1 
ATOM   3918 C  CD  . LYS B 1 181 ? 10.985  13.062  -5.331  1.00 32.31  ? 404  LYS B CD  1 
ATOM   3919 C  CE  . LYS B 1 181 ? 11.533  13.055  -6.752  1.00 51.01  ? 404  LYS B CE  1 
ATOM   3920 N  NZ  . LYS B 1 181 ? 11.733  11.670  -7.259  1.00 111.32 ? 404  LYS B NZ  1 
ATOM   3921 N  N   . GLN B 1 182 ? 10.126  11.400  -0.534  1.00 11.55  ? 405  GLN B N   1 
ATOM   3922 C  CA  . GLN B 1 182 ? 9.691   11.296  0.855   1.00 11.59  ? 405  GLN B CA  1 
ATOM   3923 C  C   . GLN B 1 182 ? 9.070   12.587  1.373   1.00 12.02  ? 405  GLN B C   1 
ATOM   3924 O  O   . GLN B 1 182 ? 8.324   12.539  2.358   1.00 12.99  ? 405  GLN B O   1 
ATOM   3925 C  CB  . GLN B 1 182 ? 10.827  10.824  1.768   1.00 12.72  ? 405  GLN B CB  1 
ATOM   3926 C  CG  . GLN B 1 182 ? 11.886  11.898  2.042   1.00 12.19  ? 405  GLN B CG  1 
ATOM   3927 C  CD  . GLN B 1 182 ? 12.701  11.590  3.283   1.00 12.08  ? 405  GLN B CD  1 
ATOM   3928 O  OE1 . GLN B 1 182 ? 12.183  10.983  4.228   1.00 12.69  ? 405  GLN B OE1 1 
ATOM   3929 N  NE2 . GLN B 1 182 ? 13.983  11.983  3.286   1.00 12.87  ? 405  GLN B NE2 1 
ATOM   3930 N  N   . TRP B 1 183 ? 9.354   13.734  0.737   1.00 10.90  ? 406  TRP B N   1 
ATOM   3931 C  CA  . TRP B 1 183 ? 8.795   15.020  1.143   1.00 11.98  ? 406  TRP B CA  1 
ATOM   3932 C  C   . TRP B 1 183 ? 7.703   15.500  0.197   1.00 13.16  ? 406  TRP B C   1 
ATOM   3933 O  O   . TRP B 1 183 ? 7.465   16.708  0.084   1.00 14.53  ? 406  TRP B O   1 
ATOM   3934 C  CB  . TRP B 1 183 ? 9.876   16.095  1.309   1.00 12.56  ? 406  TRP B CB  1 
ATOM   3935 C  CG  . TRP B 1 183 ? 10.987  15.717  2.269   1.00 11.97  ? 406  TRP B CG  1 
ATOM   3936 C  CD1 . TRP B 1 183 ? 12.332  15.766  2.011   1.00 13.17  ? 406  TRP B CD1 1 
ATOM   3937 C  CD2 . TRP B 1 183 ? 10.859  15.246  3.628   1.00 13.09  ? 406  TRP B CD2 1 
ATOM   3938 N  NE1 . TRP B 1 183 ? 13.042  15.350  3.113   1.00 14.08  ? 406  TRP B NE1 1 
ATOM   3939 C  CE2 . TRP B 1 183 ? 12.167  15.037  4.121   1.00 12.19  ? 406  TRP B CE2 1 
ATOM   3940 C  CE3 . TRP B 1 183 ? 9.774   14.988  4.468   1.00 12.61  ? 406  TRP B CE3 1 
ATOM   3941 C  CZ2 . TRP B 1 183 ? 12.418  14.577  5.421   1.00 13.25  ? 406  TRP B CZ2 1 
ATOM   3942 C  CZ3 . TRP B 1 183 ? 10.020  14.523  5.752   1.00 13.47  ? 406  TRP B CZ3 1 
ATOM   3943 C  CH2 . TRP B 1 183 ? 11.334  14.322  6.218   1.00 13.67  ? 406  TRP B CH2 1 
ATOM   3944 N  N   A GLU B 1 184 ? 7.049   14.593  -0.511  0.68 13.90  ? 407  GLU B N   1 
ATOM   3945 N  N   B GLU B 1 184 ? 7.038   14.577  -0.489  0.32 12.91  ? 407  GLU B N   1 
ATOM   3946 C  CA  A GLU B 1 184 ? 5.890   14.956  -1.311  0.68 13.41  ? 407  GLU B CA  1 
ATOM   3947 C  CA  B GLU B 1 184 ? 5.896   14.881  -1.339  0.32 12.34  ? 407  GLU B CA  1 
ATOM   3948 C  C   A GLU B 1 184 ? 4.728   14.078  -0.890  0.68 13.11  ? 407  GLU B C   1 
ATOM   3949 C  C   B GLU B 1 184 ? 4.724   14.044  -0.853  0.32 12.64  ? 407  GLU B C   1 
ATOM   3950 O  O   A GLU B 1 184 ? 4.828   12.848  -0.933  0.68 14.08  ? 407  GLU B O   1 
ATOM   3951 O  O   B GLU B 1 184 ? 4.811   12.812  -0.816  0.32 13.12  ? 407  GLU B O   1 
ATOM   3952 C  CB  A GLU B 1 184 ? 6.151   14.853  -2.813  0.68 15.17  ? 407  GLU B CB  1 
ATOM   3953 C  CB  B GLU B 1 184 ? 6.204   14.582  -2.808  0.32 12.62  ? 407  GLU B CB  1 
ATOM   3954 C  CG  A GLU B 1 184 ? 5.141   15.673  -3.593  0.68 15.57  ? 407  GLU B CG  1 
ATOM   3955 C  CG  B GLU B 1 184 ? 7.272   15.494  -3.389  0.32 12.32  ? 407  GLU B CG  1 
ATOM   3956 C  CD  A GLU B 1 184 ? 5.536   15.936  -5.038  0.68 17.43  ? 407  GLU B CD  1 
ATOM   3957 C  CD  B GLU B 1 184 ? 7.478   15.310  -4.879  0.32 14.51  ? 407  GLU B CD  1 
ATOM   3958 O  OE1 A GLU B 1 184 ? 6.709   15.711  -5.398  0.68 19.48  ? 407  GLU B OE1 1 
ATOM   3959 O  OE1 B GLU B 1 184 ? 6.542   14.850  -5.567  0.32 15.18  ? 407  GLU B OE1 1 
ATOM   3960 O  OE2 A GLU B 1 184 ? 4.667   16.397  -5.809  0.68 18.89  ? 407  GLU B OE2 1 
ATOM   3961 O  OE2 B GLU B 1 184 ? 8.584   15.629  -5.361  0.32 15.32  ? 407  GLU B OE2 1 
ATOM   3962 N  N   . LEU B 1 185 ? 3.641   14.709  -0.466  1.00 12.99  ? 408  LEU B N   1 
ATOM   3963 C  CA  . LEU B 1 185 ? 2.496   13.971  0.042   1.00 13.75  ? 408  LEU B CA  1 
ATOM   3964 C  C   . LEU B 1 185 ? 1.692   13.393  -1.117  1.00 14.05  ? 408  LEU B C   1 
ATOM   3965 O  O   . LEU B 1 185 ? 1.593   14.014  -2.178  1.00 15.37  ? 408  LEU B O   1 
ATOM   3966 C  CB  . LEU B 1 185 ? 1.582   14.888  0.843   1.00 13.23  ? 408  LEU B CB  1 
ATOM   3967 C  CG  . LEU B 1 185 ? 2.173   15.412  2.151   1.00 13.62  ? 408  LEU B CG  1 
ATOM   3968 C  CD1 . LEU B 1 185 ? 1.187   16.395  2.763   1.00 15.27  ? 408  LEU B CD1 1 
ATOM   3969 C  CD2 . LEU B 1 185 ? 2.487   14.280  3.134   1.00 15.65  ? 408  LEU B CD2 1 
ATOM   3970 N  N   . PRO B 1 186 ? 1.130   12.202  -0.941  1.00 14.20  ? 409  PRO B N   1 
ATOM   3971 C  CA  A PRO B 1 186 ? 0.177   11.685  -1.930  0.47 16.01  ? 409  PRO B CA  1 
ATOM   3972 C  CA  B PRO B 1 186 ? 0.183   11.692  -1.937  0.53 16.46  ? 409  PRO B CA  1 
ATOM   3973 C  C   . PRO B 1 186 ? -1.087  12.525  -1.924  1.00 17.55  ? 409  PRO B C   1 
ATOM   3974 O  O   . PRO B 1 186 ? -1.359  13.302  -1.007  1.00 18.42  ? 409  PRO B O   1 
ATOM   3975 C  CB  A PRO B 1 186 ? -0.130  10.265  -1.439  0.47 16.84  ? 409  PRO B CB  1 
ATOM   3976 C  CB  B PRO B 1 186 ? -0.088  10.261  -1.469  0.53 18.28  ? 409  PRO B CB  1 
ATOM   3977 C  CG  A PRO B 1 186 ? 0.896   9.954   -0.396  0.47 14.88  ? 409  PRO B CG  1 
ATOM   3978 C  CG  B PRO B 1 186 ? 0.160   10.293  -0.002  0.53 16.85  ? 409  PRO B CG  1 
ATOM   3979 C  CD  A PRO B 1 186 ? 1.314   11.280  0.188   0.47 14.90  ? 409  PRO B CD  1 
ATOM   3980 C  CD  B PRO B 1 186 ? 1.271   11.301  0.213   0.53 15.70  ? 409  PRO B CD  1 
ATOM   3981 N  N   . ASN B 1 187 ? -1.874  12.351  -2.977  1.00 20.18  ? 410  ASN B N   1 
ATOM   3982 C  CA  . ASN B 1 187 ? -3.204  12.935  -3.038  1.00 22.98  ? 410  ASN B CA  1 
ATOM   3983 C  C   . ASN B 1 187 ? -4.146  11.922  -2.398  1.00 21.95  ? 410  ASN B C   1 
ATOM   3984 O  O   . ASN B 1 187 ? -4.576  10.966  -3.048  1.00 21.99  ? 410  ASN B O   1 
ATOM   3985 C  CB  . ASN B 1 187 ? -3.560  13.221  -4.490  1.00 27.05  ? 410  ASN B CB  1 
ATOM   3986 C  CG  . ASN B 1 187 ? -2.697  14.308  -5.085  1.00 32.95  ? 410  ASN B CG  1 
ATOM   3987 O  OD1 . ASN B 1 187 ? -2.426  15.319  -4.436  1.00 36.09  ? 410  ASN B OD1 1 
ATOM   3988 N  ND2 . ASN B 1 187 ? -2.246  14.105  -6.318  1.00 35.12  ? 410  ASN B ND2 1 
ATOM   3989 N  N   . TYR B 1 188 ? -4.462  12.120  -1.113  1.00 21.38  ? 411  TYR B N   1 
ATOM   3990 C  CA  . TYR B 1 188 ? -5.219  11.113  -0.370  1.00 20.05  ? 411  TYR B CA  1 
ATOM   3991 C  C   . TYR B 1 188 ? -6.614  10.854  -0.945  1.00 20.40  ? 411  TYR B C   1 
ATOM   3992 O  O   . TYR B 1 188 ? -7.197  9.797   -0.671  1.00 19.88  ? 411  TYR B O   1 
ATOM   3993 C  CB  . TYR B 1 188 ? -5.297  11.472  1.117   1.00 20.04  ? 411  TYR B CB  1 
ATOM   3994 C  CG  . TYR B 1 188 ? -3.963  11.538  1.841   1.00 18.61  ? 411  TYR B CG  1 
ATOM   3995 C  CD1 . TYR B 1 188 ? -3.244  10.380  2.138   1.00 17.34  ? 411  TYR B CD1 1 
ATOM   3996 C  CD2 . TYR B 1 188 ? -3.446  12.749  2.286   1.00 18.59  ? 411  TYR B CD2 1 
ATOM   3997 C  CE1 . TYR B 1 188 ? -2.033  10.437  2.821   1.00 16.38  ? 411  TYR B CE1 1 
ATOM   3998 C  CE2 . TYR B 1 188 ? -2.240  12.813  2.961   1.00 17.45  ? 411  TYR B CE2 1 
ATOM   3999 C  CZ  . TYR B 1 188 ? -1.538  11.660  3.238   1.00 15.54  ? 411  TYR B CZ  1 
ATOM   4000 O  OH  . TYR B 1 188 ? -0.344  11.755  3.925   1.00 15.43  ? 411  TYR B OH  1 
ATOM   4001 N  N   . SER B 1 189 ? -7.176  11.777  -1.735  1.00 23.27  ? 412  SER B N   1 
ATOM   4002 C  CA  . SER B 1 189 ? -8.463  11.543  -2.388  1.00 25.44  ? 412  SER B CA  1 
ATOM   4003 C  C   . SER B 1 189 ? -8.353  11.469  -3.909  1.00 27.99  ? 412  SER B C   1 
ATOM   4004 O  O   . SER B 1 189 ? -9.372  11.598  -4.605  1.00 29.15  ? 412  SER B O   1 
ATOM   4005 C  CB  . SER B 1 189 ? -9.485  12.606  -1.983  1.00 27.46  ? 412  SER B CB  1 
ATOM   4006 O  OG  . SER B 1 189 ? -9.876  12.471  -0.631  1.00 29.41  ? 412  SER B OG  1 
ATOM   4007 N  N   . GLY B 1 190 ? -7.152  11.263  -4.442  1.00 31.41  ? 413  GLY B N   1 
ATOM   4008 C  CA  . GLY B 1 190 ? -6.962  11.156  -5.877  1.00 38.24  ? 413  GLY B CA  1 
ATOM   4009 C  C   . GLY B 1 190 ? -6.870  12.517  -6.547  1.00 48.60  ? 413  GLY B C   1 
ATOM   4010 O  O   . GLY B 1 190 ? -6.611  13.536  -5.912  1.00 42.78  ? 413  GLY B O   1 
ATOM   4011 N  N   . ALA B 1 191 ? -7.101  12.531  -7.862  1.00 66.65  ? 414  ALA B N   1 
ATOM   4012 C  CA  . ALA B 1 191 ? -7.130  13.809  -8.567  1.00 86.58  ? 414  ALA B CA  1 
ATOM   4013 C  C   . ALA B 1 191 ? -8.153  14.770  -7.969  1.00 108.29 ? 414  ALA B C   1 
ATOM   4014 O  O   . ALA B 1 191 ? -8.075  15.977  -8.219  1.00 106.91 ? 414  ALA B O   1 
ATOM   4015 C  CB  . ALA B 1 191 ? -7.382  13.601  -10.062 1.00 85.81  ? 414  ALA B CB  1 
ATOM   4016 N  N   . LEU B 1 192 ? -9.094  14.258  -7.173  1.00 132.42 ? 415  LEU B N   1 
ATOM   4017 C  CA  . LEU B 1 192 ? -10.067 15.059  -6.444  1.00 64.48  ? 415  LEU B CA  1 
ATOM   4018 C  C   . LEU B 1 192 ? -9.575  15.481  -5.062  1.00 69.19  ? 415  LEU B C   1 
ATOM   4019 O  O   . LEU B 1 192 ? -10.398 15.742  -4.177  1.00 74.84  ? 415  LEU B O   1 
ATOM   4020 C  CB  . LEU B 1 192 ? -11.385 14.294  -6.314  1.00 64.22  ? 415  LEU B CB  1 
ATOM   4021 N  N   . THR B 1 193 ? -8.262  15.571  -4.862  1.00 70.49  ? 416  THR B N   1 
ATOM   4022 C  CA  . THR B 1 193 ? -7.705  15.747  -3.526  1.00 93.16  ? 416  THR B CA  1 
ATOM   4023 C  C   . THR B 1 193 ? -7.727  17.210  -3.111  1.00 76.20  ? 416  THR B C   1 
ATOM   4024 O  O   . THR B 1 193 ? -7.133  18.064  -3.776  1.00 30.30  ? 416  THR B O   1 
ATOM   4025 C  CB  . THR B 1 193 ? -6.277  15.209  -3.469  1.00 104.53 ? 416  THR B CB  1 
ATOM   4026 O  OG1 . THR B 1 193 ? -6.315  13.810  -3.170  1.00 65.39  ? 416  THR B OG1 1 
ATOM   4027 C  CG2 . THR B 1 193 ? -5.441  15.932  -2.415  1.00 45.36  ? 416  THR B CG2 1 
ATOM   4028 N  N   . LEU B 1 194 ? -8.419  17.490  -2.014  1.00 65.08  ? 417  LEU B N   1 
ATOM   4029 C  CA  . LEU B 1 194 ? -8.164  18.658  -1.181  1.00 53.70  ? 417  LEU B CA  1 
ATOM   4030 C  C   . LEU B 1 194 ? -7.821  18.066  0.180   1.00 44.62  ? 417  LEU B C   1 
ATOM   4031 O  O   . LEU B 1 194 ? -8.720  17.698  0.942   1.00 44.09  ? 417  LEU B O   1 
ATOM   4032 C  CB  . LEU B 1 194 ? -9.389  19.558  -1.096  1.00 52.65  ? 417  LEU B CB  1 
ATOM   4033 C  CG  . LEU B 1 194 ? -9.096  21.048  -0.899  1.00 51.41  ? 417  LEU B CG  1 
ATOM   4034 C  CD1 . LEU B 1 194 ? -8.268  21.582  -2.055  1.00 49.47  ? 417  LEU B CD1 1 
ATOM   4035 C  CD2 . LEU B 1 194 ? -10.377 21.842  -0.749  1.00 50.02  ? 417  LEU B CD2 1 
ATOM   4036 N  N   . ASN B 1 195 ? -6.527  17.949  0.471   1.00 39.15  ? 418  ASN B N   1 
ATOM   4037 C  CA  . ASN B 1 195 ? -6.084  17.317  1.711   1.00 35.23  ? 418  ASN B CA  1 
ATOM   4038 C  C   . ASN B 1 195 ? -6.477  18.189  2.902   1.00 36.56  ? 418  ASN B C   1 
ATOM   4039 O  O   . ASN B 1 195 ? -6.148  19.379  2.941   1.00 39.48  ? 418  ASN B O   1 
ATOM   4040 C  CB  . ASN B 1 195 ? -4.568  17.106  1.675   1.00 34.41  ? 418  ASN B CB  1 
ATOM   4041 C  CG  . ASN B 1 195 ? -4.152  15.906  0.821   1.00 33.89  ? 418  ASN B CG  1 
ATOM   4042 O  OD1 . ASN B 1 195 ? -4.965  15.040  0.499   1.00 34.84  ? 418  ASN B OD1 1 
ATOM   4043 N  ND2 . ASN B 1 195 ? -2.871  15.849  0.468   1.00 34.36  ? 418  ASN B ND2 1 
ATOM   4044 N  N   . MET B 1 196 ? -7.205  17.613  3.857   1.00 33.84  ? 419  MET B N   1 
ATOM   4045 C  CA  . MET B 1 196 ? -7.600  18.310  5.073   1.00 34.65  ? 419  MET B CA  1 
ATOM   4046 C  C   . MET B 1 196 ? -7.015  17.611  6.294   1.00 28.94  ? 419  MET B C   1 
ATOM   4047 O  O   . MET B 1 196 ? -6.665  16.428  6.252   1.00 29.31  ? 419  MET B O   1 
ATOM   4048 C  CB  . MET B 1 196 ? -9.129  18.381  5.216   1.00 43.08  ? 419  MET B CB  1 
ATOM   4049 C  CG  . MET B 1 196 ? -9.801  19.326  4.238   1.00 37.70  ? 419  MET B CG  1 
ATOM   4050 S  SD  . MET B 1 196 ? -9.278  21.042  4.446   1.00 34.87  ? 419  MET B SD  1 
ATOM   4051 C  CE  . MET B 1 196 ? -9.699  21.679  2.825   1.00 40.22  ? 419  MET B CE  1 
ATOM   4052 N  N   . GLY B 1 197 ? -6.911  18.363  7.390   1.00 24.88  ? 420  GLY B N   1 
ATOM   4053 C  CA  . GLY B 1 197 ? -6.435  17.806  8.642   1.00 22.85  ? 420  GLY B CA  1 
ATOM   4054 C  C   . GLY B 1 197 ? -4.954  17.524  8.688   1.00 19.22  ? 420  GLY B C   1 
ATOM   4055 O  O   . GLY B 1 197 ? -4.511  16.715  9.502   1.00 19.92  ? 420  GLY B O   1 
ATOM   4056 N  N   . LEU B 1 198 ? -4.165  18.165  7.833   1.00 17.46  ? 421  LEU B N   1 
ATOM   4057 C  CA  . LEU B 1 198 ? -2.746  17.845  7.762   1.00 15.57  ? 421  LEU B CA  1 
ATOM   4058 C  C   . LEU B 1 198 ? -2.002  18.401  8.971   1.00 15.17  ? 421  LEU B C   1 
ATOM   4059 O  O   . LEU B 1 198 ? -2.290  19.504  9.446   1.00 17.19  ? 421  LEU B O   1 
ATOM   4060 C  CB  . LEU B 1 198 ? -2.142  18.450  6.499   1.00 16.52  ? 421  LEU B CB  1 
ATOM   4061 C  CG  . LEU B 1 198 ? -2.588  17.872  5.157   1.00 17.33  ? 421  LEU B CG  1 
ATOM   4062 C  CD1 . LEU B 1 198 ? -1.982  18.694  4.029   1.00 18.75  ? 421  LEU B CD1 1 
ATOM   4063 C  CD2 . LEU B 1 198 ? -2.225  16.391  5.008   1.00 17.76  ? 421  LEU B CD2 1 
ATOM   4064 N  N   . ALA B 1 199 ? -1.045  17.626  9.467   1.00 14.37  ? 422  ALA B N   1 
ATOM   4065 C  CA  . ALA B 1 199 ? -0.039  18.173  10.362  1.00 14.40  ? 422  ALA B CA  1 
ATOM   4066 C  C   . ALA B 1 199 ? 0.762   19.226  9.599   1.00 13.41  ? 422  ALA B C   1 
ATOM   4067 O  O   . ALA B 1 199 ? 1.000   19.063  8.396   1.00 13.72  ? 422  ALA B O   1 
ATOM   4068 C  CB  . ALA B 1 199 ? 0.891   17.050  10.833  1.00 14.84  ? 422  ALA B CB  1 
ATOM   4069 N  N   . PRO B 1 200 ? 1.158   20.322  10.245  1.00 14.84  ? 423  PRO B N   1 
ATOM   4070 C  CA  . PRO B 1 200 ? 1.800   21.425  9.520   1.00 14.90  ? 423  PRO B CA  1 
ATOM   4071 C  C   . PRO B 1 200 ? 3.214   21.077  9.070   1.00 14.07  ? 423  PRO B C   1 
ATOM   4072 O  O   . PRO B 1 200 ? 3.867   20.173  9.600   1.00 14.38  ? 423  PRO B O   1 
ATOM   4073 C  CB  . PRO B 1 200 ? 1.816   22.558  10.556  1.00 16.56  ? 423  PRO B CB  1 
ATOM   4074 C  CG  . PRO B 1 200 ? 1.833   21.862  11.868  1.00 19.11  ? 423  PRO B CG  1 
ATOM   4075 C  CD  . PRO B 1 200 ? 0.991   20.622  11.678  1.00 17.54  ? 423  PRO B CD  1 
ATOM   4076 N  N   . SER B 1 201 ? 3.684   21.808  8.059   1.00 14.62  ? 424  SER B N   1 
ATOM   4077 C  CA  . SER B 1 201 ? 5.073   21.670  7.663   1.00 14.80  ? 424  SER B CA  1 
ATOM   4078 C  C   . SER B 1 201 ? 5.971   22.243  8.754   1.00 14.86  ? 424  SER B C   1 
ATOM   4079 O  O   . SER B 1 201 ? 5.549   23.066  9.571   1.00 17.17  ? 424  SER B O   1 
ATOM   4080 C  CB  . SER B 1 201 ? 5.340   22.360  6.329   1.00 17.37  ? 424  SER B CB  1 
ATOM   4081 O  OG  . SER B 1 201 ? 5.120   23.759  6.432   1.00 19.31  ? 424  SER B OG  1 
ATOM   4082 N  N   . VAL B 1 202 ? 7.215   21.773  8.789   1.00 13.86  ? 425  VAL B N   1 
ATOM   4083 C  CA  . VAL B 1 202 ? 8.185   22.205  9.787   1.00 14.13  ? 425  VAL B CA  1 
ATOM   4084 C  C   . VAL B 1 202 ? 9.425   22.713  9.072   1.00 15.29  ? 425  VAL B C   1 
ATOM   4085 O  O   . VAL B 1 202 ? 9.748   22.273  7.965   1.00 15.28  ? 425  VAL B O   1 
ATOM   4086 C  CB  . VAL B 1 202 ? 8.548   21.070  10.779  1.00 14.90  ? 425  VAL B CB  1 
ATOM   4087 C  CG1 . VAL B 1 202 ? 7.312   20.597  11.514  1.00 16.83  ? 425  VAL B CG1 1 
ATOM   4088 C  CG2 . VAL B 1 202 ? 9.235   19.889  10.072  1.00 15.59  ? 425  VAL B CG2 1 
ATOM   4089 N  N   . PHE B 1 203 ? 10.139  23.638  9.721   1.00 16.96  ? 426  PHE B N   1 
ATOM   4090 C  CA  A PHE B 1 203 ? 11.297  24.236  9.087   0.54 17.79  ? 426  PHE B CA  1 
ATOM   4091 C  CA  B PHE B 1 203 ? 11.219  24.373  9.057   0.46 18.03  ? 426  PHE B CA  1 
ATOM   4092 C  C   . PHE B 1 203 ? 12.126  24.950  10.143  1.00 18.16  ? 426  PHE B C   1 
ATOM   4093 O  O   . PHE B 1 203 ? 11.585  25.419  11.147  1.00 18.57  ? 426  PHE B O   1 
ATOM   4094 C  CB  A PHE B 1 203 ? 10.886  25.211  7.979   0.54 17.94  ? 426  PHE B CB  1 
ATOM   4095 C  CB  B PHE B 1 203 ? 10.575  25.528  8.273   0.46 18.37  ? 426  PHE B CB  1 
ATOM   4096 C  CG  A PHE B 1 203 ? 9.704   26.045  8.334   0.54 18.30  ? 426  PHE B CG  1 
ATOM   4097 C  CG  B PHE B 1 203 ? 11.485  26.200  7.278   0.46 18.45  ? 426  PHE B CG  1 
ATOM   4098 C  CD1 A PHE B 1 203 ? 9.857   27.226  9.040   0.54 19.63  ? 426  PHE B CD1 1 
ATOM   4099 C  CD1 B PHE B 1 203 ? 12.372  27.182  7.672   0.46 18.96  ? 426  PHE B CD1 1 
ATOM   4100 C  CD2 A PHE B 1 203 ? 8.432   25.631  7.991   0.54 17.97  ? 426  PHE B CD2 1 
ATOM   4101 C  CD2 B PHE B 1 203 ? 11.427  25.865  5.940   0.46 17.93  ? 426  PHE B CD2 1 
ATOM   4102 C  CE1 A PHE B 1 203 ? 8.762   27.978  9.380   0.54 20.36  ? 426  PHE B CE1 1 
ATOM   4103 C  CE1 B PHE B 1 203 ? 13.210  27.801  6.750   0.46 18.02  ? 426  PHE B CE1 1 
ATOM   4104 C  CE2 A PHE B 1 203 ? 7.335   26.383  8.322   0.54 19.46  ? 426  PHE B CE2 1 
ATOM   4105 C  CE2 B PHE B 1 203 ? 12.247  26.476  5.013   0.46 18.16  ? 426  PHE B CE2 1 
ATOM   4106 C  CZ  A PHE B 1 203 ? 7.499   27.558  9.015   0.54 20.26  ? 426  PHE B CZ  1 
ATOM   4107 C  CZ  B PHE B 1 203 ? 13.139  27.449  5.418   0.46 18.95  ? 426  PHE B CZ  1 
ATOM   4108 N  N   . PRO B 1 204 ? 13.442  24.972  9.963   1.00 18.38  ? 427  PRO B N   1 
ATOM   4109 C  CA  . PRO B 1 204 ? 14.306  25.684  10.921  1.00 19.58  ? 427  PRO B CA  1 
ATOM   4110 C  C   . PRO B 1 204 ? 14.282  27.172  10.603  1.00 24.33  ? 427  PRO B C   1 
ATOM   4111 O  O   . PRO B 1 204 ? 14.522  27.577  9.466   1.00 30.67  ? 427  PRO B O   1 
ATOM   4112 C  CB  . PRO B 1 204 ? 15.692  25.087  10.646  1.00 21.25  ? 427  PRO B CB  1 
ATOM   4113 C  CG  . PRO B 1 204 ? 15.644  24.692  9.196   1.00 22.24  ? 427  PRO B CG  1 
ATOM   4114 C  CD  . PRO B 1 204 ? 14.215  24.306  8.901   1.00 19.34  ? 427  PRO B CD  1 
ATOM   4115 N  N   . THR B 1 205 ? 13.995  27.989  11.614  1.00 23.45  ? 428  THR B N   1 
ATOM   4116 C  CA  . THR B 1 205 ? 13.932  29.431  11.407  1.00 24.65  ? 428  THR B CA  1 
ATOM   4117 C  C   . THR B 1 205 ? 15.196  30.161  11.834  1.00 24.68  ? 428  THR B C   1 
ATOM   4118 O  O   . THR B 1 205 ? 15.507  31.218  11.272  1.00 27.18  ? 428  THR B O   1 
ATOM   4119 C  CB  . THR B 1 205 ? 12.732  30.024  12.153  1.00 27.38  ? 428  THR B CB  1 
ATOM   4120 O  OG1 . THR B 1 205 ? 12.863  29.764  13.559  1.00 28.75  ? 428  THR B OG1 1 
ATOM   4121 C  CG2 . THR B 1 205 ? 11.433  29.413  11.636  1.00 27.94  ? 428  THR B CG2 1 
ATOM   4122 N  N   . TYR B 1 206 ? 15.928  29.637  12.804  1.00 24.49  ? 429  TYR B N   1 
ATOM   4123 C  CA  . TYR B 1 206 ? 17.068  30.367  13.341  1.00 26.09  ? 429  TYR B CA  1 
ATOM   4124 C  C   . TYR B 1 206 ? 18.282  30.184  12.431  1.00 25.27  ? 429  TYR B C   1 
ATOM   4125 O  O   . TYR B 1 206 ? 18.505  29.090  11.908  1.00 25.30  ? 429  TYR B O   1 
ATOM   4126 C  CB  . TYR B 1 206 ? 17.397  29.860  14.746  1.00 27.87  ? 429  TYR B CB  1 
ATOM   4127 C  CG  . TYR B 1 206 ? 18.395  30.720  15.487  1.00 30.34  ? 429  TYR B CG  1 
ATOM   4128 C  CD1 . TYR B 1 206 ? 18.014  31.937  16.034  1.00 31.46  ? 429  TYR B CD1 1 
ATOM   4129 C  CD2 . TYR B 1 206 ? 19.720  30.321  15.639  1.00 30.70  ? 429  TYR B CD2 1 
ATOM   4130 C  CE1 . TYR B 1 206 ? 18.921  32.735  16.708  1.00 32.72  ? 429  TYR B CE1 1 
ATOM   4131 C  CE2 . TYR B 1 206 ? 20.636  31.115  16.313  1.00 32.56  ? 429  TYR B CE2 1 
ATOM   4132 C  CZ  . TYR B 1 206 ? 20.227  32.314  16.848  1.00 32.86  ? 429  TYR B CZ  1 
ATOM   4133 O  OH  . TYR B 1 206 ? 21.121  33.114  17.518  1.00 34.63  ? 429  TYR B OH  1 
ATOM   4134 N  N   . PRO B 1 207 ? 19.087  31.229  12.230  1.00 25.76  ? 430  PRO B N   1 
ATOM   4135 C  CA  . PRO B 1 207 ? 20.199  31.119  11.279  1.00 25.73  ? 430  PRO B CA  1 
ATOM   4136 C  C   . PRO B 1 207 ? 21.212  30.068  11.705  1.00 26.24  ? 430  PRO B C   1 
ATOM   4137 O  O   . PRO B 1 207 ? 21.577  29.963  12.879  1.00 27.57  ? 430  PRO B O   1 
ATOM   4138 C  CB  . PRO B 1 207 ? 20.813  32.524  11.295  1.00 26.93  ? 430  PRO B CB  1 
ATOM   4139 C  CG  . PRO B 1 207 ? 19.695  33.399  11.694  1.00 27.30  ? 430  PRO B CG  1 
ATOM   4140 C  CD  . PRO B 1 207 ? 18.908  32.614  12.696  1.00 26.40  ? 430  PRO B CD  1 
ATOM   4141 N  N   . GLY B 1 208 ? 21.669  29.286  10.727  1.00 24.37  ? 431  GLY B N   1 
ATOM   4142 C  CA  . GLY B 1 208 ? 22.641  28.243  10.961  1.00 23.77  ? 431  GLY B CA  1 
ATOM   4143 C  C   . GLY B 1 208 ? 22.062  26.905  11.358  1.00 21.67  ? 431  GLY B C   1 
ATOM   4144 O  O   . GLY B 1 208 ? 22.828  25.959  11.563  1.00 22.83  ? 431  GLY B O   1 
ATOM   4145 N  N   . GLU B 1 209 ? 20.744  26.791  11.467  1.00 19.27  ? 432  GLU B N   1 
ATOM   4146 C  CA  . GLU B 1 209 ? 20.117  25.560  11.925  1.00 17.15  ? 432  GLU B CA  1 
ATOM   4147 C  C   . GLU B 1 209 ? 19.562  24.737  10.771  1.00 16.78  ? 432  GLU B C   1 
ATOM   4148 O  O   . GLU B 1 209 ? 19.120  25.273  9.752   1.00 16.93  ? 432  GLU B O   1 
ATOM   4149 C  CB  . GLU B 1 209 ? 19.014  25.832  12.948  1.00 17.50  ? 432  GLU B CB  1 
ATOM   4150 C  CG  . GLU B 1 209 ? 19.567  26.292  14.277  1.00 18.24  ? 432  GLU B CG  1 
ATOM   4151 C  CD  . GLU B 1 209 ? 18.524  26.421  15.367  1.00 18.77  ? 432  GLU B CD  1 
ATOM   4152 O  OE1 . GLU B 1 209 ? 17.395  25.911  15.201  1.00 19.74  ? 432  GLU B OE1 1 
ATOM   4153 O  OE2 . GLU B 1 209 ? 18.845  27.037  16.405  1.00 19.81  ? 432  GLU B OE2 1 
ATOM   4154 N  N   . GLN B 1 210 ? 19.606  23.420  10.953  1.00 15.60  ? 433  GLN B N   1 
ATOM   4155 C  CA  . GLN B 1 210 ? 18.961  22.460  10.069  1.00 13.79  ? 433  GLN B CA  1 
ATOM   4156 C  C   . GLN B 1 210 ? 18.095  21.537  10.913  1.00 12.74  ? 433  GLN B C   1 
ATOM   4157 O  O   . GLN B 1 210 ? 18.297  21.410  12.126  1.00 14.40  ? 433  GLN B O   1 
ATOM   4158 C  CB  . GLN B 1 210 ? 19.989  21.603  9.310   1.00 15.51  ? 433  GLN B CB  1 
ATOM   4159 C  CG  . GLN B 1 210 ? 20.647  22.347  8.157   1.00 17.36  ? 433  GLN B CG  1 
ATOM   4160 C  CD  . GLN B 1 210 ? 21.739  21.555  7.449   1.00 20.44  ? 433  GLN B CD  1 
ATOM   4161 O  OE1 . GLN B 1 210 ? 22.295  22.013  6.443   1.00 24.54  ? 433  GLN B OE1 1 
ATOM   4162 N  NE2 . GLN B 1 210 ? 22.060  20.371  7.973   1.00 19.10  ? 433  GLN B NE2 1 
ATOM   4163 N  N   . LEU B 1 211 ? 17.141  20.872  10.264  1.00 11.52  ? 434  LEU B N   1 
ATOM   4164 C  CA  . LEU B 1 211 ? 16.407  19.815  10.935  1.00 12.05  ? 434  LEU B CA  1 
ATOM   4165 C  C   . LEU B 1 211 ? 17.329  18.628  11.191  1.00 12.19  ? 434  LEU B C   1 
ATOM   4166 O  O   . LEU B 1 211 ? 18.236  18.343  10.412  1.00 12.87  ? 434  LEU B O   1 
ATOM   4167 C  CB  . LEU B 1 211 ? 15.258  19.337  10.051  1.00 12.59  ? 434  LEU B CB  1 
ATOM   4168 C  CG  . LEU B 1 211 ? 14.164  20.373  9.834   1.00 13.42  ? 434  LEU B CG  1 
ATOM   4169 C  CD1 . LEU B 1 211 ? 13.213  19.944  8.724   1.00 14.43  ? 434  LEU B CD1 1 
ATOM   4170 C  CD2 . LEU B 1 211 ? 13.401  20.558  11.108  1.00 16.72  ? 434  LEU B CD2 1 
ATOM   4171 N  N   . LEU B 1 212 ? 17.103  17.953  12.316  1.00 12.21  ? 435  LEU B N   1 
ATOM   4172 C  CA  A LEU B 1 212 ? 17.755  16.690  12.624  0.65 12.06  ? 435  LEU B CA  1 
ATOM   4173 C  CA  B LEU B 1 212 ? 17.754  16.688  12.630  0.35 11.89  ? 435  LEU B CA  1 
ATOM   4174 C  C   . LEU B 1 212 ? 16.726  15.584  12.451  1.00 12.22  ? 435  LEU B C   1 
ATOM   4175 O  O   . LEU B 1 212 ? 15.596  15.705  12.935  1.00 14.19  ? 435  LEU B O   1 
ATOM   4176 C  CB  A LEU B 1 212 ? 18.262  16.691  14.066  0.65 12.86  ? 435  LEU B CB  1 
ATOM   4177 C  CB  B LEU B 1 212 ? 18.254  16.676  14.077  0.35 12.08  ? 435  LEU B CB  1 
ATOM   4178 C  CG  A LEU B 1 212 ? 18.994  15.414  14.485  0.65 14.15  ? 435  LEU B CG  1 
ATOM   4179 C  CG  B LEU B 1 212 ? 18.871  15.374  14.609  0.35 12.28  ? 435  LEU B CG  1 
ATOM   4180 C  CD1 A LEU B 1 212 ? 20.338  15.333  13.785  0.65 14.30  ? 435  LEU B CD1 1 
ATOM   4181 C  CD1 B LEU B 1 212 ? 19.937  15.705  15.628  0.35 11.90  ? 435  LEU B CD1 1 
ATOM   4182 C  CD2 A LEU B 1 212 ? 19.168  15.357  16.002  0.65 14.26  ? 435  LEU B CD2 1 
ATOM   4183 C  CD2 B LEU B 1 212 ? 17.840  14.442  15.242  0.35 12.78  ? 435  LEU B CD2 1 
ATOM   4184 N  N   . PHE B 1 213 ? 17.114  14.511  11.764  1.00 11.97  ? 436  PHE B N   1 
ATOM   4185 C  CA  . PHE B 1 213 ? 16.195  13.422  11.479  1.00 11.75  ? 436  PHE B CA  1 
ATOM   4186 C  C   . PHE B 1 213 ? 16.684  12.122  12.095  1.00 10.47  ? 436  PHE B C   1 
ATOM   4187 O  O   . PHE B 1 213 ? 17.885  11.913  12.304  1.00 12.40  ? 436  PHE B O   1 
ATOM   4188 C  CB  . PHE B 1 213 ? 16.037  13.192  9.965   1.00 12.77  ? 436  PHE B CB  1 
ATOM   4189 C  CG  . PHE B 1 213 ? 15.495  14.381  9.224   1.00 14.04  ? 436  PHE B CG  1 
ATOM   4190 C  CD1 . PHE B 1 213 ? 14.159  14.732  9.346   1.00 14.82  ? 436  PHE B CD1 1 
ATOM   4191 C  CD2 . PHE B 1 213 ? 16.312  15.160  8.409   1.00 15.57  ? 436  PHE B CD2 1 
ATOM   4192 C  CE1 . PHE B 1 213 ? 13.640  15.822  8.655   1.00 15.40  ? 436  PHE B CE1 1 
ATOM   4193 C  CE2 . PHE B 1 213 ? 15.803  16.273  7.734   1.00 16.12  ? 436  PHE B CE2 1 
ATOM   4194 C  CZ  . PHE B 1 213 ? 14.468  16.594  7.853   1.00 15.57  ? 436  PHE B CZ  1 
ATOM   4195 N  N   . PHE B 1 214 ? 15.732  11.235  12.343  1.00 9.98   ? 437  PHE B N   1 
ATOM   4196 C  CA  . PHE B 1 214 ? 16.018  9.842   12.669  1.00 9.99   ? 437  PHE B CA  1 
ATOM   4197 C  C   . PHE B 1 214 ? 15.780  9.060   11.381  1.00 9.99   ? 437  PHE B C   1 
ATOM   4198 O  O   . PHE B 1 214 ? 14.640  8.983   10.894  1.00 10.80  ? 437  PHE B O   1 
ATOM   4199 C  CB  . PHE B 1 214 ? 15.108  9.367   13.798  1.00 11.51  ? 437  PHE B CB  1 
ATOM   4200 C  CG  . PHE B 1 214 ? 15.256  10.173  15.060  1.00 10.29  ? 437  PHE B CG  1 
ATOM   4201 C  CD1 . PHE B 1 214 ? 14.618  11.401  15.188  1.00 11.51  ? 437  PHE B CD1 1 
ATOM   4202 C  CD2 . PHE B 1 214 ? 16.043  9.721   16.116  1.00 11.73  ? 437  PHE B CD2 1 
ATOM   4203 C  CE1 . PHE B 1 214 ? 14.757  12.155  16.339  1.00 11.27  ? 437  PHE B CE1 1 
ATOM   4204 C  CE2 . PHE B 1 214 ? 16.181  10.462  17.273  1.00 12.59  ? 437  PHE B CE2 1 
ATOM   4205 C  CZ  . PHE B 1 214 ? 15.543  11.682  17.388  1.00 11.42  ? 437  PHE B CZ  1 
ATOM   4206 N  N   . ARG B 1 215 ? 16.854  8.517   10.815  1.00 10.79  ? 438  ARG B N   1 
ATOM   4207 C  CA  . ARG B 1 215 ? 16.857  7.970   9.462   1.00 10.55  ? 438  ARG B CA  1 
ATOM   4208 C  C   . ARG B 1 215 ? 16.930  6.447   9.456   1.00 10.72  ? 438  ARG B C   1 
ATOM   4209 O  O   . ARG B 1 215 ? 17.709  5.849   10.208  1.00 11.66  ? 438  ARG B O   1 
ATOM   4210 C  CB  . ARG B 1 215 ? 18.050  8.522   8.679   1.00 10.63  ? 438  ARG B CB  1 
ATOM   4211 C  CG  . ARG B 1 215 ? 18.197  7.919   7.284   1.00 11.37  ? 438  ARG B CG  1 
ATOM   4212 C  CD  . ARG B 1 215 ? 19.211  8.654   6.432   1.00 13.08  ? 438  ARG B CD  1 
ATOM   4213 N  NE  . ARG B 1 215 ? 18.735  9.993   6.138   1.00 13.72  ? 438  ARG B NE  1 
ATOM   4214 C  CZ  . ARG B 1 215 ? 19.299  10.807  5.255   1.00 14.94  ? 438  ARG B CZ  1 
ATOM   4215 N  NH1 . ARG B 1 215 ? 20.398  10.459  4.606   1.00 17.48  ? 438  ARG B NH1 1 
ATOM   4216 N  NH2 . ARG B 1 215 ? 18.752  12.001  5.026   1.00 15.83  ? 438  ARG B NH2 1 
ATOM   4217 N  N   . SER B 1 216 ? 16.152  5.829   8.574   1.00 11.32  ? 439  SER B N   1 
ATOM   4218 C  CA  . SER B 1 216 ? 16.260  4.394   8.315   1.00 10.99  ? 439  SER B CA  1 
ATOM   4219 C  C   . SER B 1 216 ? 16.369  4.138   6.821   1.00 11.57  ? 439  SER B C   1 
ATOM   4220 O  O   . SER B 1 216 ? 15.639  4.743   6.027   1.00 12.26  ? 439  SER B O   1 
ATOM   4221 C  CB  . SER B 1 216 ? 15.031  3.624   8.807   1.00 10.88  ? 439  SER B CB  1 
ATOM   4222 O  OG  . SER B 1 216 ? 14.819  3.832   10.184  1.00 11.56  ? 439  SER B OG  1 
ATOM   4223 N  N   A TYR B 1 217 ? 17.304  3.277   6.436   0.46 11.60  ? 440  TYR B N   1 
ATOM   4224 N  N   B TYR B 1 217 ? 17.220  3.187   6.448   0.54 12.62  ? 440  TYR B N   1 
ATOM   4225 C  CA  A TYR B 1 217 ? 17.280  2.738   5.088   0.46 11.93  ? 440  TYR B CA  1 
ATOM   4226 C  CA  B TYR B 1 217 ? 17.317  2.734   5.066   0.54 12.52  ? 440  TYR B CA  1 
ATOM   4227 C  C   A TYR B 1 217 ? 16.105  1.785   4.956   0.46 12.41  ? 440  TYR B C   1 
ATOM   4228 C  C   B TYR B 1 217 ? 16.360  1.565   4.835   0.54 13.19  ? 440  TYR B C   1 
ATOM   4229 O  O   A TYR B 1 217 ? 15.638  1.198   5.937   0.46 13.97  ? 440  TYR B O   1 
ATOM   4230 O  O   B TYR B 1 217 ? 16.311  0.628   5.637   0.54 14.62  ? 440  TYR B O   1 
ATOM   4231 C  CB  A TYR B 1 217 ? 18.574  1.985   4.792   0.46 13.86  ? 440  TYR B CB  1 
ATOM   4232 C  CB  B TYR B 1 217 ? 18.769  2.381   4.731   0.54 13.99  ? 440  TYR B CB  1 
ATOM   4233 C  CG  A TYR B 1 217 ? 19.767  2.891   4.660   0.46 14.88  ? 440  TYR B CG  1 
ATOM   4234 C  CG  B TYR B 1 217 ? 19.608  3.628   4.567   0.54 14.68  ? 440  TYR B CG  1 
ATOM   4235 C  CD1 A TYR B 1 217 ? 19.906  3.728   3.562   0.46 16.48  ? 440  TYR B CD1 1 
ATOM   4236 C  CD1 B TYR B 1 217 ? 20.086  4.321   5.676   0.54 15.21  ? 440  TYR B CD1 1 
ATOM   4237 C  CD2 A TYR B 1 217 ? 20.765  2.903   5.624   0.46 17.35  ? 440  TYR B CD2 1 
ATOM   4238 C  CD2 B TYR B 1 217 ? 19.881  4.145   3.306   0.54 16.86  ? 440  TYR B CD2 1 
ATOM   4239 C  CE1 A TYR B 1 217 ? 20.995  4.564   3.436   0.46 17.49  ? 440  TYR B CE1 1 
ATOM   4240 C  CE1 B TYR B 1 217 ? 20.836  5.481   5.529   0.54 17.35  ? 440  TYR B CE1 1 
ATOM   4241 C  CE2 A TYR B 1 217 ? 21.861  3.739   5.503   0.46 18.18  ? 440  TYR B CE2 1 
ATOM   4242 C  CE2 B TYR B 1 217 ? 20.630  5.304   3.152   0.54 17.85  ? 440  TYR B CE2 1 
ATOM   4243 C  CZ  A TYR B 1 217 ? 21.970  4.564   4.406   0.46 19.35  ? 440  TYR B CZ  1 
ATOM   4244 C  CZ  B TYR B 1 217 ? 21.103  5.966   4.267   0.54 18.03  ? 440  TYR B CZ  1 
ATOM   4245 O  OH  A TYR B 1 217 ? 23.055  5.396   4.274   0.46 21.02  ? 440  TYR B OH  1 
ATOM   4246 O  OH  B TYR B 1 217 ? 21.845  7.118   4.125   0.54 19.12  ? 440  TYR B OH  1 
ATOM   4247 N  N   . ILE B 1 218 ? 15.605  1.638   3.737   1.00 12.28  ? 441  ILE B N   1 
ATOM   4248 C  CA  A ILE B 1 218 ? 14.505  0.698   3.582   0.61 13.75  ? 441  ILE B CA  1 
ATOM   4249 C  CA  B ILE B 1 218 ? 14.410  0.832   3.440   0.39 13.77  ? 441  ILE B CA  1 
ATOM   4250 C  C   . ILE B 1 218 ? 14.741  -0.261  2.415   1.00 13.86  ? 441  ILE B C   1 
ATOM   4251 O  O   . ILE B 1 218 ? 15.451  0.048   1.448   1.00 14.78  ? 441  ILE B O   1 
ATOM   4252 C  CB  A ILE B 1 218 ? 13.134  1.392   3.544   0.61 13.55  ? 441  ILE B CB  1 
ATOM   4253 C  CB  B ILE B 1 218 ? 13.325  1.732   2.810   0.39 12.92  ? 441  ILE B CB  1 
ATOM   4254 C  CG1 A ILE B 1 218 ? 13.076  2.392   2.396   0.61 13.15  ? 441  ILE B CG1 1 
ATOM   4255 C  CG1 B ILE B 1 218 ? 13.068  3.004   3.626   0.39 12.93  ? 441  ILE B CG1 1 
ATOM   4256 C  CG2 A ILE B 1 218 ? 12.818  2.054   4.900   0.61 14.65  ? 441  ILE B CG2 1 
ATOM   4257 C  CG2 B ILE B 1 218 ? 12.018  0.982   2.576   0.39 12.61  ? 441  ILE B CG2 1 
ATOM   4258 C  CD1 A ILE B 1 218 ? 11.783  3.184   2.336   0.61 15.02  ? 441  ILE B CD1 1 
ATOM   4259 C  CD1 B ILE B 1 218 ? 12.032  3.917   2.998   0.39 15.82  ? 441  ILE B CD1 1 
ATOM   4260 N  N   . PRO B 1 219 ? 14.197  -1.474  2.524   1.00 12.28  ? 442  PRO B N   1 
ATOM   4261 C  CA  . PRO B 1 219 ? 14.420  -2.489  1.479   1.00 12.80  ? 442  PRO B CA  1 
ATOM   4262 C  C   . PRO B 1 219 ? 13.725  -2.142  0.166   1.00 12.52  ? 442  PRO B C   1 
ATOM   4263 O  O   . PRO B 1 219 ? 12.764  -1.370  0.123   1.00 12.83  ? 442  PRO B O   1 
ATOM   4264 C  CB  . PRO B 1 219 ? 13.786  -3.753  2.079   1.00 14.64  ? 442  PRO B CB  1 
ATOM   4265 C  CG  . PRO B 1 219 ? 13.731  -3.515  3.535   1.00 15.10  ? 442  PRO B CG  1 
ATOM   4266 C  CD  . PRO B 1 219 ? 13.534  -2.039  3.713   1.00 13.31  ? 442  PRO B CD  1 
ATOM   4267 N  N   . MET B 1 220 ? 14.216  -2.750  -0.917  1.00 12.34  ? 443  MET B N   1 
ATOM   4268 C  CA  . MET B 1 220 ? 13.574  -2.636  -2.224  1.00 12.75  ? 443  MET B CA  1 
ATOM   4269 C  C   . MET B 1 220 ? 13.365  -4.003  -2.861  1.00 12.01  ? 443  MET B C   1 
ATOM   4270 O  O   . MET B 1 220 ? 14.164  -4.927  -2.692  1.00 13.30  ? 443  MET B O   1 
ATOM   4271 C  CB  . MET B 1 220 ? 14.343  -1.739  -3.196  1.00 15.01  ? 443  MET B CB  1 
ATOM   4272 C  CG  . MET B 1 220 ? 14.411  -0.310  -2.735  1.00 15.27  ? 443  MET B CG  1 
ATOM   4273 S  SD  . MET B 1 220 ? 14.553  0.852   -4.098  1.00 15.89  ? 443  MET B SD  1 
ATOM   4274 C  CE  . MET B 1 220 ? 16.120  0.353   -4.815  1.00 17.13  ? 443  MET B CE  1 
ATOM   4275 N  N   . LYS B 1 221 ? 12.281  -4.101  -3.631  1.00 12.71  ? 444  LYS B N   1 
ATOM   4276 C  CA  . LYS B 1 221 ? 11.996  -5.314  -4.385  1.00 13.36  ? 444  LYS B CA  1 
ATOM   4277 C  C   . LYS B 1 221 ? 13.006  -5.519  -5.510  1.00 14.51  ? 444  LYS B C   1 
ATOM   4278 O  O   . LYS B 1 221 ? 13.382  -6.659  -5.817  1.00 14.68  ? 444  LYS B O   1 
ATOM   4279 C  CB  . LYS B 1 221 ? 10.572  -5.229  -4.943  1.00 13.15  ? 444  LYS B CB  1 
ATOM   4280 C  CG  . LYS B 1 221 ? 10.184  -6.337  -5.942  1.00 14.44  ? 444  LYS B CG  1 
ATOM   4281 C  CD  . LYS B 1 221 ? 10.276  -7.736  -5.336  1.00 14.91  ? 444  LYS B CD  1 
ATOM   4282 C  CE  . LYS B 1 221 ? 9.849   -8.795  -6.349  1.00 15.76  ? 444  LYS B CE  1 
ATOM   4283 N  NZ  . LYS B 1 221 ? 9.958   -10.163 -5.760  1.00 15.83  ? 444  LYS B NZ  1 
ATOM   4284 N  N   . GLY B 1 222 ? 13.450  -4.436  -6.140  1.00 14.21  ? 445  GLY B N   1 
ATOM   4285 C  CA  . GLY B 1 222 ? 14.416  -4.529  -7.219  1.00 14.60  ? 445  GLY B CA  1 
ATOM   4286 C  C   . GLY B 1 222 ? 15.015  -3.169  -7.499  1.00 16.49  ? 445  GLY B C   1 
ATOM   4287 O  O   . GLY B 1 222 ? 14.729  -2.188  -6.812  1.00 18.67  ? 445  GLY B O   1 
ATOM   4288 N  N   . GLY B 1 223 ? 15.852  -3.122  -8.533  1.00 17.04  ? 446  GLY B N   1 
ATOM   4289 C  CA  . GLY B 1 223 ? 16.457  -1.874  -8.948  1.00 18.24  ? 446  GLY B CA  1 
ATOM   4290 C  C   . GLY B 1 223 ? 17.672  -1.482  -8.125  1.00 17.47  ? 446  GLY B C   1 
ATOM   4291 O  O   . GLY B 1 223 ? 18.102  -2.168  -7.192  1.00 18.69  ? 446  GLY B O   1 
ATOM   4292 N  N   . TYR B 1 224 ? 18.233  -0.334  -8.487  1.00 17.37  ? 447  TYR B N   1 
ATOM   4293 C  CA  . TYR B 1 224 ? 19.435  0.201   -7.862  1.00 18.06  ? 447  TYR B CA  1 
ATOM   4294 C  C   . TYR B 1 224 ? 19.081  1.347   -6.928  1.00 18.94  ? 447  TYR B C   1 
ATOM   4295 O  O   . TYR B 1 224 ? 18.173  2.135   -7.209  1.00 20.45  ? 447  TYR B O   1 
ATOM   4296 C  CB  . TYR B 1 224 ? 20.427  0.690   -8.927  1.00 19.37  ? 447  TYR B CB  1 
ATOM   4297 C  CG  . TYR B 1 224 ? 21.108  -0.456  -9.645  1.00 22.21  ? 447  TYR B CG  1 
ATOM   4298 C  CD1 . TYR B 1 224 ? 20.519  -1.061  -10.748 1.00 43.10  ? 447  TYR B CD1 1 
ATOM   4299 C  CD2 . TYR B 1 224 ? 22.323  -0.952  -9.198  1.00 27.59  ? 447  TYR B CD2 1 
ATOM   4300 C  CE1 . TYR B 1 224 ? 21.134  -2.121  -11.396 1.00 47.98  ? 447  TYR B CE1 1 
ATOM   4301 C  CE2 . TYR B 1 224 ? 22.946  -2.008  -9.838  1.00 47.28  ? 447  TYR B CE2 1 
ATOM   4302 C  CZ  . TYR B 1 224 ? 22.348  -2.589  -10.936 1.00 80.84  ? 447  TYR B CZ  1 
ATOM   4303 O  OH  . TYR B 1 224 ? 22.971  -3.641  -11.571 1.00 83.66  ? 447  TYR B OH  1 
ATOM   4304 N  N   . GLY B 1 225 ? 19.791  1.427   -5.806  1.00 16.92  ? 448  GLY B N   1 
ATOM   4305 C  CA  . GLY B 1 225 ? 19.617  2.542   -4.899  1.00 15.95  ? 448  GLY B CA  1 
ATOM   4306 C  C   . GLY B 1 225 ? 19.713  2.166   -3.435  1.00 15.55  ? 448  GLY B C   1 
ATOM   4307 O  O   . GLY B 1 225 ? 19.682  0.981   -3.072  1.00 16.82  ? 448  GLY B O   1 
ATOM   4308 N  N   . SER B 1 226 ? 19.829  3.180   -2.582  1.00 15.62  ? 449  SER B N   1 
ATOM   4309 C  CA  . SER B 1 226 ? 19.821  3.022   -1.130  1.00 14.60  ? 449  SER B CA  1 
ATOM   4310 C  C   . SER B 1 226 ? 18.808  3.994   -0.551  1.00 14.49  ? 449  SER B C   1 
ATOM   4311 O  O   . SER B 1 226 ? 19.173  4.952   0.144   1.00 16.07  ? 449  SER B O   1 
ATOM   4312 C  CB  . SER B 1 226 ? 21.214  3.270   -0.552  1.00 16.37  ? 449  SER B CB  1 
ATOM   4313 O  OG  . SER B 1 226 ? 22.138  2.331   -1.084  1.00 18.90  ? 449  SER B OG  1 
ATOM   4314 N  N   . PRO B 1 227 ? 17.518  3.764   -0.797  1.00 14.38  ? 450  PRO B N   1 
ATOM   4315 C  CA  . PRO B 1 227 ? 16.501  4.697   -0.302  1.00 13.64  ? 450  PRO B CA  1 
ATOM   4316 C  C   . PRO B 1 227 ? 16.442  4.708   1.211   1.00 12.71  ? 450  PRO B C   1 
ATOM   4317 O  O   . PRO B 1 227 ? 16.692  3.702   1.881   1.00 13.89  ? 450  PRO B O   1 
ATOM   4318 C  CB  . PRO B 1 227 ? 15.195  4.147   -0.882  1.00 14.01  ? 450  PRO B CB  1 
ATOM   4319 C  CG  . PRO B 1 227 ? 15.459  2.677   -1.045  1.00 14.39  ? 450  PRO B CG  1 
ATOM   4320 C  CD  . PRO B 1 227 ? 16.915  2.581   -1.444  1.00 14.49  ? 450  PRO B CD  1 
ATOM   4321 N  N   . TYR B 1 228 ? 16.092  5.873   1.749   1.00 12.76  ? 451  TYR B N   1 
ATOM   4322 C  CA  . TYR B 1 228 ? 15.959  6.049   3.184   1.00 13.23  ? 451  TYR B CA  1 
ATOM   4323 C  C   . TYR B 1 228 ? 14.705  6.869   3.459   1.00 13.17  ? 451  TYR B C   1 
ATOM   4324 O  O   . TYR B 1 228 ? 14.129  7.502   2.561   1.00 13.76  ? 451  TYR B O   1 
ATOM   4325 C  CB  . TYR B 1 228 ? 17.202  6.721   3.788   1.00 13.68  ? 451  TYR B CB  1 
ATOM   4326 C  CG  . TYR B 1 228 ? 17.566  8.001   3.082   1.00 14.83  ? 451  TYR B CG  1 
ATOM   4327 C  CD1 . TYR B 1 228 ? 16.894  9.189   3.365   1.00 15.67  ? 451  TYR B CD1 1 
ATOM   4328 C  CD2 . TYR B 1 228 ? 18.542  8.023   2.092   1.00 16.53  ? 451  TYR B CD2 1 
ATOM   4329 C  CE1 . TYR B 1 228 ? 17.208  10.361  2.712   1.00 17.82  ? 451  TYR B CE1 1 
ATOM   4330 C  CE2 . TYR B 1 228 ? 18.860  9.203   1.432   1.00 18.48  ? 451  TYR B CE2 1 
ATOM   4331 C  CZ  . TYR B 1 228 ? 18.186  10.364  1.745   1.00 19.43  ? 451  TYR B CZ  1 
ATOM   4332 O  OH  . TYR B 1 228 ? 18.492  11.542  1.097   1.00 22.74  ? 451  TYR B OH  1 
ATOM   4333 N  N   . ILE B 1 229 ? 14.266  6.841   4.711   1.00 11.86  ? 452  ILE B N   1 
ATOM   4334 C  CA  . ILE B 1 229 ? 13.126  7.641   5.139   1.00 11.98  ? 452  ILE B CA  1 
ATOM   4335 C  C   . ILE B 1 229 ? 13.470  8.301   6.468   1.00 11.39  ? 452  ILE B C   1 
ATOM   4336 O  O   . ILE B 1 229 ? 14.038  7.661   7.361   1.00 11.60  ? 452  ILE B O   1 
ATOM   4337 C  CB  . ILE B 1 229 ? 11.801  6.837   5.166   1.00 10.65  ? 452  ILE B CB  1 
ATOM   4338 C  CG1 . ILE B 1 229 ? 10.598  7.776   5.271   1.00 10.57  ? 452  ILE B CG1 1 
ATOM   4339 C  CG2 . ILE B 1 229 ? 11.792  5.747   6.257   1.00 11.88  ? 452  ILE B CG2 1 
ATOM   4340 C  CD1 . ILE B 1 229 ? 9.295   7.082   4.970   1.00 12.37  ? 452  ILE B CD1 1 
ATOM   4341 N  N   . ASP B 1 230 ? 13.183  9.595   6.574   1.00 11.34  ? 453  ASP B N   1 
ATOM   4342 C  CA  . ASP B 1 230 ? 13.557  10.411  7.722   1.00 11.37  ? 453  ASP B CA  1 
ATOM   4343 C  C   . ASP B 1 230 ? 12.317  10.749  8.531   1.00 10.91  ? 453  ASP B C   1 
ATOM   4344 O  O   . ASP B 1 230 ? 11.363  11.315  7.990   1.00 11.64  ? 453  ASP B O   1 
ATOM   4345 C  CB  . ASP B 1 230 ? 14.177  11.718  7.237   1.00 12.39  ? 453  ASP B CB  1 
ATOM   4346 C  CG  . ASP B 1 230 ? 15.553  11.530  6.648   1.00 13.14  ? 453  ASP B CG  1 
ATOM   4347 O  OD1 . ASP B 1 230 ? 16.354  10.787  7.255   1.00 15.14  ? 453  ASP B OD1 1 
ATOM   4348 O  OD2 . ASP B 1 230 ? 15.850  12.128  5.592   1.00 13.57  ? 453  ASP B OD2 1 
ATOM   4349 N  N   . CYS B 1 231 ? 12.317  10.417  9.819   1.00 9.86   ? 454  CYS B N   1 
ATOM   4350 C  CA  . CYS B 1 231 ? 11.208  10.830  10.671  1.00 10.05  ? 454  CYS B CA  1 
ATOM   4351 C  C   . CYS B 1 231 ? 11.645  11.926  11.642  1.00 10.01  ? 454  CYS B C   1 
ATOM   4352 O  O   . CYS B 1 231 ? 12.837  12.105  11.916  1.00 11.42  ? 454  CYS B O   1 
ATOM   4353 C  CB  . CYS B 1 231 ? 10.578  9.642   11.416  1.00 11.17  ? 454  CYS B CB  1 
ATOM   4354 S  SG  . CYS B 1 231 ? 11.590  8.903   12.726  1.00 11.18  ? 454  CYS B SG  1 
ATOM   4355 N  N   . LEU B 1 232 ? 10.665  12.669  12.154  1.00 10.17  ? 455  LEU B N   1 
ATOM   4356 C  CA  . LEU B 1 232 ? 10.963  13.835  12.994  1.00 10.10  ? 455  LEU B CA  1 
ATOM   4357 C  C   . LEU B 1 232 ? 11.306  13.440  14.424  1.00 9.46   ? 455  LEU B C   1 
ATOM   4358 O  O   . LEU B 1 232 ? 12.200  14.030  15.031  1.00 11.12  ? 455  LEU B O   1 
ATOM   4359 C  CB  . LEU B 1 232 ? 9.776   14.802  12.973  1.00 10.01  ? 455  LEU B CB  1 
ATOM   4360 C  CG  . LEU B 1 232 ? 9.389   15.374  11.607  1.00 10.77  ? 455  LEU B CG  1 
ATOM   4361 C  CD1 . LEU B 1 232 ? 8.224   16.347  11.758  1.00 12.97  ? 455  LEU B CD1 1 
ATOM   4362 C  CD2 . LEU B 1 232 ? 10.585  16.046  10.944  1.00 12.84  ? 455  LEU B CD2 1 
ATOM   4363 N  N   . ILE B 1 233 ? 10.580  12.468  14.975  1.00 10.22  ? 456  ILE B N   1 
ATOM   4364 C  CA  . ILE B 1 233 ? 10.874  11.890  16.287  1.00 10.49  ? 456  ILE B CA  1 
ATOM   4365 C  C   . ILE B 1 233 ? 10.508  10.406  16.238  1.00 9.86   ? 456  ILE B C   1 
ATOM   4366 O  O   . ILE B 1 233 ? 9.670   9.997   15.446  1.00 11.97  ? 456  ILE B O   1 
ATOM   4367 C  CB  . ILE B 1 233 ? 10.077  12.596  17.419  1.00 12.16  ? 456  ILE B CB  1 
ATOM   4368 C  CG1 . ILE B 1 233 ? 8.586   12.687  17.077  1.00 13.47  ? 456  ILE B CG1 1 
ATOM   4369 C  CG2 . ILE B 1 233 ? 10.646  13.992  17.723  1.00 13.14  ? 456  ILE B CG2 1 
ATOM   4370 C  CD1 . ILE B 1 233 ? 7.728   13.239  18.228  1.00 16.12  ? 456  ILE B CD1 1 
ATOM   4371 N  N   . PRO B 1 234 ? 11.207  9.594   17.036  1.00 10.65  ? 457  PRO B N   1 
ATOM   4372 C  CA  . PRO B 1 234 ? 10.957  8.140   17.011  1.00 12.03  ? 457  PRO B CA  1 
ATOM   4373 C  C   . PRO B 1 234 ? 9.562   7.792   17.500  1.00 11.31  ? 457  PRO B C   1 
ATOM   4374 O  O   . PRO B 1 234 ? 8.953   8.519   18.286  1.00 10.93  ? 457  PRO B O   1 
ATOM   4375 C  CB  . PRO B 1 234 ? 12.014  7.587   17.979  1.00 13.50  ? 457  PRO B CB  1 
ATOM   4376 C  CG  . PRO B 1 234 ? 13.064  8.668   18.090  1.00 13.33  ? 457  PRO B CG  1 
ATOM   4377 C  CD  . PRO B 1 234 ? 12.318  9.960   17.931  1.00 11.97  ? 457  PRO B CD  1 
ATOM   4378 N  N   . GLN B 1 235 ? 9.071   6.623   17.052  1.00 11.18  ? 458  GLN B N   1 
ATOM   4379 C  CA  . GLN B 1 235 ? 7.761   6.158   17.499  1.00 11.20  ? 458  GLN B CA  1 
ATOM   4380 C  C   . GLN B 1 235 ? 7.697   6.041   19.019  1.00 11.20  ? 458  GLN B C   1 
ATOM   4381 O  O   . GLN B 1 235 ? 6.666   6.359   19.626  1.00 12.29  ? 458  GLN B O   1 
ATOM   4382 C  CB  . GLN B 1 235 ? 7.411   4.831   16.834  1.00 12.33  ? 458  GLN B CB  1 
ATOM   4383 C  CG  . GLN B 1 235 ? 5.997   4.353   17.104  1.00 13.12  ? 458  GLN B CG  1 
ATOM   4384 C  CD  . GLN B 1 235 ? 4.929   5.196   16.422  1.00 14.37  ? 458  GLN B CD  1 
ATOM   4385 O  OE1 . GLN B 1 235 ? 5.202   5.938   15.468  1.00 13.50  ? 458  GLN B OE1 1 
ATOM   4386 N  NE2 . GLN B 1 235 ? 3.693   5.065   16.897  1.00 17.41  ? 458  GLN B NE2 1 
ATOM   4387 N  N   . GLU B 1 236 ? 8.804   5.630   19.659  1.00 11.69  ? 459  GLU B N   1 
ATOM   4388 C  CA  . GLU B 1 236 ? 8.810   5.479   21.113  1.00 12.67  ? 459  GLU B CA  1 
ATOM   4389 C  C   . GLU B 1 236 ? 8.745   6.827   21.833  1.00 13.91  ? 459  GLU B C   1 
ATOM   4390 O  O   . GLU B 1 236 ? 8.267   6.902   22.975  1.00 15.34  ? 459  GLU B O   1 
ATOM   4391 C  CB  . GLU B 1 236 ? 10.032  4.676   21.549  1.00 13.43  ? 459  GLU B CB  1 
ATOM   4392 C  CG  . GLU B 1 236 ? 9.943   3.189   21.166  1.00 13.88  ? 459  GLU B CG  1 
ATOM   4393 C  CD  . GLU B 1 236 ? 10.301  2.894   19.714  1.00 14.63  ? 459  GLU B CD  1 
ATOM   4394 O  OE1 . GLU B 1 236 ? 10.720  3.822   18.998  1.00 14.16  ? 459  GLU B OE1 1 
ATOM   4395 O  OE2 . GLU B 1 236 ? 10.164  1.719   19.294  1.00 16.55  ? 459  GLU B OE2 1 
ATOM   4396 N  N   . TRP B 1 237 ? 9.239   7.899   21.210  1.00 13.01  ? 460  TRP B N   1 
ATOM   4397 C  CA  . TRP B 1 237 ? 9.032   9.207   21.821  1.00 13.35  ? 460  TRP B CA  1 
ATOM   4398 C  C   . TRP B 1 237 ? 7.573   9.612   21.734  1.00 13.21  ? 460  TRP B C   1 
ATOM   4399 O  O   . TRP B 1 237 ? 7.032   10.205  22.672  1.00 14.42  ? 460  TRP B O   1 
ATOM   4400 C  CB  . TRP B 1 237 ? 9.883   10.282  21.149  1.00 12.93  ? 460  TRP B CB  1 
ATOM   4401 C  CG  . TRP B 1 237 ? 11.367  10.235  21.447  1.00 12.15  ? 460  TRP B CG  1 
ATOM   4402 C  CD1 . TRP B 1 237 ? 12.116  9.155   21.872  1.00 12.39  ? 460  TRP B CD1 1 
ATOM   4403 C  CD2 . TRP B 1 237 ? 12.278  11.329  21.324  1.00 12.11  ? 460  TRP B CD2 1 
ATOM   4404 N  NE1 . TRP B 1 237 ? 13.431  9.525   22.007  1.00 12.11  ? 460  TRP B NE1 1 
ATOM   4405 C  CE2 . TRP B 1 237 ? 13.557  10.851  21.674  1.00 12.05  ? 460  TRP B CE2 1 
ATOM   4406 C  CE3 . TRP B 1 237 ? 12.137  12.666  20.934  1.00 12.14  ? 460  TRP B CE3 1 
ATOM   4407 C  CZ2 . TRP B 1 237 ? 14.686  11.662  21.652  1.00 13.38  ? 460  TRP B CZ2 1 
ATOM   4408 C  CZ3 . TRP B 1 237 ? 13.261  13.481  20.924  1.00 13.70  ? 460  TRP B CZ3 1 
ATOM   4409 C  CH2 . TRP B 1 237 ? 14.521  12.973  21.282  1.00 13.92  ? 460  TRP B CH2 1 
ATOM   4410 N  N   . ILE B 1 238 ? 6.931   9.319   20.600  1.00 12.68  ? 461  ILE B N   1 
ATOM   4411 C  CA  . ILE B 1 238 ? 5.511   9.612   20.441  1.00 12.79  ? 461  ILE B CA  1 
ATOM   4412 C  C   . ILE B 1 238 ? 4.702   8.888   21.507  1.00 14.15  ? 461  ILE B C   1 
ATOM   4413 O  O   . ILE B 1 238 ? 3.825   9.473   22.151  1.00 15.18  ? 461  ILE B O   1 
ATOM   4414 C  CB  . ILE B 1 238 ? 5.061   9.250   19.014  1.00 12.35  ? 461  ILE B CB  1 
ATOM   4415 C  CG1 . ILE B 1 238 ? 5.753   10.188  18.017  1.00 12.73  ? 461  ILE B CG1 1 
ATOM   4416 C  CG2 . ILE B 1 238 ? 3.547   9.322   18.890  1.00 14.58  ? 461  ILE B CG2 1 
ATOM   4417 C  CD1 . ILE B 1 238 ? 5.535   9.813   16.586  1.00 13.63  ? 461  ILE B CD1 1 
ATOM   4418 N  N   . SER B 1 239 ? 4.998   7.603   21.713  1.00 14.54  ? 462  SER B N   1 
ATOM   4419 C  CA  A SER B 1 239 ? 4.347   6.846   22.778  0.77 16.57  ? 462  SER B CA  1 
ATOM   4420 C  CA  B SER B 1 239 ? 4.333   6.856   22.772  0.23 15.86  ? 462  SER B CA  1 
ATOM   4421 C  C   . SER B 1 239 ? 4.548   7.515   24.128  1.00 16.48  ? 462  SER B C   1 
ATOM   4422 O  O   . SER B 1 239 ? 3.612   7.617   24.929  1.00 17.24  ? 462  SER B O   1 
ATOM   4423 C  CB  A SER B 1 239 ? 4.929   5.435   22.829  0.77 18.74  ? 462  SER B CB  1 
ATOM   4424 C  CB  B SER B 1 239 ? 4.840   5.418   22.790  0.23 16.67  ? 462  SER B CB  1 
ATOM   4425 O  OG  A SER B 1 239 ? 4.545   4.668   21.702  0.77 21.70  ? 462  SER B OG  1 
ATOM   4426 O  OG  B SER B 1 239 ? 4.063   4.635   23.676  0.23 17.23  ? 462  SER B OG  1 
ATOM   4427 N  N   . HIS B 1 240 ? 5.771   7.981   24.397  1.00 17.21  ? 463  HIS B N   1 
ATOM   4428 C  CA  . HIS B 1 240 ? 6.081   8.584   25.689  1.00 17.17  ? 463  HIS B CA  1 
ATOM   4429 C  C   . HIS B 1 240 ? 5.339   9.903   25.881  1.00 17.57  ? 463  HIS B C   1 
ATOM   4430 O  O   . HIS B 1 240 ? 4.725   10.126  26.928  1.00 18.29  ? 463  HIS B O   1 
ATOM   4431 C  CB  . HIS B 1 240 ? 7.589   8.798   25.797  1.00 18.12  ? 463  HIS B CB  1 
ATOM   4432 C  CG  . HIS B 1 240 ? 8.033   9.347   27.116  1.00 20.11  ? 463  HIS B CG  1 
ATOM   4433 N  ND1 . HIS B 1 240 ? 8.053   8.590   28.265  1.00 22.90  ? 463  HIS B ND1 1 
ATOM   4434 C  CD2 . HIS B 1 240 ? 8.485   10.576  27.463  1.00 20.72  ? 463  HIS B CD2 1 
ATOM   4435 C  CE1 . HIS B 1 240 ? 8.487   9.333   29.269  1.00 23.92  ? 463  HIS B CE1 1 
ATOM   4436 N  NE2 . HIS B 1 240 ? 8.760   10.539  28.809  1.00 23.19  ? 463  HIS B NE2 1 
ATOM   4437 N  N   . PHE B 1 241 ? 5.384   10.791  24.881  1.00 16.06  ? 464  PHE B N   1 
ATOM   4438 C  CA  . PHE B 1 241 ? 4.711   12.080  25.015  1.00 15.43  ? 464  PHE B CA  1 
ATOM   4439 C  C   . PHE B 1 241 ? 3.202   11.906  25.117  1.00 16.11  ? 464  PHE B C   1 
ATOM   4440 O  O   . PHE B 1 241 ? 2.533   12.635  25.860  1.00 16.58  ? 464  PHE B O   1 
ATOM   4441 C  CB  . PHE B 1 241 ? 5.053   12.998  23.840  1.00 15.14  ? 464  PHE B CB  1 
ATOM   4442 C  CG  . PHE B 1 241 ? 6.523   13.261  23.669  1.00 14.50  ? 464  PHE B CG  1 
ATOM   4443 C  CD1 . PHE B 1 241 ? 7.398   13.182  24.737  1.00 16.30  ? 464  PHE B CD1 1 
ATOM   4444 C  CD2 . PHE B 1 241 ? 7.021   13.583  22.420  1.00 15.10  ? 464  PHE B CD2 1 
ATOM   4445 C  CE1 . PHE B 1 241 ? 8.756   13.438  24.559  1.00 16.90  ? 464  PHE B CE1 1 
ATOM   4446 C  CE2 . PHE B 1 241 ? 8.360   13.830  22.227  1.00 15.22  ? 464  PHE B CE2 1 
ATOM   4447 C  CZ  . PHE B 1 241 ? 9.239   13.750  23.301  1.00 15.94  ? 464  PHE B CZ  1 
ATOM   4448 N  N   . TYR B 1 242 ? 2.646   10.960  24.355  1.00 15.73  ? 465  TYR B N   1 
ATOM   4449 C  CA  . TYR B 1 242 ? 1.218   10.668  24.431  1.00 17.95  ? 465  TYR B CA  1 
ATOM   4450 C  C   . TYR B 1 242 ? 0.810   10.262  25.847  1.00 20.37  ? 465  TYR B C   1 
ATOM   4451 O  O   . TYR B 1 242 ? -0.214  10.719  26.365  1.00 21.99  ? 465  TYR B O   1 
ATOM   4452 C  CB  . TYR B 1 242 ? 0.870   9.576   23.414  1.00 18.61  ? 465  TYR B CB  1 
ATOM   4453 C  CG  . TYR B 1 242 ? -0.565  9.111   23.454  1.00 20.21  ? 465  TYR B CG  1 
ATOM   4454 C  CD1 . TYR B 1 242 ? -1.570  9.823   22.809  1.00 20.41  ? 465  TYR B CD1 1 
ATOM   4455 C  CD2 . TYR B 1 242 ? -0.912  7.945   24.123  1.00 20.54  ? 465  TYR B CD2 1 
ATOM   4456 C  CE1 . TYR B 1 242 ? -2.884  9.386   22.842  1.00 22.35  ? 465  TYR B CE1 1 
ATOM   4457 C  CE2 . TYR B 1 242 ? -2.212  7.502   24.160  1.00 21.96  ? 465  TYR B CE2 1 
ATOM   4458 C  CZ  . TYR B 1 242 ? -3.194  8.223   23.518  1.00 23.01  ? 465  TYR B CZ  1 
ATOM   4459 O  OH  . TYR B 1 242 ? -4.489  7.777   23.568  1.00 25.54  ? 465  TYR B OH  1 
ATOM   4460 N  N   A GLN B 1 243 ? 1.602   9.392   26.482  0.61 20.90  ? 466  GLN B N   1 
ATOM   4461 N  N   B GLN B 1 243 ? 1.608   9.411   26.497  0.39 20.89  ? 466  GLN B N   1 
ATOM   4462 C  CA  A GLN B 1 243 ? 1.299   8.948   27.841  0.61 22.25  ? 466  GLN B CA  1 
ATOM   4463 C  CA  B GLN B 1 243 ? 1.253   8.960   27.842  0.39 22.03  ? 466  GLN B CA  1 
ATOM   4464 C  C   A GLN B 1 243 ? 1.471   10.079  28.848  0.61 23.35  ? 466  GLN B C   1 
ATOM   4465 C  C   B GLN B 1 243 ? 1.495   10.045  28.890  0.39 22.68  ? 466  GLN B C   1 
ATOM   4466 O  O   A GLN B 1 243 ? 0.605   10.304  29.702  0.61 24.51  ? 466  GLN B O   1 
ATOM   4467 O  O   B GLN B 1 243 ? 0.689   10.210  29.813  0.39 23.12  ? 466  GLN B O   1 
ATOM   4468 C  CB  A GLN B 1 243 ? 2.222   7.788   28.219  0.61 22.95  ? 466  GLN B CB  1 
ATOM   4469 C  CB  B GLN B 1 243 ? 2.021   7.683   28.190  0.39 22.81  ? 466  GLN B CB  1 
ATOM   4470 C  CG  A GLN B 1 243 ? 1.974   6.513   27.454  0.61 24.53  ? 466  GLN B CG  1 
ATOM   4471 C  CG  B GLN B 1 243 ? 2.097   7.375   29.682  0.39 23.90  ? 466  GLN B CG  1 
ATOM   4472 C  CD  A GLN B 1 243 ? 0.669   5.864   27.835  0.61 24.61  ? 466  GLN B CD  1 
ATOM   4473 C  CD  B GLN B 1 243 ? 0.807   6.807   30.247  0.39 24.43  ? 466  GLN B CD  1 
ATOM   4474 O  OE1 A GLN B 1 243 ? 0.354   5.724   29.014  0.61 26.62  ? 466  GLN B OE1 1 
ATOM   4475 O  OE1 B GLN B 1 243 ? 0.058   6.123   29.550  0.39 24.51  ? 466  GLN B OE1 1 
ATOM   4476 N  NE2 A GLN B 1 243 ? -0.105  5.472   26.837  0.61 20.54  ? 466  GLN B NE2 1 
ATOM   4477 N  NE2 B GLN B 1 243 ? 0.545   7.082   31.522  0.39 25.15  ? 466  GLN B NE2 1 
ATOM   4478 N  N   . GLU B 1 244 ? 2.594   10.794  28.769  1.00 22.06  ? 467  GLU B N   1 
ATOM   4479 C  CA  . GLU B 1 244 ? 2.960   11.747  29.815  1.00 23.80  ? 467  GLU B CA  1 
ATOM   4480 C  C   . GLU B 1 244 ? 2.131   13.022  29.756  1.00 23.33  ? 467  GLU B C   1 
ATOM   4481 O  O   . GLU B 1 244 ? 1.700   13.537  30.795  1.00 23.98  ? 467  GLU B O   1 
ATOM   4482 C  CB  . GLU B 1 244 ? 4.447   12.076  29.708  1.00 28.03  ? 467  GLU B CB  1 
ATOM   4483 C  CG  . GLU B 1 244 ? 5.339   10.897  30.036  1.00 32.38  ? 467  GLU B CG  1 
ATOM   4484 C  CD  . GLU B 1 244 ? 5.142   10.403  31.455  1.00 37.62  ? 467  GLU B CD  1 
ATOM   4485 O  OE1 . GLU B 1 244 ? 5.220   11.235  32.380  1.00 40.27  ? 467  GLU B OE1 1 
ATOM   4486 O  OE2 . GLU B 1 244 ? 4.902   9.191   31.645  1.00 38.65  ? 467  GLU B OE2 1 
ATOM   4487 N  N   . SER B 1 245 ? 1.921   13.558  28.555  1.00 21.62  ? 468  SER B N   1 
ATOM   4488 C  CA  . SER B 1 245 ? 1.179   14.807  28.368  1.00 22.81  ? 468  SER B CA  1 
ATOM   4489 C  C   . SER B 1 245 ? 1.709   15.931  29.261  1.00 21.45  ? 468  SER B C   1 
ATOM   4490 O  O   . SER B 1 245 ? 0.950   16.664  29.901  1.00 22.44  ? 468  SER B O   1 
ATOM   4491 C  CB  . SER B 1 245 ? -0.327  14.604  28.544  1.00 26.38  ? 468  SER B CB  1 
ATOM   4492 O  OG  . SER B 1 245 ? -0.855  13.797  27.505  1.00 29.92  ? 468  SER B OG  1 
ATOM   4493 N  N   . ALA B 1 246 ? 3.028   16.071  29.294  1.00 21.63  ? 469  ALA B N   1 
ATOM   4494 C  CA  . ALA B 1 246 ? 3.630   17.131  30.097  1.00 21.08  ? 469  ALA B CA  1 
ATOM   4495 C  C   . ALA B 1 246 ? 3.498   18.461  29.366  1.00 21.11  ? 469  ALA B C   1 
ATOM   4496 O  O   . ALA B 1 246 ? 3.780   18.530  28.167  1.00 20.00  ? 469  ALA B O   1 
ATOM   4497 C  CB  . ALA B 1 246 ? 5.102   16.832  30.376  1.00 20.95  ? 469  ALA B CB  1 
ATOM   4498 N  N   . PRO B 1 247 ? 3.060   19.522  30.042  1.00 21.56  ? 470  PRO B N   1 
ATOM   4499 C  CA  . PRO B 1 247 ? 2.909   20.814  29.366  1.00 21.66  ? 470  PRO B CA  1 
ATOM   4500 C  C   . PRO B 1 247 ? 4.252   21.341  28.890  1.00 20.68  ? 470  PRO B C   1 
ATOM   4501 O  O   . PRO B 1 247 ? 5.268   21.215  29.578  1.00 22.50  ? 470  PRO B O   1 
ATOM   4502 C  CB  . PRO B 1 247 ? 2.317   21.715  30.456  1.00 24.43  ? 470  PRO B CB  1 
ATOM   4503 C  CG  . PRO B 1 247 ? 1.747   20.771  31.478  1.00 26.33  ? 470  PRO B CG  1 
ATOM   4504 C  CD  . PRO B 1 247 ? 2.613   19.560  31.443  1.00 23.84  ? 470  PRO B CD  1 
ATOM   4505 N  N   . SER B 1 248 ? 4.253   21.934  27.700  1.00 20.01  ? 471  SER B N   1 
ATOM   4506 C  CA  . SER B 1 248 ? 5.448   22.588  27.182  1.00 20.49  ? 471  SER B CA  1 
ATOM   4507 C  C   . SER B 1 248 ? 5.540   23.984  27.785  1.00 21.15  ? 471  SER B C   1 
ATOM   4508 O  O   . SER B 1 248 ? 4.625   24.795  27.621  1.00 22.58  ? 471  SER B O   1 
ATOM   4509 C  CB  . SER B 1 248 ? 5.381   22.664  25.657  1.00 20.61  ? 471  SER B CB  1 
ATOM   4510 O  OG  . SER B 1 248 ? 5.239   21.371  25.082  1.00 22.04  ? 471  SER B OG  1 
ATOM   4511 N  N   . GLN B 1 249 ? 6.645   24.264  28.484  1.00 21.12  ? 472  GLN B N   1 
ATOM   4512 C  CA  . GLN B 1 249 ? 6.763   25.527  29.214  1.00 22.67  ? 472  GLN B CA  1 
ATOM   4513 C  C   . GLN B 1 249 ? 7.170   26.677  28.305  1.00 21.89  ? 472  GLN B C   1 
ATOM   4514 O  O   . GLN B 1 249 ? 6.858   27.839  28.604  1.00 23.05  ? 472  GLN B O   1 
ATOM   4515 C  CB  . GLN B 1 249 ? 7.764   25.396  30.362  1.00 24.48  ? 472  GLN B CB  1 
ATOM   4516 C  CG  . GLN B 1 249 ? 7.357   24.410  31.440  1.00 26.67  ? 472  GLN B CG  1 
ATOM   4517 C  CD  . GLN B 1 249 ? 6.054   24.777  32.120  1.00 28.72  ? 472  GLN B CD  1 
ATOM   4518 O  OE1 . GLN B 1 249 ? 5.717   25.955  32.253  1.00 28.81  ? 472  GLN B OE1 1 
ATOM   4519 N  NE2 . GLN B 1 249 ? 5.312   23.765  32.556  1.00 29.49  ? 472  GLN B NE2 1 
ATOM   4520 N  N   . THR B 1 250 ? 7.886   26.381  27.221  1.00 20.32  ? 473  THR B N   1 
ATOM   4521 C  CA  . THR B 1 250 ? 8.161   27.339  26.157  1.00 19.59  ? 473  THR B CA  1 
ATOM   4522 C  C   . THR B 1 250 ? 7.999   26.601  24.836  1.00 19.24  ? 473  THR B C   1 
ATOM   4523 O  O   . THR B 1 250 ? 7.561   25.447  24.795  1.00 20.44  ? 473  THR B O   1 
ATOM   4524 C  CB  . THR B 1 250 ? 9.581   27.920  26.242  1.00 19.64  ? 473  THR B CB  1 
ATOM   4525 O  OG1 . THR B 1 250 ? 10.536  26.885  25.948  1.00 20.33  ? 473  THR B OG1 1 
ATOM   4526 C  CG2 . THR B 1 250 ? 9.878   28.518  27.618  1.00 21.13  ? 473  THR B CG2 1 
ATOM   4527 N  N   . ASP B 1 251 ? 8.395   27.251  23.747  1.00 19.91  ? 474  ASP B N   1 
ATOM   4528 C  CA  . ASP B 1 251 ? 8.309   26.627  22.434  1.00 20.80  ? 474  ASP B CA  1 
ATOM   4529 C  C   . ASP B 1 251 ? 9.442   25.647  22.166  1.00 17.64  ? 474  ASP B C   1 
ATOM   4530 O  O   . ASP B 1 251 ? 9.371   24.896  21.183  1.00 16.82  ? 474  ASP B O   1 
ATOM   4531 C  CB  . ASP B 1 251 ? 8.334   27.698  21.343  1.00 26.03  ? 474  ASP B CB  1 
ATOM   4532 C  CG  . ASP B 1 251 ? 7.034   28.465  21.245  1.00 31.32  ? 474  ASP B CG  1 
ATOM   4533 O  OD1 . ASP B 1 251 ? 6.038   28.046  21.877  1.00 31.89  ? 474  ASP B OD1 1 
ATOM   4534 O  OD2 . ASP B 1 251 ? 7.019   29.483  20.528  1.00 34.86  ? 474  ASP B OD2 1 
ATOM   4535 N  N   . VAL B 1 252 ? 10.489  25.645  22.987  1.00 17.16  ? 475  VAL B N   1 
ATOM   4536 C  CA  . VAL B 1 252 ? 11.708  24.900  22.683  1.00 16.51  ? 475  VAL B CA  1 
ATOM   4537 C  C   . VAL B 1 252 ? 12.261  24.259  23.953  1.00 15.91  ? 475  VAL B C   1 
ATOM   4538 O  O   . VAL B 1 252 ? 12.618  24.962  24.911  1.00 17.55  ? 475  VAL B O   1 
ATOM   4539 C  CB  . VAL B 1 252 ? 12.792  25.784  22.040  1.00 20.05  ? 475  VAL B CB  1 
ATOM   4540 C  CG1 . VAL B 1 252 ? 14.040  24.976  21.812  1.00 21.87  ? 475  VAL B CG1 1 
ATOM   4541 C  CG2 . VAL B 1 252 ? 12.294  26.415  20.734  1.00 21.78  ? 475  VAL B CG2 1 
ATOM   4542 N  N   . ALA B 1 253 ? 12.386  22.931  23.942  1.00 15.89  ? 476  ALA B N   1 
ATOM   4543 C  CA  . ALA B 1 253 ? 13.116  22.199  24.969  1.00 16.15  ? 476  ALA B CA  1 
ATOM   4544 C  C   . ALA B 1 253 ? 14.559  22.018  24.512  1.00 15.12  ? 476  ALA B C   1 
ATOM   4545 O  O   . ALA B 1 253 ? 14.815  21.484  23.422  1.00 17.19  ? 476  ALA B O   1 
ATOM   4546 C  CB  . ALA B 1 253 ? 12.466  20.840  25.220  1.00 18.15  ? 476  ALA B CB  1 
ATOM   4547 N  N   . LEU B 1 254 ? 15.501  22.458  25.340  1.00 15.07  ? 477  LEU B N   1 
ATOM   4548 C  CA  . LEU B 1 254 ? 16.907  22.248  25.039  1.00 15.14  ? 477  LEU B CA  1 
ATOM   4549 C  C   . LEU B 1 254 ? 17.279  20.831  25.447  1.00 14.36  ? 477  LEU B C   1 
ATOM   4550 O  O   . LEU B 1 254 ? 17.067  20.435  26.599  1.00 16.07  ? 477  LEU B O   1 
ATOM   4551 C  CB  . LEU B 1 254 ? 17.763  23.255  25.807  1.00 16.81  ? 477  LEU B CB  1 
ATOM   4552 C  CG  . LEU B 1 254 ? 19.286  23.187  25.660  1.00 17.43  ? 477  LEU B CG  1 
ATOM   4553 C  CD1 . LEU B 1 254 ? 19.730  23.400  24.220  1.00 17.03  ? 477  LEU B CD1 1 
ATOM   4554 C  CD2 . LEU B 1 254 ? 19.948  24.202  26.587  1.00 17.68  ? 477  LEU B CD2 1 
ATOM   4555 N  N   . ILE B 1 255 ? 17.827  20.064  24.501  1.00 14.45  ? 478  ILE B N   1 
ATOM   4556 C  CA  . ILE B 1 255 ? 18.200  18.673  24.738  1.00 13.94  ? 478  ILE B CA  1 
ATOM   4557 C  C   . ILE B 1 255 ? 19.671  18.472  24.396  1.00 12.85  ? 478  ILE B C   1 
ATOM   4558 O  O   . ILE B 1 255 ? 20.205  19.094  23.476  1.00 15.11  ? 478  ILE B O   1 
ATOM   4559 C  CB  . ILE B 1 255 ? 17.289  17.675  23.986  1.00 14.81  ? 478  ILE B CB  1 
ATOM   4560 C  CG1 . ILE B 1 255 ? 17.327  17.916  22.475  1.00 15.00  ? 478  ILE B CG1 1 
ATOM   4561 C  CG2 . ILE B 1 255 ? 15.868  17.850  24.440  1.00 16.68  ? 478  ILE B CG2 1 
ATOM   4562 C  CD1 . ILE B 1 255 ? 16.543  16.884  21.667  1.00 15.66  ? 478  ILE B CD1 1 
ATOM   4563 N  N   . ARG B 1 256 ? 20.338  17.617  25.175  1.00 13.35  ? 479  ARG B N   1 
ATOM   4564 C  CA  . ARG B 1 256 ? 21.745  17.293  24.978  1.00 13.94  ? 479  ARG B CA  1 
ATOM   4565 C  C   . ARG B 1 256 ? 21.880  15.803  24.703  1.00 13.45  ? 479  ARG B C   1 
ATOM   4566 O  O   . ARG B 1 256 ? 21.290  14.985  25.416  1.00 13.90  ? 479  ARG B O   1 
ATOM   4567 C  CB  . ARG B 1 256 ? 22.584  17.686  26.207  1.00 15.08  ? 479  ARG B CB  1 
ATOM   4568 C  CG  . ARG B 1 256 ? 23.131  19.124  26.180  1.00 16.91  ? 479  ARG B CG  1 
ATOM   4569 C  CD  . ARG B 1 256 ? 22.030  20.183  26.225  1.00 18.36  ? 479  ARG B CD  1 
ATOM   4570 N  NE  . ARG B 1 256 ? 22.577  21.538  26.241  1.00 18.99  ? 479  ARG B NE  1 
ATOM   4571 C  CZ  . ARG B 1 256 ? 22.981  22.168  27.333  1.00 20.57  ? 479  ARG B CZ  1 
ATOM   4572 N  NH1 . ARG B 1 256 ? 22.926  21.590  28.519  1.00 21.64  ? 479  ARG B NH1 1 
ATOM   4573 N  NH2 . ARG B 1 256 ? 23.453  23.404  27.228  1.00 20.63  ? 479  ARG B NH2 1 
ATOM   4574 N  N   . TYR B 1 257 ? 22.642  15.451  23.669  1.00 14.03  ? 480  TYR B N   1 
ATOM   4575 C  CA  . TYR B 1 257 ? 22.938  14.047  23.388  1.00 13.97  ? 480  TYR B CA  1 
ATOM   4576 C  C   . TYR B 1 257 ? 24.169  13.668  24.205  1.00 14.31  ? 480  TYR B C   1 
ATOM   4577 O  O   . TYR B 1 257 ? 25.248  14.229  23.998  1.00 16.77  ? 480  TYR B O   1 
ATOM   4578 C  CB  . TYR B 1 257 ? 23.197  13.826  21.899  1.00 14.58  ? 480  TYR B CB  1 
ATOM   4579 C  CG  . TYR B 1 257 ? 22.827  12.431  21.414  1.00 15.15  ? 480  TYR B CG  1 
ATOM   4580 C  CD1 . TYR B 1 257 ? 21.520  12.134  21.041  1.00 15.19  ? 480  TYR B CD1 1 
ATOM   4581 C  CD2 . TYR B 1 257 ? 23.770  11.415  21.329  1.00 19.26  ? 480  TYR B CD2 1 
ATOM   4582 C  CE1 . TYR B 1 257 ? 21.162  10.870  20.590  1.00 16.31  ? 480  TYR B CE1 1 
ATOM   4583 C  CE2 . TYR B 1 257 ? 23.417  10.154  20.879  1.00 19.37  ? 480  TYR B CE2 1 
ATOM   4584 C  CZ  . TYR B 1 257 ? 22.112  9.892   20.519  1.00 17.60  ? 480  TYR B CZ  1 
ATOM   4585 O  OH  . TYR B 1 257 ? 21.737  8.649   20.069  1.00 20.86  ? 480  TYR B OH  1 
ATOM   4586 N  N   . VAL B 1 258 ? 24.011  12.731  25.132  1.00 15.28  ? 481  VAL B N   1 
ATOM   4587 C  CA  A VAL B 1 258 ? 25.020  12.462  26.151  0.64 16.33  ? 481  VAL B CA  1 
ATOM   4588 C  CA  B VAL B 1 258 ? 25.052  12.466  26.113  0.36 16.36  ? 481  VAL B CA  1 
ATOM   4589 C  C   . VAL B 1 258 ? 25.473  11.006  26.067  1.00 17.16  ? 481  VAL B C   1 
ATOM   4590 O  O   . VAL B 1 258 ? 24.683  10.106  25.765  1.00 19.31  ? 481  VAL B O   1 
ATOM   4591 C  CB  A VAL B 1 258 ? 24.457  12.797  27.555  0.64 18.07  ? 481  VAL B CB  1 
ATOM   4592 C  CB  B VAL B 1 258 ? 24.616  12.836  27.539  0.36 17.40  ? 481  VAL B CB  1 
ATOM   4593 C  CG1 A VAL B 1 258 ? 25.452  12.473  28.668  0.64 17.20  ? 481  VAL B CG1 1 
ATOM   4594 C  CG1 B VAL B 1 258 ? 24.290  14.320  27.625  0.36 17.64  ? 481  VAL B CG1 1 
ATOM   4595 C  CG2 A VAL B 1 258 ? 24.058  14.262  27.620  0.64 19.40  ? 481  VAL B CG2 1 
ATOM   4596 C  CG2 B VAL B 1 258 ? 23.436  11.990  27.923  0.36 17.72  ? 481  VAL B CG2 1 
ATOM   4597 N  N   . ASN B 1 259 ? 26.754  10.785  26.344  1.00 18.17  ? 482  ASN B N   1 
ATOM   4598 C  CA  . ASN B 1 259 ? 27.270  9.446   26.550  1.00 20.25  ? 482  ASN B CA  1 
ATOM   4599 C  C   . ASN B 1 259 ? 27.055  9.164   28.027  1.00 20.94  ? 482  ASN B C   1 
ATOM   4600 O  O   . ASN B 1 259 ? 27.664  9.838   28.872  1.00 21.94  ? 482  ASN B O   1 
ATOM   4601 C  CB  . ASN B 1 259 ? 28.752  9.411   26.221  1.00 21.17  ? 482  ASN B CB  1 
ATOM   4602 C  CG  . ASN B 1 259 ? 29.365  8.039   26.420  1.00 22.81  ? 482  ASN B CG  1 
ATOM   4603 O  OD1 . ASN B 1 259 ? 28.947  7.271   27.288  1.00 22.89  ? 482  ASN B OD1 1 
ATOM   4604 N  ND2 . ASN B 1 259 ? 30.356  7.722   25.603  1.00 24.23  ? 482  ASN B ND2 1 
ATOM   4605 N  N   . PRO B 1 260 ? 26.181  8.221   28.402  1.00 21.96  ? 483  PRO B N   1 
ATOM   4606 C  CA  . PRO B 1 260 ? 25.886  8.037   29.832  1.00 24.65  ? 483  PRO B CA  1 
ATOM   4607 C  C   . PRO B 1 260 ? 27.056  7.517   30.642  1.00 27.07  ? 483  PRO B C   1 
ATOM   4608 O  O   . PRO B 1 260 ? 27.059  7.704   31.865  1.00 27.63  ? 483  PRO B O   1 
ATOM   4609 C  CB  . PRO B 1 260 ? 24.713  7.052   29.831  1.00 24.12  ? 483  PRO B CB  1 
ATOM   4610 C  CG  . PRO B 1 260 ? 24.883  6.290   28.563  1.00 23.39  ? 483  PRO B CG  1 
ATOM   4611 C  CD  . PRO B 1 260 ? 25.426  7.278   27.557  1.00 22.67  ? 483  PRO B CD  1 
ATOM   4612 N  N   . ASP B 1 261 ? 28.045  6.880   30.007  1.00 28.46  ? 484  ASP B N   1 
ATOM   4613 C  CA  . ASP B 1 261 ? 29.218  6.402   30.738  1.00 30.63  ? 484  ASP B CA  1 
ATOM   4614 C  C   . ASP B 1 261 ? 30.066  7.561   31.239  1.00 31.20  ? 484  ASP B C   1 
ATOM   4615 O  O   . ASP B 1 261 ? 30.496  7.574   32.400  1.00 32.69  ? 484  ASP B O   1 
ATOM   4616 C  CB  . ASP B 1 261 ? 30.064  5.513   29.828  1.00 34.03  ? 484  ASP B CB  1 
ATOM   4617 C  CG  . ASP B 1 261 ? 29.408  4.193   29.535  1.00 36.33  ? 484  ASP B CG  1 
ATOM   4618 O  OD1 . ASP B 1 261 ? 28.419  3.865   30.221  1.00 37.48  ? 484  ASP B OD1 1 
ATOM   4619 O  OD2 . ASP B 1 261 ? 29.884  3.483   28.623  1.00 37.12  ? 484  ASP B OD2 1 
ATOM   4620 N  N   . THR B 1 262 ? 30.339  8.531   30.365  1.00 31.23  ? 485  THR B N   1 
ATOM   4621 C  CA  . THR B 1 262 ? 31.281  9.604   30.644  1.00 30.45  ? 485  THR B CA  1 
ATOM   4622 C  C   . THR B 1 262 ? 30.612  10.920  30.997  1.00 30.24  ? 485  THR B C   1 
ATOM   4623 O  O   . THR B 1 262 ? 31.282  11.811  31.532  1.00 31.09  ? 485  THR B O   1 
ATOM   4624 C  CB  . THR B 1 262 ? 32.166  9.841   29.416  1.00 30.12  ? 485  THR B CB  1 
ATOM   4625 O  OG1 . THR B 1 262 ? 31.342  10.235  28.307  1.00 28.30  ? 485  THR B OG1 1 
ATOM   4626 C  CG2 . THR B 1 262 ? 32.922  8.571   29.052  1.00 31.65  ? 485  THR B CG2 1 
ATOM   4627 N  N   . GLY B 1 263 ? 29.319  11.065  30.710  1.00 28.74  ? 486  GLY B N   1 
ATOM   4628 C  CA  . GLY B 1 263 ? 28.650  12.341  30.821  1.00 29.44  ? 486  GLY B CA  1 
ATOM   4629 C  C   . GLY B 1 263 ? 29.001  13.331  29.736  1.00 29.24  ? 486  GLY B C   1 
ATOM   4630 O  O   . GLY B 1 263 ? 28.531  14.473  29.789  1.00 30.53  ? 486  GLY B O   1 
ATOM   4631 N  N   . ARG B 1 264 ? 29.814  12.931  28.761  1.00 28.04  ? 487  ARG B N   1 
ATOM   4632 C  CA  . ARG B 1 264 ? 30.203  13.821  27.678  1.00 30.19  ? 487  ARG B CA  1 
ATOM   4633 C  C   . ARG B 1 264 ? 28.991  14.181  26.830  1.00 24.48  ? 487  ARG B C   1 
ATOM   4634 O  O   . ARG B 1 264 ? 28.196  13.314  26.454  1.00 23.20  ? 487  ARG B O   1 
ATOM   4635 C  CB  . ARG B 1 264 ? 31.250  13.130  26.804  1.00 37.07  ? 487  ARG B CB  1 
ATOM   4636 C  CG  . ARG B 1 264 ? 31.609  13.884  25.533  1.00 66.46  ? 487  ARG B CG  1 
ATOM   4637 C  CD  . ARG B 1 264 ? 32.424  13.014  24.586  1.00 67.51  ? 487  ARG B CD  1 
ATOM   4638 N  NE  . ARG B 1 264 ? 32.839  13.736  23.388  1.00 76.66  ? 487  ARG B NE  1 
ATOM   4639 C  CZ  . ARG B 1 264 ? 33.453  13.179  22.353  1.00 153.59 ? 487  ARG B CZ  1 
ATOM   4640 N  NH1 . ARG B 1 264 ? 33.730  11.885  22.327  1.00 67.07  ? 487  ARG B NH1 1 
ATOM   4641 N  NH2 . ARG B 1 264 ? 33.797  13.938  21.317  1.00 89.32  ? 487  ARG B NH2 1 
ATOM   4642 N  N   . VAL B 1 265 ? 28.850  15.470  26.535  1.00 23.68  ? 488  VAL B N   1 
ATOM   4643 C  CA  . VAL B 1 265 ? 27.842  15.952  25.602  1.00 21.52  ? 488  VAL B CA  1 
ATOM   4644 C  C   . VAL B 1 265 ? 28.420  15.848  24.196  1.00 21.69  ? 488  VAL B C   1 
ATOM   4645 O  O   . VAL B 1 265 ? 29.436  16.477  23.882  1.00 24.06  ? 488  VAL B O   1 
ATOM   4646 C  CB  . VAL B 1 265 ? 27.438  17.398  25.924  1.00 23.26  ? 488  VAL B CB  1 
ATOM   4647 C  CG1 . VAL B 1 265 ? 26.480  17.927  24.866  1.00 22.34  ? 488  VAL B CG1 1 
ATOM   4648 C  CG2 . VAL B 1 265 ? 26.808  17.481  27.305  1.00 23.39  ? 488  VAL B CG2 1 
ATOM   4649 N  N   . LEU B 1 266 ? 27.775  15.052  23.347  1.00 19.69  ? 489  LEU B N   1 
ATOM   4650 C  CA  . LEU B 1 266 ? 28.211  14.968  21.961  1.00 19.74  ? 489  LEU B CA  1 
ATOM   4651 C  C   . LEU B 1 266 ? 27.782  16.203  21.179  1.00 19.51  ? 489  LEU B C   1 
ATOM   4652 O  O   . LEU B 1 266 ? 28.565  16.744  20.390  1.00 22.13  ? 489  LEU B O   1 
ATOM   4653 C  CB  . LEU B 1 266 ? 27.666  13.696  21.306  1.00 21.10  ? 489  LEU B CB  1 
ATOM   4654 C  CG  . LEU B 1 266 ? 28.305  12.349  21.659  1.00 23.59  ? 489  LEU B CG  1 
ATOM   4655 C  CD1 . LEU B 1 266 ? 29.818  12.408  21.497  1.00 25.15  ? 489  LEU B CD1 1 
ATOM   4656 C  CD2 . LEU B 1 266 ? 27.925  11.889  23.053  1.00 22.51  ? 489  LEU B CD2 1 
ATOM   4657 N  N   . PHE B 1 267 ? 26.556  16.668  21.402  1.00 17.48  ? 490  PHE B N   1 
ATOM   4658 C  CA  . PHE B 1 267 ? 26.036  17.886  20.789  1.00 16.64  ? 490  PHE B CA  1 
ATOM   4659 C  C   . PHE B 1 267 ? 24.753  18.256  21.521  1.00 15.59  ? 490  PHE B C   1 
ATOM   4660 O  O   . PHE B 1 267 ? 24.205  17.461  22.291  1.00 15.98  ? 490  PHE B O   1 
ATOM   4661 C  CB  . PHE B 1 267 ? 25.783  17.705  19.287  1.00 15.50  ? 490  PHE B CB  1 
ATOM   4662 C  CG  . PHE B 1 267 ? 24.692  16.719  18.963  1.00 14.28  ? 490  PHE B CG  1 
ATOM   4663 C  CD1 . PHE B 1 267 ? 24.974  15.359  18.848  1.00 14.55  ? 490  PHE B CD1 1 
ATOM   4664 C  CD2 . PHE B 1 267 ? 23.388  17.151  18.738  1.00 14.58  ? 490  PHE B CD2 1 
ATOM   4665 C  CE1 . PHE B 1 267 ? 23.980  14.447  18.543  1.00 15.17  ? 490  PHE B CE1 1 
ATOM   4666 C  CE2 . PHE B 1 267 ? 22.384  16.243  18.425  1.00 14.56  ? 490  PHE B CE2 1 
ATOM   4667 C  CZ  . PHE B 1 267 ? 22.684  14.880  18.329  1.00 14.03  ? 490  PHE B CZ  1 
ATOM   4668 N  N   . GLU B 1 268 ? 24.281  19.477  21.281  1.00 14.88  ? 491  GLU B N   1 
ATOM   4669 C  CA  . GLU B 1 268 ? 23.000  19.931  21.800  1.00 14.27  ? 491  GLU B CA  1 
ATOM   4670 C  C   . GLU B 1 268 ? 22.062  20.281  20.654  1.00 14.01  ? 491  GLU B C   1 
ATOM   4671 O  O   . GLU B 1 268 ? 22.488  20.529  19.517  1.00 13.95  ? 491  GLU B O   1 
ATOM   4672 C  CB  . GLU B 1 268 ? 23.133  21.122  22.763  1.00 15.13  ? 491  GLU B CB  1 
ATOM   4673 C  CG  . GLU B 1 268 ? 23.938  22.275  22.231  1.00 16.94  ? 491  GLU B CG  1 
ATOM   4674 C  CD  . GLU B 1 268 ? 23.863  23.493  23.136  1.00 17.94  ? 491  GLU B CD  1 
ATOM   4675 O  OE1 . GLU B 1 268 ? 23.368  23.368  24.280  1.00 20.00  ? 491  GLU B OE1 1 
ATOM   4676 O  OE2 . GLU B 1 268 ? 24.302  24.587  22.719  1.00 19.43  ? 491  GLU B OE2 1 
ATOM   4677 N  N   . ALA B 1 269 ? 20.768  20.281  20.967  1.00 13.19  ? 492  ALA B N   1 
ATOM   4678 C  CA  . ALA B 1 269 ? 19.741  20.439  19.946  1.00 13.27  ? 492  ALA B CA  1 
ATOM   4679 C  C   . ALA B 1 269 ? 18.526  21.118  20.555  1.00 12.14  ? 492  ALA B C   1 
ATOM   4680 O  O   . ALA B 1 269 ? 18.386  21.201  21.783  1.00 13.16  ? 492  ALA B O   1 
ATOM   4681 C  CB  . ALA B 1 269 ? 19.349  19.085  19.346  1.00 14.62  ? 492  ALA B CB  1 
ATOM   4682 N  N   . LYS B 1 270 ? 17.659  21.628  19.683  1.00 12.96  ? 493  LYS B N   1 
ATOM   4683 C  CA  . LYS B 1 270 ? 16.403  22.253  20.077  1.00 13.22  ? 493  LYS B CA  1 
ATOM   4684 C  C   . LYS B 1 270 ? 15.256  21.322  19.709  1.00 13.05  ? 493  LYS B C   1 
ATOM   4685 O  O   . LYS B 1 270 ? 15.072  20.989  18.530  1.00 13.36  ? 493  LYS B O   1 
ATOM   4686 C  CB  . LYS B 1 270 ? 16.226  23.592  19.368  1.00 15.56  ? 493  LYS B CB  1 
ATOM   4687 C  CG  . LYS B 1 270 ? 17.043  24.681  19.994  1.00 18.76  ? 493  LYS B CG  1 
ATOM   4688 C  CD  . LYS B 1 270 ? 17.400  25.740  18.980  1.00 23.39  ? 493  LYS B CD  1 
ATOM   4689 C  CE  . LYS B 1 270 ? 16.721  27.053  19.254  1.00 22.22  ? 493  LYS B CE  1 
ATOM   4690 N  NZ  . LYS B 1 270 ? 17.184  28.105  18.304  1.00 19.48  ? 493  LYS B NZ  1 
ATOM   4691 N  N   . LEU B 1 271 ? 14.490  20.906  20.714  1.00 13.02  ? 494  LEU B N   1 
ATOM   4692 C  CA  . LEU B 1 271 ? 13.311  20.068  20.529  1.00 13.79  ? 494  LEU B CA  1 
ATOM   4693 C  C   . LEU B 1 271 ? 12.091  20.991  20.572  1.00 12.87  ? 494  LEU B C   1 
ATOM   4694 O  O   . LEU B 1 271 ? 11.734  21.529  21.629  1.00 14.16  ? 494  LEU B O   1 
ATOM   4695 C  CB  . LEU B 1 271 ? 13.260  18.970  21.592  1.00 12.96  ? 494  LEU B CB  1 
ATOM   4696 C  CG  . LEU B 1 271 ? 12.035  18.053  21.538  1.00 12.22  ? 494  LEU B CG  1 
ATOM   4697 C  CD1 . LEU B 1 271 ? 11.880  17.383  20.171  1.00 13.31  ? 494  LEU B CD1 1 
ATOM   4698 C  CD2 . LEU B 1 271 ? 12.110  17.014  22.656  1.00 12.84  ? 494  LEU B CD2 1 
ATOM   4699 N  N   . HIS B 1 272 ? 11.482  21.213  19.413  1.00 12.69  ? 495  HIS B N   1 
ATOM   4700 C  CA  . HIS B 1 272 ? 10.417  22.196  19.290  1.00 13.55  ? 495  HIS B CA  1 
ATOM   4701 C  C   . HIS B 1 272 ? 9.090   21.603  19.743  1.00 13.95  ? 495  HIS B C   1 
ATOM   4702 O  O   . HIS B 1 272 ? 8.839   20.403  19.591  1.00 14.46  ? 495  HIS B O   1 
ATOM   4703 C  CB  . HIS B 1 272 ? 10.333  22.670  17.839  1.00 13.67  ? 495  HIS B CB  1 
ATOM   4704 C  CG  . HIS B 1 272 ? 11.591  23.331  17.370  1.00 13.99  ? 495  HIS B CG  1 
ATOM   4705 N  ND1 . HIS B 1 272 ? 11.739  24.703  17.312  1.00 15.89  ? 495  HIS B ND1 1 
ATOM   4706 C  CD2 . HIS B 1 272 ? 12.785  22.807  17.006  1.00 14.68  ? 495  HIS B CD2 1 
ATOM   4707 C  CE1 . HIS B 1 272 ? 12.963  24.992  16.900  1.00 17.10  ? 495  HIS B CE1 1 
ATOM   4708 N  NE2 . HIS B 1 272 ? 13.620  23.859  16.715  1.00 15.65  ? 495  HIS B NE2 1 
ATOM   4709 N  N   . ARG B 1 273 ? 8.222   22.468  20.287  1.00 15.85  ? 496  ARG B N   1 
ATOM   4710 C  CA  . ARG B 1 273 ? 6.964   21.992  20.859  1.00 18.90  ? 496  ARG B CA  1 
ATOM   4711 C  C   . ARG B 1 273 ? 6.115   21.235  19.837  1.00 17.22  ? 496  ARG B C   1 
ATOM   4712 O  O   . ARG B 1 273 ? 5.346   20.339  20.210  1.00 16.35  ? 496  ARG B O   1 
ATOM   4713 C  CB  . ARG B 1 273 ? 6.187   23.151  21.494  1.00 25.15  ? 496  ARG B CB  1 
ATOM   4714 C  CG  . ARG B 1 273 ? 5.170   23.799  20.587  1.00 31.95  ? 496  ARG B CG  1 
ATOM   4715 C  CD  . ARG B 1 273 ? 3.957   24.246  21.387  1.00 37.91  ? 496  ARG B CD  1 
ATOM   4716 N  NE  . ARG B 1 273 ? 4.328   25.149  22.467  1.00 42.48  ? 496  ARG B NE  1 
ATOM   4717 C  CZ  . ARG B 1 273 ? 3.601   25.352  23.559  1.00 46.57  ? 496  ARG B CZ  1 
ATOM   4718 N  NH1 . ARG B 1 273 ? 2.465   24.705  23.763  1.00 48.38  ? 496  ARG B NH1 1 
ATOM   4719 N  NH2 . ARG B 1 273 ? 4.032   26.216  24.473  1.00 47.17  ? 496  ARG B NH2 1 
ATOM   4720 N  N   . GLN B 1 274 ? 6.269   21.546  18.549  1.00 15.12  ? 497  GLN B N   1 
ATOM   4721 C  CA  . GLN B 1 274 ? 5.529   20.879  17.493  1.00 16.13  ? 497  GLN B CA  1 
ATOM   4722 C  C   . GLN B 1 274 ? 5.972   19.434  17.274  1.00 14.80  ? 497  GLN B C   1 
ATOM   4723 O  O   . GLN B 1 274 ? 5.266   18.689  16.585  1.00 16.19  ? 497  GLN B O   1 
ATOM   4724 C  CB  . GLN B 1 274 ? 5.682   21.696  16.207  1.00 20.34  ? 497  GLN B CB  1 
ATOM   4725 C  CG  . GLN B 1 274 ? 5.057   23.103  16.273  1.00 23.70  ? 497  GLN B CG  1 
ATOM   4726 C  CD  . GLN B 1 274 ? 5.901   24.183  17.004  1.00 26.83  ? 497  GLN B CD  1 
ATOM   4727 O  OE1 . GLN B 1 274 ? 7.105   24.024  17.274  1.00 21.25  ? 497  GLN B OE1 1 
ATOM   4728 N  NE2 . GLN B 1 274 ? 5.249   25.299  17.311  1.00 31.17  ? 497  GLN B NE2 1 
ATOM   4729 N  N   . GLY B 1 275 ? 7.109   19.015  17.839  1.00 13.60  ? 498  GLY B N   1 
ATOM   4730 C  CA  . GLY B 1 275 ? 7.595   17.648  17.717  1.00 14.09  ? 498  GLY B CA  1 
ATOM   4731 C  C   . GLY B 1 275 ? 8.648   17.442  16.643  1.00 12.61  ? 498  GLY B C   1 
ATOM   4732 O  O   . GLY B 1 275 ? 8.531   16.518  15.827  1.00 14.33  ? 498  GLY B O   1 
ATOM   4733 N  N   . TYR B 1 276 ? 9.679   18.284  16.620  1.00 13.18  ? 499  TYR B N   1 
ATOM   4734 C  CA  . TYR B 1 276 ? 10.796  18.109  15.696  1.00 12.28  ? 499  TYR B CA  1 
ATOM   4735 C  C   . TYR B 1 276 ? 12.032  18.751  16.312  1.00 12.07  ? 499  TYR B C   1 
ATOM   4736 O  O   . TYR B 1 276 ? 11.942  19.524  17.274  1.00 13.81  ? 499  TYR B O   1 
ATOM   4737 C  CB  . TYR B 1 276 ? 10.502  18.669  14.289  1.00 12.78  ? 499  TYR B CB  1 
ATOM   4738 C  CG  . TYR B 1 276 ? 10.350  20.179  14.261  1.00 12.99  ? 499  TYR B CG  1 
ATOM   4739 C  CD1 . TYR B 1 276 ? 9.123   20.768  14.522  1.00 13.47  ? 499  TYR B CD1 1 
ATOM   4740 C  CD2 . TYR B 1 276 ? 11.434  21.009  14.003  1.00 14.18  ? 499  TYR B CD2 1 
ATOM   4741 C  CE1 . TYR B 1 276 ? 8.958   22.134  14.501  1.00 14.26  ? 499  TYR B CE1 1 
ATOM   4742 C  CE2 . TYR B 1 276 ? 11.289  22.390  13.986  1.00 15.23  ? 499  TYR B CE2 1 
ATOM   4743 C  CZ  . TYR B 1 276 ? 10.053  22.952  14.243  1.00 15.29  ? 499  TYR B CZ  1 
ATOM   4744 O  OH  . TYR B 1 276 ? 9.916   24.325  14.226  1.00 17.19  ? 499  TYR B OH  1 
ATOM   4745 N  N   . ILE B 1 277 ? 13.192  18.427  15.744  1.00 11.58  ? 500  ILE B N   1 
ATOM   4746 C  CA  . ILE B 1 277 ? 14.482  18.808  16.308  1.00 11.42  ? 500  ILE B CA  1 
ATOM   4747 C  C   . ILE B 1 277 ? 15.265  19.624  15.295  1.00 11.79  ? 500  ILE B C   1 
ATOM   4748 O  O   . ILE B 1 277 ? 15.282  19.301  14.103  1.00 12.25  ? 500  ILE B O   1 
ATOM   4749 C  CB  . ILE B 1 277 ? 15.295  17.557  16.703  1.00 11.06  ? 500  ILE B CB  1 
ATOM   4750 C  CG1 . ILE B 1 277 ? 14.515  16.704  17.712  1.00 12.69  ? 500  ILE B CG1 1 
ATOM   4751 C  CG2 . ILE B 1 277 ? 16.688  17.964  17.245  1.00 12.83  ? 500  ILE B CG2 1 
ATOM   4752 C  CD1 . ILE B 1 277 ? 15.237  15.423  18.138  1.00 13.44  ? 500  ILE B CD1 1 
ATOM   4753 N  N   . THR B 1 278 ? 15.923  20.687  15.768  1.00 12.42  ? 501  THR B N   1 
ATOM   4754 C  CA  . THR B 1 278 ? 16.915  21.390  14.961  1.00 13.23  ? 501  THR B CA  1 
ATOM   4755 C  C   . THR B 1 278 ? 18.281  21.396  15.647  1.00 13.81  ? 501  THR B C   1 
ATOM   4756 O  O   . THR B 1 278 ? 18.382  21.298  16.876  1.00 14.05  ? 501  THR B O   1 
ATOM   4757 C  CB  . THR B 1 278 ? 16.501  22.840  14.638  1.00 14.02  ? 501  THR B CB  1 
ATOM   4758 O  OG1 . THR B 1 278 ? 16.278  23.557  15.860  1.00 14.92  ? 501  THR B OG1 1 
ATOM   4759 C  CG2 . THR B 1 278 ? 15.233  22.863  13.786  1.00 15.24  ? 501  THR B CG2 1 
ATOM   4760 N  N   . VAL B 1 279 ? 19.334  21.511  14.832  1.00 14.09  ? 502  VAL B N   1 
ATOM   4761 C  CA  . VAL B 1 279 ? 20.719  21.534  15.292  1.00 13.94  ? 502  VAL B CA  1 
ATOM   4762 C  C   . VAL B 1 279 ? 21.456  22.617  14.522  1.00 15.16  ? 502  VAL B C   1 
ATOM   4763 O  O   . VAL B 1 279 ? 21.070  22.994  13.416  1.00 16.41  ? 502  VAL B O   1 
ATOM   4764 C  CB  . VAL B 1 279 ? 21.444  20.181  15.060  1.00 13.78  ? 502  VAL B CB  1 
ATOM   4765 C  CG1 . VAL B 1 279 ? 20.948  19.121  16.020  1.00 14.52  ? 502  VAL B CG1 1 
ATOM   4766 C  CG2 . VAL B 1 279 ? 21.257  19.715  13.612  1.00 14.20  ? 502  VAL B CG2 1 
ATOM   4767 N  N   . ALA B 1 280 ? 22.556  23.096  15.110  1.00 15.34  ? 503  ALA B N   1 
ATOM   4768 C  CA  . ALA B 1 280 ? 23.423  24.070  14.446  1.00 16.01  ? 503  ALA B CA  1 
ATOM   4769 C  C   . ALA B 1 280 ? 24.471  23.319  13.630  1.00 16.75  ? 503  ALA B C   1 
ATOM   4770 O  O   . ALA B 1 280 ? 25.600  23.086  14.066  1.00 18.61  ? 503  ALA B O   1 
ATOM   4771 C  CB  . ALA B 1 280 ? 24.053  25.010  15.471  1.00 16.17  ? 503  ALA B CB  1 
ATOM   4772 N  N   . LYS B 1 281 ? 24.080  22.930  12.417  1.00 18.13  ? 504  LYS B N   1 
ATOM   4773 C  CA  . LYS B 1 281 ? 24.982  22.284  11.475  1.00 21.05  ? 504  LYS B CA  1 
ATOM   4774 C  C   . LYS B 1 281 ? 24.541  22.638  10.064  1.00 23.21  ? 504  LYS B C   1 
ATOM   4775 O  O   . LYS B 1 281 ? 23.354  22.853  9.810   1.00 24.34  ? 504  LYS B O   1 
ATOM   4776 C  CB  . LYS B 1 281 ? 25.013  20.757  11.644  1.00 25.12  ? 504  LYS B CB  1 
ATOM   4777 C  CG  . LYS B 1 281 ? 26.173  20.101  10.899  1.00 28.71  ? 504  LYS B CG  1 
ATOM   4778 C  CD  . LYS B 1 281 ? 26.391  18.657  11.310  1.00 33.30  ? 504  LYS B CD  1 
ATOM   4779 C  CE  . LYS B 1 281 ? 27.619  18.079  10.621  1.00 37.64  ? 504  LYS B CE  1 
ATOM   4780 N  NZ  . LYS B 1 281 ? 28.825  18.917  10.848  1.00 40.24  ? 504  LYS B NZ  1 
ATOM   4781 N  N   . THR B 1 282 ? 25.512  22.703  9.152   1.00 24.97  ? 505  THR B N   1 
ATOM   4782 C  CA  . THR B 1 282 ? 25.278  23.000  7.746   1.00 29.71  ? 505  THR B CA  1 
ATOM   4783 C  C   . THR B 1 282 ? 25.793  21.836  6.908   1.00 28.79  ? 505  THR B C   1 
ATOM   4784 O  O   . THR B 1 282 ? 26.909  21.358  7.126   1.00 30.62  ? 505  THR B O   1 
ATOM   4785 C  CB  . THR B 1 282 ? 26.019  24.289  7.360   1.00 34.44  ? 505  THR B CB  1 
ATOM   4786 O  OG1 . THR B 1 282 ? 25.605  25.365  8.220   1.00 37.69  ? 505  THR B OG1 1 
ATOM   4787 C  CG2 . THR B 1 282 ? 25.736  24.664  5.924   1.00 36.21  ? 505  THR B CG2 1 
ATOM   4788 N  N   . GLY B 1 283 ? 24.986  21.376  5.963   1.00 26.36  ? 506  GLY B N   1 
ATOM   4789 C  CA  . GLY B 1 283 ? 25.384  20.323  5.050   1.00 24.84  ? 506  GLY B CA  1 
ATOM   4790 C  C   . GLY B 1 283 ? 24.665  19.013  5.339   1.00 23.98  ? 506  GLY B C   1 
ATOM   4791 O  O   . GLY B 1 283 ? 23.920  18.872  6.305   1.00 23.44  ? 506  GLY B O   1 
ATOM   4792 N  N   . ASP B 1 284 ? 24.909  18.043  4.458   1.00 25.84  ? 507  ASP B N   1 
ATOM   4793 C  CA  . ASP B 1 284 ? 24.228  16.749  4.483   1.00 26.72  ? 507  ASP B CA  1 
ATOM   4794 C  C   . ASP B 1 284 ? 25.206  15.717  5.025   1.00 27.07  ? 507  ASP B C   1 
ATOM   4795 O  O   . ASP B 1 284 ? 26.162  15.345  4.341   1.00 28.59  ? 507  ASP B O   1 
ATOM   4796 C  CB  . ASP B 1 284 ? 23.787  16.376  3.069   1.00 30.11  ? 507  ASP B CB  1 
ATOM   4797 C  CG  . ASP B 1 284 ? 23.016  15.063  3.015   1.00 34.41  ? 507  ASP B CG  1 
ATOM   4798 O  OD1 . ASP B 1 284 ? 23.590  14.008  3.342   1.00 36.46  ? 507  ASP B OD1 1 
ATOM   4799 O  OD2 . ASP B 1 284 ? 21.830  15.092  2.638   1.00 37.76  ? 507  ASP B OD2 1 
ATOM   4800 N  N   . SER B 1 285 ? 24.960  15.223  6.236   1.00 26.29  ? 508  SER B N   1 
ATOM   4801 C  CA  A SER B 1 285 ? 25.919  14.320  6.857   0.62 27.00  ? 508  SER B CA  1 
ATOM   4802 C  CA  B SER B 1 285 ? 25.920  14.323  6.860   0.38 26.81  ? 508  SER B CA  1 
ATOM   4803 C  C   . SER B 1 285 ? 25.223  13.519  7.943   1.00 26.13  ? 508  SER B C   1 
ATOM   4804 O  O   . SER B 1 285 ? 24.261  14.004  8.551   1.00 22.18  ? 508  SER B O   1 
ATOM   4805 C  CB  A SER B 1 285 ? 27.081  15.112  7.467   0.62 29.75  ? 508  SER B CB  1 
ATOM   4806 C  CB  B SER B 1 285 ? 27.086  15.116  7.467   0.38 28.74  ? 508  SER B CB  1 
ATOM   4807 O  OG  A SER B 1 285 ? 26.592  16.012  8.440   0.62 31.18  ? 508  SER B OG  1 
ATOM   4808 O  OG  B SER B 1 285 ? 27.965  14.266  8.178   0.38 29.42  ? 508  SER B OG  1 
ATOM   4809 N  N   . PRO B 1 286 ? 25.676  12.297  8.205   1.00 28.30  ? 509  PRO B N   1 
ATOM   4810 C  CA  . PRO B 1 286 ? 25.224  11.592  9.403   1.00 27.54  ? 509  PRO B CA  1 
ATOM   4811 C  C   . PRO B 1 286 ? 25.851  12.229  10.632  1.00 25.37  ? 509  PRO B C   1 
ATOM   4812 O  O   . PRO B 1 286 ? 26.827  12.979  10.555  1.00 25.83  ? 509  PRO B O   1 
ATOM   4813 C  CB  . PRO B 1 286 ? 25.757  10.169  9.196   1.00 30.18  ? 509  PRO B CB  1 
ATOM   4814 C  CG  . PRO B 1 286 ? 26.946  10.352  8.323   1.00 31.51  ? 509  PRO B CG  1 
ATOM   4815 C  CD  . PRO B 1 286 ? 26.594  11.477  7.395   1.00 30.74  ? 509  PRO B CD  1 
ATOM   4816 N  N   . ILE B 1 287 ? 25.262  11.931  11.778  1.00 24.33  ? 510  ILE B N   1 
ATOM   4817 C  CA  . ILE B 1 287 ? 25.752  12.407  13.065  1.00 24.13  ? 510  ILE B CA  1 
ATOM   4818 C  C   . ILE B 1 287 ? 26.352  11.205  13.777  1.00 27.84  ? 510  ILE B C   1 
ATOM   4819 O  O   . ILE B 1 287 ? 25.628  10.284  14.172  1.00 28.19  ? 510  ILE B O   1 
ATOM   4820 C  CB  . ILE B 1 287 ? 24.627  13.037  13.896  1.00 25.30  ? 510  ILE B CB  1 
ATOM   4821 C  CG1 . ILE B 1 287 ? 23.924  14.137  13.101  1.00 26.41  ? 510  ILE B CG1 1 
ATOM   4822 C  CG2 . ILE B 1 287 ? 25.170  13.568  15.206  1.00 25.25  ? 510  ILE B CG2 1 
ATOM   4823 C  CD1 . ILE B 1 287 ? 24.862  15.121  12.461  1.00 28.50  ? 510  ILE B CD1 1 
ATOM   4824 N  N   . ASN B 1 288 ? 27.673  11.202  13.935  1.00 31.14  ? 511  ASN B N   1 
ATOM   4825 C  CA  . ASN B 1 288 ? 28.359  10.075  14.555  1.00 35.87  ? 511  ASN B CA  1 
ATOM   4826 C  C   . ASN B 1 288 ? 28.268  10.195  16.071  1.00 34.24  ? 511  ASN B C   1 
ATOM   4827 O  O   . ASN B 1 288 ? 28.730  11.183  16.654  1.00 37.83  ? 511  ASN B O   1 
ATOM   4828 C  CB  . ASN B 1 288 ? 29.814  10.025  14.096  1.00 41.64  ? 511  ASN B CB  1 
ATOM   4829 C  CG  . ASN B 1 288 ? 29.945  9.684   12.625  1.00 46.16  ? 511  ASN B CG  1 
ATOM   4830 O  OD1 . ASN B 1 288 ? 29.207  8.848   12.101  1.00 47.43  ? 511  ASN B OD1 1 
ATOM   4831 N  ND2 . ASN B 1 288 ? 30.883  10.335  11.947  1.00 48.34  ? 511  ASN B ND2 1 
ATOM   4832 N  N   . VAL B 1 289 ? 27.665  9.194   16.703  1.00 31.38  ? 512  VAL B N   1 
ATOM   4833 C  CA  . VAL B 1 289 ? 27.443  9.188   18.148  1.00 29.51  ? 512  VAL B CA  1 
ATOM   4834 C  C   . VAL B 1 289 ? 27.715  7.790   18.680  1.00 26.98  ? 512  VAL B C   1 
ATOM   4835 O  O   . VAL B 1 289 ? 27.660  6.803   17.935  1.00 26.15  ? 512  VAL B O   1 
ATOM   4836 C  CB  . VAL B 1 289 ? 26.004  9.614   18.504  1.00 31.48  ? 512  VAL B CB  1 
ATOM   4837 C  CG1 . VAL B 1 289 ? 25.811  11.112  18.290  1.00 32.85  ? 512  VAL B CG1 1 
ATOM   4838 C  CG2 . VAL B 1 289 ? 25.007  8.834   17.678  1.00 32.35  ? 512  VAL B CG2 1 
ATOM   4839 N  N   . PRO B 1 290 ? 28.028  7.675   19.969  1.00 25.49  ? 513  PRO B N   1 
ATOM   4840 C  CA  . PRO B 1 290 ? 28.216  6.341   20.549  1.00 25.08  ? 513  PRO B CA  1 
ATOM   4841 C  C   . PRO B 1 290 ? 26.894  5.593   20.597  1.00 24.11  ? 513  PRO B C   1 
ATOM   4842 O  O   . PRO B 1 290 ? 25.827  6.186   20.767  1.00 24.28  ? 513  PRO B O   1 
ATOM   4843 C  CB  . PRO B 1 290 ? 28.732  6.646   21.959  1.00 25.94  ? 513  PRO B CB  1 
ATOM   4844 C  CG  . PRO B 1 290 ? 28.178  7.983   22.271  1.00 27.02  ? 513  PRO B CG  1 
ATOM   4845 C  CD  . PRO B 1 290 ? 28.253  8.736   20.969  1.00 26.24  ? 513  PRO B CD  1 
ATOM   4846 N  N   . ALA B 1 291 ? 26.974  4.269   20.429  1.00 24.39  ? 514  ALA B N   1 
ATOM   4847 C  CA  . ALA B 1 291 ? 25.762  3.454   20.393  1.00 24.60  ? 514  ALA B CA  1 
ATOM   4848 C  C   . ALA B 1 291 ? 24.966  3.551   21.690  1.00 23.36  ? 514  ALA B C   1 
ATOM   4849 O  O   . ALA B 1 291 ? 23.756  3.311   21.694  1.00 25.33  ? 514  ALA B O   1 
ATOM   4850 C  CB  . ALA B 1 291 ? 26.118  1.998   20.084  1.00 26.81  ? 514  ALA B CB  1 
ATOM   4851 N  N   . ASN B 1 292 ? 25.613  3.901   22.792  1.00 23.45  ? 515  ASN B N   1 
ATOM   4852 C  CA  . ASN B 1 292 ? 24.937  3.987   24.076  1.00 23.06  ? 515  ASN B CA  1 
ATOM   4853 C  C   . ASN B 1 292 ? 24.310  5.354   24.338  1.00 21.19  ? 515  ASN B C   1 
ATOM   4854 O  O   . ASN B 1 292 ? 23.694  5.540   25.391  1.00 21.02  ? 515  ASN B O   1 
ATOM   4855 C  CB  . ASN B 1 292 ? 25.903  3.617   25.212  1.00 24.21  ? 515  ASN B CB  1 
ATOM   4856 C  CG  . ASN B 1 292 ? 26.957  4.685   25.473  1.00 26.40  ? 515  ASN B CG  1 
ATOM   4857 O  OD1 . ASN B 1 292 ? 27.152  5.609   24.679  1.00 27.83  ? 515  ASN B OD1 1 
ATOM   4858 N  ND2 . ASN B 1 292 ? 27.654  4.550   26.590  1.00 26.88  ? 515  ASN B ND2 1 
ATOM   4859 N  N   . GLY B 1 293 ? 24.428  6.307   23.406  1.00 19.94  ? 516  GLY B N   1 
ATOM   4860 C  CA  . GLY B 1 293 ? 24.023  7.669   23.694  1.00 17.93  ? 516  GLY B CA  1 
ATOM   4861 C  C   . GLY B 1 293 ? 22.530  7.885   23.560  1.00 16.30  ? 516  GLY B C   1 
ATOM   4862 O  O   . GLY B 1 293 ? 21.816  7.141   22.883  1.00 17.02  ? 516  GLY B O   1 
ATOM   4863 N  N   . TYR B 1 294 ? 22.052  8.945   24.218  1.00 15.09  ? 517  TYR B N   1 
ATOM   4864 C  CA  . TYR B 1 294 ? 20.654  9.346   24.110  1.00 13.99  ? 517  TYR B CA  1 
ATOM   4865 C  C   . TYR B 1 294 ? 20.503  10.804  24.515  1.00 13.65  ? 517  TYR B C   1 
ATOM   4866 O  O   . TYR B 1 294 ? 21.364  11.381  25.193  1.00 14.64  ? 517  TYR B O   1 
ATOM   4867 C  CB  . TYR B 1 294 ? 19.722  8.444   24.937  1.00 14.04  ? 517  TYR B CB  1 
ATOM   4868 C  CG  . TYR B 1 294 ? 20.050  8.340   26.415  1.00 14.71  ? 517  TYR B CG  1 
ATOM   4869 C  CD1 . TYR B 1 294 ? 19.501  9.227   27.336  1.00 16.50  ? 517  TYR B CD1 1 
ATOM   4870 C  CD2 . TYR B 1 294 ? 20.880  7.324   26.896  1.00 16.85  ? 517  TYR B CD2 1 
ATOM   4871 C  CE1 . TYR B 1 294 ? 19.798  9.126   28.696  1.00 19.67  ? 517  TYR B CE1 1 
ATOM   4872 C  CE2 . TYR B 1 294 ? 21.169  7.212   28.246  1.00 19.39  ? 517  TYR B CE2 1 
ATOM   4873 C  CZ  . TYR B 1 294 ? 20.628  8.112   29.138  1.00 20.21  ? 517  TYR B CZ  1 
ATOM   4874 O  OH  . TYR B 1 294 ? 20.927  7.996   30.482  1.00 24.48  ? 517  TYR B OH  1 
ATOM   4875 N  N   . PHE B 1 295 ? 19.388  11.390  24.096  1.00 13.17  ? 518  PHE B N   1 
ATOM   4876 C  CA  . PHE B 1 295 ? 19.069  12.773  24.434  1.00 13.27  ? 518  PHE B CA  1 
ATOM   4877 C  C   . PHE B 1 295 ? 18.548  12.878  25.864  1.00 14.18  ? 518  PHE B C   1 
ATOM   4878 O  O   . PHE B 1 295 ? 17.751  12.047  26.312  1.00 14.85  ? 518  PHE B O   1 
ATOM   4879 C  CB  . PHE B 1 295 ? 17.988  13.314  23.500  1.00 12.91  ? 518  PHE B CB  1 
ATOM   4880 C  CG  . PHE B 1 295 ? 18.509  13.809  22.188  1.00 12.76  ? 518  PHE B CG  1 
ATOM   4881 C  CD1 . PHE B 1 295 ? 19.342  14.917  22.122  1.00 13.38  ? 518  PHE B CD1 1 
ATOM   4882 C  CD2 . PHE B 1 295 ? 18.132  13.184  21.003  1.00 13.04  ? 518  PHE B CD2 1 
ATOM   4883 C  CE1 . PHE B 1 295 ? 19.795  15.383  20.893  1.00 14.35  ? 518  PHE B CE1 1 
ATOM   4884 C  CE2 . PHE B 1 295 ? 18.577  13.638  19.780  1.00 14.02  ? 518  PHE B CE2 1 
ATOM   4885 C  CZ  . PHE B 1 295 ? 19.409  14.736  19.718  1.00 13.77  ? 518  PHE B CZ  1 
ATOM   4886 N  N   . ARG B 1 296 ? 18.986  13.920  26.568  0.95 13.95  ? 519  ARG B N   1 
ATOM   4887 C  CA  . ARG B 1 296 ? 18.447  14.281  27.871  0.95 14.47  ? 519  ARG B CA  1 
ATOM   4888 C  C   . ARG B 1 296 ? 17.887  15.694  27.820  0.95 14.63  ? 519  ARG B C   1 
ATOM   4889 O  O   . ARG B 1 296 ? 18.502  16.591  27.238  0.95 15.54  ? 519  ARG B O   1 
ATOM   4890 C  CB  . ARG B 1 296 ? 19.532  14.238  28.953  0.95 16.40  ? 519  ARG B CB  1 
ATOM   4891 C  CG  . ARG B 1 296 ? 20.151  12.881  29.151  0.95 20.31  ? 519  ARG B CG  1 
ATOM   4892 C  CD  . ARG B 1 296 ? 21.113  12.901  30.326  0.95 23.87  ? 519  ARG B CD  1 
ATOM   4893 N  NE  . ARG B 1 296 ? 21.758  11.606  30.497  0.95 27.11  ? 519  ARG B NE  1 
ATOM   4894 C  CZ  . ARG B 1 296 ? 22.629  11.319  31.453  0.95 28.98  ? 519  ARG B CZ  1 
ATOM   4895 N  NH1 . ARG B 1 296 ? 22.960  12.207  32.375  0.95 31.33  ? 519  ARG B NH1 1 
ATOM   4896 N  NH2 . ARG B 1 296 ? 23.178  10.109  31.485  0.95 30.08  ? 519  ARG B NH2 1 
ATOM   4897 N  N   . PHE B 1 297 ? 16.727  15.888  28.440  1.00 15.24  ? 520  PHE B N   1 
ATOM   4898 C  CA  . PHE B 1 297 ? 16.157  17.225  28.566  1.00 15.63  ? 520  PHE B CA  1 
ATOM   4899 C  C   . PHE B 1 297 ? 16.958  18.043  29.570  1.00 16.12  ? 520  PHE B C   1 
ATOM   4900 O  O   . PHE B 1 297 ? 17.267  17.568  30.666  1.00 17.46  ? 520  PHE B O   1 
ATOM   4901 C  CB  . PHE B 1 297 ? 14.703  17.129  29.026  1.00 16.95  ? 520  PHE B CB  1 
ATOM   4902 C  CG  . PHE B 1 297 ? 14.096  18.455  29.411  1.00 18.84  ? 520  PHE B CG  1 
ATOM   4903 C  CD1 . PHE B 1 297 ? 13.717  19.377  28.446  1.00 18.99  ? 520  PHE B CD1 1 
ATOM   4904 C  CD2 . PHE B 1 297 ? 13.906  18.779  30.746  1.00 20.73  ? 520  PHE B CD2 1 
ATOM   4905 C  CE1 . PHE B 1 297 ? 13.152  20.591  28.810  1.00 19.80  ? 520  PHE B CE1 1 
ATOM   4906 C  CE2 . PHE B 1 297 ? 13.349  19.992  31.115  1.00 22.38  ? 520  PHE B CE2 1 
ATOM   4907 C  CZ  . PHE B 1 297 ? 12.973  20.897  30.147  1.00 20.77  ? 520  PHE B CZ  1 
ATOM   4908 N  N   . ASP B 1 298 ? 17.305  19.272  29.193  1.00 14.54  ? 521  ASP B N   1 
ATOM   4909 C  CA  . ASP B 1 298 ? 18.066  20.153  30.071  1.00 14.55  ? 521  ASP B CA  1 
ATOM   4910 C  C   . ASP B 1 298 ? 17.228  21.265  30.679  1.00 14.51  ? 521  ASP B C   1 
ATOM   4911 O  O   . ASP B 1 298 ? 17.309  21.501  31.890  1.00 16.55  ? 521  ASP B O   1 
ATOM   4912 C  CB  . ASP B 1 298 ? 19.242  20.781  29.320  1.00 15.04  ? 521  ASP B CB  1 
ATOM   4913 C  CG  . ASP B 1 298 ? 20.118  21.617  30.231  1.00 17.02  ? 521  ASP B CG  1 
ATOM   4914 O  OD1 . ASP B 1 298 ? 20.921  21.030  30.987  1.00 18.84  ? 521  ASP B OD1 1 
ATOM   4915 O  OD2 . ASP B 1 298 ? 19.996  22.860  30.227  1.00 17.92  ? 521  ASP B OD2 1 
ATOM   4916 N  N   . SER B 1 299 ? 16.427  21.955  29.872  1.00 15.54  ? 522  SER B N   1 
ATOM   4917 C  CA  . SER B 1 299 ? 15.745  23.174  30.286  1.00 16.33  ? 522  SER B CA  1 
ATOM   4918 C  C   . SER B 1 299 ? 14.895  23.651  29.112  1.00 16.98  ? 522  SER B C   1 
ATOM   4919 O  O   . SER B 1 299 ? 15.051  23.179  27.980  1.00 17.43  ? 522  SER B O   1 
ATOM   4920 C  CB  . SER B 1 299 ? 16.772  24.246  30.662  1.00 17.10  ? 522  SER B CB  1 
ATOM   4921 O  OG  . SER B 1 299 ? 17.685  24.466  29.593  1.00 18.08  ? 522  SER B OG  1 
ATOM   4922 N  N   . TRP B 1 300 ? 13.990  24.590  29.397  1.00 17.65  ? 523  TRP B N   1 
ATOM   4923 C  CA  . TRP B 1 300 ? 13.160  25.235  28.383  1.00 17.68  ? 523  TRP B CA  1 
ATOM   4924 C  C   . TRP B 1 300 ? 13.806  26.557  27.998  1.00 19.52  ? 523  TRP B C   1 
ATOM   4925 O  O   . TRP B 1 300 ? 14.194  27.342  28.873  1.00 21.32  ? 523  TRP B O   1 
ATOM   4926 C  CB  . TRP B 1 300 ? 11.753  25.491  28.917  1.00 19.68  ? 523  TRP B CB  1 
ATOM   4927 C  CG  . TRP B 1 300 ? 10.966  24.256  29.150  1.00 20.72  ? 523  TRP B CG  1 
ATOM   4928 C  CD1 . TRP B 1 300 ? 10.769  23.619  30.341  1.00 21.00  ? 523  TRP B CD1 1 
ATOM   4929 C  CD2 . TRP B 1 300 ? 10.267  23.491  28.160  1.00 20.80  ? 523  TRP B CD2 1 
ATOM   4930 N  NE1 . TRP B 1 300 ? 9.975   22.511  30.155  1.00 21.68  ? 523  TRP B NE1 1 
ATOM   4931 C  CE2 . TRP B 1 300 ? 9.664   22.402  28.822  1.00 21.12  ? 523  TRP B CE2 1 
ATOM   4932 C  CE3 . TRP B 1 300 ? 10.091  23.625  26.782  1.00 19.49  ? 523  TRP B CE3 1 
ATOM   4933 C  CZ2 . TRP B 1 300 ? 8.896   21.451  28.152  1.00 21.56  ? 523  TRP B CZ2 1 
ATOM   4934 C  CZ3 . TRP B 1 300 ? 9.325   22.677  26.112  1.00 21.94  ? 523  TRP B CZ3 1 
ATOM   4935 C  CH2 . TRP B 1 300 ? 8.739   21.603  26.800  1.00 22.01  ? 523  TRP B CH2 1 
ATOM   4936 N  N   . VAL B 1 301 ? 13.935  26.791  26.696  1.00 19.24  ? 524  VAL B N   1 
ATOM   4937 C  CA  . VAL B 1 301 ? 14.591  27.979  26.156  1.00 20.47  ? 524  VAL B CA  1 
ATOM   4938 C  C   . VAL B 1 301 ? 13.689  28.622  25.104  1.00 21.24  ? 524  VAL B C   1 
ATOM   4939 O  O   . VAL B 1 301 ? 12.542  28.205  24.918  1.00 22.05  ? 524  VAL B O   1 
ATOM   4940 C  CB  . VAL B 1 301 ? 15.991  27.640  25.605  1.00 18.74  ? 524  VAL B CB  1 
ATOM   4941 C  CG1 . VAL B 1 301 ? 16.874  27.050  26.714  1.00 18.95  ? 524  VAL B CG1 1 
ATOM   4942 C  CG2 . VAL B 1 301 ? 15.898  26.677  24.434  1.00 19.03  ? 524  VAL B CG2 1 
ATOM   4943 N  N   . SER B 1 302 ? 14.180  29.651  24.421  1.00 24.26  ? 525  SER B N   1 
ATOM   4944 C  CA  . SER B 1 302 ? 13.385  30.319  23.401  1.00 26.52  ? 525  SER B CA  1 
ATOM   4945 C  C   . SER B 1 302 ? 13.791  29.857  22.005  1.00 27.76  ? 525  SER B C   1 
ATOM   4946 O  O   . SER B 1 302 ? 14.809  29.189  21.806  1.00 28.09  ? 525  SER B O   1 
ATOM   4947 C  CB  . SER B 1 302 ? 13.537  31.838  23.497  1.00 28.60  ? 525  SER B CB  1 
ATOM   4948 O  OG  . SER B 1 302 ? 14.578  32.284  22.645  1.00 30.34  ? 525  SER B OG  1 
ATOM   4949 N  N   . GLN B 1 303 ? 12.981  30.254  21.019  1.00 30.66  ? 526  GLN B N   1 
ATOM   4950 C  CA  . GLN B 1 303 ? 13.313  29.953  19.630  1.00 32.16  ? 526  GLN B CA  1 
ATOM   4951 C  C   . GLN B 1 303 ? 14.635  30.579  19.210  1.00 32.44  ? 526  GLN B C   1 
ATOM   4952 O  O   . GLN B 1 303 ? 15.226  30.149  18.214  1.00 33.84  ? 526  GLN B O   1 
ATOM   4953 C  CB  . GLN B 1 303 ? 12.188  30.401  18.687  1.00 34.53  ? 526  GLN B CB  1 
ATOM   4954 C  CG  . GLN B 1 303 ? 11.964  31.911  18.649  1.00 37.27  ? 526  GLN B CG  1 
ATOM   4955 C  CD  . GLN B 1 303 ? 11.023  32.338  17.536  1.00 40.96  ? 526  GLN B CD  1 
ATOM   4956 O  OE1 . GLN B 1 303 ? 11.179  31.929  16.387  1.00 43.23  ? 526  GLN B OE1 1 
ATOM   4957 N  NE2 . GLN B 1 303 ? 10.040  33.164  17.874  1.00 41.07  ? 526  GLN B NE2 1 
ATOM   4958 N  N   . PHE B 1 304 ? 15.121  31.567  19.958  1.00 32.00  ? 527  PHE B N   1 
ATOM   4959 C  CA  . PHE B 1 304 ? 16.326  32.295  19.604  1.00 32.97  ? 527  PHE B CA  1 
ATOM   4960 C  C   . PHE B 1 304 ? 17.580  31.775  20.300  1.00 31.41  ? 527  PHE B C   1 
ATOM   4961 O  O   . PHE B 1 304 ? 18.661  32.322  20.070  1.00 33.70  ? 527  PHE B O   1 
ATOM   4962 C  CB  . PHE B 1 304 ? 16.138  33.786  19.896  1.00 34.02  ? 527  PHE B CB  1 
ATOM   4963 C  CG  . PHE B 1 304 ? 14.958  34.398  19.188  1.00 35.24  ? 527  PHE B CG  1 
ATOM   4964 C  CD1 . PHE B 1 304 ? 14.962  34.541  17.810  1.00 35.76  ? 527  PHE B CD1 1 
ATOM   4965 C  CD2 . PHE B 1 304 ? 13.849  34.827  19.899  1.00 35.87  ? 527  PHE B CD2 1 
ATOM   4966 C  CE1 . PHE B 1 304 ? 13.884  35.110  17.150  1.00 37.08  ? 527  PHE B CE1 1 
ATOM   4967 C  CE2 . PHE B 1 304 ? 12.764  35.398  19.245  1.00 36.29  ? 527  PHE B CE2 1 
ATOM   4968 C  CZ  . PHE B 1 304 ? 12.782  35.535  17.867  1.00 37.30  ? 527  PHE B CZ  1 
ATOM   4969 N  N   . TYR B 1 305 ? 17.470  30.739  21.132  1.00 29.22  ? 528  TYR B N   1 
ATOM   4970 C  CA  . TYR B 1 305 ? 18.648  30.171  21.783  1.00 26.85  ? 528  TYR B CA  1 
ATOM   4971 C  C   . TYR B 1 305 ? 19.663  29.740  20.732  1.00 24.93  ? 528  TYR B C   1 
ATOM   4972 O  O   . TYR B 1 305 ? 19.309  29.097  19.741  1.00 26.30  ? 528  TYR B O   1 
ATOM   4973 C  CB  . TYR B 1 305 ? 18.233  28.964  22.631  1.00 25.67  ? 528  TYR B CB  1 
ATOM   4974 C  CG  . TYR B 1 305 ? 19.359  28.389  23.461  1.00 24.42  ? 528  TYR B CG  1 
ATOM   4975 C  CD1 . TYR B 1 305 ? 20.196  27.403  22.951  1.00 23.89  ? 528  TYR B CD1 1 
ATOM   4976 C  CD2 . TYR B 1 305 ? 19.589  28.833  24.752  1.00 24.98  ? 528  TYR B CD2 1 
ATOM   4977 C  CE1 . TYR B 1 305 ? 21.224  26.874  23.697  1.00 24.53  ? 528  TYR B CE1 1 
ATOM   4978 C  CE2 . TYR B 1 305 ? 20.611  28.313  25.502  1.00 25.28  ? 528  TYR B CE2 1 
ATOM   4979 C  CZ  . TYR B 1 305 ? 21.428  27.335  24.975  1.00 25.68  ? 528  TYR B CZ  1 
ATOM   4980 O  OH  . TYR B 1 305 ? 22.453  26.825  25.737  1.00 29.83  ? 528  TYR B OH  1 
ATOM   4981 N  N   . SER B 1 306 ? 20.928  30.102  20.942  1.00 25.09  ? 529  SER B N   1 
ATOM   4982 C  CA  . SER B 1 306 ? 21.984  29.818  19.975  1.00 25.20  ? 529  SER B CA  1 
ATOM   4983 C  C   . SER B 1 306 ? 22.727  28.559  20.406  1.00 22.26  ? 529  SER B C   1 
ATOM   4984 O  O   . SER B 1 306 ? 23.458  28.567  21.400  1.00 24.10  ? 529  SER B O   1 
ATOM   4985 C  CB  . SER B 1 306 ? 22.940  30.998  19.831  1.00 29.30  ? 529  SER B CB  1 
ATOM   4986 O  OG  . SER B 1 306 ? 23.846  30.772  18.762  1.00 32.05  ? 529  SER B OG  1 
ATOM   4987 N  N   . LEU B 1 307 ? 22.540  27.483  19.655  1.00 19.98  ? 530  LEU B N   1 
ATOM   4988 C  CA  . LEU B 1 307 ? 23.158  26.212  19.994  1.00 18.25  ? 530  LEU B CA  1 
ATOM   4989 C  C   . LEU B 1 307 ? 24.638  26.223  19.647  1.00 18.45  ? 530  LEU B C   1 
ATOM   4990 O  O   . LEU B 1 307 ? 25.075  26.903  18.715  1.00 19.99  ? 530  LEU B O   1 
ATOM   4991 C  CB  . LEU B 1 307 ? 22.505  25.095  19.183  1.00 18.88  ? 530  LEU B CB  1 
ATOM   4992 C  CG  . LEU B 1 307 ? 21.021  24.797  19.408  1.00 17.82  ? 530  LEU B CG  1 
ATOM   4993 C  CD1 . LEU B 1 307 ? 20.465  23.955  18.272  1.00 18.09  ? 530  LEU B CD1 1 
ATOM   4994 C  CD2 . LEU B 1 307 ? 20.807  24.089  20.738  1.00 17.61  ? 530  LEU B CD2 1 
ATOM   4995 N  N   . ALA B 1 308 ? 25.407  25.439  20.390  1.00 19.92  ? 531  ALA B N   1 
ATOM   4996 C  CA  . ALA B 1 308 ? 26.799  25.238  20.034  1.00 22.41  ? 531  ALA B CA  1 
ATOM   4997 C  C   . ALA B 1 308 ? 26.867  24.518  18.688  1.00 27.75  ? 531  ALA B C   1 
ATOM   4998 O  O   . ALA B 1 308 ? 26.127  23.556  18.465  1.00 23.76  ? 531  ALA B O   1 
ATOM   4999 C  CB  . ALA B 1 308 ? 27.499  24.394  21.098  1.00 22.11  ? 531  ALA B CB  1 
ATOM   5000 N  N   A PRO B 1 309 ? 27.745  24.942  17.785  0.42 47.66  ? 532  PRO B N   1 
ATOM   5001 N  N   B PRO B 1 309 ? 27.720  24.969  17.771  0.58 21.54  ? 532  PRO B N   1 
ATOM   5002 C  CA  A PRO B 1 309 ? 27.786  24.330  16.452  0.42 65.04  ? 532  PRO B CA  1 
ATOM   5003 C  CA  B PRO B 1 309 ? 27.807  24.313  16.461  0.58 19.10  ? 532  PRO B CA  1 
ATOM   5004 C  C   A PRO B 1 309 ? 28.330  22.911  16.505  0.42 87.96  ? 532  PRO B C   1 
ATOM   5005 C  C   B PRO B 1 309 ? 28.289  22.878  16.587  0.58 19.51  ? 532  PRO B C   1 
ATOM   5006 O  O   A PRO B 1 309 ? 28.812  22.424  17.530  0.42 87.55  ? 532  PRO B O   1 
ATOM   5007 O  O   B PRO B 1 309 ? 29.088  22.538  17.464  0.58 21.03  ? 532  PRO B O   1 
ATOM   5008 C  CB  A PRO B 1 309 ? 28.733  25.250  15.680  0.42 59.98  ? 532  PRO B CB  1 
ATOM   5009 C  CB  B PRO B 1 309 ? 28.826  25.171  15.700  0.58 21.36  ? 532  PRO B CB  1 
ATOM   5010 C  CG  A PRO B 1 309 ? 29.645  25.792  16.730  0.42 55.12  ? 532  PRO B CG  1 
ATOM   5011 C  CG  B PRO B 1 309 ? 28.863  26.472  16.439  0.58 22.89  ? 532  PRO B CG  1 
ATOM   5012 C  CD  A PRO B 1 309 ? 28.788  25.967  17.957  0.42 51.16  ? 532  PRO B CD  1 
ATOM   5013 C  CD  B PRO B 1 309 ? 28.600  26.145  17.867  0.58 22.12  ? 532  PRO B CD  1 
ATOM   5014 N  N   A MET B 1 310 ? 28.239  22.242  15.360  0.42 111.44 ? 533  MET B N   1 
ATOM   5015 N  N   B MET B 1 310 ? 27.792  22.033  15.690  0.58 17.80  ? 533  MET B N   1 
ATOM   5016 C  CA  A MET B 1 310 ? 28.761  20.891  15.204  0.42 26.72  ? 533  MET B CA  1 
ATOM   5017 C  CA  B MET B 1 310 ? 28.171  20.626  15.675  0.58 34.26  ? 533  MET B CA  1 
ATOM   5018 C  C   A MET B 1 310 ? 29.738  20.858  14.035  0.42 51.76  ? 533  MET B C   1 
ATOM   5019 C  C   B MET B 1 310 ? 29.423  20.427  14.833  0.58 30.72  ? 533  MET B C   1 
ATOM   5020 O  O   A MET B 1 310 ? 29.693  21.720  13.156  0.42 25.23  ? 533  MET B O   1 
ATOM   5021 O  O   B MET B 1 310 ? 29.540  20.983  13.741  0.58 60.97  ? 533  MET B O   1 
ATOM   5022 C  CB  A MET B 1 310 ? 27.618  19.899  14.967  0.42 26.60  ? 533  MET B CB  1 
ATOM   5023 C  CB  B MET B 1 310 ? 27.031  19.774  15.125  0.58 31.64  ? 533  MET B CB  1 
ATOM   5024 C  CG  A MET B 1 310 ? 26.592  19.844  16.098  0.42 11.02  ? 533  MET B CG  1 
ATOM   5025 C  CG  B MET B 1 310 ? 25.687  20.121  15.718  0.58 42.26  ? 533  MET B CG  1 
ATOM   5026 S  SD  A MET B 1 310 ? 25.091  18.918  15.693  0.42 20.97  ? 533  MET B SD  1 
ATOM   5027 S  SD  B MET B 1 310 ? 24.645  18.679  15.970  0.58 34.76  ? 533  MET B SD  1 
ATOM   5028 C  CE  A MET B 1 310 ? 25.753  17.277  15.419  0.42 15.22  ? 533  MET B CE  1 
ATOM   5029 C  CE  B MET B 1 310 ? 24.467  18.060  14.300  0.58 16.98  ? 533  MET B CE  1 
HETATM 5030 CL CL  . CL  C 2 .   ? 17.849  -28.221 6.918   1.00 25.60  ? 601  CL  A CL  1 
HETATM 5031 O  O   . HOH D 3 .   ? -12.460 7.061   33.409  1.00 55.14  ? 701  HOH A O   1 
HETATM 5032 O  O   B HOH D 3 .   ? 26.771  2.912   -3.719  1.00 35.39  ? 702  HOH A O   1 
HETATM 5033 O  O   . HOH D 3 .   ? -14.440 -17.283 37.628  1.00 45.35  ? 703  HOH A O   1 
HETATM 5034 O  O   . HOH D 3 .   ? -3.218  -25.936 8.214   1.00 8.39   ? 704  HOH A O   1 
HETATM 5035 O  O   . HOH D 3 .   ? 10.274  6.404   31.438  1.00 57.11  ? 705  HOH A O   1 
HETATM 5036 O  O   . HOH D 3 .   ? 20.174  -15.149 28.476  1.00 44.67  ? 706  HOH A O   1 
HETATM 5037 O  O   . HOH D 3 .   ? 9.694   -8.004  12.836  1.00 58.91  ? 707  HOH A O   1 
HETATM 5038 O  O   . HOH D 3 .   ? -9.883  -8.398  45.601  1.00 35.17  ? 708  HOH A O   1 
HETATM 5039 O  O   . HOH D 3 .   ? 17.287  -13.335 34.851  1.00 48.90  ? 709  HOH A O   1 
HETATM 5040 O  O   C HOH D 3 .   ? 27.413  5.730   -5.173  1.00 48.50  ? 710  HOH A O   1 
HETATM 5041 O  O   . HOH D 3 .   ? 18.495  5.637   -6.077  1.00 59.28  ? 711  HOH A O   1 
HETATM 5042 O  O   . HOH D 3 .   ? 12.727  -4.798  41.958  1.00 38.22  ? 712  HOH A O   1 
HETATM 5043 O  O   . HOH D 3 .   ? -13.833 7.796   28.841  1.00 46.16  ? 713  HOH A O   1 
HETATM 5044 O  O   . HOH D 3 .   ? 29.263  -1.834  1.374   1.00 37.98  ? 714  HOH A O   1 
HETATM 5045 O  O   A HOH D 3 .   ? 27.353  -18.133 -3.902  1.00 47.13  ? 715  HOH A O   1 
HETATM 5046 O  O   . HOH D 3 .   ? -5.362  -18.967 26.582  1.00 102.85 ? 716  HOH A O   1 
HETATM 5047 O  O   . HOH D 3 .   ? 8.094   0.785   43.446  1.00 38.58  ? 717  HOH A O   1 
HETATM 5048 O  O   . HOH D 3 .   ? 8.492   -2.736  39.468  1.00 30.28  ? 718  HOH A O   1 
HETATM 5049 O  O   . HOH D 3 .   ? 2.178   -18.232 41.748  1.00 37.36  ? 719  HOH A O   1 
HETATM 5050 O  O   . HOH D 3 .   ? -11.868 -6.048  41.712  1.00 42.85  ? 720  HOH A O   1 
HETATM 5051 O  O   . HOH D 3 .   ? -0.083  -28.201 4.849   1.00 34.88  ? 721  HOH A O   1 
HETATM 5052 O  O   . HOH D 3 .   ? 29.396  -7.978  18.499  1.00 38.42  ? 722  HOH A O   1 
HETATM 5053 O  O   . HOH D 3 .   ? -4.985  -25.303 26.851  1.00 48.59  ? 723  HOH A O   1 
HETATM 5054 O  O   . HOH D 3 .   ? 4.559   -2.265  49.283  1.00 50.17  ? 724  HOH A O   1 
HETATM 5055 O  O   . HOH D 3 .   ? -16.335 5.497   24.525  1.00 55.39  ? 725  HOH A O   1 
HETATM 5056 O  O   . HOH D 3 .   ? -3.787  -22.449 39.509  1.00 36.05  ? 726  HOH A O   1 
HETATM 5057 O  O   . HOH D 3 .   ? 14.833  -15.338 -11.571 1.00 53.88  ? 727  HOH A O   1 
HETATM 5058 O  O   . HOH D 3 .   ? 22.073  6.744   -4.742  1.00 55.02  ? 728  HOH A O   1 
HETATM 5059 O  O   . HOH D 3 .   ? -7.540  -24.189 34.910  1.00 37.50  ? 729  HOH A O   1 
HETATM 5060 O  O   . HOH D 3 .   ? 30.757  -13.502 16.299  1.00 50.19  ? 730  HOH A O   1 
HETATM 5061 O  O   . HOH D 3 .   ? 26.277  -1.667  1.798   1.00 45.40  ? 731  HOH A O   1 
HETATM 5062 O  O   . HOH D 3 .   ? -1.180  -18.378 40.455  1.00 30.05  ? 732  HOH A O   1 
HETATM 5063 O  O   . HOH D 3 .   ? -0.078  -25.201 2.729   1.00 31.99  ? 733  HOH A O   1 
HETATM 5064 O  O   . HOH D 3 .   ? 21.659  -10.623 19.574  1.00 19.94  ? 734  HOH A O   1 
HETATM 5065 O  O   . HOH D 3 .   ? 10.458  -13.891 33.688  1.00 30.62  ? 735  HOH A O   1 
HETATM 5066 O  O   . HOH D 3 .   ? 15.658  -9.270  -9.132  1.00 39.01  ? 736  HOH A O   1 
HETATM 5067 O  O   . HOH D 3 .   ? 7.896   4.589   29.989  1.00 35.43  ? 737  HOH A O   1 
HETATM 5068 O  O   . HOH D 3 .   ? 25.673  -20.361 28.489  1.00 42.91  ? 738  HOH A O   1 
HETATM 5069 O  O   . HOH D 3 .   ? 32.410  -16.289 20.179  1.00 57.63  ? 739  HOH A O   1 
HETATM 5070 O  O   . HOH D 3 .   ? 3.595   -31.566 20.020  1.00 47.66  ? 740  HOH A O   1 
HETATM 5071 O  O   . HOH D 3 .   ? 6.788   3.773   36.990  1.00 43.57  ? 741  HOH A O   1 
HETATM 5072 O  O   . HOH D 3 .   ? 10.618  -7.035  38.973  1.00 33.20  ? 742  HOH A O   1 
HETATM 5073 O  O   . HOH D 3 .   ? 12.994  -7.775  4.155   1.00 16.01  ? 743  HOH A O   1 
HETATM 5074 O  O   . HOH D 3 .   ? 20.542  -18.222 32.087  1.00 25.27  ? 744  HOH A O   1 
HETATM 5075 O  O   . HOH D 3 .   ? 27.720  -12.894 1.899   1.00 24.62  ? 745  HOH A O   1 
HETATM 5076 O  O   . HOH D 3 .   ? 17.382  -2.037  3.733   1.00 28.45  ? 746  HOH A O   1 
HETATM 5077 O  O   . HOH D 3 .   ? 26.275  -21.995 11.479  1.00 53.62  ? 747  HOH A O   1 
HETATM 5078 O  O   . HOH D 3 .   ? 26.533  5.257   -14.096 1.00 55.11  ? 748  HOH A O   1 
HETATM 5079 O  O   . HOH D 3 .   ? 30.235  -8.579  -2.221  1.00 38.26  ? 749  HOH A O   1 
HETATM 5080 O  O   . HOH D 3 .   ? 25.443  -3.447  -6.723  1.00 25.58  ? 750  HOH A O   1 
HETATM 5081 O  O   . HOH D 3 .   ? -11.237 -20.334 38.984  1.00 40.88  ? 751  HOH A O   1 
HETATM 5082 O  O   . HOH D 3 .   ? 26.561  -10.522 -5.855  1.00 30.31  ? 752  HOH A O   1 
HETATM 5083 O  O   . HOH D 3 .   ? 14.676  -8.266  37.821  1.00 31.23  ? 753  HOH A O   1 
HETATM 5084 O  O   . HOH D 3 .   ? 0.152   4.924   33.434  1.00 36.88  ? 754  HOH A O   1 
HETATM 5085 O  O   . HOH D 3 .   ? -8.716  -2.481  25.334  1.00 25.23  ? 755  HOH A O   1 
HETATM 5086 O  O   . HOH D 3 .   ? 9.154   -31.275 17.071  1.00 38.35  ? 756  HOH A O   1 
HETATM 5087 O  O   . HOH D 3 .   ? 20.179  -25.597 29.490  1.00 50.63  ? 757  HOH A O   1 
HETATM 5088 O  O   . HOH D 3 .   ? 18.751  -8.386  30.822  1.00 43.92  ? 758  HOH A O   1 
HETATM 5089 O  O   . HOH D 3 .   ? -7.573  5.629   23.017  1.00 40.29  ? 759  HOH A O   1 
HETATM 5090 O  O   . HOH D 3 .   ? -11.703 -15.070 17.632  1.00 43.99  ? 760  HOH A O   1 
HETATM 5091 O  O   . HOH D 3 .   ? -7.585  -20.610 15.762  1.00 28.72  ? 761  HOH A O   1 
HETATM 5092 O  O   . HOH D 3 .   ? 24.598  -31.902 20.178  1.00 69.06  ? 762  HOH A O   1 
HETATM 5093 O  O   . HOH D 3 .   ? 11.763  -28.073 8.206   1.00 27.36  ? 763  HOH A O   1 
HETATM 5094 O  O   . HOH D 3 .   ? 1.523   1.773   21.382  1.00 23.33  ? 764  HOH A O   1 
HETATM 5095 O  O   . HOH D 3 .   ? -10.167 -4.471  25.733  1.00 35.57  ? 765  HOH A O   1 
HETATM 5096 O  O   . HOH D 3 .   ? 22.120  -23.893 22.641  1.00 30.30  ? 766  HOH A O   1 
HETATM 5097 O  O   . HOH D 3 .   ? -3.240  -10.918 11.818  1.00 50.08  ? 767  HOH A O   1 
HETATM 5098 O  O   . HOH D 3 .   ? 16.758  -5.005  18.171  1.00 16.56  ? 768  HOH A O   1 
HETATM 5099 O  O   . HOH D 3 .   ? 10.351  -1.001  36.007  1.00 27.31  ? 769  HOH A O   1 
HETATM 5100 O  O   . HOH D 3 .   ? 4.752   -23.855 32.139  1.00 24.56  ? 770  HOH A O   1 
HETATM 5101 O  O   B HOH D 3 .   ? -10.495 -14.978 22.735  0.81 31.63  ? 771  HOH A O   1 
HETATM 5102 O  O   . HOH D 3 .   ? 2.824   -28.107 22.504  1.00 29.28  ? 772  HOH A O   1 
HETATM 5103 O  O   . HOH D 3 .   ? 13.202  -15.642 -9.525  1.00 41.88  ? 773  HOH A O   1 
HETATM 5104 O  O   . HOH D 3 .   ? 20.507  -12.320 -8.772  1.00 31.88  ? 774  HOH A O   1 
HETATM 5105 O  O   . HOH D 3 .   ? -17.323 -7.901  35.002  1.00 49.84  ? 775  HOH A O   1 
HETATM 5106 O  O   . HOH D 3 .   ? 13.525  -16.917 20.800  1.00 12.84  ? 776  HOH A O   1 
HETATM 5107 O  O   . HOH D 3 .   ? -5.229  -2.325  16.385  1.00 32.48  ? 777  HOH A O   1 
HETATM 5108 O  O   . HOH D 3 .   ? 5.261   -10.825 48.454  1.00 41.95  ? 778  HOH A O   1 
HETATM 5109 O  O   . HOH D 3 .   ? 7.391   -0.603  22.384  1.00 25.50  ? 779  HOH A O   1 
HETATM 5110 O  O   . HOH D 3 .   ? 24.147  -3.236  1.704   1.00 29.32  ? 780  HOH A O   1 
HETATM 5111 O  O   . HOH D 3 .   ? 30.642  -0.225  -1.573  1.00 41.91  ? 781  HOH A O   1 
HETATM 5112 O  O   . HOH D 3 .   ? 4.168   -13.885 47.825  1.00 38.82  ? 782  HOH A O   1 
HETATM 5113 O  O   . HOH D 3 .   ? -18.965 -0.538  32.306  1.00 46.11  ? 783  HOH A O   1 
HETATM 5114 O  O   . HOH D 3 .   ? 10.835  -16.798 -3.414  1.00 17.62  ? 784  HOH A O   1 
HETATM 5115 O  O   . HOH D 3 .   ? 28.125  -1.871  -14.025 1.00 56.46  ? 785  HOH A O   1 
HETATM 5116 O  O   . HOH D 3 .   ? 28.626  -13.642 4.502   1.00 40.76  ? 786  HOH A O   1 
HETATM 5117 O  O   . HOH D 3 .   ? -6.761  5.318   34.654  1.00 42.99  ? 787  HOH A O   1 
HETATM 5118 O  O   . HOH D 3 .   ? -1.038  -25.633 15.306  1.00 44.68  ? 788  HOH A O   1 
HETATM 5119 O  O   . HOH D 3 .   ? 0.631   -13.227 31.075  1.00 14.38  ? 789  HOH A O   1 
HETATM 5120 O  O   . HOH D 3 .   ? 14.834  -26.654 15.952  1.00 19.83  ? 790  HOH A O   1 
HETATM 5121 O  O   . HOH D 3 .   ? 19.593  -26.088 20.884  1.00 25.31  ? 791  HOH A O   1 
HETATM 5122 O  O   . HOH D 3 .   ? 8.546   -15.093 18.867  1.00 13.00  ? 792  HOH A O   1 
HETATM 5123 O  O   . HOH D 3 .   ? -4.344  1.386   17.346  1.00 18.83  ? 793  HOH A O   1 
HETATM 5124 O  O   . HOH D 3 .   ? -3.883  -7.625  14.994  1.00 23.47  ? 794  HOH A O   1 
HETATM 5125 O  O   . HOH D 3 .   ? 4.091   -23.426 10.901  1.00 16.04  ? 795  HOH A O   1 
HETATM 5126 O  O   . HOH D 3 .   ? 22.237  -22.752 8.725   1.00 24.03  ? 796  HOH A O   1 
HETATM 5127 O  O   . HOH D 3 .   ? -20.333 5.052   36.236  1.00 45.94  ? 797  HOH A O   1 
HETATM 5128 O  O   . HOH D 3 .   ? 6.490   -7.307  9.688   1.00 13.15  ? 798  HOH A O   1 
HETATM 5129 O  O   . HOH D 3 .   ? 1.948   -18.056 39.105  1.00 29.43  ? 799  HOH A O   1 
HETATM 5130 O  O   . HOH D 3 .   ? 20.856  -29.856 13.603  1.00 37.06  ? 800  HOH A O   1 
HETATM 5131 O  O   A HOH D 3 .   ? 23.908  -16.972 -5.388  0.43 24.82  ? 801  HOH A O   1 
HETATM 5132 O  O   B HOH D 3 .   ? 24.080  -17.095 -3.481  0.57 27.85  ? 801  HOH A O   1 
HETATM 5133 O  O   . HOH D 3 .   ? 31.149  -19.286 3.071   1.00 75.07  ? 802  HOH A O   1 
HETATM 5134 O  O   . HOH D 3 .   ? -4.740  5.288   25.176  1.00 22.42  ? 803  HOH A O   1 
HETATM 5135 O  O   . HOH D 3 .   ? 4.382   -2.268  16.750  1.00 14.32  ? 804  HOH A O   1 
HETATM 5136 O  O   . HOH D 3 .   ? -2.267  -20.721 24.669  1.00 28.18  ? 805  HOH A O   1 
HETATM 5137 O  O   . HOH D 3 .   ? 3.048   -22.254 0.783   1.00 25.43  ? 806  HOH A O   1 
HETATM 5138 O  O   . HOH D 3 .   ? -7.117  -5.057  18.082  1.00 32.95  ? 807  HOH A O   1 
HETATM 5139 O  O   . HOH D 3 .   ? 33.663  -14.628 23.799  1.00 53.59  ? 808  HOH A O   1 
HETATM 5140 O  O   . HOH D 3 .   ? 9.667   -9.077  22.517  1.00 12.26  ? 809  HOH A O   1 
HETATM 5141 O  O   . HOH D 3 .   ? 4.620   -13.929 41.750  1.00 31.34  ? 810  HOH A O   1 
HETATM 5142 O  O   . HOH D 3 .   ? -10.526 -9.682  24.754  1.00 27.15  ? 811  HOH A O   1 
HETATM 5143 O  O   . HOH D 3 .   ? 2.392   -25.295 32.433  1.00 30.49  ? 812  HOH A O   1 
HETATM 5144 O  O   . HOH D 3 .   ? 26.916  -15.598 11.609  1.00 35.29  ? 813  HOH A O   1 
HETATM 5145 O  O   . HOH D 3 .   ? 11.832  -30.396 20.614  1.00 31.35  ? 814  HOH A O   1 
HETATM 5146 O  O   . HOH D 3 .   ? -12.196 -10.384 38.845  1.00 33.35  ? 815  HOH A O   1 
HETATM 5147 O  O   . HOH D 3 .   ? 6.043   -30.903 17.912  1.00 50.23  ? 816  HOH A O   1 
HETATM 5148 O  O   . HOH D 3 .   ? 22.258  -15.958 32.915  1.00 46.72  ? 817  HOH A O   1 
HETATM 5149 O  O   . HOH D 3 .   ? -15.855 -7.078  23.582  1.00 67.69  ? 818  HOH A O   1 
HETATM 5150 O  O   . HOH D 3 .   ? 4.834   -27.043 25.471  1.00 27.84  ? 819  HOH A O   1 
HETATM 5151 O  O   . HOH D 3 .   ? 14.057  -3.139  11.819  1.00 19.01  ? 820  HOH A O   1 
HETATM 5152 O  O   . HOH D 3 .   ? 12.040  -25.906 31.188  1.00 36.29  ? 821  HOH A O   1 
HETATM 5153 O  O   . HOH D 3 .   ? -14.273 -5.457  22.571  1.00 54.71  ? 822  HOH A O   1 
HETATM 5154 O  O   . HOH D 3 .   ? 15.832  -9.093  15.600  1.00 16.74  ? 823  HOH A O   1 
HETATM 5155 O  O   . HOH D 3 .   ? 18.624  -12.238 27.655  1.00 38.50  ? 824  HOH A O   1 
HETATM 5156 O  O   . HOH D 3 .   ? 13.005  -28.189 19.811  1.00 30.38  ? 825  HOH A O   1 
HETATM 5157 O  O   . HOH D 3 .   ? -15.814 -20.453 34.962  1.00 58.10  ? 826  HOH A O   1 
HETATM 5158 O  O   . HOH D 3 .   ? 15.904  -1.698  32.914  1.00 27.56  ? 827  HOH A O   1 
HETATM 5159 O  O   . HOH D 3 .   ? 24.324  2.546   0.733   1.00 34.62  ? 828  HOH A O   1 
HETATM 5160 O  O   . HOH D 3 .   ? -5.549  -10.186 13.372  1.00 25.52  ? 829  HOH A O   1 
HETATM 5161 O  O   . HOH D 3 .   ? 3.114   -29.209 31.284  1.00 66.62  ? 830  HOH A O   1 
HETATM 5162 O  O   . HOH D 3 .   ? -14.108 5.201   25.501  1.00 42.84  ? 831  HOH A O   1 
HETATM 5163 O  O   . HOH D 3 .   ? 27.154  -12.798 13.765  1.00 37.93  ? 832  HOH A O   1 
HETATM 5164 O  O   . HOH D 3 .   ? 21.806  -27.006 -4.151  1.00 48.83  ? 833  HOH A O   1 
HETATM 5165 O  O   . HOH D 3 .   ? -7.782  -22.642 19.655  1.00 60.58  ? 834  HOH A O   1 
HETATM 5166 O  O   . HOH D 3 .   ? 17.297  -15.074 29.910  1.00 22.33  ? 835  HOH A O   1 
HETATM 5167 O  O   . HOH D 3 .   ? 23.109  -7.109  6.910   1.00 37.17  ? 836  HOH A O   1 
HETATM 5168 O  O   . HOH D 3 .   ? 1.211   -29.836 24.443  1.00 65.47  ? 837  HOH A O   1 
HETATM 5169 O  O   . HOH D 3 .   ? -2.127  -1.004  28.816  1.00 17.63  ? 838  HOH A O   1 
HETATM 5170 O  O   . HOH D 3 .   ? -2.890  2.119   33.899  1.00 24.13  ? 839  HOH A O   1 
HETATM 5171 O  O   . HOH D 3 .   ? 16.940  -28.174 22.834  1.00 60.17  ? 840  HOH A O   1 
HETATM 5172 O  O   . HOH D 3 .   ? -3.397  -24.676 33.768  1.00 37.75  ? 841  HOH A O   1 
HETATM 5173 O  O   . HOH D 3 .   ? 3.699   -13.631 -4.304  1.00 21.66  ? 842  HOH A O   1 
HETATM 5174 O  O   . HOH D 3 .   ? 9.278   -1.014  19.864  1.00 19.38  ? 843  HOH A O   1 
HETATM 5175 O  O   . HOH D 3 .   ? 16.880  -4.128  -0.551  1.00 14.83  ? 844  HOH A O   1 
HETATM 5176 O  O   . HOH D 3 .   ? 18.565  -9.298  -8.851  1.00 23.33  ? 845  HOH A O   1 
HETATM 5177 O  O   . HOH D 3 .   ? 2.210   -9.393  9.212   1.00 13.39  ? 846  HOH A O   1 
HETATM 5178 O  O   . HOH D 3 .   ? -4.910  -23.623 35.876  1.00 38.58  ? 847  HOH A O   1 
HETATM 5179 O  O   . HOH D 3 .   ? 11.163  -25.343 27.112  1.00 34.46  ? 848  HOH A O   1 
HETATM 5180 O  O   . HOH D 3 .   ? 3.137   -34.168 11.946  1.00 43.02  ? 849  HOH A O   1 
HETATM 5181 O  O   . HOH D 3 .   ? 17.622  -28.500 -6.105  1.00 36.92  ? 850  HOH A O   1 
HETATM 5182 O  O   . HOH D 3 .   ? 20.956  -25.457 -0.235  1.00 32.78  ? 851  HOH A O   1 
HETATM 5183 O  O   . HOH D 3 .   ? -0.308  -19.418 -1.497  1.00 30.66  ? 852  HOH A O   1 
HETATM 5184 O  O   . HOH D 3 .   ? 21.496  -21.100 -7.413  1.00 30.71  ? 853  HOH A O   1 
HETATM 5185 O  O   . HOH D 3 .   ? -9.397  4.127   26.602  1.00 32.44  ? 854  HOH A O   1 
HETATM 5186 O  O   . HOH D 3 .   ? -5.496  -2.583  27.304  1.00 21.98  ? 855  HOH A O   1 
HETATM 5187 O  O   . HOH D 3 .   ? 16.040  -22.712 9.219   1.00 14.23  ? 856  HOH A O   1 
HETATM 5188 O  O   . HOH D 3 .   ? 16.385  -2.954  35.858  1.00 47.37  ? 857  HOH A O   1 
HETATM 5189 O  O   . HOH D 3 .   ? 26.270  -11.529 8.026   1.00 25.18  ? 858  HOH A O   1 
HETATM 5190 O  O   . HOH D 3 .   ? 10.942  -5.983  10.138  1.00 30.09  ? 859  HOH A O   1 
HETATM 5191 O  O   . HOH D 3 .   ? 10.979  -27.572 22.819  1.00 41.38  ? 860  HOH A O   1 
HETATM 5192 O  O   A HOH D 3 .   ? -6.882  -22.823 13.019  1.00 29.29  ? 861  HOH A O   1 
HETATM 5193 O  O   . HOH D 3 .   ? -8.467  -18.120 42.350  1.00 51.82  ? 862  HOH A O   1 
HETATM 5194 O  O   . HOH D 3 .   ? 1.069   -22.746 2.395   1.00 23.28  ? 863  HOH A O   1 
HETATM 5195 O  O   . HOH D 3 .   ? 7.367   -14.050 41.972  1.00 46.56  ? 864  HOH A O   1 
HETATM 5196 O  O   . HOH D 3 .   ? 20.742  -1.236  -15.063 1.00 52.01  ? 865  HOH A O   1 
HETATM 5197 O  O   . HOH D 3 .   ? -11.487 -12.746 23.987  1.00 41.37  ? 866  HOH A O   1 
HETATM 5198 O  O   . HOH D 3 .   ? 3.943   -7.667  10.627  1.00 19.89  ? 867  HOH A O   1 
HETATM 5199 O  O   . HOH D 3 .   ? 27.367  -18.833 9.175   1.00 29.36  ? 868  HOH A O   1 
HETATM 5200 O  O   . HOH D 3 .   ? 17.811  -3.276  13.908  1.00 19.97  ? 869  HOH A O   1 
HETATM 5201 O  O   . HOH D 3 .   ? -7.034  -16.002 43.119  1.00 31.70  ? 870  HOH A O   1 
HETATM 5202 O  O   . HOH D 3 .   ? 19.381  -10.782 13.392  1.00 19.55  ? 871  HOH A O   1 
HETATM 5203 O  O   . HOH D 3 .   ? -8.872  -2.001  21.705  1.00 25.26  ? 872  HOH A O   1 
HETATM 5204 O  O   . HOH D 3 .   ? -16.172 -1.843  23.131  1.00 58.29  ? 873  HOH A O   1 
HETATM 5205 O  O   . HOH D 3 .   ? 26.496  -6.181  9.635   1.00 43.31  ? 874  HOH A O   1 
HETATM 5206 O  O   . HOH D 3 .   ? -3.945  -2.816  29.731  1.00 18.02  ? 875  HOH A O   1 
HETATM 5207 O  O   . HOH D 3 .   ? 2.732   -26.243 8.087   1.00 40.93  ? 876  HOH A O   1 
HETATM 5208 O  O   . HOH D 3 .   ? -5.159  -17.249 50.529  1.00 50.24  ? 877  HOH A O   1 
HETATM 5209 O  O   . HOH D 3 .   ? -3.122  -21.328 32.601  1.00 23.68  ? 878  HOH A O   1 
HETATM 5210 O  O   . HOH D 3 .   ? 32.641  -3.273  -8.097  1.00 55.96  ? 879  HOH A O   1 
HETATM 5211 O  O   . HOH D 3 .   ? 6.362   -29.018 15.329  1.00 40.80  ? 880  HOH A O   1 
HETATM 5212 O  O   . HOH D 3 .   ? 17.123  -26.950 14.580  1.00 19.26  ? 881  HOH A O   1 
HETATM 5213 O  O   . HOH D 3 .   ? 7.453   -20.866 23.282  1.00 17.31  ? 882  HOH A O   1 
HETATM 5214 O  O   . HOH D 3 .   ? 3.488   1.196   47.324  1.00 48.46  ? 883  HOH A O   1 
HETATM 5215 O  O   . HOH D 3 .   ? 18.371  -11.475 31.725  1.00 41.00  ? 884  HOH A O   1 
HETATM 5216 O  O   . HOH D 3 .   ? -8.380  0.993   20.384  1.00 47.75  ? 885  HOH A O   1 
HETATM 5217 O  O   . HOH D 3 .   ? -9.664  -12.827 38.354  1.00 27.26  ? 886  HOH A O   1 
HETATM 5218 O  O   . HOH D 3 .   ? 3.869   -17.464 -4.576  1.00 32.97  ? 887  HOH A O   1 
HETATM 5219 O  O   . HOH D 3 .   ? -1.760  -10.451 49.515  1.00 35.37  ? 888  HOH A O   1 
HETATM 5220 O  O   . HOH D 3 .   ? 25.730  -23.849 21.128  1.00 30.11  ? 889  HOH A O   1 
HETATM 5221 O  O   . HOH D 3 .   ? 6.248   1.030   35.911  1.00 32.44  ? 890  HOH A O   1 
HETATM 5222 O  O   . HOH D 3 .   ? -5.011  5.657   19.252  1.00 39.34  ? 891  HOH A O   1 
HETATM 5223 O  O   . HOH D 3 .   ? 27.558  -19.728 11.491  1.00 45.15  ? 892  HOH A O   1 
HETATM 5224 O  O   . HOH D 3 .   ? 23.814  -28.343 15.075  1.00 37.14  ? 893  HOH A O   1 
HETATM 5225 O  O   . HOH D 3 .   ? 13.578  -22.971 6.030   1.00 21.92  ? 894  HOH A O   1 
HETATM 5226 O  O   . HOH D 3 .   ? 4.987   1.195   43.411  1.00 32.53  ? 895  HOH A O   1 
HETATM 5227 O  O   . HOH D 3 .   ? 20.396  -21.882 23.174  1.00 19.52  ? 896  HOH A O   1 
HETATM 5228 O  O   . HOH D 3 .   ? 5.435   -19.278 37.193  1.00 24.98  ? 897  HOH A O   1 
HETATM 5229 O  O   . HOH D 3 .   ? 5.801   -13.203 26.120  1.00 13.23  ? 898  HOH A O   1 
HETATM 5230 O  O   B HOH D 3 .   ? 20.203  -4.061  7.685   1.00 55.87  ? 899  HOH A O   1 
HETATM 5231 O  O   . HOH D 3 .   ? 29.413  -6.940  4.261   1.00 46.52  ? 900  HOH A O   1 
HETATM 5232 O  O   . HOH D 3 .   ? 31.479  -0.406  -6.468  1.00 44.26  ? 901  HOH A O   1 
HETATM 5233 O  O   . HOH D 3 .   ? -3.485  -26.323 5.829   1.00 20.56  ? 902  HOH A O   1 
HETATM 5234 O  O   . HOH D 3 .   ? -3.338  -27.639 28.812  1.00 42.29  ? 903  HOH A O   1 
HETATM 5235 O  O   . HOH D 3 .   ? -2.316  -30.268 11.843  1.00 46.24  ? 904  HOH A O   1 
HETATM 5236 O  O   . HOH D 3 .   ? 26.573  -13.559 -5.120  1.00 30.62  ? 905  HOH A O   1 
HETATM 5237 O  O   . HOH D 3 .   ? -6.501  -21.341 23.536  1.00 41.79  ? 906  HOH A O   1 
HETATM 5238 O  O   . HOH D 3 .   ? 6.819   -27.450 10.736  1.00 28.77  ? 907  HOH A O   1 
HETATM 5239 O  O   . HOH D 3 .   ? 3.934   -28.780 8.212   1.00 33.56  ? 908  HOH A O   1 
HETATM 5240 O  O   A HOH D 3 .   ? 8.132   -12.043 31.295  0.78 16.99  ? 909  HOH A O   1 
HETATM 5241 O  O   B HOH D 3 .   ? 7.245   -10.991 30.338  0.22 11.09  ? 909  HOH A O   1 
HETATM 5242 O  O   . HOH D 3 .   ? 16.614  -3.630  21.902  1.00 22.64  ? 910  HOH A O   1 
HETATM 5243 O  O   A HOH D 3 .   ? 5.653   2.199   26.369  0.84 30.88  ? 911  HOH A O   1 
HETATM 5244 O  O   . HOH D 3 .   ? -9.006  -17.281 20.050  1.00 29.61  ? 912  HOH A O   1 
HETATM 5245 O  O   . HOH D 3 .   ? 7.432   -22.595 25.487  1.00 17.95  ? 913  HOH A O   1 
HETATM 5246 O  O   . HOH D 3 .   ? 28.819  -7.820  11.618  1.00 47.14  ? 914  HOH A O   1 
HETATM 5247 O  O   . HOH D 3 .   ? -6.962  -5.162  47.675  1.00 49.59  ? 915  HOH A O   1 
HETATM 5248 O  O   . HOH D 3 .   ? 16.761  -27.753 25.043  1.00 28.92  ? 916  HOH A O   1 
HETATM 5249 O  O   . HOH D 3 .   ? 19.065  -23.719 -10.279 1.00 47.41  ? 917  HOH A O   1 
HETATM 5250 O  O   . HOH D 3 .   ? 29.244  -21.163 15.377  1.00 42.37  ? 918  HOH A O   1 
HETATM 5251 O  O   . HOH D 3 .   ? -3.851  -22.509 22.947  1.00 42.50  ? 919  HOH A O   1 
HETATM 5252 O  O   . HOH D 3 .   ? 23.867  -29.976 24.834  1.00 32.90  ? 920  HOH A O   1 
HETATM 5253 O  O   . HOH D 3 .   ? 5.454   3.890   28.607  1.00 45.71  ? 921  HOH A O   1 
HETATM 5254 O  O   . HOH D 3 .   ? 6.075   -1.774  20.595  1.00 23.71  ? 922  HOH A O   1 
HETATM 5255 O  O   . HOH D 3 .   ? 2.532   -25.574 21.474  1.00 16.89  ? 923  HOH A O   1 
HETATM 5256 O  O   . HOH D 3 .   ? 27.806  -15.755 15.217  1.00 36.23  ? 924  HOH A O   1 
HETATM 5257 O  O   . HOH D 3 .   ? 29.059  -16.253 6.128   1.00 53.72  ? 925  HOH A O   1 
HETATM 5258 O  O   . HOH D 3 .   ? -14.185 -20.217 36.560  1.00 42.37  ? 926  HOH A O   1 
HETATM 5259 O  O   . HOH D 3 .   ? 0.080   -24.840 33.684  1.00 52.67  ? 927  HOH A O   1 
HETATM 5260 O  O   C HOH D 3 .   ? 13.529  -4.928  9.517   1.00 51.79  ? 928  HOH A O   1 
HETATM 5261 O  O   . HOH D 3 .   ? -15.754 -13.098 29.109  1.00 44.87  ? 929  HOH A O   1 
HETATM 5262 O  O   . HOH D 3 .   ? 17.535  -12.012 14.971  1.00 17.92  ? 930  HOH A O   1 
HETATM 5263 O  O   . HOH D 3 .   ? -16.366 -1.210  39.625  1.00 47.23  ? 931  HOH A O   1 
HETATM 5264 O  O   . HOH D 3 .   ? 19.116  -32.168 3.659   1.00 54.91  ? 932  HOH A O   1 
HETATM 5265 O  O   . HOH D 3 .   ? -7.497  -2.476  46.936  1.00 47.94  ? 933  HOH A O   1 
HETATM 5266 O  O   . HOH D 3 .   ? 23.733  -27.126 -2.709  1.00 31.28  ? 934  HOH A O   1 
HETATM 5267 O  O   . HOH D 3 .   ? 14.210  3.571   39.003  1.00 50.31  ? 935  HOH A O   1 
HETATM 5268 O  O   . HOH D 3 .   ? 17.389  -10.108 26.406  1.00 28.57  ? 936  HOH A O   1 
HETATM 5269 O  O   . HOH D 3 .   ? 32.979  2.566   -7.406  1.00 50.43  ? 937  HOH A O   1 
HETATM 5270 O  O   . HOH D 3 .   ? 6.864   -25.494 33.468  1.00 32.04  ? 938  HOH A O   1 
HETATM 5271 O  O   . HOH D 3 .   ? 30.145  -16.069 -0.245  1.00 49.30  ? 939  HOH A O   1 
HETATM 5272 O  O   B HOH D 3 .   ? 9.801   -25.226 5.453   0.94 35.20  ? 940  HOH A O   1 
HETATM 5273 O  O   . HOH D 3 .   ? 13.981  -19.204 -10.307 1.00 45.08  ? 941  HOH A O   1 
HETATM 5274 O  O   . HOH D 3 .   ? 26.401  -22.592 -2.776  1.00 23.70  ? 942  HOH A O   1 
HETATM 5275 O  O   . HOH D 3 .   ? 16.215  2.469   33.089  1.00 54.94  ? 943  HOH A O   1 
HETATM 5276 O  O   . HOH D 3 .   ? 23.948  -7.073  9.606   1.00 29.61  ? 944  HOH A O   1 
HETATM 5277 O  O   . HOH D 3 .   ? -1.741  -22.731 21.312  1.00 24.24  ? 945  HOH A O   1 
HETATM 5278 O  O   . HOH D 3 .   ? -17.965 -2.419  30.426  1.00 39.01  ? 946  HOH A O   1 
HETATM 5279 O  O   . HOH D 3 .   ? 1.177   -6.203  11.801  1.00 27.05  ? 947  HOH A O   1 
HETATM 5280 O  O   . HOH D 3 .   ? 0.453   -23.547 18.364  1.00 15.50  ? 948  HOH A O   1 
HETATM 5281 O  O   . HOH D 3 .   ? 19.354  -27.276 4.351   1.00 30.95  ? 949  HOH A O   1 
HETATM 5282 O  O   B HOH D 3 .   ? 14.000  -6.151  10.919  0.99 58.69  ? 950  HOH A O   1 
HETATM 5283 O  O   . HOH D 3 .   ? -4.073  2.822   43.657  1.00 49.48  ? 951  HOH A O   1 
HETATM 5284 O  O   . HOH D 3 .   ? 13.402  6.585   33.169  1.00 66.47  ? 952  HOH A O   1 
HETATM 5285 O  O   . HOH D 3 .   ? -1.936  3.248   38.635  1.00 42.25  ? 953  HOH A O   1 
HETATM 5286 O  O   . HOH D 3 .   ? 3.846   -26.188 10.062  1.00 18.73  ? 954  HOH A O   1 
HETATM 5287 O  O   . HOH D 3 .   ? -1.287  -21.376 18.705  1.00 17.25  ? 955  HOH A O   1 
HETATM 5288 O  O   . HOH D 3 .   ? 17.621  -5.665  30.732  1.00 24.41  ? 956  HOH A O   1 
HETATM 5289 O  O   . HOH D 3 .   ? 14.286  -25.833 25.659  1.00 24.98  ? 957  HOH A O   1 
HETATM 5290 O  O   . HOH D 3 .   ? 25.129  -24.890 11.541  1.00 46.88  ? 958  HOH A O   1 
HETATM 5291 O  O   . HOH D 3 .   ? -8.289  -6.466  15.646  1.00 49.75  ? 959  HOH A O   1 
HETATM 5292 O  O   . HOH D 3 .   ? -11.450 -8.900  20.359  1.00 48.61  ? 960  HOH A O   1 
HETATM 5293 O  O   . HOH D 3 .   ? 21.444  -5.557  18.445  1.00 26.56  ? 961  HOH A O   1 
HETATM 5294 O  O   . HOH D 3 .   ? 16.522  -7.169  -8.919  1.00 44.37  ? 962  HOH A O   1 
HETATM 5295 O  O   . HOH D 3 .   ? 12.074  -9.602  21.133  1.00 12.56  ? 963  HOH A O   1 
HETATM 5296 O  O   . HOH D 3 .   ? 6.987   -27.855 12.885  1.00 76.58  ? 964  HOH A O   1 
HETATM 5297 O  O   . HOH D 3 .   ? -1.463  1.955   36.180  1.00 29.60  ? 965  HOH A O   1 
HETATM 5298 O  O   . HOH D 3 .   ? 27.519  -6.206  -6.658  1.00 32.84  ? 966  HOH A O   1 
HETATM 5299 O  O   . HOH D 3 .   ? -9.077  4.852   36.653  1.00 45.17  ? 967  HOH A O   1 
HETATM 5300 O  O   . HOH D 3 .   ? -2.617  -22.895 -0.275  1.00 16.29  ? 968  HOH A O   1 
HETATM 5301 O  O   . HOH D 3 .   ? 21.070  -7.406  -9.300  1.00 47.31  ? 969  HOH A O   1 
HETATM 5302 O  O   . HOH D 3 .   ? -9.273  -19.328 17.545  1.00 38.87  ? 970  HOH A O   1 
HETATM 5303 O  O   . HOH D 3 .   ? 0.675   -25.657 39.401  1.00 46.81  ? 971  HOH A O   1 
HETATM 5304 O  O   . HOH D 3 .   ? 0.916   -0.813  47.268  1.00 36.08  ? 972  HOH A O   1 
HETATM 5305 O  O   . HOH D 3 .   ? 16.461  -6.437  11.840  1.00 25.48  ? 973  HOH A O   1 
HETATM 5306 O  O   . HOH D 3 .   ? -2.495  -23.307 14.461  1.00 27.72  ? 974  HOH A O   1 
HETATM 5307 O  O   . HOH D 3 .   ? -6.921  -12.317 49.814  1.00 37.63  ? 975  HOH A O   1 
HETATM 5308 O  O   . HOH D 3 .   ? 10.517  -8.780  47.593  1.00 47.75  ? 976  HOH A O   1 
HETATM 5309 O  O   . HOH D 3 .   ? 21.907  -14.843 -8.193  1.00 54.42  ? 977  HOH A O   1 
HETATM 5310 O  O   . HOH D 3 .   ? -8.621  -20.974 21.741  1.00 55.29  ? 978  HOH A O   1 
HETATM 5311 O  O   . HOH D 3 .   ? 25.947  -10.881 20.825  1.00 39.36  ? 979  HOH A O   1 
HETATM 5312 O  O   . HOH D 3 .   ? -15.042 0.876   24.100  1.00 41.53  ? 980  HOH A O   1 
HETATM 5313 O  O   . HOH D 3 .   ? 5.554   -31.104 23.440  1.00 52.61  ? 981  HOH A O   1 
HETATM 5314 O  O   . HOH D 3 .   ? 2.232   -3.659  49.761  1.00 54.38  ? 982  HOH A O   1 
HETATM 5315 O  O   . HOH D 3 .   ? -7.406  3.791   19.304  1.00 49.85  ? 983  HOH A O   1 
HETATM 5316 O  O   . HOH D 3 .   ? 0.186   -18.995 44.801  1.00 55.50  ? 984  HOH A O   1 
HETATM 5317 O  O   . HOH D 3 .   ? 25.498  -20.989 25.908  1.00 53.86  ? 985  HOH A O   1 
HETATM 5318 O  O   . HOH D 3 .   ? 29.260  -11.509 -3.382  1.00 51.52  ? 986  HOH A O   1 
HETATM 5319 O  O   . HOH D 3 .   ? -14.890 -10.473 37.086  1.00 55.15  ? 987  HOH A O   1 
HETATM 5320 O  O   . HOH D 3 .   ? 18.782  -22.167 30.342  1.00 24.69  ? 988  HOH A O   1 
HETATM 5321 O  O   . HOH D 3 .   ? 3.821   4.773   30.264  1.00 71.87  ? 989  HOH A O   1 
HETATM 5322 O  O   . HOH D 3 .   ? -14.181 -8.739  24.011  1.00 43.07  ? 990  HOH A O   1 
HETATM 5323 O  O   . HOH D 3 .   ? 25.851  -4.877  20.272  1.00 50.39  ? 991  HOH A O   1 
HETATM 5324 O  O   . HOH D 3 .   ? 4.503   -18.418 40.612  1.00 61.47  ? 992  HOH A O   1 
HETATM 5325 O  O   . HOH D 3 .   ? 12.269  -14.057 36.213  1.00 27.57  ? 993  HOH A O   1 
HETATM 5326 O  O   . HOH D 3 .   ? 9.381   -25.318 25.157  1.00 27.40  ? 994  HOH A O   1 
HETATM 5327 O  O   . HOH D 3 .   ? -0.201  -16.378 42.660  1.00 21.38  ? 995  HOH A O   1 
HETATM 5328 O  O   . HOH D 3 .   ? 29.149  -9.227  21.965  1.00 49.19  ? 996  HOH A O   1 
HETATM 5329 O  O   . HOH D 3 .   ? -3.440  -22.585 25.300  1.00 64.12  ? 997  HOH A O   1 
HETATM 5330 O  O   . HOH D 3 .   ? 25.541  -26.979 12.432  1.00 51.23  ? 998  HOH A O   1 
HETATM 5331 O  O   . HOH D 3 .   ? -2.978  -21.432 16.501  1.00 17.96  ? 999  HOH A O   1 
HETATM 5332 O  O   . HOH D 3 .   ? -19.098 1.701   37.652  1.00 55.46  ? 1000 HOH A O   1 
HETATM 5333 O  O   . HOH D 3 .   ? -18.268 2.251   27.573  1.00 54.65  ? 1001 HOH A O   1 
HETATM 5334 O  O   . HOH D 3 .   ? 28.802  -6.260  -4.184  1.00 27.24  ? 1002 HOH A O   1 
HETATM 5335 O  O   A HOH D 3 .   ? 0.272   4.197   40.043  0.55 26.82  ? 1003 HOH A O   1 
HETATM 5336 O  O   B HOH D 3 .   ? 1.914   4.146   40.900  0.45 28.84  ? 1003 HOH A O   1 
HETATM 5337 O  O   . HOH D 3 .   ? 18.508  -13.825 -11.548 1.00 47.84  ? 1004 HOH A O   1 
HETATM 5338 O  O   . HOH D 3 .   ? -4.580  -4.583  48.537  1.00 45.81  ? 1005 HOH A O   1 
HETATM 5339 O  O   . HOH D 3 .   ? 5.622   6.535   35.203  1.00 49.32  ? 1006 HOH A O   1 
HETATM 5340 O  O   . HOH D 3 .   ? 26.289  -25.607 -1.596  1.00 41.15  ? 1007 HOH A O   1 
HETATM 5341 O  O   . HOH D 3 .   ? 8.133   -15.937 -4.702  1.00 51.18  ? 1008 HOH A O   1 
HETATM 5342 O  O   . HOH D 3 .   ? 22.220  -0.696  19.161  1.00 33.38  ? 1009 HOH A O   1 
HETATM 5343 O  O   . HOH D 3 .   ? 8.234   -6.124  11.374  1.00 24.36  ? 1010 HOH A O   1 
HETATM 5344 O  O   . HOH D 3 .   ? 11.919  5.714   37.706  1.00 53.93  ? 1011 HOH A O   1 
HETATM 5345 O  O   . HOH D 3 .   ? 17.150  -29.588 15.489  1.00 31.27  ? 1012 HOH A O   1 
HETATM 5346 O  O   . HOH D 3 .   ? 19.846  -5.809  3.053   1.00 27.94  ? 1013 HOH A O   1 
HETATM 5347 O  O   . HOH D 3 .   ? 16.614  -5.060  39.939  1.00 48.62  ? 1014 HOH A O   1 
HETATM 5348 O  O   . HOH D 3 .   ? 9.589   -29.390 22.461  1.00 50.38  ? 1015 HOH A O   1 
HETATM 5349 O  O   . HOH D 3 .   ? 12.590  6.968   30.371  1.00 37.60  ? 1016 HOH A O   1 
HETATM 5350 O  O   . HOH D 3 .   ? 6.268   6.971   38.354  1.00 73.71  ? 1017 HOH A O   1 
HETATM 5351 O  O   . HOH D 3 .   ? 34.560  1.245   -3.848  1.00 51.67  ? 1018 HOH A O   1 
HETATM 5352 O  O   . HOH D 3 .   ? 11.429  -2.824  46.603  1.00 54.74  ? 1019 HOH A O   1 
HETATM 5353 O  O   . HOH D 3 .   ? 11.750  7.025   34.951  1.00 56.50  ? 1020 HOH A O   1 
HETATM 5354 O  O   . HOH D 3 .   ? 30.358  -14.821 -3.341  1.00 57.76  ? 1021 HOH A O   1 
HETATM 5355 O  O   . HOH D 3 .   ? 29.238  1.894   0.635   1.00 53.49  ? 1022 HOH A O   1 
HETATM 5356 O  O   . HOH D 3 .   ? 27.865  -19.710 28.337  1.00 70.39  ? 1023 HOH A O   1 
HETATM 5357 O  O   . HOH D 3 .   ? 12.755  -25.321 2.196   1.00 31.75  ? 1024 HOH A O   1 
HETATM 5358 O  O   . HOH D 3 .   ? 7.466   -9.807  48.103  1.00 44.73  ? 1025 HOH A O   1 
HETATM 5359 O  O   . HOH D 3 .   ? 28.003  -8.912  4.761   1.00 40.04  ? 1026 HOH A O   1 
HETATM 5360 O  O   . HOH D 3 .   ? 19.166  -21.229 -10.982 1.00 57.04  ? 1027 HOH A O   1 
HETATM 5361 O  O   . HOH D 3 .   ? 20.343  -5.994  5.771   1.00 52.97  ? 1028 HOH A O   1 
HETATM 5362 O  O   . HOH D 3 .   ? -10.988 -26.062 29.153  1.00 49.29  ? 1029 HOH A O   1 
HETATM 5363 O  O   . HOH D 3 .   ? -13.072 -18.881 38.951  1.00 87.61  ? 1030 HOH A O   1 
HETATM 5364 O  O   . HOH D 3 .   ? 8.289   -0.180  36.274  1.00 49.69  ? 1031 HOH A O   1 
HETATM 5365 O  O   . HOH D 3 .   ? 18.896  3.789   -11.153 1.00 50.15  ? 1032 HOH A O   1 
HETATM 5366 O  O   . HOH D 3 .   ? 1.491   -28.110 34.410  1.00 49.32  ? 1033 HOH A O   1 
HETATM 5367 O  O   . HOH D 3 .   ? 27.033  -21.562 20.380  1.00 49.64  ? 1034 HOH A O   1 
HETATM 5368 O  O   . HOH D 3 .   ? -8.733  -10.872 48.951  1.00 58.79  ? 1035 HOH A O   1 
HETATM 5369 O  O   . HOH D 3 .   ? -6.015  -5.170  15.929  1.00 54.41  ? 1036 HOH A O   1 
HETATM 5370 O  O   . HOH D 3 .   ? 21.642  -22.532 30.599  1.00 27.27  ? 1037 HOH A O   1 
HETATM 5371 O  O   . HOH D 3 .   ? 24.815  -24.632 8.728   1.00 40.73  ? 1038 HOH A O   1 
HETATM 5372 O  O   . HOH D 3 .   ? 19.291  -3.612  26.469  1.00 52.07  ? 1039 HOH A O   1 
HETATM 5373 O  O   . HOH D 3 .   ? 24.887  -32.532 3.005   1.00 50.06  ? 1040 HOH A O   1 
HETATM 5374 O  O   . HOH D 3 .   ? 13.073  -28.500 16.866  1.00 34.65  ? 1041 HOH A O   1 
HETATM 5375 O  O   . HOH D 3 .   ? 24.612  -23.286 23.692  1.00 52.68  ? 1042 HOH A O   1 
HETATM 5376 O  O   . HOH D 3 .   ? 24.171  4.933   -4.261  1.00 57.98  ? 1043 HOH A O   1 
HETATM 5377 O  O   . HOH D 3 .   ? 18.872  -4.975  -9.426  1.00 43.04  ? 1044 HOH A O   1 
HETATM 5378 O  O   . HOH D 3 .   ? 19.818  -1.646  4.842   1.00 45.17  ? 1045 HOH A O   1 
HETATM 5379 O  O   A HOH D 3 .   ? 14.983  -6.982  9.232   0.70 31.46  ? 1046 HOH A O   1 
HETATM 5380 O  O   B HOH D 3 .   ? 13.270  -6.615  8.944   0.30 18.68  ? 1046 HOH A O   1 
HETATM 5381 O  O   . HOH D 3 .   ? -15.122 -9.996  31.894  1.00 51.10  ? 1047 HOH A O   1 
HETATM 5382 O  O   . HOH D 3 .   ? 3.935   -19.852 -4.324  1.00 56.93  ? 1048 HOH A O   1 
HETATM 5383 O  O   . HOH D 3 .   ? 15.143  -14.887 36.607  1.00 39.74  ? 1049 HOH A O   1 
HETATM 5384 O  O   . HOH D 3 .   ? -17.235 1.467   25.656  1.00 50.21  ? 1050 HOH A O   1 
HETATM 5385 O  O   . HOH D 3 .   ? 22.833  -3.515  3.488   1.00 43.01  ? 1051 HOH A O   1 
HETATM 5386 O  O   . HOH D 3 .   ? 20.272  -29.208 -5.464  1.00 46.70  ? 1052 HOH A O   1 
HETATM 5387 O  O   . HOH D 3 .   ? 32.536  -9.309  1.661   1.00 45.59  ? 1053 HOH A O   1 
HETATM 5388 O  O   . HOH D 3 .   ? 13.978  -26.341 29.679  1.00 70.87  ? 1054 HOH A O   1 
HETATM 5389 O  O   . HOH D 3 .   ? 17.318  -8.708  13.279  1.00 20.95  ? 1055 HOH A O   1 
HETATM 5390 O  O   A HOH D 3 .   ? 35.829  -1.244  -6.651  0.28 22.30  ? 1056 HOH A O   1 
HETATM 5391 O  O   B HOH D 3 .   ? 36.255  -2.281  -8.110  0.72 39.36  ? 1056 HOH A O   1 
HETATM 5392 O  O   . HOH D 3 .   ? -3.092  -27.265 13.464  1.00 60.77  ? 1057 HOH A O   1 
HETATM 5393 O  O   . HOH D 3 .   ? 2.781   -26.031 3.005   1.00 48.53  ? 1058 HOH A O   1 
HETATM 5394 O  O   . HOH D 3 .   ? 17.556  1.393   31.393  1.00 49.19  ? 1059 HOH A O   1 
HETATM 5395 O  O   . HOH D 3 .   ? 17.540  -4.375  2.198   1.00 23.54  ? 1060 HOH A O   1 
HETATM 5396 O  O   . HOH D 3 .   ? -11.303 -16.465 21.180  1.00 44.24  ? 1061 HOH A O   1 
HETATM 5397 O  O   A HOH D 3 .   ? 25.588  3.999   -2.566  1.00 43.25  ? 1062 HOH A O   1 
HETATM 5398 O  O   A HOH D 3 .   ? 18.732  -3.213  8.816   1.00 44.16  ? 1063 HOH A O   1 
HETATM 5399 O  O   . HOH D 3 .   ? 23.383  -6.363  20.210  1.00 38.53  ? 1064 HOH A O   1 
HETATM 5400 O  O   . HOH D 3 .   ? 29.963  -13.240 0.549   1.00 51.64  ? 1065 HOH A O   1 
HETATM 5401 O  O   . HOH D 3 .   ? 12.051  -24.168 4.321   1.00 35.38  ? 1066 HOH A O   1 
HETATM 5402 O  O   . HOH D 3 .   ? 30.539  -12.825 -1.903  1.00 55.35  ? 1067 HOH A O   1 
HETATM 5403 O  O   . HOH D 3 .   ? 27.933  -22.470 4.321   1.00 54.92  ? 1068 HOH A O   1 
HETATM 5404 O  O   . HOH D 3 .   ? 21.492  -29.101 4.723   1.00 36.06  ? 1069 HOH A O   1 
HETATM 5405 O  O   . HOH D 3 .   ? -4.067  -29.226 10.701  1.00 52.12  ? 1070 HOH A O   1 
HETATM 5406 O  O   . HOH D 3 .   ? 26.678  -26.733 19.973  1.00 58.25  ? 1071 HOH A O   1 
HETATM 5407 O  O   . HOH D 3 .   ? 16.338  -13.138 -11.965 1.00 50.57  ? 1072 HOH A O   1 
HETATM 5408 O  O   . HOH D 3 .   ? 12.596  -9.354  39.436  1.00 36.81  ? 1073 HOH A O   1 
HETATM 5409 O  O   . HOH D 3 .   ? -15.433 9.704   31.637  1.00 61.61  ? 1074 HOH A O   1 
HETATM 5410 O  O   . HOH D 3 .   ? -13.102 -7.460  40.020  1.00 44.77  ? 1075 HOH A O   1 
HETATM 5411 O  O   . HOH D 3 .   ? 31.643  -11.408 2.379   1.00 43.64  ? 1076 HOH A O   1 
HETATM 5412 O  O   . HOH D 3 .   ? 12.329  -30.481 9.246   1.00 29.80  ? 1077 HOH A O   1 
HETATM 5413 O  O   . HOH D 3 .   ? 5.400   -34.176 13.417  1.00 45.62  ? 1078 HOH A O   1 
HETATM 5414 O  O   . HOH D 3 .   ? 26.071  -0.100  17.136  1.00 61.27  ? 1079 HOH A O   1 
HETATM 5415 O  O   . HOH D 3 .   ? 10.059  -15.828 -7.242  1.00 54.22  ? 1080 HOH A O   1 
HETATM 5416 O  O   . HOH D 3 .   ? 27.394  -13.257 9.899   1.00 44.86  ? 1081 HOH A O   1 
HETATM 5417 O  O   . HOH D 3 .   ? 17.879  -4.298  34.545  1.00 51.33  ? 1082 HOH A O   1 
HETATM 5418 O  O   . HOH D 3 .   ? -4.272  -24.791 18.732  1.00 52.14  ? 1083 HOH A O   1 
HETATM 5419 O  O   . HOH D 3 .   ? 26.368  -7.508  5.958   1.00 54.56  ? 1084 HOH A O   1 
HETATM 5420 O  O   . HOH D 3 .   ? 16.716  -2.842  10.677  1.00 29.93  ? 1085 HOH A O   1 
HETATM 5421 O  O   . HOH D 3 .   ? 8.665   -27.832 24.894  1.00 40.63  ? 1086 HOH A O   1 
HETATM 5422 O  O   . HOH D 3 .   ? 12.968  -25.194 -0.072  1.00 67.32  ? 1087 HOH A O   1 
HETATM 5423 O  O   . HOH D 3 .   ? 16.515  -14.963 32.445  1.00 30.69  ? 1088 HOH A O   1 
HETATM 5424 O  O   . HOH D 3 .   ? 21.731  -31.925 12.093  1.00 52.81  ? 1089 HOH A O   1 
HETATM 5425 O  O   . HOH D 3 .   ? 30.712  -10.660 4.664   1.00 53.45  ? 1090 HOH A O   1 
HETATM 5426 O  O   . HOH D 3 .   ? 20.498  -2.909  19.712  1.00 39.84  ? 1091 HOH A O   1 
HETATM 5427 O  O   . HOH D 3 .   ? 17.894  -4.730  10.182  1.00 31.58  ? 1092 HOH A O   1 
HETATM 5428 O  O   B HOH D 3 .   ? 27.710  -20.175 -3.613  0.99 36.96  ? 1093 HOH A O   1 
HETATM 5429 O  O   . HOH D 3 .   ? -12.030 -19.118 22.396  1.00 53.64  ? 1094 HOH A O   1 
HETATM 5430 O  O   . HOH D 3 .   ? 16.914  -1.495  38.138  1.00 50.54  ? 1095 HOH A O   1 
HETATM 5431 O  O   . HOH D 3 .   ? 25.035  -33.482 16.574  1.00 63.74  ? 1096 HOH A O   1 
HETATM 5432 O  O   . HOH D 3 .   ? 22.188  -18.372 -8.197  1.00 52.46  ? 1097 HOH A O   1 
HETATM 5433 O  O   . HOH D 3 .   ? 20.266  -15.318 32.181  1.00 53.45  ? 1098 HOH A O   1 
HETATM 5434 O  O   . HOH D 3 .   ? 22.755  -11.025 22.238  1.00 43.33  ? 1099 HOH A O   1 
HETATM 5435 O  O   . HOH D 3 .   ? 3.895   -9.428  50.319  1.00 46.77  ? 1100 HOH A O   1 
HETATM 5436 O  O   . HOH D 3 .   ? -12.644 -3.252  42.476  1.00 51.22  ? 1101 HOH A O   1 
HETATM 5437 O  O   . HOH D 3 .   ? 11.606  -12.274 38.599  1.00 25.03  ? 1102 HOH A O   1 
HETATM 5438 O  O   . HOH D 3 .   ? 26.832  -9.160  7.730   1.00 47.83  ? 1103 HOH A O   1 
HETATM 5439 O  O   . HOH D 3 .   ? -11.209 -5.923  22.733  1.00 48.20  ? 1104 HOH A O   1 
HETATM 5440 O  O   . HOH D 3 .   ? -11.639 -8.019  23.399  1.00 58.10  ? 1105 HOH A O   1 
HETATM 5441 O  O   . HOH D 3 .   ? -0.096  -24.963 20.668  1.00 21.50  ? 1106 HOH A O   1 
HETATM 5442 O  O   . HOH D 3 .   ? -5.591  -22.736 16.260  1.00 59.78  ? 1107 HOH A O   1 
HETATM 5443 O  O   . HOH D 3 .   ? 14.914  -28.787 6.093   1.00 38.66  ? 1108 HOH A O   1 
HETATM 5444 O  O   . HOH D 3 .   ? 12.795  -27.462 24.290  1.00 59.06  ? 1109 HOH A O   1 
HETATM 5445 O  O   . HOH D 3 .   ? -14.955 -12.157 31.347  1.00 50.72  ? 1110 HOH A O   1 
HETATM 5446 O  O   . HOH D 3 .   ? -7.055  1.771   17.599  1.00 44.19  ? 1111 HOH A O   1 
HETATM 5447 O  O   . HOH D 3 .   ? 24.951  -14.786 -6.991  1.00 47.08  ? 1112 HOH A O   1 
HETATM 5448 O  O   . HOH D 3 .   ? 19.380  -13.166 29.651  1.00 43.97  ? 1113 HOH A O   1 
HETATM 5449 O  O   . HOH D 3 .   ? 21.171  -0.649  6.513   1.00 45.83  ? 1114 HOH A O   1 
HETATM 5450 O  O   . HOH D 3 .   ? 16.991  -31.556 13.728  1.00 52.96  ? 1115 HOH A O   1 
HETATM 5451 O  O   . HOH D 3 .   ? -9.746  -4.456  20.781  1.00 38.30  ? 1116 HOH A O   1 
HETATM 5452 O  O   . HOH D 3 .   ? 17.329  -26.973 29.676  1.00 63.23  ? 1117 HOH A O   1 
HETATM 5453 O  O   . HOH D 3 .   ? 4.171   -13.601 50.180  1.00 55.56  ? 1118 HOH A O   1 
HETATM 5454 O  O   . HOH D 3 .   ? 28.500  -11.901 12.082  1.00 55.49  ? 1119 HOH A O   1 
HETATM 5455 O  O   . HOH D 3 .   ? -11.446 6.574   26.663  1.00 61.96  ? 1120 HOH A O   1 
HETATM 5456 O  O   . HOH D 3 .   ? -1.629  -27.568 17.883  1.00 51.10  ? 1121 HOH A O   1 
HETATM 5457 O  O   . HOH D 3 .   ? -15.433 -4.569  41.119  1.00 70.15  ? 1122 HOH A O   1 
HETATM 5458 O  O   . HOH D 3 .   ? -14.656 -24.678 29.701  1.00 56.28  ? 1123 HOH A O   1 
HETATM 5459 O  O   . HOH D 3 .   ? 3.023   2.475   45.127  1.00 54.60  ? 1124 HOH A O   1 
HETATM 5460 O  O   . HOH D 3 .   ? -3.373  -6.105  12.934  1.00 29.55  ? 1125 HOH A O   1 
HETATM 5461 O  O   . HOH D 3 .   ? 12.014  -30.857 16.044  1.00 44.19  ? 1126 HOH A O   1 
HETATM 5462 O  O   . HOH D 3 .   ? 33.770  0.357   -7.581  1.00 39.99  ? 1127 HOH A O   1 
HETATM 5463 O  O   . HOH D 3 .   ? -0.866  3.506   42.978  1.00 57.66  ? 1128 HOH A O   1 
HETATM 5464 O  O   . HOH D 3 .   ? -1.874  -8.124  50.431  1.00 60.40  ? 1129 HOH A O   1 
HETATM 5465 O  O   . HOH D 3 .   ? 2.384   6.390   40.442  1.00 66.21  ? 1130 HOH A O   1 
HETATM 5466 O  O   . HOH D 3 .   ? 7.798   -27.465 33.955  1.00 54.61  ? 1131 HOH A O   1 
HETATM 5467 O  O   . HOH D 3 .   ? 5.284   -30.665 27.580  1.00 66.64  ? 1132 HOH A O   1 
HETATM 5468 O  O   . HOH D 3 .   ? 4.191   -30.849 29.957  1.00 56.11  ? 1133 HOH A O   1 
HETATM 5469 O  O   . HOH D 3 .   ? 25.829  7.712   -4.507  1.00 55.07  ? 1134 HOH A O   1 
HETATM 5470 O  O   . HOH D 3 .   ? -0.313  -22.553 -0.805  1.00 54.82  ? 1135 HOH A O   1 
HETATM 5471 O  O   . HOH D 3 .   ? -14.968 4.400   23.002  1.00 48.16  ? 1136 HOH A O   1 
HETATM 5472 O  O   . HOH D 3 .   ? 11.344  -27.942 27.973  1.00 47.69  ? 1137 HOH A O   1 
HETATM 5473 O  O   . HOH D 3 .   ? 2.218   -21.517 -2.018  1.00 53.52  ? 1138 HOH A O   1 
HETATM 5474 O  O   . HOH D 3 .   ? 19.318  -6.987  26.154  1.00 53.85  ? 1139 HOH A O   1 
HETATM 5475 O  O   . HOH D 3 .   ? 6.195   -29.270 25.353  1.00 43.32  ? 1140 HOH A O   1 
HETATM 5476 O  O   . HOH D 3 .   ? 4.117   7.812   39.108  1.00 55.37  ? 1141 HOH A O   1 
HETATM 5477 O  O   . HOH D 3 .   ? 18.961  -6.279  19.614  1.00 40.06  ? 1142 HOH A O   1 
HETATM 5478 O  O   . HOH D 3 .   ? 35.169  -15.358 21.679  1.00 45.35  ? 1143 HOH A O   1 
HETATM 5479 O  O   . HOH D 3 .   ? 16.834  -24.474 30.458  1.00 44.73  ? 1144 HOH A O   1 
HETATM 5480 O  O   . HOH D 3 .   ? 4.585   -20.027 -6.543  1.00 53.63  ? 1145 HOH A O   1 
HETATM 5481 O  O   . HOH D 3 .   ? -10.321 4.363   23.875  1.00 40.52  ? 1146 HOH A O   1 
HETATM 5482 O  O   . HOH D 3 .   ? 1.687   -35.630 13.246  1.00 45.20  ? 1147 HOH A O   1 
HETATM 5483 O  O   . HOH D 3 .   ? -7.937  -25.882 26.765  1.00 60.75  ? 1148 HOH A O   1 
HETATM 5484 O  O   . HOH D 3 .   ? -3.736  4.653   37.682  1.00 57.64  ? 1149 HOH A O   1 
HETATM 5485 O  O   . HOH D 3 .   ? -8.125  -11.225 12.601  1.00 41.39  ? 1150 HOH A O   1 
HETATM 5486 O  O   . HOH D 3 .   ? 27.347  -3.445  3.078   1.00 49.06  ? 1151 HOH A O   1 
HETATM 5487 O  O   . HOH D 3 .   ? -4.326  -10.990 50.972  1.00 51.05  ? 1152 HOH A O   1 
HETATM 5488 O  O   . HOH D 3 .   ? 20.642  -3.927  4.199   1.00 74.22  ? 1153 HOH A O   1 
HETATM 5489 O  O   . HOH D 3 .   ? -11.375 8.204   28.912  1.00 57.22  ? 1154 HOH A O   1 
HETATM 5490 O  O   . HOH D 3 .   ? 0.397   3.050   45.138  1.00 71.63  ? 1155 HOH A O   1 
HETATM 5491 O  O   . HOH D 3 .   ? -9.029  6.345   28.015  1.00 64.19  ? 1156 HOH A O   1 
HETATM 5492 O  O   . HOH D 3 .   ? 6.996   -20.120 -7.849  1.00 58.51  ? 1157 HOH A O   1 
HETATM 5493 O  O   . HOH D 3 .   ? -9.341  5.328   19.083  1.00 49.27  ? 1158 HOH A O   1 
HETATM 5494 O  O   . HOH D 3 .   ? 0.024   -29.579 21.624  1.00 46.48  ? 1159 HOH A O   1 
HETATM 5495 O  O   . HOH D 3 .   ? 29.555  -10.155 11.099  1.00 54.86  ? 1160 HOH A O   1 
HETATM 5496 O  O   . HOH D 3 .   ? -3.551  -6.059  50.305  1.00 51.67  ? 1161 HOH A O   1 
HETATM 5497 O  O   . HOH D 3 .   ? 31.871  1.702   -1.663  1.00 48.10  ? 1162 HOH A O   1 
HETATM 5498 O  O   . HOH D 3 .   ? -4.083  4.429   35.027  1.00 32.16  ? 1163 HOH A O   1 
HETATM 5499 O  O   . HOH D 3 .   ? 7.838   -30.489 14.200  1.00 43.41  ? 1164 HOH A O   1 
HETATM 5500 O  O   . HOH D 3 .   ? 17.664  -1.033  -13.272 1.00 52.75  ? 1165 HOH A O   1 
HETATM 5501 O  O   . HOH D 3 .   ? 29.414  -21.656 18.760  1.00 43.69  ? 1166 HOH A O   1 
HETATM 5502 O  O   . HOH D 3 .   ? -6.295  5.101   17.038  1.00 45.03  ? 1167 HOH A O   1 
HETATM 5503 O  O   . HOH D 3 .   ? 14.762  -33.281 10.330  1.00 48.98  ? 1168 HOH A O   1 
HETATM 5504 O  O   . HOH D 3 .   ? -3.907  -24.521 16.141  1.00 59.32  ? 1169 HOH A O   1 
HETATM 5505 O  O   . HOH D 3 .   ? 14.536  -31.340 6.997   1.00 49.70  ? 1170 HOH A O   1 
HETATM 5506 O  O   A HOH D 3 .   ? 18.697  -5.034  22.840  1.00 58.75  ? 1171 HOH A O   1 
HETATM 5507 O  O   . HOH D 3 .   ? 19.276  -5.534  28.404  1.00 44.83  ? 1172 HOH A O   1 
HETATM 5508 O  O   . HOH D 3 .   ? -15.779 -19.309 23.286  1.00 55.87  ? 1173 HOH A O   1 
HETATM 5509 O  O   . HOH D 3 .   ? -12.835 -11.671 21.502  1.00 54.60  ? 1174 HOH A O   1 
HETATM 5510 O  O   . HOH D 3 .   ? 15.219  2.610   42.854  1.00 54.72  ? 1175 HOH A O   1 
HETATM 5511 O  O   . HOH D 3 .   ? -15.151 -2.219  42.017  1.00 42.12  ? 1176 HOH A O   1 
HETATM 5512 O  O   . HOH D 3 .   ? 15.431  7.996   34.052  1.00 38.45  ? 1177 HOH A O   1 
HETATM 5513 O  O   . HOH D 3 .   ? 20.317  3.055   30.562  1.00 55.07  ? 1178 HOH A O   1 
HETATM 5514 O  O   . HOH D 3 .   ? 18.966  -33.140 12.798  1.00 62.72  ? 1179 HOH A O   1 
HETATM 5515 O  O   . HOH D 3 .   ? -12.739 -14.795 20.532  1.00 63.64  ? 1180 HOH A O   1 
HETATM 5516 O  O   . HOH D 3 .   ? 15.915  -33.577 8.223   1.00 46.74  ? 1181 HOH A O   1 
HETATM 5517 O  O   . HOH D 3 .   ? -1.241  -27.677 20.469  1.00 46.74  ? 1182 HOH A O   1 
HETATM 5518 O  O   . HOH D 3 .   ? 32.850  10.214  -10.518 1.00 53.11  ? 1183 HOH A O   1 
HETATM 5519 O  O   . HOH D 3 .   ? -15.458 -19.028 40.633  1.00 59.50  ? 1184 HOH A O   1 
HETATM 5520 O  O   . HOH D 3 .   ? 33.350  -5.635  15.242  1.00 58.93  ? 1185 HOH A O   1 
HETATM 5521 O  O   . HOH D 3 .   ? 26.651  -4.779  5.237   1.00 50.46  ? 1186 HOH A O   1 
HETATM 5522 O  O   . HOH D 3 .   ? 26.785  7.257   -1.634  1.00 60.98  ? 1187 HOH A O   1 
HETATM 5523 O  O   . HOH D 3 .   ? 16.750  -34.731 2.970   1.00 52.80  ? 1188 HOH A O   1 
HETATM 5524 O  O   . HOH E 3 .   ? 20.316  33.461  21.011  1.00 50.42  ? 601  HOH B O   1 
HETATM 5525 O  O   B HOH E 3 .   ? 4.617   2.674   24.652  0.85 33.45  ? 602  HOH B O   1 
HETATM 5526 O  O   . HOH E 3 .   ? 2.274   3.614   22.719  1.00 35.96  ? 603  HOH B O   1 
HETATM 5527 O  O   . HOH E 3 .   ? -9.074  17.798  -7.287  1.00 33.96  ? 604  HOH B O   1 
HETATM 5528 O  O   . HOH E 3 .   ? 3.182   0.556   -9.423  1.00 46.46  ? 605  HOH B O   1 
HETATM 5529 O  O   . HOH E 3 .   ? 1.997   5.061   24.656  1.00 70.78  ? 606  HOH B O   1 
HETATM 5530 O  O   . HOH E 3 .   ? 5.084   28.275  24.753  1.00 48.81  ? 607  HOH B O   1 
HETATM 5531 O  O   . HOH E 3 .   ? 19.053  14.560  6.704   1.00 31.87  ? 608  HOH B O   1 
HETATM 5532 O  O   A HOH E 3 .   ? -8.699  -28.650 7.215   1.00 42.16  ? 609  HOH B O   1 
HETATM 5533 O  O   . HOH E 3 .   ? -8.158  5.637   10.817  1.00 25.33  ? 610  HOH B O   1 
HETATM 5534 O  O   . HOH E 3 .   ? -13.173 -3.873  -13.719 1.00 47.21  ? 611  HOH B O   1 
HETATM 5535 O  O   . HOH E 3 .   ? 13.768  23.012  5.997   1.00 28.22  ? 612  HOH B O   1 
HETATM 5536 O  O   . HOH E 3 .   ? 17.769  22.332  -3.476  1.00 47.64  ? 613  HOH B O   1 
HETATM 5537 O  O   . HOH E 3 .   ? -7.862  -18.289 -5.171  1.00 46.17  ? 614  HOH B O   1 
HETATM 5538 O  O   . HOH E 3 .   ? 24.790  26.104  24.599  1.00 47.57  ? 615  HOH B O   1 
HETATM 5539 O  O   . HOH E 3 .   ? 19.848  13.635  2.800   1.00 31.96  ? 616  HOH B O   1 
HETATM 5540 O  O   . HOH E 3 .   ? 3.255   -2.027  9.223   1.00 20.37  ? 617  HOH B O   1 
HETATM 5541 O  O   . HOH E 3 .   ? -12.851 16.051  -3.917  1.00 65.22  ? 618  HOH B O   1 
HETATM 5542 O  O   . HOH E 3 .   ? -4.727  21.301  2.232   1.00 33.90  ? 619  HOH B O   1 
HETATM 5543 O  O   . HOH E 3 .   ? 5.997   2.862   20.772  1.00 29.27  ? 620  HOH B O   1 
HETATM 5544 O  O   . HOH E 3 .   ? 17.738  -2.838  19.560  1.00 24.96  ? 621  HOH B O   1 
HETATM 5545 O  O   . HOH E 3 .   ? -11.444 -28.148 5.265   1.00 47.59  ? 622  HOH B O   1 
HETATM 5546 O  O   . HOH E 3 .   ? 2.528   10.003  34.255  1.00 56.71  ? 623  HOH B O   1 
HETATM 5547 O  O   . HOH E 3 .   ? 0.646   -13.312 -13.687 1.00 50.17  ? 624  HOH B O   1 
HETATM 5548 O  O   . HOH E 3 .   ? 20.675  -0.433  11.932  1.00 36.17  ? 625  HOH B O   1 
HETATM 5549 O  O   . HOH E 3 .   ? -2.413  -19.669 -2.864  1.00 24.60  ? 626  HOH B O   1 
HETATM 5550 O  O   . HOH E 3 .   ? -11.158 10.979  -6.294  1.00 46.80  ? 627  HOH B O   1 
HETATM 5551 O  O   . HOH E 3 .   ? -9.938  -21.264 10.759  1.00 21.25  ? 628  HOH B O   1 
HETATM 5552 O  O   . HOH E 3 .   ? 18.038  4.446   -8.263  1.00 50.10  ? 629  HOH B O   1 
HETATM 5553 O  O   . HOH E 3 .   ? 11.369  0.615   -12.256 1.00 49.34  ? 630  HOH B O   1 
HETATM 5554 O  O   . HOH E 3 .   ? 18.306  17.548  1.741   1.00 49.30  ? 631  HOH B O   1 
HETATM 5555 O  O   . HOH E 3 .   ? 5.172   17.702  -7.973  1.00 21.03  ? 632  HOH B O   1 
HETATM 5556 O  O   . HOH E 3 .   ? 24.020  4.142   13.849  1.00 57.58  ? 633  HOH B O   1 
HETATM 5557 O  O   . HOH E 3 .   ? 3.410   19.506  14.614  1.00 22.88  ? 634  HOH B O   1 
HETATM 5558 O  O   . HOH E 3 .   ? 22.492  7.912   1.749   1.00 32.42  ? 635  HOH B O   1 
HETATM 5559 O  O   . HOH E 3 .   ? -12.204 16.153  6.188   1.00 57.41  ? 636  HOH B O   1 
HETATM 5560 O  O   . HOH E 3 .   ? 30.810  22.856  19.373  1.00 41.25  ? 637  HOH B O   1 
HETATM 5561 O  O   . HOH E 3 .   ? 16.664  28.003  7.240   1.00 44.26  ? 638  HOH B O   1 
HETATM 5562 O  O   . HOH E 3 .   ? 25.205  4.741   5.574   1.00 44.89  ? 639  HOH B O   1 
HETATM 5563 O  O   . HOH E 3 .   ? 15.431  -0.482  7.907   1.00 47.88  ? 640  HOH B O   1 
HETATM 5564 O  O   . HOH E 3 .   ? 18.670  1.738   26.961  1.00 31.11  ? 641  HOH B O   1 
HETATM 5565 O  O   A HOH E 3 .   ? -9.730  -23.662 11.931  0.35 27.64  ? 642  HOH B O   1 
HETATM 5566 O  O   B HOH E 3 .   ? -8.751  -23.336 13.227  0.65 20.57  ? 642  HOH B O   1 
HETATM 5567 O  O   . HOH E 3 .   ? 14.637  1.012   -10.611 1.00 37.19  ? 643  HOH B O   1 
HETATM 5568 O  O   . HOH E 3 .   ? 2.761   -5.317  9.997   1.00 24.63  ? 644  HOH B O   1 
HETATM 5569 O  O   . HOH E 3 .   ? 12.040  25.820  13.859  1.00 20.88  ? 645  HOH B O   1 
HETATM 5570 O  O   A HOH E 3 .   ? 22.316  5.826   20.668  0.75 18.43  ? 646  HOH B O   1 
HETATM 5571 O  O   B HOH E 3 .   ? 23.558  6.652   19.326  0.25 14.68  ? 646  HOH B O   1 
HETATM 5572 O  O   . HOH E 3 .   ? 23.768  27.376  27.948  1.00 62.42  ? 647  HOH B O   1 
HETATM 5573 O  O   . HOH E 3 .   ? 14.937  8.590   -7.556  1.00 67.88  ? 648  HOH B O   1 
HETATM 5574 O  O   . HOH E 3 .   ? 23.801  8.385   14.166  1.00 20.80  ? 649  HOH B O   1 
HETATM 5575 O  O   . HOH E 3 .   ? 22.696  3.703   26.999  1.00 25.16  ? 650  HOH B O   1 
HETATM 5576 O  O   . HOH E 3 .   ? 15.803  27.956  30.874  1.00 27.21  ? 651  HOH B O   1 
HETATM 5577 O  O   . HOH E 3 .   ? -13.232 4.395   -2.793  1.00 37.70  ? 652  HOH B O   1 
HETATM 5578 O  O   . HOH E 3 .   ? 26.842  15.646  31.452  1.00 44.71  ? 653  HOH B O   1 
HETATM 5579 O  O   . HOH E 3 .   ? -13.569 1.970   5.930   1.00 37.50  ? 654  HOH B O   1 
HETATM 5580 O  O   . HOH E 3 .   ? -15.226 -9.526  -7.975  1.00 36.68  ? 655  HOH B O   1 
HETATM 5581 O  O   . HOH E 3 .   ? -0.123  9.708   5.601   1.00 13.92  ? 656  HOH B O   1 
HETATM 5582 O  O   . HOH E 3 .   ? -1.213  16.335  -2.301  1.00 54.14  ? 657  HOH B O   1 
HETATM 5583 O  O   . HOH E 3 .   ? 5.908   19.276  26.758  1.00 19.45  ? 658  HOH B O   1 
HETATM 5584 O  O   . HOH E 3 .   ? -7.724  10.042  -9.114  1.00 33.63  ? 659  HOH B O   1 
HETATM 5585 O  O   . HOH E 3 .   ? -15.143 -8.007  4.539   1.00 48.87  ? 660  HOH B O   1 
HETATM 5586 O  O   A HOH E 3 .   ? -7.286  14.275  3.051   0.66 21.10  ? 661  HOH B O   1 
HETATM 5587 O  O   B HOH E 3 .   ? -8.319  15.454  3.782   0.34 19.54  ? 661  HOH B O   1 
HETATM 5588 O  O   . HOH E 3 .   ? 5.288   -12.719 -6.416  1.00 44.31  ? 662  HOH B O   1 
HETATM 5589 O  O   . HOH E 3 .   ? 9.571   26.095  18.003  1.00 37.93  ? 663  HOH B O   1 
HETATM 5590 O  O   . HOH E 3 .   ? 28.270  23.827  12.349  1.00 35.19  ? 664  HOH B O   1 
HETATM 5591 O  O   . HOH E 3 .   ? 15.256  27.102  14.139  1.00 22.47  ? 665  HOH B O   1 
HETATM 5592 O  O   . HOH E 3 .   ? -12.862 -14.506 -7.594  1.00 53.57  ? 666  HOH B O   1 
HETATM 5593 O  O   . HOH E 3 .   ? 17.111  21.134  7.426   1.00 20.05  ? 667  HOH B O   1 
HETATM 5594 O  O   . HOH E 3 .   ? 21.315  18.446  31.548  1.00 48.13  ? 668  HOH B O   1 
HETATM 5595 O  O   . HOH E 3 .   ? 13.151  16.330  13.818  1.00 12.23  ? 669  HOH B O   1 
HETATM 5596 O  O   . HOH E 3 .   ? 13.173  -8.048  -8.092  1.00 31.40  ? 670  HOH B O   1 
HETATM 5597 O  O   . HOH E 3 .   ? 21.016  6.842   -0.281  1.00 23.25  ? 671  HOH B O   1 
HETATM 5598 O  O   . HOH E 3 .   ? -12.620 6.967   10.990  1.00 37.90  ? 672  HOH B O   1 
HETATM 5599 O  O   . HOH E 3 .   ? -14.765 -8.472  -0.069  1.00 24.47  ? 673  HOH B O   1 
HETATM 5600 O  O   . HOH E 3 .   ? 1.212   4.485   -10.413 1.00 26.61  ? 674  HOH B O   1 
HETATM 5601 O  O   . HOH E 3 .   ? 19.992  3.826   27.645  1.00 28.23  ? 675  HOH B O   1 
HETATM 5602 O  O   . HOH E 3 .   ? 2.343   -11.069 -6.624  1.00 25.22  ? 676  HOH B O   1 
HETATM 5603 O  O   . HOH E 3 .   ? -3.445  1.597   14.810  1.00 16.46  ? 677  HOH B O   1 
HETATM 5604 O  O   . HOH E 3 .   ? 20.056  0.544   14.357  1.00 24.20  ? 678  HOH B O   1 
HETATM 5605 O  O   . HOH E 3 .   ? -13.942 -16.012 -2.140  1.00 34.09  ? 679  HOH B O   1 
HETATM 5606 O  O   . HOH E 3 .   ? -3.888  -15.226 6.044   1.00 12.37  ? 680  HOH B O   1 
HETATM 5607 O  O   . HOH E 3 .   ? -1.613  10.415  -5.034  1.00 23.34  ? 681  HOH B O   1 
HETATM 5608 O  O   . HOH E 3 .   ? 13.114  9.743   30.913  1.00 29.09  ? 682  HOH B O   1 
HETATM 5609 O  O   A HOH E 3 .   ? -11.085 -13.600 7.851   0.52 20.86  ? 683  HOH B O   1 
HETATM 5610 O  O   B HOH E 3 .   ? -11.903 -14.364 8.556   0.48 23.05  ? 683  HOH B O   1 
HETATM 5611 O  O   . HOH E 3 .   ? 11.535  28.082  15.210  1.00 28.63  ? 684  HOH B O   1 
HETATM 5612 O  O   . HOH E 3 .   ? 26.764  2.594   28.498  1.00 39.99  ? 685  HOH B O   1 
HETATM 5613 O  O   . HOH E 3 .   ? 17.564  23.510  6.052   1.00 25.31  ? 686  HOH B O   1 
HETATM 5614 O  O   . HOH E 3 .   ? -11.187 -11.108 -6.637  1.00 30.59  ? 687  HOH B O   1 
HETATM 5615 O  O   . HOH E 3 .   ? 0.064   -9.296  5.228   1.00 13.47  ? 688  HOH B O   1 
HETATM 5616 O  O   . HOH E 3 .   ? 7.387   13.809  -7.928  1.00 46.13  ? 689  HOH B O   1 
HETATM 5617 O  O   . HOH E 3 .   ? 0.165   9.096   -11.444 1.00 58.54  ? 690  HOH B O   1 
HETATM 5618 O  O   . HOH E 3 .   ? 21.498  24.332  5.271   1.00 44.43  ? 691  HOH B O   1 
HETATM 5619 O  O   . HOH E 3 .   ? 14.345  31.271  15.270  1.00 46.97  ? 692  HOH B O   1 
HETATM 5620 O  O   . HOH E 3 .   ? -12.329 -20.780 3.767   1.00 15.38  ? 693  HOH B O   1 
HETATM 5621 O  O   . HOH E 3 .   ? 24.348  28.604  16.721  1.00 36.11  ? 694  HOH B O   1 
HETATM 5622 O  O   . HOH E 3 .   ? -15.974 4.382   12.682  1.00 50.66  ? 695  HOH B O   1 
HETATM 5623 O  O   . HOH E 3 .   ? 22.015  0.235   22.124  1.00 36.10  ? 696  HOH B O   1 
HETATM 5624 O  O   . HOH E 3 .   ? 16.442  -0.302  10.002  1.00 24.35  ? 697  HOH B O   1 
HETATM 5625 O  O   . HOH E 3 .   ? -14.390 4.659   4.547   1.00 48.99  ? 698  HOH B O   1 
HETATM 5626 O  O   . HOH E 3 .   ? -12.807 1.177   -9.500  1.00 43.42  ? 699  HOH B O   1 
HETATM 5627 O  O   . HOH E 3 .   ? 6.157   8.816   -7.002  1.00 27.42  ? 700  HOH B O   1 
HETATM 5628 O  O   . HOH E 3 .   ? 16.198  15.245  31.612  1.00 76.85  ? 701  HOH B O   1 
HETATM 5629 O  O   . HOH E 3 .   ? 16.416  11.321  28.576  1.00 17.76  ? 702  HOH B O   1 
HETATM 5630 O  O   . HOH E 3 .   ? -3.972  -20.505 -0.920  1.00 16.47  ? 703  HOH B O   1 
HETATM 5631 O  O   . HOH E 3 .   ? -6.255  9.855   23.659  1.00 72.30  ? 704  HOH B O   1 
HETATM 5632 O  O   . HOH E 3 .   ? 14.408  9.284   -4.622  1.00 48.13  ? 705  HOH B O   1 
HETATM 5633 O  O   . HOH E 3 .   ? 15.649  28.290  -2.878  1.00 23.15  ? 706  HOH B O   1 
HETATM 5634 O  O   . HOH E 3 .   ? 6.315   20.930  32.083  1.00 24.35  ? 707  HOH B O   1 
HETATM 5635 O  O   . HOH E 3 .   ? 3.036   19.822  1.556   1.00 21.10  ? 708  HOH B O   1 
HETATM 5636 O  O   . HOH E 3 .   ? -14.389 0.715   -1.636  1.00 38.34  ? 709  HOH B O   1 
HETATM 5637 O  O   . HOH E 3 .   ? 4.863   7.038   6.274   1.00 12.79  ? 710  HOH B O   1 
HETATM 5638 O  O   A HOH E 3 .   ? 10.428  25.070  1.133   0.49 13.61  ? 711  HOH B O   1 
HETATM 5639 O  O   B HOH E 3 .   ? 9.159   24.906  1.877   0.51 16.90  ? 711  HOH B O   1 
HETATM 5640 O  O   . HOH E 3 .   ? 4.835   14.888  27.370  1.00 22.57  ? 712  HOH B O   1 
HETATM 5641 O  O   . HOH E 3 .   ? 21.096  -0.028  26.239  1.00 51.21  ? 713  HOH B O   1 
HETATM 5642 O  O   . HOH E 3 .   ? 6.696   -4.886  8.259   1.00 13.31  ? 714  HOH B O   1 
HETATM 5643 O  O   . HOH E 3 .   ? -4.086  9.461   -5.846  1.00 22.38  ? 715  HOH B O   1 
HETATM 5644 O  O   . HOH E 3 .   ? 21.459  27.552  17.042  1.00 24.08  ? 716  HOH B O   1 
HETATM 5645 O  O   . HOH E 3 .   ? 9.245   22.740  5.313   1.00 14.74  ? 717  HOH B O   1 
HETATM 5646 O  O   . HOH E 3 .   ? 0.421   10.074  32.753  1.00 50.91  ? 718  HOH B O   1 
HETATM 5647 O  O   . HOH E 3 .   ? -0.924  -5.029  13.317  1.00 15.37  ? 719  HOH B O   1 
HETATM 5648 O  O   . HOH E 3 .   ? 10.468  31.250  21.518  1.00 32.91  ? 720  HOH B O   1 
HETATM 5649 O  O   . HOH E 3 .   ? -16.888 -23.225 10.455  1.00 48.34  ? 721  HOH B O   1 
HETATM 5650 O  O   . HOH E 3 .   ? -2.140  15.991  25.362  1.00 42.23  ? 722  HOH B O   1 
HETATM 5651 O  O   . HOH E 3 .   ? 14.262  28.086  16.668  1.00 21.06  ? 723  HOH B O   1 
HETATM 5652 O  O   . HOH E 3 .   ? -0.865  18.663  29.364  1.00 42.43  ? 724  HOH B O   1 
HETATM 5653 O  O   . HOH E 3 .   ? 1.786   22.576  26.324  1.00 27.32  ? 725  HOH B O   1 
HETATM 5654 O  O   . HOH E 3 .   ? 32.724  10.073  25.927  1.00 34.52  ? 726  HOH B O   1 
HETATM 5655 O  O   . HOH E 3 .   ? 23.724  32.535  16.646  1.00 65.20  ? 727  HOH B O   1 
HETATM 5656 O  O   . HOH E 3 .   ? 25.712  27.862  22.825  1.00 34.17  ? 728  HOH B O   1 
HETATM 5657 O  O   A HOH E 3 .   ? 12.066  17.284  33.686  0.37 19.03  ? 729  HOH B O   1 
HETATM 5658 O  O   B HOH E 3 .   ? 13.461  16.246  33.022  0.63 34.18  ? 729  HOH B O   1 
HETATM 5659 O  O   . HOH E 3 .   ? 5.292   7.035   29.967  1.00 46.93  ? 730  HOH B O   1 
HETATM 5660 O  O   . HOH E 3 .   ? -15.908 -2.854  -1.247  1.00 53.55  ? 731  HOH B O   1 
HETATM 5661 O  O   . HOH E 3 .   ? 9.322   -4.048  8.552   1.00 20.51  ? 732  HOH B O   1 
HETATM 5662 O  O   . HOH E 3 .   ? 17.877  28.017  9.426   1.00 34.12  ? 733  HOH B O   1 
HETATM 5663 O  O   . HOH E 3 .   ? 11.705  23.520  4.289   1.00 20.35  ? 734  HOH B O   1 
HETATM 5664 O  O   . HOH E 3 .   ? 8.882   -1.407  16.196  1.00 14.69  ? 735  HOH B O   1 
HETATM 5665 O  O   . HOH E 3 .   ? -15.364 -14.577 9.860   1.00 55.30  ? 736  HOH B O   1 
HETATM 5666 O  O   . HOH E 3 .   ? -11.227 5.180   -5.829  1.00 55.43  ? 737  HOH B O   1 
HETATM 5667 O  O   . HOH E 3 .   ? -2.624  1.312   9.873   1.00 23.45  ? 738  HOH B O   1 
HETATM 5668 O  O   . HOH E 3 .   ? 3.757   7.145   13.325  1.00 11.47  ? 739  HOH B O   1 
HETATM 5669 O  O   . HOH E 3 .   ? -9.257  2.508   -5.265  1.00 21.76  ? 740  HOH B O   1 
HETATM 5670 O  O   . HOH E 3 .   ? 8.018   5.849   27.772  1.00 41.28  ? 741  HOH B O   1 
HETATM 5671 O  O   . HOH E 3 .   ? 3.578   20.590  22.985  1.00 23.15  ? 742  HOH B O   1 
HETATM 5672 O  O   . HOH E 3 .   ? 7.801   12.223  11.513  1.00 12.23  ? 743  HOH B O   1 
HETATM 5673 O  O   . HOH E 3 .   ? -2.996  2.636   -5.133  1.00 17.05  ? 744  HOH B O   1 
HETATM 5674 O  O   . HOH E 3 .   ? 23.119  3.086   -3.586  1.00 22.14  ? 745  HOH B O   1 
HETATM 5675 O  O   . HOH E 3 .   ? 28.262  22.777  9.631   1.00 27.52  ? 746  HOH B O   1 
HETATM 5676 O  O   . HOH E 3 .   ? 22.697  18.970  29.459  1.00 27.13  ? 747  HOH B O   1 
HETATM 5677 O  O   . HOH E 3 .   ? 19.318  9.547   32.159  1.00 30.72  ? 748  HOH B O   1 
HETATM 5678 O  O   . HOH E 3 .   ? 22.870  28.080  14.489  1.00 38.78  ? 749  HOH B O   1 
HETATM 5679 O  O   . HOH E 3 .   ? 11.936  -2.940  -9.065  1.00 28.11  ? 750  HOH B O   1 
HETATM 5680 O  O   . HOH E 3 .   ? 26.267  21.114  19.820  1.00 18.40  ? 751  HOH B O   1 
HETATM 5681 O  O   . HOH E 3 .   ? -6.099  0.296   7.161   1.00 20.98  ? 752  HOH B O   1 
HETATM 5682 O  O   . HOH E 3 .   ? 10.911  -4.259  6.199   1.00 13.77  ? 753  HOH B O   1 
HETATM 5683 O  O   . HOH E 3 .   ? -10.805 -4.387  8.509   1.00 34.71  ? 754  HOH B O   1 
HETATM 5684 O  O   . HOH E 3 .   ? 5.953   28.561  31.157  1.00 49.02  ? 755  HOH B O   1 
HETATM 5685 O  O   . HOH E 3 .   ? 9.111   5.130   -7.768  1.00 20.91  ? 756  HOH B O   1 
HETATM 5686 O  O   . HOH E 3 .   ? 7.317   13.543  31.240  1.00 31.81  ? 757  HOH B O   1 
HETATM 5687 O  O   . HOH E 3 .   ? 9.010   4.374   -5.067  1.00 16.31  ? 758  HOH B O   1 
HETATM 5688 O  O   . HOH E 3 .   ? -0.742  20.633  21.694  1.00 44.68  ? 759  HOH B O   1 
HETATM 5689 O  O   . HOH E 3 .   ? -0.060  -2.108  -11.368 1.00 38.08  ? 760  HOH B O   1 
HETATM 5690 O  O   . HOH E 3 .   ? -4.303  17.052  16.166  1.00 47.77  ? 761  HOH B O   1 
HETATM 5691 O  O   . HOH E 3 .   ? 8.436   24.916  11.912  1.00 24.30  ? 762  HOH B O   1 
HETATM 5692 O  O   . HOH E 3 .   ? -17.318 -13.921 1.578   1.00 34.09  ? 763  HOH B O   1 
HETATM 5693 O  O   . HOH E 3 .   ? 18.905  -0.634  7.379   1.00 29.89  ? 764  HOH B O   1 
HETATM 5694 O  O   . HOH E 3 .   ? 15.661  8.383   23.506  1.00 13.65  ? 765  HOH B O   1 
HETATM 5695 O  O   . HOH E 3 .   ? 6.008   13.559  3.614   1.00 15.44  ? 766  HOH B O   1 
HETATM 5696 O  O   . HOH E 3 .   ? 4.783   14.247  -8.659  1.00 51.51  ? 767  HOH B O   1 
HETATM 5697 O  O   . HOH E 3 .   ? 5.439   23.698  12.316  1.00 32.31  ? 768  HOH B O   1 
HETATM 5698 O  O   . HOH E 3 .   ? -12.150 14.001  0.041   1.00 49.03  ? 769  HOH B O   1 
HETATM 5699 O  O   . HOH E 3 .   ? -3.338  16.998  12.056  1.00 22.57  ? 770  HOH B O   1 
HETATM 5700 O  O   . HOH E 3 .   ? 9.322   -13.561 -4.426  1.00 20.12  ? 771  HOH B O   1 
HETATM 5701 O  O   . HOH E 3 .   ? -13.172 -3.700  4.075   1.00 28.04  ? 772  HOH B O   1 
HETATM 5702 O  O   . HOH E 3 .   ? -6.167  -19.761 -2.455  1.00 22.03  ? 773  HOH B O   1 
HETATM 5703 O  O   . HOH E 3 .   ? -9.802  -7.199  7.327   1.00 30.63  ? 774  HOH B O   1 
HETATM 5704 O  O   . HOH E 3 .   ? 2.460   23.493  4.377   1.00 36.88  ? 775  HOH B O   1 
HETATM 5705 O  O   . HOH E 3 .   ? 5.243   18.172  1.412   1.00 21.98  ? 776  HOH B O   1 
HETATM 5706 O  O   . HOH E 3 .   ? 22.146  2.356   19.372  1.00 28.54  ? 777  HOH B O   1 
HETATM 5707 O  O   . HOH E 3 .   ? -1.933  12.652  25.143  1.00 29.80  ? 778  HOH B O   1 
HETATM 5708 O  O   . HOH E 3 .   ? -16.124 -9.220  6.245   1.00 59.99  ? 779  HOH B O   1 
HETATM 5709 O  O   . HOH E 3 .   ? 10.830  14.452  -1.582  1.00 15.24  ? 780  HOH B O   1 
HETATM 5710 O  O   . HOH E 3 .   ? 31.338  4.931   26.655  1.00 29.96  ? 781  HOH B O   1 
HETATM 5711 O  O   . HOH E 3 .   ? 21.066  28.885  7.973   1.00 47.76  ? 782  HOH B O   1 
HETATM 5712 O  O   . HOH E 3 .   ? 4.101   0.732   18.988  1.00 17.37  ? 783  HOH B O   1 
HETATM 5713 O  O   . HOH E 3 .   ? -5.357  14.557  11.790  1.00 38.72  ? 784  HOH B O   1 
HETATM 5714 O  O   . HOH E 3 .   ? 8.434   4.930   25.025  1.00 28.50  ? 785  HOH B O   1 
HETATM 5715 O  O   . HOH E 3 .   ? -1.366  21.973  8.362   1.00 36.75  ? 786  HOH B O   1 
HETATM 5716 O  O   . HOH E 3 .   ? -0.616  -0.061  -7.032  1.00 21.72  ? 787  HOH B O   1 
HETATM 5717 O  O   C HOH E 3 .   ? 22.383  8.426   4.867   0.96 44.12  ? 788  HOH B O   1 
HETATM 5718 O  O   . HOH E 3 .   ? 10.253  16.602  -3.261  1.00 26.56  ? 789  HOH B O   1 
HETATM 5719 O  O   . HOH E 3 .   ? -17.161 -20.273 9.236   1.00 56.96  ? 790  HOH B O   1 
HETATM 5720 O  O   . HOH E 3 .   ? 6.564   -4.037  12.608  1.00 16.29  ? 791  HOH B O   1 
HETATM 5721 O  O   . HOH E 3 .   ? 23.806  22.057  17.494  1.00 16.64  ? 792  HOH B O   1 
HETATM 5722 O  O   . HOH E 3 .   ? 6.233   16.217  3.262   1.00 15.47  ? 793  HOH B O   1 
HETATM 5723 O  O   . HOH E 3 .   ? 1.766   16.695  -3.156  1.00 44.23  ? 794  HOH B O   1 
HETATM 5724 O  O   . HOH E 3 .   ? -15.221 -5.245  -0.062  1.00 52.35  ? 795  HOH B O   1 
HETATM 5725 O  O   . HOH E 3 .   ? 17.649  9.941   22.340  1.00 15.06  ? 796  HOH B O   1 
HETATM 5726 O  O   . HOH E 3 .   ? -4.880  -26.104 10.606  1.00 34.32  ? 797  HOH B O   1 
HETATM 5727 O  O   . HOH E 3 .   ? 17.353  1.038   -10.844 1.00 30.56  ? 798  HOH B O   1 
HETATM 5728 O  O   . HOH E 3 .   ? -3.291  -3.246  10.162  1.00 28.94  ? 799  HOH B O   1 
HETATM 5729 O  O   . HOH E 3 .   ? 5.624   16.273  15.080  1.00 17.90  ? 800  HOH B O   1 
HETATM 5730 O  O   . HOH E 3 .   ? -17.486 -11.512 -4.902  1.00 46.36  ? 801  HOH B O   1 
HETATM 5731 O  O   . HOH E 3 .   ? -8.102  14.534  0.295   1.00 33.66  ? 802  HOH B O   1 
HETATM 5732 O  O   . HOH E 3 .   ? -10.675 -16.611 12.402  1.00 39.78  ? 803  HOH B O   1 
HETATM 5733 O  O   . HOH E 3 .   ? -7.939  -3.305  -12.231 1.00 28.90  ? 804  HOH B O   1 
HETATM 5734 O  O   . HOH E 3 .   ? -13.561 -14.079 -4.546  1.00 21.56  ? 805  HOH B O   1 
HETATM 5735 O  O   . HOH E 3 .   ? 29.607  3.099   20.298  1.00 33.89  ? 806  HOH B O   1 
HETATM 5736 O  O   . HOH E 3 .   ? -4.494  -3.173  14.188  1.00 25.71  ? 807  HOH B O   1 
HETATM 5737 O  O   . HOH E 3 .   ? -4.985  14.292  18.526  1.00 53.96  ? 808  HOH B O   1 
HETATM 5738 O  O   . HOH E 3 .   ? 18.357  24.337  2.915   1.00 46.58  ? 809  HOH B O   1 
HETATM 5739 O  O   . HOH E 3 .   ? 16.128  -5.368  -10.337 1.00 32.01  ? 810  HOH B O   1 
HETATM 5740 O  O   . HOH E 3 .   ? 12.828  10.765  -1.354  1.00 16.56  ? 811  HOH B O   1 
HETATM 5741 O  O   . HOH E 3 .   ? 24.534  8.255   33.246  1.00 40.16  ? 812  HOH B O   1 
HETATM 5742 O  O   . HOH E 3 .   ? 29.510  5.754   34.424  1.00 46.46  ? 813  HOH B O   1 
HETATM 5743 O  O   . HOH E 3 .   ? 9.215   -12.067 -7.811  1.00 30.26  ? 814  HOH B O   1 
HETATM 5744 O  O   . HOH E 3 .   ? -3.515  -0.719  -16.439 1.00 77.87  ? 815  HOH B O   1 
HETATM 5745 O  O   . HOH E 3 .   ? -13.722 -7.217  -10.899 1.00 37.02  ? 816  HOH B O   1 
HETATM 5746 O  O   . HOH E 3 .   ? 5.940   -0.293  -9.099  1.00 43.16  ? 817  HOH B O   1 
HETATM 5747 O  O   . HOH E 3 .   ? 15.188  1.573   -8.090  1.00 39.58  ? 818  HOH B O   1 
HETATM 5748 O  O   A HOH E 3 .   ? 18.833  5.901   -3.439  0.49 19.18  ? 819  HOH B O   1 
HETATM 5749 O  O   B HOH E 3 .   ? 20.297  5.810   -3.505  0.51 22.54  ? 819  HOH B O   1 
HETATM 5750 O  O   . HOH E 3 .   ? -3.108  3.885   17.830  1.00 18.65  ? 820  HOH B O   1 
HETATM 5751 O  O   . HOH E 3 .   ? 13.780  25.249  32.223  1.00 18.11  ? 821  HOH B O   1 
HETATM 5752 O  O   . HOH E 3 .   ? -4.129  2.338   7.069   1.00 19.72  ? 822  HOH B O   1 
HETATM 5753 O  O   . HOH E 3 .   ? -5.165  -7.060  -17.808 1.00 37.51  ? 823  HOH B O   1 
HETATM 5754 O  O   . HOH E 3 .   ? -16.452 -13.361 -1.398  1.00 39.27  ? 824  HOH B O   1 
HETATM 5755 O  O   . HOH E 3 .   ? -9.929  -12.183 -11.585 1.00 34.46  ? 825  HOH B O   1 
HETATM 5756 O  O   . HOH E 3 .   ? -13.965 1.109   2.412   1.00 33.30  ? 826  HOH B O   1 
HETATM 5757 O  O   . HOH E 3 .   ? 25.025  11.100  4.016   1.00 42.95  ? 827  HOH B O   1 
HETATM 5758 O  O   . HOH E 3 .   ? 21.913  11.634  2.401   1.00 36.20  ? 828  HOH B O   1 
HETATM 5759 O  O   . HOH E 3 .   ? -10.240 -6.904  -18.884 1.00 47.86  ? 829  HOH B O   1 
HETATM 5760 O  O   . HOH E 3 .   ? -3.767  12.896  20.453  1.00 28.74  ? 830  HOH B O   1 
HETATM 5761 O  O   . HOH E 3 .   ? 31.262  9.364   23.353  1.00 28.42  ? 831  HOH B O   1 
HETATM 5762 O  O   . HOH E 3 .   ? -15.493 -17.089 12.099  1.00 53.40  ? 832  HOH B O   1 
HETATM 5763 O  O   . HOH E 3 .   ? 30.615  17.574  27.578  1.00 43.72  ? 833  HOH B O   1 
HETATM 5764 O  O   . HOH E 3 .   ? 15.208  13.651  29.595  1.00 21.52  ? 834  HOH B O   1 
HETATM 5765 O  O   . HOH E 3 .   ? 10.025  -4.819  -9.233  1.00 35.78  ? 835  HOH B O   1 
HETATM 5766 O  O   . HOH E 3 .   ? -4.858  20.557  10.432  1.00 39.57  ? 836  HOH B O   1 
HETATM 5767 O  O   . HOH E 3 .   ? 26.792  12.543  3.674   1.00 64.78  ? 837  HOH B O   1 
HETATM 5768 O  O   . HOH E 3 .   ? 17.001  21.861  0.476   1.00 25.82  ? 838  HOH B O   1 
HETATM 5769 O  O   A HOH E 3 .   ? 15.872  14.708  4.161   0.66 19.76  ? 839  HOH B O   1 
HETATM 5770 O  O   B HOH E 3 .   ? 15.926  15.502  2.641   0.34 21.33  ? 839  HOH B O   1 
HETATM 5771 O  O   . HOH E 3 .   ? -3.678  11.359  14.361  1.00 27.76  ? 840  HOH B O   1 
HETATM 5772 O  O   . HOH E 3 .   ? 18.324  26.630  -0.773  1.00 62.75  ? 841  HOH B O   1 
HETATM 5773 O  O   . HOH E 3 .   ? -9.040  2.344   -12.696 1.00 30.86  ? 842  HOH B O   1 
HETATM 5774 O  O   . HOH E 3 .   ? 6.559   13.893  34.956  1.00 56.85  ? 843  HOH B O   1 
HETATM 5775 O  O   . HOH E 3 .   ? 29.327  13.533  13.155  1.00 47.03  ? 844  HOH B O   1 
HETATM 5776 O  O   . HOH E 3 .   ? 32.024  23.291  14.092  1.00 59.93  ? 845  HOH B O   1 
HETATM 5777 O  O   . HOH E 3 .   ? -8.456  2.102   14.268  1.00 43.38  ? 846  HOH B O   1 
HETATM 5778 O  O   . HOH E 3 .   ? -16.971 -17.687 10.135  1.00 51.45  ? 847  HOH B O   1 
HETATM 5779 O  O   . HOH E 3 .   ? 8.963   20.624  32.226  1.00 26.79  ? 848  HOH B O   1 
HETATM 5780 O  O   . HOH E 3 .   ? 15.234  13.087  0.816   1.00 25.35  ? 849  HOH B O   1 
HETATM 5781 O  O   . HOH E 3 .   ? -2.738  1.296   -14.368 1.00 50.89  ? 850  HOH B O   1 
HETATM 5782 O  O   . HOH E 3 .   ? 11.675  0.472   22.542  0.79 24.51  ? 851  HOH B O   1 
HETATM 5783 O  O   . HOH E 3 .   ? -2.198  17.495  -6.468  1.00 55.85  ? 852  HOH B O   1 
HETATM 5784 O  O   . HOH E 3 .   ? 27.071  6.903   14.882  1.00 35.43  ? 853  HOH B O   1 
HETATM 5785 O  O   . HOH E 3 .   ? 15.775  7.573   -3.242  1.00 27.87  ? 854  HOH B O   1 
HETATM 5786 O  O   . HOH E 3 .   ? 15.909  34.140  11.757  1.00 54.24  ? 855  HOH B O   1 
HETATM 5787 O  O   . HOH E 3 .   ? 25.801  25.755  11.321  1.00 40.35  ? 856  HOH B O   1 
HETATM 5788 O  O   . HOH E 3 .   ? 7.261   13.911  28.517  1.00 25.57  ? 857  HOH B O   1 
HETATM 5789 O  O   . HOH E 3 .   ? 19.034  7.785   21.293  1.00 18.15  ? 858  HOH B O   1 
HETATM 5790 O  O   C HOH E 3 .   ? 22.897  9.845   28.153  0.53 19.05  ? 859  HOH B O   1 
HETATM 5791 O  O   . HOH E 3 .   ? 1.847   24.001  7.152   1.00 26.69  ? 860  HOH B O   1 
HETATM 5792 O  O   . HOH E 3 .   ? 4.047   25.599  8.992   1.00 34.44  ? 861  HOH B O   1 
HETATM 5793 O  O   . HOH E 3 .   ? -0.184  11.988  -6.850  1.00 39.64  ? 862  HOH B O   1 
HETATM 5794 O  O   . HOH E 3 .   ? -2.751  10.602  -9.617  1.00 55.50  ? 863  HOH B O   1 
HETATM 5795 O  O   . HOH E 3 .   ? -6.500  1.036   -11.337 1.00 40.83  ? 864  HOH B O   1 
HETATM 5796 O  O   . HOH E 3 .   ? 7.229   1.631   18.612  1.00 26.26  ? 865  HOH B O   1 
HETATM 5797 O  O   . HOH E 3 .   ? -0.763  22.575  4.630   1.00 34.23  ? 866  HOH B O   1 
HETATM 5798 O  O   . HOH E 3 .   ? 3.723   17.650  -1.153  1.00 26.67  ? 867  HOH B O   1 
HETATM 5799 O  O   . HOH E 3 .   ? 14.600  32.086  8.523   1.00 44.78  ? 868  HOH B O   1 
HETATM 5800 O  O   . HOH E 3 .   ? 1.351   6.295   12.257  1.00 12.47  ? 869  HOH B O   1 
HETATM 5801 O  O   . HOH E 3 .   ? -4.142  -12.633 10.201  1.00 23.23  ? 870  HOH B O   1 
HETATM 5802 O  O   . HOH E 3 .   ? 18.813  -1.594  15.750  1.00 26.39  ? 871  HOH B O   1 
HETATM 5803 O  O   . HOH E 3 .   ? 6.450   6.356   -7.923  1.00 25.08  ? 872  HOH B O   1 
HETATM 5804 O  O   . HOH E 3 .   ? 8.963   30.242  23.846  1.00 34.27  ? 873  HOH B O   1 
HETATM 5805 O  O   . HOH E 3 .   ? 16.410  31.398  25.570  1.00 35.46  ? 874  HOH B O   1 
HETATM 5806 O  O   . HOH E 3 .   ? 16.289  7.957   -0.503  1.00 18.59  ? 875  HOH B O   1 
HETATM 5807 O  O   . HOH E 3 .   ? -4.914  20.521  5.983   1.00 24.04  ? 876  HOH B O   1 
HETATM 5808 O  O   . HOH E 3 .   ? 2.517   25.202  18.750  1.00 60.08  ? 877  HOH B O   1 
HETATM 5809 O  O   . HOH E 3 .   ? -13.775 -2.824  -16.746 1.00 63.58  ? 878  HOH B O   1 
HETATM 5810 O  O   . HOH E 3 .   ? 12.547  29.737  29.979  1.00 46.60  ? 879  HOH B O   1 
HETATM 5811 O  O   . HOH E 3 .   ? 21.471  32.037  23.322  1.00 31.93  ? 880  HOH B O   1 
HETATM 5812 O  O   . HOH E 3 .   ? 19.179  25.337  6.636   1.00 38.11  ? 881  HOH B O   1 
HETATM 5813 O  O   . HOH E 3 .   ? 14.635  9.896   0.625   1.00 16.95  ? 882  HOH B O   1 
HETATM 5814 O  O   C HOH E 3 .   ? 18.715  1.356   1.476   0.97 30.78  ? 883  HOH B O   1 
HETATM 5815 O  O   . HOH E 3 .   ? -1.365  18.586  0.422   1.00 41.44  ? 884  HOH B O   1 
HETATM 5816 O  O   . HOH E 3 .   ? 28.629  3.098   23.085  1.00 30.73  ? 885  HOH B O   1 
HETATM 5817 O  O   . HOH E 3 .   ? -8.726  -14.046 11.451  1.00 41.58  ? 886  HOH B O   1 
HETATM 5818 O  O   . HOH E 3 .   ? 7.528   5.086   -10.846 1.00 46.20  ? 887  HOH B O   1 
HETATM 5819 O  O   . HOH E 3 .   ? -0.062  -4.185  -14.547 1.00 57.37  ? 888  HOH B O   1 
HETATM 5820 O  O   . HOH E 3 .   ? 2.384   12.474  -8.853  1.00 43.59  ? 889  HOH B O   1 
HETATM 5821 O  O   . HOH E 3 .   ? -0.636  20.736  27.792  1.00 45.43  ? 890  HOH B O   1 
HETATM 5822 O  O   . HOH E 3 .   ? 28.764  19.689  19.285  1.00 43.23  ? 891  HOH B O   1 
HETATM 5823 O  O   . HOH E 3 .   ? 23.860  31.722  14.164  1.00 48.11  ? 892  HOH B O   1 
HETATM 5824 O  O   . HOH E 3 .   ? -4.699  20.168  -0.833  1.00 29.92  ? 893  HOH B O   1 
HETATM 5825 O  O   . HOH E 3 .   ? -9.851  10.988  -8.070  1.00 44.63  ? 894  HOH B O   1 
HETATM 5826 O  O   . HOH E 3 .   ? -4.061  11.708  -7.589  1.00 50.76  ? 895  HOH B O   1 
HETATM 5827 O  O   . HOH E 3 .   ? -3.833  13.002  23.197  1.00 57.68  ? 896  HOH B O   1 
HETATM 5828 O  O   . HOH E 3 .   ? 7.697   2.829   -10.953 1.00 55.93  ? 897  HOH B O   1 
HETATM 5829 O  O   . HOH E 3 .   ? 7.525   24.659  4.573   1.00 28.35  ? 898  HOH B O   1 
HETATM 5830 O  O   . HOH E 3 .   ? 0.681   19.329  34.362  1.00 36.79  ? 899  HOH B O   1 
HETATM 5831 O  O   . HOH E 3 .   ? 1.864   21.640  15.747  1.00 39.71  ? 900  HOH B O   1 
HETATM 5832 O  O   . HOH E 3 .   ? 30.439  16.130  9.026   1.00 48.62  ? 901  HOH B O   1 
HETATM 5833 O  O   . HOH E 3 .   ? -16.266 -3.370  12.282  1.00 54.55  ? 902  HOH B O   1 
HETATM 5834 O  O   . HOH E 3 .   ? 20.468  17.745  29.533  1.00 60.99  ? 903  HOH B O   1 
HETATM 5835 O  O   . HOH E 3 .   ? 0.314   26.392  22.028  1.00 55.37  ? 904  HOH B O   1 
HETATM 5836 O  O   . HOH E 3 .   ? -0.397  -8.482  10.221  1.00 34.25  ? 905  HOH B O   1 
HETATM 5837 O  O   . HOH E 3 .   ? 21.992  4.902   30.864  1.00 53.99  ? 906  HOH B O   1 
HETATM 5838 O  O   . HOH E 3 .   ? -4.967  3.584   -10.874 1.00 14.53  ? 907  HOH B O   1 
HETATM 5839 O  O   . HOH E 3 .   ? 21.549  11.160  -0.098  1.00 56.77  ? 908  HOH B O   1 
HETATM 5840 O  O   . HOH E 3 .   ? -5.394  7.700   20.371  1.00 45.48  ? 909  HOH B O   1 
HETATM 5841 O  O   . HOH E 3 .   ? 25.334  -4.577  -9.421  1.00 36.87  ? 910  HOH B O   1 
HETATM 5842 O  O   . HOH E 3 .   ? -6.312  -7.824  9.701   1.00 65.39  ? 911  HOH B O   1 
HETATM 5843 O  O   . HOH E 3 .   ? 26.151  7.455   12.035  1.00 44.79  ? 912  HOH B O   1 
HETATM 5844 O  O   . HOH E 3 .   ? -18.674 7.293   12.702  1.00 62.05  ? 913  HOH B O   1 
HETATM 5845 O  O   . HOH E 3 .   ? 3.883   3.709   26.927  1.00 62.68  ? 914  HOH B O   1 
HETATM 5846 O  O   . HOH E 3 .   ? -6.808  -11.200 6.663   1.00 34.29  ? 915  HOH B O   1 
HETATM 5847 O  O   . HOH E 3 .   ? 24.587  4.785   1.285   1.00 65.68  ? 916  HOH B O   1 
HETATM 5848 O  O   . HOH E 3 .   ? 30.207  12.824  34.621  1.00 60.08  ? 917  HOH B O   1 
HETATM 5849 O  O   . HOH E 3 .   ? -6.707  21.781  7.455   1.00 49.71  ? 918  HOH B O   1 
HETATM 5850 O  O   . HOH E 3 .   ? -15.959 -2.094  8.297   1.00 47.27  ? 919  HOH B O   1 
HETATM 5851 O  O   C HOH E 3 .   ? 1.561   22.034  21.792  1.00 34.05  ? 920  HOH B O   1 
HETATM 5852 O  O   . HOH E 3 .   ? -6.773  -11.683 10.399  1.00 58.16  ? 921  HOH B O   1 
HETATM 5853 O  O   . HOH E 3 .   ? 5.121   -3.873  10.218  1.00 16.26  ? 922  HOH B O   1 
HETATM 5854 O  O   . HOH E 3 .   ? -15.501 -13.436 -6.159  1.00 63.45  ? 923  HOH B O   1 
HETATM 5855 O  O   . HOH E 3 .   ? 18.711  7.827   -1.785  1.00 28.64  ? 924  HOH B O   1 
HETATM 5856 O  O   . HOH E 3 .   ? -10.504 3.900   15.071  1.00 81.08  ? 925  HOH B O   1 
HETATM 5857 O  O   . HOH E 3 .   ? 19.019  23.695  0.412   1.00 44.76  ? 926  HOH B O   1 
HETATM 5858 O  O   . HOH E 3 .   ? 5.472   22.280  39.506  1.00 65.75  ? 927  HOH B O   1 
HETATM 5859 O  O   . HOH E 3 .   ? 7.230   -4.525  -10.614 1.00 63.04  ? 928  HOH B O   1 
HETATM 5860 O  O   . HOH E 3 .   ? -4.197  -0.880  9.047   1.00 26.75  ? 929  HOH B O   1 
HETATM 5861 O  O   . HOH E 3 .   ? -0.964  22.173  18.195  1.00 51.02  ? 930  HOH B O   1 
HETATM 5862 O  O   . HOH E 3 .   ? 31.146  4.691   23.955  1.00 43.19  ? 931  HOH B O   1 
HETATM 5863 O  O   B HOH E 3 .   ? 18.221  -3.827  23.871  1.00 56.05  ? 932  HOH B O   1 
HETATM 5864 O  O   . HOH E 3 .   ? 26.976  25.020  25.010  1.00 41.80  ? 933  HOH B O   1 
HETATM 5865 O  O   . HOH E 3 .   ? -6.275  -29.783 10.630  1.00 63.36  ? 934  HOH B O   1 
HETATM 5866 O  O   . HOH E 3 .   ? -5.115  13.494  14.133  1.00 52.71  ? 935  HOH B O   1 
HETATM 5867 O  O   . HOH E 3 .   ? -8.300  -9.448  10.684  1.00 67.78  ? 936  HOH B O   1 
HETATM 5868 O  O   . HOH E 3 .   ? 24.407  0.337   23.563  1.00 43.49  ? 937  HOH B O   1 
HETATM 5869 O  O   . HOH E 3 .   ? -13.266 -29.501 5.721   1.00 50.41  ? 938  HOH B O   1 
HETATM 5870 O  O   . HOH E 3 .   ? 21.243  35.268  14.652  1.00 57.11  ? 939  HOH B O   1 
HETATM 5871 O  O   . HOH E 3 .   ? 24.675  8.574   5.794   1.00 47.19  ? 940  HOH B O   1 
HETATM 5872 O  O   . HOH E 3 .   ? -4.670  -5.693  11.046  1.00 56.03  ? 941  HOH B O   1 
HETATM 5873 O  O   . HOH E 3 .   ? -13.195 -7.589  6.226   1.00 53.62  ? 942  HOH B O   1 
HETATM 5874 O  O   . HOH E 3 .   ? 0.251   6.561   -11.874 1.00 51.66  ? 943  HOH B O   1 
HETATM 5875 O  O   B HOH E 3 .   ? -14.985 0.365   -7.476  1.00 54.27  ? 944  HOH B O   1 
HETATM 5876 O  O   . HOH E 3 .   ? -14.179 -0.993  3.711   1.00 44.59  ? 945  HOH B O   1 
HETATM 5877 O  O   . HOH E 3 .   ? -2.442  19.268  13.064  1.00 33.10  ? 946  HOH B O   1 
HETATM 5878 O  O   A HOH E 3 .   ? -2.878  8.953   28.093  0.71 46.01  ? 947  HOH B O   1 
HETATM 5879 O  O   B HOH E 3 .   ? -4.185  8.964   27.277  0.29 34.84  ? 947  HOH B O   1 
HETATM 5880 O  O   . HOH E 3 .   ? 5.776   6.540   -10.803 1.00 44.30  ? 948  HOH B O   1 
HETATM 5881 O  O   . HOH E 3 .   ? -16.143 -2.898  1.345   1.00 59.13  ? 949  HOH B O   1 
HETATM 5882 O  O   . HOH E 3 .   ? -7.804  -8.960  7.690   1.00 42.87  ? 950  HOH B O   1 
HETATM 5883 O  O   . HOH E 3 .   ? -4.527  -12.804 7.389   1.00 24.14  ? 951  HOH B O   1 
HETATM 5884 O  O   . HOH E 3 .   ? -5.756  -7.797  11.852  1.00 60.66  ? 952  HOH B O   1 
HETATM 5885 O  O   A HOH E 3 .   ? 6.756   2.041   23.141  0.85 24.51  ? 953  HOH B O   1 
HETATM 5886 O  O   B HOH E 3 .   ? 7.497   2.750   24.373  0.15 11.13  ? 953  HOH B O   1 
HETATM 5887 O  O   . HOH E 3 .   ? 15.282  33.719  14.034  1.00 48.02  ? 954  HOH B O   1 
HETATM 5888 O  O   . HOH E 3 .   ? 20.820  23.926  -3.444  1.00 49.54  ? 955  HOH B O   1 
HETATM 5889 O  O   . HOH E 3 .   ? -17.217 14.654  12.221  1.00 59.56  ? 956  HOH B O   1 
HETATM 5890 O  O   . HOH E 3 .   ? 9.962   33.714  21.608  1.00 46.65  ? 957  HOH B O   1 
HETATM 5891 O  O   . HOH E 3 .   ? 6.261   4.912   26.743  1.00 62.88  ? 958  HOH B O   1 
HETATM 5892 O  O   . HOH E 3 .   ? 12.828  31.169  27.619  1.00 57.09  ? 959  HOH B O   1 
HETATM 5893 O  O   . HOH E 3 .   ? -12.940 -1.421  18.709  1.00 53.44  ? 960  HOH B O   1 
HETATM 5894 O  O   . HOH E 3 .   ? 3.647   4.940   -11.357 1.00 51.67  ? 961  HOH B O   1 
HETATM 5895 O  O   . HOH E 3 .   ? 25.714  27.624  13.438  1.00 48.92  ? 962  HOH B O   1 
HETATM 5896 O  O   . HOH E 3 .   ? -12.809 17.913  -6.205  1.00 42.28  ? 963  HOH B O   1 
HETATM 5897 O  O   A HOH E 3 .   ? 3.086   -5.425  -9.789  0.66 43.02  ? 964  HOH B O   1 
HETATM 5898 O  O   B HOH E 3 .   ? 4.540   -4.625  -10.438 0.34 37.47  ? 964  HOH B O   1 
HETATM 5899 O  O   . HOH E 3 .   ? 29.712  17.751  16.870  1.00 58.22  ? 965  HOH B O   1 
HETATM 5900 O  O   . HOH E 3 .   ? -6.727  4.176   -13.489 1.00 42.51  ? 966  HOH B O   1 
HETATM 5901 O  O   . HOH E 3 .   ? 14.926  11.943  -4.810  1.00 48.50  ? 967  HOH B O   1 
HETATM 5902 O  O   . HOH E 3 .   ? -13.018 -8.634  -14.067 1.00 49.83  ? 968  HOH B O   1 
HETATM 5903 O  O   . HOH E 3 .   ? 11.233  14.775  -9.480  1.00 66.53  ? 969  HOH B O   1 
HETATM 5904 O  O   . HOH E 3 .   ? 24.099  15.721  31.187  1.00 40.64  ? 970  HOH B O   1 
HETATM 5905 O  O   . HOH E 3 .   ? -13.577 -12.950 9.271   1.00 58.00  ? 971  HOH B O   1 
HETATM 5906 O  O   . HOH E 3 .   ? 28.621  15.077  16.530  1.00 51.10  ? 972  HOH B O   1 
HETATM 5907 O  O   . HOH E 3 .   ? -13.277 -4.945  6.350   1.00 44.82  ? 973  HOH B O   1 
HETATM 5908 O  O   . HOH E 3 .   ? 28.050  15.752  13.012  1.00 42.68  ? 974  HOH B O   1 
HETATM 5909 O  O   . HOH E 3 .   ? 24.319  6.160   15.994  1.00 43.70  ? 975  HOH B O   1 
HETATM 5910 O  O   . HOH E 3 .   ? -9.082  8.128   11.889  1.00 34.57  ? 976  HOH B O   1 
HETATM 5911 O  O   . HOH E 3 .   ? -15.470 14.330  14.591  1.00 58.49  ? 977  HOH B O   1 
HETATM 5912 O  O   . HOH E 3 .   ? 13.137  -1.492  -10.975 1.00 37.72  ? 978  HOH B O   1 
HETATM 5913 O  O   . HOH E 3 .   ? -9.550  -12.384 8.867   1.00 35.11  ? 979  HOH B O   1 
HETATM 5914 O  O   . HOH E 3 .   ? 29.820  25.025  10.823  1.00 50.38  ? 980  HOH B O   1 
HETATM 5915 O  O   . HOH E 3 .   ? 6.606   -0.915  18.023  1.00 21.37  ? 981  HOH B O   1 
HETATM 5916 O  O   . HOH E 3 .   ? -4.391  15.371  22.492  1.00 52.52  ? 982  HOH B O   1 
HETATM 5917 O  O   . HOH E 3 .   ? 21.845  15.898  31.079  1.00 50.83  ? 983  HOH B O   1 
HETATM 5918 O  O   . HOH E 3 .   ? 19.704  10.198  -2.563  1.00 57.36  ? 984  HOH B O   1 
HETATM 5919 O  O   . HOH E 3 .   ? 13.472  13.540  -1.496  1.00 19.43  ? 985  HOH B O   1 
HETATM 5920 O  O   . HOH E 3 .   ? -0.964  21.196  2.063   1.00 54.70  ? 986  HOH B O   1 
HETATM 5921 O  O   . HOH E 3 .   ? -2.268  3.082   -12.178 1.00 39.55  ? 987  HOH B O   1 
HETATM 5922 O  O   . HOH E 3 .   ? 18.386  7.467   33.662  1.00 50.28  ? 988  HOH B O   1 
HETATM 5923 O  O   . HOH E 3 .   ? 1.399   -18.962 -5.155  1.00 59.55  ? 989  HOH B O   1 
HETATM 5924 O  O   C HOH E 3 .   ? 2.262   22.674  18.800  0.70 38.07  ? 990  HOH B O   1 
HETATM 5925 O  O   . HOH E 3 .   ? -1.973  6.278   34.687  1.00 52.37  ? 991  HOH B O   1 
HETATM 5926 O  O   . HOH E 3 .   ? 22.272  1.005   15.714  1.00 57.45  ? 992  HOH B O   1 
HETATM 5927 O  O   . HOH E 3 .   ? -2.557  -9.087  10.524  1.00 35.54  ? 993  HOH B O   1 
HETATM 5928 O  O   . HOH E 3 .   ? 23.434  2.799   17.147  1.00 56.12  ? 994  HOH B O   1 
HETATM 5929 O  O   . HOH E 3 .   ? -4.775  11.468  25.536  1.00 73.35  ? 995  HOH B O   1 
HETATM 5930 O  O   . HOH E 3 .   ? 17.155  34.378  9.054   1.00 52.71  ? 996  HOH B O   1 
HETATM 5931 O  O   . HOH E 3 .   ? -8.057  -2.724  17.451  1.00 46.84  ? 997  HOH B O   1 
HETATM 5932 O  O   . HOH E 3 .   ? 10.329  31.691  25.793  1.00 45.68  ? 998  HOH B O   1 
HETATM 5933 O  O   . HOH E 3 .   ? -7.007  5.623   26.190  1.00 56.31  ? 999  HOH B O   1 
HETATM 5934 O  O   . HOH E 3 .   ? -6.399  16.481  18.618  1.00 54.11  ? 1000 HOH B O   1 
HETATM 5935 O  O   . HOH E 3 .   ? 0.261   2.074   -11.224 1.00 29.61  ? 1001 HOH B O   1 
HETATM 5936 O  O   . HOH E 3 .   ? -6.179  8.005   27.473  1.00 63.50  ? 1002 HOH B O   1 
HETATM 5937 O  O   . HOH E 3 .   ? -5.121  16.525  13.903  1.00 65.54  ? 1003 HOH B O   1 
HETATM 5938 O  O   . HOH E 3 .   ? 17.564  11.098  31.177  1.00 24.41  ? 1004 HOH B O   1 
HETATM 5939 O  O   . HOH E 3 .   ? 22.603  1.028   7.396   1.00 58.88  ? 1005 HOH B O   1 
HETATM 5940 O  O   . HOH E 3 .   ? 11.445  -6.740  -9.654  1.00 39.84  ? 1006 HOH B O   1 
HETATM 5941 O  O   . HOH E 3 .   ? -9.298  -0.723  19.229  1.00 40.22  ? 1007 HOH B O   1 
HETATM 5942 O  O   . HOH E 3 .   ? 0.763   -0.177  -9.504  1.00 31.79  ? 1008 HOH B O   1 
HETATM 5943 O  O   A HOH E 3 .   ? 4.374   -2.686  -10.142 1.00 61.71  ? 1009 HOH B O   1 
HETATM 5944 O  O   . HOH E 3 .   ? 2.616   9.268   -11.563 1.00 55.22  ? 1010 HOH B O   1 
HETATM 5945 O  O   . HOH E 3 .   ? 25.936  7.038   7.060   1.00 44.00  ? 1011 HOH B O   1 
HETATM 5946 O  O   . HOH E 3 .   ? 22.360  -2.776  25.955  1.00 49.27  ? 1012 HOH B O   1 
HETATM 5947 O  O   . HOH E 3 .   ? -7.110  10.793  -11.860 1.00 51.43  ? 1013 HOH B O   1 
HETATM 5948 O  O   . HOH E 3 .   ? -18.109 -11.841 -2.568  1.00 46.69  ? 1014 HOH B O   1 
HETATM 5949 O  O   . HOH E 3 .   ? -3.414  16.454  29.974  1.00 48.51  ? 1015 HOH B O   1 
HETATM 5950 O  O   . HOH E 3 .   ? 23.481  1.201   25.951  1.00 36.13  ? 1016 HOH B O   1 
HETATM 5951 O  O   . HOH E 3 .   ? -13.709 12.430  -5.053  1.00 50.98  ? 1017 HOH B O   1 
HETATM 5952 O  O   . HOH E 3 .   ? -15.616 -0.126  6.174   1.00 55.08  ? 1018 HOH B O   1 
HETATM 5953 O  O   . HOH E 3 .   ? 29.459  0.644   19.572  1.00 47.21  ? 1019 HOH B O   1 
HETATM 5954 O  O   . HOH E 3 .   ? 4.813   8.743   -11.102 1.00 57.29  ? 1020 HOH B O   1 
HETATM 5955 O  O   . HOH E 3 .   ? -3.247  22.257  6.032   1.00 50.58  ? 1021 HOH B O   1 
HETATM 5956 O  O   . HOH E 3 .   ? 18.071  13.456  32.295  1.00 49.59  ? 1022 HOH B O   1 
HETATM 5957 O  O   . HOH E 3 .   ? 23.994  2.941   29.114  1.00 38.21  ? 1023 HOH B O   1 
HETATM 5958 O  O   . HOH E 3 .   ? 15.115  10.616  32.749  1.00 38.58  ? 1024 HOH B O   1 
HETATM 5959 O  O   . HOH E 3 .   ? -5.476  3.491   14.735  1.00 34.08  ? 1025 HOH B O   1 
HETATM 5960 O  O   . HOH E 3 .   ? 22.841  6.708   -2.254  1.00 40.69  ? 1026 HOH B O   1 
HETATM 5961 O  O   . HOH E 3 .   ? 5.335   10.931  -8.898  1.00 39.47  ? 1027 HOH B O   1 
HETATM 5962 O  O   . HOH E 3 .   ? -14.195 6.349   -4.638  1.00 49.19  ? 1028 HOH B O   1 
HETATM 5963 O  O   . HOH E 3 .   ? -15.015 -10.315 8.421   1.00 52.48  ? 1029 HOH B O   1 
HETATM 5964 O  O   . HOH E 3 .   ? 3.095   25.357  12.813  1.00 46.79  ? 1030 HOH B O   1 
HETATM 5965 O  O   . HOH E 3 .   ? -12.404 8.106   -6.874  1.00 43.37  ? 1031 HOH B O   1 
HETATM 5966 O  O   . HOH E 3 .   ? -14.817 -31.215 3.531   1.00 35.25  ? 1032 HOH B O   1 
HETATM 5967 O  O   . HOH E 3 .   ? 1.559   23.733  14.820  1.00 63.47  ? 1033 HOH B O   1 
HETATM 5968 O  O   . HOH E 3 .   ? -6.054  9.665   17.198  1.00 49.76  ? 1034 HOH B O   1 
HETATM 5969 O  O   . HOH E 3 .   ? -12.399 -8.049  8.545   1.00 58.95  ? 1035 HOH B O   1 
HETATM 5970 O  O   . HOH E 3 .   ? 1.148   18.803  -0.461  1.00 48.77  ? 1036 HOH B O   1 
HETATM 5971 O  O   . HOH E 3 .   ? 25.558  0.423   27.893  1.00 55.62  ? 1037 HOH B O   1 
HETATM 5972 O  O   . HOH E 3 .   ? -5.220  11.035  19.918  1.00 43.19  ? 1038 HOH B O   1 
HETATM 5973 O  O   . HOH E 3 .   ? 2.750   20.352  41.730  1.00 57.67  ? 1039 HOH B O   1 
HETATM 5974 O  O   . HOH E 3 .   ? 17.426  35.446  14.575  1.00 50.89  ? 1040 HOH B O   1 
HETATM 5975 O  O   . HOH E 3 .   ? 11.987  11.232  35.449  1.00 53.51  ? 1041 HOH B O   1 
HETATM 5976 O  O   . HOH E 3 .   ? 28.417  9.256   5.083   1.00 51.12  ? 1042 HOH B O   1 
HETATM 5977 O  O   . HOH E 3 .   ? 14.231  12.598  34.522  1.00 48.00  ? 1043 HOH B 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   . LYS A 2   ? 0.7858 0.6052 0.6441 -0.1357 0.0522  0.0290  225  LYS A N   
2    C CA  . LYS A 2   ? 0.7721 0.6024 0.6264 -0.1185 0.0374  0.0234  225  LYS A CA  
3    C C   . LYS A 2   ? 0.8331 0.5175 0.5359 -0.0981 0.0051  0.0101  225  LYS A C   
4    O O   . LYS A 2   ? 0.8545 0.5120 0.5400 -0.0872 0.0093  0.0174  225  LYS A O   
7    N N   . PRO A 3   ? 0.8637 0.4344 0.4449 -0.0679 -0.0249 -0.0169 226  PRO A N   
8    C CA  . PRO A 3   ? 0.8817 0.3816 0.3944 -0.0684 -0.0296 -0.0317 226  PRO A CA  
9    C C   . PRO A 3   ? 0.9058 0.3273 0.3335 -0.1018 -0.0447 -0.0598 226  PRO A C   
10   O O   . PRO A 3   ? 0.9344 0.3233 0.3484 -0.1268 -0.0317 -0.0607 226  PRO A O   
11   C CB  . PRO A 3   ? 0.8744 0.3830 0.3945 -0.0514 -0.0310 -0.0274 226  PRO A CB  
12   C CG  . PRO A 3   ? 0.8735 0.4039 0.4179 -0.0454 -0.0316 -0.0187 226  PRO A CG  
13   C CD  . PRO A 3   ? 0.8708 0.4207 0.4335 -0.0455 -0.0248 -0.0154 226  PRO A CD  
14   N N   . PHE A 4   ? 0.8610 0.2879 0.2906 -0.0851 -0.0569 -0.0540 227  PHE A N   
15   C CA  . PHE A 4   ? 0.8186 0.2601 0.2543 -0.0489 -0.0704 -0.0376 227  PHE A CA  
16   C C   . PHE A 4   ? 0.8190 0.2506 0.2488 -0.0091 -0.0353 -0.0427 227  PHE A C   
17   O O   . PHE A 4   ? 0.8541 0.2557 0.2679 0.0175  -0.0168 -0.0476 227  PHE A O   
18   C CB  . PHE A 4   ? 0.7769 0.2396 0.2457 -0.0346 -0.0997 -0.0276 227  PHE A CB  
19   C CG  . PHE A 4   ? 0.7069 0.2096 0.2262 -0.0157 -0.1142 -0.0182 227  PHE A CG  
20   C CD1 . PHE A 4   ? 0.6853 0.2027 0.2549 -0.0036 -0.1428 -0.0122 227  PHE A CD1 
21   C CD2 . PHE A 4   ? 0.7044 0.2165 0.2463 0.0046  -0.0830 -0.0123 227  PHE A CD2 
22   C CE1 . PHE A 4   ? 0.6542 0.1871 0.2714 0.0238  -0.1306 -0.0055 227  PHE A CE1 
23   C CE2 . PHE A 4   ? 0.6773 0.2038 0.2594 0.0215  -0.1084 -0.0137 227  PHE A CE2 
24   C CZ  . PHE A 4   ? 0.6584 0.1881 0.2404 0.0399  -0.1275 -0.0102 227  PHE A CZ  
25   N N   . THR A 5   ? 0.7848 0.2186 0.2312 0.0151  -0.0226 -0.0276 228  THR A N   
26   C CA  . THR A 5   ? 0.7334 0.1957 0.2296 0.0553  -0.0158 -0.0168 228  THR A CA  
27   C C   . THR A 5   ? 0.6730 0.1868 0.2067 0.0804  -0.0559 -0.0134 228  THR A C   
28   O O   . THR A 5   ? 0.6625 0.1916 0.2277 0.0644  -0.0403 -0.0335 228  THR A O   
29   C CB  . THR A 5   ? 0.7489 0.1992 0.2456 0.0626  0.0354  -0.0079 228  THR A CB  
30   O OG1 . THR A 5   ? 0.7629 0.2045 0.2662 0.0706  0.0642  0.0009  228  THR A OG1 
31   C CG2 . THR A 5   ? 0.7462 0.2076 0.2363 0.0509  0.0352  -0.0228 228  THR A CG2 
32   N N   . ILE A 6   ? 0.6330 0.1980 0.1842 0.1053  -0.0639 -0.0060 229  ILE A N   
33   C CA  . ILE A 6   ? 0.5770 0.2202 0.1767 0.1123  -0.0683 -0.0089 229  ILE A CA  
34   C C   . ILE A 6   ? 0.5079 0.2419 0.1887 0.1341  -0.0293 -0.0193 229  ILE A C   
35   O O   . ILE A 6   ? 0.5135 0.2485 0.2231 0.1570  0.0150  -0.0038 229  ILE A O   
36   C CB  . ILE A 6   ? 0.6084 0.2412 0.1982 0.0747  -0.0879 0.0063  229  ILE A CB  
37   C CG1 . ILE A 6   ? 0.6392 0.2511 0.2516 0.0706  -0.0885 0.0500  229  ILE A CG1 
38   C CG2 . ILE A 6   ? 0.6333 0.2458 0.2134 0.0284  -0.0516 -0.0429 229  ILE A CG2 
39   C CD1 . ILE A 6   ? 0.6636 0.2677 0.2846 0.0709  -0.0941 0.0659  229  ILE A CD1 
40   N N   . PRO A 7   ? 0.4186 0.2536 0.1705 0.1396  -0.0713 -0.0217 230  PRO A N   
41   C CA  . PRO A 7   ? 0.4009 0.2633 0.1786 0.1287  -0.0755 -0.0261 230  PRO A CA  
42   C C   . PRO A 7   ? 0.4349 0.2609 0.2369 0.1618  -0.0137 -0.0236 230  PRO A C   
43   O O   . PRO A 7   ? 0.4285 0.2447 0.2739 0.1542  0.0000  -0.0337 230  PRO A O   
44   C CB  . PRO A 7   ? 0.3888 0.2912 0.1865 0.1175  -0.0682 -0.0394 230  PRO A CB  
45   C CG  . PRO A 7   ? 0.4194 0.2745 0.1973 0.0961  -0.0530 -0.0407 230  PRO A CG  
46   C CD  . PRO A 7   ? 0.4027 0.2681 0.1724 0.1138  -0.0857 -0.0449 230  PRO A CD  
47   N N   . ILE A 8   ? 0.4360 0.2569 0.2142 0.1778  -0.0333 -0.0172 231  ILE A N   
48   C CA  . ILE A 8   ? 0.4296 0.2685 0.2199 0.1892  -0.0372 -0.0034 231  ILE A CA  
49   C C   . ILE A 8   ? 0.4155 0.2455 0.2411 0.1607  -0.0198 0.0005  231  ILE A C   
50   O O   . ILE A 8   ? 0.4124 0.2606 0.2956 0.1232  -0.0545 -0.0013 231  ILE A O   
51   C CB  . ILE A 8   ? 0.4795 0.2996 0.2594 0.2082  -0.0075 -0.0172 231  ILE A CB  
52   C CG1 . ILE A 8   ? 0.5365 0.3164 0.2834 0.1963  0.0298  -0.0342 231  ILE A CG1 
53   C CG2 . ILE A 8   ? 0.5332 0.3293 0.3169 0.1779  0.0349  -0.0105 231  ILE A CG2 
54   C CD1 . ILE A 8   ? 0.5883 0.3244 0.3321 0.1901  0.0560  -0.0328 231  ILE A CD1 
55   N N   . LEU A 9   ? 0.3768 0.2121 0.2210 0.1450  0.0039  0.0013  232  LEU A N   
56   C CA  . LEU A 9   ? 0.3008 0.2258 0.2075 0.1335  -0.0195 -0.0039 232  LEU A CA  
57   C C   . LEU A 9   ? 0.3003 0.2314 0.2155 0.1246  -0.0018 0.0119  232  LEU A C   
58   O O   . LEU A 9   ? 0.3295 0.2382 0.1825 0.1006  -0.0020 0.0203  232  LEU A O   
59   C CB  . LEU A 9   ? 0.2957 0.2488 0.2261 0.0994  -0.0247 -0.0116 232  LEU A CB  
60   C CG  . LEU A 9   ? 0.2527 0.2642 0.2254 0.0873  -0.0638 -0.0047 232  LEU A CG  
61   C CD1 . LEU A 9   ? 0.2855 0.2917 0.2515 0.0579  -0.0501 -0.0199 232  LEU A CD1 
62   C CD2 . LEU A 9   ? 0.3099 0.2889 0.2607 0.0239  -0.0203 0.0059  232  LEU A CD2 
63   N N   . THR A 10  ? 0.2479 0.2391 0.1912 0.1136  -0.0382 0.0114  233  THR A N   
64   C CA  . THR A 10  ? 0.2670 0.2622 0.2121 0.1217  -0.0188 0.0235  233  THR A CA  
65   C C   . THR A 10  ? 0.2735 0.2687 0.1825 0.1066  -0.0353 0.0245  233  THR A C   
66   O O   . THR A 10  ? 0.3037 0.2788 0.1694 0.1183  -0.0434 0.0218  233  THR A O   
67   C CB  . THR A 10  ? 0.2736 0.2710 0.2319 0.1347  -0.0104 0.0268  233  THR A CB  
68   O OG1 . THR A 10  ? 0.3098 0.2817 0.2015 0.1010  -0.0220 0.0207  233  THR A OG1 
69   C CG2 . THR A 10  ? 0.2808 0.2752 0.2671 0.1623  -0.0169 0.0221  233  THR A CG2 
70   N N   . ILE A 11  ? 0.2784 0.2848 0.2141 0.0756  -0.0061 0.0287  234  ILE A N   
71   C CA  . ILE A 11  ? 0.3176 0.2802 0.2301 0.0554  0.0312  0.0382  234  ILE A CA  
72   C C   . ILE A 11  ? 0.2774 0.2623 0.1878 0.0612  -0.0110 0.0307  234  ILE A C   
73   O O   . ILE A 11  ? 0.2518 0.2451 0.2191 0.0743  -0.0037 0.0290  234  ILE A O   
74   C CB  . ILE A 11  ? 0.4203 0.3130 0.2967 0.0306  0.0661  0.0720  234  ILE A CB  
75   C CG1 . ILE A 11  ? 0.4096 0.3172 0.3196 0.0077  0.0424  0.0949  234  ILE A CG1 
76   C CG2 . ILE A 11  ? 0.4819 0.3259 0.3151 0.0322  0.0972  0.0821  234  ILE A CG2 
77   C CD1 . ILE A 11  ? 0.4238 0.3309 0.3320 0.0008  0.0398  0.0894  234  ILE A CD1 
78   N N   . GLY A 12  ? 0.2694 0.2497 0.1806 0.0478  -0.0319 0.0121  235  GLY A N   
79   C CA  . GLY A 12  ? 0.2140 0.2337 0.1963 0.0417  -0.0520 0.0105  235  GLY A CA  
80   C C   . GLY A 12  ? 0.1841 0.2193 0.1931 0.0187  -0.0293 0.0165  235  GLY A C   
81   O O   . GLY A 12  ? 0.2286 0.2168 0.2115 0.0314  0.0101  0.0160  235  GLY A O   
82   N N   . GLU A 13  ? 0.1901 0.1988 0.2090 0.0484  -0.0402 0.0026  236  GLU A N   
83   C CA  . GLU A 13  ? 0.2231 0.1782 0.1989 0.0916  -0.0551 -0.0067 236  GLU A CA  
84   C C   . GLU A 13  ? 0.2162 0.1907 0.1960 0.0887  -0.0743 -0.0385 236  GLU A C   
85   O O   . GLU A 13  ? 0.2148 0.2255 0.2646 0.0990  -0.0909 -0.0521 236  GLU A O   
86   C CB  . GLU A 13  ? 0.2468 0.1813 0.2168 0.1076  -0.0354 -0.0133 236  GLU A CB  
87   C CG  . GLU A 13  ? 0.2488 0.1934 0.2293 0.1232  -0.0359 0.0118  236  GLU A CG  
88   C CD  . GLU A 13  ? 0.3095 0.2155 0.2414 0.1280  -0.0314 0.0191  236  GLU A CD  
89   O OE1 . GLU A 13  ? 0.3121 0.2348 0.2415 0.1274  -0.0116 0.0244  236  GLU A OE1 
90   O OE2 . GLU A 13  ? 0.3365 0.2223 0.2780 0.1332  -0.0228 0.0393  236  GLU A OE2 
91   N N   . MET A 14  ? 0.2133 0.1814 0.1561 0.0909  -0.0641 -0.0131 237  MET A N   
92   C CA  . MET A 14  ? 0.2302 0.1845 0.1326 0.0805  -0.0548 -0.0223 237  MET A CA  
93   C C   . MET A 14  ? 0.2160 0.1636 0.1429 0.0630  -0.0483 -0.0224 237  MET A C   
94   O O   . MET A 14  ? 0.2109 0.1769 0.1428 0.0445  -0.0591 -0.0183 237  MET A O   
95   C CB  . MET A 14  ? 0.2777 0.2227 0.1624 0.1063  -0.0279 -0.0168 237  MET A CB  
96   C CG  . MET A 14  ? 0.2876 0.2405 0.1373 0.1147  -0.0403 -0.0179 237  MET A CG  
97   S SD  . MET A 14  ? 0.2930 0.2449 0.1805 0.1086  -0.0487 -0.0041 237  MET A SD  
98   C CE  . MET A 14  ? 0.2586 0.2720 0.1977 0.1042  -0.0371 0.0231  237  MET A CE  
99   N N   . THR A 15  ? 0.2031 0.1394 0.1358 0.0694  -0.0206 0.0046  238  THR A N   
100  C CA  . THR A 15  ? 0.1739 0.1160 0.1565 0.0393  -0.0090 0.0125  238  THR A CA  
101  C C   . THR A 15  ? 0.1919 0.1230 0.1500 0.0471  -0.0357 0.0049  238  THR A C   
102  O O   . THR A 15  ? 0.2065 0.1411 0.1331 0.0389  -0.0487 0.0052  238  THR A O   
103  C CB  . THR A 15  ? 0.1660 0.1369 0.1648 0.0298  -0.0287 0.0036  238  THR A CB  
104  O OG1 . THR A 15  ? 0.2041 0.1276 0.1759 0.0338  -0.0422 0.0308  238  THR A OG1 
105  C CG2 . THR A 15  ? 0.1832 0.1646 0.1767 0.0375  0.0313  -0.0075 238  THR A CG2 
106  N N   . ASN A 16  ? 0.1741 0.1060 0.1564 0.0272  -0.0586 -0.0008 239  ASN A N   
107  C CA  . ASN A 16  ? 0.1711 0.1190 0.1387 0.0133  -0.0801 0.0131  239  ASN A CA  
108  C C   . ASN A 16  ? 0.1539 0.1198 0.1256 0.0280  -0.0645 0.0274  239  ASN A C   
109  O O   . ASN A 16  ? 0.1762 0.1520 0.1411 0.0280  -0.0411 0.0145  239  ASN A O   
110  C CB  . ASN A 16  ? 0.2031 0.1297 0.1406 0.0050  -0.0666 0.0150  239  ASN A CB  
111  C CG  . ASN A 16  ? 0.1893 0.1442 0.1462 0.0032  -0.0455 0.0113  239  ASN A CG  
112  O OD1 . ASN A 16  ? 0.1777 0.1423 0.1410 0.0120  -0.0506 0.0006  239  ASN A OD1 
113  N ND2 . ASN A 16  ? 0.1643 0.1733 0.1337 0.0171  -0.0488 -0.0034 239  ASN A ND2 
114  N N   . SER A 17  ? 0.1352 0.1288 0.1424 0.0369  -0.0616 0.0051  240  SER A N   
115  C CA  . SER A 17  ? 0.1480 0.1256 0.0964 0.0196  -0.0529 -0.0036 240  SER A CA  
116  C C   . SER A 17  ? 0.1523 0.1105 0.1185 0.0175  -0.0376 0.0213  240  SER A C   
117  O O   . SER A 17  ? 0.1686 0.1174 0.1270 0.0079  -0.0523 0.0168  240  SER A O   
118  C CB  . SER A 17  ? 0.1829 0.1481 0.1104 -0.0082 -0.0372 0.0046  240  SER A CB  
119  O OG  . SER A 17  ? 0.1716 0.1391 0.1348 0.0126  -0.0500 0.0244  240  SER A OG  
120  N N   . ARG A 18  ? 0.1667 0.0976 0.1480 0.0084  -0.0450 0.0026  241  ARG A N   
121  C CA  . ARG A 18  ? 0.1590 0.1021 0.1512 0.0274  -0.0522 0.0128  241  ARG A CA  
122  C C   . ARG A 18  ? 0.1577 0.1140 0.1590 0.0136  -0.0402 0.0143  241  ARG A C   
123  O O   . ARG A 18  ? 0.1829 0.1202 0.1499 0.0218  -0.0564 0.0019  241  ARG A O   
124  C CB  . ARG A 18  ? 0.1848 0.1075 0.1280 -0.0074 -0.0604 0.0199  241  ARG A CB  
125  C CG  . ARG A 18  ? 0.1838 0.1145 0.1150 -0.0149 -0.0475 0.0168  241  ARG A CG  
126  C CD  . ARG A 18  ? 0.1694 0.0865 0.1710 0.0063  -0.0301 0.0158  241  ARG A CD  
127  N NE  . ARG A 18  ? 0.1712 0.0961 0.1563 0.0261  -0.0342 0.0006  241  ARG A NE  
128  C CZ  . ARG A 18  ? 0.1571 0.0973 0.1554 0.0135  -0.0395 0.0258  241  ARG A CZ  
129  N NH1 . ARG A 18  ? 0.1912 0.1240 0.1744 0.0058  -0.0686 0.0244  241  ARG A NH1 
130  N NH2 . ARG A 18  ? 0.1776 0.1281 0.1871 0.0168  -0.0159 0.0159  241  ARG A NH2 
131  N N   . PHE A 19  ? 0.1755 0.1363 0.1409 0.0121  -0.0753 0.0404  242  PHE A N   
132  C CA  . PHE A 19  ? 0.1889 0.1173 0.1382 0.0236  -0.0675 0.0252  242  PHE A CA  
133  C C   . PHE A 19  ? 0.1612 0.1129 0.1442 0.0284  -0.0403 0.0167  242  PHE A C   
134  O O   . PHE A 19  ? 0.1902 0.1608 0.1295 0.0475  -0.0212 0.0054  242  PHE A O   
135  C CB  . PHE A 19  ? 0.1642 0.1237 0.1357 -0.0087 -0.0683 0.0011  242  PHE A CB  
136  C CG  . PHE A 19  ? 0.1743 0.1204 0.1239 0.0065  -0.0541 -0.0282 242  PHE A CG  
137  C CD1 . PHE A 19  ? 0.1960 0.1401 0.1745 -0.0042 -0.0378 -0.0372 242  PHE A CD1 
138  C CD2 . PHE A 19  ? 0.1871 0.1407 0.1131 -0.0007 -0.0627 0.0022  242  PHE A CD2 
139  C CE1 . PHE A 19  ? 0.1978 0.1472 0.1874 -0.0211 -0.0250 -0.0338 242  PHE A CE1 
140  C CE2 . PHE A 19  ? 0.2047 0.1535 0.1507 -0.0291 -0.0337 -0.0165 242  PHE A CE2 
141  C CZ  . PHE A 19  ? 0.2130 0.1619 0.1634 -0.0253 -0.0429 -0.0217 242  PHE A CZ  
142  N N   . PRO A 20  ? 0.1773 0.1183 0.1519 0.0287  -0.0241 0.0023  243  PRO A N   
143  C CA  . PRO A 20  ? 0.1795 0.1306 0.1559 0.0296  -0.0422 0.0102  243  PRO A CA  
144  C C   . PRO A 20  ? 0.2020 0.1535 0.1653 0.0420  -0.0417 0.0202  243  PRO A C   
145  O O   . PRO A 20  ? 0.2407 0.1985 0.1649 0.0832  -0.0216 0.0262  243  PRO A O   
146  C CB  . PRO A 20  ? 0.2198 0.1277 0.1409 0.0402  0.0039  0.0031  243  PRO A CB  
147  C CG  . PRO A 20  ? 0.2150 0.1085 0.1248 0.0446  -0.0183 0.0112  243  PRO A CG  
148  C CD  . PRO A 20  ? 0.2055 0.1126 0.1233 0.0412  -0.0321 0.0127  243  PRO A CD  
149  N N   A VAL A 21  ? 0.1889 0.1464 0.1527 0.0368  -0.0527 -0.0008 244  VAL A N   
150  N N   B VAL A 21  ? 0.1761 0.1464 0.1585 0.0360  -0.0409 0.0088  244  VAL A N   
151  C CA  A VAL A 21  ? 0.1946 0.1536 0.1676 0.0365  -0.0377 -0.0251 244  VAL A CA  
152  C CA  B VAL A 21  ? 0.1580 0.1488 0.1610 0.0348  -0.0329 -0.0030 244  VAL A CA  
153  C C   A VAL A 21  ? 0.1731 0.1594 0.1564 0.0400  -0.0573 -0.0096 244  VAL A C   
154  C C   B VAL A 21  ? 0.1530 0.1475 0.1554 0.0404  -0.0429 -0.0057 244  VAL A C   
155  O O   A VAL A 21  ? 0.1937 0.1824 0.1304 0.0321  -0.0593 -0.0007 244  VAL A O   
156  O O   B VAL A 21  ? 0.1613 0.1536 0.1483 0.0340  -0.0333 -0.0195 244  VAL A O   
157  C CB  A VAL A 21  ? 0.2261 0.1717 0.1685 0.0317  -0.0049 -0.0332 244  VAL A CB  
158  C CB  B VAL A 21  ? 0.1501 0.1619 0.1601 0.0273  -0.0214 0.0024  244  VAL A CB  
159  C CG1 A VAL A 21  ? 0.2712 0.2159 0.2183 0.0576  0.0140  -0.0212 244  VAL A CG1 
160  C CG1 B VAL A 21  ? 0.0977 0.1493 0.1193 0.0262  -0.0540 0.0249  244  VAL A CG1 
161  C CG2 A VAL A 21  ? 0.1977 0.1628 0.1349 0.0016  -0.0135 -0.0265 244  VAL A CG2 
162  C CG2 B VAL A 21  ? 0.1856 0.1887 0.2136 0.0333  0.0197  -0.0055 244  VAL A CG2 
163  N N   . ALA A 22  ? 0.1720 0.1504 0.1578 0.0431  -0.0323 0.0020  245  ALA A N   
164  C CA  . ALA A 22  ? 0.1599 0.1551 0.1614 0.0495  -0.0375 0.0124  245  ALA A CA  
165  C C   . ALA A 22  ? 0.1869 0.1722 0.1518 0.0481  -0.0460 0.0072  245  ALA A C   
166  O O   . ALA A 22  ? 0.1761 0.1760 0.1692 0.0467  -0.0463 0.0166  245  ALA A O   
167  C CB  . ALA A 22  ? 0.1608 0.1622 0.1976 0.0633  -0.0355 0.0170  245  ALA A CB  
168  N N   . ILE A 23  ? 0.1912 0.1775 0.1228 0.0388  -0.0334 0.0092  246  ILE A N   
169  C CA  . ILE A 23  ? 0.1767 0.1809 0.1494 0.0310  -0.0507 0.0069  246  ILE A CA  
170  C C   . ILE A 23  ? 0.2060 0.1916 0.1769 0.0247  -0.0270 -0.0109 246  ILE A C   
171  O O   . ILE A 23  ? 0.2302 0.2018 0.2190 0.0302  -0.0335 -0.0089 246  ILE A O   
172  C CB  . ILE A 23  ? 0.1947 0.1962 0.1592 0.0124  -0.0488 0.0009  246  ILE A CB  
173  C CG1 . ILE A 23  ? 0.2060 0.2344 0.1787 0.0042  -0.0628 -0.0206 246  ILE A CG1 
174  C CG2 . ILE A 23  ? 0.2023 0.1943 0.1555 0.0170  -0.0262 -0.0012 246  ILE A CG2 
175  C CD1 . ILE A 23  ? 0.2296 0.2301 0.2008 0.0001  -0.0489 -0.0261 246  ILE A CD1 
176  N N   . ASP A 24  ? 0.1841 0.2032 0.1583 0.0176  -0.0463 0.0067  247  ASP A N   
177  C CA  . ASP A 24  ? 0.1863 0.2276 0.1717 0.0244  -0.0556 -0.0069 247  ASP A CA  
178  C C   . ASP A 24  ? 0.1726 0.2535 0.1695 0.0562  -0.0703 -0.0005 247  ASP A C   
179  O O   . ASP A 24  ? 0.1962 0.2854 0.2252 0.0855  -0.0500 0.0118  247  ASP A O   
180  C CB  . ASP A 24  ? 0.1816 0.2212 0.1824 0.0126  -0.0786 -0.0091 247  ASP A CB  
181  C CG  . ASP A 24  ? 0.2334 0.2079 0.1903 0.0315  -0.0585 0.0103  247  ASP A CG  
182  O OD1 . ASP A 24  ? 0.3185 0.2141 0.2132 0.0597  -0.0122 0.0174  247  ASP A OD1 
183  O OD2 . ASP A 24  ? 0.2375 0.1975 0.2212 0.0341  -0.0425 0.0133  247  ASP A OD2 
184  N N   . MET A 25  ? 0.1741 0.2651 0.1750 0.0332  -0.0537 0.0072  248  MET A N   
185  C CA  A MET A 25  ? 0.1866 0.2780 0.1787 0.0297  -0.0391 0.0077  248  MET A CA  
186  C CA  B MET A 25  ? 0.1855 0.2705 0.2080 0.0259  -0.0368 0.0141  248  MET A CA  
187  C C   . MET A 25  ? 0.1810 0.2667 0.1935 0.0382  -0.0266 0.0190  248  MET A C   
188  O O   . MET A 25  ? 0.2192 0.2524 0.1996 0.0269  -0.0154 0.0255  248  MET A O   
189  C CB  A MET A 25  ? 0.2012 0.3086 0.1984 0.0362  -0.0638 -0.0318 248  MET A CB  
190  C CB  B MET A 25  ? 0.2060 0.2802 0.2771 0.0183  -0.0301 0.0119  248  MET A CB  
191  C CG  A MET A 25  ? 0.2606 0.3285 0.3126 0.0051  0.0520  -0.0952 248  MET A CG  
192  C CG  B MET A 25  ? 0.2300 0.2874 0.3445 0.0011  -0.0102 0.0141  248  MET A CG  
193  S SD  A MET A 25  ? 0.3067 0.3835 0.4657 -0.0275 0.0886  -0.1285 248  MET A SD  
194  S SD  B MET A 25  ? 0.2330 0.2854 0.3860 -0.0152 -0.0090 0.0255  248  MET A SD  
195  C CE  A MET A 25  ? 0.3142 0.3946 0.4526 -0.0457 0.0524  -0.1441 248  MET A CE  
196  C CE  B MET A 25  ? 0.2207 0.2823 0.3903 -0.0169 0.0023  0.0234  248  MET A CE  
197  N N   . LEU A 26  ? 0.1881 0.2867 0.1890 0.0478  -0.0167 0.0159  249  LEU A N   
198  C CA  . LEU A 26  ? 0.2035 0.2982 0.1837 0.0333  -0.0248 0.0133  249  LEU A CA  
199  C C   . LEU A 26  ? 0.2047 0.3097 0.2065 0.0129  -0.0343 0.0269  249  LEU A C   
200  O O   . LEU A 26  ? 0.2173 0.3114 0.2443 -0.0077 -0.0405 0.0265  249  LEU A O   
201  C CB  . LEU A 26  ? 0.2125 0.3102 0.1978 0.0524  -0.0187 0.0055  249  LEU A CB  
202  C CG  . LEU A 26  ? 0.2384 0.3145 0.2231 0.0386  -0.0105 0.0078  249  LEU A CG  
203  C CD1 . LEU A 26  ? 0.2936 0.3090 0.2143 0.0289  -0.0210 0.0127  249  LEU A CD1 
204  C CD2 . LEU A 26  ? 0.2378 0.3240 0.2803 0.0235  -0.0314 -0.0042 249  LEU A CD2 
205  N N   . HIS A 27  ? 0.2145 0.3057 0.1715 0.0091  -0.0412 0.0137  250  HIS A N   
206  C CA  . HIS A 27  ? 0.2084 0.3127 0.2134 -0.0202 -0.0230 0.0036  250  HIS A CA  
207  C C   . HIS A 27  ? 0.1957 0.3101 0.2332 -0.0377 -0.0639 0.0310  250  HIS A C   
208  O O   . HIS A 27  ? 0.1927 0.3130 0.2974 -0.0416 -0.0311 0.0184  250  HIS A O   
209  C CB  . HIS A 27  ? 0.2280 0.3145 0.2308 -0.0340 -0.0258 -0.0266 250  HIS A CB  
210  C CG  . HIS A 27  ? 0.2743 0.3370 0.2525 -0.0410 -0.0512 -0.0394 250  HIS A CG  
211  N ND1 . HIS A 27  ? 0.3081 0.3522 0.2724 -0.0363 -0.0496 -0.0350 250  HIS A ND1 
212  C CD2 . HIS A 27  ? 0.3087 0.3385 0.2579 -0.0442 -0.0367 -0.0466 250  HIS A CD2 
213  C CE1 . HIS A 27  ? 0.3252 0.3456 0.2879 -0.0471 -0.0315 -0.0536 250  HIS A CE1 
214  N NE2 . HIS A 27  ? 0.3392 0.3460 0.2829 -0.0403 -0.0318 -0.0516 250  HIS A NE2 
215  N N   . THR A 28  ? 0.2249 0.3289 0.2395 -0.0484 -0.0605 0.0466  251  THR A N   
216  C CA  . THR A 28  ? 0.2366 0.3434 0.2383 -0.0473 -0.0602 0.0633  251  THR A CA  
217  C C   . THR A 28  ? 0.2773 0.3504 0.2767 -0.0535 -0.0473 0.0486  251  THR A C   
218  O O   . THR A 28  ? 0.2695 0.3515 0.2992 -0.0799 -0.0547 0.0123  251  THR A O   
219  C CB  . THR A 28  ? 0.2397 0.3568 0.2625 -0.0515 -0.0385 0.0609  251  THR A CB  
220  O OG1 . THR A 28  ? 0.2548 0.3357 0.2445 -0.0619 -0.0162 0.0718  251  THR A OG1 
221  C CG2 . THR A 28  ? 0.2483 0.3757 0.2686 -0.0575 -0.0215 0.0490  251  THR A CG2 
222  N N   . SER A 29  ? 0.3028 0.3457 0.3092 -0.0568 -0.0566 0.0475  252  SER A N   
223  C CA  . SER A 29  ? 0.4088 0.3549 0.3679 -0.0488 -0.0032 0.0489  252  SER A CA  
224  C C   . SER A 29  ? 0.3542 0.3319 0.3557 -0.0652 -0.0578 0.0761  252  SER A C   
225  O O   . SER A 29  ? 0.3512 0.3068 0.3145 -0.0811 -0.0481 0.1031  252  SER A O   
226  C CB  . SER A 29  ? 0.5178 0.3796 0.4172 -0.0502 0.0853  0.0224  252  SER A CB  
227  O OG  . SER A 29  ? 0.5878 0.3896 0.4431 -0.0564 0.1294  -0.0025 252  SER A OG  
228  N N   . PRO A 30  ? 0.3414 0.3356 0.3981 -0.0773 -0.0776 0.0522  253  PRO A N   
229  C CA  . PRO A 30  ? 0.3425 0.3312 0.3932 -0.0877 -0.0601 0.0485  253  PRO A CA  
230  C C   . PRO A 30  ? 0.3590 0.3275 0.3807 -0.1082 -0.0049 0.0377  253  PRO A C   
231  O O   . PRO A 30  ? 0.4089 0.3420 0.3900 -0.0912 0.0156  0.0172  253  PRO A O   
232  C CB  . PRO A 30  ? 0.3412 0.3330 0.4219 -0.0895 -0.0722 0.0381  253  PRO A CB  
233  C CG  . PRO A 30  ? 0.3670 0.3372 0.4385 -0.0920 -0.0725 0.0410  253  PRO A CG  
234  C CD  . PRO A 30  ? 0.3414 0.3308 0.4194 -0.0921 -0.0784 0.0580  253  PRO A CD  
235  N N   . THR A 31  ? 0.3430 0.3078 0.3483 -0.1272 0.0085  0.0602  254  THR A N   
236  C CA  . THR A 31  ? 0.3736 0.3051 0.3571 -0.1045 0.0078  0.0624  254  THR A CA  
237  C C   . THR A 31  ? 0.4010 0.3020 0.3817 -0.1010 0.0128  0.0849  254  THR A C   
238  O O   . THR A 31  ? 0.3932 0.2859 0.3650 -0.0919 0.0031  0.0613  254  THR A O   
239  C CB  . THR A 31  ? 0.4010 0.3148 0.3394 -0.0895 0.0150  0.0539  254  THR A CB  
240  O OG1 . THR A 31  ? 0.3927 0.3258 0.3163 -0.0761 -0.0147 0.0381  254  THR A OG1 
241  C CG2 . THR A 31  ? 0.4035 0.3195 0.3672 -0.0879 0.0329  0.0636  254  THR A CG2 
242  N N   . ASP A 32  ? 0.4608 0.3235 0.4455 -0.0863 0.0787  0.1160  255  ASP A N   
243  C CA  . ASP A 32  ? 0.5014 0.3519 0.4925 -0.0672 0.0812  0.1273  255  ASP A CA  
244  C C   . ASP A 32  ? 0.5055 0.3651 0.5107 -0.0841 0.0573  0.1372  255  ASP A C   
245  O O   . ASP A 32  ? 0.5286 0.3646 0.5353 -0.0720 0.0499  0.1566  255  ASP A O   
246  C CB  . ASP A 32  ? 0.5432 0.3698 0.5183 -0.0379 0.1295  0.1412  255  ASP A CB  
247  C CG  . ASP A 32  ? 0.5753 0.3808 0.5449 -0.0271 0.1575  0.1280  255  ASP A CG  
248  N N   . ASN A 33  ? 0.4847 0.3675 0.4861 -0.1191 0.0389  0.1155  256  ASN A N   
249  C CA  . ASN A 33  ? 0.4615 0.3954 0.4562 -0.1335 0.0163  0.0978  256  ASN A CA  
250  C C   . ASN A 33  ? 0.4328 0.3377 0.3885 -0.1353 -0.0350 0.0715  256  ASN A C   
251  O O   . ASN A 33  ? 0.4412 0.3187 0.3871 -0.1619 -0.0734 0.0253  256  ASN A O   
256  N N   . PHE A 34  ? 0.3710 0.2937 0.3219 -0.1237 -0.0626 0.0775  257  PHE A N   
257  C CA  . PHE A 34  ? 0.3344 0.2799 0.2895 -0.0907 -0.0799 0.0728  257  PHE A CA  
258  C C   . PHE A 34  ? 0.3187 0.2603 0.3038 -0.0815 -0.0690 0.0540  257  PHE A C   
259  O O   . PHE A 34  ? 0.3462 0.2646 0.2959 -0.0843 -0.0168 0.0496  257  PHE A O   
260  C CB  . PHE A 34  ? 0.3266 0.2873 0.2741 -0.1031 -0.0652 0.0802  257  PHE A CB  
261  C CG  . PHE A 34  ? 0.3168 0.3445 0.2969 -0.1025 -0.0699 0.0713  257  PHE A CG  
262  C CD1 . PHE A 34  ? 0.3224 0.3573 0.2628 -0.1115 -0.1063 0.0616  257  PHE A CD1 
263  C CD2 . PHE A 34  ? 0.3420 0.3923 0.3288 -0.1087 -0.0550 0.0476  257  PHE A CD2 
264  C CE1 . PHE A 34  ? 0.3347 0.3869 0.2910 -0.1123 -0.0850 0.0452  257  PHE A CE1 
265  C CE2 . PHE A 34  ? 0.3595 0.4074 0.3225 -0.0995 -0.0533 0.0375  257  PHE A CE2 
266  C CZ  . PHE A 34  ? 0.3535 0.4087 0.2904 -0.1017 -0.0819 0.0374  257  PHE A CZ  
267  N N   . ILE A 35  ? 0.3066 0.2195 0.3302 -0.0720 -0.0590 0.0409  258  ILE A N   
268  C CA  . ILE A 35  ? 0.2836 0.1903 0.3465 -0.0584 -0.0546 0.0370  258  ILE A CA  
269  C C   . ILE A 35  ? 0.2916 0.1775 0.2939 -0.0350 -0.0060 0.0327  258  ILE A C   
270  O O   . ILE A 35  ? 0.3733 0.1856 0.2705 -0.0278 -0.0115 0.0080  258  ILE A O   
271  C CB  . ILE A 35  ? 0.2733 0.1801 0.4129 -0.0448 -0.0818 0.0343  258  ILE A CB  
272  C CG1 . ILE A 35  ? 0.3512 0.2027 0.4808 -0.0068 -0.0025 0.0509  258  ILE A CG1 
273  C CG2 . ILE A 35  ? 0.2920 0.1882 0.4256 -0.0235 -0.0873 0.0274  258  ILE A CG2 
274  C CD1 . ILE A 35  ? 0.4049 0.2327 0.5124 0.0100  0.0377  0.0668  258  ILE A CD1 
275  N N   . VAL A 36  ? 0.2496 0.1780 0.2396 -0.0190 -0.0215 0.0416  259  VAL A N   
276  C CA  . VAL A 36  ? 0.2216 0.1696 0.2137 -0.0041 -0.0461 0.0445  259  VAL A CA  
277  C C   . VAL A 36  ? 0.2238 0.1717 0.1730 -0.0019 -0.0503 0.0265  259  VAL A C   
278  O O   . VAL A 36  ? 0.2434 0.1921 0.1572 -0.0023 -0.0670 0.0157  259  VAL A O   
279  C CB  . VAL A 36  ? 0.2065 0.1902 0.2040 -0.0135 -0.0503 0.0319  259  VAL A CB  
280  C CG1 . VAL A 36  ? 0.2125 0.1959 0.2133 -0.0033 -0.0457 0.0604  259  VAL A CG1 
281  C CG2 . VAL A 36  ? 0.2417 0.1977 0.2140 -0.0267 -0.0460 -0.0040 259  VAL A CG2 
282  N N   . GLN A 37  ? 0.2270 0.1516 0.1585 -0.0115 -0.0663 0.0158  260  GLN A N   
283  C CA  . GLN A 37  ? 0.1893 0.1317 0.1588 0.0062  -0.0726 0.0178  260  GLN A CA  
284  C C   . GLN A 37  ? 0.1984 0.1424 0.1755 -0.0025 -0.0564 0.0102  260  GLN A C   
285  O O   . GLN A 37  ? 0.1858 0.1344 0.1758 0.0284  -0.0624 0.0267  260  GLN A O   
286  C CB  . GLN A 37  ? 0.1963 0.1501 0.1898 0.0204  -0.0872 0.0166  260  GLN A CB  
287  C CG  . GLN A 37  ? 0.1940 0.1420 0.2303 0.0247  -0.1081 0.0182  260  GLN A CG  
288  C CD  . GLN A 37  ? 0.2218 0.1621 0.2287 0.0132  -0.0914 0.0242  260  GLN A CD  
289  O OE1 . GLN A 37  ? 0.2551 0.1749 0.2468 -0.0062 -0.0795 0.0286  260  GLN A OE1 
290  N NE2 . GLN A 37  ? 0.2188 0.1745 0.2092 0.0152  -0.0867 0.0306  260  GLN A NE2 
291  N N   . PRO A 38  ? 0.1955 0.1257 0.1566 0.0007  -0.0476 0.0295  261  PRO A N   
292  C CA  . PRO A 38  ? 0.1878 0.1275 0.1495 0.0218  -0.0722 0.0421  261  PRO A CA  
293  C C   . PRO A 38  ? 0.1748 0.1224 0.1359 0.0194  -0.0657 0.0118  261  PRO A C   
294  O O   . PRO A 38  ? 0.1855 0.1383 0.1562 0.0243  -0.0698 0.0107  261  PRO A O   
295  C CB  . PRO A 38  ? 0.2023 0.1493 0.1487 0.0232  -0.0608 0.0141  261  PRO A CB  
296  C CG  . PRO A 38  ? 0.2102 0.1271 0.1325 0.0043  -0.0400 0.0059  261  PRO A CG  
297  C CD  . PRO A 38  ? 0.2070 0.1313 0.1668 0.0103  -0.0377 0.0177  261  PRO A CD  
298  N N   . GLN A 39  ? 0.1757 0.1152 0.1343 0.0161  -0.0508 0.0323  262  GLN A N   
299  C CA  . GLN A 39  ? 0.1746 0.1162 0.1549 0.0131  -0.0513 0.0155  262  GLN A CA  
300  C C   . GLN A 39  ? 0.1707 0.1060 0.1350 0.0229  -0.0535 0.0185  262  GLN A C   
301  O O   . GLN A 39  ? 0.1899 0.1076 0.1525 0.0028  -0.0466 0.0195  262  GLN A O   
302  C CB  . GLN A 39  ? 0.2066 0.1065 0.1761 0.0242  -0.0398 0.0445  262  GLN A CB  
303  C CG  . GLN A 39  ? 0.2340 0.1155 0.1657 0.0198  -0.0313 0.0349  262  GLN A CG  
304  C CD  . GLN A 39  ? 0.2139 0.1200 0.1766 0.0134  -0.0314 0.0256  262  GLN A CD  
305  O OE1 . GLN A 39  ? 0.2170 0.1357 0.1884 0.0162  -0.0453 0.0553  262  GLN A OE1 
306  N NE2 . GLN A 39  ? 0.1892 0.1228 0.1850 0.0361  -0.0468 0.0299  262  GLN A NE2 
307  N N   . ASN A 40  ? 0.1569 0.1133 0.1218 0.0309  -0.0565 0.0318  263  ASN A N   
308  C CA  . ASN A 40  ? 0.1616 0.1324 0.1212 0.0316  -0.0621 0.0304  263  ASN A CA  
309  C C   . ASN A 40  ? 0.1829 0.1215 0.1570 0.0445  -0.0271 0.0193  263  ASN A C   
310  O O   . ASN A 40  ? 0.1975 0.1261 0.1701 0.0151  -0.0330 0.0109  263  ASN A O   
311  C CB  . ASN A 40  ? 0.1798 0.1436 0.1187 0.0315  -0.0477 0.0164  263  ASN A CB  
312  C CG  . ASN A 40  ? 0.1597 0.1215 0.1496 0.0221  -0.0477 0.0203  263  ASN A CG  
313  O OD1 . ASN A 40  ? 0.1755 0.1022 0.1885 0.0337  -0.0497 0.0191  263  ASN A OD1 
314  N ND2 . ASN A 40  ? 0.1888 0.1296 0.1599 0.0168  -0.0638 0.0185  263  ASN A ND2 
315  N N   . GLY A 41  ? 0.1777 0.1133 0.1416 0.0390  -0.0659 -0.0018 264  GLY A N   
316  C CA  . GLY A 41  ? 0.1719 0.1330 0.1184 0.0298  -0.0693 0.0089  264  GLY A CA  
317  C C   . GLY A 41  ? 0.1903 0.1308 0.1222 0.0172  -0.0719 0.0011  264  GLY A C   
318  O O   . GLY A 41  ? 0.1827 0.1409 0.1706 0.0196  -0.0593 0.0138  264  GLY A O   
319  N N   . ARG A 42  ? 0.1874 0.1471 0.1171 0.0119  -0.0822 0.0090  265  ARG A N   
320  C CA  . ARG A 42  ? 0.1667 0.1320 0.1593 0.0226  -0.0921 0.0033  265  ARG A CA  
321  C C   . ARG A 42  ? 0.1842 0.1421 0.1572 0.0050  -0.0722 0.0001  265  ARG A C   
322  O O   . ARG A 42  ? 0.1788 0.1533 0.1794 0.0075  -0.0737 0.0021  265  ARG A O   
323  C CB  . ARG A 42  ? 0.1686 0.1142 0.1804 0.0242  -0.0549 0.0168  265  ARG A CB  
324  C CG  . ARG A 42  ? 0.1856 0.1254 0.1727 0.0002  -0.0550 0.0213  265  ARG A CG  
325  C CD  . ARG A 42  ? 0.2020 0.1455 0.1457 0.0045  -0.0615 0.0451  265  ARG A CD  
326  N NE  . ARG A 42  ? 0.2195 0.1371 0.1400 0.0004  -0.0718 0.0523  265  ARG A NE  
327  C CZ  . ARG A 42  ? 0.2336 0.1226 0.1163 0.0165  -0.0473 0.0383  265  ARG A CZ  
328  N NH1 . ARG A 42  ? 0.2110 0.1324 0.1710 0.0192  -0.0292 0.0084  265  ARG A NH1 
329  N NH2 . ARG A 42  ? 0.2443 0.1327 0.1484 0.0012  -0.0407 0.0332  265  ARG A NH2 
330  N N   . CYS A 43  ? 0.2276 0.1370 0.1393 0.0103  -0.0989 -0.0185 266  CYS A N   
331  C CA  . CYS A 43  ? 0.2458 0.1389 0.1463 0.0204  -0.0832 -0.0084 266  CYS A CA  
332  C C   . CYS A 43  ? 0.2577 0.1427 0.1495 0.0188  -0.0717 0.0030  266  CYS A C   
333  O O   . CYS A 43  ? 0.2661 0.1735 0.1609 -0.0005 -0.0875 -0.0197 266  CYS A O   
334  C CB  . CYS A 43  ? 0.2443 0.1282 0.1651 0.0356  -0.0941 0.0172  266  CYS A CB  
335  S SG  . CYS A 43  ? 0.2891 0.1485 0.1692 0.0114  -0.0654 0.0062  266  CYS A SG  
336  N N   . THR A 44  ? 0.2482 0.1412 0.1316 0.0102  -0.0709 0.0151  267  THR A N   
337  C CA  . THR A 44  ? 0.2781 0.1628 0.1336 0.0296  -0.0841 0.0024  267  THR A CA  
338  C C   . THR A 44  ? 0.2916 0.1618 0.1634 0.0020  -0.0643 -0.0219 267  THR A C   
339  O O   . THR A 44  ? 0.2882 0.1628 0.1542 -0.0186 -0.0488 -0.0287 267  THR A O   
340  C CB  . THR A 44  ? 0.2660 0.1572 0.1558 0.0210  -0.1121 -0.0009 267  THR A CB  
341  O OG1 . THR A 44  ? 0.2646 0.1818 0.1664 -0.0006 -0.0725 -0.0101 267  THR A OG1 
342  C CG2 . THR A 44  ? 0.2925 0.1495 0.1950 0.0335  -0.1032 0.0196  267  THR A CG2 
343  N N   . LEU A 45  ? 0.2806 0.1636 0.1783 0.0246  -0.0629 -0.0218 268  LEU A N   
344  C CA  . LEU A 45  ? 0.2889 0.1727 0.1741 0.0365  -0.0457 -0.0221 268  LEU A CA  
345  C C   . LEU A 45  ? 0.3420 0.1995 0.1838 0.0247  -0.0525 -0.0185 268  LEU A C   
346  O O   . LEU A 45  ? 0.4074 0.2062 0.2219 0.0005  -0.0463 -0.0383 268  LEU A O   
347  C CB  . LEU A 45  ? 0.2731 0.1908 0.1879 0.0244  -0.0151 -0.0357 268  LEU A CB  
348  C CG  . LEU A 45  ? 0.2781 0.2099 0.1784 0.0238  -0.0070 -0.0273 268  LEU A CG  
349  C CD1 . LEU A 45  ? 0.2655 0.2148 0.2257 0.0370  0.0061  -0.0134 268  LEU A CD1 
350  C CD2 . LEU A 45  ? 0.2807 0.2223 0.1601 0.0230  -0.0416 -0.0047 268  LEU A CD2 
351  N N   . ASP A 46  ? 0.3682 0.2143 0.1641 -0.0119 -0.0523 -0.0433 269  ASP A N   
352  C CA  . ASP A 46  ? 0.4134 0.2525 0.1755 -0.0380 -0.0949 -0.0347 269  ASP A CA  
353  C C   . ASP A 46  ? 0.3736 0.2295 0.1480 -0.0385 -0.0954 -0.0229 269  ASP A C   
354  O O   . ASP A 46  ? 0.4011 0.2444 0.1550 -0.0397 -0.0889 -0.0174 269  ASP A O   
355  C CB  . ASP A 46  ? 0.4970 0.2865 0.2089 -0.0181 -0.1076 -0.0147 269  ASP A CB  
356  C CG  . ASP A 46  ? 0.5524 0.2986 0.2435 -0.0115 -0.1397 -0.0295 269  ASP A CG  
357  O OD1 . ASP A 46  ? 0.5608 0.3307 0.2901 -0.0075 -0.1456 -0.0234 269  ASP A OD1 
358  O OD2 . ASP A 46  ? 0.6275 0.3195 0.2848 0.0066  -0.1132 -0.0145 269  ASP A OD2 
359  N N   . GLY A 47  ? 0.3326 0.2013 0.1522 0.0070  -0.0607 -0.0101 270  GLY A N   
360  C CA  . GLY A 47  ? 0.2882 0.1917 0.1439 -0.0289 -0.0536 -0.0096 270  GLY A CA  
361  C C   . GLY A 47  ? 0.2584 0.1872 0.1845 -0.0209 -0.0685 -0.0140 270  GLY A C   
362  O O   . GLY A 47  ? 0.2596 0.2090 0.2183 -0.0030 -0.0350 0.0204  270  GLY A O   
363  N N   . GLU A 48  ? 0.2687 0.1759 0.1799 0.0049  -0.0973 -0.0147 271  GLU A N   
364  C CA  . GLU A 48  ? 0.2991 0.1819 0.2063 0.0141  -0.0974 0.0076  271  GLU A CA  
365  C C   . GLU A 48  ? 0.2604 0.1534 0.1972 -0.0118 -0.1047 -0.0031 271  GLU A C   
366  O O   . GLU A 48  ? 0.2331 0.1375 0.1919 0.0099  -0.0849 0.0086  271  GLU A O   
367  C CB  . GLU A 48  ? 0.3520 0.2241 0.2206 0.0317  -0.1514 0.0083  271  GLU A CB  
368  C CG  . GLU A 48  ? 0.4533 0.2898 0.2571 0.0212  -0.1873 0.0069  271  GLU A CG  
369  C CD  . GLU A 48  ? 0.5503 0.3588 0.3035 0.0361  -0.2210 0.0071  271  GLU A CD  
370  O OE1 . GLU A 48  ? 0.6248 0.3955 0.3460 0.0655  -0.1699 0.0236  271  GLU A OE1 
371  O OE2 . GLU A 48  ? 0.5911 0.3989 0.3383 0.0546  -0.2307 0.0423  271  GLU A OE2 
372  N N   . LEU A 49  ? 0.2449 0.1330 0.1890 -0.0023 -0.0798 0.0075  272  LEU A N   
373  C CA  . LEU A 49  ? 0.2578 0.1405 0.1887 -0.0058 -0.0705 0.0060  272  LEU A CA  
374  C C   . LEU A 49  ? 0.2384 0.1581 0.1710 -0.0213 -0.0891 0.0137  272  LEU A C   
375  O O   . LEU A 49  ? 0.2486 0.1907 0.2141 -0.0356 -0.0954 0.0135  272  LEU A O   
376  C CB  . LEU A 49  ? 0.2886 0.1498 0.2119 -0.0256 -0.0526 0.0036  272  LEU A CB  
377  C CG  . LEU A 49  ? 0.3033 0.1635 0.2240 -0.0280 -0.0389 0.0001  272  LEU A CG  
378  C CD1 . LEU A 49  ? 0.3441 0.1593 0.2371 0.0039  -0.0061 0.0113  272  LEU A CD1 
379  C CD2 . LEU A 49  ? 0.2647 0.1881 0.2420 -0.0336 -0.0795 0.0118  272  LEU A CD2 
380  N N   . GLN A 50  ? 0.2085 0.1467 0.1740 0.0000  -0.0713 0.0015  273  GLN A N   
381  C CA  . GLN A 50  ? 0.2254 0.1412 0.1585 0.0058  -0.0609 0.0303  273  GLN A CA  
382  C C   . GLN A 50  ? 0.1858 0.1328 0.1781 0.0244  -0.0900 0.0310  273  GLN A C   
383  O O   . GLN A 50  ? 0.2003 0.1327 0.1956 0.0162  -0.0941 0.0223  273  GLN A O   
384  C CB  . GLN A 50  ? 0.2333 0.1678 0.1604 -0.0048 -0.0636 0.0179  273  GLN A CB  
385  C CG  . GLN A 50  ? 0.2748 0.1845 0.1821 0.0100  -0.0581 0.0030  273  GLN A CG  
386  C CD  . GLN A 50  ? 0.3192 0.1912 0.1980 0.0159  -0.0533 0.0074  273  GLN A CD  
387  O OE1 . GLN A 50  ? 0.3434 0.2268 0.2513 0.0138  -0.0139 0.0132  273  GLN A OE1 
388  N NE2 . GLN A 50  ? 0.3991 0.2132 0.2245 0.0336  -0.0382 0.0525  273  GLN A NE2 
389  N N   . GLY A 51  ? 0.2087 0.1188 0.1809 0.0302  -0.0667 0.0364  274  GLY A N   
390  C CA  . GLY A 51  ? 0.2293 0.1379 0.1568 0.0260  -0.0591 0.0193  274  GLY A CA  
391  C C   . GLY A 51  ? 0.1942 0.1460 0.1675 0.0197  -0.0890 0.0214  274  GLY A C   
392  O O   . GLY A 51  ? 0.2009 0.1741 0.1962 0.0120  -0.0664 0.0094  274  GLY A O   
393  N N   . THR A 52  ? 0.1980 0.1269 0.1379 0.0288  -0.0653 0.0226  275  THR A N   
394  C CA  . THR A 52  ? 0.1963 0.1129 0.1461 0.0375  -0.0569 0.0271  275  THR A CA  
395  C C   . THR A 52  ? 0.1695 0.1159 0.1661 0.0307  -0.0715 0.0106  275  THR A C   
396  O O   . THR A 52  ? 0.1861 0.1258 0.1791 0.0246  -0.0719 0.0234  275  THR A O   
397  C CB  . THR A 52  ? 0.1853 0.1201 0.1742 0.0336  -0.0659 0.0028  275  THR A CB  
398  O OG1 . THR A 52  ? 0.1621 0.1344 0.1855 0.0117  -0.0852 0.0030  275  THR A OG1 
399  C CG2 . THR A 52  ? 0.2268 0.1308 0.1843 0.0500  -0.0474 -0.0042 275  THR A CG2 
400  N N   . THR A 53  ? 0.1816 0.1215 0.1735 0.0132  -0.0544 -0.0009 276  THR A N   
401  C CA  . THR A 53  ? 0.1837 0.0986 0.1572 0.0022  -0.0604 0.0229  276  THR A CA  
402  C C   . THR A 53  ? 0.1950 0.1193 0.1320 -0.0100 -0.0902 0.0100  276  THR A C   
403  O O   . THR A 53  ? 0.2222 0.1295 0.1721 0.0073  -0.0808 0.0250  276  THR A O   
404  C CB  . THR A 53  ? 0.1731 0.1068 0.1592 0.0195  -0.0630 -0.0004 276  THR A CB  
405  O OG1 . THR A 53  ? 0.1879 0.1047 0.1862 -0.0086 -0.0462 0.0069  276  THR A OG1 
406  C CG2 . THR A 53  ? 0.2047 0.1185 0.1845 0.0491  -0.0811 0.0038  276  THR A CG2 
407  N N   . GLN A 54  ? 0.1949 0.1155 0.1491 -0.0021 -0.0715 0.0179  277  GLN A N   
408  C CA  . GLN A 54  ? 0.2014 0.1182 0.1657 0.0129  -0.0492 0.0085  277  GLN A CA  
409  C C   . GLN A 54  ? 0.1861 0.1055 0.1796 0.0134  -0.0599 0.0122  277  GLN A C   
410  O O   . GLN A 54  ? 0.1960 0.1224 0.2006 0.0021  -0.0481 0.0125  277  GLN A O   
411  C CB  . GLN A 54  ? 0.1913 0.1407 0.1521 0.0088  -0.0497 -0.0148 277  GLN A CB  
412  C CG  . GLN A 54  ? 0.1739 0.1346 0.1679 0.0236  -0.0736 -0.0094 277  GLN A CG  
413  C CD  . GLN A 54  ? 0.1659 0.1290 0.1743 0.0283  -0.0504 0.0023  277  GLN A CD  
414  O OE1 . GLN A 54  ? 0.2155 0.0933 0.1631 0.0159  -0.0575 0.0096  277  GLN A OE1 
415  N NE2 . GLN A 54  ? 0.1764 0.1390 0.1427 0.0121  -0.0517 -0.0123 277  GLN A NE2 
416  N N   . LEU A 55  ? 0.1817 0.0985 0.1834 -0.0011 -0.0432 0.0021  278  LEU A N   
417  C CA  . LEU A 55  ? 0.1988 0.1268 0.1666 0.0255  -0.0661 -0.0118 278  LEU A CA  
418  C C   . LEU A 55  ? 0.2080 0.1234 0.1794 0.0128  -0.0418 0.0147  278  LEU A C   
419  O O   . LEU A 55  ? 0.2208 0.1803 0.1931 0.0480  -0.0366 0.0032  278  LEU A O   
420  C CB  . LEU A 55  ? 0.2324 0.1549 0.1303 0.0194  -0.0759 -0.0116 278  LEU A CB  
421  C CG  . LEU A 55  ? 0.2753 0.2068 0.1583 -0.0139 -0.0687 -0.0243 278  LEU A CG  
422  C CD1 . LEU A 55  ? 0.3075 0.2186 0.2089 -0.0762 -0.0830 -0.0552 278  LEU A CD1 
423  C CD2 . LEU A 55  ? 0.3142 0.2311 0.1534 0.0230  0.0028  -0.0174 278  LEU A CD2 
424  N N   . VAL A 56  ? 0.2003 0.1047 0.1676 0.0165  -0.0531 0.0151  279  VAL A N   
425  C CA  . VAL A 56  ? 0.1832 0.1227 0.1760 0.0028  -0.0525 0.0235  279  VAL A CA  
426  C C   . VAL A 56  ? 0.1617 0.1169 0.1638 -0.0074 -0.0520 0.0195  279  VAL A C   
427  O O   . VAL A 56  ? 0.2004 0.1064 0.1541 0.0098  -0.0218 0.0117  279  VAL A O   
428  C CB  . VAL A 56  ? 0.1881 0.1338 0.1675 -0.0177 -0.0544 0.0089  279  VAL A CB  
429  C CG1 . VAL A 56  ? 0.2009 0.1248 0.1748 -0.0063 -0.0612 0.0154  279  VAL A CG1 
430  C CG2 . VAL A 56  ? 0.1992 0.1634 0.1857 -0.0383 -0.0622 -0.0056 279  VAL A CG2 
431  N N   . ALA A 57  ? 0.1869 0.1119 0.1907 -0.0148 -0.0609 0.0226  280  ALA A N   
432  C CA  . ALA A 57  ? 0.1753 0.1152 0.1769 0.0218  -0.0323 0.0028  280  ALA A CA  
433  C C   . ALA A 57  ? 0.1875 0.1040 0.1421 0.0174  -0.0204 0.0151  280  ALA A C   
434  O O   . ALA A 57  ? 0.1873 0.1149 0.1732 -0.0104 -0.0400 0.0205  280  ALA A O   
435  C CB  . ALA A 57  ? 0.1922 0.1050 0.2119 0.0471  -0.0104 0.0102  280  ALA A CB  
436  N N   . SER A 58  ? 0.2139 0.1222 0.1194 0.0064  -0.0427 0.0394  281  SER A N   
437  C CA  . SER A 58  ? 0.2142 0.1316 0.1268 0.0355  -0.0474 0.0474  281  SER A CA  
438  C C   . SER A 58  ? 0.2271 0.1391 0.1663 0.0488  -0.0205 0.0362  281  SER A C   
439  O O   . SER A 58  ? 0.2841 0.1619 0.1789 0.0407  -0.0255 0.0190  281  SER A O   
440  C CB  . SER A 58  ? 0.2100 0.1191 0.1701 0.0415  -0.0580 0.0447  281  SER A CB  
441  O OG  . SER A 58  ? 0.2191 0.1107 0.2092 0.0214  -0.0604 0.0372  281  SER A OG  
442  N N   . ASN A 59  ? 0.1388 0.1153 0.1609 0.0136  -0.0504 0.0287  282  ASN A N   
443  C CA  . ASN A 59  ? 0.1389 0.1178 0.1767 0.0166  -0.0453 0.0090  282  ASN A CA  
444  C C   . ASN A 59  ? 0.1660 0.1216 0.1475 0.0045  -0.0515 0.0294  282  ASN A C   
445  O O   . ASN A 59  ? 0.1722 0.1315 0.1780 0.0030  -0.0425 0.0236  282  ASN A O   
446  C CB  . ASN A 59  ? 0.1337 0.1153 0.2065 0.0083  -0.0411 0.0222  282  ASN A CB  
447  C CG  . ASN A 59  ? 0.1764 0.1242 0.2153 0.0084  -0.0260 0.0176  282  ASN A CG  
448  O OD1 . ASN A 59  ? 0.2116 0.1408 0.2142 -0.0204 -0.0264 0.0435  282  ASN A OD1 
449  N ND2 . ASN A 59  ? 0.1627 0.1260 0.2171 0.0017  -0.0300 -0.0227 282  ASN A ND2 
450  N N   . ILE A 60  ? 0.1684 0.1080 0.1355 -0.0122 -0.0498 0.0167  283  ILE A N   
451  C CA  . ILE A 60  ? 0.1788 0.0979 0.1360 -0.0121 -0.0458 0.0257  283  ILE A CA  
452  C C   . ILE A 60  ? 0.1738 0.0902 0.1257 0.0053  -0.0421 0.0079  283  ILE A C   
453  O O   . ILE A 60  ? 0.1919 0.1113 0.1390 0.0009  -0.0473 -0.0043 283  ILE A O   
454  C CB  . ILE A 60  ? 0.1842 0.1152 0.1146 -0.0120 -0.0330 0.0283  283  ILE A CB  
455  C CG1 . ILE A 60  ? 0.1890 0.1396 0.1260 0.0014  -0.0398 0.0209  283  ILE A CG1 
456  C CG2 . ILE A 60  ? 0.1849 0.1043 0.1414 -0.0094 -0.0022 0.0165  283  ILE A CG2 
457  C CD1 . ILE A 60  ? 0.2342 0.1525 0.1517 0.0090  -0.0334 0.0306  283  ILE A CD1 
458  N N   . CYS A 61  ? 0.1647 0.0946 0.1388 -0.0049 -0.0560 -0.0072 284  CYS A N   
459  C CA  . CYS A 61  ? 0.1587 0.1198 0.1486 -0.0078 -0.0611 -0.0119 284  CYS A CA  
460  C C   . CYS A 61  ? 0.1481 0.1372 0.1512 0.0130  -0.0515 0.0116  284  CYS A C   
461  O O   . CYS A 61  ? 0.1677 0.1572 0.1840 0.0022  -0.0456 -0.0046 284  CYS A O   
462  C CB  . CYS A 61  ? 0.1738 0.1161 0.1475 -0.0243 -0.0480 -0.0032 284  CYS A CB  
463  S SG  . CYS A 61  ? 0.1792 0.1218 0.1888 0.0091  -0.0472 0.0133  284  CYS A SG  
464  N N   . ALA A 62  ? 0.1480 0.1367 0.1604 0.0155  -0.0508 0.0085  285  ALA A N   
465  C CA  . ALA A 62  ? 0.1717 0.1440 0.1639 0.0154  -0.0426 0.0062  285  ALA A CA  
466  C C   . ALA A 62  ? 0.1609 0.1568 0.1681 0.0197  -0.0540 -0.0055 285  ALA A C   
467  O O   . ALA A 62  ? 0.1837 0.1712 0.1799 0.0201  -0.0477 0.0064  285  ALA A O   
468  C CB  . ALA A 62  ? 0.1964 0.1479 0.1571 -0.0099 -0.0007 0.0200  285  ALA A CB  
469  N N   . PHE A 63  ? 0.1533 0.1688 0.1910 0.0165  -0.0285 -0.0203 286  PHE A N   
470  C CA  . PHE A 63  ? 0.1487 0.1798 0.1868 0.0445  -0.0351 -0.0167 286  PHE A CA  
471  C C   . PHE A 63  ? 0.1405 0.1976 0.2075 0.0367  -0.0456 -0.0068 286  PHE A C   
472  O O   . PHE A 63  ? 0.1625 0.1970 0.1990 0.0139  -0.0360 -0.0002 286  PHE A O   
473  C CB  . PHE A 63  ? 0.2201 0.1688 0.1848 0.0614  -0.0220 -0.0271 286  PHE A CB  
474  C CG  . PHE A 63  ? 0.2224 0.1738 0.2087 0.0389  -0.0162 -0.0318 286  PHE A CG  
475  C CD1 . PHE A 63  ? 0.2335 0.1808 0.2209 0.0648  -0.0330 -0.0072 286  PHE A CD1 
476  C CD2 . PHE A 63  ? 0.2428 0.1765 0.2102 0.0343  -0.0439 -0.0617 286  PHE A CD2 
477  C CE1 . PHE A 63  ? 0.2375 0.1992 0.2297 0.0498  -0.0059 -0.0192 286  PHE A CE1 
478  C CE2 . PHE A 63  ? 0.2743 0.1912 0.2152 0.0498  -0.0089 -0.0345 286  PHE A CE2 
479  C CZ  . PHE A 63  ? 0.2556 0.1874 0.2267 0.0615  -0.0170 -0.0408 286  PHE A CZ  
480  N N   . ARG A 64  ? 0.1545 0.2035 0.2309 0.0119  -0.0344 -0.0298 287  ARG A N   
481  C CA  . ARG A 64  ? 0.1550 0.2044 0.2568 0.0128  -0.0381 -0.0598 287  ARG A CA  
482  C C   . ARG A 64  ? 0.1482 0.1993 0.2233 0.0086  -0.0419 -0.0472 287  ARG A C   
483  O O   . ARG A 64  ? 0.1786 0.2063 0.2250 0.0100  -0.0299 -0.0287 287  ARG A O   
484  C CB  . ARG A 64  ? 0.2220 0.2183 0.3323 0.0231  -0.0236 -0.0467 287  ARG A CB  
485  C CG  . ARG A 64  ? 0.3692 0.2687 0.4069 0.0535  0.0154  -0.0203 287  ARG A CG  
486  C CD  . ARG A 64  ? 0.5014 0.2987 0.4270 0.0397  0.0391  -0.0141 287  ARG A CD  
487  N NE  . ARG A 64  ? 0.5859 0.3156 0.4385 0.0341  0.0609  -0.0097 287  ARG A NE  
488  C CZ  . ARG A 64  ? 0.6326 0.3131 0.4173 0.0142  0.0605  -0.0018 287  ARG A CZ  
489  N NH1 . ARG A 64  ? 0.5898 0.2817 0.3391 0.0314  0.0121  0.0113  287  ARG A NH1 
490  N NH2 . ARG A 64  ? 0.6795 0.3457 0.4402 0.0116  0.0972  -0.0041 287  ARG A NH2 
491  N N   . GLY A 65  ? 0.1472 0.1975 0.2190 0.0151  -0.0180 -0.0633 288  GLY A N   
492  C CA  . GLY A 65  ? 0.1609 0.2094 0.2286 0.0144  0.0302  -0.0471 288  GLY A CA  
493  C C   . GLY A 65  ? 0.1602 0.2007 0.2340 0.0097  -0.0036 -0.0560 288  GLY A C   
494  O O   . GLY A 65  ? 0.1941 0.2022 0.2562 0.0137  -0.0206 -0.0437 288  GLY A O   
495  N N   . SER A 66  ? 0.1835 0.1963 0.2085 0.0215  -0.0103 -0.0663 289  SER A N   
496  C CA  . SER A 66  ? 0.1765 0.1769 0.2173 0.0015  -0.0149 -0.0542 289  SER A CA  
497  C C   . SER A 66  ? 0.2034 0.1668 0.1878 0.0253  -0.0056 -0.0303 289  SER A C   
498  O O   . SER A 66  ? 0.2651 0.1897 0.2260 0.0210  0.0025  0.0017  289  SER A O   
499  C CB  . SER A 66  ? 0.1731 0.2047 0.2699 0.0369  -0.0324 -0.0246 289  SER A CB  
500  O OG  . SER A 66  ? 0.2265 0.2607 0.3134 0.0258  -0.0080 -0.0535 289  SER A OG  
501  N N   . ILE A 67  ? 0.1671 0.1987 0.2299 0.0150  -0.0006 -0.0405 290  ILE A N   
502  C CA  . ILE A 67  ? 0.1757 0.1922 0.2469 0.0200  0.0298  -0.0494 290  ILE A CA  
503  C C   . ILE A 67  ? 0.1910 0.2193 0.2632 0.0251  0.0011  -0.0350 290  ILE A C   
504  O O   . ILE A 67  ? 0.2317 0.2257 0.2940 0.0256  0.0366  -0.0251 290  ILE A O   
505  C CB  . ILE A 67  ? 0.1852 0.1885 0.2215 0.0162  -0.0106 -0.0580 290  ILE A CB  
506  C CG1 . ILE A 67  ? 0.2000 0.1960 0.2288 0.0293  0.0230  -0.0280 290  ILE A CG1 
507  C CG2 . ILE A 67  ? 0.2348 0.1736 0.2597 0.0201  0.0244  -0.0683 290  ILE A CG2 
508  C CD1 . ILE A 67  ? 0.2109 0.1962 0.2452 0.0202  0.0029  -0.0029 290  ILE A CD1 
509  N N   . SER A 68  ? 0.1818 0.2446 0.2943 0.0584  -0.0294 -0.0510 291  SER A N   
510  C CA  . SER A 68  ? 0.2122 0.2955 0.3183 0.0712  -0.0247 -0.0663 291  SER A CA  
511  C C   . SER A 68  ? 0.2349 0.2927 0.3445 0.0785  -0.0241 -0.0627 291  SER A C   
512  O O   . SER A 68  ? 0.2596 0.3140 0.4009 0.0756  -0.0352 -0.0338 291  SER A O   
513  C CB  . SER A 68  ? 0.2401 0.3606 0.3901 0.0930  0.0092  -0.0458 291  SER A CB  
514  O OG  . SER A 68  ? 0.3105 0.4099 0.4527 0.0642  0.0256  -0.0487 291  SER A OG  
515  N N   . GLY A 69  ? 0.2290 0.2713 0.2774 0.0721  -0.0050 -0.0684 292  GLY A N   
516  C CA  . GLY A 69  ? 0.2582 0.2578 0.2755 0.0447  0.0489  -0.0701 292  GLY A CA  
517  C C   . GLY A 69  ? 0.2617 0.2393 0.2771 0.0380  0.0472  -0.0488 292  GLY A C   
518  O O   . GLY A 69  ? 0.2823 0.2358 0.2727 0.0374  0.0491  -0.0391 292  GLY A O   
519  N N   . HIS A 70  ? 0.2463 0.2315 0.2929 0.0561  0.0258  -0.0424 293  HIS A N   
520  C CA  . HIS A 70  ? 0.2610 0.2332 0.3133 0.0413  0.0351  -0.0490 293  HIS A CA  
521  C C   . HIS A 70  ? 0.3107 0.3004 0.3658 0.0364  0.0352  -0.0364 293  HIS A C   
522  O O   . HIS A 70  ? 0.2964 0.2968 0.3561 0.0568  0.0229  -0.0418 293  HIS A O   
523  C CB  . HIS A 70  ? 0.2627 0.1969 0.3019 0.0429  0.0409  -0.0477 293  HIS A CB  
524  C CG  . HIS A 70  ? 0.2828 0.1771 0.3001 0.0320  0.0565  -0.0438 293  HIS A CG  
525  N ND1 . HIS A 70  ? 0.2851 0.1717 0.2855 0.0290  0.0351  -0.0324 293  HIS A ND1 
526  C CD2 . HIS A 70  ? 0.2962 0.1885 0.3223 0.0655  0.0597  -0.0418 293  HIS A CD2 
527  C CE1 . HIS A 70  ? 0.3231 0.1756 0.3235 0.0433  0.0388  -0.0173 293  HIS A CE1 
528  N NE2 . HIS A 70  ? 0.3175 0.1797 0.3315 0.0547  0.0667  -0.0239 293  HIS A NE2 
529  N N   . GLU A 71  ? 0.3670 0.3814 0.4519 0.0046  0.0305  -0.0378 294  GLU A N   
530  C CA  . GLU A 71  ? 0.4133 0.4655 0.5293 -0.0172 0.0238  -0.0385 294  GLU A CA  
531  C C   . GLU A 71  ? 0.5544 0.5814 0.6230 -0.0603 -0.0044 -0.0521 294  GLU A C   
532  O O   . GLU A 71  ? 0.5434 0.5716 0.6271 -0.0846 -0.0232 -0.0675 294  GLU A O   
533  C CB  . GLU A 71  ? 0.3431 0.4275 0.5341 0.0067  0.0566  -0.0293 294  GLU A CB  
534  C CG  . GLU A 71  ? 0.2623 0.3679 0.5169 0.0540  0.0608  -0.0203 294  GLU A CG  
535  C CD  . GLU A 71  ? 0.2620 0.3186 0.4856 0.0829  0.0699  0.0131  294  GLU A CD  
536  O OE1 . GLU A 71  ? 0.3150 0.3102 0.4726 0.0802  0.0706  0.0297  294  GLU A OE1 
537  O OE2 . GLU A 71  ? 0.2525 0.2726 0.4844 0.0779  0.0823  0.0166  294  GLU A OE2 
555  N N   . ASP A 75  ? 1.0501 1.0729 1.0702 0.1509  -0.1817 -0.1111 298  ASP A N   
556  C CA  . ASP A 75  ? 0.7292 0.7792 0.7743 0.1691  -0.1705 -0.1099 298  ASP A CA  
557  C C   . ASP A 75  ? 0.4846 0.6061 0.5998 0.2017  -0.1346 -0.1129 298  ASP A C   
558  O O   . ASP A 75  ? 0.3864 0.5671 0.5628 0.2395  -0.1433 -0.0983 298  ASP A O   
563  N N   . GLN A 76  ? 0.3832 0.4720 0.4680 0.2073  -0.0828 -0.1276 299  GLN A N   
564  C CA  . GLN A 76  ? 0.3521 0.3870 0.3506 0.1641  -0.0549 -0.1275 299  GLN A CA  
565  C C   . GLN A 76  ? 0.3299 0.3139 0.3071 0.1188  -0.0208 -0.1070 299  GLN A C   
566  O O   . GLN A 76  ? 0.3161 0.2986 0.2950 0.1024  -0.0001 -0.0816 299  GLN A O   
567  C CB  . GLN A 76  ? 0.3785 0.3796 0.3418 0.1604  -0.0515 -0.1278 299  GLN A CB  
568  C CG  . GLN A 76  ? 0.4249 0.3822 0.3913 0.1429  -0.0360 -0.0980 299  GLN A CG  
569  C CD  . GLN A 76  ? 0.5087 0.3969 0.4243 0.1248  0.0047  -0.0737 299  GLN A CD  
570  O OE1 . GLN A 76  ? 0.5443 0.4064 0.4296 0.0979  0.0102  -0.0758 299  GLN A OE1 
571  N NE2 . GLN A 76  ? 0.5356 0.4065 0.4476 0.1063  0.0352  -0.0664 299  GLN A NE2 
572  N N   . HIS A 77  ? 0.3082 0.2565 0.2507 0.0969  -0.0104 -0.1091 300  HIS A N   
573  C CA  . HIS A 77  ? 0.3083 0.2239 0.2162 0.0726  -0.0525 -0.0971 300  HIS A CA  
574  C C   . HIS A 77  ? 0.2958 0.1982 0.2081 0.0592  -0.0330 -0.0893 300  HIS A C   
575  O O   . HIS A 77  ? 0.3159 0.2400 0.1976 0.0990  -0.0016 -0.0716 300  HIS A O   
576  C CB  . HIS A 77  ? 0.3294 0.2341 0.2456 0.0672  -0.0833 -0.0869 300  HIS A CB  
577  C CG  . HIS A 77  ? 0.3958 0.2323 0.2797 0.0290  -0.0682 -0.1048 300  HIS A CG  
578  N ND1 . HIS A 77  ? 0.4305 0.2382 0.2845 0.0158  -0.0561 -0.0866 300  HIS A ND1 
579  C CD2 . HIS A 77  ? 0.4312 0.2366 0.2841 0.0112  -0.0586 -0.1139 300  HIS A CD2 
580  C CE1 . HIS A 77  ? 0.4466 0.2444 0.2934 0.0185  -0.0492 -0.0938 300  HIS A CE1 
581  N NE2 . HIS A 77  ? 0.4463 0.2516 0.3124 0.0205  -0.0568 -0.0912 300  HIS A NE2 
582  N N   . GLN A 78  ? 0.2829 0.1717 0.2427 0.0299  -0.0156 -0.0552 301  GLN A N   
583  C CA  . GLN A 78  ? 0.2343 0.1658 0.2470 0.0157  -0.0184 -0.0592 301  GLN A CA  
584  C C   . GLN A 78  ? 0.2111 0.1899 0.2411 0.0157  -0.0026 -0.0856 301  GLN A C   
585  O O   . GLN A 78  ? 0.2580 0.2012 0.2756 0.0283  0.0495  -0.0945 301  GLN A O   
586  C CB  . GLN A 78  ? 0.2371 0.1901 0.2583 0.0108  -0.0020 -0.0256 301  GLN A CB  
587  C CG  . GLN A 78  ? 0.2464 0.1931 0.2659 -0.0004 -0.0409 -0.0252 301  GLN A CG  
588  C CD  . GLN A 78  ? 0.3363 0.2443 0.3184 -0.0018 -0.0407 -0.0013 301  GLN A CD  
589  O OE1 . GLN A 78  ? 0.3768 0.2702 0.3532 0.0052  -0.0534 0.0264  301  GLN A OE1 
590  N NE2 . GLN A 78  ? 0.3795 0.2477 0.3309 -0.0434 -0.0369 -0.0186 301  GLN A NE2 
591  N N   . TRP A 79  ? 0.2131 0.1770 0.2264 0.0093  -0.0420 -0.0646 302  TRP A N   
592  C CA  . TRP A 79  ? 0.1859 0.1759 0.2227 0.0421  -0.0427 -0.0429 302  TRP A CA  
593  C C   . TRP A 79  ? 0.2137 0.1859 0.2202 0.0388  -0.0275 -0.0391 302  TRP A C   
594  O O   . TRP A 79  ? 0.2082 0.1922 0.2305 0.0210  -0.0260 -0.0471 302  TRP A O   
595  C CB  . TRP A 79  ? 0.1921 0.1593 0.2356 0.0374  -0.0282 -0.0195 302  TRP A CB  
596  C CG  . TRP A 79  ? 0.2250 0.1635 0.2254 0.0423  -0.0092 -0.0203 302  TRP A CG  
597  C CD1 . TRP A 79  ? 0.2225 0.1690 0.2176 0.0562  -0.0215 -0.0078 302  TRP A CD1 
598  C CD2 . TRP A 79  ? 0.2465 0.1605 0.2447 0.0330  0.0207  -0.0471 302  TRP A CD2 
599  N NE1 . TRP A 79  ? 0.2355 0.1849 0.2137 0.0422  0.0220  -0.0207 302  TRP A NE1 
600  C CE2 . TRP A 79  ? 0.2578 0.1821 0.2315 0.0300  0.0254  -0.0425 302  TRP A CE2 
601  C CE3 . TRP A 79  ? 0.3032 0.1661 0.2740 0.0123  0.0614  -0.0620 302  TRP A CE3 
602  C CZ2 . TRP A 79  ? 0.2904 0.1988 0.2340 0.0013  0.0283  -0.0612 302  TRP A CZ2 
603  C CZ3 . TRP A 79  ? 0.3183 0.1788 0.2762 0.0027  0.0606  -0.0684 302  TRP A CZ3 
604  C CH2 . TRP A 79  ? 0.3245 0.2057 0.2510 0.0009  0.0716  -0.0610 302  TRP A CH2 
605  N N   . HIS A 80  ? 0.2037 0.1802 0.2241 0.0576  -0.0174 -0.0385 303  HIS A N   
606  C CA  . HIS A 80  ? 0.1969 0.1885 0.2463 0.0847  -0.0512 -0.0183 303  HIS A CA  
607  C C   . HIS A 80  ? 0.2165 0.1763 0.2446 0.0585  -0.0179 -0.0346 303  HIS A C   
608  O O   . HIS A 80  ? 0.2342 0.1931 0.2541 0.0642  -0.0008 -0.0339 303  HIS A O   
609  C CB  . HIS A 80  ? 0.2096 0.2082 0.2728 0.1004  -0.0172 -0.0191 303  HIS A CB  
610  C CG  . HIS A 80  ? 0.2208 0.2291 0.2931 0.0794  -0.0311 -0.0387 303  HIS A CG  
611  N ND1 . HIS A 80  ? 0.2436 0.2580 0.3226 0.0734  -0.0141 -0.0435 303  HIS A ND1 
612  C CD2 . HIS A 80  ? 0.2263 0.2671 0.3123 0.0702  -0.0152 -0.0341 303  HIS A CD2 
613  C CE1 . HIS A 80  ? 0.2499 0.2728 0.3404 0.0724  -0.0152 -0.0210 303  HIS A CE1 
614  N NE2 . HIS A 80  ? 0.2176 0.2704 0.3416 0.0724  -0.0133 -0.0408 303  HIS A NE2 
615  N N   . PHE A 81  ? 0.1854 0.1613 0.2232 0.0464  -0.0358 -0.0409 304  PHE A N   
616  C CA  . PHE A 81  ? 0.1822 0.1837 0.2568 0.0605  -0.0340 -0.0393 304  PHE A CA  
617  C C   . PHE A 81  ? 0.1825 0.1856 0.2443 0.0374  -0.0277 -0.0415 304  PHE A C   
618  O O   . PHE A 81  ? 0.2123 0.1700 0.2375 0.0291  -0.0187 -0.0088 304  PHE A O   
619  C CB  . PHE A 81  ? 0.1698 0.1847 0.2619 0.0746  -0.0379 -0.0345 304  PHE A CB  
620  C CG  . PHE A 81  ? 0.1691 0.1910 0.2639 0.0666  -0.0661 -0.0634 304  PHE A CG  
621  C CD1 . PHE A 81  ? 0.1826 0.1901 0.3145 0.0474  -0.0548 -0.0562 304  PHE A CD1 
622  C CD2 . PHE A 81  ? 0.2217 0.2198 0.3607 0.0514  -0.0275 -0.0862 304  PHE A CD2 
623  C CE1 . PHE A 81  ? 0.1764 0.1987 0.3360 0.0187  -0.0608 -0.0562 304  PHE A CE1 
624  C CE2 . PHE A 81  ? 0.2255 0.2243 0.4088 0.0580  -0.0441 -0.0756 304  PHE A CE2 
625  C CZ  . PHE A 81  ? 0.2120 0.1948 0.3731 0.0313  -0.0349 -0.0736 304  PHE A CZ  
626  N N   . SER A 82  ? 0.1703 0.1880 0.2796 0.0448  -0.0319 -0.0554 305  SER A N   
627  C CA  . SER A 82  ? 0.1859 0.2065 0.2872 0.0668  -0.0149 -0.0406 305  SER A CA  
628  C C   . SER A 82  ? 0.2237 0.2007 0.2636 0.0687  -0.0433 -0.0357 305  SER A C   
629  O O   . SER A 82  ? 0.3130 0.2030 0.2618 0.0753  -0.0165 -0.0274 305  SER A O   
630  C CB  . SER A 82  ? 0.1881 0.2299 0.3181 0.0566  -0.0063 -0.0731 305  SER A CB  
631  O OG  . SER A 82  ? 0.2296 0.2666 0.3490 0.0414  -0.0136 -0.0748 305  SER A OG  
632  N N   . ILE A 83  ? 0.1703 0.2075 0.2559 0.0535  -0.0587 -0.0359 306  ILE A N   
633  C CA  . ILE A 83  ? 0.1730 0.2264 0.2857 0.0693  -0.0746 -0.0399 306  ILE A CA  
634  C C   . ILE A 83  ? 0.2081 0.2473 0.2941 0.0955  -0.1087 -0.0295 306  ILE A C   
635  O O   . ILE A 83  ? 0.2651 0.2654 0.3166 0.0959  -0.1270 -0.0503 306  ILE A O   
636  C CB  . ILE A 83  ? 0.1980 0.2331 0.3243 0.0475  -0.0314 -0.0333 306  ILE A CB  
637  C CG1 . ILE A 83  ? 0.2092 0.2476 0.3787 0.0703  -0.0001 -0.0059 306  ILE A CG1 
638  C CG2 . ILE A 83  ? 0.2142 0.2528 0.3676 0.0097  0.0204  -0.0653 306  ILE A CG2 
639  C CD1 . ILE A 83  ? 0.2190 0.2377 0.3982 0.0660  -0.0361 0.0333  306  ILE A CD1 
640  N N   . THR A 84  ? 0.2256 0.2593 0.3168 0.0714  -0.1050 -0.0776 307  THR A N   
641  C CA  . THR A 84  ? 0.2384 0.2656 0.3298 0.0686  -0.1233 -0.0858 307  THR A CA  
642  C C   . THR A 84  ? 0.2315 0.2666 0.3129 0.0655  -0.1334 -0.0803 307  THR A C   
643  O O   . THR A 84  ? 0.2260 0.2769 0.3245 0.0657  -0.1077 -0.0899 307  THR A O   
644  C CB  . THR A 84  ? 0.2420 0.2778 0.3870 0.0495  -0.0769 -0.1069 307  THR A CB  
645  O OG1 . THR A 84  ? 0.2423 0.2664 0.3908 0.0207  -0.0945 -0.1077 307  THR A OG1 
646  C CG2 . THR A 84  ? 0.2332 0.3084 0.4078 0.0285  -0.0809 -0.1240 307  THR A CG2 
647  N N   . ASN A 85  ? 0.2571 0.2539 0.3092 0.0413  -0.1010 -0.0741 308  ASN A N   
648  C CA  . ASN A 85  ? 0.2610 0.2544 0.3043 0.0275  -0.0869 -0.0543 308  ASN A CA  
649  C C   . ASN A 85  ? 0.2553 0.2200 0.2623 0.0118  -0.0862 -0.0400 308  ASN A C   
650  O O   . ASN A 85  ? 0.2679 0.2119 0.2679 0.0291  -0.0539 -0.0440 308  ASN A O   
651  C CB  . ASN A 85  ? 0.2552 0.2822 0.3095 0.0280  -0.1236 -0.0436 308  ASN A CB  
652  C CG  . ASN A 85  ? 0.2718 0.3104 0.3435 0.0104  -0.1097 -0.0407 308  ASN A CG  
653  O OD1 . ASN A 85  ? 0.2704 0.3002 0.3739 0.0209  -0.1127 -0.0247 308  ASN A OD1 
654  N ND2 . ASN A 85  ? 0.2921 0.3346 0.3415 -0.0095 -0.0911 -0.0641 308  ASN A ND2 
655  N N   . PRO A 86  ? 0.2419 0.2205 0.2552 0.0179  -0.0824 0.0119  309  PRO A N   
656  C CA  . PRO A 86  ? 0.2722 0.2115 0.2607 0.0232  -0.0536 0.0190  309  PRO A CA  
657  C C   . PRO A 86  ? 0.3126 0.2125 0.2556 0.0125  -0.0859 -0.0062 309  PRO A C   
658  O O   . PRO A 86  ? 0.3265 0.2108 0.2755 0.0596  -0.0305 0.0064  309  PRO A O   
659  C CB  . PRO A 86  ? 0.2575 0.2151 0.2744 0.0406  -0.0335 0.0131  309  PRO A CB  
660  C CG  . PRO A 86  ? 0.2539 0.2246 0.2903 0.0080  -0.0413 0.0122  309  PRO A CG  
661  C CD  . PRO A 86  ? 0.2479 0.2245 0.2758 0.0108  -0.0567 0.0127  309  PRO A CD  
662  N N   . ASN A 87  ? 0.3776 0.2318 0.2956 -0.0586 -0.0646 -0.0181 310  ASN A N   
663  C CA  . ASN A 87  ? 0.4268 0.2657 0.3129 -0.1070 -0.0464 -0.0285 310  ASN A CA  
664  C C   . ASN A 87  ? 0.4270 0.2971 0.3545 -0.1273 -0.0480 -0.0240 310  ASN A C   
665  O O   . ASN A 87  ? 0.4609 0.3104 0.3771 -0.1445 -0.0075 -0.0223 310  ASN A O   
666  C CB  . ASN A 87  ? 0.4726 0.2876 0.3217 -0.1366 -0.0740 -0.0477 310  ASN A CB  
667  C CG  . ASN A 87  ? 0.4707 0.3259 0.3412 -0.1553 -0.0949 -0.0466 310  ASN A CG  
668  O OD1 . ASN A 87  ? 0.4511 0.3576 0.3651 -0.1481 -0.0984 -0.0070 310  ASN A OD1 
669  N ND2 . ASN A 87  ? 0.5153 0.3409 0.3586 -0.1598 -0.0446 -0.0584 310  ASN A ND2 
670  N N   . GLY A 88  ? 0.3889 0.3262 0.3674 -0.0995 -0.0759 -0.0196 311  GLY A N   
671  C CA  . GLY A 88  ? 0.3723 0.3557 0.3943 -0.1027 -0.1025 -0.0176 311  GLY A CA  
672  C C   . GLY A 88  ? 0.3566 0.3805 0.4302 -0.0778 -0.1092 0.0133  311  GLY A C   
673  O O   . GLY A 88  ? 0.3464 0.3933 0.4593 -0.0663 -0.1029 0.0242  311  GLY A O   
674  N N   . THR A 89  ? 0.3510 0.3962 0.4234 -0.0852 -0.1183 0.0197  312  THR A N   
675  C CA  . THR A 89  ? 0.3246 0.4105 0.4365 -0.0955 -0.1388 0.0135  312  THR A CA  
676  C C   . THR A 89  ? 0.3052 0.4304 0.4792 -0.0671 -0.1181 -0.0052 312  THR A C   
677  O O   . THR A 89  ? 0.3018 0.4237 0.4778 -0.0976 -0.1110 -0.0229 312  THR A O   
678  C CB  . THR A 89  ? 0.3615 0.4033 0.4505 -0.1385 -0.1072 -0.0062 312  THR A CB  
679  O OG1 . THR A 89  ? 0.3503 0.4035 0.4492 -0.1315 -0.1160 -0.0126 312  THR A OG1 
680  C CG2 . THR A 89  ? 0.4024 0.4080 0.4638 -0.1415 -0.0701 -0.0106 312  THR A CG2 
681  N N   . PRO A 90  ? 0.2701 0.4443 0.5405 -0.0547 -0.1057 -0.0075 313  PRO A N   
682  C CA  . PRO A 90  ? 0.2385 0.4291 0.5563 -0.0548 -0.1400 -0.0165 313  PRO A CA  
683  C C   . PRO A 90  ? 0.2655 0.4184 0.5701 -0.0520 -0.1603 -0.0250 313  PRO A C   
684  O O   . PRO A 90  ? 0.2955 0.4200 0.5981 -0.0547 -0.1218 -0.0103 313  PRO A O   
685  C CB  . PRO A 90  ? 0.2641 0.4427 0.5638 -0.0422 -0.1081 -0.0107 313  PRO A CB  
686  C CG  . PRO A 90  ? 0.2874 0.4484 0.5741 -0.0300 -0.0680 -0.0022 313  PRO A CG  
687  C CD  . PRO A 90  ? 0.2904 0.4527 0.5689 -0.0394 -0.0714 -0.0066 313  PRO A CD  
688  N N   . PHE A 91  ? 0.2768 0.4084 0.5839 -0.0337 -0.1940 -0.0424 314  PHE A N   
689  C CA  . PHE A 91  ? 0.2873 0.4198 0.5977 0.0045  -0.2139 -0.0356 314  PHE A CA  
690  C C   . PHE A 91  ? 0.3045 0.4836 0.5905 0.0132  -0.2264 -0.0264 314  PHE A C   
691  O O   . PHE A 91  ? 0.3282 0.5021 0.5985 0.0193  -0.2272 -0.0262 314  PHE A O   
692  C CB  . PHE A 91  ? 0.2866 0.3832 0.6301 0.0284  -0.1817 -0.0209 314  PHE A CB  
693  C CG  . PHE A 91  ? 0.2812 0.3517 0.6454 0.0343  -0.1755 -0.0144 314  PHE A CG  
694  C CD1 . PHE A 91  ? 0.2645 0.3472 0.6470 0.0210  -0.1877 -0.0104 314  PHE A CD1 
695  C CD2 . PHE A 91  ? 0.2633 0.3336 0.6418 0.0326  -0.1886 -0.0048 314  PHE A CD2 
696  C CE1 . PHE A 91  ? 0.2608 0.3411 0.6321 0.0161  -0.1921 -0.0096 314  PHE A CE1 
697  C CE2 . PHE A 91  ? 0.2652 0.3337 0.6437 0.0245  -0.1940 -0.0178 314  PHE A CE2 
698  C CZ  . PHE A 91  ? 0.2649 0.3354 0.6340 0.0235  -0.1940 -0.0082 314  PHE A CZ  
699  N N   . ASP A 92  ? 0.3235 0.5273 0.6242 -0.0004 -0.2024 -0.0350 315  ASP A N   
700  C CA  . ASP A 92  ? 0.3440 0.5724 0.6484 0.0012  -0.1651 -0.0244 315  ASP A CA  
701  C C   . ASP A 92  ? 0.3067 0.5897 0.6581 -0.0054 -0.1581 -0.0126 315  ASP A C   
702  O O   . ASP A 92  ? 0.2900 0.5950 0.6485 -0.0327 -0.1780 -0.0058 315  ASP A O   
703  C CB  . ASP A 92  ? 0.3972 0.5963 0.6668 0.0032  -0.1543 -0.0258 315  ASP A CB  
704  C CG  . ASP A 92  ? 0.4476 0.6212 0.6993 0.0106  -0.1218 -0.0227 315  ASP A CG  
705  O OD1 . ASP A 92  ? 0.4646 0.6323 0.7069 0.0119  -0.1158 -0.0257 315  ASP A OD1 
706  O OD2 . ASP A 92  ? 0.4763 0.6312 0.7108 0.0063  -0.1004 -0.0180 315  ASP A OD2 
707  N N   . PRO A 93  ? 0.3074 0.5996 0.6756 0.0060  -0.1145 0.0027  316  PRO A N   
708  C CA  . PRO A 93  ? 0.3042 0.6057 0.6866 0.0134  -0.0852 0.0079  316  PRO A CA  
709  C C   . PRO A 93  ? 0.3093 0.6106 0.6942 0.0351  -0.0796 0.0170  316  PRO A C   
710  O O   . PRO A 93  ? 0.2723 0.6144 0.7016 0.0592  -0.1024 0.0201  316  PRO A O   
711  C CB  . PRO A 93  ? 0.3409 0.6110 0.7065 0.0005  -0.0365 0.0058  316  PRO A CB  
712  C CG  . PRO A 93  ? 0.3521 0.6122 0.7095 -0.0020 -0.0218 0.0027  316  PRO A CG  
713  C CD  . PRO A 93  ? 0.3226 0.6071 0.6908 -0.0001 -0.0666 0.0036  316  PRO A CD  
714  N N   . THR A 94  ? 0.3338 0.6085 0.6763 0.0401  -0.0865 0.0240  317  THR A N   
715  C CA  . THR A 94  ? 0.3514 0.6004 0.6467 0.0432  -0.1025 0.0426  317  THR A CA  
716  C C   . THR A 94  ? 0.3892 0.5763 0.6070 0.0179  -0.0670 0.0351  317  THR A C   
717  O O   . THR A 94  ? 0.4015 0.5862 0.6059 0.0345  -0.0728 0.0381  317  THR A O   
718  C CB  . THR A 94  ? 0.3359 0.6143 0.6498 0.0704  -0.1524 0.0668  317  THR A CB  
719  O OG1 . THR A 94  ? 0.3403 0.6229 0.6641 0.0550  -0.1463 0.0471  317  THR A OG1 
720  C CG2 . THR A 94  ? 0.3464 0.6182 0.6447 0.0820  -0.1634 0.0919  317  THR A CG2 
721  N N   . GLU A 95  ? 0.3911 0.5351 0.5570 -0.0066 -0.0599 0.0223  318  GLU A N   
722  C CA  . GLU A 95  ? 0.3983 0.4889 0.4931 -0.0371 -0.0591 0.0113  318  GLU A CA  
723  C C   . GLU A 95  ? 0.3425 0.4770 0.4659 -0.0542 -0.0573 0.0029  318  GLU A C   
724  O O   . GLU A 95  ? 0.3325 0.4983 0.4609 -0.0448 -0.0196 0.0309  318  GLU A O   
730  N N   . ASP A 96  ? 0.2945 0.4509 0.4228 -0.0532 -0.0989 -0.0165 319  ASP A N   
731  C CA  . ASP A 96  ? 0.2683 0.4294 0.3868 -0.0219 -0.1294 -0.0058 319  ASP A CA  
732  C C   . ASP A 96  ? 0.2647 0.3914 0.3790 -0.0075 -0.1007 0.0045  319  ASP A C   
733  O O   . ASP A 96  ? 0.2925 0.3703 0.3366 -0.0131 -0.1002 0.0173  319  ASP A O   
734  C CB  . ASP A 96  ? 0.2856 0.4441 0.4074 0.0094  -0.1255 0.0100  319  ASP A CB  
735  C CG  . ASP A 96  ? 0.3146 0.4556 0.4180 0.0296  -0.1290 0.0102  319  ASP A CG  
736  O OD1 . ASP A 96  ? 0.3264 0.4582 0.4134 0.0240  -0.1434 -0.0094 319  ASP A OD1 
737  O OD2 . ASP A 96  ? 0.3106 0.4599 0.4231 0.0383  -0.1211 0.0348  319  ASP A OD2 
738  N N   . VAL A 97  ? 0.2575 0.3706 0.3705 0.0099  -0.0988 -0.0136 320  VAL A N   
739  C CA  A VAL A 97  ? 0.2505 0.3520 0.3459 0.0171  -0.0982 -0.0281 320  VAL A CA  
740  C CA  B VAL A 97  ? 0.2520 0.3499 0.3560 0.0086  -0.0855 -0.0349 320  VAL A CA  
741  C C   . VAL A 97  ? 0.2408 0.3194 0.2985 0.0456  -0.0957 -0.0300 320  VAL A C   
742  O O   . VAL A 97  ? 0.2408 0.3560 0.2907 0.0736  -0.1144 -0.0486 320  VAL A O   
743  C CB  A VAL A 97  ? 0.2773 0.3570 0.3638 0.0078  -0.0751 -0.0315 320  VAL A CB  
744  C CB  B VAL A 97  ? 0.2802 0.3535 0.3951 -0.0157 -0.0430 -0.0527 320  VAL A CB  
745  C CG1 A VAL A 97  ? 0.2897 0.3562 0.3646 0.0062  -0.0731 -0.0320 320  VAL A CG1 
746  C CG1 B VAL A 97  ? 0.2917 0.3634 0.4202 -0.0268 -0.0271 -0.0571 320  VAL A CG1 
747  C CG2 A VAL A 97  ? 0.2973 0.3705 0.3841 0.0021  -0.0502 -0.0344 320  VAL A CG2 
748  C CG2 B VAL A 97  ? 0.3019 0.3563 0.4072 -0.0218 -0.0208 -0.0588 320  VAL A CG2 
749  N N   . PRO A 98  ? 0.2221 0.2335 0.2248 0.0379  -0.0731 -0.0038 321  PRO A N   
750  C CA  . PRO A 98  ? 0.2404 0.2170 0.1629 0.0496  -0.0859 -0.0006 321  PRO A CA  
751  C C   . PRO A 98  ? 0.2248 0.2102 0.1754 0.0756  -0.0793 0.0171  321  PRO A C   
752  O O   . PRO A 98  ? 0.2540 0.2070 0.2169 0.0830  -0.0391 0.0256  321  PRO A O   
753  C CB  . PRO A 98  ? 0.2139 0.2097 0.1847 0.0355  -0.0599 0.0184  321  PRO A CB  
754  C CG  . PRO A 98  ? 0.2262 0.2055 0.1808 0.0265  -0.0517 0.0364  321  PRO A CG  
755  C CD  . PRO A 98  ? 0.2339 0.2196 0.2081 0.0075  -0.0218 -0.0060 321  PRO A CD  
756  N N   . ALA A 99  ? 0.1965 0.1913 0.1674 0.0409  -0.0813 0.0230  322  ALA A N   
757  C CA  . ALA A 99  ? 0.2048 0.1661 0.1905 0.0357  -0.0533 0.0285  322  ALA A CA  
758  C C   . ALA A 99  ? 0.1765 0.1656 0.2165 0.0406  -0.0391 0.0115  322  ALA A C   
759  O O   . ALA A 99  ? 0.1656 0.1847 0.2458 0.0280  -0.0418 0.0071  322  ALA A O   
760  C CB  . ALA A 99  ? 0.2053 0.1651 0.1944 0.0274  -0.0832 -0.0084 322  ALA A CB  
761  N N   . PRO A 100 ? 0.1592 0.1514 0.1898 0.0286  -0.0450 0.0050  323  PRO A N   
762  C CA  . PRO A 100 ? 0.1633 0.1556 0.2094 0.0324  -0.0302 0.0258  323  PRO A CA  
763  C C   . PRO A 100 ? 0.1712 0.1545 0.2092 0.0073  -0.0467 0.0011  323  PRO A C   
764  O O   . PRO A 100 ? 0.1670 0.1553 0.2346 0.0052  -0.0775 0.0067  323  PRO A O   
765  C CB  . PRO A 100 ? 0.1791 0.1606 0.2146 0.0340  -0.0409 0.0346  323  PRO A CB  
766  C CG  . PRO A 100 ? 0.1651 0.1703 0.2523 0.0443  -0.0287 0.0545  323  PRO A CG  
767  C CD  . PRO A 100 ? 0.1644 0.1674 0.2214 0.0508  -0.0189 0.0220  323  PRO A CD  
768  N N   . LEU A 101 ? 0.1762 0.1387 0.2101 0.0249  -0.0542 0.0000  324  LEU A N   
769  C CA  . LEU A 101 ? 0.1627 0.1600 0.2142 0.0261  -0.0771 -0.0297 324  LEU A CA  
770  C C   . LEU A 101 ? 0.1656 0.1466 0.1901 0.0019  -0.0499 -0.0054 324  LEU A C   
771  O O   . LEU A 101 ? 0.1625 0.1626 0.2048 0.0206  -0.0362 -0.0057 324  LEU A O   
772  C CB  . LEU A 101 ? 0.2196 0.1929 0.2683 0.0162  -0.1192 -0.0410 324  LEU A CB  
773  C CG  . LEU A 101 ? 0.2391 0.2275 0.3064 -0.0306 -0.1406 -0.0474 324  LEU A CG  
774  C CD1 . LEU A 101 ? 0.2958 0.2530 0.3537 -0.0142 -0.1404 -0.0719 324  LEU A CD1 
775  C CD2 . LEU A 101 ? 0.2809 0.2793 0.3300 -0.0180 -0.0770 -0.0435 324  LEU A CD2 
776  N N   . GLY A 102 ? 0.1392 0.1179 0.1650 0.0114  -0.0629 -0.0141 325  GLY A N   
777  C CA  . GLY A 102 ? 0.1628 0.1288 0.1660 0.0266  -0.0799 0.0018  325  GLY A CA  
778  C C   . GLY A 102 ? 0.1661 0.1129 0.1765 0.0212  -0.0617 0.0160  325  GLY A C   
779  O O   . GLY A 102 ? 0.1585 0.1535 0.1786 0.0269  -0.0595 0.0319  325  GLY A O   
780  N N   . THR A 103 ? 0.1954 0.1012 0.1848 0.0368  -0.0229 0.0131  326  THR A N   
781  C CA  . THR A 103 ? 0.1598 0.1056 0.2043 0.0308  -0.0428 -0.0037 326  THR A CA  
782  C C   . THR A 103 ? 0.1664 0.1097 0.1718 0.0150  -0.0687 0.0047  326  THR A C   
783  O O   . THR A 103 ? 0.1658 0.1289 0.1748 0.0223  -0.0478 0.0168  326  THR A O   
784  C CB  . THR A 103 ? 0.1563 0.1318 0.2019 0.0402  -0.0522 -0.0114 326  THR A CB  
785  O OG1 . THR A 103 ? 0.1583 0.1698 0.2059 0.0173  -0.0446 -0.0022 326  THR A OG1 
786  C CG2 . THR A 103 ? 0.1685 0.1419 0.1845 0.0446  -0.0254 -0.0405 326  THR A CG2 
787  N N   . PRO A 104 ? 0.1678 0.1131 0.1299 0.0127  -0.0410 0.0000  327  PRO A N   
788  C CA  . PRO A 104 ? 0.1778 0.1200 0.1440 0.0024  -0.0421 -0.0068 327  PRO A CA  
789  C C   . PRO A 104 ? 0.1736 0.1135 0.1713 0.0224  -0.0471 0.0038  327  PRO A C   
790  O O   . PRO A 104 ? 0.1839 0.1164 0.2004 0.0271  -0.0306 0.0180  327  PRO A O   
791  C CB  . PRO A 104 ? 0.1681 0.1261 0.1435 0.0153  -0.0396 -0.0053 327  PRO A CB  
792  C CG  . PRO A 104 ? 0.2063 0.1588 0.1997 0.0057  -0.0362 -0.0137 327  PRO A CG  
793  C CD  . PRO A 104 ? 0.2009 0.1140 0.1407 0.0056  -0.0468 -0.0298 327  PRO A CD  
794  N N   . ASP A 105 ? 0.1891 0.1170 0.1503 -0.0078 -0.0461 0.0183  328  ASP A N   
795  C CA  . ASP A 105 ? 0.2002 0.1114 0.1390 0.0112  -0.0559 0.0071  328  ASP A CA  
796  C C   . ASP A 105 ? 0.2047 0.1181 0.1720 0.0245  -0.0465 0.0010  328  ASP A C   
797  O O   . ASP A 105 ? 0.2394 0.1493 0.1747 -0.0062 -0.0654 -0.0149 328  ASP A O   
798  C CB  . ASP A 105 ? 0.1909 0.1193 0.1624 0.0347  -0.0575 -0.0092 328  ASP A CB  
799  C CG  . ASP A 105 ? 0.1619 0.1133 0.1703 -0.0116 -0.0583 -0.0111 328  ASP A CG  
800  O OD1 . ASP A 105 ? 0.1741 0.1231 0.1777 0.0065  -0.0606 0.0037  328  ASP A OD1 
801  O OD2 . ASP A 105 ? 0.1943 0.1066 0.1806 0.0034  -0.0596 0.0080  328  ASP A OD2 
802  N N   . PHE A 106 ? 0.1691 0.0927 0.1717 -0.0019 -0.0571 -0.0028 329  PHE A N   
803  C CA  . PHE A 106 ? 0.1789 0.1194 0.1764 0.0018  -0.0513 0.0078  329  PHE A CA  
804  C C   . PHE A 106 ? 0.1775 0.0986 0.1811 0.0083  -0.0590 -0.0022 329  PHE A C   
805  O O   . PHE A 106 ? 0.1844 0.1213 0.2105 0.0013  -0.0400 0.0058  329  PHE A O   
806  C CB  . PHE A 106 ? 0.2012 0.1359 0.1634 0.0168  -0.0577 0.0068  329  PHE A CB  
807  C CG  . PHE A 106 ? 0.2086 0.1327 0.1526 0.0158  -0.0668 0.0058  329  PHE A CG  
808  C CD1 . PHE A 106 ? 0.2007 0.1462 0.1515 0.0105  -0.0740 0.0179  329  PHE A CD1 
809  C CD2 . PHE A 106 ? 0.1953 0.1221 0.1630 0.0088  -0.0668 0.0310  329  PHE A CD2 
810  C CE1 . PHE A 106 ? 0.2172 0.1339 0.1762 -0.0042 -0.0660 0.0149  329  PHE A CE1 
811  C CE2 . PHE A 106 ? 0.1725 0.1549 0.1770 0.0038  -0.0640 0.0266  329  PHE A CE2 
812  C CZ  . PHE A 106 ? 0.1821 0.1446 0.1681 0.0066  -0.0480 0.0170  329  PHE A CZ  
813  N N   . LYS A 107 ? 0.1987 0.0810 0.1968 0.0331  -0.0606 -0.0084 330  LYS A N   
814  C CA  . LYS A 107 ? 0.2023 0.0903 0.1956 0.0142  -0.0621 -0.0085 330  LYS A CA  
815  C C   . LYS A 107 ? 0.1869 0.1103 0.1997 0.0208  -0.0693 0.0045  330  LYS A C   
816  O O   . LYS A 107 ? 0.2066 0.1412 0.1957 0.0188  -0.0649 -0.0026 330  LYS A O   
817  C CB  . LYS A 107 ? 0.2396 0.0962 0.2191 0.0270  -0.0633 -0.0018 330  LYS A CB  
818  C CG  . LYS A 107 ? 0.2421 0.0953 0.2330 0.0289  -0.0790 0.0216  330  LYS A CG  
819  C CD  . LYS A 107 ? 0.2781 0.1112 0.2563 0.0471  -0.0808 0.0198  330  LYS A CD  
820  C CE  . LYS A 107 ? 0.3468 0.1397 0.2803 0.0678  -0.0887 0.0248  330  LYS A CE  
821  N NZ  . LYS A 107 ? 0.4073 0.1439 0.3300 0.0644  -0.0809 0.0340  330  LYS A NZ  
822  N N   . GLY A 108 ? 0.2267 0.1085 0.1773 0.0097  -0.0888 0.0260  331  GLY A N   
823  C CA  . GLY A 108 ? 0.2187 0.1429 0.1846 0.0000  -0.0620 0.0300  331  GLY A CA  
824  C C   . GLY A 108 ? 0.2206 0.1315 0.1799 0.0052  -0.0435 0.0095  331  GLY A C   
825  O O   . GLY A 108 ? 0.2242 0.1593 0.2144 0.0148  -0.0523 0.0076  331  GLY A O   
826  N N   A GLN A 109 ? 0.2063 0.1127 0.1689 0.0060  -0.0415 0.0069  332  GLN A N   
827  N N   B GLN A 109 ? 0.1965 0.1049 0.1607 0.0290  -0.0448 0.0088  332  GLN A N   
828  C CA  A GLN A 109 ? 0.1993 0.1059 0.1935 -0.0094 -0.0438 0.0008  332  GLN A CA  
829  C CA  B GLN A 109 ? 0.1936 0.0980 0.1905 0.0248  -0.0517 0.0013  332  GLN A CA  
830  C C   A GLN A 109 ? 0.1930 0.0901 0.1817 -0.0002 -0.0392 -0.0070 332  GLN A C   
831  C C   B GLN A 109 ? 0.1632 0.0873 0.1769 0.0286  -0.0626 0.0013  332  GLN A C   
832  O O   A GLN A 109 ? 0.2245 0.0917 0.1937 0.0011  -0.0104 -0.0165 332  GLN A O   
833  O O   B GLN A 109 ? 0.1617 0.0951 0.1992 0.0413  -0.0685 -0.0029 332  GLN A O   
834  C CB  A GLN A 109 ? 0.1947 0.1084 0.2168 -0.0156 -0.0608 -0.0038 332  GLN A CB  
835  C CB  B GLN A 109 ? 0.2215 0.0937 0.2135 0.0437  -0.0624 -0.0164 332  GLN A CB  
836  C CG  A GLN A 109 ? 0.2089 0.1335 0.2513 -0.0170 -0.0638 0.0046  332  GLN A CG  
837  C CG  B GLN A 109 ? 0.2668 0.1192 0.2513 0.0303  -0.0584 -0.0347 332  GLN A CG  
838  C CD  A GLN A 109 ? 0.2070 0.1560 0.2594 -0.0250 -0.0803 0.0200  332  GLN A CD  
839  C CD  B GLN A 109 ? 0.2935 0.1454 0.2843 0.0122  -0.0666 -0.0455 332  GLN A CD  
840  O OE1 A GLN A 109 ? 0.2388 0.1810 0.2966 -0.0556 -0.0925 -0.0011 332  GLN A OE1 
841  O OE1 B GLN A 109 ? 0.3277 0.1663 0.2988 0.0091  -0.0683 -0.0306 332  GLN A OE1 
842  N NE2 A GLN A 109 ? 0.2019 0.1446 0.2558 0.0066  -0.0701 0.0303  332  GLN A NE2 
843  N NE2 B GLN A 109 ? 0.3329 0.1673 0.3223 0.0176  -0.0381 -0.0329 332  GLN A NE2 
844  N N   . LEU A 110 ? 0.1854 0.0730 0.1826 -0.0068 -0.0557 -0.0004 333  LEU A N   
845  C CA  . LEU A 110 ? 0.1998 0.0883 0.1605 -0.0076 -0.0440 0.0012  333  LEU A CA  
846  C C   . LEU A 110 ? 0.1665 0.1043 0.1649 0.0226  -0.0316 0.0056  333  LEU A C   
847  O O   . LEU A 110 ? 0.2025 0.1396 0.1667 0.0224  -0.0244 0.0040  333  LEU A O   
848  C CB  . LEU A 110 ? 0.1804 0.1139 0.1880 -0.0136 -0.0752 -0.0269 333  LEU A CB  
849  C CG  . LEU A 110 ? 0.1703 0.1156 0.2078 0.0213  -0.0468 -0.0174 333  LEU A CG  
850  C CD1 . LEU A 110 ? 0.1661 0.1280 0.2256 0.0160  -0.0244 -0.0126 333  LEU A CD1 
851  C CD2 . LEU A 110 ? 0.1595 0.1312 0.2639 0.0308  -0.0490 -0.0151 333  LEU A CD2 
852  N N   . TYR A 111 ? 0.1625 0.0843 0.1569 0.0064  -0.0640 0.0044  334  TYR A N   
853  C CA  . TYR A 111 ? 0.1560 0.0798 0.1623 -0.0122 -0.0605 -0.0115 334  TYR A CA  
854  C C   . TYR A 111 ? 0.1653 0.0866 0.1570 -0.0190 -0.0409 0.0019  334  TYR A C   
855  O O   . TYR A 111 ? 0.1728 0.1080 0.1616 0.0003  -0.0361 -0.0115 334  TYR A O   
856  C CB  . TYR A 111 ? 0.1400 0.0990 0.1759 -0.0150 -0.0741 0.0051  334  TYR A CB  
857  C CG  . TYR A 111 ? 0.1393 0.0910 0.1754 -0.0012 -0.0536 -0.0209 334  TYR A CG  
858  C CD1 . TYR A 111 ? 0.1703 0.1047 0.1684 -0.0033 -0.0351 -0.0066 334  TYR A CD1 
859  C CD2 . TYR A 111 ? 0.1713 0.0965 0.2159 0.0190  -0.0691 -0.0088 334  TYR A CD2 
860  C CE1 . TYR A 111 ? 0.1601 0.1007 0.1824 0.0127  -0.0423 -0.0037 334  TYR A CE1 
861  C CE2 . TYR A 111 ? 0.1949 0.1033 0.1745 -0.0048 -0.0426 -0.0091 334  TYR A CE2 
862  C CZ  . TYR A 111 ? 0.1778 0.1027 0.1690 -0.0125 -0.0483 0.0081  334  TYR A CZ  
863  O OH  . TYR A 111 ? 0.2107 0.1228 0.1932 -0.0211 -0.0609 0.0203  334  TYR A OH  
864  N N   . GLY A 112 ? 0.1884 0.0850 0.1551 -0.0070 -0.0471 0.0032  335  GLY A N   
865  C CA  . GLY A 112 ? 0.1895 0.0891 0.1315 -0.0226 -0.0139 -0.0058 335  GLY A CA  
866  C C   . GLY A 112 ? 0.1475 0.0928 0.1378 -0.0226 -0.0515 -0.0034 335  GLY A C   
867  O O   . GLY A 112 ? 0.1629 0.1177 0.1470 -0.0135 -0.0361 -0.0172 335  GLY A O   
868  N N   . VAL A 113 ? 0.1386 0.0974 0.1568 -0.0250 -0.0307 -0.0011 336  VAL A N   
869  C CA  . VAL A 113 ? 0.1460 0.1076 0.1650 0.0075  -0.0302 0.0033  336  VAL A CA  
870  C C   . VAL A 113 ? 0.1336 0.1049 0.1519 0.0046  -0.0316 -0.0025 336  VAL A C   
871  O O   . VAL A 113 ? 0.1572 0.1185 0.1737 0.0028  -0.0416 -0.0200 336  VAL A O   
872  C CB  . VAL A 113 ? 0.1594 0.1096 0.1553 -0.0095 -0.0412 0.0055  336  VAL A CB  
873  C CG1 . VAL A 113 ? 0.1846 0.1160 0.1681 -0.0013 -0.0009 0.0102  336  VAL A CG1 
874  C CG2 . VAL A 113 ? 0.1663 0.1110 0.1896 0.0057  -0.0497 -0.0099 336  VAL A CG2 
875  N N   . ILE A 114 ? 0.1303 0.1107 0.1572 0.0145  -0.0188 -0.0015 337  ILE A N   
876  C CA  . ILE A 114 ? 0.1447 0.1139 0.1727 0.0264  -0.0332 0.0005  337  ILE A CA  
877  C C   . ILE A 114 ? 0.1739 0.1166 0.1362 -0.0039 -0.0148 -0.0173 337  ILE A C   
878  O O   . ILE A 114 ? 0.1839 0.1239 0.1519 -0.0083 -0.0149 -0.0041 337  ILE A O   
879  C CB  . ILE A 114 ? 0.1742 0.1227 0.1812 0.0454  -0.0325 -0.0400 337  ILE A CB  
880  C CG1 . ILE A 114 ? 0.1691 0.1360 0.2517 0.0526  -0.0194 -0.0301 337  ILE A CG1 
881  C CG2 . ILE A 114 ? 0.1853 0.1086 0.1971 0.0345  -0.0032 -0.0376 337  ILE A CG2 
882  C CD1 . ILE A 114 ? 0.2229 0.1542 0.2797 0.0480  -0.0003 -0.0268 337  ILE A CD1 
883  N N   A SER A 115 ? 0.1576 0.1005 0.1599 -0.0084 0.0001  -0.0114 338  SER A N   
884  N N   B SER A 115 ? 0.1611 0.1146 0.1413 -0.0069 -0.0064 -0.0126 338  SER A N   
885  C CA  A SER A 115 ? 0.1402 0.1053 0.1698 -0.0018 -0.0022 -0.0241 338  SER A CA  
886  C CA  B SER A 115 ? 0.1465 0.1157 0.1462 -0.0020 -0.0066 -0.0072 338  SER A CA  
887  C C   A SER A 115 ? 0.1766 0.1156 0.1651 0.0046  -0.0264 0.0007  338  SER A C   
888  C C   B SER A 115 ? 0.1619 0.1204 0.1717 0.0001  -0.0001 -0.0033 338  SER A C   
889  O O   A SER A 115 ? 0.1862 0.1395 0.1758 -0.0031 -0.0330 -0.0047 338  SER A O   
890  O O   B SER A 115 ? 0.1514 0.1166 0.1844 0.0129  0.0152  0.0010  338  SER A O   
891  C CB  A SER A 115 ? 0.1432 0.1185 0.2006 0.0290  0.0108  -0.0134 338  SER A CB  
892  C CB  B SER A 115 ? 0.1362 0.1173 0.1243 0.0129  -0.0226 0.0159  338  SER A CB  
893  O OG  A SER A 115 ? 0.1769 0.1169 0.1961 0.0263  -0.0078 -0.0298 338  SER A OG  
894  O OG  B SER A 115 ? 0.1464 0.1141 0.0949 0.0201  -0.0375 0.0380  338  SER A OG  
895  N N   . GLN A 116 ? 0.1836 0.1383 0.1955 -0.0158 -0.0069 -0.0115 339  GLN A N   
896  C CA  . GLN A 116 ? 0.1660 0.1394 0.2012 -0.0112 -0.0070 -0.0069 339  GLN A CA  
897  C C   . GLN A 116 ? 0.2149 0.1368 0.1869 -0.0240 0.0017  -0.0174 339  GLN A C   
898  O O   . GLN A 116 ? 0.2006 0.1416 0.1933 -0.0157 -0.0140 -0.0042 339  GLN A O   
899  C CB  . GLN A 116 ? 0.1783 0.1426 0.2296 0.0059  0.0096  -0.0168 339  GLN A CB  
900  C CG  . GLN A 116 ? 0.2111 0.1282 0.2224 0.0088  0.0614  -0.0153 339  GLN A CG  
901  C CD  . GLN A 116 ? 0.2291 0.1303 0.2289 0.0157  0.0423  -0.0203 339  GLN A CD  
902  O OE1 . GLN A 116 ? 0.2239 0.1522 0.2176 0.0247  0.0255  -0.0087 339  GLN A OE1 
903  N NE2 . GLN A 116 ? 0.2252 0.1254 0.2349 0.0219  0.0130  -0.0153 339  GLN A NE2 
904  N N   A ARG A 117 ? 0.2042 0.1385 0.1876 -0.0287 -0.0063 -0.0216 340  ARG A N   
905  N N   B ARG A 117 ? 0.2130 0.1443 0.1835 -0.0360 0.0028  -0.0189 340  ARG A N   
906  C CA  A ARG A 117 ? 0.1968 0.1471 0.2016 -0.0136 -0.0170 -0.0199 340  ARG A CA  
907  C CA  B ARG A 117 ? 0.2157 0.1565 0.2037 -0.0219 -0.0056 -0.0066 340  ARG A CA  
908  C C   A ARG A 117 ? 0.1897 0.1714 0.2317 -0.0092 -0.0083 -0.0066 340  ARG A C   
909  C C   B ARG A 117 ? 0.1839 0.1757 0.2227 -0.0251 -0.0252 0.0022  340  ARG A C   
910  O O   A ARG A 117 ? 0.2228 0.1935 0.2620 0.0059  0.0073  0.0071  340  ARG A O   
911  O O   B ARG A 117 ? 0.1977 0.1970 0.2328 -0.0228 -0.0523 0.0196  340  ARG A O   
912  C CB  A ARG A 117 ? 0.1948 0.1442 0.1787 -0.0244 -0.0349 -0.0265 340  ARG A CB  
913  C CB  B ARG A 117 ? 0.2408 0.1609 0.1846 -0.0399 -0.0015 -0.0019 340  ARG A CB  
914  C CG  A ARG A 117 ? 0.1955 0.1450 0.1926 -0.0129 -0.0396 -0.0409 340  ARG A CG  
915  C CG  B ARG A 117 ? 0.2743 0.1643 0.1971 -0.0381 0.0312  -0.0156 340  ARG A CG  
916  C CD  A ARG A 117 ? 0.2138 0.1514 0.2012 -0.0168 -0.0367 -0.0436 340  ARG A CD  
917  C CD  B ARG A 117 ? 0.2754 0.1660 0.2053 -0.0289 0.0643  -0.0320 340  ARG A CD  
918  N NE  A ARG A 117 ? 0.2364 0.1533 0.2266 -0.0185 -0.0074 -0.0402 340  ARG A NE  
919  N NE  B ARG A 117 ? 0.2579 0.1710 0.2200 0.0050  0.0481  -0.0464 340  ARG A NE  
920  C CZ  A ARG A 117 ? 0.2258 0.1527 0.2456 -0.0221 -0.0361 -0.0586 340  ARG A CZ  
921  C CZ  B ARG A 117 ? 0.2689 0.1502 0.2029 0.0123  0.0711  -0.0373 340  ARG A CZ  
922  N NH1 A ARG A 117 ? 0.2290 0.1569 0.2577 -0.0334 -0.0252 -0.0746 340  ARG A NH1 
923  N NH1 B ARG A 117 ? 0.3201 0.1491 0.2369 0.0004  0.0577  -0.0278 340  ARG A NH1 
924  N NH2 A ARG A 117 ? 0.1887 0.1551 0.2501 -0.0068 -0.0667 -0.0571 340  ARG A NH2 
925  N NH2 B ARG A 117 ? 0.1604 0.1152 0.1513 -0.0001 -0.0277 -0.0363 340  ARG A NH2 
926  N N   . ASN A 118 ? 0.1842 0.1799 0.2525 -0.0102 0.0140  -0.0202 341  ASN A N   
927  C CA  . ASN A 118 ? 0.1817 0.2129 0.2398 -0.0057 0.0169  -0.0290 341  ASN A CA  
928  C C   . ASN A 118 ? 0.2088 0.2189 0.2810 -0.0239 0.0081  -0.0447 341  ASN A C   
929  O O   . ASN A 118 ? 0.2137 0.2002 0.2974 -0.0400 0.0099  -0.0132 341  ASN A O   
930  C CB  . ASN A 118 ? 0.2178 0.2220 0.2332 -0.0130 0.0090  -0.0384 341  ASN A CB  
931  C CG  . ASN A 118 ? 0.2292 0.2311 0.2697 -0.0086 0.0192  -0.0447 341  ASN A CG  
932  O OD1 . ASN A 118 ? 0.2293 0.2248 0.2815 -0.0275 0.0068  -0.0503 341  ASN A OD1 
933  N ND2 . ASN A 118 ? 0.2693 0.2396 0.2768 0.0072  0.0438  -0.0493 341  ASN A ND2 
934  N N   . ARG A 119 ? 0.2166 0.2804 0.3212 -0.0471 -0.0242 -0.0620 342  ARG A N   
935  C CA  . ARG A 119 ? 0.2335 0.3328 0.3986 -0.0381 -0.0564 -0.0397 342  ARG A CA  
936  C C   . ARG A 119 ? 0.2977 0.4094 0.4724 0.0216  -0.0055 -0.0142 342  ARG A C   
937  O O   . ARG A 119 ? 0.3004 0.4090 0.4804 -0.0406 -0.0325 -0.0338 342  ARG A O   
938  C CB  . ARG A 119 ? 0.2549 0.3361 0.4495 -0.0444 -0.0976 0.0043  342  ARG A CB  
939  C CG  . ARG A 119 ? 0.2664 0.3327 0.5110 -0.0261 -0.1159 0.0084  342  ARG A CG  
940  C CD  . ARG A 119 ? 0.2728 0.3283 0.5565 0.0041  -0.1399 0.0325  342  ARG A CD  
941  N NE  . ARG A 119 ? 0.2768 0.3346 0.6217 0.0191  -0.1393 0.0333  342  ARG A NE  
942  C CZ  . ARG A 119 ? 0.2813 0.3321 0.6307 0.0352  -0.1915 0.0317  342  ARG A CZ  
943  N NH1 . ARG A 119 ? 0.2764 0.3316 0.6283 0.0489  -0.1865 0.0227  342  ARG A NH1 
944  N NH2 . ARG A 119 ? 0.3190 0.3568 0.6434 0.0187  -0.1573 0.0477  342  ARG A NH2 
945  N N   A GLU A 120 ? 0.3298 0.4514 0.5011 0.0653  0.0259  -0.0025 343  GLU A N   
946  N N   B GLU A 120 ? 0.3298 0.4514 0.5011 0.0653  0.0259  -0.0025 343  GLU A N   
947  C CA  A GLU A 120 ? 0.4154 0.5058 0.5466 0.0907  0.0689  -0.0081 343  GLU A CA  
948  C CA  B GLU A 120 ? 0.4154 0.5058 0.5466 0.0907  0.0689  -0.0081 343  GLU A CA  
949  C C   A GLU A 120 ? 0.4441 0.5336 0.5545 0.0753  0.1073  -0.0027 343  GLU A C   
950  C C   B GLU A 120 ? 0.4441 0.5336 0.5545 0.0753  0.1073  -0.0027 343  GLU A C   
951  O O   A GLU A 120 ? 0.4345 0.5309 0.5409 0.0804  0.1095  -0.0139 343  GLU A O   
952  O O   B GLU A 120 ? 0.4345 0.5309 0.5409 0.0804  0.1095  -0.0139 343  GLU A O   
953  C CB  A GLU A 120 ? 0.4786 0.5274 0.5848 0.1188  0.0768  -0.0257 343  GLU A CB  
954  C CB  B GLU A 120 ? 0.4786 0.5274 0.5848 0.1188  0.0768  -0.0257 343  GLU A CB  
955  C CG  A GLU A 120 ? 0.5313 0.5429 0.6180 0.1399  0.0714  -0.0408 343  GLU A CG  
956  C CG  B GLU A 120 ? 0.5313 0.5429 0.6180 0.1399  0.0714  -0.0408 343  GLU A CG  
957  C CD  A GLU A 120 ? 0.5853 0.5586 0.6444 0.1492  0.0770  -0.0539 343  GLU A CD  
958  C CD  B GLU A 120 ? 0.5853 0.5586 0.6444 0.1492  0.0770  -0.0539 343  GLU A CD  
959  O OE1 . GLU A 120 ? 0.6058 0.5652 0.6537 0.1504  0.0749  -0.0601 343  GLU A OE1 
960  O OE2 . GLU A 120 ? 0.5978 0.5619 0.6569 0.1501  0.0820  -0.0563 343  GLU A OE2 
961  N N   . GLY A 121 ? 0.4798 0.5617 0.5742 0.0498  0.1252  0.0114  344  GLY A N   
962  C CA  . GLY A 121 ? 0.5494 0.6064 0.6087 0.0115  0.1404  0.0344  344  GLY A CA  
963  C C   . GLY A 121 ? 0.6240 0.6533 0.6483 -0.0281 0.1448  0.0496  344  GLY A C   
964  O O   . GLY A 121 ? 0.6310 0.6554 0.6484 -0.0366 0.1626  0.0431  344  GLY A O   
965  N N   . SER A 122 ? 0.6888 0.6981 0.6767 -0.0454 0.1146  0.0695  345  SER A N   
966  C CA  . SER A 122 ? 0.7625 0.7411 0.7065 -0.0593 0.0893  0.0802  345  SER A CA  
967  C C   . SER A 122 ? 0.8218 0.7741 0.7269 -0.0524 0.0892  0.1018  345  SER A C   
968  O O   . SER A 122 ? 0.8435 0.7775 0.7363 -0.0426 0.1089  0.1166  345  SER A O   
969  C CB  . SER A 122 ? 0.7642 0.7470 0.7166 -0.0798 0.0571  0.0694  345  SER A CB  
970  O OG  . SER A 122 ? 0.7681 0.7522 0.7164 -0.0914 0.0321  0.0635  345  SER A OG  
971  N N   . SER A 123 ? 0.8448 0.8007 0.7237 -0.0557 0.0613  0.0993  346  SER A N   
972  C CA  . SER A 123 ? 0.8632 0.8275 0.7179 -0.0660 0.0233  0.0779  346  SER A CA  
973  C C   . SER A 123 ? 0.9011 0.8455 0.7145 -0.0732 0.0218  0.0433  346  SER A C   
974  O O   . SER A 123 ? 0.9034 0.8502 0.7202 -0.0753 0.0218  0.0465  346  SER A O   
975  C CB  . SER A 123 ? 0.8475 0.8311 0.7131 -0.0671 -0.0046 0.0875  346  SER A CB  
976  N N   . GLY A 124 ? 0.9388 0.8547 0.7045 -0.0750 0.0271  0.0003  347  GLY A N   
977  C CA  . GLY A 124 ? 0.9757 0.8578 0.6919 -0.0767 0.0395  -0.0444 347  GLY A CA  
978  C C   . GLY A 124 ? 1.0014 0.8554 0.6780 -0.0811 0.0502  -0.0868 347  GLY A C   
979  O O   . GLY A 124 ? 1.0205 0.8615 0.6715 -0.0719 0.0620  -0.0928 347  GLY A O   
980  N N   . ASN A 125 ? 0.9911 0.8403 0.6639 -0.0963 0.0463  -0.1181 348  ASN A N   
981  C CA  . ASN A 125 ? 0.9680 0.8194 0.6473 -0.1166 0.0409  -0.1444 348  ASN A CA  
982  C C   . ASN A 125 ? 0.9253 0.7990 0.6302 -0.1239 0.0272  -0.1323 348  ASN A C   
983  O O   . ASN A 125 ? 0.9259 0.7983 0.6286 -0.1267 0.0240  -0.1381 348  ASN A O   
984  C CB  . ASN A 125 ? 0.9821 0.8138 0.6449 -0.1295 0.0515  -0.1768 348  ASN A CB  
985  C CG  . ASN A 125 ? 0.9940 0.8112 0.6457 -0.1370 0.0699  -0.2016 348  ASN A CG  
986  O OD1 . ASN A 125 ? 0.9994 0.8114 0.6531 -0.1438 0.0712  -0.2076 348  ASN A OD1 
987  N ND2 . ASN A 125 ? 0.9949 0.8087 0.6407 -0.1404 0.0778  -0.2167 348  ASN A ND2 
988  N N   . GLY A 126 ? 0.8736 0.7753 0.6126 -0.1323 0.0256  -0.1033 349  GLY A N   
989  C CA  . GLY A 126 ? 0.8163 0.7473 0.5950 -0.1470 0.0231  -0.0709 349  GLY A CA  
990  C C   . GLY A 126 ? 0.7555 0.7194 0.5829 -0.1626 0.0275  -0.0328 349  GLY A C   
991  O O   . GLY A 126 ? 0.7408 0.7210 0.5868 -0.1564 0.0184  -0.0359 349  GLY A O   
992  N N   . ASN A 127 ? 0.7088 0.6803 0.5549 -0.1857 0.0501  0.0002  350  ASN A N   
993  C CA  A ASN A 127 ? 0.6819 0.6569 0.5559 -0.2046 0.0571  0.0248  350  ASN A CA  
994  C CA  B ASN A 127 ? 0.6892 0.6592 0.5283 -0.1924 0.0668  0.0242  350  ASN A CA  
995  C C   . ASN A 127 ? 0.6616 0.6242 0.5273 -0.1964 0.0710  0.0331  350  ASN A C   
996  O O   . ASN A 127 ? 0.6815 0.6279 0.5457 -0.2076 0.0872  0.0229  350  ASN A O   
997  C CB  A ASN A 127 ? 0.6655 0.6663 0.5824 -0.2266 0.0370  0.0336  350  ASN A CB  
998  C CB  B ASN A 127 ? 0.6865 0.6720 0.5012 -0.1930 0.0647  0.0326  350  ASN A CB  
999  C CG  A ASN A 127 ? 0.6447 0.6724 0.6093 -0.2418 0.0155  0.0380  350  ASN A CG  
1000 C CG  B ASN A 127 ? 0.6774 0.6814 0.4814 -0.1906 0.0583  0.0368  350  ASN A CG  
1001 O OD1 A ASN A 127 ? 0.6306 0.6729 0.6288 -0.2516 0.0111  0.0418  350  ASN A OD1 
1002 O OD1 B ASN A 127 ? 0.6774 0.6856 0.4797 -0.1905 0.0514  0.0378  350  ASN A OD1 
1003 N ND2 A ASN A 127 ? 0.6386 0.6752 0.6051 -0.2430 0.0038  0.0379  350  ASN A ND2 
1004 N ND2 B ASN A 127 ? 0.6674 0.6830 0.4688 -0.1897 0.0544  0.0398  350  ASN A ND2 
1005 N N   . GLN A 128 ? 0.5812 0.5500 0.4692 -0.1685 0.0598  0.0644  351  GLN A N   
1006 C CA  . GLN A 128 ? 0.4899 0.4623 0.3976 -0.1509 0.0383  0.0862  351  GLN A CA  
1007 C C   . GLN A 128 ? 0.4241 0.4029 0.3120 -0.1286 0.0130  0.0315  351  GLN A C   
1008 O O   . GLN A 128 ? 0.4149 0.4251 0.3313 -0.1189 0.0557  0.0254  351  GLN A O   
1009 C CB  . GLN A 128 ? 0.5109 0.4534 0.4442 -0.0981 0.0228  0.1401  351  GLN A CB  
1010 C CG  . GLN A 128 ? 0.5868 0.4781 0.5176 -0.0275 0.0228  0.1550  351  GLN A CG  
1011 C CD  . GLN A 128 ? 0.6747 0.4917 0.5820 0.0349  0.0532  0.1812  351  GLN A CD  
1012 O OE1 . GLN A 128 ? 0.6882 0.4898 0.6065 0.0697  0.0367  0.1934  351  GLN A OE1 
1013 N NE2 . GLN A 128 ? 0.7067 0.5045 0.6096 0.0500  0.0809  0.1985  351  GLN A NE2 
1014 N N   . LYS A 129 ? 0.3600 0.3222 0.2118 -0.1276 -0.0048 -0.0045 352  LYS A N   
1015 C CA  . LYS A 129 ? 0.3287 0.2654 0.1936 -0.0964 -0.0130 -0.0514 352  LYS A CA  
1016 C C   . LYS A 129 ? 0.2618 0.2323 0.1931 -0.0759 0.0148  -0.0354 352  LYS A C   
1017 O O   . LYS A 129 ? 0.2526 0.2228 0.2206 -0.0597 0.0438  -0.0542 352  LYS A O   
1018 C CB  . LYS A 129 ? 0.3020 0.2655 0.1815 -0.0858 -0.0338 -0.0525 352  LYS A CB  
1019 C CG  . LYS A 129 ? 0.3053 0.2858 0.2145 -0.0767 -0.0568 -0.0550 352  LYS A CG  
1020 C CD  . LYS A 129 ? 0.3135 0.3191 0.2425 -0.0540 -0.0941 -0.0435 352  LYS A CD  
1021 C CE  . LYS A 129 ? 0.3636 0.3607 0.2868 -0.0194 -0.1051 -0.0258 352  LYS A CE  
1022 N NZ  . LYS A 129 ? 0.3891 0.3892 0.3304 -0.0175 -0.1131 -0.0214 352  LYS A NZ  
1023 N N   . ALA A 130 ? 0.2530 0.2191 0.1991 -0.0626 0.0416  -0.0429 353  ALA A N   
1024 C CA  . ALA A 130 ? 0.2380 0.1926 0.2080 -0.0654 0.0414  -0.0490 353  ALA A CA  
1025 C C   . ALA A 130 ? 0.2385 0.1839 0.2242 -0.0326 0.0515  -0.0174 353  ALA A C   
1026 O O   . ALA A 130 ? 0.2445 0.2140 0.2715 -0.0197 0.0177  -0.0157 353  ALA A O   
1027 C CB  . ALA A 130 ? 0.2414 0.1859 0.2203 -0.0253 0.0371  -0.0743 353  ALA A CB  
1028 N N   . ASN A 131 ? 0.2282 0.1578 0.2094 -0.0372 0.0582  -0.0293 354  ASN A N   
1029 C CA  . ASN A 131 ? 0.1850 0.1441 0.1838 -0.0375 0.0317  -0.0160 354  ASN A CA  
1030 C C   . ASN A 131 ? 0.2046 0.1471 0.1789 -0.0230 0.0028  -0.0077 354  ASN A C   
1031 O O   . ASN A 131 ? 0.2508 0.1706 0.1909 -0.0157 -0.0077 0.0025  354  ASN A O   
1032 C CB  . ASN A 131 ? 0.1921 0.1449 0.1697 -0.0285 0.0044  -0.0188 354  ASN A CB  
1033 C CG  . ASN A 131 ? 0.2059 0.1503 0.1663 -0.0419 0.0033  -0.0309 354  ASN A CG  
1034 O OD1 . ASN A 131 ? 0.2447 0.1513 0.1551 -0.0188 -0.0043 -0.0184 354  ASN A OD1 
1035 N ND2 . ASN A 131 ? 0.2380 0.1592 0.2117 -0.0383 0.0529  -0.0024 354  ASN A ND2 
1036 N N   . ARG A 132 ? 0.1986 0.1476 0.1806 -0.0193 -0.0063 -0.0218 355  ARG A N   
1037 C CA  . ARG A 132 ? 0.2138 0.1503 0.1776 -0.0218 0.0162  -0.0365 355  ARG A CA  
1038 C C   . ARG A 132 ? 0.1621 0.1598 0.1543 -0.0252 -0.0189 -0.0139 355  ARG A C   
1039 O O   . ARG A 132 ? 0.1744 0.1882 0.1933 -0.0245 -0.0209 -0.0245 355  ARG A O   
1040 C CB  . ARG A 132 ? 0.2187 0.1546 0.1884 -0.0099 0.0103  -0.0235 355  ARG A CB  
1041 C CG  . ARG A 132 ? 0.1928 0.1623 0.2169 0.0127  0.0142  -0.0279 355  ARG A CG  
1042 C CD  . ARG A 132 ? 0.2035 0.1719 0.2398 0.0103  0.0302  -0.0169 355  ARG A CD  
1043 N NE  . ARG A 132 ? 0.2020 0.1811 0.2634 -0.0132 0.0511  -0.0144 355  ARG A NE  
1044 C CZ  . ARG A 132 ? 0.2108 0.1997 0.2647 -0.0320 0.0250  -0.0076 355  ARG A CZ  
1045 N NH1 . ARG A 132 ? 0.2180 0.2139 0.2512 -0.0061 0.0075  -0.0375 355  ARG A NH1 
1046 N NH2 . ARG A 132 ? 0.2168 0.2036 0.2874 -0.0319 0.0447  -0.0031 355  ARG A NH2 
1047 N N   . SER A 133 ? 0.1689 0.1292 0.1724 -0.0031 -0.0113 -0.0006 356  SER A N   
1048 C CA  . SER A 133 ? 0.2024 0.0988 0.1599 -0.0082 0.0040  -0.0161 356  SER A CA  
1049 C C   . SER A 133 ? 0.2175 0.1028 0.1810 0.0052  -0.0032 -0.0341 356  SER A C   
1050 O O   . SER A 133 ? 0.2439 0.1264 0.1517 0.0055  -0.0045 -0.0173 356  SER A O   
1051 C CB  . SER A 133 ? 0.2119 0.0837 0.1759 -0.0223 -0.0067 -0.0306 356  SER A CB  
1052 O OG  . SER A 133 ? 0.2145 0.1022 0.1896 -0.0202 -0.0372 -0.0158 356  SER A OG  
1053 N N   . HIS A 134 ? 0.2032 0.0972 0.1842 -0.0035 -0.0293 -0.0314 357  HIS A N   
1054 C CA  . HIS A 134 ? 0.2078 0.0964 0.1981 -0.0037 -0.0016 -0.0260 357  HIS A CA  
1055 C C   . HIS A 134 ? 0.1739 0.0992 0.1730 -0.0134 -0.0447 -0.0285 357  HIS A C   
1056 O O   . HIS A 134 ? 0.1998 0.1312 0.1759 -0.0158 -0.0391 -0.0469 357  HIS A O   
1057 C CB  . HIS A 134 ? 0.2123 0.1205 0.1875 -0.0011 -0.0066 -0.0269 357  HIS A CB  
1058 C CG  . HIS A 134 ? 0.2444 0.1571 0.1800 0.0062  -0.0069 -0.0207 357  HIS A CG  
1059 N ND1 . HIS A 134 ? 0.2964 0.1863 0.2155 0.0094  0.0111  -0.0272 357  HIS A ND1 
1060 C CD2 . HIS A 134 ? 0.2645 0.1733 0.2129 0.0003  0.0293  -0.0370 357  HIS A CD2 
1061 C CE1 . HIS A 134 ? 0.3061 0.2134 0.2118 -0.0039 0.0446  -0.0246 357  HIS A CE1 
1062 N NE2 . HIS A 134 ? 0.2888 0.1960 0.2206 -0.0293 0.0387  -0.0509 357  HIS A NE2 
1063 N N   . GLU A 135 ? 0.1671 0.1056 0.1871 -0.0132 -0.0277 -0.0189 358  GLU A N   
1064 C CA  . GLU A 135 ? 0.1479 0.1076 0.1833 -0.0008 -0.0310 -0.0011 358  GLU A CA  
1065 C C   . GLU A 135 ? 0.1819 0.1117 0.1566 0.0059  -0.0494 -0.0176 358  GLU A C   
1066 O O   . GLU A 135 ? 0.2259 0.1404 0.1547 0.0246  0.0057  -0.0228 358  GLU A O   
1067 C CB  . GLU A 135 ? 0.1687 0.1383 0.2375 0.0101  -0.0397 0.0069  358  GLU A CB  
1068 C CG  . GLU A 135 ? 0.1821 0.1777 0.2204 -0.0037 -0.0560 -0.0030 358  GLU A CG  
1069 C CD  . GLU A 135 ? 0.2291 0.2446 0.1848 -0.0006 -0.0760 -0.0019 358  GLU A CD  
1070 O OE1 . GLU A 135 ? 0.2789 0.3055 0.2131 -0.0373 -0.0446 -0.0212 358  GLU A OE1 
1071 O OE2 . GLU A 135 ? 0.2251 0.2330 0.1880 -0.0169 -0.0415 0.0212  358  GLU A OE2 
1072 N N   . GLY A 136 ? 0.1863 0.1042 0.1434 0.0065  -0.0371 0.0009  359  GLY A N   
1073 C CA  . GLY A 136 ? 0.2066 0.1105 0.1815 0.0316  -0.0161 0.0209  359  GLY A CA  
1074 C C   . GLY A 136 ? 0.1894 0.1073 0.1581 0.0050  -0.0479 -0.0069 359  GLY A C   
1075 O O   . GLY A 136 ? 0.1875 0.1116 0.1842 0.0156  -0.0205 -0.0141 359  GLY A O   
1076 N N   . VAL A 137 ? 0.1869 0.0913 0.1731 0.0083  -0.0188 0.0065  360  VAL A N   
1077 C CA  . VAL A 137 ? 0.1616 0.1186 0.1531 -0.0145 -0.0440 0.0139  360  VAL A CA  
1078 C C   . VAL A 137 ? 0.1642 0.1226 0.1570 0.0202  -0.0315 0.0002  360  VAL A C   
1079 O O   . VAL A 137 ? 0.1817 0.1404 0.1840 0.0295  -0.0112 -0.0239 360  VAL A O   
1080 C CB  . VAL A 137 ? 0.1775 0.1243 0.1696 -0.0058 -0.0548 -0.0001 360  VAL A CB  
1081 C CG1 . VAL A 137 ? 0.2376 0.1321 0.1773 0.0013  -0.0154 -0.0146 360  VAL A CG1 
1082 C CG2 . VAL A 137 ? 0.1813 0.1511 0.2113 -0.0078 -0.0660 -0.0114 360  VAL A CG2 
1083 N N   . ILE A 138 ? 0.1729 0.1241 0.1474 0.0039  -0.0519 0.0173  361  ILE A N   
1084 C CA  . ILE A 138 ? 0.1820 0.1281 0.1610 0.0062  -0.0557 -0.0115 361  ILE A CA  
1085 C C   . ILE A 138 ? 0.1859 0.1217 0.1628 0.0253  -0.0379 -0.0204 361  ILE A C   
1086 O O   . ILE A 138 ? 0.1978 0.1192 0.1764 0.0371  -0.0312 0.0156  361  ILE A O   
1087 C CB  . ILE A 138 ? 0.1611 0.1277 0.1712 0.0014  -0.0588 0.0013  361  ILE A CB  
1088 C CG1 . ILE A 138 ? 0.1666 0.1307 0.1972 0.0219  -0.0196 -0.0186 361  ILE A CG1 
1089 C CG2 . ILE A 138 ? 0.1732 0.1573 0.1825 0.0060  -0.0421 0.0046  361  ILE A CG2 
1090 C CD1 . ILE A 138 ? 0.1698 0.1269 0.2081 -0.0030 -0.0184 -0.0277 361  ILE A CD1 
1091 N N   . SER A 139 ? 0.1742 0.1096 0.1951 0.0157  -0.0505 -0.0182 362  SER A N   
1092 C CA  . SER A 139 ? 0.2329 0.0914 0.2012 0.0141  -0.0196 -0.0179 362  SER A CA  
1093 C C   . SER A 139 ? 0.1901 0.1261 0.2052 0.0180  -0.0686 -0.0108 362  SER A C   
1094 O O   . SER A 139 ? 0.1706 0.1622 0.2290 0.0116  -0.0496 0.0030  362  SER A O   
1095 C CB  . SER A 139 ? 0.2499 0.1019 0.2287 0.0349  -0.0621 -0.0176 362  SER A CB  
1096 O OG  . SER A 139 ? 0.2533 0.1513 0.3168 0.0070  -0.0650 0.0086  362  SER A OG  
1097 N N   . THR A 140 ? 0.2114 0.1136 0.2214 0.0098  -0.0307 -0.0138 363  THR A N   
1098 C CA  . THR A 140 ? 0.2030 0.1079 0.2190 0.0174  -0.0439 -0.0096 363  THR A CA  
1099 C C   . THR A 140 ? 0.1870 0.1171 0.2076 0.0131  -0.0743 0.0010  363  THR A C   
1100 O O   . THR A 140 ? 0.2016 0.1436 0.2405 0.0396  -0.0858 0.0038  363  THR A O   
1101 C CB  . THR A 140 ? 0.1961 0.1088 0.2062 0.0187  -0.0345 -0.0154 363  THR A CB  
1102 O OG1 . THR A 140 ? 0.1636 0.1158 0.2163 0.0004  -0.0375 -0.0033 363  THR A OG1 
1103 C CG2 . THR A 140 ? 0.2097 0.1064 0.2035 0.0306  -0.0449 0.0059  363  THR A CG2 
1104 N N   . VAL A 141 ? 0.2269 0.1015 0.2209 0.0143  -0.0464 -0.0123 364  VAL A N   
1105 C CA  . VAL A 141 ? 0.2362 0.1156 0.2515 0.0247  -0.0104 -0.0036 364  VAL A CA  
1106 C C   . VAL A 141 ? 0.2709 0.1401 0.2745 0.0366  0.0042  0.0117  364  VAL A C   
1107 O O   . VAL A 141 ? 0.3122 0.1615 0.3257 0.0592  0.0390  0.0213  364  VAL A O   
1108 C CB  . VAL A 141 ? 0.2355 0.1505 0.2502 -0.0002 -0.0123 -0.0171 364  VAL A CB  
1109 C CG1 . VAL A 141 ? 0.2209 0.1517 0.2477 0.0143  0.0038  -0.0205 364  VAL A CG1 
1110 C CG2 . VAL A 141 ? 0.2679 0.1828 0.2925 -0.0238 0.0080  -0.0231 364  VAL A CG2 
1111 N N   . ALA A 142 ? 0.2522 0.1411 0.2418 0.0378  -0.0308 -0.0077 365  ALA A N   
1112 C CA  . ALA A 142 ? 0.2507 0.1406 0.2363 0.0694  -0.0431 -0.0100 365  ALA A CA  
1113 C C   . ALA A 142 ? 0.2541 0.1460 0.2455 0.0827  -0.0489 -0.0161 365  ALA A C   
1114 O O   . ALA A 142 ? 0.2706 0.1458 0.2453 0.0585  -0.0401 -0.0162 365  ALA A O   
1115 C CB  . ALA A 142 ? 0.2579 0.1410 0.2294 0.0659  -0.0425 -0.0142 365  ALA A CB  
1116 N N   . PRO A 143 ? 0.2531 0.1431 0.2624 0.0708  -0.0522 -0.0292 366  PRO A N   
1117 C CA  . PRO A 143 ? 0.2632 0.1530 0.3113 0.0611  -0.0413 -0.0268 366  PRO A CA  
1118 C C   . PRO A 143 ? 0.2167 0.1596 0.2941 0.0798  -0.0631 -0.0057 366  PRO A C   
1119 O O   . PRO A 143 ? 0.2529 0.1876 0.3071 0.0894  -0.0557 -0.0030 366  PRO A O   
1120 C CB  . PRO A 143 ? 0.2863 0.1566 0.3253 0.0620  -0.0250 -0.0268 366  PRO A CB  
1121 C CG  . PRO A 143 ? 0.2937 0.1463 0.3007 0.0651  -0.0207 -0.0585 366  PRO A CG  
1122 C CD  . PRO A 143 ? 0.2775 0.1432 0.2553 0.0763  -0.0412 -0.0577 366  PRO A CD  
1123 N N   . ARG A 144 ? 0.2445 0.1358 0.2968 0.0880  -0.0282 0.0010  367  ARG A N   
1124 C CA  . ARG A 144 ? 0.2634 0.1473 0.3123 0.0608  -0.0175 -0.0327 367  ARG A CA  
1125 C C   . ARG A 144 ? 0.2335 0.1506 0.2670 0.0677  -0.0466 -0.0045 367  ARG A C   
1126 O O   . ARG A 144 ? 0.2164 0.1469 0.2629 0.0534  -0.0397 -0.0107 367  ARG A O   
1127 C CB  . ARG A 144 ? 0.3164 0.1641 0.3852 0.0908  -0.0140 -0.0561 367  ARG A CB  
1128 C CG  . ARG A 144 ? 0.3665 0.2154 0.4654 0.1176  -0.0335 -0.0623 367  ARG A CG  
1129 C CD  . ARG A 144 ? 0.4601 0.2947 0.5748 0.1300  -0.0444 -0.0341 367  ARG A CD  
1130 N NE  . ARG A 144 ? 0.5432 0.3675 0.6744 0.1163  -0.0512 -0.0027 367  ARG A NE  
1131 C CZ  . ARG A 144 ? 0.6083 0.4219 0.7498 0.1163  -0.0825 0.0232  367  ARG A CZ  
1132 N NH1 . ARG A 144 ? 0.6362 0.4426 0.7805 0.1239  -0.0823 0.0239  367  ARG A NH1 
1133 N NH2 . ARG A 144 ? 0.6408 0.4464 0.7827 0.1025  -0.0777 0.0325  367  ARG A NH2 
1134 N N   . PHE A 145 ? 0.2155 0.1526 0.2185 0.0849  -0.0690 -0.0102 368  PHE A N   
1135 C CA  . PHE A 145 ? 0.1740 0.1477 0.2206 0.0518  -0.0643 -0.0224 368  PHE A CA  
1136 C C   . PHE A 145 ? 0.1513 0.1598 0.2345 0.0466  -0.0625 -0.0049 368  PHE A C   
1137 O O   . PHE A 145 ? 0.1963 0.1687 0.2556 0.0518  -0.0463 -0.0180 368  PHE A O   
1138 C CB  . PHE A 145 ? 0.1763 0.1529 0.2388 0.0642  -0.0250 -0.0175 368  PHE A CB  
1139 C CG  . PHE A 145 ? 0.1739 0.1490 0.1925 0.0537  -0.0514 -0.0169 368  PHE A CG  
1140 C CD1 . PHE A 145 ? 0.1612 0.1442 0.2255 0.0325  -0.0529 -0.0191 368  PHE A CD1 
1141 C CD2 . PHE A 145 ? 0.1871 0.1529 0.1850 0.0252  -0.0587 -0.0320 368  PHE A CD2 
1142 C CE1 . PHE A 145 ? 0.1779 0.1637 0.2174 0.0365  -0.0395 -0.0161 368  PHE A CE1 
1143 C CE2 . PHE A 145 ? 0.1806 0.1447 0.2134 0.0159  -0.0673 -0.0124 368  PHE A CE2 
1144 C CZ  . PHE A 145 ? 0.1832 0.1529 0.2071 0.0223  -0.0543 -0.0078 368  PHE A CZ  
1145 N N   . THR A 146 ? 0.1657 0.1696 0.2253 0.0259  -0.0641 -0.0217 369  THR A N   
1146 C CA  . THR A 146 ? 0.1790 0.1863 0.2390 0.0484  -0.0867 -0.0391 369  THR A CA  
1147 C C   . THR A 146 ? 0.1777 0.2016 0.2266 0.0550  -0.0615 -0.0392 369  THR A C   
1148 O O   . THR A 146 ? 0.1762 0.2290 0.2291 0.0741  -0.0738 -0.0427 369  THR A O   
1149 C CB  . THR A 146 ? 0.2023 0.1818 0.2903 0.0745  -0.0446 -0.0139 369  THR A CB  
1150 O OG1 . THR A 146 ? 0.2153 0.1998 0.3184 0.0480  -0.0266 -0.0498 369  THR A OG1 
1151 C CG2 . THR A 146 ? 0.2126 0.1790 0.2898 0.0781  -0.0542 0.0052  369  THR A CG2 
1152 N N   . PRO A 147 ? 0.1612 0.1925 0.2380 0.0589  -0.0555 -0.0252 370  PRO A N   
1153 C CA  . PRO A 147 ? 0.1642 0.1940 0.2187 0.0649  -0.0760 -0.0284 370  PRO A CA  
1154 C C   . PRO A 147 ? 0.1724 0.2095 0.2494 0.0550  -0.0800 -0.0447 370  PRO A C   
1155 O O   . PRO A 147 ? 0.1591 0.2138 0.2935 0.0518  -0.0761 -0.0697 370  PRO A O   
1156 C CB  . PRO A 147 ? 0.1720 0.1786 0.2185 0.0784  -0.0376 0.0034  370  PRO A CB  
1157 C CG  . PRO A 147 ? 0.1839 0.1568 0.2026 0.0842  -0.0299 -0.0052 370  PRO A CG  
1158 C CD  . PRO A 147 ? 0.1594 0.1816 0.2119 0.0694  -0.0299 -0.0089 370  PRO A CD  
1159 N N   A LYS A 148 ? 0.1831 0.2241 0.2447 0.0594  -0.0820 -0.0605 371  LYS A N   
1160 N N   B LYS A 148 ? 0.1804 0.2183 0.2487 0.0599  -0.0827 -0.0455 371  LYS A N   
1161 C CA  A LYS A 148 ? 0.1823 0.2537 0.2545 0.0751  -0.0944 -0.0438 371  LYS A CA  
1162 C CA  B LYS A 148 ? 0.1772 0.2416 0.2603 0.0762  -0.0954 -0.0172 371  LYS A CA  
1163 C C   A LYS A 148 ? 0.1809 0.2527 0.2794 0.0591  -0.0873 -0.0342 371  LYS A C   
1164 C C   B LYS A 148 ? 0.1641 0.2454 0.2764 0.0629  -0.0970 -0.0188 371  LYS A C   
1165 O O   A LYS A 148 ? 0.2078 0.2674 0.3010 0.0597  -0.0810 -0.0463 371  LYS A O   
1166 O O   B LYS A 148 ? 0.1693 0.2587 0.2751 0.0615  -0.1075 -0.0226 371  LYS A O   
1167 C CB  A LYS A 148 ? 0.1909 0.2812 0.2556 0.0713  -0.0861 -0.0629 371  LYS A CB  
1168 C CB  B LYS A 148 ? 0.1924 0.2615 0.2703 0.0752  -0.0809 -0.0115 371  LYS A CB  
1169 C CG  A LYS A 148 ? 0.1842 0.3049 0.2522 0.0553  -0.1069 -0.0887 371  LYS A CG  
1170 C CG  B LYS A 148 ? 0.1906 0.2843 0.2832 0.0692  -0.0905 -0.0118 371  LYS A CG  
1171 C CD  A LYS A 148 ? 0.1961 0.3240 0.2488 0.0577  -0.1109 -0.0845 371  LYS A CD  
1172 C CD  B LYS A 148 ? 0.2224 0.2963 0.2836 0.0878  -0.0947 0.0209  371  LYS A CD  
1173 C CE  A LYS A 148 ? 0.2150 0.3476 0.2640 0.0651  -0.0985 -0.0949 371  LYS A CE  
1174 C CE  B LYS A 148 ? 0.2494 0.3042 0.2998 0.0734  -0.0625 0.0124  371  LYS A CE  
1175 N NZ  A LYS A 148 ? 0.2123 0.3534 0.2877 0.0574  -0.0950 -0.1068 371  LYS A NZ  
1176 N NZ  B LYS A 148 ? 0.2502 0.3072 0.2990 0.0702  -0.0618 0.0180  371  LYS A NZ  
1177 N N   . LEU A 149 ? 0.1677 0.2325 0.2772 0.0597  -0.0786 -0.0167 372  LEU A N   
1178 C CA  . LEU A 149 ? 0.1775 0.2347 0.3083 0.0529  -0.0739 -0.0007 372  LEU A CA  
1179 C C   . LEU A 149 ? 0.1918 0.2280 0.3068 0.0425  -0.0575 -0.0002 372  LEU A C   
1180 O O   . LEU A 149 ? 0.2388 0.2378 0.3734 0.0649  -0.0007 0.0240  372  LEU A O   
1181 C CB  . LEU A 149 ? 0.2191 0.2395 0.3350 0.0584  -0.0533 -0.0083 372  LEU A CB  
1182 C CG  . LEU A 149 ? 0.2754 0.2498 0.3539 0.0564  -0.0666 -0.0368 372  LEU A CG  
1183 C CD1 . LEU A 149 ? 0.2696 0.2436 0.3703 0.0615  -0.0632 -0.0561 372  LEU A CD1 
1184 C CD2 . LEU A 149 ? 0.3105 0.2540 0.3492 0.0683  -0.1052 -0.0167 372  LEU A CD2 
1185 N N   . GLY A 150 ? 0.1944 0.2154 0.2585 0.0463  -0.0951 -0.0016 373  GLY A N   
1186 C CA  . GLY A 150 ? 0.1965 0.2074 0.2595 0.0327  -0.0726 -0.0335 373  GLY A CA  
1187 C C   . GLY A 150 ? 0.1781 0.2015 0.2474 0.0323  -0.0969 -0.0321 373  GLY A C   
1188 O O   . GLY A 150 ? 0.2272 0.2142 0.2580 0.0595  -0.0580 -0.0236 373  GLY A O   
1189 N N   . SER A 151 ? 0.1389 0.1850 0.2507 0.0259  -0.0861 -0.0353 374  SER A N   
1190 C CA  . SER A 151 ? 0.1409 0.1934 0.2526 0.0430  -0.0721 -0.0470 374  SER A CA  
1191 C C   . SER A 151 ? 0.1584 0.1778 0.2270 0.0274  -0.0483 -0.0413 374  SER A C   
1192 O O   . SER A 151 ? 0.1689 0.1821 0.2323 0.0248  -0.0546 -0.0300 374  SER A O   
1193 C CB  . SER A 151 ? 0.1851 0.1996 0.2744 0.0892  -0.0164 -0.0381 374  SER A CB  
1194 O OG  . SER A 151 ? 0.2193 0.2202 0.3274 0.0884  0.0032  -0.0561 374  SER A OG  
1195 N N   . VAL A 152 ? 0.1592 0.1612 0.2272 0.0381  -0.0573 -0.0436 375  VAL A N   
1196 C CA  . VAL A 152 ? 0.1422 0.1383 0.2223 0.0120  -0.0354 -0.0468 375  VAL A CA  
1197 C C   . VAL A 152 ? 0.1585 0.1469 0.2191 0.0243  -0.0501 -0.0349 375  VAL A C   
1198 O O   . VAL A 152 ? 0.2008 0.1657 0.2442 -0.0033 -0.0091 -0.0433 375  VAL A O   
1199 C CB  . VAL A 152 ? 0.1849 0.1489 0.2099 0.0526  -0.0205 -0.0258 375  VAL A CB  
1200 C CG1 . VAL A 152 ? 0.1931 0.1793 0.1951 0.0465  -0.0417 -0.0271 375  VAL A CG1 
1201 C CG2 . VAL A 152 ? 0.2095 0.1442 0.2190 0.0648  -0.0237 -0.0003 375  VAL A CG2 
1202 N N   . MET A 153 ? 0.1732 0.1495 0.2048 0.0219  -0.0637 -0.0480 376  MET A N   
1203 C CA  . MET A 153 ? 0.2122 0.1301 0.2008 0.0213  -0.0571 -0.0426 376  MET A CA  
1204 C C   . MET A 153 ? 0.2157 0.1423 0.1721 0.0197  -0.0552 -0.0144 376  MET A C   
1205 O O   . MET A 153 ? 0.2254 0.1437 0.2039 0.0174  -0.0056 -0.0049 376  MET A O   
1206 C CB  . MET A 153 ? 0.2394 0.1323 0.2343 0.0285  -0.0333 -0.0602 376  MET A CB  
1207 C CG  . MET A 153 ? 0.2098 0.1444 0.2588 0.0455  -0.0255 -0.0770 376  MET A CG  
1208 S SD  . MET A 153 ? 0.2322 0.1532 0.2538 0.0257  -0.0187 -0.0403 376  MET A SD  
1209 C CE  . MET A 153 ? 0.2357 0.1250 0.3116 0.0113  -0.0015 -0.0249 376  MET A CE  
1210 N N   . ILE A 154 ? 0.1995 0.1302 0.1834 0.0295  -0.0425 -0.0242 377  ILE A N   
1211 C CA  . ILE A 154 ? 0.1968 0.1170 0.1969 0.0603  -0.0600 -0.0214 377  ILE A CA  
1212 C C   . ILE A 154 ? 0.2087 0.1329 0.1804 0.0429  -0.0147 -0.0144 377  ILE A C   
1213 O O   . ILE A 154 ? 0.2262 0.1257 0.2112 0.0234  -0.0290 -0.0203 377  ILE A O   
1214 C CB  . ILE A 154 ? 0.1803 0.1216 0.2171 0.0618  -0.0133 -0.0094 377  ILE A CB  
1215 C CG1 . ILE A 154 ? 0.1780 0.0991 0.2167 0.0521  -0.0390 -0.0154 377  ILE A CG1 
1216 C CG2 . ILE A 154 ? 0.1873 0.1551 0.2377 0.0429  0.0093  -0.0093 377  ILE A CG2 
1217 C CD1 . ILE A 154 ? 0.1814 0.1050 0.2278 0.0341  -0.0439 -0.0226 377  ILE A CD1 
1218 N N   . GLY A 155 ? 0.2010 0.1248 0.1649 0.0278  -0.0081 -0.0193 378  GLY A N   
1219 C CA  . GLY A 155 ? 0.1992 0.1348 0.1625 0.0444  -0.0150 -0.0229 378  GLY A CA  
1220 C C   . GLY A 155 ? 0.2076 0.1288 0.1647 0.0389  0.0167  -0.0322 378  GLY A C   
1221 O O   . GLY A 155 ? 0.2387 0.1344 0.1718 0.0419  0.0225  -0.0338 378  GLY A O   
1222 N N   . THR A 156 ? 0.2038 0.1429 0.1746 0.0176  -0.0022 -0.0206 379  THR A N   
1223 C CA  . THR A 156 ? 0.2335 0.1506 0.1799 0.0090  -0.0514 -0.0375 379  THR A CA  
1224 C C   . THR A 156 ? 0.2649 0.1596 0.1943 0.0215  -0.0341 -0.0332 379  THR A C   
1225 O O   . THR A 156 ? 0.2911 0.1542 0.2122 0.0369  -0.0241 -0.0354 379  THR A O   
1226 C CB  . THR A 156 ? 0.2160 0.1517 0.1992 0.0093  0.0025  -0.0428 379  THR A CB  
1227 O OG1 . THR A 156 ? 0.2340 0.2015 0.2007 0.0512  0.0005  -0.0296 379  THR A OG1 
1228 C CG2 . THR A 156 ? 0.2347 0.1524 0.2176 -0.0032 0.0033  -0.0681 379  THR A CG2 
1229 N N   . TRP A 157 ? 0.2611 0.1630 0.1863 0.0045  -0.0584 -0.0328 380  TRP A N   
1230 C CA  . TRP A 157 ? 0.2995 0.1854 0.1986 0.0143  -0.0448 -0.0503 380  TRP A CA  
1231 C C   . TRP A 157 ? 0.3765 0.1949 0.2045 -0.0042 -0.0146 -0.0428 380  TRP A C   
1232 O O   . TRP A 157 ? 0.4170 0.2104 0.2168 -0.0295 0.0195  -0.0736 380  TRP A O   
1233 C CB  . TRP A 157 ? 0.2670 0.1939 0.2259 0.0230  -0.0602 -0.0459 380  TRP A CB  
1234 C CG  . TRP A 157 ? 0.2747 0.1972 0.2666 -0.0191 -0.0185 -0.0667 380  TRP A CG  
1235 C CD1 . TRP A 157 ? 0.3119 0.2229 0.2979 -0.0329 0.0173  -0.0845 380  TRP A CD1 
1236 C CD2 . TRP A 157 ? 0.2731 0.1961 0.2445 -0.0278 -0.0483 -0.0509 380  TRP A CD2 
1237 N NE1 . TRP A 157 ? 0.3024 0.2264 0.2996 -0.0207 0.0138  -0.0895 380  TRP A NE1 
1238 C CE2 . TRP A 157 ? 0.2685 0.1972 0.2617 -0.0204 -0.0453 -0.0551 380  TRP A CE2 
1239 C CE3 . TRP A 157 ? 0.2585 0.1786 0.2484 -0.0181 -0.0173 -0.0327 380  TRP A CE3 
1240 C CZ2 . TRP A 157 ? 0.2846 0.1801 0.2949 0.0066  -0.0334 -0.0228 380  TRP A CZ2 
1241 C CZ3 . TRP A 157 ? 0.2348 0.1700 0.2768 -0.0068 -0.0498 -0.0140 380  TRP A CZ3 
1242 C CH2 . TRP A 157 ? 0.2567 0.1688 0.2606 0.0273  -0.0679 -0.0079 380  TRP A CH2 
1243 N N   . THR A 158 ? 0.3951 0.2000 0.2055 -0.0405 0.0127  -0.0547 381  THR A N   
1244 C CA  . THR A 158 ? 0.4438 0.2238 0.2287 -0.0600 0.0313  -0.0423 381  THR A CA  
1245 C C   . THR A 158 ? 0.4502 0.2207 0.2482 -0.0527 0.0576  -0.0572 381  THR A C   
1246 O O   . THR A 158 ? 0.4147 0.2106 0.2258 -0.0105 0.0115  -0.0120 381  THR A O   
1247 C CB  . THR A 158 ? 0.4466 0.2397 0.2223 -0.0691 0.0426  -0.0401 381  THR A CB  
1248 O OG1 . THR A 158 ? 0.4955 0.2580 0.2256 -0.0461 0.0733  -0.0497 381  THR A OG1 
1249 C CG2 . THR A 158 ? 0.4387 0.2245 0.2451 -0.0501 0.0346  -0.0353 381  THR A CG2 
1250 N N   . THR A 159 ? 0.4923 0.2581 0.2755 -0.0867 0.0677  -0.0692 382  THR A N   
1251 C CA  . THR A 159 ? 0.5500 0.2896 0.3249 -0.0647 0.0823  -0.0742 382  THR A CA  
1252 C C   . THR A 159 ? 0.5561 0.3094 0.3452 -0.0217 0.0793  -0.0913 382  THR A C   
1253 O O   . THR A 159 ? 0.5754 0.3427 0.3738 -0.0148 0.0849  -0.0834 382  THR A O   
1254 C CB  . THR A 159 ? 0.5831 0.3031 0.3436 -0.0707 0.1018  -0.0646 382  THR A CB  
1255 O OG1 . THR A 159 ? 0.6035 0.3159 0.3496 -0.0721 0.0946  -0.0640 382  THR A OG1 
1256 C CG2 . THR A 159 ? 0.5971 0.3114 0.3442 -0.0681 0.1069  -0.0702 382  THR A CG2 
1257 N N   . ASP A 160 ? 0.5395 0.2700 0.3199 0.0036  0.0703  -0.1230 383  ASP A N   
1258 C CA  . ASP A 160 ? 0.5375 0.2851 0.3468 0.0303  0.0656  -0.1210 383  ASP A CA  
1259 C C   . ASP A 160 ? 0.4861 0.2681 0.3560 0.0286  0.0819  -0.1055 383  ASP A C   
1260 O O   . ASP A 160 ? 0.5110 0.2898 0.4213 0.0526  0.1034  -0.1063 383  ASP A O   
1261 C CB  . ASP A 160 ? 0.6265 0.3438 0.3914 0.0100  0.0868  -0.1110 383  ASP A CB  
1262 C CG  . ASP A 160 ? 0.7093 0.3939 0.4540 -0.0025 0.1179  -0.1010 383  ASP A CG  
1263 O OD1 . ASP A 160 ? 0.7325 0.4089 0.4874 -0.0050 0.0997  -0.0839 383  ASP A OD1 
1264 O OD2 . ASP A 160 ? 0.7571 0.4243 0.4832 -0.0199 0.1406  -0.0891 383  ASP A OD2 
1265 N N   . ASP A 161 ? 0.3675 0.2385 0.2598 0.0432  0.0165  -0.0921 384  ASP A N   
1266 C CA  . ASP A 161 ? 0.3180 0.2018 0.2215 0.0294  -0.0017 -0.0611 384  ASP A CA  
1267 C C   . ASP A 161 ? 0.2773 0.1881 0.2056 0.0474  0.0104  -0.0422 384  ASP A C   
1268 O O   . ASP A 161 ? 0.2628 0.1754 0.2321 0.0360  0.0069  -0.0547 384  ASP A O   
1269 C CB  . ASP A 161 ? 0.3262 0.2084 0.2332 0.0283  0.0063  -0.0501 384  ASP A CB  
1270 C CG  . ASP A 161 ? 0.3210 0.2220 0.2494 0.0259  0.0287  -0.0419 384  ASP A CG  
1271 O OD1 . ASP A 161 ? 0.3310 0.2431 0.2671 0.0459  0.0386  -0.0408 384  ASP A OD1 
1272 O OD2 . ASP A 161 ? 0.2937 0.2333 0.2616 0.0360  -0.0064 -0.0170 384  ASP A OD2 
1273 N N   . ILE A 162 ? 0.2698 0.1986 0.2424 0.0275  0.0273  -0.0131 385  ILE A N   
1274 C CA  . ILE A 162 ? 0.2501 0.1981 0.2474 0.0457  0.0391  -0.0198 385  ILE A CA  
1275 C C   . ILE A 162 ? 0.2613 0.1991 0.2707 0.0400  0.0117  -0.0281 385  ILE A C   
1276 O O   . ILE A 162 ? 0.2753 0.2057 0.3048 0.0534  0.0201  -0.0342 385  ILE A O   
1277 C CB  . ILE A 162 ? 0.2317 0.2097 0.2134 0.0438  0.0133  -0.0029 385  ILE A CB  
1278 C CG1 . ILE A 162 ? 0.2451 0.2170 0.2344 0.0536  0.0092  -0.0125 385  ILE A CG1 
1279 C CG2 . ILE A 162 ? 0.2314 0.2124 0.1891 0.0293  -0.0011 -0.0275 385  ILE A CG2 
1280 C CD1 . ILE A 162 ? 0.2757 0.2090 0.2313 0.0620  0.0165  -0.0092 385  ILE A CD1 
1281 N N   . GLN A 163 ? 0.2379 0.2024 0.2579 0.0252  0.0124  -0.0621 386  GLN A N   
1282 C CA  . GLN A 163 ? 0.2397 0.2050 0.2649 0.0127  0.0028  -0.0597 386  GLN A CA  
1283 C C   . GLN A 163 ? 0.2188 0.2015 0.2868 0.0405  0.0022  -0.0331 386  GLN A C   
1284 O O   . GLN A 163 ? 0.1976 0.2045 0.2783 0.0321  -0.0014 -0.0199 386  GLN A O   
1285 C CB  . GLN A 163 ? 0.2574 0.2132 0.2602 0.0278  0.0171  -0.0263 386  GLN A CB  
1286 C CG  . GLN A 163 ? 0.2838 0.2167 0.2567 0.0043  0.0162  -0.0210 386  GLN A CG  
1287 C CD  . GLN A 163 ? 0.3258 0.2434 0.2806 0.0063  0.0311  -0.0258 386  GLN A CD  
1288 O OE1 . GLN A 163 ? 0.3418 0.2562 0.2786 0.0144  0.0187  -0.0295 386  GLN A OE1 
1289 N NE2 . GLN A 163 ? 0.3214 0.2511 0.2494 0.0050  0.0472  -0.0396 386  GLN A NE2 
1290 N N   . ASP A 164 ? 0.2237 0.1882 0.3098 0.0225  0.0322  -0.0333 387  ASP A N   
1291 C CA  . ASP A 164 ? 0.1892 0.1868 0.3265 0.0404  0.0240  -0.0326 387  ASP A CA  
1292 C C   . ASP A 164 ? 0.2019 0.2116 0.3130 0.0292  0.0270  -0.0220 387  ASP A C   
1293 O O   . ASP A 164 ? 0.1964 0.2340 0.3642 0.0293  0.0263  -0.0225 387  ASP A O   
1294 C CB  . ASP A 164 ? 0.1901 0.2125 0.4003 0.0662  0.0689  -0.0171 387  ASP A CB  
1295 C CG  . ASP A 164 ? 0.2205 0.2383 0.4718 0.0696  0.1029  -0.0253 387  ASP A CG  
1296 O OD1 . ASP A 164 ? 0.2501 0.2260 0.4665 0.0609  0.0958  -0.0258 387  ASP A OD1 
1297 O OD2 . ASP A 164 ? 0.3005 0.2838 0.5538 0.0737  0.1199  -0.0093 387  ASP A OD2 
1298 N N   . GLN A 165 ? 0.1864 0.1958 0.2509 0.0469  0.0138  -0.0074 388  GLN A N   
1299 C CA  . GLN A 165 ? 0.1910 0.1940 0.2594 0.0198  0.0118  -0.0170 388  GLN A CA  
1300 C C   . GLN A 165 ? 0.1749 0.1982 0.2559 -0.0139 -0.0236 -0.0209 388  GLN A C   
1301 O O   . GLN A 165 ? 0.1876 0.1999 0.2654 0.0041  -0.0313 -0.0428 388  GLN A O   
1302 C CB  . GLN A 165 ? 0.2039 0.2058 0.2443 0.0251  -0.0073 -0.0073 388  GLN A CB  
1303 C CG  . GLN A 165 ? 0.2184 0.2131 0.2547 -0.0043 0.0306  -0.0155 388  GLN A CG  
1304 C CD  . GLN A 165 ? 0.2258 0.2308 0.2679 -0.0205 0.0366  -0.0212 388  GLN A CD  
1305 O OE1 . GLN A 165 ? 0.2179 0.2457 0.2497 0.0024  0.0006  0.0042  388  GLN A OE1 
1306 N NE2 . GLN A 165 ? 0.2546 0.2516 0.2964 -0.0286 0.0647  -0.0241 388  GLN A NE2 
1307 N N   . PRO A 166 ? 0.1823 0.1990 0.2603 -0.0317 -0.0011 -0.0246 389  PRO A N   
1308 C CA  . PRO A 166 ? 0.1728 0.2050 0.2584 -0.0384 -0.0011 -0.0326 389  PRO A CA  
1309 C C   . PRO A 166 ? 0.1723 0.2076 0.2469 -0.0106 -0.0243 -0.0272 389  PRO A C   
1310 O O   . PRO A 166 ? 0.1704 0.2263 0.2520 -0.0138 -0.0123 -0.0168 389  PRO A O   
1311 C CB  . PRO A 166 ? 0.1744 0.1913 0.2505 -0.0316 0.0228  -0.0403 389  PRO A CB  
1312 C CG  . PRO A 166 ? 0.2058 0.1911 0.2411 -0.0190 0.0033  -0.0359 389  PRO A CG  
1313 C CD  . PRO A 166 ? 0.2024 0.1920 0.2660 -0.0427 0.0090  -0.0203 389  PRO A CD  
1314 N N   . SER A 167 ? 0.1627 0.1659 0.2176 -0.0093 -0.0406 -0.0302 390  SER A N   
1315 C CA  . SER A 167 ? 0.1828 0.1724 0.2134 -0.0134 -0.0146 -0.0452 390  SER A CA  
1316 C C   . SER A 167 ? 0.1508 0.1790 0.2037 0.0060  -0.0473 -0.0481 390  SER A C   
1317 O O   . SER A 167 ? 0.1508 0.2126 0.2098 0.0021  -0.0418 -0.0344 390  SER A O   
1318 C CB  . SER A 167 ? 0.2161 0.1586 0.2130 -0.0084 0.0012  -0.0429 390  SER A CB  
1319 O OG  . SER A 167 ? 0.2033 0.1555 0.2242 -0.0027 -0.0084 -0.0422 390  SER A OG  
1320 N N   . ARG A 168 ? 0.1626 0.1711 0.2087 -0.0038 -0.0193 -0.0264 391  ARG A N   
1321 C CA  . ARG A 168 ? 0.1796 0.1879 0.2002 -0.0096 -0.0313 -0.0284 391  ARG A CA  
1322 C C   . ARG A 168 ? 0.1636 0.1758 0.2035 -0.0058 -0.0194 -0.0132 391  ARG A C   
1323 O O   . ARG A 168 ? 0.2152 0.2104 0.1799 -0.0493 -0.0426 0.0188  391  ARG A O   
1331 N N   . PHE A 169 ? 0.1367 0.1500 0.1990 0.0198  -0.0065 -0.0015 392  PHE A N   
1332 C CA  . PHE A 169 ? 0.1156 0.1302 0.1877 0.0110  -0.0442 -0.0020 392  PHE A CA  
1333 C C   . PHE A 169 ? 0.1306 0.1235 0.1741 0.0102  -0.0395 -0.0080 392  PHE A C   
1334 O O   . PHE A 169 ? 0.1677 0.1538 0.1871 0.0067  -0.0547 -0.0146 392  PHE A O   
1335 C CB  . PHE A 169 ? 0.1386 0.1378 0.1906 -0.0020 -0.0445 -0.0047 392  PHE A CB  
1336 C CG  . PHE A 169 ? 0.1372 0.1278 0.1753 0.0213  -0.0629 -0.0162 392  PHE A CG  
1337 C CD1 . PHE A 169 ? 0.1492 0.1204 0.1778 0.0191  -0.0429 -0.0187 392  PHE A CD1 
1338 C CD2 . PHE A 169 ? 0.1596 0.1294 0.1838 0.0314  -0.0412 0.0053  392  PHE A CD2 
1339 C CE1 . PHE A 169 ? 0.1779 0.1260 0.2067 0.0395  -0.0341 -0.0090 392  PHE A CE1 
1340 C CE2 . PHE A 169 ? 0.1544 0.1300 0.1910 0.0330  -0.0624 0.0001  392  PHE A CE2 
1341 C CZ  . PHE A 169 ? 0.1715 0.1401 0.2054 0.0205  -0.0557 -0.0163 392  PHE A CZ  
1342 N N   . THR A 170 ? 0.1459 0.0822 0.1859 0.0190  -0.0273 0.0094  393  THR A N   
1343 C CA  . THR A 170 ? 0.1436 0.0844 0.1704 0.0260  -0.0509 0.0116  393  THR A CA  
1344 C C   . THR A 170 ? 0.1448 0.1081 0.1428 -0.0023 -0.0584 -0.0096 393  THR A C   
1345 O O   . THR A 170 ? 0.1615 0.1115 0.1395 0.0108  -0.0260 0.0056  393  THR A O   
1346 C CB  . THR A 170 ? 0.1498 0.1002 0.1653 0.0118  -0.0308 0.0073  393  THR A CB  
1347 O OG1 . THR A 170 ? 0.1757 0.1041 0.1910 -0.0202 -0.0333 -0.0048 393  THR A OG1 
1348 C CG2 . THR A 170 ? 0.1783 0.1099 0.1684 0.0382  -0.0116 -0.0138 393  THR A CG2 
1349 N N   . PRO A 171 ? 0.1444 0.1164 0.1347 -0.0195 -0.0393 -0.0154 394  PRO A N   
1350 C CA  . PRO A 171 ? 0.1499 0.1165 0.1180 -0.0118 -0.0475 -0.0029 394  PRO A CA  
1351 C C   . PRO A 171 ? 0.1525 0.0987 0.1362 -0.0047 -0.0520 -0.0066 394  PRO A C   
1352 O O   . PRO A 171 ? 0.1672 0.0910 0.1677 0.0004  -0.0253 -0.0071 394  PRO A O   
1353 C CB  . PRO A 171 ? 0.1678 0.1239 0.1224 -0.0120 -0.0489 -0.0053 394  PRO A CB  
1354 C CG  . PRO A 171 ? 0.1399 0.1179 0.1645 -0.0073 -0.0633 0.0106  394  PRO A CG  
1355 C CD  . PRO A 171 ? 0.1599 0.1247 0.1323 -0.0102 -0.0529 -0.0095 394  PRO A CD  
1356 N N   . VAL A 172 ? 0.1318 0.1109 0.1289 0.0108  -0.0545 -0.0057 395  VAL A N   
1357 C CA  . VAL A 172 ? 0.1563 0.0988 0.1279 0.0066  -0.0685 -0.0155 395  VAL A CA  
1358 C C   . VAL A 172 ? 0.1864 0.0874 0.1630 -0.0059 -0.0358 -0.0066 395  VAL A C   
1359 O O   . VAL A 172 ? 0.1659 0.1001 0.1773 0.0080  -0.0389 -0.0044 395  VAL A O   
1360 C CB  . VAL A 172 ? 0.1634 0.1051 0.1426 -0.0037 -0.0674 -0.0112 395  VAL A CB  
1361 C CG1 . VAL A 172 ? 0.1514 0.1173 0.1848 0.0291  -0.0568 -0.0103 395  VAL A CG1 
1362 C CG2 . VAL A 172 ? 0.2159 0.1016 0.1231 -0.0006 -0.0240 0.0075  395  VAL A CG2 
1363 N N   . GLY A 173 ? 0.1820 0.0788 0.1619 -0.0227 -0.0665 0.0110  396  GLY A N   
1364 C CA  . GLY A 173 ? 0.1785 0.0700 0.1892 0.0005  -0.0293 0.0006  396  GLY A CA  
1365 C C   . GLY A 173 ? 0.1586 0.0735 0.1528 -0.0003 -0.0235 0.0031  396  GLY A C   
1366 O O   . GLY A 173 ? 0.1610 0.1084 0.1640 -0.0129 -0.0251 0.0122  396  GLY A O   
1367 N N   . LEU A 174 ? 0.1750 0.0733 0.1684 0.0003  -0.0421 0.0079  397  LEU A N   
1368 C CA  . LEU A 174 ? 0.1832 0.0814 0.1627 -0.0122 -0.0370 0.0082  397  LEU A CA  
1369 C C   . LEU A 174 ? 0.1567 0.1027 0.1628 -0.0144 -0.0496 -0.0015 397  LEU A C   
1370 O O   . LEU A 174 ? 0.1819 0.1230 0.1634 0.0151  -0.0610 0.0013  397  LEU A O   
1371 C CB  . LEU A 174 ? 0.1573 0.1186 0.1594 -0.0166 -0.0530 0.0284  397  LEU A CB  
1372 C CG  . LEU A 174 ? 0.1681 0.1580 0.1868 -0.0253 -0.0490 0.0135  397  LEU A CG  
1373 C CD1 . LEU A 174 ? 0.1648 0.1726 0.1967 -0.0266 -0.0244 0.0341  397  LEU A CD1 
1374 C CD2 . LEU A 174 ? 0.1758 0.1900 0.2203 -0.0303 -0.0443 0.0163  397  LEU A CD2 
1375 N N   . ASN A 175 ? 0.1645 0.0873 0.1736 -0.0046 -0.0400 -0.0109 398  ASN A N   
1376 C CA  . ASN A 175 ? 0.1630 0.1238 0.1938 -0.0005 -0.0590 -0.0280 398  ASN A CA  
1377 C C   . ASN A 175 ? 0.1832 0.1385 0.2227 0.0142  -0.0772 -0.0161 398  ASN A C   
1378 O O   . ASN A 175 ? 0.2184 0.1533 0.2217 0.0016  -0.0477 -0.0161 398  ASN A O   
1379 C CB  . ASN A 175 ? 0.1976 0.1299 0.1917 0.0243  -0.0810 -0.0033 398  ASN A CB  
1380 C CG  . ASN A 175 ? 0.2462 0.1483 0.1995 0.0316  -0.1278 -0.0082 398  ASN A CG  
1381 O OD1 . ASN A 175 ? 0.2543 0.1718 0.1951 0.0518  -0.0577 -0.0152 398  ASN A OD1 
1382 N ND2 . ASN A 175 ? 0.3939 0.1618 0.2516 0.0341  -0.1014 -0.0540 398  ASN A ND2 
1383 N N   . ASP A 176 ? 0.2024 0.1414 0.2373 -0.0182 -0.0375 -0.0117 399  ASP A N   
1384 C CA  . ASP A 176 ? 0.2240 0.1319 0.2194 -0.0097 -0.0453 -0.0173 399  ASP A CA  
1385 C C   . ASP A 176 ? 0.2442 0.1193 0.2147 -0.0219 -0.0878 0.0025  399  ASP A C   
1386 O O   . ASP A 176 ? 0.2864 0.1370 0.2496 -0.0445 -0.0969 0.0301  399  ASP A O   
1387 C CB  . ASP A 176 ? 0.2720 0.1573 0.2235 -0.0234 -0.0307 -0.0448 399  ASP A CB  
1388 C CG  . ASP A 176 ? 0.3621 0.1779 0.2336 -0.0069 -0.0387 -0.0643 399  ASP A CG  
1389 O OD1 . ASP A 176 ? 0.3457 0.1815 0.2403 -0.0034 -0.0869 -0.0287 399  ASP A OD1 
1390 O OD2 . ASP A 176 ? 0.3862 0.2231 0.2497 -0.0204 -0.0548 -0.0497 399  ASP A OD2 
1391 N N   . ASP A 177 ? 0.2805 0.1214 0.1882 -0.0356 -0.0421 0.0164  400  ASP A N   
1392 C CA  . ASP A 177 ? 0.2845 0.1282 0.2107 -0.0160 -0.0604 0.0344  400  ASP A CA  
1393 C C   . ASP A 177 ? 0.2803 0.1143 0.2207 -0.0372 -0.0747 0.0085  400  ASP A C   
1394 O O   . ASP A 177 ? 0.2931 0.1380 0.2211 -0.0295 -0.0575 0.0199  400  ASP A O   
1395 C CB  . ASP A 177 ? 0.2613 0.1459 0.2058 0.0141  -0.0595 0.0227  400  ASP A CB  
1396 C CG  . ASP A 177 ? 0.2592 0.1930 0.2314 0.0164  -0.0486 0.0088  400  ASP A CG  
1397 O OD1 . ASP A 177 ? 0.2476 0.2224 0.2163 0.0039  -0.0547 -0.0175 400  ASP A OD1 
1398 O OD2 . ASP A 177 ? 0.3034 0.2399 0.3012 0.0095  -0.0127 0.0168  400  ASP A OD2 
1399 N N   . ASP A 178 ? 0.3027 0.1205 0.2401 -0.0314 -0.1065 -0.0198 401  ASP A N   
1400 C CA  . ASP A 178 ? 0.3367 0.1346 0.2693 -0.0145 -0.1104 -0.0222 401  ASP A CA  
1401 C C   . ASP A 178 ? 0.3491 0.1483 0.2916 -0.0006 -0.1118 -0.0109 401  ASP A C   
1402 O O   . ASP A 178 ? 0.3774 0.1643 0.3276 0.0123  -0.0941 0.0455  401  ASP A O   
1403 C CB  . ASP A 178 ? 0.3742 0.1787 0.2946 -0.0102 -0.1324 -0.0740 401  ASP A CB  
1404 C CG  . ASP A 178 ? 0.4066 0.2160 0.3403 0.0079  -0.1278 -0.0776 401  ASP A CG  
1405 O OD1 . ASP A 178 ? 0.4425 0.2321 0.3408 0.0103  -0.1204 -0.0737 401  ASP A OD1 
1406 O OD2 . ASP A 178 ? 0.4116 0.2427 0.4047 0.0340  -0.1050 -0.0709 401  ASP A OD2 
1407 N N   . ASN A 179 ? 0.3308 0.1440 0.2696 0.0341  -0.1341 -0.0478 402  ASN A N   
1408 C CA  . ASN A 179 ? 0.3535 0.1444 0.2843 0.0472  -0.1182 -0.0289 402  ASN A CA  
1409 C C   . ASN A 179 ? 0.2835 0.1496 0.2479 0.0396  -0.0932 -0.0279 402  ASN A C   
1410 O O   . ASN A 179 ? 0.2780 0.1801 0.2969 0.0387  -0.0633 -0.0332 402  ASN A O   
1411 C CB  . ASN A 179 ? 0.3982 0.1559 0.3645 0.0607  -0.1111 -0.0598 402  ASN A CB  
1412 C CG  . ASN A 179 ? 0.4818 0.2075 0.4294 0.0613  -0.0769 -0.0520 402  ASN A CG  
1413 O OD1 . ASN A 179 ? 0.5121 0.2240 0.4460 0.0439  -0.0683 -0.0372 402  ASN A OD1 
1414 N ND2 . ASN A 179 ? 0.5057 0.2276 0.4647 0.0769  -0.0562 -0.0545 402  ASN A ND2 
1415 N N   . TYR A 180 ? 0.2483 0.1033 0.2261 0.0298  -0.0884 -0.0333 403  TYR A N   
1416 C CA  . TYR A 180 ? 0.2145 0.1124 0.1832 0.0119  -0.0829 -0.0114 403  TYR A CA  
1417 C C   . TYR A 180 ? 0.2085 0.1345 0.1749 0.0084  -0.0496 0.0137  403  TYR A C   
1418 O O   . TYR A 180 ? 0.2302 0.1693 0.2127 -0.0107 -0.0466 0.0294  403  TYR A O   
1419 C CB  . TYR A 180 ? 0.1972 0.1018 0.1912 0.0231  -0.0737 -0.0073 403  TYR A CB  
1420 C CG  . TYR A 180 ? 0.1769 0.1052 0.1680 0.0038  -0.0739 -0.0008 403  TYR A CG  
1421 C CD1 . TYR A 180 ? 0.1979 0.1101 0.1672 0.0074  -0.0573 -0.0010 403  TYR A CD1 
1422 C CD2 . TYR A 180 ? 0.1883 0.1194 0.1730 0.0183  -0.0400 0.0016  403  TYR A CD2 
1423 C CE1 . TYR A 180 ? 0.1966 0.1236 0.1704 0.0189  -0.0343 0.0052  403  TYR A CE1 
1424 C CE2 . TYR A 180 ? 0.1773 0.1288 0.1786 0.0074  -0.0402 0.0018  403  TYR A CE2 
1425 C CZ  . TYR A 180 ? 0.1897 0.1303 0.1771 0.0083  -0.0487 0.0015  403  TYR A CZ  
1426 O OH  . TYR A 180 ? 0.1936 0.1314 0.1677 0.0143  -0.0504 -0.0167 403  TYR A OH  
1427 N N   . LYS A 181 ? 0.2060 0.1257 0.1725 0.0192  -0.0624 0.0174  404  LYS A N   
1428 C CA  . LYS A 181 ? 0.2239 0.1228 0.1857 0.0069  -0.0624 0.0084  404  LYS A CA  
1429 C C   . LYS A 181 ? 0.1889 0.1251 0.1984 -0.0045 -0.0720 0.0038  404  LYS A C   
1430 O O   . LYS A 181 ? 0.1866 0.1231 0.2114 -0.0076 -0.0760 0.0098  404  LYS A O   
1431 C CB  . LYS A 181 ? 0.2958 0.1193 0.2208 0.0092  -0.1013 0.0182  404  LYS A CB  
1432 C CG  . LYS A 181 ? 0.3663 0.1600 0.2889 0.0029  -0.0754 0.0048  404  LYS A CG  
1433 C CD  . LYS A 181 ? 0.4617 0.2125 0.3449 -0.0199 -0.0660 -0.0142 404  LYS A CD  
1434 C CE  . LYS A 181 ? 0.5684 0.2736 0.3764 -0.0353 -0.0354 -0.0398 404  LYS A CE  
1435 N NZ  . LYS A 181 ? 0.6157 0.3139 0.3861 -0.0615 -0.0217 -0.0445 404  LYS A NZ  
1436 N N   . GLN A 182 ? 0.1849 0.1002 0.1746 0.0202  -0.0587 -0.0013 405  GLN A N   
1437 C CA  . GLN A 182 ? 0.1669 0.1156 0.1841 0.0093  -0.0525 -0.0092 405  GLN A CA  
1438 C C   . GLN A 182 ? 0.1925 0.1210 0.1647 -0.0061 -0.0634 0.0038  405  GLN A C   
1439 O O   . GLN A 182 ? 0.2046 0.1264 0.1896 -0.0269 -0.0694 0.0009  405  GLN A O   
1440 C CB  . GLN A 182 ? 0.1526 0.1369 0.1999 0.0058  -0.0239 -0.0100 405  GLN A CB  
1441 C CG  . GLN A 182 ? 0.1464 0.1523 0.2037 0.0046  -0.0269 -0.0088 405  GLN A CG  
1442 C CD  . GLN A 182 ? 0.1457 0.1519 0.1723 -0.0033 -0.0566 0.0089  405  GLN A CD  
1443 O OE1 . GLN A 182 ? 0.1793 0.1464 0.1953 -0.0105 -0.0488 -0.0163 405  GLN A OE1 
1444 N NE2 . GLN A 182 ? 0.1655 0.1840 0.1755 0.0080  -0.0424 0.0209  405  GLN A NE2 
1445 N N   . TRP A 183 ? 0.1957 0.1340 0.1488 0.0267  -0.0578 0.0314  406  TRP A N   
1446 C CA  . TRP A 183 ? 0.2006 0.1510 0.1810 0.0108  -0.0412 0.0362  406  TRP A CA  
1447 C C   . TRP A 183 ? 0.2131 0.1577 0.2079 0.0228  -0.0534 0.0265  406  TRP A C   
1448 O O   . TRP A 183 ? 0.2585 0.1845 0.1929 0.0345  -0.0664 0.0196  406  TRP A O   
1449 C CB  . TRP A 183 ? 0.1924 0.1654 0.1838 0.0094  -0.0393 0.0414  406  TRP A CB  
1450 C CG  . TRP A 183 ? 0.2118 0.1783 0.1874 -0.0017 -0.0609 0.0355  406  TRP A CG  
1451 C CD1 . TRP A 183 ? 0.2082 0.1946 0.2285 -0.0062 -0.0459 0.0426  406  TRP A CD1 
1452 C CD2 . TRP A 183 ? 0.2083 0.1765 0.1606 -0.0054 -0.0776 0.0418  406  TRP A CD2 
1453 N NE1 . TRP A 183 ? 0.2177 0.1942 0.2079 0.0032  -0.0528 0.0318  406  TRP A NE1 
1454 C CE2 . TRP A 183 ? 0.2083 0.1875 0.1674 0.0005  -0.0657 0.0365  406  TRP A CE2 
1455 C CE3 . TRP A 183 ? 0.2490 0.1913 0.1375 -0.0004 -0.0787 0.0401  406  TRP A CE3 
1456 C CZ2 . TRP A 183 ? 0.1937 0.1989 0.1712 -0.0034 -0.0499 0.0219  406  TRP A CZ2 
1457 C CZ3 . TRP A 183 ? 0.2551 0.1925 0.1548 0.0125  -0.0593 0.0434  406  TRP A CZ3 
1458 C CH2 . TRP A 183 ? 0.2496 0.2010 0.1600 -0.0037 -0.0510 0.0341  406  TRP A CH2 
1459 N N   . GLU A 184 ? 0.1995 0.1361 0.2149 0.0261  -0.0547 0.0134  407  GLU A N   
1460 C CA  . GLU A 184 ? 0.1828 0.1360 0.1962 0.0264  -0.0648 0.0170  407  GLU A CA  
1461 C C   . GLU A 184 ? 0.1906 0.1375 0.1898 0.0305  -0.0641 0.0279  407  GLU A C   
1462 O O   . GLU A 184 ? 0.1956 0.1509 0.1874 0.0225  -0.0620 0.0174  407  GLU A O   
1463 C CB  . GLU A 184 ? 0.2304 0.1481 0.2115 0.0062  -0.0535 0.0085  407  GLU A CB  
1464 C CG  . GLU A 184 ? 0.2614 0.1528 0.2494 -0.0179 -0.0441 0.0279  407  GLU A CG  
1465 C CD  . GLU A 184 ? 0.3110 0.1758 0.3007 -0.0338 -0.0139 0.0202  407  GLU A CD  
1466 O OE1 . GLU A 184 ? 0.3658 0.1907 0.3353 -0.0344 0.0337  0.0114  407  GLU A OE1 
1467 O OE2 . GLU A 184 ? 0.3733 0.1874 0.3482 -0.0381 0.0059  0.0105  407  GLU A OE2 
1468 N N   . LEU A 185 ? 0.1997 0.1396 0.2021 0.0316  -0.0950 0.0229  408  LEU A N   
1469 C CA  . LEU A 185 ? 0.2240 0.1476 0.2118 0.0199  -0.0973 -0.0047 408  LEU A CA  
1470 C C   . LEU A 185 ? 0.2527 0.1293 0.2232 0.0342  -0.0706 0.0005  408  LEU A C   
1471 O O   . LEU A 185 ? 0.2666 0.1349 0.2416 0.0211  -0.0508 0.0051  408  LEU A O   
1472 C CB  . LEU A 185 ? 0.2399 0.1432 0.1969 0.0330  -0.1062 -0.0023 408  LEU A CB  
1473 C CG  . LEU A 185 ? 0.2592 0.1453 0.1920 0.0609  -0.1078 -0.0129 408  LEU A CG  
1474 C CD1 . LEU A 185 ? 0.2678 0.1797 0.1953 0.0545  -0.1230 -0.0187 408  LEU A CD1 
1475 C CD2 . LEU A 185 ? 0.2506 0.1294 0.2131 0.0669  -0.0956 -0.0047 408  LEU A CD2 
1476 N N   . PRO A 186 ? 0.2187 0.1170 0.2110 0.0491  -0.0769 0.0041  409  PRO A N   
1477 C CA  . PRO A 186 ? 0.2274 0.1327 0.2239 0.0433  -0.0588 0.0060  409  PRO A CA  
1478 C C   . PRO A 186 ? 0.2104 0.1522 0.2397 0.0594  -0.0860 -0.0059 409  PRO A C   
1479 O O   . PRO A 186 ? 0.2229 0.1725 0.2443 0.0580  -0.0980 -0.0166 409  PRO A O   
1480 C CB  . PRO A 186 ? 0.2980 0.1534 0.2654 0.0466  0.0309  0.0163  409  PRO A CB  
1481 C CG  . PRO A 186 ? 0.2835 0.1443 0.2393 0.0118  0.0060  -0.0003 409  PRO A CG  
1482 C CD  . PRO A 186 ? 0.2232 0.1228 0.2175 0.0285  -0.0526 0.0052  409  PRO A CD  
1483 N N   . ASN A 187 ? 0.2135 0.1552 0.2753 0.0857  -0.0684 0.0050  410  ASN A N   
1484 C CA  . ASN A 187 ? 0.2322 0.1665 0.2932 0.0960  -0.0706 -0.0052 410  ASN A CA  
1485 C C   . ASN A 187 ? 0.2299 0.1650 0.2658 0.0860  -0.0843 0.0068  410  ASN A C   
1486 O O   . ASN A 187 ? 0.2423 0.1927 0.2769 0.0634  -0.0712 -0.0327 410  ASN A O   
1487 C CB  . ASN A 187 ? 0.2547 0.1727 0.3368 0.1015  -0.0612 -0.0032 410  ASN A CB  
1488 C CG  . ASN A 187 ? 0.3089 0.1946 0.3913 0.1015  -0.0459 0.0014  410  ASN A CG  
1489 O OD1 . ASN A 187 ? 0.3449 0.2156 0.4336 0.0767  -0.0002 0.0014  410  ASN A OD1 
1490 N ND2 . ASN A 187 ? 0.3642 0.2171 0.4092 0.0897  -0.0443 -0.0112 410  ASN A ND2 
1491 N N   . TYR A 188 ? 0.1966 0.1708 0.2601 0.0731  -0.0803 0.0077  411  TYR A N   
1492 C CA  . TYR A 188 ? 0.1961 0.1663 0.2615 0.0801  -0.0802 -0.0103 411  TYR A CA  
1493 C C   . TYR A 188 ? 0.1969 0.1910 0.2476 0.0680  -0.0918 -0.0261 411  TYR A C   
1494 O O   . TYR A 188 ? 0.2050 0.1953 0.2513 0.0648  -0.0560 -0.0051 411  TYR A O   
1495 C CB  . TYR A 188 ? 0.1937 0.1695 0.2483 0.0596  -0.0791 -0.0089 411  TYR A CB  
1496 C CG  . TYR A 188 ? 0.1894 0.1463 0.2377 0.0534  -0.0727 0.0043  411  TYR A CG  
1497 C CD1 . TYR A 188 ? 0.1900 0.1446 0.2211 0.0397  -0.0623 0.0130  411  TYR A CD1 
1498 C CD2 . TYR A 188 ? 0.2185 0.1422 0.2397 0.0601  -0.0570 0.0323  411  TYR A CD2 
1499 C CE1 . TYR A 188 ? 0.1821 0.1442 0.1871 0.0305  -0.0526 0.0112  411  TYR A CE1 
1500 C CE2 . TYR A 188 ? 0.1993 0.1421 0.2217 0.0505  -0.0755 0.0075  411  TYR A CE2 
1501 C CZ  . TYR A 188 ? 0.1794 0.1355 0.2019 0.0666  -0.0511 0.0145  411  TYR A CZ  
1502 O OH  . TYR A 188 ? 0.1855 0.1393 0.2123 0.0401  -0.0469 0.0156  411  TYR A OH  
1503 N N   . SER A 189 ? 0.2166 0.2060 0.2624 0.1081  -0.0733 -0.0047 412  SER A N   
1504 C CA  . SER A 189 ? 0.2387 0.2284 0.2711 0.1031  -0.1067 -0.0118 412  SER A CA  
1505 C C   . SER A 189 ? 0.2732 0.2427 0.2703 0.1120  -0.1129 -0.0028 412  SER A C   
1506 O O   . SER A 189 ? 0.2776 0.2554 0.3048 0.1301  -0.0760 -0.0142 412  SER A O   
1507 C CB  . SER A 189 ? 0.2650 0.2226 0.3008 0.1073  -0.1101 -0.0204 412  SER A CB  
1508 O OG  . SER A 189 ? 0.2922 0.2422 0.3381 0.0855  -0.0956 -0.0093 412  SER A OG  
1509 N N   . GLY A 190 ? 0.3152 0.2298 0.2783 0.1034  -0.1243 -0.0199 413  GLY A N   
1510 C CA  . GLY A 190 ? 0.3777 0.2238 0.2931 0.1268  -0.1269 -0.0289 413  GLY A CA  
1511 C C   . GLY A 190 ? 0.4234 0.2402 0.3085 0.1634  -0.1003 -0.0300 413  GLY A C   
1512 O O   . GLY A 190 ? 0.3873 0.2442 0.2877 0.1617  -0.1022 -0.0395 413  GLY A O   
1513 N N   . ALA A 191 ? 0.5120 0.2602 0.3212 0.1818  -0.1001 -0.0211 414  ALA A N   
1514 C CA  . ALA A 191 ? 0.6519 0.2858 0.3676 0.1712  -0.0882 -0.0313 414  ALA A CA  
1515 C C   . ALA A 191 ? 0.6818 0.3062 0.3852 0.1747  -0.1050 -0.0610 414  ALA A C   
1516 O O   . ALA A 191 ? 0.7139 0.3404 0.4047 0.1620  -0.0835 -0.0774 414  ALA A O   
1517 C CB  . ALA A 191 ? 0.7099 0.2941 0.3944 0.1496  -0.0696 -0.0202 414  ALA A CB  
1518 N N   . THR A 193 ? 0.6122 0.5408 0.6403 0.2613  -0.0712 0.1176  416  THR A N   
1519 C CA  . THR A 193 ? 0.6021 0.4877 0.6539 0.2592  -0.0670 0.1290  416  THR A CA  
1520 C C   . THR A 193 ? 0.5190 0.4291 0.5917 0.2238  -0.1306 0.1057  416  THR A C   
1521 O O   . THR A 193 ? 0.5107 0.4483 0.6005 0.2155  -0.1691 0.0790  416  THR A O   
1522 C CB  . THR A 193 ? 0.6494 0.4975 0.6928 0.2500  -0.0151 0.1613  416  THR A CB  
1523 O OG1 . THR A 193 ? 0.6789 0.4821 0.7024 0.2583  0.0061  0.1938  416  THR A OG1 
1524 C CG2 . THR A 193 ? 0.6748 0.5211 0.7241 0.2397  0.0226  0.1508  416  THR A CG2 
1525 N N   . LEU A 194 ? 0.4484 0.3588 0.5024 0.1765  -0.1402 0.0734  417  LEU A N   
1526 C CA  . LEU A 194 ? 0.3967 0.2835 0.4436 0.1207  -0.1516 0.0572  417  LEU A CA  
1527 C C   . LEU A 194 ? 0.3282 0.2530 0.3753 0.1107  -0.1304 0.0385  417  LEU A C   
1528 O O   . LEU A 194 ? 0.3146 0.2490 0.3837 0.1108  -0.1231 0.0199  417  LEU A O   
1529 C CB  . LEU A 194 ? 0.4296 0.2586 0.4712 0.0695  -0.1573 0.0590  417  LEU A CB  
1530 C CG  . LEU A 194 ? 0.4541 0.2616 0.5033 0.0313  -0.1603 0.0699  417  LEU A CG  
1531 C CD1 . LEU A 194 ? 0.4817 0.2605 0.5312 0.0089  -0.1303 0.0639  417  LEU A CD1 
1532 C CD2 . LEU A 194 ? 0.4823 0.2658 0.5530 0.0023  -0.1073 0.0581  417  LEU A CD2 
1533 N N   . ASN A 195 ? 0.2867 0.2177 0.3157 0.0947  -0.1197 0.0233  418  ASN A N   
1534 C CA  . ASN A 195 ? 0.2618 0.1998 0.2674 0.0665  -0.1256 0.0213  418  ASN A CA  
1535 C C   . ASN A 195 ? 0.2559 0.1991 0.2680 0.0460  -0.1139 0.0454  418  ASN A C   
1536 O O   . ASN A 195 ? 0.2848 0.1970 0.3101 0.0341  -0.0870 0.0534  418  ASN A O   
1537 C CB  . ASN A 195 ? 0.2399 0.2033 0.2366 0.0722  -0.1128 0.0139  418  ASN A CB  
1538 C CG  . ASN A 195 ? 0.2372 0.2028 0.2451 0.0812  -0.1091 0.0071  418  ASN A CG  
1539 O OD1 . ASN A 195 ? 0.2391 0.2092 0.2702 0.0987  -0.0851 -0.0066 418  ASN A OD1 
1540 N ND2 . ASN A 195 ? 0.2356 0.1901 0.2687 0.0777  -0.1056 0.0173  418  ASN A ND2 
1541 N N   A MET A 196 ? 0.2443 0.2068 0.2725 0.0337  -0.1171 0.0494  419  MET A N   
1542 N N   B MET A 196 ? 0.2288 0.2171 0.2703 0.0429  -0.0753 0.0374  419  MET A N   
1543 C CA  A MET A 196 ? 0.2311 0.2225 0.2791 0.0257  -0.1383 0.0376  419  MET A CA  
1544 C CA  B MET A 196 ? 0.2104 0.2409 0.2723 0.0457  -0.0536 0.0247  419  MET A CA  
1545 C C   A MET A 196 ? 0.1992 0.2102 0.2376 0.0173  -0.1210 0.0346  419  MET A C   
1546 C C   B MET A 196 ? 0.2009 0.2251 0.2466 0.0195  -0.0628 0.0168  419  MET A C   
1547 O O   A MET A 196 ? 0.2160 0.2085 0.2166 -0.0022 -0.1166 0.0572  419  MET A O   
1548 O O   B MET A 196 ? 0.2120 0.2317 0.2432 0.0072  -0.0179 0.0223  419  MET A O   
1549 C CB  A MET A 196 ? 0.2537 0.2419 0.3282 0.0134  -0.1631 0.0362  419  MET A CB  
1550 C CB  B MET A 196 ? 0.2199 0.2768 0.3087 0.0627  -0.0027 0.0260  419  MET A CB  
1551 C CG  A MET A 196 ? 0.2967 0.2615 0.3566 0.0095  -0.1822 0.0523  419  MET A CG  
1552 C CG  B MET A 196 ? 0.2387 0.3135 0.3279 0.0661  0.0236  0.0277  419  MET A CG  
1553 S SD  A MET A 196 ? 0.3677 0.2872 0.4364 0.0208  -0.1268 0.0754  419  MET A SD  
1554 S SD  B MET A 196 ? 0.2692 0.3547 0.3653 0.0731  0.0682  0.0305  419  MET A SD  
1555 C CE  A MET A 196 ? 0.3980 0.3015 0.4388 0.0077  -0.1122 0.0651  419  MET A CE  
1556 C CE  B MET A 196 ? 0.2430 0.3539 0.3768 0.0899  0.0886  0.0368  419  MET A CE  
1557 N N   . GLY A 197 ? 0.2017 0.2113 0.2367 -0.0105 -0.0728 0.0040  420  GLY A N   
1558 C CA  . GLY A 197 ? 0.1940 0.2064 0.2402 -0.0141 -0.0631 -0.0046 420  GLY A CA  
1559 C C   . GLY A 197 ? 0.1842 0.1858 0.2101 0.0082  -0.0727 0.0277  420  GLY A C   
1560 O O   . GLY A 197 ? 0.2379 0.1937 0.2437 0.0086  -0.0462 0.0432  420  GLY A O   
1561 N N   . LEU A 198 ? 0.1864 0.1644 0.2038 -0.0076 -0.0814 0.0360  421  LEU A N   
1562 C CA  . LEU A 198 ? 0.1977 0.1561 0.2085 0.0072  -0.0786 0.0176  421  LEU A CA  
1563 C C   . LEU A 198 ? 0.1960 0.1610 0.1802 -0.0098 -0.0925 0.0279  421  LEU A C   
1564 O O   . LEU A 198 ? 0.2372 0.1804 0.1951 -0.0074 -0.0942 0.0364  421  LEU A O   
1565 C CB  . LEU A 198 ? 0.2173 0.1484 0.2192 0.0251  -0.0711 0.0322  421  LEU A CB  
1566 C CG  . LEU A 198 ? 0.2526 0.1469 0.2321 0.0125  -0.0590 0.0394  421  LEU A CG  
1567 C CD1 . LEU A 198 ? 0.2859 0.1525 0.2658 -0.0027 -0.0347 0.0251  421  LEU A CD1 
1568 C CD2 . LEU A 198 ? 0.2732 0.1623 0.2077 0.0248  -0.0751 0.0246  421  LEU A CD2 
1569 N N   . ALA A 199 ? 0.1913 0.1366 0.1863 -0.0037 -0.0766 0.0380  422  ALA A N   
1570 C CA  . ALA A 199 ? 0.2151 0.1344 0.1815 0.0078  -0.0757 0.0351  422  ALA A CA  
1571 C C   . ALA A 199 ? 0.2345 0.1289 0.1850 0.0152  -0.0716 0.0428  422  ALA A C   
1572 O O   . ALA A 199 ? 0.2368 0.1221 0.1978 0.0094  -0.0797 0.0201  422  ALA A O   
1573 C CB  . ALA A 199 ? 0.2106 0.1491 0.1694 0.0233  -0.0719 0.0536  422  ALA A CB  
1574 N N   . PRO A 200 ? 0.2403 0.1305 0.1692 -0.0177 -0.0926 0.0532  423  PRO A N   
1575 C CA  A PRO A 200 ? 0.2471 0.1427 0.1786 -0.0090 -0.0802 0.0516  423  PRO A CA  
1576 C CA  B PRO A 200 ? 0.2491 0.1455 0.1722 -0.0205 -0.0876 0.0453  423  PRO A CA  
1577 C C   . PRO A 200 ? 0.2342 0.1494 0.1821 -0.0042 -0.0629 0.0475  423  PRO A C   
1578 O O   . PRO A 200 ? 0.2130 0.1554 0.1909 0.0230  -0.0769 0.0511  423  PRO A O   
1579 C CB  A PRO A 200 ? 0.2694 0.1432 0.1730 -0.0064 -0.0728 0.0535  423  PRO A CB  
1580 C CB  B PRO A 200 ? 0.2781 0.1423 0.1503 -0.0415 -0.0817 0.0350  423  PRO A CB  
1581 C CG  A PRO A 200 ? 0.2704 0.1472 0.1801 0.0073  -0.0812 0.0608  423  PRO A CG  
1582 C CG  B PRO A 200 ? 0.2902 0.1518 0.1637 -0.0327 -0.0669 0.0457  423  PRO A CG  
1583 C CD  A PRO A 200 ? 0.2573 0.1424 0.1700 -0.0021 -0.0852 0.0510  423  PRO A CD  
1584 C CD  B PRO A 200 ? 0.2840 0.1482 0.1663 -0.0170 -0.0590 0.0440  423  PRO A CD  
1585 N N   . SER A 201 ? 0.2134 0.1533 0.1831 -0.0268 -0.0770 0.0525  424  SER A N   
1586 C CA  . SER A 201 ? 0.2287 0.1501 0.1711 -0.0160 -0.0570 0.0497  424  SER A CA  
1587 C C   . SER A 201 ? 0.2363 0.1788 0.1748 0.0141  -0.0386 0.0252  424  SER A C   
1588 O O   . SER A 201 ? 0.2491 0.1853 0.1530 0.0241  -0.0570 0.0109  424  SER A O   
1589 C CB  . SER A 201 ? 0.2604 0.1423 0.1640 -0.0089 -0.0538 0.0737  424  SER A CB  
1590 O OG  . SER A 201 ? 0.2619 0.1392 0.1800 -0.0063 -0.0710 0.0500  424  SER A OG  
1591 N N   . VAL A 202 ? 0.2075 0.1850 0.1956 0.0119  -0.0456 0.0375  425  VAL A N   
1592 C CA  . VAL A 202 ? 0.2036 0.1965 0.1992 0.0044  -0.0749 0.0142  425  VAL A CA  
1593 C C   . VAL A 202 ? 0.2404 0.2296 0.2254 -0.0248 -0.0449 0.0456  425  VAL A C   
1594 O O   . VAL A 202 ? 0.2416 0.2427 0.2334 -0.0173 -0.0825 0.0385  425  VAL A O   
1595 C CB  . VAL A 202 ? 0.2546 0.2081 0.2367 0.0080  -0.0582 0.0155  425  VAL A CB  
1596 C CG1 . VAL A 202 ? 0.2524 0.2050 0.3106 -0.0082 -0.0324 -0.0198 425  VAL A CG1 
1597 C CG2 . VAL A 202 ? 0.2642 0.2010 0.1993 -0.0024 -0.0441 0.0290  425  VAL A CG2 
1598 N N   . PHE A 203 ? 0.2573 0.2600 0.2421 -0.0243 -0.0449 0.0661  426  PHE A N   
1599 C CA  . PHE A 203 ? 0.3137 0.3012 0.2734 -0.0341 -0.0415 0.0794  426  PHE A CA  
1600 C C   . PHE A 203 ? 0.3170 0.3536 0.2305 -0.0542 -0.0541 0.0887  426  PHE A C   
1601 O O   . PHE A 203 ? 0.3328 0.3712 0.2168 -0.0430 -0.0829 0.0950  426  PHE A O   
1602 C CB  . PHE A 203 ? 0.3464 0.2813 0.2864 -0.0190 -0.0372 0.0966  426  PHE A CB  
1603 C CG  . PHE A 203 ? 0.3601 0.2650 0.2863 -0.0050 -0.0941 0.1210  426  PHE A CG  
1604 C CD1 . PHE A 203 ? 0.3727 0.2696 0.2840 0.0050  -0.1079 0.1314  426  PHE A CD1 
1605 C CD2 . PHE A 203 ? 0.4143 0.2683 0.3418 0.0145  -0.0616 0.1229  426  PHE A CD2 
1606 C CE1 . PHE A 203 ? 0.4172 0.2827 0.3407 0.0206  -0.0813 0.1138  426  PHE A CE1 
1607 C CE2 . PHE A 203 ? 0.4291 0.2622 0.3420 0.0052  -0.0821 0.1219  426  PHE A CE2 
1608 C CZ  . PHE A 203 ? 0.4287 0.2661 0.3524 0.0212  -0.0676 0.1200  426  PHE A CZ  
1609 N N   . PRO A 204 ? 0.3203 0.3966 0.2414 -0.0722 -0.0359 0.0902  427  PRO A N   
1610 C CA  . PRO A 204 ? 0.3435 0.4233 0.2557 -0.0825 -0.0467 0.0965  427  PRO A CA  
1611 C C   . PRO A 204 ? 0.3947 0.4399 0.2704 -0.1059 -0.0436 0.0971  427  PRO A C   
1612 O O   . PRO A 204 ? 0.3777 0.4531 0.2741 -0.1116 -0.0180 0.0888  427  PRO A O   
1613 C CB  . PRO A 204 ? 0.3150 0.4292 0.2839 -0.0740 -0.0535 0.0871  427  PRO A CB  
1614 C CG  . PRO A 204 ? 0.2954 0.4289 0.2701 -0.0870 -0.0533 0.0820  427  PRO A CG  
1615 C CD  . PRO A 204 ? 0.2795 0.4132 0.2307 -0.0816 -0.0632 0.0831  427  PRO A CD  
1616 N N   . THR A 205 ? 0.4777 0.4491 0.2543 -0.0990 -0.0638 0.1081  428  THR A N   
1617 C CA  . THR A 205 ? 0.5558 0.4498 0.3022 -0.0917 -0.0717 0.0971  428  THR A CA  
1618 C C   . THR A 205 ? 0.6018 0.4483 0.3114 -0.0874 -0.0329 0.1194  428  THR A C   
1619 O O   . THR A 205 ? 0.6259 0.4348 0.3011 -0.0847 -0.0179 0.1491  428  THR A O   
1620 C CB  . THR A 205 ? 0.5741 0.4645 0.3361 -0.0863 -0.1244 0.0447  428  THR A CB  
1621 O OG1 . THR A 205 ? 0.5864 0.4617 0.3582 -0.0711 -0.1134 0.0186  428  THR A OG1 
1622 C CG2 . THR A 205 ? 0.5731 0.4751 0.3285 -0.0845 -0.1718 0.0198  428  THR A CG2 
1623 N N   . TYR A 206 ? 0.6167 0.4578 0.3223 -0.0735 -0.0118 0.1200  429  TYR A N   
1624 C CA  . TYR A 206 ? 0.6386 0.4680 0.3337 -0.0540 0.0279  0.1199  429  TYR A CA  
1625 C C   . TYR A 206 ? 0.6376 0.4650 0.3318 -0.0620 0.0360  0.1248  429  TYR A C   
1626 O O   . TYR A 206 ? 0.6192 0.4667 0.3252 -0.0591 0.0070  0.1150  429  TYR A O   
1627 C CB  . TYR A 206 ? 0.6648 0.4826 0.3563 -0.0299 0.0567  0.1121  429  TYR A CB  
1628 C CG  . TYR A 206 ? 0.6949 0.5013 0.3712 -0.0176 0.0962  0.0968  429  TYR A CG  
1629 C CD1 . TYR A 206 ? 0.7140 0.5161 0.3962 -0.0185 0.1002  0.0681  429  TYR A CD1 
1630 C CD2 . TYR A 206 ? 0.7281 0.5117 0.3849 -0.0079 0.1195  0.0915  429  TYR A CD2 
1631 C CE1 . TYR A 206 ? 0.7441 0.5245 0.4008 -0.0136 0.1186  0.0588  429  TYR A CE1 
1632 C CE2 . TYR A 206 ? 0.7475 0.5226 0.3998 -0.0037 0.1368  0.0729  429  TYR A CE2 
1633 C CZ  . TYR A 206 ? 0.7664 0.5290 0.4110 -0.0068 0.1468  0.0579  429  TYR A CZ  
1634 O OH  . TYR A 206 ? 0.8057 0.5398 0.4327 -0.0083 0.1704  0.0548  429  TYR A OH  
1635 N N   . PRO A 207 ? 0.6365 0.4659 0.3281 -0.0572 0.0320  0.1309  430  PRO A N   
1636 C CA  . PRO A 207 ? 0.6359 0.4588 0.3215 -0.0625 0.0412  0.1184  430  PRO A CA  
1637 C C   . PRO A 207 ? 0.6302 0.4352 0.2976 -0.0630 0.0603  0.1189  430  PRO A C   
1638 O O   . PRO A 207 ? 0.6534 0.4435 0.3211 -0.0652 0.0829  0.1088  430  PRO A O   
1639 C CB  . PRO A 207 ? 0.6390 0.4712 0.3202 -0.0622 0.0347  0.1245  430  PRO A CB  
1640 C CG  . PRO A 207 ? 0.6402 0.4756 0.3157 -0.0588 0.0185  0.1244  430  PRO A CG  
1641 C CD  . PRO A 207 ? 0.6404 0.4733 0.3282 -0.0532 0.0327  0.1244  430  PRO A CD  
1642 N N   . GLY A 208 ? 0.5777 0.4094 0.2714 -0.0786 0.0572  0.1135  431  GLY A N   
1643 C CA  . GLY A 208 ? 0.5231 0.3898 0.2682 -0.0982 0.0756  0.1165  431  GLY A CA  
1644 C C   . GLY A 208 ? 0.4790 0.3800 0.2585 -0.0875 0.0646  0.1211  431  GLY A C   
1645 O O   . GLY A 208 ? 0.4567 0.3875 0.3023 -0.0663 0.0460  0.1139  431  GLY A O   
1646 N N   . GLU A 209 ? 0.4547 0.3659 0.2395 -0.0768 0.0202  0.0961  432  GLU A N   
1647 C CA  . GLU A 209 ? 0.4301 0.3432 0.2181 -0.0738 0.0058  0.0784  432  GLU A CA  
1648 C C   . GLU A 209 ? 0.3770 0.3349 0.2289 -0.0831 -0.0252 0.0588  432  GLU A C   
1649 O O   . GLU A 209 ? 0.3924 0.3337 0.2333 -0.0942 -0.0051 0.0487  432  GLU A O   
1650 C CB  . GLU A 209 ? 0.4536 0.3404 0.2345 -0.0604 0.0356  0.0637  432  GLU A CB  
1651 C CG  . GLU A 209 ? 0.4651 0.3295 0.2144 -0.0443 0.0644  0.0458  432  GLU A CG  
1652 C CD  . GLU A 209 ? 0.4942 0.3315 0.1956 -0.0387 0.0839  0.0313  432  GLU A CD  
1653 O OE1 . GLU A 209 ? 0.4943 0.3257 0.1824 -0.0526 0.0911  0.0135  432  GLU A OE1 
1654 O OE2 . GLU A 209 ? 0.5066 0.3376 0.2123 -0.0226 0.0801  0.0203  432  GLU A OE2 
1655 N N   . GLN A 210 ? 0.3446 0.3309 0.1925 -0.0890 -0.0176 0.0572  433  GLN A N   
1656 C CA  . GLN A 210 ? 0.3152 0.3065 0.1661 -0.1000 -0.0395 0.0571  433  GLN A CA  
1657 C C   . GLN A 210 ? 0.2909 0.2842 0.1594 -0.0748 -0.0328 0.0580  433  GLN A C   
1658 O O   . GLN A 210 ? 0.2878 0.2961 0.1907 -0.0846 -0.0138 0.0378  433  GLN A O   
1659 C CB  . GLN A 210 ? 0.3314 0.3215 0.1881 -0.1285 -0.0245 0.0646  433  GLN A CB  
1660 C CG  . GLN A 210 ? 0.3399 0.3399 0.2271 -0.1448 -0.0234 0.0636  433  GLN A CG  
1661 C CD  . GLN A 210 ? 0.3453 0.3634 0.2742 -0.1551 -0.0031 0.0612  433  GLN A CD  
1662 O OE1 . GLN A 210 ? 0.3757 0.3832 0.3096 -0.1510 0.0039  0.0521  433  GLN A OE1 
1663 N NE2 . GLN A 210 ? 0.3108 0.3680 0.2793 -0.1555 -0.0058 0.0779  433  GLN A NE2 
1664 N N   . LEU A 211 ? 0.2641 0.2561 0.1728 -0.0499 -0.0213 0.0620  434  LEU A N   
1665 C CA  . LEU A 211 ? 0.2113 0.2549 0.1835 -0.0259 -0.0262 0.0497  434  LEU A CA  
1666 C C   . LEU A 211 ? 0.2273 0.2483 0.1946 -0.0236 -0.0274 0.0391  434  LEU A C   
1667 O O   . LEU A 211 ? 0.2289 0.2404 0.2124 -0.0342 -0.0395 0.0421  434  LEU A O   
1668 C CB  . LEU A 211 ? 0.1963 0.2764 0.2117 -0.0151 -0.0088 0.0177  434  LEU A CB  
1669 C CG  . LEU A 211 ? 0.2014 0.3025 0.2348 -0.0170 -0.0299 -0.0252 434  LEU A CG  
1670 C CD1 . LEU A 211 ? 0.2217 0.2921 0.2520 0.0239  0.0030  -0.0290 434  LEU A CD1 
1671 C CD2 . LEU A 211 ? 0.2358 0.3335 0.2618 -0.0319 -0.0216 -0.0759 434  LEU A CD2 
1672 N N   . LEU A 212 ? 0.2219 0.2372 0.1722 0.0110  -0.0160 0.0241  435  LEU A N   
1673 C CA  A LEU A 212 ? 0.2173 0.2423 0.1740 0.0107  -0.0340 0.0346  435  LEU A CA  
1674 C CA  B LEU A 212 ? 0.2162 0.2338 0.1730 0.0074  -0.0260 0.0241  435  LEU A CA  
1675 C C   . LEU A 212 ? 0.1989 0.2380 0.1691 -0.0006 -0.0366 0.0272  435  LEU A C   
1676 O O   . LEU A 212 ? 0.2132 0.2766 0.1938 -0.0241 -0.0391 0.0259  435  LEU A O   
1677 C CB  A LEU A 212 ? 0.2589 0.2605 0.1941 0.0536  -0.0352 0.0546  435  LEU A CB  
1678 C CB  B LEU A 212 ? 0.2406 0.2299 0.1870 0.0206  -0.0186 0.0176  435  LEU A CB  
1679 C CG  A LEU A 212 ? 0.2875 0.2884 0.1828 0.0698  -0.0391 0.0681  435  LEU A CG  
1680 C CG  B LEU A 212 ? 0.2551 0.2327 0.1957 0.0263  -0.0208 0.0116  435  LEU A CG  
1681 C CD1 A LEU A 212 ? 0.3081 0.3052 0.2156 0.0677  -0.0177 0.0507  435  LEU A CD1 
1682 C CD1 B LEU A 212 ? 0.2770 0.2396 0.2081 0.0340  -0.0236 -0.0044 435  LEU A CD1 
1683 C CD2 A LEU A 212 ? 0.3213 0.2969 0.1956 0.0666  -0.0382 0.0645  435  LEU A CD2 
1684 C CD2 B LEU A 212 ? 0.2500 0.2246 0.1983 0.0219  -0.0092 0.0167  435  LEU A CD2 
1685 N N   . PHE A 213 ? 0.1818 0.2093 0.1455 0.0124  -0.0239 0.0243  436  PHE A N   
1686 C CA  . PHE A 213 ? 0.1875 0.2078 0.1463 0.0360  -0.0386 0.0164  436  PHE A CA  
1687 C C   . PHE A 213 ? 0.1748 0.2048 0.1647 0.0323  -0.0351 0.0082  436  PHE A C   
1688 O O   . PHE A 213 ? 0.1725 0.2300 0.1980 0.0295  -0.0134 0.0206  436  PHE A O   
1689 C CB  . PHE A 213 ? 0.2319 0.2190 0.1431 0.0641  -0.0201 0.0123  436  PHE A CB  
1690 C CG  . PHE A 213 ? 0.2655 0.2213 0.1762 0.0339  -0.0269 0.0557  436  PHE A CG  
1691 C CD1 . PHE A 213 ? 0.2622 0.2211 0.1901 0.0377  -0.0397 0.0461  436  PHE A CD1 
1692 C CD2 . PHE A 213 ? 0.2936 0.2356 0.2223 0.0293  -0.0248 0.0702  436  PHE A CD2 
1693 C CE1 . PHE A 213 ? 0.2714 0.2282 0.1927 0.0262  -0.0276 0.0422  436  PHE A CE1 
1694 C CE2 . PHE A 213 ? 0.3078 0.2587 0.2313 0.0224  -0.0252 0.0728  436  PHE A CE2 
1695 C CZ  . PHE A 213 ? 0.2647 0.2467 0.2207 0.0326  -0.0012 0.0588  436  PHE A CZ  
1696 N N   . PHE A 214 ? 0.1720 0.1710 0.1301 0.0068  -0.0285 -0.0097 437  PHE A N   
1697 C CA  . PHE A 214 ? 0.1977 0.1801 0.1180 0.0064  -0.0345 0.0203  437  PHE A CA  
1698 C C   . PHE A 214 ? 0.1842 0.1939 0.1272 0.0083  -0.0431 0.0304  437  PHE A C   
1699 O O   . PHE A 214 ? 0.1763 0.1687 0.1660 0.0161  -0.0321 0.0076  437  PHE A O   
1700 C CB  . PHE A 214 ? 0.1974 0.1885 0.1292 -0.0005 -0.0124 0.0091  437  PHE A CB  
1701 C CG  . PHE A 214 ? 0.1791 0.1929 0.1346 0.0287  -0.0380 0.0036  437  PHE A CG  
1702 C CD1 . PHE A 214 ? 0.1868 0.1891 0.1320 -0.0059 -0.0399 -0.0175 437  PHE A CD1 
1703 C CD2 . PHE A 214 ? 0.2023 0.1958 0.1527 0.0438  -0.0172 -0.0168 437  PHE A CD2 
1704 C CE1 . PHE A 214 ? 0.1977 0.2001 0.1464 0.0254  -0.0238 -0.0056 437  PHE A CE1 
1705 C CE2 . PHE A 214 ? 0.2357 0.2043 0.1705 0.0405  -0.0149 -0.0010 437  PHE A CE2 
1706 C CZ  . PHE A 214 ? 0.2279 0.1978 0.1660 0.0356  -0.0072 -0.0055 437  PHE A CZ  
1707 N N   . ARG A 215 ? 0.1941 0.1831 0.1174 0.0057  -0.0717 0.0146  438  ARG A N   
1708 C CA  . ARG A 215 ? 0.1990 0.1896 0.1015 -0.0099 -0.0398 0.0060  438  ARG A CA  
1709 C C   . ARG A 215 ? 0.1932 0.1787 0.1311 0.0041  -0.0258 0.0083  438  ARG A C   
1710 O O   . ARG A 215 ? 0.1738 0.1860 0.1668 0.0202  -0.0418 -0.0004 438  ARG A O   
1711 C CB  . ARG A 215 ? 0.1722 0.1887 0.1604 -0.0151 -0.0323 -0.0075 438  ARG A CB  
1712 C CG  . ARG A 215 ? 0.1841 0.1713 0.1869 -0.0340 -0.0633 -0.0051 438  ARG A CG  
1713 C CD  . ARG A 215 ? 0.1828 0.1873 0.2131 -0.0198 -0.0510 0.0376  438  ARG A CD  
1714 N NE  . ARG A 215 ? 0.2226 0.1953 0.2355 -0.0246 -0.0235 0.0396  438  ARG A NE  
1715 C CZ  . ARG A 215 ? 0.2139 0.2228 0.2304 -0.0348 -0.0193 0.0266  438  ARG A CZ  
1716 N NH1 . ARG A 215 ? 0.2294 0.2544 0.2485 -0.0438 -0.0355 0.0268  438  ARG A NH1 
1717 N NH2 . ARG A 215 ? 0.2210 0.2159 0.2225 -0.0207 0.0029  0.0121  438  ARG A NH2 
1718 N N   . SER A 216 ? 0.1735 0.1673 0.1404 0.0025  -0.0259 0.0158  439  SER A N   
1719 C CA  . SER A 216 ? 0.1643 0.1633 0.1271 -0.0092 -0.0436 -0.0059 439  SER A CA  
1720 C C   . SER A 216 ? 0.1583 0.1574 0.1609 0.0017  -0.0578 -0.0094 439  SER A C   
1721 O O   . SER A 216 ? 0.1751 0.1636 0.1544 0.0213  -0.0633 -0.0198 439  SER A O   
1722 C CB  . SER A 216 ? 0.1572 0.1439 0.1447 -0.0112 -0.0672 -0.0242 439  SER A CB  
1723 O OG  . SER A 216 ? 0.1863 0.1257 0.1474 0.0099  -0.0589 -0.0129 439  SER A OG  
1724 N N   . TYR A 217 ? 0.1513 0.1768 0.1448 -0.0039 -0.0641 -0.0238 440  TYR A N   
1725 C CA  . TYR A 217 ? 0.1658 0.1782 0.1458 -0.0103 -0.0665 -0.0183 440  TYR A CA  
1726 C C   . TYR A 217 ? 0.2043 0.1783 0.1552 -0.0341 -0.0176 -0.0185 440  TYR A C   
1727 O O   . TYR A 217 ? 0.2992 0.1791 0.1929 -0.0551 0.0124  -0.0191 440  TYR A O   
1728 C CB  . TYR A 217 ? 0.1573 0.1972 0.1900 -0.0044 -0.0615 -0.0325 440  TYR A CB  
1729 C CG  . TYR A 217 ? 0.1773 0.2522 0.2602 -0.0115 -0.0286 -0.0814 440  TYR A CG  
1730 C CD1 . TYR A 217 ? 0.1987 0.2809 0.2858 -0.0387 -0.0551 -0.0713 440  TYR A CD1 
1731 C CD2 . TYR A 217 ? 0.2770 0.3016 0.3661 -0.0605 0.0785  -0.1128 440  TYR A CD2 
1732 C CE1 . TYR A 217 ? 0.2391 0.3286 0.3483 -0.0711 -0.0055 -0.1018 440  TYR A CE1 
1733 C CE2 . TYR A 217 ? 0.3184 0.3425 0.4103 -0.0839 0.1370  -0.1173 440  TYR A CE2 
1734 C CZ  . TYR A 217 ? 0.3284 0.3626 0.4229 -0.1058 0.1235  -0.1174 440  TYR A CZ  
1735 O OH  . TYR A 217 ? 0.4178 0.4008 0.4823 -0.1397 0.2048  -0.1121 440  TYR A OH  
1736 N N   A ILE A 218 ? 0.1790 0.1991 0.1257 -0.0249 -0.0402 -0.0476 441  ILE A N   
1737 N N   B ILE A 218 ? 0.1812 0.1621 0.1584 -0.0090 -0.0227 -0.0292 441  ILE A N   
1738 C CA  A ILE A 218 ? 0.1979 0.2279 0.1234 -0.0268 -0.0468 -0.0312 441  ILE A CA  
1739 C CA  B ILE A 218 ? 0.2082 0.1507 0.1905 0.0030  -0.0009 -0.0076 441  ILE A CA  
1740 C C   A ILE A 218 ? 0.1546 0.1693 0.1222 -0.0167 -0.0562 -0.0253 441  ILE A C   
1741 C C   B ILE A 218 ? 0.1757 0.1323 0.1683 -0.0105 -0.0181 -0.0147 441  ILE A C   
1742 O O   A ILE A 218 ? 0.1348 0.1625 0.1243 -0.0077 -0.0742 -0.0204 441  ILE A O   
1743 O O   B ILE A 218 ? 0.1966 0.1283 0.2083 -0.0096 -0.0011 -0.0083 441  ILE A O   
1744 C CB  A ILE A 218 ? 0.2015 0.2571 0.1473 -0.0249 -0.0935 -0.0334 441  ILE A CB  
1745 C CB  B ILE A 218 ? 0.1774 0.1490 0.2281 0.0332  -0.0289 -0.0082 441  ILE A CB  
1746 C CG1 A ILE A 218 ? 0.2531 0.3284 0.1681 -0.0585 -0.0505 -0.0902 441  ILE A CG1 
1747 C CG1 B ILE A 218 ? 0.1977 0.1174 0.2620 0.0274  -0.0432 0.0561  441  ILE A CG1 
1748 C CG2 A ILE A 218 ? 0.2366 0.3198 0.1797 -0.0684 -0.0924 -0.0357 441  ILE A CG2 
1749 C CG2 B ILE A 218 ? 0.1983 0.1575 0.2541 0.0835  -0.0382 -0.0246 441  ILE A CG2 
1750 C CD1 A ILE A 218 ? 0.2628 0.3237 0.2154 -0.0887 -0.0167 -0.1154 441  ILE A CD1 
1751 C CD1 B ILE A 218 ? 0.1899 0.1305 0.2648 0.0437  -0.0560 0.0576  441  ILE A CD1 
1752 N N   . PRO A 219 ? 0.1570 0.1172 0.1365 -0.0012 -0.0444 -0.0176 442  PRO A N   
1753 C CA  . PRO A 219 ? 0.1827 0.1007 0.1448 -0.0002 -0.0379 -0.0109 442  PRO A CA  
1754 C C   . PRO A 219 ? 0.1737 0.1189 0.1137 -0.0171 -0.0589 -0.0225 442  PRO A C   
1755 O O   . PRO A 219 ? 0.1894 0.1193 0.1446 -0.0182 -0.0576 -0.0094 442  PRO A O   
1756 C CB  . PRO A 219 ? 0.2583 0.1098 0.1697 -0.0036 -0.0096 0.0174  442  PRO A CB  
1757 C CG  . PRO A 219 ? 0.2355 0.1439 0.1792 -0.0070 -0.0453 0.0099  442  PRO A CG  
1758 C CD  . PRO A 219 ? 0.1806 0.1341 0.1465 -0.0315 -0.0502 0.0088  442  PRO A CD  
1759 N N   . MET A 220 ? 0.1724 0.1447 0.1197 -0.0091 -0.0272 -0.0244 443  MET A N   
1760 C CA  . MET A 220 ? 0.1819 0.1207 0.1360 -0.0223 -0.0155 -0.0188 443  MET A CA  
1761 C C   . MET A 220 ? 0.1507 0.1146 0.1237 -0.0045 -0.0432 -0.0184 443  MET A C   
1762 O O   . MET A 220 ? 0.1581 0.1102 0.1602 0.0103  -0.0521 -0.0193 443  MET A O   
1763 C CB  . MET A 220 ? 0.1816 0.1283 0.1408 -0.0421 -0.0163 0.0020  443  MET A CB  
1764 C CG  . MET A 220 ? 0.2277 0.1148 0.1372 -0.0097 -0.0068 0.0256  443  MET A CG  
1765 S SD  . MET A 220 ? 0.2063 0.1247 0.1645 -0.0093 -0.0431 -0.0035 443  MET A SD  
1766 C CE  . MET A 220 ? 0.2416 0.1287 0.1896 -0.0427 -0.0781 -0.0191 443  MET A CE  
1767 N N   . LYS A 221 ? 0.1544 0.1035 0.1140 0.0003  -0.0345 -0.0358 444  LYS A N   
1768 C CA  . LYS A 221 ? 0.1558 0.1254 0.1359 -0.0039 -0.0474 -0.0260 444  LYS A CA  
1769 C C   . LYS A 221 ? 0.1710 0.1100 0.1634 -0.0042 -0.0566 -0.0163 444  LYS A C   
1770 O O   . LYS A 221 ? 0.1864 0.1140 0.1696 0.0116  -0.0553 0.0033  444  LYS A O   
1771 C CB  . LYS A 221 ? 0.1582 0.1343 0.1359 -0.0078 -0.0273 -0.0061 444  LYS A CB  
1772 C CG  . LYS A 221 ? 0.1962 0.1397 0.1301 -0.0286 -0.0351 -0.0144 444  LYS A CG  
1773 C CD  . LYS A 221 ? 0.2136 0.1446 0.1400 -0.0172 -0.0162 -0.0017 444  LYS A CD  
1774 C CE  . LYS A 221 ? 0.2321 0.1698 0.1442 -0.0143 -0.0250 0.0084  444  LYS A CE  
1775 N NZ  . LYS A 221 ? 0.2588 0.1842 0.1581 0.0032  -0.0307 0.0118  444  LYS A NZ  
1776 N N   . GLY A 222 ? 0.1777 0.1030 0.1800 -0.0303 -0.0627 -0.0313 445  GLY A N   
1777 C CA  . GLY A 222 ? 0.1656 0.1194 0.1659 -0.0416 -0.0442 -0.0220 445  GLY A CA  
1778 C C   . GLY A 222 ? 0.1796 0.1258 0.1897 -0.0385 -0.0523 -0.0165 445  GLY A C   
1779 O O   . GLY A 222 ? 0.2004 0.1365 0.1747 -0.0296 -0.0530 -0.0243 445  GLY A O   
1780 N N   . GLY A 223 ? 0.1639 0.1147 0.2147 -0.0306 -0.0434 -0.0019 446  GLY A N   
1781 C CA  . GLY A 223 ? 0.1445 0.1094 0.1959 -0.0165 -0.0304 0.0085  446  GLY A CA  
1782 C C   . GLY A 223 ? 0.1546 0.0991 0.1823 -0.0106 -0.0572 0.0089  446  GLY A C   
1783 O O   . GLY A 223 ? 0.1917 0.1095 0.1557 0.0034  -0.0588 -0.0089 446  GLY A O   
1784 N N   . TYR A 224 ? 0.1833 0.1176 0.1994 -0.0176 -0.0231 0.0090  447  TYR A N   
1785 C CA  . TYR A 224 ? 0.1721 0.1102 0.1882 -0.0285 -0.0557 -0.0106 447  TYR A CA  
1786 C C   . TYR A 224 ? 0.2184 0.1139 0.1798 -0.0298 -0.0720 0.0041  447  TYR A C   
1787 O O   . TYR A 224 ? 0.2602 0.1288 0.2094 -0.0352 -0.0813 0.0055  447  TYR A O   
1788 C CB  . TYR A 224 ? 0.1854 0.1161 0.1711 -0.0315 -0.0525 -0.0263 447  TYR A CB  
1789 C CG  . TYR A 224 ? 0.1712 0.0960 0.1434 -0.0190 -0.0651 -0.0077 447  TYR A CG  
1790 C CD1 . TYR A 224 ? 0.2072 0.0904 0.1537 -0.0016 -0.0627 -0.0143 447  TYR A CD1 
1791 C CD2 . TYR A 224 ? 0.1802 0.1223 0.1487 -0.0002 -0.0496 -0.0095 447  TYR A CD2 
1792 C CE1 . TYR A 224 ? 0.1891 0.1106 0.1703 0.0011  -0.0638 0.0185  447  TYR A CE1 
1793 C CE2 . TYR A 224 ? 0.1927 0.1077 0.1725 0.0234  -0.0334 -0.0176 447  TYR A CE2 
1794 C CZ  . TYR A 224 ? 0.1731 0.1048 0.1737 0.0103  -0.0890 0.0067  447  TYR A CZ  
1795 O OH  . TYR A 224 ? 0.2029 0.1208 0.1590 0.0074  -0.0861 0.0042  447  TYR A OH  
1796 N N   . GLY A 225 ? 0.2386 0.1350 0.1319 -0.0445 -0.0278 -0.0110 448  GLY A N   
1797 C CA  . GLY A 225 ? 0.2736 0.1354 0.1403 -0.0566 -0.0206 -0.0144 448  GLY A CA  
1798 C C   . GLY A 225 ? 0.2342 0.1502 0.1444 -0.0345 -0.0623 -0.0106 448  GLY A C   
1799 O O   . GLY A 225 ? 0.2372 0.1476 0.1582 -0.0417 -0.0705 -0.0038 448  GLY A O   
1800 N N   . SER A 226 ? 0.2326 0.1645 0.1425 -0.0201 -0.0577 -0.0390 449  SER A N   
1801 C CA  . SER A 226 ? 0.1894 0.1754 0.1563 0.0116  -0.0625 -0.0209 449  SER A CA  
1802 C C   . SER A 226 ? 0.1851 0.1642 0.1676 -0.0112 -0.0556 -0.0154 449  SER A C   
1803 O O   . SER A 226 ? 0.2120 0.1638 0.1756 -0.0168 -0.0333 -0.0055 449  SER A O   
1804 C CB  . SER A 226 ? 0.1948 0.2196 0.1589 0.0170  -0.0772 -0.0264 449  SER A CB  
1805 O OG  . SER A 226 ? 0.2280 0.2577 0.1680 0.0053  -0.0932 -0.0309 449  SER A OG  
1806 N N   . PRO A 227 ? 0.1846 0.1407 0.1442 -0.0095 -0.0481 -0.0098 450  PRO A N   
1807 C CA  . PRO A 227 ? 0.1862 0.1512 0.1532 -0.0079 -0.0667 -0.0128 450  PRO A CA  
1808 C C   . PRO A 227 ? 0.1960 0.1433 0.1587 -0.0093 -0.0394 -0.0024 450  PRO A C   
1809 O O   . PRO A 227 ? 0.2076 0.1429 0.1597 -0.0124 -0.0515 0.0020  450  PRO A O   
1810 C CB  . PRO A 227 ? 0.2068 0.1498 0.1619 0.0164  -0.0469 -0.0003 450  PRO A CB  
1811 C CG  . PRO A 227 ? 0.2147 0.1375 0.1653 0.0040  -0.0647 -0.0086 450  PRO A CG  
1812 C CD  . PRO A 227 ? 0.1861 0.1471 0.1538 0.0005  -0.0655 -0.0102 450  PRO A CD  
1813 N N   . TYR A 228 ? 0.1564 0.1406 0.1528 -0.0218 -0.0374 -0.0155 451  TYR A N   
1814 C CA  . TYR A 228 ? 0.1877 0.1578 0.1323 -0.0096 -0.0446 -0.0314 451  TYR A CA  
1815 C C   . TYR A 228 ? 0.1919 0.1398 0.1287 -0.0010 -0.0480 -0.0166 451  TYR A C   
1816 O O   . TYR A 228 ? 0.2038 0.1230 0.1550 -0.0172 -0.0431 -0.0168 451  TYR A O   
1817 C CB  . TYR A 228 ? 0.2029 0.1790 0.1584 0.0074  -0.0237 0.0016  451  TYR A CB  
1818 C CG  . TYR A 228 ? 0.1863 0.2037 0.1654 0.0045  -0.0392 0.0099  451  TYR A CG  
1819 C CD1 . TYR A 228 ? 0.2093 0.2232 0.1596 0.0449  -0.0499 0.0104  451  TYR A CD1 
1820 C CD2 . TYR A 228 ? 0.2101 0.2124 0.2023 -0.0166 -0.0308 0.0264  451  TYR A CD2 
1821 C CE1 . TYR A 228 ? 0.2554 0.2426 0.2178 0.0098  -0.0213 0.0255  451  TYR A CE1 
1822 C CE2 . TYR A 228 ? 0.2500 0.2408 0.2250 -0.0392 -0.0251 0.0163  451  TYR A CE2 
1823 C CZ  . TYR A 228 ? 0.3055 0.2363 0.2247 -0.0391 -0.0036 0.0225  451  TYR A CZ  
1824 O OH  . TYR A 228 ? 0.3619 0.2632 0.2423 -0.0631 0.0298  0.0404  451  TYR A OH  
1825 N N   . ILE A 229 ? 0.1700 0.1599 0.1472 -0.0208 -0.0487 -0.0226 452  ILE A N   
1826 C CA  . ILE A 229 ? 0.1528 0.1497 0.1483 -0.0004 -0.0693 -0.0126 452  ILE A CA  
1827 C C   . ILE A 229 ? 0.1658 0.1280 0.1498 0.0213  -0.0852 -0.0128 452  ILE A C   
1828 O O   . ILE A 229 ? 0.1752 0.1378 0.1466 0.0136  -0.0515 -0.0048 452  ILE A O   
1829 C CB  . ILE A 229 ? 0.1293 0.1300 0.1680 -0.0154 -0.0595 0.0094  452  ILE A CB  
1830 C CG1 . ILE A 229 ? 0.1055 0.1242 0.1803 -0.0059 -0.0505 0.0111  452  ILE A CG1 
1831 C CG2 . ILE A 229 ? 0.1829 0.1398 0.1892 0.0028  -0.0238 0.0283  452  ILE A CG2 
1832 C CD1 . ILE A 229 ? 0.1595 0.1247 0.2033 0.0009  -0.0131 -0.0003 452  ILE A CD1 
1833 N N   . ASP A 230 ? 0.1667 0.1441 0.1270 0.0007  -0.0624 -0.0131 453  ASP A N   
1834 C CA  . ASP A 230 ? 0.1755 0.1401 0.1357 -0.0025 -0.0308 -0.0076 453  ASP A CA  
1835 C C   . ASP A 230 ? 0.1802 0.1438 0.1475 0.0093  -0.0630 -0.0117 453  ASP A C   
1836 O O   . ASP A 230 ? 0.1828 0.1544 0.1821 0.0204  -0.0578 -0.0163 453  ASP A O   
1837 C CB  . ASP A 230 ? 0.1581 0.1558 0.1475 -0.0012 -0.0523 0.0242  453  ASP A CB  
1838 C CG  . ASP A 230 ? 0.1883 0.1779 0.1859 0.0008  -0.0553 -0.0262 453  ASP A CG  
1839 O OD1 . ASP A 230 ? 0.1946 0.1840 0.2059 -0.0004 -0.0380 -0.0081 453  ASP A OD1 
1840 O OD2 . ASP A 230 ? 0.2030 0.1942 0.1890 -0.0063 -0.0240 -0.0218 453  ASP A OD2 
1841 N N   . CYS A 231 ? 0.1868 0.1445 0.1174 0.0013  -0.0469 -0.0148 454  CYS A N   
1842 C CA  . CYS A 231 ? 0.1682 0.1463 0.1344 -0.0220 -0.0279 -0.0152 454  CYS A CA  
1843 C C   . CYS A 231 ? 0.1299 0.1599 0.1567 0.0146  -0.0433 0.0028  454  CYS A C   
1844 O O   . CYS A 231 ? 0.1620 0.1653 0.1645 0.0049  -0.0417 0.0196  454  CYS A O   
1845 C CB  . CYS A 231 ? 0.1709 0.1302 0.1733 0.0284  -0.0099 -0.0076 454  CYS A CB  
1846 S SG  . CYS A 231 ? 0.1772 0.1523 0.1494 0.0247  -0.0323 0.0185  454  CYS A SG  
1847 N N   . LEU A 232 ? 0.1736 0.1509 0.1394 0.0088  -0.0288 0.0118  455  LEU A N   
1848 C CA  . LEU A 232 ? 0.1914 0.1680 0.1464 0.0234  -0.0370 -0.0025 455  LEU A CA  
1849 C C   . LEU A 232 ? 0.1873 0.1607 0.1546 0.0201  -0.0186 -0.0013 455  LEU A C   
1850 O O   . LEU A 232 ? 0.1970 0.1799 0.1452 0.0324  -0.0298 -0.0047 455  LEU A O   
1851 C CB  . LEU A 232 ? 0.1814 0.1765 0.1497 0.0419  -0.0313 0.0078  455  LEU A CB  
1852 C CG  . LEU A 232 ? 0.1944 0.1743 0.1622 0.0217  -0.0277 0.0034  455  LEU A CG  
1853 C CD1 . LEU A 232 ? 0.1587 0.1874 0.1641 0.0525  -0.0706 0.0066  455  LEU A CD1 
1854 C CD2 . LEU A 232 ? 0.2256 0.1844 0.1656 0.0412  -0.0384 0.0002  455  LEU A CD2 
1855 N N   . ILE A 233 ? 0.1996 0.1461 0.1392 0.0251  -0.0504 0.0070  456  ILE A N   
1856 C CA  . ILE A 233 ? 0.2235 0.1459 0.1139 0.0202  -0.0350 -0.0062 456  ILE A CA  
1857 C C   . ILE A 233 ? 0.1812 0.1495 0.1370 0.0318  -0.0452 0.0123  456  ILE A C   
1858 O O   . ILE A 233 ? 0.1956 0.1472 0.1560 0.0167  -0.0513 0.0109  456  ILE A O   
1859 C CB  . ILE A 233 ? 0.2498 0.1744 0.1102 0.0183  -0.0238 -0.0025 456  ILE A CB  
1860 C CG1 . ILE A 233 ? 0.2227 0.1905 0.1315 0.0039  -0.0649 -0.0074 456  ILE A CG1 
1861 C CG2 . ILE A 233 ? 0.2790 0.1684 0.1106 0.0229  -0.0128 0.0218  456  ILE A CG2 
1862 C CD1 . ILE A 233 ? 0.2476 0.2078 0.1388 -0.0095 -0.0413 0.0206  456  ILE A CD1 
1863 N N   . PRO A 234 ? 0.1957 0.1508 0.1553 0.0541  -0.0568 0.0303  457  PRO A N   
1864 C CA  . PRO A 234 ? 0.1991 0.1484 0.1675 0.0376  -0.0414 0.0253  457  PRO A CA  
1865 C C   . PRO A 234 ? 0.1927 0.1319 0.1541 0.0422  -0.0339 0.0228  457  PRO A C   
1866 O O   . PRO A 234 ? 0.2158 0.1341 0.1437 0.0166  -0.0407 0.0068  457  PRO A O   
1867 C CB  . PRO A 234 ? 0.2167 0.1794 0.2036 0.0643  -0.0417 0.0587  457  PRO A CB  
1868 C CG  . PRO A 234 ? 0.2324 0.1927 0.2240 0.0794  -0.0374 0.0429  457  PRO A CG  
1869 C CD  . PRO A 234 ? 0.1971 0.1808 0.2120 0.0920  -0.0377 0.0320  457  PRO A CD  
1870 N N   . GLN A 235 ? 0.1766 0.1272 0.1471 0.0370  -0.0270 0.0237  458  GLN A N   
1871 C CA  . GLN A 235 ? 0.1900 0.1313 0.1518 0.0085  -0.0241 -0.0021 458  GLN A CA  
1872 C C   . GLN A 235 ? 0.2142 0.1316 0.1498 0.0326  -0.0525 0.0110  458  GLN A C   
1873 O O   . GLN A 235 ? 0.2287 0.1344 0.1517 0.0347  -0.0622 0.0008  458  GLN A O   
1874 C CB  . GLN A 235 ? 0.1522 0.1503 0.1620 0.0366  -0.0222 0.0288  458  GLN A CB  
1875 C CG  . GLN A 235 ? 0.1465 0.1401 0.1656 0.0426  -0.0401 0.0325  458  GLN A CG  
1876 C CD  . GLN A 235 ? 0.1976 0.1527 0.1759 0.0245  -0.0622 0.0189  458  GLN A CD  
1877 O OE1 . GLN A 235 ? 0.1967 0.1267 0.1723 0.0248  -0.0568 0.0141  458  GLN A OE1 
1878 N NE2 . GLN A 235 ? 0.1880 0.1817 0.2698 0.0218  -0.0641 -0.0106 458  GLN A NE2 
1879 N N   . GLU A 236 ? 0.2174 0.1273 0.1540 0.0375  -0.0475 -0.0015 459  GLU A N   
1880 C CA  . GLU A 236 ? 0.2561 0.1461 0.1326 0.0591  -0.0745 0.0107  459  GLU A CA  
1881 C C   . GLU A 236 ? 0.2554 0.1487 0.1306 0.0463  -0.0741 0.0212  459  GLU A C   
1882 O O   . GLU A 236 ? 0.2967 0.1471 0.1937 0.0478  -0.0617 -0.0112 459  GLU A O   
1883 C CB  . GLU A 236 ? 0.2745 0.1501 0.1526 0.0738  -0.0727 0.0127  459  GLU A CB  
1884 C CG  . GLU A 236 ? 0.2755 0.1440 0.1619 0.0776  -0.0756 0.0060  459  GLU A CG  
1885 C CD  . GLU A 236 ? 0.2773 0.1570 0.1677 0.0710  -0.0842 0.0145  459  GLU A CD  
1886 O OE1 . GLU A 236 ? 0.2535 0.1437 0.1756 0.0768  -0.0572 0.0008  459  GLU A OE1 
1887 O OE2 . GLU A 236 ? 0.3300 0.1701 0.1793 0.0408  -0.0739 0.0319  459  GLU A OE2 
1888 N N   . TRP A 237 ? 0.2355 0.1571 0.1588 0.0461  -0.0473 0.0224  460  TRP A N   
1889 C CA  . TRP A 237 ? 0.2343 0.1739 0.1434 0.0507  -0.0450 0.0250  460  TRP A CA  
1890 C C   . TRP A 237 ? 0.2413 0.1605 0.1366 0.0498  -0.0457 0.0063  460  TRP A C   
1891 O O   . TRP A 237 ? 0.2556 0.1700 0.1440 0.0456  -0.0714 0.0046  460  TRP A O   
1892 C CB  . TRP A 237 ? 0.2172 0.1828 0.1584 0.0510  -0.0488 0.0098  460  TRP A CB  
1893 C CG  . TRP A 237 ? 0.2117 0.1805 0.1759 0.0788  -0.0364 0.0120  460  TRP A CG  
1894 C CD1 . TRP A 237 ? 0.2143 0.1897 0.1626 0.0727  -0.0567 -0.0107 460  TRP A CD1 
1895 C CD2 . TRP A 237 ? 0.2326 0.1882 0.1530 0.0637  -0.0205 0.0062  460  TRP A CD2 
1896 N NE1 . TRP A 237 ? 0.2474 0.1909 0.1570 0.0728  -0.0315 0.0035  460  TRP A NE1 
1897 C CE2 . TRP A 237 ? 0.2411 0.1959 0.1538 0.0604  -0.0272 0.0157  460  TRP A CE2 
1898 C CE3 . TRP A 237 ? 0.2235 0.1868 0.1502 0.0632  -0.0378 -0.0033 460  TRP A CE3 
1899 C CZ2 . TRP A 237 ? 0.2461 0.2054 0.1590 0.0599  -0.0553 0.0271  460  TRP A CZ2 
1900 C CZ3 . TRP A 237 ? 0.2205 0.1943 0.1568 0.0659  -0.0346 0.0123  460  TRP A CZ3 
1901 C CH2 . TRP A 237 ? 0.2278 0.2066 0.1817 0.0634  -0.0519 0.0278  460  TRP A CH2 
1902 N N   . ILE A 238 ? 0.2205 0.1368 0.1637 0.0583  -0.0405 0.0080  461  ILE A N   
1903 C CA  . ILE A 238 ? 0.2409 0.1338 0.1630 0.0415  -0.0227 -0.0094 461  ILE A CA  
1904 C C   . ILE A 238 ? 0.2875 0.1472 0.1539 0.0167  -0.0652 -0.0060 461  ILE A C   
1905 O O   . ILE A 238 ? 0.2791 0.1700 0.1491 0.0103  -0.0689 0.0166  461  ILE A O   
1906 C CB  . ILE A 238 ? 0.2111 0.1497 0.1520 0.0283  -0.0384 0.0100  461  ILE A CB  
1907 C CG1 . ILE A 238 ? 0.2097 0.1433 0.1456 0.0235  -0.0229 0.0024  461  ILE A CG1 
1908 C CG2 . ILE A 238 ? 0.1788 0.1699 0.1716 0.0141  -0.0550 0.0019  461  ILE A CG2 
1909 C CD1 . ILE A 238 ? 0.2343 0.1550 0.1614 0.0171  -0.0211 -0.0139 461  ILE A CD1 
1910 N N   A SER A 239 ? 0.3170 0.1411 0.1555 0.0055  -0.0800 -0.0009 462  SER A N   
1911 N N   B SER A 239 ? 0.3165 0.1198 0.1731 0.0047  -0.0682 0.0124  462  SER A N   
1912 C CA  A SER A 239 ? 0.3431 0.1431 0.1570 -0.0075 -0.0916 -0.0010 462  SER A CA  
1913 C CA  B SER A 239 ? 0.3645 0.1105 0.1719 -0.0378 -0.0811 0.0195  462  SER A CA  
1914 C C   A SER A 239 ? 0.3594 0.1480 0.1739 0.0033  -0.0966 -0.0029 462  SER A C   
1915 C C   B SER A 239 ? 0.3817 0.1367 0.1958 -0.0213 -0.0810 -0.0148 462  SER A C   
1916 O O   A SER A 239 ? 0.3621 0.1536 0.1779 0.0004  -0.0994 -0.0026 462  SER A O   
1917 O O   B SER A 239 ? 0.3942 0.1599 0.2007 -0.0304 -0.1032 -0.0193 462  SER A O   
1918 C CB  A SER A 239 ? 0.3557 0.1426 0.1634 -0.0169 -0.0909 0.0028  462  SER A CB  
1919 C CB  B SER A 239 ? 0.4006 0.1246 0.2255 -0.0253 -0.0695 0.0449  462  SER A CB  
1920 O OG  A SER A 239 ? 0.3688 0.1479 0.1729 -0.0218 -0.0767 -0.0047 462  SER A OG  
1921 O OG  B SER A 239 ? 0.4586 0.1402 0.2799 -0.0385 -0.0682 0.0294  462  SER A OG  
1922 N N   . HIS A 240 ? 0.3633 0.1533 0.1815 0.0273  -0.1068 0.0077  463  HIS A N   
1923 C CA  . HIS A 240 ? 0.3836 0.1608 0.2118 0.0370  -0.1176 0.0004  463  HIS A CA  
1924 C C   . HIS A 240 ? 0.3693 0.1594 0.2157 0.0158  -0.1327 -0.0181 463  HIS A C   
1925 O O   . HIS A 240 ? 0.3770 0.1545 0.2344 0.0116  -0.1066 -0.0319 463  HIS A O   
1926 C CB  . HIS A 240 ? 0.4022 0.1750 0.2175 0.0750  -0.1416 -0.0160 463  HIS A CB  
1927 C CG  . HIS A 240 ? 0.4539 0.2022 0.2699 0.0833  -0.1052 -0.0528 463  HIS A CG  
1928 N ND1 . HIS A 240 ? 0.5076 0.2257 0.3170 0.0593  -0.0461 -0.0943 463  HIS A ND1 
1929 C CD2 . HIS A 240 ? 0.4807 0.2274 0.2831 0.0833  -0.1164 -0.0491 463  HIS A CD2 
1930 C CE1 . HIS A 240 ? 0.5079 0.2341 0.3076 0.0529  -0.0538 -0.1055 463  HIS A CE1 
1931 N NE2 . HIS A 240 ? 0.5183 0.2475 0.2975 0.0676  -0.0808 -0.0745 463  HIS A NE2 
1932 N N   . PHE A 241 ? 0.3562 0.1706 0.1943 0.0381  -0.1362 0.0003  464  PHE A N   
1933 C CA  . PHE A 241 ? 0.3402 0.1726 0.1727 0.0307  -0.1168 -0.0023 464  PHE A CA  
1934 C C   . PHE A 241 ? 0.3245 0.1777 0.1734 0.0036  -0.1086 -0.0189 464  PHE A C   
1935 O O   . PHE A 241 ? 0.3314 0.1864 0.1767 0.0116  -0.1009 -0.0146 464  PHE A O   
1936 C CB  . PHE A 241 ? 0.3268 0.1500 0.1983 0.0339  -0.0727 -0.0170 464  PHE A CB  
1937 C CG  . PHE A 241 ? 0.3175 0.1694 0.1857 0.0564  -0.0887 -0.0016 464  PHE A CG  
1938 C CD1 . PHE A 241 ? 0.3404 0.1828 0.1966 0.0533  -0.0672 -0.0131 464  PHE A CD1 
1939 C CD2 . PHE A 241 ? 0.2996 0.1621 0.1798 0.0348  -0.0998 -0.0011 464  PHE A CD2 
1940 C CE1 . PHE A 241 ? 0.3571 0.1851 0.2027 0.0667  -0.0657 0.0014  464  PHE A CE1 
1941 C CE2 . PHE A 241 ? 0.3103 0.1742 0.1658 0.0577  -0.0914 0.0121  464  PHE A CE2 
1942 C CZ  . PHE A 241 ? 0.3290 0.1839 0.1720 0.0480  -0.0836 -0.0014 464  PHE A CZ  
1943 N N   . TYR A 242 ? 0.3097 0.1689 0.1981 0.0162  -0.1001 0.0070  465  TYR A N   
1944 C CA  . TYR A 242 ? 0.3318 0.1839 0.1932 -0.0019 -0.1009 -0.0004 465  TYR A CA  
1945 C C   . TYR A 242 ? 0.3741 0.1971 0.2104 -0.0283 -0.1322 0.0100  465  TYR A C   
1946 O O   . TYR A 242 ? 0.3721 0.2267 0.2244 -0.0786 -0.1153 0.0077  465  TYR A O   
1947 C CB  . TYR A 242 ? 0.3250 0.1910 0.1768 -0.0087 -0.1031 0.0169  465  TYR A CB  
1948 C CG  . TYR A 242 ? 0.3317 0.2153 0.1884 -0.0283 -0.0876 0.0220  465  TYR A CG  
1949 C CD1 . TYR A 242 ? 0.3269 0.2468 0.2228 -0.0188 -0.0895 0.0259  465  TYR A CD1 
1950 C CD2 . TYR A 242 ? 0.3311 0.2399 0.2133 -0.0365 -0.0764 0.0520  465  TYR A CD2 
1951 C CE1 . TYR A 242 ? 0.3289 0.2695 0.2484 -0.0478 -0.0759 0.0382  465  TYR A CE1 
1952 C CE2 . TYR A 242 ? 0.3317 0.2631 0.2285 -0.0442 -0.0624 0.0495  465  TYR A CE2 
1953 C CZ  . TYR A 242 ? 0.3240 0.2982 0.2510 -0.0492 -0.0784 0.0596  465  TYR A CZ  
1954 O OH  . TYR A 242 ? 0.3260 0.3413 0.3158 -0.0210 -0.0719 0.0833  465  TYR A OH  
1955 N N   . GLN A 243 ? 0.4123 0.1656 0.2377 -0.0096 -0.1314 0.0254  466  GLN A N   
1956 C CA  . GLN A 243 ? 0.4840 0.1587 0.2657 -0.0062 -0.1307 0.0216  466  GLN A CA  
1957 C C   . GLN A 243 ? 0.5041 0.1664 0.2693 -0.0168 -0.1134 0.0176  466  GLN A C   
1958 O O   . GLN A 243 ? 0.4962 0.1857 0.3024 -0.0714 -0.1014 0.0150  466  GLN A O   
1959 C CB  . GLN A 243 ? 0.5568 0.1636 0.2890 0.0025  -0.1136 0.0313  466  GLN A CB  
1960 C CG  . GLN A 243 ? 0.6094 0.1869 0.3043 0.0335  -0.0878 0.0513  466  GLN A CG  
1961 C CD  . GLN A 243 ? 0.6646 0.1887 0.3482 0.0350  -0.0266 0.0567  466  GLN A CD  
1962 O OE1 . GLN A 243 ? 0.7423 0.1985 0.3765 0.0231  0.0039  0.0474  466  GLN A OE1 
1963 N NE2 . GLN A 243 ? 0.6820 0.1865 0.3744 0.0255  -0.0080 0.0537  466  GLN A NE2 
1964 N N   . GLU A 244 ? 0.5022 0.1721 0.2359 -0.0185 -0.1120 -0.0097 467  GLU A N   
1965 C CA  . GLU A 244 ? 0.5431 0.2110 0.2684 -0.0354 -0.1000 -0.0286 467  GLU A CA  
1966 C C   . GLU A 244 ? 0.5476 0.2202 0.2643 -0.0570 -0.1541 -0.0306 467  GLU A C   
1967 O O   . GLU A 244 ? 0.5722 0.2241 0.2604 -0.0683 -0.1329 -0.0365 467  GLU A O   
1968 C CB  . GLU A 244 ? 0.5730 0.2400 0.3286 -0.0291 -0.0564 -0.0347 467  GLU A CB  
1969 C CG  . GLU A 244 ? 0.6109 0.2635 0.4059 -0.0231 -0.0182 -0.0420 467  GLU A CG  
1970 C CD  . GLU A 244 ? 0.6546 0.2948 0.4723 -0.0354 0.0084  -0.0448 467  GLU A CD  
1971 O OE1 . GLU A 244 ? 0.6622 0.3094 0.4999 -0.0326 -0.0020 -0.0550 467  GLU A OE1 
1972 O OE2 . GLU A 244 ? 0.6821 0.3094 0.5101 -0.0476 0.0369  -0.0485 467  GLU A OE2 
1973 N N   . SER A 245 ? 0.5876 0.2296 0.2832 -0.0522 -0.1753 -0.0267 468  SER A N   
1974 C CA  . SER A 245 ? 0.6464 0.2673 0.3261 -0.0278 -0.1698 -0.0110 468  SER A CA  
1975 C C   . SER A 245 ? 0.6999 0.2884 0.3008 -0.0272 -0.1656 -0.0202 468  SER A C   
1976 O O   . SER A 245 ? 0.7168 0.3039 0.3158 -0.0033 -0.2122 -0.0131 468  SER A O   
1977 C CB  . SER A 245 ? 0.6704 0.2956 0.3961 -0.0253 -0.1148 -0.0005 468  SER A CB  
1978 O OG  . SER A 245 ? 0.6858 0.3184 0.4243 -0.0324 -0.0941 -0.0036 468  SER A OG  
1979 N N   . ALA A 246 ? 0.7585 0.2907 0.2821 -0.0480 -0.1018 -0.0221 469  ALA A N   
1980 C CA  . ALA A 246 ? 0.7937 0.2814 0.2630 -0.0475 -0.0874 -0.0239 469  ALA A CA  
1981 C C   . ALA A 246 ? 0.7783 0.2862 0.2384 -0.0756 -0.1069 -0.0210 469  ALA A C   
1982 O O   . ALA A 246 ? 0.7667 0.2581 0.2176 -0.0669 -0.0748 -0.0164 469  ALA A O   
1983 C CB  . ALA A 246 ? 0.8229 0.2781 0.2887 -0.0296 -0.0603 -0.0163 469  ALA A CB  
1984 N N   . PRO A 247 ? 0.8052 0.3145 0.2567 -0.1020 -0.1266 -0.0162 470  PRO A N   
1985 C CA  . PRO A 247 ? 0.8006 0.3248 0.2528 -0.0788 -0.1270 -0.0238 470  PRO A CA  
1986 C C   . PRO A 247 ? 0.7829 0.3034 0.2284 -0.0298 -0.1040 -0.0152 470  PRO A C   
1987 O O   . PRO A 247 ? 0.8215 0.3017 0.2718 -0.0222 -0.0598 -0.0126 470  PRO A O   
1988 C CB  . PRO A 247 ? 0.8244 0.3404 0.2654 -0.0925 -0.1468 -0.0123 470  PRO A CB  
1989 C CG  . PRO A 247 ? 0.8317 0.3469 0.2738 -0.0933 -0.1650 -0.0007 470  PRO A CG  
1990 C CD  . PRO A 247 ? 0.8143 0.3324 0.2691 -0.1143 -0.1438 -0.0116 470  PRO A CD  
1991 N N   . SER A 248 ? 0.6742 0.2719 0.2138 0.0186  -0.1334 -0.0003 471  SER A N   
1992 C CA  . SER A 248 ? 0.6272 0.2859 0.2079 0.0442  -0.1339 -0.0224 471  SER A CA  
1993 C C   . SER A 248 ? 0.5788 0.2857 0.2165 0.0637  -0.1187 -0.0459 471  SER A C   
1994 O O   . SER A 248 ? 0.5465 0.3050 0.2395 0.0805  -0.1460 -0.0549 471  SER A O   
1995 C CB  . SER A 248 ? 0.6419 0.3006 0.2042 0.0158  -0.1272 -0.0139 471  SER A CB  
1996 O OG  . SER A 248 ? 0.6711 0.3228 0.2324 0.0062  -0.1591 -0.0053 471  SER A OG  
1997 N N   . GLN A 249 ? 0.5408 0.2731 0.2126 0.0948  -0.1101 -0.0517 472  GLN A N   
1998 C CA  . GLN A 249 ? 0.5407 0.2846 0.2052 0.0872  -0.1171 -0.0493 472  GLN A CA  
1999 C C   . GLN A 249 ? 0.4879 0.2715 0.1819 0.0761  -0.1229 -0.0192 472  GLN A C   
2000 O O   . GLN A 249 ? 0.5043 0.2878 0.2001 0.0456  -0.1337 -0.0265 472  GLN A O   
2001 C CB  . GLN A 249 ? 0.5995 0.3229 0.2627 0.0848  -0.0951 -0.0639 472  GLN A CB  
2002 C CG  . GLN A 249 ? 0.6901 0.3620 0.3329 0.0756  -0.0381 -0.0732 472  GLN A CG  
2003 C CD  . GLN A 249 ? 0.7805 0.3966 0.3714 0.0537  0.0192  -0.0916 472  GLN A CD  
2004 O OE1 . GLN A 249 ? 0.8022 0.4143 0.3632 0.0559  0.0540  -0.1023 472  GLN A OE1 
2005 N NE2 . GLN A 249 ? 0.8127 0.4037 0.3963 0.0377  0.0243  -0.0818 472  GLN A NE2 
2006 N N   . THR A 250 ? 0.4463 0.2501 0.1982 0.0740  -0.1241 -0.0158 473  THR A N   
2007 C CA  . THR A 250 ? 0.4432 0.2409 0.2039 0.0634  -0.1264 -0.0194 473  THR A CA  
2008 C C   . THR A 250 ? 0.4473 0.2349 0.2083 0.0737  -0.1102 -0.0110 473  THR A C   
2009 O O   . THR A 250 ? 0.4534 0.2297 0.2273 0.0612  -0.0585 -0.0308 473  THR A O   
2010 C CB  . THR A 250 ? 0.4688 0.2549 0.1998 0.0723  -0.0972 -0.0076 473  THR A CB  
2011 O OG1 . THR A 250 ? 0.4836 0.2642 0.1811 0.0843  -0.0726 0.0179  473  THR A OG1 
2012 C CG2 . THR A 250 ? 0.4854 0.2608 0.2181 0.0685  -0.0781 -0.0244 473  THR A CG2 
2013 N N   . ASP A 251 ? 0.4499 0.2279 0.2071 0.0764  -0.1145 -0.0141 474  ASP A N   
2014 C CA  . ASP A 251 ? 0.4332 0.2181 0.2121 0.1021  -0.1217 0.0026  474  ASP A CA  
2015 C C   . ASP A 251 ? 0.4154 0.2235 0.1762 0.0976  -0.0907 0.0121  474  ASP A C   
2016 O O   . ASP A 251 ? 0.4199 0.2324 0.1639 0.0886  -0.0530 -0.0035 474  ASP A O   
2017 C CB  . ASP A 251 ? 0.4719 0.2383 0.2989 0.1317  -0.0801 0.0434  474  ASP A CB  
2018 C CG  . ASP A 251 ? 0.5421 0.2520 0.3773 0.1299  -0.0521 0.0794  474  ASP A CG  
2019 O OD1 . ASP A 251 ? 0.5441 0.2699 0.4301 0.1292  -0.0527 0.1041  474  ASP A OD1 
2020 O OD2 . ASP A 251 ? 0.5522 0.2713 0.3936 0.1334  -0.0600 0.0759  474  ASP A OD2 
2021 N N   . VAL A 252 ? 0.4141 0.2334 0.1556 0.0824  -0.0798 0.0189  475  VAL A N   
2022 C CA  . VAL A 252 ? 0.3785 0.2347 0.1850 0.0863  -0.0709 0.0013  475  VAL A CA  
2023 C C   . VAL A 252 ? 0.3448 0.2415 0.1491 0.0929  -0.0953 -0.0195 475  VAL A C   
2024 O O   . VAL A 252 ? 0.3937 0.2662 0.1486 0.0776  -0.0326 -0.0334 475  VAL A O   
2025 C CB  . VAL A 252 ? 0.3675 0.2389 0.2120 0.0962  -0.0628 0.0161  475  VAL A CB  
2026 C CG1 . VAL A 252 ? 0.3745 0.2606 0.2173 0.0749  -0.0889 -0.0138 475  VAL A CG1 
2027 C CG2 . VAL A 252 ? 0.3510 0.2216 0.2507 0.1147  -0.0446 0.0028  475  VAL A CG2 
2028 N N   . ALA A 253 ? 0.3350 0.2272 0.1631 0.1148  -0.0516 -0.0100 476  ALA A N   
2029 C CA  . ALA A 253 ? 0.3738 0.2245 0.1746 0.1062  -0.0090 -0.0069 476  ALA A CA  
2030 C C   . ALA A 253 ? 0.3521 0.2397 0.1931 0.1252  -0.0196 -0.0191 476  ALA A C   
2031 O O   . ALA A 253 ? 0.3535 0.2438 0.2354 0.1137  -0.0440 -0.0454 476  ALA A O   
2032 C CB  . ALA A 253 ? 0.3871 0.2129 0.1935 0.0802  0.0058  -0.0084 476  ALA A CB  
2033 N N   . LEU A 254 ? 0.3424 0.2655 0.2045 0.1324  -0.0032 0.0034  477  LEU A N   
2034 C CA  . LEU A 254 ? 0.3543 0.2905 0.1768 0.1294  -0.0069 0.0029  477  LEU A CA  
2035 C C   . LEU A 254 ? 0.3552 0.2956 0.1800 0.1397  -0.0071 0.0005  477  LEU A C   
2036 O O   . LEU A 254 ? 0.4001 0.3076 0.1975 0.1489  -0.0133 0.0144  477  LEU A O   
2037 C CB  . LEU A 254 ? 0.3981 0.3070 0.1940 0.1049  0.0159  0.0110  477  LEU A CB  
2038 C CG  . LEU A 254 ? 0.4216 0.3216 0.1932 0.0881  0.0038  0.0132  477  LEU A CG  
2039 C CD1 . LEU A 254 ? 0.4343 0.3282 0.1859 0.0821  -0.0335 0.0464  477  LEU A CD1 
2040 C CD2 . LEU A 254 ? 0.4317 0.3309 0.1927 0.0853  0.0077  -0.0054 477  LEU A CD2 
2041 N N   . ILE A 255 ? 0.3307 0.2974 0.1654 0.1376  -0.0338 0.0091  478  ILE A N   
2042 C CA  . ILE A 255 ? 0.3220 0.3042 0.1674 0.1404  -0.0335 0.0091  478  ILE A CA  
2043 C C   . ILE A 255 ? 0.3402 0.3292 0.1931 0.1761  -0.0110 0.0158  478  ILE A C   
2044 O O   . ILE A 255 ? 0.3443 0.3238 0.2102 0.1514  -0.0123 0.0013  478  ILE A O   
2045 C CB  . ILE A 255 ? 0.2963 0.2757 0.1624 0.1300  -0.0321 -0.0126 478  ILE A CB  
2046 C CG1 . ILE A 255 ? 0.2927 0.2647 0.1620 0.1173  -0.0001 -0.0178 478  ILE A CG1 
2047 C CG2 . ILE A 255 ? 0.3099 0.2756 0.1940 0.1159  -0.0300 -0.0177 478  ILE A CG2 
2048 C CD1 . ILE A 255 ? 0.2875 0.2718 0.1548 0.1081  -0.0449 -0.0160 478  ILE A CD1 
2049 N N   . ARG A 256 ? 0.3479 0.3623 0.2110 0.1900  -0.0222 0.0431  479  ARG A N   
2050 C CA  . ARG A 256 ? 0.3810 0.3862 0.2115 0.2121  -0.0003 0.0506  479  ARG A CA  
2051 C C   . ARG A 256 ? 0.3665 0.3786 0.1968 0.2011  -0.0090 0.0362  479  ARG A C   
2052 O O   . ARG A 256 ? 0.3926 0.3562 0.2018 0.1959  -0.0129 0.0460  479  ARG A O   
2053 C CB  . ARG A 256 ? 0.4614 0.4190 0.2365 0.2443  0.0345  0.0642  479  ARG A CB  
2054 C CG  . ARG A 256 ? 0.5504 0.4535 0.2761 0.2528  0.0428  0.0808  479  ARG A CG  
2055 C CD  . ARG A 256 ? 0.6158 0.4784 0.3012 0.2574  0.0748  0.0860  479  ARG A CD  
2056 N NE  . ARG A 256 ? 0.6335 0.4965 0.2912 0.2727  0.0637  0.0815  479  ARG A NE  
2057 C CZ  . ARG A 256 ? 0.6174 0.5202 0.3075 0.2892  0.0415  0.0753  479  ARG A CZ  
2058 N NH1 . ARG A 256 ? 0.6050 0.5337 0.3295 0.2953  -0.0035 0.0662  479  ARG A NH1 
2059 N NH2 . ARG A 256 ? 0.6189 0.5315 0.2796 0.2705  0.0433  0.0689  479  ARG A NH2 
2060 N N   . TYR A 257 ? 0.3294 0.3962 0.2021 0.1735  0.0032  0.0274  480  TYR A N   
2061 C CA  . TYR A 257 ? 0.3248 0.4097 0.2144 0.1684  -0.0309 0.0450  480  TYR A CA  
2062 C C   . TYR A 257 ? 0.3256 0.4226 0.2539 0.1861  -0.0108 0.0421  480  TYR A C   
2063 O O   . TYR A 257 ? 0.3065 0.4340 0.2855 0.1555  0.0146  0.0436  480  TYR A O   
2064 C CB  . TYR A 257 ? 0.3433 0.4224 0.2196 0.1352  -0.0281 0.0518  480  TYR A CB  
2065 C CG  . TYR A 257 ? 0.3536 0.4250 0.2345 0.1248  -0.0421 0.0552  480  TYR A CG  
2066 C CD1 . TYR A 257 ? 0.3568 0.4247 0.2444 0.1308  -0.0281 0.0365  480  TYR A CD1 
2067 C CD2 . TYR A 257 ? 0.3813 0.4423 0.2711 0.1075  -0.0331 0.0279  480  TYR A CD2 
2068 C CE1 . TYR A 257 ? 0.3374 0.4296 0.2304 0.1434  -0.0614 0.0499  480  TYR A CE1 
2069 C CE2 . TYR A 257 ? 0.3734 0.4461 0.2710 0.1121  -0.0310 0.0307  480  TYR A CE2 
2070 C CZ  . TYR A 257 ? 0.3661 0.4468 0.2357 0.1323  -0.0358 0.0406  480  TYR A CZ  
2071 O OH  . TYR A 257 ? 0.3872 0.4637 0.2753 0.1443  0.0208  0.0323  480  TYR A OH  
2072 N N   A VAL A 258 ? 0.3454 0.4187 0.2556 0.1879  0.0007  0.0375  481  VAL A N   
2073 N N   B VAL A 258 ? 0.3418 0.4203 0.2624 0.2035  0.0021  0.0401  481  VAL A N   
2074 C CA  A VAL A 258 ? 0.3508 0.4281 0.2486 0.1972  0.0070  0.0291  481  VAL A CA  
2075 C CA  B VAL A 258 ? 0.3433 0.4284 0.2632 0.2248  0.0072  0.0350  481  VAL A CA  
2076 C C   A VAL A 258 ? 0.3587 0.4328 0.2536 0.2166  0.0196  0.0370  481  VAL A C   
2077 C C   B VAL A 258 ? 0.3519 0.4329 0.2604 0.2294  0.0170  0.0415  481  VAL A C   
2078 O O   A VAL A 258 ? 0.3649 0.4354 0.2682 0.2190  0.0160  0.0372  481  VAL A O   
2079 O O   B VAL A 258 ? 0.3555 0.4361 0.2738 0.2309  0.0130  0.0425  481  VAL A O   
2080 C CB  A VAL A 258 ? 0.3735 0.4285 0.2544 0.1849  0.0252  0.0206  481  VAL A CB  
2081 C CB  B VAL A 258 ? 0.3623 0.4291 0.2803 0.2343  0.0200  0.0282  481  VAL A CB  
2082 C CG1 A VAL A 258 ? 0.3866 0.4322 0.2598 0.1759  0.0303  0.0247  481  VAL A CG1 
2083 C CG1 B VAL A 258 ? 0.3548 0.4210 0.2894 0.2297  0.0217  0.0237  481  VAL A CG1 
2084 C CG2 A VAL A 258 ? 0.3782 0.4196 0.2376 0.1864  0.0390  0.0188  481  VAL A CG2 
2085 C CG2 B VAL A 258 ? 0.3890 0.4337 0.2780 0.2427  0.0331  0.0320  481  VAL A CG2 
2086 N N   . ASN A 259 ? 0.3473 0.4323 0.2420 0.2186  -0.0023 0.0498  482  ASN A N   
2087 C CA  . ASN A 259 ? 0.3370 0.4596 0.2658 0.2183  -0.0029 0.0566  482  ASN A CA  
2088 C C   . ASN A 259 ? 0.3232 0.4510 0.2738 0.2178  0.0002  0.0437  482  ASN A C   
2089 O O   . ASN A 259 ? 0.3339 0.4584 0.3180 0.2279  0.0295  0.0378  482  ASN A O   
2090 C CB  . ASN A 259 ? 0.3663 0.4712 0.3110 0.1993  0.0048  0.0724  482  ASN A CB  
2091 C CG  . ASN A 259 ? 0.3960 0.4783 0.3385 0.1942  0.0337  0.0764  482  ASN A CG  
2092 O OD1 . ASN A 259 ? 0.4025 0.4662 0.3275 0.2200  0.0480  0.0993  482  ASN A OD1 
2093 N ND2 . ASN A 259 ? 0.3969 0.4877 0.3508 0.1821  0.0316  0.0708  482  ASN A ND2 
2094 N N   . PRO A 260 ? 0.3484 0.4657 0.3048 0.2359  0.0253  0.0361  483  PRO A N   
2095 C CA  . PRO A 260 ? 0.3888 0.4890 0.3570 0.2532  0.0626  0.0419  483  PRO A CA  
2096 C C   . PRO A 260 ? 0.4147 0.5205 0.3923 0.2663  0.0525  0.0695  483  PRO A C   
2097 O O   . PRO A 260 ? 0.4818 0.5427 0.4152 0.2067  0.0681  0.0424  483  PRO A O   
2098 C CB  . PRO A 260 ? 0.3777 0.4723 0.3526 0.2424  0.0699  0.0332  483  PRO A CB  
2099 C CG  . PRO A 260 ? 0.3821 0.4668 0.3171 0.2387  0.0381  0.0410  483  PRO A CG  
2100 C CD  . PRO A 260 ? 0.3671 0.4632 0.2994 0.2259  0.0367  0.0370  483  PRO A CD  
2101 N N   . ASP A 261 ? 0.4275 0.5511 0.3944 0.2786  0.0405  0.0940  484  ASP A N   
2102 C CA  . ASP A 261 ? 0.4434 0.5805 0.4250 0.2891  0.0379  0.1032  484  ASP A CA  
2103 C C   . ASP A 261 ? 0.4482 0.5983 0.4506 0.2982  0.0584  0.0941  484  ASP A C   
2104 O O   . ASP A 261 ? 0.4800 0.6054 0.4772 0.3111  0.0789  0.1056  484  ASP A O   
2105 C CB  . ASP A 261 ? 0.4633 0.6005 0.4579 0.2971  0.0306  0.1154  484  ASP A CB  
2106 C CG  . ASP A 261 ? 0.4881 0.6213 0.4755 0.3087  0.0296  0.1247  484  ASP A CG  
2107 O OD1 . ASP A 261 ? 0.5344 0.6307 0.4844 0.2976  0.0416  0.1227  484  ASP A OD1 
2108 O OD2 . ASP A 261 ? 0.4797 0.6290 0.5037 0.3108  0.0335  0.1171  484  ASP A OD2 
2109 N N   . THR A 262 ? 0.4287 0.6165 0.4321 0.2942  0.0517  0.0836  485  THR A N   
2110 C CA  . THR A 262 ? 0.4166 0.6327 0.4206 0.2924  0.0452  0.0679  485  THR A CA  
2111 C C   . THR A 262 ? 0.4394 0.6396 0.4220 0.3024  0.0619  0.0379  485  THR A C   
2112 O O   . THR A 262 ? 0.4551 0.6406 0.4269 0.3007  0.0840  0.0215  485  THR A O   
2113 C CB  . THR A 262 ? 0.3899 0.6442 0.4124 0.2775  0.0421  0.0880  485  THR A CB  
2114 O OG1 . THR A 262 ? 0.3955 0.6431 0.4123 0.2789  0.0695  0.0952  485  THR A OG1 
2115 C CG2 . THR A 262 ? 0.3914 0.6590 0.4035 0.2627  0.0307  0.0914  485  THR A CG2 
2116 N N   . GLY A 263 ? 0.4464 0.6361 0.4149 0.3065  0.0512  0.0255  486  GLY A N   
2117 C CA  . GLY A 263 ? 0.4540 0.6329 0.4320 0.3051  0.0453  0.0355  486  GLY A CA  
2118 C C   . GLY A 263 ? 0.4515 0.6212 0.4358 0.3065  0.0410  0.0546  486  GLY A C   
2119 O O   . GLY A 263 ? 0.4860 0.6403 0.4379 0.2804  0.0516  0.0494  486  GLY A O   
2120 N N   . ARG A 264 ? 0.4401 0.5937 0.4425 0.2959  0.0382  0.0761  487  ARG A N   
2121 C CA  . ARG A 264 ? 0.4574 0.5771 0.4736 0.2644  0.0322  0.0938  487  ARG A CA  
2122 C C   . ARG A 264 ? 0.3749 0.5879 0.4292 0.2306  0.0140  0.1066  487  ARG A C   
2123 O O   . ARG A 264 ? 0.3568 0.5945 0.4059 0.2081  -0.0257 0.1093  487  ARG A O   
2131 N N   . VAL A 265 ? 0.3250 0.6038 0.3997 0.2026  0.0281  0.1030  488  VAL A N   
2132 C CA  . VAL A 265 ? 0.3049 0.6080 0.3607 0.1787  0.0148  0.1158  488  VAL A CA  
2133 C C   . VAL A 265 ? 0.2984 0.6155 0.3536 0.1359  0.0280  0.1275  488  VAL A C   
2134 O O   . VAL A 265 ? 0.3436 0.6276 0.3715 0.1046  0.0690  0.1235  488  VAL A O   
2135 C CB  . VAL A 265 ? 0.2914 0.6033 0.3316 0.1850  -0.0172 0.1006  488  VAL A CB  
2136 C CG1 . VAL A 265 ? 0.3224 0.5974 0.3203 0.1806  0.0024  0.1061  488  VAL A CG1 
2137 C CG2 . VAL A 265 ? 0.3279 0.6050 0.3254 0.1836  0.0101  0.0913  488  VAL A CG2 
2138 N N   . LEU A 266 ? 0.2707 0.6083 0.3587 0.1444  0.0240  0.1487  489  LEU A N   
2139 C CA  . LEU A 266 ? 0.2866 0.5994 0.3846 0.1221  0.0336  0.1548  489  LEU A CA  
2140 C C   . LEU A 266 ? 0.2864 0.5735 0.3678 0.1123  0.0059  0.1423  489  LEU A C   
2141 O O   . LEU A 266 ? 0.3018 0.5797 0.3879 0.0958  0.0058  0.1602  489  LEU A O   
2142 C CB  . LEU A 266 ? 0.3363 0.6155 0.4035 0.0958  0.0344  0.1692  489  LEU A CB  
2143 C CG  . LEU A 266 ? 0.3590 0.6308 0.4542 0.0806  0.0377  0.1649  489  LEU A CG  
2144 C CD1 . LEU A 266 ? 0.3766 0.6384 0.4740 0.0755  0.0325  0.1664  489  LEU A CD1 
2145 C CD2 . LEU A 266 ? 0.3690 0.6299 0.4735 0.0867  0.0508  0.1754  489  LEU A CD2 
2146 N N   . PHE A 267 ? 0.2652 0.5355 0.3185 0.1313  0.0083  0.1199  490  PHE A N   
2147 C CA  . PHE A 267 ? 0.2936 0.5001 0.2945 0.1243  0.0380  0.0705  490  PHE A CA  
2148 C C   . PHE A 267 ? 0.2951 0.4891 0.2551 0.1327  0.0151  0.0567  490  PHE A C   
2149 O O   . PHE A 267 ? 0.2786 0.5008 0.2488 0.1282  -0.0218 0.0628  490  PHE A O   
2150 C CB  . PHE A 267 ? 0.2904 0.4809 0.2872 0.1074  0.0399  0.0530  490  PHE A CB  
2151 C CG  . PHE A 267 ? 0.2821 0.4540 0.2586 0.0937  0.0086  0.0233  490  PHE A CG  
2152 C CD1 . PHE A 267 ? 0.2934 0.4454 0.2466 0.0829  0.0037  0.0009  490  PHE A CD1 
2153 C CD2 . PHE A 267 ? 0.2764 0.4321 0.2477 0.0978  0.0156  0.0058  490  PHE A CD2 
2154 C CE1 . PHE A 267 ? 0.3128 0.4373 0.2423 0.0668  0.0182  -0.0280 490  PHE A CE1 
2155 C CE2 . PHE A 267 ? 0.3045 0.4249 0.2303 0.0910  0.0028  -0.0115 490  PHE A CE2 
2156 C CZ  . PHE A 267 ? 0.3050 0.4237 0.2396 0.0896  0.0069  -0.0306 490  PHE A CZ  
2157 N N   . GLU A 268 ? 0.2859 0.4656 0.2157 0.1281  -0.0045 0.0344  491  GLU A N   
2158 C CA  . GLU A 268 ? 0.2912 0.4384 0.1994 0.1232  -0.0002 0.0383  491  GLU A CA  
2159 C C   . GLU A 268 ? 0.2948 0.4001 0.1961 0.1048  0.0083  0.0338  491  GLU A C   
2160 O O   . GLU A 268 ? 0.2960 0.4082 0.1876 0.1070  0.0009  0.0384  491  GLU A O   
2161 C CB  . GLU A 268 ? 0.3177 0.4560 0.1844 0.1261  0.0169  0.0265  491  GLU A CB  
2162 C CG  . GLU A 268 ? 0.3616 0.4826 0.2135 0.1102  0.0295  0.0294  491  GLU A CG  
2163 C CD  . GLU A 268 ? 0.4288 0.5062 0.2510 0.0969  0.0397  0.0341  491  GLU A CD  
2164 O OE1 . GLU A 268 ? 0.4766 0.5222 0.2685 0.0811  0.0570  0.0209  491  GLU A OE1 
2165 O OE2 . GLU A 268 ? 0.3962 0.5084 0.2428 0.1099  0.0096  0.0468  491  GLU A OE2 
2166 N N   . ALA A 269 ? 0.2852 0.3598 0.2067 0.0987  0.0192  0.0291  492  ALA A N   
2167 C CA  . ALA A 269 ? 0.2529 0.3153 0.1867 0.1000  -0.0071 0.0272  492  ALA A CA  
2168 C C   . ALA A 269 ? 0.2798 0.2869 0.1722 0.0819  -0.0099 0.0336  492  ALA A C   
2169 O O   . ALA A 269 ? 0.2761 0.2631 0.1715 0.0725  -0.0256 0.0136  492  ALA A O   
2170 C CB  . ALA A 269 ? 0.2782 0.3145 0.1741 0.0890  0.0026  0.0396  492  ALA A CB  
2171 N N   . LYS A 270 ? 0.2736 0.2851 0.1551 0.0652  -0.0055 0.0402  493  LYS A N   
2172 C CA  . LYS A 270 ? 0.2830 0.2751 0.1659 0.0557  -0.0102 0.0516  493  LYS A CA  
2173 C C   . LYS A 270 ? 0.2570 0.2515 0.1652 0.0578  -0.0281 0.0140  493  LYS A C   
2174 O O   . LYS A 270 ? 0.2776 0.2508 0.1835 0.0411  -0.0224 0.0048  493  LYS A O   
2175 C CB  . LYS A 270 ? 0.3126 0.2913 0.1766 0.0437  -0.0055 0.0794  493  LYS A CB  
2176 C CG  . LYS A 270 ? 0.3701 0.3040 0.2078 0.0179  -0.0106 0.0846  493  LYS A CG  
2177 C CD  . LYS A 270 ? 0.4310 0.3023 0.2484 0.0100  0.0012  0.0867  493  LYS A CD  
2178 C CE  . LYS A 270 ? 0.4402 0.3024 0.2620 0.0391  -0.0212 0.0843  493  LYS A CE  
2179 N NZ  . LYS A 270 ? 0.4334 0.2965 0.2450 0.0278  -0.0409 0.0899  493  LYS A NZ  
2180 N N   . LEU A 271 ? 0.2531 0.2348 0.1592 0.0661  -0.0304 -0.0024 494  LEU A N   
2181 C CA  . LEU A 271 ? 0.2838 0.2053 0.1483 0.0843  -0.0560 0.0080  494  LEU A CA  
2182 C C   . LEU A 271 ? 0.2944 0.1819 0.1391 0.0549  -0.0447 -0.0121 494  LEU A C   
2183 O O   . LEU A 271 ? 0.2995 0.1993 0.1435 0.0307  -0.0292 -0.0118 494  LEU A O   
2184 C CB  . LEU A 271 ? 0.2915 0.1958 0.1578 0.0785  -0.0412 0.0134  494  LEU A CB  
2185 C CG  . LEU A 271 ? 0.2954 0.1826 0.1475 0.0747  -0.0234 -0.0062 494  LEU A CG  
2186 C CD1 . LEU A 271 ? 0.3200 0.1896 0.1403 0.0626  -0.0197 0.0019  494  LEU A CD1 
2187 C CD2 . LEU A 271 ? 0.3132 0.1826 0.1703 0.0473  -0.0357 -0.0257 494  LEU A CD2 
2188 N N   . HIS A 272 ? 0.2830 0.1693 0.1485 0.0700  -0.0443 0.0023  495  HIS A N   
2189 C CA  . HIS A 272 ? 0.2518 0.1618 0.1602 0.0503  -0.0558 0.0008  495  HIS A CA  
2190 C C   . HIS A 272 ? 0.2604 0.1900 0.1781 0.0419  -0.0558 -0.0123 495  HIS A C   
2191 O O   . HIS A 272 ? 0.2747 0.1872 0.1615 0.0489  -0.0663 0.0092  495  HIS A O   
2192 C CB  . HIS A 272 ? 0.2517 0.1653 0.1375 0.0413  -0.0610 0.0148  495  HIS A CB  
2193 C CG  . HIS A 272 ? 0.2477 0.1935 0.1477 0.0335  -0.0523 0.0277  495  HIS A CG  
2194 N ND1 . HIS A 272 ? 0.2586 0.2147 0.1662 0.0203  -0.0260 0.0207  495  HIS A ND1 
2195 C CD2 . HIS A 272 ? 0.2674 0.2115 0.1683 0.0129  -0.0598 0.0246  495  HIS A CD2 
2196 C CE1 . HIS A 272 ? 0.2326 0.2223 0.1948 0.0177  -0.0441 0.0165  495  HIS A CE1 
2197 N NE2 . HIS A 272 ? 0.2770 0.2293 0.1958 0.0125  -0.0288 0.0165  495  HIS A NE2 
2198 N N   . ARG A 273 ? 0.2427 0.2116 0.1770 0.0425  -0.0753 -0.0153 496  ARG A N   
2199 C CA  . ARG A 273 ? 0.2756 0.2620 0.1776 0.0197  -0.0857 -0.0411 496  ARG A CA  
2200 C C   . ARG A 273 ? 0.2445 0.2251 0.1793 0.0074  -0.0600 0.0040  496  ARG A C   
2201 O O   . ARG A 273 ? 0.2448 0.2059 0.1852 0.0063  -0.0402 0.0138  496  ARG A O   
2202 C CB  . ARG A 273 ? 0.3163 0.3499 0.2451 -0.0071 -0.1460 -0.0442 496  ARG A CB  
2203 C CG  . ARG A 273 ? 0.4071 0.4214 0.2978 0.0023  -0.1966 -0.0568 496  ARG A CG  
2204 C CD  . ARG A 273 ? 0.4739 0.4703 0.3457 0.0107  -0.2290 -0.0655 496  ARG A CD  
2205 N NE  . ARG A 273 ? 0.5634 0.5073 0.4251 0.0322  -0.2186 -0.0521 496  ARG A NE  
2206 C CZ  . ARG A 273 ? 0.6320 0.5285 0.4772 0.0477  -0.2110 -0.0439 496  ARG A CZ  
2207 N NH1 . ARG A 273 ? 0.6592 0.5369 0.4811 0.0480  -0.2206 -0.0407 496  ARG A NH1 
2208 N NH2 . ARG A 273 ? 0.6551 0.5270 0.5161 0.0509  -0.2027 -0.0366 496  ARG A NH2 
2209 N N   . GLN A 274 ? 0.2203 0.1915 0.1656 0.0254  -0.0746 0.0230  497  GLN A N   
2210 C CA  . GLN A 274 ? 0.2572 0.1850 0.1754 0.0373  -0.0785 0.0578  497  GLN A CA  
2211 C C   . GLN A 274 ? 0.2308 0.1898 0.1511 0.0192  -0.0571 0.0389  497  GLN A C   
2212 O O   . GLN A 274 ? 0.2189 0.2068 0.2008 0.0087  -0.0421 0.0151  497  GLN A O   
2213 C CB  . GLN A 274 ? 0.3320 0.1842 0.2353 0.0064  -0.0594 0.0631  497  GLN A CB  
2214 C CG  . GLN A 274 ? 0.3926 0.1978 0.2855 0.0282  -0.0527 0.0656  497  GLN A CG  
2215 C CD  . GLN A 274 ? 0.4366 0.2116 0.3158 0.0397  -0.0213 0.0736  497  GLN A CD  
2216 O OE1 . GLN A 274 ? 0.3695 0.2056 0.2834 0.0257  -0.0496 0.0473  497  GLN A OE1 
2217 N NE2 . GLN A 274 ? 0.5247 0.2332 0.3525 0.0740  0.0184  0.0913  497  GLN A NE2 
2218 N N   . GLY A 275 ? 0.2390 0.1625 0.1221 0.0207  -0.0429 0.0390  498  GLY A N   
2219 C CA  . GLY A 275 ? 0.2156 0.1542 0.1385 0.0032  -0.0445 0.0303  498  GLY A CA  
2220 C C   . GLY A 275 ? 0.2210 0.1564 0.1378 0.0322  -0.0225 0.0212  498  GLY A C   
2221 O O   . GLY A 275 ? 0.2425 0.1840 0.1507 0.0239  -0.0202 0.0213  498  GLY A O   
2222 N N   . TYR A 276 ? 0.2230 0.1479 0.1638 0.0143  -0.0254 0.0146  499  TYR A N   
2223 C CA  . TYR A 276 ? 0.2106 0.1522 0.1535 0.0096  -0.0530 -0.0053 499  TYR A CA  
2224 C C   . TYR A 276 ? 0.2244 0.1687 0.1572 0.0088  -0.0363 -0.0056 499  TYR A C   
2225 O O   . TYR A 276 ? 0.2415 0.2037 0.1384 0.0225  -0.0476 0.0041  499  TYR A O   
2226 C CB  . TYR A 276 ? 0.2507 0.1561 0.1566 0.0027  -0.0570 0.0277  499  TYR A CB  
2227 C CG  . TYR A 276 ? 0.2901 0.1756 0.1496 0.0084  -0.0653 0.0289  499  TYR A CG  
2228 C CD1 . TYR A 276 ? 0.2865 0.1618 0.1539 0.0223  -0.0818 0.0424  499  TYR A CD1 
2229 C CD2 . TYR A 276 ? 0.2839 0.2012 0.1743 0.0041  -0.0176 0.0276  499  TYR A CD2 
2230 C CE1 . TYR A 276 ? 0.2907 0.1512 0.1564 0.0137  -0.0243 0.0376  499  TYR A CE1 
2231 C CE2 . TYR A 276 ? 0.3019 0.2067 0.1958 0.0155  0.0021  0.0276  499  TYR A CE2 
2232 C CZ  . TYR A 276 ? 0.3128 0.1819 0.1787 0.0362  -0.0087 0.0508  499  TYR A CZ  
2233 O OH  . TYR A 276 ? 0.3333 0.2144 0.2012 0.0286  -0.0293 0.0623  499  TYR A OH  
2234 N N   . ILE A 277 ? 0.2295 0.1737 0.1544 0.0346  -0.0092 0.0053  500  ILE A N   
2235 C CA  . ILE A 277 ? 0.2082 0.1951 0.1412 0.0247  -0.0327 0.0066  500  ILE A CA  
2236 C C   . ILE A 277 ? 0.2369 0.2144 0.1572 0.0057  -0.0005 -0.0052 500  ILE A C   
2237 O O   . ILE A 277 ? 0.2273 0.2183 0.1526 0.0096  -0.0147 -0.0057 500  ILE A O   
2238 C CB  . ILE A 277 ? 0.2152 0.2022 0.1661 0.0410  -0.0412 0.0200  500  ILE A CB  
2239 C CG1 . ILE A 277 ? 0.2523 0.2024 0.1631 0.0112  -0.0603 0.0252  500  ILE A CG1 
2240 C CG2 . ILE A 277 ? 0.2458 0.2428 0.1618 0.0465  -0.0010 0.0076  500  ILE A CG2 
2241 C CD1 . ILE A 277 ? 0.2576 0.2022 0.1544 0.0441  -0.0396 0.0156  500  ILE A CD1 
2242 N N   . THR A 278 ? 0.2436 0.2243 0.1631 -0.0007 0.0126  0.0066  501  THR A N   
2243 C CA  . THR A 278 ? 0.2341 0.2478 0.1614 -0.0024 -0.0004 0.0351  501  THR A CA  
2244 C C   . THR A 278 ? 0.2631 0.2771 0.1750 0.0067  0.0063  0.0414  501  THR A C   
2245 O O   . THR A 278 ? 0.2704 0.2752 0.1980 0.0022  -0.0054 0.0426  501  THR A O   
2246 C CB  . THR A 278 ? 0.2631 0.2551 0.1582 0.0126  -0.0030 0.0216  501  THR A CB  
2247 O OG1 . THR A 278 ? 0.2998 0.2636 0.1637 0.0121  -0.0074 0.0011  501  THR A OG1 
2248 C CG2 . THR A 278 ? 0.2632 0.2613 0.1900 0.0023  -0.0107 0.0250  501  THR A CG2 
2249 N N   . VAL A 279 ? 0.2387 0.3141 0.1778 0.0011  -0.0035 0.0433  502  VAL A N   
2250 C CA  . VAL A 279 ? 0.2610 0.3553 0.1908 0.0029  0.0027  0.0619  502  VAL A CA  
2251 C C   . VAL A 279 ? 0.2731 0.3898 0.2059 -0.0248 0.0254  0.0644  502  VAL A C   
2252 O O   . VAL A 279 ? 0.3094 0.3906 0.2280 -0.0233 0.0467  0.0574  502  VAL A O   
2253 C CB  . VAL A 279 ? 0.2861 0.3590 0.2061 0.0165  -0.0090 0.0512  502  VAL A CB  
2254 C CG1 . VAL A 279 ? 0.2887 0.3637 0.2311 0.0067  -0.0021 0.0516  502  VAL A CG1 
2255 C CG2 . VAL A 279 ? 0.3077 0.3551 0.2123 0.0275  -0.0255 0.0540  502  VAL A CG2 
2256 N N   . ALA A 280 ? 0.2945 0.4384 0.2064 -0.0490 0.0492  0.0596  503  ALA A N   
2257 C CA  . ALA A 280 ? 0.3377 0.4804 0.2102 -0.0647 0.0754  0.0565  503  ALA A CA  
2258 C C   . ALA A 280 ? 0.3495 0.5227 0.2492 -0.0872 0.0426  0.0515  503  ALA A C   
2259 O O   . ALA A 280 ? 0.3766 0.5313 0.2546 -0.0745 0.0579  0.0526  503  ALA A O   
2260 C CB  . ALA A 280 ? 0.3765 0.4843 0.2030 -0.0429 0.0965  0.0546  503  ALA A CB  
2261 N N   . LYS A 281 ? 0.3368 0.5588 0.2807 -0.1263 -0.0169 0.0443  504  LYS A N   
2262 C CA  . LYS A 281 ? 0.3403 0.5995 0.3556 -0.1583 -0.0345 0.0298  504  LYS A CA  
2263 C C   . LYS A 281 ? 0.3736 0.6227 0.3985 -0.1744 -0.0349 0.0127  504  LYS A C   
2264 O O   . LYS A 281 ? 0.3799 0.6199 0.3968 -0.1772 -0.0355 -0.0024 504  LYS A O   
2265 C CB  . LYS A 281 ? 0.3285 0.6171 0.3898 -0.1770 -0.0463 0.0343  504  LYS A CB  
2266 C CG  . LYS A 281 ? 0.3375 0.6417 0.4358 -0.1762 -0.0367 0.0337  504  LYS A CG  
2267 C CD  . LYS A 281 ? 0.3543 0.6543 0.4782 -0.1897 -0.0468 0.0348  504  LYS A CD  
2268 C CE  . LYS A 281 ? 0.3747 0.6649 0.5075 -0.1978 -0.0486 0.0269  504  LYS A CE  
2269 N NZ  . LYS A 281 ? 0.3901 0.6689 0.5229 -0.1984 -0.0505 0.0318  504  LYS A NZ  
2270 N N   . THR A 282 ? 0.4103 0.6428 0.4477 -0.1982 -0.0212 0.0046  505  THR A N   
2271 C CA  . THR A 282 ? 0.4655 0.6670 0.4868 -0.2082 0.0162  0.0022  505  THR A CA  
2272 C C   . THR A 282 ? 0.4571 0.6704 0.4897 -0.2356 -0.0101 -0.0213 505  THR A C   
2273 O O   . THR A 282 ? 0.4783 0.6836 0.5098 -0.2164 -0.0061 -0.0252 505  THR A O   
2274 C CB  . THR A 282 ? 0.5246 0.6780 0.5070 -0.2053 0.0671  0.0163  505  THR A CB  
2275 O OG1 . THR A 282 ? 0.5448 0.6835 0.5136 -0.2056 0.0918  0.0232  505  THR A OG1 
2276 C CG2 . THR A 282 ? 0.5447 0.6809 0.5177 -0.1989 0.0724  0.0159  505  THR A CG2 
2277 N N   . GLY A 283 ? 0.4325 0.6612 0.4820 -0.2714 -0.0164 -0.0279 506  GLY A N   
2278 C CA  . GLY A 283 ? 0.4385 0.6597 0.4835 -0.2748 -0.0170 -0.0325 506  GLY A CA  
2279 C C   . GLY A 283 ? 0.4456 0.6545 0.5014 -0.2799 -0.0086 -0.0422 506  GLY A C   
2280 O O   . GLY A 283 ? 0.4225 0.6458 0.4868 -0.2918 -0.0330 -0.0439 506  GLY A O   
2281 N N   . ASP A 284 ? 0.4544 0.6540 0.5291 -0.2591 -0.0069 -0.0498 507  ASP A N   
2282 C CA  . ASP A 284 ? 0.4572 0.6483 0.5755 -0.2313 -0.0130 -0.0497 507  ASP A CA  
2283 C C   . ASP A 284 ? 0.4193 0.6305 0.5960 -0.1697 -0.0609 -0.0357 507  ASP A C   
2284 O O   . ASP A 284 ? 0.4345 0.6309 0.6109 -0.1662 -0.0736 -0.0476 507  ASP A O   
2285 C CB  . ASP A 284 ? 0.4711 0.6618 0.5889 -0.2720 -0.0010 -0.0777 507  ASP A CB  
2286 C CG  . ASP A 284 ? 0.5252 0.6840 0.6145 -0.2732 0.0352  -0.0867 507  ASP A CG  
2287 O OD1 . ASP A 284 ? 0.5435 0.6816 0.6252 -0.2833 0.0518  -0.0943 507  ASP A OD1 
2288 O OD2 . ASP A 284 ? 0.5741 0.7012 0.6319 -0.2501 0.0694  -0.0707 507  ASP A OD2 
2289 N N   . SER A 285 ? 0.3810 0.6070 0.5952 -0.1158 -0.0846 -0.0087 508  SER A N   
2290 C CA  . SER A 285 ? 0.3657 0.5886 0.5891 -0.0567 -0.0999 0.0190  508  SER A CA  
2291 C C   . SER A 285 ? 0.3118 0.5810 0.5147 -0.0016 -0.1411 0.0408  508  SER A C   
2292 O O   . SER A 285 ? 0.2581 0.5683 0.4715 0.0160  -0.1356 0.0364  508  SER A O   
2293 C CB  . SER A 285 ? 0.3794 0.5810 0.6471 -0.0566 -0.0877 0.0261  508  SER A CB  
2294 O OG  . SER A 285 ? 0.3738 0.5739 0.7088 -0.0606 -0.0735 0.0285  508  SER A OG  
2295 N N   . PRO A 286 ? 0.3240 0.5911 0.4974 0.0242  -0.1591 0.0605  509  PRO A N   
2296 C CA  . PRO A 286 ? 0.3162 0.5881 0.4721 0.0337  -0.1504 0.0711  509  PRO A CA  
2297 C C   . PRO A 286 ? 0.3345 0.5850 0.4663 0.0499  -0.0652 0.0701  509  PRO A C   
2298 O O   . PRO A 286 ? 0.3711 0.5870 0.5143 0.0380  0.0112  0.0512  509  PRO A O   
2299 C CB  . PRO A 286 ? 0.3386 0.5949 0.4923 0.0338  -0.1615 0.0786  509  PRO A CB  
2300 C CG  . PRO A 286 ? 0.3681 0.5974 0.5193 0.0325  -0.1249 0.0764  509  PRO A CG  
2301 C CD  . PRO A 286 ? 0.3334 0.5984 0.5099 0.0208  -0.1619 0.0656  509  PRO A CD  
2302 N N   . ILE A 287 ? 0.3339 0.5765 0.4118 0.0831  -0.0517 0.0868  510  ILE A N   
2303 C CA  . ILE A 287 ? 0.3600 0.5841 0.4019 0.0869  -0.0164 0.0824  510  ILE A CA  
2304 C C   . ILE A 287 ? 0.4217 0.6031 0.4512 0.1023  0.0013  0.0606  510  ILE A C   
2305 O O   . ILE A 287 ? 0.4253 0.5979 0.4461 0.0926  0.0172  0.0554  510  ILE A O   
2306 C CB  . ILE A 287 ? 0.3479 0.5766 0.3523 0.0790  -0.0016 0.0819  510  ILE A CB  
2307 C CG1 . ILE A 287 ? 0.3245 0.5815 0.3357 0.0628  -0.0378 0.0724  510  ILE A CG1 
2308 C CG2 . ILE A 287 ? 0.3234 0.5700 0.3514 0.1025  -0.0051 0.0845  510  ILE A CG2 
2309 C CD1 . ILE A 287 ? 0.3534 0.5881 0.3457 0.0453  -0.0369 0.0745  510  ILE A CD1 
2310 N N   . ASN A 288 ? 0.4884 0.6320 0.5187 0.1223  0.0104  0.0505  511  ASN A N   
2311 C CA  . ASN A 288 ? 0.5889 0.6699 0.6037 0.1411  0.0359  0.0466  511  ASN A CA  
2312 C C   . ASN A 288 ? 0.5472 0.6541 0.5587 0.1654  0.0464  0.0452  511  ASN A C   
2313 O O   . ASN A 288 ? 0.5621 0.6513 0.5755 0.1757  0.0827  0.0591  511  ASN A O   
2318 N N   . VAL A 289 ? 0.4885 0.6419 0.5014 0.1720  0.0140  0.0388  512  VAL A N   
2319 C CA  . VAL A 289 ? 0.4715 0.6328 0.4525 0.1790  -0.0026 0.0445  512  VAL A CA  
2320 C C   . VAL A 289 ? 0.4353 0.6177 0.3843 0.1644  -0.0068 0.0380  512  VAL A C   
2321 O O   . VAL A 289 ? 0.4302 0.6127 0.3482 0.1594  -0.0145 0.0256  512  VAL A O   
2322 C CB  . VAL A 289 ? 0.5205 0.6400 0.4754 0.1804  0.0023  0.0552  512  VAL A CB  
2323 C CG1 . VAL A 289 ? 0.5580 0.6412 0.4873 0.1771  0.0202  0.0614  512  VAL A CG1 
2324 C CG2 . VAL A 289 ? 0.5271 0.6422 0.4941 0.1870  0.0123  0.0508  512  VAL A CG2 
2325 N N   . PRO A 290 ? 0.4012 0.6042 0.3515 0.1685  -0.0157 0.0559  513  PRO A N   
2326 C CA  . PRO A 290 ? 0.3879 0.5987 0.3319 0.1534  -0.0054 0.0559  513  PRO A CA  
2327 C C   . PRO A 290 ? 0.3316 0.5940 0.2921 0.1364  -0.0274 0.0467  513  PRO A C   
2328 O O   . PRO A 290 ? 0.3022 0.5977 0.2779 0.1453  -0.0298 0.0481  513  PRO A O   
2329 C CB  . PRO A 290 ? 0.4004 0.5974 0.3542 0.1653  -0.0090 0.0650  513  PRO A CB  
2330 C CG  . PRO A 290 ? 0.4252 0.6008 0.3696 0.1645  0.0133  0.0666  513  PRO A CG  
2331 C CD  . PRO A 290 ? 0.4228 0.6043 0.3738 0.1655  0.0088  0.0563  513  PRO A CD  
2332 N N   . ALA A 291 ? 0.3287 0.5830 0.2713 0.0914  -0.0358 0.0166  514  ALA A N   
2333 C CA  . ALA A 291 ? 0.3485 0.5715 0.2382 0.0741  -0.0045 0.0048  514  ALA A CA  
2334 C C   . ALA A 291 ? 0.3476 0.5563 0.2431 0.0713  0.0016  -0.0044 514  ALA A C   
2335 O O   . ALA A 291 ? 0.3631 0.5608 0.2464 0.0784  0.0111  -0.0176 514  ALA A O   
2336 C CB  . ALA A 291 ? 0.3682 0.5755 0.2365 0.0530  0.0199  0.0009  514  ALA A CB  
2337 N N   . ASN A 292 ? 0.3349 0.5302 0.2348 0.0906  -0.0390 0.0161  515  ASN A N   
2338 C CA  . ASN A 292 ? 0.3374 0.5067 0.2414 0.1016  -0.0140 0.0305  515  ASN A CA  
2339 C C   . ASN A 292 ? 0.3249 0.4890 0.2109 0.0914  -0.0172 0.0273  515  ASN A C   
2340 O O   . ASN A 292 ? 0.3280 0.5036 0.2220 0.0756  -0.0251 0.0295  515  ASN A O   
2341 C CB  . ASN A 292 ? 0.3348 0.5054 0.2693 0.1204  -0.0050 0.0554  515  ASN A CB  
2342 C CG  . ASN A 292 ? 0.3513 0.5056 0.3153 0.1089  0.0294  0.0508  515  ASN A CG  
2343 O OD1 . ASN A 292 ? 0.3529 0.5097 0.3235 0.1031  0.0579  0.0424  515  ASN A OD1 
2344 N ND2 . ASN A 292 ? 0.3295 0.5062 0.3248 0.1206  0.0350  0.0519  515  ASN A ND2 
2345 N N   . GLY A 293 ? 0.2831 0.4659 0.2003 0.0942  -0.0265 0.0201  516  GLY A N   
2346 C CA  . GLY A 293 ? 0.2916 0.4430 0.2202 0.1012  -0.0465 0.0223  516  GLY A CA  
2347 C C   . GLY A 293 ? 0.2864 0.4126 0.2242 0.1095  -0.0316 0.0171  516  GLY A C   
2348 O O   . GLY A 293 ? 0.2727 0.4174 0.2259 0.0921  -0.0304 0.0118  516  GLY A O   
2349 N N   . TYR A 294 ? 0.3077 0.3595 0.2261 0.1362  -0.0040 0.0386  517  TYR A N   
2350 C CA  . TYR A 294 ? 0.3166 0.3307 0.2091 0.1585  -0.0097 0.0522  517  TYR A CA  
2351 C C   . TYR A 294 ? 0.3223 0.3149 0.1956 0.1546  -0.0155 0.0464  517  TYR A C   
2352 O O   . TYR A 294 ? 0.3407 0.3117 0.2171 0.1531  0.0034  0.0351  517  TYR A O   
2353 C CB  . TYR A 294 ? 0.3258 0.3141 0.2239 0.1625  0.0198  0.0492  517  TYR A CB  
2354 C CG  . TYR A 294 ? 0.3852 0.3192 0.2615 0.1744  -0.0004 0.0398  517  TYR A CG  
2355 C CD1 . TYR A 294 ? 0.4355 0.3260 0.2981 0.1662  0.0302  0.0088  517  TYR A CD1 
2356 C CD2 . TYR A 294 ? 0.4072 0.3183 0.3085 0.1844  -0.0131 0.0152  517  TYR A CD2 
2357 C CE1 . TYR A 294 ? 0.4748 0.3234 0.3531 0.1744  0.0381  0.0005  517  TYR A CE1 
2358 C CE2 . TYR A 294 ? 0.4644 0.3166 0.3439 0.1876  0.0213  0.0101  517  TYR A CE2 
2359 C CZ  . TYR A 294 ? 0.4964 0.3213 0.3690 0.1877  0.0230  0.0013  517  TYR A CZ  
2360 O OH  . TYR A 294 ? 0.5488 0.3319 0.4012 0.1994  0.0155  -0.0093 517  TYR A OH  
2361 N N   . PHE A 295 ? 0.3157 0.2927 0.2062 0.1630  -0.0286 0.0365  518  PHE A N   
2362 C CA  . PHE A 295 ? 0.3314 0.2796 0.2063 0.1544  -0.0195 0.0429  518  PHE A CA  
2363 C C   . PHE A 295 ? 0.3545 0.2868 0.2041 0.1510  -0.0048 0.0434  518  PHE A C   
2364 O O   . PHE A 295 ? 0.3644 0.2984 0.2212 0.1306  -0.0009 0.0139  518  PHE A O   
2365 C CB  . PHE A 295 ? 0.2813 0.2592 0.2161 0.1334  -0.0585 0.0311  518  PHE A CB  
2366 C CG  . PHE A 295 ? 0.2718 0.2721 0.2047 0.0926  -0.0442 0.0246  518  PHE A CG  
2367 C CD1 . PHE A 295 ? 0.2525 0.2787 0.2298 0.0833  -0.0213 0.0274  518  PHE A CD1 
2368 C CD2 . PHE A 295 ? 0.2596 0.2729 0.2220 0.0895  -0.0656 0.0021  518  PHE A CD2 
2369 C CE1 . PHE A 295 ? 0.2636 0.2888 0.2336 0.0732  -0.0350 0.0239  518  PHE A CE1 
2370 C CE2 . PHE A 295 ? 0.2707 0.2822 0.2421 0.0671  -0.0401 0.0002  518  PHE A CE2 
2371 C CZ  . PHE A 295 ? 0.2917 0.2839 0.2266 0.0667  -0.0282 -0.0006 518  PHE A CZ  
2372 N N   . ARG A 296 ? 0.3965 0.3084 0.2045 0.1633  -0.0073 0.0161  519  ARG A N   
2373 C CA  . ARG A 296 ? 0.4416 0.3153 0.2410 0.1737  0.0012  0.0095  519  ARG A CA  
2374 C C   . ARG A 296 ? 0.4553 0.3023 0.2245 0.1772  -0.0268 0.0023  519  ARG A C   
2375 O O   . ARG A 296 ? 0.4582 0.3001 0.2376 0.1580  -0.0466 0.0154  519  ARG A O   
2376 C CB  . ARG A 296 ? 0.4650 0.3447 0.2875 0.1834  0.0129  0.0085  519  ARG A CB  
2377 C CG  . ARG A 296 ? 0.5087 0.3757 0.3649 0.1919  0.0614  0.0171  519  ARG A CG  
2378 C CD  . ARG A 296 ? 0.5642 0.4053 0.4237 0.2022  0.1230  0.0056  519  ARG A CD  
2379 N NE  . ARG A 296 ? 0.6190 0.4267 0.4657 0.2122  0.1593  -0.0027 519  ARG A NE  
2380 C CZ  . ARG A 296 ? 0.7035 0.4564 0.5101 0.1906  0.2074  -0.0091 519  ARG A CZ  
2381 N NH1 . ARG A 296 ? 0.7220 0.4636 0.5238 0.1966  0.2131  -0.0101 519  ARG A NH1 
2382 N NH2 . ARG A 296 ? 0.7359 0.4685 0.5348 0.1838  0.2166  -0.0051 519  ARG A NH2 
2383 N N   . PHE A 297 ? 0.4718 0.2891 0.2063 0.1866  -0.0496 -0.0046 520  PHE A N   
2384 C CA  . PHE A 297 ? 0.4817 0.2935 0.1998 0.1921  -0.0502 0.0061  520  PHE A CA  
2385 C C   . PHE A 297 ? 0.5327 0.3119 0.2150 0.1787  -0.0276 -0.0155 520  PHE A C   
2386 O O   . PHE A 297 ? 0.5860 0.3050 0.2305 0.1735  -0.0366 -0.0373 520  PHE A O   
2387 C CB  . PHE A 297 ? 0.4840 0.2975 0.2340 0.1724  -0.0774 0.0181  520  PHE A CB  
2388 C CG  . PHE A 297 ? 0.4767 0.3220 0.2500 0.1258  -0.0923 -0.0064 520  PHE A CG  
2389 C CD1 . PHE A 297 ? 0.4682 0.3248 0.2497 0.1072  -0.0848 0.0012  520  PHE A CD1 
2390 C CD2 . PHE A 297 ? 0.4844 0.3338 0.2525 0.0978  -0.1072 0.0000  520  PHE A CD2 
2391 C CE1 . PHE A 297 ? 0.4749 0.3309 0.2646 0.0940  -0.0773 -0.0008 520  PHE A CE1 
2392 C CE2 . PHE A 297 ? 0.4998 0.3495 0.2987 0.0870  -0.0853 0.0019  520  PHE A CE2 
2393 C CZ  . PHE A 297 ? 0.4971 0.3433 0.2950 0.0860  -0.0653 0.0023  520  PHE A CZ  
2394 N N   . ASP A 298 ? 0.5013 0.3287 0.1879 0.1739  0.0073  -0.0151 521  ASP A N   
2395 C CA  A ASP A 298 ? 0.5044 0.3429 0.1942 0.1734  0.0203  -0.0193 521  ASP A CA  
2396 C CA  B ASP A 298 ? 0.5008 0.3334 0.2222 0.1820  0.0182  -0.0082 521  ASP A CA  
2397 C C   . ASP A 298 ? 0.5137 0.3257 0.2113 0.1765  0.0161  -0.0168 521  ASP A C   
2398 O O   . ASP A 298 ? 0.5717 0.3239 0.2250 0.1711  0.0198  -0.0415 521  ASP A O   
2399 C CB  A ASP A 298 ? 0.5175 0.3742 0.2215 0.1588  0.0195  -0.0015 521  ASP A CB  
2400 C CB  B ASP A 298 ? 0.5007 0.3427 0.2838 0.1899  0.0236  0.0237  521  ASP A CB  
2401 C CG  A ASP A 298 ? 0.5216 0.3944 0.2628 0.1498  0.0162  0.0145  521  ASP A CG  
2402 C CG  B ASP A 298 ? 0.5050 0.3494 0.3421 0.1919  0.0304  0.0526  521  ASP A CG  
2403 O OD1 A ASP A 298 ? 0.5330 0.4053 0.2843 0.1416  0.0042  0.0113  521  ASP A OD1 
2404 O OD1 B ASP A 298 ? 0.5118 0.3564 0.3758 0.1925  0.0436  0.0606  521  ASP A OD1 
2405 O OD2 A ASP A 298 ? 0.5270 0.4083 0.2839 0.1620  0.0216  0.0329  521  ASP A OD2 
2406 O OD2 B ASP A 298 ? 0.5003 0.3481 0.3669 0.1977  0.0258  0.0656  521  ASP A OD2 
2407 N N   . SER A 299 ? 0.4716 0.3013 0.1958 0.1590  -0.0124 0.0022  522  SER A N   
2408 C CA  . SER A 299 ? 0.4505 0.3020 0.2157 0.1522  -0.0473 -0.0055 522  SER A CA  
2409 C C   . SER A 299 ? 0.4478 0.2811 0.2039 0.1429  -0.0492 -0.0065 522  SER A C   
2410 O O   . SER A 299 ? 0.4471 0.2844 0.2101 0.1263  -0.0462 0.0029  522  SER A O   
2411 C CB  . SER A 299 ? 0.4529 0.3245 0.2594 0.1290  -0.0249 -0.0123 522  SER A CB  
2412 O OG  . SER A 299 ? 0.4846 0.3509 0.2684 0.1093  -0.0079 -0.0281 522  SER A OG  
2413 N N   . TRP A 300 ? 0.4555 0.2612 0.1872 0.1438  -0.0497 -0.0188 523  TRP A N   
2414 C CA  . TRP A 300 ? 0.4517 0.2642 0.1626 0.1380  -0.0596 -0.0221 523  TRP A CA  
2415 C C   . TRP A 300 ? 0.4728 0.2703 0.1629 0.1382  -0.0205 -0.0284 523  TRP A C   
2416 O O   . TRP A 300 ? 0.5281 0.2986 0.1943 0.1222  0.0242  -0.0278 523  TRP A O   
2417 C CB  . TRP A 300 ? 0.4543 0.2721 0.1822 0.1133  -0.0419 0.0005  523  TRP A CB  
2418 C CG  . TRP A 300 ? 0.4655 0.2795 0.1838 0.1025  -0.0744 -0.0056 523  TRP A CG  
2419 C CD1 . TRP A 300 ? 0.4915 0.2877 0.1989 0.0913  -0.0593 -0.0285 523  TRP A CD1 
2420 C CD2 . TRP A 300 ? 0.4615 0.2915 0.1655 0.0816  -0.0854 -0.0124 523  TRP A CD2 
2421 N NE1 . TRP A 300 ? 0.4970 0.2894 0.1858 0.0972  -0.0736 -0.0243 523  TRP A NE1 
2422 C CE2 . TRP A 300 ? 0.4789 0.2859 0.1787 0.0876  -0.0926 -0.0125 523  TRP A CE2 
2423 C CE3 . TRP A 300 ? 0.4553 0.2962 0.1672 0.0861  -0.0791 -0.0062 523  TRP A CE3 
2424 C CZ2 . TRP A 300 ? 0.4732 0.2834 0.2041 0.1002  -0.0850 0.0074  523  TRP A CZ2 
2425 C CZ3 . TRP A 300 ? 0.4692 0.3021 0.1694 0.0918  -0.0776 0.0143  523  TRP A CZ3 
2426 C CH2 . TRP A 300 ? 0.4719 0.2823 0.1869 0.1101  -0.0678 0.0118  523  TRP A CH2 
2427 N N   . VAL A 301 ? 0.4500 0.2703 0.1646 0.1382  -0.0348 0.0017  524  VAL A N   
2428 C CA  . VAL A 301 ? 0.4410 0.2840 0.1891 0.1293  -0.0220 -0.0007 524  VAL A CA  
2429 C C   . VAL A 301 ? 0.4472 0.2926 0.2360 0.1363  -0.0313 0.0144  524  VAL A C   
2430 O O   . VAL A 301 ? 0.4772 0.2937 0.2684 0.1327  -0.0258 0.0076  524  VAL A O   
2431 C CB  . VAL A 301 ? 0.4047 0.2938 0.1958 0.1222  -0.0185 -0.0082 524  VAL A CB  
2432 C CG1 . VAL A 301 ? 0.4032 0.3079 0.2053 0.1098  -0.0165 -0.0163 524  VAL A CG1 
2433 C CG2 . VAL A 301 ? 0.4038 0.3079 0.2031 0.1054  -0.0016 -0.0160 524  VAL A CG2 
2434 N N   . SER A 302 ? 0.4372 0.3117 0.3259 0.1492  -0.0293 0.0480  525  SER A N   
2435 C CA  . SER A 302 ? 0.4085 0.3314 0.3295 0.1506  -0.0571 0.0679  525  SER A CA  
2436 C C   . SER A 302 ? 0.3702 0.3125 0.3120 0.1684  -0.0508 0.0725  525  SER A C   
2437 O O   . SER A 302 ? 0.3670 0.3102 0.2847 0.1409  -0.0330 0.0437  525  SER A O   
2438 C CB  . SER A 302 ? 0.4542 0.3707 0.3322 0.1165  -0.0517 0.0716  525  SER A CB  
2439 O OG  . SER A 302 ? 0.4921 0.3898 0.3299 0.0776  -0.0528 0.0702  525  SER A OG  
2440 N N   . GLN A 303 ? 0.3717 0.3159 0.3348 0.1623  -0.0425 0.0704  526  GLN A N   
2441 C CA  . GLN A 303 ? 0.3899 0.3383 0.3644 0.1377  -0.0249 0.0597  526  GLN A CA  
2442 C C   . GLN A 303 ? 0.4338 0.3779 0.3601 0.1186  0.0136  0.0498  526  GLN A C   
2443 O O   . GLN A 303 ? 0.4289 0.3790 0.3707 0.1064  0.0288  0.0297  526  GLN A O   
2444 C CB  . GLN A 303 ? 0.3900 0.3329 0.4104 0.1311  -0.0480 0.0716  526  GLN A CB  
2445 C CG  . GLN A 303 ? 0.3992 0.3304 0.4713 0.1317  -0.0459 0.0777  526  GLN A CG  
2446 C CD  . GLN A 303 ? 0.4175 0.3117 0.4991 0.1163  -0.0626 0.0793  526  GLN A CD  
2447 O OE1 . GLN A 303 ? 0.4148 0.3303 0.5228 0.1313  -0.1039 0.0769  526  GLN A OE1 
2448 N NE2 . GLN A 303 ? 0.3999 0.2916 0.4786 0.0906  -0.0824 0.0867  526  GLN A NE2 
2449 N N   . PHE A 304 ? 0.4578 0.4095 0.3076 0.1279  0.0074  0.0698  527  PHE A N   
2450 C CA  . PHE A 304 ? 0.4976 0.4564 0.2981 0.1369  -0.0113 0.0876  527  PHE A CA  
2451 C C   . PHE A 304 ? 0.4653 0.4632 0.2963 0.0942  0.0216  0.0572  527  PHE A C   
2452 O O   . PHE A 304 ? 0.4766 0.4791 0.3113 0.0734  0.0281  0.0303  527  PHE A O   
2453 C CB  . PHE A 304 ? 0.5654 0.4961 0.2917 0.1796  -0.0394 0.1304  527  PHE A CB  
2454 C CG  . PHE A 304 ? 0.6666 0.5440 0.3078 0.1964  -0.0157 0.1468  527  PHE A CG  
2455 C CD1 . PHE A 304 ? 0.7068 0.5615 0.3081 0.2066  0.0028  0.1535  527  PHE A CD1 
2456 C CD2 . PHE A 304 ? 0.7042 0.5610 0.3227 0.2082  -0.0150 0.1582  527  PHE A CD2 
2457 C CE1 . PHE A 304 ? 0.7299 0.5740 0.3155 0.2126  0.0135  0.1494  527  PHE A CE1 
2458 C CE2 . PHE A 304 ? 0.7424 0.5760 0.3433 0.2077  0.0094  0.1475  527  PHE A CE2 
2459 C CZ  . PHE A 304 ? 0.7453 0.5782 0.3332 0.2112  0.0237  0.1429  527  PHE A CZ  
2460 N N   . TYR A 305 ? 0.4262 0.4591 0.2764 0.0782  0.0437  0.0606  528  TYR A N   
2461 C CA  . TYR A 305 ? 0.3943 0.4704 0.2962 0.0696  0.0621  0.0693  528  TYR A CA  
2462 C C   . TYR A 305 ? 0.4085 0.4790 0.2919 0.0534  0.0738  0.0762  528  TYR A C   
2463 O O   . TYR A 305 ? 0.4298 0.4735 0.2790 0.0659  0.0986  0.0810  528  TYR A O   
2464 C CB  . TYR A 305 ? 0.3770 0.4746 0.3340 0.0790  0.0625  0.0698  528  TYR A CB  
2465 C CG  . TYR A 305 ? 0.3623 0.4789 0.3806 0.0974  0.0932  0.0890  528  TYR A CG  
2466 C CD1 . TYR A 305 ? 0.3538 0.4821 0.4008 0.1062  0.1245  0.0929  528  TYR A CD1 
2467 C CD2 . TYR A 305 ? 0.3498 0.4833 0.3931 0.1124  0.0974  0.0933  528  TYR A CD2 
2468 C CE1 . TYR A 305 ? 0.3696 0.4940 0.4249 0.1073  0.1308  0.0929  528  TYR A CE1 
2469 C CE2 . TYR A 305 ? 0.3568 0.4868 0.4110 0.1159  0.0967  0.1021  528  TYR A CE2 
2470 C CZ  . TYR A 305 ? 0.3780 0.4945 0.4359 0.1052  0.1084  0.0901  528  TYR A CZ  
2471 O OH  . TYR A 305 ? 0.4211 0.5014 0.4660 0.1033  0.1200  0.0746  528  TYR A OH  
2472 N N   . SER A 306 ? 0.4137 0.4961 0.3084 0.0289  0.0622  0.0901  529  SER A N   
2473 C CA  . SER A 306 ? 0.4125 0.5052 0.3209 0.0286  0.0633  0.0939  529  SER A CA  
2474 C C   . SER A 306 ? 0.3946 0.5062 0.2861 0.0389  0.0487  0.0918  529  SER A C   
2475 O O   . SER A 306 ? 0.4396 0.5084 0.2874 0.0477  0.0496  0.0894  529  SER A O   
2476 C CB  . SER A 306 ? 0.4341 0.5194 0.3428 0.0104  0.0625  0.0932  529  SER A CB  
2477 O OG  . SER A 306 ? 0.4406 0.5327 0.3821 -0.0015 0.0540  0.0804  529  SER A OG  
2478 N N   . LEU A 307 ? 0.3596 0.5023 0.2647 0.0121  0.0611  0.0788  530  LEU A N   
2479 C CA  . LEU A 307 ? 0.3427 0.5016 0.2521 0.0003  0.0646  0.0660  530  LEU A CA  
2480 C C   . LEU A 307 ? 0.3802 0.5110 0.2772 -0.0060 0.0923  0.0644  530  LEU A C   
2481 O O   . LEU A 307 ? 0.3744 0.5130 0.2756 -0.0363 0.0935  0.0672  530  LEU A O   
2482 C CB  . LEU A 307 ? 0.3184 0.4934 0.2117 -0.0020 0.0571  0.0600  530  LEU A CB  
2483 C CG  . LEU A 307 ? 0.3179 0.4762 0.2167 -0.0065 0.0511  0.0518  530  LEU A CG  
2484 C CD1 . LEU A 307 ? 0.3027 0.4764 0.1811 -0.0090 0.0561  0.0563  530  LEU A CD1 
2485 C CD2 . LEU A 307 ? 0.3279 0.4647 0.2182 0.0162  0.0152  0.0611  530  LEU A CD2 
2486 N N   . ALA A 308 ? 0.3863 0.5179 0.2993 0.0246  0.1025  0.0396  531  ALA A N   
2487 C CA  . ALA A 308 ? 0.4098 0.5355 0.3309 0.0366  0.1281  0.0443  531  ALA A CA  
2488 C C   . ALA A 308 ? 0.4276 0.5493 0.3284 0.0427  0.1267  0.0660  531  ALA A C   
2489 O O   . ALA A 308 ? 0.4096 0.5425 0.3046 0.0409  0.1303  0.0796  531  ALA A O   
2490 C CB  . ALA A 308 ? 0.4145 0.5351 0.3519 0.0379  0.1282  0.0355  531  ALA A CB  
2491 N N   . PRO A 309 ? 0.4651 0.5696 0.3611 0.0241  0.1209  0.0468  532  PRO A N   
2492 C CA  . PRO A 309 ? 0.5242 0.5952 0.3863 0.0064  0.1156  0.0330  532  PRO A CA  
2493 C C   . PRO A 309 ? 0.6136 0.6310 0.4303 -0.0094 0.1146  0.0158  532  PRO A C   
2494 O O   . PRO A 309 ? 0.6577 0.6352 0.4372 -0.0051 0.1089  0.0119  532  PRO A O   
2495 C CB  . PRO A 309 ? 0.5030 0.5887 0.3878 0.0093  0.1122  0.0262  532  PRO A CB  
2496 C CG  . PRO A 309 ? 0.4903 0.5836 0.3903 0.0136  0.1015  0.0300  532  PRO A CG  
2497 C CD  . PRO A 309 ? 0.4750 0.5751 0.3774 0.0180  0.1215  0.0286  532  PRO A CD  
2498 N N   . MET A 310 ? 0.6328 0.6639 0.4595 -0.0254 0.1106  0.0223  533  MET A N   
2499 C CA  . MET A 310 ? 0.6384 0.6941 0.5064 -0.0401 0.0981  0.0248  533  MET A CA  
2500 C C   . MET A 310 ? 0.6268 0.7090 0.5230 -0.0480 0.0678  0.0115  533  MET A C   
2501 O O   . MET A 310 ? 0.6154 0.7186 0.5325 -0.0494 0.0493  0.0105  533  MET A O   
2502 C CB  . MET A 310 ? 0.6359 0.7024 0.5229 -0.0455 0.0976  0.0513  533  MET A CB  
2503 C CG  . MET A 310 ? 0.6146 0.7079 0.5221 -0.0479 0.0800  0.0791  533  MET A CG  
2504 S SD  . MET A 310 ? 0.5831 0.7102 0.5181 -0.0400 0.0581  0.1066  533  MET A SD  
2505 C CE  . MET A 310 ? 0.5911 0.7131 0.4973 -0.0515 0.0777  0.1145  533  MET A CE  
2511 N N   . LYS B 2   ? 0.4622 0.4833 0.4173 -0.0576 -0.0589 -0.0772 225  LYS B N   
2512 C CA  . LYS B 2   ? 0.4639 0.4824 0.3557 -0.0591 -0.0499 -0.0742 225  LYS B CA  
2513 C C   . LYS B 2   ? 0.4344 0.4668 0.2893 -0.0302 -0.0312 -0.0438 225  LYS B C   
2514 O O   . LYS B 2   ? 0.4189 0.4678 0.3052 -0.0185 -0.0216 -0.0464 225  LYS B O   
2515 C CB  . LYS B 2   ? 0.4988 0.4946 0.3589 -0.0809 -0.0532 -0.1030 225  LYS B CB  
2516 C CG  . LYS B 2   ? 0.5368 0.5112 0.3691 -0.0926 -0.0216 -0.1257 225  LYS B CG  
2517 C CD  . LYS B 2   ? 0.5745 0.5228 0.3712 -0.1073 0.0047  -0.1353 225  LYS B CD  
2518 C CE  . LYS B 2   ? 0.6194 0.5271 0.3750 -0.1191 0.0437  -0.1367 225  LYS B CE  
2519 N NZ  . LYS B 2   ? 0.6461 0.5293 0.3879 -0.1311 0.0772  -0.1256 225  LYS B NZ  
2520 N N   . PRO B 3   ? 0.4553 0.4439 0.2366 -0.0125 0.0067  -0.0161 226  PRO B N   
2521 C CA  . PRO B 3   ? 0.4450 0.4135 0.2320 0.0060  0.0023  -0.0096 226  PRO B CA  
2522 C C   . PRO B 3   ? 0.4208 0.3620 0.2048 0.0081  -0.0114 -0.0035 226  PRO B C   
2523 O O   . PRO B 3   ? 0.4298 0.3561 0.2159 -0.0248 -0.0032 -0.0173 226  PRO B O   
2524 C CB  . PRO B 3   ? 0.4822 0.4378 0.2356 0.0123  0.0037  -0.0001 226  PRO B CB  
2525 C CG  . PRO B 3   ? 0.5105 0.4640 0.2709 0.0022  0.0129  0.0146  226  PRO B CG  
2526 C CD  . PRO B 3   ? 0.4851 0.4625 0.2418 -0.0158 -0.0137 0.0028  226  PRO B CD  
2527 N N   . PHE B 4   ? 0.3648 0.3019 0.1872 0.0191  0.0034  -0.0095 227  PHE B N   
2528 C CA  . PHE B 4   ? 0.3479 0.2510 0.1908 0.0346  -0.0239 -0.0104 227  PHE B CA  
2529 C C   . PHE B 4   ? 0.3857 0.2427 0.2243 0.0309  -0.0634 -0.0241 227  PHE B C   
2530 O O   . PHE B 4   ? 0.4309 0.2528 0.2577 0.0280  -0.0436 -0.0264 227  PHE B O   
2531 C CB  . PHE B 4   ? 0.3398 0.2427 0.1692 0.0237  -0.0112 -0.0011 227  PHE B CB  
2532 C CG  . PHE B 4   ? 0.3199 0.2324 0.1544 0.0299  -0.0267 -0.0023 227  PHE B CG  
2533 C CD1 . PHE B 4   ? 0.3136 0.2208 0.1608 0.0181  -0.0664 0.0081  227  PHE B CD1 
2534 C CD2 . PHE B 4   ? 0.3317 0.2278 0.1726 0.0195  -0.0551 -0.0071 227  PHE B CD2 
2535 C CE1 . PHE B 4   ? 0.3381 0.2214 0.1891 0.0163  -0.0413 0.0116  227  PHE B CE1 
2536 C CE2 . PHE B 4   ? 0.3525 0.2140 0.1557 0.0090  -0.0802 -0.0017 227  PHE B CE2 
2537 C CZ  . PHE B 4   ? 0.3317 0.2061 0.1719 0.0067  -0.0919 -0.0049 227  PHE B CZ  
2538 N N   . THR B 5   ? 0.3997 0.2149 0.2055 0.0354  -0.0539 -0.0190 228  THR B N   
2539 C CA  . THR B 5   ? 0.4315 0.2234 0.1810 0.0305  -0.0417 -0.0013 228  THR B CA  
2540 C C   . THR B 5   ? 0.3985 0.2071 0.1714 0.0268  -0.0807 0.0094  228  THR B C   
2541 O O   . THR B 5   ? 0.3881 0.2114 0.2036 0.0173  -0.0757 0.0252  228  THR B O   
2542 C CB  . THR B 5   ? 0.4917 0.2469 0.1891 0.0185  -0.0402 0.0182  228  THR B CB  
2543 O OG1 . THR B 5   ? 0.5234 0.2642 0.2076 -0.0006 -0.0358 0.0098  228  THR B OG1 
2544 C CG2 . THR B 5   ? 0.5127 0.2575 0.1897 0.0074  -0.0450 -0.0028 228  THR B CG2 
2545 N N   . ILE B 6   ? 0.3696 0.2000 0.1837 0.0227  -0.0853 -0.0018 229  ILE B N   
2546 C CA  . ILE B 6   ? 0.3916 0.2014 0.1934 0.0269  -0.0530 0.0050  229  ILE B CA  
2547 C C   . ILE B 6   ? 0.3421 0.2051 0.1825 0.0157  -0.0580 0.0076  229  ILE B C   
2548 O O   . ILE B 6   ? 0.3024 0.2196 0.1844 -0.0213 -0.0590 0.0113  229  ILE B O   
2549 C CB  . ILE B 6   ? 0.4717 0.2072 0.2113 0.0428  -0.0301 -0.0116 229  ILE B CB  
2550 C CG1 . ILE B 6   ? 0.5444 0.2244 0.2385 0.0394  0.0114  -0.0006 229  ILE B CG1 
2551 C CG2 . ILE B 6   ? 0.4727 0.2172 0.2255 0.0290  -0.0249 -0.0116 229  ILE B CG2 
2552 C CD1 . ILE B 6   ? 0.5949 0.2521 0.2896 0.0466  0.0465  -0.0060 229  ILE B CD1 
2553 N N   . PRO B 7   ? 0.2907 0.1934 0.1682 0.0180  -0.0857 0.0052  230  PRO B N   
2554 C CA  . PRO B 7   ? 0.2668 0.1947 0.2121 0.0285  -0.0950 -0.0010 230  PRO B CA  
2555 C C   . PRO B 7   ? 0.2883 0.2192 0.2409 0.0201  -0.0794 -0.0198 230  PRO B C   
2556 O O   . PRO B 7   ? 0.2980 0.2449 0.2248 0.0353  -0.0955 0.0108  230  PRO B O   
2557 C CB  . PRO B 7   ? 0.2574 0.1928 0.2130 0.0084  -0.1043 -0.0032 230  PRO B CB  
2558 C CG  . PRO B 7   ? 0.2712 0.1753 0.2018 0.0152  -0.0758 0.0109  230  PRO B CG  
2559 C CD  . PRO B 7   ? 0.2844 0.1868 0.1786 0.0108  -0.0719 -0.0084 230  PRO B CD  
2560 N N   A ILE B 8   ? 0.2896 0.2032 0.2428 0.0448  -0.0731 -0.0282 231  ILE B N   
2561 N N   B ILE B 8   ? 0.2851 0.2111 0.2236 0.0384  -0.0757 -0.0328 231  ILE B N   
2562 C CA  A ILE B 8   ? 0.3118 0.2138 0.2353 0.0363  -0.0907 -0.0069 231  ILE B CA  
2563 C CA  B ILE B 8   ? 0.3071 0.2278 0.2056 0.0247  -0.0966 -0.0190 231  ILE B CA  
2564 C C   A ILE B 8   ? 0.3120 0.1925 0.2052 0.0139  -0.1095 0.0032  231  ILE B C   
2565 C C   B ILE B 8   ? 0.3264 0.2171 0.2067 0.0203  -0.0816 -0.0097 231  ILE B C   
2566 O O   A ILE B 8   ? 0.3175 0.1874 0.2178 -0.0092 -0.1425 0.0194  231  ILE B O   
2567 O O   B ILE B 8   ? 0.3568 0.2411 0.2504 0.0096  -0.0655 -0.0095 231  ILE B O   
2568 C CB  A ILE B 8   ? 0.3539 0.2341 0.2726 0.0575  -0.0636 0.0014  231  ILE B CB  
2569 C CB  B ILE B 8   ? 0.3379 0.2423 0.2133 0.0279  -0.0880 -0.0163 231  ILE B CB  
2570 C CG1 A ILE B 8   ? 0.3665 0.2481 0.2804 0.0640  -0.0545 0.0178  231  ILE B CG1 
2571 C CG1 B ILE B 8   ? 0.3403 0.2499 0.2199 0.0258  -0.1006 0.0141  231  ILE B CG1 
2572 C CG2 A ILE B 8   ? 0.3562 0.2392 0.2804 0.0618  -0.0734 -0.0067 231  ILE B CG2 
2573 C CG2 B ILE B 8   ? 0.3327 0.2435 0.1968 0.0254  -0.1022 -0.0368 231  ILE B CG2 
2574 C CD1 A ILE B 8   ? 0.3739 0.2546 0.2905 0.0691  -0.0242 0.0179  231  ILE B CD1 
2575 C CD1 B ILE B 8   ? 0.3459 0.2543 0.2355 0.0237  -0.0926 0.0426  231  ILE B CD1 
2576 N N   . LEU B 9   ? 0.3178 0.1842 0.1372 0.0082  -0.0861 -0.0173 232  LEU B N   
2577 C CA  . LEU B 9   ? 0.2551 0.1596 0.1970 0.0121  -0.1048 -0.0015 232  LEU B CA  
2578 C C   . LEU B 9   ? 0.2207 0.1461 0.1879 0.0295  -0.1165 -0.0012 232  LEU B C   
2579 O O   . LEU B 9   ? 0.2730 0.1233 0.1844 0.0250  -0.0862 -0.0018 232  LEU B O   
2580 C CB  . LEU B 9   ? 0.2354 0.1785 0.2182 -0.0062 -0.0998 -0.0013 232  LEU B CB  
2581 C CG  . LEU B 9   ? 0.2197 0.2035 0.2361 -0.0024 -0.1080 0.0116  232  LEU B CG  
2582 C CD1 . LEU B 9   ? 0.2577 0.2381 0.2428 -0.0013 -0.0968 0.0137  232  LEU B CD1 
2583 C CD2 . LEU B 9   ? 0.2715 0.1979 0.2822 -0.0127 -0.0565 0.0238  232  LEU B CD2 
2584 N N   . THR B 10  ? 0.2250 0.1464 0.2260 0.0075  -0.0739 -0.0134 233  THR B N   
2585 C CA  . THR B 10  ? 0.2274 0.1545 0.2572 0.0547  -0.0950 -0.0084 233  THR B CA  
2586 C C   . THR B 10  ? 0.2550 0.1531 0.2265 0.0406  -0.1073 -0.0562 233  THR B C   
2587 O O   . THR B 10  ? 0.2638 0.1339 0.2250 0.0340  -0.1002 -0.0428 233  THR B O   
2588 C CB  . THR B 10  ? 0.2614 0.1605 0.3068 0.0436  -0.0911 0.0108  233  THR B CB  
2589 O OG1 . THR B 10  ? 0.2650 0.1628 0.3555 0.0281  -0.0876 0.0132  233  THR B OG1 
2590 C CG2 . THR B 10  ? 0.2535 0.1766 0.3106 0.0404  -0.1292 0.0295  233  THR B CG2 
2591 N N   . ILE B 11  ? 0.3030 0.1718 0.2259 0.0464  -0.0704 -0.0627 234  ILE B N   
2592 C CA  . ILE B 11  ? 0.3289 0.2277 0.2681 0.0385  -0.0440 -0.0578 234  ILE B CA  
2593 C C   . ILE B 11  ? 0.2805 0.2398 0.2816 0.0215  -0.0735 -0.0878 234  ILE B C   
2594 O O   . ILE B 11  ? 0.2833 0.2582 0.2851 -0.0007 -0.0393 -0.0913 234  ILE B O   
2595 C CB  . ILE B 11  ? 0.3756 0.2662 0.3138 0.0233  -0.0269 -0.0518 234  ILE B CB  
2596 C CG1 . ILE B 11  ? 0.3848 0.2721 0.3455 0.0534  -0.0419 -0.0255 234  ILE B CG1 
2597 C CG2 . ILE B 11  ? 0.4084 0.3129 0.3578 0.0262  0.0217  -0.0484 234  ILE B CG2 
2598 C CD1 . ILE B 11  ? 0.3680 0.2681 0.3510 0.0720  -0.0484 -0.0145 234  ILE B CD1 
2599 N N   . GLY B 12  ? 0.2664 0.2033 0.3401 0.0354  -0.0582 -0.1108 235  GLY B N   
2600 C CA  . GLY B 12  ? 0.2679 0.1932 0.3650 0.0212  -0.0255 -0.1422 235  GLY B CA  
2601 C C   . GLY B 12  ? 0.2495 0.1791 0.3778 0.0217  -0.0475 -0.1137 235  GLY B C   
2602 O O   . GLY B 12  ? 0.2500 0.1994 0.4636 0.0197  -0.0262 -0.1198 235  GLY B O   
2603 N N   . GLU B 13  ? 0.2276 0.1659 0.2927 0.0257  -0.1141 -0.0461 236  GLU B N   
2604 C CA  . GLU B 13  ? 0.2161 0.1640 0.2505 0.0347  -0.1335 -0.0100 236  GLU B CA  
2605 C C   . GLU B 13  ? 0.1990 0.1408 0.2197 0.0442  -0.1080 0.0016  236  GLU B C   
2606 O O   . GLU B 13  ? 0.2388 0.1712 0.2503 0.0375  -0.0864 0.0178  236  GLU B O   
2607 C CB  . GLU B 13  ? 0.2283 0.1720 0.2814 0.0229  -0.1462 0.0026  236  GLU B CB  
2608 C CG  . GLU B 13  ? 0.2468 0.1645 0.3035 0.0274  -0.1522 0.0092  236  GLU B CG  
2609 C CD  . GLU B 13  ? 0.2849 0.1700 0.3231 0.0358  -0.1595 0.0169  236  GLU B CD  
2610 O OE1 . GLU B 13  ? 0.2925 0.1750 0.3108 0.0536  -0.1561 0.0025  236  GLU B OE1 
2611 O OE2 . GLU B 13  ? 0.3272 0.1839 0.3594 0.0421  -0.1710 0.0257  236  GLU B OE2 
2612 N N   . MET B 14  ? 0.1967 0.1197 0.1920 0.0244  -0.0999 -0.0062 237  MET B N   
2613 C CA  . MET B 14  ? 0.1793 0.1128 0.1631 0.0216  -0.0863 -0.0159 237  MET B CA  
2614 C C   . MET B 14  ? 0.1657 0.1105 0.1477 0.0249  -0.0627 -0.0168 237  MET B C   
2615 O O   . MET B 14  ? 0.1747 0.1262 0.1669 0.0226  -0.0413 -0.0312 237  MET B O   
2616 C CB  . MET B 14  ? 0.2047 0.1310 0.1653 0.0047  -0.0883 -0.0285 237  MET B CB  
2617 C CG  . MET B 14  ? 0.2289 0.1321 0.1788 0.0326  -0.0920 -0.0238 237  MET B CG  
2618 S SD  . MET B 14  ? 0.2488 0.1281 0.2053 0.0329  -0.0715 -0.0145 237  MET B SD  
2619 C CE  . MET B 14  ? 0.2330 0.1251 0.2149 0.0150  -0.0631 -0.0089 237  MET B CE  
2620 N N   . THR B 15  ? 0.1745 0.1051 0.1440 0.0261  -0.0546 0.0245  238  THR B N   
2621 C CA  . THR B 15  ? 0.1521 0.0942 0.1416 -0.0008 -0.0677 0.0155  238  THR B CA  
2622 C C   . THR B 15  ? 0.1733 0.0809 0.1388 0.0093  -0.0328 -0.0222 238  THR B C   
2623 O O   . THR B 15  ? 0.1665 0.0947 0.1594 0.0255  -0.0537 -0.0253 238  THR B O   
2624 C CB  . THR B 15  ? 0.1800 0.0962 0.1641 -0.0056 -0.0634 0.0145  238  THR B CB  
2625 O OG1 . THR B 15  ? 0.1818 0.0999 0.2203 0.0138  -0.0570 0.0383  238  THR B OG1 
2626 C CG2 . THR B 15  ? 0.1948 0.0995 0.1702 -0.0186 -0.0962 0.0251  238  THR B CG2 
2627 N N   . ASN B 16  ? 0.1580 0.0856 0.1261 -0.0020 -0.0484 0.0227  239  ASN B N   
2628 C CA  . ASN B 16  ? 0.1688 0.0811 0.1385 0.0207  -0.0379 -0.0011 239  ASN B CA  
2629 C C   . ASN B 16  ? 0.1677 0.0802 0.1600 0.0301  -0.0425 0.0092  239  ASN B C   
2630 O O   . ASN B 16  ? 0.1762 0.0989 0.1855 0.0033  -0.0423 0.0014  239  ASN B O   
2631 C CB  . ASN B 16  ? 0.1790 0.0931 0.1194 0.0049  -0.0192 0.0024  239  ASN B CB  
2632 C CG  . ASN B 16  ? 0.1656 0.1009 0.1486 0.0127  -0.0331 0.0030  239  ASN B CG  
2633 O OD1 . ASN B 16  ? 0.1879 0.1212 0.1479 0.0007  -0.0393 -0.0119 239  ASN B OD1 
2634 N ND2 . ASN B 16  ? 0.1647 0.1079 0.1653 0.0042  -0.0391 -0.0017 239  ASN B ND2 
2635 N N   . SER B 17  ? 0.1458 0.0896 0.1567 0.0149  -0.0751 0.0058  240  SER B N   
2636 C CA  . SER B 17  ? 0.1565 0.0772 0.1417 0.0103  -0.0466 -0.0115 240  SER B CA  
2637 C C   . SER B 17  ? 0.1382 0.0829 0.1345 0.0168  -0.0582 0.0068  240  SER B C   
2638 O O   . SER B 17  ? 0.1658 0.0983 0.1465 0.0121  -0.0414 -0.0046 240  SER B O   
2639 C CB  . SER B 17  ? 0.1570 0.0768 0.1475 -0.0018 -0.0361 -0.0182 240  SER B CB  
2640 O OG  . SER B 17  ? 0.1755 0.0810 0.1615 -0.0049 -0.0418 0.0014  240  SER B OG  
2641 N N   . ARG B 18  ? 0.1945 0.0716 0.1213 0.0188  -0.0315 0.0032  241  ARG B N   
2642 C CA  . ARG B 18  ? 0.1847 0.0707 0.1488 0.0007  -0.0440 0.0129  241  ARG B CA  
2643 C C   . ARG B 18  ? 0.1710 0.0808 0.1680 0.0108  -0.0608 0.0050  241  ARG B C   
2644 O O   . ARG B 18  ? 0.1848 0.0916 0.1643 -0.0200 -0.0562 0.0094  241  ARG B O   
2645 C CB  . ARG B 18  ? 0.1831 0.0614 0.1555 -0.0137 -0.0210 0.0110  241  ARG B CB  
2646 C CG  . ARG B 18  ? 0.1995 0.0674 0.1140 0.0017  -0.0395 -0.0016 241  ARG B CG  
2647 C CD  . ARG B 18  ? 0.1881 0.0807 0.1071 0.0041  -0.0339 0.0198  241  ARG B CD  
2648 N NE  . ARG B 18  ? 0.1927 0.1025 0.1278 -0.0087 -0.0422 0.0166  241  ARG B NE  
2649 C CZ  . ARG B 18  ? 0.1619 0.0980 0.1446 0.0036  -0.0465 0.0301  241  ARG B CZ  
2650 N NH1 . ARG B 18  ? 0.1682 0.1081 0.1617 -0.0081 -0.0481 0.0048  241  ARG B NH1 
2651 N NH2 . ARG B 18  ? 0.1740 0.1246 0.1445 0.0081  -0.0544 0.0177  241  ARG B NH2 
2652 N N   . PHE B 19  ? 0.1822 0.0678 0.1619 0.0048  -0.0436 0.0019  242  PHE B N   
2653 C CA  . PHE B 19  ? 0.2024 0.0844 0.1336 -0.0104 -0.0325 -0.0021 242  PHE B CA  
2654 C C   . PHE B 19  ? 0.1745 0.0829 0.1459 -0.0090 -0.0459 -0.0100 242  PHE B C   
2655 O O   . PHE B 19  ? 0.2091 0.0793 0.1602 0.0076  -0.0830 -0.0147 242  PHE B O   
2656 C CB  . PHE B 19  ? 0.1887 0.0863 0.1489 -0.0290 -0.0615 -0.0073 242  PHE B CB  
2657 C CG  . PHE B 19  ? 0.2024 0.1030 0.1461 -0.0224 -0.0422 -0.0200 242  PHE B CG  
2658 C CD1 . PHE B 19  ? 0.2028 0.1276 0.1486 -0.0370 -0.0510 -0.0047 242  PHE B CD1 
2659 C CD2 . PHE B 19  ? 0.1910 0.1032 0.1543 -0.0048 -0.0173 -0.0146 242  PHE B CD2 
2660 C CE1 . PHE B 19  ? 0.2324 0.1466 0.1766 -0.0284 -0.0236 -0.0248 242  PHE B CE1 
2661 C CE2 . PHE B 19  ? 0.2057 0.1234 0.1913 -0.0196 -0.0087 -0.0304 242  PHE B CE2 
2662 C CZ  . PHE B 19  ? 0.2355 0.1358 0.2031 -0.0113 0.0018  -0.0420 242  PHE B CZ  
2663 N N   . PRO B 20  ? 0.1535 0.0926 0.1292 0.0030  -0.0570 -0.0044 243  PRO B N   
2664 C CA  . PRO B 20  ? 0.1582 0.1092 0.1430 -0.0078 -0.0465 0.0047  243  PRO B CA  
2665 C C   . PRO B 20  ? 0.1838 0.1021 0.1654 0.0041  -0.0541 -0.0102 243  PRO B C   
2666 O O   . PRO B 20  ? 0.2080 0.1076 0.1811 -0.0054 -0.0739 -0.0104 243  PRO B O   
2667 C CB  . PRO B 20  ? 0.1652 0.1206 0.1490 -0.0419 -0.0524 0.0127  243  PRO B CB  
2668 C CG  . PRO B 20  ? 0.1908 0.1190 0.1458 -0.0234 -0.0666 0.0195  243  PRO B CG  
2669 C CD  . PRO B 20  ? 0.1875 0.0983 0.1472 -0.0114 -0.0578 0.0003  243  PRO B CD  
2670 N N   . VAL B 21  ? 0.1620 0.1094 0.1711 0.0225  -0.0298 -0.0242 244  VAL B N   
2671 C CA  . VAL B 21  ? 0.1662 0.1157 0.1565 0.0072  -0.0460 -0.0191 244  VAL B CA  
2672 C C   . VAL B 21  ? 0.1514 0.1050 0.1331 0.0219  -0.0523 -0.0238 244  VAL B C   
2673 O O   . VAL B 21  ? 0.1693 0.1155 0.1647 0.0326  -0.0347 -0.0223 244  VAL B O   
2674 C CB  . VAL B 21  ? 0.2034 0.1100 0.1615 -0.0176 -0.0405 -0.0111 244  VAL B CB  
2675 C CG1 . VAL B 21  ? 0.2214 0.1286 0.1893 -0.0170 -0.0278 -0.0238 244  VAL B CG1 
2676 C CG2 . VAL B 21  ? 0.2351 0.1072 0.1735 -0.0460 -0.0209 -0.0055 244  VAL B CG2 
2677 N N   . ALA B 22  ? 0.1444 0.1143 0.1442 0.0017  -0.0354 -0.0045 245  ALA B N   
2678 C CA  . ALA B 22  ? 0.1353 0.1073 0.1696 0.0258  -0.0599 0.0093  245  ALA B CA  
2679 C C   . ALA B 22  ? 0.1742 0.0945 0.1616 0.0259  -0.0490 -0.0002 245  ALA B C   
2680 O O   . ALA B 22  ? 0.1876 0.1123 0.1643 0.0136  -0.0506 -0.0039 245  ALA B O   
2681 C CB  . ALA B 22  ? 0.1733 0.1217 0.2052 0.0559  -0.0397 0.0176  245  ALA B CB  
2682 N N   . ILE B 23  ? 0.1692 0.0874 0.1688 -0.0001 -0.0341 -0.0091 246  ILE B N   
2683 C CA  . ILE B 23  ? 0.1697 0.0925 0.1672 0.0012  -0.0252 -0.0209 246  ILE B CA  
2684 C C   . ILE B 23  ? 0.1736 0.1156 0.1674 0.0084  -0.0342 0.0048  246  ILE B C   
2685 O O   . ILE B 23  ? 0.2043 0.1279 0.1756 0.0299  -0.0444 -0.0016 246  ILE B O   
2686 C CB  . ILE B 23  ? 0.1859 0.1125 0.1731 -0.0081 -0.0206 -0.0236 246  ILE B CB  
2687 C CG1 . ILE B 23  ? 0.1838 0.1479 0.1988 -0.0172 0.0105  -0.0492 246  ILE B CG1 
2688 C CG2 . ILE B 23  ? 0.1715 0.1071 0.1849 -0.0143 -0.0366 -0.0395 246  ILE B CG2 
2689 C CD1 . ILE B 23  ? 0.2216 0.1718 0.1875 -0.0236 0.0079  -0.0137 246  ILE B CD1 
2690 N N   . ASP B 24  ? 0.1347 0.1251 0.1967 0.0169  -0.0267 -0.0097 247  ASP B N   
2691 C CA  . ASP B 24  ? 0.1636 0.1511 0.2038 0.0201  -0.0576 -0.0128 247  ASP B CA  
2692 C C   . ASP B 24  ? 0.1927 0.1493 0.2286 0.0060  -0.0417 -0.0093 247  ASP B C   
2693 O O   . ASP B 24  ? 0.1987 0.1640 0.2769 0.0181  -0.0467 -0.0251 247  ASP B O   
2694 C CB  . ASP B 24  ? 0.2010 0.1556 0.2054 0.0296  -0.0474 -0.0146 247  ASP B CB  
2695 C CG  . ASP B 24  ? 0.2592 0.1555 0.2017 0.0498  -0.0714 -0.0307 247  ASP B CG  
2696 O OD1 . ASP B 24  ? 0.3402 0.1666 0.2812 0.0229  -0.0669 -0.0124 247  ASP B OD1 
2697 O OD2 . ASP B 24  ? 0.2815 0.1752 0.1851 0.0681  -0.0743 -0.0165 247  ASP B OD2 
2698 N N   A MET B 25  ? 0.1679 0.1333 0.1976 -0.0151 -0.0369 -0.0140 248  MET B N   
2699 N N   B MET B 25  ? 0.1955 0.1401 0.2122 0.0064  -0.0353 -0.0037 248  MET B N   
2700 C CA  A MET B 25  ? 0.1357 0.1436 0.2046 -0.0186 -0.0442 -0.0246 248  MET B CA  
2701 C CA  B MET B 25  ? 0.1921 0.1403 0.2082 0.0118  -0.0242 0.0014  248  MET B CA  
2702 C C   A MET B 25  ? 0.1337 0.1333 0.2179 0.0042  -0.0443 -0.0173 248  MET B C   
2703 C C   B MET B 25  ? 0.1744 0.1255 0.2038 0.0036  -0.0286 0.0001  248  MET B C   
2704 O O   A MET B 25  ? 0.1402 0.1379 0.2287 -0.0045 -0.0401 -0.0204 248  MET B O   
2705 O O   B MET B 25  ? 0.1720 0.1243 0.2014 -0.0094 -0.0257 -0.0018 248  MET B O   
2706 C CB  A MET B 25  ? 0.1634 0.1923 0.2123 -0.0223 -0.0407 -0.0239 248  MET B CB  
2707 C CB  B MET B 25  ? 0.2169 0.1633 0.2105 0.0237  -0.0137 0.0102  248  MET B CB  
2708 C CG  A MET B 25  ? 0.1829 0.2350 0.2336 -0.0482 -0.0136 -0.0212 248  MET B CG  
2709 C CG  B MET B 25  ? 0.2261 0.1779 0.2076 0.0153  -0.0041 0.0112  248  MET B CG  
2710 S SD  A MET B 25  ? 0.2501 0.2971 0.2487 -0.0540 0.0155  -0.0285 248  MET B SD  
2711 S SD  B MET B 25  ? 0.2409 0.1996 0.2088 0.0068  -0.0088 0.0082  248  MET B SD  
2712 C CE  A MET B 25  ? 0.2640 0.3168 0.2754 -0.0457 0.0159  -0.0109 248  MET B CE  
2713 C CE  B MET B 25  ? 0.2248 0.1930 0.1928 0.0007  -0.0203 0.0200  248  MET B CE  
2714 N N   . LEU B 26  ? 0.1592 0.1080 0.2018 -0.0009 -0.0436 -0.0060 249  LEU B N   
2715 C CA  . LEU B 26  ? 0.1638 0.1201 0.1693 0.0064  -0.0569 -0.0034 249  LEU B CA  
2716 C C   . LEU B 26  ? 0.1563 0.1496 0.1971 -0.0065 -0.0425 -0.0016 249  LEU B C   
2717 O O   . LEU B 26  ? 0.1678 0.1785 0.2101 0.0015  -0.0123 -0.0154 249  LEU B O   
2718 C CB  . LEU B 26  ? 0.1844 0.1528 0.1600 -0.0210 -0.0758 -0.0195 249  LEU B CB  
2719 C CG  . LEU B 26  ? 0.2023 0.1811 0.1889 -0.0030 -0.0657 0.0003  249  LEU B CG  
2720 C CD1 . LEU B 26  ? 0.2491 0.1754 0.1785 -0.0009 -0.0696 -0.0110 249  LEU B CD1 
2721 C CD2 . LEU B 26  ? 0.2248 0.2452 0.2428 -0.0011 -0.0556 0.0018  249  LEU B CD2 
2722 N N   . HIS B 27  ? 0.1790 0.1522 0.1896 -0.0347 -0.0534 0.0109  250  HIS B N   
2723 C CA  . HIS B 27  ? 0.2201 0.1674 0.1871 -0.0333 -0.0405 0.0056  250  HIS B CA  
2724 C C   . HIS B 27  ? 0.1993 0.1442 0.1985 -0.0550 -0.0261 0.0154  250  HIS B C   
2725 O O   . HIS B 27  ? 0.2058 0.1664 0.2214 -0.0573 -0.0092 0.0148  250  HIS B O   
2726 C CB  . HIS B 27  ? 0.2318 0.1855 0.1756 -0.0536 -0.0216 0.0052  250  HIS B CB  
2727 C CG  . HIS B 27  ? 0.2679 0.2177 0.1961 -0.0414 -0.0491 0.0162  250  HIS B CG  
2728 N ND1 . HIS B 27  ? 0.2809 0.2315 0.2271 -0.0559 -0.0294 0.0071  250  HIS B ND1 
2729 C CD2 . HIS B 27  ? 0.2896 0.2458 0.2081 -0.0284 -0.0518 0.0526  250  HIS B CD2 
2730 C CE1 . HIS B 27  ? 0.3043 0.2396 0.2528 -0.0199 -0.0313 0.0284  250  HIS B CE1 
2731 N NE2 . HIS B 27  ? 0.3132 0.2482 0.2399 -0.0310 -0.0492 0.0541  250  HIS B NE2 
2732 N N   . THR B 28  ? 0.2026 0.1232 0.2229 -0.0285 -0.0341 0.0158  251  THR B N   
2733 C CA  . THR B 28  ? 0.2138 0.1353 0.2427 -0.0289 -0.0674 0.0352  251  THR B CA  
2734 C C   . THR B 28  ? 0.2048 0.1773 0.2775 -0.0429 -0.0504 0.0693  251  THR B C   
2735 O O   . THR B 28  ? 0.2055 0.1951 0.3275 -0.0241 -0.0191 0.0879  251  THR B O   
2736 C CB  . THR B 28  ? 0.2145 0.1409 0.2825 -0.0382 -0.0804 0.0258  251  THR B CB  
2737 O OG1 . THR B 28  ? 0.2193 0.1477 0.2826 -0.0440 -0.0643 0.0729  251  THR B OG1 
2738 C CG2 . THR B 28  ? 0.2004 0.1383 0.3394 0.0013  -0.0631 0.0181  251  THR B CG2 
2739 N N   A SER B 29  ? 0.2350 0.2049 0.2853 -0.0336 -0.0447 0.0819  252  SER B N   
2740 N N   B SER B 29  ? 0.2432 0.2225 0.2817 -0.0414 -0.0587 0.0728  252  SER B N   
2741 C CA  A SER B 29  ? 0.2578 0.2301 0.2915 -0.0170 -0.0340 0.0961  252  SER B CA  
2742 C CA  B SER B 29  ? 0.2756 0.2614 0.2879 -0.0272 -0.0499 0.0810  252  SER B CA  
2743 C C   A SER B 29  ? 0.2522 0.2576 0.2879 -0.0150 -0.0215 0.1003  252  SER B C   
2744 C C   B SER B 29  ? 0.2548 0.2706 0.2878 -0.0271 -0.0259 0.0990  252  SER B C   
2745 O O   A SER B 29  ? 0.2431 0.2477 0.2642 -0.0206 -0.0444 0.0924  252  SER B O   
2746 O O   B SER B 29  ? 0.2321 0.2519 0.2508 -0.0541 -0.0612 0.0907  252  SER B O   
2747 C CB  A SER B 29  ? 0.2920 0.2327 0.3001 -0.0041 -0.0260 0.0958  252  SER B CB  
2748 C CB  B SER B 29  ? 0.3464 0.2981 0.3032 -0.0216 -0.0389 0.0355  252  SER B CB  
2749 O OG  A SER B 29  ? 0.3094 0.2322 0.2836 0.0110  -0.0388 0.1080  252  SER B OG  
2750 O OG  B SER B 29  ? 0.3518 0.3261 0.2777 -0.0241 -0.0864 -0.0016 252  SER B OG  
2751 N N   . PRO B 30  ? 0.2580 0.2941 0.2978 -0.0142 -0.0004 0.1085  253  PRO B N   
2752 C CA  . PRO B 30  ? 0.2458 0.3004 0.2948 -0.0132 -0.0181 0.1021  253  PRO B CA  
2753 C C   . PRO B 30  ? 0.2438 0.2749 0.2745 -0.0373 -0.0326 0.0713  253  PRO B C   
2754 O O   . PRO B 30  ? 0.2601 0.2738 0.3025 -0.0224 -0.0473 0.0502  253  PRO B O   
2755 C CB  . PRO B 30  ? 0.2935 0.3247 0.3351 -0.0118 0.0350  0.1020  253  PRO B CB  
2756 C CG  . PRO B 30  ? 0.3366 0.3410 0.3661 -0.0191 0.0587  0.0921  253  PRO B CG  
2757 C CD  . PRO B 30  ? 0.3027 0.3421 0.3448 -0.0073 0.0127  0.0933  253  PRO B CD  
2758 N N   . THR B 31  ? 0.1853 0.2531 0.2215 -0.0476 -0.0646 0.0893  254  THR B N   
2759 C CA  . THR B 31  ? 0.1867 0.2439 0.2169 -0.0467 -0.0867 0.0677  254  THR B CA  
2760 C C   . THR B 31  ? 0.2254 0.2020 0.2007 -0.0297 -0.0782 0.0505  254  THR B C   
2761 O O   . THR B 31  ? 0.2386 0.2133 0.1927 -0.0414 -0.0643 0.0374  254  THR B O   
2762 C CB  . THR B 31  ? 0.2266 0.2905 0.2414 -0.0571 -0.0319 0.0620  254  THR B CB  
2763 O OG1 . THR B 31  ? 0.2142 0.3272 0.2216 -0.0494 -0.0311 0.0469  254  THR B OG1 
2764 C CG2 . THR B 31  ? 0.2644 0.2847 0.2515 -0.0488 -0.0445 0.0983  254  THR B CG2 
2765 N N   . ASP B 32  ? 0.2531 0.1773 0.2390 -0.0153 -0.0841 0.0585  255  ASP B N   
2766 C CA  . ASP B 32  ? 0.2678 0.1709 0.3071 -0.0338 -0.1050 0.0355  255  ASP B CA  
2767 C C   . ASP B 32  ? 0.2487 0.1433 0.2606 -0.0394 -0.0525 0.0383  255  ASP B C   
2768 O O   . ASP B 32  ? 0.2668 0.1516 0.2767 0.0045  -0.0614 0.0284  255  ASP B O   
2769 C CB  . ASP B 32  ? 0.3874 0.2033 0.3850 -0.0729 -0.0971 0.0176  255  ASP B CB  
2770 C CG  . ASP B 32  ? 0.4640 0.2679 0.4476 -0.0873 -0.1166 -0.0139 255  ASP B CG  
2771 O OD1 . ASP B 32  ? 0.4798 0.2995 0.4333 -0.0777 -0.1442 -0.0297 255  ASP B OD1 
2772 O OD2 . ASP B 32  ? 0.5150 0.3158 0.4913 -0.0784 -0.1210 -0.0344 255  ASP B OD2 
2773 N N   . ASN B 33  ? 0.1970 0.1768 0.2069 -0.0538 -0.0840 0.0332  256  ASN B N   
2774 C CA  . ASN B 33  ? 0.2212 0.2045 0.2255 -0.0239 -0.0759 0.0452  256  ASN B CA  
2775 C C   . ASN B 33  ? 0.1985 0.1600 0.2094 0.0056  -0.0662 0.0314  256  ASN B C   
2776 O O   . ASN B 33  ? 0.1989 0.1704 0.2015 0.0026  -0.0446 0.0411  256  ASN B O   
2777 C CB  . ASN B 33  ? 0.3059 0.2785 0.2448 -0.0477 -0.0762 0.0552  256  ASN B CB  
2778 C CG  . ASN B 33  ? 0.3938 0.3286 0.2896 -0.0549 -0.0567 0.0617  256  ASN B CG  
2779 O OD1 . ASN B 33  ? 0.4058 0.3402 0.2913 -0.1159 -0.0658 0.0203  256  ASN B OD1 
2780 N ND2 . ASN B 33  ? 0.4386 0.3663 0.3183 -0.0283 -0.0620 0.0915  256  ASN B ND2 
2781 N N   . PHE B 34  ? 0.2005 0.1287 0.2166 -0.0152 -0.0584 0.0368  257  PHE B N   
2782 C CA  . PHE B 34  ? 0.1784 0.1265 0.1852 -0.0232 -0.0643 0.0289  257  PHE B CA  
2783 C C   . PHE B 34  ? 0.2049 0.1325 0.1739 -0.0143 -0.0625 0.0079  257  PHE B C   
2784 O O   . PHE B 34  ? 0.2214 0.1337 0.1772 -0.0135 -0.0453 -0.0058 257  PHE B O   
2785 C CB  . PHE B 34  ? 0.2297 0.1221 0.1997 -0.0011 -0.0476 0.0053  257  PHE B CB  
2786 C CG  . PHE B 34  ? 0.2107 0.1269 0.2093 -0.0035 -0.0648 -0.0104 257  PHE B CG  
2787 C CD1 . PHE B 34  ? 0.2372 0.1076 0.2136 0.0032  -0.0159 -0.0089 257  PHE B CD1 
2788 C CD2 . PHE B 34  ? 0.2368 0.1722 0.2798 -0.0004 -0.0245 -0.0833 257  PHE B CD2 
2789 C CE1 . PHE B 34  ? 0.2497 0.1442 0.2650 0.0197  -0.0415 0.0038  257  PHE B CE1 
2790 C CE2 . PHE B 34  ? 0.2535 0.1933 0.3431 0.0069  0.0073  -0.0673 257  PHE B CE2 
2791 C CZ  . PHE B 34  ? 0.2422 0.1710 0.3213 0.0170  -0.0219 -0.0468 257  PHE B CZ  
2792 N N   . ILE B 35  ? 0.1752 0.1378 0.1769 -0.0228 -0.0374 0.0225  258  ILE B N   
2793 C CA  . ILE B 35  ? 0.1832 0.1231 0.1489 0.0061  -0.0558 0.0323  258  ILE B CA  
2794 C C   . ILE B 35  ? 0.1763 0.1011 0.1531 -0.0152 -0.0870 0.0204  258  ILE B C   
2795 O O   . ILE B 35  ? 0.2357 0.1038 0.1739 -0.0337 -0.0707 -0.0044 258  ILE B O   
2796 C CB  . ILE B 35  ? 0.1919 0.1463 0.1840 -0.0095 -0.0392 0.0646  258  ILE B CB  
2797 C CG1 . ILE B 35  ? 0.2281 0.1584 0.1710 0.0035  -0.0579 0.0713  258  ILE B CG1 
2798 C CG2 . ILE B 35  ? 0.2338 0.1603 0.1976 -0.0236 -0.0235 0.0480  258  ILE B CG2 
2799 C CD1 . ILE B 35  ? 0.2695 0.1550 0.1899 0.0118  -0.0745 0.0537  258  ILE B CD1 
2800 N N   . VAL B 36  ? 0.1636 0.1070 0.1534 0.0013  -0.0771 0.0159  259  VAL B N   
2801 C CA  . VAL B 36  ? 0.1514 0.1214 0.1494 -0.0119 -0.0878 0.0253  259  VAL B CA  
2802 C C   . VAL B 36  ? 0.1628 0.1010 0.1520 -0.0232 -0.0677 -0.0014 259  VAL B C   
2803 O O   . VAL B 36  ? 0.1990 0.1066 0.1659 -0.0273 -0.0562 -0.0036 259  VAL B O   
2804 C CB  . VAL B 36  ? 0.1900 0.1284 0.1520 -0.0077 -0.0713 0.0237  259  VAL B CB  
2805 C CG1 . VAL B 36  ? 0.2017 0.1213 0.1546 -0.0219 -0.0828 0.0325  259  VAL B CG1 
2806 C CG2 . VAL B 36  ? 0.1939 0.1532 0.1695 -0.0083 -0.0441 0.0082  259  VAL B CG2 
2807 N N   . GLN B 37  ? 0.1661 0.0999 0.1709 -0.0093 -0.0472 0.0118  260  GLN B N   
2808 C CA  . GLN B 37  ? 0.1601 0.0920 0.1724 -0.0110 -0.0771 0.0179  260  GLN B CA  
2809 C C   . GLN B 37  ? 0.1668 0.0989 0.1674 -0.0273 -0.0747 -0.0114 260  GLN B C   
2810 O O   . GLN B 37  ? 0.1873 0.1068 0.1500 -0.0087 -0.0665 -0.0086 260  GLN B O   
2811 C CB  . GLN B 37  ? 0.1768 0.0900 0.1844 -0.0091 -0.0412 0.0126  260  GLN B CB  
2812 C CG  . GLN B 37  ? 0.1800 0.1092 0.2149 0.0038  -0.0607 0.0400  260  GLN B CG  
2813 C CD  . GLN B 37  ? 0.2265 0.1390 0.2230 -0.0012 -0.0228 0.0625  260  GLN B CD  
2814 O OE1 . GLN B 37  ? 0.2467 0.1803 0.2349 0.0502  -0.0334 0.0749  260  GLN B OE1 
2815 N NE2 . GLN B 37  ? 0.2308 0.1484 0.2154 -0.0214 -0.0175 0.0157  260  GLN B NE2 
2816 N N   . PRO B 38  ? 0.1775 0.0860 0.1538 -0.0204 -0.0544 0.0054  261  PRO B N   
2817 C CA  . PRO B 38  ? 0.1692 0.0874 0.1632 -0.0111 -0.0585 0.0160  261  PRO B CA  
2818 C C   . PRO B 38  ? 0.1480 0.0953 0.1597 -0.0051 -0.0645 0.0068  261  PRO B C   
2819 O O   . PRO B 38  ? 0.1699 0.1001 0.1632 0.0017  -0.0194 0.0045  261  PRO B O   
2820 C CB  . PRO B 38  ? 0.1956 0.0819 0.1715 0.0091  -0.0809 0.0137  261  PRO B CB  
2821 C CG  . PRO B 38  ? 0.2069 0.0694 0.1668 -0.0168 -0.0781 0.0059  261  PRO B CG  
2822 C CD  . PRO B 38  ? 0.1786 0.0893 0.1813 -0.0092 -0.0826 0.0132  261  PRO B CD  
2823 N N   . GLN B 39  ? 0.1332 0.0927 0.1761 -0.0054 -0.0494 0.0138  262  GLN B N   
2824 C CA  . GLN B 39  ? 0.1478 0.0938 0.1656 -0.0147 -0.0634 0.0079  262  GLN B CA  
2825 C C   . GLN B 39  ? 0.1601 0.0937 0.1930 -0.0050 -0.0446 0.0127  262  GLN B C   
2826 O O   . GLN B 39  ? 0.1436 0.1037 0.1994 -0.0061 -0.0462 0.0099  262  GLN B O   
2827 C CB  . GLN B 39  ? 0.1771 0.0889 0.1617 0.0091  -0.0762 0.0186  262  GLN B CB  
2828 C CG  . GLN B 39  ? 0.2078 0.0820 0.1645 0.0213  -0.0644 0.0154  262  GLN B CG  
2829 C CD  . GLN B 39  ? 0.2007 0.0950 0.2205 0.0089  -0.0584 0.0227  262  GLN B CD  
2830 O OE1 . GLN B 39  ? 0.1867 0.1182 0.2078 0.0034  -0.0609 0.0118  262  GLN B OE1 
2831 N NE2 . GLN B 39  ? 0.2135 0.0900 0.2276 -0.0097 -0.0957 0.0158  262  GLN B NE2 
2832 N N   . ASN B 40  ? 0.1512 0.0749 0.1931 -0.0009 -0.0607 0.0141  263  ASN B N   
2833 C CA  . ASN B 40  ? 0.1790 0.0643 0.1595 0.0132  -0.0630 -0.0097 263  ASN B CA  
2834 C C   . ASN B 40  ? 0.1598 0.0828 0.1672 -0.0077 -0.0597 0.0011  263  ASN B C   
2835 O O   . ASN B 40  ? 0.1686 0.0848 0.1813 -0.0111 -0.0489 -0.0048 263  ASN B O   
2836 C CB  . ASN B 40  ? 0.1725 0.0702 0.1585 -0.0160 -0.0654 -0.0131 263  ASN B CB  
2837 C CG  . ASN B 40  ? 0.1783 0.0875 0.1749 -0.0233 -0.0649 0.0025  263  ASN B CG  
2838 O OD1 . ASN B 40  ? 0.1754 0.1136 0.1881 -0.0281 -0.0554 0.0129  263  ASN B OD1 
2839 N ND2 . ASN B 40  ? 0.1982 0.0935 0.1628 0.0104  -0.0619 -0.0058 263  ASN B ND2 
2840 N N   . GLY B 41  ? 0.1884 0.0905 0.1421 0.0146  -0.0545 -0.0073 264  GLY B N   
2841 C CA  . GLY B 41  ? 0.1819 0.1009 0.1587 -0.0081 -0.0536 -0.0232 264  GLY B CA  
2842 C C   . GLY B 41  ? 0.1505 0.0856 0.1585 0.0000  -0.0354 -0.0280 264  GLY B C   
2843 O O   . GLY B 41  ? 0.1376 0.1046 0.1673 -0.0117 -0.0456 -0.0051 264  GLY B O   
2844 N N   . ARG B 42  ? 0.1484 0.0989 0.1779 0.0106  -0.0258 -0.0150 265  ARG B N   
2845 C CA  . ARG B 42  ? 0.1662 0.0851 0.1536 0.0293  -0.0264 0.0052  265  ARG B CA  
2846 C C   . ARG B 42  ? 0.1811 0.1041 0.1576 0.0126  -0.0384 -0.0115 265  ARG B C   
2847 O O   . ARG B 42  ? 0.1901 0.1245 0.1730 0.0112  -0.0269 -0.0138 265  ARG B O   
2848 C CB  . ARG B 42  ? 0.1905 0.1004 0.1775 0.0195  -0.0508 -0.0057 265  ARG B CB  
2849 C CG  . ARG B 42  ? 0.1767 0.0935 0.1893 -0.0083 -0.0607 -0.0223 265  ARG B CG  
2850 C CD  . ARG B 42  ? 0.1945 0.0810 0.2020 -0.0023 -0.0374 0.0014  265  ARG B CD  
2851 N NE  . ARG B 42  ? 0.2100 0.0731 0.1903 0.0024  -0.0401 0.0031  265  ARG B NE  
2852 C CZ  . ARG B 42  ? 0.2251 0.0972 0.1748 -0.0107 -0.0310 -0.0139 265  ARG B CZ  
2853 N NH1 . ARG B 42  ? 0.2157 0.1194 0.1613 0.0061  -0.0540 -0.0134 265  ARG B NH1 
2854 N NH2 . ARG B 42  ? 0.2284 0.1094 0.2211 -0.0124 -0.0396 -0.0292 265  ARG B NH2 
2855 N N   . CYS B 43  ? 0.2047 0.1161 0.1307 0.0355  -0.0372 -0.0153 266  CYS B N   
2856 C CA  . CYS B 43  ? 0.2158 0.1192 0.1517 0.0189  -0.0382 -0.0095 266  CYS B CA  
2857 C C   . CYS B 43  ? 0.1999 0.1278 0.1618 0.0153  -0.0641 -0.0290 266  CYS B C   
2858 O O   . CYS B 43  ? 0.2016 0.1440 0.1760 0.0218  -0.0413 -0.0080 266  CYS B O   
2859 C CB  . CYS B 43  ? 0.2268 0.1230 0.1533 0.0263  -0.0378 0.0138  266  CYS B CB  
2860 S SG  . CYS B 43  ? 0.2401 0.1481 0.1855 0.0079  -0.0167 0.0026  266  CYS B SG  
2861 N N   . THR B 44  ? 0.2516 0.1215 0.1648 0.0495  -0.0359 -0.0389 267  THR B N   
2862 C CA  . THR B 44  ? 0.2088 0.1124 0.1834 0.0389  -0.0416 -0.0537 267  THR B CA  
2863 C C   . THR B 44  ? 0.2052 0.1291 0.2004 0.0207  -0.0210 -0.0479 267  THR B C   
2864 O O   . THR B 44  ? 0.2225 0.1223 0.1926 0.0145  -0.0014 -0.0411 267  THR B O   
2865 C CB  . THR B 44  ? 0.1808 0.1536 0.2148 0.0563  -0.0242 -0.0346 267  THR B CB  
2866 O OG1 . THR B 44  ? 0.1947 0.1731 0.2434 0.0328  -0.0234 -0.0238 267  THR B OG1 
2867 C CG2 . THR B 44  ? 0.1746 0.1637 0.2472 0.0513  -0.0510 -0.0318 267  THR B CG2 
2868 N N   . LEU B 45  ? 0.1931 0.1506 0.1768 0.0273  -0.0619 -0.0564 268  LEU B N   
2869 C CA  . LEU B 45  ? 0.2163 0.1675 0.1883 0.0295  -0.0421 -0.0460 268  LEU B CA  
2870 C C   . LEU B 45  ? 0.2233 0.1842 0.2118 0.0439  -0.0400 -0.0420 268  LEU B C   
2871 O O   . LEU B 45  ? 0.2192 0.2121 0.2146 0.0506  -0.0308 -0.0231 268  LEU B O   
2872 C CB  . LEU B 45  ? 0.2017 0.1652 0.1937 0.0308  -0.0452 -0.0774 268  LEU B CB  
2873 C CG  . LEU B 45  ? 0.1873 0.1547 0.2038 0.0393  -0.0467 -0.0634 268  LEU B CG  
2874 C CD1 . LEU B 45  ? 0.2081 0.1481 0.2085 0.0190  -0.0677 -0.0536 268  LEU B CD1 
2875 C CD2 . LEU B 45  ? 0.2065 0.1632 0.2214 0.0496  -0.0311 -0.0633 268  LEU B CD2 
2876 N N   . ASP B 46  ? 0.2197 0.2029 0.2268 0.0317  -0.0283 -0.0488 269  ASP B N   
2877 C CA  . ASP B 46  ? 0.2543 0.2274 0.2394 0.0281  -0.0047 -0.0544 269  ASP B CA  
2878 C C   . ASP B 46  ? 0.2764 0.2174 0.2067 0.0102  -0.0195 -0.0640 269  ASP B C   
2879 O O   . ASP B 46  ? 0.2984 0.2386 0.2334 0.0168  -0.0210 -0.0317 269  ASP B O   
2880 C CB  . ASP B 46  ? 0.2859 0.2379 0.2670 0.0849  0.0025  -0.0596 269  ASP B CB  
2881 C CG  . ASP B 46  ? 0.3065 0.2464 0.3042 0.1093  -0.0001 -0.0947 269  ASP B CG  
2882 O OD1 . ASP B 46  ? 0.3031 0.2536 0.3084 0.0811  -0.0204 -0.0844 269  ASP B OD1 
2883 O OD2 . ASP B 46  ? 0.3378 0.2505 0.3462 0.1214  -0.0343 -0.1189 269  ASP B OD2 
2884 N N   . GLY B 47  ? 0.2516 0.2028 0.1920 0.0072  -0.0233 -0.0511 270  GLY B N   
2885 C CA  . GLY B 47  ? 0.2181 0.2072 0.1846 0.0027  -0.0273 -0.0533 270  GLY B CA  
2886 C C   . GLY B 47  ? 0.2287 0.2126 0.2255 0.0136  -0.0346 -0.0366 270  GLY B C   
2887 O O   . GLY B 47  ? 0.2513 0.2160 0.2409 -0.0182 -0.0106 -0.0397 270  GLY B O   
2888 N N   . GLU B 48  ? 0.2235 0.2072 0.2075 0.0400  -0.0657 -0.0409 271  GLU B N   
2889 C CA  . GLU B 48  ? 0.2184 0.1920 0.2249 0.0411  -0.0543 -0.0537 271  GLU B CA  
2890 C C   . GLU B 48  ? 0.1922 0.1666 0.2338 0.0296  -0.0424 -0.0400 271  GLU B C   
2891 O O   . GLU B 48  ? 0.1928 0.1662 0.2443 0.0201  -0.0480 -0.0436 271  GLU B O   
2892 C CB  . GLU B 48  ? 0.2826 0.2216 0.2738 0.0965  -0.0612 -0.0961 271  GLU B CB  
2893 C CG  . GLU B 48  ? 0.4243 0.2723 0.3552 0.1325  -0.0412 -0.0932 271  GLU B CG  
2894 C CD  . GLU B 48  ? 0.5301 0.3099 0.4128 0.1671  -0.0507 -0.0818 271  GLU B CD  
2895 O OE1 . GLU B 48  ? 0.5903 0.3363 0.4623 0.1652  -0.0436 -0.0725 271  GLU B OE1 
2896 O OE2 . GLU B 48  ? 0.5757 0.3243 0.4441 0.1809  -0.0495 -0.0659 271  GLU B OE2 
2897 N N   . LEU B 49  ? 0.2011 0.1587 0.2095 0.0050  -0.0141 -0.0606 272  LEU B N   
2898 C CA  . LEU B 49  ? 0.2212 0.1490 0.2192 0.0160  -0.0055 -0.0167 272  LEU B CA  
2899 C C   . LEU B 49  ? 0.1934 0.1571 0.2185 0.0235  -0.0480 -0.0107 272  LEU B C   
2900 O O   . LEU B 49  ? 0.2295 0.1829 0.2599 0.0330  -0.0295 -0.0089 272  LEU B O   
2901 C CB  . LEU B 49  ? 0.2413 0.1457 0.2204 -0.0176 -0.0330 -0.0040 272  LEU B CB  
2902 C CG  . LEU B 49  ? 0.2394 0.1503 0.2681 -0.0094 -0.0599 0.0201  272  LEU B CG  
2903 C CD1 . LEU B 49  ? 0.2557 0.1537 0.2659 -0.0391 -0.0740 0.0152  272  LEU B CD1 
2904 C CD2 . LEU B 49  ? 0.2030 0.1484 0.3085 0.0007  -0.0580 0.0096  272  LEU B CD2 
2905 N N   . GLN B 50  ? 0.2093 0.1551 0.1952 0.0192  -0.0601 -0.0132 273  GLN B N   
2906 C CA  . GLN B 50  ? 0.1915 0.1384 0.1939 -0.0046 -0.0608 -0.0227 273  GLN B CA  
2907 C C   . GLN B 50  ? 0.1632 0.1244 0.1905 0.0242  -0.0529 -0.0109 273  GLN B C   
2908 O O   . GLN B 50  ? 0.1871 0.1270 0.2060 0.0071  -0.0507 -0.0225 273  GLN B O   
2909 C CB  . GLN B 50  ? 0.2255 0.1305 0.2099 -0.0080 -0.0578 -0.0337 273  GLN B CB  
2910 C CG  . GLN B 50  ? 0.2638 0.1376 0.2491 -0.0303 -0.0737 -0.0378 273  GLN B CG  
2911 C CD  . GLN B 50  ? 0.3297 0.1774 0.2741 -0.0219 -0.0833 -0.0166 273  GLN B CD  
2912 O OE1 . GLN B 50  ? 0.3471 0.2025 0.3134 -0.0229 -0.0999 -0.0198 273  GLN B OE1 
2913 N NE2 . GLN B 50  ? 0.3950 0.1625 0.2799 -0.0046 -0.0761 -0.0164 273  GLN B NE2 
2914 N N   . GLY B 51  ? 0.1805 0.1327 0.1866 0.0112  -0.0475 0.0064  274  GLY B N   
2915 C CA  . GLY B 51  ? 0.2001 0.1238 0.1816 0.0062  -0.0385 0.0116  274  GLY B CA  
2916 C C   . GLY B 51  ? 0.1581 0.1176 0.2127 0.0019  -0.0156 -0.0059 274  GLY B C   
2917 O O   . GLY B 51  ? 0.1862 0.1710 0.2557 -0.0064 -0.0326 -0.0125 274  GLY B O   
2918 N N   . THR B 52  ? 0.1569 0.1115 0.2191 0.0098  -0.0533 0.0038  275  THR B N   
2919 C CA  . THR B 52  ? 0.1672 0.1244 0.2023 -0.0105 -0.0529 0.0007  275  THR B CA  
2920 C C   . THR B 52  ? 0.1726 0.1293 0.1807 0.0064  -0.0777 0.0111  275  THR B C   
2921 O O   . THR B 52  ? 0.1848 0.1343 0.2020 0.0152  -0.0686 0.0015  275  THR B O   
2922 C CB  . THR B 52  ? 0.1629 0.1611 0.1871 -0.0098 -0.0635 0.0085  275  THR B CB  
2923 O OG1 . THR B 52  ? 0.1629 0.1516 0.2200 0.0054  -0.0575 0.0074  275  THR B OG1 
2924 C CG2 . THR B 52  ? 0.1648 0.1607 0.2169 0.0067  -0.0778 0.0264  275  THR B CG2 
2925 N N   . THR B 53  ? 0.1712 0.1215 0.1841 -0.0012 -0.0548 0.0061  276  THR B N   
2926 C CA  . THR B 53  ? 0.1712 0.1038 0.1741 -0.0048 -0.0662 0.0116  276  THR B CA  
2927 C C   . THR B 53  ? 0.1820 0.1136 0.1911 0.0008  -0.0514 0.0004  276  THR B C   
2928 O O   . THR B 53  ? 0.1964 0.1151 0.2195 0.0029  -0.0460 0.0081  276  THR B O   
2929 C CB  . THR B 53  ? 0.1640 0.1084 0.1812 -0.0073 -0.0710 0.0035  276  THR B CB  
2930 O OG1 . THR B 53  ? 0.1756 0.1165 0.1793 -0.0078 -0.0391 0.0072  276  THR B OG1 
2931 C CG2 . THR B 53  ? 0.1735 0.1155 0.1827 0.0023  -0.0503 0.0061  276  THR B CG2 
2932 N N   . GLN B 54  ? 0.1869 0.0955 0.1820 0.0070  -0.0258 0.0327  277  GLN B N   
2933 C CA  . GLN B 54  ? 0.1494 0.1089 0.1932 -0.0093 -0.0563 0.0172  277  GLN B CA  
2934 C C   . GLN B 54  ? 0.1570 0.1385 0.2068 0.0091  -0.0621 0.0116  277  GLN B C   
2935 O O   . GLN B 54  ? 0.1562 0.1474 0.2093 0.0003  -0.0483 0.0280  277  GLN B O   
2936 C CB  . GLN B 54  ? 0.1480 0.1184 0.2222 -0.0132 -0.0541 -0.0065 277  GLN B CB  
2937 C CG  . GLN B 54  ? 0.1521 0.1100 0.2087 -0.0007 -0.0570 -0.0011 277  GLN B CG  
2938 C CD  . GLN B 54  ? 0.1733 0.1110 0.1871 0.0174  -0.0773 0.0217  277  GLN B CD  
2939 O OE1 . GLN B 54  ? 0.2121 0.0980 0.1983 0.0036  -0.0682 0.0253  277  GLN B OE1 
2940 N NE2 . GLN B 54  ? 0.1845 0.1088 0.1881 -0.0005 -0.0482 0.0140  277  GLN B NE2 
2941 N N   . LEU B 55  ? 0.1704 0.1245 0.2019 0.0317  -0.0315 0.0139  278  LEU B N   
2942 C CA  . LEU B 55  ? 0.1417 0.1338 0.2190 0.0339  -0.0319 0.0068  278  LEU B CA  
2943 C C   . LEU B 55  ? 0.1572 0.1264 0.1919 0.0180  -0.0549 -0.0055 278  LEU B C   
2944 O O   . LEU B 55  ? 0.1870 0.1578 0.2161 0.0287  -0.0506 -0.0164 278  LEU B O   
2945 C CB  . LEU B 55  ? 0.1640 0.1335 0.2491 0.0379  -0.0026 0.0194  278  LEU B CB  
2946 C CG  . LEU B 55  ? 0.1996 0.1460 0.2652 0.0322  0.0288  0.0014  278  LEU B CG  
2947 C CD1 . LEU B 55  ? 0.2476 0.1765 0.2707 0.0427  0.0304  0.0008  278  LEU B CD1 
2948 C CD2 . LEU B 55  ? 0.2407 0.1455 0.2915 0.0212  0.0337  -0.0089 278  LEU B CD2 
2949 N N   . VAL B 56  ? 0.1576 0.1092 0.1810 0.0130  -0.0184 -0.0052 279  VAL B N   
2950 C CA  . VAL B 56  ? 0.1396 0.1222 0.2069 -0.0207 -0.0078 0.0097  279  VAL B CA  
2951 C C   . VAL B 56  ? 0.1527 0.1345 0.1887 -0.0006 -0.0285 0.0016  279  VAL B C   
2952 O O   . VAL B 56  ? 0.1857 0.1213 0.1571 0.0073  -0.0620 -0.0050 279  VAL B O   
2953 C CB  . VAL B 56  ? 0.1281 0.1164 0.2111 -0.0087 -0.0088 0.0147  279  VAL B CB  
2954 C CG1 . VAL B 56  ? 0.1635 0.0873 0.1960 0.0032  -0.0436 0.0190  279  VAL B CG1 
2955 C CG2 . VAL B 56  ? 0.1509 0.1476 0.2418 -0.0110 0.0552  0.0181  279  VAL B CG2 
2956 N N   . ALA B 57  ? 0.1592 0.1268 0.1795 0.0203  0.0018  0.0069  280  ALA B N   
2957 C CA  . ALA B 57  ? 0.1485 0.1532 0.2030 -0.0095 -0.0326 -0.0008 280  ALA B CA  
2958 C C   . ALA B 57  ? 0.1790 0.1206 0.1662 -0.0059 -0.0577 -0.0064 280  ALA B C   
2959 O O   . ALA B 57  ? 0.1820 0.1221 0.1821 0.0167  -0.0423 0.0063  280  ALA B O   
2960 C CB  . ALA B 57  ? 0.1400 0.1832 0.2280 -0.0148 -0.0556 -0.0165 280  ALA B CB  
2961 N N   . SER B 58  ? 0.1479 0.1135 0.1734 -0.0135 -0.0581 0.0054  281  SER B N   
2962 C CA  . SER B 58  ? 0.1906 0.0986 0.1993 0.0107  -0.0679 0.0023  281  SER B CA  
2963 C C   . SER B 58  ? 0.2137 0.1075 0.1922 -0.0081 -0.0660 -0.0071 281  SER B C   
2964 O O   . SER B 58  ? 0.2828 0.1204 0.1997 0.0221  -0.0769 -0.0192 281  SER B O   
2965 C CB  . SER B 58  ? 0.2142 0.1132 0.2232 0.0316  -0.0362 0.0225  281  SER B CB  
2966 O OG  . SER B 58  ? 0.2142 0.1069 0.2330 0.0347  -0.0357 0.0201  281  SER B OG  
2967 N N   . ASN B 59  ? 0.1935 0.1174 0.1815 -0.0021 -0.0614 0.0091  282  ASN B N   
2968 C CA  . ASN B 59  ? 0.1637 0.1210 0.2025 -0.0131 -0.0418 0.0176  282  ASN B CA  
2969 C C   . ASN B 59  ? 0.1845 0.1003 0.1850 0.0042  -0.0316 0.0060  282  ASN B C   
2970 O O   . ASN B 59  ? 0.2031 0.0932 0.1933 0.0179  -0.0468 -0.0105 282  ASN B O   
2971 C CB  . ASN B 59  ? 0.1635 0.1316 0.2094 -0.0213 -0.0369 0.0009  282  ASN B CB  
2972 C CG  . ASN B 59  ? 0.1736 0.1318 0.2228 -0.0126 -0.0521 0.0223  282  ASN B CG  
2973 O OD1 . ASN B 59  ? 0.2052 0.1443 0.2569 -0.0382 -0.0491 0.0369  282  ASN B OD1 
2974 N ND2 . ASN B 59  ? 0.1585 0.1481 0.1972 -0.0112 -0.0621 0.0272  282  ASN B ND2 
2975 N N   . ILE B 60  ? 0.1883 0.0935 0.1501 -0.0153 -0.0297 0.0058  283  ILE B N   
2976 C CA  . ILE B 60  ? 0.1890 0.1087 0.1226 -0.0101 -0.0399 -0.0008 283  ILE B CA  
2977 C C   . ILE B 60  ? 0.1911 0.1053 0.1373 0.0027  -0.0372 -0.0200 283  ILE B C   
2978 O O   . ILE B 60  ? 0.1728 0.1061 0.1589 0.0163  -0.0453 -0.0228 283  ILE B O   
2979 C CB  . ILE B 60  ? 0.1736 0.1187 0.1302 0.0009  -0.0346 -0.0237 283  ILE B CB  
2980 C CG1 . ILE B 60  ? 0.1791 0.1220 0.1525 0.0160  -0.0353 -0.0363 283  ILE B CG1 
2981 C CG2 . ILE B 60  ? 0.1758 0.1341 0.1450 -0.0274 0.0082  -0.0181 283  ILE B CG2 
2982 C CD1 . ILE B 60  ? 0.1944 0.1336 0.1562 -0.0102 -0.0406 -0.0390 283  ILE B CD1 
2983 N N   . CYS B 61  ? 0.1747 0.1171 0.1525 0.0019  -0.0537 -0.0077 284  CYS B N   
2984 C CA  . CYS B 61  ? 0.1804 0.1235 0.1699 -0.0181 -0.0554 -0.0222 284  CYS B CA  
2985 C C   . CYS B 61  ? 0.1658 0.1151 0.1650 0.0009  -0.0546 -0.0133 284  CYS B C   
2986 O O   . CYS B 61  ? 0.1856 0.1170 0.1723 -0.0112 -0.0403 -0.0202 284  CYS B O   
2987 C CB  . CYS B 61  ? 0.1883 0.1170 0.1986 -0.0237 -0.0250 -0.0185 284  CYS B CB  
2988 S SG  . CYS B 61  ? 0.2001 0.1134 0.1773 -0.0082 -0.0445 -0.0010 284  CYS B SG  
2989 N N   . ALA B 62  ? 0.1554 0.1117 0.2003 -0.0055 -0.0602 -0.0215 285  ALA B N   
2990 C CA  . ALA B 62  ? 0.1483 0.1130 0.2291 -0.0084 -0.0477 -0.0106 285  ALA B CA  
2991 C C   . ALA B 62  ? 0.1538 0.1233 0.2152 0.0088  -0.0704 -0.0323 285  ALA B C   
2992 O O   . ALA B 62  ? 0.1769 0.1174 0.2411 0.0217  -0.0558 -0.0343 285  ALA B O   
2993 C CB  . ALA B 62  ? 0.2035 0.1102 0.2129 -0.0114 -0.0320 0.0076  285  ALA B CB  
2994 N N   . PHE B 63  ? 0.1598 0.1389 0.2059 0.0001  -0.0688 -0.0264 286  PHE B N   
2995 C CA  . PHE B 63  ? 0.1706 0.1266 0.2389 0.0114  -0.0677 -0.0212 286  PHE B CA  
2996 C C   . PHE B 63  ? 0.1434 0.1295 0.2581 -0.0010 -0.0768 -0.0087 286  PHE B C   
2997 O O   . PHE B 63  ? 0.1637 0.1143 0.3103 0.0093  -0.0451 -0.0265 286  PHE B O   
2998 C CB  . PHE B 63  ? 0.1812 0.1388 0.2353 0.0009  -0.0887 -0.0275 286  PHE B CB  
2999 C CG  . PHE B 63  ? 0.1933 0.1415 0.2540 0.0004  -0.0930 -0.0138 286  PHE B CG  
3000 C CD1 . PHE B 63  ? 0.2198 0.1194 0.2848 -0.0150 -0.1112 0.0052  286  PHE B CD1 
3001 C CD2 . PHE B 63  ? 0.2211 0.1596 0.2625 -0.0226 -0.0927 -0.0412 286  PHE B CD2 
3002 C CE1 . PHE B 63  ? 0.2114 0.1326 0.2924 -0.0352 -0.1157 -0.0092 286  PHE B CE1 
3003 C CE2 . PHE B 63  ? 0.2470 0.1473 0.2447 -0.0341 -0.1043 -0.0459 286  PHE B CE2 
3004 C CZ  . PHE B 63  ? 0.2381 0.1457 0.2653 -0.0281 -0.1170 -0.0053 286  PHE B CZ  
3005 N N   . ARG B 64  ? 0.1454 0.1331 0.2826 -0.0143 -0.0735 -0.0180 287  ARG B N   
3006 C CA  . ARG B 64  ? 0.1544 0.1559 0.2843 -0.0129 -0.0961 -0.0130 287  ARG B CA  
3007 C C   . ARG B 64  ? 0.1663 0.1377 0.2802 -0.0164 -0.0800 -0.0349 287  ARG B C   
3008 O O   . ARG B 64  ? 0.1747 0.1227 0.3040 0.0148  -0.0555 -0.0259 287  ARG B O   
3009 C CB  . ARG B 64  ? 0.2686 0.2185 0.2963 -0.0470 -0.0953 0.0219  287  ARG B CB  
3010 C CG  . ARG B 64  ? 0.4397 0.2760 0.3153 -0.0657 -0.0383 0.0385  287  ARG B CG  
3011 C CD  . ARG B 64  ? 0.6058 0.3232 0.3786 -0.0627 0.0513  0.0548  287  ARG B CD  
3012 N NE  . ARG B 64  ? 0.7185 0.3566 0.4544 -0.0558 0.0872  0.0672  287  ARG B NE  
3013 C CZ  . ARG B 64  ? 0.7859 0.3757 0.5081 -0.0534 0.1266  0.0654  287  ARG B CZ  
3014 N NH1 . ARG B 64  ? 0.8152 0.3823 0.5207 -0.0447 0.1348  0.0599  287  ARG B NH1 
3015 N NH2 . ARG B 64  ? 0.8094 0.3833 0.5400 -0.0491 0.1388  0.0732  287  ARG B NH2 
3016 N N   . GLY B 65  ? 0.1549 0.1409 0.2619 0.0030  -0.0851 -0.0192 288  GLY B N   
3017 C CA  . GLY B 65  ? 0.1650 0.1309 0.2764 0.0041  -0.0934 -0.0115 288  GLY B CA  
3018 C C   . GLY B 65  ? 0.1904 0.1311 0.2825 0.0099  -0.0964 -0.0082 288  GLY B C   
3019 O O   . GLY B 65  ? 0.1806 0.1264 0.2790 0.0127  -0.0626 0.0021  288  GLY B O   
3020 N N   . SER B 66  ? 0.2264 0.1156 0.2806 0.0119  -0.0941 -0.0171 289  SER B N   
3021 C CA  . SER B 66  ? 0.2091 0.1262 0.3043 -0.0138 -0.1321 -0.0114 289  SER B CA  
3022 C C   . SER B 66  ? 0.2474 0.1298 0.3020 -0.0080 -0.1107 0.0086  289  SER B C   
3023 O O   . SER B 66  ? 0.2952 0.1279 0.3049 -0.0089 -0.1196 0.0048  289  SER B O   
3024 C CB  . SER B 66  ? 0.2191 0.1567 0.3534 0.0182  -0.1320 -0.0044 289  SER B CB  
3025 O OG  . SER B 66  ? 0.2158 0.1987 0.4000 0.0035  -0.1093 -0.0078 289  SER B OG  
3026 N N   . ILE B 67  ? 0.2334 0.1330 0.2777 -0.0053 -0.0778 0.0231  290  ILE B N   
3027 C CA  . ILE B 67  ? 0.2264 0.1443 0.2869 -0.0137 -0.1191 0.0313  290  ILE B CA  
3028 C C   . ILE B 67  ? 0.2187 0.1507 0.3463 -0.0362 -0.1371 0.0503  290  ILE B C   
3029 O O   . ILE B 67  ? 0.2288 0.1606 0.3729 -0.0288 -0.1162 0.0467  290  ILE B O   
3030 C CB  . ILE B 67  ? 0.2398 0.1384 0.2634 -0.0317 -0.1194 0.0289  290  ILE B CB  
3031 C CG1 . ILE B 67  ? 0.2280 0.1316 0.2733 -0.0494 -0.1105 0.0266  290  ILE B CG1 
3032 C CG2 . ILE B 67  ? 0.2602 0.1612 0.2565 -0.0198 -0.1272 0.0308  290  ILE B CG2 
3033 C CD1 . ILE B 67  ? 0.2345 0.1405 0.2971 -0.0496 -0.1270 0.0325  290  ILE B CD1 
3034 N N   . SER B 68  ? 0.2337 0.1682 0.3438 -0.0270 -0.1560 0.0640  291  SER B N   
3035 C CA  . SER B 68  ? 0.2626 0.2091 0.3648 -0.0210 -0.1726 0.0646  291  SER B CA  
3036 C C   . SER B 68  ? 0.3046 0.2017 0.3707 -0.0411 -0.1923 0.0717  291  SER B C   
3037 O O   . SER B 68  ? 0.3325 0.2115 0.4061 -0.0373 -0.1847 0.0819  291  SER B O   
3038 C CB  . SER B 68  ? 0.2453 0.2708 0.4241 -0.0106 -0.1776 0.0395  291  SER B CB  
3039 O OG  . SER B 68  ? 0.2849 0.3177 0.4804 -0.0092 -0.1216 0.0309  291  SER B OG  
3040 N N   . GLY B 69  ? 0.3249 0.2159 0.3773 -0.0658 -0.1906 0.0583  292  GLY B N   
3041 C CA  . GLY B 69  ? 0.3427 0.2118 0.3976 -0.0927 -0.1735 0.0247  292  GLY B CA  
3042 C C   . GLY B 69  ? 0.3487 0.2001 0.3758 -0.0773 -0.2023 0.0520  292  GLY B C   
3043 O O   . GLY B 69  ? 0.3421 0.1672 0.3700 -0.0598 -0.2058 0.0554  292  GLY B O   
3044 N N   . HIS B 70  ? 0.3846 0.2398 0.3637 -0.0945 -0.2056 0.0446  293  HIS B N   
3045 C CA  . HIS B 70  ? 0.4273 0.2585 0.3633 -0.1039 -0.2184 0.0510  293  HIS B CA  
3046 C C   . HIS B 70  ? 0.5125 0.2822 0.4508 -0.1131 -0.2285 0.0427  293  HIS B C   
3047 O O   . HIS B 70  ? 0.5149 0.2837 0.4619 -0.1101 -0.2120 0.0462  293  HIS B O   
3048 C CB  . HIS B 70  ? 0.4371 0.2649 0.3378 -0.1012 -0.2137 0.0476  293  HIS B CB  
3049 C CG  . HIS B 70  ? 0.4361 0.2612 0.3316 -0.1134 -0.2002 0.0381  293  HIS B CG  
3050 N ND1 . HIS B 70  ? 0.4550 0.2454 0.3441 -0.1279 -0.1913 0.0494  293  HIS B ND1 
3051 C CD2 . HIS B 70  ? 0.4744 0.2684 0.3319 -0.1083 -0.1974 0.0374  293  HIS B CD2 
3052 C CE1 . HIS B 70  ? 0.4574 0.2380 0.3216 -0.1349 -0.1832 0.0524  293  HIS B CE1 
3053 N NE2 . HIS B 70  ? 0.4791 0.2580 0.3221 -0.1242 -0.1964 0.0432  293  HIS B NE2 
3054 N N   . GLU B 71  ? 0.5532 0.2952 0.4902 -0.1114 -0.2638 0.0498  294  GLU B N   
3055 C CA  . GLU B 71  ? 0.5647 0.3227 0.5135 -0.0927 -0.3160 0.0667  294  GLU B CA  
3056 C C   . GLU B 71  ? 0.6206 0.3970 0.5529 -0.0638 -0.3426 0.0915  294  GLU B C   
3057 O O   . GLU B 71  ? 0.6108 0.4125 0.5627 -0.0569 -0.3408 0.0997  294  GLU B O   
3058 C CB  . GLU B 71  ? 0.5373 0.2896 0.5016 -0.0886 -0.3026 0.0577  294  GLU B CB  
3059 C CG  . GLU B 71  ? 0.5129 0.2594 0.5078 -0.0818 -0.3012 0.0850  294  GLU B CG  
3060 C CD  . GLU B 71  ? 0.4894 0.2346 0.4867 -0.0845 -0.2874 0.0867  294  GLU B CD  
3061 O OE1 . GLU B 71  ? 0.5120 0.2617 0.4766 -0.0773 -0.2883 0.0880  294  GLU B OE1 
3062 O OE2 . GLU B 71  ? 0.4739 0.2224 0.4655 -0.0894 -0.2746 0.0854  294  GLU B OE2 
3063 N N   . ASN B 72  ? 0.6738 0.4584 0.5756 -0.0251 -0.3541 0.1019  295  ASN B N   
3064 C CA  . ASN B 72  ? 0.7776 0.5079 0.6259 -0.0016 -0.3736 0.1336  295  ASN B CA  
3065 C C   . ASN B 72  ? 0.7902 0.5352 0.6256 0.0030  -0.3634 0.1557  295  ASN B C   
3066 O O   . ASN B 72  ? 0.7581 0.5504 0.6194 0.0097  -0.3583 0.1527  295  ASN B O   
3067 C CB  . ASN B 72  ? 0.8525 0.5270 0.6844 0.0144  -0.3520 0.1318  295  ASN B CB  
3068 C CG  . ASN B 72  ? 0.9226 0.5472 0.7418 0.0193  -0.3243 0.1143  295  ASN B CG  
3069 O OD1 . ASN B 72  ? 0.9454 0.5519 0.7550 0.0226  -0.3236 0.1233  295  ASN B OD1 
3070 N ND2 . ASN B 72  ? 0.9491 0.5575 0.7671 0.0145  -0.3096 0.0983  295  ASN B ND2 
3071 N N   . ASN B 73  ? 0.8240 0.5393 0.6254 -0.0070 -0.3605 0.1708  296  ASN B N   
3072 C CA  . ASN B 73  ? 0.8585 0.5400 0.6151 -0.0370 -0.3652 0.1764  296  ASN B CA  
3073 C C   . ASN B 73  ? 0.8885 0.5288 0.6121 -0.0329 -0.3458 0.1701  296  ASN B C   
3074 O O   . ASN B 73  ? 0.8912 0.5348 0.6025 -0.0149 -0.3402 0.1862  296  ASN B O   
3075 C CB  . ASN B 73  ? 0.8598 0.5493 0.6179 -0.0826 -0.3825 0.1776  296  ASN B CB  
3076 C CG  . ASN B 73  ? 0.8528 0.5595 0.6313 -0.1247 -0.3988 0.1655  296  ASN B CG  
3077 O OD1 . ASN B 73  ? 0.8561 0.5639 0.6376 -0.1468 -0.3906 0.1466  296  ASN B OD1 
3078 N ND2 . ASN B 73  ? 0.8392 0.5632 0.6419 -0.1388 -0.4121 0.1644  296  ASN B ND2 
3079 N N   . GLY B 74  ? 0.8938 0.5083 0.6128 -0.0486 -0.3244 0.1371  297  GLY B N   
3080 C CA  . GLY B 74  ? 0.8930 0.4903 0.6033 -0.0663 -0.3003 0.0959  297  GLY B CA  
3081 C C   . GLY B 74  ? 0.8718 0.4660 0.5696 -0.0818 -0.2906 0.0671  297  GLY B C   
3082 O O   . GLY B 74  ? 0.8818 0.4633 0.6036 -0.0743 -0.2971 0.0631  297  GLY B O   
3083 N N   . ASP B 75  ? 0.8304 0.4345 0.4951 -0.1133 -0.2509 0.0397  298  ASP B N   
3084 C CA  . ASP B 75  ? 0.7850 0.4018 0.4173 -0.1378 -0.2056 0.0160  298  ASP B CA  
3085 C C   . ASP B 75  ? 0.7386 0.3796 0.3534 -0.1336 -0.2240 -0.0043 298  ASP B C   
3086 O O   . ASP B 75  ? 0.6882 0.3653 0.3200 -0.1153 -0.2129 -0.0070 298  ASP B O   
3087 C CB  . ASP B 75  ? 0.7768 0.3911 0.3917 -0.1519 -0.1657 0.0075  298  ASP B CB  
3088 C CG  . ASP B 75  ? 0.7675 0.3899 0.3884 -0.1509 -0.1279 0.0104  298  ASP B CG  
3089 O OD1 . ASP B 75  ? 0.7552 0.3843 0.3619 -0.1296 -0.1437 0.0117  298  ASP B OD1 
3090 O OD2 . ASP B 75  ? 0.7764 0.3888 0.4070 -0.1477 -0.0869 0.0154  298  ASP B OD2 
3091 N N   . GLN B 76  ? 0.6958 0.3706 0.3291 -0.1193 -0.2172 -0.0085 299  GLN B N   
3092 C CA  . GLN B 76  ? 0.6443 0.3730 0.3231 -0.0928 -0.2242 -0.0070 299  GLN B CA  
3093 C C   . GLN B 76  ? 0.5972 0.3515 0.3002 -0.0895 -0.1988 -0.0239 299  GLN B C   
3094 O O   . GLN B 76  ? 0.6465 0.3407 0.2983 -0.0925 -0.1623 -0.0318 299  GLN B O   
3095 C CB  . GLN B 76  ? 0.6936 0.3981 0.3310 -0.0925 -0.2239 -0.0250 299  GLN B CB  
3096 C CG  . GLN B 76  ? 0.7576 0.4199 0.3523 -0.0893 -0.2166 -0.0197 299  GLN B CG  
3097 C CD  . GLN B 76  ? 0.8036 0.4425 0.3892 -0.0875 -0.1813 -0.0147 299  GLN B CD  
3098 O OE1 . GLN B 76  ? 0.8192 0.4447 0.3986 -0.0960 -0.1587 -0.0110 299  GLN B OE1 
3099 N NE2 . GLN B 76  ? 0.8157 0.4551 0.3998 -0.0823 -0.1796 -0.0095 299  GLN B NE2 
3100 N N   . HIS B 77  ? 0.4913 0.3346 0.3028 -0.0799 -0.1819 -0.0219 300  HIS B N   
3101 C CA  A HIS B 77  ? 0.4253 0.3167 0.2989 -0.0810 -0.1827 -0.0254 300  HIS B CA  
3102 C CA  B HIS B 77  ? 0.4465 0.3402 0.3242 -0.0769 -0.1795 -0.0215 300  HIS B CA  
3103 C C   . HIS B 77  ? 0.4250 0.2700 0.2563 -0.0554 -0.1741 -0.0081 300  HIS B C   
3104 O O   . HIS B 77  ? 0.4486 0.2413 0.2401 -0.0136 -0.1553 -0.0106 300  HIS B O   
3117 N N   . GLN B 78  ? 0.3901 0.2129 0.2321 -0.0709 -0.1481 -0.0047 301  GLN B N   
3118 C CA  . GLN B 78  ? 0.3540 0.1941 0.2456 -0.0575 -0.1533 0.0227  301  GLN B CA  
3119 C C   . GLN B 78  ? 0.3016 0.1848 0.2592 -0.0373 -0.1639 0.0160  301  GLN B C   
3120 O O   . GLN B 78  ? 0.3288 0.2154 0.2832 -0.0528 -0.1752 0.0154  301  GLN B O   
3121 C CB  . GLN B 78  ? 0.3783 0.1948 0.2594 -0.0800 -0.1302 0.0393  301  GLN B CB  
3122 C CG  . GLN B 78  ? 0.4253 0.2093 0.2719 -0.1118 -0.1266 0.0166  301  GLN B CG  
3123 C CD  . GLN B 78  ? 0.4936 0.2401 0.3283 -0.1194 -0.1019 0.0130  301  GLN B CD  
3124 O OE1 . GLN B 78  ? 0.5200 0.2497 0.3287 -0.1022 -0.1096 0.0379  301  GLN B OE1 
3125 N NE2 . GLN B 78  ? 0.5334 0.2626 0.3486 -0.1345 -0.0715 0.0139  301  GLN B NE2 
3126 N N   . TRP B 79  ? 0.2862 0.1392 0.2588 -0.0347 -0.1610 0.0258  302  TRP B N   
3127 C CA  . TRP B 79  ? 0.2832 0.1236 0.2617 -0.0347 -0.1400 0.0154  302  TRP B CA  
3128 C C   . TRP B 79  ? 0.2658 0.1225 0.2801 -0.0197 -0.1217 0.0291  302  TRP B C   
3129 O O   . TRP B 79  ? 0.2373 0.1276 0.2994 -0.0281 -0.1346 0.0096  302  TRP B O   
3130 C CB  . TRP B 79  ? 0.2990 0.1214 0.2641 -0.0224 -0.1337 0.0120  302  TRP B CB  
3131 C CG  . TRP B 79  ? 0.3171 0.1390 0.2488 -0.0415 -0.1465 0.0068  302  TRP B CG  
3132 C CD1 . TRP B 79  ? 0.3434 0.1433 0.2441 -0.0112 -0.1422 0.0227  302  TRP B CD1 
3133 C CD2 . TRP B 79  ? 0.3294 0.1477 0.2258 -0.0503 -0.1446 0.0095  302  TRP B CD2 
3134 N NE1 . TRP B 79  ? 0.3423 0.1442 0.2487 -0.0462 -0.1429 0.0078  302  TRP B NE1 
3135 C CE2 . TRP B 79  ? 0.3538 0.1489 0.2435 -0.0639 -0.1356 0.0051  302  TRP B CE2 
3136 C CE3 . TRP B 79  ? 0.3474 0.1659 0.2368 -0.0734 -0.1431 0.0154  302  TRP B CE3 
3137 C CZ2 . TRP B 79  ? 0.3986 0.1648 0.2418 -0.0654 -0.1342 -0.0080 302  TRP B CZ2 
3138 C CZ3 . TRP B 79  ? 0.3934 0.1656 0.2586 -0.0682 -0.1397 -0.0054 302  TRP B CZ3 
3139 C CH2 . TRP B 79  ? 0.3866 0.1759 0.2503 -0.0713 -0.1209 -0.0251 302  TRP B CH2 
3140 N N   . HIS B 80  ? 0.2567 0.1252 0.2768 -0.0138 -0.1207 0.0446  303  HIS B N   
3141 C CA  . HIS B 80  ? 0.2537 0.1201 0.2939 -0.0235 -0.1622 0.0273  303  HIS B CA  
3142 C C   . HIS B 80  ? 0.2436 0.1167 0.2874 -0.0335 -0.1558 0.0392  303  HIS B C   
3143 O O   . HIS B 80  ? 0.2540 0.1287 0.3128 -0.0350 -0.1606 0.0293  303  HIS B O   
3144 C CB  . HIS B 80  ? 0.2583 0.1449 0.3442 -0.0176 -0.1685 -0.0015 303  HIS B CB  
3145 C CG  . HIS B 80  ? 0.2733 0.1452 0.4017 -0.0217 -0.1759 0.0106  303  HIS B CG  
3146 N ND1 . HIS B 80  ? 0.2939 0.1492 0.4240 -0.0293 -0.1664 0.0285  303  HIS B ND1 
3147 C CD2 . HIS B 80  ? 0.2943 0.1649 0.4347 -0.0013 -0.1565 0.0176  303  HIS B CD2 
3148 C CE1 . HIS B 80  ? 0.2950 0.1550 0.4292 -0.0173 -0.1732 0.0242  303  HIS B CE1 
3149 N NE2 . HIS B 80  ? 0.2883 0.1565 0.4227 -0.0112 -0.1829 0.0290  303  HIS B NE2 
3150 N N   . PHE B 81  ? 0.2657 0.1355 0.2821 -0.0326 -0.1618 0.0266  304  PHE B N   
3151 C CA  . PHE B 81  ? 0.2378 0.1455 0.2910 -0.0129 -0.1538 0.0187  304  PHE B CA  
3152 C C   . PHE B 81  ? 0.2447 0.1051 0.3066 -0.0053 -0.1109 -0.0099 304  PHE B C   
3153 O O   . PHE B 81  ? 0.2427 0.1079 0.3127 -0.0079 -0.1066 -0.0073 304  PHE B O   
3154 C CB  . PHE B 81  ? 0.2030 0.1672 0.2896 0.0038  -0.1385 0.0194  304  PHE B CB  
3155 C CG  . PHE B 81  ? 0.2010 0.1544 0.3045 0.0006  -0.1411 0.0131  304  PHE B CG  
3156 C CD1 . PHE B 81  ? 0.2280 0.1492 0.2897 0.0243  -0.1362 0.0195  304  PHE B CD1 
3157 C CD2 . PHE B 81  ? 0.2331 0.2236 0.2866 0.0167  -0.1228 0.0440  304  PHE B CD2 
3158 C CE1 . PHE B 81  ? 0.2303 0.1435 0.3032 -0.0047 -0.1202 0.0162  304  PHE B CE1 
3159 C CE2 . PHE B 81  ? 0.2434 0.2355 0.2659 0.0060  -0.1376 0.0465  304  PHE B CE2 
3160 C CZ  . PHE B 81  ? 0.2473 0.1930 0.2603 -0.0322 -0.1092 0.0445  304  PHE B CZ  
3161 N N   . SER B 82  ? 0.2321 0.1203 0.3072 0.0050  -0.1247 -0.0123 305  SER B N   
3162 C CA  . SER B 82  ? 0.2531 0.1323 0.3310 -0.0171 -0.1192 0.0044  305  SER B CA  
3163 C C   . SER B 82  ? 0.2602 0.1253 0.3141 -0.0111 -0.1186 0.0048  305  SER B C   
3164 O O   . SER B 82  ? 0.2947 0.1226 0.3347 0.0059  -0.1008 -0.0026 305  SER B O   
3165 C CB  . SER B 82  ? 0.2533 0.1852 0.3473 -0.0292 -0.1395 0.0044  305  SER B CB  
3166 O OG  . SER B 82  ? 0.2929 0.2194 0.3783 -0.0255 -0.1231 -0.0292 305  SER B OG  
3167 N N   . ILE B 83  ? 0.2174 0.1285 0.2985 0.0351  -0.1113 0.0123  306  ILE B N   
3168 C CA  . ILE B 83  ? 0.2032 0.1400 0.3268 0.0219  -0.1062 -0.0053 306  ILE B CA  
3169 C C   . ILE B 83  ? 0.1950 0.1614 0.3260 0.0603  -0.1036 -0.0073 306  ILE B C   
3170 O O   . ILE B 83  ? 0.2495 0.1691 0.3889 0.0583  -0.0739 0.0127  306  ILE B O   
3171 C CB  . ILE B 83  ? 0.1963 0.1386 0.3261 -0.0093 -0.0788 -0.0038 306  ILE B CB  
3172 C CG1 . ILE B 83  ? 0.1962 0.1588 0.3325 0.0110  -0.1138 0.0202  306  ILE B CG1 
3173 C CG2 . ILE B 83  ? 0.2223 0.1640 0.3022 -0.0200 -0.0405 0.0128  306  ILE B CG2 
3174 C CD1 . ILE B 83  ? 0.2091 0.1752 0.3605 -0.0029 -0.0890 0.0231  306  ILE B CD1 
3175 N N   . THR B 84  ? 0.2086 0.1625 0.3300 0.0397  -0.0877 -0.0360 307  THR B N   
3176 C CA  . THR B 84  ? 0.2390 0.1894 0.3637 0.0326  -0.0673 -0.0312 307  THR B CA  
3177 C C   . THR B 84  ? 0.2960 0.2046 0.3702 0.0343  -0.0604 -0.0370 307  THR B C   
3178 O O   . THR B 84  ? 0.2645 0.2046 0.3371 0.0427  -0.0786 -0.0477 307  THR B O   
3179 C CB  . THR B 84  ? 0.2301 0.2050 0.3952 0.0264  -0.0372 0.0015  307  THR B CB  
3180 O OG1 . THR B 84  ? 0.2586 0.1966 0.4100 0.0159  -0.0063 0.0140  307  THR B OG1 
3181 C CG2 . THR B 84  ? 0.2235 0.2304 0.4166 0.0159  -0.0465 -0.0128 307  THR B CG2 
3182 N N   . ASN B 85  ? 0.3486 0.2005 0.3866 0.0271  -0.0589 -0.0421 308  ASN B N   
3183 C CA  . ASN B 85  ? 0.3990 0.2075 0.4211 0.0057  -0.0649 -0.0342 308  ASN B CA  
3184 C C   . ASN B 85  ? 0.4373 0.1983 0.4113 0.0137  -0.1116 0.0004  308  ASN B C   
3185 O O   . ASN B 85  ? 0.4423 0.1895 0.4046 0.0027  -0.0838 -0.0251 308  ASN B O   
3186 C CB  . ASN B 85  ? 0.4067 0.2126 0.4380 0.0007  -0.0290 -0.0471 308  ASN B CB  
3187 C CG  . ASN B 85  ? 0.3921 0.2438 0.4717 0.0111  -0.0140 -0.0347 308  ASN B CG  
3188 O OD1 . ASN B 85  ? 0.3730 0.2316 0.4900 0.0261  -0.0243 -0.0051 308  ASN B OD1 
3189 N ND2 . ASN B 85  ? 0.4317 0.2690 0.4884 -0.0012 0.0339  -0.0536 308  ASN B ND2 
3190 N N   . PRO B 86  ? 0.4667 0.2241 0.4413 0.0170  -0.1681 0.0357  309  PRO B N   
3191 C CA  . PRO B 86  ? 0.5202 0.2855 0.4742 0.0228  -0.1439 0.0506  309  PRO B CA  
3192 C C   . PRO B 86  ? 0.6198 0.3764 0.5296 0.0268  -0.0510 0.0580  309  PRO B C   
3193 O O   . PRO B 86  ? 0.6287 0.3544 0.4993 0.0151  -0.0749 0.0676  309  PRO B O   
3194 C CB  . PRO B 86  ? 0.4964 0.2695 0.4339 0.0139  -0.2010 0.0548  309  PRO B CB  
3195 C CG  . PRO B 86  ? 0.4750 0.2441 0.4343 0.0083  -0.2075 0.0428  309  PRO B CG  
3196 C CD  . PRO B 86  ? 0.4642 0.2308 0.4258 0.0034  -0.2190 0.0317  309  PRO B CD  
3197 N N   . ASN B 87  ? 0.6850 0.4855 0.5991 0.0072  0.0496  0.0457  310  ASN B N   
3198 C CA  . ASN B 87  ? 0.7280 0.5892 0.6647 0.0056  0.1400  0.0449  310  ASN B CA  
3199 C C   . ASN B 87  ? 0.7682 0.5550 0.6694 0.0022  0.2212  0.0501  310  ASN B C   
3200 O O   . ASN B 87  ? 0.7891 0.5605 0.6710 0.0064  0.2505  0.0504  310  ASN B O   
3205 N N   . GLY B 88  ? 0.7697 0.5172 0.6658 -0.0103 0.2590  0.0517  311  GLY B N   
3206 C CA  . GLY B 88  ? 0.7580 0.4901 0.6798 -0.0182 0.2992  0.0444  311  GLY B CA  
3207 C C   . GLY B 88  ? 0.7358 0.4609 0.7096 -0.0228 0.3338  0.0227  311  GLY B C   
3208 O O   . GLY B 88  ? 0.7625 0.4540 0.7169 -0.0320 0.3613  0.0124  311  GLY B O   
3209 N N   . THR B 89  ? 0.6752 0.4353 0.7353 -0.0192 0.3176  0.0076  312  THR B N   
3210 C CA  . THR B 89  ? 0.6117 0.4181 0.7705 -0.0018 0.2930  -0.0038 312  THR B CA  
3211 C C   . THR B 89  ? 0.5068 0.3932 0.8059 -0.0079 0.2584  -0.0120 312  THR B C   
3212 O O   . THR B 89  ? 0.4642 0.3616 0.8029 -0.0098 0.2654  -0.0298 312  THR B O   
3213 C CB  . THR B 89  ? 0.6399 0.4283 0.7740 0.0379  0.3101  -0.0087 312  THR B CB  
3214 N N   . PRO B 90  ? 0.4168 0.3980 0.8427 -0.0177 0.1973  -0.0073 313  PRO B N   
3215 C CA  A PRO B 90  ? 0.3981 0.3991 0.8418 -0.0105 0.1787  -0.0034 313  PRO B CA  
3216 C CA  B PRO B 90  ? 0.3880 0.4022 0.8492 -0.0149 0.1767  -0.0035 313  PRO B CA  
3217 C C   . PRO B 90  ? 0.3689 0.4028 0.8343 0.0002  0.1545  -0.0023 313  PRO B C   
3218 O O   . PRO B 90  ? 0.3852 0.4030 0.8380 0.0197  0.1656  -0.0220 313  PRO B O   
3219 C CB  A PRO B 90  ? 0.4043 0.3976 0.8476 -0.0137 0.1815  -0.0017 313  PRO B CB  
3220 C CB  B PRO B 90  ? 0.3934 0.4047 0.8696 -0.0233 0.1937  0.0008  313  PRO B CB  
3221 C CG  A PRO B 90  ? 0.4067 0.3966 0.8492 -0.0161 0.1841  -0.0019 313  PRO B CG  
3222 C CG  B PRO B 90  ? 0.3825 0.4049 0.8735 -0.0384 0.1879  0.0004  313  PRO B CG  
3223 C CD  A PRO B 90  ? 0.4117 0.3971 0.8472 -0.0179 0.1919  -0.0036 313  PRO B CD  
3224 C CD  B PRO B 90  ? 0.3991 0.4024 0.8637 -0.0325 0.1949  0.0001  313  PRO B CD  
3225 N N   . PHE B 91  ? 0.2857 0.4038 0.8011 0.0120  0.0824  0.0210  314  PHE B N   
3226 C CA  . PHE B 91  ? 0.2203 0.4134 0.7737 0.0338  0.0173  0.0414  314  PHE B CA  
3227 C C   . PHE B 91  ? 0.2705 0.4467 0.8304 0.0545  0.0363  0.0711  314  PHE B C   
3228 O O   . PHE B 91  ? 0.2591 0.4588 0.8285 0.0639  0.0058  0.0680  314  PHE B O   
3229 C CB  . PHE B 91  ? 0.2164 0.3945 0.7032 0.0352  -0.0132 0.0516  314  PHE B CB  
3230 C CG  . PHE B 91  ? 0.1972 0.3699 0.6417 0.0554  -0.0475 0.0751  314  PHE B CG  
3231 C CD1 . PHE B 91  ? 0.1959 0.3615 0.6020 0.0667  -0.0536 0.0851  314  PHE B CD1 
3232 C CD2 . PHE B 91  ? 0.1979 0.3724 0.6314 0.0567  -0.0464 0.0674  314  PHE B CD2 
3233 C CE1 . PHE B 91  ? 0.1989 0.3523 0.5874 0.0789  -0.0372 0.0881  314  PHE B CE1 
3234 C CE2 . PHE B 91  ? 0.1857 0.3771 0.6127 0.0573  -0.0512 0.0731  314  PHE B CE2 
3235 C CZ  . PHE B 91  ? 0.1953 0.3673 0.6022 0.0682  -0.0429 0.0789  314  PHE B CZ  
3236 N N   . ASP B 92  ? 0.3079 0.4726 0.8925 0.0768  0.0750  0.0946  315  ASP B N   
3237 C CA  . ASP B 92  ? 0.3647 0.5047 0.9450 0.0882  0.1114  0.1325  315  ASP B CA  
3238 C C   . ASP B 92  ? 0.3867 0.5300 0.9564 0.0810  0.0971  0.1574  315  ASP B C   
3239 O O   . ASP B 92  ? 0.3863 0.5172 0.9568 0.0787  0.1315  0.1696  315  ASP B O   
3240 C CB  . ASP B 92  ? 0.4013 0.5123 0.9852 0.1118  0.1705  0.1447  315  ASP B CB  
3241 C CG  . ASP B 92  ? 0.4442 0.5200 1.0190 0.1345  0.2178  0.1562  315  ASP B CG  
3242 O OD1 . ASP B 92  ? 0.4432 0.5212 1.0236 0.1283  0.2280  0.1684  315  ASP B OD1 
3243 O OD2 . ASP B 92  ? 0.4800 0.5202 1.0342 0.1534  0.2550  0.1534  315  ASP B OD2 
3244 N N   . PRO B 93  ? 0.4114 0.5661 0.9678 0.0572  0.0453  0.1606  316  PRO B N   
3245 C CA  . PRO B 93  ? 0.4149 0.5842 0.9812 0.0458  0.0188  0.1676  316  PRO B CA  
3246 C C   . PRO B 93  ? 0.4204 0.5910 1.0012 0.0551  0.0136  0.1869  316  PRO B C   
3247 O O   . PRO B 93  ? 0.4056 0.5946 1.0086 0.0597  0.0007  0.1939  316  PRO B O   
3248 C CB  . PRO B 93  ? 0.4284 0.5901 0.9775 0.0347  0.0135  0.1610  316  PRO B CB  
3249 C CG  . PRO B 93  ? 0.4443 0.5878 0.9708 0.0322  0.0188  0.1573  316  PRO B CG  
3250 C CD  . PRO B 93  ? 0.4386 0.5787 0.9676 0.0369  0.0360  0.1568  316  PRO B CD  
3251 N N   . THR B 94  ? 0.4301 0.5967 0.9952 0.0687  0.0025  0.1891  317  THR B N   
3252 C CA  . THR B 94  ? 0.4383 0.6072 0.9746 0.0683  -0.0204 0.1848  317  THR B CA  
3253 C C   . THR B 94  ? 0.4929 0.6285 0.9274 0.0706  -0.0264 0.1798  317  THR B C   
3254 O O   . THR B 94  ? 0.4965 0.6288 0.9363 0.0637  -0.0284 0.1809  317  THR B O   
3255 C CB  . THR B 94  ? 0.3817 0.5942 0.9896 0.0681  -0.0452 0.1800  317  THR B CB  
3256 O OG1 . THR B 94  ? 0.3637 0.5899 1.0007 0.0689  -0.0405 0.1776  317  THR B OG1 
3257 C CG2 . THR B 94  ? 0.3897 0.5902 0.9960 0.0593  -0.0418 0.1717  317  THR B CG2 
3258 N N   . GLU B 95  ? 0.5530 0.6518 0.8765 0.0808  -0.0172 0.1634  318  GLU B N   
3259 C CA  . GLU B 95  ? 0.6246 0.6754 0.8202 0.0909  -0.0052 0.1387  318  GLU B CA  
3260 C C   . GLU B 95  ? 0.5297 0.5766 0.7820 0.0913  0.0125  0.1014  318  GLU B C   
3261 O O   . GLU B 95  ? 0.4844 0.5718 0.7866 0.0827  -0.0055 0.1098  318  GLU B O   
3267 N N   . ASP B 96  ? 0.5176 0.4852 0.7349 0.0916  0.0676  0.0521  319  ASP B N   
3268 C CA  A ASP B 96  ? 0.5183 0.4372 0.7054 0.0857  0.0916  0.0281  319  ASP B CA  
3269 C CA  B ASP B 96  ? 0.5183 0.4372 0.7054 0.0857  0.0917  0.0281  319  ASP B CA  
3270 C C   . ASP B 96  ? 0.4665 0.3892 0.6691 0.0642  0.0780  -0.0069 319  ASP B C   
3271 O O   . ASP B 96  ? 0.4860 0.3771 0.6810 0.0584  0.1359  -0.0312 319  ASP B O   
3272 C CB  A ASP B 96  ? 0.5711 0.4369 0.7130 0.1025  0.1251  0.0364  319  ASP B CB  
3273 C CB  B ASP B 96  ? 0.5711 0.4369 0.7130 0.1025  0.1251  0.0364  319  ASP B CB  
3274 C CG  A ASP B 96  ? 0.6198 0.4411 0.7243 0.1004  0.1654  0.0435  319  ASP B CG  
3275 C CG  B ASP B 96  ? 0.6198 0.4411 0.7243 0.1004  0.1655  0.0435  319  ASP B CG  
3276 O OD1 . ASP B 96  ? 0.6380 0.4375 0.7168 0.0981  0.1706  0.0567  319  ASP B OD1 
3277 O OD2 . ASP B 96  ? 0.6293 0.4435 0.7318 0.1044  0.1755  0.0452  319  ASP B OD2 
3278 N N   A VAL B 97  ? 0.4002 0.3393 0.6298 0.0550  0.0330  -0.0418 320  VAL B N   
3279 N N   B VAL B 97  ? 0.4093 0.3479 0.6229 0.0561  0.0267  -0.0236 320  VAL B N   
3280 C CA  A VAL B 97  ? 0.3486 0.3044 0.5927 0.0299  -0.0149 -0.0750 320  VAL B CA  
3281 C CA  B VAL B 97  ? 0.3520 0.3077 0.5776 0.0429  -0.0273 -0.0431 320  VAL B CA  
3282 C C   A VAL B 97  ? 0.3245 0.2590 0.5472 0.0320  -0.0608 -0.0944 320  VAL B C   
3283 C C   B VAL B 97  ? 0.3185 0.2663 0.5346 0.0360  -0.0678 -0.0629 320  VAL B C   
3284 O O   A VAL B 97  ? 0.2958 0.2690 0.5532 0.0356  -0.0973 -0.1187 320  VAL B O   
3285 O O   B VAL B 97  ? 0.3121 0.2740 0.5330 0.0374  -0.0737 -0.0582 320  VAL B O   
3286 C CB  A VAL B 97  ? 0.3476 0.3206 0.6075 -0.0125 -0.0097 -0.0858 320  VAL B CB  
3287 C CB  B VAL B 97  ? 0.3344 0.3083 0.5755 0.0363  -0.0368 -0.0418 320  VAL B CB  
3288 C CG1 A VAL B 97  ? 0.3485 0.3160 0.6176 -0.0069 0.0028  -0.0862 320  VAL B CG1 
3289 C CG1 B VAL B 97  ? 0.3266 0.3118 0.5771 0.0332  -0.0408 -0.0413 320  VAL B CG1 
3290 C CG2 A VAL B 97  ? 0.3404 0.3341 0.6159 -0.0423 -0.0303 -0.0889 320  VAL B CG2 
3291 C CG2 B VAL B 97  ? 0.3254 0.3037 0.5725 0.0371  -0.0435 -0.0401 320  VAL B CG2 
3292 N N   . PRO B 98  ? 0.2773 0.2192 0.4958 0.0282  -0.1048 -0.0848 321  PRO B N   
3293 C CA  . PRO B 98  ? 0.2747 0.2001 0.4728 0.0200  -0.1203 -0.0671 321  PRO B CA  
3294 C C   . PRO B 98  ? 0.2360 0.1989 0.4108 0.0020  -0.1642 -0.0492 321  PRO B C   
3295 O O   . PRO B 98  ? 0.2528 0.2087 0.4258 0.0281  -0.1817 -0.0222 321  PRO B O   
3296 C CB  . PRO B 98  ? 0.2514 0.2061 0.4731 0.0124  -0.1298 -0.0782 321  PRO B CB  
3297 C CG  . PRO B 98  ? 0.2750 0.2072 0.4788 0.0064  -0.1208 -0.0970 321  PRO B CG  
3298 C CD  . PRO B 98  ? 0.2546 0.2193 0.4888 0.0167  -0.1291 -0.0892 321  PRO B CD  
3299 N N   . ALA B 99  ? 0.2305 0.1689 0.3931 0.0273  -0.1217 -0.0294 322  ALA B N   
3300 C CA  . ALA B 99  ? 0.1961 0.1715 0.3720 0.0373  -0.1129 -0.0189 322  ALA B CA  
3301 C C   . ALA B 99  ? 0.1996 0.1885 0.3253 0.0275  -0.1044 -0.0243 322  ALA B C   
3302 O O   . ALA B 99  ? 0.2050 0.2032 0.3253 0.0285  -0.0990 -0.0311 322  ALA B O   
3303 C CB  . ALA B 99  ? 0.2012 0.1803 0.3639 0.0204  -0.1269 -0.0200 322  ALA B CB  
3304 N N   . PRO B 100 ? 0.2137 0.1823 0.2886 0.0190  -0.1132 -0.0148 323  PRO B N   
3305 C CA  . PRO B 100 ? 0.2104 0.1842 0.2727 0.0022  -0.1133 0.0126  323  PRO B CA  
3306 C C   . PRO B 100 ? 0.1887 0.1875 0.2489 0.0176  -0.0971 0.0225  323  PRO B C   
3307 O O   . PRO B 100 ? 0.1947 0.2089 0.2881 0.0270  -0.0937 0.0166  323  PRO B O   
3308 C CB  . PRO B 100 ? 0.2325 0.1826 0.2892 -0.0003 -0.1045 0.0168  323  PRO B CB  
3309 C CG  . PRO B 100 ? 0.2354 0.1737 0.3220 0.0523  -0.0979 0.0207  323  PRO B CG  
3310 C CD  . PRO B 100 ? 0.2189 0.1881 0.3068 0.0457  -0.1151 -0.0041 323  PRO B CD  
3311 N N   . LEU B 101 ? 0.1687 0.1575 0.2591 0.0159  -0.0822 0.0102  324  LEU B N   
3312 C CA  . LEU B 101 ? 0.1388 0.1721 0.2508 0.0200  -0.0633 0.0250  324  LEU B CA  
3313 C C   . LEU B 101 ? 0.1449 0.1727 0.2718 0.0053  -0.0561 0.0036  324  LEU B C   
3314 O O   . LEU B 101 ? 0.1840 0.1788 0.3118 -0.0034 -0.0479 0.0057  324  LEU B O   
3315 C CB  . LEU B 101 ? 0.1772 0.2102 0.2903 0.0373  -0.0197 0.0384  324  LEU B CB  
3316 C CG  . LEU B 101 ? 0.2230 0.2257 0.3208 0.0308  0.0178  0.0595  324  LEU B CG  
3317 C CD1 . LEU B 101 ? 0.2853 0.2714 0.3455 0.0145  0.0687  0.0662  324  LEU B CD1 
3318 C CD2 . LEU B 101 ? 0.2440 0.2302 0.3474 0.0129  0.0075  0.0154  324  LEU B CD2 
3319 N N   . GLY B 102 ? 0.1249 0.1381 0.2400 0.0168  -0.0439 -0.0068 325  GLY B N   
3320 C CA  . GLY B 102 ? 0.1503 0.1331 0.2262 0.0329  -0.0579 0.0082  325  GLY B CA  
3321 C C   . GLY B 102 ? 0.1582 0.1084 0.2003 0.0168  -0.0682 0.0173  325  GLY B C   
3322 O O   . GLY B 102 ? 0.1629 0.1141 0.2400 0.0142  -0.0511 0.0110  325  GLY B O   
3323 N N   . THR B 103 ? 0.1786 0.1092 0.1918 0.0126  -0.0670 0.0087  326  THR B N   
3324 C CA  . THR B 103 ? 0.1828 0.1139 0.1814 0.0194  -0.0635 0.0013  326  THR B CA  
3325 C C   . THR B 103 ? 0.1911 0.1113 0.1809 0.0048  -0.0564 0.0062  326  THR B C   
3326 O O   . THR B 103 ? 0.2210 0.0908 0.1860 0.0120  -0.0778 0.0037  326  THR B O   
3327 C CB  . THR B 103 ? 0.1842 0.1157 0.2234 0.0140  -0.0598 0.0004  326  THR B CB  
3328 O OG1 . THR B 103 ? 0.1696 0.1528 0.2576 0.0032  -0.0803 -0.0013 326  THR B OG1 
3329 C CG2 . THR B 103 ? 0.2173 0.1195 0.2159 0.0015  -0.0695 -0.0068 326  THR B CG2 
3330 N N   . PRO B 104 ? 0.1894 0.0998 0.1804 -0.0142 -0.0955 -0.0184 327  PRO B N   
3331 C CA  . PRO B 104 ? 0.2129 0.1035 0.1795 0.0032  -0.0643 -0.0228 327  PRO B CA  
3332 C C   . PRO B 104 ? 0.1967 0.1094 0.1693 0.0053  -0.0896 -0.0105 327  PRO B C   
3333 O O   . PRO B 104 ? 0.2016 0.1188 0.1975 -0.0072 -0.0911 -0.0024 327  PRO B O   
3334 C CB  . PRO B 104 ? 0.2163 0.1175 0.2130 -0.0175 -0.0598 -0.0366 327  PRO B CB  
3335 C CG  . PRO B 104 ? 0.2301 0.1345 0.2138 -0.0346 -0.0752 -0.0360 327  PRO B CG  
3336 C CD  . PRO B 104 ? 0.2543 0.1290 0.1751 -0.0254 -0.0778 -0.0176 327  PRO B CD  
3337 N N   . ASP B 105 ? 0.1963 0.0993 0.1632 -0.0254 -0.0549 -0.0199 328  ASP B N   
3338 C CA  . ASP B 105 ? 0.2051 0.0952 0.1435 -0.0029 -0.0607 -0.0070 328  ASP B CA  
3339 C C   . ASP B 105 ? 0.2100 0.1075 0.1564 -0.0047 -0.0727 0.0033  328  ASP B C   
3340 O O   . ASP B 105 ? 0.2686 0.1258 0.1916 -0.0352 -0.0376 -0.0204 328  ASP B O   
3341 C CB  . ASP B 105 ? 0.2059 0.1098 0.1526 -0.0184 -0.0773 -0.0074 328  ASP B CB  
3342 C CG  . ASP B 105 ? 0.2047 0.0919 0.1468 -0.0165 -0.0662 0.0118  328  ASP B CG  
3343 O OD1 . ASP B 105 ? 0.2041 0.1067 0.1567 -0.0083 -0.0465 0.0059  328  ASP B OD1 
3344 O OD2 . ASP B 105 ? 0.1878 0.0906 0.1523 -0.0051 -0.0581 0.0050  328  ASP B OD2 
3345 N N   . PHE B 106 ? 0.1832 0.1109 0.1475 -0.0243 -0.0425 -0.0104 329  PHE B N   
3346 C CA  . PHE B 106 ? 0.1929 0.1035 0.1434 0.0008  -0.0748 0.0074  329  PHE B CA  
3347 C C   . PHE B 106 ? 0.2261 0.0960 0.1529 0.0105  -0.0685 -0.0105 329  PHE B C   
3348 O O   . PHE B 106 ? 0.2209 0.1254 0.1823 -0.0206 -0.0655 -0.0019 329  PHE B O   
3349 C CB  . PHE B 106 ? 0.2126 0.0943 0.1726 -0.0082 -0.0793 -0.0032 329  PHE B CB  
3350 C CG  . PHE B 106 ? 0.2030 0.0827 0.1828 -0.0103 -0.0636 0.0099  329  PHE B CG  
3351 C CD1 . PHE B 106 ? 0.2057 0.0948 0.1886 -0.0097 -0.0399 0.0047  329  PHE B CD1 
3352 C CD2 . PHE B 106 ? 0.2029 0.1095 0.1995 -0.0074 -0.0759 0.0352  329  PHE B CD2 
3353 C CE1 . PHE B 106 ? 0.1988 0.1085 0.2296 -0.0018 -0.0516 0.0023  329  PHE B CE1 
3354 C CE2 . PHE B 106 ? 0.2086 0.1180 0.2321 0.0086  -0.0668 0.0144  329  PHE B CE2 
3355 C CZ  . PHE B 106 ? 0.2052 0.1049 0.2427 -0.0155 -0.0436 0.0177  329  PHE B CZ  
3356 N N   . LYS B 107 ? 0.2494 0.1013 0.1592 0.0068  -0.0606 0.0044  330  LYS B N   
3357 C CA  . LYS B 107 ? 0.2418 0.0809 0.1570 0.0015  -0.0510 0.0108  330  LYS B CA  
3358 C C   . LYS B 107 ? 0.2272 0.0854 0.1685 -0.0037 -0.0969 -0.0096 330  LYS B C   
3359 O O   . LYS B 107 ? 0.2268 0.1161 0.1841 0.0005  -0.0896 -0.0074 330  LYS B O   
3360 C CB  . LYS B 107 ? 0.2475 0.0941 0.1773 -0.0112 -0.0590 0.0256  330  LYS B CB  
3361 C CG  . LYS B 107 ? 0.2313 0.1159 0.1637 -0.0055 -0.0914 0.0413  330  LYS B CG  
3362 C CD  . LYS B 107 ? 0.2821 0.1145 0.1848 -0.0066 -0.0796 0.0497  330  LYS B CD  
3363 C CE  . LYS B 107 ? 0.2995 0.1457 0.2273 0.0020  -0.1052 0.0620  330  LYS B CE  
3364 N NZ  . LYS B 107 ? 0.3675 0.1454 0.2687 0.0053  -0.0943 0.0611  330  LYS B NZ  
3365 N N   . GLY B 108 ? 0.2581 0.0788 0.1597 -0.0015 -0.0787 -0.0123 331  GLY B N   
3366 C CA  . GLY B 108 ? 0.2532 0.0782 0.1994 0.0054  -0.0706 -0.0172 331  GLY B CA  
3367 C C   . GLY B 108 ? 0.2493 0.0736 0.1941 -0.0058 -0.0660 0.0002  331  GLY B C   
3368 O O   . GLY B 108 ? 0.2366 0.1146 0.1928 -0.0184 -0.0656 -0.0139 331  GLY B O   
3369 N N   . GLN B 109 ? 0.2692 0.0787 0.1648 -0.0074 -0.0798 0.0064  332  GLN B N   
3370 C CA  . GLN B 109 ? 0.2874 0.0869 0.1376 -0.0168 -0.0609 -0.0106 332  GLN B CA  
3371 C C   . GLN B 109 ? 0.2531 0.1110 0.1179 -0.0191 -0.0763 0.0105  332  GLN B C   
3372 O O   . GLN B 109 ? 0.2258 0.1368 0.1485 0.0099  -0.0724 0.0000  332  GLN B O   
3373 C CB  . GLN B 109 ? 0.3061 0.1021 0.1376 -0.0213 -0.0707 0.0056  332  GLN B CB  
3374 C CG  . GLN B 109 ? 0.3126 0.1244 0.1688 -0.0261 -0.0858 0.0189  332  GLN B CG  
3375 C CD  . GLN B 109 ? 0.3570 0.1307 0.2062 -0.0271 -0.0920 0.0186  332  GLN B CD  
3376 O OE1 . GLN B 109 ? 0.3706 0.1431 0.2949 -0.0386 -0.1052 0.0204  332  GLN B OE1 
3377 N NE2 . GLN B 109 ? 0.3959 0.1404 0.1798 -0.0175 -0.0878 0.0090  332  GLN B NE2 
3378 N N   . LEU B 110 ? 0.2409 0.1124 0.1280 -0.0243 -0.0608 0.0122  333  LEU B N   
3379 C CA  . LEU B 110 ? 0.2298 0.0934 0.1465 -0.0274 -0.0500 -0.0010 333  LEU B CA  
3380 C C   . LEU B 110 ? 0.1957 0.0959 0.1792 -0.0211 -0.0747 0.0071  333  LEU B C   
3381 O O   . LEU B 110 ? 0.2117 0.1097 0.1922 0.0054  -0.0888 -0.0211 333  LEU B O   
3382 C CB  . LEU B 110 ? 0.2081 0.0986 0.1615 -0.0031 -0.0289 0.0001  333  LEU B CB  
3383 C CG  . LEU B 110 ? 0.1811 0.1160 0.1431 0.0089  -0.0565 0.0051  333  LEU B CG  
3384 C CD1 . LEU B 110 ? 0.2061 0.1339 0.1634 0.0168  -0.0724 0.0178  333  LEU B CD1 
3385 C CD2 . LEU B 110 ? 0.1629 0.1215 0.2057 0.0228  -0.0220 0.0007  333  LEU B CD2 
3386 N N   . TYR B 111 ? 0.1967 0.0861 0.1750 -0.0053 -0.0469 0.0092  334  TYR B N   
3387 C CA  . TYR B 111 ? 0.1866 0.0911 0.1495 -0.0043 -0.0349 0.0090  334  TYR B CA  
3388 C C   . TYR B 111 ? 0.1809 0.0936 0.1428 -0.0225 -0.0528 0.0041  334  TYR B C   
3389 O O   . TYR B 111 ? 0.1927 0.1222 0.1541 -0.0201 -0.0589 0.0057  334  TYR B O   
3390 C CB  . TYR B 111 ? 0.1691 0.0934 0.1690 0.0259  -0.0236 0.0007  334  TYR B CB  
3391 C CG  . TYR B 111 ? 0.1769 0.1092 0.1628 0.0140  -0.0401 0.0013  334  TYR B CG  
3392 C CD1 . TYR B 111 ? 0.2194 0.1042 0.1710 -0.0159 -0.0360 0.0025  334  TYR B CD1 
3393 C CD2 . TYR B 111 ? 0.1998 0.1249 0.1514 0.0385  -0.0364 0.0047  334  TYR B CD2 
3394 C CE1 . TYR B 111 ? 0.2217 0.1063 0.1585 0.0019  -0.0312 -0.0174 334  TYR B CE1 
3395 C CE2 . TYR B 111 ? 0.2177 0.0997 0.1496 0.0180  -0.0383 -0.0290 334  TYR B CE2 
3396 C CZ  . TYR B 111 ? 0.2221 0.1037 0.1872 0.0209  -0.0334 -0.0182 334  TYR B CZ  
3397 O OH  . TYR B 111 ? 0.2237 0.1172 0.2001 -0.0019 -0.0395 -0.0214 334  TYR B OH  
3398 N N   . GLY B 112 ? 0.1968 0.0732 0.1336 -0.0174 -0.0510 0.0115  335  GLY B N   
3399 C CA  . GLY B 112 ? 0.1978 0.0869 0.1572 -0.0234 -0.0587 0.0047  335  GLY B CA  
3400 C C   . GLY B 112 ? 0.1876 0.0918 0.1385 -0.0060 -0.0688 -0.0033 335  GLY B C   
3401 O O   . GLY B 112 ? 0.2155 0.1025 0.1311 -0.0245 -0.0584 -0.0040 335  GLY B O   
3402 N N   . VAL B 113 ? 0.1808 0.0822 0.1543 -0.0050 -0.0488 0.0047  336  VAL B N   
3403 C CA  . VAL B 113 ? 0.1922 0.0894 0.1598 -0.0244 -0.0714 -0.0004 336  VAL B CA  
3404 C C   . VAL B 113 ? 0.1755 0.0865 0.1652 -0.0079 -0.0590 0.0033  336  VAL B C   
3405 O O   . VAL B 113 ? 0.1876 0.0971 0.1752 -0.0132 -0.0589 -0.0127 336  VAL B O   
3406 C CB  . VAL B 113 ? 0.1465 0.0806 0.1650 -0.0122 -0.0452 0.0011  336  VAL B CB  
3407 C CG1 . VAL B 113 ? 0.1661 0.0762 0.1831 -0.0353 -0.0463 0.0091  336  VAL B CG1 
3408 C CG2 . VAL B 113 ? 0.1694 0.1079 0.1760 0.0096  -0.0391 -0.0106 336  VAL B CG2 
3409 N N   . ILE B 114 ? 0.1407 0.0969 0.1554 -0.0129 -0.0666 0.0233  337  ILE B N   
3410 C CA  . ILE B 114 ? 0.1599 0.1154 0.1867 -0.0201 -0.0566 0.0207  337  ILE B CA  
3411 C C   . ILE B 114 ? 0.1704 0.1136 0.1539 -0.0242 -0.0597 0.0127  337  ILE B C   
3412 O O   . ILE B 114 ? 0.2034 0.1155 0.1524 -0.0133 -0.0296 -0.0013 337  ILE B O   
3413 C CB  . ILE B 114 ? 0.1674 0.1328 0.1902 0.0047  -0.0997 0.0015  337  ILE B CB  
3414 C CG1 . ILE B 114 ? 0.2020 0.1544 0.2089 0.0336  -0.1156 0.0013  337  ILE B CG1 
3415 C CG2 . ILE B 114 ? 0.2116 0.1428 0.1794 -0.0075 -0.0692 -0.0291 337  ILE B CG2 
3416 C CD1 . ILE B 114 ? 0.2350 0.1750 0.2267 0.0255  -0.1012 0.0010  337  ILE B CD1 
3417 N N   A SER B 115 ? 0.1866 0.1058 0.1390 -0.0240 -0.0342 0.0190  338  SER B N   
3418 N N   B SER B 115 ? 0.1607 0.1086 0.1522 -0.0211 -0.0576 0.0036  338  SER B N   
3419 C CA  A SER B 115 ? 0.1726 0.1010 0.1617 -0.0360 -0.0531 0.0082  338  SER B CA  
3420 C CA  B SER B 115 ? 0.1460 0.0979 0.1610 -0.0199 -0.0632 -0.0091 338  SER B CA  
3421 C C   A SER B 115 ? 0.1711 0.0898 0.1733 0.0006  -0.0512 -0.0035 338  SER B C   
3422 C C   B SER B 115 ? 0.1532 0.0951 0.1681 -0.0075 -0.0684 -0.0095 338  SER B C   
3423 O O   A SER B 115 ? 0.1762 0.0883 0.2366 -0.0075 -0.0653 -0.0228 338  SER B O   
3424 O O   B SER B 115 ? 0.1553 0.1005 0.1762 -0.0107 -0.0842 -0.0121 338  SER B O   
3425 C CB  A SER B 115 ? 0.1574 0.1283 0.1517 -0.0242 -0.0910 0.0196  338  SER B CB  
3426 C CB  B SER B 115 ? 0.1232 0.0952 0.1563 -0.0139 -0.0718 -0.0193 338  SER B CB  
3427 O OG  A SER B 115 ? 0.1602 0.1248 0.1455 -0.0230 -0.0766 0.0084  338  SER B OG  
3428 O OG  B SER B 115 ? 0.1012 0.0871 0.1417 -0.0027 -0.0647 -0.0211 338  SER B OG  
3429 N N   . GLN B 116 ? 0.1595 0.0919 0.1769 -0.0075 -0.0621 -0.0158 339  GLN B N   
3430 C CA  . GLN B 116 ? 0.1802 0.1079 0.1862 -0.0291 -0.0686 -0.0123 339  GLN B CA  
3431 C C   . GLN B 116 ? 0.1576 0.0930 0.1781 -0.0235 -0.0620 -0.0008 339  GLN B C   
3432 O O   . GLN B 116 ? 0.1857 0.1121 0.1741 -0.0018 -0.0573 0.0168  339  GLN B O   
3433 C CB  . GLN B 116 ? 0.2103 0.1080 0.1762 -0.0282 -0.0939 0.0125  339  GLN B CB  
3434 C CG  . GLN B 116 ? 0.2050 0.1137 0.1947 -0.0244 -0.1046 0.0103  339  GLN B CG  
3435 C CD  . GLN B 116 ? 0.2209 0.1039 0.2188 -0.0299 -0.1156 0.0037  339  GLN B CD  
3436 O OE1 . GLN B 116 ? 0.2576 0.1010 0.2192 -0.0149 -0.1193 0.0039  339  GLN B OE1 
3437 N NE2 . GLN B 116 ? 0.2276 0.1119 0.2448 -0.0134 -0.1175 0.0206  339  GLN B NE2 
3438 N N   . ARG B 117 ? 0.1621 0.1130 0.1916 -0.0207 -0.0346 -0.0261 340  ARG B N   
3439 C CA  . ARG B 117 ? 0.1621 0.1396 0.1878 -0.0337 -0.0495 -0.0066 340  ARG B CA  
3440 C C   . ARG B 117 ? 0.1774 0.1385 0.2208 -0.0192 -0.0507 0.0036  340  ARG B C   
3441 O O   . ARG B 117 ? 0.1794 0.1340 0.2589 -0.0074 -0.0410 -0.0075 340  ARG B O   
3442 C CB  . ARG B 117 ? 0.1814 0.1589 0.1874 -0.0251 -0.0279 -0.0069 340  ARG B CB  
3443 C CG  . ARG B 117 ? 0.1814 0.1789 0.1782 -0.0326 -0.0501 0.0004  340  ARG B CG  
3444 C CD  . ARG B 117 ? 0.2151 0.2084 0.2241 -0.0183 -0.0578 0.0027  340  ARG B CD  
3445 N NE  . ARG B 117 ? 0.2080 0.1973 0.2595 -0.0254 -0.0842 0.0202  340  ARG B NE  
3446 C CZ  . ARG B 117 ? 0.2050 0.1809 0.2224 -0.0332 -0.1053 -0.0087 340  ARG B CZ  
3447 N NH1 . ARG B 117 ? 0.2406 0.1959 0.2722 -0.0376 -0.0607 -0.0306 340  ARG B NH1 
3448 N NH2 . ARG B 117 ? 0.1759 0.1754 0.2025 -0.0081 -0.0934 0.0057  340  ARG B NH2 
3449 N N   . ASN B 118 ? 0.1591 0.1391 0.2020 -0.0098 -0.0500 0.0036  341  ASN B N   
3450 C CA  . ASN B 118 ? 0.1691 0.1476 0.2358 -0.0148 -0.0562 -0.0319 341  ASN B CA  
3451 C C   . ASN B 118 ? 0.1581 0.1558 0.2521 -0.0195 -0.0619 -0.0268 341  ASN B C   
3452 O O   . ASN B 118 ? 0.1991 0.1773 0.2394 -0.0179 -0.0440 -0.0095 341  ASN B O   
3453 C CB  . ASN B 118 ? 0.1808 0.1481 0.2341 -0.0183 -0.0695 -0.0522 341  ASN B CB  
3454 C CG  . ASN B 118 ? 0.2312 0.1728 0.2476 0.0068  -0.0709 -0.0449 341  ASN B CG  
3455 O OD1 . ASN B 118 ? 0.2164 0.1729 0.2291 0.0228  -0.0771 -0.0342 341  ASN B OD1 
3456 N ND2 . ASN B 118 ? 0.2885 0.1863 0.2776 0.0090  -0.0604 -0.0520 341  ASN B ND2 
3457 N N   . ARG B 119 ? 0.1504 0.1703 0.3291 0.0025  -0.0721 -0.0344 342  ARG B N   
3458 C CA  . ARG B 119 ? 0.1719 0.2081 0.3984 0.0255  -0.0328 -0.0050 342  ARG B CA  
3459 C C   . ARG B 119 ? 0.2123 0.2525 0.4230 -0.0041 -0.0064 0.0003  342  ARG B C   
3460 O O   . ARG B 119 ? 0.2359 0.2723 0.4339 0.0040  0.0295  0.0001  342  ARG B O   
3461 C CB  . ARG B 119 ? 0.1989 0.2302 0.4645 0.0454  -0.0061 0.0163  342  ARG B CB  
3462 C CG  . ARG B 119 ? 0.2233 0.2501 0.5023 0.0624  -0.0142 0.0289  342  ARG B CG  
3463 C CD  . ARG B 119 ? 0.2069 0.2492 0.5199 0.0845  -0.0193 0.0623  342  ARG B CD  
3464 N NE  . ARG B 119 ? 0.2384 0.2683 0.5196 0.0523  -0.0274 0.0703  342  ARG B NE  
3465 C CZ  . ARG B 119 ? 0.2510 0.2894 0.5084 0.0680  -0.0435 0.1096  342  ARG B CZ  
3466 N NH1 . ARG B 119 ? 0.2218 0.3014 0.4960 0.0877  -0.0629 0.0954  342  ARG B NH1 
3467 N NH2 . ARG B 119 ? 0.2761 0.2985 0.5118 0.0278  -0.0609 0.1143  342  ARG B NH2 
3468 N N   . GLU B 120 ? 0.2066 0.2584 0.4177 -0.0287 -0.0528 -0.0046 343  GLU B N   
3469 C CA  . GLU B 120 ? 0.2340 0.2801 0.4281 -0.0200 -0.0504 -0.0109 343  GLU B CA  
3470 C C   . GLU B 120 ? 0.2388 0.2868 0.4013 -0.0117 -0.0517 -0.0146 343  GLU B C   
3471 O O   . GLU B 120 ? 0.2519 0.2786 0.3710 0.0063  0.0034  -0.0197 343  GLU B O   
3472 C CB  . GLU B 120 ? 0.2728 0.3184 0.4700 0.0003  -0.0417 -0.0189 343  GLU B CB  
3473 C CG  . GLU B 120 ? 0.3308 0.3557 0.5187 0.0032  -0.0306 -0.0228 343  GLU B CG  
3474 C CD  . GLU B 120 ? 0.3960 0.3815 0.5488 0.0070  -0.0179 -0.0284 343  GLU B CD  
3475 N N   . GLY B 121 ? 0.2836 0.2938 0.4002 -0.0203 -0.0272 -0.0239 344  GLY B N   
3476 C CA  . GLY B 121 ? 0.3471 0.3044 0.4082 -0.0176 -0.0007 -0.0208 344  GLY B CA  
3477 C C   . GLY B 121 ? 0.4336 0.3348 0.4207 -0.0278 0.0392  -0.0400 344  GLY B C   
3478 O O   . GLY B 121 ? 0.4623 0.3100 0.4074 -0.0354 0.0324  -0.0509 344  GLY B O   
3479 N N   . SER B 122 ? 0.4800 0.3904 0.4545 -0.0403 0.0598  -0.0605 345  SER B N   
3480 C CA  . SER B 122 ? 0.5369 0.4385 0.5011 -0.0645 0.0762  -0.0945 345  SER B CA  
3481 C C   . SER B 122 ? 0.6828 0.4983 0.5453 -0.0896 0.1270  -0.1052 345  SER B C   
3482 O O   . SER B 122 ? 0.7092 0.4939 0.5386 -0.0975 0.1339  -0.1322 345  SER B O   
3483 C CB  . SER B 122 ? 0.4480 0.4375 0.5121 -0.0548 0.0392  -0.1150 345  SER B CB  
3484 O OG  . SER B 122 ? 0.3964 0.4337 0.5386 -0.0618 0.0356  -0.1476 345  SER B OG  
3485 N N   . SER B 123 ? 0.7767 0.5547 0.5712 -0.1055 0.1294  -0.0940 346  SER B N   
3486 C CA  . SER B 123 ? 0.8619 0.6120 0.6058 -0.1067 0.1338  -0.0824 346  SER B CA  
3487 C C   . SER B 123 ? 0.8764 0.6339 0.6183 -0.0952 0.1365  -0.0769 346  SER B C   
3488 O O   . SER B 123 ? 0.8853 0.6457 0.6319 -0.0870 0.1411  -0.0658 346  SER B O   
3489 C CB  . SER B 123 ? 0.9141 0.6335 0.6210 -0.1210 0.1424  -0.0832 346  SER B CB  
3490 O OG  . SER B 123 ? 0.9431 0.6425 0.6278 -0.1281 0.1481  -0.0841 346  SER B OG  
3491 N N   . ASN B 127 ? 0.8189 0.5044 0.5710 -0.0505 0.2089  0.0277  350  ASN B N   
3492 C CA  . ASN B 127 ? 0.8062 0.4953 0.5581 -0.0436 0.1994  0.0220  350  ASN B CA  
3493 C C   . ASN B 127 ? 0.7027 0.4404 0.4607 -0.0566 0.1192  0.0274  350  ASN B C   
3494 O O   . ASN B 127 ? 0.7195 0.4620 0.4627 -0.0465 0.0684  0.0427  350  ASN B O   
3495 C CB  . ASN B 127 ? 0.8689 0.5225 0.6226 -0.0280 0.2479  0.0157  350  ASN B CB  
3496 C CG  . ASN B 127 ? 0.9177 0.5452 0.6777 -0.0081 0.2792  0.0049  350  ASN B CG  
3497 O OD1 . ASN B 127 ? 0.9345 0.5483 0.6951 -0.0023 0.2862  0.0016  350  ASN B OD1 
3498 N ND2 . ASN B 127 ? 0.9405 0.5561 0.6937 -0.0097 0.2854  -0.0044 350  ASN B ND2 
3499 N N   . GLN B 128 ? 0.5517 0.3471 0.3479 -0.0883 0.0556  0.0250  351  GLN B N   
3500 C CA  . GLN B 128 ? 0.4377 0.2956 0.3249 -0.0673 0.0240  0.0482  351  GLN B CA  
3501 C C   . GLN B 128 ? 0.3401 0.2385 0.2776 -0.0494 0.0031  0.0065  351  GLN B C   
3502 O O   . GLN B 128 ? 0.3441 0.1959 0.2883 -0.0577 -0.0003 -0.0299 351  GLN B O   
3503 C CB  . GLN B 128 ? 0.4550 0.3235 0.3408 -0.0428 0.0187  0.0906  351  GLN B CB  
3504 C CG  . GLN B 128 ? 0.4466 0.3598 0.3841 -0.0272 0.0112  0.1261  351  GLN B CG  
3505 C CD  . GLN B 128 ? 0.4570 0.3888 0.4244 -0.0114 -0.0115 0.1450  351  GLN B CD  
3506 O OE1 . GLN B 128 ? 0.4441 0.4135 0.4532 -0.0004 -0.0248 0.1407  351  GLN B OE1 
3507 N NE2 . GLN B 128 ? 0.4547 0.3800 0.4235 -0.0199 -0.0154 0.1523  351  GLN B NE2 
3508 N N   . LYS B 129 ? 0.2502 0.1943 0.2301 -0.0586 -0.0016 -0.0076 352  LYS B N   
3509 C CA  . LYS B 129 ? 0.1907 0.1828 0.1928 -0.0199 -0.0079 -0.0265 352  LYS B CA  
3510 C C   . LYS B 129 ? 0.2014 0.1416 0.1848 -0.0321 -0.0124 0.0024  352  LYS B C   
3511 O O   . LYS B 129 ? 0.2005 0.1420 0.1959 -0.0190 -0.0388 0.0158  352  LYS B O   
3512 C CB  . LYS B 129 ? 0.1955 0.2167 0.2087 -0.0019 -0.0171 -0.0552 352  LYS B CB  
3513 C CG  . LYS B 129 ? 0.2240 0.2482 0.1934 0.0229  -0.0329 -0.0950 352  LYS B CG  
3514 C CD  . LYS B 129 ? 0.2442 0.2894 0.1911 0.0800  -0.0484 -0.0895 352  LYS B CD  
3515 C CE  . LYS B 129 ? 0.2762 0.3287 0.2412 0.0839  -0.0424 -0.1162 352  LYS B CE  
3516 N NZ  . LYS B 129 ? 0.3213 0.3510 0.2815 0.0814  -0.0196 -0.1341 352  LYS B NZ  
3517 N N   . ALA B 130 ? 0.1618 0.1275 0.1681 -0.0323 -0.0323 0.0086  353  ALA B N   
3518 C CA  . ALA B 130 ? 0.1658 0.1278 0.1750 -0.0318 -0.0403 -0.0185 353  ALA B CA  
3519 C C   . ALA B 130 ? 0.1691 0.1008 0.1839 0.0058  -0.0363 0.0061  353  ALA B C   
3520 O O   . ALA B 130 ? 0.1644 0.1107 0.1959 -0.0092 -0.0485 -0.0255 353  ALA B O   
3521 C CB  . ALA B 130 ? 0.1641 0.1425 0.1944 -0.0184 -0.0575 0.0042  353  ALA B CB  
3522 N N   . ASN B 131 ? 0.1597 0.1010 0.1730 -0.0039 -0.0321 0.0010  354  ASN B N   
3523 C CA  . ASN B 131 ? 0.1535 0.1156 0.1778 -0.0253 -0.0385 0.0149  354  ASN B CA  
3524 C C   . ASN B 131 ? 0.1680 0.1042 0.1746 -0.0257 -0.0603 -0.0002 354  ASN B C   
3525 O O   . ASN B 131 ? 0.1709 0.1128 0.1878 -0.0180 -0.0405 -0.0051 354  ASN B O   
3526 C CB  . ASN B 131 ? 0.1595 0.1146 0.1847 0.0090  -0.0557 0.0116  354  ASN B CB  
3527 C CG  . ASN B 131 ? 0.1631 0.1233 0.1831 -0.0119 -0.0398 -0.0021 354  ASN B CG  
3528 O OD1 . ASN B 131 ? 0.1998 0.1436 0.1823 -0.0067 -0.0511 -0.0145 354  ASN B OD1 
3529 N ND2 . ASN B 131 ? 0.1698 0.1299 0.1972 -0.0286 -0.0567 0.0028  354  ASN B ND2 
3530 N N   . ARG B 132 ? 0.1612 0.0885 0.1851 -0.0140 -0.0498 0.0226  355  ARG B N   
3531 C CA  . ARG B 132 ? 0.1783 0.1056 0.1472 -0.0258 -0.0678 0.0315  355  ARG B CA  
3532 C C   . ARG B 132 ? 0.1632 0.1046 0.1704 -0.0195 -0.0634 0.0040  355  ARG B C   
3533 O O   . ARG B 132 ? 0.1868 0.1154 0.2000 0.0052  -0.0388 -0.0051 355  ARG B O   
3534 C CB  . ARG B 132 ? 0.1943 0.1372 0.1687 0.0022  -0.0720 0.0172  355  ARG B CB  
3535 C CG  . ARG B 132 ? 0.2090 0.1358 0.1904 -0.0245 -0.0881 0.0154  355  ARG B CG  
3536 C CD  . ARG B 132 ? 0.2126 0.1321 0.1852 -0.0224 -0.0660 0.0133  355  ARG B CD  
3537 N NE  . ARG B 132 ? 0.2125 0.1431 0.1904 -0.0268 -0.0744 0.0463  355  ARG B NE  
3538 C CZ  . ARG B 132 ? 0.2155 0.1110 0.2337 -0.0164 -0.0467 0.0056  355  ARG B CZ  
3539 N NH1 . ARG B 132 ? 0.2087 0.1201 0.2313 -0.0015 -0.0980 -0.0171 355  ARG B NH1 
3540 N NH2 . ARG B 132 ? 0.2186 0.1227 0.2650 -0.0112 -0.0482 0.0415  355  ARG B NH2 
3541 N N   . SER B 133 ? 0.1575 0.1142 0.1759 -0.0339 -0.0619 0.0012  356  SER B N   
3542 C CA  . SER B 133 ? 0.1679 0.1162 0.1778 -0.0335 -0.0466 -0.0052 356  SER B CA  
3543 C C   . SER B 133 ? 0.2001 0.1256 0.1800 -0.0182 -0.0561 -0.0028 356  SER B C   
3544 O O   . SER B 133 ? 0.1928 0.1273 0.1794 -0.0336 -0.0477 -0.0189 356  SER B O   
3545 C CB  . SER B 133 ? 0.1864 0.1330 0.1668 -0.0300 -0.0578 0.0169  356  SER B CB  
3546 O OG  . SER B 133 ? 0.1964 0.1325 0.1549 -0.0263 -0.0424 -0.0078 356  SER B OG  
3547 N N   . HIS B 134 ? 0.1854 0.1227 0.1702 -0.0313 -0.0442 0.0008  357  HIS B N   
3548 C CA  . HIS B 134 ? 0.1985 0.1330 0.1551 -0.0399 -0.0859 -0.0006 357  HIS B CA  
3549 C C   . HIS B 134 ? 0.1500 0.1138 0.1529 -0.0138 -0.0741 -0.0017 357  HIS B C   
3550 O O   . HIS B 134 ? 0.1873 0.1284 0.1547 0.0152  -0.0245 -0.0150 357  HIS B O   
3551 C CB  . HIS B 134 ? 0.2702 0.1778 0.1582 -0.0389 -0.0991 -0.0028 357  HIS B CB  
3552 C CG  . HIS B 134 ? 0.3652 0.2037 0.1903 -0.0651 -0.0875 -0.0364 357  HIS B CG  
3553 N ND1 . HIS B 134 ? 0.4247 0.2051 0.2014 -0.0546 -0.0597 -0.0504 357  HIS B ND1 
3554 C CD2 . HIS B 134 ? 0.3710 0.2234 0.1984 -0.0661 -0.0965 -0.0296 357  HIS B CD2 
3555 C CE1 . HIS B 134 ? 0.4185 0.2147 0.2151 -0.0771 -0.0907 -0.0518 357  HIS B CE1 
3556 N NE2 . HIS B 134 ? 0.3991 0.2326 0.2248 -0.0702 -0.0790 -0.0489 357  HIS B NE2 
3557 N N   . GLU B 135 ? 0.1654 0.1078 0.1763 -0.0118 -0.0477 0.0046  358  GLU B N   
3558 C CA  . GLU B 135 ? 0.2179 0.1039 0.1839 -0.0031 -0.0353 0.0335  358  GLU B CA  
3559 C C   . GLU B 135 ? 0.2362 0.1065 0.1609 0.0005  -0.0556 0.0056  358  GLU B C   
3560 O O   . GLU B 135 ? 0.2561 0.1284 0.1606 -0.0301 -0.0461 0.0067  358  GLU B O   
3561 C CB  . GLU B 135 ? 0.2225 0.1278 0.1919 0.0273  -0.0549 0.0235  358  GLU B CB  
3562 C CG  . GLU B 135 ? 0.2328 0.1281 0.2003 0.0109  -0.0445 0.0081  358  GLU B CG  
3563 C CD  . GLU B 135 ? 0.2532 0.1453 0.2219 0.0060  -0.0245 -0.0478 358  GLU B CD  
3564 O OE1 . GLU B 135 ? 0.3062 0.1765 0.3099 0.0101  -0.0036 -0.0877 358  GLU B OE1 
3565 O OE2 . GLU B 135 ? 0.2628 0.1302 0.2020 -0.0213 -0.0305 -0.0316 358  GLU B OE2 
3566 N N   . GLY B 136 ? 0.2478 0.0836 0.1763 0.0015  -0.0529 0.0042  359  GLY B N   
3567 C CA  . GLY B 136 ? 0.2584 0.0836 0.1869 -0.0020 -0.0852 0.0187  359  GLY B CA  
3568 C C   . GLY B 136 ? 0.2448 0.0974 0.1826 -0.0185 -0.0753 0.0041  359  GLY B C   
3569 O O   . GLY B 136 ? 0.2392 0.1207 0.1728 -0.0121 -0.0764 0.0085  359  GLY B O   
3570 N N   . VAL B 137 ? 0.2338 0.0984 0.1687 -0.0342 -0.0737 0.0040  360  VAL B N   
3571 C CA  . VAL B 137 ? 0.2237 0.0916 0.1887 -0.0277 -0.0743 0.0045  360  VAL B CA  
3572 C C   . VAL B 137 ? 0.2266 0.0975 0.1724 -0.0163 -0.1065 -0.0069 360  VAL B C   
3573 O O   . VAL B 137 ? 0.2441 0.1203 0.1875 -0.0146 -0.1037 -0.0157 360  VAL B O   
3574 C CB  . VAL B 137 ? 0.2705 0.1101 0.1793 -0.0215 -0.0320 0.0055  360  VAL B CB  
3575 C CG1 . VAL B 137 ? 0.2860 0.1205 0.1946 -0.0544 -0.0485 -0.0135 360  VAL B CG1 
3576 C CG2 . VAL B 137 ? 0.2889 0.1473 0.2066 0.0050  -0.0048 0.0117  360  VAL B CG2 
3577 N N   . ILE B 138 ? 0.2282 0.0967 0.1727 -0.0087 -0.1024 0.0132  361  ILE B N   
3578 C CA  . ILE B 138 ? 0.2212 0.0980 0.1901 -0.0035 -0.0960 0.0192  361  ILE B CA  
3579 C C   . ILE B 138 ? 0.2600 0.0977 0.2018 -0.0026 -0.0772 0.0065  361  ILE B C   
3580 O O   . ILE B 138 ? 0.2381 0.1132 0.1969 -0.0102 -0.0786 -0.0133 361  ILE B O   
3581 C CB  . ILE B 138 ? 0.2004 0.0952 0.1930 0.0087  -0.0829 0.0289  361  ILE B CB  
3582 C CG1 . ILE B 138 ? 0.2302 0.1157 0.1804 -0.0232 -0.0628 0.0215  361  ILE B CG1 
3583 C CG2 . ILE B 138 ? 0.2248 0.1138 0.2155 0.0266  -0.1027 0.0108  361  ILE B CG2 
3584 C CD1 . ILE B 138 ? 0.2280 0.1358 0.1661 -0.0033 -0.0455 0.0209  361  ILE B CD1 
3585 N N   . SER B 139 ? 0.3062 0.0991 0.2016 -0.0116 -0.0861 0.0313  362  SER B N   
3586 C CA  . SER B 139 ? 0.2925 0.0933 0.1861 -0.0337 -0.0857 0.0226  362  SER B CA  
3587 C C   . SER B 139 ? 0.2693 0.0970 0.2224 -0.0366 -0.1007 0.0115  362  SER B C   
3588 O O   . SER B 139 ? 0.2371 0.1112 0.2314 -0.0316 -0.1205 0.0063  362  SER B O   
3589 C CB  . SER B 139 ? 0.3237 0.1211 0.1643 -0.0471 -0.0976 0.0405  362  SER B CB  
3590 O OG  . SER B 139 ? 0.3311 0.1335 0.2030 -0.0485 -0.1124 0.0437  362  SER B OG  
3591 N N   . THR B 140 ? 0.2490 0.0955 0.2090 -0.0212 -0.1300 0.0126  363  THR B N   
3592 C CA  . THR B 140 ? 0.2521 0.1042 0.1868 -0.0224 -0.1251 0.0234  363  THR B CA  
3593 C C   . THR B 140 ? 0.2767 0.1164 0.1809 -0.0321 -0.1265 0.0268  363  THR B C   
3594 O O   . THR B 140 ? 0.2854 0.1307 0.2137 -0.0203 -0.1113 0.0247  363  THR B O   
3595 C CB  . THR B 140 ? 0.2453 0.1268 0.1801 -0.0377 -0.1213 0.0288  363  THR B CB  
3596 O OG1 . THR B 140 ? 0.2438 0.1154 0.1892 -0.0447 -0.0863 0.0262  363  THR B OG1 
3597 C CG2 . THR B 140 ? 0.2632 0.1346 0.1827 -0.0323 -0.1241 0.0334  363  THR B CG2 
3598 N N   . VAL B 141 ? 0.2929 0.1524 0.1964 -0.0470 -0.1269 0.0358  364  VAL B N   
3599 C CA  . VAL B 141 ? 0.2983 0.1574 0.2156 -0.0595 -0.1347 0.0476  364  VAL B CA  
3600 C C   . VAL B 141 ? 0.3354 0.1729 0.2355 -0.0543 -0.1250 0.0594  364  VAL B C   
3601 O O   . VAL B 141 ? 0.3645 0.1955 0.2355 -0.0693 -0.1579 0.0641  364  VAL B O   
3602 C CB  . VAL B 141 ? 0.3228 0.1599 0.2410 -0.0677 -0.1370 0.0124  364  VAL B CB  
3603 C CG1 . VAL B 141 ? 0.3190 0.1768 0.2149 -0.0726 -0.1309 0.0087  364  VAL B CG1 
3604 C CG2 . VAL B 141 ? 0.3421 0.1629 0.2635 -0.0583 -0.1037 0.0258  364  VAL B CG2 
3605 N N   . ALA B 142 ? 0.3244 0.1518 0.2473 -0.0431 -0.1505 0.0280  365  ALA B N   
3606 C CA  . ALA B 142 ? 0.3241 0.1373 0.2798 -0.0318 -0.1782 0.0239  365  ALA B CA  
3607 C C   . ALA B 142 ? 0.3171 0.1510 0.2769 -0.0312 -0.1740 0.0373  365  ALA B C   
3608 O O   . ALA B 142 ? 0.3463 0.1360 0.2789 -0.0474 -0.1537 0.0490  365  ALA B O   
3609 C CB  . ALA B 142 ? 0.3250 0.1274 0.2858 -0.0189 -0.1818 0.0164  365  ALA B CB  
3610 N N   . PRO B 143 ? 0.3374 0.1723 0.2775 -0.0274 -0.1794 0.0292  366  PRO B N   
3611 C CA  . PRO B 143 ? 0.3158 0.1908 0.2784 -0.0006 -0.1692 0.0357  366  PRO B CA  
3612 C C   . PRO B 143 ? 0.3185 0.1543 0.3036 -0.0045 -0.1785 0.0278  366  PRO B C   
3613 O O   . PRO B 143 ? 0.3169 0.1395 0.3316 0.0155  -0.1643 0.0206  366  PRO B O   
3614 C CB  . PRO B 143 ? 0.3325 0.2322 0.2856 0.0057  -0.1778 0.0326  366  PRO B CB  
3615 C CG  . PRO B 143 ? 0.3353 0.2289 0.2910 0.0044  -0.1743 0.0300  366  PRO B CG  
3616 C CD  . PRO B 143 ? 0.3423 0.1981 0.2683 0.0011  -0.1714 0.0336  366  PRO B CD  
3617 N N   . ARG B 144 ? 0.3155 0.1470 0.2807 -0.0157 -0.1723 0.0306  367  ARG B N   
3618 C CA  . ARG B 144 ? 0.2722 0.1600 0.2936 -0.0520 -0.1451 0.0117  367  ARG B CA  
3619 C C   . ARG B 144 ? 0.2718 0.1275 0.2917 -0.0319 -0.1657 0.0270  367  ARG B C   
3620 O O   . ARG B 144 ? 0.2838 0.1219 0.3257 -0.0198 -0.1605 0.0069  367  ARG B O   
3628 N N   . PHE B 145 ? 0.2875 0.1374 0.2711 -0.0245 -0.1649 0.0127  368  PHE B N   
3629 C CA  . PHE B 145 ? 0.2638 0.1318 0.2464 -0.0154 -0.1505 0.0022  368  PHE B CA  
3630 C C   . PHE B 145 ? 0.2559 0.1181 0.2924 -0.0076 -0.1629 0.0051  368  PHE B C   
3631 O O   . PHE B 145 ? 0.2983 0.1113 0.2982 -0.0190 -0.1353 0.0050  368  PHE B O   
3632 C CB  . PHE B 145 ? 0.2752 0.1298 0.2157 -0.0366 -0.1426 0.0285  368  PHE B CB  
3633 C CG  . PHE B 145 ? 0.2514 0.1284 0.2298 -0.0275 -0.1334 0.0427  368  PHE B CG  
3634 C CD1 . PHE B 145 ? 0.2090 0.1490 0.2173 -0.0316 -0.1213 0.0520  368  PHE B CD1 
3635 C CD2 . PHE B 145 ? 0.2499 0.1446 0.2618 -0.0313 -0.1335 0.0361  368  PHE B CD2 
3636 C CE1 . PHE B 145 ? 0.2021 0.1401 0.2331 -0.0329 -0.1122 0.0293  368  PHE B CE1 
3637 C CE2 . PHE B 145 ? 0.2496 0.1293 0.2569 -0.0455 -0.1134 0.0227  368  PHE B CE2 
3638 C CZ  . PHE B 145 ? 0.2363 0.1337 0.2370 -0.0384 -0.1142 0.0140  368  PHE B CZ  
3639 N N   . THR B 146 ? 0.2311 0.1291 0.3232 -0.0026 -0.1581 0.0133  369  THR B N   
3640 C CA  . THR B 146 ? 0.2208 0.1501 0.3120 0.0026  -0.1418 0.0363  369  THR B CA  
3641 C C   . THR B 146 ? 0.2196 0.1379 0.3334 -0.0014 -0.1536 0.0136  369  THR B C   
3642 O O   . THR B 146 ? 0.2146 0.1386 0.3488 0.0118  -0.1520 -0.0125 369  THR B O   
3643 C CB  . THR B 146 ? 0.2387 0.1514 0.3386 -0.0316 -0.1638 0.0450  369  THR B CB  
3644 O OG1 . THR B 146 ? 0.2443 0.1630 0.4059 -0.0283 -0.1687 0.0194  369  THR B OG1 
3645 C CG2 . THR B 146 ? 0.2390 0.1664 0.3362 -0.0338 -0.1601 0.0516  369  THR B CG2 
3646 N N   . PRO B 147 ? 0.2252 0.1120 0.3147 0.0049  -0.1472 -0.0032 370  PRO B N   
3647 C CA  . PRO B 147 ? 0.2075 0.1271 0.3285 0.0120  -0.1413 -0.0097 370  PRO B CA  
3648 C C   . PRO B 147 ? 0.2161 0.1294 0.3709 0.0218  -0.1450 -0.0233 370  PRO B C   
3649 O O   . PRO B 147 ? 0.2004 0.1501 0.3857 0.0155  -0.1419 -0.0325 370  PRO B O   
3650 C CB  . PRO B 147 ? 0.1753 0.1199 0.3215 -0.0186 -0.1220 0.0213  370  PRO B CB  
3651 C CG  . PRO B 147 ? 0.1963 0.1121 0.3107 -0.0030 -0.1365 0.0175  370  PRO B CG  
3652 C CD  . PRO B 147 ? 0.2095 0.1123 0.3102 -0.0044 -0.1475 0.0068  370  PRO B CD  
3653 N N   . LYS B 148 ? 0.2147 0.1275 0.3917 0.0223  -0.1579 -0.0377 371  LYS B N   
3654 C CA  . LYS B 148 ? 0.2336 0.1397 0.4494 0.0216  -0.1607 -0.0368 371  LYS B CA  
3655 C C   . LYS B 148 ? 0.2319 0.1612 0.4571 0.0384  -0.1554 -0.0355 371  LYS B C   
3656 O O   . LYS B 148 ? 0.2308 0.1947 0.4582 0.0624  -0.1370 -0.0336 371  LYS B O   
3657 C CB  . LYS B 148 ? 0.2611 0.1506 0.5085 0.0333  -0.1241 -0.0372 371  LYS B CB  
3658 C CG  . LYS B 148 ? 0.2838 0.1953 0.5505 0.0433  -0.1249 -0.0661 371  LYS B CG  
3659 C CD  . LYS B 148 ? 0.3121 0.2304 0.5924 0.0372  -0.0948 -0.0875 371  LYS B CD  
3660 C CE  . LYS B 148 ? 0.3412 0.2418 0.6104 0.0071  -0.0777 -0.1125 371  LYS B CE  
3661 N NZ  . LYS B 148 ? 0.3479 0.2629 0.6207 -0.0215 -0.0915 -0.1066 371  LYS B NZ  
3662 N N   . LEU B 149 ? 0.2197 0.1514 0.4270 0.0181  -0.1579 -0.0086 372  LEU B N   
3663 C CA  . LEU B 149 ? 0.2387 0.1709 0.4267 0.0129  -0.1701 0.0097  372  LEU B CA  
3664 C C   . LEU B 149 ? 0.2400 0.1695 0.4515 0.0040  -0.1776 0.0043  372  LEU B C   
3665 O O   . LEU B 149 ? 0.2571 0.2138 0.4800 -0.0216 -0.1685 0.0091  372  LEU B O   
3666 C CB  . LEU B 149 ? 0.2527 0.2012 0.4358 0.0149  -0.1773 0.0213  372  LEU B CB  
3667 C CG  . LEU B 149 ? 0.2802 0.2137 0.4602 0.0346  -0.1555 0.0607  372  LEU B CG  
3668 C CD1 . LEU B 149 ? 0.3071 0.2279 0.4695 0.0156  -0.1336 0.0734  372  LEU B CD1 
3669 C CD2 . LEU B 149 ? 0.2980 0.2191 0.4899 0.0490  -0.1151 0.0676  372  LEU B CD2 
3670 N N   . GLY B 150 ? 0.2283 0.1422 0.4268 0.0196  -0.1378 0.0151  373  GLY B N   
3671 C CA  . GLY B 150 ? 0.2411 0.1239 0.4404 0.0018  -0.1184 0.0008  373  GLY B CA  
3672 C C   . GLY B 150 ? 0.2274 0.1287 0.3979 0.0148  -0.1504 -0.0031 373  GLY B C   
3673 O O   . GLY B 150 ? 0.2274 0.1240 0.4186 0.0048  -0.1394 0.0028  373  GLY B O   
3674 N N   . SER B 151 ? 0.2491 0.1356 0.3779 0.0347  -0.1434 -0.0090 374  SER B N   
3675 C CA  . SER B 151 ? 0.2482 0.1402 0.3766 0.0238  -0.1558 0.0011  374  SER B CA  
3676 C C   . SER B 151 ? 0.2323 0.1226 0.3305 0.0082  -0.1360 0.0254  374  SER B C   
3677 O O   . SER B 151 ? 0.2210 0.1188 0.3415 -0.0026 -0.1303 0.0126  374  SER B O   
3678 C CB  . SER B 151 ? 0.2520 0.1724 0.3564 -0.0056 -0.1748 0.0068  374  SER B CB  
3679 O OG  . SER B 151 ? 0.2886 0.1912 0.3865 -0.0291 -0.1820 0.0308  374  SER B OG  
3680 N N   . VAL B 152 ? 0.2402 0.1124 0.2995 0.0021  -0.1487 0.0121  375  VAL B N   
3681 C CA  . VAL B 152 ? 0.2473 0.1168 0.2695 -0.0176 -0.1433 0.0051  375  VAL B CA  
3682 C C   . VAL B 152 ? 0.2590 0.1164 0.2516 -0.0122 -0.1460 0.0248  375  VAL B C   
3683 O O   . VAL B 152 ? 0.2710 0.1122 0.2742 -0.0191 -0.1186 0.0085  375  VAL B O   
3684 C CB  . VAL B 152 ? 0.2435 0.1195 0.2381 -0.0079 -0.1421 0.0184  375  VAL B CB  
3685 C CG1 . VAL B 152 ? 0.2481 0.1395 0.2593 0.0002  -0.1432 -0.0025 375  VAL B CG1 
3686 C CG2 . VAL B 152 ? 0.2543 0.1494 0.2580 -0.0052 -0.1215 0.0633  375  VAL B CG2 
3687 N N   . MET B 153 ? 0.2562 0.1223 0.2479 -0.0203 -0.1447 0.0013  376  MET B N   
3688 C CA  . MET B 153 ? 0.2628 0.1265 0.2266 -0.0263 -0.1370 -0.0001 376  MET B CA  
3689 C C   . MET B 153 ? 0.2573 0.1139 0.2400 -0.0268 -0.1230 0.0093  376  MET B C   
3690 O O   . MET B 153 ? 0.2758 0.1080 0.2416 -0.0151 -0.1214 0.0029  376  MET B O   
3691 C CB  . MET B 153 ? 0.3029 0.1407 0.2461 -0.0381 -0.1220 0.0135  376  MET B CB  
3692 C CG  . MET B 153 ? 0.3167 0.1678 0.2456 -0.0320 -0.1132 0.0280  376  MET B CG  
3693 S SD  . MET B 153 ? 0.3422 0.1804 0.2255 -0.0267 -0.1342 0.0177  376  MET B SD  
3694 C CE  . MET B 153 ? 0.3340 0.1634 0.2494 -0.0449 -0.0794 0.0794  376  MET B CE  
3695 N N   . ILE B 154 ? 0.2378 0.1137 0.2245 -0.0241 -0.1159 0.0184  377  ILE B N   
3696 C CA  . ILE B 154 ? 0.2509 0.1216 0.2079 -0.0246 -0.1048 0.0253  377  ILE B CA  
3697 C C   . ILE B 154 ? 0.2737 0.1223 0.2126 -0.0388 -0.1296 0.0084  377  ILE B C   
3698 O O   . ILE B 154 ? 0.3061 0.1291 0.2246 -0.0560 -0.1357 0.0218  377  ILE B O   
3699 C CB  . ILE B 154 ? 0.2262 0.1251 0.1996 -0.0461 -0.0905 0.0386  377  ILE B CB  
3700 C CG1 . ILE B 154 ? 0.2181 0.1165 0.1868 -0.0326 -0.0799 0.0465  377  ILE B CG1 
3701 C CG2 . ILE B 154 ? 0.2395 0.1316 0.2141 -0.0751 -0.0896 0.0153  377  ILE B CG2 
3702 C CD1 . ILE B 154 ? 0.2270 0.1267 0.1882 -0.0178 -0.0734 0.0305  377  ILE B CD1 
3703 N N   . GLY B 155 ? 0.2698 0.1154 0.2085 -0.0292 -0.1075 0.0094  378  GLY B N   
3704 C CA  . GLY B 155 ? 0.2855 0.1246 0.2140 -0.0198 -0.1260 -0.0128 378  GLY B CA  
3705 C C   . GLY B 155 ? 0.2761 0.1457 0.2105 -0.0282 -0.1384 0.0048  378  GLY B C   
3706 O O   . GLY B 155 ? 0.2885 0.1288 0.2064 -0.0523 -0.1060 -0.0009 378  GLY B O   
3707 N N   . THR B 156 ? 0.3273 0.1682 0.2385 -0.0092 -0.1634 0.0010  379  THR B N   
3708 C CA  . THR B 156 ? 0.3836 0.2363 0.2552 -0.0012 -0.1753 -0.0302 379  THR B CA  
3709 C C   . THR B 156 ? 0.5062 0.3817 0.2976 -0.0058 -0.1946 -0.0816 379  THR B C   
3710 O O   . THR B 156 ? 0.5862 0.3475 0.2873 -0.0060 -0.1848 -0.0776 379  THR B O   
3711 C CB  . THR B 156 ? 0.3623 0.2084 0.2536 -0.0245 -0.1510 -0.0325 379  THR B CB  
3712 O OG1 . THR B 156 ? 0.3701 0.2001 0.2917 -0.0177 -0.1460 0.0052  379  THR B OG1 
3713 C CG2 . THR B 156 ? 0.3475 0.2161 0.2714 -0.0247 -0.1188 0.0005  379  THR B CG2 
3714 N N   . TRP B 157 ? 0.6410 0.5565 0.4322 0.0183  -0.2206 -0.1243 380  TRP B N   
3715 C CA  . TRP B 157 ? 0.7937 0.7486 0.6260 0.0254  -0.1861 -0.1631 380  TRP B CA  
3716 C C   . TRP B 157 ? 0.9444 0.9364 0.8795 0.0328  -0.1961 -0.1770 380  TRP B C   
3717 O O   . TRP B 157 ? 0.9249 0.9370 0.8812 0.0393  -0.2051 -0.1817 380  TRP B O   
3718 C CB  . TRP B 157 ? 0.8153 0.7511 0.5759 0.0315  -0.1047 -0.1804 380  TRP B CB  
3719 C CG  . TRP B 157 ? 0.8375 0.7492 0.5150 0.0365  -0.0349 -0.1929 380  TRP B CG  
3720 C CD1 . TRP B 157 ? 0.8622 0.7511 0.5086 0.0350  0.0040  -0.1952 380  TRP B CD1 
3721 C CD2 . TRP B 157 ? 0.8311 0.7466 0.4516 0.0442  -0.0165 -0.1897 380  TRP B CD2 
3722 N NE1 . TRP B 157 ? 0.8633 0.7517 0.4784 0.0386  0.0174  -0.1964 380  TRP B NE1 
3723 C CE2 . TRP B 157 ? 0.8437 0.7466 0.4346 0.0451  -0.0010 -0.1960 380  TRP B CE2 
3724 C CE3 . TRP B 157 ? 0.8110 0.7408 0.4070 0.0493  -0.0325 -0.1913 380  TRP B CE3 
3725 C CZ2 . TRP B 157 ? 0.8283 0.7441 0.4033 0.0515  -0.0005 -0.1834 380  TRP B CZ2 
3726 C CZ3 . TRP B 157 ? 0.8061 0.7403 0.3769 0.0576  -0.0210 -0.1860 380  TRP B CZ3 
3727 C CH2 . TRP B 157 ? 0.8124 0.7388 0.3663 0.0581  -0.0195 -0.1933 380  TRP B CH2 
3744 N N   . ASP B 161 ? 0.4214 0.3195 0.3445 -0.0154 -0.0993 -0.0629 384  ASP B N   
3745 C CA  . ASP B 161 ? 0.4229 0.2637 0.2969 -0.0374 -0.1160 -0.0369 384  ASP B CA  
3746 C C   . ASP B 161 ? 0.3634 0.2063 0.2316 -0.0386 -0.1475 -0.0095 384  ASP B C   
3747 O O   . ASP B 161 ? 0.3577 0.1945 0.2305 -0.0351 -0.1453 -0.0050 384  ASP B O   
3748 C CB  . ASP B 161 ? 0.4577 0.2611 0.3567 -0.0605 -0.0983 -0.0385 384  ASP B CB  
3749 C CG  . ASP B 161 ? 0.4739 0.2688 0.4000 -0.1264 -0.1026 -0.0606 384  ASP B CG  
3750 O OD1 . ASP B 161 ? 0.4784 0.2900 0.4148 -0.1681 -0.0963 -0.0635 384  ASP B OD1 
3751 O OD2 . ASP B 161 ? 0.4806 0.2597 0.4033 -0.1400 -0.0910 -0.0702 384  ASP B OD2 
3752 N N   . ILE B 162 ? 0.3602 0.1902 0.2493 -0.0398 -0.1042 0.0161  385  ILE B N   
3753 C CA  . ILE B 162 ? 0.3206 0.1912 0.2658 -0.0498 -0.1156 0.0060  385  ILE B CA  
3754 C C   . ILE B 162 ? 0.3005 0.1947 0.2472 -0.0524 -0.1302 0.0207  385  ILE B C   
3755 O O   . ILE B 162 ? 0.3344 0.2441 0.2444 -0.0652 -0.1296 0.0139  385  ILE B O   
3756 C CB  . ILE B 162 ? 0.2853 0.1776 0.2828 -0.0357 -0.1491 0.0177  385  ILE B CB  
3757 C CG1 . ILE B 162 ? 0.2977 0.1976 0.3058 -0.0539 -0.1576 0.0010  385  ILE B CG1 
3758 C CG2 . ILE B 162 ? 0.3200 0.1725 0.3270 -0.0129 -0.1050 0.0208  385  ILE B CG2 
3759 C CD1 . ILE B 162 ? 0.3010 0.2112 0.3220 -0.0440 -0.1611 0.0250  385  ILE B CD1 
3760 N N   . GLN B 163 ? 0.2649 0.1420 0.2507 -0.0574 -0.1247 0.0268  386  GLN B N   
3761 C CA  A GLN B 163 ? 0.2610 0.1449 0.2720 -0.0423 -0.1369 0.0402  386  GLN B CA  
3762 C CA  B GLN B 163 ? 0.2537 0.1377 0.2659 -0.0506 -0.1357 0.0324  386  GLN B CA  
3763 C C   . GLN B 163 ? 0.2518 0.1393 0.2588 -0.0385 -0.1361 0.0350  386  GLN B C   
3764 O O   . GLN B 163 ? 0.2555 0.1235 0.2855 -0.0390 -0.1485 0.0245  386  GLN B O   
3765 C CB  A GLN B 163 ? 0.2880 0.1585 0.3090 -0.0361 -0.1326 0.0400  386  GLN B CB  
3766 C CB  B GLN B 163 ? 0.2609 0.1359 0.2890 -0.0590 -0.1269 0.0234  386  GLN B CB  
3767 C CG  A GLN B 163 ? 0.3334 0.1854 0.3261 -0.0226 -0.1309 0.0513  386  GLN B CG  
3768 C CG  B GLN B 163 ? 0.2716 0.1389 0.3007 -0.0536 -0.1210 0.0155  386  GLN B CG  
3769 C CD  A GLN B 163 ? 0.3558 0.2128 0.3252 -0.0312 -0.1524 0.0558  386  GLN B CD  
3770 C CD  B GLN B 163 ? 0.2733 0.1464 0.3157 -0.0563 -0.1310 0.0000  386  GLN B CD  
3771 O OE1 A GLN B 163 ? 0.4215 0.2277 0.3212 0.0042  -0.1051 0.0862  386  GLN B OE1 
3772 O OE1 B GLN B 163 ? 0.2806 0.1603 0.2973 -0.0517 -0.1456 -0.0030 386  GLN B OE1 
3773 N NE2 A GLN B 163 ? 0.3619 0.2392 0.3484 -0.0367 -0.1449 0.0363  386  GLN B NE2 
3774 N NE2 B GLN B 163 ? 0.2639 0.1527 0.3184 -0.0543 -0.1266 -0.0127 386  GLN B NE2 
3775 N N   . ASP B 164 ? 0.2313 0.1531 0.2751 -0.0240 -0.1252 0.0402  387  ASP B N   
3776 C CA  . ASP B 164 ? 0.2331 0.1730 0.2940 -0.0195 -0.1524 0.0212  387  ASP B CA  
3777 C C   . ASP B 164 ? 0.2227 0.1853 0.3097 -0.0049 -0.1330 0.0450  387  ASP B C   
3778 O O   . ASP B 164 ? 0.2370 0.2247 0.3118 -0.0061 -0.1373 0.0331  387  ASP B O   
3779 C CB  . ASP B 164 ? 0.2402 0.1863 0.3128 -0.0173 -0.1613 0.0157  387  ASP B CB  
3780 C CG  . ASP B 164 ? 0.2661 0.2265 0.3336 0.0015  -0.1757 0.0154  387  ASP B CG  
3781 O OD1 . ASP B 164 ? 0.2605 0.2115 0.3346 0.0004  -0.1613 0.0097  387  ASP B OD1 
3782 O OD2 . ASP B 164 ? 0.2957 0.2815 0.3504 0.0033  -0.1729 0.0176  387  ASP B OD2 
3783 N N   . GLN B 165 ? 0.2147 0.1447 0.3118 -0.0104 -0.1253 0.0307  388  GLN B N   
3784 C CA  . GLN B 165 ? 0.2026 0.1105 0.2844 -0.0081 -0.1041 0.0313  388  GLN B CA  
3785 C C   . GLN B 165 ? 0.1682 0.1270 0.2993 -0.0324 -0.0831 0.0279  388  GLN B C   
3786 O O   . GLN B 165 ? 0.1712 0.1291 0.2775 -0.0139 -0.0941 0.0221  388  GLN B O   
3787 C CB  . GLN B 165 ? 0.1872 0.1047 0.3033 -0.0263 -0.1140 0.0173  388  GLN B CB  
3788 C CG  . GLN B 165 ? 0.2111 0.1281 0.2994 -0.0565 -0.0905 0.0015  388  GLN B CG  
3789 C CD  . GLN B 165 ? 0.2063 0.1536 0.3123 -0.0426 -0.1236 -0.0027 388  GLN B CD  
3790 O OE1 . GLN B 165 ? 0.2163 0.1448 0.3103 -0.0335 -0.0786 0.0083  388  GLN B OE1 
3791 N NE2 . GLN B 165 ? 0.2448 0.1777 0.3522 -0.0603 -0.1291 0.0017  388  GLN B NE2 
3792 N N   . PRO B 166 ? 0.1642 0.1410 0.3038 -0.0308 -0.0846 0.0109  389  PRO B N   
3793 C CA  . PRO B 166 ? 0.1784 0.1439 0.2643 -0.0266 -0.0892 0.0194  389  PRO B CA  
3794 C C   . PRO B 166 ? 0.1777 0.1346 0.2439 -0.0027 -0.0942 0.0148  389  PRO B C   
3795 O O   . PRO B 166 ? 0.1853 0.1443 0.2761 -0.0047 -0.0870 -0.0014 389  PRO B O   
3796 C CB  . PRO B 166 ? 0.1858 0.1425 0.2591 -0.0204 -0.0596 0.0074  389  PRO B CB  
3797 C CG  . PRO B 166 ? 0.1884 0.1395 0.2707 -0.0269 -0.0679 -0.0138 389  PRO B CG  
3798 C CD  . PRO B 166 ? 0.1777 0.1401 0.3011 -0.0244 -0.0737 0.0002  389  PRO B CD  
3799 N N   . SER B 167 ? 0.1668 0.1255 0.2472 -0.0319 -0.0773 0.0016  390  SER B N   
3800 C CA  . SER B 167 ? 0.1950 0.1230 0.2287 -0.0301 -0.0851 0.0037  390  SER B CA  
3801 C C   . SER B 167 ? 0.1846 0.1136 0.2185 -0.0073 -0.0859 -0.0071 390  SER B C   
3802 O O   . SER B 167 ? 0.2136 0.1278 0.2470 0.0165  -0.0861 -0.0290 390  SER B O   
3803 C CB  . SER B 167 ? 0.2119 0.1293 0.2368 -0.0261 -0.0720 0.0112  390  SER B CB  
3804 O OG  . SER B 167 ? 0.2029 0.1217 0.2319 -0.0123 -0.0890 -0.0023 390  SER B OG  
3805 N N   . ARG B 168 ? 0.1523 0.1208 0.1976 -0.0158 -0.0832 -0.0119 391  ARG B N   
3806 C CA  . ARG B 168 ? 0.1552 0.1332 0.2154 -0.0280 -0.0876 -0.0144 391  ARG B CA  
3807 C C   . ARG B 168 ? 0.1516 0.1189 0.2078 -0.0187 -0.0685 -0.0195 391  ARG B C   
3808 O O   . ARG B 168 ? 0.1852 0.1274 0.2555 -0.0273 -0.0155 -0.0630 391  ARG B O   
3809 C CB  . ARG B 168 ? 0.2303 0.1896 0.2266 -0.0452 -0.0883 -0.0448 391  ARG B CB  
3810 C CG  . ARG B 168 ? 0.3103 0.2311 0.2998 -0.0442 -0.0585 -0.0288 391  ARG B CG  
3811 C CD  . ARG B 168 ? 0.3960 0.2362 0.3117 -0.0546 -0.0257 -0.0496 391  ARG B CD  
3812 N NE  . ARG B 168 ? 0.4028 0.2240 0.2830 -0.0816 -0.0454 -0.0488 391  ARG B NE  
3813 C CZ  . ARG B 168 ? 0.3943 0.2325 0.2628 -0.0322 -0.0363 -0.0066 391  ARG B CZ  
3814 N NH1 . ARG B 168 ? 0.3815 0.2293 0.2557 0.0073  -0.0212 -0.0055 391  ARG B NH1 
3815 N NH2 . ARG B 168 ? 0.4051 0.2599 0.2494 -0.0156 -0.0244 0.0378  391  ARG B NH2 
3816 N N   . PHE B 169 ? 0.1596 0.1149 0.1893 -0.0083 -0.0500 0.0100  392  PHE B N   
3817 C CA  . PHE B 169 ? 0.1529 0.1190 0.1612 -0.0068 -0.0483 -0.0018 392  PHE B CA  
3818 C C   . PHE B 169 ? 0.1446 0.1093 0.1437 0.0013  -0.0619 -0.0171 392  PHE B C   
3819 O O   . PHE B 169 ? 0.1777 0.1174 0.1564 0.0046  -0.0282 -0.0308 392  PHE B O   
3820 C CB  . PHE B 169 ? 0.1690 0.1084 0.1611 0.0003  -0.0496 0.0102  392  PHE B CB  
3821 C CG  . PHE B 169 ? 0.1760 0.1126 0.1697 -0.0103 -0.0485 0.0142  392  PHE B CG  
3822 C CD1 . PHE B 169 ? 0.1598 0.1238 0.1932 0.0203  -0.0414 -0.0013 392  PHE B CD1 
3823 C CD2 . PHE B 169 ? 0.1508 0.1147 0.1754 -0.0202 -0.0553 0.0409  392  PHE B CD2 
3824 C CE1 . PHE B 169 ? 0.1782 0.1271 0.2099 0.0103  -0.0376 0.0267  392  PHE B CE1 
3825 C CE2 . PHE B 169 ? 0.1828 0.1213 0.2173 0.0101  -0.0485 0.0368  392  PHE B CE2 
3826 C CZ  . PHE B 169 ? 0.1650 0.1203 0.2178 -0.0021 -0.0461 0.0216  392  PHE B CZ  
3827 N N   . THR B 170 ? 0.1304 0.0904 0.1576 0.0031  -0.0573 0.0102  393  THR B N   
3828 C CA  . THR B 170 ? 0.1408 0.1072 0.1338 0.0030  -0.0600 0.0281  393  THR B CA  
3829 C C   . THR B 170 ? 0.1774 0.1037 0.1335 0.0017  -0.0557 0.0044  393  THR B C   
3830 O O   . THR B 170 ? 0.1693 0.1163 0.1470 -0.0205 -0.0542 -0.0063 393  THR B O   
3831 C CB  . THR B 170 ? 0.1661 0.1206 0.1425 -0.0054 -0.0635 0.0261  393  THR B CB  
3832 O OG1 . THR B 170 ? 0.1890 0.1194 0.1622 -0.0326 -0.0378 0.0104  393  THR B OG1 
3833 C CG2 . THR B 170 ? 0.1712 0.1455 0.1232 0.0011  -0.0829 0.0165  393  THR B CG2 
3834 N N   . PRO B 171 ? 0.1544 0.0951 0.1331 -0.0087 -0.0360 0.0010  394  PRO B N   
3835 C CA  . PRO B 171 ? 0.1679 0.0902 0.1452 0.0083  -0.0347 -0.0098 394  PRO B CA  
3836 C C   . PRO B 171 ? 0.1677 0.1089 0.1491 0.0129  -0.0583 -0.0100 394  PRO B C   
3837 O O   . PRO B 171 ? 0.1950 0.1266 0.1387 0.0136  -0.0449 0.0041  394  PRO B O   
3838 C CB  . PRO B 171 ? 0.1934 0.0817 0.1334 0.0225  -0.0209 -0.0149 394  PRO B CB  
3839 C CG  . PRO B 171 ? 0.1801 0.0884 0.1380 0.0010  -0.0272 -0.0285 394  PRO B CG  
3840 C CD  . PRO B 171 ? 0.1657 0.0914 0.1527 -0.0121 -0.0342 -0.0393 394  PRO B CD  
3841 N N   . VAL B 172 ? 0.1588 0.0956 0.1423 0.0005  -0.0450 -0.0130 395  VAL B N   
3842 C CA  . VAL B 172 ? 0.1702 0.0852 0.1403 0.0143  -0.0165 0.0009  395  VAL B CA  
3843 C C   . VAL B 172 ? 0.1850 0.0940 0.1276 -0.0177 -0.0159 -0.0057 395  VAL B C   
3844 O O   . VAL B 172 ? 0.1768 0.1165 0.1395 -0.0275 -0.0452 -0.0021 395  VAL B O   
3845 C CB  . VAL B 172 ? 0.1807 0.0870 0.1479 0.0024  -0.0226 -0.0203 395  VAL B CB  
3846 C CG1 . VAL B 172 ? 0.1796 0.1037 0.1553 0.0237  -0.0295 -0.0093 395  VAL B CG1 
3847 C CG2 . VAL B 172 ? 0.2261 0.1049 0.1369 -0.0103 -0.0384 -0.0008 395  VAL B CG2 
3848 N N   . GLY B 173 ? 0.1840 0.0891 0.1323 -0.0129 0.0038  0.0058  396  GLY B N   
3849 C CA  . GLY B 173 ? 0.1997 0.0908 0.1063 -0.0038 0.0015  0.0017  396  GLY B CA  
3850 C C   . GLY B 173 ? 0.1892 0.0963 0.1187 0.0040  -0.0350 -0.0022 396  GLY B C   
3851 O O   . GLY B 173 ? 0.1782 0.1010 0.1493 -0.0135 -0.0293 -0.0009 396  GLY B O   
3852 N N   . LEU B 174 ? 0.2084 0.1081 0.1115 -0.0044 -0.0315 0.0087  397  LEU B N   
3853 C CA  . LEU B 174 ? 0.2150 0.0982 0.1174 -0.0253 -0.0348 0.0012  397  LEU B CA  
3854 C C   . LEU B 174 ? 0.2278 0.1089 0.1303 -0.0120 -0.0412 0.0038  397  LEU B C   
3855 O O   . LEU B 174 ? 0.2338 0.1040 0.1743 0.0095  -0.0380 -0.0127 397  LEU B O   
3856 C CB  . LEU B 174 ? 0.2109 0.0977 0.1625 -0.0111 -0.0350 -0.0310 397  LEU B CB  
3857 C CG  . LEU B 174 ? 0.1919 0.1109 0.1849 -0.0144 -0.0413 -0.0118 397  LEU B CG  
3858 C CD1 . LEU B 174 ? 0.2102 0.1039 0.2265 -0.0383 -0.0681 0.0283  397  LEU B CD1 
3859 C CD2 . LEU B 174 ? 0.2342 0.1508 0.2286 -0.0118 -0.0247 -0.0193 397  LEU B CD2 
3860 N N   . ASN B 175 ? 0.2506 0.1273 0.1324 -0.0253 -0.0406 0.0017  398  ASN B N   
3861 C CA  . ASN B 175 ? 0.2816 0.1555 0.1397 0.0042  -0.0223 -0.0183 398  ASN B CA  
3862 C C   . ASN B 175 ? 0.2880 0.1540 0.1452 -0.0037 -0.0226 -0.0185 398  ASN B C   
3863 O O   . ASN B 175 ? 0.3139 0.1556 0.1702 0.0026  0.0154  -0.0146 398  ASN B O   
3864 C CB  . ASN B 175 ? 0.2933 0.1761 0.1457 0.0390  -0.0818 -0.0055 398  ASN B CB  
3865 C CG  . ASN B 175 ? 0.3657 0.2085 0.2013 0.0313  -0.0623 -0.0066 398  ASN B CG  
3866 O OD1 . ASN B 175 ? 0.3626 0.2284 0.2267 -0.0457 -0.0627 -0.0211 398  ASN B OD1 
3867 N ND2 . ASN B 175 ? 0.4578 0.2518 0.2477 0.0484  -0.0396 -0.0001 398  ASN B ND2 
3868 N N   . ASP B 176 ? 0.2842 0.1470 0.1627 -0.0351 -0.0124 0.0102  399  ASP B N   
3869 C CA  . ASP B 176 ? 0.3496 0.1538 0.1675 -0.0492 -0.0223 0.0032  399  ASP B CA  
3870 C C   . ASP B 176 ? 0.3304 0.1459 0.1639 -0.0729 -0.0316 0.0000  399  ASP B C   
3871 O O   . ASP B 176 ? 0.3603 0.1498 0.1454 -0.0378 -0.0304 0.0132  399  ASP B O   
3872 C CB  . ASP B 176 ? 0.4257 0.1776 0.1829 -0.0589 -0.0458 0.0170  399  ASP B CB  
3873 C CG  . ASP B 176 ? 0.4817 0.2090 0.2008 -0.0618 -0.0581 0.0261  399  ASP B CG  
3874 O OD1 . ASP B 176 ? 0.4771 0.2134 0.2016 -0.0472 -0.0521 0.0212  399  ASP B OD1 
3875 O OD2 . ASP B 176 ? 0.4996 0.2252 0.2783 -0.0706 -0.0443 0.0359  399  ASP B OD2 
3876 N N   . ASP B 177 ? 0.3378 0.1580 0.1634 -0.0766 -0.0542 0.0143  400  ASP B N   
3877 C CA  . ASP B 177 ? 0.3562 0.1793 0.1912 -0.0848 -0.0936 0.0410  400  ASP B CA  
3878 C C   . ASP B 177 ? 0.3767 0.1732 0.2195 -0.0640 -0.0793 0.0412  400  ASP B C   
3879 O O   . ASP B 177 ? 0.4253 0.1940 0.3004 -0.1189 -0.0819 0.0412  400  ASP B O   
3880 C CB  . ASP B 177 ? 0.3671 0.2155 0.2782 -0.0931 -0.0733 0.0355  400  ASP B CB  
3881 C CG  . ASP B 177 ? 0.4134 0.2556 0.3537 -0.0352 -0.0123 0.0184  400  ASP B CG  
3882 O OD1 . ASP B 177 ? 0.4328 0.2567 0.3907 0.0041  -0.0087 0.0282  400  ASP B OD1 
3883 O OD2 . ASP B 177 ? 0.4712 0.2823 0.3745 -0.0365 0.0246  -0.0233 400  ASP B OD2 
3884 N N   . ASP B 178 ? 0.3917 0.1790 0.1801 -0.0054 -0.0359 0.0286  401  ASP B N   
3885 C CA  . ASP B 178 ? 0.4309 0.1916 0.1717 0.0038  -0.0309 0.0323  401  ASP B CA  
3886 C C   . ASP B 178 ? 0.4218 0.1795 0.1853 -0.0176 -0.0146 0.0342  401  ASP B C   
3887 O O   . ASP B 178 ? 0.4507 0.1981 0.2267 -0.0250 0.0109  0.0526  401  ASP B O   
3888 C CB  . ASP B 178 ? 0.5063 0.2253 0.1540 0.0244  -0.0410 -0.0073 401  ASP B CB  
3889 C CG  . ASP B 178 ? 0.6089 0.2985 0.2302 0.0292  -0.0122 -0.0242 401  ASP B CG  
3890 O OD1 . ASP B 178 ? 0.6276 0.3317 0.2506 0.0321  0.0129  -0.0017 401  ASP B OD1 
3891 O OD2 . ASP B 178 ? 0.6913 0.3292 0.2675 0.0243  0.0167  -0.0551 401  ASP B OD2 
3892 N N   . ASN B 179 ? 0.3846 0.1731 0.1599 0.0155  -0.0586 0.0000  402  ASN B N   
3893 C CA  . ASN B 179 ? 0.3906 0.1986 0.1750 0.0425  -0.0786 0.0087  402  ASN B CA  
3894 C C   . ASN B 179 ? 0.3524 0.1940 0.2132 0.0376  -0.0574 -0.0171 402  ASN B C   
3895 O O   . ASN B 179 ? 0.3704 0.2200 0.2180 0.0514  -0.0740 -0.0169 402  ASN B O   
3896 C CB  . ASN B 179 ? 0.4581 0.2649 0.2105 0.0437  -0.0777 0.0247  402  ASN B CB  
3897 C CG  . ASN B 179 ? 0.5285 0.3340 0.2797 0.0298  -0.0699 0.0582  402  ASN B CG  
3898 O OD1 . ASN B 179 ? 0.5422 0.3775 0.3024 0.0099  -0.0698 0.0799  402  ASN B OD1 
3899 N ND2 . ASN B 179 ? 0.5612 0.3623 0.3188 0.0483  -0.0592 0.0521  402  ASN B ND2 
3900 N N   . TYR B 180 ? 0.2960 0.1483 0.1638 0.0321  -0.0618 -0.0152 403  TYR B N   
3901 C CA  . TYR B 180 ? 0.2914 0.1264 0.1361 0.0095  -0.0439 -0.0042 403  TYR B CA  
3902 C C   . TYR B 180 ? 0.2583 0.1215 0.1610 -0.0003 -0.0478 -0.0178 403  TYR B C   
3903 O O   . TYR B 180 ? 0.2681 0.1484 0.1863 0.0027  -0.0389 -0.0004 403  TYR B O   
3904 C CB  . TYR B 180 ? 0.2501 0.1216 0.1222 0.0228  -0.0543 0.0004  403  TYR B CB  
3905 C CG  . TYR B 180 ? 0.2331 0.1192 0.1163 0.0075  -0.0445 -0.0022 403  TYR B CG  
3906 C CD1 . TYR B 180 ? 0.2307 0.1098 0.1524 -0.0118 -0.0459 0.0131  403  TYR B CD1 
3907 C CD2 . TYR B 180 ? 0.2195 0.1305 0.1384 0.0182  -0.0409 0.0143  403  TYR B CD2 
3908 C CE1 . TYR B 180 ? 0.2149 0.1218 0.1450 -0.0129 -0.0569 0.0175  403  TYR B CE1 
3909 C CE2 . TYR B 180 ? 0.2060 0.1232 0.1272 0.0173  -0.0293 -0.0016 403  TYR B CE2 
3910 C CZ  . TYR B 180 ? 0.1952 0.1198 0.1531 -0.0135 -0.0473 0.0100  403  TYR B CZ  
3911 O OH  . TYR B 180 ? 0.2057 0.1222 0.1548 -0.0067 -0.0586 -0.0077 403  TYR B OH  
3912 N N   . LYS B 181 ? 0.2459 0.0998 0.1318 -0.0042 -0.0409 -0.0185 404  LYS B N   
3913 C CA  . LYS B 181 ? 0.2108 0.1117 0.1352 0.0064  -0.0501 -0.0147 404  LYS B CA  
3914 C C   . LYS B 181 ? 0.2068 0.1085 0.1585 -0.0040 -0.0479 -0.0046 404  LYS B C   
3915 O O   . LYS B 181 ? 0.1949 0.1028 0.1695 -0.0045 -0.0533 0.0142  404  LYS B O   
3921 N N   . GLN B 182 ? 0.2089 0.0896 0.1405 -0.0293 -0.0660 -0.0006 405  GLN B N   
3922 C CA  . GLN B 182 ? 0.1990 0.0941 0.1473 0.0037  -0.0761 0.0132  405  GLN B CA  
3923 C C   . GLN B 182 ? 0.1954 0.0919 0.1694 0.0006  -0.0421 0.0082  405  GLN B C   
3924 O O   . GLN B 182 ? 0.2084 0.1106 0.1744 -0.0212 -0.0392 0.0221  405  GLN B O   
3925 C CB  . GLN B 182 ? 0.2137 0.0988 0.1708 -0.0032 -0.0673 0.0236  405  GLN B CB  
3926 C CG  . GLN B 182 ? 0.1884 0.1092 0.1656 -0.0062 -0.0813 0.0109  405  GLN B CG  
3927 C CD  . GLN B 182 ? 0.1839 0.1132 0.1621 -0.0057 -0.0210 0.0093  405  GLN B CD  
3928 O OE1 . GLN B 182 ? 0.2132 0.1125 0.1563 0.0030  -0.0709 -0.0051 405  GLN B OE1 
3929 N NE2 . GLN B 182 ? 0.1752 0.1263 0.1874 -0.0069 -0.0436 0.0051  405  GLN B NE2 
3930 N N   . TRP B 183 ? 0.1940 0.0672 0.1530 -0.0078 -0.0581 0.0045  406  TRP B N   
3931 C CA  . TRP B 183 ? 0.1903 0.0765 0.1884 -0.0116 -0.0830 0.0092  406  TRP B CA  
3932 C C   . TRP B 183 ? 0.2083 0.1036 0.1883 -0.0083 -0.0648 0.0046  406  TRP B C   
3933 O O   . TRP B 183 ? 0.2262 0.1142 0.2118 -0.0203 -0.0647 -0.0120 406  TRP B O   
3934 C CB  . TRP B 183 ? 0.1839 0.0817 0.2117 -0.0227 -0.0734 0.0058  406  TRP B CB  
3935 C CG  . TRP B 183 ? 0.1930 0.0909 0.1709 -0.0155 -0.0825 -0.0036 406  TRP B CG  
3936 C CD1 . TRP B 183 ? 0.2141 0.0971 0.1891 -0.0049 -0.0907 -0.0050 406  TRP B CD1 
3937 C CD2 . TRP B 183 ? 0.2356 0.0880 0.1736 -0.0064 -0.0674 0.0098  406  TRP B CD2 
3938 N NE1 . TRP B 183 ? 0.2654 0.1071 0.1626 -0.0198 -0.0588 0.0115  406  TRP B NE1 
3939 C CE2 . TRP B 183 ? 0.2360 0.0908 0.1365 -0.0136 -0.0809 -0.0078 406  TRP B CE2 
3940 C CE3 . TRP B 183 ? 0.2369 0.0876 0.1547 -0.0168 -0.0829 -0.0139 406  TRP B CE3 
3941 C CZ2 . TRP B 183 ? 0.2424 0.1024 0.1585 0.0088  -0.0614 -0.0308 406  TRP B CZ2 
3942 C CZ3 . TRP B 183 ? 0.2422 0.1013 0.1683 -0.0097 -0.0883 -0.0254 406  TRP B CZ3 
3943 C CH2 . TRP B 183 ? 0.2440 0.1087 0.1665 0.0077  -0.0846 -0.0212 406  TRP B CH2 
3944 N N   A GLU B 184 ? 0.2212 0.1292 0.1778 0.0012  -0.0594 -0.0013 407  GLU B N   
3945 N N   B GLU B 184 ? 0.1946 0.1106 0.1853 -0.0100 -0.0621 0.0068  407  GLU B N   
3946 C CA  A GLU B 184 ? 0.2199 0.1348 0.1548 0.0228  -0.0772 0.0095  407  GLU B CA  
3947 C CA  B GLU B 184 ? 0.1770 0.1102 0.1816 -0.0080 -0.0695 0.0153  407  GLU B CA  
3948 C C   A GLU B 184 ? 0.2019 0.1256 0.1707 0.0033  -0.0860 0.0220  407  GLU B C   
3949 C C   B GLU B 184 ? 0.1744 0.1157 0.1903 -0.0103 -0.0742 0.0169  407  GLU B C   
3950 O O   A GLU B 184 ? 0.2162 0.1208 0.1978 0.0081  -0.0910 0.0115  407  GLU B O   
3951 O O   B GLU B 184 ? 0.1818 0.1049 0.2120 -0.0207 -0.0790 0.0070  407  GLU B O   
3952 C CB  A GLU B 184 ? 0.2566 0.1505 0.1691 0.0343  -0.0592 0.0249  407  GLU B CB  
3953 C CB  B GLU B 184 ? 0.1754 0.1092 0.1949 -0.0287 -0.0587 0.0352  407  GLU B CB  
3954 C CG  A GLU B 184 ? 0.2695 0.1439 0.1782 0.0320  -0.0744 0.0433  407  GLU B CG  
3955 C CG  B GLU B 184 ? 0.1659 0.1003 0.2020 -0.0488 -0.0727 0.0416  407  GLU B CG  
3956 C CD  A GLU B 184 ? 0.3154 0.1526 0.1941 -0.0087 -0.0573 0.0407  407  GLU B CD  
3957 C CD  B GLU B 184 ? 0.2083 0.1202 0.2227 -0.0708 -0.0589 0.0336  407  GLU B CD  
3958 O OE1 A GLU B 184 ? 0.3562 0.1726 0.2115 -0.0134 -0.0269 0.0546  407  GLU B OE1 
3959 O OE1 B GLU B 184 ? 0.2432 0.1225 0.2112 -0.0786 -0.0645 0.0070  407  GLU B OE1 
3960 O OE2 A GLU B 184 ? 0.3484 0.1573 0.2122 -0.0246 -0.0546 0.0092  407  GLU B OE2 
3961 O OE2 B GLU B 184 ? 0.2220 0.1380 0.2221 -0.0588 -0.0070 0.0395  407  GLU B OE2 
3962 N N   . LEU B 185 ? 0.1627 0.1367 0.1943 0.0039  -0.0474 0.0084  408  LEU B N   
3963 C CA  . LEU B 185 ? 0.1852 0.1499 0.1874 -0.0203 -0.0379 0.0016  408  LEU B CA  
3964 C C   . LEU B 185 ? 0.2296 0.1468 0.1574 -0.0354 -0.0677 0.0180  408  LEU B C   
3965 O O   . LEU B 185 ? 0.2596 0.1479 0.1764 -0.0421 -0.0485 0.0008  408  LEU B O   
3966 C CB  . LEU B 185 ? 0.1786 0.1481 0.1761 -0.0124 -0.0555 0.0159  408  LEU B CB  
3967 C CG  . LEU B 185 ? 0.1993 0.1452 0.1731 0.0100  -0.0830 -0.0211 408  LEU B CG  
3968 C CD1 . LEU B 185 ? 0.2035 0.1764 0.2004 0.0053  -0.0567 -0.0315 408  LEU B CD1 
3969 C CD2 . LEU B 185 ? 0.2577 0.1459 0.1912 0.0112  -0.0264 0.0050  408  LEU B CD2 
3970 N N   . PRO B 186 ? 0.2244 0.1226 0.1925 -0.0283 -0.1215 0.0325  409  PRO B N   
3971 C CA  A PRO B 186 ? 0.2487 0.1249 0.2347 -0.0283 -0.1369 0.0433  409  PRO B CA  
3972 C CA  B PRO B 186 ? 0.2503 0.1331 0.2419 -0.0413 -0.1300 0.0448  409  PRO B CA  
3973 C C   . PRO B 186 ? 0.2496 0.1363 0.2807 -0.0425 -0.1441 0.0284  409  PRO B C   
3974 O O   . PRO B 186 ? 0.2276 0.1569 0.3155 -0.0236 -0.1199 0.0209  409  PRO B O   
3975 C CB  A PRO B 186 ? 0.2858 0.1183 0.2359 -0.0181 -0.1142 0.0409  409  PRO B CB  
3976 C CB  B PRO B 186 ? 0.2952 0.1425 0.2568 -0.0526 -0.0893 0.0441  409  PRO B CB  
3977 C CG  A PRO B 186 ? 0.2495 0.1056 0.2104 -0.0304 -0.1285 0.0172  409  PRO B CG  
3978 C CG  B PRO B 186 ? 0.2625 0.1399 0.2379 -0.0840 -0.0824 0.0306  409  PRO B CG  
3979 C CD  A PRO B 186 ? 0.2453 0.1074 0.2134 -0.0374 -0.0996 0.0289  409  PRO B CD  
3980 C CD  B PRO B 186 ? 0.2450 0.1247 0.2270 -0.0648 -0.0802 0.0339  409  PRO B CD  
3981 N N   . ASN B 187 ? 0.2964 0.1524 0.3178 -0.0294 -0.1807 0.0413  410  ASN B N   
3982 C CA  . ASN B 187 ? 0.3498 0.1739 0.3495 -0.0091 -0.1925 0.0462  410  ASN B CA  
3983 C C   . ASN B 187 ? 0.3142 0.1495 0.3703 -0.0011 -0.1904 0.0246  410  ASN B C   
3984 O O   . ASN B 187 ? 0.3192 0.1480 0.3685 -0.0026 -0.2045 0.0000  410  ASN B O   
3985 C CB  . ASN B 187 ? 0.4333 0.2274 0.3672 0.0094  -0.2031 0.0646  410  ASN B CB  
3986 C CG  . ASN B 187 ? 0.5696 0.2480 0.4342 0.0239  -0.1877 0.0945  410  ASN B CG  
3987 O OD1 . ASN B 187 ? 0.6386 0.2511 0.4816 0.0160  -0.1228 0.0953  410  ASN B OD1 
3988 N ND2 . ASN B 187 ? 0.6292 0.2676 0.4374 0.0280  -0.1362 0.1084  410  ASN B ND2 
3989 N N   . TYR B 188 ? 0.2816 0.1517 0.3792 -0.0009 -0.1755 0.0346  411  TYR B N   
3990 C CA  . TYR B 188 ? 0.2686 0.1396 0.3535 0.0013  -0.1677 0.0261  411  TYR B CA  
3991 C C   . TYR B 188 ? 0.2686 0.1391 0.3674 -0.0023 -0.1793 0.0169  411  TYR B C   
3992 O O   . TYR B 188 ? 0.2631 0.1274 0.3650 -0.0076 -0.1757 0.0164  411  TYR B O   
3993 C CB  . TYR B 188 ? 0.2545 0.1374 0.3695 0.0190  -0.1654 -0.0007 411  TYR B CB  
3994 C CG  . TYR B 188 ? 0.2588 0.1299 0.3183 0.0239  -0.1667 -0.0174 411  TYR B CG  
3995 C CD1 . TYR B 188 ? 0.2323 0.1388 0.2878 0.0301  -0.1420 -0.0014 411  TYR B CD1 
3996 C CD2 . TYR B 188 ? 0.2821 0.1321 0.2923 0.0274  -0.1666 -0.0140 411  TYR B CD2 
3997 C CE1 . TYR B 188 ? 0.2247 0.1204 0.2774 -0.0070 -0.1308 0.0105  411  TYR B CE1 
3998 C CE2 . TYR B 188 ? 0.2733 0.1317 0.2578 0.0236  -0.1418 0.0125  411  TYR B CE2 
3999 C CZ  . TYR B 188 ? 0.2292 0.1210 0.2403 -0.0148 -0.1379 0.0270  411  TYR B CZ  
4000 O OH  . TYR B 188 ? 0.2168 0.1185 0.2509 -0.0132 -0.1156 0.0047  411  TYR B OH  
4001 N N   . SER B 189 ? 0.3046 0.1811 0.3986 0.0152  -0.1957 0.0174  412  SER B N   
4002 C CA  . SER B 189 ? 0.3236 0.1895 0.4535 -0.0110 -0.2168 0.0407  412  SER B CA  
4003 C C   . SER B 189 ? 0.3629 0.2039 0.4966 -0.0283 -0.2452 0.0510  412  SER B C   
4004 O O   . SER B 189 ? 0.3641 0.2226 0.5210 -0.0034 -0.2390 0.0510  412  SER B O   
4005 C CB  . SER B 189 ? 0.3442 0.2065 0.4925 0.0013  -0.2133 0.0579  412  SER B CB  
4006 O OG  . SER B 189 ? 0.3671 0.2102 0.5402 0.0028  -0.2119 0.0692  412  SER B OG  
4007 N N   . GLY B 190 ? 0.3991 0.2590 0.5353 -0.0341 -0.2674 0.0652  413  GLY B N   
4008 C CA  . GLY B 190 ? 0.4687 0.3979 0.5865 -0.0273 -0.3050 0.0756  413  GLY B CA  
4009 C C   . GLY B 190 ? 0.5660 0.5878 0.6929 0.0049  -0.3594 0.0956  413  GLY B C   
4010 O O   . GLY B 190 ? 0.4891 0.5374 0.5992 0.0102  -0.3032 0.1063  413  GLY B O   
4011 N N   . ALA B 191 ? 0.7905 0.8395 0.9024 0.0099  -0.4975 0.0811  414  ALA B N   
4012 C CA  . ALA B 191 ? 1.0460 1.1098 1.1337 0.0055  -0.6152 0.0641  414  ALA B CA  
4013 C C   . ALA B 191 ? 1.3395 1.3907 1.3844 0.0082  -0.6760 0.0554  414  ALA B C   
4014 O O   . ALA B 191 ? 1.3158 1.3890 1.3575 0.0091  -0.7136 0.0494  414  ALA B O   
4015 C CB  . ALA B 191 ? 1.0290 1.1041 1.1273 0.0085  -0.6011 0.0628  414  ALA B CB  
4028 N N   . LEU B 194 ? 0.8346 0.8113 0.8269 0.0887  -0.1908 0.2688  417  LEU B N   
4029 C CA  . LEU B 194 ? 0.6986 0.6541 0.6876 0.0960  -0.1984 0.2843  417  LEU B CA  
4030 C C   . LEU B 194 ? 0.5770 0.5373 0.5809 0.0869  -0.1882 0.2458  417  LEU B C   
4031 O O   . LEU B 194 ? 0.5550 0.5221 0.5982 0.0767  -0.1986 0.2379  417  LEU B O   
4032 C CB  . LEU B 194 ? 0.7060 0.6270 0.6676 0.1089  -0.1586 0.2775  417  LEU B CB  
4033 C CG  . LEU B 194 ? 0.7044 0.6093 0.6395 0.1277  -0.1646 0.2867  417  LEU B CG  
4034 C CD1 . LEU B 194 ? 0.6987 0.5905 0.5904 0.1557  -0.1734 0.2642  417  LEU B CD1 
4035 C CD2 . LEU B 194 ? 0.7038 0.6001 0.5968 0.1378  -0.1770 0.2751  417  LEU B CD2 
4036 N N   . ASN B 195 ? 0.4800 0.4629 0.5444 0.0583  -0.1745 0.2183  418  ASN B N   
4037 C CA  . ASN B 195 ? 0.4192 0.4167 0.5027 0.0349  -0.1727 0.1929  418  ASN B CA  
4038 C C   . ASN B 195 ? 0.4074 0.4145 0.5674 0.0129  -0.1359 0.1995  418  ASN B C   
4039 O O   . ASN B 195 ? 0.4410 0.4295 0.6297 -0.0004 -0.0473 0.1479  418  ASN B O   
4040 C CB  . ASN B 195 ? 0.4123 0.4034 0.4918 0.0101  -0.1950 0.1762  418  ASN B CB  
4041 C CG  . ASN B 195 ? 0.4230 0.3814 0.4832 -0.0116 -0.2100 0.1660  418  ASN B CG  
4042 O OD1 . ASN B 195 ? 0.4667 0.3758 0.4811 0.0049  -0.1782 0.1917  418  ASN B OD1 
4043 N ND2 . ASN B 195 ? 0.4553 0.3710 0.4792 -0.0336 -0.2214 0.1365  418  ASN B ND2 
4044 N N   . MET B 196 ? 0.3641 0.4142 0.5076 0.0008  -0.1793 0.1840  419  MET B N   
4045 C CA  . MET B 196 ? 0.3805 0.4339 0.5021 -0.0065 -0.1350 0.1478  419  MET B CA  
4046 C C   . MET B 196 ? 0.2912 0.3622 0.4459 -0.0174 -0.0772 0.0963  419  MET B C   
4047 O O   . MET B 196 ? 0.3124 0.3403 0.4610 -0.0452 -0.0411 0.0684  419  MET B O   
4052 N N   . GLY B 197 ? 0.2242 0.3086 0.4125 0.0222  -0.0036 0.0755  420  GLY B N   
4053 C CA  . GLY B 197 ? 0.2313 0.2738 0.3631 0.0376  0.0541  0.0291  420  GLY B CA  
4054 C C   . GLY B 197 ? 0.2096 0.2166 0.3042 0.0509  0.0024  0.0208  420  GLY B C   
4055 O O   . GLY B 197 ? 0.2452 0.2127 0.2989 0.0344  0.0036  -0.0017 420  GLY B O   
4056 N N   . LEU B 198 ? 0.1991 0.1839 0.2803 0.0439  0.0002  0.0140  421  LEU B N   
4057 C CA  . LEU B 198 ? 0.1857 0.1680 0.2381 0.0333  -0.0392 -0.0064 421  LEU B CA  
4058 C C   . LEU B 198 ? 0.1888 0.1500 0.2376 0.0357  -0.0473 -0.0202 421  LEU B C   
4059 O O   . LEU B 198 ? 0.2456 0.1326 0.2748 0.0517  -0.0082 -0.0091 421  LEU B O   
4060 C CB  . LEU B 198 ? 0.1985 0.1889 0.2403 0.0389  -0.0652 0.0008  421  LEU B CB  
4061 C CG  . LEU B 198 ? 0.2401 0.1890 0.2294 0.0624  -0.0695 0.0059  421  LEU B CG  
4062 C CD1 . LEU B 198 ? 0.2822 0.1989 0.2315 0.0319  -0.0326 0.0235  421  LEU B CD1 
4063 C CD2 . LEU B 198 ? 0.2476 0.1722 0.2551 0.0522  -0.0664 -0.0199 421  LEU B CD2 
4064 N N   . ALA B 199 ? 0.1858 0.1436 0.2165 0.0191  -0.0354 -0.0165 422  ALA B N   
4065 C CA  . ALA B 199 ? 0.2097 0.1381 0.1992 0.0061  -0.0459 0.0066  422  ALA B CA  
4066 C C   . ALA B 199 ? 0.1995 0.1259 0.1840 0.0098  -0.0402 0.0087  422  ALA B C   
4067 O O   . ALA B 199 ? 0.2118 0.1206 0.1889 0.0180  -0.0438 0.0195  422  ALA B O   
4068 C CB  . ALA B 199 ? 0.2396 0.1228 0.2014 0.0078  -0.0804 0.0070  422  ALA B CB  
4069 N N   . PRO B 200 ? 0.2323 0.1376 0.1940 -0.0055 -0.0260 -0.0039 423  PRO B N   
4070 C CA  . PRO B 200 ? 0.2484 0.1152 0.2026 -0.0062 -0.0284 -0.0063 423  PRO B CA  
4071 C C   . PRO B 200 ? 0.2317 0.1096 0.1932 -0.0098 -0.0545 0.0220  423  PRO B C   
4072 O O   . PRO B 200 ? 0.2342 0.1006 0.2117 -0.0005 -0.0623 0.0073  423  PRO B O   
4073 C CB  . PRO B 200 ? 0.2954 0.1240 0.2097 -0.0216 -0.0147 -0.0204 423  PRO B CB  
4074 C CG  . PRO B 200 ? 0.3400 0.1618 0.2244 -0.0458 0.0123  -0.0585 423  PRO B CG  
4075 C CD  . PRO B 200 ? 0.2936 0.1545 0.2185 -0.0318 0.0065  -0.0292 423  PRO B CD  
4076 N N   . SER B 201 ? 0.2166 0.1256 0.2133 -0.0063 -0.0793 0.0131  424  SER B N   
4077 C CA  . SER B 201 ? 0.2066 0.1320 0.2238 -0.0140 -0.1044 -0.0017 424  SER B CA  
4078 C C   . SER B 201 ? 0.2224 0.1203 0.2220 -0.0046 -0.0982 -0.0113 424  SER B C   
4079 O O   . SER B 201 ? 0.2561 0.1291 0.2672 0.0069  -0.0887 -0.0231 424  SER B O   
4080 C CB  . SER B 201 ? 0.2447 0.1479 0.2673 0.0034  -0.0762 0.0189  424  SER B CB  
4081 O OG  . SER B 201 ? 0.2888 0.1565 0.2883 0.0197  -0.0659 0.0348  424  SER B OG  
4082 N N   . VAL B 202 ? 0.1946 0.1198 0.2122 -0.0074 -0.1007 -0.0004 425  VAL B N   
4083 C CA  . VAL B 202 ? 0.2333 0.1081 0.1956 -0.0068 -0.0923 -0.0045 425  VAL B CA  
4084 C C   . VAL B 202 ? 0.2775 0.1055 0.1979 -0.0148 -0.0792 -0.0233 425  VAL B C   
4085 O O   . VAL B 202 ? 0.2652 0.1194 0.1960 -0.0141 -0.0812 -0.0073 425  VAL B O   
4086 C CB  . VAL B 202 ? 0.2505 0.1189 0.1968 -0.0015 -0.0596 0.0064  425  VAL B CB  
4087 C CG1 . VAL B 202 ? 0.2563 0.1614 0.2219 -0.0311 -0.0558 -0.0136 425  VAL B CG1 
4088 C CG2 . VAL B 202 ? 0.2791 0.1090 0.2043 -0.0158 -0.0315 -0.0058 425  VAL B CG2 
4089 N N   . PHE B 203 ? 0.2901 0.1339 0.2203 -0.0414 -0.0920 -0.0232 426  PHE B N   
4090 C CA  A PHE B 203 ? 0.3106 0.1438 0.2215 -0.0348 -0.1039 -0.0155 426  PHE B CA  
4091 C CA  B PHE B 203 ? 0.3012 0.1511 0.2327 -0.0508 -0.0783 -0.0154 426  PHE B CA  
4092 C C   . PHE B 203 ? 0.3111 0.1486 0.2303 -0.0391 -0.0966 -0.0217 426  PHE B C   
4093 O O   . PHE B 203 ? 0.3207 0.1739 0.2110 -0.0257 -0.0805 -0.0131 426  PHE B O   
4094 C CB  A PHE B 203 ? 0.3378 0.1437 0.2002 -0.0160 -0.1294 -0.0036 426  PHE B CB  
4095 C CB  B PHE B 203 ? 0.3032 0.1697 0.2252 -0.0742 -0.0694 0.0004  426  PHE B CB  
4096 C CG  A PHE B 203 ? 0.3470 0.1395 0.2086 0.0455  -0.1326 -0.0182 426  PHE B CG  
4097 C CG  B PHE B 203 ? 0.2975 0.1756 0.2279 -0.0711 -0.0642 0.0119  426  PHE B CG  
4098 C CD1 A PHE B 203 ? 0.3636 0.1638 0.2185 0.0436  -0.1424 -0.0425 426  PHE B CD1 
4099 C CD1 B PHE B 203 ? 0.2915 0.1870 0.2418 -0.0759 -0.0647 0.0286  426  PHE B CD1 
4100 C CD2 A PHE B 203 ? 0.3260 0.1517 0.2050 0.0503  -0.1364 -0.0086 426  PHE B CD2 
4101 C CD2 B PHE B 203 ? 0.2927 0.1675 0.2208 -0.0223 -0.0644 0.0491  426  PHE B CD2 
4102 C CE1 A PHE B 203 ? 0.3626 0.1741 0.2369 0.0606  -0.1446 -0.0454 426  PHE B CE1 
4103 C CE1 B PHE B 203 ? 0.2693 0.1793 0.2361 -0.0863 -0.0778 0.0325  426  PHE B CE1 
4104 C CE2 A PHE B 203 ? 0.3535 0.1574 0.2284 0.0595  -0.1187 -0.0399 426  PHE B CE2 
4105 C CE2 B PHE B 203 ? 0.2914 0.1598 0.2389 -0.0220 -0.0522 0.0616  426  PHE B CE2 
4106 C CZ  A PHE B 203 ? 0.3720 0.1726 0.2251 0.0354  -0.1271 -0.0647 426  PHE B CZ  
4107 C CZ  B PHE B 203 ? 0.3032 0.1717 0.2450 -0.0365 -0.0543 0.0587  426  PHE B CZ  
4108 N N   . PRO B 204 ? 0.3194 0.1444 0.2345 -0.0378 -0.1101 -0.0142 427  PRO B N   
4109 C CA  . PRO B 204 ? 0.3464 0.1668 0.2308 -0.0077 -0.1571 0.0281  427  PRO B CA  
4110 C C   . PRO B 204 ? 0.4892 0.1662 0.2692 -0.0403 -0.1163 0.0178  427  PRO B C   
4111 O O   . PRO B 204 ? 0.6509 0.1829 0.3314 -0.0574 -0.0294 0.0046  427  PRO B O   
4112 C CB  . PRO B 204 ? 0.3228 0.2227 0.2618 -0.0023 -0.1435 0.0327  427  PRO B CB  
4113 C CG  . PRO B 204 ? 0.3274 0.2160 0.3015 -0.0128 -0.0956 0.0163  427  PRO B CG  
4114 C CD  . PRO B 204 ? 0.3246 0.1580 0.2521 -0.0498 -0.0953 0.0017  427  PRO B CD  
4115 N N   . THR B 205 ? 0.4568 0.1474 0.2869 -0.0170 -0.1717 0.0158  428  THR B N   
4116 C CA  . THR B 205 ? 0.4451 0.1635 0.3281 -0.0092 -0.1984 0.0321  428  THR B CA  
4117 C C   . THR B 205 ? 0.4295 0.1658 0.3424 -0.0270 -0.1902 0.0513  428  THR B C   
4118 O O   . THR B 205 ? 0.4714 0.1818 0.3797 -0.0493 -0.1554 0.0703  428  THR B O   
4119 C CB  . THR B 205 ? 0.4875 0.1846 0.3680 0.0069  -0.1832 0.0134  428  THR B CB  
4120 O OG1 . THR B 205 ? 0.5015 0.1988 0.3919 0.0549  -0.1629 0.0107  428  THR B OG1 
4121 C CG2 . THR B 205 ? 0.4836 0.1971 0.3810 0.0129  -0.1859 0.0188  428  THR B CG2 
4122 N N   . TYR B 206 ? 0.4281 0.1686 0.3337 -0.0213 -0.1745 0.0589  429  TYR B N   
4123 C CA  . TYR B 206 ? 0.4425 0.1787 0.3700 -0.0181 -0.1804 0.0667  429  TYR B CA  
4124 C C   . TYR B 206 ? 0.4292 0.1579 0.3731 -0.0499 -0.1488 0.0598  429  TYR B C   
4125 O O   . TYR B 206 ? 0.4408 0.1620 0.3584 -0.0590 -0.1405 0.0328  429  TYR B O   
4126 C CB  . TYR B 206 ? 0.4627 0.2109 0.3854 -0.0401 -0.2183 0.0656  429  TYR B CB  
4127 C CG  . TYR B 206 ? 0.4748 0.2706 0.4072 -0.0421 -0.2546 0.0438  429  TYR B CG  
4128 C CD1 . TYR B 206 ? 0.4879 0.2952 0.4122 -0.0624 -0.2544 0.0001  429  TYR B CD1 
4129 C CD2 . TYR B 206 ? 0.4642 0.2974 0.4051 -0.0426 -0.2575 0.0312  429  TYR B CD2 
4130 C CE1 . TYR B 206 ? 0.4929 0.3240 0.4264 -0.0713 -0.2530 -0.0155 429  TYR B CE1 
4131 C CE2 . TYR B 206 ? 0.4834 0.3206 0.4332 -0.0525 -0.2681 0.0101  429  TYR B CE2 
4132 C CZ  . TYR B 206 ? 0.4949 0.3287 0.4250 -0.0694 -0.2526 -0.0201 429  TYR B CZ  
4133 O OH  . TYR B 206 ? 0.5295 0.3462 0.4402 -0.0637 -0.2595 -0.0424 429  TYR B OH  
4134 N N   . PRO B 207 ? 0.4271 0.1535 0.3983 -0.0627 -0.1218 0.0477  430  PRO B N   
4135 C CA  . PRO B 207 ? 0.4288 0.1561 0.3926 -0.0745 -0.1023 0.0526  430  PRO B CA  
4136 C C   . PRO B 207 ? 0.4510 0.1584 0.3878 -0.0732 -0.0885 0.0609  430  PRO B C   
4137 O O   . PRO B 207 ? 0.4990 0.1780 0.3704 -0.0521 -0.0944 0.0423  430  PRO B O   
4138 C CB  . PRO B 207 ? 0.4516 0.1535 0.4181 -0.0681 -0.0793 0.0535  430  PRO B CB  
4139 C CG  . PRO B 207 ? 0.4528 0.1545 0.4299 -0.0655 -0.0889 0.0505  430  PRO B CG  
4140 C CD  . PRO B 207 ? 0.4282 0.1581 0.4169 -0.0765 -0.0984 0.0504  430  PRO B CD  
4141 N N   . GLY B 208 ? 0.3939 0.1559 0.3762 -0.0826 -0.0753 0.0644  431  GLY B N   
4142 C CA  . GLY B 208 ? 0.3710 0.1566 0.3757 -0.0821 -0.0853 0.0664  431  GLY B CA  
4143 C C   . GLY B 208 ? 0.3336 0.1489 0.3409 -0.0735 -0.1037 0.0674  431  GLY B C   
4144 O O   . GLY B 208 ? 0.3207 0.1732 0.3733 -0.0766 -0.1198 0.0760  431  GLY B O   
4145 N N   . GLU B 209 ? 0.3087 0.1409 0.2826 -0.0793 -0.1123 0.0483  432  GLU B N   
4146 C CA  . GLU B 209 ? 0.2607 0.1307 0.2602 -0.0712 -0.1086 0.0342  432  GLU B CA  
4147 C C   . GLU B 209 ? 0.2532 0.1330 0.2515 -0.0643 -0.1009 0.0252  432  GLU B C   
4148 O O   . GLU B 209 ? 0.2535 0.1372 0.2526 -0.0602 -0.1087 0.0313  432  GLU B O   
4149 C CB  . GLU B 209 ? 0.2761 0.1236 0.2652 -0.0474 -0.1493 0.0431  432  GLU B CB  
4150 C CG  . GLU B 209 ? 0.2955 0.1379 0.2595 -0.0540 -0.1438 0.0169  432  GLU B CG  
4151 C CD  . GLU B 209 ? 0.3014 0.1394 0.2725 -0.0286 -0.1564 0.0183  432  GLU B CD  
4152 O OE1 . GLU B 209 ? 0.3165 0.1473 0.2862 -0.0278 -0.1387 0.0025  432  GLU B OE1 
4153 O OE2 . GLU B 209 ? 0.3256 0.1559 0.2711 -0.0502 -0.1371 0.0155  432  GLU B OE2 
4154 N N   . GLN B 210 ? 0.2316 0.1169 0.2444 -0.0739 -0.0601 0.0152  433  GLN B N   
4155 C CA  . GLN B 210 ? 0.2002 0.1175 0.2062 -0.0600 -0.0618 0.0031  433  GLN B CA  
4156 C C   . GLN B 210 ? 0.1977 0.1186 0.1679 -0.0398 -0.0892 0.0141  433  GLN B C   
4157 O O   . GLN B 210 ? 0.2473 0.1437 0.1562 -0.0494 -0.0875 0.0083  433  GLN B O   
4158 C CB  . GLN B 210 ? 0.2052 0.1319 0.2525 -0.0510 -0.0440 0.0360  433  GLN B CB  
4159 C CG  . GLN B 210 ? 0.2213 0.1458 0.2926 -0.0512 0.0068  0.0909  433  GLN B CG  
4160 C CD  . GLN B 210 ? 0.2477 0.1652 0.3636 -0.0308 0.0341  0.1074  433  GLN B CD  
4161 O OE1 . GLN B 210 ? 0.3008 0.2001 0.4318 -0.0064 0.0802  0.0886  433  GLN B OE1 
4162 N NE2 . GLN B 210 ? 0.1914 0.1684 0.3659 -0.0629 -0.0239 0.0905  433  GLN B NE2 
4163 N N   . LEU B 211 ? 0.1703 0.0978 0.1696 -0.0286 -0.0575 0.0350  434  LEU B N   
4164 C CA  . LEU B 211 ? 0.1897 0.1096 0.1585 -0.0320 -0.0696 0.0306  434  LEU B CA  
4165 C C   . LEU B 211 ? 0.1883 0.1110 0.1638 -0.0227 -0.0513 0.0124  434  LEU B C   
4166 O O   . LEU B 211 ? 0.2100 0.1162 0.1628 -0.0343 -0.0477 0.0129  434  LEU B O   
4167 C CB  . LEU B 211 ? 0.1886 0.1532 0.1367 -0.0256 -0.0786 0.0026  434  LEU B CB  
4168 C CG  . LEU B 211 ? 0.1675 0.1777 0.1649 -0.0074 -0.0992 -0.0040 434  LEU B CG  
4169 C CD1 . LEU B 211 ? 0.1823 0.1956 0.1704 -0.0035 -0.0834 0.0065  434  LEU B CD1 
4170 C CD2 . LEU B 211 ? 0.2384 0.2058 0.1909 -0.0141 -0.0876 -0.0382 434  LEU B CD2 
4171 N N   . LEU B 212 ? 0.2024 0.1053 0.1563 -0.0146 -0.0671 0.0242  435  LEU B N   
4172 C CA  A LEU B 212 ? 0.2074 0.1091 0.1416 -0.0115 -0.0726 0.0057  435  LEU B CA  
4173 C CA  B LEU B 212 ? 0.1928 0.1097 0.1493 -0.0181 -0.0600 0.0172  435  LEU B CA  
4174 C C   . LEU B 212 ? 0.1910 0.1038 0.1695 -0.0135 -0.0403 -0.0003 435  LEU B C   
4175 O O   . LEU B 212 ? 0.2049 0.1315 0.2028 -0.0250 -0.0159 -0.0188 435  LEU B O   
4176 C CB  A LEU B 212 ? 0.2410 0.1228 0.1248 0.0137  -0.0927 -0.0047 435  LEU B CB  
4177 C CB  B LEU B 212 ? 0.1981 0.1218 0.1389 -0.0176 -0.0661 0.0294  435  LEU B CB  
4178 C CG  A LEU B 212 ? 0.2448 0.1498 0.1431 0.0211  -0.0797 -0.0099 435  LEU B CG  
4179 C CG  B LEU B 212 ? 0.1861 0.1386 0.1419 -0.0274 -0.0499 0.0405  435  LEU B CG  
4180 C CD1 A LEU B 212 ? 0.2218 0.1575 0.1639 0.0264  -0.0687 -0.0369 435  LEU B CD1 
4181 C CD1 B LEU B 212 ? 0.1650 0.1538 0.1334 -0.0445 -0.0563 0.0537  435  LEU B CD1 
4182 C CD2 A LEU B 212 ? 0.2406 0.1610 0.1402 0.0062  -0.1021 -0.0102 435  LEU B CD2 
4183 C CD2 B LEU B 212 ? 0.1954 0.1352 0.1552 -0.0280 -0.0305 0.0217  435  LEU B CD2 
4184 N N   . PHE B 213 ? 0.2065 0.0736 0.1745 -0.0181 -0.0528 -0.0035 436  PHE B N   
4185 C CA  . PHE B 213 ? 0.2108 0.0788 0.1567 -0.0346 -0.0452 -0.0100 436  PHE B CA  
4186 C C   . PHE B 213 ? 0.1530 0.0879 0.1569 -0.0229 -0.0668 -0.0232 436  PHE B C   
4187 O O   . PHE B 213 ? 0.1787 0.1169 0.1755 -0.0321 -0.0516 -0.0114 436  PHE B O   
4188 C CB  . PHE B 213 ? 0.2481 0.0913 0.1459 -0.0330 -0.0617 -0.0043 436  PHE B CB  
4189 C CG  . PHE B 213 ? 0.2365 0.0917 0.2054 -0.0497 -0.0591 0.0320  436  PHE B CG  
4190 C CD1 . PHE B 213 ? 0.2265 0.1178 0.2188 -0.0251 -0.1074 0.0153  436  PHE B CD1 
4191 C CD2 . PHE B 213 ? 0.2398 0.1143 0.2374 -0.0519 -0.0746 0.0614  436  PHE B CD2 
4192 C CE1 . PHE B 213 ? 0.2292 0.1182 0.2377 -0.0512 -0.0799 -0.0016 436  PHE B CE1 
4193 C CE2 . PHE B 213 ? 0.2525 0.1310 0.2290 -0.0156 -0.0718 0.0433  436  PHE B CE2 
4194 C CZ  . PHE B 213 ? 0.2339 0.1314 0.2262 -0.0453 -0.0965 0.0201  436  PHE B CZ  
4195 N N   . PHE B 214 ? 0.1472 0.0861 0.1460 -0.0099 -0.0349 -0.0107 437  PHE B N   
4196 C CA  . PHE B 214 ? 0.1599 0.0709 0.1488 -0.0110 -0.0247 0.0063  437  PHE B CA  
4197 C C   . PHE B 214 ? 0.1516 0.0885 0.1393 -0.0150 -0.0337 -0.0335 437  PHE B C   
4198 O O   . PHE B 214 ? 0.1543 0.1138 0.1425 -0.0121 -0.0423 -0.0070 437  PHE B O   
4199 C CB  . PHE B 214 ? 0.1773 0.0954 0.1647 -0.0147 -0.0166 -0.0141 437  PHE B CB  
4200 C CG  . PHE B 214 ? 0.1581 0.0871 0.1456 0.0030  -0.0367 0.0023  437  PHE B CG  
4201 C CD1 . PHE B 214 ? 0.1742 0.0978 0.1656 -0.0078 -0.0216 -0.0152 437  PHE B CD1 
4202 C CD2 . PHE B 214 ? 0.1723 0.1152 0.1584 -0.0021 -0.0305 -0.0289 437  PHE B CD2 
4203 C CE1 . PHE B 214 ? 0.1587 0.1137 0.1557 -0.0237 -0.0341 -0.0139 437  PHE B CE1 
4204 C CE2 . PHE B 214 ? 0.1824 0.1243 0.1717 0.0024  -0.0255 -0.0331 437  PHE B CE2 
4205 C CZ  . PHE B 214 ? 0.1364 0.1383 0.1590 -0.0103 -0.0523 -0.0094 437  PHE B CZ  
4206 N N   . ARG B 215 ? 0.1761 0.0934 0.1403 0.0119  -0.0253 -0.0228 438  ARG B N   
4207 C CA  . ARG B 215 ? 0.1724 0.0983 0.1300 0.0111  -0.0213 -0.0265 438  ARG B CA  
4208 C C   . ARG B 215 ? 0.1557 0.1038 0.1478 -0.0079 -0.0451 -0.0220 438  ARG B C   
4209 O O   . ARG B 215 ? 0.1554 0.1229 0.1646 -0.0001 -0.0531 -0.0058 438  ARG B O   
4210 C CB  . ARG B 215 ? 0.1423 0.1310 0.1307 -0.0084 -0.0112 -0.0163 438  ARG B CB  
4211 C CG  . ARG B 215 ? 0.1509 0.1352 0.1458 -0.0106 -0.0152 -0.0053 438  ARG B CG  
4212 C CD  . ARG B 215 ? 0.1622 0.1304 0.2046 -0.0161 -0.0370 0.0259  438  ARG B CD  
4213 N NE  . ARG B 215 ? 0.2144 0.1332 0.1739 -0.0376 -0.0279 0.0315  438  ARG B NE  
4214 C CZ  . ARG B 215 ? 0.2206 0.1608 0.1861 -0.0452 -0.0212 0.0247  438  ARG B CZ  
4215 N NH1 . ARG B 215 ? 0.2373 0.1953 0.2315 -0.0405 -0.0236 0.0158  438  ARG B NH1 
4216 N NH2 . ARG B 215 ? 0.2326 0.1649 0.2041 -0.0398 -0.0355 0.0355  438  ARG B NH2 
4217 N N   . SER B 216 ? 0.1942 0.0893 0.1466 -0.0033 -0.0419 -0.0298 439  SER B N   
4218 C CA  . SER B 216 ? 0.1833 0.0918 0.1423 -0.0075 -0.0355 -0.0231 439  SER B CA  
4219 C C   . SER B 216 ? 0.1814 0.1092 0.1491 -0.0090 -0.0407 -0.0167 439  SER B C   
4220 O O   . SER B 216 ? 0.2044 0.1194 0.1421 0.0051  -0.0338 -0.0043 439  SER B O   
4221 C CB  . SER B 216 ? 0.1744 0.1058 0.1334 -0.0097 0.0016  0.0088  439  SER B CB  
4222 O OG  . SER B 216 ? 0.1911 0.1205 0.1278 0.0132  -0.0094 0.0032  439  SER B OG  
4223 N N   A TYR B 217 ? 0.1835 0.1122 0.1451 -0.0203 -0.0370 -0.0278 440  TYR B N   
4224 N N   B TYR B 217 ? 0.1944 0.1255 0.1595 -0.0137 -0.0119 -0.0305 440  TYR B N   
4225 C CA  A TYR B 217 ? 0.1900 0.1147 0.1486 -0.0078 -0.0321 -0.0117 440  TYR B CA  
4226 C CA  B TYR B 217 ? 0.1847 0.1351 0.1560 -0.0085 -0.0265 -0.0215 440  TYR B CA  
4227 C C   A TYR B 217 ? 0.2128 0.0964 0.1622 -0.0062 -0.0038 -0.0266 440  TYR B C   
4228 C C   B TYR B 217 ? 0.2151 0.1183 0.1675 -0.0262 -0.0108 -0.0223 440  TYR B C   
4229 O O   A TYR B 217 ? 0.2528 0.0965 0.1813 -0.0063 0.0423  -0.0539 440  TYR B O   
4230 O O   B TYR B 217 ? 0.2771 0.1066 0.1720 -0.0233 0.0071  -0.0303 440  TYR B O   
4231 C CB  A TYR B 217 ? 0.2094 0.1306 0.1868 0.0096  -0.0148 0.0185  440  TYR B CB  
4232 C CB  B TYR B 217 ? 0.1840 0.1642 0.1833 0.0198  -0.0253 -0.0034 440  TYR B CB  
4233 C CG  A TYR B 217 ? 0.2232 0.1451 0.1970 0.0010  -0.0126 -0.0125 440  TYR B CG  
4234 C CG  B TYR B 217 ? 0.1713 0.1772 0.2091 0.0088  -0.0189 -0.0032 440  TYR B CG  
4235 C CD1 A TYR B 217 ? 0.2522 0.1558 0.2182 0.0039  0.0079  -0.0120 440  TYR B CD1 
4236 C CD1 B TYR B 217 ? 0.1739 0.1797 0.2245 -0.0174 -0.0040 -0.0020 440  TYR B CD1 
4237 C CD2 A TYR B 217 ? 0.2563 0.1632 0.2398 -0.0104 0.0236  -0.0306 440  TYR B CD2 
4238 C CD2 B TYR B 217 ? 0.2046 0.1955 0.2404 -0.0101 0.0025  -0.0033 440  TYR B CD2 
4239 C CE1 A TYR B 217 ? 0.2531 0.1733 0.2381 -0.0054 0.0044  -0.0158 440  TYR B CE1 
4240 C CE1 B TYR B 217 ? 0.1962 0.2121 0.2510 -0.0385 0.0154  -0.0100 440  TYR B CE1 
4241 C CE2 A TYR B 217 ? 0.2629 0.1729 0.2549 -0.0353 0.0208  -0.0415 440  TYR B CE2 
4242 C CE2 B TYR B 217 ? 0.2128 0.2096 0.2558 -0.0290 0.0006  -0.0119 440  TYR B CE2 
4243 C CZ  A TYR B 217 ? 0.2838 0.1790 0.2724 -0.0287 0.0291  -0.0344 440  TYR B CZ  
4244 C CZ  B TYR B 217 ? 0.2086 0.2168 0.2598 -0.0418 0.0031  0.0000  440  TYR B CZ  
4245 O OH  A TYR B 217 ? 0.3063 0.1796 0.3128 -0.0484 0.0574  -0.0303 440  TYR B OH  
4246 O OH  B TYR B 217 ? 0.2246 0.2366 0.2653 -0.0486 0.0119  0.0035  440  TYR B OH  
4247 N N   . ILE B 218 ? 0.1807 0.1185 0.1675 -0.0389 -0.0287 -0.0413 441  ILE B N   
4248 C CA  A ILE B 218 ? 0.2175 0.1293 0.1758 -0.0390 -0.0264 -0.0411 441  ILE B CA  
4249 C CA  B ILE B 218 ? 0.2088 0.1184 0.1961 -0.0208 -0.0127 -0.0515 441  ILE B CA  
4250 C C   . ILE B 218 ? 0.2143 0.1266 0.1859 -0.0367 -0.0189 -0.0469 441  ILE B C   
4251 O O   . ILE B 218 ? 0.2154 0.1408 0.2054 -0.0270 -0.0050 -0.0397 441  ILE B O   
4252 C CB  A ILE B 218 ? 0.2131 0.1463 0.1555 -0.0156 -0.0538 -0.0434 441  ILE B CB  
4253 C CB  B ILE B 218 ? 0.1899 0.0976 0.2033 0.0370  -0.0174 -0.0631 441  ILE B CB  
4254 C CG1 A ILE B 218 ? 0.1848 0.1592 0.1558 -0.0040 -0.1010 -0.0021 441  ILE B CG1 
4255 C CG1 B ILE B 218 ? 0.2091 0.1008 0.1815 0.0427  -0.0504 -0.0459 441  ILE B CG1 
4256 C CG2 A ILE B 218 ? 0.2468 0.1514 0.1585 -0.0477 -0.0162 -0.0244 441  ILE B CG2 
4257 C CG2 B ILE B 218 ? 0.1692 0.1059 0.2042 0.0593  -0.0314 -0.0492 441  ILE B CG2 
4258 C CD1 A ILE B 218 ? 0.2022 0.1879 0.1806 0.0083  -0.0679 -0.0307 441  ILE B CD1 
4259 C CD1 B ILE B 218 ? 0.2545 0.1377 0.2089 0.0125  -0.0211 -0.0753 441  ILE B CD1 
4260 N N   . PRO B 219 ? 0.1918 0.1021 0.1726 -0.0219 -0.0367 -0.0210 442  PRO B N   
4261 C CA  . PRO B 219 ? 0.2124 0.1138 0.1602 -0.0086 -0.0333 -0.0384 442  PRO B CA  
4262 C C   . PRO B 219 ? 0.2188 0.1115 0.1455 -0.0142 -0.0434 -0.0273 442  PRO B C   
4263 O O   . PRO B 219 ? 0.2134 0.1171 0.1568 -0.0049 -0.0463 -0.0032 442  PRO B O   
4264 C CB  . PRO B 219 ? 0.2464 0.1272 0.1825 -0.0210 -0.0205 -0.0385 442  PRO B CB  
4265 C CG  . PRO B 219 ? 0.2460 0.1307 0.1969 -0.0058 -0.0034 -0.0294 442  PRO B CG  
4266 C CD  . PRO B 219 ? 0.2154 0.1158 0.1746 -0.0197 0.0039  -0.0032 442  PRO B CD  
4267 N N   . MET B 220 ? 0.2201 0.1146 0.1343 -0.0355 -0.0434 -0.0304 443  MET B N   
4268 C CA  . MET B 220 ? 0.2288 0.1156 0.1399 -0.0514 -0.0239 -0.0209 443  MET B CA  
4269 C C   . MET B 220 ? 0.2173 0.1136 0.1256 0.0131  -0.0437 -0.0071 443  MET B C   
4270 O O   . MET B 220 ? 0.2210 0.1280 0.1564 0.0067  -0.0312 -0.0185 443  MET B O   
4271 C CB  . MET B 220 ? 0.2509 0.1233 0.1961 -0.0369 0.0124  -0.0016 443  MET B CB  
4272 C CG  . MET B 220 ? 0.2514 0.1278 0.2010 -0.0580 -0.0159 -0.0192 443  MET B CG  
4273 S SD  . MET B 220 ? 0.2770 0.1296 0.1972 -0.0297 -0.0169 -0.0075 443  MET B SD  
4274 C CE  . MET B 220 ? 0.2874 0.1101 0.2534 -0.0024 0.0341  -0.0018 443  MET B CE  
4275 N N   . LYS B 221 ? 0.2228 0.1281 0.1319 -0.0145 -0.0272 -0.0244 444  LYS B N   
4276 C CA  . LYS B 221 ? 0.2366 0.1251 0.1458 -0.0058 -0.0508 -0.0470 444  LYS B CA  
4277 C C   . LYS B 221 ? 0.2443 0.1332 0.1736 0.0258  -0.0298 -0.0106 444  LYS B C   
4278 O O   . LYS B 221 ? 0.2244 0.1250 0.2083 0.0122  -0.0158 -0.0194 444  LYS B O   
4279 C CB  . LYS B 221 ? 0.2279 0.1246 0.1471 -0.0099 -0.0496 -0.0388 444  LYS B CB  
4280 C CG  . LYS B 221 ? 0.2690 0.1228 0.1569 -0.0153 -0.0343 -0.0355 444  LYS B CG  
4281 C CD  . LYS B 221 ? 0.2745 0.1189 0.1733 -0.0264 -0.0306 -0.0519 444  LYS B CD  
4282 C CE  . LYS B 221 ? 0.3131 0.1262 0.1594 -0.0202 -0.0321 -0.0311 444  LYS B CE  
4283 N NZ  . LYS B 221 ? 0.2622 0.1260 0.2134 0.0067  -0.0469 -0.0085 444  LYS B NZ  
4284 N N   . GLY B 222 ? 0.2485 0.1405 0.1510 0.0008  -0.0175 -0.0217 445  GLY B N   
4285 C CA  . GLY B 222 ? 0.2407 0.1524 0.1615 -0.0334 -0.0293 -0.0234 445  GLY B CA  
4286 C C   . GLY B 222 ? 0.2634 0.1684 0.1949 -0.0259 -0.0192 -0.0152 445  GLY B C   
4287 O O   . GLY B 222 ? 0.3061 0.1750 0.2284 -0.0187 -0.0081 -0.0233 445  GLY B O   
4288 N N   . GLY B 223 ? 0.2858 0.1786 0.1830 -0.0400 -0.0174 0.0101  446  GLY B N   
4289 C CA  . GLY B 223 ? 0.2981 0.1947 0.2004 -0.0474 -0.0212 0.0070  446  GLY B CA  
4290 C C   . GLY B 223 ? 0.2933 0.1916 0.1789 -0.0354 -0.0200 0.0017  446  GLY B C   
4291 O O   . GLY B 223 ? 0.3169 0.1922 0.2010 -0.0417 -0.0228 -0.0038 446  GLY B O   
4292 N N   . TYR B 224 ? 0.2675 0.1900 0.2027 -0.0427 0.0087  -0.0033 447  TYR B N   
4293 C CA  . TYR B 224 ? 0.2840 0.2109 0.1915 -0.0387 0.0440  -0.0229 447  TYR B CA  
4294 C C   . TYR B 224 ? 0.3289 0.1880 0.2026 -0.0132 0.0484  -0.0004 447  TYR B C   
4295 O O   . TYR B 224 ? 0.3608 0.1895 0.2268 0.0334  0.0440  0.0036  447  TYR B O   
4304 N N   . GLY B 225 ? 0.3066 0.1660 0.1702 -0.0512 0.0281  -0.0325 448  GLY B N   
4305 C CA  . GLY B 225 ? 0.2974 0.1591 0.1496 -0.0340 0.0355  -0.0429 448  GLY B CA  
4306 C C   . GLY B 225 ? 0.2764 0.1452 0.1692 -0.0423 0.0248  -0.0474 448  GLY B C   
4307 O O   . GLY B 225 ? 0.2946 0.1466 0.1980 -0.0349 0.0286  -0.0328 448  GLY B O   
4308 N N   . SER B 226 ? 0.2488 0.1683 0.1762 -0.0185 0.0089  -0.0559 449  SER B N   
4309 C CA  . SER B 226 ? 0.1964 0.1673 0.1908 -0.0137 0.0043  -0.0283 449  SER B CA  
4310 C C   . SER B 226 ? 0.2204 0.1533 0.1768 -0.0187 -0.0017 -0.0224 449  SER B C   
4311 O O   . SER B 226 ? 0.2527 0.1624 0.1956 -0.0205 -0.0244 -0.0314 449  SER B O   
4312 C CB  . SER B 226 ? 0.1880 0.1848 0.2493 0.0147  0.0183  -0.0420 449  SER B CB  
4313 O OG  . SER B 226 ? 0.2330 0.1943 0.2909 0.0184  0.0513  -0.0322 449  SER B OG  
4314 N N   . PRO B 227 ? 0.2318 0.1474 0.1674 -0.0315 -0.0128 -0.0076 450  PRO B N   
4315 C CA  . PRO B 227 ? 0.2390 0.1226 0.1566 -0.0294 -0.0182 -0.0236 450  PRO B CA  
4316 C C   . PRO B 227 ? 0.2302 0.1090 0.1436 -0.0502 -0.0185 -0.0205 450  PRO B C   
4317 O O   . PRO B 227 ? 0.2477 0.1246 0.1554 -0.0299 -0.0004 -0.0198 450  PRO B O   
4318 C CB  . PRO B 227 ? 0.2315 0.1295 0.1715 -0.0179 -0.0462 -0.0206 450  PRO B CB  
4319 C CG  . PRO B 227 ? 0.2221 0.1453 0.1794 -0.0132 -0.0181 -0.0018 450  PRO B CG  
4320 C CD  . PRO B 227 ? 0.2222 0.1688 0.1594 -0.0367 -0.0104 -0.0153 450  PRO B CD  
4321 N N   . TYR B 228 ? 0.2145 0.1206 0.1497 -0.0220 -0.0319 -0.0231 451  TYR B N   
4322 C CA  . TYR B 228 ? 0.1959 0.1330 0.1739 -0.0073 -0.0412 -0.0139 451  TYR B CA  
4323 C C   . TYR B 228 ? 0.1960 0.1369 0.1677 -0.0008 -0.0395 -0.0192 451  TYR B C   
4324 O O   . TYR B 228 ? 0.2130 0.1461 0.1637 0.0054  -0.0398 -0.0001 451  TYR B O   
4325 C CB  . TYR B 228 ? 0.1933 0.1364 0.1901 -0.0320 -0.0422 -0.0087 451  TYR B CB  
4326 C CG  . TYR B 228 ? 0.2015 0.1470 0.2150 -0.0334 -0.0365 0.0037  451  TYR B CG  
4327 C CD1 . TYR B 228 ? 0.2235 0.1384 0.2335 -0.0207 -0.0681 -0.0064 451  TYR B CD1 
4328 C CD2 . TYR B 228 ? 0.2276 0.1682 0.2323 -0.0719 -0.0220 -0.0039 451  TYR B CD2 
4329 C CE1 . TYR B 228 ? 0.2449 0.1715 0.2605 -0.0528 -0.0781 0.0135  451  TYR B CE1 
4330 C CE2 . TYR B 228 ? 0.2686 0.1759 0.2578 -0.0757 -0.0041 0.0275  451  TYR B CE2 
4331 C CZ  . TYR B 228 ? 0.2865 0.1790 0.2726 -0.0830 -0.0268 0.0331  451  TYR B CZ  
4332 O OH  . TYR B 228 ? 0.3598 0.1856 0.3187 -0.0929 -0.0131 0.0463  451  TYR B OH  
4333 N N   . ILE B 229 ? 0.1895 0.1178 0.1433 0.0157  -0.0372 -0.0362 452  ILE B N   
4334 C CA  . ILE B 229 ? 0.1857 0.1036 0.1660 0.0108  -0.0309 -0.0169 452  ILE B CA  
4335 C C   . ILE B 229 ? 0.1984 0.0949 0.1395 0.0145  -0.0599 -0.0084 452  ILE B C   
4336 O O   . ILE B 229 ? 0.1888 0.1181 0.1338 0.0018  -0.0264 -0.0084 452  ILE B O   
4337 C CB  . ILE B 229 ? 0.1385 0.1028 0.1635 0.0032  -0.0355 0.0082  452  ILE B CB  
4338 C CG1 . ILE B 229 ? 0.1273 0.1189 0.1556 -0.0032 -0.0395 -0.0044 452  ILE B CG1 
4339 C CG2 . ILE B 229 ? 0.1653 0.1143 0.1718 -0.0016 -0.0478 0.0125  452  ILE B CG2 
4340 C CD1 . ILE B 229 ? 0.1631 0.1433 0.1636 0.0007  -0.0251 -0.0002 452  ILE B CD1 
4341 N N   . ASP B 230 ? 0.1993 0.1015 0.1299 -0.0081 -0.0456 -0.0113 453  ASP B N   
4342 C CA  . ASP B 230 ? 0.1898 0.1115 0.1309 0.0036  -0.0559 -0.0055 453  ASP B CA  
4343 C C   . ASP B 230 ? 0.1701 0.1022 0.1421 0.0064  -0.0568 -0.0123 453  ASP B C   
4344 O O   . ASP B 230 ? 0.1733 0.1137 0.1554 -0.0030 -0.0532 0.0034  453  ASP B O   
4345 C CB  . ASP B 230 ? 0.1770 0.1271 0.1667 0.0063  -0.0570 0.0080  453  ASP B CB  
4346 C CG  . ASP B 230 ? 0.1937 0.1422 0.1634 0.0140  -0.0655 -0.0036 453  ASP B CG  
4347 O OD1 . ASP B 230 ? 0.2040 0.1806 0.1906 0.0236  -0.0682 0.0107  453  ASP B OD1 
4348 O OD2 . ASP B 230 ? 0.1989 0.1489 0.1678 -0.0115 -0.0512 -0.0029 453  ASP B OD2 
4349 N N   . CYS B 231 ? 0.1585 0.0918 0.1242 -0.0006 -0.0442 -0.0128 454  CYS B N   
4350 C CA  . CYS B 231 ? 0.1521 0.1029 0.1271 -0.0112 -0.0257 -0.0244 454  CYS B CA  
4351 C C   . CYS B 231 ? 0.1626 0.0885 0.1291 0.0126  -0.0688 -0.0099 454  CYS B C   
4352 O O   . CYS B 231 ? 0.1801 0.0872 0.1665 0.0129  -0.0682 -0.0151 454  CYS B O   
4353 C CB  . CYS B 231 ? 0.1800 0.0972 0.1471 -0.0019 -0.0515 0.0082  454  CYS B CB  
4354 S SG  . CYS B 231 ? 0.1708 0.0926 0.1613 -0.0041 -0.0527 0.0045  454  CYS B SG  
4355 N N   . LEU B 232 ? 0.1784 0.0837 0.1244 0.0066  -0.0386 -0.0116 455  LEU B N   
4356 C CA  . LEU B 232 ? 0.1708 0.0780 0.1350 0.0268  -0.0515 -0.0187 455  LEU B CA  
4357 C C   . LEU B 232 ? 0.1410 0.0802 0.1384 -0.0142 -0.0571 -0.0126 455  LEU B C   
4358 O O   . LEU B 232 ? 0.1641 0.0956 0.1629 -0.0122 -0.0617 -0.0081 455  LEU B O   
4359 C CB  . LEU B 232 ? 0.1520 0.0877 0.1406 0.0260  -0.0533 -0.0164 455  LEU B CB  
4360 C CG  . LEU B 232 ? 0.1810 0.0885 0.1399 0.0075  -0.0615 0.0138  455  LEU B CG  
4361 C CD1 . LEU B 232 ? 0.2100 0.0875 0.1952 0.0437  -0.0738 -0.0081 455  LEU B CD1 
4362 C CD2 . LEU B 232 ? 0.2198 0.1067 0.1614 -0.0051 -0.0177 0.0233  455  LEU B CD2 
4363 N N   . ILE B 233 ? 0.1679 0.0872 0.1331 0.0061  -0.0350 0.0165  456  ILE B N   
4364 C CA  . ILE B 233 ? 0.1676 0.0897 0.1413 0.0121  -0.0117 -0.0072 456  ILE B CA  
4365 C C   . ILE B 233 ? 0.1591 0.0914 0.1239 -0.0030 -0.0400 -0.0022 456  ILE B C   
4366 O O   . ILE B 233 ? 0.1944 0.1077 0.1528 0.0146  -0.0597 -0.0102 456  ILE B O   
4367 C CB  . ILE B 233 ? 0.1756 0.1077 0.1787 -0.0135 -0.0293 -0.0389 456  ILE B CB  
4368 C CG1 . ILE B 233 ? 0.1558 0.1408 0.2153 0.0052  -0.0069 -0.0519 456  ILE B CG1 
4369 C CG2 . ILE B 233 ? 0.2312 0.0864 0.1819 -0.0078 -0.0519 -0.0236 456  ILE B CG2 
4370 C CD1 . ILE B 233 ? 0.1909 0.1655 0.2561 0.0015  0.0193  -0.0637 456  ILE B CD1 
4371 N N   . PRO B 234 ? 0.1779 0.0959 0.1308 0.0088  -0.0550 0.0182  457  PRO B N   
4372 C CA  . PRO B 234 ? 0.1771 0.1019 0.1779 0.0035  -0.0356 0.0474  457  PRO B CA  
4373 C C   . PRO B 234 ? 0.1623 0.0912 0.1763 -0.0030 -0.0440 0.0346  457  PRO B C   
4374 O O   . PRO B 234 ? 0.1646 0.1090 0.1418 -0.0048 -0.0294 -0.0016 457  PRO B O   
4375 C CB  . PRO B 234 ? 0.1846 0.0948 0.2333 0.0132  -0.0587 0.0387  457  PRO B CB  
4376 C CG  . PRO B 234 ? 0.1942 0.1026 0.2098 0.0248  -0.0620 0.0368  457  PRO B CG  
4377 C CD  . PRO B 234 ? 0.1863 0.1052 0.1633 0.0187  -0.0797 0.0306  457  PRO B CD  
4378 N N   . GLN B 235 ? 0.1569 0.0955 0.1725 -0.0250 -0.0479 0.0132  458  GLN B N   
4379 C CA  . GLN B 235 ? 0.1713 0.0998 0.1542 -0.0065 -0.0744 -0.0108 458  GLN B CA  
4380 C C   . GLN B 235 ? 0.1525 0.1086 0.1642 0.0099  -0.0557 0.0088  458  GLN B C   
4381 O O   . GLN B 235 ? 0.1619 0.1241 0.1809 0.0079  -0.0136 0.0074  458  GLN B O   
4382 C CB  . GLN B 235 ? 0.1750 0.1018 0.1918 -0.0190 -0.0374 -0.0020 458  GLN B CB  
4383 C CG  . GLN B 235 ? 0.1634 0.1368 0.1983 -0.0088 -0.0523 0.0217  458  GLN B CG  
4384 C CD  . GLN B 235 ? 0.1621 0.1758 0.2081 -0.0009 -0.0354 0.0158  458  GLN B CD  
4385 O OE1 . GLN B 235 ? 0.1698 0.1600 0.1830 -0.0112 -0.0353 -0.0146 458  GLN B OE1 
4386 N NE2 . GLN B 235 ? 0.1816 0.2328 0.2471 0.0365  -0.0570 0.0659  458  GLN B NE2 
4387 N N   . GLU B 236 ? 0.1860 0.1085 0.1496 -0.0020 -0.0343 0.0100  459  GLU B N   
4388 C CA  . GLU B 236 ? 0.2103 0.1150 0.1563 0.0706  -0.0424 0.0071  459  GLU B CA  
4389 C C   . GLU B 236 ? 0.2392 0.1165 0.1729 0.0674  -0.0087 0.0107  459  GLU B C   
4390 O O   . GLU B 236 ? 0.2448 0.1445 0.1936 0.0384  -0.0070 -0.0039 459  GLU B O   
4391 C CB  . GLU B 236 ? 0.2367 0.1115 0.1621 0.0761  -0.0391 0.0046  459  GLU B CB  
4392 C CG  . GLU B 236 ? 0.2545 0.1126 0.1601 0.0774  -0.0208 0.0159  459  GLU B CG  
4393 C CD  . GLU B 236 ? 0.2467 0.1177 0.1915 0.0687  -0.0311 0.0083  459  GLU B CD  
4394 O OE1 . GLU B 236 ? 0.2191 0.1337 0.1851 0.0525  -0.0465 0.0015  459  GLU B OE1 
4395 O OE2 . GLU B 236 ? 0.2769 0.1254 0.2266 0.0462  -0.0197 -0.0243 459  GLU B OE2 
4396 N N   . TRP B 237 ? 0.2163 0.1083 0.1698 0.0325  -0.0446 0.0200  460  TRP B N   
4397 C CA  . TRP B 237 ? 0.2269 0.1181 0.1622 0.0452  -0.0238 0.0032  460  TRP B CA  
4398 C C   . TRP B 237 ? 0.2040 0.1330 0.1649 0.0272  -0.0399 -0.0106 460  TRP B C   
4399 O O   . TRP B 237 ? 0.2177 0.1426 0.1877 0.0099  -0.0088 -0.0136 460  TRP B O   
4400 C CB  . TRP B 237 ? 0.2084 0.1237 0.1594 0.0139  -0.0487 -0.0061 460  TRP B CB  
4401 C CG  . TRP B 237 ? 0.1873 0.1258 0.1486 0.0191  -0.0754 0.0028  460  TRP B CG  
4402 C CD1 . TRP B 237 ? 0.1981 0.1409 0.1317 0.0081  -0.0524 -0.0092 460  TRP B CD1 
4403 C CD2 . TRP B 237 ? 0.1928 0.1184 0.1489 -0.0011 -0.0654 -0.0122 460  TRP B CD2 
4404 N NE1 . TRP B 237 ? 0.1849 0.1086 0.1668 0.0085  -0.0417 -0.0026 460  TRP B NE1 
4405 C CE2 . TRP B 237 ? 0.1795 0.1110 0.1674 -0.0043 -0.0416 -0.0003 460  TRP B CE2 
4406 C CE3 . TRP B 237 ? 0.2076 0.1100 0.1437 0.0023  -0.0651 -0.0248 460  TRP B CE3 
4407 C CZ2 . TRP B 237 ? 0.1899 0.1168 0.2018 -0.0143 -0.0349 0.0058  460  TRP B CZ2 
4408 C CZ3 . TRP B 237 ? 0.2292 0.1247 0.1665 -0.0092 -0.0736 -0.0156 460  TRP B CZ3 
4409 C CH2 . TRP B 237 ? 0.2141 0.1291 0.1859 0.0002  -0.0690 0.0000  460  TRP B CH2 
4410 N N   . ILE B 238 ? 0.1824 0.1316 0.1677 0.0345  -0.0409 0.0069  461  ILE B N   
4411 C CA  . ILE B 238 ? 0.1864 0.1341 0.1656 0.0271  -0.0136 0.0063  461  ILE B CA  
4412 C C   . ILE B 238 ? 0.1941 0.1433 0.2004 -0.0018 0.0047  -0.0085 461  ILE B C   
4413 O O   . ILE B 238 ? 0.1938 0.1681 0.2149 -0.0047 0.0218  -0.0241 461  ILE B O   
4414 C CB  . ILE B 238 ? 0.1585 0.1297 0.1810 0.0207  -0.0328 0.0058  461  ILE B CB  
4415 C CG1 . ILE B 238 ? 0.1952 0.1467 0.1417 0.0212  -0.0227 0.0196  461  ILE B CG1 
4416 C CG2 . ILE B 238 ? 0.1766 0.1508 0.2267 0.0164  -0.0280 0.0266  461  ILE B CG2 
4417 C CD1 . ILE B 238 ? 0.1879 0.1685 0.1614 0.0211  -0.0258 -0.0065 461  ILE B CD1 
4418 N N   . SER B 239 ? 0.2335 0.1290 0.1901 0.0008  0.0165  0.0092  462  SER B N   
4419 C CA  A SER B 239 ? 0.2767 0.1412 0.2115 0.0130  0.0224  0.0159  462  SER B CA  
4420 C CA  B SER B 239 ? 0.2564 0.1447 0.2016 0.0138  0.0257  0.0210  462  SER B CA  
4421 C C   . SER B 239 ? 0.2564 0.1590 0.2108 0.0049  0.0277  0.0096  462  SER B C   
4422 O O   . SER B 239 ? 0.2362 0.1896 0.2291 0.0300  0.0191  0.0052  462  SER B O   
4423 C CB  A SER B 239 ? 0.3507 0.1310 0.2303 -0.0025 0.0035  -0.0097 462  SER B CB  
4424 C CB  B SER B 239 ? 0.2797 0.1439 0.2097 0.0202  0.0332  0.0329  462  SER B CB  
4425 O OG  A SER B 239 ? 0.4146 0.1532 0.2566 0.0018  0.0346  -0.0088 462  SER B OG  
4426 O OG  B SER B 239 ? 0.2884 0.1499 0.2164 0.0281  0.0459  0.0456  462  SER B OG  
4427 N N   . HIS B 240 ? 0.2629 0.1684 0.2227 0.0263  0.0045  0.0118  463  HIS B N   
4428 C CA  . HIS B 240 ? 0.2593 0.1789 0.2141 0.0393  -0.0429 0.0095  463  HIS B CA  
4429 C C   . HIS B 240 ? 0.2624 0.1867 0.2187 0.0229  -0.0397 -0.0104 463  HIS B C   
4430 O O   . HIS B 240 ? 0.2792 0.2041 0.2116 0.0105  -0.0054 -0.0305 463  HIS B O   
4431 C CB  . HIS B 240 ? 0.2737 0.1955 0.2194 0.0456  -0.0574 -0.0036 463  HIS B CB  
4432 C CG  . HIS B 240 ? 0.3357 0.2075 0.2208 0.0220  -0.0562 0.0160  463  HIS B CG  
4433 N ND1 . HIS B 240 ? 0.3896 0.2391 0.2413 -0.0070 -0.0496 -0.0051 463  HIS B ND1 
4434 C CD2 . HIS B 240 ? 0.3577 0.2150 0.2148 0.0192  -0.0619 0.0306  463  HIS B CD2 
4435 C CE1 . HIS B 240 ? 0.4317 0.2371 0.2402 0.0010  -0.0249 0.0170  463  HIS B CE1 
4436 N NE2 . HIS B 240 ? 0.4148 0.2234 0.2431 -0.0025 -0.0382 0.0286  463  HIS B NE2 
4437 N N   . PHE B 241 ? 0.2531 0.1622 0.1949 0.0428  -0.0354 0.0027  464  PHE B N   
4438 C CA  . PHE B 241 ? 0.2365 0.1561 0.1935 0.0235  -0.0216 -0.0095 464  PHE B CA  
4439 C C   . PHE B 241 ? 0.2326 0.1680 0.2114 0.0118  -0.0224 -0.0283 464  PHE B C   
4440 O O   . PHE B 241 ? 0.2678 0.1755 0.1867 0.0277  0.0005  -0.0226 464  PHE B O   
4441 C CB  . PHE B 241 ? 0.2312 0.1578 0.1861 0.0332  -0.0308 0.0140  464  PHE B CB  
4442 C CG  . PHE B 241 ? 0.2418 0.1417 0.1674 0.0090  -0.0637 -0.0158 464  PHE B CG  
4443 C CD1 . PHE B 241 ? 0.2739 0.1485 0.1968 -0.0018 -0.0310 -0.0200 464  PHE B CD1 
4444 C CD2 . PHE B 241 ? 0.2624 0.1263 0.1852 0.0039  -0.0399 -0.0092 464  PHE B CD2 
4445 C CE1 . PHE B 241 ? 0.2871 0.1611 0.1940 0.0300  -0.0444 -0.0028 464  PHE B CE1 
4446 C CE2 . PHE B 241 ? 0.2585 0.1252 0.1946 0.0155  -0.0717 -0.0333 464  PHE B CE2 
4447 C CZ  . PHE B 241 ? 0.2778 0.1404 0.1876 0.0330  -0.0543 -0.0089 464  PHE B CZ  
4448 N N   . TYR B 242 ? 0.2186 0.1766 0.2025 -0.0149 -0.0118 -0.0417 465  TYR B N   
4449 C CA  . TYR B 242 ? 0.2386 0.1921 0.2513 -0.0097 0.0024  -0.0488 465  TYR B CA  
4450 C C   . TYR B 242 ? 0.2842 0.2307 0.2590 -0.0100 0.0317  -0.0571 465  TYR B C   
4451 O O   . TYR B 242 ? 0.3107 0.2389 0.2859 -0.0096 0.0684  -0.0628 465  TYR B O   
4452 C CB  . TYR B 242 ? 0.2237 0.2039 0.2794 -0.0189 -0.0048 -0.0676 465  TYR B CB  
4453 C CG  . TYR B 242 ? 0.2432 0.2263 0.2984 -0.0175 0.0136  -0.0694 465  TYR B CG  
4454 C CD1 . TYR B 242 ? 0.1849 0.2484 0.3422 -0.0113 -0.0010 -0.0669 465  TYR B CD1 
4455 C CD2 . TYR B 242 ? 0.2589 0.2385 0.2832 -0.0127 0.0265  -0.0711 465  TYR B CD2 
4456 C CE1 . TYR B 242 ? 0.2178 0.2626 0.3686 -0.0030 -0.0027 -0.0574 465  TYR B CE1 
4457 C CE2 . TYR B 242 ? 0.2532 0.2599 0.3213 -0.0159 0.0064  -0.0798 465  TYR B CE2 
4458 C CZ  . TYR B 242 ? 0.2367 0.2704 0.3670 -0.0030 -0.0034 -0.0696 465  TYR B CZ  
4459 O OH  . TYR B 242 ? 0.2750 0.2910 0.4043 -0.0314 0.0051  -0.0908 465  TYR B OH  
4460 N N   A GLN B 243 ? 0.3050 0.2446 0.2444 -0.0028 0.0214  -0.0432 466  GLN B N   
4461 N N   B GLN B 243 ? 0.3060 0.2391 0.2485 0.0052  0.0403  -0.0549 466  GLN B N   
4462 C CA  A GLN B 243 ? 0.3338 0.2587 0.2530 -0.0184 0.0405  -0.0230 466  GLN B CA  
4463 C CA  B GLN B 243 ? 0.3348 0.2493 0.2530 0.0044  0.0663  -0.0503 466  GLN B CA  
4464 C C   A GLN B 243 ? 0.3719 0.2680 0.2474 -0.0070 0.0753  -0.0256 466  GLN B C   
4465 C C   B GLN B 243 ? 0.3646 0.2634 0.2338 0.0036  0.0763  -0.0394 466  GLN B C   
4466 O O   A GLN B 243 ? 0.3853 0.2699 0.2760 -0.0100 0.0979  -0.0254 466  GLN B O   
4467 O O   B GLN B 243 ? 0.3724 0.2681 0.2378 0.0000  0.0903  -0.0399 466  GLN B O   
4468 C CB  A GLN B 243 ? 0.3544 0.2627 0.2550 -0.0382 0.0332  -0.0024 466  GLN B CB  
4469 C CB  B GLN B 243 ? 0.3572 0.2484 0.2610 0.0052  0.0826  -0.0608 466  GLN B CB  
4470 C CG  A GLN B 243 ? 0.3773 0.2736 0.2811 -0.0492 0.0534  0.0088  466  GLN B CG  
4471 C CG  B GLN B 243 ? 0.3808 0.2524 0.2750 0.0089  0.1023  -0.0760 466  GLN B CG  
4472 C CD  A GLN B 243 ? 0.4077 0.2827 0.2447 -0.0378 0.0423  0.0064  466  GLN B CD  
4473 C CD  B GLN B 243 ? 0.3938 0.2528 0.2815 0.0195  0.1040  -0.0839 466  GLN B CD  
4474 O OE1 A GLN B 243 ? 0.4724 0.2935 0.2455 -0.0371 0.0394  -0.0008 466  GLN B OE1 
4475 O OE1 B GLN B 243 ? 0.3946 0.2465 0.2903 0.0327  0.1276  -0.1002 466  GLN B OE1 
4476 N NE2 A GLN B 243 ? 0.3383 0.2716 0.1704 -0.0241 -0.0493 0.0087  466  GLN B NE2 
4477 N NE2 B GLN B 243 ? 0.4183 0.2649 0.2725 0.0092  0.0922  -0.0578 466  GLN B NE2 
4478 N N   . GLU B 244 ? 0.3761 0.2684 0.1938 0.0080  0.0442  -0.0262 467  GLU B N   
4479 C CA  . GLU B 244 ? 0.4133 0.2971 0.1941 0.0302  0.0109  -0.0224 467  GLU B CA  
4480 C C   . GLU B 244 ? 0.3795 0.2855 0.2216 0.0300  0.0242  -0.0357 467  GLU B C   
4481 O O   . GLU B 244 ? 0.3995 0.2786 0.2330 0.0319  0.0301  -0.0631 467  GLU B O   
4482 C CB  . GLU B 244 ? 0.5022 0.3322 0.2305 0.0321  -0.0077 -0.0121 467  GLU B CB  
4483 C CG  . GLU B 244 ? 0.6076 0.3621 0.2604 0.0642  0.0030  0.0083  467  GLU B CG  
4484 C CD  . GLU B 244 ? 0.7248 0.4016 0.3028 0.0803  0.0364  0.0213  467  GLU B CD  
4485 O OE1 . GLU B 244 ? 0.7816 0.4304 0.3183 0.1007  0.0745  0.0099  467  GLU B OE1 
4486 O OE2 . GLU B 244 ? 0.7550 0.4089 0.3046 0.0623  0.0341  0.0639  467  GLU B OE2 
4487 N N   . SER B 245 ? 0.3045 0.2873 0.2298 0.0130  -0.0136 -0.0269 468  SER B N   
4488 C CA  . SER B 245 ? 0.2913 0.2914 0.2842 0.0277  -0.0132 -0.0432 468  SER B CA  
4489 C C   . SER B 245 ? 0.2810 0.2841 0.2499 0.0287  -0.0275 -0.0405 468  SER B C   
4490 O O   . SER B 245 ? 0.3039 0.2728 0.2761 0.0204  0.0223  -0.0493 468  SER B O   
4491 C CB  . SER B 245 ? 0.3287 0.3214 0.3522 0.0183  -0.0348 -0.0567 468  SER B CB  
4492 O OG  . SER B 245 ? 0.3922 0.3432 0.4012 0.0189  -0.0109 -0.0541 468  SER B OG  
4493 N N   . ALA B 246 ? 0.3114 0.2742 0.2363 0.0124  -0.0353 -0.0377 469  ALA B N   
4494 C CA  . ALA B 246 ? 0.3026 0.2677 0.2305 0.0338  -0.0425 -0.0547 469  ALA B CA  
4495 C C   . ALA B 246 ? 0.3123 0.2451 0.2446 0.0350  -0.0328 -0.0639 469  ALA B C   
4496 O O   . ALA B 246 ? 0.3169 0.2263 0.2168 0.0350  -0.0281 -0.0438 469  ALA B O   
4497 C CB  . ALA B 246 ? 0.3023 0.2826 0.2109 0.0340  -0.0717 -0.0637 469  ALA B CB  
4498 N N   . PRO B 247 ? 0.3245 0.2296 0.2651 0.0435  -0.0148 -0.0759 470  PRO B N   
4499 C CA  . PRO B 247 ? 0.3217 0.2323 0.2691 0.0445  -0.0422 -0.0806 470  PRO B CA  
4500 C C   . PRO B 247 ? 0.3048 0.2265 0.2543 0.0658  -0.0582 -0.0692 470  PRO B C   
4501 O O   . PRO B 247 ? 0.3170 0.2534 0.2845 0.0458  -0.0481 -0.0626 470  PRO B O   
4502 C CB  . PRO B 247 ? 0.3630 0.2440 0.3212 0.0541  0.0098  -0.0618 470  PRO B CB  
4503 C CG  . PRO B 247 ? 0.3918 0.2643 0.3445 0.0517  0.0249  -0.0683 470  PRO B CG  
4504 C CD  . PRO B 247 ? 0.3574 0.2379 0.3104 0.0553  -0.0003 -0.0966 470  PRO B CD  
4505 N N   . SER B 248 ? 0.2974 0.2142 0.2487 0.0689  -0.0580 -0.0745 471  SER B N   
4506 C CA  . SER B 248 ? 0.3053 0.2313 0.2420 0.0774  -0.0784 -0.0856 471  SER B CA  
4507 C C   . SER B 248 ? 0.3094 0.2460 0.2482 0.0859  -0.0826 -0.0985 471  SER B C   
4508 O O   . SER B 248 ? 0.3073 0.2486 0.3022 0.0643  -0.0578 -0.0974 471  SER B O   
4509 C CB  . SER B 248 ? 0.3424 0.2128 0.2277 0.0604  -0.0787 -0.0764 471  SER B CB  
4510 O OG  . SER B 248 ? 0.3684 0.2059 0.2631 0.0515  -0.0508 -0.0893 471  SER B OG  
4511 N N   . GLN B 249 ? 0.3181 0.2473 0.2371 0.0921  -0.0938 -0.1069 472  GLN B N   
4512 C CA  . GLN B 249 ? 0.3456 0.2539 0.2620 0.0847  -0.0815 -0.1309 472  GLN B CA  
4513 C C   . GLN B 249 ? 0.3274 0.2319 0.2726 0.1093  -0.0892 -0.1129 472  GLN B C   
4514 O O   . GLN B 249 ? 0.3195 0.2484 0.3079 0.1146  -0.0578 -0.1319 472  GLN B O   
4515 C CB  . GLN B 249 ? 0.3687 0.2699 0.2913 0.0677  -0.0976 -0.1291 472  GLN B CB  
4516 C CG  . GLN B 249 ? 0.3986 0.2903 0.3243 0.0562  -0.0754 -0.1211 472  GLN B CG  
4517 C CD  . GLN B 249 ? 0.4350 0.3056 0.3506 0.0356  -0.0603 -0.1356 472  GLN B CD  
4518 O OE1 . GLN B 249 ? 0.4363 0.3110 0.3473 0.0396  -0.0494 -0.1639 472  GLN B OE1 
4519 N NE2 . GLN B 249 ? 0.4261 0.3174 0.3771 -0.0019 -0.0783 -0.1319 472  GLN B NE2 
4520 N N   . THR B 250 ? 0.3104 0.2133 0.2483 0.0951  -0.0796 -0.0943 473  THR B N   
4521 C CA  . THR B 250 ? 0.2869 0.2094 0.2481 0.0795  -0.1145 -0.0783 473  THR B CA  
4522 C C   . THR B 250 ? 0.2918 0.2030 0.2362 0.0812  -0.1130 -0.0818 473  THR B C   
4523 O O   . THR B 250 ? 0.3083 0.2038 0.2645 0.0487  -0.0806 -0.0946 473  THR B O   
4524 C CB  . THR B 250 ? 0.2923 0.1929 0.2610 0.0699  -0.1016 -0.1021 473  THR B CB  
4525 O OG1 . THR B 250 ? 0.3086 0.1850 0.2790 0.0841  -0.0957 -0.1054 473  THR B OG1 
4526 C CG2 . THR B 250 ? 0.3326 0.2002 0.2701 0.0835  -0.0764 -0.1055 473  THR B CG2 
4527 N N   . ASP B 251 ? 0.3169 0.2039 0.2357 0.0867  -0.0967 -0.0769 474  ASP B N   
4528 C CA  . ASP B 251 ? 0.3561 0.2039 0.2304 0.1257  -0.0952 -0.0570 474  ASP B CA  
4529 C C   . ASP B 251 ? 0.2680 0.1732 0.2289 0.0807  -0.1131 -0.0681 474  ASP B C   
4530 O O   . ASP B 251 ? 0.2389 0.1745 0.2256 0.0421  -0.0958 -0.0697 474  ASP B O   
4531 C CB  . ASP B 251 ? 0.4354 0.2641 0.2893 0.1601  -0.1229 -0.0345 474  ASP B CB  
4532 C CG  . ASP B 251 ? 0.5026 0.3154 0.3718 0.1765  -0.1147 -0.0184 474  ASP B CG  
4533 O OD1 . ASP B 251 ? 0.4748 0.3452 0.3917 0.1856  -0.1418 -0.0391 474  ASP B OD1 
4534 O OD2 . ASP B 251 ? 0.5688 0.3368 0.4190 0.1694  -0.0727 0.0064  474  ASP B OD2 
4535 N N   . VAL B 252 ? 0.2396 0.1673 0.2452 0.0594  -0.1181 -0.0631 475  VAL B N   
4536 C CA  . VAL B 252 ? 0.2297 0.1634 0.2341 0.0555  -0.1178 -0.0852 475  VAL B CA  
4537 C C   . VAL B 252 ? 0.2346 0.1646 0.2054 0.0596  -0.1037 -0.0844 475  VAL B C   
4538 O O   . VAL B 252 ? 0.2713 0.1753 0.2202 0.0591  -0.1057 -0.0910 475  VAL B O   
4539 C CB  . VAL B 252 ? 0.2816 0.2149 0.2653 0.0263  -0.0831 -0.0484 475  VAL B CB  
4540 C CG1 . VAL B 252 ? 0.3118 0.2167 0.3024 0.0145  -0.0454 -0.0712 475  VAL B CG1 
4541 C CG2 . VAL B 252 ? 0.3308 0.2456 0.2510 0.0066  -0.0726 -0.0456 475  VAL B CG2 
4542 N N   . ALA B 253 ? 0.2338 0.1502 0.2199 0.0646  -0.1112 -0.0808 476  ALA B N   
4543 C CA  . ALA B 253 ? 0.2279 0.1698 0.2158 0.0493  -0.1207 -0.0703 476  ALA B CA  
4544 C C   . ALA B 253 ? 0.2095 0.1767 0.1884 0.0529  -0.1083 -0.0660 476  ALA B C   
4545 O O   . ALA B 253 ? 0.2448 0.2285 0.1800 0.0397  -0.1044 -0.0742 476  ALA B O   
4546 C CB  . ALA B 253 ? 0.2575 0.1886 0.2434 0.0495  -0.0925 -0.0544 476  ALA B CB  
4547 N N   . LEU B 254 ? 0.1936 0.1748 0.2043 0.0433  -0.1025 -0.0515 477  LEU B N   
4548 C CA  . LEU B 254 ? 0.2164 0.1684 0.1905 0.0340  -0.1061 -0.0408 477  LEU B CA  
4549 C C   . LEU B 254 ? 0.2243 0.1565 0.1648 0.0428  -0.0897 -0.0434 477  LEU B C   
4550 O O   . LEU B 254 ? 0.2540 0.1680 0.1887 0.0500  -0.0759 -0.0597 477  LEU B O   
4551 C CB  . LEU B 254 ? 0.2564 0.1811 0.2012 0.0028  -0.1217 -0.0377 477  LEU B CB  
4552 C CG  . LEU B 254 ? 0.2818 0.1736 0.2069 -0.0128 -0.1065 -0.0478 477  LEU B CG  
4553 C CD1 . LEU B 254 ? 0.3142 0.1492 0.1835 -0.0130 -0.1022 -0.0424 477  LEU B CD1 
4554 C CD2 . LEU B 254 ? 0.2764 0.1771 0.2182 0.0152  -0.1110 -0.0718 477  LEU B CD2 
4555 N N   . ILE B 255 ? 0.2282 0.1446 0.1761 0.0553  -0.0876 -0.0446 478  ILE B N   
4556 C CA  . ILE B 255 ? 0.2070 0.1409 0.1819 0.0490  -0.0841 -0.0339 478  ILE B CA  
4557 C C   . ILE B 255 ? 0.1843 0.1383 0.1657 0.0330  -0.0810 -0.0238 478  ILE B C   
4558 O O   . ILE B 255 ? 0.2119 0.1739 0.1884 0.0345  -0.0670 -0.0044 478  ILE B O   
4559 C CB  . ILE B 255 ? 0.2231 0.1676 0.1718 0.0094  -0.0935 -0.0467 478  ILE B CB  
4560 C CG1 . ILE B 255 ? 0.2359 0.1564 0.1775 0.0092  -0.1016 -0.0539 478  ILE B CG1 
4561 C CG2 . ILE B 255 ? 0.2449 0.2009 0.1880 0.0005  -0.0839 -0.0328 478  ILE B CG2 
4562 C CD1 . ILE B 255 ? 0.2268 0.1560 0.2123 0.0150  -0.0920 -0.0467 478  ILE B CD1 
4563 N N   . ARG B 256 ? 0.1744 0.1464 0.1864 0.0268  -0.0946 -0.0357 479  ARG B N   
4564 C CA  . ARG B 256 ? 0.2096 0.1311 0.1891 0.0303  -0.0991 -0.0323 479  ARG B CA  
4565 C C   . ARG B 256 ? 0.2153 0.1273 0.1683 0.0206  -0.0924 -0.0267 479  ARG B C   
4566 O O   . ARG B 256 ? 0.2159 0.1373 0.1750 0.0190  -0.0499 -0.0078 479  ARG B O   
4567 C CB  . ARG B 256 ? 0.2449 0.1346 0.1935 0.0393  -0.1140 -0.0490 479  ARG B CB  
4568 C CG  . ARG B 256 ? 0.2821 0.1431 0.2173 0.0555  -0.1185 -0.0408 479  ARG B CG  
4569 C CD  . ARG B 256 ? 0.3074 0.1503 0.2401 0.0121  -0.1134 -0.0626 479  ARG B CD  
4570 N NE  . ARG B 256 ? 0.3202 0.1790 0.2221 0.0087  -0.1174 -0.0707 479  ARG B NE  
4571 C CZ  . ARG B 256 ? 0.3571 0.1783 0.2461 0.0216  -0.1299 -0.0568 479  ARG B CZ  
4572 N NH1 . ARG B 256 ? 0.4003 0.2087 0.2132 0.0493  -0.1127 -0.0431 479  ARG B NH1 
4573 N NH2 . ARG B 256 ? 0.3436 0.1623 0.2778 0.0025  -0.1204 -0.0729 479  ARG B NH2 
4574 N N   . TYR B 257 ? 0.2162 0.1355 0.1815 0.0045  -0.0730 -0.0445 480  TYR B N   
4575 C CA  . TYR B 257 ? 0.2097 0.1293 0.1918 0.0273  -0.0870 -0.0391 480  TYR B CA  
4576 C C   . TYR B 257 ? 0.2023 0.1515 0.1898 0.0174  -0.1073 -0.0377 480  TYR B C   
4577 O O   . TYR B 257 ? 0.2200 0.1860 0.2309 0.0119  -0.0899 -0.0363 480  TYR B O   
4578 C CB  . TYR B 257 ? 0.2336 0.1350 0.1852 0.0402  -0.0757 -0.0260 480  TYR B CB  
4579 C CG  . TYR B 257 ? 0.2521 0.1306 0.1928 0.0497  -0.0633 -0.0277 480  TYR B CG  
4580 C CD1 . TYR B 257 ? 0.2567 0.1304 0.1900 0.0274  -0.0502 -0.0543 480  TYR B CD1 
4581 C CD2 . TYR B 257 ? 0.3162 0.1587 0.2569 0.0437  -0.0513 -0.0588 480  TYR B CD2 
4582 C CE1 . TYR B 257 ? 0.2727 0.1333 0.2136 0.0511  -0.0204 -0.0559 480  TYR B CE1 
4583 C CE2 . TYR B 257 ? 0.3003 0.1677 0.2678 0.0538  -0.0822 -0.0839 480  TYR B CE2 
4584 C CZ  . TYR B 257 ? 0.2875 0.1547 0.2265 0.0602  -0.0991 -0.0803 480  TYR B CZ  
4585 O OH  . TYR B 257 ? 0.3449 0.1676 0.2800 0.0563  -0.1075 -0.0853 480  TYR B OH  
4586 N N   . VAL B 258 ? 0.2245 0.1717 0.1843 0.0550  -0.1107 -0.0315 481  VAL B N   
4587 C CA  A VAL B 258 ? 0.2453 0.1831 0.1920 0.0465  -0.1161 -0.0299 481  VAL B CA  
4588 C CA  B VAL B 258 ? 0.2389 0.1815 0.2014 0.0416  -0.1216 -0.0360 481  VAL B CA  
4589 C C   . VAL B 258 ? 0.2585 0.1779 0.2154 0.0309  -0.1075 -0.0416 481  VAL B C   
4590 O O   . VAL B 258 ? 0.2728 0.1766 0.2845 0.0426  -0.1068 0.0007  481  VAL B O   
4591 C CB  A VAL B 258 ? 0.2771 0.1956 0.2138 0.0260  -0.0780 -0.0055 481  VAL B CB  
4592 C CB  B VAL B 258 ? 0.2531 0.1927 0.2154 0.0223  -0.1254 -0.0343 481  VAL B CB  
4593 C CG1 A VAL B 258 ? 0.2533 0.2038 0.1965 0.0279  -0.1228 -0.0055 481  VAL B CG1 
4594 C CG1 B VAL B 258 ? 0.2595 0.1789 0.2317 0.0268  -0.1098 -0.0614 481  VAL B CG1 
4595 C CG2 A VAL B 258 ? 0.2996 0.1919 0.2456 0.0396  -0.0411 -0.0248 481  VAL B CG2 
4596 C CG2 B VAL B 258 ? 0.2569 0.2116 0.2049 0.0120  -0.1337 -0.0283 481  VAL B CG2 
4597 N N   . ASN B 259 ? 0.2617 0.1919 0.2367 0.0776  -0.1117 -0.0391 482  ASN B N   
4598 C CA  . ASN B 259 ? 0.2657 0.2229 0.2809 0.0768  -0.1373 -0.0297 482  ASN B CA  
4599 C C   . ASN B 259 ? 0.2745 0.2296 0.2914 0.0651  -0.1544 -0.0080 482  ASN B C   
4600 O O   . ASN B 259 ? 0.2900 0.2364 0.3072 0.0414  -0.1468 -0.0169 482  ASN B O   
4601 C CB  . ASN B 259 ? 0.2506 0.2242 0.3295 0.1050  -0.1104 -0.0324 482  ASN B CB  
4602 C CG  . ASN B 259 ? 0.2717 0.2269 0.3682 0.0965  -0.1026 -0.0337 482  ASN B CG  
4603 O OD1 . ASN B 259 ? 0.2662 0.2202 0.3831 0.0914  -0.1328 -0.0272 482  ASN B OD1 
4604 N ND2 . ASN B 259 ? 0.2839 0.2442 0.3925 0.0841  -0.0781 -0.0692 482  ASN B ND2 
4605 N N   . PRO B 260 ? 0.3065 0.2208 0.3071 0.0577  -0.1381 -0.0129 483  PRO B N   
4606 C CA  . PRO B 260 ? 0.3387 0.2560 0.3420 0.0632  -0.1404 -0.0003 483  PRO B CA  
4607 C C   . PRO B 260 ? 0.3780 0.2998 0.3505 0.0603  -0.1683 0.0136  483  PRO B C   
4608 O O   . PRO B 260 ? 0.4012 0.3151 0.3336 0.0452  -0.1342 0.0114  483  PRO B O   
4609 C CB  . PRO B 260 ? 0.3305 0.2328 0.3534 0.0674  -0.1130 -0.0089 483  PRO B CB  
4610 C CG  . PRO B 260 ? 0.3334 0.2245 0.3311 0.0556  -0.1082 -0.0080 483  PRO B CG  
4611 C CD  . PRO B 260 ? 0.3194 0.2105 0.3314 0.0526  -0.1111 0.0021  483  PRO B CD  
4612 N N   . ASP B 261 ? 0.3951 0.3167 0.3694 0.0764  -0.2054 0.0146  484  ASP B N   
4613 C CA  . ASP B 261 ? 0.4125 0.3469 0.4043 0.0841  -0.2162 0.0298  484  ASP B CA  
4614 C C   . ASP B 261 ? 0.4146 0.3707 0.4002 0.0921  -0.2112 0.0383  484  ASP B C   
4615 O O   . ASP B 261 ? 0.4636 0.3885 0.3900 0.0913  -0.2243 0.0353  484  ASP B O   
4616 C CB  . ASP B 261 ? 0.4472 0.3493 0.4966 0.0956  -0.2340 0.0296  484  ASP B CB  
4617 C CG  . ASP B 261 ? 0.4593 0.3547 0.5664 0.0983  -0.2266 0.0197  484  ASP B CG  
4618 O OD1 . ASP B 261 ? 0.4652 0.3583 0.6005 0.1132  -0.2068 0.0368  484  ASP B OD1 
4619 O OD2 . ASP B 261 ? 0.4640 0.3633 0.5831 0.0881  -0.2224 -0.0087 484  ASP B OD2 
4620 N N   . THR B 262 ? 0.3837 0.3794 0.4235 0.0809  -0.1875 0.0286  485  THR B N   
4621 C CA  . THR B 262 ? 0.3457 0.3927 0.4187 0.0729  -0.1635 0.0024  485  THR B CA  
4622 C C   . THR B 262 ? 0.3225 0.4165 0.4097 0.0457  -0.1375 -0.0400 485  THR B C   
4623 O O   . THR B 262 ? 0.3107 0.4411 0.4295 0.0296  -0.1341 -0.0395 485  THR B O   
4624 C CB  . THR B 262 ? 0.3230 0.3866 0.4350 0.0869  -0.1428 0.0223  485  THR B CB  
4625 O OG1 . THR B 262 ? 0.2991 0.3758 0.4005 0.0988  -0.1472 0.0280  485  THR B OG1 
4626 C CG2 . THR B 262 ? 0.3356 0.3887 0.4782 0.0806  -0.1096 0.0182  485  THR B CG2 
4627 N N   . GLY B 263 ? 0.3046 0.4116 0.3757 0.0681  -0.1695 -0.0363 486  GLY B N   
4628 C CA  . GLY B 263 ? 0.3203 0.4128 0.3855 0.0585  -0.1467 -0.0668 486  GLY B CA  
4629 C C   . GLY B 263 ? 0.3146 0.3994 0.3970 0.0533  -0.1768 -0.0939 486  GLY B C   
4630 O O   . GLY B 263 ? 0.3257 0.4054 0.4288 0.0442  -0.1477 -0.1187 486  GLY B O   
4631 N N   . ARG B 264 ? 0.2962 0.3896 0.3796 0.0500  -0.1895 -0.0735 487  ARG B N   
4632 C CA  . ARG B 264 ? 0.3439 0.3940 0.4091 0.0556  -0.1781 -0.0886 487  ARG B CA  
4633 C C   . ARG B 264 ? 0.2672 0.3077 0.3551 0.0553  -0.1683 -0.0998 487  ARG B C   
4634 O O   . ARG B 264 ? 0.2556 0.2741 0.3519 0.0557  -0.1481 -0.1145 487  ARG B O   
4642 N N   . VAL B 265 ? 0.2490 0.2819 0.3689 0.0593  -0.1353 -0.0964 488  VAL B N   
4643 C CA  . VAL B 265 ? 0.2336 0.2453 0.3389 0.0584  -0.1265 -0.0863 488  VAL B CA  
4644 C C   . VAL B 265 ? 0.2349 0.2276 0.3615 0.0242  -0.1030 -0.0534 488  VAL B C   
4645 O O   . VAL B 265 ? 0.2674 0.2453 0.4016 0.0133  -0.0369 -0.0664 488  VAL B O   
4646 C CB  . VAL B 265 ? 0.2945 0.2516 0.3377 0.0699  -0.0968 -0.0647 488  VAL B CB  
4647 C CG1 . VAL B 265 ? 0.2815 0.2421 0.3251 0.0731  -0.0925 -0.0539 488  VAL B CG1 
4648 C CG2 . VAL B 265 ? 0.3223 0.2668 0.2994 0.0657  -0.1408 -0.0518 488  VAL B CG2 
4649 N N   . LEU B 266 ? 0.2334 0.1908 0.3241 0.0405  -0.1003 -0.0138 489  LEU B N   
4650 C CA  . LEU B 266 ? 0.2366 0.1890 0.3246 0.0252  -0.0670 -0.0200 489  LEU B CA  
4651 C C   . LEU B 266 ? 0.2363 0.1969 0.3082 0.0189  -0.0702 0.0034  489  LEU B C   
4652 O O   . LEU B 266 ? 0.2556 0.2361 0.3493 0.0080  -0.0290 0.0185  489  LEU B O   
4653 C CB  . LEU B 266 ? 0.2636 0.2057 0.3324 0.0337  -0.0602 -0.0470 489  LEU B CB  
4654 C CG  . LEU B 266 ? 0.2961 0.2474 0.3527 0.0562  -0.0624 -0.0287 489  LEU B CG  
4655 C CD1 . LEU B 266 ? 0.3056 0.2572 0.3928 0.0668  -0.0624 -0.0234 489  LEU B CD1 
4656 C CD2 . LEU B 266 ? 0.2946 0.2633 0.2975 0.0770  -0.0798 -0.0093 489  LEU B CD2 
4657 N N   . PHE B 267 ? 0.2217 0.1799 0.2627 0.0194  -0.0861 -0.0111 490  PHE B N   
4658 C CA  . PHE B 267 ? 0.2289 0.1718 0.2316 -0.0087 -0.0820 -0.0190 490  PHE B CA  
4659 C C   . PHE B 267 ? 0.2171 0.1555 0.2198 -0.0023 -0.0766 -0.0183 490  PHE B C   
4660 O O   . PHE B 267 ? 0.2483 0.1444 0.2144 0.0021  -0.0529 -0.0147 490  PHE B O   
4661 C CB  . PHE B 267 ? 0.2086 0.1737 0.2065 -0.0157 -0.0799 -0.0293 490  PHE B CB  
4662 C CG  . PHE B 267 ? 0.2035 0.1464 0.1929 -0.0169 -0.0609 0.0004  490  PHE B CG  
4663 C CD1 . PHE B 267 ? 0.2231 0.1473 0.1824 -0.0132 -0.0514 -0.0121 490  PHE B CD1 
4664 C CD2 . PHE B 267 ? 0.2147 0.1509 0.1886 -0.0251 -0.0856 -0.0141 490  PHE B CD2 
4665 C CE1 . PHE B 267 ? 0.2519 0.1511 0.1735 0.0060  -0.0422 0.0061  490  PHE B CE1 
4666 C CE2 . PHE B 267 ? 0.2361 0.1390 0.1780 -0.0234 -0.0553 -0.0167 490  PHE B CE2 
4667 C CZ  . PHE B 267 ? 0.2232 0.1386 0.1713 0.0021  -0.0758 -0.0025 490  PHE B CZ  
4668 N N   . GLU B 268 ? 0.2069 0.1491 0.2093 0.0083  -0.1129 -0.0033 491  GLU B N   
4669 C CA  . GLU B 268 ? 0.2163 0.1468 0.1792 0.0120  -0.1023 -0.0141 491  GLU B CA  
4670 C C   . GLU B 268 ? 0.2245 0.1416 0.1660 -0.0041 -0.0764 -0.0160 491  GLU B C   
4671 O O   . GLU B 268 ? 0.2031 0.1388 0.1883 -0.0024 -0.0795 -0.0162 491  GLU B O   
4672 C CB  . GLU B 268 ? 0.2458 0.1478 0.1814 0.0044  -0.0824 -0.0168 491  GLU B CB  
4673 C CG  . GLU B 268 ? 0.2859 0.1669 0.1907 -0.0077 -0.0924 -0.0180 491  GLU B CG  
4674 C CD  . GLU B 268 ? 0.3099 0.1758 0.1959 -0.0413 -0.1119 -0.0143 491  GLU B CD  
4675 O OE1 . GLU B 268 ? 0.3496 0.1963 0.2140 -0.0375 -0.1268 -0.0322 491  GLU B OE1 
4676 O OE2 . GLU B 268 ? 0.3225 0.1919 0.2240 -0.0629 -0.0834 -0.0066 491  GLU B OE2 
4677 N N   . ALA B 269 ? 0.2039 0.1269 0.1704 0.0007  -0.0978 -0.0204 492  ALA B N   
4678 C CA  . ALA B 269 ? 0.1981 0.1246 0.1817 -0.0028 -0.0883 -0.0492 492  ALA B CA  
4679 C C   . ALA B 269 ? 0.2023 0.1024 0.1566 0.0227  -0.0805 -0.0162 492  ALA B C   
4680 O O   . ALA B 269 ? 0.2220 0.1268 0.1512 0.0169  -0.0542 -0.0223 492  ALA B O   
4681 C CB  . ALA B 269 ? 0.2275 0.1184 0.2095 -0.0072 -0.0974 -0.0452 492  ALA B CB  
4682 N N   . LYS B 270 ? 0.1951 0.1013 0.1958 0.0173  -0.0805 -0.0354 493  LYS B N   
4683 C CA  . LYS B 270 ? 0.2059 0.1090 0.1873 0.0117  -0.0771 -0.0248 493  LYS B CA  
4684 C C   . LYS B 270 ? 0.2171 0.1022 0.1764 0.0172  -0.0701 -0.0345 493  LYS B C   
4685 O O   . LYS B 270 ? 0.2444 0.1187 0.1443 -0.0049 -0.0521 -0.0228 493  LYS B O   
4686 C CB  . LYS B 270 ? 0.2850 0.1177 0.1886 0.0158  -0.0837 -0.0207 493  LYS B CB  
4687 C CG  . LYS B 270 ? 0.3468 0.1235 0.2426 -0.0274 -0.0265 -0.0333 493  LYS B CG  
4688 C CD  . LYS B 270 ? 0.4195 0.1661 0.3032 -0.0219 0.0277  -0.0048 493  LYS B CD  
4689 C CE  . LYS B 270 ? 0.3814 0.1633 0.2994 0.0105  -0.0095 0.0330  493  LYS B CE  
4690 N NZ  . LYS B 270 ? 0.3057 0.1465 0.2879 -0.0276 -0.0816 0.0099  493  LYS B NZ  
4691 N N   . LEU B 271 ? 0.2067 0.1076 0.1803 0.0193  -0.0712 -0.0344 494  LEU B N   
4692 C CA  . LEU B 271 ? 0.2053 0.1241 0.1945 0.0186  -0.0656 -0.0110 494  LEU B CA  
4693 C C   . LEU B 271 ? 0.1976 0.1185 0.1727 0.0236  -0.0790 -0.0196 494  LEU B C   
4694 O O   . LEU B 271 ? 0.2435 0.1329 0.1617 0.0145  -0.0825 -0.0250 494  LEU B O   
4695 C CB  . LEU B 271 ? 0.1911 0.1223 0.1789 0.0147  -0.0729 -0.0232 494  LEU B CB  
4696 C CG  . LEU B 271 ? 0.1840 0.1267 0.1537 0.0068  -0.0458 -0.0250 494  LEU B CG  
4697 C CD1 . LEU B 271 ? 0.1884 0.1519 0.1655 0.0257  -0.0423 -0.0206 494  LEU B CD1 
4698 C CD2 . LEU B 271 ? 0.2259 0.1264 0.1357 0.0159  -0.0533 0.0122  494  LEU B CD2 
4699 N N   . HIS B 272 ? 0.1904 0.1178 0.1740 0.0410  -0.0880 -0.0190 495  HIS B N   
4700 C CA  . HIS B 272 ? 0.2059 0.1247 0.1843 0.0382  -0.0751 -0.0272 495  HIS B CA  
4701 C C   . HIS B 272 ? 0.2013 0.1285 0.2001 0.0443  -0.0656 -0.0393 495  HIS B C   
4702 O O   . HIS B 272 ? 0.2309 0.1168 0.2016 0.0442  -0.0840 -0.0349 495  HIS B O   
4703 C CB  . HIS B 272 ? 0.2214 0.0980 0.2000 0.0126  -0.0790 -0.0392 495  HIS B CB  
4704 C CG  . HIS B 272 ? 0.2153 0.1031 0.2132 -0.0037 -0.0636 -0.0228 495  HIS B CG  
4705 N ND1 . HIS B 272 ? 0.2491 0.1189 0.2357 0.0028  -0.0704 0.0007  495  HIS B ND1 
4706 C CD2 . HIS B 272 ? 0.2280 0.1257 0.2043 -0.0040 -0.0673 -0.0270 495  HIS B CD2 
4707 C CE1 . HIS B 272 ? 0.2577 0.1388 0.2534 -0.0009 -0.0626 -0.0105 495  HIS B CE1 
4708 N NE2 . HIS B 272 ? 0.2490 0.1347 0.2107 -0.0064 -0.0899 -0.0251 495  HIS B NE2 
4709 N N   . ARG B 273 ? 0.2236 0.1457 0.2331 0.0464  -0.0653 -0.0422 496  ARG B N   
4710 C CA  . ARG B 273 ? 0.2702 0.1718 0.2763 0.0696  -0.0506 -0.0688 496  ARG B CA  
4711 C C   . ARG B 273 ? 0.2480 0.1562 0.2500 0.0562  -0.0722 -0.0241 496  ARG B C   
4712 O O   . ARG B 273 ? 0.2145 0.1580 0.2487 0.0457  -0.0649 -0.0093 496  ARG B O   
4713 C CB  . ARG B 273 ? 0.3712 0.2491 0.3352 0.0973  -0.0334 -0.0988 496  ARG B CB  
4714 C CG  . ARG B 273 ? 0.4642 0.3296 0.4202 0.1429  0.0067  -0.1079 496  ARG B CG  
4715 C CD  . ARG B 273 ? 0.5365 0.4077 0.4962 0.1540  0.0402  -0.1002 496  ARG B CD  
4716 N NE  . ARG B 273 ? 0.5872 0.4703 0.5566 0.1732  0.0570  -0.1009 496  ARG B NE  
4717 C CZ  . ARG B 273 ? 0.6376 0.5170 0.6149 0.1717  0.0662  -0.0892 496  ARG B CZ  
4718 N NH1 . ARG B 273 ? 0.6647 0.5379 0.6358 0.1614  0.0714  -0.0819 496  ARG B NH1 
4719 N NH2 . ARG B 273 ? 0.6426 0.5211 0.6283 0.1792  0.0648  -0.0925 496  ARG B NH2 
4720 N N   . GLN B 274 ? 0.2229 0.1181 0.2336 0.0407  -0.0946 -0.0363 497  GLN B N   
4721 C CA  . GLN B 274 ? 0.2318 0.1337 0.2476 0.0294  -0.0732 -0.0099 497  GLN B CA  
4722 C C   . GLN B 274 ? 0.2168 0.1290 0.2166 -0.0037 -0.0798 -0.0081 497  GLN B C   
4723 O O   . GLN B 274 ? 0.2307 0.1634 0.2210 0.0083  -0.0639 0.0009  497  GLN B O   
4724 C CB  . GLN B 274 ? 0.3075 0.1760 0.2896 0.0586  -0.0578 -0.0175 497  GLN B CB  
4725 C CG  . GLN B 274 ? 0.3585 0.1801 0.3618 0.0850  -0.0242 -0.0118 497  GLN B CG  
4726 C CD  . GLN B 274 ? 0.3794 0.1964 0.4435 0.0825  -0.0351 0.0043  497  GLN B CD  
4727 O OE1 . GLN B 274 ? 0.2747 0.1751 0.3575 0.0681  -0.1157 0.0164  497  GLN B OE1 
4728 N NE2 . GLN B 274 ? 0.4304 0.2356 0.5182 0.0831  -0.0133 -0.0050 497  GLN B NE2 
4729 N N   . GLY B 275 ? 0.2016 0.1103 0.2047 0.0113  -0.0787 -0.0027 498  GLY B N   
4730 C CA  . GLY B 275 ? 0.2066 0.1113 0.2175 -0.0102 -0.0520 -0.0085 498  GLY B CA  
4731 C C   . GLY B 275 ? 0.1882 0.1019 0.1892 0.0075  -0.0776 -0.0052 498  GLY B C   
4732 O O   . GLY B 275 ? 0.2367 0.1033 0.2045 -0.0205 -0.0300 -0.0283 498  GLY B O   
4733 N N   . TYR B 276 ? 0.2140 0.1055 0.1814 -0.0023 -0.0638 -0.0060 499  TYR B N   
4734 C CA  . TYR B 276 ? 0.1901 0.1150 0.1614 0.0098  -0.0612 -0.0022 499  TYR B CA  
4735 C C   . TYR B 276 ? 0.1983 0.1033 0.1571 -0.0164 -0.0655 -0.0086 499  TYR B C   
4736 O O   . TYR B 276 ? 0.2509 0.1200 0.1540 -0.0011 -0.0678 -0.0302 499  TYR B O   
4737 C CB  . TYR B 276 ? 0.2311 0.1097 0.1445 0.0063  -0.0506 -0.0107 499  TYR B CB  
4738 C CG  . TYR B 276 ? 0.2277 0.1132 0.1525 0.0002  -0.0725 -0.0109 499  TYR B CG  
4739 C CD1 . TYR B 276 ? 0.2276 0.1304 0.1539 0.0208  -0.0667 0.0034  499  TYR B CD1 
4740 C CD2 . TYR B 276 ? 0.2446 0.1174 0.1766 -0.0025 -0.0796 0.0029  499  TYR B CD2 
4741 C CE1 . TYR B 276 ? 0.2645 0.1184 0.1589 0.0220  -0.0748 -0.0137 499  TYR B CE1 
4742 C CE2 . TYR B 276 ? 0.2690 0.1263 0.1834 0.0197  -0.1261 -0.0138 499  TYR B CE2 
4743 C CZ  . TYR B 276 ? 0.2734 0.1213 0.1864 0.0338  -0.1047 0.0158  499  TYR B CZ  
4744 O OH  . TYR B 276 ? 0.3181 0.1178 0.2171 0.0233  -0.1067 -0.0028 499  TYR B OH  
4745 N N   . ILE B 277 ? 0.1994 0.0855 0.1551 -0.0042 -0.0683 0.0005  500  ILE B N   
4746 C CA  . ILE B 277 ? 0.1925 0.0935 0.1481 -0.0246 -0.0858 0.0046  500  ILE B CA  
4747 C C   . ILE B 277 ? 0.2053 0.0940 0.1487 -0.0237 -0.0828 0.0041  500  ILE B C   
4748 O O   . ILE B 277 ? 0.2032 0.0981 0.1641 -0.0292 -0.0802 -0.0049 500  ILE B O   
4749 C CB  . ILE B 277 ? 0.1849 0.0890 0.1465 0.0119  -0.0676 0.0152  500  ILE B CB  
4750 C CG1 . ILE B 277 ? 0.2266 0.1046 0.1508 0.0108  -0.0550 0.0303  500  ILE B CG1 
4751 C CG2 . ILE B 277 ? 0.2026 0.1220 0.1630 0.0122  -0.0938 0.0147  500  ILE B CG2 
4752 C CD1 . ILE B 277 ? 0.2323 0.1118 0.1665 0.0143  -0.0373 0.0095  500  ILE B CD1 
4753 N N   . THR B 278 ? 0.2234 0.0983 0.1501 -0.0379 -0.0726 -0.0095 501  THR B N   
4754 C CA  . THR B 278 ? 0.2154 0.1094 0.1778 -0.0299 -0.0898 0.0318  501  THR B CA  
4755 C C   . THR B 278 ? 0.2258 0.1108 0.1881 -0.0226 -0.0690 0.0074  501  THR B C   
4756 O O   . THR B 278 ? 0.2344 0.1064 0.1930 -0.0282 -0.0586 0.0031  501  THR B O   
4757 C CB  . THR B 278 ? 0.2388 0.1159 0.1781 -0.0057 -0.0972 0.0086  501  THR B CB  
4758 O OG1 . THR B 278 ? 0.2404 0.1235 0.2030 -0.0054 -0.0942 -0.0329 501  THR B OG1 
4759 C CG2 . THR B 278 ? 0.2448 0.1338 0.2004 -0.0042 -0.0833 0.0117  501  THR B CG2 
4760 N N   . VAL B 279 ? 0.2092 0.1244 0.2017 -0.0384 -0.0853 -0.0092 502  VAL B N   
4761 C CA  . VAL B 279 ? 0.2129 0.1295 0.1872 -0.0500 -0.0763 -0.0027 502  VAL B CA  
4762 C C   . VAL B 279 ? 0.2267 0.1360 0.2135 -0.0602 -0.0927 -0.0031 502  VAL B C   
4763 O O   . VAL B 279 ? 0.2376 0.1557 0.2301 -0.0734 -0.1029 0.0127  502  VAL B O   
4764 C CB  . VAL B 279 ? 0.2291 0.1363 0.1582 -0.0381 -0.0461 0.0099  502  VAL B CB  
4765 C CG1 . VAL B 279 ? 0.2214 0.1630 0.1672 -0.0372 -0.0229 0.0184  502  VAL B CG1 
4766 C CG2 . VAL B 279 ? 0.2410 0.1532 0.1452 -0.0583 -0.0419 -0.0037 502  VAL B CG2 
4767 N N   . ALA B 280 ? 0.2094 0.1347 0.2387 -0.0631 -0.0829 -0.0128 503  ALA B N   
4768 C CA  . ALA B 280 ? 0.2192 0.1375 0.2516 -0.0671 -0.0761 -0.0219 503  ALA B CA  
4769 C C   . ALA B 280 ? 0.2102 0.1616 0.2646 -0.0654 -0.0962 -0.0011 503  ALA B C   
4770 O O   . ALA B 280 ? 0.2494 0.1775 0.2801 -0.0166 -0.1050 -0.0171 503  ALA B O   
4771 C CB  . ALA B 280 ? 0.2317 0.1519 0.2308 -0.0674 -0.0952 -0.0132 503  ALA B CB  
4772 N N   . LYS B 281 ? 0.2209 0.2082 0.2596 -0.0571 -0.0892 0.0195  504  LYS B N   
4773 C CA  . LYS B 281 ? 0.2868 0.2499 0.2633 -0.0631 -0.0445 0.0299  504  LYS B CA  
4774 C C   . LYS B 281 ? 0.3264 0.3053 0.2502 -0.0367 -0.0276 0.0360  504  LYS B C   
4775 O O   . LYS B 281 ? 0.3293 0.3616 0.2339 -0.0171 -0.0149 0.0463  504  LYS B O   
4776 C CB  . LYS B 281 ? 0.3486 0.2752 0.3305 -0.0644 0.0087  0.0000  504  LYS B CB  
4777 C CG  . LYS B 281 ? 0.3964 0.3076 0.3870 -0.0579 0.0401  -0.0282 504  LYS B CG  
4778 C CD  . LYS B 281 ? 0.4322 0.3754 0.4576 -0.0497 0.0490  -0.0509 504  LYS B CD  
4779 C CE  . LYS B 281 ? 0.4694 0.4379 0.5227 -0.0496 0.0600  -0.0560 504  LYS B CE  
4780 N NZ  . LYS B 281 ? 0.4856 0.4722 0.5712 -0.0438 0.0768  -0.0549 504  LYS B NZ  
4781 N N   . THR B 282 ? 0.3529 0.3127 0.2831 -0.0371 0.0072  0.0211  505  THR B N   
4782 C CA  . THR B 282 ? 0.4571 0.3339 0.3378 0.0035  0.0750  0.0277  505  THR B CA  
4783 C C   . THR B 282 ? 0.4433 0.3403 0.3102 0.0291  0.0799  0.0501  505  THR B C   
4784 O O   . THR B 282 ? 0.4961 0.3837 0.2836 0.0834  0.0769  0.0384  505  THR B O   
4785 C CB  . THR B 282 ? 0.5706 0.3368 0.4011 0.0225  0.1382  0.0144  505  THR B CB  
4786 O OG1 . THR B 282 ? 0.6373 0.3572 0.4375 0.0365  0.1713  0.0042  505  THR B OG1 
4787 C CG2 . THR B 282 ? 0.5977 0.3477 0.4306 0.0116  0.1433  0.0107  505  THR B CG2 
4788 N N   . GLY B 283 ? 0.3653 0.2910 0.3452 -0.0267 0.0682  0.0802  506  GLY B N   
4789 C CA  . GLY B 283 ? 0.3344 0.2519 0.3574 -0.0479 0.0578  0.0826  506  GLY B CA  
4790 C C   . GLY B 283 ? 0.2911 0.2373 0.3827 -0.0315 0.0429  0.0882  506  GLY B C   
4791 O O   . GLY B 283 ? 0.2739 0.2303 0.3865 0.0151  0.0545  0.1148  506  GLY B O   
4792 N N   . ASP B 284 ? 0.3171 0.2561 0.4087 -0.0477 0.0176  0.0803  507  ASP B N   
4793 C CA  . ASP B 284 ? 0.3131 0.2862 0.4161 -0.0441 -0.0169 0.0818  507  ASP B CA  
4794 C C   . ASP B 284 ? 0.3076 0.3161 0.4048 -0.0152 0.0020  0.0871  507  ASP B C   
4795 O O   . ASP B 284 ? 0.3403 0.3267 0.4191 -0.0042 0.0626  0.1019  507  ASP B O   
4796 C CB  . ASP B 284 ? 0.3799 0.3104 0.4537 -0.0389 -0.0453 0.0737  507  ASP B CB  
4797 C CG  . ASP B 284 ? 0.4551 0.3444 0.5079 -0.0215 -0.0595 0.0424  507  ASP B CG  
4798 O OD1 . ASP B 284 ? 0.5104 0.3646 0.5105 -0.0413 -0.0134 0.0620  507  ASP B OD1 
4799 O OD2 . ASP B 284 ? 0.4988 0.3612 0.5745 -0.0230 -0.0405 0.0197  507  ASP B OD2 
4800 N N   . SER B 285 ? 0.2923 0.3263 0.3801 -0.0040 -0.0193 0.0788  508  SER B N   
4801 C CA  A SER B 285 ? 0.3036 0.3420 0.3801 0.0099  -0.0484 0.0538  508  SER B CA  
4802 C CA  B SER B 285 ? 0.3044 0.3453 0.3691 0.0295  -0.0434 0.0794  508  SER B CA  
4803 C C   . SER B 285 ? 0.2962 0.3284 0.3681 0.0472  -0.0400 0.0646  508  SER B C   
4804 O O   . SER B 285 ? 0.2313 0.2857 0.3257 0.0080  -0.0616 0.0459  508  SER B O   
4805 C CB  A SER B 285 ? 0.3518 0.3676 0.4111 -0.0080 -0.0372 0.0086  508  SER B CB  
4806 C CB  B SER B 285 ? 0.3394 0.3767 0.3760 0.0375  -0.0437 0.0788  508  SER B CB  
4807 O OG  A SER B 285 ? 0.3763 0.3773 0.4310 -0.0139 -0.0062 -0.0108 508  SER B OG  
4808 O OG  B SER B 285 ? 0.3492 0.3926 0.3759 0.0473  -0.0448 0.0902  508  SER B OG  
4809 N N   . PRO B 286 ? 0.3316 0.3472 0.3966 0.1147  0.0139  0.0714  509  PRO B N   
4810 C CA  . PRO B 286 ? 0.3283 0.3440 0.3742 0.1158  0.0004  0.0814  509  PRO B CA  
4811 C C   . PRO B 286 ? 0.3026 0.3323 0.3291 0.0545  -0.0516 0.0696  509  PRO B C   
4812 O O   . PRO B 286 ? 0.2882 0.3662 0.3272 0.0051  -0.0167 0.0886  509  PRO B O   
4813 C CB  . PRO B 286 ? 0.3638 0.3639 0.4189 0.1337  0.0591  0.0898  509  PRO B CB  
4814 C CG  . PRO B 286 ? 0.3740 0.3810 0.4422 0.1525  0.0729  0.0892  509  PRO B CG  
4815 C CD  . PRO B 286 ? 0.3662 0.3730 0.4287 0.1326  0.0686  0.0707  509  PRO B CD  
4816 N N   . ILE B 287 ? 0.3321 0.3101 0.2821 0.0178  -0.0853 0.0559  510  ILE B N   
4817 C CA  . ILE B 287 ? 0.3329 0.3115 0.2725 -0.0210 -0.1460 0.0301  510  ILE B CA  
4818 C C   . ILE B 287 ? 0.4136 0.3292 0.3151 -0.0042 -0.1338 0.0436  510  ILE B C   
4819 O O   . ILE B 287 ? 0.4163 0.3330 0.3218 -0.0287 -0.1257 0.0633  510  ILE B O   
4820 C CB  . ILE B 287 ? 0.3536 0.3155 0.2923 -0.0657 -0.1160 0.0187  510  ILE B CB  
4821 C CG1 . ILE B 287 ? 0.3874 0.3160 0.3000 -0.0803 -0.0843 0.0249  510  ILE B CG1 
4822 C CG2 . ILE B 287 ? 0.3592 0.3265 0.2735 -0.0644 -0.1056 0.0364  510  ILE B CG2 
4823 C CD1 . ILE B 287 ? 0.4267 0.3301 0.3262 -0.0515 -0.0506 0.0445  510  ILE B CD1 
4824 N N   . ASN B 288 ? 0.4700 0.3397 0.3736 0.0410  -0.1304 0.0491  511  ASN B N   
4825 C CA  . ASN B 288 ? 0.5522 0.3677 0.4432 0.0538  -0.1081 0.0217  511  ASN B CA  
4826 C C   . ASN B 288 ? 0.5410 0.3497 0.4102 0.0621  -0.1674 0.0000  511  ASN B C   
4827 O O   . ASN B 288 ? 0.6043 0.3624 0.4708 0.0512  -0.1099 0.0102  511  ASN B O   
4828 C CB  . ASN B 288 ? 0.6422 0.4102 0.5297 0.0507  -0.0439 0.0142  511  ASN B CB  
4829 C CG  . ASN B 288 ? 0.7138 0.4390 0.6012 0.0404  0.0135  0.0048  511  ASN B CG  
4830 O OD1 . ASN B 288 ? 0.7418 0.4419 0.6185 0.0442  0.0400  -0.0048 511  ASN B OD1 
4831 N ND2 . ASN B 288 ? 0.7465 0.4552 0.6350 0.0393  0.0330  0.0066  511  ASN B ND2 
4832 N N   . VAL B 289 ? 0.4893 0.3182 0.3849 0.0936  -0.1804 -0.0260 512  VAL B N   
4833 C CA  . VAL B 289 ? 0.4764 0.2933 0.3517 0.1144  -0.1678 -0.0436 512  VAL B CA  
4834 C C   . VAL B 289 ? 0.4168 0.2553 0.3529 0.0942  -0.1642 -0.0559 512  VAL B C   
4835 O O   . VAL B 289 ? 0.3954 0.2447 0.3535 0.0758  -0.1079 -0.0844 512  VAL B O   
4836 C CB  . VAL B 289 ? 0.5197 0.3168 0.3596 0.1367  -0.1158 -0.0631 512  VAL B CB  
4837 C CG1 . VAL B 289 ? 0.5720 0.3203 0.3558 0.1495  -0.0764 -0.0456 512  VAL B CG1 
4838 C CG2 . VAL B 289 ? 0.5181 0.3334 0.3775 0.1471  -0.1200 -0.0713 512  VAL B CG2 
4839 N N   . PRO B 290 ? 0.3842 0.2297 0.3545 0.0891  -0.1864 -0.0449 513  PRO B N   
4840 C CA  . PRO B 290 ? 0.3465 0.2221 0.3842 0.1001  -0.1659 -0.0487 513  PRO B CA  
4841 C C   . PRO B 290 ? 0.3234 0.2094 0.3832 0.0880  -0.1419 -0.0924 513  PRO B C   
4842 O O   . PRO B 290 ? 0.3249 0.2326 0.3649 0.1061  -0.1669 -0.0804 513  PRO B O   
4843 C CB  . PRO B 290 ? 0.3726 0.2273 0.3858 0.0874  -0.1646 -0.0361 513  PRO B CB  
4844 C CG  . PRO B 290 ? 0.4130 0.2435 0.3702 0.0633  -0.1640 -0.0414 513  PRO B CG  
4845 C CD  . PRO B 290 ? 0.4013 0.2409 0.3548 0.0645  -0.1805 -0.0483 513  PRO B CD  
4846 N N   . ALA B 291 ? 0.3130 0.2062 0.4073 0.0491  -0.1006 -0.1117 514  ALA B N   
4847 C CA  . ALA B 291 ? 0.2922 0.2101 0.4326 0.0572  -0.0884 -0.1349 514  ALA B CA  
4848 C C   . ALA B 291 ? 0.2516 0.2151 0.4208 0.0660  -0.1187 -0.1353 514  ALA B C   
4849 O O   . ALA B 291 ? 0.2612 0.2440 0.4572 0.0343  -0.0785 -0.1450 514  ALA B O   
4850 C CB  . ALA B 291 ? 0.3433 0.2136 0.4615 0.0610  -0.0553 -0.1453 514  ALA B CB  
4851 N N   . ASN B 292 ? 0.2504 0.2074 0.4332 0.0700  -0.1050 -0.1123 515  ASN B N   
4852 C CA  . ASN B 292 ? 0.2476 0.2123 0.4162 0.0854  -0.1161 -0.0826 515  ASN B CA  
4853 C C   . ASN B 292 ? 0.2293 0.1930 0.3829 0.0536  -0.0828 -0.0900 515  ASN B C   
4854 O O   . ASN B 292 ? 0.2106 0.2082 0.3798 0.0582  -0.0504 -0.0847 515  ASN B O   
4855 C CB  . ASN B 292 ? 0.2560 0.2348 0.4290 0.0895  -0.1583 -0.0824 515  ASN B CB  
4856 C CG  . ASN B 292 ? 0.2921 0.2696 0.4413 0.0803  -0.1588 -0.0840 515  ASN B CG  
4857 O OD1 . ASN B 292 ? 0.2969 0.2919 0.4686 0.0674  -0.1390 -0.0975 515  ASN B OD1 
4858 N ND2 . ASN B 292 ? 0.3030 0.2742 0.4442 0.0865  -0.1478 -0.0821 515  ASN B ND2 
4859 N N   . GLY B 293 ? 0.2236 0.1828 0.3512 0.0593  -0.0837 -0.0813 516  GLY B N   
4860 C CA  . GLY B 293 ? 0.2151 0.1512 0.3150 0.0608  -0.0617 -0.0747 516  GLY B CA  
4861 C C   . GLY B 293 ? 0.2111 0.1452 0.2630 0.0543  -0.0440 -0.0632 516  GLY B C   
4862 O O   . GLY B 293 ? 0.2020 0.1732 0.2715 0.0094  -0.0441 -0.0700 516  GLY B O   
4863 N N   . TYR B 294 ? 0.2139 0.1305 0.2290 0.0660  -0.0905 -0.0360 517  TYR B N   
4864 C CA  . TYR B 294 ? 0.1956 0.1343 0.2016 0.0405  -0.0575 -0.0148 517  TYR B CA  
4865 C C   . TYR B 294 ? 0.1833 0.1351 0.2003 0.0123  -0.0705 -0.0225 517  TYR B C   
4866 O O   . TYR B 294 ? 0.2003 0.1344 0.2214 0.0149  -0.0819 -0.0170 517  TYR B O   
4867 C CB  . TYR B 294 ? 0.2107 0.1562 0.1666 0.0124  -0.0509 -0.0079 517  TYR B CB  
4868 C CG  . TYR B 294 ? 0.2228 0.1780 0.1579 0.0341  -0.0685 0.0028  517  TYR B CG  
4869 C CD1 . TYR B 294 ? 0.2857 0.2006 0.1407 0.0138  -0.0470 -0.0122 517  TYR B CD1 
4870 C CD2 . TYR B 294 ? 0.2469 0.2282 0.1652 0.0276  -0.0723 0.0455  517  TYR B CD2 
4871 C CE1 . TYR B 294 ? 0.3361 0.2406 0.1707 0.0128  -0.0398 0.0001  517  TYR B CE1 
4872 C CE2 . TYR B 294 ? 0.3036 0.2524 0.1809 0.0221  -0.0747 0.0372  517  TYR B CE2 
4873 C CZ  . TYR B 294 ? 0.3434 0.2707 0.1539 0.0180  -0.0764 0.0250  517  TYR B CZ  
4874 O OH  . TYR B 294 ? 0.4032 0.3175 0.2093 0.0196  -0.0651 0.0493  517  TYR B OH  
4875 N N   . PHE B 295 ? 0.1858 0.1388 0.1756 0.0368  -0.0560 -0.0013 518  PHE B N   
4876 C CA  . PHE B 295 ? 0.2119 0.1364 0.1560 0.0405  -0.0362 -0.0022 518  PHE B CA  
4877 C C   . PHE B 295 ? 0.2239 0.1375 0.1775 0.0271  -0.0401 -0.0024 518  PHE B C   
4878 O O   . PHE B 295 ? 0.2287 0.1233 0.2124 0.0288  -0.0467 0.0118  518  PHE B O   
4879 C CB  . PHE B 295 ? 0.2026 0.1307 0.1571 0.0371  -0.0583 0.0053  518  PHE B CB  
4880 C CG  . PHE B 295 ? 0.1997 0.1178 0.1675 0.0054  -0.0597 -0.0007 518  PHE B CG  
4881 C CD1 . PHE B 295 ? 0.1956 0.1249 0.1879 0.0200  -0.0486 0.0147  518  PHE B CD1 
4882 C CD2 . PHE B 295 ? 0.1967 0.1388 0.1601 0.0074  -0.0556 0.0036  518  PHE B CD2 
4883 C CE1 . PHE B 295 ? 0.2129 0.1446 0.1879 0.0166  -0.0518 0.0036  518  PHE B CE1 
4884 C CE2 . PHE B 295 ? 0.1872 0.1550 0.1907 0.0085  -0.0549 0.0055  518  PHE B CE2 
4885 C CZ  . PHE B 295 ? 0.1961 0.1487 0.1785 0.0153  -0.0597 -0.0036 518  PHE B CZ  
4886 N N   . ARG B 296 ? 0.2215 0.1420 0.1666 0.0344  -0.0522 -0.0298 519  ARG B N   
4887 C CA  . ARG B 296 ? 0.2188 0.1736 0.1575 0.0446  -0.0739 -0.0256 519  ARG B CA  
4888 C C   . ARG B 296 ? 0.2197 0.1707 0.1657 0.0290  -0.0425 -0.0352 519  ARG B C   
4889 O O   . ARG B 296 ? 0.2463 0.1771 0.1669 0.0400  -0.0392 -0.0129 519  ARG B O   
4890 C CB  . ARG B 296 ? 0.2331 0.2105 0.1796 0.0884  -0.0844 0.0101  519  ARG B CB  
4891 C CG  . ARG B 296 ? 0.2729 0.2419 0.2570 0.1044  -0.1141 0.0049  519  ARG B CG  
4892 C CD  . ARG B 296 ? 0.3016 0.2927 0.3127 0.1024  -0.1422 0.0216  519  ARG B CD  
4893 N NE  . ARG B 296 ? 0.3531 0.3395 0.3374 0.0916  -0.1762 0.0291  519  ARG B NE  
4894 C CZ  . ARG B 296 ? 0.3995 0.3747 0.3269 0.0957  -0.1897 0.0191  519  ARG B CZ  
4895 N NH1 . ARG B 296 ? 0.4528 0.3978 0.3397 0.0898  -0.1826 0.0044  519  ARG B NH1 
4896 N NH2 . ARG B 296 ? 0.4182 0.3841 0.3407 0.0866  -0.1495 -0.0116 519  ARG B NH2 
4897 N N   . PHE B 297 ? 0.2222 0.1645 0.1922 0.0295  -0.0691 -0.0245 520  PHE B N   
4898 C CA  . PHE B 297 ? 0.2045 0.1706 0.2189 0.0298  -0.0513 -0.0372 520  PHE B CA  
4899 C C   . PHE B 297 ? 0.2436 0.1505 0.2184 0.0165  -0.0538 -0.0301 520  PHE B C   
4900 O O   . PHE B 297 ? 0.2926 0.1618 0.2089 0.0126  -0.0469 -0.0328 520  PHE B O   
4901 C CB  . PHE B 297 ? 0.2029 0.1973 0.2437 0.0326  -0.0381 -0.0418 520  PHE B CB  
4902 C CG  . PHE B 297 ? 0.2499 0.2099 0.2560 0.0758  -0.0283 -0.0524 520  PHE B CG  
4903 C CD1 . PHE B 297 ? 0.2576 0.2160 0.2481 0.0630  -0.0643 -0.0878 520  PHE B CD1 
4904 C CD2 . PHE B 297 ? 0.2873 0.2310 0.2694 0.0779  0.0180  -0.0469 520  PHE B CD2 
4905 C CE1 . PHE B 297 ? 0.2800 0.2203 0.2519 0.0667  -0.0632 -0.0918 520  PHE B CE1 
4906 C CE2 . PHE B 297 ? 0.3291 0.2310 0.2904 0.0622  0.0007  -0.0637 520  PHE B CE2 
4907 C CZ  . PHE B 297 ? 0.2897 0.2273 0.2720 0.0656  -0.0364 -0.0738 520  PHE B CZ  
4908 N N   . ASP B 298 ? 0.2182 0.1392 0.1951 0.0171  -0.0780 -0.0694 521  ASP B N   
4909 C CA  . ASP B 298 ? 0.2035 0.1562 0.1930 0.0138  -0.0768 -0.0658 521  ASP B CA  
4910 C C   . ASP B 298 ? 0.2142 0.1605 0.1767 0.0311  -0.0686 -0.0654 521  ASP B C   
4911 O O   . ASP B 298 ? 0.2544 0.1917 0.1826 0.0199  -0.0583 -0.0621 521  ASP B O   
4912 C CB  . ASP B 298 ? 0.2077 0.1714 0.1924 -0.0098 -0.0794 -0.0459 521  ASP B CB  
4913 C CG  . ASP B 298 ? 0.2523 0.1774 0.2169 -0.0001 -0.0899 -0.0319 521  ASP B CG  
4914 O OD1 . ASP B 298 ? 0.2384 0.2215 0.2561 0.0212  -0.1070 -0.0179 521  ASP B OD1 
4915 O OD2 . ASP B 298 ? 0.2669 0.1737 0.2404 0.0016  -0.0768 -0.0695 521  ASP B OD2 
4916 N N   . SER B 299 ? 0.2115 0.1548 0.2241 0.0302  -0.0723 -0.0513 522  SER B N   
4917 C CA  . SER B 299 ? 0.2423 0.1634 0.2148 0.0326  -0.0815 -0.0580 522  SER B CA  
4918 C C   . SER B 299 ? 0.2425 0.1650 0.2377 0.0349  -0.0972 -0.0501 522  SER B C   
4919 O O   . SER B 299 ? 0.2603 0.1733 0.2285 0.0304  -0.0832 -0.0591 522  SER B O   
4920 C CB  . SER B 299 ? 0.2517 0.1785 0.2194 0.0104  -0.0667 -0.0484 522  SER B CB  
4921 O OG  . SER B 299 ? 0.2692 0.1715 0.2462 -0.0115 -0.0936 -0.0439 522  SER B OG  
4922 N N   . TRP B 300 ? 0.2535 0.1663 0.2507 0.0544  -0.1249 -0.0626 523  TRP B N   
4923 C CA  . TRP B 300 ? 0.2709 0.1692 0.2315 0.0759  -0.1349 -0.0800 523  TRP B CA  
4924 C C   . TRP B 300 ? 0.3051 0.1773 0.2594 0.0606  -0.1345 -0.0895 523  TRP B C   
4925 O O   . TRP B 300 ? 0.3544 0.1967 0.2588 0.0642  -0.1110 -0.1036 523  TRP B O   
4926 C CB  . TRP B 300 ? 0.2878 0.2054 0.2546 0.0840  -0.1274 -0.0898 523  TRP B CB  
4927 C CG  . TRP B 300 ? 0.2905 0.2309 0.2659 0.0930  -0.1114 -0.0794 523  TRP B CG  
4928 C CD1 . TRP B 300 ? 0.2986 0.2429 0.2565 0.1049  -0.0994 -0.0952 523  TRP B CD1 
4929 C CD2 . TRP B 300 ? 0.2795 0.2264 0.2844 0.0868  -0.1046 -0.1085 523  TRP B CD2 
4930 N NE1 . TRP B 300 ? 0.2847 0.2698 0.2691 0.0820  -0.1285 -0.0846 523  TRP B NE1 
4931 C CE2 . TRP B 300 ? 0.2779 0.2441 0.2804 0.0945  -0.1160 -0.0913 523  TRP B CE2 
4932 C CE3 . TRP B 300 ? 0.2450 0.2183 0.2771 0.0965  -0.1266 -0.1235 523  TRP B CE3 
4933 C CZ2 . TRP B 300 ? 0.2833 0.2387 0.2973 0.0964  -0.1048 -0.0874 523  TRP B CZ2 
4934 C CZ3 . TRP B 300 ? 0.2943 0.2170 0.3222 0.0929  -0.0755 -0.1136 523  TRP B CZ3 
4935 C CH2 . TRP B 300 ? 0.2998 0.2252 0.3113 0.0910  -0.0741 -0.0992 523  TRP B CH2 
4936 N N   . VAL B 301 ? 0.2989 0.1618 0.2705 0.0470  -0.1262 -0.0860 524  VAL B N   
4937 C CA  . VAL B 301 ? 0.3143 0.1670 0.2967 0.0467  -0.1207 -0.0720 524  VAL B CA  
4938 C C   . VAL B 301 ? 0.3292 0.1738 0.3040 0.0430  -0.1301 -0.0406 524  VAL B C   
4939 O O   . VAL B 301 ? 0.3251 0.1954 0.3174 0.0612  -0.1282 -0.0120 524  VAL B O   
4940 C CB  . VAL B 301 ? 0.2828 0.1782 0.2510 0.0385  -0.1444 -0.0691 524  VAL B CB  
4941 C CG1 . VAL B 301 ? 0.2889 0.1852 0.2460 0.0365  -0.1437 -0.0690 524  VAL B CG1 
4942 C CG2 . VAL B 301 ? 0.2977 0.2032 0.2223 0.0389  -0.1226 -0.0578 524  VAL B CG2 
4943 N N   . SER B 302 ? 0.3716 0.2026 0.3477 0.0941  -0.1431 -0.0030 525  SER B N   
4944 C CA  . SER B 302 ? 0.4465 0.2077 0.3535 0.1105  -0.1268 0.0151  525  SER B CA  
4945 C C   . SER B 302 ? 0.4688 0.2296 0.3563 0.1173  -0.1530 0.0142  525  SER B C   
4946 O O   . SER B 302 ? 0.4816 0.2374 0.3481 0.1271  -0.1602 -0.0004 525  SER B O   
4947 C CB  . SER B 302 ? 0.4885 0.2166 0.3814 0.1030  -0.0738 0.0023  525  SER B CB  
4948 O OG  . SER B 302 ? 0.5382 0.2235 0.3910 0.0876  -0.0483 -0.0052 525  SER B OG  
4949 N N   . GLN B 303 ? 0.5230 0.2627 0.3793 0.1254  -0.1704 0.0238  526  GLN B N   
4950 C CA  . GLN B 303 ? 0.5351 0.3017 0.3852 0.1135  -0.2128 0.0195  526  GLN B CA  
4951 C C   . GLN B 303 ? 0.5336 0.3111 0.3880 0.0866  -0.2325 0.0238  526  GLN B C   
4952 O O   . GLN B 303 ? 0.5487 0.3288 0.4082 0.0664  -0.2363 0.0121  526  GLN B O   
4953 C CB  . GLN B 303 ? 0.5662 0.3306 0.4150 0.1357  -0.2120 0.0294  526  GLN B CB  
4954 C CG  . GLN B 303 ? 0.6091 0.3673 0.4398 0.1478  -0.2194 0.0444  526  GLN B CG  
4955 C CD  . GLN B 303 ? 0.6682 0.4025 0.4858 0.1494  -0.2214 0.0299  526  GLN B CD  
4956 O OE1 . GLN B 303 ? 0.7102 0.4229 0.5096 0.1441  -0.1786 0.0307  526  GLN B OE1 
4957 N NE2 . GLN B 303 ? 0.6530 0.4192 0.4884 0.1500  -0.2560 0.0258  526  GLN B NE2 
4958 N N   . PHE B 304 ? 0.5066 0.3181 0.3911 0.0652  -0.2354 0.0364  527  PHE B N   
4959 C CA  . PHE B 304 ? 0.5427 0.3083 0.4017 0.0770  -0.2212 0.0562  527  PHE B CA  
4960 C C   . PHE B 304 ? 0.5134 0.2856 0.3945 0.0546  -0.2271 0.0457  527  PHE B C   
4961 O O   . PHE B 304 ? 0.5352 0.3060 0.4391 0.0637  -0.2010 0.0582  527  PHE B O   
4962 C CB  . PHE B 304 ? 0.5770 0.3169 0.3988 0.0918  -0.2022 0.0713  527  PHE B CB  
4963 C CG  . PHE B 304 ? 0.6072 0.3266 0.4053 0.1077  -0.1872 0.0618  527  PHE B CG  
4964 C CD1 . PHE B 304 ? 0.6250 0.3360 0.3976 0.1177  -0.1696 0.0707  527  PHE B CD1 
4965 C CD2 . PHE B 304 ? 0.6180 0.3366 0.4084 0.1128  -0.1760 0.0604  527  PHE B CD2 
4966 C CE1 . PHE B 304 ? 0.6415 0.3453 0.4221 0.1153  -0.1434 0.0606  527  PHE B CE1 
4967 C CE2 . PHE B 304 ? 0.6351 0.3369 0.4067 0.1154  -0.1587 0.0634  527  PHE B CE2 
4968 C CZ  . PHE B 304 ? 0.6513 0.3438 0.4221 0.1117  -0.1264 0.0567  527  PHE B CZ  
4969 N N   . TYR B 305 ? 0.4630 0.2573 0.3901 0.0420  -0.1901 0.0410  528  TYR B N   
4970 C CA  . TYR B 305 ? 0.4124 0.2226 0.3851 0.0182  -0.1720 0.0411  528  TYR B CA  
4971 C C   . TYR B 305 ? 0.3691 0.1932 0.3849 -0.0121 -0.1782 0.0171  528  TYR B C   
4972 O O   . TYR B 305 ? 0.3996 0.2254 0.3744 -0.0297 -0.1616 -0.0180 528  TYR B O   
4973 C CB  . TYR B 305 ? 0.3810 0.2217 0.3729 0.0170  -0.1734 0.0258  528  TYR B CB  
4974 C CG  . TYR B 305 ? 0.3764 0.2169 0.3344 -0.0071 -0.1745 -0.0135 528  TYR B CG  
4975 C CD1 . TYR B 305 ? 0.3592 0.2095 0.3391 -0.0033 -0.1830 -0.0228 528  TYR B CD1 
4976 C CD2 . TYR B 305 ? 0.3679 0.2461 0.3352 -0.0160 -0.1710 -0.0202 528  TYR B CD2 
4977 C CE1 . TYR B 305 ? 0.3745 0.2277 0.3299 0.0065  -0.1843 -0.0149 528  TYR B CE1 
4978 C CE2 . TYR B 305 ? 0.3782 0.2603 0.3221 -0.0099 -0.1718 -0.0021 528  TYR B CE2 
4979 C CZ  . TYR B 305 ? 0.3629 0.2810 0.3319 0.0195  -0.2005 0.0280  528  TYR B CZ  
4980 O OH  . TYR B 305 ? 0.3857 0.3551 0.3925 0.0298  -0.1577 0.0636  528  TYR B OH  
4981 N N   . SER B 306 ? 0.3851 0.1594 0.4090 -0.0136 -0.1452 0.0360  529  SER B N   
4982 C CA  . SER B 306 ? 0.3740 0.1673 0.4161 -0.0325 -0.1648 0.0338  529  SER B CA  
4983 C C   . SER B 306 ? 0.3481 0.1473 0.3505 -0.0201 -0.1750 0.0108  529  SER B C   
4984 O O   . SER B 306 ? 0.4044 0.1625 0.3488 -0.0336 -0.1486 -0.0221 529  SER B O   
4985 C CB  . SER B 306 ? 0.4218 0.2095 0.4818 -0.0738 -0.1250 0.0103  529  SER B CB  
4986 O OG  . SER B 306 ? 0.4651 0.2439 0.5086 -0.0692 -0.1097 0.0216  529  SER B OG  
4987 N N   . LEU B 307 ? 0.3066 0.1321 0.3204 -0.0355 -0.1387 0.0000  530  LEU B N   
4988 C CA  . LEU B 307 ? 0.2894 0.1473 0.2569 -0.0219 -0.1450 -0.0055 530  LEU B CA  
4989 C C   . LEU B 307 ? 0.2909 0.1736 0.2365 -0.0451 -0.1335 -0.0197 530  LEU B C   
4990 O O   . LEU B 307 ? 0.3038 0.1679 0.2880 -0.0436 -0.1138 0.0142  530  LEU B O   
4991 C CB  . LEU B 307 ? 0.3032 0.1620 0.2520 -0.0650 -0.1087 -0.0295 530  LEU B CB  
4992 C CG  . LEU B 307 ? 0.3104 0.1493 0.2174 -0.0545 -0.0942 -0.0282 530  LEU B CG  
4993 C CD1 . LEU B 307 ? 0.3164 0.1535 0.2174 -0.0691 -0.0835 -0.0340 530  LEU B CD1 
4994 C CD2 . LEU B 307 ? 0.3387 0.1417 0.1887 -0.0374 -0.1038 -0.0196 530  LEU B CD2 
4995 N N   . ALA B 308 ? 0.2908 0.1885 0.2775 -0.0433 -0.1535 -0.0138 531  ALA B N   
4996 C CA  . ALA B 308 ? 0.2957 0.2465 0.3092 -0.0529 -0.1764 0.0293  531  ALA B CA  
4997 C C   . ALA B 308 ? 0.3409 0.3375 0.3759 -0.0565 -0.2064 0.0035  531  ALA B C   
4998 O O   . ALA B 308 ? 0.3281 0.2568 0.3179 -0.0385 -0.1880 -0.0024 531  ALA B O   
4999 C CB  . ALA B 308 ? 0.2901 0.2416 0.3084 -0.0466 -0.1575 0.0360  531  ALA B CB  
5000 N N   A PRO B 309 ? 0.5821 0.6068 0.6220 -0.0707 -0.2946 -0.0005 532  PRO B N   
5001 N N   B PRO B 309 ? 0.2556 0.2710 0.2920 -0.0828 -0.1297 -0.0267 532  PRO B N   
5002 C CA  A PRO B 309 ? 0.8032 0.8321 0.8360 -0.0715 -0.3153 -0.0044 532  PRO B CA  
5003 C CA  B PRO B 309 ? 0.2170 0.2466 0.2620 -0.0783 -0.1072 -0.0291 532  PRO B CA  
5004 C C   A PRO B 309 ? 1.1034 1.1207 1.1181 -0.0731 -0.3265 -0.0113 532  PRO B C   
5005 C C   B PRO B 309 ? 0.2450 0.2449 0.2515 -0.0272 -0.1389 -0.0314 532  PRO B C   
5006 O O   A PRO B 309 ? 1.0965 1.1189 1.1112 -0.0752 -0.3382 -0.0159 532  PRO B O   
5007 O O   B PRO B 309 ? 0.2809 0.2611 0.2572 0.0328  -0.1281 -0.0244 532  PRO B O   
5008 C CB  A PRO B 309 ? 0.7330 0.7735 0.7724 -0.0724 -0.3231 -0.0048 532  PRO B CB  
5009 C CB  B PRO B 309 ? 0.2509 0.2652 0.2956 -0.1128 -0.0967 -0.0330 532  PRO B CB  
5010 C CG  A PRO B 309 ? 0.6679 0.7148 0.7117 -0.0728 -0.3264 -0.0031 532  PRO B CG  
5011 C CG  B PRO B 309 ? 0.2894 0.2664 0.3141 -0.1450 -0.0702 -0.0308 532  PRO B CG  
5012 C CD  A PRO B 309 ? 0.6202 0.6585 0.6650 -0.0719 -0.3094 0.0006  532  PRO B CD  
5013 C CD  B PRO B 309 ? 0.2687 0.2630 0.3089 -0.1246 -0.0925 -0.0294 532  PRO B CD  
5063 O O   . HOH D .   ? 0.6589 0.1999 0.3568 0.0210  -0.0190 -0.0472 733  HOH A O   
5065 O O   . HOH D .   ? 0.2697 0.2534 0.6403 -0.0140 0.0068  -0.1842 735  HOH A O   
5073 O O   . HOH D .   ? 0.2279 0.1569 0.2234 0.0324  -0.0401 0.0080  743  HOH A O   
5075 O O   . HOH D .   ? 0.2159 0.3366 0.3831 -0.0360 0.0590  -0.0570 745  HOH A O   
5080 O O   . HOH D .   ? 0.2665 0.3178 0.3877 -0.0486 0.1237  -0.0216 750  HOH A O   
5082 O O   . HOH D .   ? 0.3466 0.4512 0.3539 -0.0176 -0.0023 -0.0575 752  HOH A O   
5084 O O   . HOH D .   ? 0.6695 0.3378 0.3940 0.0122  -0.0384 -0.0069 754  HOH A O   
5085 O O   . HOH D .   ? 0.3290 0.3884 0.2413 0.0450  -0.0242 -0.0047 755  HOH A O   
5088 O O   . HOH D .   ? 0.3294 0.5764 0.7629 -0.0275 -0.1152 -0.1089 758  HOH A O   
5089 O O   . HOH D .   ? 0.5067 0.3823 0.6419 0.1823  -0.1049 -0.0815 759  HOH A O   
5091 O O   . HOH D .   ? 0.3476 0.4213 0.3222 -0.1282 -0.1046 0.0531  761  HOH A O   
5096 O O   . HOH D .   ? 0.4355 0.2552 0.4605 0.1818  0.0256  0.0113  766  HOH A O   
5098 O O   . HOH D .   ? 0.2368 0.1565 0.2359 0.0095  -0.0263 -0.0110 768  HOH A O   
5100 O O   . HOH D .   ? 0.5348 0.2209 0.1773 -0.0153 0.0005  0.0612  770  HOH A O   
5102 O O   . HOH D .   ? 0.3432 0.2388 0.5305 0.0239  0.0620  0.1590  772  HOH A O   
5104 O O   . HOH D .   ? 0.5717 0.2676 0.3720 0.0211  -0.0416 0.0293  774  HOH A O   
5106 O O   . HOH D .   ? 0.1814 0.1280 0.1782 0.0219  -0.0736 0.0151  776  HOH A O   
5109 O O   . HOH D .   ? 0.3446 0.3301 0.2942 0.0077  -0.0687 0.0742  779  HOH A O   
5112 O O   . HOH D .   ? 0.5099 0.5475 0.4177 0.1556  -0.0381 0.1543  782  HOH A O   
5114 O O   . HOH D .   ? 0.3185 0.1581 0.1928 0.0262  -0.0256 -0.0212 784  HOH A O   
5118 O O   . HOH D .   ? 0.5232 0.5259 0.6485 -0.2315 0.0016  -0.0008 788  HOH A O   
5119 O O   . HOH D .   ? 0.1901 0.1966 0.1595 -0.0015 -0.0319 0.0194  789  HOH A O   
5120 O O   . HOH D .   ? 0.3507 0.1707 0.2319 0.0991  -0.0784 -0.0006 790  HOH A O   
5121 O O   . HOH D .   ? 0.3100 0.2396 0.4121 0.1246  -0.0035 0.0906  791  HOH A O   
5122 O O   . HOH D .   ? 0.1742 0.1634 0.1563 0.0144  -0.0522 0.0096  792  HOH A O   
5123 O O   . HOH D .   ? 0.2365 0.2582 0.2207 0.0106  -0.0083 0.0076  793  HOH A O   
5125 O O   . HOH D .   ? 0.1718 0.2072 0.2305 -0.0226 -0.0320 0.0103  795  HOH A O   
5128 O O   . HOH D .   ? 0.1998 0.1283 0.1717 0.0314  -0.0440 0.0071  798  HOH A O   
5130 O O   . HOH D .   ? 0.5657 0.4537 0.3888 0.2705  -0.1782 -0.0910 800  HOH A O   
5135 O O   . HOH D .   ? 0.1856 0.1687 0.1899 0.0165  -0.0320 0.0208  804  HOH A O   
5136 O O   . HOH D .   ? 0.3205 0.3467 0.4036 0.0301  -0.0498 0.0751  805  HOH A O   
5140 O O   . HOH D .   ? 0.1708 0.1090 0.1862 0.0101  -0.0619 0.0115  809  HOH A O   
5142 O O   . HOH D .   ? 0.2671 0.4857 0.2789 0.1181  -0.0030 0.0188  811  HOH A O   
5146 O O   . HOH D .   ? 0.2852 0.7140 0.2682 0.0913  0.0010  0.0538  815  HOH A O   
5147 O O   . HOH D .   ? 0.7233 0.3774 0.8077 -0.0520 0.0536  -0.2497 816  HOH A O   
5150 O O   . HOH D .   ? 0.5310 0.1757 0.3511 -0.0575 -0.0670 0.0569  819  HOH A O   
5151 O O   . HOH D .   ? 0.3686 0.1192 0.2344 0.0551  -0.0965 -0.0213 820  HOH A O   
5154 O O   . HOH D .   ? 0.2255 0.1749 0.2357 0.0052  -0.0449 -0.0271 823  HOH A O   
5156 O O   . HOH D .   ? 0.3902 0.2460 0.5182 0.0667  -0.0548 0.0372  825  HOH A O   
5158 O O   . HOH D .   ? 0.4705 0.2986 0.2779 -0.0933 -0.1397 0.0556  827  HOH A O   
5163 O O   . HOH D .   ? 0.3414 0.5701 0.5298 0.1271  -0.1465 -0.1474 832  HOH A O   
5166 O O   . HOH D .   ? 0.2948 0.2418 0.3118 0.0549  -0.1340 0.0706  835  HOH A O   
5167 O O   . HOH D .   ? 0.8191 0.2511 0.3422 -0.0309 0.0181  -0.0665 836  HOH A O   
5168 O O   . HOH D .   ? 1.5764 0.4481 0.4629 0.2241  0.0378  0.0098  837  HOH A O   
5173 O O   . HOH D .   ? 0.4171 0.1634 0.2426 0.0936  -0.1059 -0.0513 842  HOH A O   
5175 O O   . HOH D .   ? 0.2067 0.1428 0.2140 -0.0151 -0.0072 -0.0218 844  HOH A O   
5177 O O   . HOH D .   ? 0.2077 0.1158 0.1854 0.0028  -0.0473 -0.0145 846  HOH A O   
5179 O O   . HOH D .   ? 0.6822 0.2438 0.3834 0.0759  -0.1997 -0.0383 848  HOH A O   
5183 O O   . HOH D .   ? 0.5745 0.3277 0.2626 -0.0208 -0.0879 -0.0515 852  HOH A O   
5184 O O   . HOH D .   ? 0.5286 0.4060 0.2324 0.2068  0.0411  0.0197  853  HOH A O   
5186 O O   . HOH D .   ? 0.2888 0.3548 0.1917 0.0639  -0.0062 0.0160  855  HOH A O   
5187 O O   . HOH D .   ? 0.1834 0.1377 0.2197 0.0209  -0.0247 -0.0111 856  HOH A O   
5197 O O   . HOH D .   ? 0.3692 0.8106 0.3923 -0.1403 0.0035  0.0454  866  HOH A O   
5198 O O   . HOH D .   ? 0.2512 0.3466 0.1580 -0.0873 -0.0672 0.0262  867  HOH A O   
5200 O O   . HOH D .   ? 0.2211 0.2239 0.3136 0.0279  0.0411  0.0494  869  HOH A O   
5201 O O   . HOH D .   ? 0.4206 0.5134 0.2704 -0.0328 0.0882  0.0207  870  HOH A O   
5202 O O   . HOH D .   ? 0.1921 0.3333 0.2174 0.0427  -0.0543 -0.0029 871  HOH A O   
5204 O O   . HOH D .   ? 0.6042 0.8959 0.7147 0.1975  -0.3068 0.1579  873  HOH A O   
5209 O O   . HOH D .   ? 0.3450 0.2998 0.2549 -0.0833 0.0246  -0.0004 878  HOH A O   
5212 O O   . HOH D .   ? 0.2611 0.1672 0.3033 0.0812  -0.0688 0.0103  881  HOH A O   
5213 O O   . HOH D .   ? 0.2122 0.2654 0.1799 -0.0081 -0.0705 0.0322  882  HOH A O   
5215 O O   . HOH D .   ? 0.3231 0.5898 0.6451 0.0564  -0.0927 0.0876  884  HOH A O   
5217 O O   . HOH D .   ? 0.2886 0.4353 0.3118 0.0621  0.0192  0.0683  886  HOH A O   
5225 O O   . HOH D .   ? 0.2720 0.2232 0.3376 -0.0064 0.0416  -0.1092 894  HOH A O   
5227 O O   . HOH D .   ? 0.3421 0.2020 0.1975 0.0806  -0.0503 0.0289  896  HOH A O   
5229 O O   . HOH D .   ? 0.1742 0.1711 0.1575 0.0171  -0.0601 0.0285  898  HOH A O   
5233 O O   . HOH D .   ? 0.2196 0.1896 0.3722 0.0313  -0.0548 0.0398  902  HOH A O   
5236 O O   . HOH D .   ? 0.3969 0.4663 0.3001 0.0520  0.0913  -0.0471 905  HOH A O   
5237 O O   . HOH D .   ? 0.7265 0.3171 0.5441 -0.1865 0.1902  0.0104  906  HOH A O   
5250 O O   . HOH D .   ? 0.2561 0.6328 0.7212 0.0473  -0.0577 -0.0679 918  HOH A O   
5254 O O   . HOH D .   ? 0.3608 0.2052 0.3348 0.0521  -0.0173 0.0785  922  HOH A O   
5255 O O   . HOH D .   ? 0.2341 0.2039 0.2039 -0.0461 -0.0406 0.0066  923  HOH A O   
5256 O O   . HOH D .   ? 0.3674 0.4140 0.5951 0.0444  -0.1143 0.0263  924  HOH A O   
5262 O O   . HOH D .   ? 0.2211 0.2410 0.2188 0.0270  -0.0639 -0.0206 930  HOH A O   
5273 O O   . HOH D .   ? 0.3898 0.8783 0.4447 -0.0502 -0.0792 -0.0995 941  HOH A O   
5280 O O   . HOH D .   ? 0.2257 0.1582 0.2050 -0.0304 -0.0596 0.0211  948  HOH A O   
5281 O O   . HOH D .   ? 0.4227 0.3040 0.4491 0.0050  0.0328  0.0419  949  HOH A O   
5285 O O   . HOH D .   ? 0.8388 0.4134 0.3531 0.2238  -0.1636 -0.0712 953  HOH A O   
5287 O O   . HOH D .   ? 0.2335 0.2403 0.1816 -0.0035 -0.0738 -0.0039 955  HOH A O   
5288 O O   . HOH D .   ? 0.3388 0.2636 0.3250 -0.1004 -0.0345 -0.0030 956  HOH A O   
5289 O O   . HOH D .   ? 0.3725 0.2436 0.3332 0.0025  -0.0408 0.0353  957  HOH A O   
5293 O O   . HOH D .   ? 0.3710 0.3095 0.3286 -0.0684 -0.0827 -0.0539 961  HOH A O   
5295 O O   . HOH D .   ? 0.1955 0.1313 0.1505 0.0046  -0.0668 0.0167  963  HOH A O   
5297 O O   . HOH D .   ? 0.5896 0.3083 0.2266 0.1353  0.0240  -0.0305 965  HOH A O   
5299 O O   . HOH D .   ? 0.6246 0.5778 0.5138 0.3402  0.0352  0.0557  967  HOH A O   
5302 O O   . HOH D .   ? 0.3865 0.5330 0.5575 -0.1720 -0.0303 -0.0392 970  HOH A O   
5303 O O   . HOH D .   ? 0.4758 0.7442 0.5584 0.0379  -0.2278 -0.1961 971  HOH A O   
5304 O O   . HOH D .   ? 0.6583 0.3682 0.3446 0.1184  -0.1446 -0.1569 972  HOH A O   
5305 O O   . HOH D .   ? 0.3899 0.2807 0.2975 0.0224  -0.0039 0.0311  973  HOH A O   
5306 O O   . HOH D .   ? 0.4347 0.2857 0.3330 -0.1380 -0.0447 -0.0265 974  HOH A O   
5309 O O   . HOH D .   ? 0.7715 0.7437 0.5526 0.2835  -0.0772 -0.3110 977  HOH A O   
5310 O O   . HOH D .   ? 0.6942 0.4453 0.9614 -0.1630 0.3550  -0.0775 978  HOH A O   
5319 O O   . HOH D .   ? 0.3921 0.8535 0.8501 0.1652  0.0894  0.4270  987  HOH A O   
5320 O O   . HOH D .   ? 0.3742 0.2359 0.3280 0.0828  0.0088  0.1068  988  HOH A O   
5322 O O   . HOH D .   ? 0.5656 0.6419 0.4291 0.1655  -0.0843 -0.0322 990  HOH A O   
5327 O O   . HOH D .   ? 0.3289 0.2639 0.2195 0.0318  -0.0009 0.0142  995  HOH A O   
5331 O O   . HOH D .   ? 0.2906 0.1805 0.2113 -0.0025 -0.0471 0.0393  999  HOH A O   
5343 O O   . HOH D .   ? 0.4106 0.2013 0.3135 -0.0354 -0.1848 0.0158  1010 HOH A O   
5345 O O   . HOH D .   ? 0.4214 0.2733 0.4933 0.0530  -0.0470 0.0513  1012 HOH A O   
5346 O O   . HOH D .   ? 0.4921 0.2235 0.3459 0.1122  0.1272  -0.0071 1013 HOH A O   
5357 O O   . HOH D .   ? 0.4405 0.3389 0.4271 -0.0764 0.0836  -0.0957 1024 HOH A O   
5374 O O   . HOH D .   ? 0.5319 0.2246 0.5601 -0.0676 -0.2386 0.0111  1041 HOH A O   
5389 O O   . HOH D .   ? 0.2461 0.2675 0.2824 0.0074  -0.0349 -0.0184 1055 HOH A O   
5399 O O   . HOH D .   ? 0.4056 0.4829 0.5752 0.0031  -0.0621 -0.1492 1064 HOH A O   
5400 O O   . HOH D .   ? 0.4078 0.7234 0.8307 0.1428  0.1899  -0.1893 1065 HOH A O   
5416 O O   . HOH D .   ? 0.7381 0.4290 0.5375 0.0239  -0.1219 -0.0021 1081 HOH A O   
5423 O O   . HOH D .   ? 0.5766 0.2954 0.2939 0.0085  -0.1180 0.0500  1088 HOH A O   
5426 O O   . HOH D .   ? 0.3813 0.3670 0.7656 0.0305  -0.1385 0.0590  1091 HOH A O   
5432 O O   . HOH D .   ? 0.4582 0.4824 1.0528 0.1869  0.1221  0.1493  1097 HOH A O   
5437 O O   . HOH D .   ? 0.3762 0.3163 0.2587 -0.0321 -0.0971 -0.0260 1102 HOH A O   
5441 O O   . HOH D .   ? 0.2869 0.2086 0.3214 -0.0204 -0.0790 0.0472  1106 HOH A O   
5452 O O   . HOH D .   ? 0.8038 0.4901 1.1087 -0.0148 0.4120  -0.0959 1117 HOH A O   
5461 O O   . HOH D .   ? 0.9807 0.2757 0.4224 -0.0475 0.0104  -0.0508 1126 HOH A O   
5472 O O   . HOH D .   ? 0.4742 0.2732 1.0644 0.0142  0.0256  0.0622  1137 HOH A O   
5477 O O   . HOH D .   ? 0.5269 0.3488 0.6465 -0.0413 -0.2628 0.1842  1142 HOH A O   
5479 O O   . HOH D .   ? 0.6211 0.7279 0.3506 0.1680  -0.1194 0.1619  1144 HOH A O   
5528 O O   . HOH E .   ? 0.5624 0.8273 0.3756 -0.2210 -0.0540 -0.1720 605  HOH B O   
5531 O O   . HOH E .   ? 0.5077 0.3201 0.3830 0.0565  -0.0878 -0.0017 608  HOH B O   
5533 O O   . HOH E .   ? 0.2175 0.3708 0.3742 0.0005  -0.0178 0.0901  610  HOH B O   
5540 O O   . HOH E .   ? 0.2447 0.2345 0.2949 0.0326  -0.0401 0.0092  617  HOH B O   
5548 O O   . HOH E .   ? 0.7316 0.3175 0.3254 0.1913  -0.1344 -0.0160 625  HOH B O   
5554 O O   . HOH E .   ? 0.6102 0.5647 0.6981 0.2738  -0.2256 -0.2321 631  HOH B O   
5556 O O   . HOH E .   ? 0.7267 0.6433 0.8179 0.2606  -0.3764 -0.0653 633  HOH B O   
5558 O O   . HOH E .   ? 0.2861 0.6100 0.3358 -0.1589 0.0047  -0.0406 635  HOH B O   
5567 O O   . HOH E .   ? 0.4957 0.2962 0.6211 0.0171  -0.0194 -0.0005 643  HOH B O   
5572 O O   . HOH E .   ? 0.9798 0.7938 0.5980 -0.1206 -0.4178 -0.0145 647  HOH B O   
5574 O O   . HOH E .   ? 0.2013 0.2648 0.3242 0.0050  -0.1354 -0.0282 649  HOH B O   
5576 O O   . HOH E .   ? 0.4745 0.2424 0.3168 -0.0144 -0.1109 -0.0367 651  HOH B O   
5581 O O   . HOH E .   ? 0.1943 0.0983 0.2364 0.0094  -0.0799 0.0081  656  HOH B O   
5583 O O   . HOH E .   ? 0.3408 0.1944 0.2037 0.0285  -0.0328 -0.0368 658  HOH B O   
5584 O O   . HOH E .   ? 0.6069 0.2699 0.4012 0.1243  -0.2252 -0.0109 659  HOH B O   
5589 O O   . HOH E .   ? 0.5580 0.4083 0.4747 0.2340  -0.1488 -0.1812 663  HOH B O   
5591 O O   . HOH E .   ? 0.3876 0.1999 0.2662 -0.0213 -0.1318 0.0545  665  HOH B O   
5593 O O   . HOH E .   ? 0.2379 0.3486 0.1752 -0.0452 -0.0731 0.0291  667  HOH B O   
5595 O O   . HOH E .   ? 0.2120 0.1032 0.1496 -0.0106 -0.0685 -0.0241 669  HOH B O   
5600 O O   . HOH E .   ? 0.5093 0.3247 0.1771 -0.0720 -0.0633 -0.0181 674  HOH B O   
5601 O O   . HOH E .   ? 0.3167 0.3563 0.3994 0.0372  -0.0481 0.0843  675  HOH B O   
5602 O O   . HOH E .   ? 0.4563 0.3310 0.1711 0.0011  -0.0321 -0.0432 676  HOH B O   
5603 O O   . HOH E .   ? 0.2410 0.1611 0.2234 -0.0192 -0.0357 -0.0081 677  HOH B O   
5604 O O   . HOH E .   ? 0.3342 0.2688 0.3163 0.0702  -0.0250 0.0353  678  HOH B O   
5605 O O   . HOH E .   ? 0.4820 0.3338 0.4794 -0.0816 -0.0399 -0.1820 679  HOH B O   
5606 O O   . HOH E .   ? 0.1444 0.1387 0.1868 0.0017  -0.0449 -0.0202 680  HOH B O   
5607 O O   . HOH E .   ? 0.4132 0.1519 0.3217 -0.0030 -0.2010 0.0177  681  HOH B O   
5608 O O   . HOH E .   ? 0.4790 0.3656 0.2607 0.0254  -0.0577 0.0905  682  HOH B O   
5613 O O   . HOH E .   ? 0.3241 0.3316 0.3057 -0.0613 -0.0685 -0.0024 686  HOH B O   
5615 O O   . HOH E .   ? 0.1985 0.1140 0.1993 -0.0072 -0.0792 0.0017  688  HOH B O   
5619 O O   . HOH E .   ? 0.7960 0.6060 0.3826 -0.3387 -0.0984 -0.0420 692  HOH B O   
5620 O O   . HOH E .   ? 0.2108 0.1682 0.2055 -0.0044 -0.0843 -0.0313 693  HOH B O   
5621 O O   . HOH E .   ? 0.6893 0.2439 0.4389 -0.0700 -0.1333 -0.0187 694  HOH B O   
5627 O O   . HOH E .   ? 0.3379 0.4593 0.2445 -0.0011 -0.0299 -0.0136 700  HOH B O   
5629 O O   . HOH E .   ? 0.2868 0.1838 0.2043 -0.0028 -0.0389 -0.0194 702  HOH B O   
5632 O O   . HOH E .   ? 0.6155 0.7281 0.4853 0.0685  0.0491  0.2074  705  HOH B O   
5634 O O   . HOH E .   ? 0.3785 0.3161 0.2306 -0.0081 -0.0346 -0.0370 707  HOH B O   
5635 O O   . HOH E .   ? 0.2968 0.2185 0.2862 -0.0194 -0.0341 0.0417  708  HOH B O   
5637 O O   . HOH E .   ? 0.2047 0.1104 0.1711 -0.0203 -0.0628 0.0214  710  HOH B O   
5640 O O   . HOH E .   ? 0.3655 0.2533 0.2389 0.0577  -0.0031 -0.0315 712  HOH B O   
5641 O O   . HOH E .   ? 0.6324 0.4453 0.8681 -0.2058 -0.3282 0.1054  713  HOH B O   
5642 O O   . HOH E .   ? 0.2356 0.1270 0.1429 -0.0097 -0.0507 0.0085  714  HOH B O   
5643 O O   . HOH E .   ? 0.3996 0.1597 0.2909 -0.0047 -0.1971 0.0143  715  HOH B O   
5644 O O   . HOH E .   ? 0.3871 0.2106 0.3172 -0.0674 -0.1700 0.0409  716  HOH B O   
5645 O O   . HOH E .   ? 0.2494 0.0942 0.2162 0.0059  -0.0493 -0.0098 717  HOH B O   
5647 O O   . HOH E .   ? 0.2404 0.1863 0.1575 0.0237  -0.0617 0.0188  719  HOH B O   
5653 O O   . HOH E .   ? 0.3753 0.3248 0.3378 0.1265  -0.1636 -0.0605 725  HOH B O   
5661 O O   . HOH E .   ? 0.3259 0.1584 0.2949 0.0093  -0.0656 -0.0828 732  HOH B O   
5663 O O   . HOH E .   ? 0.2483 0.2854 0.2395 -0.0662 -0.0034 -0.0471 734  HOH B O   
5664 O O   . HOH E .   ? 0.1954 0.1336 0.2291 0.0073  -0.0515 0.0300  735  HOH B O   
5667 O O   . HOH E .   ? 0.3410 0.2461 0.3037 0.0055  -0.0914 -0.0061 738  HOH B O   
5668 O O   . HOH E .   ? 0.1590 0.1031 0.1737 -0.0023 -0.0337 0.0013  739  HOH B O   
5671 O O   . HOH E .   ? 0.3517 0.2165 0.3114 0.0348  -0.0859 -0.0873 742  HOH B O   
5672 O O   . HOH E .   ? 0.1736 0.1035 0.1874 -0.0056 -0.0449 0.0026  743  HOH B O   
5673 O O   . HOH E .   ? 0.2205 0.1169 0.3105 -0.0267 -0.1334 0.0337  744  HOH B O   
5675 O O   . HOH E .   ? 0.2875 0.2828 0.4753 -0.0722 -0.0103 0.0029  746  HOH B O   
5678 O O   . HOH E .   ? 0.3933 0.2543 0.8257 -0.0121 -0.1763 0.0758  749  HOH B O   
5679 O O   . HOH E .   ? 0.5263 0.3276 0.2144 0.0604  0.0265  -0.0684 750  HOH B O   
5680 O O   . HOH E .   ? 0.2469 0.1861 0.2660 -0.0326 -0.0869 -0.0124 751  HOH B O   
5681 O O   . HOH E .   ? 0.2378 0.1339 0.4253 -0.0137 -0.0730 -0.0606 752  HOH B O   
5682 O O   . HOH E .   ? 0.2004 0.1290 0.1936 -0.0051 -0.0473 0.0019  753  HOH B O   
5683 O O   . HOH E .   ? 0.3769 0.3824 0.5593 -0.0160 -0.0837 -0.1480 754  HOH B O   
5687 O O   . HOH E .   ? 0.2568 0.1480 0.2150 -0.0293 -0.0488 -0.0110 758  HOH B O   
5688 O O   . HOH E .   ? 0.6986 0.5210 0.4779 0.2030  0.0232  -0.2284 759  HOH B O   
5691 O O   . HOH E .   ? 0.3989 0.2049 0.3197 0.0519  -0.1018 -0.0659 762  HOH B O   
5694 O O   . HOH E .   ? 0.1977 0.1345 0.1865 0.0146  -0.0689 -0.0025 765  HOH B O   
5695 O O   . HOH E .   ? 0.2204 0.1569 0.2093 0.0148  -0.0685 -0.0215 766  HOH B O   
5699 O O   . HOH E .   ? 0.3211 0.2077 0.3286 0.1363  -0.0466 0.0322  770  HOH B O   
5700 O O   . HOH E .   ? 0.3631 0.2125 0.1889 0.0184  -0.0699 -0.0303 771  HOH B O   
5704 O O   . HOH E .   ? 0.6866 0.2745 0.4400 0.0922  0.1287  0.0996  775  HOH B O   
5705 O O   . HOH E .   ? 0.3393 0.1900 0.3060 -0.0067 -0.0324 0.0777  776  HOH B O   
5706 O O   . HOH E .   ? 0.2544 0.3412 0.4887 0.0646  -0.0860 -0.1697 777  HOH B O   
5707 O O   . HOH E .   ? 0.3396 0.4199 0.3727 0.0688  0.1323  -0.0604 778  HOH B O   
5712 O O   . HOH E .   ? 0.2368 0.2080 0.2151 0.0388  -0.0376 -0.0254 783  HOH B O   
5715 O O   . HOH E .   ? 0.6054 0.2480 0.5430 -0.0158 0.0501  0.0858  786  HOH B O   
5716 O O   . HOH E .   ? 0.3686 0.2571 0.1995 -0.1235 -0.1289 0.0504  787  HOH B O   
5720 O O   . HOH E .   ? 0.2202 0.1623 0.2362 0.0104  -0.0162 0.0608  791  HOH B O   
5721 O O   . HOH E .   ? 0.2473 0.1597 0.2254 -0.0035 -0.1092 -0.0277 792  HOH B O   
5722 O O   . HOH E .   ? 0.2399 0.1384 0.2097 -0.0219 -0.0482 -0.0274 793  HOH B O   
5725 O O   . HOH E .   ? 0.2427 0.1258 0.2039 -0.0140 -0.0885 0.0051  796  HOH B O   
5733 O O   . HOH E .   ? 0.3664 0.2787 0.4530 -0.0205 -0.0990 0.0887  804  HOH B O   
5737 O O   . HOH E .   ? 0.3429 0.7219 0.9855 0.0889  0.1119  0.2219  808  HOH B O   
5740 O O   . HOH E .   ? 0.2639 0.1706 0.1945 -0.0127 -0.0422 0.0051  811  HOH B O   
5745 O O   . HOH E .   ? 0.5054 0.4905 0.4105 -0.1378 -0.2376 -0.0053 816  HOH B O   
5747 O O   . HOH E .   ? 0.6881 0.5108 0.3049 0.2445  0.0062  -0.1182 818  HOH B O   
5750 O O   . HOH E .   ? 0.2450 0.2308 0.2328 -0.0181 -0.0279 0.0082  820  HOH B O   
5751 O O   . HOH E .   ? 0.2258 0.2766 0.1858 -0.0014 -0.0518 -0.0894 821  HOH B O   
5752 O O   . HOH E .   ? 0.2237 0.1720 0.3535 0.0163  -0.0418 -0.0455 822  HOH B O   
5760 O O   . HOH E .   ? 0.2898 0.3815 0.4208 -0.0351 0.0654  0.0093  830  HOH B O   
5761 O O   . HOH E .   ? 0.3720 0.3596 0.3482 0.1192  -0.0991 -0.0234 831  HOH B O   
5763 O O   . HOH E .   ? 0.4217 0.5711 0.6685 -0.1428 -0.2460 -0.0596 833  HOH B O   
5764 O O   . HOH E .   ? 0.3784 0.1979 0.2415 -0.0373 0.0083  -0.0155 834  HOH B O   
5768 O O   . HOH E .   ? 0.3658 0.3144 0.3009 0.1503  0.0246  0.1292  838  HOH B O   
5780 O O   . HOH E .   ? 0.3487 0.4164 0.1979 -0.1269 -0.0424 0.0611  849  HOH B O   
5781 O O   . HOH E .   ? 0.8786 0.4612 0.5937 -0.1802 -0.1157 -0.0061 850  HOH B O   
5784 O O   . HOH E .   ? 0.4219 0.3225 0.6019 0.0888  -0.1249 -0.1312 853  HOH B O   
5788 O O   . HOH E .   ? 0.3706 0.2386 0.3624 0.0490  0.0014  0.0200  857  HOH B O   
5789 O O   . HOH E .   ? 0.3022 0.1658 0.2218 0.0134  -0.0308 -0.0407 858  HOH B O   
5791 O O   . HOH E .   ? 0.3291 0.1908 0.4942 0.0625  -0.0274 0.1089  860  HOH B O   
5796 O O   . HOH E .   ? 0.4378 0.1986 0.3613 0.0898  -0.1690 -0.0295 865  HOH B O   
5798 O O   . HOH E .   ? 0.2685 0.2694 0.4753 -0.0436 -0.1085 -0.0607 867  HOH B O   
5800 O O   . HOH E .   ? 0.1648 0.1078 0.2013 -0.0125 -0.0343 0.0027  869  HOH B O   
5801 O O   . HOH E .   ? 0.2015 0.2986 0.3823 0.0250  -0.0501 -0.0758 870  HOH B O   
5802 O O   . HOH E .   ? 0.4127 0.3120 0.2781 0.1196  -0.0437 -0.0378 871  HOH B O   
5803 O O   . HOH E .   ? 0.4157 0.1987 0.3387 -0.0590 -0.1550 0.0528  872  HOH B O   
5806 O O   . HOH E .   ? 0.3346 0.1763 0.1954 0.0030  -0.0238 0.0019  875  HOH B O   
5813 O O   . HOH E .   ? 0.2761 0.1718 0.1963 0.0114  -0.0323 -0.0212 882  HOH B O   
5815 O O   . HOH E .   ? 0.4804 0.7293 0.3648 -0.3098 -0.1029 0.0434  884  HOH B O   
5816 O O   . HOH E .   ? 0.2910 0.2980 0.5786 0.1209  -0.0624 -0.0370 885  HOH B O   
5821 O O   . HOH E .   ? 0.4854 0.8270 0.4138 -0.0051 -0.0524 0.0060  890  HOH B O   
5824 O O   . HOH E .   ? 0.3749 0.4304 0.3313 0.0415  -0.0371 0.1151  893  HOH B O   
5829 O O   . HOH E .   ? 0.4076 0.2712 0.3983 0.0940  -0.1886 -0.0130 898  HOH B O   
5830 O O   . HOH E .   ? 0.4266 0.5028 0.4683 -0.0002 0.0606  -0.0521 899  HOH B O   
5853 O O   . HOH E .   ? 0.2576 0.1500 0.2104 0.0329  0.0126  0.0355  922  HOH B O   
5860 O O   . HOH E .   ? 0.4080 0.2192 0.3891 -0.0361 -0.0038 -0.0189 929  HOH B O   
5876 O O   . HOH E .   ? 0.6784 0.3927 0.6231 0.1332  -0.0855 0.0864  945  HOH B O   
5877 O O   . HOH E .   ? 0.3822 0.3689 0.5065 -0.0117 -0.0440 -0.0801 946  HOH B O   
5892 O O   . HOH E .   ? 0.7681 0.6460 0.7549 -0.2356 0.0233  -0.3506 959  HOH B O   
5910 O O   . HOH E .   ? 0.4288 0.3437 0.5410 0.0217  -0.1526 0.0093  976  HOH B O   
5912 O O   . HOH E .   ? 0.7103 0.4298 0.2932 0.0846  -0.0012 0.0091  978  HOH B O   
5932 O O   . HOH E .   ? 0.8760 0.2662 0.5935 -0.1070 -0.1285 0.0811  998  HOH B O   
5942 O O   . HOH E .   ? 0.4615 0.4623 0.2839 -0.1106 -0.0328 -0.0729 1008 HOH B O   
5952 O O   . HOH E .   ? 0.3368 0.8480 0.9082 0.1321  -0.0994 0.1089  1018 HOH B O   
5956 O O   . HOH E .   ? 1.0388 0.3389 0.5065 0.1484  0.0049  0.0547  1022 HOH B O   
5958 O O   . HOH E .   ? 0.5040 0.6753 0.2864 -0.1489 -0.0030 -0.0183 1024 HOH B O   
5959 O O   . HOH E .   ? 0.2661 0.3067 0.7219 0.0698  -0.0358 0.0683  1025 HOH B O   
5961 O O   . HOH E .   ? 0.6586 0.6062 0.2351 -0.1619 -0.0215 0.0802  1027 HOH B O   
5970 O O   . HOH E .   ? 0.6760 0.4800 0.6968 0.2131  -0.3054 -0.0296 1036 HOH B O   
5975 O O   . HOH E .   ? 1.1091 0.4503 0.4737 0.0888  0.0751  0.1441  1041 HOH B O   
5977 O O   . HOH E .   ? 0.9117 0.3857 0.5265 -0.0558 -0.2161 0.1113  1043 HOH B O   
# 
