data_9JQF
# 
_entry.id   9JQF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   9JQF         pdb_00009jqf 10.2210/pdb9jqf/pdb 
WWPDB D_1300051974 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JQF 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sungil@kangwon.ac.kr 
_pdbx_contact_author.name_first         Sung-il 
_pdbx_contact_author.name_last          Yoon 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0777-0457 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ki, D.U.'   1 ? 
'Choi, H.J.' 2 ? 
'Song, W.S.' 3 ? 
'Yoon, S.I.' 4 ? 
# 
_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            Biochem.Biophys.Res.Commun. 
_citation.journal_id_ASTM           BBRCA9 
_citation.journal_id_CSD            0146 
_citation.journal_id_ISSN           1090-2104 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            735 
_citation.language                  ? 
_citation.page_first                150810 
_citation.page_last                 150810 
_citation.title                     'Structural analysis of the CJ0600 protein from Campylobacter jejuni.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bbrc.2024.150810 
_citation.pdbx_database_id_PubMed   39418773 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ki, D.U.'   1 ? 
primary 'Choi, H.J.' 2 ? 
primary 'Song, W.S.' 3 ? 
primary 'Yoon, S.I.' 4 ? 
# 
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 '1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase' 34246.398 1   ? ? ? ? 
2 non-polymer syn 'SULFATE ION'                                                          96.063    3   ? ? ? ? 
3 water       nat water                                                                  18.015    141 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        CJ0600 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;GSAKDPLNFIKTISPIQKINFNGFEFYIKRDDLLGEINGN(LLP)ARKLAFYIHQRYPKNQSFVSYGGSQSNALAALSIF
AKQRSYKLVFACEKISTFLKNNPCGNYALALENGVDFVENIHSLSLKQFALSLCKKDDVFIEQGIANLEAQYGYMELAQE
IQMQSQSLKLDFDIFLPSGTGTSAAFLAKYSKFKVFTCACVGDIKYLKKQILTLDPSYDFSNLEFLTSDKKYHFAKPYKE
FYELYMDLKLKCNIEFDLLYDILGLSIALKQEWKKPLLYIHQGGILGNSTMLERYKFKKSV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSAKDPLNFIKTISPIQKINFNGFEFYIKRDDLLGEINGNKARKLAFYIHQRYPKNQSFVSYGGSQSNALAALSIFAKQR
SYKLVFACEKISTFLKNNPCGNYALALENGVDFVENIHSLSLKQFALSLCKKDDVFIEQGIANLEAQYGYMELAQEIQMQ
SQSLKLDFDIFLPSGTGTSAAFLAKYSKFKVFTCACVGDIKYLKKQILTLDPSYDFSNLEFLTSDKKYHFAKPYKEFYEL
YMDLKLKCNIEFDLLYDILGLSIALKQEWKKPLLYIHQGGILGNSTMLERYKFKKSV
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   ALA n 
1 4   LYS n 
1 5   ASP n 
1 6   PRO n 
1 7   LEU n 
1 8   ASN n 
1 9   PHE n 
1 10  ILE n 
1 11  LYS n 
1 12  THR n 
1 13  ILE n 
1 14  SER n 
1 15  PRO n 
1 16  ILE n 
1 17  GLN n 
1 18  LYS n 
1 19  ILE n 
1 20  ASN n 
1 21  PHE n 
1 22  ASN n 
1 23  GLY n 
1 24  PHE n 
1 25  GLU n 
1 26  PHE n 
1 27  TYR n 
1 28  ILE n 
1 29  LYS n 
1 30  ARG n 
1 31  ASP n 
1 32  ASP n 
1 33  LEU n 
1 34  LEU n 
1 35  GLY n 
1 36  GLU n 
1 37  ILE n 
1 38  ASN n 
1 39  GLY n 
1 40  ASN n 
1 41  LLP n 
1 42  ALA n 
1 43  ARG n 
1 44  LYS n 
1 45  LEU n 
1 46  ALA n 
1 47  PHE n 
1 48  TYR n 
1 49  ILE n 
1 50  HIS n 
1 51  GLN n 
1 52  ARG n 
1 53  TYR n 
1 54  PRO n 
1 55  LYS n 
1 56  ASN n 
1 57  GLN n 
1 58  SER n 
1 59  PHE n 
1 60  VAL n 
1 61  SER n 
1 62  TYR n 
1 63  GLY n 
1 64  GLY n 
1 65  SER n 
1 66  GLN n 
1 67  SER n 
1 68  ASN n 
1 69  ALA n 
1 70  LEU n 
1 71  ALA n 
1 72  ALA n 
1 73  LEU n 
1 74  SER n 
1 75  ILE n 
1 76  PHE n 
1 77  ALA n 
1 78  LYS n 
1 79  GLN n 
1 80  ARG n 
1 81  SER n 
1 82  TYR n 
1 83  LYS n 
1 84  LEU n 
1 85  VAL n 
1 86  PHE n 
1 87  ALA n 
1 88  CYS n 
1 89  GLU n 
1 90  LYS n 
1 91  ILE n 
1 92  SER n 
1 93  THR n 
1 94  PHE n 
1 95  LEU n 
1 96  LYS n 
1 97  ASN n 
1 98  ASN n 
1 99  PRO n 
1 100 CYS n 
1 101 GLY n 
1 102 ASN n 
1 103 TYR n 
1 104 ALA n 
1 105 LEU n 
1 106 ALA n 
1 107 LEU n 
1 108 GLU n 
1 109 ASN n 
1 110 GLY n 
1 111 VAL n 
1 112 ASP n 
1 113 PHE n 
1 114 VAL n 
1 115 GLU n 
1 116 ASN n 
1 117 ILE n 
1 118 HIS n 
1 119 SER n 
1 120 LEU n 
1 121 SER n 
1 122 LEU n 
1 123 LYS n 
1 124 GLN n 
1 125 PHE n 
1 126 ALA n 
1 127 LEU n 
1 128 SER n 
1 129 LEU n 
1 130 CYS n 
1 131 LYS n 
1 132 LYS n 
1 133 ASP n 
1 134 ASP n 
1 135 VAL n 
1 136 PHE n 
1 137 ILE n 
1 138 GLU n 
1 139 GLN n 
1 140 GLY n 
1 141 ILE n 
1 142 ALA n 
1 143 ASN n 
1 144 LEU n 
1 145 GLU n 
1 146 ALA n 
1 147 GLN n 
1 148 TYR n 
1 149 GLY n 
1 150 TYR n 
1 151 MET n 
1 152 GLU n 
1 153 LEU n 
1 154 ALA n 
1 155 GLN n 
1 156 GLU n 
1 157 ILE n 
1 158 GLN n 
1 159 MET n 
1 160 GLN n 
1 161 SER n 
1 162 GLN n 
1 163 SER n 
1 164 LEU n 
1 165 LYS n 
1 166 LEU n 
1 167 ASP n 
1 168 PHE n 
1 169 ASP n 
1 170 ILE n 
1 171 PHE n 
1 172 LEU n 
1 173 PRO n 
1 174 SER n 
1 175 GLY n 
1 176 THR n 
1 177 GLY n 
1 178 THR n 
1 179 SER n 
1 180 ALA n 
1 181 ALA n 
1 182 PHE n 
1 183 LEU n 
1 184 ALA n 
1 185 LYS n 
1 186 TYR n 
1 187 SER n 
1 188 LYS n 
1 189 PHE n 
1 190 LYS n 
1 191 VAL n 
1 192 PHE n 
1 193 THR n 
1 194 CYS n 
1 195 ALA n 
1 196 CYS n 
1 197 VAL n 
1 198 GLY n 
1 199 ASP n 
1 200 ILE n 
1 201 LYS n 
1 202 TYR n 
1 203 LEU n 
1 204 LYS n 
1 205 LYS n 
1 206 GLN n 
1 207 ILE n 
1 208 LEU n 
1 209 THR n 
1 210 LEU n 
1 211 ASP n 
1 212 PRO n 
1 213 SER n 
1 214 TYR n 
1 215 ASP n 
1 216 PHE n 
1 217 SER n 
1 218 ASN n 
1 219 LEU n 
1 220 GLU n 
1 221 PHE n 
1 222 LEU n 
1 223 THR n 
1 224 SER n 
1 225 ASP n 
1 226 LYS n 
1 227 LYS n 
1 228 TYR n 
1 229 HIS n 
1 230 PHE n 
1 231 ALA n 
1 232 LYS n 
1 233 PRO n 
1 234 TYR n 
1 235 LYS n 
1 236 GLU n 
1 237 PHE n 
1 238 TYR n 
1 239 GLU n 
1 240 LEU n 
1 241 TYR n 
1 242 MET n 
1 243 ASP n 
1 244 LEU n 
1 245 LYS n 
1 246 LEU n 
1 247 LYS n 
1 248 CYS n 
1 249 ASN n 
1 250 ILE n 
1 251 GLU n 
1 252 PHE n 
1 253 ASP n 
1 254 LEU n 
1 255 LEU n 
1 256 TYR n 
1 257 ASP n 
1 258 ILE n 
1 259 LEU n 
1 260 GLY n 
1 261 LEU n 
1 262 SER n 
1 263 ILE n 
1 264 ALA n 
1 265 LEU n 
1 266 LYS n 
1 267 GLN n 
1 268 GLU n 
1 269 TRP n 
1 270 LYS n 
1 271 LYS n 
1 272 PRO n 
1 273 LEU n 
1 274 LEU n 
1 275 TYR n 
1 276 ILE n 
1 277 HIS n 
1 278 GLN n 
1 279 GLY n 
1 280 GLY n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 ASN n 
1 285 SER n 
1 286 THR n 
1 287 MET n 
1 288 LEU n 
1 289 GLU n 
1 290 ARG n 
1 291 TYR n 
1 292 LYS n 
1 293 PHE n 
1 294 LYS n 
1 295 LYS n 
1 296 SER n 
1 297 VAL n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   297 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'F0E97_00965, FZK63_02140, QE916_000133' 
_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      'Campylobacter jejuni' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     197 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                                 
?                                      'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                                                                                
?                                      'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                              
?                                      'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                                         
?                                      'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                                                
?                                      'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                                               
?                                      'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                         
?                                      'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                                                                                                 
?                                      'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                               
?                                      'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                                                                                                   
?                                      'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                              
?                                      'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                                 
?                                      'C6 H13 N O2'     131.173 
LLP 'L-peptide linking' n '(2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid' 
"N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE" 'C14 H22 N3 O7 P' 375.314 
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 
SO4 non-polymer         . 'SULFATE ION'                                                                                           
?                                      'O4 S -2'         96.063  
THR 'L-peptide linking' y THREONINE                                                                                               
?                                      'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                              
?                                      'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                                
?                                      'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                                                                                                  
?                                      'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_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   GLY 1   -5  ?   ?   ?   A . n 
A 1 2   SER 2   -4  ?   ?   ?   A . n 
A 1 3   ALA 3   -3  ?   ?   ?   A . n 
A 1 4   LYS 4   -2  ?   ?   ?   A . n 
A 1 5   ASP 5   -1  ?   ?   ?   A . n 
A 1 6   PRO 6   0   ?   ?   ?   A . n 
A 1 7   LEU 7   1   ?   ?   ?   A . n 
A 1 8   ASN 8   2   2   ASN ASN A . n 
A 1 9   PHE 9   3   3   PHE PHE A . n 
A 1 10  ILE 10  4   4   ILE ILE A . n 
A 1 11  LYS 11  5   5   LYS LYS A . n 
A 1 12  THR 12  6   6   THR THR A . n 
A 1 13  ILE 13  7   7   ILE ILE A . n 
A 1 14  SER 14  8   8   SER SER A . n 
A 1 15  PRO 15  9   9   PRO PRO A . n 
A 1 16  ILE 16  10  10  ILE ILE A . n 
A 1 17  GLN 17  11  11  GLN GLN A . n 
A 1 18  LYS 18  12  12  LYS LYS A . n 
A 1 19  ILE 19  13  13  ILE ILE A . n 
A 1 20  ASN 20  14  14  ASN ASN A . n 
A 1 21  PHE 21  15  15  PHE PHE A . n 
A 1 22  ASN 22  16  16  ASN ASN A . n 
A 1 23  GLY 23  17  17  GLY GLY A . n 
A 1 24  PHE 24  18  18  PHE PHE A . n 
A 1 25  GLU 25  19  19  GLU GLU A . n 
A 1 26  PHE 26  20  20  PHE PHE A . n 
A 1 27  TYR 27  21  21  TYR TYR A . n 
A 1 28  ILE 28  22  22  ILE ILE A . n 
A 1 29  LYS 29  23  23  LYS LYS A . n 
A 1 30  ARG 30  24  24  ARG ARG A . n 
A 1 31  ASP 31  25  25  ASP ASP A . n 
A 1 32  ASP 32  26  26  ASP ASP A . n 
A 1 33  LEU 33  27  27  LEU LEU A . n 
A 1 34  LEU 34  28  28  LEU LEU A . n 
A 1 35  GLY 35  29  29  GLY GLY A . n 
A 1 36  GLU 36  30  30  GLU GLU A . n 
A 1 37  ILE 37  31  31  ILE ILE A . n 
A 1 38  ASN 38  32  32  ASN ASN A . n 
A 1 39  GLY 39  33  33  GLY GLY A . n 
A 1 40  ASN 40  34  34  ASN ASN A . n 
A 1 41  LLP 41  35  35  LLP LLP A . n 
A 1 42  ALA 42  36  36  ALA ALA A . n 
A 1 43  ARG 43  37  37  ARG ARG A . n 
A 1 44  LYS 44  38  38  LYS LYS A . n 
A 1 45  LEU 45  39  39  LEU LEU A . n 
A 1 46  ALA 46  40  40  ALA ALA A . n 
A 1 47  PHE 47  41  41  PHE PHE A . n 
A 1 48  TYR 48  42  42  TYR TYR A . n 
A 1 49  ILE 49  43  43  ILE ILE A . n 
A 1 50  HIS 50  44  44  HIS HIS A . n 
A 1 51  GLN 51  45  45  GLN GLN A . n 
A 1 52  ARG 52  46  46  ARG ARG A . n 
A 1 53  TYR 53  47  47  TYR TYR A . n 
A 1 54  PRO 54  48  48  PRO PRO A . n 
A 1 55  LYS 55  49  49  LYS LYS A . n 
A 1 56  ASN 56  50  50  ASN ASN A . n 
A 1 57  GLN 57  51  51  GLN GLN A . n 
A 1 58  SER 58  52  52  SER SER A . n 
A 1 59  PHE 59  53  53  PHE PHE A . n 
A 1 60  VAL 60  54  54  VAL VAL A . n 
A 1 61  SER 61  55  55  SER SER A . n 
A 1 62  TYR 62  56  56  TYR TYR A . n 
A 1 63  GLY 63  57  57  GLY GLY A . n 
A 1 64  GLY 64  58  58  GLY GLY A . n 
A 1 65  SER 65  59  59  SER SER A . n 
A 1 66  GLN 66  60  60  GLN GLN A . n 
A 1 67  SER 67  61  61  SER SER A . n 
A 1 68  ASN 68  62  62  ASN ASN A . n 
A 1 69  ALA 69  63  63  ALA ALA A . n 
A 1 70  LEU 70  64  64  LEU LEU A . n 
A 1 71  ALA 71  65  65  ALA ALA A . n 
A 1 72  ALA 72  66  66  ALA ALA A . n 
A 1 73  LEU 73  67  67  LEU LEU A . n 
A 1 74  SER 74  68  68  SER SER A . n 
A 1 75  ILE 75  69  69  ILE ILE A . n 
A 1 76  PHE 76  70  70  PHE PHE A . n 
A 1 77  ALA 77  71  71  ALA ALA A . n 
A 1 78  LYS 78  72  72  LYS LYS A . n 
A 1 79  GLN 79  73  73  GLN GLN A . n 
A 1 80  ARG 80  74  74  ARG ARG A . n 
A 1 81  SER 81  75  75  SER SER A . n 
A 1 82  TYR 82  76  76  TYR TYR A . n 
A 1 83  LYS 83  77  77  LYS LYS A . n 
A 1 84  LEU 84  78  78  LEU LEU A . n 
A 1 85  VAL 85  79  79  VAL VAL A . n 
A 1 86  PHE 86  80  80  PHE PHE A . n 
A 1 87  ALA 87  81  81  ALA ALA A . n 
A 1 88  CYS 88  82  82  CYS CYS A . n 
A 1 89  GLU 89  83  83  GLU GLU A . n 
A 1 90  LYS 90  84  84  LYS LYS A . n 
A 1 91  ILE 91  85  85  ILE ILE A . n 
A 1 92  SER 92  86  86  SER SER A . n 
A 1 93  THR 93  87  87  THR THR A . n 
A 1 94  PHE 94  88  88  PHE PHE A . n 
A 1 95  LEU 95  89  89  LEU LEU A . n 
A 1 96  LYS 96  90  90  LYS LYS A . n 
A 1 97  ASN 97  91  91  ASN ASN A . n 
A 1 98  ASN 98  92  92  ASN ASN A . n 
A 1 99  PRO 99  93  ?   ?   ?   A . n 
A 1 100 CYS 100 94  ?   ?   ?   A . n 
A 1 101 GLY 101 95  ?   ?   ?   A . n 
A 1 102 ASN 102 96  96  ASN ASN A . n 
A 1 103 TYR 103 97  97  TYR TYR A . n 
A 1 104 ALA 104 98  98  ALA ALA A . n 
A 1 105 LEU 105 99  99  LEU LEU A . n 
A 1 106 ALA 106 100 100 ALA ALA A . n 
A 1 107 LEU 107 101 101 LEU LEU A . n 
A 1 108 GLU 108 102 102 GLU GLU A . n 
A 1 109 ASN 109 103 103 ASN ASN A . n 
A 1 110 GLY 110 104 104 GLY GLY A . n 
A 1 111 VAL 111 105 105 VAL VAL A . n 
A 1 112 ASP 112 106 106 ASP ASP A . n 
A 1 113 PHE 113 107 107 PHE PHE A . n 
A 1 114 VAL 114 108 108 VAL VAL A . n 
A 1 115 GLU 115 109 109 GLU GLU A . n 
A 1 116 ASN 116 110 110 ASN ASN A . n 
A 1 117 ILE 117 111 111 ILE ILE A . n 
A 1 118 HIS 118 112 112 HIS HIS A . n 
A 1 119 SER 119 113 113 SER SER A . n 
A 1 120 LEU 120 114 114 LEU LEU A . n 
A 1 121 SER 121 115 115 SER SER A . n 
A 1 122 LEU 122 116 116 LEU LEU A . n 
A 1 123 LYS 123 117 117 LYS LYS A . n 
A 1 124 GLN 124 118 118 GLN GLN A . n 
A 1 125 PHE 125 119 119 PHE PHE A . n 
A 1 126 ALA 126 120 120 ALA ALA A . n 
A 1 127 LEU 127 121 121 LEU LEU A . n 
A 1 128 SER 128 122 122 SER SER A . n 
A 1 129 LEU 129 123 123 LEU LEU A . n 
A 1 130 CYS 130 124 124 CYS CYS A . n 
A 1 131 LYS 131 125 125 LYS LYS A . n 
A 1 132 LYS 132 126 126 LYS LYS A . n 
A 1 133 ASP 133 127 127 ASP ASP A . n 
A 1 134 ASP 134 128 128 ASP ASP A . n 
A 1 135 VAL 135 129 129 VAL VAL A . n 
A 1 136 PHE 136 130 130 PHE PHE A . n 
A 1 137 ILE 137 131 131 ILE ILE A . n 
A 1 138 GLU 138 132 132 GLU GLU A . n 
A 1 139 GLN 139 133 133 GLN GLN A . n 
A 1 140 GLY 140 134 134 GLY GLY A . n 
A 1 141 ILE 141 135 135 ILE ILE A . n 
A 1 142 ALA 142 136 136 ALA ALA A . n 
A 1 143 ASN 143 137 137 ASN ASN A . n 
A 1 144 LEU 144 138 138 LEU LEU A . n 
A 1 145 GLU 145 139 139 GLU GLU A . n 
A 1 146 ALA 146 140 140 ALA ALA A . n 
A 1 147 GLN 147 141 141 GLN GLN A . n 
A 1 148 TYR 148 142 142 TYR TYR A . n 
A 1 149 GLY 149 143 143 GLY GLY A . n 
A 1 150 TYR 150 144 144 TYR TYR A . n 
A 1 151 MET 151 145 145 MET MET A . n 
A 1 152 GLU 152 146 146 GLU GLU A . n 
A 1 153 LEU 153 147 147 LEU LEU A . n 
A 1 154 ALA 154 148 148 ALA ALA A . n 
A 1 155 GLN 155 149 149 GLN GLN A . n 
A 1 156 GLU 156 150 150 GLU GLU A . n 
A 1 157 ILE 157 151 151 ILE ILE A . n 
A 1 158 GLN 158 152 152 GLN GLN A . n 
A 1 159 MET 159 153 153 MET MET A . n 
A 1 160 GLN 160 154 154 GLN GLN A . n 
A 1 161 SER 161 155 155 SER SER A . n 
A 1 162 GLN 162 156 156 GLN GLN A . n 
A 1 163 SER 163 157 157 SER SER A . n 
A 1 164 LEU 164 158 158 LEU LEU A . n 
A 1 165 LYS 165 159 159 LYS LYS A . n 
A 1 166 LEU 166 160 160 LEU LEU A . n 
A 1 167 ASP 167 161 161 ASP ASP A . n 
A 1 168 PHE 168 162 162 PHE PHE A . n 
A 1 169 ASP 169 163 163 ASP ASP A . n 
A 1 170 ILE 170 164 164 ILE ILE A . n 
A 1 171 PHE 171 165 165 PHE PHE A . n 
A 1 172 LEU 172 166 166 LEU LEU A . n 
A 1 173 PRO 173 167 167 PRO PRO A . n 
A 1 174 SER 174 168 168 SER SER A . n 
A 1 175 GLY 175 169 169 GLY GLY A . n 
A 1 176 THR 176 170 170 THR THR A . n 
A 1 177 GLY 177 171 171 GLY GLY A . n 
A 1 178 THR 178 172 172 THR THR A . n 
A 1 179 SER 179 173 173 SER SER A . n 
A 1 180 ALA 180 174 174 ALA ALA A . n 
A 1 181 ALA 181 175 175 ALA ALA A . n 
A 1 182 PHE 182 176 176 PHE PHE A . n 
A 1 183 LEU 183 177 177 LEU LEU A . n 
A 1 184 ALA 184 178 178 ALA ALA A . n 
A 1 185 LYS 185 179 179 LYS LYS A . n 
A 1 186 TYR 186 180 180 TYR TYR A . n 
A 1 187 SER 187 181 181 SER SER A . n 
A 1 188 LYS 188 182 182 LYS LYS A . n 
A 1 189 PHE 189 183 183 PHE PHE A . n 
A 1 190 LYS 190 184 184 LYS LYS A . n 
A 1 191 VAL 191 185 185 VAL VAL A . n 
A 1 192 PHE 192 186 186 PHE PHE A . n 
A 1 193 THR 193 187 187 THR THR A . n 
A 1 194 CYS 194 188 188 CYS CYS A . n 
A 1 195 ALA 195 189 189 ALA ALA A . n 
A 1 196 CYS 196 190 190 CYS CYS A . n 
A 1 197 VAL 197 191 191 VAL VAL A . n 
A 1 198 GLY 198 192 192 GLY GLY A . n 
A 1 199 ASP 199 193 193 ASP ASP A . n 
A 1 200 ILE 200 194 194 ILE ILE A . n 
A 1 201 LYS 201 195 195 LYS LYS A . n 
A 1 202 TYR 202 196 196 TYR TYR A . n 
A 1 203 LEU 203 197 197 LEU LEU A . n 
A 1 204 LYS 204 198 198 LYS LYS A . n 
A 1 205 LYS 205 199 199 LYS LYS A . n 
A 1 206 GLN 206 200 200 GLN GLN A . n 
A 1 207 ILE 207 201 201 ILE ILE A . n 
A 1 208 LEU 208 202 202 LEU LEU A . n 
A 1 209 THR 209 203 203 THR THR A . n 
A 1 210 LEU 210 204 204 LEU LEU A . n 
A 1 211 ASP 211 205 205 ASP ASP A . n 
A 1 212 PRO 212 206 206 PRO PRO A . n 
A 1 213 SER 213 207 207 SER SER A . n 
A 1 214 TYR 214 208 208 TYR TYR A . n 
A 1 215 ASP 215 209 209 ASP ASP A . n 
A 1 216 PHE 216 210 210 PHE PHE A . n 
A 1 217 SER 217 211 211 SER SER A . n 
A 1 218 ASN 218 212 212 ASN ASN A . n 
A 1 219 LEU 219 213 213 LEU LEU A . n 
A 1 220 GLU 220 214 214 GLU GLU A . n 
A 1 221 PHE 221 215 215 PHE PHE A . n 
A 1 222 LEU 222 216 216 LEU LEU A . n 
A 1 223 THR 223 217 217 THR THR A . n 
A 1 224 SER 224 218 218 SER SER A . n 
A 1 225 ASP 225 219 219 ASP ASP A . n 
A 1 226 LYS 226 220 220 LYS LYS A . n 
A 1 227 LYS 227 221 221 LYS LYS A . n 
A 1 228 TYR 228 222 222 TYR TYR A . n 
A 1 229 HIS 229 223 223 HIS HIS A . n 
A 1 230 PHE 230 224 224 PHE PHE A . n 
A 1 231 ALA 231 225 225 ALA ALA A . n 
A 1 232 LYS 232 226 226 LYS LYS A . n 
A 1 233 PRO 233 227 227 PRO PRO A . n 
A 1 234 TYR 234 228 228 TYR TYR A . n 
A 1 235 LYS 235 229 229 LYS LYS A . n 
A 1 236 GLU 236 230 230 GLU GLU A . n 
A 1 237 PHE 237 231 231 PHE PHE A . n 
A 1 238 TYR 238 232 232 TYR TYR A . n 
A 1 239 GLU 239 233 233 GLU GLU A . n 
A 1 240 LEU 240 234 234 LEU LEU A . n 
A 1 241 TYR 241 235 235 TYR TYR A . n 
A 1 242 MET 242 236 236 MET MET A . n 
A 1 243 ASP 243 237 237 ASP ASP A . n 
A 1 244 LEU 244 238 238 LEU LEU A . n 
A 1 245 LYS 245 239 239 LYS LYS A . n 
A 1 246 LEU 246 240 240 LEU LEU A . n 
A 1 247 LYS 247 241 241 LYS LYS A . n 
A 1 248 CYS 248 242 242 CYS CYS A . n 
A 1 249 ASN 249 243 243 ASN ASN A . n 
A 1 250 ILE 250 244 244 ILE ILE A . n 
A 1 251 GLU 251 245 245 GLU GLU A . n 
A 1 252 PHE 252 246 246 PHE PHE A . n 
A 1 253 ASP 253 247 247 ASP ASP A . n 
A 1 254 LEU 254 248 248 LEU LEU A . n 
A 1 255 LEU 255 249 249 LEU LEU A . n 
A 1 256 TYR 256 250 250 TYR TYR A . n 
A 1 257 ASP 257 251 251 ASP ASP A . n 
A 1 258 ILE 258 252 252 ILE ILE A . n 
A 1 259 LEU 259 253 253 LEU LEU A . n 
A 1 260 GLY 260 254 254 GLY GLY A . n 
A 1 261 LEU 261 255 255 LEU LEU A . n 
A 1 262 SER 262 256 256 SER SER A . n 
A 1 263 ILE 263 257 257 ILE ILE A . n 
A 1 264 ALA 264 258 258 ALA ALA A . n 
A 1 265 LEU 265 259 259 LEU LEU A . n 
A 1 266 LYS 266 260 260 LYS LYS A . n 
A 1 267 GLN 267 261 261 GLN GLN A . n 
A 1 268 GLU 268 262 262 GLU GLU A . n 
A 1 269 TRP 269 263 263 TRP TRP A . n 
A 1 270 LYS 270 264 264 LYS LYS A . n 
A 1 271 LYS 271 265 265 LYS LYS A . n 
A 1 272 PRO 272 266 266 PRO PRO A . n 
A 1 273 LEU 273 267 267 LEU LEU A . n 
A 1 274 LEU 274 268 268 LEU LEU A . n 
A 1 275 TYR 275 269 269 TYR TYR A . n 
A 1 276 ILE 276 270 270 ILE ILE A . n 
A 1 277 HIS 277 271 271 HIS HIS A . n 
A 1 278 GLN 278 272 272 GLN GLN A . n 
A 1 279 GLY 279 273 273 GLY GLY A . n 
A 1 280 GLY 280 274 274 GLY GLY A . n 
A 1 281 ILE 281 275 275 ILE ILE A . n 
A 1 282 LEU 282 276 276 LEU LEU A . n 
A 1 283 GLY 283 277 277 GLY GLY A . n 
A 1 284 ASN 284 278 278 ASN ASN A . n 
A 1 285 SER 285 279 279 SER SER A . n 
A 1 286 THR 286 280 280 THR THR A . n 
A 1 287 MET 287 281 281 MET MET A . n 
A 1 288 LEU 288 282 282 LEU LEU A . n 
A 1 289 GLU 289 283 283 GLU GLU A . n 
A 1 290 ARG 290 284 284 ARG ARG A . n 
A 1 291 TYR 291 285 285 TYR TYR A . n 
A 1 292 LYS 292 286 ?   ?   ?   A . n 
A 1 293 PHE 293 287 ?   ?   ?   A . n 
A 1 294 LYS 294 288 ?   ?   ?   A . n 
A 1 295 LYS 295 289 ?   ?   ?   A . n 
A 1 296 SER 296 290 ?   ?   ?   A . n 
A 1 297 VAL 297 291 ?   ?   ?   A . 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 
B 2 SO4 1   301 1   SO4 SO4 A . 
C 2 SO4 1   302 2   SO4 SO4 A . 
D 2 SO4 1   303 3   SO4 SO4 A . 
E 3 HOH 1   401 76  HOH HOH A . 
E 3 HOH 2   402 196 HOH HOH A . 
E 3 HOH 3   403 92  HOH HOH A . 
E 3 HOH 4   404 55  HOH HOH A . 
E 3 HOH 5   405 66  HOH HOH A . 
E 3 HOH 6   406 171 HOH HOH A . 
E 3 HOH 7   407 60  HOH HOH A . 
E 3 HOH 8   408 35  HOH HOH A . 
E 3 HOH 9   409 58  HOH HOH A . 
E 3 HOH 10  410 62  HOH HOH A . 
E 3 HOH 11  411 194 HOH HOH A . 
E 3 HOH 12  412 74  HOH HOH A . 
E 3 HOH 13  413 10  HOH HOH A . 
E 3 HOH 14  414 5   HOH HOH A . 
E 3 HOH 15  415 33  HOH HOH A . 
E 3 HOH 16  416 30  HOH HOH A . 
E 3 HOH 17  417 73  HOH HOH A . 
E 3 HOH 18  418 117 HOH HOH A . 
E 3 HOH 19  419 34  HOH HOH A . 
E 3 HOH 20  420 54  HOH HOH A . 
E 3 HOH 21  421 44  HOH HOH A . 
E 3 HOH 22  422 11  HOH HOH A . 
E 3 HOH 23  423 170 HOH HOH A . 
E 3 HOH 24  424 75  HOH HOH A . 
E 3 HOH 25  425 43  HOH HOH A . 
E 3 HOH 26  426 132 HOH HOH A . 
E 3 HOH 27  427 63  HOH HOH A . 
E 3 HOH 28  428 18  HOH HOH A . 
E 3 HOH 29  429 69  HOH HOH A . 
E 3 HOH 30  430 64  HOH HOH A . 
E 3 HOH 31  431 51  HOH HOH A . 
E 3 HOH 32  432 49  HOH HOH A . 
E 3 HOH 33  433 45  HOH HOH A . 
E 3 HOH 34  434 104 HOH HOH A . 
E 3 HOH 35  435 16  HOH HOH A . 
E 3 HOH 36  436 96  HOH HOH A . 
E 3 HOH 37  437 78  HOH HOH A . 
E 3 HOH 38  438 38  HOH HOH A . 
E 3 HOH 39  439 8   HOH HOH A . 
E 3 HOH 40  440 25  HOH HOH A . 
E 3 HOH 41  441 89  HOH HOH A . 
E 3 HOH 42  442 3   HOH HOH A . 
E 3 HOH 43  443 48  HOH HOH A . 
E 3 HOH 44  444 197 HOH HOH A . 
E 3 HOH 45  445 9   HOH HOH A . 
E 3 HOH 46  446 31  HOH HOH A . 
E 3 HOH 47  447 36  HOH HOH A . 
E 3 HOH 48  448 14  HOH HOH A . 
E 3 HOH 49  449 13  HOH HOH A . 
E 3 HOH 50  450 59  HOH HOH A . 
E 3 HOH 51  451 27  HOH HOH A . 
E 3 HOH 52  452 83  HOH HOH A . 
E 3 HOH 53  453 149 HOH HOH A . 
E 3 HOH 54  454 95  HOH HOH A . 
E 3 HOH 55  455 130 HOH HOH A . 
E 3 HOH 56  456 20  HOH HOH A . 
E 3 HOH 57  457 102 HOH HOH A . 
E 3 HOH 58  458 201 HOH HOH A . 
E 3 HOH 59  459 199 HOH HOH A . 
E 3 HOH 60  460 108 HOH HOH A . 
E 3 HOH 61  461 100 HOH HOH A . 
E 3 HOH 62  462 91  HOH HOH A . 
E 3 HOH 63  463 24  HOH HOH A . 
E 3 HOH 64  464 47  HOH HOH A . 
E 3 HOH 65  465 32  HOH HOH A . 
E 3 HOH 66  466 39  HOH HOH A . 
E 3 HOH 67  467 98  HOH HOH A . 
E 3 HOH 68  468 56  HOH HOH A . 
E 3 HOH 69  469 65  HOH HOH A . 
E 3 HOH 70  470 29  HOH HOH A . 
E 3 HOH 71  471 70  HOH HOH A . 
E 3 HOH 72  472 40  HOH HOH A . 
E 3 HOH 73  473 19  HOH HOH A . 
E 3 HOH 74  474 93  HOH HOH A . 
E 3 HOH 75  475 82  HOH HOH A . 
E 3 HOH 76  476 12  HOH HOH A . 
E 3 HOH 77  477 21  HOH HOH A . 
E 3 HOH 78  478 42  HOH HOH A . 
E 3 HOH 79  479 87  HOH HOH A . 
E 3 HOH 80  480 164 HOH HOH A . 
E 3 HOH 81  481 133 HOH HOH A . 
E 3 HOH 82  482 125 HOH HOH A . 
E 3 HOH 83  483 68  HOH HOH A . 
E 3 HOH 84  484 7   HOH HOH A . 
E 3 HOH 85  485 72  HOH HOH A . 
E 3 HOH 86  486 22  HOH HOH A . 
E 3 HOH 87  487 156 HOH HOH A . 
E 3 HOH 88  488 57  HOH HOH A . 
E 3 HOH 89  489 116 HOH HOH A . 
E 3 HOH 90  490 86  HOH HOH A . 
E 3 HOH 91  491 177 HOH HOH A . 
E 3 HOH 92  492 23  HOH HOH A . 
E 3 HOH 93  493 101 HOH HOH A . 
E 3 HOH 94  494 121 HOH HOH A . 
E 3 HOH 95  495 26  HOH HOH A . 
E 3 HOH 96  496 67  HOH HOH A . 
E 3 HOH 97  497 15  HOH HOH A . 
E 3 HOH 98  498 79  HOH HOH A . 
E 3 HOH 99  499 106 HOH HOH A . 
E 3 HOH 100 500 94  HOH HOH A . 
E 3 HOH 101 501 17  HOH HOH A . 
E 3 HOH 102 502 6   HOH HOH A . 
E 3 HOH 103 503 145 HOH HOH A . 
E 3 HOH 104 504 88  HOH HOH A . 
E 3 HOH 105 505 4   HOH HOH A . 
E 3 HOH 106 506 61  HOH HOH A . 
E 3 HOH 107 507 90  HOH HOH A . 
E 3 HOH 108 508 159 HOH HOH A . 
E 3 HOH 109 509 160 HOH HOH A . 
E 3 HOH 110 510 52  HOH HOH A . 
E 3 HOH 111 511 144 HOH HOH A . 
E 3 HOH 112 512 77  HOH HOH A . 
E 3 HOH 113 513 115 HOH HOH A . 
E 3 HOH 114 514 137 HOH HOH A . 
E 3 HOH 115 515 165 HOH HOH A . 
E 3 HOH 116 516 178 HOH HOH A . 
E 3 HOH 117 517 50  HOH HOH A . 
E 3 HOH 118 518 84  HOH HOH A . 
E 3 HOH 119 519 122 HOH HOH A . 
E 3 HOH 120 520 202 HOH HOH A . 
E 3 HOH 121 521 131 HOH HOH A . 
E 3 HOH 122 522 113 HOH HOH A . 
E 3 HOH 123 523 167 HOH HOH A . 
E 3 HOH 124 524 37  HOH HOH A . 
E 3 HOH 125 525 128 HOH HOH A . 
E 3 HOH 126 526 154 HOH HOH A . 
E 3 HOH 127 527 182 HOH HOH A . 
E 3 HOH 128 528 134 HOH HOH A . 
E 3 HOH 129 529 103 HOH HOH A . 
E 3 HOH 130 530 71  HOH HOH A . 
E 3 HOH 131 531 110 HOH HOH A . 
E 3 HOH 132 532 139 HOH HOH A . 
E 3 HOH 133 533 176 HOH HOH A . 
E 3 HOH 134 534 127 HOH HOH A . 
E 3 HOH 135 535 124 HOH HOH A . 
E 3 HOH 136 536 198 HOH HOH A . 
E 3 HOH 137 537 157 HOH HOH A . 
E 3 HOH 138 538 111 HOH HOH A . 
E 3 HOH 139 539 200 HOH HOH A . 
E 3 HOH 140 540 120 HOH HOH A . 
E 3 HOH 141 541 28  HOH HOH A . 
# 
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 5   ? CD  ? A LYS 11  CD  
2  1 Y 1 A LYS 5   ? CE  ? A LYS 11  CE  
3  1 Y 1 A LYS 5   ? NZ  ? A LYS 11  NZ  
4  1 Y 1 A LYS 49  ? CD  ? A LYS 55  CD  
5  1 Y 1 A LYS 49  ? CE  ? A LYS 55  CE  
6  1 Y 1 A LYS 49  ? NZ  ? A LYS 55  NZ  
7  1 Y 1 A LYS 72  ? CD  ? A LYS 78  CD  
8  1 Y 1 A LYS 72  ? CE  ? A LYS 78  CE  
9  1 Y 1 A LYS 72  ? NZ  ? A LYS 78  NZ  
10 1 Y 1 A LYS 77  ? CD  ? A LYS 83  CD  
11 1 Y 1 A LYS 77  ? CE  ? A LYS 83  CE  
12 1 Y 1 A LYS 77  ? NZ  ? A LYS 83  NZ  
13 1 Y 1 A LYS 84  ? CG  ? A LYS 90  CG  
14 1 Y 1 A LYS 84  ? CD  ? A LYS 90  CD  
15 1 Y 1 A LYS 84  ? CE  ? A LYS 90  CE  
16 1 Y 1 A LYS 84  ? NZ  ? A LYS 90  NZ  
17 1 Y 1 A ILE 85  ? CG1 ? A ILE 91  CG1 
18 1 Y 1 A ILE 85  ? CG2 ? A ILE 91  CG2 
19 1 Y 1 A ILE 85  ? CD1 ? A ILE 91  CD1 
20 1 Y 1 A PHE 88  ? CG  ? A PHE 94  CG  
21 1 Y 1 A PHE 88  ? CD1 ? A PHE 94  CD1 
22 1 Y 1 A PHE 88  ? CD2 ? A PHE 94  CD2 
23 1 Y 1 A PHE 88  ? CE1 ? A PHE 94  CE1 
24 1 Y 1 A PHE 88  ? CE2 ? A PHE 94  CE2 
25 1 Y 1 A PHE 88  ? CZ  ? A PHE 94  CZ  
26 1 Y 1 A LYS 90  ? CD  ? A LYS 96  CD  
27 1 Y 1 A LYS 90  ? CE  ? A LYS 96  CE  
28 1 Y 1 A LYS 90  ? NZ  ? A LYS 96  NZ  
29 1 Y 1 A ASN 91  ? CG  ? A ASN 97  CG  
30 1 Y 1 A ASN 91  ? OD1 ? A ASN 97  OD1 
31 1 Y 1 A ASN 91  ? ND2 ? A ASN 97  ND2 
32 1 Y 1 A ASN 92  ? CG  ? A ASN 98  CG  
33 1 Y 1 A ASN 92  ? OD1 ? A ASN 98  OD1 
34 1 Y 1 A ASN 92  ? ND2 ? A ASN 98  ND2 
35 1 Y 1 A GLU 102 ? CG  ? A GLU 108 CG  
36 1 Y 1 A GLU 102 ? CD  ? A GLU 108 CD  
37 1 Y 1 A GLU 102 ? OE1 ? A GLU 108 OE1 
38 1 Y 1 A GLU 102 ? OE2 ? A GLU 108 OE2 
39 1 Y 1 A SER 113 ? OG  ? A SER 119 OG  
40 1 Y 1 A LEU 114 ? CG  ? A LEU 120 CG  
41 1 Y 1 A LEU 114 ? CD1 ? A LEU 120 CD1 
42 1 Y 1 A LEU 114 ? CD2 ? A LEU 120 CD2 
43 1 Y 1 A SER 115 ? OG  ? A SER 121 OG  
44 1 Y 1 A GLN 118 ? CG  ? A GLN 124 CG  
45 1 Y 1 A GLN 118 ? CD  ? A GLN 124 CD  
46 1 Y 1 A GLN 118 ? OE1 ? A GLN 124 OE1 
47 1 Y 1 A GLN 118 ? NE2 ? A GLN 124 NE2 
48 1 Y 1 A LYS 125 ? CD  ? A LYS 131 CD  
49 1 Y 1 A LYS 125 ? CE  ? A LYS 131 CE  
50 1 Y 1 A LYS 125 ? NZ  ? A LYS 131 NZ  
51 1 Y 1 A LYS 126 ? CG  ? A LYS 132 CG  
52 1 Y 1 A LYS 126 ? CD  ? A LYS 132 CD  
53 1 Y 1 A LYS 126 ? CE  ? A LYS 132 CE  
54 1 Y 1 A LYS 126 ? NZ  ? A LYS 132 NZ  
55 1 Y 1 A LYS 159 ? CE  ? A LYS 165 CE  
56 1 Y 1 A LYS 159 ? NZ  ? A LYS 165 NZ  
57 1 Y 1 A LYS 195 ? CG  ? A LYS 201 CG  
58 1 Y 1 A LYS 195 ? CD  ? A LYS 201 CD  
59 1 Y 1 A LYS 195 ? CE  ? A LYS 201 CE  
60 1 Y 1 A LYS 195 ? NZ  ? A LYS 201 NZ  
61 1 Y 1 A LYS 229 ? CD  ? A LYS 235 CD  
62 1 Y 1 A LYS 229 ? CE  ? A LYS 235 CE  
63 1 Y 1 A LYS 229 ? NZ  ? A LYS 235 NZ  
64 1 Y 1 A LYS 260 ? CE  ? A LYS 266 CE  
65 1 Y 1 A LYS 260 ? NZ  ? A LYS 266 NZ  
66 1 Y 1 A LYS 264 ? CG  ? A LYS 270 CG  
67 1 Y 1 A LYS 264 ? CD  ? A LYS 270 CD  
68 1 Y 1 A LYS 264 ? CE  ? A LYS 270 CE  
69 1 Y 1 A LYS 264 ? NZ  ? A LYS 270 NZ  
70 1 Y 1 A LEU 276 ? CG  ? A LEU 282 CG  
71 1 Y 1 A LEU 276 ? CD1 ? A LEU 282 CD1 
72 1 Y 1 A LEU 276 ? CD2 ? A LEU 282 CD2 
73 1 Y 1 A SER 279 ? OG  ? A SER 285 OG  
74 1 Y 1 A THR 280 ? OG1 ? A THR 286 OG1 
75 1 Y 1 A THR 280 ? CG2 ? A THR 286 CG2 
76 1 Y 1 A GLU 283 ? CG  ? A GLU 289 CG  
77 1 Y 1 A GLU 283 ? CD  ? A GLU 289 CD  
78 1 Y 1 A GLU 283 ? OE1 ? A GLU 289 OE1 
79 1 Y 1 A GLU 283 ? OE2 ? A GLU 289 OE2 
# 
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   ? ? ? 1.15.2_3472 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.entry_id           9JQF 
_cell.length_a           122.748 
_cell.length_b           122.748 
_cell.length_c           104.691 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              18 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         9JQF 
_symmetry.space_group_name_H-M             'H 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                155 
# 
_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                   9JQF 
_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             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.87 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'PEG 3350,  Bis-Tris, lithium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 270' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-06-11 
_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   0.97934 
_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                        'PAL/PLS BEAMLINE 7A (6B, 6C1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97934 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   '7A (6B, 6C1)' 
_diffrn_source.pdbx_synchrotron_site       PAL/PLS 
# 
_reflns.B_iso_Wilson_estimate                          22.58 
_reflns.entry_id                                       9JQF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               30 
_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                                     33159 
_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                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.7 
_reflns.pdbx_netI_over_av_sigmaI                       31.0 
_reflns.pdbx_netI_over_sigmaI                          31.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.70 
_reflns_shell.d_res_low                                     1.73 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1644 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.3 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.699 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               31.64 
_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                                 9JQF 
_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                            1.70 
_refine.ls_d_res_low                             25.69 
_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                     33133 
_refine.ls_number_reflns_R_free                  1662 
_refine.ls_number_reflns_R_work                  31471 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.27 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1812 
_refine.ls_R_factor_R_free                       0.2056 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1800 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.3733 
_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                            0.1606 
_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                       1.70 
_refine_hist.d_res_low                        25.69 
_refine_hist.number_atoms_solvent             141 
_refine_hist.number_atoms_total               2376 
_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        2205 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_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' ? 0.0063  ? 2289 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9050  ? 3100 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0538  ? 336  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0046  ? 392  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 22.1564 ? 806  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.70 1.75  . . 143 2605 99.24 . . . . 0.2465 . . . . . . . . . . . 0.2615 
'X-RAY DIFFRACTION' 1.75 1.81  . . 148 2584 99.53 . . . . 0.2304 . . . . . . . . . . . 0.2749 
'X-RAY DIFFRACTION' 1.81 1.87  . . 157 2590 99.75 . . . . 0.2108 . . . . . . . . . . . 0.2519 
'X-RAY DIFFRACTION' 1.87 1.95  . . 146 2617 99.86 . . . . 0.1944 . . . . . . . . . . . 0.1938 
'X-RAY DIFFRACTION' 1.95 2.03  . . 123 2628 99.89 . . . . 0.1941 . . . . . . . . . . . 0.2012 
'X-RAY DIFFRACTION' 2.03 2.14  . . 134 2633 99.89 . . . . 0.1811 . . . . . . . . . . . 0.2051 
'X-RAY DIFFRACTION' 2.14 2.28  . . 139 2625 99.82 . . . . 0.1761 . . . . . . . . . . . 0.2341 
'X-RAY DIFFRACTION' 2.28 2.45  . . 143 2612 99.82 . . . . 0.1885 . . . . . . . . . . . 0.2157 
'X-RAY DIFFRACTION' 2.45 2.70  . . 143 2646 99.64 . . . . 0.1834 . . . . . . . . . . . 0.2003 
'X-RAY DIFFRACTION' 2.70 3.09  . . 122 2636 99.35 . . . . 0.1877 . . . . . . . . . . . 0.2046 
'X-RAY DIFFRACTION' 3.09 3.89  . . 150 2625 98.65 . . . . 0.1640 . . . . . . . . . . . 0.1946 
'X-RAY DIFFRACTION' 3.89 25.69 . . 114 2670 96.00 . . . . 0.1649 . . . . . . . . . . . 0.1838 
# 
_struct.entry_id                     9JQF 
_struct.title                        'Crystal structure of the CJ0600 protein from Campylobacter jejuni' 
_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        9JQF 
_struct_keywords.text            'PLP-dependent lyase, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A5Z1H273_CAMJU 
_struct_ref.pdbx_db_accession          A0A5Z1H273 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;NFIKTISPIQKINFNGFEFYIKRDDLLGEINGNKARKLAFYIHQRYPKNQSFVSYGGSQSNALAALSIFAKQRSYKLVFA
CEKISTFLKNNPCGNYALALENGVDFVENIHSLSLKQFALSLCKKDDVFIEQGIANLEAQYGYMELAQEIQMQSQSLKLD
FDIFLPSGTGTSAAFLAKYSKFKVFTCACVGDIKYLKKQILTLDPSYDFSNLEFLTSDKKYHFAKPYKEFYELYMDLKLK
CNIEFDLLYDILGLSIALKQEWKKPLLYIHQGGILGNSTMLERYKFKKLV
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9JQF 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 8 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 297 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A5Z1H273 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  291 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       291 
# 
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 9JQF GLY A 1   ? UNP A0A5Z1H273 ?   ?   'expression tag' -5  1 
1 9JQF SER A 2   ? UNP A0A5Z1H273 ?   ?   'expression tag' -4  2 
1 9JQF ALA A 3   ? UNP A0A5Z1H273 ?   ?   'expression tag' -3  3 
1 9JQF LYS A 4   ? UNP A0A5Z1H273 ?   ?   'expression tag' -2  4 
1 9JQF ASP A 5   ? UNP A0A5Z1H273 ?   ?   'expression tag' -1  5 
1 9JQF PRO A 6   ? UNP A0A5Z1H273 ?   ?   'expression tag' 0   6 
1 9JQF LEU A 7   ? UNP A0A5Z1H273 ?   ?   'expression tag' 1   7 
1 9JQF SER A 296 ? UNP A0A5Z1H273 LEU 290 conflict         290 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 31  ? LEU A 34  ? ASP A 25  LEU A 28  5 ? 4  
HELX_P HELX_P2  AA2 ASN A 38  ? LEU A 45  ? ASN A 32  LEU A 39  1 ? 8  
HELX_P HELX_P3  AA3 LEU A 45  ? GLN A 51  ? LEU A 39  GLN A 45  1 ? 7  
HELX_P HELX_P4  AA4 SER A 67  ? ARG A 80  ? SER A 61  ARG A 74  1 ? 14 
HELX_P HELX_P5  AA5 SER A 92  ? ASN A 98  ? SER A 86  ASN A 92  1 ? 7  
HELX_P HELX_P6  AA6 TYR A 103 ? ASN A 109 ? TYR A 97  ASN A 103 1 ? 7  
HELX_P HELX_P7  AA7 SER A 121 ? LEU A 129 ? SER A 115 LEU A 123 1 ? 9  
HELX_P HELX_P8  AA8 GLU A 138 ? ALA A 142 ? GLU A 132 ALA A 136 5 ? 5  
HELX_P HELX_P9  AA9 ASN A 143 ? GLU A 145 ? ASN A 137 GLU A 139 5 ? 3  
HELX_P HELX_P10 AB1 ALA A 146 ? LYS A 165 ? ALA A 140 LYS A 159 1 ? 20 
HELX_P HELX_P11 AB2 GLY A 177 ? SER A 187 ? GLY A 171 SER A 181 1 ? 11 
HELX_P HELX_P12 AB3 ASP A 199 ? ASP A 211 ? ASP A 193 ASP A 205 1 ? 13 
HELX_P HELX_P13 AB4 ASP A 215 ? SER A 217 ? ASP A 209 SER A 211 5 ? 3  
HELX_P HELX_P14 AB5 TYR A 234 ? ASN A 249 ? TYR A 228 ASN A 243 1 ? 16 
HELX_P HELX_P15 AB6 TYR A 256 ? LEU A 265 ? TYR A 250 LEU A 259 1 ? 10 
HELX_P HELX_P16 AB7 GLY A 280 ? LEU A 282 ? GLY A 274 LEU A 276 5 ? 3  
HELX_P HELX_P17 AB8 GLY A 283 ? TYR A 291 ? GLY A 277 TYR A 285 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A ASN 40 C ? ? ? 1_555 A LLP 41 N ? ? A ASN 34 A LLP 35 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale2 covale both ? A LLP 41 C ? ? ? 1_555 A ALA 42 N ? ? A LLP 35 A ALA 36 1_555 ? ? ? ? ? ? ? 1.342 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      LLP 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       41 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       LLP 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        35 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                LYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        LLP 
_pdbx_modification_feature.type                               'Pyridoxal phosphate' 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 4 ? 
# 
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 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? 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 ILE A 16  ? PHE A 21  ? ILE A 10  PHE A 15  
AA1 2 PHE A 24  ? LYS A 29  ? PHE A 18  LYS A 23  
AA1 3 LEU A 273 ? ILE A 276 ? LEU A 267 ILE A 270 
AA1 4 ASP A 169 ? PHE A 171 ? ASP A 163 PHE A 165 
AA1 5 VAL A 191 ? THR A 193 ? VAL A 185 THR A 187 
AA1 6 LEU A 219 ? PHE A 221 ? LEU A 213 PHE A 215 
AA2 1 ASP A 112 ? ASN A 116 ? ASP A 106 ASN A 110 
AA2 2 LYS A 83  ? GLU A 89  ? LYS A 77  GLU A 83  
AA2 3 SER A 58  ? TYR A 62  ? SER A 52  TYR A 56  
AA2 4 VAL A 135 ? PHE A 136 ? VAL A 129 PHE A 130 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 17  ? N GLN A 11  O ILE A 28  ? O ILE A 22  
AA1 2 3 N TYR A 27  ? N TYR A 21  O TYR A 275 ? O TYR A 269 
AA1 3 4 O LEU A 274 ? O LEU A 268 N ASP A 169 ? N ASP A 163 
AA1 4 5 N ILE A 170 ? N ILE A 164 O PHE A 192 ? O PHE A 186 
AA1 5 6 N VAL A 191 ? N VAL A 185 O GLU A 220 ? O GLU A 214 
AA2 1 2 O ASP A 112 ? O ASP A 106 N LEU A 84  ? N LEU A 78  
AA2 2 3 O VAL A 85  ? O VAL A 79  N PHE A 59  ? N PHE A 53  
AA2 3 4 N VAL A 60  ? N VAL A 54  O VAL A 135 ? O VAL A 129 
# 
_pdbx_entry_details.entry_id                   9JQF 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASP 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     127 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             79.55 
_pdbx_validate_torsion.psi             -9.38 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    LLP 
_pdbx_struct_mod_residue.label_seq_id     41 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     LLP 
_pdbx_struct_mod_residue.auth_seq_id      35 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   LYS 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A SO4 302 ? C SO4 . 
2 1 A SO4 302 ? C SO4 . 
3 1 A HOH 510 ? E HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z                  
2  -y,x-y,z               
3  -x+y,-x,z              
4  x-y,-y,-z              
5  -x,-x+y,-z             
6  y,x,-z                 
7  x+1/3,y+2/3,z+2/3      
8  -y+1/3,x-y+2/3,z+2/3   
9  -x+y+1/3,-x+2/3,z+2/3  
10 x-y+1/3,-y+2/3,-z+2/3  
11 -x+1/3,-x+y+2/3,-z+2/3 
12 y+1/3,x+2/3,-z+2/3     
13 x+2/3,y+1/3,z+1/3      
14 -y+2/3,x-y+1/3,z+1/3   
15 -x+y+2/3,-x+1/3,z+1/3  
16 x-y+2/3,-y+1/3,-z+1/3  
17 -x+2/3,-x+y+1/3,-z+1/3 
18 y+2/3,x+1/3,-z+1/3     
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 14.1919 -31.0455 -34.4703 0.1475 0.1599 0.1093 0.0467  -0.0058 -0.0177 3.2938 9.9705 5.6412 1.8068 
-1.4823 -4.4512 0.0899  0.1372  0.0287  -0.2879 -0.1780 -0.0451 0.0663  -0.0245 0.0764  
'X-RAY DIFFRACTION' 2 ? refined 4.7963  -32.1346 -20.8183 0.1788 0.1681 0.2071 -0.0035 0.0182  -0.0055 1.5403 1.6363 9.4150 
-0.1968 -2.0988 0.1379  -0.0561 -0.0768 -0.1133 0.0244  -0.0402 0.2612  0.4123  -0.1922 0.0912  
'X-RAY DIFFRACTION' 3 ? refined -8.3465 -26.9461 -11.6172 0.2980 0.4392 0.3722 0.0788  0.1414  0.1075  4.4991 2.9599 2.3959 0.1301 
-0.9011 -0.2023 -0.0697 0.0678  0.2833  0.4872  0.3732  0.7626  -0.1557 -0.8228 -0.3016 
'X-RAY DIFFRACTION' 4 ? refined 16.2492 -24.4595 -21.5958 0.1622 0.1276 0.1320 -0.0001 -0.0142 -0.0097 2.2784 1.9670 1.9368 
-0.7763 -0.2905 0.0135  -0.0041 -0.1045 0.0985  0.1279  0.0178  -0.0253 -0.0646 0.0629  -0.0063 
'X-RAY DIFFRACTION' 5 ? refined 13.8741 -12.9054 -14.0882 0.2817 0.1685 0.2522 0.0052  -0.0299 -0.0822 3.7557 4.7369 7.5309 
-0.5849 -2.4810 -0.5796 0.0243  -0.4876 0.6193  0.6418  0.1597  -0.0230 -0.5114 0.1922  -0.1869 
'X-RAY DIFFRACTION' 6 ? refined 3.4680  -15.7164 -35.1493 0.2162 0.2030 0.2374 0.0515  0.0023  0.0427  2.6174 2.8816 1.3310 
-1.0304 -0.2140 -0.0111 0.1153  0.2798  0.2788  -0.2037 -0.1089 0.1529  -0.1984 -0.0916 -0.0066 
'X-RAY DIFFRACTION' 7 ? refined 6.3432  -19.9480 -31.8509 0.1697 0.1309 0.1711 0.0390  -0.0093 0.0253  3.8469 2.4341 2.7803 0.0034 
0.5077  -0.2429 0.0998  0.2451  0.4647  -0.0356 -0.0197 0.3479  -0.1436 -0.2671 -0.0869 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 2 THROUGH 23 )
;
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 24 THROUGH 44 )
;
'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 45 THROUGH 137 )
;
'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 138 THROUGH 193 )
;
'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 194 THROUGH 215 )
;
'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 216 THROUGH 260 )
;
'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 261 THROUGH 285 )
;
# 
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 GLY -5  ? A GLY 1   
2  1 Y 1 A SER -4  ? A SER 2   
3  1 Y 1 A ALA -3  ? A ALA 3   
4  1 Y 1 A LYS -2  ? A LYS 4   
5  1 Y 1 A ASP -1  ? A ASP 5   
6  1 Y 1 A PRO 0   ? A PRO 6   
7  1 Y 1 A LEU 1   ? A LEU 7   
8  1 Y 1 A PRO 93  ? A PRO 99  
9  1 Y 1 A CYS 94  ? A CYS 100 
10 1 Y 1 A GLY 95  ? A GLY 101 
11 1 Y 1 A LYS 286 ? A LYS 292 
12 1 Y 1 A PHE 287 ? A PHE 293 
13 1 Y 1 A LYS 288 ? A LYS 294 
14 1 Y 1 A LYS 289 ? A LYS 295 
15 1 Y 1 A SER 290 ? A SER 296 
16 1 Y 1 A VAL 291 ? A VAL 297 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
GLN N      N N N 88  
GLN CA     C N S 89  
GLN C      C N N 90  
GLN O      O N N 91  
GLN CB     C N N 92  
GLN CG     C N N 93  
GLN CD     C N N 94  
GLN OE1    O N N 95  
GLN NE2    N N N 96  
GLN OXT    O N N 97  
GLN H      H N N 98  
GLN H2     H N N 99  
GLN HA     H N N 100 
GLN HB2    H N N 101 
GLN HB3    H N N 102 
GLN HG2    H N N 103 
GLN HG3    H N N 104 
GLN HE21   H N N 105 
GLN HE22   H N N 106 
GLN HXT    H N N 107 
GLU N      N N N 108 
GLU CA     C N S 109 
GLU C      C N N 110 
GLU O      O N N 111 
GLU CB     C N N 112 
GLU CG     C N N 113 
GLU CD     C N N 114 
GLU OE1    O N N 115 
GLU OE2    O N N 116 
GLU OXT    O N N 117 
GLU H      H N N 118 
GLU H2     H N N 119 
GLU HA     H N N 120 
GLU HB2    H N N 121 
GLU HB3    H N N 122 
GLU HG2    H N N 123 
GLU HG3    H N N 124 
GLU HE2    H N N 125 
GLU HXT    H N N 126 
GLY N      N N N 127 
GLY CA     C N N 128 
GLY C      C N N 129 
GLY O      O N N 130 
GLY OXT    O N N 131 
GLY H      H N N 132 
GLY H2     H N N 133 
GLY HA2    H N N 134 
GLY HA3    H N N 135 
GLY HXT    H N N 136 
HIS N      N N N 137 
HIS CA     C N S 138 
HIS C      C N N 139 
HIS O      O N N 140 
HIS CB     C N N 141 
HIS CG     C Y N 142 
HIS ND1    N Y N 143 
HIS CD2    C Y N 144 
HIS CE1    C Y N 145 
HIS NE2    N Y N 146 
HIS OXT    O N N 147 
HIS H      H N N 148 
HIS H2     H N N 149 
HIS HA     H N N 150 
HIS HB2    H N N 151 
HIS HB3    H N N 152 
HIS HD1    H N N 153 
HIS HD2    H N N 154 
HIS HE1    H N N 155 
HIS HE2    H N N 156 
HIS HXT    H N N 157 
HOH O      O N N 158 
HOH H1     H N N 159 
HOH H2     H N N 160 
ILE N      N N N 161 
ILE CA     C N S 162 
ILE C      C N N 163 
ILE O      O N N 164 
ILE CB     C N S 165 
ILE CG1    C N N 166 
ILE CG2    C N N 167 
ILE CD1    C N N 168 
ILE OXT    O N N 169 
ILE H      H N N 170 
ILE H2     H N N 171 
ILE HA     H N N 172 
ILE HB     H N N 173 
ILE HG12   H N N 174 
ILE HG13   H N N 175 
ILE HG21   H N N 176 
ILE HG22   H N N 177 
ILE HG23   H N N 178 
ILE HD11   H N N 179 
ILE HD12   H N N 180 
ILE HD13   H N N 181 
ILE HXT    H N N 182 
LEU N      N N N 183 
LEU CA     C N S 184 
LEU C      C N N 185 
LEU O      O N N 186 
LEU CB     C N N 187 
LEU CG     C N N 188 
LEU CD1    C N N 189 
LEU CD2    C N N 190 
LEU OXT    O N N 191 
LEU H      H N N 192 
LEU H2     H N N 193 
LEU HA     H N N 194 
LEU HB2    H N N 195 
LEU HB3    H N N 196 
LEU HG     H N N 197 
LEU HD11   H N N 198 
LEU HD12   H N N 199 
LEU HD13   H N N 200 
LEU HD21   H N N 201 
LEU HD22   H N N 202 
LEU HD23   H N N 203 
LEU HXT    H N N 204 
LLP N1     N Y N 205 
LLP C2     C Y N 206 
LLP "C2'"  C N N 207 
LLP C3     C Y N 208 
LLP O3     O N N 209 
LLP C4     C Y N 210 
LLP "C4'"  C N N 211 
LLP C5     C Y N 212 
LLP C6     C Y N 213 
LLP "C5'"  C N N 214 
LLP OP4    O N N 215 
LLP P      P N N 216 
LLP OP1    O N N 217 
LLP OP2    O N N 218 
LLP OP3    O N N 219 
LLP N      N N N 220 
LLP CA     C N S 221 
LLP CB     C N N 222 
LLP CG     C N N 223 
LLP CD     C N N 224 
LLP CE     C N N 225 
LLP NZ     N N N 226 
LLP C      C N N 227 
LLP O      O N N 228 
LLP OXT    O N N 229 
LLP "H2'1" H N N 230 
LLP "H2'2" H N N 231 
LLP "H2'3" H N N 232 
LLP HO3    H N N 233 
LLP "H4'1" H N N 234 
LLP H6     H N N 235 
LLP "H5'1" H N N 236 
LLP "H5'2" H N N 237 
LLP HOP2   H N N 238 
LLP HOP3   H N N 239 
LLP H      H N N 240 
LLP H2     H N N 241 
LLP HA     H N N 242 
LLP HB2    H N N 243 
LLP HB3    H N N 244 
LLP HG2    H N N 245 
LLP HG3    H N N 246 
LLP HD2    H N N 247 
LLP HD3    H N N 248 
LLP HE2    H N N 249 
LLP HE3    H N N 250 
LLP HXT    H N N 251 
LYS N      N N N 252 
LYS CA     C N S 253 
LYS C      C N N 254 
LYS O      O N N 255 
LYS CB     C N N 256 
LYS CG     C N N 257 
LYS CD     C N N 258 
LYS CE     C N N 259 
LYS NZ     N N N 260 
LYS OXT    O N N 261 
LYS H      H N N 262 
LYS H2     H N N 263 
LYS HA     H N N 264 
LYS HB2    H N N 265 
LYS HB3    H N N 266 
LYS HG2    H N N 267 
LYS HG3    H N N 268 
LYS HD2    H N N 269 
LYS HD3    H N N 270 
LYS HE2    H N N 271 
LYS HE3    H N N 272 
LYS HZ1    H N N 273 
LYS HZ2    H N N 274 
LYS HZ3    H N N 275 
LYS HXT    H N N 276 
MET N      N N N 277 
MET CA     C N S 278 
MET C      C N N 279 
MET O      O N N 280 
MET CB     C N N 281 
MET CG     C N N 282 
MET SD     S N N 283 
MET CE     C N N 284 
MET OXT    O N N 285 
MET H      H N N 286 
MET H2     H N N 287 
MET HA     H N N 288 
MET HB2    H N N 289 
MET HB3    H N N 290 
MET HG2    H N N 291 
MET HG3    H N N 292 
MET HE1    H N N 293 
MET HE2    H N N 294 
MET HE3    H N N 295 
MET HXT    H N N 296 
PHE N      N N N 297 
PHE CA     C N S 298 
PHE C      C N N 299 
PHE O      O N N 300 
PHE CB     C N N 301 
PHE CG     C Y N 302 
PHE CD1    C Y N 303 
PHE CD2    C Y N 304 
PHE CE1    C Y N 305 
PHE CE2    C Y N 306 
PHE CZ     C Y N 307 
PHE OXT    O N N 308 
PHE H      H N N 309 
PHE H2     H N N 310 
PHE HA     H N N 311 
PHE HB2    H N N 312 
PHE HB3    H N N 313 
PHE HD1    H N N 314 
PHE HD2    H N N 315 
PHE HE1    H N N 316 
PHE HE2    H N N 317 
PHE HZ     H N N 318 
PHE HXT    H N N 319 
PRO N      N N N 320 
PRO CA     C N S 321 
PRO C      C N N 322 
PRO O      O N N 323 
PRO CB     C N N 324 
PRO CG     C N N 325 
PRO CD     C N N 326 
PRO OXT    O N N 327 
PRO H      H N N 328 
PRO HA     H N N 329 
PRO HB2    H N N 330 
PRO HB3    H N N 331 
PRO HG2    H N N 332 
PRO HG3    H N N 333 
PRO HD2    H N N 334 
PRO HD3    H N N 335 
PRO HXT    H N N 336 
SER N      N N N 337 
SER CA     C N S 338 
SER C      C N N 339 
SER O      O N N 340 
SER CB     C N N 341 
SER OG     O N N 342 
SER OXT    O N N 343 
SER H      H N N 344 
SER H2     H N N 345 
SER HA     H N N 346 
SER HB2    H N N 347 
SER HB3    H N N 348 
SER HG     H N N 349 
SER HXT    H N N 350 
SO4 S      S N N 351 
SO4 O1     O N N 352 
SO4 O2     O N N 353 
SO4 O3     O N N 354 
SO4 O4     O N N 355 
THR N      N N N 356 
THR CA     C N S 357 
THR C      C N N 358 
THR O      O N N 359 
THR CB     C N R 360 
THR OG1    O N N 361 
THR CG2    C N N 362 
THR OXT    O N N 363 
THR H      H N N 364 
THR H2     H N N 365 
THR HA     H N N 366 
THR HB     H N N 367 
THR HG1    H N N 368 
THR HG21   H N N 369 
THR HG22   H N N 370 
THR HG23   H N N 371 
THR HXT    H N N 372 
TRP N      N N N 373 
TRP CA     C N S 374 
TRP C      C N N 375 
TRP O      O N N 376 
TRP CB     C N N 377 
TRP CG     C Y N 378 
TRP CD1    C Y N 379 
TRP CD2    C Y N 380 
TRP NE1    N Y N 381 
TRP CE2    C Y N 382 
TRP CE3    C Y N 383 
TRP CZ2    C Y N 384 
TRP CZ3    C Y N 385 
TRP CH2    C Y N 386 
TRP OXT    O N N 387 
TRP H      H N N 388 
TRP H2     H N N 389 
TRP HA     H N N 390 
TRP HB2    H N N 391 
TRP HB3    H N N 392 
TRP HD1    H N N 393 
TRP HE1    H N N 394 
TRP HE3    H N N 395 
TRP HZ2    H N N 396 
TRP HZ3    H N N 397 
TRP HH2    H N N 398 
TRP HXT    H N N 399 
TYR N      N N N 400 
TYR CA     C N S 401 
TYR C      C N N 402 
TYR O      O N N 403 
TYR CB     C N N 404 
TYR CG     C Y N 405 
TYR CD1    C Y N 406 
TYR CD2    C Y N 407 
TYR CE1    C Y N 408 
TYR CE2    C Y N 409 
TYR CZ     C Y N 410 
TYR OH     O N N 411 
TYR OXT    O N N 412 
TYR H      H N N 413 
TYR H2     H N N 414 
TYR HA     H N N 415 
TYR HB2    H N N 416 
TYR HB3    H N N 417 
TYR HD1    H N N 418 
TYR HD2    H N N 419 
TYR HE1    H N N 420 
TYR HE2    H N N 421 
TYR HH     H N N 422 
TYR HXT    H N N 423 
VAL N      N N N 424 
VAL CA     C N S 425 
VAL C      C N N 426 
VAL O      O N N 427 
VAL CB     C N N 428 
VAL CG1    C N N 429 
VAL CG2    C N N 430 
VAL OXT    O N N 431 
VAL H      H N N 432 
VAL H2     H N N 433 
VAL HA     H N N 434 
VAL HB     H N N 435 
VAL HG11   H N N 436 
VAL HG12   H N N 437 
VAL HG13   H N N 438 
VAL HG21   H N N 439 
VAL HG22   H N N 440 
VAL HG23   H N N 441 
VAL HXT    H N N 442 
# 
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 
LLP N1    C2     doub Y N 194 
LLP N1    C6     sing Y N 195 
LLP C2    "C2'"  sing N N 196 
LLP C2    C3     sing Y N 197 
LLP C3    O3     sing N N 198 
LLP C3    C4     doub Y N 199 
LLP C4    "C4'"  sing N N 200 
LLP C4    C5     sing Y N 201 
LLP "C4'" NZ     doub N N 202 
LLP C5    C6     doub Y N 203 
LLP C5    "C5'"  sing N N 204 
LLP "C5'" OP4    sing N N 205 
LLP OP4   P      sing N N 206 
LLP P     OP1    doub N N 207 
LLP P     OP2    sing N N 208 
LLP P     OP3    sing N N 209 
LLP N     CA     sing N N 210 
LLP CA    CB     sing N N 211 
LLP CA    C      sing N N 212 
LLP CB    CG     sing N N 213 
LLP CG    CD     sing N N 214 
LLP CD    CE     sing N N 215 
LLP CE    NZ     sing N N 216 
LLP C     O      doub N N 217 
LLP C     OXT    sing N N 218 
LLP "C2'" "H2'1" sing N N 219 
LLP "C2'" "H2'2" sing N N 220 
LLP "C2'" "H2'3" sing N N 221 
LLP O3    HO3    sing N N 222 
LLP "C4'" "H4'1" sing N N 223 
LLP C6    H6     sing N N 224 
LLP "C5'" "H5'1" sing N N 225 
LLP "C5'" "H5'2" sing N N 226 
LLP OP2   HOP2   sing N N 227 
LLP OP3   HOP3   sing N N 228 
LLP N     H      sing N N 229 
LLP N     H2     sing N N 230 
LLP CA    HA     sing N N 231 
LLP CB    HB2    sing N N 232 
LLP CB    HB3    sing N N 233 
LLP CG    HG2    sing N N 234 
LLP CG    HG3    sing N N 235 
LLP CD    HD2    sing N N 236 
LLP CD    HD3    sing N N 237 
LLP CE    HE2    sing N N 238 
LLP CE    HE3    sing N N 239 
LLP OXT   HXT    sing N N 240 
LYS N     CA     sing N N 241 
LYS N     H      sing N N 242 
LYS N     H2     sing N N 243 
LYS CA    C      sing N N 244 
LYS CA    CB     sing N N 245 
LYS CA    HA     sing N N 246 
LYS C     O      doub N N 247 
LYS C     OXT    sing N N 248 
LYS CB    CG     sing N N 249 
LYS CB    HB2    sing N N 250 
LYS CB    HB3    sing N N 251 
LYS CG    CD     sing N N 252 
LYS CG    HG2    sing N N 253 
LYS CG    HG3    sing N N 254 
LYS CD    CE     sing N N 255 
LYS CD    HD2    sing N N 256 
LYS CD    HD3    sing N N 257 
LYS CE    NZ     sing N N 258 
LYS CE    HE2    sing N N 259 
LYS CE    HE3    sing N N 260 
LYS NZ    HZ1    sing N N 261 
LYS NZ    HZ2    sing N N 262 
LYS NZ    HZ3    sing N N 263 
LYS OXT   HXT    sing N N 264 
MET N     CA     sing N N 265 
MET N     H      sing N N 266 
MET N     H2     sing N N 267 
MET CA    C      sing N N 268 
MET CA    CB     sing N N 269 
MET CA    HA     sing N N 270 
MET C     O      doub N N 271 
MET C     OXT    sing N N 272 
MET CB    CG     sing N N 273 
MET CB    HB2    sing N N 274 
MET CB    HB3    sing N N 275 
MET CG    SD     sing N N 276 
MET CG    HG2    sing N N 277 
MET CG    HG3    sing N N 278 
MET SD    CE     sing N N 279 
MET CE    HE1    sing N N 280 
MET CE    HE2    sing N N 281 
MET CE    HE3    sing N N 282 
MET OXT   HXT    sing N N 283 
PHE N     CA     sing N N 284 
PHE N     H      sing N N 285 
PHE N     H2     sing N N 286 
PHE CA    C      sing N N 287 
PHE CA    CB     sing N N 288 
PHE CA    HA     sing N N 289 
PHE C     O      doub N N 290 
PHE C     OXT    sing N N 291 
PHE CB    CG     sing N N 292 
PHE CB    HB2    sing N N 293 
PHE CB    HB3    sing N N 294 
PHE CG    CD1    doub Y N 295 
PHE CG    CD2    sing Y N 296 
PHE CD1   CE1    sing Y N 297 
PHE CD1   HD1    sing N N 298 
PHE CD2   CE2    doub Y N 299 
PHE CD2   HD2    sing N N 300 
PHE CE1   CZ     doub Y N 301 
PHE CE1   HE1    sing N N 302 
PHE CE2   CZ     sing Y N 303 
PHE CE2   HE2    sing N N 304 
PHE CZ    HZ     sing N N 305 
PHE OXT   HXT    sing N N 306 
PRO N     CA     sing N N 307 
PRO N     CD     sing N N 308 
PRO N     H      sing N N 309 
PRO CA    C      sing N N 310 
PRO CA    CB     sing N N 311 
PRO CA    HA     sing N N 312 
PRO C     O      doub N N 313 
PRO C     OXT    sing N N 314 
PRO CB    CG     sing N N 315 
PRO CB    HB2    sing N N 316 
PRO CB    HB3    sing N N 317 
PRO CG    CD     sing N N 318 
PRO CG    HG2    sing N N 319 
PRO CG    HG3    sing N N 320 
PRO CD    HD2    sing N N 321 
PRO CD    HD3    sing N N 322 
PRO OXT   HXT    sing N N 323 
SER N     CA     sing N N 324 
SER N     H      sing N N 325 
SER N     H2     sing N N 326 
SER CA    C      sing N N 327 
SER CA    CB     sing N N 328 
SER CA    HA     sing N N 329 
SER C     O      doub N N 330 
SER C     OXT    sing N N 331 
SER CB    OG     sing N N 332 
SER CB    HB2    sing N N 333 
SER CB    HB3    sing N N 334 
SER OG    HG     sing N N 335 
SER OXT   HXT    sing N N 336 
SO4 S     O1     doub N N 337 
SO4 S     O2     doub N N 338 
SO4 S     O3     sing N N 339 
SO4 S     O4     sing N N 340 
THR N     CA     sing N N 341 
THR N     H      sing N N 342 
THR N     H2     sing N N 343 
THR CA    C      sing N N 344 
THR CA    CB     sing N N 345 
THR CA    HA     sing N N 346 
THR C     O      doub N N 347 
THR C     OXT    sing N N 348 
THR CB    OG1    sing N N 349 
THR CB    CG2    sing N N 350 
THR CB    HB     sing N N 351 
THR OG1   HG1    sing N N 352 
THR CG2   HG21   sing N N 353 
THR CG2   HG22   sing N N 354 
THR CG2   HG23   sing N N 355 
THR OXT   HXT    sing N N 356 
TRP N     CA     sing N N 357 
TRP N     H      sing N N 358 
TRP N     H2     sing N N 359 
TRP CA    C      sing N N 360 
TRP CA    CB     sing N N 361 
TRP CA    HA     sing N N 362 
TRP C     O      doub N N 363 
TRP C     OXT    sing N N 364 
TRP CB    CG     sing N N 365 
TRP CB    HB2    sing N N 366 
TRP CB    HB3    sing N N 367 
TRP CG    CD1    doub Y N 368 
TRP CG    CD2    sing Y N 369 
TRP CD1   NE1    sing Y N 370 
TRP CD1   HD1    sing N N 371 
TRP CD2   CE2    doub Y N 372 
TRP CD2   CE3    sing Y N 373 
TRP NE1   CE2    sing Y N 374 
TRP NE1   HE1    sing N N 375 
TRP CE2   CZ2    sing Y N 376 
TRP CE3   CZ3    doub Y N 377 
TRP CE3   HE3    sing N N 378 
TRP CZ2   CH2    doub Y N 379 
TRP CZ2   HZ2    sing N N 380 
TRP CZ3   CH2    sing Y N 381 
TRP CZ3   HZ3    sing N N 382 
TRP CH2   HH2    sing N N 383 
TRP OXT   HXT    sing N N 384 
TYR N     CA     sing N N 385 
TYR N     H      sing N N 386 
TYR N     H2     sing N N 387 
TYR CA    C      sing N N 388 
TYR CA    CB     sing N N 389 
TYR CA    HA     sing N N 390 
TYR C     O      doub N N 391 
TYR C     OXT    sing N N 392 
TYR CB    CG     sing N N 393 
TYR CB    HB2    sing N N 394 
TYR CB    HB3    sing N N 395 
TYR CG    CD1    doub Y N 396 
TYR CG    CD2    sing Y N 397 
TYR CD1   CE1    sing Y N 398 
TYR CD1   HD1    sing N N 399 
TYR CD2   CE2    doub Y N 400 
TYR CD2   HD2    sing N N 401 
TYR CE1   CZ     doub Y N 402 
TYR CE1   HE1    sing N N 403 
TYR CE2   CZ     sing Y N 404 
TYR CE2   HE2    sing N N 405 
TYR CZ    OH     sing N N 406 
TYR OH    HH     sing N N 407 
TYR OXT   HXT    sing N N 408 
VAL N     CA     sing N N 409 
VAL N     H      sing N N 410 
VAL N     H2     sing N N 411 
VAL CA    C      sing N N 412 
VAL CA    CB     sing N N 413 
VAL CA    HA     sing N N 414 
VAL C     O      doub N N 415 
VAL C     OXT    sing N N 416 
VAL CB    CG1    sing N N 417 
VAL CB    CG2    sing N N 418 
VAL CB    HB     sing N N 419 
VAL CG1   HG11   sing N N 420 
VAL CG1   HG12   sing N N 421 
VAL CG1   HG13   sing N N 422 
VAL CG2   HG21   sing N N 423 
VAL CG2   HG22   sing N N 424 
VAL CG2   HG23   sing N N 425 
VAL OXT   HXT    sing N N 426 
# 
_pdbx_audit_support.funding_organization   'National Research Foundation (NRF, Korea)' 
_pdbx_audit_support.country                'Korea, Republic Of' 
_pdbx_audit_support.grant_number           RS-2023-00208153 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'R 3 2 :H' 
_space_group.name_Hall        
;R 3 2"
;
_space_group.IT_number        155 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9JQF 
_atom_sites.fract_transf_matrix[1][1]   0.008147 
_atom_sites.fract_transf_matrix[1][2]   0.004704 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009407 
_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]   0.009552 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . ASN A 1 8   ? 7.706   -54.738 -21.385 1.00 54.65 ? 2   ASN A N     1 
ATOM   2    C CA    . ASN A 1 8   ? 8.491   -53.827 -22.212 1.00 43.21 ? 2   ASN A CA    1 
ATOM   3    C C     . ASN A 1 8   ? 8.796   -52.511 -21.517 1.00 44.84 ? 2   ASN A C     1 
ATOM   4    O O     . ASN A 1 8   ? 7.898   -51.852 -20.994 1.00 48.44 ? 2   ASN A O     1 
ATOM   5    C CB    . ASN A 1 8   ? 7.764   -53.514 -23.520 1.00 44.97 ? 2   ASN A CB    1 
ATOM   6    C CG    . ASN A 1 8   ? 7.797   -54.660 -24.503 1.00 51.84 ? 2   ASN A CG    1 
ATOM   7    O OD1   . ASN A 1 8   ? 8.660   -55.534 -24.431 1.00 57.15 ? 2   ASN A OD1   1 
ATOM   8    N ND2   . ASN A 1 8   ? 6.858   -54.653 -25.444 1.00 53.73 ? 2   ASN A ND2   1 
ATOM   9    N N     . PHE A 1 9   ? 10.065  -52.115 -21.543 1.00 43.26 ? 3   PHE A N     1 
ATOM   10   C CA    . PHE A 1 9   ? 10.486  -50.780 -21.146 1.00 35.49 ? 3   PHE A CA    1 
ATOM   11   C C     . PHE A 1 9   ? 10.818  -50.019 -22.422 1.00 35.88 ? 3   PHE A C     1 
ATOM   12   O O     . PHE A 1 9   ? 11.647  -50.473 -23.217 1.00 38.34 ? 3   PHE A O     1 
ATOM   13   C CB    . PHE A 1 9   ? 11.696  -50.818 -20.212 1.00 37.12 ? 3   PHE A CB    1 
ATOM   14   C CG    . PHE A 1 9   ? 12.373  -49.488 -20.058 1.00 41.04 ? 3   PHE A CG    1 
ATOM   15   C CD1   . PHE A 1 9   ? 11.940  -48.580 -19.108 1.00 44.85 ? 3   PHE A CD1   1 
ATOM   16   C CD2   . PHE A 1 9   ? 13.432  -49.131 -20.885 1.00 49.16 ? 3   PHE A CD2   1 
ATOM   17   C CE1   . PHE A 1 9   ? 12.560  -47.342 -18.980 1.00 47.59 ? 3   PHE A CE1   1 
ATOM   18   C CE2   . PHE A 1 9   ? 14.050  -47.898 -20.763 1.00 45.81 ? 3   PHE A CE2   1 
ATOM   19   C CZ    . PHE A 1 9   ? 13.615  -47.004 -19.805 1.00 46.05 ? 3   PHE A CZ    1 
ATOM   20   N N     . ILE A 1 10  ? 10.147  -48.891 -22.638 1.00 33.13 ? 4   ILE A N     1 
ATOM   21   C CA    . ILE A 1 10  ? 10.369  -48.088 -23.833 1.00 30.99 ? 4   ILE A CA    1 
ATOM   22   C C     . ILE A 1 10  ? 10.442  -46.628 -23.422 1.00 26.09 ? 4   ILE A C     1 
ATOM   23   O O     . ILE A 1 10  ? 9.641   -46.157 -22.607 1.00 31.42 ? 4   ILE A O     1 
ATOM   24   C CB    . ILE A 1 10  ? 9.280   -48.295 -24.909 1.00 29.03 ? 4   ILE A CB    1 
ATOM   25   C CG1   . ILE A 1 10  ? 8.791   -49.744 -24.933 1.00 31.72 ? 4   ILE A CG1   1 
ATOM   26   C CG2   . ILE A 1 10  ? 9.846   -47.932 -26.265 1.00 34.49 ? 4   ILE A CG2   1 
ATOM   27   C CD1   . ILE A 1 10  ? 7.732   -49.994 -25.976 1.00 44.66 ? 4   ILE A CD1   1 
ATOM   28   N N     . LYS A 1 11  ? 11.413  -45.917 -23.984 1.00 22.82 ? 5   LYS A N     1 
ATOM   29   C CA    . LYS A 1 11  ? 11.649  -44.517 -23.677 1.00 21.35 ? 5   LYS A CA    1 
ATOM   30   C C     . LYS A 1 11  ? 12.110  -43.810 -24.943 1.00 20.81 ? 5   LYS A C     1 
ATOM   31   O O     . LYS A 1 11  ? 12.871  -44.376 -25.731 1.00 24.86 ? 5   LYS A O     1 
ATOM   32   C CB    . LYS A 1 11  ? 12.710  -44.355 -22.581 1.00 34.79 ? 5   LYS A CB    1 
ATOM   33   C CG    . LYS A 1 11  ? 13.013  -42.918 -22.211 1.00 39.53 ? 5   LYS A CG    1 
ATOM   34   N N     . THR A 1 12  ? 11.630  -42.593 -25.142 1.00 19.42 ? 6   THR A N     1 
ATOM   35   C CA    . THR A 1 12  ? 12.135  -41.751 -26.221 1.00 18.09 ? 6   THR A CA    1 
ATOM   36   C C     . THR A 1 12  ? 12.241  -40.330 -25.692 1.00 21.37 ? 6   THR A C     1 
ATOM   37   O O     . THR A 1 12  ? 11.805  -40.025 -24.575 1.00 23.67 ? 6   THR A O     1 
ATOM   38   C CB    . THR A 1 12  ? 11.241  -41.823 -27.466 1.00 20.23 ? 6   THR A CB    1 
ATOM   39   O OG1   . THR A 1 12  ? 11.888  -41.168 -28.571 1.00 24.95 ? 6   THR A OG1   1 
ATOM   40   C CG2   . THR A 1 12  ? 9.927   -41.127 -27.201 1.00 18.30 ? 6   THR A CG2   1 
ATOM   41   N N     . ILE A 1 13  ? 12.862  -39.461 -26.486 1.00 20.18 ? 7   ILE A N     1 
ATOM   42   C CA    . ILE A 1 13  ? 12.903  -38.039 -26.171 1.00 21.05 ? 7   ILE A CA    1 
ATOM   43   C C     . ILE A 1 13  ? 12.514  -37.296 -27.435 1.00 17.78 ? 7   ILE A C     1 
ATOM   44   O O     . ILE A 1 13  ? 12.715  -37.783 -28.555 1.00 18.49 ? 7   ILE A O     1 
ATOM   45   C CB    . ILE A 1 13  ? 14.280  -37.558 -25.650 1.00 26.08 ? 7   ILE A CB    1 
ATOM   46   C CG1   . ILE A 1 13  ? 15.338  -37.685 -26.737 1.00 26.20 ? 7   ILE A CG1   1 
ATOM   47   C CG2   . ILE A 1 13  ? 14.677  -38.306 -24.356 1.00 24.01 ? 7   ILE A CG2   1 
ATOM   48   C CD1   . ILE A 1 13  ? 16.672  -37.046 -26.356 1.00 32.58 ? 7   ILE A CD1   1 
ATOM   49   N N     . SER A 1 14  ? 11.926  -36.125 -27.265 1.00 15.00 ? 8   SER A N     1 
ATOM   50   C CA    . SER A 1 14  ? 11.362  -35.469 -28.432 1.00 14.30 ? 8   SER A CA    1 
ATOM   51   C C     . SER A 1 14  ? 12.475  -35.122 -29.414 1.00 16.32 ? 8   SER A C     1 
ATOM   52   O O     . SER A 1 14  ? 13.591  -34.769 -28.998 1.00 18.35 ? 8   SER A O     1 
ATOM   53   C CB    . SER A 1 14  ? 10.577  -34.215 -28.027 1.00 15.88 ? 8   SER A CB    1 
ATOM   54   O OG    . SER A 1 14  ? 11.416  -33.283 -27.380 1.00 18.08 ? 8   SER A OG    1 
ATOM   55   N N     . PRO A 1 15  ? 12.229  -35.241 -30.713 1.00 15.61 ? 9   PRO A N     1 
ATOM   56   C CA    . PRO A 1 15  ? 13.309  -35.085 -31.678 1.00 15.07 ? 9   PRO A CA    1 
ATOM   57   C C     . PRO A 1 15  ? 13.625  -33.623 -31.945 1.00 17.05 ? 9   PRO A C     1 
ATOM   58   O O     . PRO A 1 15  ? 12.836  -32.720 -31.664 1.00 17.27 ? 9   PRO A O     1 
ATOM   59   C CB    . PRO A 1 15  ? 12.762  -35.775 -32.939 1.00 18.45 ? 9   PRO A CB    1 
ATOM   60   C CG    . PRO A 1 15  ? 11.269  -35.551 -32.839 1.00 18.16 ? 9   PRO A CG    1 
ATOM   61   C CD    . PRO A 1 15  ? 10.962  -35.657 -31.350 1.00 19.84 ? 9   PRO A CD    1 
ATOM   62   N N     . ILE A 1 16  ? 14.820  -33.408 -32.483 1.00 17.46 ? 10  ILE A N     1 
ATOM   63   C CA    . ILE A 1 16  ? 15.231  -32.102 -32.975 1.00 17.23 ? 10  ILE A CA    1 
ATOM   64   C C     . ILE A 1 16  ? 15.164  -32.139 -34.491 1.00 20.39 ? 10  ILE A C     1 
ATOM   65   O O     . ILE A 1 16  ? 15.733  -33.036 -35.132 1.00 21.95 ? 10  ILE A O     1 
ATOM   66   C CB    . ILE A 1 16  ? 16.638  -31.734 -32.482 1.00 20.64 ? 10  ILE A CB    1 
ATOM   67   C CG1   . ILE A 1 16  ? 16.589  -31.465 -30.975 1.00 21.51 ? 10  ILE A CG1   1 
ATOM   68   C CG2   . ILE A 1 16  ? 17.165  -30.509 -33.225 1.00 22.77 ? 10  ILE A CG2   1 
ATOM   69   C CD1   . ILE A 1 16  ? 17.901  -30.990 -30.393 1.00 20.76 ? 10  ILE A CD1   1 
ATOM   70   N N     . GLN A 1 17  ? 14.455  -31.180 -35.065 1.00 18.64 ? 11  GLN A N     1 
ATOM   71   C CA    . GLN A 1 17  ? 14.163  -31.170 -36.488 1.00 16.60 ? 11  GLN A CA    1 
ATOM   72   C C     . GLN A 1 17  ? 14.798  -29.948 -37.131 1.00 18.66 ? 11  GLN A C     1 
ATOM   73   O O     . GLN A 1 17  ? 14.750  -28.853 -36.568 1.00 21.01 ? 11  GLN A O     1 
ATOM   74   C CB    . GLN A 1 17  ? 12.646  -31.153 -36.689 1.00 17.97 ? 11  GLN A CB    1 
ATOM   75   C CG    . GLN A 1 17  ? 12.176  -31.145 -38.115 1.00 22.49 ? 11  GLN A CG    1 
ATOM   76   C CD    . GLN A 1 17  ? 10.706  -31.498 -38.210 1.00 23.93 ? 11  GLN A CD    1 
ATOM   77   O OE1   . GLN A 1 17  ? 10.097  -31.924 -37.218 1.00 24.37 ? 11  GLN A OE1   1 
ATOM   78   N NE2   . GLN A 1 17  ? 10.138  -31.376 -39.406 1.00 22.30 ? 11  GLN A NE2   1 
ATOM   79   N N     . LYS A 1 18  ? 15.386  -30.137 -38.311 1.00 18.70 ? 12  LYS A N     1 
ATOM   80   C CA    . LYS A 1 18  ? 16.029  -29.051 -39.037 1.00 20.53 ? 12  LYS A CA    1 
ATOM   81   C C     . LYS A 1 18  ? 15.035  -28.362 -39.963 1.00 21.95 ? 12  LYS A C     1 
ATOM   82   O O     . LYS A 1 18  ? 14.239  -29.017 -40.638 1.00 25.77 ? 12  LYS A O     1 
ATOM   83   C CB    . LYS A 1 18  ? 17.217  -29.593 -39.832 1.00 24.96 ? 12  LYS A CB    1 
ATOM   84   C CG    . LYS A 1 18  ? 18.223  -28.554 -40.246 1.00 32.19 ? 12  LYS A CG    1 
ATOM   85   C CD    . LYS A 1 18  ? 19.462  -29.249 -40.823 1.00 37.12 ? 12  LYS A CD    1 
ATOM   86   C CE    . LYS A 1 18  ? 20.492  -28.245 -41.293 1.00 47.78 ? 12  LYS A CE    1 
ATOM   87   N NZ    . LYS A 1 18  ? 21.536  -28.908 -42.136 1.00 52.12 ? 12  LYS A NZ    1 
ATOM   88   N N     . ILE A 1 19  ? 15.095  -27.034 -40.008 1.00 19.64 ? 13  ILE A N     1 
ATOM   89   C CA    . ILE A 1 19  ? 14.196  -26.257 -40.853 1.00 20.09 ? 13  ILE A CA    1 
ATOM   90   C C     . ILE A 1 19  ? 14.987  -25.147 -41.533 1.00 23.68 ? 13  ILE A C     1 
ATOM   91   O O     . ILE A 1 19  ? 15.897  -24.566 -40.934 1.00 24.28 ? 13  ILE A O     1 
ATOM   92   C CB    . ILE A 1 19  ? 13.023  -25.689 -40.023 1.00 27.30 ? 13  ILE A CB    1 
ATOM   93   C CG1   . ILE A 1 19  ? 12.184  -24.717 -40.842 1.00 26.69 ? 13  ILE A CG1   1 
ATOM   94   C CG2   . ILE A 1 19  ? 13.540  -25.018 -38.771 1.00 36.67 ? 13  ILE A CG2   1 
ATOM   95   C CD1   . ILE A 1 19  ? 10.886  -24.312 -40.166 1.00 36.03 ? 13  ILE A CD1   1 
ATOM   96   N N     . ASN A 1 20  ? 14.632  -24.850 -42.785 1.00 20.95 ? 14  ASN A N     1 
ATOM   97   C CA    . ASN A 1 20  ? 15.240  -23.781 -43.567 1.00 22.25 ? 14  ASN A CA    1 
ATOM   98   C C     . ASN A 1 20  ? 14.171  -22.732 -43.815 1.00 23.03 ? 14  ASN A C     1 
ATOM   99   O O     . ASN A 1 20  ? 13.188  -23.001 -44.511 1.00 27.83 ? 14  ASN A O     1 
ATOM   100  C CB    . ASN A 1 20  ? 15.792  -24.311 -44.895 1.00 27.75 ? 14  ASN A CB    1 
ATOM   101  C CG    . ASN A 1 20  ? 16.475  -23.236 -45.724 1.00 36.96 ? 14  ASN A CG    1 
ATOM   102  O OD1   . ASN A 1 20  ? 16.200  -22.042 -45.582 1.00 36.47 ? 14  ASN A OD1   1 
ATOM   103  N ND2   . ASN A 1 20  ? 17.365  -23.661 -46.613 1.00 45.87 ? 14  ASN A ND2   1 
ATOM   104  N N     . PHE A 1 21  ? 14.360  -21.541 -43.255 1.00 24.84 ? 15  PHE A N     1 
ATOM   105  C CA    . PHE A 1 21  ? 13.421  -20.436 -43.435 1.00 27.13 ? 15  PHE A CA    1 
ATOM   106  C C     . PHE A 1 21  ? 14.139  -19.329 -44.202 1.00 28.51 ? 15  PHE A C     1 
ATOM   107  O O     . PHE A 1 21  ? 14.951  -18.595 -43.627 1.00 29.28 ? 15  PHE A O     1 
ATOM   108  C CB    . PHE A 1 21  ? 12.903  -19.955 -42.079 1.00 26.18 ? 15  PHE A CB    1 
ATOM   109  C CG    . PHE A 1 21  ? 11.848  -18.892 -42.172 1.00 32.96 ? 15  PHE A CG    1 
ATOM   110  C CD1   . PHE A 1 21  ? 12.194  -17.554 -42.153 1.00 32.96 ? 15  PHE A CD1   1 
ATOM   111  C CD2   . PHE A 1 21  ? 10.510  -19.233 -42.263 1.00 39.41 ? 15  PHE A CD2   1 
ATOM   112  C CE1   . PHE A 1 21  ? 11.226  -16.575 -42.227 1.00 41.92 ? 15  PHE A CE1   1 
ATOM   113  C CE2   . PHE A 1 21  ? 9.538   -18.256 -42.344 1.00 35.31 ? 15  PHE A CE2   1 
ATOM   114  C CZ    . PHE A 1 21  ? 9.894   -16.931 -42.325 1.00 37.98 ? 15  PHE A CZ    1 
ATOM   115  N N     . ASN A 1 22  ? 13.838  -19.221 -45.498 1.00 28.73 ? 16  ASN A N     1 
ATOM   116  C CA    . ASN A 1 22  ? 14.409  -18.189 -46.376 1.00 31.03 ? 16  ASN A CA    1 
ATOM   117  C C     . ASN A 1 22  ? 15.932  -18.217 -46.357 1.00 38.88 ? 16  ASN A C     1 
ATOM   118  O O     . ASN A 1 22  ? 16.595  -17.178 -46.394 1.00 40.65 ? 16  ASN A O     1 
ATOM   119  C CB    . ASN A 1 22  ? 13.900  -16.790 -46.011 1.00 38.50 ? 16  ASN A CB    1 
ATOM   120  C CG    . ASN A 1 22  ? 12.421  -16.623 -46.267 1.00 43.19 ? 16  ASN A CG    1 
ATOM   121  O OD1   . ASN A 1 22  ? 11.892  -17.132 -47.250 1.00 42.72 ? 16  ASN A OD1   1 
ATOM   122  N ND2   . ASN A 1 22  ? 11.742  -15.908 -45.377 1.00 50.26 ? 16  ASN A ND2   1 
ATOM   123  N N     . GLY A 1 23  ? 16.497  -19.419 -46.297 1.00 30.53 ? 17  GLY A N     1 
ATOM   124  C CA    . GLY A 1 23  ? 17.929  -19.585 -46.307 1.00 29.49 ? 17  GLY A CA    1 
ATOM   125  C C     . GLY A 1 23  ? 18.554  -19.674 -44.939 1.00 35.03 ? 17  GLY A C     1 
ATOM   126  O O     . GLY A 1 23  ? 19.730  -20.037 -44.841 1.00 34.65 ? 17  GLY A O     1 
ATOM   127  N N     . PHE A 1 24  ? 17.806  -19.360 -43.886 1.00 32.32 ? 18  PHE A N     1 
ATOM   128  C CA    . PHE A 1 24  ? 18.293  -19.477 -42.518 1.00 27.80 ? 18  PHE A CA    1 
ATOM   129  C C     . PHE A 1 24  ? 17.904  -20.847 -41.982 1.00 23.02 ? 18  PHE A C     1 
ATOM   130  O O     . PHE A 1 24  ? 16.725  -21.102 -41.713 1.00 25.17 ? 18  PHE A O     1 
ATOM   131  C CB    . PHE A 1 24  ? 17.723  -18.365 -41.640 1.00 29.13 ? 18  PHE A CB    1 
ATOM   132  C CG    . PHE A 1 24  ? 18.060  -18.522 -40.186 1.00 30.08 ? 18  PHE A CG    1 
ATOM   133  C CD1   . PHE A 1 24  ? 17.058  -18.602 -39.233 1.00 31.30 ? 18  PHE A CD1   1 
ATOM   134  C CD2   . PHE A 1 24  ? 19.381  -18.606 -39.779 1.00 29.08 ? 18  PHE A CD2   1 
ATOM   135  C CE1   . PHE A 1 24  ? 17.366  -18.753 -37.898 1.00 30.78 ? 18  PHE A CE1   1 
ATOM   136  C CE2   . PHE A 1 24  ? 19.695  -18.761 -38.440 1.00 30.00 ? 18  PHE A CE2   1 
ATOM   137  C CZ    . PHE A 1 24  ? 18.689  -18.827 -37.507 1.00 25.30 ? 18  PHE A CZ    1 
ATOM   138  N N     . GLU A 1 25  ? 18.894  -21.719 -41.811 1.00 26.40 ? 19  GLU A N     1 
ATOM   139  C CA    . GLU A 1 25  ? 18.672  -23.056 -41.277 1.00 22.84 ? 19  GLU A CA    1 
ATOM   140  C C     . GLU A 1 25  ? 18.776  -23.009 -39.758 1.00 23.95 ? 19  GLU A C     1 
ATOM   141  O O     . GLU A 1 25  ? 19.760  -22.497 -39.215 1.00 25.46 ? 19  GLU A O     1 
ATOM   142  C CB    . GLU A 1 25  ? 19.690  -24.046 -41.846 1.00 28.17 ? 19  GLU A CB    1 
ATOM   143  C CG    . GLU A 1 25  ? 19.596  -24.222 -43.364 1.00 32.49 ? 19  GLU A CG    1 
ATOM   144  C CD    . GLU A 1 25  ? 20.745  -25.029 -43.930 1.00 45.51 ? 19  GLU A CD    1 
ATOM   145  O OE1   . GLU A 1 25  ? 21.324  -25.832 -43.171 1.00 54.33 ? 19  GLU A OE1   1 
ATOM   146  O OE2   . GLU A 1 25  ? 21.075  -24.845 -45.125 1.00 51.68 ? 19  GLU A OE2   1 
ATOM   147  N N     . PHE A 1 26  ? 17.756  -23.520 -39.073 1.00 19.43 ? 20  PHE A N     1 
ATOM   148  C CA    . PHE A 1 26  ? 17.804  -23.609 -37.614 1.00 20.05 ? 20  PHE A CA    1 
ATOM   149  C C     . PHE A 1 26  ? 17.140  -24.918 -37.203 1.00 18.34 ? 20  PHE A C     1 
ATOM   150  O O     . PHE A 1 26  ? 16.791  -25.751 -38.046 1.00 20.59 ? 20  PHE A O     1 
ATOM   151  C CB    . PHE A 1 26  ? 17.180  -22.366 -36.951 1.00 21.74 ? 20  PHE A CB    1 
ATOM   152  C CG    . PHE A 1 26  ? 15.703  -22.197 -37.188 1.00 21.48 ? 20  PHE A CG    1 
ATOM   153  C CD1   . PHE A 1 26  ? 15.216  -21.708 -38.402 1.00 21.55 ? 20  PHE A CD1   1 
ATOM   154  C CD2   . PHE A 1 26  ? 14.796  -22.492 -36.178 1.00 22.17 ? 20  PHE A CD2   1 
ATOM   155  C CE1   . PHE A 1 26  ? 13.858  -21.541 -38.601 1.00 24.45 ? 20  PHE A CE1   1 
ATOM   156  C CE2   . PHE A 1 26  ? 13.434  -22.329 -36.378 1.00 21.05 ? 20  PHE A CE2   1 
ATOM   157  C CZ    . PHE A 1 26  ? 12.966  -21.853 -37.582 1.00 24.91 ? 20  PHE A CZ    1 
ATOM   158  N N     . TYR A 1 27  ? 17.001  -25.134 -35.891 1.00 17.17 ? 21  TYR A N     1 
ATOM   159  C CA    . TYR A 1 27  ? 16.543  -26.414 -35.369 1.00 18.82 ? 21  TYR A CA    1 
ATOM   160  C C     . TYR A 1 27  ? 15.356  -26.175 -34.453 1.00 17.69 ? 21  TYR A C     1 
ATOM   161  O O     . TYR A 1 27  ? 15.305  -25.154 -33.771 1.00 18.50 ? 21  TYR A O     1 
ATOM   162  C CB    . TYR A 1 27  ? 17.671  -27.127 -34.614 1.00 17.84 ? 21  TYR A CB    1 
ATOM   163  C CG    . TYR A 1 27  ? 18.874  -27.383 -35.507 1.00 17.60 ? 21  TYR A CG    1 
ATOM   164  C CD1   . TYR A 1 27  ? 19.063  -28.619 -36.088 1.00 19.67 ? 21  TYR A CD1   1 
ATOM   165  C CD2   . TYR A 1 27  ? 19.797  -26.380 -35.770 1.00 21.95 ? 21  TYR A CD2   1 
ATOM   166  C CE1   . TYR A 1 27  ? 20.163  -28.872 -36.907 1.00 18.64 ? 21  TYR A CE1   1 
ATOM   167  C CE2   . TYR A 1 27  ? 20.893  -26.613 -36.605 1.00 23.27 ? 21  TYR A CE2   1 
ATOM   168  C CZ    . TYR A 1 27  ? 21.063  -27.858 -37.166 1.00 25.96 ? 21  TYR A CZ    1 
ATOM   169  O OH    . TYR A 1 27  ? 22.145  -28.097 -37.979 1.00 32.46 ? 21  TYR A OH    1 
ATOM   170  N N     . ILE A 1 28  ? 14.390  -27.098 -34.459 1.00 16.99 ? 22  ILE A N     1 
ATOM   171  C CA    . ILE A 1 28  ? 13.234  -27.023 -33.567 1.00 15.21 ? 22  ILE A CA    1 
ATOM   172  C C     . ILE A 1 28  ? 13.226  -28.262 -32.683 1.00 17.83 ? 22  ILE A C     1 
ATOM   173  O O     . ILE A 1 28  ? 13.330  -29.394 -33.181 1.00 17.95 ? 22  ILE A O     1 
ATOM   174  C CB    . ILE A 1 28  ? 11.907  -26.909 -34.343 1.00 18.44 ? 22  ILE A CB    1 
ATOM   175  C CG1   . ILE A 1 28  ? 11.856  -25.620 -35.172 1.00 28.76 ? 22  ILE A CG1   1 
ATOM   176  C CG2   . ILE A 1 28  ? 10.709  -26.923 -33.381 1.00 18.30 ? 22  ILE A CG2   1 
ATOM   177  C CD1   . ILE A 1 28  ? 10.719  -25.617 -36.207 1.00 32.56 ? 22  ILE A CD1   1 
ATOM   178  N N     . LYS A 1 29  ? 13.093  -28.047 -31.375 1.00 15.22 ? 23  LYS A N     1 
ATOM   179  C CA    . LYS A 1 29  ? 12.888  -29.134 -30.423 1.00 15.90 ? 23  LYS A CA    1 
ATOM   180  C C     . LYS A 1 29  ? 11.392  -29.435 -30.404 1.00 17.15 ? 23  LYS A C     1 
ATOM   181  O O     . LYS A 1 29  ? 10.600  -28.619 -29.924 1.00 15.57 ? 23  LYS A O     1 
ATOM   182  C CB    . LYS A 1 29  ? 13.429  -28.728 -29.054 1.00 14.70 ? 23  LYS A CB    1 
ATOM   183  C CG    . LYS A 1 29  ? 13.115  -29.682 -27.884 1.00 16.59 ? 23  LYS A CG    1 
ATOM   184  C CD    . LYS A 1 29  ? 13.846  -31.021 -28.030 1.00 16.57 ? 23  LYS A CD    1 
ATOM   185  C CE    . LYS A 1 29  ? 13.907  -31.679 -26.653 1.00 15.89 ? 23  LYS A CE    1 
ATOM   186  N NZ    . LYS A 1 29  ? 14.199  -33.160 -26.794 1.00 15.62 ? 23  LYS A NZ    1 
ATOM   187  N N     . ARG A 1 30  ? 11.000  -30.594 -30.953 1.00 16.90 ? 24  ARG A N     1 
ATOM   188  C CA    . ARG A 1 30  ? 9.590   -30.906 -31.228 1.00 18.76 ? 24  ARG A CA    1 
ATOM   189  C C     . ARG A 1 30  ? 8.850   -31.399 -29.980 1.00 16.40 ? 24  ARG A C     1 
ATOM   190  O O     . ARG A 1 30  ? 8.338   -32.517 -29.935 1.00 16.26 ? 24  ARG A O     1 
ATOM   191  C CB    . ARG A 1 30  ? 9.472   -31.956 -32.331 1.00 15.17 ? 24  ARG A CB    1 
ATOM   192  C CG    . ARG A 1 30  ? 9.913   -31.534 -33.711 1.00 18.51 ? 24  ARG A CG    1 
ATOM   193  C CD    . ARG A 1 30  ? 8.998   -30.491 -34.342 1.00 18.90 ? 24  ARG A CD    1 
ATOM   194  N NE    . ARG A 1 30  ? 7.572   -30.824 -34.335 1.00 18.31 ? 24  ARG A NE    1 
ATOM   195  C CZ    . ARG A 1 30  ? 6.913   -31.415 -35.332 1.00 20.18 ? 24  ARG A CZ    1 
ATOM   196  N NH1   . ARG A 1 30  ? 7.551   -31.820 -36.443 1.00 20.90 ? 24  ARG A NH1   1 
ATOM   197  N NH2   . ARG A 1 30  ? 5.596   -31.609 -35.211 1.00 20.28 ? 24  ARG A NH2   1 
ATOM   198  N N     . ASP A 1 31  ? 8.754   -30.524 -28.975 1.00 13.67 ? 25  ASP A N     1 
ATOM   199  C CA    . ASP A 1 31  ? 8.043   -30.892 -27.757 1.00 15.96 ? 25  ASP A CA    1 
ATOM   200  C C     . ASP A 1 31  ? 6.540   -31.014 -27.985 1.00 19.91 ? 25  ASP A C     1 
ATOM   201  O O     . ASP A 1 31  ? 5.839   -31.540 -27.114 1.00 18.25 ? 25  ASP A O     1 
ATOM   202  C CB    . ASP A 1 31  ? 8.319   -29.863 -26.642 1.00 17.54 ? 25  ASP A CB    1 
ATOM   203  C CG    . ASP A 1 31  ? 9.566   -30.185 -25.837 1.00 16.06 ? 25  ASP A CG    1 
ATOM   204  O OD1   . ASP A 1 31  ? 10.326  -31.104 -26.230 1.00 17.44 ? 25  ASP A OD1   1 
ATOM   205  O OD2   . ASP A 1 31  ? 9.805   -29.496 -24.809 1.00 16.04 ? 25  ASP A OD2   1 
ATOM   206  N N     . ASP A 1 32  ? 6.024   -30.545 -29.125 1.00 16.91 ? 26  ASP A N     1 
ATOM   207  C CA    . ASP A 1 32  ? 4.624   -30.797 -29.428 1.00 18.79 ? 26  ASP A CA    1 
ATOM   208  C C     . ASP A 1 32  ? 4.341   -32.278 -29.635 1.00 20.57 ? 26  ASP A C     1 
ATOM   209  O O     . ASP A 1 32  ? 3.169   -32.674 -29.623 1.00 22.88 ? 26  ASP A O     1 
ATOM   210  C CB    . ASP A 1 32  ? 4.186   -29.995 -30.663 1.00 17.18 ? 26  ASP A CB    1 
ATOM   211  C CG    . ASP A 1 32  ? 5.028   -30.296 -31.896 1.00 18.78 ? 26  ASP A CG    1 
ATOM   212  O OD1   . ASP A 1 32  ? 6.256   -30.472 -31.757 1.00 18.47 ? 26  ASP A OD1   1 
ATOM   213  O OD2   . ASP A 1 32  ? 4.452   -30.336 -33.003 1.00 21.81 ? 26  ASP A OD2   1 
ATOM   214  N N     . LEU A 1 33  ? 5.378   -33.101 -29.791 1.00 17.58 ? 27  LEU A N     1 
ATOM   215  C CA    . LEU A 1 33  ? 5.233   -34.536 -30.016 1.00 17.79 ? 27  LEU A CA    1 
ATOM   216  C C     . LEU A 1 33  ? 5.315   -35.357 -28.732 1.00 19.87 ? 27  LEU A C     1 
ATOM   217  O O     . LEU A 1 33  ? 5.406   -36.588 -28.809 1.00 24.28 ? 27  LEU A O     1 
ATOM   218  C CB    . LEU A 1 33  ? 6.308   -35.021 -30.986 1.00 17.42 ? 27  LEU A CB    1 
ATOM   219  C CG    . LEU A 1 33  ? 6.355   -34.309 -32.339 1.00 21.33 ? 27  LEU A CG    1 
ATOM   220  C CD1   . LEU A 1 33  ? 7.521   -34.833 -33.196 1.00 22.43 ? 27  LEU A CD1   1 
ATOM   221  C CD2   . LEU A 1 33  ? 5.034   -34.496 -33.069 1.00 24.68 ? 27  LEU A CD2   1 
ATOM   222  N N     . LEU A 1 34  ? 5.291   -34.710 -27.562 1.00 20.81 ? 28  LEU A N     1 
ATOM   223  C CA    . LEU A 1 34  ? 5.450   -35.444 -26.308 1.00 22.81 ? 28  LEU A CA    1 
ATOM   224  C C     . LEU A 1 34  ? 4.245   -36.304 -25.955 1.00 24.36 ? 28  LEU A C     1 
ATOM   225  O O     . LEU A 1 34  ? 4.382   -37.201 -25.122 1.00 30.95 ? 28  LEU A O     1 
ATOM   226  C CB    . LEU A 1 34  ? 5.735   -34.478 -25.152 1.00 18.38 ? 28  LEU A CB    1 
ATOM   227  C CG    . LEU A 1 34  ? 7.153   -33.890 -25.142 1.00 20.30 ? 28  LEU A CG    1 
ATOM   228  C CD1   . LEU A 1 34  ? 7.246   -32.804 -24.075 1.00 24.65 ? 28  LEU A CD1   1 
ATOM   229  C CD2   . LEU A 1 34  ? 8.205   -34.976 -24.926 1.00 24.24 ? 28  LEU A CD2   1 
ATOM   230  N N     . GLY A 1 35  ? 3.082   -36.064 -26.541 1.00 24.74 ? 29  GLY A N     1 
ATOM   231  C CA    . GLY A 1 35  ? 1.928   -36.876 -26.229 1.00 30.18 ? 29  GLY A CA    1 
ATOM   232  C C     . GLY A 1 35  ? 0.683   -36.035 -26.078 1.00 25.94 ? 29  GLY A C     1 
ATOM   233  O O     . GLY A 1 35  ? 0.656   -34.855 -26.429 1.00 27.51 ? 29  GLY A O     1 
ATOM   234  N N     . GLU A 1 36  ? -0.375  -36.677 -25.568 1.00 27.83 ? 30  GLU A N     1 
ATOM   235  C CA    . GLU A 1 36  ? -1.619  -35.967 -25.305 1.00 31.36 ? 30  GLU A CA    1 
ATOM   236  C C     . GLU A 1 36  ? -1.356  -34.748 -24.445 1.00 30.69 ? 30  GLU A C     1 
ATOM   237  O O     . GLU A 1 36  ? -1.918  -33.673 -24.683 1.00 37.33 ? 30  GLU A O     1 
ATOM   238  C CB    . GLU A 1 36  ? -2.621  -36.889 -24.617 1.00 30.47 ? 30  GLU A CB    1 
ATOM   239  C CG    . GLU A 1 36  ? -3.892  -37.135 -25.379 1.00 50.98 ? 30  GLU A CG    1 
ATOM   240  C CD    . GLU A 1 36  ? -5.014  -37.557 -24.453 1.00 57.79 ? 30  GLU A CD    1 
ATOM   241  O OE1   . GLU A 1 36  ? -6.011  -36.811 -24.352 1.00 62.39 ? 30  GLU A OE1   1 
ATOM   242  O OE2   . GLU A 1 36  ? -4.881  -38.618 -23.804 1.00 60.56 ? 30  GLU A OE2   1 
ATOM   243  N N     . ILE A 1 37  ? -0.492  -34.894 -23.448 1.00 22.95 ? 31  ILE A N     1 
ATOM   244  C CA    . ILE A 1 37  ? 0.089   -33.750 -22.758 1.00 21.38 ? 31  ILE A CA    1 
ATOM   245  C C     . ILE A 1 37  ? 1.407   -33.439 -23.453 1.00 21.66 ? 31  ILE A C     1 
ATOM   246  O O     . ILE A 1 37  ? 2.301   -34.291 -23.506 1.00 22.38 ? 31  ILE A O     1 
ATOM   247  C CB    . ILE A 1 37  ? 0.315   -34.031 -21.264 1.00 27.40 ? 31  ILE A CB    1 
ATOM   248  C CG1   . ILE A 1 37  ? -0.904  -34.679 -20.616 1.00 29.62 ? 31  ILE A CG1   1 
ATOM   249  C CG2   . ILE A 1 37  ? 0.615   -32.734 -20.539 1.00 30.51 ? 31  ILE A CG2   1 
ATOM   250  C CD1   . ILE A 1 37  ? -0.718  -34.937 -19.136 1.00 34.27 ? 31  ILE A CD1   1 
ATOM   251  N N     . ASN A 1 38  ? 1.540   -32.233 -24.000 1.00 20.36 ? 32  ASN A N     1 
ATOM   252  C CA    . ASN A 1 38  ? 2.749   -31.925 -24.756 1.00 17.84 ? 32  ASN A CA    1 
ATOM   253  C C     . ASN A 1 38  ? 3.157   -30.476 -24.521 1.00 20.57 ? 32  ASN A C     1 
ATOM   254  O O     . ASN A 1 38  ? 2.460   -29.701 -23.856 1.00 19.97 ? 32  ASN A O     1 
ATOM   255  C CB    . ASN A 1 38  ? 2.572   -32.226 -26.257 1.00 20.64 ? 32  ASN A CB    1 
ATOM   256  C CG    . ASN A 1 38  ? 1.478   -31.386 -26.909 1.00 24.93 ? 32  ASN A CG    1 
ATOM   257  O OD1   . ASN A 1 38  ? 1.620   -30.168 -27.079 1.00 23.37 ? 32  ASN A OD1   1 
ATOM   258  N ND2   . ASN A 1 38  ? 0.382   -32.041 -27.287 1.00 27.84 ? 32  ASN A ND2   1 
ATOM   259  N N     . GLY A 1 39  ? 4.338   -30.138 -25.029 1.00 17.49 ? 33  GLY A N     1 
ATOM   260  C CA    . GLY A 1 39  ? 4.778   -28.759 -25.015 1.00 18.03 ? 33  GLY A CA    1 
ATOM   261  C C     . GLY A 1 39  ? 5.124   -28.268 -23.617 1.00 18.99 ? 33  GLY A C     1 
ATOM   262  O O     . GLY A 1 39  ? 5.482   -29.034 -22.709 1.00 17.19 ? 33  GLY A O     1 
ATOM   263  N N     . ASN A 1 40  ? 4.990   -26.953 -23.467 1.00 17.57 ? 34  ASN A N     1 
ATOM   264  C CA    . ASN A 1 40  ? 5.358   -26.232 -22.255 1.00 14.51 ? 34  ASN A CA    1 
ATOM   265  C C     . ASN A 1 40  ? 4.719   -26.850 -21.015 1.00 19.74 ? 34  ASN A C     1 
ATOM   266  O O     . ASN A 1 40  ? 5.410   -27.201 -20.045 1.00 18.00 ? 34  ASN A O     1 
ATOM   267  C CB    . ASN A 1 40  ? 4.923   -24.776 -22.453 1.00 15.67 ? 34  ASN A CB    1 
ATOM   268  C CG    . ASN A 1 40  ? 5.275   -23.881 -21.292 1.00 17.69 ? 34  ASN A CG    1 
ATOM   269  O OD1   . ASN A 1 40  ? 4.819   -24.093 -20.175 1.00 20.08 ? 34  ASN A OD1   1 
ATOM   270  N ND2   . ASN A 1 40  ? 6.045   -22.832 -21.568 1.00 18.79 ? 34  ASN A ND2   1 
HETATM 271  N N1    . LLP A 1 41  ? 3.637   -20.941 -24.709 1.00 17.36 ? 35  LLP A N1    1 
HETATM 272  C C2    . LLP A 1 41  ? 2.672   -21.886 -24.529 1.00 18.17 ? 35  LLP A C2    1 
HETATM 273  C "C2'" . LLP A 1 41  ? 2.132   -22.599 -25.740 1.00 19.13 ? 35  LLP A "C2'" 1 
HETATM 274  C C3    . LLP A 1 41  ? 2.215   -22.172 -23.251 1.00 21.10 ? 35  LLP A C3    1 
HETATM 275  O O3    . LLP A 1 41  ? 1.268   -23.145 -23.112 1.00 21.24 ? 35  LLP A O3    1 
HETATM 276  C C4    . LLP A 1 41  ? 2.728   -21.473 -22.151 1.00 16.18 ? 35  LLP A C4    1 
HETATM 277  C "C4'" . LLP A 1 41  ? 2.355   -21.852 -20.752 1.00 19.03 ? 35  LLP A "C4'" 1 
HETATM 278  C C5    . LLP A 1 41  ? 3.711   -20.493 -22.363 1.00 17.29 ? 35  LLP A C5    1 
HETATM 279  C C6    . LLP A 1 41  ? 4.152   -20.237 -23.651 1.00 16.43 ? 35  LLP A C6    1 
HETATM 280  C "C5'" . LLP A 1 41  ? 4.323   -19.644 -21.272 1.00 19.85 ? 35  LLP A "C5'" 1 
HETATM 281  O OP4   . LLP A 1 41  ? 5.050   -20.297 -20.251 1.00 18.50 ? 35  LLP A OP4   1 
HETATM 282  P P     . LLP A 1 41  ? 5.687   -19.388 -19.081 1.00 17.96 ? 35  LLP A P     1 
HETATM 283  O OP1   . LLP A 1 41  ? 4.491   -18.856 -18.297 1.00 20.58 ? 35  LLP A OP1   1 
HETATM 284  O OP2   . LLP A 1 41  ? 6.519   -20.330 -18.262 1.00 19.73 ? 35  LLP A OP2   1 
HETATM 285  O OP3   . LLP A 1 41  ? 6.477   -18.240 -19.667 1.00 16.92 ? 35  LLP A OP3   1 
HETATM 286  N N     . LLP A 1 41  ? 3.397   -27.006 -21.030 1.00 17.56 ? 35  LLP A N     1 
HETATM 287  C CA    . LLP A 1 41  ? 2.734   -27.480 -19.813 1.00 17.66 ? 35  LLP A CA    1 
HETATM 288  C CB    . LLP A 1 41  ? 1.220   -27.269 -19.903 1.00 17.58 ? 35  LLP A CB    1 
HETATM 289  C CG    . LLP A 1 41  ? 0.798   -25.809 -20.130 1.00 19.38 ? 35  LLP A CG    1 
HETATM 290  C CD    . LLP A 1 41  ? 1.417   -24.879 -19.090 1.00 18.43 ? 35  LLP A CD    1 
HETATM 291  C CE    . LLP A 1 41  ? 0.952   -23.441 -19.294 1.00 19.97 ? 35  LLP A CE    1 
HETATM 292  N NZ    . LLP A 1 41  ? 1.417   -22.921 -20.605 1.00 19.92 ? 35  LLP A NZ    1 
HETATM 293  C C     . LLP A 1 41  ? 3.073   -28.937 -19.514 1.00 17.96 ? 35  LLP A C     1 
HETATM 294  O O     . LLP A 1 41  ? 3.040   -29.342 -18.342 1.00 18.75 ? 35  LLP A O     1 
ATOM   295  N N     . ALA A 1 42  ? 3.420   -29.731 -20.539 1.00 17.36 ? 36  ALA A N     1 
ATOM   296  C CA    . ALA A 1 42  ? 3.912   -31.082 -20.273 1.00 20.78 ? 36  ALA A CA    1 
ATOM   297  C C     . ALA A 1 42  ? 5.235   -31.047 -19.525 1.00 19.31 ? 36  ALA A C     1 
ATOM   298  O O     . ALA A 1 42  ? 5.460   -31.849 -18.606 1.00 18.82 ? 36  ALA A O     1 
ATOM   299  C CB    . ALA A 1 42  ? 4.078   -31.867 -21.573 1.00 19.94 ? 36  ALA A CB    1 
ATOM   300  N N     . ARG A 1 43  ? 6.145   -30.160 -19.934 1.00 15.28 ? 37  ARG A N     1 
ATOM   301  C CA    . ARG A 1 43  ? 7.397   -30.004 -19.201 1.00 16.17 ? 37  ARG A CA    1 
ATOM   302  C C     . ARG A 1 43  ? 7.126   -29.563 -17.767 1.00 17.37 ? 37  ARG A C     1 
ATOM   303  O O     . ARG A 1 43  ? 7.642   -30.153 -16.806 1.00 16.78 ? 37  ARG A O     1 
ATOM   304  C CB    . ARG A 1 43  ? 8.314   -29.002 -19.920 1.00 15.85 ? 37  ARG A CB    1 
ATOM   305  C CG    . ARG A 1 43  ? 8.777   -29.466 -21.318 1.00 13.78 ? 37  ARG A CG    1 
ATOM   306  C CD    . ARG A 1 43  ? 9.691   -30.674 -21.208 1.00 17.53 ? 37  ARG A CD    1 
ATOM   307  N NE    . ARG A 1 43  ? 10.215  -31.069 -22.517 1.00 16.31 ? 37  ARG A NE    1 
ATOM   308  C CZ    . ARG A 1 43  ? 10.982  -32.139 -22.715 1.00 19.00 ? 37  ARG A CZ    1 
ATOM   309  N NH1   . ARG A 1 43  ? 11.327  -32.916 -21.689 1.00 16.00 ? 37  ARG A NH1   1 
ATOM   310  N NH2   . ARG A 1 43  ? 11.404  -32.422 -23.939 1.00 16.63 ? 37  ARG A NH2   1 
ATOM   311  N N     . LYS A 1 44  ? 6.274   -28.554 -17.592 1.00 16.17 ? 38  LYS A N     1 
ATOM   312  C CA    . LYS A 1 44  ? 5.970   -28.128 -16.231 1.00 16.98 ? 38  LYS A CA    1 
ATOM   313  C C     . LYS A 1 44  ? 5.384   -29.260 -15.392 1.00 19.50 ? 38  LYS A C     1 
ATOM   314  O O     . LYS A 1 44  ? 5.617   -29.306 -14.183 1.00 18.51 ? 38  LYS A O     1 
ATOM   315  C CB    . LYS A 1 44  ? 5.007   -26.944 -16.255 1.00 17.52 ? 38  LYS A CB    1 
ATOM   316  C CG    . LYS A 1 44  ? 5.648   -25.649 -16.788 1.00 15.72 ? 38  LYS A CG    1 
ATOM   317  C CD    . LYS A 1 44  ? 4.865   -24.438 -16.289 1.00 17.03 ? 38  LYS A CD    1 
ATOM   318  C CE    . LYS A 1 44  ? 5.576   -23.144 -16.605 1.00 17.96 ? 38  LYS A CE    1 
ATOM   319  N NZ    . LYS A 1 44  ? 5.107   -22.608 -17.921 1.00 20.12 ? 38  LYS A NZ    1 
ATOM   320  N N     . LEU A 1 45  ? 4.602   -30.161 -15.994 1.00 18.94 ? 39  LEU A N     1 
ATOM   321  C CA    . LEU A 1 45  ? 3.953   -31.222 -15.222 1.00 21.09 ? 39  LEU A CA    1 
ATOM   322  C C     . LEU A 1 45  ? 4.884   -32.373 -14.860 1.00 18.52 ? 39  LEU A C     1 
ATOM   323  O O     . LEU A 1 45  ? 4.456   -33.278 -14.139 1.00 20.72 ? 39  LEU A O     1 
ATOM   324  C CB    . LEU A 1 45  ? 2.752   -31.785 -15.990 1.00 18.29 ? 39  LEU A CB    1 
ATOM   325  C CG    . LEU A 1 45  ? 1.481   -30.947 -15.872 1.00 23.12 ? 39  LEU A CG    1 
ATOM   326  C CD1   . LEU A 1 45  ? 0.440   -31.438 -16.879 1.00 26.16 ? 39  LEU A CD1   1 
ATOM   327  C CD2   . LEU A 1 45  ? 0.941   -30.994 -14.426 1.00 23.16 ? 39  LEU A CD2   1 
ATOM   328  N N     . ALA A 1 46  ? 6.137   -32.366 -15.323 1.00 17.58 ? 40  ALA A N     1 
ATOM   329  C CA    . ALA A 1 46  ? 6.999   -33.532 -15.128 1.00 20.72 ? 40  ALA A CA    1 
ATOM   330  C C     . ALA A 1 46  ? 7.097   -33.932 -13.662 1.00 22.09 ? 40  ALA A C     1 
ATOM   331  O O     . ALA A 1 46  ? 7.056   -35.126 -13.334 1.00 21.11 ? 40  ALA A O     1 
ATOM   332  C CB    . ALA A 1 46  ? 8.396   -33.263 -15.695 1.00 22.12 ? 40  ALA A CB    1 
ATOM   333  N N     . PHE A 1 47  ? 7.231   -32.952 -12.769 1.00 20.26 ? 41  PHE A N     1 
ATOM   334  C CA    . PHE A 1 47  ? 7.292   -33.253 -11.339 1.00 20.88 ? 41  PHE A CA    1 
ATOM   335  C C     . PHE A 1 47  ? 6.090   -34.078 -10.893 1.00 21.65 ? 41  PHE A C     1 
ATOM   336  O O     . PHE A 1 47  ? 6.233   -35.075 -10.180 1.00 23.92 ? 41  PHE A O     1 
ATOM   337  C CB    . PHE A 1 47  ? 7.362   -31.958 -10.532 1.00 19.65 ? 41  PHE A CB    1 
ATOM   338  C CG    . PHE A 1 47  ? 7.253   -32.168 -9.048  1.00 20.71 ? 41  PHE A CG    1 
ATOM   339  C CD1   . PHE A 1 47  ? 6.023   -32.064 -8.405  1.00 24.12 ? 41  PHE A CD1   1 
ATOM   340  C CD2   . PHE A 1 47  ? 8.376   -32.469 -8.294  1.00 24.62 ? 41  PHE A CD2   1 
ATOM   341  C CE1   . PHE A 1 47  ? 5.909   -32.261 -7.029  1.00 29.52 ? 41  PHE A CE1   1 
ATOM   342  C CE2   . PHE A 1 47  ? 8.276   -32.672 -6.916  1.00 27.08 ? 41  PHE A CE2   1 
ATOM   343  C CZ    . PHE A 1 47  ? 7.037   -32.567 -6.282  1.00 26.15 ? 41  PHE A CZ    1 
ATOM   344  N N     . TYR A 1 48  ? 4.892   -33.657 -11.290 1.00 20.14 ? 42  TYR A N     1 
ATOM   345  C CA    . TYR A 1 48  ? 3.676   -34.317 -10.826 1.00 24.74 ? 42  TYR A CA    1 
ATOM   346  C C     . TYR A 1 48  ? 3.491   -35.682 -11.473 1.00 26.99 ? 42  TYR A C     1 
ATOM   347  O O     . TYR A 1 48  ? 2.946   -36.601 -10.852 1.00 29.87 ? 42  TYR A O     1 
ATOM   348  C CB    . TYR A 1 48  ? 2.484   -33.411 -11.110 1.00 23.37 ? 42  TYR A CB    1 
ATOM   349  C CG    . TYR A 1 48  ? 2.631   -32.072 -10.428 1.00 22.74 ? 42  TYR A CG    1 
ATOM   350  C CD1   . TYR A 1 48  ? 2.313   -31.921 -9.087  1.00 21.51 ? 42  TYR A CD1   1 
ATOM   351  C CD2   . TYR A 1 48  ? 3.127   -30.968 -11.114 1.00 21.60 ? 42  TYR A CD2   1 
ATOM   352  C CE1   . TYR A 1 48  ? 2.460   -30.710 -8.450  1.00 24.24 ? 42  TYR A CE1   1 
ATOM   353  C CE2   . TYR A 1 48  ? 3.280   -29.742 -10.483 1.00 22.75 ? 42  TYR A CE2   1 
ATOM   354  C CZ    . TYR A 1 48  ? 2.940   -29.623 -9.155  1.00 24.78 ? 42  TYR A CZ    1 
ATOM   355  O OH    . TYR A 1 48  ? 3.087   -28.421 -8.523  1.00 24.04 ? 42  TYR A OH    1 
ATOM   356  N N     . ILE A 1 49  ? 3.929   -35.828 -12.724 1.00 22.16 ? 43  ILE A N     1 
ATOM   357  C CA    . ILE A 1 49  ? 3.815   -37.107 -13.418 1.00 26.33 ? 43  ILE A CA    1 
ATOM   358  C C     . ILE A 1 49  ? 4.732   -38.147 -12.789 1.00 30.95 ? 43  ILE A C     1 
ATOM   359  O O     . ILE A 1 49  ? 4.392   -39.336 -12.741 1.00 33.76 ? 43  ILE A O     1 
ATOM   360  C CB    . ILE A 1 49  ? 4.115   -36.911 -14.915 1.00 27.56 ? 43  ILE A CB    1 
ATOM   361  C CG1   . ILE A 1 49  ? 2.997   -36.101 -15.581 1.00 28.54 ? 43  ILE A CG1   1 
ATOM   362  C CG2   . ILE A 1 49  ? 4.319   -38.262 -15.623 1.00 27.31 ? 43  ILE A CG2   1 
ATOM   363  C CD1   . ILE A 1 49  ? 3.426   -35.466 -16.914 1.00 27.70 ? 43  ILE A CD1   1 
ATOM   364  N N     . HIS A 1 50  ? 5.891   -37.722 -12.281 1.00 29.44 ? 44  HIS A N     1 
ATOM   365  C CA    . HIS A 1 50  ? 6.838   -38.646 -11.670 1.00 38.88 ? 44  HIS A CA    1 
ATOM   366  C C     . HIS A 1 50  ? 6.454   -39.030 -10.246 1.00 36.76 ? 44  HIS A C     1 
ATOM   367  O O     . HIS A 1 50  ? 6.951   -40.042 -9.738  1.00 42.60 ? 44  HIS A O     1 
ATOM   368  C CB    . HIS A 1 50  ? 8.242   -38.040 -11.710 1.00 39.20 ? 44  HIS A CB    1 
ATOM   369  C CG    . HIS A 1 50  ? 8.791   -37.903 -13.099 1.00 49.29 ? 44  HIS A CG    1 
ATOM   370  N ND1   . HIS A 1 50  ? 9.764   -36.983 -13.434 1.00 51.47 ? 44  HIS A ND1   1 
ATOM   371  C CD2   . HIS A 1 50  ? 8.491   -38.564 -14.243 1.00 49.89 ? 44  HIS A CD2   1 
ATOM   372  C CE1   . HIS A 1 50  ? 10.044  -37.090 -14.722 1.00 47.62 ? 44  HIS A CE1   1 
ATOM   373  N NE2   . HIS A 1 50  ? 9.286   -38.042 -15.235 1.00 51.77 ? 44  HIS A NE2   1 
ATOM   374  N N     . GLN A 1 51  ? 5.593   -38.256 -9.589  1.00 26.96 ? 45  GLN A N     1 
ATOM   375  C CA    . GLN A 1 51  ? 5.084   -38.663 -8.288  1.00 28.66 ? 45  GLN A CA    1 
ATOM   376  C C     . GLN A 1 51  ? 4.127   -39.843 -8.449  1.00 31.37 ? 45  GLN A C     1 
ATOM   377  O O     . GLN A 1 51  ? 3.615   -40.124 -9.538  1.00 30.09 ? 45  GLN A O     1 
ATOM   378  C CB    . GLN A 1 51  ? 4.363   -37.508 -7.584  1.00 27.84 ? 45  GLN A CB    1 
ATOM   379  C CG    . GLN A 1 51  ? 5.125   -36.183 -7.456  1.00 33.39 ? 45  GLN A CG    1 
ATOM   380  C CD    . GLN A 1 51  ? 6.511   -36.335 -6.859  1.00 45.92 ? 45  GLN A CD    1 
ATOM   381  O OE1   . GLN A 1 51  ? 6.664   -36.574 -5.660  1.00 47.48 ? 45  GLN A OE1   1 
ATOM   382  N NE2   . GLN A 1 51  ? 7.533   -36.183 -7.697  1.00 48.85 ? 45  GLN A NE2   1 
ATOM   383  N N     . ARG A 1 52  ? 3.899   -40.556 -7.352  1.00 29.80 ? 46  ARG A N     1 
ATOM   384  C CA    . ARG A 1 52  ? 2.909   -41.631 -7.319  1.00 31.62 ? 46  ARG A CA    1 
ATOM   385  C C     . ARG A 1 52  ? 1.974   -41.289 -6.171  1.00 37.37 ? 46  ARG A C     1 
ATOM   386  O O     . ARG A 1 52  ? 2.227   -41.646 -5.019  1.00 47.75 ? 46  ARG A O     1 
ATOM   387  C CB    . ARG A 1 52  ? 3.551   -43.026 -7.148  1.00 37.89 ? 46  ARG A CB    1 
ATOM   388  C CG    . ARG A 1 52  ? 4.312   -43.519 -8.381  1.00 46.24 ? 46  ARG A CG    1 
ATOM   389  C CD    . ARG A 1 52  ? 3.382   -43.713 -9.573  1.00 45.05 ? 46  ARG A CD    1 
ATOM   390  N NE    . ARG A 1 52  ? 4.071   -44.176 -10.778 1.00 43.68 ? 46  ARG A NE    1 
ATOM   391  C CZ    . ARG A 1 52  ? 4.685   -43.374 -11.646 1.00 45.81 ? 46  ARG A CZ    1 
ATOM   392  N NH1   . ARG A 1 52  ? 4.720   -42.064 -11.434 1.00 39.68 ? 46  ARG A NH1   1 
ATOM   393  N NH2   . ARG A 1 52  ? 5.279   -43.879 -12.720 1.00 43.96 ? 46  ARG A NH2   1 
ATOM   394  N N     . TYR A 1 53  ? 0.911   -40.584 -6.491  1.00 32.84 ? 47  TYR A N     1 
ATOM   395  C CA    . TYR A 1 53  ? -0.058  -40.138 -5.511  1.00 33.72 ? 47  TYR A CA    1 
ATOM   396  C C     . TYR A 1 53  ? -1.075  -41.237 -5.227  1.00 40.21 ? 47  TYR A C     1 
ATOM   397  O O     . TYR A 1 53  ? -1.330  -42.094 -6.079  1.00 42.84 ? 47  TYR A O     1 
ATOM   398  C CB    . TYR A 1 53  ? -0.788  -38.894 -6.006  1.00 33.90 ? 47  TYR A CB    1 
ATOM   399  C CG    . TYR A 1 53  ? 0.067   -37.668 -6.179  1.00 31.32 ? 47  TYR A CG    1 
ATOM   400  C CD1   . TYR A 1 53  ? 0.404   -36.884 -5.093  1.00 34.30 ? 47  TYR A CD1   1 
ATOM   401  C CD2   . TYR A 1 53  ? 0.522   -37.281 -7.439  1.00 31.73 ? 47  TYR A CD2   1 
ATOM   402  C CE1   . TYR A 1 53  ? 1.169   -35.748 -5.240  1.00 31.88 ? 47  TYR A CE1   1 
ATOM   403  C CE2   . TYR A 1 53  ? 1.290   -36.138 -7.596  1.00 33.77 ? 47  TYR A CE2   1 
ATOM   404  C CZ    . TYR A 1 53  ? 1.616   -35.381 -6.492  1.00 35.70 ? 47  TYR A CZ    1 
ATOM   405  O OH    . TYR A 1 53  ? 2.382   -34.248 -6.620  1.00 36.79 ? 47  TYR A OH    1 
ATOM   406  N N     . PRO A 1 54  ? -1.663  -41.234 -4.034  1.00 38.81 ? 48  PRO A N     1 
ATOM   407  C CA    . PRO A 1 54  ? -2.736  -42.187 -3.746  1.00 45.44 ? 48  PRO A CA    1 
ATOM   408  C C     . PRO A 1 54  ? -3.866  -42.044 -4.749  1.00 44.80 ? 48  PRO A C     1 
ATOM   409  O O     . PRO A 1 54  ? -4.047  -40.996 -5.368  1.00 42.24 ? 48  PRO A O     1 
ATOM   410  C CB    . PRO A 1 54  ? -3.185  -41.801 -2.335  1.00 47.97 ? 48  PRO A CB    1 
ATOM   411  C CG    . PRO A 1 54  ? -1.998  -41.111 -1.745  1.00 44.07 ? 48  PRO A CG    1 
ATOM   412  C CD    . PRO A 1 54  ? -1.383  -40.361 -2.881  1.00 41.17 ? 48  PRO A CD    1 
ATOM   413  N N     . LYS A 1 55  ? -4.621  -43.123 -4.915  1.00 47.51 ? 49  LYS A N     1 
ATOM   414  C CA    . LYS A 1 55  ? -5.709  -43.110 -5.880  1.00 48.47 ? 49  LYS A CA    1 
ATOM   415  C C     . LYS A 1 55  ? -6.742  -42.059 -5.492  1.00 45.88 ? 49  LYS A C     1 
ATOM   416  O O     . LYS A 1 55  ? -7.011  -41.838 -4.307  1.00 45.84 ? 49  LYS A O     1 
ATOM   417  C CB    . LYS A 1 55  ? -6.356  -44.493 -5.968  1.00 53.47 ? 49  LYS A CB    1 
ATOM   418  C CG    . LYS A 1 55  ? -7.233  -44.693 -7.195  1.00 54.93 ? 49  LYS A CG    1 
ATOM   419  N N     . ASN A 1 56  ? -7.300  -41.395 -6.508  1.00 44.50 ? 50  ASN A N     1 
ATOM   420  C CA    . ASN A 1 56  ? -8.295  -40.331 -6.368  1.00 46.93 ? 50  ASN A CA    1 
ATOM   421  C C     . ASN A 1 56  ? -7.750  -39.094 -5.654  1.00 42.61 ? 50  ASN A C     1 
ATOM   422  O O     . ASN A 1 56  ? -8.521  -38.322 -5.070  1.00 45.15 ? 50  ASN A O     1 
ATOM   423  C CB    . ASN A 1 56  ? -9.556  -40.839 -5.663  1.00 49.90 ? 50  ASN A CB    1 
ATOM   424  C CG    . ASN A 1 56  ? -10.066 -42.134 -6.257  1.00 55.93 ? 50  ASN A CG    1 
ATOM   425  O OD1   . ASN A 1 56  ? -10.540 -43.016 -5.537  1.00 63.37 ? 50  ASN A OD1   1 
ATOM   426  N ND2   . ASN A 1 56  ? -9.954  -42.265 -7.574  1.00 58.33 ? 50  ASN A ND2   1 
ATOM   427  N N     . GLN A 1 57  ? -6.434  -38.898 -5.682  1.00 40.02 ? 51  GLN A N     1 
ATOM   428  C CA    . GLN A 1 57  ? -5.834  -37.666 -5.186  1.00 37.56 ? 51  GLN A CA    1 
ATOM   429  C C     . GLN A 1 57  ? -6.468  -36.450 -5.854  1.00 39.18 ? 51  GLN A C     1 
ATOM   430  O O     . GLN A 1 57  ? -6.692  -36.435 -7.066  1.00 39.46 ? 51  GLN A O     1 
ATOM   431  C CB    . GLN A 1 57  ? -4.325  -37.689 -5.451  1.00 32.85 ? 51  GLN A CB    1 
ATOM   432  C CG    . GLN A 1 57  ? -3.602  -36.382 -5.154  1.00 37.11 ? 51  GLN A CG    1 
ATOM   433  C CD    . GLN A 1 57  ? -3.426  -36.129 -3.668  1.00 34.73 ? 51  GLN A CD    1 
ATOM   434  O OE1   . GLN A 1 57  ? -2.952  -36.999 -2.932  1.00 37.63 ? 51  GLN A OE1   1 
ATOM   435  N NE2   . GLN A 1 57  ? -3.814  -34.937 -3.217  1.00 37.79 ? 51  GLN A NE2   1 
ATOM   436  N N     . SER A 1 58  ? -6.750  -35.420 -5.062  1.00 41.51 ? 52  SER A N     1 
ATOM   437  C CA    . SER A 1 58  ? -7.330  -34.189 -5.585  1.00 38.68 ? 52  SER A CA    1 
ATOM   438  C C     . SER A 1 58  ? -6.267  -33.122 -5.788  1.00 33.51 ? 52  SER A C     1 
ATOM   439  O O     . SER A 1 58  ? -5.357  -32.969 -4.967  1.00 36.02 ? 52  SER A O     1 
ATOM   440  C CB    . SER A 1 58  ? -8.418  -33.653 -4.652  1.00 43.58 ? 52  SER A CB    1 
ATOM   441  O OG    . SER A 1 58  ? -9.667  -34.226 -4.975  1.00 53.17 ? 52  SER A OG    1 
ATOM   442  N N     . PHE A 1 59  ? -6.400  -32.379 -6.888  1.00 31.31 ? 53  PHE A N     1 
ATOM   443  C CA    . PHE A 1 59  ? -5.528  -31.271 -7.243  1.00 27.70 ? 53  PHE A CA    1 
ATOM   444  C C     . PHE A 1 59  ? -6.369  -30.015 -7.409  1.00 34.66 ? 53  PHE A C     1 
ATOM   445  O O     . PHE A 1 59  ? -7.451  -30.059 -8.002  1.00 44.78 ? 53  PHE A O     1 
ATOM   446  C CB    . PHE A 1 59  ? -4.765  -31.565 -8.535  1.00 29.32 ? 53  PHE A CB    1 
ATOM   447  C CG    . PHE A 1 59  ? -3.763  -32.675 -8.404  1.00 30.67 ? 53  PHE A CG    1 
ATOM   448  C CD1   . PHE A 1 59  ? -2.430  -32.393 -8.155  1.00 30.53 ? 53  PHE A CD1   1 
ATOM   449  C CD2   . PHE A 1 59  ? -4.161  -33.999 -8.508  1.00 32.04 ? 53  PHE A CD2   1 
ATOM   450  C CE1   . PHE A 1 59  ? -1.506  -33.414 -8.008  1.00 29.92 ? 53  PHE A CE1   1 
ATOM   451  C CE2   . PHE A 1 59  ? -3.244  -35.027 -8.371  1.00 32.38 ? 53  PHE A CE2   1 
ATOM   452  C CZ    . PHE A 1 59  ? -1.917  -34.737 -8.119  1.00 29.97 ? 53  PHE A CZ    1 
ATOM   453  N N     . VAL A 1 60  ? -5.879  -28.900 -6.869  1.00 34.87 ? 54  VAL A N     1 
ATOM   454  C CA    . VAL A 1 60  ? -6.555  -27.607 -6.958  1.00 35.74 ? 54  VAL A CA    1 
ATOM   455  C C     . VAL A 1 60  ? -5.662  -26.651 -7.737  1.00 33.02 ? 54  VAL A C     1 
ATOM   456  O O     . VAL A 1 60  ? -4.491  -26.470 -7.389  1.00 31.32 ? 54  VAL A O     1 
ATOM   457  C CB    . VAL A 1 60  ? -6.869  -27.031 -5.567  1.00 33.66 ? 54  VAL A CB    1 
ATOM   458  C CG1   . VAL A 1 60  ? -7.537  -25.651 -5.685  1.00 34.95 ? 54  VAL A CG1   1 
ATOM   459  C CG2   . VAL A 1 60  ? -7.752  -27.989 -4.785  1.00 36.24 ? 54  VAL A CG2   1 
ATOM   460  N N     . SER A 1 61  ? -6.214  -26.036 -8.778  1.00 28.37 ? 55  SER A N     1 
ATOM   461  C CA    . SER A 1 61  ? -5.529  -24.961 -9.477  1.00 27.64 ? 55  SER A CA    1 
ATOM   462  C C     . SER A 1 61  ? -6.556  -23.887 -9.820  1.00 33.05 ? 55  SER A C     1 
ATOM   463  O O     . SER A 1 61  ? -7.721  -23.956 -9.414  1.00 33.69 ? 55  SER A O     1 
ATOM   464  C CB    . SER A 1 61  ? -4.799  -25.482 -10.726 1.00 25.71 ? 55  SER A CB    1 
ATOM   465  O OG    . SER A 1 61  ? -3.880  -24.518 -11.216 1.00 27.67 ? 55  SER A OG    1 
ATOM   466  N N     . TYR A 1 62  ? -6.111  -22.886 -10.574 1.00 34.98 ? 56  TYR A N     1 
ATOM   467  C CA    . TYR A 1 62  ? -6.956  -21.756 -10.933 1.00 36.87 ? 56  TYR A CA    1 
ATOM   468  C C     . TYR A 1 62  ? -6.355  -21.069 -12.152 1.00 30.51 ? 56  TYR A C     1 
ATOM   469  O O     . TYR A 1 62  ? -5.217  -21.339 -12.542 1.00 30.59 ? 56  TYR A O     1 
ATOM   470  C CB    . TYR A 1 62  ? -7.094  -20.777 -9.766  1.00 34.00 ? 56  TYR A CB    1 
ATOM   471  C CG    . TYR A 1 62  ? -5.810  -20.048 -9.429  1.00 35.86 ? 56  TYR A CG    1 
ATOM   472  C CD1   . TYR A 1 62  ? -4.795  -20.679 -8.717  1.00 34.94 ? 56  TYR A CD1   1 
ATOM   473  C CD2   . TYR A 1 62  ? -5.618  -18.726 -9.814  1.00 37.57 ? 56  TYR A CD2   1 
ATOM   474  C CE1   . TYR A 1 62  ? -3.621  -20.015 -8.401  1.00 36.60 ? 56  TYR A CE1   1 
ATOM   475  C CE2   . TYR A 1 62  ? -4.451  -18.056 -9.503  1.00 39.35 ? 56  TYR A CE2   1 
ATOM   476  C CZ    . TYR A 1 62  ? -3.458  -18.704 -8.797  1.00 42.34 ? 56  TYR A CZ    1 
ATOM   477  O OH    . TYR A 1 62  ? -2.298  -18.039 -8.487  1.00 55.31 ? 56  TYR A OH    1 
ATOM   478  N N     . GLY A 1 63  ? -7.136  -20.175 -12.746 1.00 33.02 ? 57  GLY A N     1 
ATOM   479  C CA    . GLY A 1 63  ? -6.693  -19.426 -13.898 1.00 33.49 ? 57  GLY A CA    1 
ATOM   480  C C     . GLY A 1 63  ? -7.806  -19.301 -14.908 1.00 37.52 ? 57  GLY A C     1 
ATOM   481  O O     . GLY A 1 63  ? -8.985  -19.433 -14.574 1.00 40.18 ? 57  GLY A O     1 
ATOM   482  N N     . GLY A 1 64  ? -7.416  -19.033 -16.153 1.00 37.24 ? 58  GLY A N     1 
ATOM   483  C CA    . GLY A 1 64  ? -8.404  -18.804 -17.191 1.00 40.98 ? 58  GLY A CA    1 
ATOM   484  C C     . GLY A 1 64  ? -9.139  -20.081 -17.551 1.00 35.52 ? 58  GLY A C     1 
ATOM   485  O O     . GLY A 1 64  ? -8.552  -21.162 -17.631 1.00 35.42 ? 58  GLY A O     1 
ATOM   486  N N     . SER A 1 65  ? -10.451 -19.948 -17.769 1.00 43.43 ? 59  SER A N     1 
ATOM   487  C CA    . SER A 1 65  ? -11.281 -21.085 -18.147 1.00 43.68 ? 59  SER A CA    1 
ATOM   488  C C     . SER A 1 65  ? -10.956 -21.622 -19.535 1.00 45.92 ? 59  SER A C     1 
ATOM   489  O O     . SER A 1 65  ? -11.474 -22.679 -19.905 1.00 42.57 ? 59  SER A O     1 
ATOM   490  C CB    . SER A 1 65  ? -12.762 -20.697 -18.072 1.00 47.36 ? 59  SER A CB    1 
ATOM   491  O OG    . SER A 1 65  ? -12.938 -19.300 -18.243 1.00 48.17 ? 59  SER A OG    1 
ATOM   492  N N     . GLN A 1 66  ? -10.117 -20.929 -20.305 1.00 45.28 ? 60  GLN A N     1 
ATOM   493  C CA    . GLN A 1 66  ? -9.681  -21.403 -21.614 1.00 43.18 ? 60  GLN A CA    1 
ATOM   494  C C     . GLN A 1 66  ? -8.177  -21.655 -21.680 1.00 36.75 ? 60  GLN A C     1 
ATOM   495  O O     . GLN A 1 66  ? -7.614  -21.697 -22.782 1.00 37.30 ? 60  GLN A O     1 
ATOM   496  C CB    . GLN A 1 66  ? -10.079 -20.402 -22.696 1.00 45.72 ? 60  GLN A CB    1 
ATOM   497  C CG    . GLN A 1 66  ? -11.563 -20.359 -22.983 1.00 49.36 ? 60  GLN A CG    1 
ATOM   498  C CD    . GLN A 1 66  ? -12.017 -21.492 -23.880 1.00 49.91 ? 60  GLN A CD    1 
ATOM   499  O OE1   . GLN A 1 66  ? -11.410 -22.566 -23.912 1.00 44.68 ? 60  GLN A OE1   1 
ATOM   500  N NE2   . GLN A 1 66  ? -13.090 -21.255 -24.622 1.00 54.19 ? 60  GLN A NE2   1 
ATOM   501  N N     . SER A 1 67  ? -7.513  -21.835 -20.540 1.00 36.82 ? 61  SER A N     1 
ATOM   502  C CA    . SER A 1 67  ? -6.053  -21.823 -20.509 1.00 35.84 ? 61  SER A CA    1 
ATOM   503  C C     . SER A 1 67  ? -5.449  -23.181 -20.866 1.00 33.69 ? 61  SER A C     1 
ATOM   504  O O     . SER A 1 67  ? -6.047  -24.236 -20.634 1.00 29.85 ? 61  SER A O     1 
ATOM   505  C CB    . SER A 1 67  ? -5.557  -21.388 -19.128 1.00 38.95 ? 61  SER A CB    1 
ATOM   506  O OG    . SER A 1 67  ? -5.981  -22.287 -18.114 1.00 35.92 ? 61  SER A OG    1 
ATOM   507  N N     . ASN A 1 68  ? -4.238  -23.138 -21.435 1.00 34.63 ? 62  ASN A N     1 
ATOM   508  C CA    . ASN A 1 68  ? -3.498  -24.364 -21.733 1.00 26.65 ? 62  ASN A CA    1 
ATOM   509  C C     . ASN A 1 68  ? -3.236  -25.177 -20.476 1.00 25.44 ? 62  ASN A C     1 
ATOM   510  O O     . ASN A 1 68  ? -3.246  -26.411 -20.517 1.00 29.03 ? 62  ASN A O     1 
ATOM   511  C CB    . ASN A 1 68  ? -2.161  -24.042 -22.405 1.00 26.59 ? 62  ASN A CB    1 
ATOM   512  C CG    . ASN A 1 68  ? -2.312  -23.595 -23.846 1.00 34.45 ? 62  ASN A CG    1 
ATOM   513  O OD1   . ASN A 1 68  ? -3.336  -23.845 -24.490 1.00 39.23 ? 62  ASN A OD1   1 
ATOM   514  N ND2   . ASN A 1 68  ? -1.277  -22.931 -24.367 1.00 28.72 ? 62  ASN A ND2   1 
ATOM   515  N N     . ALA A 1 69  ? -2.953  -24.503 -19.359 1.00 28.13 ? 63  ALA A N     1 
ATOM   516  C CA    . ALA A 1 69  ? -2.697  -25.220 -18.116 1.00 25.40 ? 63  ALA A CA    1 
ATOM   517  C C     . ALA A 1 69  ? -3.923  -26.003 -17.665 1.00 23.47 ? 63  ALA A C     1 
ATOM   518  O O     . ALA A 1 69  ? -3.799  -27.143 -17.202 1.00 24.58 ? 63  ALA A O     1 
ATOM   519  C CB    . ALA A 1 69  ? -2.247  -24.245 -17.029 1.00 27.53 ? 63  ALA A CB    1 
ATOM   520  N N     . LEU A 1 70  ? -5.113  -25.401 -17.785 1.00 25.26 ? 64  LEU A N     1 
ATOM   521  C CA    . LEU A 1 70  ? -6.353  -26.107 -17.472 1.00 29.52 ? 64  LEU A CA    1 
ATOM   522  C C     . LEU A 1 70  ? -6.469  -27.387 -18.289 1.00 27.44 ? 64  LEU A C     1 
ATOM   523  O O     . LEU A 1 70  ? -6.712  -28.471 -17.740 1.00 27.34 ? 64  LEU A O     1 
ATOM   524  C CB    . LEU A 1 70  ? -7.558  -25.194 -17.729 1.00 28.73 ? 64  LEU A CB    1 
ATOM   525  C CG    . LEU A 1 70  ? -8.900  -25.934 -17.725 1.00 30.39 ? 64  LEU A CG    1 
ATOM   526  C CD1   . LEU A 1 70  ? -9.205  -26.471 -16.329 1.00 30.97 ? 64  LEU A CD1   1 
ATOM   527  C CD2   . LEU A 1 70  ? -10.052 -25.065 -18.240 1.00 34.09 ? 64  LEU A CD2   1 
ATOM   528  N N     . ALA A 1 71  ? -6.267  -27.280 -19.608 1.00 30.76 ? 65  ALA A N     1 
ATOM   529  C CA    . ALA A 1 71  ? -6.353  -28.440 -20.489 1.00 27.07 ? 65  ALA A CA    1 
ATOM   530  C C     . ALA A 1 71  ? -5.333  -29.509 -20.109 1.00 25.29 ? 65  ALA A C     1 
ATOM   531  O O     . ALA A 1 71  ? -5.677  -30.691 -19.977 1.00 29.37 ? 65  ALA A O     1 
ATOM   532  C CB    . ALA A 1 71  ? -6.173  -27.997 -21.945 1.00 28.67 ? 65  ALA A CB    1 
ATOM   533  N N     . ALA A 1 72  ? -4.077  -29.108 -19.894 1.00 26.51 ? 66  ALA A N     1 
ATOM   534  C CA    . ALA A 1 72  ? -3.034  -30.070 -19.539 1.00 23.65 ? 66  ALA A CA    1 
ATOM   535  C C     . ALA A 1 72  ? -3.335  -30.750 -18.207 1.00 26.46 ? 66  ALA A C     1 
ATOM   536  O O     . ALA A 1 72  ? -3.228  -31.980 -18.080 1.00 26.38 ? 66  ALA A O     1 
ATOM   537  C CB    . ALA A 1 72  ? -1.678  -29.367 -19.492 1.00 22.18 ? 66  ALA A CB    1 
ATOM   538  N N     . LEU A 1 73  ? -3.710  -29.961 -17.198 1.00 24.71 ? 67  LEU A N     1 
ATOM   539  C CA    . LEU A 1 73  ? -4.036  -30.529 -15.893 1.00 23.58 ? 67  LEU A CA    1 
ATOM   540  C C     . LEU A 1 73  ? -5.206  -31.500 -15.982 1.00 25.65 ? 67  LEU A C     1 
ATOM   541  O O     . LEU A 1 73  ? -5.220  -32.533 -15.300 1.00 26.69 ? 67  LEU A O     1 
ATOM   542  C CB    . LEU A 1 73  ? -4.345  -29.405 -14.903 1.00 24.09 ? 67  LEU A CB    1 
ATOM   543  C CG    . LEU A 1 73  ? -3.146  -28.611 -14.392 1.00 22.04 ? 67  LEU A CG    1 
ATOM   544  C CD1   . LEU A 1 73  ? -3.657  -27.305 -13.794 1.00 25.32 ? 67  LEU A CD1   1 
ATOM   545  C CD2   . LEU A 1 73  ? -2.399  -29.423 -13.334 1.00 23.77 ? 67  LEU A CD2   1 
ATOM   546  N N     . SER A 1 74  ? -6.199  -31.187 -16.821 1.00 28.20 ? 68  SER A N     1 
ATOM   547  C CA    . SER A 1 74  ? -7.361  -32.062 -16.934 1.00 32.70 ? 68  SER A CA    1 
ATOM   548  C C     . SER A 1 74  ? -6.973  -33.428 -17.491 1.00 27.76 ? 68  SER A C     1 
ATOM   549  O O     . SER A 1 74  ? -7.484  -34.459 -17.033 1.00 31.35 ? 68  SER A O     1 
ATOM   550  C CB    . SER A 1 74  ? -8.439  -31.401 -17.794 1.00 33.65 ? 68  SER A CB    1 
ATOM   551  O OG    . SER A 1 74  ? -8.152  -31.489 -19.168 1.00 30.14 ? 68  SER A OG    1 
ATOM   552  N N     . ILE A 1 75  ? -6.045  -33.455 -18.458 1.00 29.06 ? 69  ILE A N     1 
ATOM   553  C CA    . ILE A 1 75  ? -5.556  -34.720 -19.007 1.00 28.15 ? 69  ILE A CA    1 
ATOM   554  C C     . ILE A 1 75  ? -4.724  -35.463 -17.970 1.00 27.08 ? 69  ILE A C     1 
ATOM   555  O O     . ILE A 1 75  ? -4.890  -36.673 -17.763 1.00 31.09 ? 69  ILE A O     1 
ATOM   556  C CB    . ILE A 1 75  ? -4.743  -34.466 -20.292 1.00 31.88 ? 69  ILE A CB    1 
ATOM   557  C CG1   . ILE A 1 75  ? -5.590  -33.733 -21.329 1.00 35.70 ? 69  ILE A CG1   1 
ATOM   558  C CG2   . ILE A 1 75  ? -4.202  -35.777 -20.853 1.00 33.24 ? 69  ILE A CG2   1 
ATOM   559  C CD1   . ILE A 1 75  ? -4.769  -33.115 -22.447 1.00 37.77 ? 69  ILE A CD1   1 
ATOM   560  N N     . PHE A 1 76  ? -3.810  -34.746 -17.310 1.00 25.37 ? 70  PHE A N     1 
ATOM   561  C CA    . PHE A 1 76  ? -3.001  -35.338 -16.248 1.00 25.69 ? 70  PHE A CA    1 
ATOM   562  C C     . PHE A 1 76  ? -3.879  -36.034 -15.219 1.00 28.49 ? 70  PHE A C     1 
ATOM   563  O O     . PHE A 1 76  ? -3.631  -37.186 -14.842 1.00 30.62 ? 70  PHE A O     1 
ATOM   564  C CB    . PHE A 1 76  ? -2.146  -34.250 -15.592 1.00 22.64 ? 70  PHE A CB    1 
ATOM   565  C CG    . PHE A 1 76  ? -1.566  -34.647 -14.264 1.00 25.97 ? 70  PHE A CG    1 
ATOM   566  C CD1   . PHE A 1 76  ? -2.126  -34.179 -13.084 1.00 26.86 ? 70  PHE A CD1   1 
ATOM   567  C CD2   . PHE A 1 76  ? -0.454  -35.466 -14.192 1.00 26.68 ? 70  PHE A CD2   1 
ATOM   568  C CE1   . PHE A 1 76  ? -1.595  -34.529 -11.854 1.00 30.16 ? 70  PHE A CE1   1 
ATOM   569  C CE2   . PHE A 1 76  ? 0.080   -35.818 -12.959 1.00 25.04 ? 70  PHE A CE2   1 
ATOM   570  C CZ    . PHE A 1 76  ? -0.494  -35.352 -11.794 1.00 28.46 ? 70  PHE A CZ    1 
ATOM   571  N N     . ALA A 1 77  ? -4.942  -35.358 -14.784 1.00 27.70 ? 71  ALA A N     1 
ATOM   572  C CA    . ALA A 1 77  ? -5.814  -35.946 -13.775 1.00 29.24 ? 71  ALA A CA    1 
ATOM   573  C C     . ALA A 1 77  ? -6.611  -37.114 -14.345 1.00 32.40 ? 71  ALA A C     1 
ATOM   574  O O     . ALA A 1 77  ? -6.730  -38.162 -13.698 1.00 32.30 ? 71  ALA A O     1 
ATOM   575  C CB    . ALA A 1 77  ? -6.750  -34.880 -13.205 1.00 27.72 ? 71  ALA A CB    1 
ATOM   576  N N     . LYS A 1 78  ? -7.154  -36.961 -15.556 1.00 32.61 ? 72  LYS A N     1 
ATOM   577  C CA    . LYS A 1 78  ? -8.011  -38.007 -16.112 1.00 40.16 ? 72  LYS A CA    1 
ATOM   578  C C     . LYS A 1 78  ? -7.234  -39.297 -16.358 1.00 41.86 ? 72  LYS A C     1 
ATOM   579  O O     . LYS A 1 78  ? -7.742  -40.393 -16.090 1.00 45.51 ? 72  LYS A O     1 
ATOM   580  C CB    . LYS A 1 78  ? -8.665  -37.522 -17.405 1.00 39.24 ? 72  LYS A CB    1 
ATOM   581  C CG    . LYS A 1 78  ? -9.622  -38.535 -18.032 1.00 46.19 ? 72  LYS A CG    1 
ATOM   582  N N     . GLN A 1 79  ? -6.006  -39.188 -16.869 1.00 42.01 ? 73  GLN A N     1 
ATOM   583  C CA    . GLN A 1 79  ? -5.199  -40.372 -17.151 1.00 39.76 ? 73  GLN A CA    1 
ATOM   584  C C     . GLN A 1 79  ? -4.914  -41.181 -15.893 1.00 43.41 ? 73  GLN A C     1 
ATOM   585  O O     . GLN A 1 79  ? -4.770  -42.406 -15.962 1.00 48.13 ? 73  GLN A O     1 
ATOM   586  C CB    . GLN A 1 79  ? -3.875  -39.967 -17.806 1.00 36.40 ? 73  GLN A CB    1 
ATOM   587  C CG    . GLN A 1 79  ? -3.976  -39.445 -19.232 1.00 37.27 ? 73  GLN A CG    1 
ATOM   588  C CD    . GLN A 1 79  ? -2.656  -38.877 -19.724 1.00 39.48 ? 73  GLN A CD    1 
ATOM   589  O OE1   . GLN A 1 79  ? -1.802  -38.491 -18.924 1.00 38.35 ? 73  GLN A OE1   1 
ATOM   590  N NE2   . GLN A 1 79  ? -2.480  -38.824 -21.048 1.00 42.90 ? 73  GLN A NE2   1 
ATOM   591  N N     . ARG A 1 80  ? -4.826  -40.519 -14.739 1.00 38.50 ? 74  ARG A N     1 
ATOM   592  C CA    . ARG A 1 80  ? -4.366  -41.151 -13.510 1.00 40.09 ? 74  ARG A CA    1 
ATOM   593  C C     . ARG A 1 80  ? -5.480  -41.326 -12.488 1.00 44.42 ? 74  ARG A C     1 
ATOM   594  O O     . ARG A 1 80  ? -5.200  -41.683 -11.338 1.00 48.97 ? 74  ARG A O     1 
ATOM   595  C CB    . ARG A 1 80  ? -3.206  -40.344 -12.918 1.00 36.27 ? 74  ARG A CB    1 
ATOM   596  C CG    . ARG A 1 80  ? -1.955  -40.373 -13.802 1.00 33.06 ? 74  ARG A CG    1 
ATOM   597  C CD    . ARG A 1 80  ? -0.964  -39.221 -13.573 1.00 31.01 ? 74  ARG A CD    1 
ATOM   598  N NE    . ARG A 1 80  ? 0.123   -39.355 -14.543 1.00 31.83 ? 74  ARG A NE    1 
ATOM   599  C CZ    . ARG A 1 80  ? 0.016   -39.034 -15.828 1.00 32.94 ? 74  ARG A CZ    1 
ATOM   600  N NH1   . ARG A 1 80  ? -1.112  -38.521 -16.296 1.00 33.46 ? 74  ARG A NH1   1 
ATOM   601  N NH2   . ARG A 1 80  ? 1.035   -39.230 -16.654 1.00 36.78 ? 74  ARG A NH2   1 
ATOM   602  N N     . SER A 1 81  ? -6.734  -41.101 -12.883 1.00 38.16 ? 75  SER A N     1 
ATOM   603  C CA    . SER A 1 81  ? -7.882  -41.175 -11.976 1.00 44.38 ? 75  SER A CA    1 
ATOM   604  C C     . SER A 1 81  ? -7.715  -40.250 -10.774 1.00 45.16 ? 75  SER A C     1 
ATOM   605  O O     . SER A 1 81  ? -8.214  -40.531 -9.680  1.00 47.54 ? 75  SER A O     1 
ATOM   606  C CB    . SER A 1 81  ? -8.149  -42.613 -11.515 1.00 46.16 ? 75  SER A CB    1 
ATOM   607  O OG    . SER A 1 81  ? -8.616  -43.404 -12.591 1.00 50.04 ? 75  SER A OG    1 
ATOM   608  N N     . TYR A 1 82  ? -7.002  -39.146 -10.965 1.00 41.22 ? 76  TYR A N     1 
ATOM   609  C CA    . TYR A 1 82  ? -6.984  -38.073 -9.988  1.00 36.44 ? 76  TYR A CA    1 
ATOM   610  C C     . TYR A 1 82  ? -8.176  -37.146 -10.232 1.00 39.21 ? 76  TYR A C     1 
ATOM   611  O O     . TYR A 1 82  ? -8.881  -37.246 -11.239 1.00 41.28 ? 76  TYR A O     1 
ATOM   612  C CB    . TYR A 1 82  ? -5.674  -37.284 -10.071 1.00 38.81 ? 76  TYR A CB    1 
ATOM   613  C CG    . TYR A 1 82  ? -4.380  -38.062 -9.878  1.00 36.12 ? 76  TYR A CG    1 
ATOM   614  C CD1   . TYR A 1 82  ? -4.318  -39.218 -9.104  1.00 41.83 ? 76  TYR A CD1   1 
ATOM   615  C CD2   . TYR A 1 82  ? -3.204  -37.611 -10.469 1.00 33.85 ? 76  TYR A CD2   1 
ATOM   616  C CE1   . TYR A 1 82  ? -3.110  -39.904 -8.934  1.00 36.76 ? 76  TYR A CE1   1 
ATOM   617  C CE2   . TYR A 1 82  ? -2.008  -38.278 -10.303 1.00 39.65 ? 76  TYR A CE2   1 
ATOM   618  C CZ    . TYR A 1 82  ? -1.960  -39.425 -9.541  1.00 39.75 ? 76  TYR A CZ    1 
ATOM   619  O OH    . TYR A 1 82  ? -0.744  -40.072 -9.403  1.00 37.31 ? 76  TYR A OH    1 
ATOM   620  N N     . LYS A 1 83  ? -8.406  -36.232 -9.296  1.00 39.38 ? 77  LYS A N     1 
ATOM   621  C CA    . LYS A 1 83  ? -9.453  -35.234 -9.446  1.00 41.28 ? 77  LYS A CA    1 
ATOM   622  C C     . LYS A 1 83  ? -8.827  -33.852 -9.569  1.00 39.17 ? 77  LYS A C     1 
ATOM   623  O O     . LYS A 1 83  ? -7.843  -33.548 -8.886  1.00 43.00 ? 77  LYS A O     1 
ATOM   624  C CB    . LYS A 1 83  ? -10.419 -35.275 -8.264  1.00 41.64 ? 77  LYS A CB    1 
ATOM   625  C CG    . LYS A 1 83  ? -10.981 -36.661 -7.967  1.00 45.51 ? 77  LYS A CG    1 
ATOM   626  N N     . LEU A 1 84  ? -9.390  -33.016 -10.443 1.00 33.88 ? 78  LEU A N     1 
ATOM   627  C CA    . LEU A 1 84  ? -8.930  -31.641 -10.612 1.00 33.18 ? 78  LEU A CA    1 
ATOM   628  C C     . LEU A 1 84  ? -10.038 -30.679 -10.215 1.00 35.79 ? 78  LEU A C     1 
ATOM   629  O O     . LEU A 1 84  ? -11.119 -30.689 -10.813 1.00 40.25 ? 78  LEU A O     1 
ATOM   630  C CB    . LEU A 1 84  ? -8.497  -31.358 -12.050 1.00 32.10 ? 78  LEU A CB    1 
ATOM   631  C CG    . LEU A 1 84  ? -8.065  -29.899 -12.253 1.00 34.58 ? 78  LEU A CG    1 
ATOM   632  C CD1   . LEU A 1 84  ? -6.807  -29.576 -11.455 1.00 32.28 ? 78  LEU A CD1   1 
ATOM   633  C CD2   . LEU A 1 84  ? -7.856  -29.570 -13.714 1.00 31.43 ? 78  LEU A CD2   1 
ATOM   634  N N     . VAL A 1 85  ? -9.763  -29.844 -9.222  1.00 36.27 ? 79  VAL A N     1 
ATOM   635  C CA    . VAL A 1 85  ? -10.635 -28.738 -8.850  1.00 38.20 ? 79  VAL A CA    1 
ATOM   636  C C     . VAL A 1 85  ? -10.031 -27.471 -9.438  1.00 35.61 ? 79  VAL A C     1 
ATOM   637  O O     . VAL A 1 85  ? -8.866  -27.150 -9.174  1.00 34.56 ? 79  VAL A O     1 
ATOM   638  C CB    . VAL A 1 85  ? -10.782 -28.632 -7.326  1.00 37.95 ? 79  VAL A CB    1 
ATOM   639  C CG1   . VAL A 1 85  ? -11.544 -27.361 -6.953  1.00 41.56 ? 79  VAL A CG1   1 
ATOM   640  C CG2   . VAL A 1 85  ? -11.501 -29.859 -6.787  1.00 39.38 ? 79  VAL A CG2   1 
ATOM   641  N N     . PHE A 1 86  ? -10.800 -26.751 -10.251 1.00 35.53 ? 80  PHE A N     1 
ATOM   642  C CA    . PHE A 1 86  ? -10.261 -25.606 -10.979 1.00 33.96 ? 80  PHE A CA    1 
ATOM   643  C C     . PHE A 1 86  ? -11.092 -24.369 -10.668 1.00 36.33 ? 80  PHE A C     1 
ATOM   644  O O     . PHE A 1 86  ? -12.255 -24.275 -11.076 1.00 40.08 ? 80  PHE A O     1 
ATOM   645  C CB    . PHE A 1 86  ? -10.219 -25.866 -12.481 1.00 34.89 ? 80  PHE A CB    1 
ATOM   646  C CG    . PHE A 1 86  ? -9.364  -24.887 -13.228 1.00 34.23 ? 80  PHE A CG    1 
ATOM   647  C CD1   . PHE A 1 86  ? -9.924  -23.769 -13.833 1.00 39.05 ? 80  PHE A CD1   1 
ATOM   648  C CD2   . PHE A 1 86  ? -7.992  -25.066 -13.299 1.00 36.00 ? 80  PHE A CD2   1 
ATOM   649  C CE1   . PHE A 1 86  ? -9.126  -22.862 -14.519 1.00 35.25 ? 80  PHE A CE1   1 
ATOM   650  C CE2   . PHE A 1 86  ? -7.199  -24.170 -13.979 1.00 31.93 ? 80  PHE A CE2   1 
ATOM   651  C CZ    . PHE A 1 86  ? -7.765  -23.065 -14.585 1.00 33.11 ? 80  PHE A CZ    1 
ATOM   652  N N     . ALA A 1 87  ? -10.494 -23.428 -9.946  1.00 36.28 ? 81  ALA A N     1 
ATOM   653  C CA    . ALA A 1 87  ? -11.162 -22.184 -9.599  1.00 37.81 ? 81  ALA A CA    1 
ATOM   654  C C     . ALA A 1 87  ? -10.956 -21.167 -10.714 1.00 38.84 ? 81  ALA A C     1 
ATOM   655  O O     . ALA A 1 87  ? -9.896  -21.114 -11.333 1.00 41.21 ? 81  ALA A O     1 
ATOM   656  C CB    . ALA A 1 87  ? -10.628 -21.638 -8.275  1.00 38.37 ? 81  ALA A CB    1 
ATOM   657  N N     . CYS A 1 88  ? -11.977 -20.359 -10.974 1.00 42.52 ? 82  CYS A N     1 
ATOM   658  C CA    . CYS A 1 88  ? -11.853 -19.388 -12.052 1.00 46.23 ? 82  CYS A CA    1 
ATOM   659  C C     . CYS A 1 88  ? -12.842 -18.259 -11.818 1.00 47.12 ? 82  CYS A C     1 
ATOM   660  O O     . CYS A 1 88  ? -13.794 -18.394 -11.044 1.00 52.30 ? 82  CYS A O     1 
ATOM   661  C CB    . CYS A 1 88  ? -12.078 -20.038 -13.421 1.00 45.41 ? 82  CYS A CB    1 
ATOM   662  S SG    . CYS A 1 88  ? -13.647 -20.914 -13.562 1.00 50.31 ? 82  CYS A SG    1 
ATOM   663  N N     . GLU A 1 89  ? -12.593 -17.137 -12.493 1.00 50.66 ? 83  GLU A N     1 
ATOM   664  C CA    . GLU A 1 89  ? -13.521 -16.018 -12.431 1.00 52.60 ? 83  GLU A CA    1 
ATOM   665  C C     . GLU A 1 89  ? -14.865 -16.432 -13.015 1.00 56.81 ? 83  GLU A C     1 
ATOM   666  O O     . GLU A 1 89  ? -14.952 -17.355 -13.832 1.00 49.36 ? 83  GLU A O     1 
ATOM   667  C CB    . GLU A 1 89  ? -12.965 -14.808 -13.188 1.00 57.80 ? 83  GLU A CB    1 
ATOM   668  C CG    . GLU A 1 89  ? -11.592 -14.332 -12.719 1.00 57.62 ? 83  GLU A CG    1 
ATOM   669  C CD    . GLU A 1 89  ? -11.616 -13.673 -11.347 1.00 64.65 ? 83  GLU A CD    1 
ATOM   670  O OE1   . GLU A 1 89  ? -10.532 -13.278 -10.865 1.00 69.35 ? 83  GLU A OE1   1 
ATOM   671  O OE2   . GLU A 1 89  ? -12.707 -13.545 -10.749 1.00 67.62 ? 83  GLU A OE2   1 
ATOM   672  N N     . LYS A 1 90  ? -15.921 -15.752 -12.567 1.00 61.86 ? 84  LYS A N     1 
ATOM   673  C CA    . LYS A 1 90  ? -17.270 -16.049 -13.035 1.00 63.49 ? 84  LYS A CA    1 
ATOM   674  C C     . LYS A 1 90  ? -17.288 -16.155 -14.553 1.00 63.58 ? 84  LYS A C     1 
ATOM   675  O O     . LYS A 1 90  ? -16.956 -15.199 -15.261 1.00 68.06 ? 84  LYS A O     1 
ATOM   676  C CB    . LYS A 1 90  ? -18.241 -14.968 -12.559 1.00 71.03 ? 84  LYS A CB    1 
ATOM   677  N N     . ILE A 1 91  ? -17.633 -17.334 -15.045 1.00 56.88 ? 85  ILE A N     1 
ATOM   678  C CA    . ILE A 1 91  ? -17.516 -17.628 -16.466 1.00 55.17 ? 85  ILE A CA    1 
ATOM   679  C C     . ILE A 1 91  ? -18.652 -16.959 -17.222 1.00 61.19 ? 85  ILE A C     1 
ATOM   680  O O     . ILE A 1 91  ? -19.788 -16.878 -16.734 1.00 61.66 ? 85  ILE A O     1 
ATOM   681  C CB    . ILE A 1 91  ? -17.502 -19.150 -16.690 1.00 57.66 ? 85  ILE A CB    1 
ATOM   682  N N     . SER A 1 92  ? -18.333 -16.459 -18.414 1.00 59.71 ? 86  SER A N     1 
ATOM   683  C CA    . SER A 1 92  ? -19.319 -15.831 -19.279 1.00 67.71 ? 86  SER A CA    1 
ATOM   684  C C     . SER A 1 92  ? -20.505 -16.758 -19.518 1.00 65.18 ? 86  SER A C     1 
ATOM   685  O O     . SER A 1 92  ? -20.335 -17.954 -19.779 1.00 63.17 ? 86  SER A O     1 
ATOM   686  C CB    . SER A 1 92  ? -18.660 -15.450 -20.606 1.00 63.35 ? 86  SER A CB    1 
ATOM   687  O OG    . SER A 1 92  ? -19.516 -15.700 -21.703 1.00 66.07 ? 86  SER A OG    1 
ATOM   688  N N     . THR A 1 93  ? -21.712 -16.195 -19.408 1.00 69.22 ? 87  THR A N     1 
ATOM   689  C CA    . THR A 1 93  ? -22.924 -16.956 -19.690 1.00 71.63 ? 87  THR A CA    1 
ATOM   690  C C     . THR A 1 93  ? -22.872 -17.585 -21.076 1.00 71.72 ? 87  THR A C     1 
ATOM   691  O O     . THR A 1 93  ? -23.241 -18.752 -21.252 1.00 71.35 ? 87  THR A O     1 
ATOM   692  C CB    . THR A 1 93  ? -24.151 -16.048 -19.554 1.00 76.50 ? 87  THR A CB    1 
ATOM   693  O OG1   . THR A 1 93  ? -24.291 -15.629 -18.191 1.00 76.68 ? 87  THR A OG1   1 
ATOM   694  C CG2   . THR A 1 93  ? -25.415 -16.774 -19.991 1.00 80.22 ? 87  THR A CG2   1 
ATOM   695  N N     . PHE A 1 94  ? -22.399 -16.830 -22.072 1.00 72.47 ? 88  PHE A N     1 
ATOM   696  C CA    . PHE A 1 94  ? -22.300 -17.364 -23.427 1.00 72.91 ? 88  PHE A CA    1 
ATOM   697  C C     . PHE A 1 94  ? -21.409 -18.598 -23.470 1.00 70.11 ? 88  PHE A C     1 
ATOM   698  O O     . PHE A 1 94  ? -21.766 -19.613 -24.080 1.00 70.53 ? 88  PHE A O     1 
ATOM   699  C CB    . PHE A 1 94  ? -21.777 -16.288 -24.380 1.00 74.24 ? 88  PHE A CB    1 
ATOM   700  N N     . LEU A 1 95  ? -20.245 -18.536 -22.813 1.00 64.92 ? 89  LEU A N     1 
ATOM   701  C CA    . LEU A 1 95  ? -19.313 -19.658 -22.857 1.00 64.16 ? 89  LEU A CA    1 
ATOM   702  C C     . LEU A 1 95  ? -19.881 -20.883 -22.149 1.00 66.58 ? 89  LEU A C     1 
ATOM   703  O O     . LEU A 1 95  ? -19.718 -22.010 -22.632 1.00 62.33 ? 89  LEU A O     1 
ATOM   704  C CB    . LEU A 1 95  ? -17.970 -19.255 -22.243 1.00 62.07 ? 89  LEU A CB    1 
ATOM   705  C CG    . LEU A 1 95  ? -16.878 -20.331 -22.200 1.00 59.04 ? 89  LEU A CG    1 
ATOM   706  C CD1   . LEU A 1 95  ? -16.664 -20.945 -23.580 1.00 62.87 ? 89  LEU A CD1   1 
ATOM   707  C CD2   . LEU A 1 95  ? -15.571 -19.761 -21.661 1.00 56.23 ? 89  LEU A CD2   1 
ATOM   708  N N     . LYS A 1 96  ? -20.541 -20.685 -21.003 1.00 62.33 ? 90  LYS A N     1 
ATOM   709  C CA    . LYS A 1 96  ? -21.132 -21.811 -20.284 1.00 63.25 ? 90  LYS A CA    1 
ATOM   710  C C     . LYS A 1 96  ? -22.087 -22.585 -21.180 1.00 67.83 ? 90  LYS A C     1 
ATOM   711  O O     . LYS A 1 96  ? -22.039 -23.818 -21.246 1.00 68.88 ? 90  LYS A O     1 
ATOM   712  C CB    . LYS A 1 96  ? -21.865 -21.321 -19.035 1.00 66.96 ? 90  LYS A CB    1 
ATOM   713  C CG    . LYS A 1 96  ? -20.981 -21.105 -17.838 1.00 62.80 ? 90  LYS A CG    1 
ATOM   714  N N     . ASN A 1 97  ? -22.960 -21.865 -21.886 1.00 71.20 ? 91  ASN A N     1 
ATOM   715  C CA    . ASN A 1 97  ? -23.932 -22.496 -22.764 1.00 72.28 ? 91  ASN A CA    1 
ATOM   716  C C     . ASN A 1 97  ? -23.314 -22.989 -24.065 1.00 72.27 ? 91  ASN A C     1 
ATOM   717  O O     . ASN A 1 97  ? -23.896 -23.863 -24.717 1.00 74.32 ? 91  ASN A O     1 
ATOM   718  C CB    . ASN A 1 97  ? -25.070 -21.515 -23.061 1.00 78.70 ? 91  ASN A CB    1 
ATOM   719  N N     . ASN A 1 98  ? -22.150 -22.466 -24.449 1.00 67.81 ? 92  ASN A N     1 
ATOM   720  C CA    . ASN A 1 98  ? -21.496 -22.814 -25.711 1.00 67.44 ? 92  ASN A CA    1 
ATOM   721  C C     . ASN A 1 98  ? -20.032 -23.155 -25.453 1.00 66.25 ? 92  ASN A C     1 
ATOM   722  O O     . ASN A 1 98  ? -19.129 -22.383 -25.799 1.00 67.14 ? 92  ASN A O     1 
ATOM   723  C CB    . ASN A 1 98  ? -21.619 -21.668 -26.718 1.00 73.01 ? 92  ASN A CB    1 
ATOM   724  N N     . ASN A 1 102 ? -10.142 -25.276 -25.056 1.00 46.30 ? 96  ASN A N     1 
ATOM   725  C CA    . ASN A 1 102 ? -9.601  -25.895 -23.848 1.00 40.43 ? 96  ASN A CA    1 
ATOM   726  C C     . ASN A 1 102 ? -10.692 -26.104 -22.800 1.00 42.45 ? 96  ASN A C     1 
ATOM   727  O O     . ASN A 1 102 ? -10.686 -27.112 -22.082 1.00 42.86 ? 96  ASN A O     1 
ATOM   728  C CB    . ASN A 1 102 ? -8.468  -25.040 -23.272 1.00 38.74 ? 96  ASN A CB    1 
ATOM   729  C CG    . ASN A 1 102 ? -7.153  -25.164 -24.059 1.00 37.56 ? 96  ASN A CG    1 
ATOM   730  O OD1   . ASN A 1 102 ? -6.849  -26.203 -24.642 1.00 40.80 ? 96  ASN A OD1   1 
ATOM   731  N ND2   . ASN A 1 102 ? -6.354  -24.103 -24.037 1.00 32.02 ? 96  ASN A ND2   1 
ATOM   732  N N     . TYR A 1 103 ? -11.627 -25.152 -22.689 1.00 47.32 ? 97  TYR A N     1 
ATOM   733  C CA    . TYR A 1 103 ? -12.715 -25.277 -21.719 1.00 48.41 ? 97  TYR A CA    1 
ATOM   734  C C     . TYR A 1 103 ? -13.571 -26.501 -22.007 1.00 53.28 ? 97  TYR A C     1 
ATOM   735  O O     . TYR A 1 103 ? -13.981 -27.214 -21.082 1.00 55.88 ? 97  TYR A O     1 
ATOM   736  C CB    . TYR A 1 103 ? -13.578 -24.013 -21.719 1.00 43.72 ? 97  TYR A CB    1 
ATOM   737  C CG    . TYR A 1 103 ? -14.843 -24.107 -20.875 1.00 45.09 ? 97  TYR A CG    1 
ATOM   738  C CD1   . TYR A 1 103 ? -16.100 -24.190 -21.473 1.00 49.39 ? 97  TYR A CD1   1 
ATOM   739  C CD2   . TYR A 1 103 ? -14.782 -24.104 -19.486 1.00 47.64 ? 97  TYR A CD2   1 
ATOM   740  C CE1   . TYR A 1 103 ? -17.252 -24.269 -20.716 1.00 49.64 ? 97  TYR A CE1   1 
ATOM   741  C CE2   . TYR A 1 103 ? -15.937 -24.187 -18.716 1.00 51.22 ? 97  TYR A CE2   1 
ATOM   742  C CZ    . TYR A 1 103 ? -17.168 -24.267 -19.339 1.00 50.37 ? 97  TYR A CZ    1 
ATOM   743  O OH    . TYR A 1 103 ? -18.320 -24.352 -18.588 1.00 59.77 ? 97  TYR A OH    1 
ATOM   744  N N     . ALA A 1 104 ? -13.851 -26.764 -23.284 1.00 51.64 ? 98  ALA A N     1 
ATOM   745  C CA    . ALA A 1 104 ? -14.649 -27.934 -23.632 1.00 51.54 ? 98  ALA A CA    1 
ATOM   746  C C     . ALA A 1 104 ? -13.906 -29.224 -23.313 1.00 51.59 ? 98  ALA A C     1 
ATOM   747  O O     . ALA A 1 104 ? -14.509 -30.189 -22.829 1.00 56.56 ? 98  ALA A O     1 
ATOM   748  C CB    . ALA A 1 104 ? -15.034 -27.892 -25.110 1.00 56.17 ? 98  ALA A CB    1 
ATOM   749  N N     . LEU A 1 105 ? -12.598 -29.266 -23.581 1.00 50.24 ? 99  LEU A N     1 
ATOM   750  C CA    . LEU A 1 105 ? -11.830 -30.470 -23.275 1.00 48.39 ? 99  LEU A CA    1 
ATOM   751  C C     . LEU A 1 105 ? -11.743 -30.700 -21.772 1.00 47.88 ? 99  LEU A C     1 
ATOM   752  O O     . LEU A 1 105 ? -11.794 -31.847 -21.310 1.00 46.48 ? 99  LEU A O     1 
ATOM   753  C CB    . LEU A 1 105 ? -10.429 -30.379 -23.874 1.00 48.01 ? 99  LEU A CB    1 
ATOM   754  C CG    . LEU A 1 105 ? -9.528  -31.562 -23.509 1.00 46.92 ? 99  LEU A CG    1 
ATOM   755  C CD1   . LEU A 1 105 ? -9.301  -32.476 -24.699 1.00 52.90 ? 99  LEU A CD1   1 
ATOM   756  C CD2   . LEU A 1 105 ? -8.210  -31.068 -22.940 1.00 47.80 ? 99  LEU A CD2   1 
ATOM   757  N N     . ALA A 1 106 ? -11.606 -29.621 -20.996 1.00 43.49 ? 100 ALA A N     1 
ATOM   758  C CA    . ALA A 1 106 ? -11.586 -29.754 -19.544 1.00 41.16 ? 100 ALA A CA    1 
ATOM   759  C C     . ALA A 1 106 ? -12.942 -30.204 -19.017 1.00 42.57 ? 100 ALA A C     1 
ATOM   760  O O     . ALA A 1 106 ? -13.010 -31.024 -18.092 1.00 40.88 ? 100 ALA A O     1 
ATOM   761  C CB    . ALA A 1 106 ? -11.169 -28.435 -18.902 1.00 41.15 ? 100 ALA A CB    1 
ATOM   762  N N     . LEU A 1 107 ? -14.031 -29.679 -19.593 1.00 45.50 ? 101 LEU A N     1 
ATOM   763  C CA    . LEU A 1 107 ? -15.362 -30.174 -19.249 1.00 50.71 ? 101 LEU A CA    1 
ATOM   764  C C     . LEU A 1 107 ? -15.491 -31.656 -19.569 1.00 51.97 ? 101 LEU A C     1 
ATOM   765  O O     . LEU A 1 107 ? -16.063 -32.422 -18.785 1.00 57.79 ? 101 LEU A O     1 
ATOM   766  C CB    . LEU A 1 107 ? -16.446 -29.380 -19.989 1.00 52.66 ? 101 LEU A CB    1 
ATOM   767  C CG    . LEU A 1 107 ? -17.041 -28.088 -19.411 1.00 52.11 ? 101 LEU A CG    1 
ATOM   768  C CD1   . LEU A 1 107 ? -18.246 -27.641 -20.236 1.00 53.67 ? 101 LEU A CD1   1 
ATOM   769  C CD2   . LEU A 1 107 ? -17.445 -28.244 -17.954 1.00 52.00 ? 101 LEU A CD2   1 
ATOM   770  N N     . GLU A 1 108 ? -14.956 -32.083 -20.716 1.00 47.92 ? 102 GLU A N     1 
ATOM   771  C CA    . GLU A 1 108 ? -15.069 -33.486 -21.098 1.00 49.96 ? 102 GLU A CA    1 
ATOM   772  C C     . GLU A 1 108 ? -14.225 -34.381 -20.199 1.00 51.81 ? 102 GLU A C     1 
ATOM   773  O O     . GLU A 1 108 ? -14.599 -35.533 -19.950 1.00 55.84 ? 102 GLU A O     1 
ATOM   774  C CB    . GLU A 1 108 ? -14.667 -33.669 -22.560 1.00 49.80 ? 102 GLU A CB    1 
ATOM   775  N N     . ASN A 1 109 ? -13.100 -33.874 -19.695 1.00 41.27 ? 103 ASN A N     1 
ATOM   776  C CA    . ASN A 1 109 ? -12.254 -34.639 -18.790 1.00 41.56 ? 103 ASN A CA    1 
ATOM   777  C C     . ASN A 1 109 ? -12.731 -34.598 -17.345 1.00 43.98 ? 103 ASN A C     1 
ATOM   778  O O     . ASN A 1 109 ? -12.030 -35.109 -16.466 1.00 44.44 ? 103 ASN A O     1 
ATOM   779  C CB    . ASN A 1 109 ? -10.806 -34.145 -18.873 1.00 38.47 ? 103 ASN A CB    1 
ATOM   780  C CG    . ASN A 1 109 ? -10.079 -34.683 -20.092 1.00 40.98 ? 103 ASN A CG    1 
ATOM   781  O OD1   . ASN A 1 109 ? -10.347 -35.799 -20.537 1.00 52.71 ? 103 ASN A OD1   1 
ATOM   782  N ND2   . ASN A 1 109 ? -9.147  -33.896 -20.634 1.00 40.15 ? 103 ASN A ND2   1 
ATOM   783  N N     . GLY A 1 110 ? -13.888 -34.002 -17.073 1.00 41.87 ? 104 GLY A N     1 
ATOM   784  C CA    . GLY A 1 110 ? -14.468 -34.087 -15.746 1.00 46.40 ? 104 GLY A CA    1 
ATOM   785  C C     . GLY A 1 110 ? -13.899 -33.141 -14.716 1.00 44.87 ? 104 GLY A C     1 
ATOM   786  O O     . GLY A 1 110 ? -13.933 -33.449 -13.521 1.00 44.08 ? 104 GLY A O     1 
ATOM   787  N N     . VAL A 1 111 ? -13.382 -31.988 -15.140 1.00 37.79 ? 105 VAL A N     1 
ATOM   788  C CA    . VAL A 1 111 ? -12.859 -31.010 -14.194 1.00 40.86 ? 105 VAL A CA    1 
ATOM   789  C C     . VAL A 1 111 ? -13.992 -30.443 -13.353 1.00 39.93 ? 105 VAL A C     1 
ATOM   790  O O     . VAL A 1 111 ? -15.097 -30.195 -13.854 1.00 44.04 ? 105 VAL A O     1 
ATOM   791  C CB    . VAL A 1 111 ? -12.117 -29.894 -14.946 1.00 37.86 ? 105 VAL A CB    1 
ATOM   792  C CG1   . VAL A 1 111 ? -11.731 -28.773 -13.999 1.00 39.03 ? 105 VAL A CG1   1 
ATOM   793  C CG2   . VAL A 1 111 ? -10.887 -30.464 -15.630 1.00 32.03 ? 105 VAL A CG2   1 
ATOM   794  N N     . ASP A 1 112 ? -13.723 -30.235 -12.061 1.00 40.95 ? 106 ASP A N     1 
ATOM   795  C CA    . ASP A 1 112 ? -14.672 -29.605 -11.141 1.00 42.82 ? 106 ASP A CA    1 
ATOM   796  C C     . ASP A 1 112 ? -14.399 -28.103 -11.123 1.00 41.53 ? 106 ASP A C     1 
ATOM   797  O O     . ASP A 1 112 ? -13.525 -27.631 -10.391 1.00 40.55 ? 106 ASP A O     1 
ATOM   798  C CB    . ASP A 1 112 ? -14.547 -30.217 -9.748  1.00 44.00 ? 106 ASP A CB    1 
ATOM   799  C CG    . ASP A 1 112 ? -15.568 -29.661 -8.760  1.00 55.26 ? 106 ASP A CG    1 
ATOM   800  O OD1   . ASP A 1 112 ? -16.504 -28.949 -9.184  1.00 61.74 ? 106 ASP A OD1   1 
ATOM   801  O OD2   . ASP A 1 112 ? -15.433 -29.942 -7.547  1.00 55.27 ? 106 ASP A OD2   1 
ATOM   802  N N     . PHE A 1 113 ? -15.146 -27.345 -11.925 1.00 42.00 ? 107 PHE A N     1 
ATOM   803  C CA    . PHE A 1 113 ? -15.006 -25.893 -11.942 1.00 41.21 ? 107 PHE A CA    1 
ATOM   804  C C     . PHE A 1 113 ? -15.703 -25.277 -10.736 1.00 43.39 ? 107 PHE A C     1 
ATOM   805  O O     . PHE A 1 113 ? -16.840 -25.635 -10.412 1.00 45.72 ? 107 PHE A O     1 
ATOM   806  C CB    . PHE A 1 113 ? -15.582 -25.304 -13.232 1.00 42.52 ? 107 PHE A CB    1 
ATOM   807  C CG    . PHE A 1 113 ? -14.761 -25.588 -14.451 1.00 50.75 ? 107 PHE A CG    1 
ATOM   808  C CD1   . PHE A 1 113 ? -13.705 -24.763 -14.790 1.00 39.01 ? 107 PHE A CD1   1 
ATOM   809  C CD2   . PHE A 1 113 ? -15.050 -26.672 -15.265 1.00 48.22 ? 107 PHE A CD2   1 
ATOM   810  C CE1   . PHE A 1 113 ? -12.933 -25.018 -15.925 1.00 37.49 ? 107 PHE A CE1   1 
ATOM   811  C CE2   . PHE A 1 113 ? -14.287 -26.933 -16.396 1.00 43.71 ? 107 PHE A CE2   1 
ATOM   812  C CZ    . PHE A 1 113 ? -13.233 -26.104 -16.724 1.00 39.54 ? 107 PHE A CZ    1 
ATOM   813  N N     . VAL A 1 114 ? -15.024 -24.341 -10.077 1.00 43.54 ? 108 VAL A N     1 
ATOM   814  C CA    . VAL A 1 114 ? -15.580 -23.611 -8.941  1.00 45.20 ? 108 VAL A CA    1 
ATOM   815  C C     . VAL A 1 114 ? -15.428 -22.127 -9.230  1.00 46.02 ? 108 VAL A C     1 
ATOM   816  O O     . VAL A 1 114 ? -14.303 -21.631 -9.368  1.00 46.23 ? 108 VAL A O     1 
ATOM   817  C CB    . VAL A 1 114 ? -14.891 -23.981 -7.618  1.00 46.08 ? 108 VAL A CB    1 
ATOM   818  C CG1   . VAL A 1 114 ? -15.596 -23.309 -6.455  1.00 49.94 ? 108 VAL A CG1   1 
ATOM   819  C CG2   . VAL A 1 114 ? -14.877 -25.481 -7.435  1.00 43.55 ? 108 VAL A CG2   1 
ATOM   820  N N     . GLU A 1 115 ? -16.550 -21.421 -9.326  1.00 49.01 ? 109 GLU A N     1 
ATOM   821  C CA    . GLU A 1 115 ? -16.533 -20.042 -9.785  1.00 50.27 ? 109 GLU A CA    1 
ATOM   822  C C     . GLU A 1 115 ? -16.333 -19.069 -8.630  1.00 51.72 ? 109 GLU A C     1 
ATOM   823  O O     . GLU A 1 115 ? -16.803 -19.287 -7.509  1.00 53.25 ? 109 GLU A O     1 
ATOM   824  C CB    . GLU A 1 115 ? -17.822 -19.718 -10.534 1.00 57.86 ? 109 GLU A CB    1 
ATOM   825  C CG    . GLU A 1 115 ? -18.123 -20.719 -11.632 1.00 60.51 ? 109 GLU A CG    1 
ATOM   826  C CD    . GLU A 1 115 ? -19.127 -20.204 -12.633 1.00 66.31 ? 109 GLU A CD    1 
ATOM   827  O OE1   . GLU A 1 115 ? -19.171 -18.976 -12.861 1.00 68.37 ? 109 GLU A OE1   1 
ATOM   828  O OE2   . GLU A 1 115 ? -19.871 -21.031 -13.198 1.00 70.57 ? 109 GLU A OE2   1 
ATOM   829  N N     . ASN A 1 116 ? -15.621 -17.982 -8.930  1.00 51.52 ? 110 ASN A N     1 
ATOM   830  C CA    . ASN A 1 116 ? -15.269 -16.947 -7.962  1.00 53.00 ? 110 ASN A CA    1 
ATOM   831  C C     . ASN A 1 116 ? -16.447 -15.978 -7.834  1.00 57.89 ? 110 ASN A C     1 
ATOM   832  O O     . ASN A 1 116 ? -16.392 -14.816 -8.238  1.00 64.47 ? 110 ASN A O     1 
ATOM   833  C CB    . ASN A 1 116 ? -13.993 -16.247 -8.408  1.00 51.26 ? 110 ASN A CB    1 
ATOM   834  C CG    . ASN A 1 116 ? -13.462 -15.272 -7.382  1.00 58.72 ? 110 ASN A CG    1 
ATOM   835  O OD1   . ASN A 1 116 ? -13.770 -15.369 -6.195  1.00 56.78 ? 110 ASN A OD1   1 
ATOM   836  N ND2   . ASN A 1 116 ? -12.647 -14.322 -7.839  1.00 52.50 ? 110 ASN A ND2   1 
ATOM   837  N N     . ILE A 1 117 ? -17.538 -16.497 -7.259  1.00 59.05 ? 111 ILE A N     1 
ATOM   838  C CA    . ILE A 1 117 ? -18.798 -15.754 -7.222  1.00 63.24 ? 111 ILE A CA    1 
ATOM   839  C C     . ILE A 1 117 ? -18.633 -14.438 -6.474  1.00 69.79 ? 111 ILE A C     1 
ATOM   840  O O     . ILE A 1 117 ? -19.188 -13.407 -6.874  1.00 73.59 ? 111 ILE A O     1 
ATOM   841  C CB    . ILE A 1 117 ? -19.916 -16.616 -6.604  1.00 64.88 ? 111 ILE A CB    1 
ATOM   842  C CG1   . ILE A 1 117 ? -19.461 -17.221 -5.272  1.00 65.67 ? 111 ILE A CG1   1 
ATOM   843  C CG2   . ILE A 1 117 ? -20.357 -17.696 -7.582  1.00 63.53 ? 111 ILE A CG2   1 
ATOM   844  C CD1   . ILE A 1 117 ? -20.595 -17.741 -4.409  1.00 69.67 ? 111 ILE A CD1   1 
ATOM   845  N N     . HIS A 1 118 ? -17.870 -14.445 -5.384  1.00 70.85 ? 112 HIS A N     1 
ATOM   846  C CA    . HIS A 1 118 ? -17.647 -13.242 -4.594  1.00 75.22 ? 112 HIS A CA    1 
ATOM   847  C C     . HIS A 1 118 ? -16.555 -12.349 -5.174  1.00 73.62 ? 112 HIS A C     1 
ATOM   848  O O     . HIS A 1 118 ? -16.071 -11.451 -4.474  1.00 74.13 ? 112 HIS A O     1 
ATOM   849  C CB    . HIS A 1 118 ? -17.327 -13.626 -3.147  1.00 72.78 ? 112 HIS A CB    1 
ATOM   850  C CG    . HIS A 1 118 ? -18.456 -14.324 -2.453  1.00 77.26 ? 112 HIS A CG    1 
ATOM   851  N ND1   . HIS A 1 118 ? -18.327 -15.575 -1.890  1.00 75.37 ? 112 HIS A ND1   1 
ATOM   852  C CD2   . HIS A 1 118 ? -19.740 -13.948 -2.241  1.00 81.12 ? 112 HIS A CD2   1 
ATOM   853  C CE1   . HIS A 1 118 ? -19.480 -15.939 -1.360  1.00 77.81 ? 112 HIS A CE1   1 
ATOM   854  N NE2   . HIS A 1 118 ? -20.354 -14.969 -1.558  1.00 82.09 ? 112 HIS A NE2   1 
ATOM   855  N N     . SER A 1 119 ? -16.179 -12.588 -6.435  1.00 69.78 ? 113 SER A N     1 
ATOM   856  C CA    . SER A 1 119 ? -15.196 -11.801 -7.175  1.00 65.84 ? 113 SER A CA    1 
ATOM   857  C C     . SER A 1 119 ? -13.963 -11.485 -6.337  1.00 65.96 ? 113 SER A C     1 
ATOM   858  O O     . SER A 1 119 ? -13.421 -10.378 -6.415  1.00 69.26 ? 113 SER A O     1 
ATOM   859  C CB    . SER A 1 119 ? -15.833 -10.508 -7.695  1.00 66.55 ? 113 SER A CB    1 
ATOM   860  N N     . LEU A 1 120 ? -13.515 -12.448 -5.535  1.00 63.00 ? 114 LEU A N     1 
ATOM   861  C CA    . LEU A 1 120 ? -12.362 -12.258 -4.673  1.00 62.49 ? 114 LEU A CA    1 
ATOM   862  C C     . LEU A 1 120 ? -11.075 -12.526 -5.451  1.00 62.91 ? 114 LEU A C     1 
ATOM   863  O O     . LEU A 1 120 ? -11.088 -12.834 -6.646  1.00 63.79 ? 114 LEU A O     1 
ATOM   864  C CB    . LEU A 1 120 ? -12.462 -13.161 -3.444  1.00 60.68 ? 114 LEU A CB    1 
ATOM   865  N N     . SER A 1 121 ? -9.942  -12.392 -4.766  1.00 63.89 ? 115 SER A N     1 
ATOM   866  C CA    . SER A 1 121 ? -8.662  -12.741 -5.368  1.00 57.03 ? 115 SER A CA    1 
ATOM   867  C C     . SER A 1 121 ? -8.660  -14.214 -5.742  1.00 52.68 ? 115 SER A C     1 
ATOM   868  O O     . SER A 1 121 ? -8.782  -15.085 -4.875  1.00 50.16 ? 115 SER A O     1 
ATOM   869  C CB    . SER A 1 121 ? -7.520  -12.427 -4.404  1.00 60.58 ? 115 SER A CB    1 
ATOM   870  N N     . LEU A 1 122 ? -8.519  -14.489 -7.039  1.00 51.37 ? 116 LEU A N     1 
ATOM   871  C CA    . LEU A 1 122 ? -8.721  -15.846 -7.534  1.00 51.94 ? 116 LEU A CA    1 
ATOM   872  C C     . LEU A 1 122 ? -7.730  -16.825 -6.914  1.00 47.34 ? 116 LEU A C     1 
ATOM   873  O O     . LEU A 1 122 ? -8.083  -17.977 -6.631  1.00 48.81 ? 116 LEU A O     1 
ATOM   874  C CB    . LEU A 1 122 ? -8.623  -15.859 -9.058  1.00 51.75 ? 116 LEU A CB    1 
ATOM   875  C CG    . LEU A 1 122 ? -9.177  -17.126 -9.697  1.00 50.88 ? 116 LEU A CG    1 
ATOM   876  C CD1   . LEU A 1 122 ? -10.625 -17.304 -9.291  1.00 48.51 ? 116 LEU A CD1   1 
ATOM   877  C CD2   . LEU A 1 122 ? -9.025  -17.080 -11.210 1.00 51.46 ? 116 LEU A CD2   1 
ATOM   878  N N     . LYS A 1 123 ? -6.489  -16.389 -6.682  1.00 46.49 ? 117 LYS A N     1 
ATOM   879  C CA    . LYS A 1 123 ? -5.514  -17.275 -6.050  1.00 42.70 ? 117 LYS A CA    1 
ATOM   880  C C     . LYS A 1 123 ? -5.901  -17.584 -4.607  1.00 46.89 ? 117 LYS A C     1 
ATOM   881  O O     . LYS A 1 123 ? -5.830  -18.740 -4.169  1.00 42.77 ? 117 LYS A O     1 
ATOM   882  C CB    . LYS A 1 123 ? -4.118  -16.663 -6.092  1.00 44.68 ? 117 LYS A CB    1 
ATOM   883  C CG    . LYS A 1 123 ? -3.131  -17.431 -5.227  1.00 45.55 ? 117 LYS A CG    1 
ATOM   884  C CD    . LYS A 1 123 ? -1.715  -16.942 -5.389  1.00 44.09 ? 117 LYS A CD    1 
ATOM   885  C CE    . LYS A 1 123 ? -0.745  -17.895 -4.720  1.00 48.38 ? 117 LYS A CE    1 
ATOM   886  N NZ    . LYS A 1 123 ? 0.663   -17.510 -4.999  1.00 51.19 ? 117 LYS A NZ    1 
ATOM   887  N N     . GLN A 1 124 ? -6.285  -16.556 -3.845  1.00 46.48 ? 118 GLN A N     1 
ATOM   888  C CA    . GLN A 1 124 ? -6.730  -16.781 -2.472  1.00 49.75 ? 118 GLN A CA    1 
ATOM   889  C C     . GLN A 1 124 ? -7.963  -17.672 -2.449  1.00 46.02 ? 118 GLN A C     1 
ATOM   890  O O     . GLN A 1 124 ? -8.061  -18.600 -1.638  1.00 46.64 ? 118 GLN A O     1 
ATOM   891  C CB    . GLN A 1 124 ? -7.019  -15.446 -1.781  1.00 50.02 ? 118 GLN A CB    1 
ATOM   892  N N     . PHE A 1 125 ? -8.921  -17.391 -3.333  1.00 51.11 ? 119 PHE A N     1 
ATOM   893  C CA    . PHE A 1 125 ? -10.083 -18.257 -3.496  1.00 50.34 ? 119 PHE A CA    1 
ATOM   894  C C     . PHE A 1 125 ? -9.659  -19.699 -3.734  1.00 47.11 ? 119 PHE A C     1 
ATOM   895  O O     . PHE A 1 125 ? -10.100 -20.617 -3.034  1.00 44.35 ? 119 PHE A O     1 
ATOM   896  C CB    . PHE A 1 125 ? -10.940 -17.744 -4.656  1.00 49.50 ? 119 PHE A CB    1 
ATOM   897  C CG    . PHE A 1 125 ? -12.181 -18.556 -4.910  1.00 52.78 ? 119 PHE A CG    1 
ATOM   898  C CD1   . PHE A 1 125 ? -12.367 -19.206 -6.117  1.00 49.25 ? 119 PHE A CD1   1 
ATOM   899  C CD2   . PHE A 1 125 ? -13.166 -18.657 -3.945  1.00 54.75 ? 119 PHE A CD2   1 
ATOM   900  C CE1   . PHE A 1 125 ? -13.514 -19.948 -6.353  1.00 46.89 ? 119 PHE A CE1   1 
ATOM   901  C CE2   . PHE A 1 125 ? -14.315 -19.397 -4.176  1.00 57.09 ? 119 PHE A CE2   1 
ATOM   902  C CZ    . PHE A 1 125 ? -14.492 -20.039 -5.380  1.00 49.60 ? 119 PHE A CZ    1 
ATOM   903  N N     . ALA A 1 126 ? -8.778  -19.915 -4.712  1.00 44.64 ? 120 ALA A N     1 
ATOM   904  C CA    . ALA A 1 126 ? -8.338  -21.268 -5.029  1.00 40.97 ? 120 ALA A CA    1 
ATOM   905  C C     . ALA A 1 126 ? -7.638  -21.922 -3.842  1.00 38.69 ? 120 ALA A C     1 
ATOM   906  O O     . ALA A 1 126 ? -7.906  -23.083 -3.518  1.00 38.57 ? 120 ALA A O     1 
ATOM   907  C CB    . ALA A 1 126 ? -7.419  -21.238 -6.246  1.00 37.45 ? 120 ALA A CB    1 
ATOM   908  N N     . LEU A 1 127 ? -6.723  -21.194 -3.192  1.00 42.92 ? 121 LEU A N     1 
ATOM   909  C CA    . LEU A 1 127 ? -5.995  -21.749 -2.054  1.00 39.21 ? 121 LEU A CA    1 
ATOM   910  C C     . LEU A 1 127 ? -6.947  -22.163 -0.939  1.00 44.37 ? 121 LEU A C     1 
ATOM   911  O O     . LEU A 1 127 ? -6.697  -23.145 -0.231  1.00 49.00 ? 121 LEU A O     1 
ATOM   912  C CB    . LEU A 1 127 ? -4.992  -20.731 -1.515  1.00 53.05 ? 121 LEU A CB    1 
ATOM   913  C CG    . LEU A 1 127 ? -3.604  -20.577 -2.127  1.00 48.88 ? 121 LEU A CG    1 
ATOM   914  C CD1   . LEU A 1 127 ? -3.010  -19.249 -1.671  1.00 53.98 ? 121 LEU A CD1   1 
ATOM   915  C CD2   . LEU A 1 127 ? -2.714  -21.737 -1.710  1.00 47.08 ? 121 LEU A CD2   1 
ATOM   916  N N     . SER A 1 128 ? -8.042  -21.420 -0.765  1.00 49.11 ? 122 SER A N     1 
ATOM   917  C CA    . SER A 1 128 ? -8.979  -21.727 0.309   1.00 50.20 ? 122 SER A CA    1 
ATOM   918  C C     . SER A 1 128 ? -9.697  -23.047 0.067   1.00 49.44 ? 122 SER A C     1 
ATOM   919  O O     . SER A 1 128 ? -10.051 -23.740 1.026   1.00 50.28 ? 122 SER A O     1 
ATOM   920  C CB    . SER A 1 128 ? -9.985  -20.590 0.465   1.00 52.32 ? 122 SER A CB    1 
ATOM   921  O OG    . SER A 1 128 ? -9.346  -19.394 0.879   1.00 51.19 ? 122 SER A OG    1 
ATOM   922  N N     . LEU A 1 129 ? -9.906  -23.421 -1.198  1.00 46.78 ? 123 LEU A N     1 
ATOM   923  C CA    . LEU A 1 129 ? -10.534 -24.702 -1.503  1.00 48.82 ? 123 LEU A CA    1 
ATOM   924  C C     . LEU A 1 129 ? -9.616  -25.886 -1.251  1.00 51.30 ? 123 LEU A C     1 
ATOM   925  O O     . LEU A 1 129 ? -10.065 -27.035 -1.351  1.00 53.68 ? 123 LEU A O     1 
ATOM   926  C CB    . LEU A 1 129 ? -10.995 -24.730 -2.958  1.00 45.61 ? 123 LEU A CB    1 
ATOM   927  C CG    . LEU A 1 129 ? -11.770 -23.509 -3.445  1.00 50.26 ? 123 LEU A CG    1 
ATOM   928  C CD1   . LEU A 1 129 ? -12.118 -23.684 -4.916  1.00 47.22 ? 123 LEU A CD1   1 
ATOM   929  C CD2   . LEU A 1 129 ? -13.018 -23.290 -2.600  1.00 55.32 ? 123 LEU A CD2   1 
ATOM   930  N N     . CYS A 1 130 ? -8.352  -25.645 -0.927  1.00 47.09 ? 124 CYS A N     1 
ATOM   931  C CA    . CYS A 1 130 ? -7.351  -26.704 -0.890  1.00 44.35 ? 124 CYS A CA    1 
ATOM   932  C C     . CYS A 1 130 ? -7.300  -27.255 0.528   1.00 51.93 ? 124 CYS A C     1 
ATOM   933  O O     . CYS A 1 130 ? -6.773  -26.611 1.439   1.00 56.97 ? 124 CYS A O     1 
ATOM   934  C CB    . CYS A 1 130 ? -6.003  -26.166 -1.357  1.00 55.16 ? 124 CYS A CB    1 
ATOM   935  S SG    . CYS A 1 130 ? -4.842  -27.430 -1.856  1.00 52.73 ? 124 CYS A SG    1 
ATOM   936  N N     . LYS A 1 131 ? -7.870  -28.445 0.721   1.00 48.34 ? 125 LYS A N     1 
ATOM   937  C CA    . LYS A 1 131 ? -7.911  -29.072 2.032   1.00 52.74 ? 125 LYS A CA    1 
ATOM   938  C C     . LYS A 1 131 ? -6.563  -29.704 2.366   1.00 48.96 ? 125 LYS A C     1 
ATOM   939  O O     . LYS A 1 131 ? -5.617  -29.687 1.572   1.00 46.66 ? 125 LYS A O     1 
ATOM   940  C CB    . LYS A 1 131 ? -9.016  -30.129 2.092   1.00 53.69 ? 125 LYS A CB    1 
ATOM   941  C CG    . LYS A 1 131 ? -10.432 -29.576 2.129   1.00 55.24 ? 125 LYS A CG    1 
ATOM   942  N N     . LYS A 1 132 ? -6.470  -30.260 3.569   1.00 52.46 ? 126 LYS A N     1 
ATOM   943  C CA    . LYS A 1 132 ? -5.369  -31.159 3.867   1.00 55.40 ? 126 LYS A CA    1 
ATOM   944  C C     . LYS A 1 132 ? -5.484  -32.384 2.972   1.00 56.08 ? 126 LYS A C     1 
ATOM   945  O O     . LYS A 1 132 ? -6.586  -32.869 2.697   1.00 65.81 ? 126 LYS A O     1 
ATOM   946  C CB    . LYS A 1 132 ? -5.380  -31.564 5.342   1.00 56.22 ? 126 LYS A CB    1 
ATOM   947  N N     . ASP A 1 133 ? -4.340  -32.859 2.498   1.00 45.72 ? 127 ASP A N     1 
ATOM   948  C CA    . ASP A 1 133 ? -4.150  -33.966 1.568   1.00 47.16 ? 127 ASP A CA    1 
ATOM   949  C C     . ASP A 1 133 ? -4.403  -33.558 0.118   1.00 44.41 ? 127 ASP A C     1 
ATOM   950  O O     . ASP A 1 133 ? -4.114  -34.350 -0.775  1.00 45.54 ? 127 ASP A O     1 
ATOM   951  C CB    . ASP A 1 133 ? -5.014  -35.204 1.890   1.00 46.30 ? 127 ASP A CB    1 
ATOM   952  C CG    . ASP A 1 133 ? -4.676  -35.820 3.233   1.00 56.91 ? 127 ASP A CG    1 
ATOM   953  O OD1   . ASP A 1 133 ? -3.588  -35.519 3.769   1.00 61.44 ? 127 ASP A OD1   1 
ATOM   954  O OD2   . ASP A 1 133 ? -5.493  -36.616 3.748   1.00 60.15 ? 127 ASP A OD2   1 
ATOM   955  N N     . ASP A 1 134 ? -4.933  -32.366 -0.157  1.00 40.71 ? 128 ASP A N     1 
ATOM   956  C CA    . ASP A 1 134 ? -5.002  -31.892 -1.536  1.00 36.12 ? 128 ASP A CA    1 
ATOM   957  C C     . ASP A 1 134 ? -3.674  -31.268 -1.957  1.00 32.48 ? 128 ASP A C     1 
ATOM   958  O O     . ASP A 1 134 ? -2.909  -30.769 -1.128  1.00 41.35 ? 128 ASP A O     1 
ATOM   959  C CB    . ASP A 1 134 ? -6.116  -30.856 -1.710  1.00 38.16 ? 128 ASP A CB    1 
ATOM   960  C CG    . ASP A 1 134 ? -7.503  -31.414 -1.422  1.00 43.89 ? 128 ASP A CG    1 
ATOM   961  O OD1   . ASP A 1 134 ? -7.707  -32.641 -1.534  1.00 48.46 ? 128 ASP A OD1   1 
ATOM   962  O OD2   . ASP A 1 134 ? -8.402  -30.606 -1.108  1.00 47.02 ? 128 ASP A OD2   1 
ATOM   963  N N     . VAL A 1 135 ? -3.405  -31.293 -3.260  1.00 30.26 ? 129 VAL A N     1 
ATOM   964  C CA    . VAL A 1 135 ? -2.203  -30.691 -3.832  1.00 28.40 ? 129 VAL A CA    1 
ATOM   965  C C     . VAL A 1 135 ? -2.609  -29.410 -4.548  1.00 28.65 ? 129 VAL A C     1 
ATOM   966  O O     . VAL A 1 135 ? -3.422  -29.439 -5.479  1.00 33.38 ? 129 VAL A O     1 
ATOM   967  C CB    . VAL A 1 135 ? -1.482  -31.662 -4.782  1.00 32.58 ? 129 VAL A CB    1 
ATOM   968  C CG1   . VAL A 1 135 ? -0.282  -30.990 -5.450  1.00 33.84 ? 129 VAL A CG1   1 
ATOM   969  C CG2   . VAL A 1 135 ? -1.058  -32.929 -4.023  1.00 34.23 ? 129 VAL A CG2   1 
ATOM   970  N N     . PHE A 1 136 ? -2.036  -28.286 -4.121  1.00 32.37 ? 130 PHE A N     1 
ATOM   971  C CA    . PHE A 1 136 ? -2.269  -26.996 -4.761  1.00 31.31 ? 130 PHE A CA    1 
ATOM   972  C C     . PHE A 1 136 ? -1.257  -26.784 -5.878  1.00 27.16 ? 130 PHE A C     1 
ATOM   973  O O     . PHE A 1 136 ? -0.053  -26.962 -5.671  1.00 31.24 ? 130 PHE A O     1 
ATOM   974  C CB    . PHE A 1 136 ? -2.161  -25.858 -3.749  1.00 37.29 ? 130 PHE A CB    1 
ATOM   975  C CG    . PHE A 1 136 ? -2.381  -24.485 -4.341  1.00 38.21 ? 130 PHE A CG    1 
ATOM   976  C CD1   . PHE A 1 136 ? -1.313  -23.626 -4.550  1.00 38.73 ? 130 PHE A CD1   1 
ATOM   977  C CD2   . PHE A 1 136 ? -3.655  -24.052 -4.667  1.00 41.68 ? 130 PHE A CD2   1 
ATOM   978  C CE1   . PHE A 1 136 ? -1.508  -22.359 -5.084  1.00 36.46 ? 130 PHE A CE1   1 
ATOM   979  C CE2   . PHE A 1 136 ? -3.864  -22.782 -5.196  1.00 37.74 ? 130 PHE A CE2   1 
ATOM   980  C CZ    . PHE A 1 136 ? -2.788  -21.938 -5.407  1.00 42.03 ? 130 PHE A CZ    1 
ATOM   981  N N     . ILE A 1 137 ? -1.748  -26.405 -7.054  1.00 28.16 ? 131 ILE A N     1 
ATOM   982  C CA    . ILE A 1 137 ? -0.898  -26.117 -8.204  1.00 24.20 ? 131 ILE A CA    1 
ATOM   983  C C     . ILE A 1 137 ? -1.184  -24.688 -8.647  1.00 29.24 ? 131 ILE A C     1 
ATOM   984  O O     . ILE A 1 137 ? -2.308  -24.365 -9.057  1.00 32.08 ? 131 ILE A O     1 
ATOM   985  C CB    . ILE A 1 137 ? -1.113  -27.123 -9.343  1.00 22.26 ? 131 ILE A CB    1 
ATOM   986  C CG1   . ILE A 1 137 ? -0.758  -28.531 -8.848  1.00 24.72 ? 131 ILE A CG1   1 
ATOM   987  C CG2   . ILE A 1 137 ? -0.251  -26.729 -10.556 1.00 23.58 ? 131 ILE A CG2   1 
ATOM   988  C CD1   . ILE A 1 137 ? -0.832  -29.625 -9.897  1.00 26.82 ? 131 ILE A CD1   1 
ATOM   989  N N     . GLU A 1 138 ? -0.168  -23.832 -8.537  1.00 28.30 ? 132 GLU A N     1 
ATOM   990  C CA    . GLU A 1 138 ? -0.263  -22.429 -8.916  1.00 30.56 ? 132 GLU A CA    1 
ATOM   991  C C     . GLU A 1 138 ? -0.774  -22.273 -10.347 1.00 31.78 ? 132 GLU A C     1 
ATOM   992  O O     . GLU A 1 138 ? -0.589  -23.149 -11.201 1.00 30.69 ? 132 GLU A O     1 
ATOM   993  C CB    . GLU A 1 138 ? 1.118   -21.774 -8.770  1.00 37.27 ? 132 GLU A CB    1 
ATOM   994  C CG    . GLU A 1 138 ? 1.201   -20.307 -9.151  1.00 44.43 ? 132 GLU A CG    1 
ATOM   995  C CD    . GLU A 1 138 ? 0.718   -19.381 -8.053  1.00 50.94 ? 132 GLU A CD    1 
ATOM   996  O OE1   . GLU A 1 138 ? 0.389   -19.873 -6.952  1.00 57.94 ? 132 GLU A OE1   1 
ATOM   997  O OE2   . GLU A 1 138 ? 0.678   -18.155 -8.290  1.00 56.84 ? 132 GLU A OE2   1 
ATOM   998  N N     . GLN A 1 139 ? -1.433  -21.142 -10.602 1.00 33.63 ? 133 GLN A N     1 
ATOM   999  C CA    . GLN A 1 139 ? -1.903  -20.819 -11.945 1.00 26.13 ? 133 GLN A CA    1 
ATOM   1000 C C     . GLN A 1 139 ? -0.789  -20.981 -12.969 1.00 26.75 ? 133 GLN A C     1 
ATOM   1001 O O     . GLN A 1 139 ? 0.327   -20.491 -12.775 1.00 24.95 ? 133 GLN A O     1 
ATOM   1002 C CB    . GLN A 1 139 ? -2.434  -19.383 -11.981 1.00 32.53 ? 133 GLN A CB    1 
ATOM   1003 C CG    . GLN A 1 139 ? -2.955  -18.960 -13.335 1.00 33.32 ? 133 GLN A CG    1 
ATOM   1004 C CD    . GLN A 1 139 ? -3.421  -17.527 -13.347 1.00 40.32 ? 133 GLN A CD    1 
ATOM   1005 O OE1   . GLN A 1 139 ? -3.050  -16.738 -12.483 1.00 45.56 ? 133 GLN A OE1   1 
ATOM   1006 N NE2   . GLN A 1 139 ? -4.248  -17.181 -14.327 1.00 46.56 ? 133 GLN A NE2   1 
ATOM   1007 N N     . GLY A 1 140 ? -1.109  -21.660 -14.070 1.00 25.89 ? 134 GLY A N     1 
ATOM   1008 C CA    . GLY A 1 140 ? -0.134  -21.887 -15.120 1.00 26.15 ? 134 GLY A CA    1 
ATOM   1009 C C     . GLY A 1 140 ? 1.010   -22.788 -14.718 1.00 30.24 ? 134 GLY A C     1 
ATOM   1010 O O     . GLY A 1 140 ? 1.996   -22.866 -15.450 1.00 30.30 ? 134 GLY A O     1 
ATOM   1011 N N     . ILE A 1 141 ? 0.887   -23.490 -13.586 1.00 25.15 ? 135 ILE A N     1 
ATOM   1012 C CA    . ILE A 1 141 ? 1.968   -24.264 -12.968 1.00 23.16 ? 135 ILE A CA    1 
ATOM   1013 C C     . ILE A 1 141 ? 3.219   -23.402 -12.841 1.00 24.27 ? 135 ILE A C     1 
ATOM   1014 O O     . ILE A 1 141 ? 4.348   -23.894 -12.975 1.00 23.03 ? 135 ILE A O     1 
ATOM   1015 C CB    . ILE A 1 141 ? 2.253   -25.562 -13.746 1.00 23.38 ? 135 ILE A CB    1 
ATOM   1016 C CG1   . ILE A 1 141 ? 0.959   -26.108 -14.350 1.00 29.99 ? 135 ILE A CG1   1 
ATOM   1017 C CG2   . ILE A 1 141 ? 2.886   -26.618 -12.819 1.00 25.41 ? 135 ILE A CG2   1 
ATOM   1018 C CD1   . ILE A 1 141 ? 1.125   -27.355 -15.166 1.00 29.17 ? 135 ILE A CD1   1 
ATOM   1019 N N     . ALA A 1 142 ? 3.024   -22.118 -12.545 1.00 22.43 ? 136 ALA A N     1 
ATOM   1020 C CA    . ALA A 1 142 ? 4.122   -21.163 -12.385 1.00 24.99 ? 136 ALA A CA    1 
ATOM   1021 C C     . ALA A 1 142 ? 4.662   -21.267 -10.958 1.00 25.32 ? 136 ALA A C     1 
ATOM   1022 O O     . ALA A 1 142 ? 4.458   -20.397 -10.105 1.00 29.68 ? 136 ALA A O     1 
ATOM   1023 C CB    . ALA A 1 142 ? 3.657   -19.749 -12.709 1.00 28.95 ? 136 ALA A CB    1 
ATOM   1024 N N     . ASN A 1 143 ? 5.345   -22.382 -10.700 1.00 24.75 ? 137 ASN A N     1 
ATOM   1025 C CA    . ASN A 1 143 ? 5.812   -22.674 -9.351  1.00 28.23 ? 137 ASN A CA    1 
ATOM   1026 C C     . ASN A 1 143 ? 7.183   -23.339 -9.426  1.00 23.62 ? 137 ASN A C     1 
ATOM   1027 O O     . ASN A 1 143 ? 7.706   -23.628 -10.509 1.00 23.52 ? 137 ASN A O     1 
ATOM   1028 C CB    . ASN A 1 143 ? 4.785   -23.536 -8.596  1.00 27.10 ? 137 ASN A CB    1 
ATOM   1029 C CG    . ASN A 1 143 ? 4.522   -24.883 -9.258  1.00 25.49 ? 137 ASN A CG    1 
ATOM   1030 O OD1   . ASN A 1 143 ? 5.320   -25.385 -10.053 1.00 22.40 ? 137 ASN A OD1   1 
ATOM   1031 N ND2   . ASN A 1 143 ? 3.387   -25.489 -8.910  1.00 27.71 ? 137 ASN A ND2   1 
ATOM   1032 N N     . LEU A 1 144 ? 7.755   -23.614 -8.252  1.00 24.67 ? 138 LEU A N     1 
ATOM   1033 C CA    . LEU A 1 144 ? 9.082   -24.220 -8.204  1.00 21.46 ? 138 LEU A CA    1 
ATOM   1034 C C     . LEU A 1 144 ? 9.073   -25.666 -8.699  1.00 23.30 ? 138 LEU A C     1 
ATOM   1035 O O     . LEU A 1 144 ? 10.092  -26.154 -9.200  1.00 23.17 ? 138 LEU A O     1 
ATOM   1036 C CB    . LEU A 1 144 ? 9.624   -24.142 -6.776  1.00 23.40 ? 138 LEU A CB    1 
ATOM   1037 C CG    . LEU A 1 144 ? 9.915   -22.731 -6.262  1.00 25.62 ? 138 LEU A CG    1 
ATOM   1038 C CD1   . LEU A 1 144 ? 10.493  -22.797 -4.866  1.00 31.42 ? 138 LEU A CD1   1 
ATOM   1039 C CD2   . LEU A 1 144 ? 10.837  -21.966 -7.203  1.00 25.27 ? 138 LEU A CD2   1 
ATOM   1040 N N     . GLU A 1 145 ? 7.946   -26.363 -8.558  1.00 23.98 ? 139 GLU A N     1 
ATOM   1041 C CA    . GLU A 1 145 ? 7.844   -27.742 -9.031  1.00 20.42 ? 139 GLU A CA    1 
ATOM   1042 C C     . GLU A 1 145 ? 8.026   -27.828 -10.542 1.00 21.46 ? 139 GLU A C     1 
ATOM   1043 O O     . GLU A 1 145 ? 8.500   -28.852 -11.062 1.00 19.94 ? 139 GLU A O     1 
ATOM   1044 C CB    . GLU A 1 145 ? 6.493   -28.329 -8.621  1.00 21.61 ? 139 GLU A CB    1 
ATOM   1045 C CG    . GLU A 1 145 ? 6.377   -28.662 -7.132  1.00 25.55 ? 139 GLU A CG    1 
ATOM   1046 C CD    . GLU A 1 145 ? 6.237   -27.434 -6.224  1.00 31.53 ? 139 GLU A CD    1 
ATOM   1047 O OE1   . GLU A 1 145 ? 6.492   -27.560 -4.995  1.00 36.83 ? 139 GLU A OE1   1 
ATOM   1048 O OE2   . GLU A 1 145 ? 5.844   -26.356 -6.712  1.00 27.32 ? 139 GLU A OE2   1 
ATOM   1049 N N     . ALA A 1 146 ? 7.675   -26.761 -11.256 1.00 21.04 ? 140 ALA A N     1 
ATOM   1050 C CA    . ALA A 1 146 ? 7.768   -26.766 -12.707 1.00 19.78 ? 140 ALA A CA    1 
ATOM   1051 C C     . ALA A 1 146 ? 9.203   -26.883 -13.194 1.00 19.78 ? 140 ALA A C     1 
ATOM   1052 O O     . ALA A 1 146 ? 9.422   -27.226 -14.361 1.00 19.88 ? 140 ALA A O     1 
ATOM   1053 C CB    . ALA A 1 146 ? 7.138   -25.495 -13.277 1.00 21.47 ? 140 ALA A CB    1 
ATOM   1054 N N     . GLN A 1 147 ? 10.189  -26.618 -12.332 1.00 19.97 ? 141 GLN A N     1 
ATOM   1055 C CA    . GLN A 1 147 ? 11.564  -26.605 -12.814 1.00 19.20 ? 141 GLN A CA    1 
ATOM   1056 C C     . GLN A 1 147 ? 12.089  -27.987 -13.151 1.00 19.58 ? 141 GLN A C     1 
ATOM   1057 O O     . GLN A 1 147 ? 13.055  -28.089 -13.916 1.00 19.17 ? 141 GLN A O     1 
ATOM   1058 C CB    . GLN A 1 147 ? 12.485  -25.957 -11.789 1.00 18.20 ? 141 GLN A CB    1 
ATOM   1059 C CG    . GLN A 1 147 ? 12.811  -26.788 -10.578 1.00 20.89 ? 141 GLN A CG    1 
ATOM   1060 C CD    . GLN A 1 147 ? 13.575  -25.970 -9.577  1.00 24.87 ? 141 GLN A CD    1 
ATOM   1061 O OE1   . GLN A 1 147 ? 14.763  -25.734 -9.754  1.00 22.80 ? 141 GLN A OE1   1 
ATOM   1062 N NE2   . GLN A 1 147 ? 12.895  -25.504 -8.529  1.00 22.59 ? 141 GLN A NE2   1 
ATOM   1063 N N     . TYR A 1 148 ? 11.503  -29.043 -12.585 1.00 19.20 ? 142 TYR A N     1 
ATOM   1064 C CA    . TYR A 1 148 ? 12.073  -30.370 -12.795 1.00 16.95 ? 142 TYR A CA    1 
ATOM   1065 C C     . TYR A 1 148 ? 11.914  -30.823 -14.238 1.00 19.09 ? 142 TYR A C     1 
ATOM   1066 O O     . TYR A 1 148 ? 12.827  -31.463 -14.791 1.00 17.62 ? 142 TYR A O     1 
ATOM   1067 C CB    . TYR A 1 148 ? 11.461  -31.342 -11.778 1.00 17.91 ? 142 TYR A CB    1 
ATOM   1068 C CG    . TYR A 1 148 ? 11.911  -30.881 -10.412 1.00 19.48 ? 142 TYR A CG    1 
ATOM   1069 C CD1   . TYR A 1 148 ? 13.240  -31.045 -10.024 1.00 21.67 ? 142 TYR A CD1   1 
ATOM   1070 C CD2   . TYR A 1 148 ? 11.063  -30.163 -9.568  1.00 22.95 ? 142 TYR A CD2   1 
ATOM   1071 C CE1   . TYR A 1 148 ? 13.702  -30.566 -8.813  1.00 26.93 ? 142 TYR A CE1   1 
ATOM   1072 C CE2   . TYR A 1 148 ? 11.522  -29.672 -8.333  1.00 24.74 ? 142 TYR A CE2   1 
ATOM   1073 C CZ    . TYR A 1 148 ? 12.851  -29.878 -7.975  1.00 26.74 ? 142 TYR A CZ    1 
ATOM   1074 O OH    . TYR A 1 148 ? 13.351  -29.419 -6.766  1.00 28.46 ? 142 TYR A OH    1 
ATOM   1075 N N     . GLY A 1 149 ? 10.804  -30.466 -14.885 1.00 17.20 ? 143 GLY A N     1 
ATOM   1076 C CA    . GLY A 1 149 ? 10.672  -30.780 -16.302 1.00 16.63 ? 143 GLY A CA    1 
ATOM   1077 C C     . GLY A 1 149 ? 11.649  -30.019 -17.172 1.00 16.45 ? 143 GLY A C     1 
ATOM   1078 O O     . GLY A 1 149 ? 12.012  -30.484 -18.259 1.00 16.43 ? 143 GLY A O     1 
ATOM   1079 N N     . TYR A 1 150 ? 12.085  -28.840 -16.719 1.00 16.58 ? 144 TYR A N     1 
ATOM   1080 C CA    . TYR A 1 150 ? 13.075  -28.094 -17.481 1.00 15.39 ? 144 TYR A CA    1 
ATOM   1081 C C     . TYR A 1 150 ? 14.492  -28.547 -17.173 1.00 16.80 ? 144 TYR A C     1 
ATOM   1082 O O     . TYR A 1 150 ? 15.357  -28.414 -18.041 1.00 16.89 ? 144 TYR A O     1 
ATOM   1083 C CB    . TYR A 1 150 ? 12.883  -26.581 -17.263 1.00 14.55 ? 144 TYR A CB    1 
ATOM   1084 C CG    . TYR A 1 150 ? 11.674  -26.195 -18.077 1.00 16.26 ? 144 TYR A CG    1 
ATOM   1085 C CD1   . TYR A 1 150 ? 11.803  -25.937 -19.429 1.00 16.46 ? 144 TYR A CD1   1 
ATOM   1086 C CD2   . TYR A 1 150 ? 10.393  -26.211 -17.519 1.00 18.72 ? 144 TYR A CD2   1 
ATOM   1087 C CE1   . TYR A 1 150 ? 10.690  -25.664 -20.222 1.00 16.18 ? 144 TYR A CE1   1 
ATOM   1088 C CE2   . TYR A 1 150 ? 9.278   -25.935 -18.289 1.00 16.56 ? 144 TYR A CE2   1 
ATOM   1089 C CZ    . TYR A 1 150 ? 9.443   -25.670 -19.648 1.00 15.58 ? 144 TYR A CZ    1 
ATOM   1090 O OH    . TYR A 1 150 ? 8.333   -25.422 -20.433 1.00 16.37 ? 144 TYR A OH    1 
ATOM   1091 N N     . MET A 1 151 ? 14.752  -29.088 -15.975 1.00 16.34 ? 145 MET A N     1 
ATOM   1092 C CA    . MET A 1 151 ? 15.983  -29.857 -15.786 1.00 17.36 ? 145 MET A CA    1 
ATOM   1093 C C     . MET A 1 151 ? 16.031  -31.024 -16.767 1.00 17.19 ? 145 MET A C     1 
ATOM   1094 O O     . MET A 1 151 ? 17.053  -31.262 -17.434 1.00 16.28 ? 145 MET A O     1 
ATOM   1095 C CB    . MET A 1 151 ? 16.081  -30.355 -14.341 1.00 17.35 ? 145 MET A CB    1 
ATOM   1096 C CG    . MET A 1 151 ? 17.418  -31.017 -14.016 1.00 19.38 ? 145 MET A CG    1 
ATOM   1097 S SD    . MET A 1 151 ? 17.384  -31.907 -12.457 1.00 20.66 ? 145 MET A SD    1 
ATOM   1098 C CE    . MET A 1 151 ? 17.072  -30.572 -11.315 1.00 20.85 ? 145 MET A CE    1 
ATOM   1099 N N     . GLU A 1 152 ? 14.914  -31.735 -16.906 1.00 15.67 ? 146 GLU A N     1 
ATOM   1100 C CA    . GLU A 1 152 ? 14.860  -32.833 -17.867 1.00 16.73 ? 146 GLU A CA    1 
ATOM   1101 C C     . GLU A 1 152 ? 15.078  -32.339 -19.296 1.00 15.82 ? 146 GLU A C     1 
ATOM   1102 O O     . GLU A 1 152 ? 15.841  -32.948 -20.066 1.00 15.64 ? 146 GLU A O     1 
ATOM   1103 C CB    . GLU A 1 152 ? 13.520  -33.558 -17.727 1.00 16.89 ? 146 GLU A CB    1 
ATOM   1104 C CG    . GLU A 1 152 ? 13.397  -34.841 -18.562 1.00 23.55 ? 146 GLU A CG    1 
ATOM   1105 C CD    . GLU A 1 152 ? 12.143  -35.629 -18.219 1.00 30.66 ? 146 GLU A CD    1 
ATOM   1106 O OE1   . GLU A 1 152 ? 12.038  -36.804 -18.658 1.00 31.70 ? 146 GLU A OE1   1 
ATOM   1107 O OE2   . GLU A 1 152 ? 11.282  -35.076 -17.489 1.00 22.61 ? 146 GLU A OE2   1 
ATOM   1108 N N     . LEU A 1 153 ? 14.412  -31.249 -19.680 1.00 14.86 ? 147 LEU A N     1 
ATOM   1109 C CA    . LEU A 1 153 ? 14.591  -30.702 -21.023 1.00 17.12 ? 147 LEU A CA    1 
ATOM   1110 C C     . LEU A 1 153 ? 16.040  -30.294 -21.257 1.00 15.44 ? 147 LEU A C     1 
ATOM   1111 O O     . LEU A 1 153 ? 16.607  -30.580 -22.324 1.00 15.04 ? 147 LEU A O     1 
ATOM   1112 C CB    . LEU A 1 153 ? 13.647  -29.511 -21.236 1.00 16.91 ? 147 LEU A CB    1 
ATOM   1113 C CG    . LEU A 1 153 ? 13.802  -28.748 -22.567 1.00 13.90 ? 147 LEU A CG    1 
ATOM   1114 C CD1   . LEU A 1 153 ? 13.663  -29.721 -23.757 1.00 15.72 ? 147 LEU A CD1   1 
ATOM   1115 C CD2   . LEU A 1 153 ? 12.796  -27.607 -22.664 1.00 15.90 ? 147 LEU A CD2   1 
ATOM   1116 N N     . ALA A 1 154 ? 16.664  -29.639 -20.264 1.00 15.47 ? 148 ALA A N     1 
ATOM   1117 C CA    . ALA A 1 154 ? 18.076  -29.288 -20.390 1.00 12.60 ? 148 ALA A CA    1 
ATOM   1118 C C     . ALA A 1 154 ? 18.928  -30.533 -20.589 1.00 15.79 ? 148 ALA A C     1 
ATOM   1119 O O     . ALA A 1 154 ? 19.878  -30.524 -21.381 1.00 17.44 ? 148 ALA A O     1 
ATOM   1120 C CB    . ALA A 1 154 ? 18.553  -28.507 -19.152 1.00 15.09 ? 148 ALA A CB    1 
ATOM   1121 N N     . GLN A 1 155 ? 18.614  -31.614 -19.871 1.00 13.97 ? 149 GLN A N     1 
ATOM   1122 C CA    . GLN A 1 155 ? 19.404  -32.836 -20.012 1.00 16.65 ? 149 GLN A CA    1 
ATOM   1123 C C     . GLN A 1 155 ? 19.217  -33.467 -21.388 1.00 15.72 ? 149 GLN A C     1 
ATOM   1124 O O     . GLN A 1 155 ? 20.185  -33.946 -21.990 1.00 15.85 ? 149 GLN A O     1 
ATOM   1125 C CB    . GLN A 1 155 ? 19.050  -33.822 -18.896 1.00 14.80 ? 149 GLN A CB    1 
ATOM   1126 C CG    . GLN A 1 155 ? 19.521  -33.239 -17.550 1.00 17.09 ? 149 GLN A CG    1 
ATOM   1127 C CD    . GLN A 1 155 ? 19.288  -34.131 -16.363 1.00 22.79 ? 149 GLN A CD    1 
ATOM   1128 O OE1   . GLN A 1 155 ? 18.815  -35.267 -16.487 1.00 28.14 ? 149 GLN A OE1   1 
ATOM   1129 N NE2   . GLN A 1 155 ? 19.638  -33.624 -15.185 1.00 19.17 ? 149 GLN A NE2   1 
ATOM   1130 N N     . GLU A 1 156 ? 17.990  -33.469 -21.908 1.00 14.49 ? 150 GLU A N     1 
ATOM   1131 C CA    . GLU A 1 156 ? 17.775  -33.942 -23.278 1.00 13.18 ? 150 GLU A CA    1 
ATOM   1132 C C     . GLU A 1 156 ? 18.583  -33.123 -24.287 1.00 15.31 ? 150 GLU A C     1 
ATOM   1133 O O     . GLU A 1 156 ? 19.218  -33.681 -25.199 1.00 15.82 ? 150 GLU A O     1 
ATOM   1134 C CB    . GLU A 1 156 ? 16.286  -33.858 -23.637 1.00 16.52 ? 150 GLU A CB    1 
ATOM   1135 C CG    . GLU A 1 156 ? 15.426  -34.865 -22.871 1.00 18.21 ? 150 GLU A CG    1 
ATOM   1136 C CD    . GLU A 1 156 ? 13.953  -34.728 -23.186 1.00 20.94 ? 150 GLU A CD    1 
ATOM   1137 O OE1   . GLU A 1 156 ? 13.113  -35.219 -22.395 1.00 17.50 ? 150 GLU A OE1   1 
ATOM   1138 O OE2   . GLU A 1 156 ? 13.628  -34.151 -24.245 1.00 16.29 ? 150 GLU A OE2   1 
ATOM   1139 N N     . ILE A 1 157 ? 18.531  -31.793 -24.162 1.00 15.31 ? 151 ILE A N     1 
ATOM   1140 C CA    . ILE A 1 157 ? 19.250  -30.935 -25.102 1.00 16.77 ? 151 ILE A CA    1 
ATOM   1141 C C     . ILE A 1 157 ? 20.749  -31.156 -24.967 1.00 17.38 ? 151 ILE A C     1 
ATOM   1142 O O     . ILE A 1 157 ? 21.485  -31.124 -25.963 1.00 16.56 ? 151 ILE A O     1 
ATOM   1143 C CB    . ILE A 1 157 ? 18.866  -29.461 -24.872 1.00 15.84 ? 151 ILE A CB    1 
ATOM   1144 C CG1   . ILE A 1 157 ? 17.404  -29.235 -25.252 1.00 13.42 ? 151 ILE A CG1   1 
ATOM   1145 C CG2   . ILE A 1 157 ? 19.769  -28.525 -25.687 1.00 17.26 ? 151 ILE A CG2   1 
ATOM   1146 C CD1   . ILE A 1 157 ? 16.901  -27.863 -24.825 1.00 16.57 ? 151 ILE A CD1   1 
ATOM   1147 N N     . GLN A 1 158 ? 21.224  -31.421 -23.749 1.00 14.56 ? 152 GLN A N     1 
ATOM   1148 C CA    . GLN A 1 158 ? 22.642  -31.713 -23.569 1.00 15.63 ? 152 GLN A CA    1 
ATOM   1149 C C     . GLN A 1 158 ? 23.041  -32.945 -24.368 1.00 17.08 ? 152 GLN A C     1 
ATOM   1150 O O     . GLN A 1 158 ? 24.058  -32.939 -25.078 1.00 17.60 ? 152 GLN A O     1 
ATOM   1151 C CB    . GLN A 1 158 ? 22.946  -31.898 -22.081 1.00 14.91 ? 152 GLN A CB    1 
ATOM   1152 C CG    . GLN A 1 158 ? 24.393  -32.280 -21.798 1.00 17.82 ? 152 GLN A CG    1 
ATOM   1153 C CD    . GLN A 1 158 ? 24.723  -32.127 -20.337 1.00 17.78 ? 152 GLN A CD    1 
ATOM   1154 O OE1   . GLN A 1 158 ? 24.278  -32.924 -19.510 1.00 20.89 ? 152 GLN A OE1   1 
ATOM   1155 N NE2   . GLN A 1 158 ? 25.481  -31.088 -20.001 1.00 18.91 ? 152 GLN A NE2   1 
ATOM   1156 N N     . MET A 1 159 ? 22.237  -34.010 -24.287 1.00 16.01 ? 153 MET A N     1 
ATOM   1157 C CA    . MET A 1 159 ? 22.541  -35.216 -25.052 1.00 15.77 ? 153 MET A CA    1 
ATOM   1158 C C     . MET A 1 159 ? 22.437  -34.957 -26.553 1.00 16.93 ? 153 MET A C     1 
ATOM   1159 O O     . MET A 1 159 ? 23.306  -35.382 -27.318 1.00 17.92 ? 153 MET A O     1 
ATOM   1160 C CB    . MET A 1 159 ? 21.604  -36.354 -24.659 1.00 17.79 ? 153 MET A CB    1 
ATOM   1161 C CG    . MET A 1 159 ? 21.484  -36.630 -23.183 1.00 35.74 ? 153 MET A CG    1 
ATOM   1162 S SD    . MET A 1 159 ? 20.105  -37.767 -22.881 1.00 52.59 ? 153 MET A SD    1 
ATOM   1163 C CE    . MET A 1 159 ? 19.334  -37.022 -21.449 1.00 52.97 ? 153 MET A CE    1 
ATOM   1164 N N     . GLN A 1 160 ? 21.385  -34.254 -26.987 1.00 15.08 ? 154 GLN A N     1 
ATOM   1165 C CA    . GLN A 1 160 ? 21.147  -34.099 -28.425 1.00 16.68 ? 154 GLN A CA    1 
ATOM   1166 C C     . GLN A 1 160 ? 22.155  -33.154 -29.065 1.00 17.69 ? 154 GLN A C     1 
ATOM   1167 O O     . GLN A 1 160 ? 22.588  -33.374 -30.211 1.00 17.78 ? 154 GLN A O     1 
ATOM   1168 C CB    . GLN A 1 160 ? 19.721  -33.613 -28.658 1.00 15.93 ? 154 GLN A CB    1 
ATOM   1169 C CG    . GLN A 1 160 ? 18.703  -34.708 -28.351 1.00 17.43 ? 154 GLN A CG    1 
ATOM   1170 C CD    . GLN A 1 160 ? 17.274  -34.221 -28.427 1.00 17.91 ? 154 GLN A CD    1 
ATOM   1171 O OE1   . GLN A 1 160 ? 16.908  -33.268 -27.746 1.00 17.54 ? 154 GLN A OE1   1 
ATOM   1172 N NE2   . GLN A 1 160 ? 16.456  -34.884 -29.244 1.00 20.51 ? 154 GLN A NE2   1 
ATOM   1173 N N     . SER A 1 161 ? 22.503  -32.079 -28.366 1.00 15.32 ? 155 SER A N     1 
ATOM   1174 C CA    A SER A 1 161 ? 23.545  -31.174 -28.848 0.50 17.39 ? 155 SER A CA    1 
ATOM   1175 C CA    B SER A 1 161 ? 23.538  -31.179 -28.863 0.50 17.17 ? 155 SER A CA    1 
ATOM   1176 C C     . SER A 1 161 ? 24.852  -31.921 -29.078 1.00 20.20 ? 155 SER A C     1 
ATOM   1177 O O     . SER A 1 161 ? 25.519  -31.737 -30.104 1.00 20.67 ? 155 SER A O     1 
ATOM   1178 C CB    A SER A 1 161 ? 23.760  -30.033 -27.849 0.50 20.46 ? 155 SER A CB    1 
ATOM   1179 C CB    B SER A 1 161 ? 23.721  -30.017 -27.886 0.50 20.77 ? 155 SER A CB    1 
ATOM   1180 O OG    A SER A 1 161 ? 24.980  -29.357 -28.124 0.50 19.29 ? 155 SER A OG    1 
ATOM   1181 O OG    B SER A 1 161 ? 22.482  -29.379 -27.652 0.50 21.88 ? 155 SER A OG    1 
ATOM   1182 N N     . GLN A 1 162 ? 25.239  -32.772 -28.121 1.00 17.37 ? 156 GLN A N     1 
ATOM   1183 C CA    . GLN A 1 162 ? 26.484  -33.519 -28.266 1.00 16.97 ? 156 GLN A CA    1 
ATOM   1184 C C     . GLN A 1 162 ? 26.408  -34.495 -29.439 1.00 17.84 ? 156 GLN A C     1 
ATOM   1185 O O     . GLN A 1 162 ? 27.405  -34.702 -30.156 1.00 19.66 ? 156 GLN A O     1 
ATOM   1186 C CB    . GLN A 1 162 ? 26.792  -34.253 -26.950 1.00 19.05 ? 156 GLN A CB    1 
ATOM   1187 C CG    . GLN A 1 162 ? 27.961  -35.240 -27.023 1.00 17.96 ? 156 GLN A CG    1 
ATOM   1188 C CD    . GLN A 1 162 ? 29.266  -34.610 -27.514 1.00 21.54 ? 156 GLN A CD    1 
ATOM   1189 O OE1   . GLN A 1 162 ? 29.473  -33.396 -27.395 1.00 22.56 ? 156 GLN A OE1   1 
ATOM   1190 N NE2   . GLN A 1 162 ? 30.157  -35.439 -28.053 1.00 21.53 ? 156 GLN A NE2   1 
ATOM   1191 N N     . SER A 1 163 ? 25.233  -35.101 -29.653 1.00 16.94 ? 157 SER A N     1 
ATOM   1192 C CA    A SER A 1 163 ? 25.081  -36.069 -30.739 0.50 19.79 ? 157 SER A CA    1 
ATOM   1193 C CA    B SER A 1 163 ? 25.096  -36.070 -30.738 0.50 19.84 ? 157 SER A CA    1 
ATOM   1194 C C     . SER A 1 163 ? 25.232  -35.406 -32.100 1.00 21.12 ? 157 SER A C     1 
ATOM   1195 O O     . SER A 1 163 ? 25.645  -36.060 -33.066 1.00 19.00 ? 157 SER A O     1 
ATOM   1196 C CB    A SER A 1 163 ? 23.723  -36.768 -30.648 0.50 20.95 ? 157 SER A CB    1 
ATOM   1197 C CB    B SER A 1 163 ? 23.751  -36.784 -30.650 0.50 21.19 ? 157 SER A CB    1 
ATOM   1198 O OG    A SER A 1 163 ? 23.656  -37.620 -29.515 0.50 16.74 ? 157 SER A OG    1 
ATOM   1199 O OG    B SER A 1 163 ? 22.714  -35.908 -31.037 0.50 22.75 ? 157 SER A OG    1 
ATOM   1200 N N     . LEU A 1 164 ? 24.883  -34.122 -32.191 1.00 18.00 ? 158 LEU A N     1 
ATOM   1201 C CA    . LEU A 1 164 ? 25.019  -33.321 -33.401 1.00 16.30 ? 158 LEU A CA    1 
ATOM   1202 C C     . LEU A 1 164 ? 26.312  -32.518 -33.441 1.00 25.41 ? 158 LEU A C     1 
ATOM   1203 O O     . LEU A 1 164 ? 26.609  -31.906 -34.476 1.00 26.00 ? 158 LEU A O     1 
ATOM   1204 C CB    . LEU A 1 164 ? 23.837  -32.350 -33.515 1.00 18.72 ? 158 LEU A CB    1 
ATOM   1205 C CG    . LEU A 1 164 ? 22.469  -32.987 -33.787 1.00 20.53 ? 158 LEU A CG    1 
ATOM   1206 C CD1   . LEU A 1 164 ? 21.359  -32.011 -33.479 1.00 22.88 ? 158 LEU A CD1   1 
ATOM   1207 C CD2   . LEU A 1 164 ? 22.366  -33.467 -35.235 1.00 19.83 ? 158 LEU A CD2   1 
ATOM   1208 N N     . LYS A 1 165 ? 27.058  -32.484 -32.335 1.00 23.08 ? 159 LYS A N     1 
ATOM   1209 C CA    . LYS A 1 165 ? 28.224  -31.611 -32.178 1.00 21.08 ? 159 LYS A CA    1 
ATOM   1210 C C     . LYS A 1 165 ? 27.896  -30.168 -32.558 1.00 25.16 ? 159 LYS A C     1 
ATOM   1211 O O     . LYS A 1 165 ? 28.625  -29.507 -33.304 1.00 27.91 ? 159 LYS A O     1 
ATOM   1212 C CB    . LYS A 1 165 ? 29.421  -32.158 -32.967 1.00 24.04 ? 159 LYS A CB    1 
ATOM   1213 C CG    . LYS A 1 165 ? 30.030  -33.395 -32.304 1.00 26.71 ? 159 LYS A CG    1 
ATOM   1214 C CD    . LYS A 1 165 ? 31.119  -34.032 -33.168 1.00 39.05 ? 159 LYS A CD    1 
ATOM   1215 N N     . LEU A 1 166 ? 26.773  -29.675 -32.030 1.00 21.33 ? 160 LEU A N     1 
ATOM   1216 C CA    . LEU A 1 166 ? 26.332  -28.301 -32.230 1.00 22.64 ? 160 LEU A CA    1 
ATOM   1217 C C     . LEU A 1 166 ? 26.219  -27.607 -30.880 1.00 27.05 ? 160 LEU A C     1 
ATOM   1218 O O     . LEU A 1 166 ? 25.647  -28.161 -29.936 1.00 34.54 ? 160 LEU A O     1 
ATOM   1219 C CB    . LEU A 1 166 ? 24.976  -28.225 -32.948 1.00 24.95 ? 160 LEU A CB    1 
ATOM   1220 C CG    . LEU A 1 166 ? 24.830  -28.746 -34.375 1.00 34.00 ? 160 LEU A CG    1 
ATOM   1221 C CD1   . LEU A 1 166 ? 23.355  -28.740 -34.772 1.00 34.36 ? 160 LEU A CD1   1 
ATOM   1222 C CD2   . LEU A 1 166 ? 25.656  -27.909 -35.334 1.00 31.05 ? 160 LEU A CD2   1 
ATOM   1223 N N     . ASP A 1 167 ? 26.755  -26.399 -30.804 1.00 23.74 ? 161 ASP A N     1 
ATOM   1224 C CA    . ASP A 1 167 ? 26.728  -25.552 -29.613 1.00 26.97 ? 161 ASP A CA    1 
ATOM   1225 C C     . ASP A 1 167 ? 25.589  -24.542 -29.789 1.00 27.68 ? 161 ASP A C     1 
ATOM   1226 O O     . ASP A 1 167 ? 25.781  -23.492 -30.403 1.00 27.47 ? 161 ASP A O     1 
ATOM   1227 C CB    . ASP A 1 167 ? 28.095  -24.879 -29.477 1.00 34.99 ? 161 ASP A CB    1 
ATOM   1228 C CG    . ASP A 1 167 ? 28.186  -23.911 -28.315 1.00 43.39 ? 161 ASP A CG    1 
ATOM   1229 O OD1   . ASP A 1 167 ? 27.418  -24.050 -27.347 1.00 40.07 ? 161 ASP A OD1   1 
ATOM   1230 O OD2   . ASP A 1 167 ? 29.050  -23.003 -28.385 1.00 41.69 ? 161 ASP A OD2   1 
ATOM   1231 N N     . PHE A 1 168 ? 24.434  -24.849 -29.237 1.00 20.38 ? 162 PHE A N     1 
ATOM   1232 C CA    . PHE A 1 168 ? 23.280  -24.010 -29.572 1.00 17.50 ? 162 PHE A CA    1 
ATOM   1233 C C     . PHE A 1 168 ? 23.077  -22.802 -28.675 1.00 20.25 ? 162 PHE A C     1 
ATOM   1234 O O     . PHE A 1 168 ? 23.485  -22.791 -27.560 1.00 20.64 ? 162 PHE A O     1 
ATOM   1235 C CB    . PHE A 1 168 ? 22.014  -24.791 -29.254 1.00 19.35 ? 162 PHE A CB    1 
ATOM   1236 C CG    . PHE A 1 168 ? 21.712  -25.972 -30.132 1.00 20.62 ? 162 PHE A CG    1 
ATOM   1237 C CD1   . PHE A 1 168 ? 21.473  -25.802 -31.470 1.00 20.13 ? 162 PHE A CD1   1 
ATOM   1238 C CD2   . PHE A 1 168 ? 21.600  -27.235 -29.605 1.00 22.29 ? 162 PHE A CD2   1 
ATOM   1239 C CE1   . PHE A 1 168 ? 21.166  -26.866 -32.282 1.00 25.12 ? 162 PHE A CE1   1 
ATOM   1240 C CE2   . PHE A 1 168 ? 21.298  -28.303 -30.416 1.00 23.59 ? 162 PHE A CE2   1 
ATOM   1241 C CZ    . PHE A 1 168 ? 21.076  -28.104 -31.751 1.00 22.37 ? 162 PHE A CZ    1 
ATOM   1242 N N     . ASP A 1 169 ? 22.421  -21.829 -29.293 1.00 17.68 ? 163 ASP A N     1 
ATOM   1243 C CA    . ASP A 1 169 ? 21.705  -20.751 -28.582 1.00 18.78 ? 163 ASP A CA    1 
ATOM   1244 C C     . ASP A 1 169 ? 20.253  -21.262 -28.587 1.00 20.37 ? 163 ASP A C     1 
ATOM   1245 O O     . ASP A 1 169 ? 19.819  -21.741 -29.596 1.00 19.61 ? 163 ASP A O     1 
ATOM   1246 C CB    . ASP A 1 169 ? 21.778  -19.400 -29.280 1.00 18.16 ? 163 ASP A CB    1 
ATOM   1247 C CG    . ASP A 1 169 ? 23.071  -18.662 -29.041 1.00 23.33 ? 163 ASP A CG    1 
ATOM   1248 O OD1   . ASP A 1 169 ? 23.661  -18.862 -28.008 1.00 22.96 ? 163 ASP A OD1   1 
ATOM   1249 O OD2   . ASP A 1 169 ? 23.412  -17.875 -29.874 1.00 24.42 ? 163 ASP A OD2   1 
ATOM   1250 N N     . ILE A 1 170 ? 19.569  -21.152 -27.460 1.00 16.01 ? 164 ILE A N     1 
ATOM   1251 C CA    . ILE A 1 170 ? 18.212  -21.681 -27.298 1.00 17.09 ? 164 ILE A CA    1 
ATOM   1252 C C     . ILE A 1 170 ? 17.226  -20.527 -27.197 1.00 18.83 ? 164 ILE A C     1 
ATOM   1253 O O     . ILE A 1 170 ? 17.492  -19.540 -26.511 1.00 18.79 ? 164 ILE A O     1 
ATOM   1254 C CB    . ILE A 1 170 ? 18.097  -22.563 -26.041 1.00 18.08 ? 164 ILE A CB    1 
ATOM   1255 C CG1   . ILE A 1 170 ? 19.061  -23.741 -26.130 1.00 15.23 ? 164 ILE A CG1   1 
ATOM   1256 C CG2   . ILE A 1 170 ? 16.647  -23.003 -25.843 1.00 18.62 ? 164 ILE A CG2   1 
ATOM   1257 C CD1   . ILE A 1 170 ? 19.171  -24.528 -24.812 1.00 18.29 ? 164 ILE A CD1   1 
ATOM   1258 N N     . PHE A 1 171 ? 16.084  -20.645 -27.869 1.00 16.64 ? 165 PHE A N     1 
ATOM   1259 C CA    . PHE A 1 171 ? 15.050  -19.629 -27.743 1.00 15.41 ? 165 PHE A CA    1 
ATOM   1260 C C     . PHE A 1 171 ? 13.715  -20.270 -27.388 1.00 16.92 ? 165 PHE A C     1 
ATOM   1261 O O     . PHE A 1 171 ? 13.337  -21.301 -27.956 1.00 15.01 ? 165 PHE A O     1 
ATOM   1262 C CB    . PHE A 1 171 ? 14.880  -18.791 -29.035 1.00 16.71 ? 165 PHE A CB    1 
ATOM   1263 C CG    . PHE A 1 171 ? 13.880  -17.672 -28.879 1.00 17.86 ? 165 PHE A CG    1 
ATOM   1264 C CD1   . PHE A 1 171 ? 12.506  -17.924 -28.974 1.00 19.06 ? 165 PHE A CD1   1 
ATOM   1265 C CD2   . PHE A 1 171 ? 14.298  -16.393 -28.566 1.00 21.94 ? 165 PHE A CD2   1 
ATOM   1266 C CE1   . PHE A 1 171 ? 11.587  -16.915 -28.795 1.00 19.63 ? 165 PHE A CE1   1 
ATOM   1267 C CE2   . PHE A 1 171 ? 13.370  -15.369 -28.395 1.00 22.51 ? 165 PHE A CE2   1 
ATOM   1268 C CZ    . PHE A 1 171 ? 12.019  -15.640 -28.500 1.00 20.42 ? 165 PHE A CZ    1 
ATOM   1269 N N     . LEU A 1 172 ? 12.999  -19.651 -26.443 1.00 14.88 ? 166 LEU A N     1 
ATOM   1270 C CA    . LEU A 1 172 ? 11.604  -19.991 -26.190 1.00 15.39 ? 166 LEU A CA    1 
ATOM   1271 C C     . LEU A 1 172 ? 10.890  -18.742 -25.697 1.00 18.85 ? 166 LEU A C     1 
ATOM   1272 O O     . LEU A 1 172 ? 11.503  -17.918 -25.009 1.00 17.39 ? 166 LEU A O     1 
ATOM   1273 C CB    . LEU A 1 172 ? 11.469  -21.133 -25.165 1.00 15.18 ? 166 LEU A CB    1 
ATOM   1274 C CG    . LEU A 1 172 ? 11.752  -20.895 -23.680 1.00 18.79 ? 166 LEU A CG    1 
ATOM   1275 C CD1   . LEU A 1 172 ? 11.370  -22.168 -22.928 1.00 17.48 ? 166 LEU A CD1   1 
ATOM   1276 C CD2   . LEU A 1 172 ? 13.210  -20.582 -23.479 1.00 18.86 ? 166 LEU A CD2   1 
ATOM   1277 N N     . PRO A 1 173 ? 9.615   -18.561 -26.052 1.00 15.64 ? 167 PRO A N     1 
ATOM   1278 C CA    . PRO A 1 173 ? 8.878   -17.352 -25.661 1.00 17.09 ? 167 PRO A CA    1 
ATOM   1279 C C     . PRO A 1 173 ? 8.327   -17.464 -24.249 1.00 17.14 ? 167 PRO A C     1 
ATOM   1280 O O     . PRO A 1 173 ? 8.100   -18.561 -23.733 1.00 18.54 ? 167 PRO A O     1 
ATOM   1281 C CB    . PRO A 1 173 ? 7.734   -17.300 -26.680 1.00 17.34 ? 167 PRO A CB    1 
ATOM   1282 C CG    . PRO A 1 173 ? 7.435   -18.791 -26.941 1.00 18.78 ? 167 PRO A CG    1 
ATOM   1283 C CD    . PRO A 1 173 ? 8.814   -19.467 -26.899 1.00 17.79 ? 167 PRO A CD    1 
ATOM   1284 N N     . SER A 1 174 ? 8.088   -16.299 -23.629 1.00 14.96 ? 168 SER A N     1 
ATOM   1285 C CA    . SER A 1 174 ? 7.641   -16.261 -22.237 1.00 18.12 ? 168 SER A CA    1 
ATOM   1286 C C     . SER A 1 174 ? 6.275   -15.610 -22.068 1.00 20.92 ? 168 SER A C     1 
ATOM   1287 O O     . SER A 1 174 ? 5.916   -14.665 -22.775 1.00 19.04 ? 168 SER A O     1 
ATOM   1288 C CB    . SER A 1 174 ? 8.629   -15.502 -21.331 1.00 18.23 ? 168 SER A CB    1 
ATOM   1289 O OG    . SER A 1 174 ? 9.789   -16.294 -21.097 1.00 18.62 ? 168 SER A OG    1 
ATOM   1290 N N     . GLY A 1 175 ? 5.529   -16.141 -21.103 1.00 17.50 ? 169 GLY A N     1 
ATOM   1291 C CA    . GLY A 1 175 ? 4.383   -15.480 -20.493 1.00 17.50 ? 169 GLY A CA    1 
ATOM   1292 C C     . GLY A 1 175 ? 4.797   -15.011 -19.109 1.00 19.17 ? 169 GLY A C     1 
ATOM   1293 O O     . GLY A 1 175 ? 5.135   -13.834 -18.926 1.00 20.40 ? 169 GLY A O     1 
ATOM   1294 N N     . THR A 1 176 ? 4.816   -15.934 -18.135 1.00 21.17 ? 170 THR A N     1 
ATOM   1295 C CA    . THR A 1 176 ? 5.315   -15.647 -16.794 1.00 22.02 ? 170 THR A CA    1 
ATOM   1296 C C     . THR A 1 176 ? 6.831   -15.719 -16.700 1.00 21.00 ? 170 THR A C     1 
ATOM   1297 O O     . THR A 1 176 ? 7.401   -15.206 -15.727 1.00 22.22 ? 170 THR A O     1 
ATOM   1298 C CB    . THR A 1 176 ? 4.741   -16.632 -15.768 1.00 19.67 ? 170 THR A CB    1 
ATOM   1299 O OG1   . THR A 1 176 ? 5.320   -17.932 -15.972 1.00 19.55 ? 170 THR A OG1   1 
ATOM   1300 C CG2   . THR A 1 176 ? 3.223   -16.707 -15.870 1.00 23.07 ? 170 THR A CG2   1 
ATOM   1301 N N     . GLY A 1 177 ? 7.482   -16.356 -17.674 1.00 16.80 ? 171 GLY A N     1 
ATOM   1302 C CA    . GLY A 1 177 ? 8.919   -16.550 -17.669 1.00 18.09 ? 171 GLY A CA    1 
ATOM   1303 C C     . GLY A 1 177 ? 9.383   -17.764 -16.905 1.00 18.30 ? 171 GLY A C     1 
ATOM   1304 O O     . GLY A 1 177 ? 10.594  -18.008 -16.845 1.00 19.93 ? 171 GLY A O     1 
ATOM   1305 N N     . THR A 1 178 ? 8.457   -18.538 -16.337 1.00 19.26 ? 172 THR A N     1 
ATOM   1306 C CA    . THR A 1 178 ? 8.831   -19.689 -15.517 1.00 18.13 ? 172 THR A CA    1 
ATOM   1307 C C     . THR A 1 178 ? 9.649   -20.695 -16.317 1.00 17.23 ? 172 THR A C     1 
ATOM   1308 O O     . THR A 1 178 ? 10.749  -21.091 -15.909 1.00 17.07 ? 172 THR A O     1 
ATOM   1309 C CB    . THR A 1 178 ? 7.564   -20.341 -14.963 1.00 20.57 ? 172 THR A CB    1 
ATOM   1310 O OG1   . THR A 1 178 ? 6.854   -19.377 -14.161 1.00 19.00 ? 172 THR A OG1   1 
ATOM   1311 C CG2   . THR A 1 178 ? 7.919   -21.565 -14.138 1.00 18.92 ? 172 THR A CG2   1 
ATOM   1312 N N     . SER A 1 179 ? 9.133   -21.096 -17.477 1.00 17.07 ? 173 SER A N     1 
ATOM   1313 C CA    . SER A 1 179 ? 9.806   -22.101 -18.292 1.00 15.52 ? 173 SER A CA    1 
ATOM   1314 C C     . SER A 1 179 ? 11.184  -21.631 -18.738 1.00 18.80 ? 173 SER A C     1 
ATOM   1315 O O     . SER A 1 179 ? 12.170  -22.369 -18.629 1.00 19.58 ? 173 SER A O     1 
ATOM   1316 C CB    . SER A 1 179 ? 8.926   -22.435 -19.497 1.00 17.56 ? 173 SER A CB    1 
ATOM   1317 O OG    . SER A 1 179 ? 7.788   -23.155 -19.047 1.00 17.95 ? 173 SER A OG    1 
ATOM   1318 N N     . ALA A 1 180 ? 11.275  -20.399 -19.249 1.00 15.66 ? 174 ALA A N     1 
ATOM   1319 C CA    . ALA A 1 180 ? 12.565  -19.901 -19.712 1.00 16.42 ? 174 ALA A CA    1 
ATOM   1320 C C     . ALA A 1 180 ? 13.550  -19.764 -18.559 1.00 17.46 ? 174 ALA A C     1 
ATOM   1321 O O     . ALA A 1 180 ? 14.732  -20.112 -18.696 1.00 20.00 ? 174 ALA A O     1 
ATOM   1322 C CB    . ALA A 1 180 ? 12.385  -18.555 -20.427 1.00 15.70 ? 174 ALA A CB    1 
ATOM   1323 N N     . ALA A 1 181 ? 13.087  -19.251 -17.414 1.00 19.84 ? 175 ALA A N     1 
ATOM   1324 C CA    . ALA A 1 181 ? 13.974  -19.107 -16.270 1.00 18.75 ? 175 ALA A CA    1 
ATOM   1325 C C     . ALA A 1 181 ? 14.568  -20.449 -15.861 1.00 17.56 ? 175 ALA A C     1 
ATOM   1326 O O     . ALA A 1 181 ? 15.771  -20.541 -15.584 1.00 20.98 ? 175 ALA A O     1 
ATOM   1327 C CB    . ALA A 1 181 ? 13.232  -18.471 -15.090 1.00 16.82 ? 175 ALA A CB    1 
ATOM   1328 N N     . PHE A 1 182 ? 13.750  -21.508 -15.836 1.00 19.52 ? 176 PHE A N     1 
ATOM   1329 C CA    . PHE A 1 182 ? 14.278  -22.786 -15.370 1.00 18.36 ? 176 PHE A CA    1 
ATOM   1330 C C     . PHE A 1 182 ? 15.100  -23.483 -16.439 1.00 17.05 ? 176 PHE A C     1 
ATOM   1331 O O     . PHE A 1 182 ? 16.033  -24.223 -16.108 1.00 18.12 ? 176 PHE A O     1 
ATOM   1332 C CB    . PHE A 1 182 ? 13.145  -23.684 -14.878 1.00 18.88 ? 176 PHE A CB    1 
ATOM   1333 C CG    . PHE A 1 182 ? 12.538  -23.211 -13.593 1.00 16.71 ? 176 PHE A CG    1 
ATOM   1334 C CD1   . PHE A 1 182 ? 13.350  -22.771 -12.554 1.00 18.44 ? 176 PHE A CD1   1 
ATOM   1335 C CD2   . PHE A 1 182 ? 11.159  -23.209 -13.412 1.00 17.92 ? 176 PHE A CD2   1 
ATOM   1336 C CE1   . PHE A 1 182 ? 12.795  -22.329 -11.355 1.00 19.45 ? 176 PHE A CE1   1 
ATOM   1337 C CE2   . PHE A 1 182 ? 10.607  -22.783 -12.214 1.00 22.57 ? 176 PHE A CE2   1 
ATOM   1338 C CZ    . PHE A 1 182 ? 11.419  -22.339 -11.191 1.00 23.84 ? 176 PHE A CZ    1 
ATOM   1339 N N     . LEU A 1 183 ? 14.785  -23.277 -17.719 1.00 16.30 ? 177 LEU A N     1 
ATOM   1340 C CA    . LEU A 1 183 ? 15.666  -23.849 -18.733 1.00 16.33 ? 177 LEU A CA    1 
ATOM   1341 C C     . LEU A 1 183 ? 17.048  -23.207 -18.663 1.00 18.20 ? 177 LEU A C     1 
ATOM   1342 O O     . LEU A 1 183 ? 18.069  -23.907 -18.747 1.00 18.41 ? 177 LEU A O     1 
ATOM   1343 C CB    . LEU A 1 183 ? 15.053  -23.703 -20.132 1.00 15.89 ? 177 LEU A CB    1 
ATOM   1344 C CG    . LEU A 1 183 ? 15.852  -24.443 -21.220 1.00 14.43 ? 177 LEU A CG    1 
ATOM   1345 C CD1   . LEU A 1 183 ? 16.042  -25.938 -20.907 1.00 15.81 ? 177 LEU A CD1   1 
ATOM   1346 C CD2   . LEU A 1 183 ? 15.178  -24.248 -22.574 1.00 17.87 ? 177 LEU A CD2   1 
ATOM   1347 N N     . ALA A 1 184 ? 17.100  -21.878 -18.481 1.00 16.84 ? 178 ALA A N     1 
ATOM   1348 C CA    . ALA A 1 184 ? 18.381  -21.190 -18.346 1.00 17.68 ? 178 ALA A CA    1 
ATOM   1349 C C     . ALA A 1 184 ? 19.110  -21.612 -17.078 1.00 19.21 ? 178 ALA A C     1 
ATOM   1350 O O     . ALA A 1 184 ? 20.349  -21.637 -17.053 1.00 19.33 ? 178 ALA A O     1 
ATOM   1351 C CB    . ALA A 1 184 ? 18.178  -19.665 -18.346 1.00 17.26 ? 178 ALA A CB    1 
ATOM   1352 N N     . LYS A 1 185 ? 18.362  -21.947 -16.023 1.00 16.08 ? 179 LYS A N     1 
ATOM   1353 C CA    . LYS A 1 185 ? 18.990  -22.421 -14.789 1.00 16.07 ? 179 LYS A CA    1 
ATOM   1354 C C     . LYS A 1 185 ? 19.783  -23.704 -15.020 1.00 17.62 ? 179 LYS A C     1 
ATOM   1355 O O     . LYS A 1 185 ? 20.870  -23.880 -14.450 1.00 19.79 ? 179 LYS A O     1 
ATOM   1356 C CB    . LYS A 1 185 ? 17.918  -22.625 -13.715 1.00 17.96 ? 179 LYS A CB    1 
ATOM   1357 C CG    . LYS A 1 185 ? 18.434  -23.131 -12.359 1.00 18.26 ? 179 LYS A CG    1 
ATOM   1358 C CD    . LYS A 1 185 ? 17.285  -23.266 -11.352 1.00 19.34 ? 179 LYS A CD    1 
ATOM   1359 C CE    . LYS A 1 185 ? 17.791  -23.773 -10.023 1.00 22.86 ? 179 LYS A CE    1 
ATOM   1360 N NZ    . LYS A 1 185 ? 16.705  -23.714 -8.980  1.00 24.16 ? 179 LYS A NZ    1 
ATOM   1361 N N     . TYR A 1 186 ? 19.273  -24.608 -15.855 1.00 16.22 ? 180 TYR A N     1 
ATOM   1362 C CA    . TYR A 1 186 ? 19.887  -25.930 -15.962 1.00 16.57 ? 180 TYR A CA    1 
ATOM   1363 C C     . TYR A 1 186 ? 20.677  -26.168 -17.244 1.00 17.02 ? 180 TYR A C     1 
ATOM   1364 O O     . TYR A 1 186 ? 21.503  -27.082 -17.263 1.00 18.44 ? 180 TYR A O     1 
ATOM   1365 C CB    . TYR A 1 186 ? 18.814  -27.018 -15.812 1.00 18.16 ? 180 TYR A CB    1 
ATOM   1366 C CG    . TYR A 1 186 ? 18.210  -27.028 -14.427 1.00 20.02 ? 180 TYR A CG    1 
ATOM   1367 C CD1   . TYR A 1 186 ? 19.017  -27.290 -13.322 1.00 18.88 ? 180 TYR A CD1   1 
ATOM   1368 C CD2   . TYR A 1 186 ? 16.846  -26.763 -14.210 1.00 18.13 ? 180 TYR A CD2   1 
ATOM   1369 C CE1   . TYR A 1 186 ? 18.509  -27.306 -12.032 1.00 18.89 ? 180 TYR A CE1   1 
ATOM   1370 C CE2   . TYR A 1 186 ? 16.319  -26.771 -12.900 1.00 18.76 ? 180 TYR A CE2   1 
ATOM   1371 C CZ    . TYR A 1 186 ? 17.167  -27.043 -11.826 1.00 19.38 ? 180 TYR A CZ    1 
ATOM   1372 O OH    . TYR A 1 186 ? 16.728  -27.069 -10.515 1.00 21.19 ? 180 TYR A OH    1 
ATOM   1373 N N     . SER A 1 187 ? 20.466  -25.386 -18.302 1.00 15.21 ? 181 SER A N     1 
ATOM   1374 C CA    . SER A 1 187 ? 21.220  -25.603 -19.539 1.00 16.84 ? 181 SER A CA    1 
ATOM   1375 C C     . SER A 1 187 ? 22.611  -24.972 -19.475 1.00 15.14 ? 181 SER A C     1 
ATOM   1376 O O     . SER A 1 187 ? 22.792  -23.892 -18.912 1.00 17.08 ? 181 SER A O     1 
ATOM   1377 C CB    . SER A 1 187 ? 20.469  -25.031 -20.739 1.00 15.26 ? 181 SER A CB    1 
ATOM   1378 O OG    . SER A 1 187 ? 21.133  -25.403 -21.936 1.00 16.84 ? 181 SER A OG    1 
ATOM   1379 N N     . LYS A 1 188 ? 23.600  -25.657 -20.073 1.00 14.94 ? 182 LYS A N     1 
ATOM   1380 C CA    . LYS A 1 188 ? 24.900  -25.030 -20.313 1.00 18.22 ? 182 LYS A CA    1 
ATOM   1381 C C     . LYS A 1 188 ? 24.834  -23.992 -21.431 1.00 19.45 ? 182 LYS A C     1 
ATOM   1382 O O     . LYS A 1 188 ? 25.737  -23.150 -21.540 1.00 20.47 ? 182 LYS A O     1 
ATOM   1383 C CB    . LYS A 1 188 ? 25.947  -26.089 -20.680 1.00 18.74 ? 182 LYS A CB    1 
ATOM   1384 C CG    . LYS A 1 188 ? 26.296  -27.074 -19.564 1.00 21.36 ? 182 LYS A CG    1 
ATOM   1385 C CD    . LYS A 1 188 ? 27.355  -26.547 -18.642 1.00 24.29 ? 182 LYS A CD    1 
ATOM   1386 C CE    . LYS A 1 188 ? 28.740  -26.567 -19.285 1.00 22.69 ? 182 LYS A CE    1 
ATOM   1387 N NZ    . LYS A 1 188 ? 29.792  -26.165 -18.315 1.00 24.69 ? 182 LYS A NZ    1 
ATOM   1388 N N     . PHE A 1 189 ? 23.803  -24.048 -22.272 1.00 16.50 ? 183 PHE A N     1 
ATOM   1389 C CA    . PHE A 1 189 ? 23.692  -23.155 -23.416 1.00 15.55 ? 183 PHE A CA    1 
ATOM   1390 C C     . PHE A 1 189 ? 22.953  -21.901 -22.996 1.00 17.95 ? 183 PHE A C     1 
ATOM   1391 O O     . PHE A 1 189 ? 22.144  -21.924 -22.068 1.00 17.61 ? 183 PHE A O     1 
ATOM   1392 C CB    . PHE A 1 189 ? 22.969  -23.856 -24.574 1.00 16.73 ? 183 PHE A CB    1 
ATOM   1393 C CG    . PHE A 1 189 ? 23.614  -25.160 -24.949 1.00 17.13 ? 183 PHE A CG    1 
ATOM   1394 C CD1   . PHE A 1 189 ? 24.864  -25.169 -25.556 1.00 20.46 ? 183 PHE A CD1   1 
ATOM   1395 C CD2   . PHE A 1 189 ? 23.002  -26.374 -24.643 1.00 18.65 ? 183 PHE A CD2   1 
ATOM   1396 C CE1   . PHE A 1 189 ? 25.486  -26.366 -25.892 1.00 19.86 ? 183 PHE A CE1   1 
ATOM   1397 C CE2   . PHE A 1 189 ? 23.623  -27.590 -24.970 1.00 19.08 ? 183 PHE A CE2   1 
ATOM   1398 C CZ    . PHE A 1 189 ? 24.872  -27.579 -25.597 1.00 18.38 ? 183 PHE A CZ    1 
ATOM   1399 N N     . LYS A 1 190 ? 23.244  -20.796 -23.676 1.00 17.75 ? 184 LYS A N     1 
ATOM   1400 C CA    . LYS A 1 190 ? 22.555  -19.551 -23.352 1.00 17.73 ? 184 LYS A CA    1 
ATOM   1401 C C     . LYS A 1 190 ? 21.105  -19.622 -23.824 1.00 19.34 ? 184 LYS A C     1 
ATOM   1402 O O     . LYS A 1 190 ? 20.823  -20.114 -24.921 1.00 19.05 ? 184 LYS A O     1 
ATOM   1403 C CB    . LYS A 1 190 ? 23.274  -18.365 -23.998 1.00 19.10 ? 184 LYS A CB    1 
ATOM   1404 C CG    . LYS A 1 190 ? 22.695  -17.004 -23.588 1.00 21.57 ? 184 LYS A CG    1 
ATOM   1405 C CD    . LYS A 1 190 ? 23.013  -16.633 -22.151 1.00 24.68 ? 184 LYS A CD    1 
ATOM   1406 C CE    . LYS A 1 190 ? 24.490  -16.287 -21.986 1.00 31.76 ? 184 LYS A CE    1 
ATOM   1407 N NZ    . LYS A 1 190 ? 24.836  -16.042 -20.559 1.00 49.00 ? 184 LYS A NZ    1 
ATOM   1408 N N     . VAL A 1 191 ? 20.187  -19.140 -22.982 1.00 15.42 ? 185 VAL A N     1 
ATOM   1409 C CA    . VAL A 1 191 ? 18.754  -19.187 -23.248 1.00 18.65 ? 185 VAL A CA    1 
ATOM   1410 C C     . VAL A 1 191 ? 18.276  -17.768 -23.530 1.00 17.18 ? 185 VAL A C     1 
ATOM   1411 O O     . VAL A 1 191 ? 18.620  -16.823 -22.799 1.00 20.05 ? 185 VAL A O     1 
ATOM   1412 C CB    . VAL A 1 191 ? 17.974  -19.823 -22.082 1.00 18.05 ? 185 VAL A CB    1 
ATOM   1413 C CG1   . VAL A 1 191 ? 16.484  -19.779 -22.349 1.00 18.72 ? 185 VAL A CG1   1 
ATOM   1414 C CG2   . VAL A 1 191 ? 18.398  -21.290 -21.890 1.00 15.99 ? 185 VAL A CG2   1 
ATOM   1415 N N     . PHE A 1 192 ? 17.492  -17.628 -24.590 1.00 16.91 ? 186 PHE A N     1 
ATOM   1416 C CA    . PHE A 1 192 ? 16.944  -16.354 -25.034 1.00 21.45 ? 186 PHE A CA    1 
ATOM   1417 C C     . PHE A 1 192 ? 15.426  -16.414 -24.978 1.00 19.07 ? 186 PHE A C     1 
ATOM   1418 O O     . PHE A 1 192 ? 14.825  -17.457 -25.244 1.00 18.03 ? 186 PHE A O     1 
ATOM   1419 C CB    . PHE A 1 192 ? 17.392  -16.047 -26.468 1.00 18.44 ? 186 PHE A CB    1 
ATOM   1420 C CG    . PHE A 1 192 ? 18.876  -15.824 -26.605 1.00 17.40 ? 186 PHE A CG    1 
ATOM   1421 C CD1   . PHE A 1 192 ? 19.372  -14.544 -26.755 1.00 18.66 ? 186 PHE A CD1   1 
ATOM   1422 C CD2   . PHE A 1 192 ? 19.771  -16.898 -26.591 1.00 17.60 ? 186 PHE A CD2   1 
ATOM   1423 C CE1   . PHE A 1 192 ? 20.736  -14.310 -26.888 1.00 26.81 ? 186 PHE A CE1   1 
ATOM   1424 C CE2   . PHE A 1 192 ? 21.129  -16.673 -26.731 1.00 19.22 ? 186 PHE A CE2   1 
ATOM   1425 C CZ    . PHE A 1 192 ? 21.616  -15.392 -26.878 1.00 22.23 ? 186 PHE A CZ    1 
ATOM   1426 N N     . THR A 1 193 ? 14.795  -15.289 -24.647 1.00 15.90 ? 187 THR A N     1 
ATOM   1427 C CA    . THR A 1 193 ? 13.341  -15.286 -24.559 1.00 19.09 ? 187 THR A CA    1 
ATOM   1428 C C     . THR A 1 193 ? 12.818  -13.907 -24.923 1.00 20.71 ? 187 THR A C     1 
ATOM   1429 O O     . THR A 1 193 ? 13.582  -12.995 -25.254 1.00 19.62 ? 187 THR A O     1 
ATOM   1430 C CB    . THR A 1 193 ? 12.854  -15.727 -23.167 1.00 17.49 ? 187 THR A CB    1 
ATOM   1431 O OG1   . THR A 1 193 ? 11.457  -16.061 -23.242 1.00 16.90 ? 187 THR A OG1   1 
ATOM   1432 C CG2   . THR A 1 193 ? 13.077  -14.616 -22.112 1.00 16.62 ? 187 THR A CG2   1 
ATOM   1433 N N     . CYS A 1 194 ? 11.492  -13.782 -24.902 1.00 20.24 ? 188 CYS A N     1 
ATOM   1434 C CA    . CYS A 1 194 ? 10.804  -12.533 -25.182 1.00 19.26 ? 188 CYS A CA    1 
ATOM   1435 C C     . CYS A 1 194 ? 9.599   -12.446 -24.262 1.00 17.80 ? 188 CYS A C     1 
ATOM   1436 O O     . CYS A 1 194 ? 9.116   -13.455 -23.743 1.00 20.30 ? 188 CYS A O     1 
ATOM   1437 C CB    . CYS A 1 194 ? 10.351  -12.419 -26.655 1.00 18.11 ? 188 CYS A CB    1 
ATOM   1438 S SG    . CYS A 1 194 ? 9.088   -13.650 -27.160 1.00 20.51 ? 188 CYS A SG    1 
ATOM   1439 N N     . ALA A 1 195 ? 9.127   -11.227 -24.053 1.00 18.72 ? 189 ALA A N     1 
ATOM   1440 C CA    . ALA A 1 195 ? 7.970   -10.988 -23.200 1.00 19.78 ? 189 ALA A CA    1 
ATOM   1441 C C     . ALA A 1 195 ? 6.726   -10.981 -24.083 1.00 21.71 ? 189 ALA A C     1 
ATOM   1442 O O     . ALA A 1 195 ? 6.485   -10.021 -24.820 1.00 25.14 ? 189 ALA A O     1 
ATOM   1443 C CB    . ALA A 1 195 ? 8.125   -9.668  -22.452 1.00 21.65 ? 189 ALA A CB    1 
ATOM   1444 N N     . CYS A 1 196 ? 5.933   -12.058 -24.029 1.00 19.90 ? 190 CYS A N     1 
ATOM   1445 C CA    . CYS A 1 196 ? 4.673   -12.026 -24.772 1.00 19.50 ? 190 CYS A CA    1 
ATOM   1446 C C     . CYS A 1 196 ? 3.581   -11.303 -24.010 1.00 21.24 ? 190 CYS A C     1 
ATOM   1447 O O     . CYS A 1 196 ? 2.627   -10.811 -24.625 1.00 24.13 ? 190 CYS A O     1 
ATOM   1448 C CB    . CYS A 1 196 ? 4.190   -13.443 -25.106 1.00 21.63 ? 190 CYS A CB    1 
ATOM   1449 S SG    . CYS A 1 196 ? 5.374   -14.442 -26.036 1.00 20.73 ? 190 CYS A SG    1 
ATOM   1450 N N     . VAL A 1 197 ? 3.709   -11.246 -22.693 1.00 24.77 ? 191 VAL A N     1 
ATOM   1451 C CA    . VAL A 1 197 ? 2.773   -10.576 -21.803 1.00 27.66 ? 191 VAL A CA    1 
ATOM   1452 C C     . VAL A 1 197 ? 3.519   -9.423  -21.138 1.00 30.47 ? 191 VAL A C     1 
ATOM   1453 O O     . VAL A 1 197 ? 4.542   -9.640  -20.477 1.00 30.92 ? 191 VAL A O     1 
ATOM   1454 C CB    . VAL A 1 197 ? 2.220   -11.553 -20.752 1.00 23.21 ? 191 VAL A CB    1 
ATOM   1455 C CG1   . VAL A 1 197 ? 1.240   -10.845 -19.843 1.00 29.07 ? 191 VAL A CG1   1 
ATOM   1456 C CG2   . VAL A 1 197 ? 1.553   -12.729 -21.428 1.00 24.18 ? 191 VAL A CG2   1 
ATOM   1457 N N     . GLY A 1 198 ? 3.034   -8.202  -21.332 1.00 31.47 ? 192 GLY A N     1 
ATOM   1458 C CA    . GLY A 1 198 ? 3.736   -7.088  -20.716 1.00 35.13 ? 192 GLY A CA    1 
ATOM   1459 C C     . GLY A 1 198 ? 5.052   -6.806  -21.419 1.00 41.59 ? 192 GLY A C     1 
ATOM   1460 O O     . GLY A 1 198 ? 5.236   -7.124  -22.598 1.00 47.35 ? 192 GLY A O     1 
ATOM   1461 N N     . ASP A 1 199 ? 5.989   -6.206  -20.686 1.00 34.32 ? 193 ASP A N     1 
ATOM   1462 C CA    . ASP A 1 199 ? 7.309   -5.905  -21.235 1.00 27.91 ? 193 ASP A CA    1 
ATOM   1463 C C     . ASP A 1 199 ? 8.393   -6.669  -20.468 1.00 30.25 ? 193 ASP A C     1 
ATOM   1464 O O     . ASP A 1 199 ? 8.117   -7.459  -19.556 1.00 31.53 ? 193 ASP A O     1 
ATOM   1465 C CB    . ASP A 1 199 ? 7.586   -4.396  -21.245 1.00 29.84 ? 193 ASP A CB    1 
ATOM   1466 C CG    . ASP A 1 199 ? 7.501   -3.753  -19.868 1.00 34.42 ? 193 ASP A CG    1 
ATOM   1467 O OD1   . ASP A 1 199 ? 7.430   -4.455  -18.843 1.00 33.53 ? 193 ASP A OD1   1 
ATOM   1468 O OD2   . ASP A 1 199 ? 7.482   -2.504  -19.815 1.00 38.72 ? 193 ASP A OD2   1 
ATOM   1469 N N     . ILE A 1 200 ? 9.643   -6.447  -20.880 1.00 30.28 ? 194 ILE A N     1 
ATOM   1470 C CA    . ILE A 1 200 ? 10.756  -7.188  -20.298 1.00 26.36 ? 194 ILE A CA    1 
ATOM   1471 C C     . ILE A 1 200 ? 10.905  -6.853  -18.818 1.00 28.39 ? 194 ILE A C     1 
ATOM   1472 O O     . ILE A 1 200 ? 11.211  -7.733  -18.006 1.00 27.06 ? 194 ILE A O     1 
ATOM   1473 C CB    . ILE A 1 200 ? 12.051  -6.923  -21.087 1.00 31.36 ? 194 ILE A CB    1 
ATOM   1474 C CG1   . ILE A 1 200 ? 11.974  -7.602  -22.459 1.00 30.74 ? 194 ILE A CG1   1 
ATOM   1475 C CG2   . ILE A 1 200 ? 13.272  -7.464  -20.342 1.00 26.26 ? 194 ILE A CG2   1 
ATOM   1476 C CD1   . ILE A 1 200 ? 13.139  -7.294  -23.365 1.00 35.23 ? 194 ILE A CD1   1 
ATOM   1477 N N     . LYS A 1 201 ? 10.692  -5.586  -18.442 1.00 32.69 ? 195 LYS A N     1 
ATOM   1478 C CA    . LYS A 1 201 ? 10.733  -5.235  -17.022 1.00 35.36 ? 195 LYS A CA    1 
ATOM   1479 C C     . LYS A 1 201 ? 9.723   -6.060  -16.229 1.00 35.57 ? 195 LYS A C     1 
ATOM   1480 O O     . LYS A 1 201 ? 10.047  -6.605  -15.166 1.00 31.33 ? 195 LYS A O     1 
ATOM   1481 C CB    . LYS A 1 201 ? 10.472  -3.731  -16.826 1.00 34.22 ? 195 LYS A CB    1 
ATOM   1482 N N     . TYR A 1 202 ? 8.496   -6.172  -16.743 1.00 36.89 ? 196 TYR A N     1 
ATOM   1483 C CA    . TYR A 1 202 ? 7.460   -6.947  -16.071 1.00 35.86 ? 196 TYR A CA    1 
ATOM   1484 C C     . TYR A 1 202 ? 7.838   -8.421  -16.002 1.00 32.03 ? 196 TYR A C     1 
ATOM   1485 O O     . TYR A 1 202 ? 7.589   -9.097  -14.994 1.00 31.19 ? 196 TYR A O     1 
ATOM   1486 C CB    . TYR A 1 202 ? 6.133   -6.758  -16.810 1.00 35.93 ? 196 TYR A CB    1 
ATOM   1487 C CG    . TYR A 1 202 ? 5.008   -7.609  -16.283 1.00 40.61 ? 196 TYR A CG    1 
ATOM   1488 C CD1   . TYR A 1 202 ? 4.579   -8.738  -16.975 1.00 44.90 ? 196 TYR A CD1   1 
ATOM   1489 C CD2   . TYR A 1 202 ? 4.386   -7.299  -15.087 1.00 50.70 ? 196 TYR A CD2   1 
ATOM   1490 C CE1   . TYR A 1 202 ? 3.551   -9.524  -16.487 1.00 47.27 ? 196 TYR A CE1   1 
ATOM   1491 C CE2   . TYR A 1 202 ? 3.360   -8.073  -14.595 1.00 54.43 ? 196 TYR A CE2   1 
ATOM   1492 C CZ    . TYR A 1 202 ? 2.947   -9.183  -15.296 1.00 53.45 ? 196 TYR A CZ    1 
ATOM   1493 O OH    . TYR A 1 202 ? 1.921   -9.952  -14.796 1.00 63.59 ? 196 TYR A OH    1 
ATOM   1494 N N     . LEU A 1 203 ? 8.452   -8.933  -17.065 1.00 24.96 ? 197 LEU A N     1 
ATOM   1495 C CA    . LEU A 1 203 ? 8.815   -10.342 -17.109 1.00 24.09 ? 197 LEU A CA    1 
ATOM   1496 C C     . LEU A 1 203 ? 9.890   -10.665 -16.079 1.00 23.66 ? 197 LEU A C     1 
ATOM   1497 O O     . LEU A 1 203 ? 9.773   -11.651 -15.339 1.00 24.63 ? 197 LEU A O     1 
ATOM   1498 C CB    . LEU A 1 203 ? 9.267   -10.692 -18.526 1.00 23.92 ? 197 LEU A CB    1 
ATOM   1499 C CG    . LEU A 1 203 ? 9.756   -12.102 -18.808 1.00 20.50 ? 197 LEU A CG    1 
ATOM   1500 C CD1   . LEU A 1 203 ? 8.680   -13.137 -18.494 1.00 20.69 ? 197 LEU A CD1   1 
ATOM   1501 C CD2   . LEU A 1 203 ? 10.162  -12.184 -20.287 1.00 19.50 ? 197 LEU A CD2   1 
ATOM   1502 N N     . LYS A 1 204 ? 10.924  -9.819  -15.984 1.00 25.11 ? 198 LYS A N     1 
ATOM   1503 C CA    . LYS A 1 204 ? 11.918  -9.988  -14.930 1.00 23.83 ? 198 LYS A CA    1 
ATOM   1504 C C     . LYS A 1 204 ? 11.270  -9.943  -13.553 1.00 26.24 ? 198 LYS A C     1 
ATOM   1505 O O     . LYS A 1 204 ? 11.618  -10.737 -12.670 1.00 27.14 ? 198 LYS A O     1 
ATOM   1506 C CB    . LYS A 1 204 ? 13.002  -8.915  -15.048 1.00 26.16 ? 198 LYS A CB    1 
ATOM   1507 C CG    . LYS A 1 204 ? 13.972  -9.129  -16.215 1.00 27.26 ? 198 LYS A CG    1 
ATOM   1508 C CD    . LYS A 1 204 ? 14.974  -7.981  -16.295 1.00 41.21 ? 198 LYS A CD    1 
ATOM   1509 C CE    . LYS A 1 204 ? 15.886  -8.117  -17.508 1.00 39.31 ? 198 LYS A CE    1 
ATOM   1510 N NZ    . LYS A 1 204 ? 16.754  -6.926  -17.717 1.00 46.00 ? 198 LYS A NZ    1 
ATOM   1511 N N     . LYS A 1 205 ? 10.317  -9.030  -13.357 1.00 29.65 ? 199 LYS A N     1 
ATOM   1512 C CA    . LYS A 1 205 ? 9.639   -8.937  -12.066 1.00 33.21 ? 199 LYS A CA    1 
ATOM   1513 C C     . LYS A 1 205 ? 8.922   -10.241 -11.720 1.00 34.22 ? 199 LYS A C     1 
ATOM   1514 O O     . LYS A 1 205 ? 8.989   -10.708 -10.577 1.00 30.22 ? 199 LYS A O     1 
ATOM   1515 C CB    . LYS A 1 205 ? 8.664   -7.758  -12.080 1.00 37.19 ? 199 LYS A CB    1 
ATOM   1516 C CG    . LYS A 1 205 ? 7.837   -7.599  -10.822 1.00 43.61 ? 199 LYS A CG    1 
ATOM   1517 C CD    . LYS A 1 205 ? 6.810   -6.486  -11.006 1.00 48.07 ? 199 LYS A CD    1 
ATOM   1518 C CE    . LYS A 1 205 ? 5.718   -6.554  -9.949  1.00 52.64 ? 199 LYS A CE    1 
ATOM   1519 N NZ    . LYS A 1 205 ? 4.530   -5.740  -10.335 1.00 59.14 ? 199 LYS A NZ    1 
ATOM   1520 N N     . GLN A 1 206 ? 8.234   -10.847 -12.696 1.00 29.67 ? 200 GLN A N     1 
ATOM   1521 C CA    . GLN A 1 206 ? 7.574   -12.128 -12.450 1.00 28.03 ? 200 GLN A CA    1 
ATOM   1522 C C     . GLN A 1 206 ? 8.583   -13.200 -12.067 1.00 24.11 ? 200 GLN A C     1 
ATOM   1523 O O     . GLN A 1 206 ? 8.348   -13.989 -11.144 1.00 23.22 ? 200 GLN A O     1 
ATOM   1524 C CB    . GLN A 1 206 ? 6.795   -12.586 -13.683 1.00 28.32 ? 200 GLN A CB    1 
ATOM   1525 C CG    . GLN A 1 206 ? 5.800   -11.593 -14.238 1.00 33.23 ? 200 GLN A CG    1 
ATOM   1526 C CD    . GLN A 1 206 ? 4.890   -11.032 -13.175 1.00 46.72 ? 200 GLN A CD    1 
ATOM   1527 O OE1   . GLN A 1 206 ? 3.950   -11.694 -12.732 1.00 52.69 ? 200 GLN A OE1   1 
ATOM   1528 N NE2   . GLN A 1 206 ? 5.162   -9.800  -12.753 1.00 47.12 ? 200 GLN A NE2   1 
ATOM   1529 N N     . ILE A 1 207 ? 9.695   -13.274 -12.795 1.00 23.29 ? 201 ILE A N     1 
ATOM   1530 C CA    . ILE A 1 207 ? 10.677  -14.313 -12.511 1.00 22.89 ? 201 ILE A CA    1 
ATOM   1531 C C     . ILE A 1 207 ? 11.233  -14.139 -11.104 1.00 24.96 ? 201 ILE A C     1 
ATOM   1532 O O     . ILE A 1 207 ? 11.413  -15.116 -10.369 1.00 25.86 ? 201 ILE A O     1 
ATOM   1533 C CB    . ILE A 1 207 ? 11.785  -14.303 -13.579 1.00 21.44 ? 201 ILE A CB    1 
ATOM   1534 C CG1   . ILE A 1 207 ? 11.220  -14.776 -14.920 1.00 20.11 ? 201 ILE A CG1   1 
ATOM   1535 C CG2   . ILE A 1 207 ? 12.961  -15.190 -13.135 1.00 18.81 ? 201 ILE A CG2   1 
ATOM   1536 C CD1   . ILE A 1 207 ? 12.124  -14.457 -16.116 1.00 18.79 ? 201 ILE A CD1   1 
ATOM   1537 N N     . LEU A 1 208 ? 11.517  -12.891 -10.710 1.00 24.68 ? 202 LEU A N     1 
ATOM   1538 C CA    . LEU A 1 208 ? 12.009  -12.622 -9.359  1.00 24.85 ? 202 LEU A CA    1 
ATOM   1539 C C     . LEU A 1 208 ? 10.951  -12.887 -8.298  1.00 33.77 ? 202 LEU A C     1 
ATOM   1540 O O     . LEU A 1 208 ? 11.294  -13.158 -7.142  1.00 34.09 ? 202 LEU A O     1 
ATOM   1541 C CB    . LEU A 1 208 ? 12.504  -11.183 -9.260  1.00 27.30 ? 202 LEU A CB    1 
ATOM   1542 C CG    . LEU A 1 208 ? 13.889  -10.999 -9.879  1.00 34.99 ? 202 LEU A CG    1 
ATOM   1543 C CD1   . LEU A 1 208 ? 14.244  -9.527  -9.976  1.00 39.07 ? 202 LEU A CD1   1 
ATOM   1544 C CD2   . LEU A 1 208 ? 14.917  -11.758 -9.050  1.00 38.31 ? 202 LEU A CD2   1 
ATOM   1545 N N     . THR A 1 209 ? 9.667   -12.794 -8.650  1.00 32.31 ? 203 THR A N     1 
ATOM   1546 C CA    . THR A 1 209 ? 8.639   -13.202 -7.696  1.00 33.52 ? 203 THR A CA    1 
ATOM   1547 C C     . THR A 1 209 ? 8.649   -14.714 -7.505  1.00 35.69 ? 203 THR A C     1 
ATOM   1548 O O     . THR A 1 209 ? 8.530   -15.207 -6.375  1.00 40.59 ? 203 THR A O     1 
ATOM   1549 C CB    . THR A 1 209 ? 7.259   -12.726 -8.158  1.00 42.07 ? 203 THR A CB    1 
ATOM   1550 O OG1   . THR A 1 209 ? 7.209   -11.297 -8.120  1.00 43.21 ? 203 THR A OG1   1 
ATOM   1551 C CG2   . THR A 1 209 ? 6.174   -13.273 -7.244  1.00 44.25 ? 203 THR A CG2   1 
ATOM   1552 N N     . LEU A 1 210 ? 8.800   -15.456 -8.605  1.00 29.14 ? 204 LEU A N     1 
ATOM   1553 C CA    . LEU A 1 210 ? 8.921   -16.910 -8.553  1.00 31.54 ? 204 LEU A CA    1 
ATOM   1554 C C     . LEU A 1 210 ? 10.133  -17.337 -7.737  1.00 36.76 ? 204 LEU A C     1 
ATOM   1555 O O     . LEU A 1 210 ? 10.033  -18.199 -6.858  1.00 33.39 ? 204 LEU A O     1 
ATOM   1556 C CB    . LEU A 1 210 ? 9.014   -17.463 -9.974  1.00 30.09 ? 204 LEU A CB    1 
ATOM   1557 C CG    . LEU A 1 210 ? 9.245   -18.962 -10.209 1.00 29.25 ? 204 LEU A CG    1 
ATOM   1558 C CD1   . LEU A 1 210 ? 8.030   -19.754 -9.766  1.00 46.74 ? 204 LEU A CD1   1 
ATOM   1559 C CD2   . LEU A 1 210 ? 9.557   -19.220 -11.663 1.00 31.38 ? 204 LEU A CD2   1 
ATOM   1560 N N     . ASP A 1 211 ? 11.294  -16.752 -8.027  1.00 32.13 ? 205 ASP A N     1 
ATOM   1561 C CA    . ASP A 1 211 ? 12.549  -17.112 -7.369  1.00 30.93 ? 205 ASP A CA    1 
ATOM   1562 C C     . ASP A 1 211 ? 13.292  -15.819 -7.059  1.00 30.01 ? 205 ASP A C     1 
ATOM   1563 O O     . ASP A 1 211 ? 13.992  -15.271 -7.928  1.00 30.87 ? 205 ASP A O     1 
ATOM   1564 C CB    . ASP A 1 211 ? 13.385  -18.046 -8.242  1.00 30.53 ? 205 ASP A CB    1 
ATOM   1565 C CG    . ASP A 1 211 ? 14.784  -18.274 -7.686  1.00 39.95 ? 205 ASP A CG    1 
ATOM   1566 O OD1   . ASP A 1 211 ? 15.017  -18.036 -6.482  1.00 42.60 ? 205 ASP A OD1   1 
ATOM   1567 O OD2   . ASP A 1 211 ? 15.661  -18.694 -8.468  1.00 38.29 ? 205 ASP A OD2   1 
ATOM   1568 N N     . PRO A 1 212 ? 13.150  -15.294 -5.843  1.00 29.69 ? 206 PRO A N     1 
ATOM   1569 C CA    . PRO A 1 212 ? 13.811  -14.023 -5.495  1.00 33.28 ? 206 PRO A CA    1 
ATOM   1570 C C     . PRO A 1 212 ? 15.323  -14.045 -5.621  1.00 33.74 ? 206 PRO A C     1 
ATOM   1571 O O     . PRO A 1 212 ? 15.937  -12.970 -5.686  1.00 37.14 ? 206 PRO A O     1 
ATOM   1572 C CB    . PRO A 1 212 ? 13.381  -13.793 -4.041  1.00 37.08 ? 206 PRO A CB    1 
ATOM   1573 C CG    . PRO A 1 212 ? 12.089  -14.530 -3.923  1.00 38.78 ? 206 PRO A CG    1 
ATOM   1574 C CD    . PRO A 1 212 ? 12.204  -15.734 -4.803  1.00 32.46 ? 206 PRO A CD    1 
ATOM   1575 N N     . SER A 1 213 ? 15.945  -15.220 -5.637  1.00 34.07 ? 207 SER A N     1 
ATOM   1576 C CA    . SER A 1 213 ? 17.388  -15.336 -5.773  1.00 38.02 ? 207 SER A CA    1 
ATOM   1577 C C     . SER A 1 213 ? 17.810  -15.624 -7.202  1.00 37.97 ? 207 SER A C     1 
ATOM   1578 O O     . SER A 1 213 ? 18.967  -15.991 -7.433  1.00 42.17 ? 207 SER A O     1 
ATOM   1579 C CB    . SER A 1 213 ? 17.914  -16.434 -4.854  1.00 48.03 ? 207 SER A CB    1 
ATOM   1580 O OG    . SER A 1 213 ? 17.448  -17.699 -5.290  1.00 56.91 ? 207 SER A OG    1 
ATOM   1581 N N     . TYR A 1 214 ? 16.903  -15.479 -8.164  1.00 30.08 ? 208 TYR A N     1 
ATOM   1582 C CA    . TYR A 1 214 ? 17.217  -15.905 -9.518  1.00 28.01 ? 208 TYR A CA    1 
ATOM   1583 C C     . TYR A 1 214 ? 18.402  -15.129 -10.067 1.00 34.95 ? 208 TYR A C     1 
ATOM   1584 O O     . TYR A 1 214 ? 18.512  -13.911 -9.889  1.00 38.55 ? 208 TYR A O     1 
ATOM   1585 C CB    . TYR A 1 214 ? 16.016  -15.738 -10.447 1.00 23.09 ? 208 TYR A CB    1 
ATOM   1586 C CG    . TYR A 1 214 ? 16.273  -16.398 -11.786 1.00 25.02 ? 208 TYR A CG    1 
ATOM   1587 C CD1   . TYR A 1 214 ? 16.591  -15.649 -12.911 1.00 22.26 ? 208 TYR A CD1   1 
ATOM   1588 C CD2   . TYR A 1 214 ? 16.243  -17.780 -11.905 1.00 23.23 ? 208 TYR A CD2   1 
ATOM   1589 C CE1   . TYR A 1 214 ? 16.859  -16.271 -14.120 1.00 20.85 ? 208 TYR A CE1   1 
ATOM   1590 C CE2   . TYR A 1 214 ? 16.505  -18.401 -13.097 1.00 22.03 ? 208 TYR A CE2   1 
ATOM   1591 C CZ    . TYR A 1 214 ? 16.803  -17.652 -14.200 1.00 20.05 ? 208 TYR A CZ    1 
ATOM   1592 O OH    . TYR A 1 214 ? 17.080  -18.294 -15.389 1.00 19.56 ? 208 TYR A OH    1 
ATOM   1593 N N     . ASP A 1 215 ? 19.289  -15.865 -10.727 1.00 38.64 ? 209 ASP A N     1 
ATOM   1594 C CA    . ASP A 1 215 ? 20.475  -15.338 -11.383 1.00 43.03 ? 209 ASP A CA    1 
ATOM   1595 C C     . ASP A 1 215 ? 20.191  -15.293 -12.881 1.00 39.29 ? 209 ASP A C     1 
ATOM   1596 O O     . ASP A 1 215 ? 20.128  -16.340 -13.536 1.00 37.57 ? 209 ASP A O     1 
ATOM   1597 C CB    . ASP A 1 215 ? 21.669  -16.236 -11.065 1.00 51.31 ? 209 ASP A CB    1 
ATOM   1598 C CG    . ASP A 1 215 ? 22.950  -15.771 -11.709 1.00 57.18 ? 209 ASP A CG    1 
ATOM   1599 O OD1   . ASP A 1 215 ? 22.933  -14.782 -12.468 1.00 57.48 ? 209 ASP A OD1   1 
ATOM   1600 O OD2   . ASP A 1 215 ? 23.991  -16.406 -11.442 1.00 58.66 ? 209 ASP A OD2   1 
ATOM   1601 N N     . PHE A 1 216 ? 20.032  -14.084 -13.421 1.00 28.90 ? 210 PHE A N     1 
ATOM   1602 C CA    . PHE A 1 216 ? 19.767  -13.900 -14.845 1.00 26.19 ? 210 PHE A CA    1 
ATOM   1603 C C     . PHE A 1 216 ? 21.005  -14.095 -15.721 1.00 26.77 ? 210 PHE A C     1 
ATOM   1604 O O     . PHE A 1 216 ? 20.954  -13.737 -16.905 1.00 32.70 ? 210 PHE A O     1 
ATOM   1605 C CB    . PHE A 1 216 ? 19.185  -12.505 -15.105 1.00 28.30 ? 210 PHE A CB    1 
ATOM   1606 C CG    . PHE A 1 216 ? 17.817  -12.302 -14.526 1.00 27.14 ? 210 PHE A CG    1 
ATOM   1607 C CD1   . PHE A 1 216 ? 16.703  -12.760 -15.201 1.00 23.10 ? 210 PHE A CD1   1 
ATOM   1608 C CD2   . PHE A 1 216 ? 17.648  -11.659 -13.308 1.00 33.57 ? 210 PHE A CD2   1 
ATOM   1609 C CE1   . PHE A 1 216 ? 15.439  -12.583 -14.683 1.00 28.70 ? 210 PHE A CE1   1 
ATOM   1610 C CE2   . PHE A 1 216 ? 16.382  -11.477 -12.780 1.00 36.55 ? 210 PHE A CE2   1 
ATOM   1611 C CZ    . PHE A 1 216 ? 15.274  -11.946 -13.474 1.00 30.31 ? 210 PHE A CZ    1 
ATOM   1612 N N     . SER A 1 217 ? 22.091  -14.667 -15.193 1.00 26.63 ? 211 SER A N     1 
ATOM   1613 C CA    . SER A 1 217 ? 23.346  -14.702 -15.941 1.00 28.77 ? 211 SER A CA    1 
ATOM   1614 C C     . SER A 1 217 ? 23.248  -15.521 -17.223 1.00 27.06 ? 211 SER A C     1 
ATOM   1615 O O     . SER A 1 217 ? 24.027  -15.279 -18.154 1.00 30.80 ? 211 SER A O     1 
ATOM   1616 C CB    . SER A 1 217 ? 24.472  -15.256 -15.064 1.00 40.37 ? 211 SER A CB    1 
ATOM   1617 O OG    . SER A 1 217 ? 24.106  -16.514 -14.516 1.00 44.50 ? 211 SER A OG    1 
ATOM   1618 N N     . ASN A 1 218 ? 22.313  -16.471 -17.299 1.00 23.23 ? 212 ASN A N     1 
ATOM   1619 C CA    . ASN A 1 218 ? 22.207  -17.346 -18.458 1.00 20.49 ? 212 ASN A CA    1 
ATOM   1620 C C     . ASN A 1 218 ? 20.912  -17.136 -19.224 1.00 20.52 ? 212 ASN A C     1 
ATOM   1621 O O     . ASN A 1 218 ? 20.541  -17.982 -20.041 1.00 18.25 ? 212 ASN A O     1 
ATOM   1622 C CB    . ASN A 1 218 ? 22.338  -18.821 -18.054 1.00 20.41 ? 212 ASN A CB    1 
ATOM   1623 C CG    . ASN A 1 218 ? 22.719  -19.710 -19.227 1.00 21.96 ? 212 ASN A CG    1 
ATOM   1624 O OD1   . ASN A 1 218 ? 23.552  -19.335 -20.053 1.00 21.70 ? 212 ASN A OD1   1 
ATOM   1625 N ND2   . ASN A 1 218 ? 22.101  -20.904 -19.314 1.00 21.69 ? 212 ASN A ND2   1 
ATOM   1626 N N     . LEU A 1 219 ? 20.213  -16.025 -18.991 1.00 20.72 ? 213 LEU A N     1 
ATOM   1627 C CA    . LEU A 1 219 ? 18.950  -15.750 -19.672 1.00 21.18 ? 213 LEU A CA    1 
ATOM   1628 C C     . LEU A 1 219 ? 19.007  -14.366 -20.299 1.00 21.24 ? 213 LEU A C     1 
ATOM   1629 O O     . LEU A 1 219 ? 19.225  -13.370 -19.599 1.00 22.43 ? 213 LEU A O     1 
ATOM   1630 C CB    . LEU A 1 219 ? 17.768  -15.838 -18.697 1.00 19.71 ? 213 LEU A CB    1 
ATOM   1631 C CG    . LEU A 1 219 ? 16.365  -15.574 -19.265 1.00 19.61 ? 213 LEU A CG    1 
ATOM   1632 C CD1   . LEU A 1 219 ? 16.025  -16.592 -20.373 1.00 21.39 ? 213 LEU A CD1   1 
ATOM   1633 C CD2   . LEU A 1 219 ? 15.318  -15.637 -18.138 1.00 25.23 ? 213 LEU A CD2   1 
ATOM   1634 N N     . GLU A 1 220 ? 18.811  -14.299 -21.612 1.00 20.78 ? 214 GLU A N     1 
ATOM   1635 C CA    . GLU A 1 220 ? 18.844  -13.040 -22.338 1.00 21.31 ? 214 GLU A CA    1 
ATOM   1636 C C     . GLU A 1 220 ? 17.448  -12.723 -22.853 1.00 16.56 ? 214 GLU A C     1 
ATOM   1637 O O     . GLU A 1 220 ? 16.668  -13.626 -23.178 1.00 21.41 ? 214 GLU A O     1 
ATOM   1638 C CB    . GLU A 1 220 ? 19.829  -13.096 -23.508 1.00 25.14 ? 214 GLU A CB    1 
ATOM   1639 C CG    . GLU A 1 220 ? 21.243  -13.417 -23.092 1.00 29.18 ? 214 GLU A CG    1 
ATOM   1640 C CD    . GLU A 1 220 ? 21.944  -12.245 -22.449 1.00 39.51 ? 214 GLU A CD    1 
ATOM   1641 O OE1   . GLU A 1 220 ? 21.407  -11.119 -22.525 1.00 38.83 ? 214 GLU A OE1   1 
ATOM   1642 O OE2   . GLU A 1 220 ? 23.037  -12.449 -21.874 1.00 45.79 ? 214 GLU A OE2   1 
ATOM   1643 N N     . PHE A 1 221 ? 17.138  -11.430 -22.899 1.00 22.36 ? 215 PHE A N     1 
ATOM   1644 C CA    . PHE A 1 221 ? 15.813  -10.964 -23.288 1.00 20.35 ? 215 PHE A CA    1 
ATOM   1645 C C     . PHE A 1 221 ? 15.906  -10.220 -24.611 1.00 19.02 ? 215 PHE A C     1 
ATOM   1646 O O     . PHE A 1 221 ? 16.679  -9.259  -24.738 1.00 25.32 ? 215 PHE A O     1 
ATOM   1647 C CB    . PHE A 1 221 ? 15.221  -10.071 -22.199 1.00 23.05 ? 215 PHE A CB    1 
ATOM   1648 C CG    . PHE A 1 221 ? 15.049  -10.772 -20.886 1.00 22.02 ? 215 PHE A CG    1 
ATOM   1649 C CD1   . PHE A 1 221 ? 13.903  -11.503 -20.638 1.00 22.80 ? 215 PHE A CD1   1 
ATOM   1650 C CD2   . PHE A 1 221 ? 16.043  -10.727 -19.914 1.00 24.35 ? 215 PHE A CD2   1 
ATOM   1651 C CE1   . PHE A 1 221 ? 13.733  -12.172 -19.449 1.00 22.51 ? 215 PHE A CE1   1 
ATOM   1652 C CE2   . PHE A 1 221 ? 15.882  -11.393 -18.706 1.00 23.15 ? 215 PHE A CE2   1 
ATOM   1653 C CZ    . PHE A 1 221 ? 14.728  -12.108 -18.466 1.00 22.81 ? 215 PHE A CZ    1 
ATOM   1654 N N     . LEU A 1 222 ? 15.108  -10.656 -25.584 1.00 23.42 ? 216 LEU A N     1 
ATOM   1655 C CA    . LEU A 1 222 ? 15.048  -10.025 -26.894 1.00 23.49 ? 216 LEU A CA    1 
ATOM   1656 C C     . LEU A 1 222 ? 13.769  -9.206  -27.040 1.00 23.86 ? 216 LEU A C     1 
ATOM   1657 O O     . LEU A 1 222 ? 12.708  -9.587  -26.543 1.00 25.22 ? 216 LEU A O     1 
ATOM   1658 C CB    . LEU A 1 222 ? 15.121  -11.083 -27.993 1.00 22.22 ? 216 LEU A CB    1 
ATOM   1659 C CG    . LEU A 1 222 ? 16.394  -11.935 -28.015 1.00 24.26 ? 216 LEU A CG    1 
ATOM   1660 C CD1   . LEU A 1 222 ? 16.286  -13.018 -29.106 1.00 25.76 ? 216 LEU A CD1   1 
ATOM   1661 C CD2   . LEU A 1 222 ? 17.652  -11.086 -28.202 1.00 30.01 ? 216 LEU A CD2   1 
ATOM   1662 N N     . THR A 1 223 ? 13.882  -8.075  -27.722 1.00 34.60 ? 217 THR A N     1 
ATOM   1663 C CA    . THR A 1 223 ? 12.764  -7.178  -27.968 1.00 39.69 ? 217 THR A CA    1 
ATOM   1664 C C     . THR A 1 223 ? 12.254  -7.363  -29.391 1.00 37.07 ? 217 THR A C     1 
ATOM   1665 O O     . THR A 1 223 ? 13.022  -7.670  -30.305 1.00 41.03 ? 217 THR A O     1 
ATOM   1666 C CB    . THR A 1 223 ? 13.187  -5.720  -27.785 1.00 40.37 ? 217 THR A CB    1 
ATOM   1667 O OG1   . THR A 1 223 ? 14.206  -5.410  -28.744 1.00 47.88 ? 217 THR A OG1   1 
ATOM   1668 C CG2   . THR A 1 223 ? 13.743  -5.472  -26.387 1.00 41.84 ? 217 THR A CG2   1 
ATOM   1669 N N     . SER A 1 224 ? 10.959  -7.142  -29.586 1.00 27.90 ? 218 SER A N     1 
ATOM   1670 C CA    . SER A 1 224 ? 10.429  -7.111  -30.939 1.00 31.74 ? 218 SER A CA    1 
ATOM   1671 C C     . SER A 1 224 ? 10.578  -5.697  -31.474 1.00 27.87 ? 218 SER A C     1 
ATOM   1672 O O     . SER A 1 224 ? 10.562  -4.726  -30.716 1.00 32.53 ? 218 SER A O     1 
ATOM   1673 C CB    . SER A 1 224 ? 8.962   -7.542  -30.986 1.00 35.06 ? 218 SER A CB    1 
ATOM   1674 O OG    . SER A 1 224 ? 8.162   -6.651  -30.232 1.00 45.08 ? 218 SER A OG    1 
ATOM   1675 N N     . ASP A 1 225 ? 10.772  -5.589  -32.783 1.00 29.00 ? 219 ASP A N     1 
ATOM   1676 C CA    . ASP A 1 225 ? 10.863  -4.264  -33.373 1.00 31.64 ? 219 ASP A CA    1 
ATOM   1677 C C     . ASP A 1 225 ? 9.494   -3.623  -33.526 1.00 27.72 ? 219 ASP A C     1 
ATOM   1678 O O     . ASP A 1 225 ? 9.399   -2.456  -33.896 1.00 29.35 ? 219 ASP A O     1 
ATOM   1679 C CB    . ASP A 1 225 ? 11.609  -4.331  -34.710 1.00 37.95 ? 219 ASP A CB    1 
ATOM   1680 C CG    . ASP A 1 225 ? 10.902  -5.176  -35.742 1.00 47.23 ? 219 ASP A CG    1 
ATOM   1681 O OD1   . ASP A 1 225 ? 11.306  -5.110  -36.925 1.00 52.97 ? 219 ASP A OD1   1 
ATOM   1682 O OD2   . ASP A 1 225 ? 9.946   -5.893  -35.387 1.00 49.07 ? 219 ASP A OD2   1 
ATOM   1683 N N     . LYS A 1 226 ? 8.440   -4.350  -33.214 1.00 31.34 ? 220 LYS A N     1 
ATOM   1684 C CA    . LYS A 1 226 ? 7.086   -3.831  -33.200 1.00 34.81 ? 220 LYS A CA    1 
ATOM   1685 C C     . LYS A 1 226 ? 6.447   -4.244  -31.887 1.00 34.49 ? 220 LYS A C     1 
ATOM   1686 O O     . LYS A 1 226 ? 6.706   -5.342  -31.392 1.00 31.21 ? 220 LYS A O     1 
ATOM   1687 C CB    . LYS A 1 226 ? 6.288   -4.376  -34.380 1.00 35.31 ? 220 LYS A CB    1 
ATOM   1688 C CG    . LYS A 1 226 ? 4.829   -4.031  -34.362 1.00 39.36 ? 220 LYS A CG    1 
ATOM   1689 C CD    . LYS A 1 226 ? 4.163   -4.510  -35.629 1.00 41.11 ? 220 LYS A CD    1 
ATOM   1690 C CE    . LYS A 1 226 ? 2.669   -4.254  -35.593 1.00 41.05 ? 220 LYS A CE    1 
ATOM   1691 N NZ    . LYS A 1 226 ? 2.027   -4.787  -36.820 1.00 44.38 ? 220 LYS A NZ    1 
ATOM   1692 N N     . LYS A 1 227 ? 5.653   -3.351  -31.304 1.00 36.07 ? 221 LYS A N     1 
ATOM   1693 C CA    . LYS A 1 227 ? 4.881   -3.691  -30.117 1.00 33.54 ? 221 LYS A CA    1 
ATOM   1694 C C     . LYS A 1 227 ? 3.677   -4.530  -30.530 1.00 31.12 ? 221 LYS A C     1 
ATOM   1695 O O     . LYS A 1 227 ? 2.792   -4.045  -31.247 1.00 32.32 ? 221 LYS A O     1 
ATOM   1696 C CB    . LYS A 1 227 ? 4.438   -2.428  -29.385 1.00 38.66 ? 221 LYS A CB    1 
ATOM   1697 C CG    . LYS A 1 227 ? 3.280   -2.626  -28.418 1.00 38.32 ? 221 LYS A CG    1 
ATOM   1698 C CD    . LYS A 1 227 ? 3.671   -3.484  -27.238 1.00 39.78 ? 221 LYS A CD    1 
ATOM   1699 C CE    . LYS A 1 227 ? 2.510   -3.638  -26.271 1.00 46.35 ? 221 LYS A CE    1 
ATOM   1700 N NZ    . LYS A 1 227 ? 2.930   -4.358  -25.035 1.00 55.97 ? 221 LYS A NZ    1 
ATOM   1701 N N     . TYR A 1 228 ? 3.654   -5.786  -30.087 1.00 28.16 ? 222 TYR A N     1 
ATOM   1702 C CA    . TYR A 1 228 ? 2.532   -6.684  -30.311 1.00 27.00 ? 222 TYR A CA    1 
ATOM   1703 C C     . TYR A 1 228 ? 1.761   -6.817  -29.008 1.00 26.36 ? 222 TYR A C     1 
ATOM   1704 O O     . TYR A 1 228 ? 2.357   -7.024  -27.947 1.00 29.00 ? 222 TYR A O     1 
ATOM   1705 C CB    . TYR A 1 228 ? 3.004   -8.059  -30.796 1.00 26.88 ? 222 TYR A CB    1 
ATOM   1706 C CG    . TYR A 1 228 ? 3.671   -8.029  -32.151 1.00 23.63 ? 222 TYR A CG    1 
ATOM   1707 C CD1   . TYR A 1 228 ? 2.909   -8.010  -33.309 1.00 27.73 ? 222 TYR A CD1   1 
ATOM   1708 C CD2   . TYR A 1 228 ? 5.054   -8.018  -32.275 1.00 27.43 ? 222 TYR A CD2   1 
ATOM   1709 C CE1   . TYR A 1 228 ? 3.491   -7.972  -34.556 1.00 33.76 ? 222 TYR A CE1   1 
ATOM   1710 C CE2   . TYR A 1 228 ? 5.647   -7.988  -33.528 1.00 27.08 ? 222 TYR A CE2   1 
ATOM   1711 C CZ    . TYR A 1 228 ? 4.860   -7.962  -34.661 1.00 36.49 ? 222 TYR A CZ    1 
ATOM   1712 O OH    . TYR A 1 228 ? 5.432   -7.935  -35.918 1.00 39.89 ? 222 TYR A OH    1 
ATOM   1713 N N     . HIS A 1 229 ? 0.442   -6.673  -29.081 1.00 24.85 ? 223 HIS A N     1 
ATOM   1714 C CA    . HIS A 1 229 ? -0.395  -6.821  -27.900 1.00 23.50 ? 223 HIS A CA    1 
ATOM   1715 C C     . HIS A 1 229 ? -0.863  -8.262  -27.773 1.00 26.42 ? 223 HIS A C     1 
ATOM   1716 O O     . HIS A 1 229 ? -1.333  -8.859  -28.748 1.00 25.18 ? 223 HIS A O     1 
ATOM   1717 C CB    . HIS A 1 229 ? -1.582  -5.868  -27.979 1.00 25.09 ? 223 HIS A CB    1 
ATOM   1718 C CG    . HIS A 1 229 ? -1.179  -4.430  -28.057 1.00 26.91 ? 223 HIS A CG    1 
ATOM   1719 N ND1   . HIS A 1 229 ? -0.864  -3.685  -26.939 1.00 31.58 ? 223 HIS A ND1   1 
ATOM   1720 C CD2   . HIS A 1 229 ? -1.031  -3.600  -29.118 1.00 26.88 ? 223 HIS A CD2   1 
ATOM   1721 C CE1   . HIS A 1 229 ? -0.554  -2.452  -27.309 1.00 33.89 ? 223 HIS A CE1   1 
ATOM   1722 N NE2   . HIS A 1 229 ? -0.642  -2.377  -28.625 1.00 33.59 ? 223 HIS A NE2   1 
ATOM   1723 N N     . PHE A 1 230 ? -0.721  -8.815  -26.568 1.00 23.44 ? 224 PHE A N     1 
ATOM   1724 C CA    . PHE A 1 230 ? -1.054  -10.211 -26.329 1.00 22.73 ? 224 PHE A CA    1 
ATOM   1725 C C     . PHE A 1 230 ? -2.500  -10.514 -26.707 1.00 23.61 ? 224 PHE A C     1 
ATOM   1726 O O     . PHE A 1 230 ? -3.421  -9.757  -26.362 1.00 26.37 ? 224 PHE A O     1 
ATOM   1727 C CB    . PHE A 1 230 ? -0.808  -10.553 -24.860 1.00 23.78 ? 224 PHE A CB    1 
ATOM   1728 C CG    . PHE A 1 230 ? -0.968  -12.016 -24.547 1.00 26.72 ? 224 PHE A CG    1 
ATOM   1729 C CD1   . PHE A 1 230 ? -2.073  -12.471 -23.852 1.00 33.04 ? 224 PHE A CD1   1 
ATOM   1730 C CD2   . PHE A 1 230 ? -0.016  -12.934 -24.951 1.00 23.96 ? 224 PHE A CD2   1 
ATOM   1731 C CE1   . PHE A 1 230 ? -2.218  -13.824 -23.564 1.00 33.00 ? 224 PHE A CE1   1 
ATOM   1732 C CE2   . PHE A 1 230 ? -0.161  -14.284 -24.672 1.00 26.20 ? 224 PHE A CE2   1 
ATOM   1733 C CZ    . PHE A 1 230 ? -1.254  -14.726 -23.974 1.00 26.98 ? 224 PHE A CZ    1 
ATOM   1734 N N     . ALA A 1 231 ? -2.679  -11.625 -27.426 1.00 22.72 ? 225 ALA A N     1 
ATOM   1735 C CA    . ALA A 1 231 ? -3.961  -12.193 -27.849 1.00 23.39 ? 225 ALA A CA    1 
ATOM   1736 C C     . ALA A 1 231 ? -4.674  -11.340 -28.889 1.00 28.01 ? 225 ALA A C     1 
ATOM   1737 O O     . ALA A 1 231 ? -5.845  -11.598 -29.187 1.00 28.31 ? 225 ALA A O     1 
ATOM   1738 C CB    . ALA A 1 231 ? -4.901  -12.454 -26.663 1.00 31.02 ? 225 ALA A CB    1 
ATOM   1739 N N     . LYS A 1 232 ? -4.008  -10.328 -29.446 1.00 25.07 ? 226 LYS A N     1 
ATOM   1740 C CA    . LYS A 1 232 ? -4.632  -9.667  -30.588 1.00 25.17 ? 226 LYS A CA    1 
ATOM   1741 C C     . LYS A 1 232 ? -4.140  -10.298 -31.885 1.00 24.56 ? 226 LYS A C     1 
ATOM   1742 O O     . LYS A 1 232 ? -2.965  -10.677 -31.983 1.00 24.06 ? 226 LYS A O     1 
ATOM   1743 C CB    . LYS A 1 232 ? -4.307  -8.179  -30.602 1.00 27.06 ? 226 LYS A CB    1 
ATOM   1744 C CG    . LYS A 1 232 ? -4.922  -7.385  -29.458 1.00 30.89 ? 226 LYS A CG    1 
ATOM   1745 C CD    . LYS A 1 232 ? -6.325  -6.947  -29.801 1.00 32.97 ? 226 LYS A CD    1 
ATOM   1746 C CE    . LYS A 1 232 ? -6.888  -5.968  -28.774 1.00 38.25 ? 226 LYS A CE    1 
ATOM   1747 N NZ    . LYS A 1 232 ? -7.217  -6.653  -27.506 1.00 45.20 ? 226 LYS A NZ    1 
ATOM   1748 N N     . PRO A 1 233 ? -5.009  -10.421 -32.887 1.00 25.52 ? 227 PRO A N     1 
ATOM   1749 C CA    . PRO A 1 233 ? -4.590  -11.020 -34.157 1.00 26.46 ? 227 PRO A CA    1 
ATOM   1750 C C     . PRO A 1 233 ? -3.739  -10.060 -34.970 1.00 24.36 ? 227 PRO A C     1 
ATOM   1751 O O     . PRO A 1 233 ? -3.967  -8.849  -34.969 1.00 25.52 ? 227 PRO A O     1 
ATOM   1752 C CB    . PRO A 1 233 ? -5.920  -11.306 -34.861 1.00 27.19 ? 227 PRO A CB    1 
ATOM   1753 C CG    . PRO A 1 233 ? -6.848  -10.246 -34.327 1.00 26.59 ? 227 PRO A CG    1 
ATOM   1754 C CD    . PRO A 1 233 ? -6.446  -10.090 -32.877 1.00 24.52 ? 227 PRO A CD    1 
ATOM   1755 N N     . TYR A 1 234 ? -2.746  -10.615 -35.670 1.00 24.00 ? 228 TYR A N     1 
ATOM   1756 C CA    . TYR A 1 234 ? -1.880  -9.853  -36.564 1.00 24.86 ? 228 TYR A CA    1 
ATOM   1757 C C     . TYR A 1 234 ? -1.732  -10.601 -37.882 1.00 23.62 ? 228 TYR A C     1 
ATOM   1758 O O     . TYR A 1 234 ? -1.433  -11.802 -37.885 1.00 24.46 ? 228 TYR A O     1 
ATOM   1759 C CB    . TYR A 1 234 ? -0.495  -9.606  -35.936 1.00 22.55 ? 228 TYR A CB    1 
ATOM   1760 C CG    . TYR A 1 234 ? -0.539  -8.630  -34.775 1.00 22.86 ? 228 TYR A CG    1 
ATOM   1761 C CD1   . TYR A 1 234 ? -0.443  -7.265  -34.990 1.00 24.02 ? 228 TYR A CD1   1 
ATOM   1762 C CD2   . TYR A 1 234 ? -0.693  -9.085  -33.468 1.00 23.39 ? 228 TYR A CD2   1 
ATOM   1763 C CE1   . TYR A 1 234 ? -0.496  -6.365  -33.937 1.00 25.02 ? 228 TYR A CE1   1 
ATOM   1764 C CE2   . TYR A 1 234 ? -0.751  -8.186  -32.406 1.00 23.26 ? 228 TYR A CE2   1 
ATOM   1765 C CZ    . TYR A 1 234 ? -0.648  -6.835  -32.646 1.00 23.69 ? 228 TYR A CZ    1 
ATOM   1766 O OH    . TYR A 1 234 ? -0.710  -5.919  -31.603 1.00 26.07 ? 228 TYR A OH    1 
ATOM   1767 N N     . LYS A 1 235 ? -1.941  -9.885  -38.993 1.00 25.70 ? 229 LYS A N     1 
ATOM   1768 C CA    . LYS A 1 235 ? -1.852  -10.502 -40.317 1.00 28.98 ? 229 LYS A CA    1 
ATOM   1769 C C     . LYS A 1 235 ? -0.558  -11.290 -40.491 1.00 28.85 ? 229 LYS A C     1 
ATOM   1770 O O     . LYS A 1 235 ? -0.570  -12.425 -40.983 1.00 29.00 ? 229 LYS A O     1 
ATOM   1771 C CB    . LYS A 1 235 ? -1.959  -9.437  -41.407 1.00 31.14 ? 229 LYS A CB    1 
ATOM   1772 C CG    . LYS A 1 235 ? -1.738  -10.004 -42.795 1.00 36.57 ? 229 LYS A CG    1 
ATOM   1773 N N     . GLU A 1 236 ? 0.573   -10.708 -40.080 1.00 28.48 ? 230 GLU A N     1 
ATOM   1774 C CA    . GLU A 1 236 ? 1.853   -11.371 -40.308 1.00 30.25 ? 230 GLU A CA    1 
ATOM   1775 C C     . GLU A 1 236 ? 1.973   -12.651 -39.491 1.00 31.19 ? 230 GLU A C     1 
ATOM   1776 O O     . GLU A 1 236 ? 2.645   -13.595 -39.921 1.00 29.05 ? 230 GLU A O     1 
ATOM   1777 C CB    . GLU A 1 236 ? 3.013   -10.422 -39.993 1.00 36.15 ? 230 GLU A CB    1 
ATOM   1778 C CG    . GLU A 1 236 ? 3.020   -9.873  -38.578 1.00 36.12 ? 230 GLU A CG    1 
ATOM   1779 C CD    . GLU A 1 236 ? 2.464   -8.456  -38.481 1.00 45.12 ? 230 GLU A CD    1 
ATOM   1780 O OE1   . GLU A 1 236 ? 3.167   -7.585  -37.919 1.00 47.07 ? 230 GLU A OE1   1 
ATOM   1781 O OE2   . GLU A 1 236 ? 1.332   -8.207  -38.965 1.00 44.02 ? 230 GLU A OE2   1 
ATOM   1782 N N     . PHE A 1 237 ? 1.320   -12.708 -38.330 1.00 25.15 ? 231 PHE A N     1 
ATOM   1783 C CA    . PHE A 1 237 ? 1.323   -13.936 -37.533 1.00 22.54 ? 231 PHE A CA    1 
ATOM   1784 C C     . PHE A 1 237 ? 0.510   -15.035 -38.207 1.00 23.63 ? 231 PHE A C     1 
ATOM   1785 O O     . PHE A 1 237 ? 0.917   -16.203 -38.215 1.00 22.73 ? 231 PHE A O     1 
ATOM   1786 C CB    . PHE A 1 237 ? 0.770   -13.674 -36.134 1.00 24.28 ? 231 PHE A CB    1 
ATOM   1787 C CG    . PHE A 1 237 ? 1.663   -12.839 -35.250 1.00 25.68 ? 231 PHE A CG    1 
ATOM   1788 C CD1   . PHE A 1 237 ? 2.920   -12.435 -35.666 1.00 29.60 ? 231 PHE A CD1   1 
ATOM   1789 C CD2   . PHE A 1 237 ? 1.234   -12.476 -33.987 1.00 31.86 ? 231 PHE A CD2   1 
ATOM   1790 C CE1   . PHE A 1 237 ? 3.726   -11.675 -34.837 1.00 28.49 ? 231 PHE A CE1   1 
ATOM   1791 C CE2   . PHE A 1 237 ? 2.036   -11.711 -33.161 1.00 32.09 ? 231 PHE A CE2   1 
ATOM   1792 C CZ    . PHE A 1 237 ? 3.278   -11.315 -33.591 1.00 29.45 ? 231 PHE A CZ    1 
ATOM   1793 N N     . TYR A 1 238 ? -0.659  -14.691 -38.752 1.00 23.77 ? 232 TYR A N     1 
ATOM   1794 C CA    . TYR A 1 238 ? -1.466  -15.696 -39.437 1.00 27.59 ? 232 TYR A CA    1 
ATOM   1795 C C     . TYR A 1 238 ? -0.726  -16.244 -40.644 1.00 28.39 ? 232 TYR A C     1 
ATOM   1796 O O     . TYR A 1 238 ? -0.745  -17.454 -40.903 1.00 26.34 ? 232 TYR A O     1 
ATOM   1797 C CB    . TYR A 1 238 ? -2.812  -15.106 -39.866 1.00 29.31 ? 232 TYR A CB    1 
ATOM   1798 C CG    . TYR A 1 238 ? -3.751  -16.147 -40.441 1.00 31.22 ? 232 TYR A CG    1 
ATOM   1799 C CD1   . TYR A 1 238 ? -3.989  -16.230 -41.804 1.00 36.63 ? 232 TYR A CD1   1 
ATOM   1800 C CD2   . TYR A 1 238 ? -4.377  -17.068 -39.609 1.00 33.77 ? 232 TYR A CD2   1 
ATOM   1801 C CE1   . TYR A 1 238 ? -4.846  -17.193 -42.323 1.00 41.18 ? 232 TYR A CE1   1 
ATOM   1802 C CE2   . TYR A 1 238 ? -5.226  -18.029 -40.115 1.00 36.60 ? 232 TYR A CE2   1 
ATOM   1803 C CZ    . TYR A 1 238 ? -5.460  -18.089 -41.467 1.00 43.47 ? 232 TYR A CZ    1 
ATOM   1804 O OH    . TYR A 1 238 ? -6.308  -19.056 -41.958 1.00 49.64 ? 232 TYR A OH    1 
ATOM   1805 N N     . GLU A 1 239 ? -0.027  -15.371 -41.368 1.00 25.27 ? 233 GLU A N     1 
ATOM   1806 C CA    . GLU A 1 239 ? 0.686   -15.805 -42.562 1.00 29.95 ? 233 GLU A CA    1 
ATOM   1807 C C     . GLU A 1 239 ? 1.847   -16.721 -42.211 1.00 29.40 ? 233 GLU A C     1 
ATOM   1808 O O     . GLU A 1 239 ? 2.063   -17.737 -42.880 1.00 30.70 ? 233 GLU A O     1 
ATOM   1809 C CB    . GLU A 1 239 ? 1.161   -14.586 -43.344 1.00 34.50 ? 233 GLU A CB    1 
ATOM   1810 C CG    . GLU A 1 239 ? 0.004   -13.776 -43.908 1.00 42.35 ? 233 GLU A CG    1 
ATOM   1811 C CD    . GLU A 1 239 ? 0.457   -12.536 -44.649 1.00 48.61 ? 233 GLU A CD    1 
ATOM   1812 O OE1   . GLU A 1 239 ? -0.357  -11.975 -45.414 1.00 53.91 ? 233 GLU A OE1   1 
ATOM   1813 O OE2   . GLU A 1 239 ? 1.624   -12.123 -44.462 1.00 53.39 ? 233 GLU A OE2   1 
ATOM   1814 N N     . LEU A 1 240 ? 2.597   -16.384 -41.163 1.00 25.74 ? 234 LEU A N     1 
ATOM   1815 C CA    . LEU A 1 240 ? 3.686   -17.249 -40.726 1.00 26.78 ? 234 LEU A CA    1 
ATOM   1816 C C     . LEU A 1 240 ? 3.156   -18.585 -40.222 1.00 24.34 ? 234 LEU A C     1 
ATOM   1817 O O     . LEU A 1 240 ? 3.715   -19.643 -40.537 1.00 21.99 ? 234 LEU A O     1 
ATOM   1818 C CB    . LEU A 1 240 ? 4.494   -16.549 -39.639 1.00 23.68 ? 234 LEU A CB    1 
ATOM   1819 C CG    . LEU A 1 240 ? 5.676   -17.317 -39.059 1.00 24.57 ? 234 LEU A CG    1 
ATOM   1820 C CD1   . LEU A 1 240 ? 6.651   -17.667 -40.175 1.00 22.34 ? 234 LEU A CD1   1 
ATOM   1821 C CD2   . LEU A 1 240 ? 6.348   -16.454 -38.000 1.00 26.59 ? 234 LEU A CD2   1 
ATOM   1822 N N     . TYR A 1 241 ? 2.082   -18.546 -39.431 1.00 22.60 ? 235 TYR A N     1 
ATOM   1823 C CA    . TYR A 1 241 ? 1.434   -19.758 -38.945 1.00 21.75 ? 235 TYR A CA    1 
ATOM   1824 C C     . TYR A 1 241 ? 1.036   -20.666 -40.102 1.00 20.16 ? 235 TYR A C     1 
ATOM   1825 O O     . TYR A 1 241 ? 1.309   -21.872 -40.084 1.00 23.91 ? 235 TYR A O     1 
ATOM   1826 C CB    . TYR A 1 241 ? 0.213   -19.354 -38.111 1.00 21.42 ? 235 TYR A CB    1 
ATOM   1827 C CG    . TYR A 1 241 ? -0.805  -20.435 -37.831 1.00 21.25 ? 235 TYR A CG    1 
ATOM   1828 C CD1   . TYR A 1 241 ? -1.938  -20.565 -38.620 1.00 24.93 ? 235 TYR A CD1   1 
ATOM   1829 C CD2   . TYR A 1 241 ? -0.647  -21.309 -36.750 1.00 23.65 ? 235 TYR A CD2   1 
ATOM   1830 C CE1   . TYR A 1 241 ? -2.887  -21.540 -38.355 1.00 32.31 ? 235 TYR A CE1   1 
ATOM   1831 C CE2   . TYR A 1 241 ? -1.588  -22.287 -36.489 1.00 24.39 ? 235 TYR A CE2   1 
ATOM   1832 C CZ    . TYR A 1 241 ? -2.703  -22.395 -37.292 1.00 35.77 ? 235 TYR A CZ    1 
ATOM   1833 O OH    . TYR A 1 241 ? -3.643  -23.367 -37.029 1.00 36.75 ? 235 TYR A OH    1 
ATOM   1834 N N     . MET A 1 242 ? 0.384   -20.098 -41.123 1.00 21.50 ? 236 MET A N     1 
ATOM   1835 C CA    . MET A 1 242 ? -0.088  -20.913 -42.241 1.00 24.10 ? 236 MET A CA    1 
ATOM   1836 C C     . MET A 1 242 ? 1.069   -21.450 -43.073 1.00 26.65 ? 236 MET A C     1 
ATOM   1837 O O     . MET A 1 242 ? 1.011   -22.587 -43.552 1.00 28.54 ? 236 MET A O     1 
ATOM   1838 C CB    . MET A 1 242 ? -1.036  -20.104 -43.119 1.00 30.45 ? 236 MET A CB    1 
ATOM   1839 C CG    . MET A 1 242 ? -2.343  -19.763 -42.451 1.00 31.04 ? 236 MET A CG    1 
ATOM   1840 S SD    . MET A 1 242 ? -3.313  -21.233 -42.083 1.00 36.13 ? 236 MET A SD    1 
ATOM   1841 C CE    . MET A 1 242 ? -3.623  -21.867 -43.728 1.00 43.75 ? 236 MET A CE    1 
ATOM   1842 N N     . ASP A 1 243 ? 2.111   -20.639 -43.281 1.00 25.35 ? 237 ASP A N     1 
ATOM   1843 C CA    . ASP A 1 243 ? 3.298   -21.108 -43.993 1.00 29.05 ? 237 ASP A CA    1 
ATOM   1844 C C     . ASP A 1 243 ? 3.962   -22.275 -43.264 1.00 26.40 ? 237 ASP A C     1 
ATOM   1845 O O     . ASP A 1 243 ? 4.345   -23.273 -43.885 1.00 28.51 ? 237 ASP A O     1 
ATOM   1846 C CB    . ASP A 1 243 ? 4.306   -19.971 -44.158 1.00 33.69 ? 237 ASP A CB    1 
ATOM   1847 C CG    . ASP A 1 243 ? 3.917   -18.983 -45.236 1.00 42.90 ? 237 ASP A CG    1 
ATOM   1848 O OD1   . ASP A 1 243 ? 2.898   -19.203 -45.929 1.00 43.98 ? 237 ASP A OD1   1 
ATOM   1849 O OD2   . ASP A 1 243 ? 4.642   -17.976 -45.377 1.00 43.36 ? 237 ASP A OD2   1 
ATOM   1850 N N     . LEU A 1 244 ? 4.139   -22.162 -41.946 1.00 25.51 ? 238 LEU A N     1 
ATOM   1851 C CA    . LEU A 1 244 ? 4.779   -23.257 -41.221 1.00 24.28 ? 238 LEU A CA    1 
ATOM   1852 C C     . LEU A 1 244 ? 3.917   -24.511 -41.266 1.00 25.93 ? 238 LEU A C     1 
ATOM   1853 O O     . LEU A 1 244 ? 4.432   -25.626 -41.410 1.00 24.55 ? 238 LEU A O     1 
ATOM   1854 C CB    . LEU A 1 244 ? 5.066   -22.838 -39.780 1.00 22.80 ? 238 LEU A CB    1 
ATOM   1855 C CG    . LEU A 1 244 ? 6.199   -21.819 -39.702 1.00 28.93 ? 238 LEU A CG    1 
ATOM   1856 C CD1   . LEU A 1 244 ? 6.250   -21.137 -38.345 1.00 23.64 ? 238 LEU A CD1   1 
ATOM   1857 C CD2   . LEU A 1 244 ? 7.518   -22.509 -40.043 1.00 28.29 ? 238 LEU A CD2   1 
ATOM   1858 N N     . LYS A 1 245 ? 2.600   -24.344 -41.161 1.00 23.94 ? 239 LYS A N     1 
ATOM   1859 C CA    . LYS A 1 245 ? 1.677   -25.472 -41.235 1.00 25.09 ? 239 LYS A CA    1 
ATOM   1860 C C     . LYS A 1 245 ? 1.683   -26.121 -42.615 1.00 28.29 ? 239 LYS A C     1 
ATOM   1861 O O     . LYS A 1 245 ? 1.829   -27.343 -42.744 1.00 31.28 ? 239 LYS A O     1 
ATOM   1862 C CB    . LYS A 1 245 ? 0.276   -24.980 -40.876 1.00 32.68 ? 239 LYS A CB    1 
ATOM   1863 C CG    . LYS A 1 245 ? -0.723  -26.042 -40.509 1.00 40.38 ? 239 LYS A CG    1 
ATOM   1864 C CD    . LYS A 1 245 ? -1.859  -25.399 -39.729 1.00 43.65 ? 239 LYS A CD    1 
ATOM   1865 C CE    . LYS A 1 245 ? -3.191  -26.005 -40.090 1.00 45.92 ? 239 LYS A CE    1 
ATOM   1866 N NZ    . LYS A 1 245 ? -4.308  -25.100 -39.694 1.00 50.81 ? 239 LYS A NZ    1 
ATOM   1867 N N     . LEU A 1 246 ? 1.515   -25.325 -43.669 1.00 27.61 ? 240 LEU A N     1 
ATOM   1868 C CA    . LEU A 1 246 ? 1.366   -25.911 -44.999 1.00 29.82 ? 240 LEU A CA    1 
ATOM   1869 C C     . LEU A 1 246 ? 2.693   -26.415 -45.557 1.00 29.97 ? 240 LEU A C     1 
ATOM   1870 O O     . LEU A 1 246 ? 2.736   -27.470 -46.200 1.00 34.46 ? 240 LEU A O     1 
ATOM   1871 C CB    . LEU A 1 246 ? 0.724   -24.895 -45.946 1.00 29.82 ? 240 LEU A CB    1 
ATOM   1872 C CG    . LEU A 1 246 ? -0.663  -24.409 -45.487 1.00 43.19 ? 240 LEU A CG    1 
ATOM   1873 C CD1   . LEU A 1 246 ? -1.264  -23.378 -46.443 1.00 44.20 ? 240 LEU A CD1   1 
ATOM   1874 C CD2   . LEU A 1 246 ? -1.621  -25.573 -45.273 1.00 45.71 ? 240 LEU A CD2   1 
ATOM   1875 N N     . LYS A 1 247 ? 3.786   -25.691 -45.329 1.00 29.48 ? 241 LYS A N     1 
ATOM   1876 C CA    . LYS A 1 247 ? 5.057   -26.055 -45.950 1.00 29.09 ? 241 LYS A CA    1 
ATOM   1877 C C     . LYS A 1 247 ? 5.894   -27.014 -45.116 1.00 29.01 ? 241 LYS A C     1 
ATOM   1878 O O     . LYS A 1 247 ? 6.702   -27.762 -45.681 1.00 31.91 ? 241 LYS A O     1 
ATOM   1879 C CB    . LYS A 1 247 ? 5.873   -24.795 -46.247 1.00 28.96 ? 241 LYS A CB    1 
ATOM   1880 C CG    . LYS A 1 247 ? 5.138   -23.841 -47.166 1.00 38.74 ? 241 LYS A CG    1 
ATOM   1881 C CD    . LYS A 1 247 ? 5.905   -22.560 -47.404 1.00 40.08 ? 241 LYS A CD    1 
ATOM   1882 C CE    . LYS A 1 247 ? 5.144   -21.671 -48.368 1.00 47.92 ? 241 LYS A CE    1 
ATOM   1883 N NZ    . LYS A 1 247 ? 6.085   -20.930 -49.233 1.00 45.86 ? 241 LYS A NZ    1 
ATOM   1884 N N     . CYS A 1 248 ? 5.714   -27.022 -43.795 1.00 27.96 ? 242 CYS A N     1 
ATOM   1885 C CA    . CYS A 1 248 ? 6.508   -27.854 -42.897 1.00 27.03 ? 242 CYS A CA    1 
ATOM   1886 C C     . CYS A 1 248 ? 5.696   -28.834 -42.067 1.00 25.30 ? 242 CYS A C     1 
ATOM   1887 O O     . CYS A 1 248 ? 6.294   -29.645 -41.351 1.00 26.56 ? 242 CYS A O     1 
ATOM   1888 C CB    . CYS A 1 248 ? 7.323   -26.978 -41.935 1.00 29.28 ? 242 CYS A CB    1 
ATOM   1889 S SG    . CYS A 1 248 ? 8.563   -25.989 -42.756 1.00 34.11 ? 242 CYS A SG    1 
ATOM   1890 N N     . ASN A 1 249 ? 4.371   -28.793 -42.150 1.00 23.30 ? 243 ASN A N     1 
ATOM   1891 C CA    . ASN A 1 249 ? 3.490   -29.592 -41.297 1.00 23.17 ? 243 ASN A CA    1 
ATOM   1892 C C     . ASN A 1 249 ? 3.854   -29.448 -39.828 1.00 22.40 ? 243 ASN A C     1 
ATOM   1893 O O     . ASN A 1 249 ? 3.837   -30.416 -39.070 1.00 24.48 ? 243 ASN A O     1 
ATOM   1894 C CB    . ASN A 1 249 ? 3.482   -31.070 -41.698 1.00 24.04 ? 243 ASN A CB    1 
ATOM   1895 C CG    . ASN A 1 249 ? 2.377   -31.855 -40.983 1.00 31.77 ? 243 ASN A CG    1 
ATOM   1896 O OD1   . ASN A 1 249 ? 1.261   -31.362 -40.835 1.00 30.40 ? 243 ASN A OD1   1 
ATOM   1897 N ND2   . ASN A 1 249 ? 2.696   -33.061 -40.517 1.00 39.63 ? 243 ASN A ND2   1 
ATOM   1898 N N     . ILE A 1 250 ? 4.182   -28.226 -39.411 1.00 19.15 ? 244 ILE A N     1 
ATOM   1899 C CA    . ILE A 1 250 ? 4.363   -27.924 -37.996 1.00 21.83 ? 244 ILE A CA    1 
ATOM   1900 C C     . ILE A 1 250 ? 3.384   -26.820 -37.631 1.00 20.58 ? 244 ILE A C     1 
ATOM   1901 O O     . ILE A 1 250 ? 3.530   -25.677 -38.085 1.00 24.32 ? 244 ILE A O     1 
ATOM   1902 C CB    . ILE A 1 250 ? 5.800   -27.503 -37.666 1.00 19.22 ? 244 ILE A CB    1 
ATOM   1903 C CG1   . ILE A 1 250 ? 6.781   -28.568 -38.146 1.00 21.67 ? 244 ILE A CG1   1 
ATOM   1904 C CG2   . ILE A 1 250 ? 5.954   -27.299 -36.148 1.00 19.03 ? 244 ILE A CG2   1 
ATOM   1905 C CD1   . ILE A 1 250 ? 8.242   -28.212 -37.894 1.00 19.72 ? 244 ILE A CD1   1 
ATOM   1906 N N     . GLU A 1 251 ? 2.400   -27.146 -36.799 1.00 21.50 ? 245 GLU A N     1 
ATOM   1907 C CA    . GLU A 1 251 ? 1.485   -26.137 -36.277 1.00 18.41 ? 245 GLU A CA    1 
ATOM   1908 C C     . GLU A 1 251 ? 2.064   -25.550 -34.996 1.00 20.08 ? 245 GLU A C     1 
ATOM   1909 O O     . GLU A 1 251 ? 2.613   -26.277 -34.161 1.00 19.96 ? 245 GLU A O     1 
ATOM   1910 C CB    . GLU A 1 251 ? 0.096   -26.728 -36.010 1.00 23.14 ? 245 GLU A CB    1 
ATOM   1911 C CG    . GLU A 1 251 ? -0.898  -25.683 -35.507 1.00 27.40 ? 245 GLU A CG    1 
ATOM   1912 C CD    . GLU A 1 251 ? -2.358  -26.119 -35.534 1.00 31.62 ? 245 GLU A CD    1 
ATOM   1913 O OE1   . GLU A 1 251 ? -3.207  -25.306 -35.081 1.00 26.86 ? 245 GLU A OE1   1 
ATOM   1914 O OE2   . GLU A 1 251 ? -2.655  -27.253 -35.992 1.00 32.85 ? 245 GLU A OE2   1 
ATOM   1915 N N     . PHE A 1 252 ? 1.970   -24.226 -34.868 1.00 21.86 ? 246 PHE A N     1 
ATOM   1916 C CA    . PHE A 1 252 ? 2.410   -23.506 -33.685 1.00 20.15 ? 246 PHE A CA    1 
ATOM   1917 C C     . PHE A 1 252 ? 1.236   -22.808 -33.023 1.00 21.12 ? 246 PHE A C     1 
ATOM   1918 O O     . PHE A 1 252 ? 0.264   -22.417 -33.676 1.00 23.46 ? 246 PHE A O     1 
ATOM   1919 C CB    . PHE A 1 252 ? 3.468   -22.457 -34.018 1.00 20.79 ? 246 PHE A CB    1 
ATOM   1920 C CG    . PHE A 1 252 ? 4.825   -23.029 -34.279 1.00 19.63 ? 246 PHE A CG    1 
ATOM   1921 C CD1   . PHE A 1 252 ? 5.704   -23.256 -33.224 1.00 18.33 ? 246 PHE A CD1   1 
ATOM   1922 C CD2   . PHE A 1 252 ? 5.234   -23.339 -35.578 1.00 21.75 ? 246 PHE A CD2   1 
ATOM   1923 C CE1   . PHE A 1 252 ? 6.974   -23.782 -33.458 1.00 20.53 ? 246 PHE A CE1   1 
ATOM   1924 C CE2   . PHE A 1 252 ? 6.494   -23.872 -35.815 1.00 22.26 ? 246 PHE A CE2   1 
ATOM   1925 C CZ    . PHE A 1 252 ? 7.368   -24.080 -34.756 1.00 23.27 ? 246 PHE A CZ    1 
ATOM   1926 N N     . ASP A 1 253 ? 1.355   -22.648 -31.712 1.00 20.38 ? 247 ASP A N     1 
ATOM   1927 C CA    . ASP A 1 253 ? 0.422   -21.833 -30.959 1.00 17.60 ? 247 ASP A CA    1 
ATOM   1928 C C     . ASP A 1 253 ? 0.513   -20.372 -31.392 1.00 19.18 ? 247 ASP A C     1 
ATOM   1929 O O     . ASP A 1 253 ? 1.606   -19.820 -31.556 1.00 22.66 ? 247 ASP A O     1 
ATOM   1930 C CB    . ASP A 1 253 ? 0.734   -21.960 -29.474 1.00 20.56 ? 247 ASP A CB    1 
ATOM   1931 C CG    . ASP A 1 253 ? 0.334   -20.727 -28.706 1.00 22.92 ? 247 ASP A CG    1 
ATOM   1932 O OD1   . ASP A 1 253 ? -0.873  -20.532 -28.509 1.00 26.56 ? 247 ASP A OD1   1 
ATOM   1933 O OD2   . ASP A 1 253 ? 1.223   -19.952 -28.318 1.00 24.40 ? 247 ASP A OD2   1 
ATOM   1934 N N     . LEU A 1 254 ? -0.651  -19.743 -31.567 1.00 21.37 ? 248 LEU A N     1 
ATOM   1935 C CA    . LEU A 1 254 ? -0.731  -18.374 -32.057 1.00 18.47 ? 248 LEU A CA    1 
ATOM   1936 C C     . LEU A 1 254 ? -0.593  -17.312 -30.970 1.00 22.49 ? 248 LEU A C     1 
ATOM   1937 O O     . LEU A 1 254 ? -0.410  -16.137 -31.312 1.00 26.82 ? 248 LEU A O     1 
ATOM   1938 C CB    . LEU A 1 254 ? -2.054  -18.182 -32.784 1.00 18.23 ? 248 LEU A CB    1 
ATOM   1939 C CG    . LEU A 1 254 ? -2.145  -18.872 -34.140 1.00 20.92 ? 248 LEU A CG    1 
ATOM   1940 C CD1   . LEU A 1 254 ? -3.595  -19.074 -34.518 1.00 21.54 ? 248 LEU A CD1   1 
ATOM   1941 C CD2   . LEU A 1 254 ? -1.507  -17.980 -35.167 1.00 20.71 ? 248 LEU A CD2   1 
ATOM   1942 N N     . LEU A 1 255 ? -0.693  -17.682 -29.686 1.00 21.22 ? 249 LEU A N     1 
ATOM   1943 C CA    . LEU A 1 255 ? -0.602  -16.704 -28.606 1.00 20.20 ? 249 LEU A CA    1 
ATOM   1944 C C     . LEU A 1 255 ? 0.839   -16.368 -28.246 1.00 22.84 ? 249 LEU A C     1 
ATOM   1945 O O     . LEU A 1 255 ? 1.163   -15.192 -28.017 1.00 22.70 ? 249 LEU A O     1 
ATOM   1946 C CB    . LEU A 1 255 ? -1.326  -17.210 -27.354 1.00 23.92 ? 249 LEU A CB    1 
ATOM   1947 C CG    . LEU A 1 255 ? -2.836  -17.167 -27.314 1.00 32.71 ? 249 LEU A CG    1 
ATOM   1948 C CD1   . LEU A 1 255 ? -3.295  -17.917 -26.068 1.00 36.07 ? 249 LEU A CD1   1 
ATOM   1949 C CD2   . LEU A 1 255 ? -3.311  -15.721 -27.272 1.00 36.32 ? 249 LEU A CD2   1 
ATOM   1950 N N     . TYR A 1 256 ? 1.711   -17.378 -28.182 1.00 19.97 ? 250 TYR A N     1 
ATOM   1951 C CA    . TYR A 1 256 ? 3.095   -17.204 -27.759 1.00 19.39 ? 250 TYR A CA    1 
ATOM   1952 C C     . TYR A 1 256 ? 4.095   -17.586 -28.836 1.00 19.82 ? 250 TYR A C     1 
ATOM   1953 O O     . TYR A 1 256 ? 5.026   -16.826 -29.125 1.00 19.41 ? 250 TYR A O     1 
ATOM   1954 C CB    . TYR A 1 256 ? 3.401   -18.054 -26.511 1.00 19.77 ? 250 TYR A CB    1 
ATOM   1955 C CG    . TYR A 1 256 ? 2.532   -17.826 -25.311 1.00 18.80 ? 250 TYR A CG    1 
ATOM   1956 C CD1   . TYR A 1 256 ? 2.901   -16.933 -24.328 1.00 18.00 ? 250 TYR A CD1   1 
ATOM   1957 C CD2   . TYR A 1 256 ? 1.384   -18.575 -25.124 1.00 22.51 ? 250 TYR A CD2   1 
ATOM   1958 C CE1   . TYR A 1 256 ? 2.133   -16.758 -23.206 1.00 20.81 ? 250 TYR A CE1   1 
ATOM   1959 C CE2   . TYR A 1 256 ? 0.613   -18.416 -24.016 1.00 24.33 ? 250 TYR A CE2   1 
ATOM   1960 C CZ    . TYR A 1 256 ? 0.989   -17.499 -23.054 1.00 26.79 ? 250 TYR A CZ    1 
ATOM   1961 O OH    . TYR A 1 256 ? 0.212   -17.334 -21.937 1.00 30.12 ? 250 TYR A OH    1 
ATOM   1962 N N     . ASP A 1 257 ? 3.956   -18.777 -29.420 1.00 18.70 ? 251 ASP A N     1 
ATOM   1963 C CA    . ASP A 1 257 ? 5.038   -19.274 -30.257 1.00 19.83 ? 251 ASP A CA    1 
ATOM   1964 C C     . ASP A 1 257 ? 5.164   -18.500 -31.563 1.00 20.35 ? 251 ASP A C     1 
ATOM   1965 O O     . ASP A 1 257 ? 6.275   -18.342 -32.072 1.00 21.12 ? 251 ASP A O     1 
ATOM   1966 C CB    . ASP A 1 257 ? 4.843   -20.765 -30.531 1.00 20.80 ? 251 ASP A CB    1 
ATOM   1967 C CG    . ASP A 1 257 ? 5.877   -21.630 -29.816 1.00 18.24 ? 251 ASP A CG    1 
ATOM   1968 O OD1   . ASP A 1 257 ? 6.889   -21.087 -29.295 1.00 16.69 ? 251 ASP A OD1   1 
ATOM   1969 O OD2   . ASP A 1 257 ? 5.650   -22.864 -29.770 1.00 16.24 ? 251 ASP A OD2   1 
ATOM   1970 N N     . ILE A 1 258 ? 4.062   -18.021 -32.143 1.00 19.26 ? 252 ILE A N     1 
ATOM   1971 C CA    . ILE A 1 258 ? 4.214   -17.342 -33.432 1.00 21.45 ? 252 ILE A CA    1 
ATOM   1972 C C     . ILE A 1 258 ? 4.923   -16.000 -33.248 1.00 22.37 ? 252 ILE A C     1 
ATOM   1973 O O     . ILE A 1 258 ? 5.761   -15.614 -34.068 1.00 22.51 ? 252 ILE A O     1 
ATOM   1974 C CB    . ILE A 1 258 ? 2.855   -17.206 -34.139 1.00 22.35 ? 252 ILE A CB    1 
ATOM   1975 C CG1   . ILE A 1 258 ? 2.405   -18.571 -34.655 1.00 30.79 ? 252 ILE A CG1   1 
ATOM   1976 C CG2   . ILE A 1 258 ? 2.974   -16.314 -35.331 1.00 29.65 ? 252 ILE A CG2   1 
ATOM   1977 C CD1   . ILE A 1 258 ? 3.213   -19.055 -35.858 1.00 27.05 ? 252 ILE A CD1   1 
ATOM   1978 N N     . LEU A 1 259 ? 4.656   -15.304 -32.135 1.00 19.53 ? 253 LEU A N     1 
ATOM   1979 C CA    . LEU A 1 259 ? 5.453   -14.123 -31.794 1.00 18.18 ? 253 LEU A CA    1 
ATOM   1980 C C     . LEU A 1 259 ? 6.907   -14.501 -31.535 1.00 19.59 ? 253 LEU A C     1 
ATOM   1981 O O     . LEU A 1 259 ? 7.834   -13.835 -32.012 1.00 20.26 ? 253 LEU A O     1 
ATOM   1982 C CB    . LEU A 1 259 ? 4.866   -13.417 -30.565 1.00 21.93 ? 253 LEU A CB    1 
ATOM   1983 C CG    . LEU A 1 259 ? 5.761   -12.298 -30.000 1.00 27.62 ? 253 LEU A CG    1 
ATOM   1984 C CD1   . LEU A 1 259 ? 5.921   -11.174 -31.024 1.00 27.71 ? 253 LEU A CD1   1 
ATOM   1985 C CD2   . LEU A 1 259 ? 5.243   -11.725 -28.687 1.00 33.70 ? 253 LEU A CD2   1 
ATOM   1986 N N     . GLY A 1 260 ? 7.125   -15.568 -30.763 1.00 20.31 ? 254 GLY A N     1 
ATOM   1987 C CA    . GLY A 1 260 ? 8.486   -15.991 -30.472 1.00 18.97 ? 254 GLY A CA    1 
ATOM   1988 C C     . GLY A 1 260 ? 9.270   -16.305 -31.731 1.00 19.23 ? 254 GLY A C     1 
ATOM   1989 O O     . GLY A 1 260 ? 10.411  -15.870 -31.891 1.00 18.55 ? 254 GLY A O     1 
ATOM   1990 N N     . LEU A 1 261 ? 8.664   -17.065 -32.647 1.00 18.84 ? 255 LEU A N     1 
ATOM   1991 C CA    . LEU A 1 261 ? 9.327   -17.340 -33.923 1.00 18.85 ? 255 LEU A CA    1 
ATOM   1992 C C     . LEU A 1 261 ? 9.604   -16.064 -34.693 1.00 20.06 ? 255 LEU A C     1 
ATOM   1993 O O     . LEU A 1 261 ? 10.673  -15.922 -35.302 1.00 21.66 ? 255 LEU A O     1 
ATOM   1994 C CB    . LEU A 1 261 ? 8.476   -18.269 -34.783 1.00 23.95 ? 255 LEU A CB    1 
ATOM   1995 C CG    . LEU A 1 261 ? 8.503   -19.716 -34.343 1.00 22.73 ? 255 LEU A CG    1 
ATOM   1996 C CD1   . LEU A 1 261 ? 7.276   -20.416 -34.886 1.00 30.01 ? 255 LEU A CD1   1 
ATOM   1997 C CD2   . LEU A 1 261 ? 9.787   -20.367 -34.848 1.00 22.57 ? 255 LEU A CD2   1 
ATOM   1998 N N     . SER A 1 262 ? 8.639   -15.136 -34.708 1.00 18.32 ? 256 SER A N     1 
ATOM   1999 C CA    . SER A 1 262 ? 8.799   -13.917 -35.489 1.00 20.12 ? 256 SER A CA    1 
ATOM   2000 C C     . SER A 1 262 ? 10.005  -13.130 -35.002 1.00 24.23 ? 256 SER A C     1 
ATOM   2001 O O     . SER A 1 262 ? 10.771  -12.588 -35.805 1.00 25.89 ? 256 SER A O     1 
ATOM   2002 C CB    . SER A 1 262 ? 7.531   -13.065 -35.412 1.00 25.63 ? 256 SER A CB    1 
ATOM   2003 O OG    . SER A 1 262 ? 6.406   -13.763 -35.920 1.00 33.82 ? 256 SER A OG    1 
ATOM   2004 N N     . ILE A 1 263 ? 10.210  -13.102 -33.685 1.00 21.54 ? 257 ILE A N     1 
ATOM   2005 C CA    . ILE A 1 263 ? 11.367  -12.423 -33.108 1.00 20.71 ? 257 ILE A CA    1 
ATOM   2006 C C     . ILE A 1 263 ? 12.656  -13.187 -33.392 1.00 22.00 ? 257 ILE A C     1 
ATOM   2007 O O     . ILE A 1 263 ? 13.663  -12.594 -33.797 1.00 26.18 ? 257 ILE A O     1 
ATOM   2008 C CB    . ILE A 1 263 ? 11.155  -12.221 -31.599 1.00 22.49 ? 257 ILE A CB    1 
ATOM   2009 C CG1   . ILE A 1 263 ? 10.033  -11.215 -31.375 1.00 23.03 ? 257 ILE A CG1   1 
ATOM   2010 C CG2   . ILE A 1 263 ? 12.456  -11.766 -30.936 1.00 26.48 ? 257 ILE A CG2   1 
ATOM   2011 C CD1   . ILE A 1 263 ? 9.634   -11.034 -29.947 1.00 22.35 ? 257 ILE A CD1   1 
ATOM   2012 N N     . ALA A 1 264 ? 12.662  -14.505 -33.131 1.00 19.62 ? 258 ALA A N     1 
ATOM   2013 C CA    . ALA A 1 264 ? 13.870  -15.301 -33.313 1.00 18.67 ? 258 ALA A CA    1 
ATOM   2014 C C     . ALA A 1 264 ? 14.369  -15.226 -34.749 1.00 23.68 ? 258 ALA A C     1 
ATOM   2015 O O     . ALA A 1 264 ? 15.582  -15.154 -34.994 1.00 25.49 ? 258 ALA A O     1 
ATOM   2016 C CB    . ALA A 1 264 ? 13.603  -16.757 -32.911 1.00 19.82 ? 258 ALA A CB    1 
ATOM   2017 N N     . LEU A 1 265 ? 13.444  -15.227 -35.714 1.00 23.23 ? 259 LEU A N     1 
ATOM   2018 C CA    . LEU A 1 265 ? 13.829  -15.202 -37.121 1.00 24.91 ? 259 LEU A CA    1 
ATOM   2019 C C     . LEU A 1 265 ? 14.391  -13.859 -37.560 1.00 31.10 ? 259 LEU A C     1 
ATOM   2020 O O     . LEU A 1 265 ? 14.991  -13.787 -38.634 1.00 33.39 ? 259 LEU A O     1 
ATOM   2021 C CB    . LEU A 1 265 ? 12.633  -15.584 -37.995 1.00 26.77 ? 259 LEU A CB    1 
ATOM   2022 C CG    . LEU A 1 265 ? 12.212  -17.045 -37.834 1.00 29.75 ? 259 LEU A CG    1 
ATOM   2023 C CD1   . LEU A 1 265 ? 10.951  -17.345 -38.631 1.00 31.83 ? 259 LEU A CD1   1 
ATOM   2024 C CD2   . LEU A 1 265 ? 13.354  -17.961 -38.255 1.00 38.71 ? 259 LEU A CD2   1 
ATOM   2025 N N     . LYS A 1 266 ? 14.233  -12.803 -36.764 1.00 29.75 ? 260 LYS A N     1 
ATOM   2026 C CA    . LYS A 1 266 ? 14.811  -11.511 -37.100 1.00 33.77 ? 260 LYS A CA    1 
ATOM   2027 C C     . LYS A 1 266 ? 16.166  -11.264 -36.440 1.00 34.81 ? 260 LYS A C     1 
ATOM   2028 O O     . LYS A 1 266 ? 16.831  -10.281 -36.780 1.00 42.55 ? 260 LYS A O     1 
ATOM   2029 C CB    . LYS A 1 266 ? 13.832  -10.386 -36.736 1.00 38.65 ? 260 LYS A CB    1 
ATOM   2030 C CG    . LYS A 1 266 ? 12.581  -10.371 -37.612 1.00 37.19 ? 260 LYS A CG    1 
ATOM   2031 C CD    . LYS A 1 266 ? 11.721  -9.144  -37.359 1.00 44.71 ? 260 LYS A CD    1 
ATOM   2032 N N     . GLN A 1 267 ? 16.600  -12.134 -35.534 1.00 27.29 ? 261 GLN A N     1 
ATOM   2033 C CA    . GLN A 1 267 ? 17.889  -11.985 -34.862 1.00 33.05 ? 261 GLN A CA    1 
ATOM   2034 C C     . GLN A 1 267 ? 19.024  -12.539 -35.708 1.00 33.67 ? 261 GLN A C     1 
ATOM   2035 O O     . GLN A 1 267 ? 18.852  -13.502 -36.460 1.00 39.58 ? 261 GLN A O     1 
ATOM   2036 C CB    . GLN A 1 267 ? 17.897  -12.725 -33.523 1.00 34.20 ? 261 GLN A CB    1 
ATOM   2037 C CG    . GLN A 1 267 ? 16.763  -12.371 -32.628 1.00 36.51 ? 261 GLN A CG    1 
ATOM   2038 C CD    . GLN A 1 267 ? 16.759  -10.908 -32.277 1.00 40.38 ? 261 GLN A CD    1 
ATOM   2039 O OE1   . GLN A 1 267 ? 17.777  -10.357 -31.838 1.00 36.90 ? 261 GLN A OE1   1 
ATOM   2040 N NE2   . GLN A 1 267 ? 15.618  -10.257 -32.489 1.00 44.73 ? 261 GLN A NE2   1 
ATOM   2041 N N     . GLU A 1 268 ? 20.203  -11.938 -35.556 1.00 26.26 ? 262 GLU A N     1 
ATOM   2042 C CA    . GLU A 1 268 ? 21.443  -12.515 -36.055 1.00 29.14 ? 262 GLU A CA    1 
ATOM   2043 C C     . GLU A 1 268 ? 22.011  -13.436 -34.981 1.00 36.97 ? 262 GLU A C     1 
ATOM   2044 O O     . GLU A 1 268 ? 22.388  -12.974 -33.900 1.00 49.21 ? 262 GLU A O     1 
ATOM   2045 C CB    . GLU A 1 268 ? 22.456  -11.425 -36.410 1.00 34.89 ? 262 GLU A CB    1 
ATOM   2046 C CG    . GLU A 1 268 ? 22.054  -10.562 -37.594 1.00 41.67 ? 262 GLU A CG    1 
ATOM   2047 C CD    . GLU A 1 268 ? 23.168  -9.629  -38.026 1.00 49.74 ? 262 GLU A CD    1 
ATOM   2048 O OE1   . GLU A 1 268 ? 23.188  -9.239  -39.212 1.00 59.49 ? 262 GLU A OE1   1 
ATOM   2049 O OE2   . GLU A 1 268 ? 24.025  -9.294  -37.178 1.00 51.06 ? 262 GLU A OE2   1 
ATOM   2050 N N     . TRP A 1 269 ? 22.066  -14.728 -35.267 1.00 27.35 ? 263 TRP A N     1 
ATOM   2051 C CA    . TRP A 1 269 ? 22.530  -15.712 -34.300 1.00 22.98 ? 263 TRP A CA    1 
ATOM   2052 C C     . TRP A 1 269 ? 23.998  -16.028 -34.570 1.00 26.73 ? 263 TRP A C     1 
ATOM   2053 O O     . TRP A 1 269 ? 24.388  -16.228 -35.723 1.00 32.85 ? 263 TRP A O     1 
ATOM   2054 C CB    . TRP A 1 269 ? 21.665  -16.975 -34.365 1.00 25.39 ? 263 TRP A CB    1 
ATOM   2055 C CG    . TRP A 1 269 ? 20.235  -16.692 -33.998 1.00 22.05 ? 263 TRP A CG    1 
ATOM   2056 C CD1   . TRP A 1 269 ? 19.194  -16.456 -34.853 1.00 26.28 ? 263 TRP A CD1   1 
ATOM   2057 C CD2   . TRP A 1 269 ? 19.706  -16.570 -32.674 1.00 20.87 ? 263 TRP A CD2   1 
ATOM   2058 N NE1   . TRP A 1 269 ? 18.041  -16.212 -34.139 1.00 23.13 ? 263 TRP A NE1   1 
ATOM   2059 C CE2   . TRP A 1 269 ? 18.331  -16.281 -32.797 1.00 19.93 ? 263 TRP A CE2   1 
ATOM   2060 C CE3   . TRP A 1 269 ? 20.262  -16.695 -31.394 1.00 22.05 ? 263 TRP A CE3   1 
ATOM   2061 C CZ2   . TRP A 1 269 ? 17.501  -16.108 -31.689 1.00 19.24 ? 263 TRP A CZ2   1 
ATOM   2062 C CZ3   . TRP A 1 269 ? 19.440  -16.514 -30.291 1.00 21.60 ? 263 TRP A CZ3   1 
ATOM   2063 C CH2   . TRP A 1 269 ? 18.072  -16.225 -30.449 1.00 23.81 ? 263 TRP A CH2   1 
ATOM   2064 N N     . LYS A 1 270 ? 24.819  -16.018 -33.516 1.00 25.24 ? 264 LYS A N     1 
ATOM   2065 C CA    . LYS A 1 270 ? 26.232  -16.354 -33.652 1.00 30.46 ? 264 LYS A CA    1 
ATOM   2066 C C     . LYS A 1 270 ? 26.507  -17.838 -33.435 1.00 27.02 ? 264 LYS A C     1 
ATOM   2067 O O     . LYS A 1 270 ? 27.643  -18.285 -33.634 1.00 35.22 ? 264 LYS A O     1 
ATOM   2068 C CB    . LYS A 1 270 ? 27.077  -15.526 -32.672 1.00 41.52 ? 264 LYS A CB    1 
ATOM   2069 N N     . LYS A 1 271 ? 25.501  -18.589 -33.034 1.00 23.46 ? 265 LYS A N     1 
ATOM   2070 C CA    . LYS A 1 271 ? 25.525  -20.030 -32.834 1.00 23.61 ? 265 LYS A CA    1 
ATOM   2071 C C     . LYS A 1 271 ? 24.309  -20.607 -33.533 1.00 24.57 ? 265 LYS A C     1 
ATOM   2072 O O     . LYS A 1 271 ? 23.338  -19.886 -33.797 1.00 25.63 ? 265 LYS A O     1 
ATOM   2073 C CB    . LYS A 1 271 ? 25.475  -20.384 -31.341 1.00 23.61 ? 265 LYS A CB    1 
ATOM   2074 C CG    . LYS A 1 271 ? 26.688  -19.954 -30.529 1.00 26.28 ? 265 LYS A CG    1 
ATOM   2075 C CD    . LYS A 1 271 ? 26.539  -20.436 -29.084 1.00 25.82 ? 265 LYS A CD    1 
ATOM   2076 C CE    . LYS A 1 271 ? 27.711  -20.034 -28.215 1.00 36.31 ? 265 LYS A CE    1 
ATOM   2077 N NZ    . LYS A 1 271 ? 27.631  -20.746 -26.897 1.00 41.21 ? 265 LYS A NZ    1 
ATOM   2078 N N     . PRO A 1 272 ? 24.319  -21.903 -33.850 1.00 23.22 ? 266 PRO A N     1 
ATOM   2079 C CA    . PRO A 1 272 ? 23.087  -22.537 -34.334 1.00 21.26 ? 266 PRO A CA    1 
ATOM   2080 C C     . PRO A 1 272 ? 21.965  -22.319 -33.330 1.00 20.98 ? 266 PRO A C     1 
ATOM   2081 O O     . PRO A 1 272 ? 22.180  -22.339 -32.118 1.00 23.43 ? 266 PRO A O     1 
ATOM   2082 C CB    . PRO A 1 272 ? 23.460  -24.020 -34.455 1.00 26.92 ? 266 PRO A CB    1 
ATOM   2083 C CG    . PRO A 1 272 ? 24.776  -24.173 -33.743 1.00 31.58 ? 266 PRO A CG    1 
ATOM   2084 C CD    . PRO A 1 272 ? 25.457  -22.843 -33.817 1.00 27.43 ? 266 PRO A CD    1 
ATOM   2085 N N     . LEU A 1 273 ? 20.770  -22.079 -33.843 1.00 19.34 ? 267 LEU A N     1 
ATOM   2086 C CA    . LEU A 1 273 ? 19.609  -21.768 -33.017 1.00 21.11 ? 267 LEU A CA    1 
ATOM   2087 C C     . LEU A 1 273 ? 18.764  -23.015 -32.800 1.00 18.04 ? 267 LEU A C     1 
ATOM   2088 O O     . LEU A 1 273 ? 18.382  -23.684 -33.764 1.00 19.33 ? 267 LEU A O     1 
ATOM   2089 C CB    . LEU A 1 273 ? 18.759  -20.683 -33.690 1.00 23.50 ? 267 LEU A CB    1 
ATOM   2090 C CG    . LEU A 1 273 ? 17.357  -20.452 -33.108 1.00 19.05 ? 267 LEU A CG    1 
ATOM   2091 C CD1   . LEU A 1 273 ? 17.447  -19.880 -31.683 1.00 19.71 ? 267 LEU A CD1   1 
ATOM   2092 C CD2   . LEU A 1 273 ? 16.574  -19.526 -34.042 1.00 24.84 ? 267 LEU A CD2   1 
ATOM   2093 N N     . LEU A 1 274 ? 18.456  -23.313 -31.536 1.00 15.99 ? 268 LEU A N     1 
ATOM   2094 C CA    . LEU A 1 274 ? 17.451  -24.317 -31.188 1.00 16.13 ? 268 LEU A CA    1 
ATOM   2095 C C     . LEU A 1 274 ? 16.223  -23.581 -30.657 1.00 14.91 ? 268 LEU A C     1 
ATOM   2096 O O     . LEU A 1 274 ? 16.287  -22.941 -29.599 1.00 17.78 ? 268 LEU A O     1 
ATOM   2097 C CB    . LEU A 1 274 ? 17.993  -25.299 -30.152 1.00 17.63 ? 268 LEU A CB    1 
ATOM   2098 C CG    . LEU A 1 274 ? 17.033  -26.403 -29.740 1.00 15.43 ? 268 LEU A CG    1 
ATOM   2099 C CD1   . LEU A 1 274 ? 16.745  -27.285 -30.943 1.00 16.09 ? 268 LEU A CD1   1 
ATOM   2100 C CD2   . LEU A 1 274 ? 17.628  -27.218 -28.574 1.00 17.76 ? 268 LEU A CD2   1 
ATOM   2101 N N     . TYR A 1 275 ? 15.116  -23.678 -31.398 1.00 15.82 ? 269 TYR A N     1 
ATOM   2102 C CA    . TYR A 1 275 ? 13.825  -23.123 -30.999 1.00 15.66 ? 269 TYR A CA    1 
ATOM   2103 C C     . TYR A 1 275 ? 13.027  -24.205 -30.271 1.00 16.48 ? 269 TYR A C     1 
ATOM   2104 O O     . TYR A 1 275 ? 12.868  -25.304 -30.803 1.00 18.74 ? 269 TYR A O     1 
ATOM   2105 C CB    . TYR A 1 275 ? 13.051  -22.639 -32.237 1.00 16.49 ? 269 TYR A CB    1 
ATOM   2106 C CG    . TYR A 1 275 ? 11.889  -21.791 -31.811 1.00 16.36 ? 269 TYR A CG    1 
ATOM   2107 C CD1   . TYR A 1 275 ? 10.715  -22.384 -31.358 1.00 17.02 ? 269 TYR A CD1   1 
ATOM   2108 C CD2   . TYR A 1 275 ? 11.987  -20.408 -31.802 1.00 17.26 ? 269 TYR A CD2   1 
ATOM   2109 C CE1   . TYR A 1 275 ? 9.646   -21.608 -30.906 1.00 15.61 ? 269 TYR A CE1   1 
ATOM   2110 C CE2   . TYR A 1 275 ? 10.943  -19.624 -31.349 1.00 17.65 ? 269 TYR A CE2   1 
ATOM   2111 C CZ    . TYR A 1 275 ? 9.783   -20.233 -30.892 1.00 16.69 ? 269 TYR A CZ    1 
ATOM   2112 O OH    . TYR A 1 275 ? 8.752   -19.463 -30.423 1.00 17.58 ? 269 TYR A OH    1 
ATOM   2113 N N     . ILE A 1 276 ? 12.515  -23.905 -29.073 1.00 15.56 ? 270 ILE A N     1 
ATOM   2114 C CA    . ILE A 1 276 ? 11.742  -24.897 -28.311 1.00 16.48 ? 270 ILE A CA    1 
ATOM   2115 C C     . ILE A 1 276 ? 10.260  -24.755 -28.665 1.00 15.52 ? 270 ILE A C     1 
ATOM   2116 O O     . ILE A 1 276 ? 9.650   -23.724 -28.375 1.00 16.18 ? 270 ILE A O     1 
ATOM   2117 C CB    . ILE A 1 276 ? 11.941  -24.748 -26.792 1.00 16.69 ? 270 ILE A CB    1 
ATOM   2118 C CG1   . ILE A 1 276 ? 13.428  -24.640 -26.391 1.00 16.00 ? 270 ILE A CG1   1 
ATOM   2119 C CG2   . ILE A 1 276 ? 11.269  -25.939 -26.075 1.00 18.53 ? 270 ILE A CG2   1 
ATOM   2120 C CD1   . ILE A 1 276 ? 14.329  -25.839 -26.826 1.00 16.87 ? 270 ILE A CD1   1 
ATOM   2121 N N     . HIS A 1 277 ? 9.677   -25.789 -29.293 1.00 14.93 ? 271 HIS A N     1 
ATOM   2122 C CA    . HIS A 1 277 ? 8.244   -25.774 -29.579 1.00 14.79 ? 271 HIS A CA    1 
ATOM   2123 C C     . HIS A 1 277 ? 7.481   -25.810 -28.256 1.00 17.72 ? 271 HIS A C     1 
ATOM   2124 O O     . HIS A 1 277 ? 7.741   -26.668 -27.408 1.00 18.03 ? 271 HIS A O     1 
ATOM   2125 C CB    . HIS A 1 277 ? 7.868   -26.976 -30.460 1.00 17.24 ? 271 HIS A CB    1 
ATOM   2126 C CG    . HIS A 1 277 ? 6.572   -26.820 -31.205 1.00 16.39 ? 271 HIS A CG    1 
ATOM   2127 N ND1   . HIS A 1 277 ? 5.372   -26.558 -30.575 1.00 16.76 ? 271 HIS A ND1   1 
ATOM   2128 C CD2   . HIS A 1 277 ? 6.290   -26.927 -32.528 1.00 17.46 ? 271 HIS A CD2   1 
ATOM   2129 C CE1   . HIS A 1 277 ? 4.409   -26.492 -31.480 1.00 17.94 ? 271 HIS A CE1   1 
ATOM   2130 N NE2   . HIS A 1 277 ? 4.939   -26.719 -32.674 1.00 19.14 ? 271 HIS A NE2   1 
ATOM   2131 N N     . GLN A 1 278 ? 6.523   -24.899 -28.078 1.00 14.99 ? 272 GLN A N     1 
ATOM   2132 C CA    . GLN A 1 278 ? 5.765   -24.813 -26.829 1.00 16.24 ? 272 GLN A CA    1 
ATOM   2133 C C     . GLN A 1 278 ? 4.491   -25.658 -26.832 1.00 17.75 ? 272 GLN A C     1 
ATOM   2134 O O     . GLN A 1 278 ? 3.817   -25.747 -25.791 1.00 16.86 ? 272 GLN A O     1 
ATOM   2135 C CB    . GLN A 1 278 ? 5.399   -23.344 -26.518 1.00 16.92 ? 272 GLN A CB    1 
ATOM   2136 C CG    . GLN A 1 278 ? 6.609   -22.435 -26.297 1.00 15.92 ? 272 GLN A CG    1 
ATOM   2137 C CD    . GLN A 1 278 ? 7.550   -23.037 -25.300 1.00 17.96 ? 272 GLN A CD    1 
ATOM   2138 O OE1   . GLN A 1 278 ? 7.199   -23.188 -24.132 1.00 19.53 ? 272 GLN A OE1   1 
ATOM   2139 N NE2   . GLN A 1 278 ? 8.745   -23.429 -25.757 1.00 19.67 ? 272 GLN A NE2   1 
ATOM   2140 N N     . GLY A 1 279 ? 4.154   -26.295 -27.951 1.00 18.12 ? 273 GLY A N     1 
ATOM   2141 C CA    . GLY A 1 279 ? 2.925   -27.060 -28.004 1.00 19.82 ? 273 GLY A CA    1 
ATOM   2142 C C     . GLY A 1 279 ? 1.710   -26.167 -27.832 1.00 21.18 ? 273 GLY A C     1 
ATOM   2143 O O     . GLY A 1 279 ? 1.686   -25.004 -28.260 1.00 19.36 ? 273 GLY A O     1 
ATOM   2144 N N     . GLY A 1 280 ? 0.673   -26.728 -27.214 1.00 21.83 ? 274 GLY A N     1 
ATOM   2145 C CA    . GLY A 1 280 ? -0.543  -25.978 -26.951 1.00 23.95 ? 274 GLY A CA    1 
ATOM   2146 C C     . GLY A 1 280 ? -1.375  -25.645 -28.174 1.00 25.16 ? 274 GLY A C     1 
ATOM   2147 O O     . GLY A 1 280 ? -2.132  -24.668 -28.150 1.00 29.09 ? 274 GLY A O     1 
ATOM   2148 N N     . ILE A 1 281 ? -1.270  -26.430 -29.249 1.00 25.90 ? 275 ILE A N     1 
ATOM   2149 C CA    . ILE A 1 281 ? -1.984  -26.027 -30.458 1.00 30.55 ? 275 ILE A CA    1 
ATOM   2150 C C     . ILE A 1 281 ? -3.486  -26.253 -30.332 1.00 28.75 ? 275 ILE A C     1 
ATOM   2151 O O     . ILE A 1 281 ? -4.257  -25.673 -31.103 1.00 29.48 ? 275 ILE A O     1 
ATOM   2152 C CB    . ILE A 1 281 ? -1.432  -26.731 -31.713 1.00 33.63 ? 275 ILE A CB    1 
ATOM   2153 C CG1   . ILE A 1 281 ? -1.820  -28.202 -31.732 1.00 40.05 ? 275 ILE A CG1   1 
ATOM   2154 C CG2   . ILE A 1 281 ? 0.088   -26.552 -31.822 1.00 28.63 ? 275 ILE A CG2   1 
ATOM   2155 C CD1   . ILE A 1 281 ? -1.430  -28.893 -33.027 1.00 44.12 ? 275 ILE A CD1   1 
ATOM   2156 N N     . LEU A 1 282 ? -3.937  -27.070 -29.374 1.00 27.49 ? 276 LEU A N     1 
ATOM   2157 C CA    . LEU A 1 282 ? -5.374  -27.196 -29.164 1.00 30.18 ? 276 LEU A CA    1 
ATOM   2158 C C     . LEU A 1 282 ? -5.981  -25.897 -28.651 1.00 29.64 ? 276 LEU A C     1 
ATOM   2159 O O     . LEU A 1 282 ? -7.188  -25.682 -28.805 1.00 37.10 ? 276 LEU A O     1 
ATOM   2160 C CB    . LEU A 1 282 ? -5.679  -28.348 -28.202 1.00 39.07 ? 276 LEU A CB    1 
ATOM   2161 N N     . GLY A 1 283 ? -5.172  -25.019 -28.066 1.00 34.92 ? 277 GLY A N     1 
ATOM   2162 C CA    . GLY A 1 283 ? -5.651  -23.701 -27.708 1.00 37.76 ? 277 GLY A CA    1 
ATOM   2163 C C     . GLY A 1 283 ? -5.848  -22.758 -28.873 1.00 40.36 ? 277 GLY A C     1 
ATOM   2164 O O     . GLY A 1 283 ? -6.352  -21.650 -28.673 1.00 44.45 ? 277 GLY A O     1 
ATOM   2165 N N     . ASN A 1 284 ? -5.463  -23.157 -30.088 1.00 31.34 ? 278 ASN A N     1 
ATOM   2166 C CA    . ASN A 1 284 ? -5.608  -22.266 -31.230 1.00 29.38 ? 278 ASN A CA    1 
ATOM   2167 C C     . ASN A 1 284 ? -7.054  -22.061 -31.643 1.00 37.68 ? 278 ASN A C     1 
ATOM   2168 O O     . ASN A 1 284 ? -7.318  -21.155 -32.439 1.00 36.26 ? 278 ASN A O     1 
ATOM   2169 C CB    . ASN A 1 284 ? -4.808  -22.790 -32.423 1.00 26.45 ? 278 ASN A CB    1 
ATOM   2170 C CG    . ASN A 1 284 ? -3.366  -22.385 -32.360 1.00 26.12 ? 278 ASN A CG    1 
ATOM   2171 O OD1   . ASN A 1 284 ? -3.010  -21.472 -31.616 1.00 26.67 ? 278 ASN A OD1   1 
ATOM   2172 N ND2   . ASN A 1 284 ? -2.518  -23.057 -33.141 1.00 24.36 ? 278 ASN A ND2   1 
ATOM   2173 N N     . SER A 1 285 ? -7.984  -22.879 -31.136 1.00 43.61 ? 279 SER A N     1 
ATOM   2174 C CA    . SER A 1 285 ? -9.395  -22.717 -31.479 1.00 45.65 ? 279 SER A CA    1 
ATOM   2175 C C     . SER A 1 285 ? -9.848  -21.282 -31.256 1.00 43.96 ? 279 SER A C     1 
ATOM   2176 O O     . SER A 1 285 ? -10.468 -20.668 -32.130 1.00 48.91 ? 279 SER A O     1 
ATOM   2177 C CB    . SER A 1 285 ? -10.258 -23.671 -30.647 1.00 48.31 ? 279 SER A CB    1 
ATOM   2178 N N     . THR A 1 286 ? -9.523  -20.725 -30.088 1.00 43.93 ? 280 THR A N     1 
ATOM   2179 C CA    . THR A 1 286 ? -10.008 -19.395 -29.741 1.00 49.45 ? 280 THR A CA    1 
ATOM   2180 C C     . THR A 1 286 ? -9.349  -18.320 -30.595 1.00 46.78 ? 280 THR A C     1 
ATOM   2181 O O     . THR A 1 286 ? -10.034 -17.422 -31.096 1.00 49.44 ? 280 THR A O     1 
ATOM   2182 C CB    . THR A 1 286 ? -9.781  -19.122 -28.252 1.00 54.40 ? 280 THR A CB    1 
ATOM   2183 N N     . MET A 1 287 ? -8.025  -18.397 -30.791 1.00 42.90 ? 281 MET A N     1 
ATOM   2184 C CA    . MET A 1 287 ? -7.354  -17.368 -31.582 1.00 41.65 ? 281 MET A CA    1 
ATOM   2185 C C     . MET A 1 287 ? -7.804  -17.398 -33.038 1.00 41.47 ? 281 MET A C     1 
ATOM   2186 O O     . MET A 1 287 ? -8.031  -16.345 -33.640 1.00 39.63 ? 281 MET A O     1 
ATOM   2187 C CB    . MET A 1 287 ? -5.834  -17.516 -31.505 1.00 39.31 ? 281 MET A CB    1 
ATOM   2188 C CG    . MET A 1 287 ? -5.168  -16.779 -30.353 1.00 43.89 ? 281 MET A CG    1 
ATOM   2189 S SD    . MET A 1 287 ? -5.674  -15.058 -30.130 1.00 44.78 ? 281 MET A SD    1 
ATOM   2190 C CE    . MET A 1 287 ? -5.422  -14.337 -31.757 1.00 50.75 ? 281 MET A CE    1 
ATOM   2191 N N     . LEU A 1 288 ? -7.939  -18.589 -33.624 1.00 41.10 ? 282 LEU A N     1 
ATOM   2192 C CA    . LEU A 1 288 ? -8.330  -18.667 -35.028 1.00 39.14 ? 282 LEU A CA    1 
ATOM   2193 C C     . LEU A 1 288 ? -9.671  -17.992 -35.287 1.00 49.49 ? 282 LEU A C     1 
ATOM   2194 O O     . LEU A 1 288 ? -9.879  -17.424 -36.367 1.00 49.25 ? 282 LEU A O     1 
ATOM   2195 C CB    . LEU A 1 288 ? -8.367  -20.124 -35.478 1.00 38.65 ? 282 LEU A CB    1 
ATOM   2196 C CG    . LEU A 1 288 ? -6.993  -20.766 -35.644 1.00 44.83 ? 282 LEU A CG    1 
ATOM   2197 C CD1   . LEU A 1 288 ? -7.101  -22.276 -35.561 1.00 47.84 ? 282 LEU A CD1   1 
ATOM   2198 C CD2   . LEU A 1 288 ? -6.366  -20.339 -36.960 1.00 46.38 ? 282 LEU A CD2   1 
ATOM   2199 N N     . GLU A 1 289 ? -10.587 -18.034 -34.316 1.00 47.24 ? 283 GLU A N     1 
ATOM   2200 C CA    . GLU A 1 289 ? -11.837 -17.292 -34.455 1.00 47.64 ? 283 GLU A CA    1 
ATOM   2201 C C     . GLU A 1 289 ? -11.573 -15.801 -34.627 1.00 50.86 ? 283 GLU A C     1 
ATOM   2202 O O     . GLU A 1 289 ? -12.269 -15.123 -35.392 1.00 54.08 ? 283 GLU A O     1 
ATOM   2203 C CB    . GLU A 1 289 ? -12.740 -17.542 -33.244 1.00 47.10 ? 283 GLU A CB    1 
ATOM   2204 N N     . ARG A 1 290 ? -10.568 -15.270 -33.929 1.00 46.35 ? 284 ARG A N     1 
ATOM   2205 C CA    . ARG A 1 290 ? -10.239 -13.856 -34.068 1.00 47.82 ? 284 ARG A CA    1 
ATOM   2206 C C     . ARG A 1 290 ? -9.572  -13.533 -35.395 1.00 49.03 ? 284 ARG A C     1 
ATOM   2207 O O     . ARG A 1 290 ? -9.425  -12.349 -35.719 1.00 55.86 ? 284 ARG A O     1 
ATOM   2208 C CB    . ARG A 1 290 ? -9.331  -13.417 -32.925 1.00 50.31 ? 284 ARG A CB    1 
ATOM   2209 C CG    . ARG A 1 290 ? -10.057 -13.203 -31.624 1.00 53.09 ? 284 ARG A CG    1 
ATOM   2210 C CD    . ARG A 1 290 ? -9.097  -13.316 -30.464 1.00 55.03 ? 284 ARG A CD    1 
ATOM   2211 N NE    . ARG A 1 290 ? -9.748  -12.991 -29.203 1.00 59.95 ? 284 ARG A NE    1 
ATOM   2212 C CZ    . ARG A 1 290 ? -9.315  -13.398 -28.017 1.00 58.77 ? 284 ARG A CZ    1 
ATOM   2213 N NH1   . ARG A 1 290 ? -9.972  -13.053 -26.917 1.00 61.11 ? 284 ARG A NH1   1 
ATOM   2214 N NH2   . ARG A 1 290 ? -8.234  -14.162 -27.933 1.00 54.87 ? 284 ARG A NH2   1 
ATOM   2215 N N     . TYR A 1 291 ? -9.164  -14.543 -36.156 1.00 43.85 ? 285 TYR A N     1 
ATOM   2216 C CA    . TYR A 1 291 ? -8.498  -14.329 -37.433 1.00 44.77 ? 285 TYR A CA    1 
ATOM   2217 C C     . TYR A 1 291 ? -9.474  -14.421 -38.599 1.00 52.96 ? 285 TYR A C     1 
ATOM   2218 O O     . TYR A 1 291 ? -9.322  -13.714 -39.593 1.00 56.97 ? 285 TYR A O     1 
ATOM   2219 C CB    . TYR A 1 291 ? -7.353  -15.335 -37.613 1.00 39.96 ? 285 TYR A CB    1 
ATOM   2220 C CG    . TYR A 1 291 ? -6.073  -14.882 -36.961 1.00 38.81 ? 285 TYR A CG    1 
ATOM   2221 C CD1   . TYR A 1 291 ? -5.301  -13.889 -37.541 1.00 36.28 ? 285 TYR A CD1   1 
ATOM   2222 C CD2   . TYR A 1 291 ? -5.634  -15.442 -35.767 1.00 37.80 ? 285 TYR A CD2   1 
ATOM   2223 C CE1   . TYR A 1 291 ? -4.129  -13.468 -36.961 1.00 30.84 ? 285 TYR A CE1   1 
ATOM   2224 C CE2   . TYR A 1 291 ? -4.453  -15.021 -35.176 1.00 38.56 ? 285 TYR A CE2   1 
ATOM   2225 C CZ    . TYR A 1 291 ? -3.717  -14.023 -35.780 1.00 28.89 ? 285 TYR A CZ    1 
ATOM   2226 O OH    . TYR A 1 291 ? -2.551  -13.584 -35.221 1.00 27.57 ? 285 TYR A OH    1 
HETATM 2227 S S     . SO4 B 2 .   ? 14.662  -23.319 -5.533  1.00 44.14 ? 301 SO4 A S     1 
HETATM 2228 O O1    . SO4 B 2 .   ? 16.042  -22.990 -5.184  1.00 45.69 ? 301 SO4 A O1    1 
HETATM 2229 O O2    . SO4 B 2 .   ? 14.643  -24.319 -6.594  1.00 36.78 ? 301 SO4 A O2    1 
HETATM 2230 O O3    . SO4 B 2 .   ? 13.957  -23.859 -4.367  1.00 44.00 ? 301 SO4 A O3    1 
HETATM 2231 O O4    . SO4 B 2 .   ? 14.014  -22.101 -6.013  1.00 44.69 ? 301 SO4 A O4    1 
HETATM 2232 S S     . SO4 C 2 .   ? 0.003   0.005   -31.070 0.33 37.58 ? 302 SO4 A S     1 
HETATM 2233 O O1    . SO4 C 2 .   ? 1.369   0.166   -31.557 0.33 40.85 ? 302 SO4 A O1    1 
HETATM 2234 O O2    . SO4 C 2 .   ? -0.818  1.110   -31.556 0.33 41.30 ? 302 SO4 A O2    1 
HETATM 2235 O O3    . SO4 C 2 .   ? -0.542  -1.256  -31.563 0.33 41.01 ? 302 SO4 A O3    1 
HETATM 2236 O O4    . SO4 C 2 .   ? 0.001   0.001   -29.608 0.33 36.07 ? 302 SO4 A O4    1 
HETATM 2237 S S     . SO4 D 2 .   ? 0.285   -6.818  -23.631 1.00 66.85 ? 303 SO4 A S     1 
HETATM 2238 O O1    . SO4 D 2 .   ? 0.978   -7.510  -24.714 1.00 49.84 ? 303 SO4 A O1    1 
HETATM 2239 O O2    . SO4 D 2 .   ? -1.046  -6.424  -24.092 1.00 71.79 ? 303 SO4 A O2    1 
HETATM 2240 O O3    . SO4 D 2 .   ? 0.181   -7.697  -22.462 1.00 59.36 ? 303 SO4 A O3    1 
HETATM 2241 O O4    . SO4 D 2 .   ? 1.034   -5.620  -23.258 1.00 73.66 ? 303 SO4 A O4    1 
HETATM 2242 O O     . HOH E 3 .   ? 2.952   -33.147 -4.563  1.00 36.74 ? 401 HOH A O     1 
HETATM 2243 O O     . HOH E 3 .   ? -20.619 -25.060 -19.087 1.00 42.98 ? 402 HOH A O     1 
HETATM 2244 O O     . HOH E 3 .   ? 8.144   -20.637 -22.329 1.00 44.72 ? 403 HOH A O     1 
HETATM 2245 O O     . HOH E 3 .   ? 11.599  -39.279 -22.173 1.00 36.50 ? 404 HOH A O     1 
HETATM 2246 O O     . HOH E 3 .   ? -3.335  -20.066 -29.539 1.00 29.69 ? 405 HOH A O     1 
HETATM 2247 O O     . HOH E 3 .   ? -11.943 -33.099 -4.966  1.00 40.62 ? 406 HOH A O     1 
HETATM 2248 O O     . HOH E 3 .   ? 0.486   -3.606  -32.237 1.00 33.61 ? 407 HOH A O     1 
HETATM 2249 O O     . HOH E 3 .   ? 2.361   -29.044 -33.687 1.00 31.16 ? 408 HOH A O     1 
HETATM 2250 O O     . HOH E 3 .   ? 13.514  -37.269 -20.923 1.00 26.73 ? 409 HOH A O     1 
HETATM 2251 O O     . HOH E 3 .   ? -2.060  -22.250 -27.020 1.00 31.85 ? 410 HOH A O     1 
HETATM 2252 O O     . HOH E 3 .   ? 3.853   -42.145 -3.093  1.00 37.68 ? 411 HOH A O     1 
HETATM 2253 O O     . HOH E 3 .   ? 2.544   -40.877 -13.654 1.00 34.33 ? 412 HOH A O     1 
HETATM 2254 O O     . HOH E 3 .   ? 19.914  -17.578 -15.790 1.00 22.31 ? 413 HOH A O     1 
HETATM 2255 O O     . HOH E 3 .   ? 8.804   -25.166 -22.964 1.00 17.26 ? 414 HOH A O     1 
HETATM 2256 O O     . HOH E 3 .   ? 19.717  -10.907 -18.973 1.00 31.80 ? 415 HOH A O     1 
HETATM 2257 O O     . HOH E 3 .   ? 3.361   -23.959 -30.311 1.00 22.17 ? 416 HOH A O     1 
HETATM 2258 O O     . HOH E 3 .   ? 1.643   -38.858 -10.815 1.00 31.25 ? 417 HOH A O     1 
HETATM 2259 O O     . HOH E 3 .   ? 6.416   -3.257  -16.751 1.00 47.76 ? 418 HOH A O     1 
HETATM 2260 O O     . HOH E 3 .   ? -1.776  -14.467 -32.883 1.00 27.29 ? 419 HOH A O     1 
HETATM 2261 O O     . HOH E 3 .   ? 4.956   -32.558 -38.052 1.00 31.44 ? 420 HOH A O     1 
HETATM 2262 O O     . HOH E 3 .   ? 23.848  -15.488 -30.875 1.00 38.71 ? 421 HOH A O     1 
HETATM 2263 O O     . HOH E 3 .   ? 10.326  -9.073  -25.558 1.00 24.71 ? 422 HOH A O     1 
HETATM 2264 O O     . HOH E 3 .   ? 18.323  -15.048 -38.538 1.00 38.29 ? 423 HOH A O     1 
HETATM 2265 O O     . HOH E 3 .   ? 0.574   -29.040 -29.241 1.00 29.51 ? 424 HOH A O     1 
HETATM 2266 O O     . HOH E 3 .   ? 25.766  -32.029 -36.991 1.00 28.23 ? 425 HOH A O     1 
HETATM 2267 O O     . HOH E 3 .   ? -11.653 -21.702 -34.275 1.00 48.38 ? 426 HOH A O     1 
HETATM 2268 O O     . HOH E 3 .   ? 1.390   -16.890 -19.592 1.00 31.07 ? 427 HOH A O     1 
HETATM 2269 O O     . HOH E 3 .   ? 23.175  -28.723 -18.528 1.00 20.10 ? 428 HOH A O     1 
HETATM 2270 O O     . HOH E 3 .   ? 2.274   -28.233 -5.921  1.00 29.43 ? 429 HOH A O     1 
HETATM 2271 O O     . HOH E 3 .   ? 18.131  -24.144 -6.379  1.00 29.06 ? 430 HOH A O     1 
HETATM 2272 O O     . HOH E 3 .   ? 3.667   -7.319  -24.749 1.00 36.54 ? 431 HOH A O     1 
HETATM 2273 O O     . HOH E 3 .   ? 24.594  -20.716 -26.286 1.00 23.10 ? 432 HOH A O     1 
HETATM 2274 O O     . HOH E 3 .   ? -4.069  -6.305  -34.139 1.00 27.25 ? 433 HOH A O     1 
HETATM 2275 O O     . HOH E 3 .   ? 20.278  -35.123 -31.825 1.00 38.87 ? 434 HOH A O     1 
HETATM 2276 O O     . HOH E 3 .   ? 5.888   -11.928 -20.840 1.00 23.23 ? 435 HOH A O     1 
HETATM 2277 O O     . HOH E 3 .   ? -3.626  -20.795 -22.610 1.00 37.61 ? 436 HOH A O     1 
HETATM 2278 O O     . HOH E 3 .   ? 10.029  -12.524 -38.396 1.00 33.67 ? 437 HOH A O     1 
HETATM 2279 O O     . HOH E 3 .   ? 25.690  -20.462 -21.249 1.00 28.63 ? 438 HOH A O     1 
HETATM 2280 O O     . HOH E 3 .   ? 9.071   -18.833 -20.143 1.00 17.84 ? 439 HOH A O     1 
HETATM 2281 O O     . HOH E 3 .   ? 10.230  -33.092 -19.001 1.00 24.28 ? 440 HOH A O     1 
HETATM 2282 O O     . HOH E 3 .   ? 7.334   -41.671 -7.609  1.00 31.62 ? 441 HOH A O     1 
HETATM 2283 O O     . HOH E 3 .   ? 21.068  -28.092 -22.252 1.00 17.55 ? 442 HOH A O     1 
HETATM 2284 O O     . HOH E 3 .   ? 14.831  -21.675 -8.565  1.00 33.59 ? 443 HOH A O     1 
HETATM 2285 O O     . HOH E 3 .   ? -18.902 -22.645 -8.738  1.00 43.59 ? 444 HOH A O     1 
HETATM 2286 O O     . HOH E 3 .   ? 16.422  -35.138 -36.721 1.00 20.07 ? 445 HOH A O     1 
HETATM 2287 O O     . HOH E 3 .   ? 32.215  -26.335 -19.551 1.00 31.31 ? 446 HOH A O     1 
HETATM 2288 O O     . HOH E 3 .   ? -0.344  -12.981 -28.540 1.00 22.80 ? 447 HOH A O     1 
HETATM 2289 O O     . HOH E 3 .   ? 20.851  -21.921 -36.780 1.00 22.30 ? 448 HOH A O     1 
HETATM 2290 O O     . HOH E 3 .   ? 8.248   -30.242 -13.402 1.00 17.66 ? 449 HOH A O     1 
HETATM 2291 O O     . HOH E 3 .   ? 22.761  -19.737 -36.474 1.00 28.20 ? 450 HOH A O     1 
HETATM 2292 O O     . HOH E 3 .   ? -2.188  -12.931 -30.619 1.00 31.29 ? 451 HOH A O     1 
HETATM 2293 O O     . HOH E 3 .   ? 12.021  -5.472  -13.628 1.00 42.87 ? 452 HOH A O     1 
HETATM 2294 O O     . HOH E 3 .   ? 25.020  -37.463 -26.788 1.00 24.36 ? 453 HOH A O     1 
HETATM 2295 O O     . HOH E 3 .   ? 17.089  -36.868 -17.917 1.00 39.98 ? 454 HOH A O     1 
HETATM 2296 O O     . HOH E 3 .   ? 9.455   -9.122  -8.370  1.00 35.80 ? 455 HOH A O     1 
HETATM 2297 O O     . HOH E 3 .   ? 1.836   -25.793 -23.640 1.00 21.35 ? 456 HOH A O     1 
HETATM 2298 O O     . HOH E 3 .   ? -6.873  -35.225 -2.034  1.00 40.31 ? 457 HOH A O     1 
HETATM 2299 O O     . HOH E 3 .   ? 21.595  -15.469 -37.888 1.00 33.06 ? 458 HOH A O     1 
HETATM 2300 O O     . HOH E 3 .   ? 5.847   -29.884 -3.644  1.00 39.85 ? 459 HOH A O     1 
HETATM 2301 O O     . HOH E 3 .   ? -10.679 -17.243 -14.537 1.00 39.63 ? 460 HOH A O     1 
HETATM 2302 O O     . HOH E 3 .   ? 1.840   -24.388 -6.699  1.00 34.24 ? 461 HOH A O     1 
HETATM 2303 O O     . HOH E 3 .   ? 29.036  -30.010 -36.006 1.00 37.24 ? 462 HOH A O     1 
HETATM 2304 O O     . HOH E 3 .   ? 25.415  -16.948 -27.016 1.00 32.29 ? 463 HOH A O     1 
HETATM 2305 O O     . HOH E 3 .   ? 23.671  -32.139 -16.913 1.00 26.02 ? 464 HOH A O     1 
HETATM 2306 O O     . HOH E 3 .   ? 1.888   -29.793 -36.109 1.00 30.46 ? 465 HOH A O     1 
HETATM 2307 O O     . HOH E 3 .   ? 1.769   -35.070 -29.403 1.00 28.34 ? 466 HOH A O     1 
HETATM 2308 O O     . HOH E 3 .   ? 20.725  -22.048 -46.489 1.00 40.47 ? 467 HOH A O     1 
HETATM 2309 O O     . HOH E 3 .   ? 2.476   -9.908  -27.264 1.00 29.95 ? 468 HOH A O     1 
HETATM 2310 O O     . HOH E 3 .   ? 19.156  -9.633  -21.787 1.00 29.91 ? 469 HOH A O     1 
HETATM 2311 O O     . HOH E 3 .   ? 9.168   -29.012 -46.127 1.00 25.66 ? 470 HOH A O     1 
HETATM 2312 O O     . HOH E 3 .   ? 10.974  -10.891 -5.528  1.00 44.48 ? 471 HOH A O     1 
HETATM 2313 O O     . HOH E 3 .   ? 27.780  -29.363 -28.229 1.00 32.03 ? 472 HOH A O     1 
HETATM 2314 O O     . HOH E 3 .   ? 2.298   -23.194 -37.665 1.00 20.53 ? 473 HOH A O     1 
HETATM 2315 O O     . HOH E 3 .   ? 0.945   -38.249 -19.442 1.00 46.49 ? 474 HOH A O     1 
HETATM 2316 O O     . HOH E 3 .   ? -2.659  -7.176  -38.827 1.00 32.54 ? 475 HOH A O     1 
HETATM 2317 O O     . HOH E 3 .   ? 22.609  -24.863 -12.474 1.00 22.51 ? 476 HOH A O     1 
HETATM 2318 O O     . HOH E 3 .   ? 28.258  -31.087 -26.352 1.00 22.81 ? 477 HOH A O     1 
HETATM 2319 O O     . HOH E 3 .   ? -3.362  -23.345 -13.896 1.00 30.33 ? 478 HOH A O     1 
HETATM 2320 O O     . HOH E 3 .   ? 29.231  -36.744 -30.844 1.00 37.55 ? 479 HOH A O     1 
HETATM 2321 O O     . HOH E 3 .   ? 23.659  -25.779 -38.538 1.00 41.88 ? 480 HOH A O     1 
HETATM 2322 O O     . HOH E 3 .   ? -4.795  -18.194 -16.907 1.00 45.15 ? 481 HOH A O     1 
HETATM 2323 O O     . HOH E 3 .   ? 22.202  -12.314 -19.005 1.00 40.74 ? 482 HOH A O     1 
HETATM 2324 O O     . HOH E 3 .   ? 5.382   -0.714  -32.293 1.00 31.97 ? 483 HOH A O     1 
HETATM 2325 O O     . HOH E 3 .   ? 8.077   -27.260 -24.599 1.00 18.78 ? 484 HOH A O     1 
HETATM 2326 O O     . HOH E 3 .   ? 2.723   -20.991 -17.454 1.00 26.58 ? 485 HOH A O     1 
HETATM 2327 O O     . HOH E 3 .   ? 11.242  -35.957 -24.401 1.00 22.83 ? 486 HOH A O     1 
HETATM 2328 O O     . HOH E 3 .   ? 0.492   -17.743 -13.523 1.00 41.96 ? 487 HOH A O     1 
HETATM 2329 O O     . HOH E 3 .   ? 15.092  -32.829 -39.241 1.00 26.18 ? 488 HOH A O     1 
HETATM 2330 O O     . HOH E 3 .   ? 4.519   -19.907 -7.282  1.00 44.71 ? 489 HOH A O     1 
HETATM 2331 O O     . HOH E 3 .   ? -7.320  -21.074 -25.566 1.00 41.11 ? 490 HOH A O     1 
HETATM 2332 O O     . HOH E 3 .   ? 16.406  -7.683  -29.027 1.00 49.73 ? 491 HOH A O     1 
HETATM 2333 O O     . HOH E 3 .   ? 7.571   -16.715 -13.288 1.00 24.17 ? 492 HOH A O     1 
HETATM 2334 O O     . HOH E 3 .   ? 3.839   -35.770 -21.580 1.00 35.17 ? 493 HOH A O     1 
HETATM 2335 O O     . HOH E 3 .   ? 4.425   -13.307 -42.170 1.00 39.27 ? 494 HOH A O     1 
HETATM 2336 O O     . HOH E 3 .   ? 8.297   -22.738 -49.624 1.00 36.94 ? 495 HOH A O     1 
HETATM 2337 O O     . HOH E 3 .   ? 5.791   -6.868  -28.468 1.00 35.25 ? 496 HOH A O     1 
HETATM 2338 O O     . HOH E 3 .   ? 26.047  -30.880 -24.668 1.00 19.02 ? 497 HOH A O     1 
HETATM 2339 O O     . HOH E 3 .   ? -9.677  -33.980 -15.209 1.00 30.67 ? 498 HOH A O     1 
HETATM 2340 O O     . HOH E 3 .   ? 11.752  -27.291 -5.634  1.00 39.72 ? 499 HOH A O     1 
HETATM 2341 O O     . HOH E 3 .   ? 6.132   -23.829 -5.290  1.00 41.04 ? 500 HOH A O     1 
HETATM 2342 O O     . HOH E 3 .   ? 17.396  -37.163 -30.806 1.00 31.71 ? 501 HOH A O     1 
HETATM 2343 O O     . HOH E 3 .   ? 26.022  -29.399 -22.332 1.00 20.08 ? 502 HOH A O     1 
HETATM 2344 O O     . HOH E 3 .   ? 14.775  -31.861 -5.980  1.00 38.02 ? 503 HOH A O     1 
HETATM 2345 O O     . HOH E 3 .   ? 4.876   -8.672  -26.876 1.00 41.08 ? 504 HOH A O     1 
HETATM 2346 O O     . HOH E 3 .   ? 23.637  -28.390 -21.222 1.00 17.85 ? 505 HOH A O     1 
HETATM 2347 O O     . HOH E 3 .   ? 28.285  -25.392 -33.139 1.00 28.30 ? 506 HOH A O     1 
HETATM 2348 O O     . HOH E 3 .   ? 7.169   -32.071 -39.834 1.00 40.22 ? 507 HOH A O     1 
HETATM 2349 O O     . HOH E 3 .   ? 20.848  -19.256 -13.692 1.00 45.08 ? 508 HOH A O     1 
HETATM 2350 O O     . HOH E 3 .   ? 29.145  -23.479 -17.123 1.00 49.69 ? 509 HOH A O     1 
HETATM 2351 O O     . HOH E 3 .   ? 27.978  -35.455 -34.891 0.50 25.18 ? 510 HOH A O     1 
HETATM 2352 O O     . HOH E 3 .   ? 11.076  -3.299  -20.384 1.00 33.77 ? 511 HOH A O     1 
HETATM 2353 O O     . HOH E 3 .   ? -4.321  -21.167 -25.494 1.00 34.30 ? 512 HOH A O     1 
HETATM 2354 O O     . HOH E 3 .   ? 0.731   -31.362 -30.860 1.00 41.08 ? 513 HOH A O     1 
HETATM 2355 O O     . HOH E 3 .   ? 0.255   -37.642 -22.342 1.00 39.97 ? 514 HOH A O     1 
HETATM 2356 O O     . HOH E 3 .   ? -2.260  -29.031 -27.726 1.00 39.15 ? 515 HOH A O     1 
HETATM 2357 O O     . HOH E 3 .   ? 13.384  -3.438  -30.955 1.00 48.01 ? 516 HOH A O     1 
HETATM 2358 O O     . HOH E 3 .   ? 5.940   -15.818 -11.702 1.00 32.96 ? 517 HOH A O     1 
HETATM 2359 O O     . HOH E 3 .   ? -1.069  -30.586 -23.830 1.00 42.35 ? 518 HOH A O     1 
HETATM 2360 O O     . HOH E 3 .   ? 20.231  -37.832 -31.001 1.00 33.26 ? 519 HOH A O     1 
HETATM 2361 O O     . HOH E 3 .   ? 6.383   -21.762 -6.116  1.00 35.66 ? 520 HOH A O     1 
HETATM 2362 O O     . HOH E 3 .   ? 1.139   -10.703 -29.441 1.00 36.71 ? 521 HOH A O     1 
HETATM 2363 O O     . HOH E 3 .   ? 8.360   -37.322 -27.933 1.00 39.93 ? 522 HOH A O     1 
HETATM 2364 O O     . HOH E 3 .   ? 19.606  -19.024 -11.129 1.00 40.42 ? 523 HOH A O     1 
HETATM 2365 O O     . HOH E 3 .   ? -1.950  -21.449 -19.226 1.00 26.59 ? 524 HOH A O     1 
HETATM 2366 O O     . HOH E 3 .   ? 0.024   -27.672 -23.282 1.00 36.81 ? 525 HOH A O     1 
HETATM 2367 O O     . HOH E 3 .   ? 28.746  -27.022 -27.253 1.00 37.47 ? 526 HOH A O     1 
HETATM 2368 O O     . HOH E 3 .   ? -0.716  -34.981 -29.420 1.00 46.86 ? 527 HOH A O     1 
HETATM 2369 O O     . HOH E 3 .   ? -1.044  -20.763 -21.558 1.00 39.60 ? 528 HOH A O     1 
HETATM 2370 O O     . HOH E 3 .   ? 1.063   -19.206 -18.135 1.00 42.89 ? 529 HOH A O     1 
HETATM 2371 O O     . HOH E 3 .   ? 2.331   -13.051 -16.875 1.00 36.99 ? 530 HOH A O     1 
HETATM 2372 O O     . HOH E 3 .   ? 18.875  -34.493 -34.053 1.00 31.16 ? 531 HOH A O     1 
HETATM 2373 O O     . HOH E 3 .   ? 29.278  -33.580 -36.278 1.00 42.82 ? 532 HOH A O     1 
HETATM 2374 O O     . HOH E 3 .   ? 23.114  -23.559 -37.889 1.00 42.43 ? 533 HOH A O     1 
HETATM 2375 O O     . HOH E 3 .   ? 29.978  -29.834 -29.740 1.00 37.93 ? 534 HOH A O     1 
HETATM 2376 O O     . HOH E 3 .   ? -0.442  -18.471 -16.221 1.00 41.39 ? 535 HOH A O     1 
HETATM 2377 O O     . HOH E 3 .   ? 0.740   -14.916 -18.201 1.00 41.04 ? 536 HOH A O     1 
HETATM 2378 O O     . HOH E 3 .   ? -0.442  -15.857 -15.664 1.00 43.33 ? 537 HOH A O     1 
HETATM 2379 O O     . HOH E 3 .   ? 3.223   -30.380 -4.367  1.00 36.64 ? 538 HOH A O     1 
HETATM 2380 O O     . HOH E 3 .   ? 24.558  -22.992 -12.201 1.00 30.68 ? 539 HOH A O     1 
HETATM 2381 O O     . HOH E 3 .   ? 16.344  -37.822 -20.742 1.00 40.83 ? 540 HOH A O     1 
HETATM 2382 O O     . HOH E 3 .   ? 21.366  -24.353 -9.946  1.00 31.26 ? 541 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASN A 8   ? 0.8676 0.4466 0.7622 -0.1294 0.0769  0.1369  2   ASN A N   
2    C CA  . ASN A 8   ? 0.7216 0.3095 0.6108 -0.1106 0.0705  0.1212  2   ASN A CA  
3    C C   . ASN A 8   ? 0.7240 0.3674 0.6122 -0.1004 0.0665  0.1270  2   ASN A C   
4    O O   . ASN A 8   ? 0.7559 0.4350 0.6497 -0.1159 0.0726  0.1257  2   ASN A O   
5    C CB  . ASN A 8   ? 0.7410 0.3298 0.6378 -0.1286 0.0627  0.0918  2   ASN A CB  
6    C CG  . ASN A 8   ? 0.8515 0.3845 0.7338 -0.1319 0.0599  0.0769  2   ASN A CG  
7    O OD1 . ASN A 8   ? 0.9368 0.4287 0.8059 -0.1102 0.0693  0.0849  2   ASN A OD1 
8    N ND2 . ASN A 8   ? 0.8749 0.4073 0.7591 -0.1593 0.0459  0.0570  2   ASN A ND2 
9    N N   . PHE A 9   ? 0.7022 0.3544 0.5872 -0.0736 0.0574  0.1339  3   PHE A N   
10   C CA  . PHE A 9   ? 0.5885 0.2903 0.4696 -0.0660 0.0465  0.1334  3   PHE A CA  
11   C C   . PHE A 9   ? 0.5797 0.3034 0.4801 -0.0532 0.0406  0.1087  3   PHE A C   
12   O O   . PHE A 9   ? 0.6152 0.3161 0.5253 -0.0343 0.0420  0.1084  3   PHE A O   
13   C CB  . PHE A 9   ? 0.6137 0.3153 0.4814 -0.0525 0.0324  0.1656  3   PHE A CB  
14   C CG  . PHE A 9   ? 0.6513 0.3943 0.5138 -0.0471 0.0146  0.1640  3   PHE A CG  
15   C CD1 . PHE A 9   ? 0.7099 0.4641 0.5302 -0.0645 0.0124  0.1624  3   PHE A CD1 
16   C CD2 . PHE A 9   ? 0.7363 0.4996 0.6320 -0.0257 0.0044  0.1640  3   PHE A CD2 
17   C CE1 . PHE A 9   ? 0.7410 0.5205 0.5466 -0.0641 -0.0050 0.1589  3   PHE A CE1 
18   C CE2 . PHE A 9   ? 0.6823 0.4825 0.5759 -0.0254 -0.0140 0.1640  3   PHE A CE2 
19   C CZ  . PHE A 9   ? 0.6995 0.5052 0.5451 -0.0464 -0.0213 0.1605  3   PHE A CZ  
20   N N   . ILE A 10  ? 0.5304 0.2928 0.4355 -0.0618 0.0391  0.0899  4   ILE A N   
21   C CA  . ILE A 10  ? 0.4918 0.2748 0.4110 -0.0520 0.0327  0.0683  4   ILE A CA  
22   C C   . ILE A 10  ? 0.4164 0.2422 0.3326 -0.0497 0.0277  0.0646  4   ILE A C   
23   O O   . ILE A 10  ? 0.4831 0.3212 0.3895 -0.0620 0.0367  0.0662  4   ILE A O   
24   C CB  . ILE A 10  ? 0.4656 0.2417 0.3955 -0.0688 0.0328  0.0475  4   ILE A CB  
25   C CG1 . ILE A 10  ? 0.5193 0.2447 0.4413 -0.0854 0.0382  0.0522  4   ILE A CG1 
26   C CG2 . ILE A 10  ? 0.5386 0.3079 0.4640 -0.0562 0.0267  0.0294  4   ILE A CG2 
27   C CD1 . ILE A 10  ? 0.6855 0.3992 0.6123 -0.1116 0.0287  0.0353  4   ILE A CD1 
28   N N   . LYS A 11  ? 0.3676 0.2094 0.2899 -0.0335 0.0181  0.0608  5   LYS A N   
29   C CA  . LYS A 11  ? 0.3416 0.2136 0.2558 -0.0326 0.0114  0.0569  5   LYS A CA  
30   C C   . LYS A 11  ? 0.3225 0.2120 0.2560 -0.0196 0.0067  0.0422  5   LYS A C   
31   O O   . LYS A 11  ? 0.3740 0.2505 0.3202 -0.0055 0.0076  0.0448  5   LYS A O   
32   C CB  . LYS A 11  ? 0.5194 0.3900 0.4124 -0.0327 -0.0033 0.0807  5   LYS A CB  
33   C CG  . LYS A 11  ? 0.5817 0.4684 0.4518 -0.0385 -0.0132 0.0759  5   LYS A CG  
34   N N   . THR A 12  ? 0.2973 0.2100 0.2305 -0.0225 0.0071  0.0285  6   THR A N   
35   C CA  . THR A 12  ? 0.2710 0.1999 0.2164 -0.0113 0.0019  0.0180  6   THR A CA  
36   C C   . THR A 12  ? 0.3109 0.2569 0.2440 -0.0141 -0.0012 0.0159  6   THR A C   
37   O O   . THR A 12  ? 0.3515 0.2890 0.2589 -0.0248 0.0044  0.0189  6   THR A O   
38   C CB  . THR A 12  ? 0.2948 0.2233 0.2507 -0.0136 0.0041  0.0011  6   THR A CB  
39   O OG1 . THR A 12  ? 0.3522 0.2862 0.3096 -0.0018 0.0008  -0.0065 6   THR A OG1 
40   C CG2 . THR A 12  ? 0.2587 0.2096 0.2269 -0.0244 0.0082  -0.0036 6   THR A CG2 
41   N N   . ILE A 13  ? 0.2877 0.2481 0.2308 -0.0054 -0.0069 0.0109  7   ILE A N   
42   C CA  . ILE A 13  ? 0.3014 0.2688 0.2297 -0.0093 -0.0086 0.0059  7   ILE A CA  
43   C C   . ILE A 13  ? 0.2488 0.2308 0.1960 -0.0002 -0.0048 -0.0073 7   ILE A C   
44   O O   . ILE A 13  ? 0.2522 0.2363 0.2139 0.0079  -0.0064 -0.0100 7   ILE A O   
45   C CB  . ILE A 13  ? 0.3677 0.3368 0.2865 -0.0142 -0.0265 0.0210  7   ILE A CB  
46   C CG1 . ILE A 13  ? 0.3496 0.3385 0.3074 0.0003  -0.0312 0.0294  7   ILE A CG1 
47   C CG2 . ILE A 13  ? 0.3544 0.3082 0.2499 -0.0269 -0.0382 0.0404  7   ILE A CG2 
48   C CD1 . ILE A 13  ? 0.4217 0.4258 0.3905 -0.0069 -0.0514 0.0504  7   ILE A CD1 
49   N N   . SER A 14  ? 0.2154 0.1993 0.1553 -0.0015 0.0025  -0.0145 8   SER A N   
50   C CA  . SER A 14  ? 0.1941 0.1935 0.1557 0.0069  0.0042  -0.0219 8   SER A CA  
51   C C   . SER A 14  ? 0.2174 0.2211 0.1815 0.0143  -0.0054 -0.0213 8   SER A C   
52   O O   . SER A 14  ? 0.2464 0.2477 0.2030 0.0121  -0.0112 -0.0141 8   SER A O   
53   C CB  . SER A 14  ? 0.2156 0.2128 0.1752 0.0093  0.0194  -0.0251 8   SER A CB  
54   O OG  . SER A 14  ? 0.2625 0.2371 0.1872 0.0048  0.0195  -0.0268 8   SER A OG  
55   N N   . PRO A 15  ? 0.2042 0.2121 0.1767 0.0202  -0.0082 -0.0255 9   PRO A N   
56   C CA  . PRO A 15  ? 0.1998 0.2041 0.1686 0.0289  -0.0087 -0.0235 9   PRO A CA  
57   C C   . PRO A 15  ? 0.2214 0.2342 0.1921 0.0320  -0.0089 -0.0223 9   PRO A C   
58   O O   . PRO A 15  ? 0.2226 0.2388 0.1949 0.0303  -0.0077 -0.0253 9   PRO A O   
59   C CB  . PRO A 15  ? 0.2525 0.2413 0.2071 0.0292  -0.0107 -0.0307 9   PRO A CB  
60   C CG  . PRO A 15  ? 0.2398 0.2430 0.2074 0.0194  -0.0201 -0.0325 9   PRO A CG  
61   C CD  . PRO A 15  ? 0.2530 0.2655 0.2354 0.0156  -0.0125 -0.0290 9   PRO A CD  
62   N N   . ILE A 16  ? 0.2250 0.2388 0.1995 0.0379  -0.0061 -0.0148 10  ILE A N   
63   C CA  . ILE A 16  ? 0.2202 0.2382 0.1964 0.0397  -0.0053 -0.0118 10  ILE A CA  
64   C C   . ILE A 16  ? 0.2679 0.2764 0.2306 0.0492  0.0012  -0.0141 10  ILE A C   
65   O O   . ILE A 16  ? 0.2951 0.2901 0.2490 0.0565  0.0122  -0.0123 10  ILE A O   
66   C CB  . ILE A 16  ? 0.2535 0.2823 0.2483 0.0346  -0.0081 0.0039  10  ILE A CB  
67   C CG1 . ILE A 16  ? 0.2695 0.2936 0.2542 0.0172  -0.0213 0.0050  10  ILE A CG1 
68   C CG2 . ILE A 16  ? 0.2784 0.3092 0.2776 0.0356  -0.0047 0.0094  10  ILE A CG2 
69   C CD1 . ILE A 16  ? 0.2519 0.2856 0.2512 0.0018  -0.0364 0.0242  10  ILE A CD1 
70   N N   . GLN A 17  ? 0.2485 0.2563 0.2033 0.0497  -0.0034 -0.0166 11  GLN A N   
71   C CA  . GLN A 17  ? 0.2366 0.2293 0.1647 0.0536  -0.0044 -0.0174 11  GLN A CA  
72   C C   . GLN A 17  ? 0.2641 0.2552 0.1898 0.0587  0.0024  -0.0087 11  GLN A C   
73   O O   . GLN A 17  ? 0.2844 0.2852 0.2286 0.0572  0.0003  -0.0050 11  GLN A O   
74   C CB  . GLN A 17  ? 0.2520 0.2504 0.1802 0.0474  -0.0223 -0.0192 11  GLN A CB  
75   C CG  . GLN A 17  ? 0.3272 0.3076 0.2197 0.0435  -0.0354 -0.0164 11  GLN A CG  
76   C CD  . GLN A 17  ? 0.3366 0.3306 0.2419 0.0311  -0.0610 -0.0119 11  GLN A CD  
77   O OE1 . GLN A 17  ? 0.3229 0.3381 0.2648 0.0277  -0.0616 -0.0126 11  GLN A OE1 
78   N NE2 . GLN A 17  ? 0.3304 0.3118 0.2052 0.0213  -0.0839 -0.0038 11  GLN A NE2 
79   N N   . LYS A 18  ? 0.2818 0.2516 0.1772 0.0642  0.0142  -0.0056 12  LYS A N   
80   C CA  . LYS A 18  ? 0.3082 0.2733 0.1984 0.0687  0.0244  0.0053  12  LYS A CA  
81   C C   . LYS A 18  ? 0.3406 0.2930 0.2004 0.0669  0.0090  0.0076  12  LYS A C   
82   O O   . LYS A 18  ? 0.4077 0.3416 0.2298 0.0614  -0.0049 0.0028  12  LYS A O   
83   C CB  . LYS A 18  ? 0.3768 0.3220 0.2497 0.0780  0.0537  0.0118  12  LYS A CB  
84   C CG  . LYS A 18  ? 0.4604 0.4122 0.3504 0.0818  0.0711  0.0290  12  LYS A CG  
85   C CD  . LYS A 18  ? 0.5261 0.4657 0.4184 0.0953  0.1098  0.0406  12  LYS A CD  
86   C CE  . LYS A 18  ? 0.6487 0.5994 0.5672 0.0980  0.1310  0.0630  12  LYS A CE  
87   N NZ  . LYS A 18  ? 0.7118 0.6406 0.6279 0.1128  0.1719  0.0754  12  LYS A NZ  
88   N N   . ILE A 19  ? 0.3040 0.2630 0.1791 0.0690  0.0086  0.0179  13  ILE A N   
89   C CA  . ILE A 19  ? 0.3188 0.2694 0.1752 0.0699  -0.0070 0.0276  13  ILE A CA  
90   C C   . ILE A 19  ? 0.3729 0.3090 0.2180 0.0740  0.0075  0.0411  13  ILE A C   
91   O O   . ILE A 19  ? 0.3681 0.3117 0.2426 0.0735  0.0225  0.0439  13  ILE A O   
92   C CB  . ILE A 19  ? 0.3880 0.3616 0.2876 0.0720  -0.0217 0.0306  13  ILE A CB  
93   C CG1 . ILE A 19  ? 0.3810 0.3528 0.2803 0.0772  -0.0364 0.0500  13  ILE A CG1 
94   C CG2 . ILE A 19  ? 0.4947 0.4725 0.4261 0.0731  -0.0065 0.0258  13  ILE A CG2 
95   C CD1 . ILE A 19  ? 0.4732 0.4700 0.4257 0.0845  -0.0453 0.0596  13  ILE A CD1 
96   N N   . ASN A 20  ? 0.3612 0.2741 0.1606 0.0742  -0.0004 0.0520  14  ASN A N   
97   C CA  . ASN A 20  ? 0.3900 0.2840 0.1713 0.0776  0.0130  0.0682  14  ASN A CA  
98   C C   . ASN A 20  ? 0.3954 0.2925 0.1872 0.0809  -0.0102 0.0849  14  ASN A C   
99   O O   . ASN A 20  ? 0.4666 0.3594 0.2312 0.0771  -0.0375 0.0935  14  ASN A O   
100  C CB  . ASN A 20  ? 0.4986 0.3513 0.2044 0.0761  0.0286  0.0709  14  ASN A CB  
101  C CG  . ASN A 20  ? 0.6291 0.4607 0.3146 0.0792  0.0477  0.0900  14  ASN A CG  
102  O OD1 . ASN A 20  ? 0.6102 0.4511 0.3242 0.0812  0.0382  0.1041  14  ASN A OD1 
103  N ND2 . ASN A 20  ? 0.7620 0.5674 0.4133 0.0778  0.0763  0.0870  14  ASN A ND2 
104  N N   . PHE A 21  ? 0.4039 0.3050 0.2351 0.0865  -0.0005 0.0925  15  PHE A N   
105  C CA  . PHE A 21  ? 0.4274 0.3262 0.2773 0.0956  -0.0137 0.1123  15  PHE A CA  
106  C C   . PHE A 21  ? 0.4622 0.3318 0.2892 0.0968  0.0005  0.1300  15  PHE A C   
107  O O   . PHE A 21  ? 0.4686 0.3280 0.3160 0.0942  0.0212  0.1273  15  PHE A O   
108  C CB  . PHE A 21  ? 0.3927 0.3034 0.2987 0.1030  -0.0072 0.1054  15  PHE A CB  
109  C CG  . PHE A 21  ? 0.4693 0.3766 0.4066 0.1192  -0.0121 0.1285  15  PHE A CG  
110  C CD1 . PHE A 21  ? 0.4795 0.3535 0.4193 0.1258  0.0058  0.1392  15  PHE A CD1 
111  C CD2 . PHE A 21  ? 0.5293 0.4671 0.5010 0.1263  -0.0336 0.1419  15  PHE A CD2 
112  C CE1 . PHE A 21  ? 0.5821 0.4540 0.5567 0.1374  0.0051  0.1544  15  PHE A CE1 
113  C CE2 . PHE A 21  ? 0.4618 0.4034 0.4762 0.1367  -0.0351 0.1594  15  PHE A CE2 
114  C CZ  . PHE A 21  ? 0.5071 0.4150 0.5211 0.1444  -0.0141 0.1652  15  PHE A CZ  
115  N N   . ASN A 22  ? 0.4853 0.3391 0.2672 0.0952  -0.0134 0.1479  16  ASN A N   
116  C CA  . ASN A 22  ? 0.5300 0.3584 0.2907 0.0922  -0.0016 0.1642  16  ASN A CA  
117  C C   . ASN A 22  ? 0.6379 0.4529 0.3864 0.0868  0.0340  0.1572  16  ASN A C   
118  O O   . ASN A 22  ? 0.6599 0.4619 0.4229 0.0846  0.0509  0.1680  16  ASN A O   
119  C CB  . ASN A 22  ? 0.6107 0.4351 0.4170 0.1018  -0.0031 0.1797  16  ASN A CB  
120  C CG  . ASN A 22  ? 0.6562 0.4974 0.4874 0.1081  -0.0356 0.1962  16  ASN A CG  
121  O OD1 . ASN A 22  ? 0.6604 0.5048 0.4579 0.0978  -0.0645 0.2081  16  ASN A OD1 
122  N ND2 . ASN A 22  ? 0.7238 0.5722 0.6136 0.1224  -0.0301 0.1978  16  ASN A ND2 
123  N N   . GLY A 23  ? 0.5366 0.3569 0.2664 0.0834  0.0461  0.1415  17  GLY A N   
124  C CA  . GLY A 23  ? 0.5213 0.3407 0.2586 0.0798  0.0816  0.1407  17  GLY A CA  
125  C C   . GLY A 23  ? 0.5600 0.4092 0.3620 0.0756  0.0891  0.1327  17  GLY A C   
126  O O   . GLY A 23  ? 0.5431 0.4052 0.3684 0.0717  0.1142  0.1366  17  GLY A O   
127  N N   . PHE A 24  ? 0.5099 0.3720 0.3463 0.0743  0.0674  0.1221  18  PHE A N   
128  C CA  . PHE A 24  ? 0.4293 0.3126 0.3141 0.0636  0.0666  0.1097  18  PHE A CA  
129  C C   . PHE A 24  ? 0.3601 0.2663 0.2484 0.0667  0.0573  0.0908  18  PHE A C   
130  O O   . PHE A 24  ? 0.3882 0.2966 0.2713 0.0729  0.0396  0.0810  18  PHE A O   
131  C CB  . PHE A 24  ? 0.4466 0.3120 0.3482 0.0598  0.0568  0.1066  18  PHE A CB  
132  C CG  . PHE A 24  ? 0.4480 0.3200 0.3750 0.0443  0.0515  0.0912  18  PHE A CG  
133  C CD1 . PHE A 24  ? 0.4662 0.3302 0.3928 0.0491  0.0432  0.0748  18  PHE A CD1 
134  C CD2 . PHE A 24  ? 0.4224 0.3086 0.3740 0.0235  0.0546  0.0973  18  PHE A CD2 
135  C CE1 . PHE A 24  ? 0.4599 0.3182 0.3913 0.0319  0.0385  0.0605  18  PHE A CE1 
136  C CE2 . PHE A 24  ? 0.4286 0.3171 0.3940 0.0036  0.0414  0.0867  18  PHE A CE2 
137  C CZ  . PHE A 24  ? 0.3823 0.2510 0.3281 0.0070  0.0336  0.0663  18  PHE A CZ  
138  N N   . GLU A 25  ? 0.3910 0.3159 0.2962 0.0631  0.0709  0.0900  19  GLU A N   
139  C CA  . GLU A 25  ? 0.3387 0.2806 0.2484 0.0660  0.0653  0.0745  19  GLU A CA  
140  C C   . GLU A 25  ? 0.3330 0.2940 0.2831 0.0535  0.0511  0.0666  19  GLU A C   
141  O O   . GLU A 25  ? 0.3381 0.3087 0.3206 0.0389  0.0526  0.0777  19  GLU A O   
142  C CB  . GLU A 25  ? 0.4053 0.3510 0.3141 0.0727  0.0926  0.0814  19  GLU A CB  
143  C CG  . GLU A 25  ? 0.4948 0.4021 0.3376 0.0831  0.1122  0.0856  19  GLU A CG  
144  C CD  . GLU A 25  ? 0.6631 0.5621 0.5039 0.0938  0.1546  0.0953  19  GLU A CD  
145  O OE1 . GLU A 25  ? 0.7493 0.6757 0.6395 0.0969  0.1624  0.0958  19  GLU A OE1 
146  O OE2 . GLU A 25  ? 0.7649 0.6315 0.5674 0.0978  0.1738  0.0996  19  GLU A OE2 
147  N N   . PHE A 26  ? 0.2769 0.2401 0.2213 0.0556  0.0360  0.0500  20  PHE A N   
148  C CA  . PHE A 26  ? 0.2756 0.2461 0.2402 0.0431  0.0253  0.0412  20  PHE A CA  
149  C C   . PHE A 26  ? 0.2506 0.2338 0.2124 0.0488  0.0191  0.0280  20  PHE A C   
150  O O   . PHE A 26  ? 0.2843 0.2684 0.2297 0.0591  0.0221  0.0256  20  PHE A O   
151  C CB  . PHE A 26  ? 0.3096 0.2517 0.2645 0.0372  0.0210  0.0361  20  PHE A CB  
152  C CG  . PHE A 26  ? 0.3125 0.2457 0.2578 0.0543  0.0207  0.0308  20  PHE A CG  
153  C CD1 . PHE A 26  ? 0.3172 0.2462 0.2551 0.0673  0.0212  0.0431  20  PHE A CD1 
154  C CD2 . PHE A 26  ? 0.3214 0.2518 0.2693 0.0565  0.0200  0.0187  20  PHE A CD2 
155  C CE1 . PHE A 26  ? 0.3509 0.2819 0.2962 0.0816  0.0154  0.0473  20  PHE A CE1 
156  C CE2 . PHE A 26  ? 0.3027 0.2354 0.2619 0.0733  0.0219  0.0218  20  PHE A CE2 
157  C CZ  . PHE A 26  ? 0.3485 0.2856 0.3124 0.0855  0.0169  0.0381  20  PHE A CZ  
158  N N   . TYR A 27  ? 0.2328 0.2177 0.2018 0.0386  0.0104  0.0196  21  TYR A N   
159  C CA  . TYR A 27  ? 0.2494 0.2462 0.2196 0.0411  0.0060  0.0103  21  TYR A CA  
160  C C   . TYR A 27  ? 0.2424 0.2266 0.2032 0.0402  0.0032  -0.0014 21  TYR A C   
161  O O   . TYR A 27  ? 0.2646 0.2245 0.2139 0.0327  0.0062  -0.0038 21  TYR A O   
162  C CB  . TYR A 27  ? 0.2245 0.2378 0.2156 0.0305  0.0016  0.0184  21  TYR A CB  
163  C CG  . TYR A 27  ? 0.2076 0.2374 0.2237 0.0367  0.0142  0.0364  21  TYR A CG  
164  C CD1 . TYR A 27  ? 0.2314 0.2656 0.2502 0.0516  0.0285  0.0380  21  TYR A CD1 
165  C CD2 . TYR A 27  ? 0.2547 0.2893 0.2902 0.0280  0.0167  0.0530  21  TYR A CD2 
166  C CE1 . TYR A 27  ? 0.2085 0.2504 0.2494 0.0624  0.0520  0.0562  21  TYR A CE1 
167  C CE2 . TYR A 27  ? 0.2548 0.3074 0.3219 0.0364  0.0366  0.0742  21  TYR A CE2 
168  C CZ  . TYR A 27  ? 0.2872 0.3425 0.3567 0.0559  0.0574  0.0757  21  TYR A CZ  
169  O OH  . TYR A 27  ? 0.3560 0.4216 0.4556 0.0690  0.0882  0.0982  21  TYR A OH  
170  N N   . ILE A 28  ? 0.2292 0.2239 0.1926 0.0472  0.0014  -0.0077 22  ILE A N   
171  C CA  . ILE A 28  ? 0.2078 0.1966 0.1737 0.0488  0.0060  -0.0141 22  ILE A CA  
172  C C   . ILE A 28  ? 0.2390 0.2349 0.2036 0.0413  0.0032  -0.0199 22  ILE A C   
173  O O   . ILE A 28  ? 0.2339 0.2442 0.2040 0.0424  -0.0033 -0.0195 22  ILE A O   
174  C CB  . ILE A 28  ? 0.2374 0.2399 0.2232 0.0616  0.0045  -0.0078 22  ILE A CB  
175  C CG1 . ILE A 28  ? 0.3708 0.3637 0.3582 0.0706  0.0066  0.0026  22  ILE A CG1 
176  C CG2 . ILE A 28  ? 0.2284 0.2327 0.2341 0.0664  0.0172  -0.0082 22  ILE A CG2 
177  C CD1 . ILE A 28  ? 0.4045 0.4183 0.4142 0.0799  -0.0063 0.0177  22  ILE A CD1 
178  N N   . LYS A 29  ? 0.2184 0.1939 0.1662 0.0330  0.0104  -0.0253 23  LYS A N   
179  C CA  . LYS A 29  ? 0.2286 0.2055 0.1700 0.0260  0.0099  -0.0285 23  LYS A CA  
180  C C   . LYS A 29  ? 0.2339 0.2212 0.1965 0.0362  0.0225  -0.0291 23  LYS A C   
181  O O   . LYS A 29  ? 0.2198 0.1902 0.1816 0.0430  0.0428  -0.0295 23  LYS A O   
182  C CB  . LYS A 29  ? 0.2392 0.1805 0.1388 0.0083  0.0105  -0.0317 23  LYS A CB  
183  C CG  . LYS A 29  ? 0.2736 0.2046 0.1522 -0.0006 0.0130  -0.0334 23  LYS A CG  
184  C CD  . LYS A 29  ? 0.2564 0.2165 0.1565 -0.0037 -0.0057 -0.0237 23  LYS A CD  
185  C CE  . LYS A 29  ? 0.2665 0.2054 0.1320 -0.0192 -0.0094 -0.0207 23  LYS A CE  
186  N NZ  . LYS A 29  ? 0.2450 0.2095 0.1389 -0.0153 -0.0189 -0.0103 23  LYS A NZ  
187  N N   . ARG A 30  ? 0.2379 0.2080 0.1964 0.0296  -0.0005 -0.0095 24  ARG A N   
188  C CA  . ARG A 30  ? 0.2679 0.2172 0.2276 0.0279  -0.0077 -0.0121 24  ARG A CA  
189  C C   . ARG A 30  ? 0.2335 0.1844 0.2051 0.0248  -0.0078 -0.0122 24  ARG A C   
190  O O   . ARG A 30  ? 0.2393 0.1747 0.2037 0.0235  -0.0079 -0.0140 24  ARG A O   
191  C CB  . ARG A 30  ? 0.2351 0.1642 0.1771 0.0322  -0.0097 -0.0147 24  ARG A CB  
192  C CG  . ARG A 30  ? 0.2837 0.2079 0.2117 0.0351  -0.0106 -0.0151 24  ARG A CG  
193  C CD  . ARG A 30  ? 0.2888 0.2118 0.2176 0.0315  -0.0179 -0.0158 24  ARG A CD  
194  N NE  . ARG A 30  ? 0.2776 0.2048 0.2134 0.0274  -0.0270 -0.0195 24  ARG A NE  
195  C CZ  . ARG A 30  ? 0.3062 0.2301 0.2304 0.0238  -0.0344 -0.0246 24  ARG A CZ  
196  N NH1 . ARG A 30  ? 0.3291 0.2347 0.2304 0.0265  -0.0332 -0.0263 24  ARG A NH1 
197  N NH2 . ARG A 30  ? 0.2971 0.2418 0.2316 0.0156  -0.0428 -0.0289 24  ARG A NH2 
198  N N   . ASP A 31  ? 0.1904 0.1545 0.1744 0.0209  -0.0061 -0.0110 25  ASP A N   
199  C CA  . ASP A 31  ? 0.2147 0.1822 0.2096 0.0180  -0.0052 -0.0108 25  ASP A CA  
200  C C   . ASP A 31  ? 0.2621 0.2296 0.2647 0.0129  -0.0106 -0.0139 25  ASP A C   
201  O O   . ASP A 31  ? 0.2373 0.2089 0.2474 0.0070  -0.0088 -0.0146 25  ASP A O   
202  C CB  . ASP A 31  ? 0.2282 0.2083 0.2298 0.0145  -0.0012 -0.0099 25  ASP A CB  
203  C CG  . ASP A 31  ? 0.2042 0.2025 0.2036 0.0161  0.0035  -0.0076 25  ASP A CG  
204  O OD1 . ASP A 31  ? 0.2230 0.2252 0.2146 0.0260  0.0046  -0.0050 25  ASP A OD1 
205  O OD2 . ASP A 31  ? 0.1986 0.2100 0.2008 0.0092  0.0065  -0.0084 25  ASP A OD2 
206  N N   . ASP A 32  ? 0.2242 0.1938 0.2244 0.0149  -0.0168 -0.0157 26  ASP A N   
207  C CA  . ASP A 32  ? 0.2391 0.2267 0.2480 0.0099  -0.0234 -0.0193 26  ASP A CA  
208  C C   . ASP A 32  ? 0.2680 0.2456 0.2678 -0.0059 -0.0234 -0.0248 26  ASP A C   
209  O O   . ASP A 32  ? 0.2875 0.2870 0.2950 -0.0198 -0.0270 -0.0299 26  ASP A O   
210  C CB  . ASP A 32  ? 0.2173 0.2145 0.2209 0.0198  -0.0310 -0.0190 26  ASP A CB  
211  C CG  . ASP A 32  ? 0.2513 0.2271 0.2352 0.0203  -0.0326 -0.0199 26  ASP A CG  
212  O OD1 . ASP A 32  ? 0.2568 0.2130 0.2320 0.0207  -0.0258 -0.0181 26  ASP A OD1 
213  O OD2 . ASP A 32  ? 0.2887 0.2742 0.2657 0.0215  -0.0407 -0.0224 26  ASP A OD2 
214  N N   . LEU A 33  ? 0.2479 0.1929 0.2269 -0.0044 -0.0177 -0.0240 27  LEU A N   
215  C CA  . LEU A 33  ? 0.2700 0.1832 0.2229 -0.0172 -0.0132 -0.0289 27  LEU A CA  
216  C C   . LEU A 33  ? 0.3071 0.1981 0.2497 -0.0207 -0.0024 -0.0263 27  LEU A C   
217  O O   . LEU A 33  ? 0.3901 0.2356 0.2966 -0.0276 0.0062  -0.0286 27  LEU A O   
218  C CB  . LEU A 33  ? 0.2853 0.1667 0.2099 -0.0058 -0.0100 -0.0283 27  LEU A CB  
219  C CG  . LEU A 33  ? 0.3296 0.2247 0.2562 -0.0019 -0.0188 -0.0303 27  LEU A CG  
220  C CD1 . LEU A 33  ? 0.3632 0.2283 0.2608 0.0111  -0.0130 -0.0292 27  LEU A CD1 
221  C CD2 . LEU A 33  ? 0.3673 0.2770 0.2934 -0.0211 -0.0282 -0.0391 27  LEU A CD2 
222  N N   . LEU A 34  ? 0.3037 0.2178 0.2692 -0.0153 -0.0011 -0.0214 28  LEU A N   
223  C CA  . LEU A 34  ? 0.3404 0.2334 0.2930 -0.0152 0.0093  -0.0174 28  LEU A CA  
224  C C   . LEU A 34  ? 0.3683 0.2475 0.3099 -0.0415 0.0146  -0.0231 28  LEU A C   
225  O O   . LEU A 34  ? 0.4734 0.3150 0.3876 -0.0434 0.0266  -0.0199 28  LEU A O   
226  C CB  . LEU A 34  ? 0.2659 0.1890 0.2433 -0.0050 0.0092  -0.0119 28  LEU A CB  
227  C CG  . LEU A 34  ? 0.2862 0.2206 0.2646 0.0141  0.0086  -0.0067 28  LEU A CG  
228  C CD1 . LEU A 34  ? 0.3251 0.2879 0.3234 0.0146  0.0082  -0.0050 28  LEU A CD1 
229  C CD2 . LEU A 34  ? 0.3538 0.2645 0.3027 0.0311  0.0167  -0.0007 28  LEU A CD2 
230  N N   . GLY A 35  ? 0.3568 0.2681 0.3153 -0.0619 0.0072  -0.0312 29  GLY A N   
231  C CA  . GLY A 35  ? 0.4291 0.3397 0.3780 -0.0946 0.0131  -0.0387 29  GLY A CA  
232  C C   . GLY A 35  ? 0.3365 0.3211 0.3279 -0.1042 0.0048  -0.0424 29  GLY A C   
233  O O   . GLY A 35  ? 0.3332 0.3588 0.3533 -0.0832 -0.0056 -0.0393 29  GLY A O   
234  N N   . GLU A 36  ? 0.3560 0.3560 0.3453 -0.1360 0.0115  -0.0489 30  GLU A N   
235  C CA  . GLU A 36  ? 0.3597 0.4421 0.3899 -0.1429 0.0058  -0.0518 30  GLU A CA  
236  C C   . GLU A 36  ? 0.3344 0.4386 0.3932 -0.1080 0.0046  -0.0415 30  GLU A C   
237  O O   . GLU A 36  ? 0.3898 0.5507 0.4777 -0.0895 -0.0038 -0.0400 30  GLU A O   
238  C CB  . GLU A 36  ? 0.3475 0.4412 0.3688 -0.1845 0.0175  -0.0594 30  GLU A CB  
239  C CG  . GLU A 36  ? 0.5799 0.7438 0.6135 -0.2203 0.0111  -0.0726 30  GLU A CG  
240  C CD  . GLU A 36  ? 0.6532 0.8521 0.6906 -0.2436 0.0221  -0.0749 30  GLU A CD  
241  O OE1 . GLU A 36  ? 0.6684 0.9571 0.7449 -0.2335 0.0153  -0.0745 30  GLU A OE1 
242  O OE2 . GLU A 36  ? 0.7245 0.8563 0.7201 -0.2656 0.0385  -0.0757 30  GLU A OE2 
243  N N   . ILE A 37  ? 0.2569 0.3136 0.3014 -0.0970 0.0140  -0.0344 31  ILE A N   
244  C CA  . ILE A 37  ? 0.2301 0.2920 0.2902 -0.0665 0.0129  -0.0262 31  ILE A CA  
245  C C   . ILE A 37  ? 0.2494 0.2773 0.2962 -0.0471 0.0078  -0.0225 31  ILE A C   
246  O O   . ILE A 37  ? 0.2822 0.2657 0.3026 -0.0479 0.0123  -0.0207 31  ILE A O   
247  C CB  . ILE A 37  ? 0.3160 0.3571 0.3681 -0.0670 0.0248  -0.0214 31  ILE A CB  
248  C CG1 . ILE A 37  ? 0.3351 0.3994 0.3910 -0.0943 0.0337  -0.0256 31  ILE A CG1 
249  C CG2 . ILE A 37  ? 0.3448 0.4016 0.4128 -0.0426 0.0238  -0.0163 31  ILE A CG2 
250  C CD1 . ILE A 37  ? 0.4055 0.4468 0.4498 -0.0936 0.0463  -0.0200 31  ILE A CD1 
251  N N   . ASN A 38  ? 0.2221 0.2693 0.2821 -0.0282 0.0002  -0.0209 32  ASN A N   
252  C CA  . ASN A 38  ? 0.2036 0.2241 0.2503 -0.0156 -0.0034 -0.0185 32  ASN A CA  
253  C C   . ASN A 38  ? 0.2356 0.2596 0.2864 0.0020  -0.0034 -0.0148 32  ASN A C   
254  O O   . ASN A 38  ? 0.2191 0.2603 0.2793 0.0089  -0.0006 -0.0139 32  ASN A O   
255  C CB  . ASN A 38  ? 0.2408 0.2625 0.2808 -0.0199 -0.0114 -0.0228 32  ASN A CB  
256  C CG  . ASN A 38  ? 0.2750 0.3405 0.3316 -0.0134 -0.0197 -0.0244 32  ASN A CG  
257  O OD1 . ASN A 38  ? 0.2539 0.3224 0.3115 0.0075  -0.0212 -0.0200 32  ASN A OD1 
258  N ND2 . ASN A 38  ? 0.2982 0.3977 0.3620 -0.0315 -0.0238 -0.0310 32  ASN A ND2 
259  N N   . GLY A 39  ? 0.2077 0.2115 0.2455 0.0079  -0.0040 -0.0132 33  GLY A N   
260  C CA  . GLY A 39  ? 0.2197 0.2157 0.2497 0.0168  -0.0018 -0.0117 33  GLY A CA  
261  C C   . GLY A 39  ? 0.2337 0.2264 0.2613 0.0148  0.0058  -0.0112 33  GLY A C   
262  O O   . GLY A 39  ? 0.2082 0.2055 0.2394 0.0091  0.0083  -0.0104 33  GLY A O   
263  N N   . ASN A 40  ? 0.2249 0.2037 0.2389 0.0208  0.0106  -0.0114 34  ASN A N   
264  C CA  . ASN A 40  ? 0.1943 0.1613 0.1956 0.0160  0.0191  -0.0131 34  ASN A CA  
265  C C   . ASN A 40  ? 0.2491 0.2344 0.2663 0.0155  0.0212  -0.0124 34  ASN A C   
266  O O   . ASN A 40  ? 0.2262 0.2159 0.2419 0.0066  0.0236  -0.0129 34  ASN A O   
267  C CB  . ASN A 40  ? 0.2292 0.1639 0.2024 0.0268  0.0266  -0.0133 34  ASN A CB  
268  C CG  . ASN A 40  ? 0.2722 0.1808 0.2194 0.0187  0.0380  -0.0171 34  ASN A CG  
269  O OD1 . ASN A 40  ? 0.2951 0.2161 0.2517 0.0200  0.0408  -0.0175 34  ASN A OD1 
270  N ND2 . ASN A 40  ? 0.3126 0.1804 0.2209 0.0076  0.0462  -0.0207 34  ASN A ND2 
286  N N   . LLP A 41  ? 0.2110 0.2136 0.2427 0.0249  0.0207  -0.0112 35  LLP A N   
287  C CA  . LLP A 41  ? 0.2025 0.2222 0.2462 0.0221  0.0255  -0.0108 35  LLP A CA  
288  C CB  . LLP A 41  ? 0.1866 0.2365 0.2449 0.0343  0.0268  -0.0101 35  LLP A CB  
289  C CG  . LLP A 41  ? 0.2203 0.2566 0.2596 0.0588  0.0319  -0.0086 35  LLP A CG  
290  C CD  . LLP A 41  ? 0.2320 0.2268 0.2414 0.0592  0.0430  -0.0102 35  LLP A CD  
291  C CE  . LLP A 41  ? 0.2740 0.2361 0.2488 0.0857  0.0527  -0.0085 35  LLP A CE  
292  N NZ  . LLP A 41  ? 0.2899 0.2234 0.2435 0.0912  0.0493  -0.0070 35  LLP A NZ  
293  C C   . LLP A 41  ? 0.2015 0.2274 0.2536 0.0083  0.0236  -0.0098 35  LLP A C   
294  O O   . LLP A 41  ? 0.2114 0.2384 0.2625 0.0038  0.0294  -0.0086 35  LLP A O   
295  N N   . ALA A 42  ? 0.1950 0.2170 0.2474 0.0038  0.0174  -0.0098 36  ALA A N   
296  C CA  . ALA A 42  ? 0.2451 0.2550 0.2895 -0.0039 0.0192  -0.0077 36  ALA A CA  
297  C C   . ALA A 42  ? 0.2334 0.2356 0.2645 0.0015  0.0215  -0.0044 36  ALA A C   
298  O O   . ALA A 42  ? 0.2327 0.2285 0.2537 0.0023  0.0266  -0.0005 36  ALA A O   
299  C CB  . ALA A 42  ? 0.2404 0.2388 0.2784 -0.0072 0.0142  -0.0089 36  ALA A CB  
300  N N   . ARG A 43  ? 0.1824 0.1884 0.2099 0.0044  0.0183  -0.0059 37  ARG A N   
301  C CA  . ARG A 43  ? 0.1932 0.2106 0.2108 0.0050  0.0197  -0.0047 37  ARG A CA  
302  C C   . ARG A 43  ? 0.2077 0.2300 0.2225 0.0014  0.0248  -0.0056 37  ARG A C   
303  O O   . ARG A 43  ? 0.1991 0.2319 0.2067 0.0049  0.0266  -0.0018 37  ARG A O   
304  C CB  . ARG A 43  ? 0.1888 0.2128 0.2007 -0.0006 0.0175  -0.0087 37  ARG A CB  
305  C CG  . ARG A 43  ? 0.1630 0.1854 0.1751 0.0043  0.0132  -0.0073 37  ARG A CG  
306  C CD  . ARG A 43  ? 0.2075 0.2443 0.2143 0.0163  0.0131  -0.0018 37  ARG A CD  
307  N NE  . ARG A 43  ? 0.1944 0.2285 0.1969 0.0230  0.0110  -0.0009 37  ARG A NE  
308  C CZ  . ARG A 43  ? 0.2308 0.2697 0.2216 0.0403  0.0128  0.0046  37  ARG A CZ  
309  N NH1 . ARG A 43  ? 0.1940 0.2399 0.1742 0.0546  0.0165  0.0108  37  ARG A NH1 
310  N NH2 . ARG A 43  ? 0.2048 0.2383 0.1890 0.0468  0.0122  0.0046  37  ARG A NH2 
311  N N   . LYS A 44  ? 0.1950 0.2080 0.2112 -0.0017 0.0281  -0.0096 38  LYS A N   
312  C CA  . LYS A 44  ? 0.2076 0.2207 0.2169 -0.0041 0.0347  -0.0111 38  LYS A CA  
313  C C   . LYS A 44  ? 0.2356 0.2541 0.2512 -0.0010 0.0379  -0.0059 38  LYS A C   
314  O O   . LYS A 44  ? 0.2249 0.2477 0.2306 -0.0020 0.0420  -0.0049 38  LYS A O   
315  C CB  . LYS A 44  ? 0.2219 0.2182 0.2257 -0.0003 0.0405  -0.0148 38  LYS A CB  
316  C CG  . LYS A 44  ? 0.2154 0.1872 0.1945 -0.0059 0.0428  -0.0203 38  LYS A CG  
317  C CD  . LYS A 44  ? 0.2505 0.1912 0.2053 0.0015  0.0540  -0.0234 38  LYS A CD  
318  C CE  . LYS A 44  ? 0.2905 0.1884 0.2035 -0.0097 0.0612  -0.0299 38  LYS A CE  
319  N NZ  . LYS A 44  ? 0.3294 0.2022 0.2327 0.0059  0.0620  -0.0267 38  LYS A NZ  
320  N N   . LEU A 45  ? 0.2259 0.2416 0.2523 -0.0006 0.0374  -0.0033 39  LEU A N   
321  C CA  . LEU A 45  ? 0.2553 0.2667 0.2791 -0.0043 0.0442  0.0006  39  LEU A CA  
322  C C   . LEU A 45  ? 0.2354 0.2309 0.2374 0.0011  0.0459  0.0074  39  LEU A C   
323  O O   . LEU A 45  ? 0.2735 0.2525 0.2613 -0.0016 0.0543  0.0118  39  LEU A O   
324  C CB  . LEU A 45  ? 0.2143 0.2296 0.2510 -0.0137 0.0450  -0.0013 39  LEU A CB  
325  C CG  . LEU A 45  ? 0.2592 0.3032 0.3159 -0.0137 0.0476  -0.0050 39  LEU A CG  
326  C CD1 . LEU A 45  ? 0.2850 0.3516 0.3574 -0.0243 0.0448  -0.0082 39  LEU A CD1 
327  C CD2 . LEU A 45  ? 0.2587 0.3087 0.3126 -0.0163 0.0585  -0.0034 39  LEU A CD2 
328  N N   . ALA A 46  ? 0.2244 0.2248 0.2189 0.0107  0.0398  0.0091  40  ALA A N   
329  C CA  . ALA A 46  ? 0.2769 0.2644 0.2462 0.0256  0.0423  0.0176  40  ALA A CA  
330  C C   . ALA A 46  ? 0.3011 0.2866 0.2514 0.0329  0.0491  0.0240  40  ALA A C   
331  O O   . ALA A 46  ? 0.3100 0.2618 0.2305 0.0426  0.0577  0.0322  40  ALA A O   
332  C CB  . ALA A 46  ? 0.2859 0.3000 0.2546 0.0377  0.0349  0.0183  40  ALA A CB  
333  N N   . PHE A 47  ? 0.2657 0.2793 0.2247 0.0281  0.0470  0.0202  41  PHE A N   
334  C CA  . PHE A 47  ? 0.2796 0.2943 0.2194 0.0345  0.0529  0.0257  41  PHE A CA  
335  C C   . PHE A 47  ? 0.3059 0.2825 0.2344 0.0280  0.0652  0.0296  41  PHE A C   
336  O O   . PHE A 47  ? 0.3538 0.3052 0.2500 0.0395  0.0736  0.0392  41  PHE A O   
337  C CB  . PHE A 47  ? 0.2516 0.2946 0.2003 0.0234  0.0504  0.0177  41  PHE A CB  
338  C CG  . PHE A 47  ? 0.2711 0.3152 0.2006 0.0274  0.0566  0.0219  41  PHE A CG  
339  C CD1 . PHE A 47  ? 0.3204 0.3445 0.2517 0.0181  0.0665  0.0204  41  PHE A CD1 
340  C CD2 . PHE A 47  ? 0.3181 0.3903 0.2271 0.0420  0.0526  0.0277  41  PHE A CD2 
341  C CE1 . PHE A 47  ? 0.3961 0.4187 0.3068 0.0215  0.0734  0.0245  41  PHE A CE1 
342  C CE2 . PHE A 47  ? 0.3562 0.4293 0.2435 0.0474  0.0580  0.0322  41  PHE A CE2 
343  C CZ  . PHE A 47  ? 0.3543 0.3977 0.2414 0.0360  0.0689  0.0305  41  PHE A CZ  
344  N N   . TYR A 48  ? 0.2797 0.2545 0.2311 0.0099  0.0676  0.0224  42  TYR A N   
345  C CA  . TYR A 48  ? 0.3468 0.3013 0.2919 -0.0037 0.0801  0.0238  42  TYR A CA  
346  C C   . TYR A 48  ? 0.3979 0.3098 0.3180 -0.0096 0.0871  0.0278  42  TYR A C   
347  O O   . TYR A 48  ? 0.4551 0.3331 0.3468 -0.0191 0.1013  0.0323  42  TYR A O   
348  C CB  . TYR A 48  ? 0.3090 0.2913 0.2878 -0.0176 0.0800  0.0149  42  TYR A CB  
349  C CG  . TYR A 48  ? 0.2901 0.2954 0.2785 -0.0105 0.0775  0.0107  42  TYR A CG  
350  C CD1 . TYR A 48  ? 0.2776 0.2845 0.2553 -0.0104 0.0866  0.0121  42  TYR A CD1 
351  C CD2 . TYR A 48  ? 0.2682 0.2848 0.2676 -0.0056 0.0683  0.0049  42  TYR A CD2 
352  C CE1 . TYR A 48  ? 0.3088 0.3267 0.2854 -0.0059 0.0863  0.0068  42  TYR A CE1 
353  C CE2 . TYR A 48  ? 0.2828 0.3047 0.2770 -0.0032 0.0695  -0.0004 42  TYR A CE2 
354  C CZ  . TYR A 48  ? 0.3125 0.3343 0.2947 -0.0033 0.0784  0.0001  42  TYR A CZ  
355  O OH  . TYR A 48  ? 0.3090 0.3270 0.2773 -0.0027 0.0814  -0.0065 42  TYR A OH  
356  N N   . ILE A 49  ? 0.3373 0.2437 0.2610 -0.0063 0.0795  0.0257  43  ILE A N   
357  C CA  . ILE A 49  ? 0.4181 0.2738 0.3085 -0.0127 0.0875  0.0280  43  ILE A CA  
358  C C   . ILE A 49  ? 0.5107 0.3182 0.3471 0.0117  0.0972  0.0407  43  ILE A C   
359  O O   . ILE A 49  ? 0.5834 0.3272 0.3720 0.0043  0.1128  0.0447  43  ILE A O   
360  C CB  . ILE A 49  ? 0.4261 0.2893 0.3318 -0.0122 0.0766  0.0223  43  ILE A CB  
361  C CG1 . ILE A 49  ? 0.4110 0.3144 0.3591 -0.0342 0.0697  0.0114  43  ILE A CG1 
362  C CG2 . ILE A 49  ? 0.4596 0.2598 0.3182 -0.0126 0.0857  0.0250  43  ILE A CG2 
363  C CD1 . ILE A 49  ? 0.3869 0.3097 0.3558 -0.0275 0.0562  0.0068  43  ILE A CD1 
364  N N   . HIS A 50  ? 0.4815 0.3183 0.3188 0.0408  0.0895  0.0471  44  HIS A N   
365  C CA  . HIS A 50  ? 0.6286 0.4340 0.4146 0.0739  0.0972  0.0613  44  HIS A CA  
366  C C   . HIS A 50  ? 0.6192 0.4019 0.3755 0.0751  0.1096  0.0689  44  HIS A C   
367  O O   . HIS A 50  ? 0.7284 0.4632 0.4268 0.1018  0.1215  0.0825  44  HIS A O   
368  C CB  . HIS A 50  ? 0.6076 0.4727 0.4091 0.1031  0.0830  0.0645  44  HIS A CB  
369  C CG  . HIS A 50  ? 0.7260 0.6038 0.5430 0.1075  0.0747  0.0601  44  HIS A CG  
370  N ND1 . HIS A 50  ? 0.7205 0.6658 0.5694 0.1148  0.0606  0.0564  44  HIS A ND1 
371  C CD2 . HIS A 50  ? 0.7545 0.5853 0.5560 0.1021  0.0796  0.0579  44  HIS A CD2 
372  C CE1 . HIS A 50  ? 0.6718 0.6115 0.5259 0.1168  0.0574  0.0534  44  HIS A CE1 
373  N NE2 . HIS A 50  ? 0.7569 0.6273 0.5827 0.1106  0.0682  0.0542  44  HIS A NE2 
374  N N   . GLN A 51  ? 0.4352 0.2669 0.3222 0.0137  0.0222  0.0072  45  GLN A N   
375  C CA  . GLN A 51  ? 0.4675 0.2881 0.3332 0.0222  0.0292  0.0281  45  GLN A CA  
376  C C   . GLN A 51  ? 0.4968 0.3120 0.3832 0.0100  0.0432  0.0405  45  GLN A C   
377  O O   . GLN A 51  ? 0.4678 0.2936 0.3818 -0.0060 0.0475  0.0310  45  GLN A O   
378  C CB  . GLN A 51  ? 0.4621 0.2950 0.3007 0.0297  0.0349  0.0321  45  GLN A CB  
379  C CG  . GLN A 51  ? 0.5366 0.3743 0.3576 0.0390  0.0236  0.0171  45  GLN A CG  
380  C CD  . GLN A 51  ? 0.7041 0.5291 0.5117 0.0492  0.0074  0.0133  45  GLN A CD  
381  O OE1 . GLN A 51  ? 0.7360 0.5525 0.5154 0.0602  0.0052  0.0250  45  GLN A OE1 
382  N NE2 . GLN A 51  ? 0.7338 0.5607 0.5617 0.0459  -0.0042 -0.0025 45  GLN A NE2 
383  N N   . ARG A 52  ? 0.4867 0.2861 0.3596 0.0167  0.0503  0.0623  46  ARG A N   
384  C CA  . ARG A 52  ? 0.5054 0.2979 0.3981 0.0048  0.0663  0.0775  46  ARG A CA  
385  C C   . ARG A 52  ? 0.5851 0.3842 0.4505 0.0118  0.0795  0.0982  46  ARG A C   
386  O O   . ARG A 52  ? 0.7302 0.5144 0.5696 0.0240  0.0815  0.1178  46  ARG A O   
387  C CB  . ARG A 52  ? 0.5894 0.3516 0.4985 0.0054  0.0661  0.0877  46  ARG A CB  
388  C CG  . ARG A 52  ? 0.6863 0.4418 0.6289 -0.0036 0.0585  0.0649  46  ARG A CG  
389  C CD  . ARG A 52  ? 0.6562 0.4266 0.6289 -0.0267 0.0668  0.0494  46  ARG A CD  
390  N NE  . ARG A 52  ? 0.6314 0.3970 0.6314 -0.0364 0.0614  0.0247  46  ARG A NE  
391  C CZ  . ARG A 52  ? 0.6532 0.4366 0.6507 -0.0366 0.0508  0.0028  46  ARG A CZ  
392  N NH1 . ARG A 52  ? 0.5772 0.3812 0.5494 -0.0276 0.0437  0.0030  46  ARG A NH1 
393  N NH2 . ARG A 52  ? 0.6234 0.4028 0.6442 -0.0457 0.0490  -0.0194 46  ARG A NH2 
394  N N   . TYR A 53  ? 0.5176 0.3415 0.3888 0.0048  0.0886  0.0943  47  TYR A N   
395  C CA  . TYR A 53  ? 0.5324 0.3672 0.3818 0.0114  0.1041  0.1104  47  TYR A CA  
396  C C   . TYR A 53  ? 0.6089 0.4406 0.4784 -0.0003 0.1233  0.1319  47  TYR A C   
397  O O   . TYR A 53  ? 0.6301 0.4593 0.5383 -0.0180 0.1248  0.1280  47  TYR A O   
398  C CB  . TYR A 53  ? 0.5231 0.3873 0.3775 0.0106  0.1069  0.0982  47  TYR A CB  
399  C CG  . TYR A 53  ? 0.4961 0.3625 0.3312 0.0219  0.0921  0.0794  47  TYR A CG  
400  C CD1 . TYR A 53  ? 0.5493 0.4099 0.3442 0.0388  0.0917  0.0798  47  TYR A CD1 
401  C CD2 . TYR A 53  ? 0.4911 0.3661 0.3483 0.0144  0.0793  0.0605  47  TYR A CD2 
402  C CE1 . TYR A 53  ? 0.5229 0.3839 0.3043 0.0471  0.0790  0.0610  47  TYR A CE1 
403  C CE2 . TYR A 53  ? 0.5214 0.3973 0.3646 0.0235  0.0677  0.0451  47  TYR A CE2 
404  C CZ  . TYR A 53  ? 0.5604 0.4282 0.3680 0.0393  0.0675  0.0449  47  TYR A CZ  
405  O OH  . TYR A 53  ? 0.5779 0.4446 0.3752 0.0464  0.0566  0.0282  47  TYR A OH  
406  N N   . PRO A 54  ? 0.5997 0.4314 0.4435 0.0081  0.1392  0.1536  48  PRO A N   
407  C CA  . PRO A 54  ? 0.6762 0.5081 0.5422 -0.0043 0.1608  0.1758  48  PRO A CA  
408  C C   . PRO A 54  ? 0.6434 0.5050 0.5540 -0.0230 0.1680  0.1659  48  PRO A C   
409  O O   . PRO A 54  ? 0.6014 0.4876 0.5158 -0.0213 0.1609  0.1483  48  PRO A O   
410  C CB  . PRO A 54  ? 0.7211 0.5570 0.5446 0.0107  0.1771  0.1966  48  PRO A CB  
411  C CG  . PRO A 54  ? 0.6913 0.5162 0.4669 0.0308  0.1596  0.1882  48  PRO A CG  
412  C CD  . PRO A 54  ? 0.6464 0.4789 0.4390 0.0284  0.1394  0.1578  48  PRO A CD  
413  N N   . LYS A 55  ? 0.6663 0.5258 0.6131 -0.0414 0.1817  0.1782  49  LYS A N   
414  C CA  . LYS A 55  ? 0.6522 0.5439 0.6454 -0.0618 0.1864  0.1686  49  LYS A CA  
415  C C   . LYS A 55  ? 0.6089 0.5371 0.5971 -0.0542 0.1993  0.1744  49  LYS A C   
416  O O   . LYS A 55  ? 0.6188 0.5454 0.5776 -0.0403 0.2124  0.1903  49  LYS A O   
417  C CB  . LYS A 55  ? 0.7054 0.5869 0.7394 -0.0841 0.2007  0.1814  49  LYS A CB  
418  C CG  . LYS A 55  ? 0.6959 0.6084 0.7827 -0.1100 0.1985  0.1647  49  LYS A CG  
419  N N   . ASN A 56  ? 0.5703 0.5336 0.5869 -0.0621 0.1921  0.1584  50  ASN A N   
420  C CA  . ASN A 56  ? 0.5863 0.5880 0.6089 -0.0543 0.2024  0.1616  50  ASN A CA  
421  C C   . ASN A 56  ? 0.5498 0.5444 0.5249 -0.0276 0.2010  0.1580  50  ASN A C   
422  O O   . ASN A 56  ? 0.5766 0.5920 0.5469 -0.0161 0.2155  0.1639  50  ASN A O   
423  C CB  . ASN A 56  ? 0.6114 0.6304 0.6542 -0.0611 0.2225  0.1789  50  ASN A CB  
424  C CG  . ASN A 56  ? 0.6717 0.6931 0.7602 -0.0887 0.2229  0.1802  50  ASN A CG  
425  O OD1 . ASN A 56  ? 0.7678 0.7791 0.8610 -0.0950 0.2343  0.1938  50  ASN A OD1 
426  N ND2 . ASN A 56  ? 0.6867 0.7212 0.8083 -0.1061 0.2101  0.1644  50  ASN A ND2 
427  N N   . GLN A 57  ? 0.5373 0.5034 0.4800 -0.0181 0.1830  0.1456  51  GLN A N   
428  C CA  . GLN A 57  ? 0.5214 0.4815 0.4242 0.0037  0.1778  0.1362  51  GLN A CA  
429  C C   . GLN A 57  ? 0.5244 0.5166 0.4476 0.0079  0.1773  0.1262  51  GLN A C   
430  O O   . GLN A 57  ? 0.5094 0.5219 0.4679 -0.0047 0.1664  0.1182  51  GLN A O   
431  C CB  . GLN A 57  ? 0.4787 0.4105 0.3590 0.0080  0.1548  0.1214  51  GLN A CB  
432  C CG  . GLN A 57  ? 0.5457 0.4720 0.3924 0.0263  0.1457  0.1068  51  GLN A CG  
433  C CD  . GLN A 57  ? 0.5363 0.4483 0.3349 0.0432  0.1557  0.1147  51  GLN A CD  
434  O OE1 . GLN A 57  ? 0.5872 0.4791 0.3633 0.0446  0.1555  0.1271  51  GLN A OE1 
435  N NE2 . GLN A 57  ? 0.5771 0.4994 0.3592 0.0564  0.1648  0.1077  51  GLN A NE2 
436  N N   . SER A 58  ? 0.5602 0.5568 0.4602 0.0263  0.1894  0.1266  52  SER A N   
437  C CA  . SER A 58  ? 0.5089 0.5317 0.4289 0.0342  0.1911  0.1193  52  SER A CA  
438  C C   . SER A 58  ? 0.4579 0.4623 0.3532 0.0467  0.1750  0.1004  52  SER A C   
439  O O   . SER A 58  ? 0.5134 0.4892 0.3659 0.0568  0.1715  0.0933  52  SER A O   
440  C CB  . SER A 58  ? 0.5655 0.6052 0.4852 0.0465  0.2154  0.1281  52  SER A CB  
441  O OG  . SER A 58  ? 0.6607 0.7329 0.6266 0.0330  0.2241  0.1404  52  SER A OG  
442  N N   . PHE A 59  ? 0.4142 0.4373 0.3382 0.0454  0.1651  0.0934  53  PHE A N   
443  C CA  . PHE A 59  ? 0.3774 0.3867 0.2882 0.0555  0.1520  0.0777  53  PHE A CA  
444  C C   . PHE A 59  ? 0.4516 0.4816 0.3836 0.0687  0.1630  0.0796  53  PHE A C   
445  O O   . PHE A 59  ? 0.5548 0.6200 0.5266 0.0640  0.1687  0.0917  53  PHE A O   
446  C CB  . PHE A 59  ? 0.3929 0.4026 0.3185 0.0415  0.1295  0.0698  53  PHE A CB  
447  C CG  . PHE A 59  ? 0.4244 0.4094 0.3314 0.0319  0.1184  0.0650  53  PHE A CG  
448  C CD1 . PHE A 59  ? 0.4417 0.3986 0.3199 0.0383  0.1059  0.0517  53  PHE A CD1 
449  C CD2 . PHE A 59  ? 0.4350 0.4249 0.3575 0.0166  0.1213  0.0741  53  PHE A CD2 
450  C CE1 . PHE A 59  ? 0.4450 0.3811 0.3106 0.0319  0.0959  0.0492  53  PHE A CE1 
451  C CE2 . PHE A 59  ? 0.4522 0.4165 0.3617 0.0099  0.1128  0.0711  53  PHE A CE2 
452  C CZ  . PHE A 59  ? 0.4397 0.3781 0.3210 0.0187  0.0999  0.0596  53  PHE A CZ  
453  N N   . VAL A 60  ? 0.4693 0.4780 0.3775 0.0852  0.1661  0.0674  54  VAL A N   
454  C CA  . VAL A 60  ? 0.4697 0.4899 0.3982 0.1008  0.1780  0.0676  54  VAL A CA  
455  C C   . VAL A 60  ? 0.4395 0.4446 0.3704 0.1036  0.1620  0.0560  54  VAL A C   
456  O O   . VAL A 60  ? 0.4391 0.4128 0.3379 0.1043  0.1522  0.0399  54  VAL A O   
457  C CB  . VAL A 60  ? 0.4575 0.4632 0.3582 0.1186  0.2010  0.0612  54  VAL A CB  
458  C CG1 . VAL A 60  ? 0.4627 0.4761 0.3892 0.1365  0.2151  0.0595  54  VAL A CG1 
459  C CG2 . VAL A 60  ? 0.4857 0.5071 0.3841 0.1144  0.2173  0.0750  54  VAL A CG2 
460  N N   . SER A 61  ? 0.3594 0.3889 0.3296 0.1052  0.1595  0.0658  55  SER A N   
461  C CA  . SER A 61  ? 0.3527 0.3686 0.3290 0.1104  0.1495  0.0593  55  SER A CA  
462  C C   . SER A 61  ? 0.4016 0.4380 0.4161 0.1260  0.1621  0.0724  55  SER A C   
463  O O   . SER A 61  ? 0.3952 0.4555 0.4294 0.1337  0.1790  0.0833  55  SER A O   
464  C CB  . SER A 61  ? 0.3235 0.3472 0.3062 0.0927  0.1265  0.0606  55  SER A CB  
465  O OG  . SER A 61  ? 0.3561 0.3592 0.3361 0.0964  0.1180  0.0526  55  SER A OG  
466  N N   . TYR A 62  ? 0.4245 0.4521 0.4524 0.1312  0.1549  0.0728  56  TYR A N   
467  C CA  . TYR A 62  ? 0.4310 0.4728 0.4973 0.1486  0.1661  0.0871  56  TYR A CA  
468  C C   . TYR A 62  ? 0.3459 0.3860 0.4273 0.1461  0.1509  0.0949  56  TYR A C   
469  O O   . TYR A 62  ? 0.3602 0.3826 0.4193 0.1325  0.1353  0.0845  56  TYR A O   
470  C CB  . TYR A 62  ? 0.4079 0.4186 0.4655 0.1693  0.1889  0.0732  56  TYR A CB  
471  C CG  . TYR A 62  ? 0.4572 0.4191 0.4862 0.1705  0.1847  0.0500  56  TYR A CG  
472  C CD1 . TYR A 62  ? 0.4692 0.4060 0.4524 0.1594  0.1762  0.0288  56  TYR A CD1 
473  C CD2 . TYR A 62  ? 0.4782 0.4200 0.5293 0.1825  0.1890  0.0503  56  TYR A CD2 
474  C CE1 . TYR A 62  ? 0.5108 0.4080 0.4717 0.1590  0.1706  0.0064  56  TYR A CE1 
475  C CE2 . TYR A 62  ? 0.5225 0.4213 0.5512 0.1787  0.1833  0.0275  56  TYR A CE2 
476  C CZ  . TYR A 62  ? 0.5819 0.4600 0.5666 0.1681  0.1750  0.0047  56  TYR A CZ  
477  O OH  . TYR A 62  ? 0.7635 0.6067 0.7312 0.1612  0.1657  -0.0181 56  TYR A OH  
478  N N   . GLY A 63  ? 0.3578 0.4177 0.4790 0.1602  0.1567  0.1150  57  GLY A N   
479  C CA  . GLY A 63  ? 0.3582 0.4185 0.4959 0.1604  0.1451  0.1282  57  GLY A CA  
480  C C   . GLY A 63  ? 0.3774 0.4901 0.5581 0.1653  0.1406  0.1597  57  GLY A C   
481  O O   . GLY A 63  ? 0.3923 0.5353 0.5991 0.1747  0.1513  0.1704  57  GLY A O   
482  N N   . GLY A 64  ? 0.3669 0.4930 0.5550 0.1588  0.1245  0.1754  58  GLY A N   
483  C CA  . GLY A 64  ? 0.3839 0.5624 0.6108 0.1644  0.1170  0.2077  58  GLY A CA  
484  C C   . GLY A 64  ? 0.2955 0.5273 0.5268 0.1472  0.1046  0.2119  58  GLY A C   
485  O O   . GLY A 64  ? 0.3051 0.5348 0.5061 0.1249  0.0935  0.1945  58  GLY A O   
486  N N   . SER A 65  ? 0.3653 0.6457 0.6391 0.1578  0.1069  0.2349  59  SER A N   
487  C CA  . SER A 65  ? 0.3454 0.6820 0.6324 0.1407  0.0950  0.2398  59  SER A CA  
488  C C   . SER A 65  ? 0.3660 0.7368 0.6421 0.1191  0.0683  0.2466  59  SER A C   
489  O O   . SER A 65  ? 0.3077 0.7208 0.5891 0.0997  0.0561  0.2442  59  SER A O   
490  C CB  . SER A 65  ? 0.3673 0.7378 0.6944 0.1527  0.1013  0.2589  59  SER A CB  
491  O OG  . SER A 65  ? 0.3796 0.7300 0.7207 0.1728  0.1082  0.2742  59  SER A OG  
492  N N   . GLN A 66  ? 0.3685 0.7223 0.6297 0.1211  0.0600  0.2538  60  GLN A N   
493  C CA  . GLN A 66  ? 0.3381 0.7211 0.5812 0.1006  0.0370  0.2579  60  GLN A CA  
494  C C   . GLN A 66  ? 0.2879 0.6231 0.4855 0.0866  0.0347  0.2342  60  GLN A C   
495  O O   . GLN A 66  ? 0.2957 0.6451 0.4763 0.0748  0.0204  0.2392  60  GLN A O   
496  C CB  . GLN A 66  ? 0.3515 0.7681 0.6176 0.1134  0.0278  0.2932  60  GLN A CB  
497  C CG  . GLN A 66  ? 0.3728 0.8342 0.6684 0.1149  0.0245  0.3097  60  GLN A CG  
498  C CD  . GLN A 66  ? 0.3638 0.8805 0.6520 0.0888  0.0022  0.3060  60  GLN A CD  
499  O OE1 . GLN A 66  ? 0.3037 0.8239 0.5700 0.0683  -0.0062 0.2841  60  GLN A OE1 
500  N NE2 . GLN A 66  ? 0.3977 0.9566 0.7047 0.0887  -0.0070 0.3254  60  GLN A NE2 
501  N N   . SER A 67  ? 0.3129 0.5956 0.4904 0.0877  0.0482  0.2089  61  SER A N   
502  C CA  . SER A 67  ? 0.3279 0.5638 0.4701 0.0795  0.0475  0.1892  61  SER A CA  
503  C C   . SER A 67  ? 0.3079 0.5501 0.4221 0.0534  0.0350  0.1676  61  SER A C   
504  O O   . SER A 67  ? 0.2512 0.5146 0.3684 0.0420  0.0322  0.1594  61  SER A O   
505  C CB  . SER A 67  ? 0.3893 0.5689 0.5217 0.0922  0.0651  0.1709  61  SER A CB  
506  O OG  . SER A 67  ? 0.3538 0.5310 0.4801 0.0886  0.0718  0.1554  61  SER A OG  
507  N N   . ASN A 68  ? 0.3346 0.5568 0.4244 0.0440  0.0292  0.1584  62  ASN A N   
508  C CA  . ASN A 68  ? 0.2426 0.4631 0.3068 0.0215  0.0203  0.1352  62  ASN A CA  
509  C C   . ASN A 68  ? 0.2423 0.4294 0.2950 0.0192  0.0278  0.1118  62  ASN A C   
510  O O   . ASN A 68  ? 0.2874 0.4832 0.3322 0.0028  0.0224  0.0975  62  ASN A O   
511  C CB  . ASN A 68  ? 0.2555 0.4559 0.2989 0.0153  0.0172  0.1289  62  ASN A CB  
512  C CG  . ASN A 68  ? 0.3414 0.5810 0.3866 0.0111  0.0077  0.1506  62  ASN A CG  
513  O OD1 . ASN A 68  ? 0.3819 0.6703 0.4386 0.0073  -0.0016 0.1651  62  ASN A OD1 
514  N ND2 . ASN A 68  ? 0.2789 0.5000 0.3125 0.0112  0.0099  0.1537  62  ASN A ND2 
515  N N   . ALA A 69  ? 0.2903 0.4377 0.3408 0.0352  0.0402  0.1074  63  ALA A N   
516  C CA  . ALA A 69  ? 0.2707 0.3883 0.3060 0.0346  0.0468  0.0882  63  ALA A CA  
517  C C   . ALA A 69  ? 0.2332 0.3762 0.2823 0.0323  0.0510  0.0931  63  ALA A C   
518  O O   . ALA A 69  ? 0.2535 0.3890 0.2913 0.0212  0.0506  0.0802  63  ALA A O   
519  C CB  . ALA A 69  ? 0.3141 0.3895 0.3423 0.0521  0.0587  0.0819  63  ALA A CB  
520  N N   . LEU A 70  ? 0.2364 0.4097 0.3137 0.0432  0.0561  0.1132  64  LEU A N   
521  C CA  . LEU A 70  ? 0.2727 0.4781 0.3707 0.0397  0.0604  0.1199  64  LEU A CA  
522  C C   . LEU A 70  ? 0.2363 0.4713 0.3350 0.0146  0.0464  0.1137  64  LEU A C   
523  O O   . LEU A 70  ? 0.2364 0.4688 0.3336 0.0036  0.0500  0.1043  64  LEU A O   
524  C CB  . LEU A 70  ? 0.2382 0.4800 0.3732 0.0554  0.0652  0.1446  64  LEU A CB  
525  C CG  . LEU A 70  ? 0.2332 0.5228 0.3987 0.0481  0.0660  0.1542  64  LEU A CG  
526  C CD1 . LEU A 70  ? 0.2495 0.5173 0.4099 0.0514  0.0843  0.1449  64  LEU A CD1 
527  C CD2 . LEU A 70  ? 0.2504 0.5865 0.4582 0.0626  0.0659  0.1812  64  LEU A CD2 
528  N N   . ALA A 71  ? 0.2692 0.5308 0.3686 0.0049  0.0312  0.1182  65  ALA A N   
529  C CA  . ALA A 71  ? 0.2132 0.5040 0.3113 -0.0201 0.0175  0.1082  65  ALA A CA  
530  C C   . ALA A 71  ? 0.2121 0.4642 0.2845 -0.0334 0.0185  0.0827  65  ALA A C   
531  O O   . ALA A 71  ? 0.2598 0.5183 0.3378 -0.0495 0.0180  0.0722  65  ALA A O   
532  C CB  . ALA A 71  ? 0.2236 0.5472 0.3186 -0.0262 0.0023  0.1168  65  ALA A CB  
533  N N   . ALA A 72  ? 0.2494 0.4605 0.2973 -0.0265 0.0205  0.0732  66  ALA A N   
534  C CA  . ALA A 72  ? 0.2319 0.4077 0.2589 -0.0363 0.0207  0.0509  66  ALA A CA  
535  C C   . ALA A 72  ? 0.2752 0.4277 0.3023 -0.0330 0.0315  0.0475  66  ALA A C   
536  O O   . ALA A 72  ? 0.2772 0.4220 0.3029 -0.0471 0.0310  0.0358  66  ALA A O   
537  C CB  . ALA A 72  ? 0.2316 0.3730 0.2383 -0.0276 0.0207  0.0438  66  ALA A CB  
538  N N   . LEU A 73  ? 0.2568 0.3967 0.2853 -0.0143 0.0428  0.0578  67  LEU A N   
539  C CA  . LEU A 73  ? 0.2505 0.3710 0.2746 -0.0099 0.0549  0.0571  67  LEU A CA  
540  C C   . LEU A 73  ? 0.2583 0.4097 0.3066 -0.0238 0.0578  0.0633  67  LEU A C   
541  O O   . LEU A 73  ? 0.2783 0.4132 0.3224 -0.0311 0.0638  0.0589  67  LEU A O   
542  C CB  . LEU A 73  ? 0.2623 0.3697 0.2833 0.0126  0.0680  0.0656  67  LEU A CB  
543  C CG  . LEU A 73  ? 0.2584 0.3258 0.2533 0.0250  0.0680  0.0550  67  LEU A CG  
544  C CD1 . LEU A 73  ? 0.2995 0.3626 0.3000 0.0456  0.0805  0.0628  67  LEU A CD1 
545  C CD2 . LEU A 73  ? 0.3005 0.3342 0.2684 0.0239  0.0698  0.0428  67  LEU A CD2 
546  N N   . SER A 74  ? 0.2660 0.4635 0.3419 -0.0279 0.0530  0.0749  68  SER A N   
547  C CA  . SER A 74  ? 0.3018 0.5341 0.4066 -0.0430 0.0547  0.0800  68  SER A CA  
548  C C   . SER A 74  ? 0.2414 0.4699 0.3436 -0.0682 0.0460  0.0627  68  SER A C   
549  O O   . SER A 74  ? 0.2826 0.5103 0.3984 -0.0806 0.0531  0.0611  68  SER A O   
550  C CB  . SER A 74  ? 0.2846 0.5726 0.4214 -0.0420 0.0478  0.0960  68  SER A CB  
551  O OG  . SER A 74  ? 0.2323 0.5456 0.3672 -0.0562 0.0291  0.0903  68  SER A OG  
552  N N   . ILE A 75  ? 0.2649 0.4887 0.3506 -0.0760 0.0327  0.0492  69  ILE A N   
553  C CA  . ILE A 75  ? 0.2573 0.4726 0.3395 -0.0983 0.0264  0.0288  69  ILE A CA  
554  C C   . ILE A 75  ? 0.2669 0.4297 0.3325 -0.0949 0.0360  0.0202  69  ILE A C   
555  O O   . ILE A 75  ? 0.3177 0.4699 0.3938 -0.1098 0.0401  0.0127  69  ILE A O   
556  C CB  . ILE A 75  ? 0.3066 0.5315 0.3731 -0.1052 0.0126  0.0165  69  ILE A CB  
557  C CG1 . ILE A 75  ? 0.3319 0.6123 0.4124 -0.1077 0.0016  0.0291  69  ILE A CG1 
558  C CG2 . ILE A 75  ? 0.3288 0.5424 0.3918 -0.1273 0.0086  -0.0084 69  ILE A CG2 
559  C CD1 . ILE A 75  ? 0.3623 0.6512 0.4217 -0.1077 -0.0089 0.0252  69  ILE A CD1 
560  N N   . PHE A 76  ? 0.2643 0.3940 0.3055 -0.0756 0.0392  0.0219  70  PHE A N   
561  C CA  . PHE A 76  ? 0.2895 0.3736 0.3131 -0.0693 0.0460  0.0172  70  PHE A CA  
562  C C   . PHE A 76  ? 0.3229 0.4024 0.3574 -0.0705 0.0594  0.0286  70  PHE A C   
563  O O   . PHE A 76  ? 0.3573 0.4133 0.3928 -0.0793 0.0634  0.0244  70  PHE A O   
564  C CB  . PHE A 76  ? 0.2674 0.3266 0.2662 -0.0476 0.0468  0.0193  70  PHE A CB  
565  C CG  . PHE A 76  ? 0.3289 0.3497 0.3081 -0.0373 0.0536  0.0199  70  PHE A CG  
566  C CD1 . PHE A 76  ? 0.3452 0.3602 0.3153 -0.0229 0.0653  0.0325  70  PHE A CD1 
567  C CD2 . PHE A 76  ? 0.3507 0.3432 0.3200 -0.0408 0.0485  0.0083  70  PHE A CD2 
568  C CE1 . PHE A 76  ? 0.4054 0.3887 0.3519 -0.0133 0.0704  0.0343  70  PHE A CE1 
569  C CE2 . PHE A 76  ? 0.3467 0.3076 0.2972 -0.0299 0.0526  0.0122  70  PHE A CE2 
570  C CZ  . PHE A 76  ? 0.3958 0.3531 0.3325 -0.0167 0.0628  0.0255  70  PHE A CZ  
571  N N   . ALA A 77  ? 0.3013 0.4041 0.3470 -0.0618 0.0680  0.0446  71  ALA A N   
572  C CA  . ALA A 77  ? 0.3177 0.4192 0.3740 -0.0625 0.0838  0.0574  71  ALA A CA  
573  C C   . ALA A 77  ? 0.3394 0.4630 0.4287 -0.0877 0.0837  0.0553  71  ALA A C   
574  O O   . ALA A 77  ? 0.3432 0.4466 0.4374 -0.0958 0.0938  0.0584  71  ALA A O   
575  C CB  . ALA A 77  ? 0.2889 0.4123 0.3521 -0.0459 0.0952  0.0734  71  ALA A CB  
576  N N   . LYS A 78  ? 0.3204 0.4857 0.4329 -0.1011 0.0720  0.0501  72  LYS A N   
577  C CA  . LYS A 78  ? 0.3956 0.5877 0.5425 -0.1273 0.0707  0.0455  72  LYS A CA  
578  C C   . LYS A 78  ? 0.4299 0.5881 0.5725 -0.1448 0.0683  0.0266  72  LYS A C   
579  O O   . LYS A 78  ? 0.4704 0.6227 0.6360 -0.1617 0.0768  0.0262  72  LYS A O   
580  C CB  . LYS A 78  ? 0.3585 0.6060 0.5262 -0.1376 0.0552  0.0426  72  LYS A CB  
581  C CG  . LYS A 78  ? 0.4222 0.7050 0.6279 -0.1670 0.0511  0.0350  72  LYS A CG  
582  N N   . GLN A 79  ? 0.4480 0.5832 0.5652 -0.1410 0.0582  0.0109  73  GLN A N   
583  C CA  . GLN A 79  ? 0.4309 0.5332 0.5466 -0.1550 0.0570  -0.0085 73  GLN A CA  
584  C C   . GLN A 79  ? 0.4935 0.5500 0.6060 -0.1488 0.0715  0.0014  73  GLN A C   
585  O O   . GLN A 79  ? 0.5558 0.5894 0.6836 -0.1644 0.0758  -0.0083 73  GLN A O   
586  C CB  . GLN A 79  ? 0.4023 0.4894 0.4915 -0.1476 0.0462  -0.0245 73  GLN A CB  
587  C CG  . GLN A 79  ? 0.3995 0.5278 0.4888 -0.1579 0.0319  -0.0369 73  GLN A CG  
588  C CD  . GLN A 79  ? 0.4417 0.5547 0.5038 -0.1474 0.0251  -0.0475 73  GLN A CD  
589  O OE1 . GLN A 79  ? 0.4442 0.5242 0.4886 -0.1284 0.0291  -0.0415 73  GLN A OE1 
590  N NE2 . GLN A 79  ? 0.4772 0.6169 0.5357 -0.1606 0.0149  -0.0637 73  GLN A NE2 
591  N N   . ARG A 80  ? 0.4429 0.4851 0.5350 -0.1262 0.0796  0.0206  74  ARG A N   
592  C CA  . ARG A 80  ? 0.4818 0.4810 0.5604 -0.1164 0.0912  0.0324  74  ARG A CA  
593  C C   . ARG A 80  ? 0.5306 0.5370 0.6202 -0.1154 0.1088  0.0555  74  ARG A C   
594  O O   . ARG A 80  ? 0.6044 0.5797 0.6767 -0.1043 0.1198  0.0705  74  ARG A O   
595  C CB  . ARG A 80  ? 0.4543 0.4291 0.4947 -0.0918 0.0860  0.0337  74  ARG A CB  
596  C CG  . ARG A 80  ? 0.4204 0.3825 0.4530 -0.0930 0.0717  0.0122  74  ARG A CG  
597  C CD  . ARG A 80  ? 0.4070 0.3615 0.4097 -0.0723 0.0634  0.0102  74  ARG A CD  
598  N NE  . ARG A 80  ? 0.4196 0.3676 0.4223 -0.0771 0.0524  -0.0102 74  ARG A NE  
599  C CZ  . ARG A 80  ? 0.4215 0.3968 0.4332 -0.0888 0.0450  -0.0239 74  ARG A CZ  
600  N NH1 . ARG A 80  ? 0.4120 0.4244 0.4349 -0.0958 0.0450  -0.0179 74  ARG A NH1 
601  N NH2 . ARG A 80  ? 0.4730 0.4415 0.4831 -0.0930 0.0381  -0.0426 74  ARG A NH2 
602  N N   . SER A 81  ? 0.4272 0.4766 0.5459 -0.1268 0.1121  0.0597  75  SER A N   
603  C CA  . SER A 81  ? 0.4960 0.5598 0.6302 -0.1261 0.1310  0.0817  75  SER A CA  
604  C C   . SER A 81  ? 0.5216 0.5738 0.6206 -0.0983 0.1412  0.0978  75  SER A C   
605  O O   . SER A 81  ? 0.5555 0.5997 0.6510 -0.0933 0.1601  0.1168  75  SER A O   
606  C CB  . SER A 81  ? 0.5196 0.5594 0.6748 -0.1432 0.1447  0.0891  75  SER A CB  
607  O OG  . SER A 81  ? 0.5494 0.6076 0.7444 -0.1720 0.1381  0.0728  75  SER A OG  
608  N N   . TYR A 82  ? 0.4812 0.5318 0.5531 -0.0809 0.1296  0.0895  76  TYR A N   
609  C CA  . TYR A 82  ? 0.4317 0.4784 0.4744 -0.0563 0.1383  0.0994  76  TYR A CA  
610  C C   . TYR A 82  ? 0.4435 0.5352 0.5110 -0.0523 0.1447  0.1064  76  TYR A C   
611  O O   . TYR A 82  ? 0.4452 0.5736 0.5495 -0.0676 0.1378  0.1036  76  TYR A O   
612  C CB  . TYR A 82  ? 0.4813 0.5045 0.4889 -0.0407 0.1238  0.0861  76  TYR A CB  
613  C CG  . TYR A 82  ? 0.4678 0.4507 0.4538 -0.0412 0.1151  0.0787  76  TYR A CG  
614  C CD1 . TYR A 82  ? 0.5496 0.5074 0.5324 -0.0452 0.1246  0.0902  76  TYR A CD1 
615  C CD2 . TYR A 82  ? 0.4478 0.4187 0.4195 -0.0364 0.0982  0.0621  76  TYR A CD2 
616  C CE1 . TYR A 82  ? 0.5026 0.4247 0.4696 -0.0428 0.1160  0.0856  76  TYR A CE1 
617  C CE2 . TYR A 82  ? 0.5371 0.4752 0.4942 -0.0350 0.0904  0.0556  76  TYR A CE2 
618  C CZ  . TYR A 82  ? 0.5470 0.4609 0.5025 -0.0374 0.0985  0.0674  76  TYR A CZ  
619  O OH  . TYR A 82  ? 0.5298 0.4126 0.4751 -0.0336 0.0898  0.0626  76  TYR A OH  
620  N N   . LYS A 83  ? 0.4526 0.5432 0.5006 -0.0311 0.1578  0.1151  77  LYS A N   
621  C CA  . LYS A 83  ? 0.4555 0.5853 0.5277 -0.0222 0.1656  0.1221  77  LYS A CA  
622  C C   . LYS A 83  ? 0.4390 0.5604 0.4889 -0.0018 0.1578  0.1133  77  LYS A C   
623  O O   . LYS A 83  ? 0.5135 0.5981 0.5224 0.0108  0.1568  0.1059  77  LYS A O   
624  C CB  . LYS A 83  ? 0.4560 0.5945 0.5316 -0.0142 0.1928  0.1390  77  LYS A CB  
625  C CG  . LYS A 83  ? 0.4975 0.6380 0.5936 -0.0342 0.2044  0.1507  77  LYS A CG  
626  N N   . LEU A 84  ? 0.3508 0.5069 0.4295 0.0009  0.1517  0.1149  78  LEU A N   
627  C CA  . LEU A 84  ? 0.3487 0.4976 0.4143 0.0201  0.1468  0.1096  78  LEU A CA  
628  C C   . LEU A 84  ? 0.3654 0.5404 0.4540 0.0376  0.1646  0.1216  78  LEU A C   
629  O O   . LEU A 84  ? 0.3921 0.6125 0.5246 0.0322  0.1655  0.1335  78  LEU A O   
630  C CB  . LEU A 84  ? 0.3260 0.4896 0.4040 0.0115  0.1242  0.1034  78  LEU A CB  
631  C CG  . LEU A 84  ? 0.3631 0.5182 0.4327 0.0308  0.1212  0.1014  78  LEU A CG  
632  C CD1 . LEU A 84  ? 0.3652 0.4703 0.3910 0.0412  0.1216  0.0872  78  LEU A CD1 
633  C CD2 . LEU A 84  ? 0.3103 0.4882 0.3955 0.0229  0.1017  0.1017  78  LEU A CD2 
634  N N   . VAL A 85  ? 0.3896 0.5379 0.4505 0.0585  0.1783  0.1173  79  VAL A N   
635  C CA  . VAL A 85  ? 0.4019 0.5672 0.4822 0.0792  0.1965  0.1244  79  VAL A CA  
636  C C   . VAL A 85  ? 0.3742 0.5266 0.4524 0.0924  0.1859  0.1173  79  VAL A C   
637  O O   . VAL A 85  ? 0.3868 0.4990 0.4274 0.0961  0.1786  0.1019  79  VAL A O   
638  C CB  . VAL A 85  ? 0.4171 0.5586 0.4663 0.0925  0.2196  0.1206  79  VAL A CB  
639  C CG1 . VAL A 85  ? 0.4554 0.6029 0.5207 0.1134  0.2328  0.1201  79  VAL A CG1 
640  C CG2 . VAL A 85  ? 0.4292 0.5826 0.4847 0.0777  0.2272  0.1298  79  VAL A CG2 
641  N N   . PHE A 86  ? 0.3472 0.5347 0.4682 0.0993  0.1843  0.1299  80  PHE A N   
642  C CA  . PHE A 86  ? 0.3295 0.5068 0.4540 0.1099  0.1734  0.1282  80  PHE A CA  
643  C C   . PHE A 86  ? 0.3468 0.5338 0.4999 0.1353  0.1926  0.1372  80  PHE A C   
644  O O   . PHE A 86  ? 0.3647 0.5956 0.5626 0.1384  0.1956  0.1550  80  PHE A O   
645  C CB  . PHE A 86  ? 0.3232 0.5321 0.4703 0.0944  0.1492  0.1373  80  PHE A CB  
646  C CG  . PHE A 86  ? 0.3233 0.5140 0.4631 0.1010  0.1367  0.1352  80  PHE A CG  
647  C CD1 . PHE A 86  ? 0.3661 0.5778 0.5397 0.1168  0.1379  0.1521  80  PHE A CD1 
648  C CD2 . PHE A 86  ? 0.3713 0.5235 0.4732 0.0922  0.1250  0.1180  80  PHE A CD2 
649  C CE1 . PHE A 86  ? 0.3263 0.5189 0.4942 0.1223  0.1283  0.1531  80  PHE A CE1 
650  C CE2 . PHE A 86  ? 0.3263 0.4625 0.4242 0.0967  0.1156  0.1170  80  PHE A CE2 
651  C CZ  . PHE A 86  ? 0.3245 0.4793 0.4543 0.1113  0.1179  0.1350  80  PHE A CZ  
652  N N   . ALA A 87  ? 0.3687 0.5130 0.4968 0.1521  0.2036  0.1229  81  ALA A N   
653  C CA  . ALA A 87  ? 0.3831 0.5216 0.5320 0.1734  0.2183  0.1253  81  ALA A CA  
654  C C   . ALA A 87  ? 0.3857 0.5276 0.5624 0.1819  0.2073  0.1365  81  ALA A C   
655  O O   . ALA A 87  ? 0.4265 0.5516 0.5876 0.1752  0.1925  0.1316  81  ALA A O   
656  C CB  . ALA A 87  ? 0.4210 0.5093 0.5276 0.1828  0.2321  0.1008  81  ALA A CB  
657  N N   . CYS A 88  ? 0.4133 0.5740 0.6282 0.1939  0.2120  0.1519  82  CYS A N   
658  C CA  . CYS A 88  ? 0.4507 0.6147 0.6913 0.2013  0.2011  0.1672  82  CYS A CA  
659  C C   . CYS A 88  ? 0.4522 0.6152 0.7229 0.2188  0.2143  0.1759  82  CYS A C   
660  O O   . CYS A 88  ? 0.5107 0.6853 0.7911 0.2238  0.2291  0.1743  82  CYS A O   
661  C CB  . CYS A 88  ? 0.4144 0.6310 0.6800 0.1883  0.1790  0.1898  82  CYS A CB  
662  S SG  . CYS A 88  ? 0.4438 0.7228 0.7449 0.1793  0.1768  0.2062  82  CYS A SG  
663  N N   . GLU A 89  ? 0.4968 0.6451 0.7830 0.2277  0.2099  0.1856  83  GLU A N   
664  C CA  . GLU A 89  ? 0.5098 0.6590 0.8298 0.2444  0.2217  0.1968  83  GLU A CA  
665  C C   . GLU A 89  ? 0.5295 0.7390 0.8899 0.2447  0.2161  0.2231  83  GLU A C   
666  O O   . GLU A 89  ? 0.4196 0.6706 0.7853 0.2304  0.1976  0.2362  83  GLU A O   
667  C CB  . GLU A 89  ? 0.5804 0.7048 0.9109 0.2510  0.2166  0.2060  83  GLU A CB  
668  C CG  . GLU A 89  ? 0.6096 0.6754 0.9045 0.2480  0.2194  0.1795  83  GLU A CG  
669  C CD  . GLU A 89  ? 0.7173 0.7415 0.9978 0.2572  0.2404  0.1512  83  GLU A CD  
670  O OE1 . GLU A 89  ? 0.8018 0.7803 1.0528 0.2530  0.2412  0.1261  83  GLU A OE1 
671  O OE2 . GLU A 89  ? 0.7439 0.7828 1.0425 0.2678  0.2552  0.1529  83  GLU A OE2 
672  N N   . LYS A 90  ? 0.5819 0.7971 0.9715 0.2600  0.2320  0.2286  84  LYS A N   
673  C CA  . LYS A 90  ? 0.5694 0.8417 1.0013 0.2616  0.2278  0.2524  84  LYS A CA  
674  C C   . LYS A 90  ? 0.5513 0.8629 1.0014 0.2535  0.2017  0.2794  84  LYS A C   
675  O O   . LYS A 90  ? 0.6099 0.9082 1.0678 0.2611  0.1964  0.2926  84  LYS A O   
676  C CB  . LYS A 90  ? 0.6552 0.9228 1.1208 0.2830  0.2476  0.2574  84  LYS A CB  
677  N N   . ILE A 91  ? 0.4494 0.8084 0.9034 0.2363  0.1853  0.2862  85  ILE A N   
678  C CA  . ILE A 91  ? 0.4127 0.8106 0.8729 0.2236  0.1578  0.3062  85  ILE A CA  
679  C C   . ILE A 91  ? 0.4610 0.8993 0.9647 0.2341  0.1518  0.3347  85  ILE A C   
680  O O   . ILE A 91  ? 0.4494 0.9086 0.9848 0.2433  0.1632  0.3393  85  ILE A O   
681  C CB  . ILE A 91  ? 0.4362 0.8699 0.8849 0.1988  0.1422  0.2988  85  ILE A CB  
682  N N   . SER A 92  ? 0.4380 0.8878 0.9428 0.2330  0.1345  0.3546  86  SER A N   
683  C CA  . SER A 92  ? 0.5132 1.0039 1.0557 0.2420  0.1258  0.3845  86  SER A CA  
684  C C   . SER A 92  ? 0.4512 1.0055 1.0197 0.2312  0.1136  0.3914  86  SER A C   
685  O O   . SER A 92  ? 0.4231 1.0025 0.9745 0.2085  0.0980  0.3809  86  SER A O   
686  C CB  . SER A 92  ? 0.4597 0.9585 0.9888 0.2359  0.1060  0.4029  86  SER A CB  
687  O OG  . SER A 92  ? 0.4661 1.0283 1.0160 0.2290  0.0845  0.4266  86  SER A OG  
688  N N   . THR A 93  ? 0.4794 1.0589 1.0919 0.2472  0.1213  0.4077  87  THR A N   
689  C CA  . THR A 93  ? 0.4780 1.1213 1.1224 0.2381  0.1094  0.4159  87  THR A CA  
690  C C   . THR A 93  ? 0.4660 1.1581 1.1010 0.2170  0.0766  0.4277  87  THR A C   
691  O O   . THR A 93  ? 0.4483 1.1788 1.0837 0.1955  0.0627  0.4180  87  THR A O   
692  C CB  . THR A 93  ? 0.5155 1.1797 1.2116 0.2614  0.1209  0.4362  87  THR A CB  
693  O OG1 . THR A 93  ? 0.5292 1.1522 1.2322 0.2781  0.1523  0.4201  87  THR A OG1 
694  C CG2 . THR A 93  ? 0.5263 1.2621 1.2597 0.2516  0.1055  0.4468  87  THR A CG2 
695  N N   . PHE A 94  ? 0.4795 1.1695 1.1044 0.2215  0.0649  0.4469  88  PHE A N   
696  C CA  . PHE A 94  ? 0.4750 1.2106 1.0846 0.2014  0.0346  0.4569  88  PHE A CA  
697  C C   . PHE A 94  ? 0.4560 1.1847 1.0231 0.1742  0.0236  0.4304  88  PHE A C   
698  O O   . PHE A 94  ? 0.4471 1.2214 1.0112 0.1516  0.0029  0.4244  88  PHE A O   
699  C CB  . PHE A 94  ? 0.4981 1.2241 1.0986 0.2115  0.0287  0.4809  88  PHE A CB  
700  N N   . LEU A 95  ? 0.4200 1.0913 0.9554 0.1757  0.0375  0.4125  89  LEU A N   
701  C CA  . LEU A 95  ? 0.4264 1.0889 0.9227 0.1514  0.0278  0.3882  89  LEU A CA  
702  C C   . LEU A 95  ? 0.4477 1.1281 0.9538 0.1362  0.0298  0.3678  89  LEU A C   
703  O O   . LEU A 95  ? 0.3913 1.0959 0.8811 0.1102  0.0126  0.3538  89  LEU A O   
704  C CB  . LEU A 95  ? 0.4317 1.0297 0.8968 0.1588  0.0430  0.3745  89  LEU A CB  
705  C CG  . LEU A 95  ? 0.4112 0.9949 0.8372 0.1367  0.0352  0.3494  89  LEU A CG  
706  C CD1 . LEU A 95  ? 0.4528 1.0771 0.8590 0.1135  0.0075  0.3525  89  LEU A CD1 
707  C CD2 . LEU A 95  ? 0.4048 0.9271 0.8046 0.1470  0.0494  0.3390  89  LEU A CD2 
708  N N   . LYS A 96  ? 0.3896 1.0567 0.9220 0.1510  0.0524  0.3645  90  LYS A N   
709  C CA  . LYS A 96  ? 0.3918 1.0752 0.9362 0.1366  0.0578  0.3470  90  LYS A CA  
710  C C   . LYS A 96  ? 0.4205 1.1687 0.9880 0.1167  0.0347  0.3523  90  LYS A C   
711  O O   . LYS A 96  ? 0.4318 1.1948 0.9904 0.0907  0.0254  0.3337  90  LYS A O   
712  C CB  . LYS A 96  ? 0.4352 1.1017 1.0073 0.1575  0.0864  0.3469  90  LYS A CB  
713  C CG  . LYS A 96  ? 0.4132 1.0166 0.9564 0.1677  0.1110  0.3284  90  LYS A CG  
714  N N   . ASN A 97  ? 0.4402 1.2266 1.0384 0.1282  0.0254  0.3769  91  ASN A N   
715  C CA  . ASN A 97  ? 0.4242 1.2755 1.0467 0.1110  0.0024  0.3824  91  ASN A CA  
716  C C   . ASN A 97  ? 0.4290 1.3002 1.0169 0.0885  -0.0259 0.3787  91  ASN A C   
717  O O   . ASN A 97  ? 0.4364 1.3542 1.0332 0.0660  -0.0455 0.3715  91  ASN A O   
718  C CB  . ASN A 97  ? 0.4783 1.3654 1.1464 0.1328  0.0022  0.4111  91  ASN A CB  
719  N N   . ASN A 98  ? 0.3970 1.2335 0.9458 0.0929  -0.0274 0.3816  92  ASN A N   
720  C CA  . ASN A 98  ? 0.3992 1.2521 0.9111 0.0734  -0.0514 0.3788  92  ASN A CA  
721  C C   . ASN A 98  ? 0.4163 1.2189 0.8821 0.0645  -0.0459 0.3581  92  ASN A C   
722  O O   . ASN A 98  ? 0.4449 1.2202 0.8860 0.0744  -0.0440 0.3675  92  ASN A O   
723  C CB  . ASN A 98  ? 0.4627 1.3344 0.9769 0.0888  -0.0607 0.4100  92  ASN A CB  
724  N N   . ASN A 102 ? 0.3370 0.8821 0.5399 0.0035  -0.0371 0.2299  96  ASN A N   
725  C CA  . ASN A 102 ? 0.2860 0.7750 0.4753 0.0004  -0.0204 0.2027  96  ASN A CA  
726  C C   . ASN A 102 ? 0.2967 0.7950 0.5213 0.0083  -0.0078 0.2063  96  ASN A C   
727  O O   . ASN A 102 ? 0.3094 0.7900 0.5291 -0.0047 -0.0007 0.1855  96  ASN A O   
728  C CB  . ASN A 102 ? 0.2935 0.7182 0.4603 0.0172  -0.0061 0.1994  96  ASN A CB  
729  C CG  . ASN A 102 ? 0.2982 0.7024 0.4265 0.0043  -0.0138 0.1863  96  ASN A CG  
730  O OD1 . ASN A 102 ? 0.3409 0.7587 0.4506 -0.0189 -0.0244 0.1674  96  ASN A OD1 
731  N ND2 . ASN A 102 ? 0.2428 0.6121 0.3615 0.0192  -0.0065 0.1948  96  ASN A ND2 
732  N N   . TYR A 103 ? 0.3368 0.8624 0.5988 0.0306  -0.0030 0.2340  97  TYR A N   
733  C CA  . TYR A 103 ? 0.3375 0.8701 0.6319 0.0392  0.0116  0.2373  97  TYR A CA  
734  C C   . TYR A 103 ? 0.3840 0.9524 0.6882 0.0138  0.0006  0.2263  97  TYR A C   
735  O O   . TYR A 103 ? 0.4159 0.9758 0.7316 0.0083  0.0135  0.2152  97  TYR A O   
736  C CB  . TYR A 103 ? 0.2668 0.8062 0.5881 0.0656  0.0181  0.2638  97  TYR A CB  
737  C CG  . TYR A 103 ? 0.2695 0.8201 0.6236 0.0735  0.0319  0.2672  97  TYR A CG  
738  C CD1 . TYR A 103 ? 0.2986 0.8974 0.6804 0.0691  0.0206  0.2808  97  TYR A CD1 
739  C CD2 . TYR A 103 ? 0.3136 0.8274 0.6692 0.0852  0.0568  0.2563  97  TYR A CD2 
740  C CE1 . TYR A 103 ? 0.2864 0.8981 0.7014 0.0762  0.0336  0.2840  97  TYR A CE1 
741  C CE2 . TYR A 103 ? 0.3460 0.8705 0.7294 0.0919  0.0708  0.2592  97  TYR A CE2 
742  C CZ  . TYR A 103 ? 0.3080 0.8823 0.7236 0.0874  0.0592  0.2734  97  TYR A CZ  
743  O OH  . TYR A 103 ? 0.4121 1.0000 0.8588 0.0938  0.0736  0.2763  97  TYR A OH  
744  N N   . ALA A 104 ? 0.3528 0.9587 0.6506 -0.0022 -0.0219 0.2286  98  ALA A N   
745  C CA  . ALA A 104 ? 0.3377 0.9753 0.6454 -0.0274 -0.0329 0.2146  98  ALA A CA  
746  C C   . ALA A 104 ? 0.3535 0.9657 0.6407 -0.0518 -0.0308 0.1840  98  ALA A C   
747  O O   . ALA A 104 ? 0.4099 1.0252 0.7141 -0.0662 -0.0259 0.1715  98  ALA A O   
748  C CB  . ALA A 104 ? 0.3848 1.0650 0.6843 -0.0387 -0.0562 0.2210  98  ALA A CB  
749  N N   . LEU A 105 ? 0.3569 0.9424 0.6096 -0.0570 -0.0335 0.1720  99  LEU A N   
750  C CA  . LEU A 105 ? 0.3495 0.9061 0.5831 -0.0791 -0.0303 0.1429  99  LEU A CA  
751  C C   . LEU A 105 ? 0.3537 0.8703 0.5951 -0.0703 -0.0067 0.1397  99  LEU A C   
752  O O   . LEU A 105 ? 0.3402 0.8425 0.5834 -0.0883 -0.0010 0.1226  99  LEU A O   
753  C CB  . LEU A 105 ? 0.3667 0.8976 0.5598 -0.0839 -0.0366 0.1303  99  LEU A CB  
754  C CG  . LEU A 105 ? 0.3773 0.8606 0.5448 -0.1017 -0.0306 0.0987  99  LEU A CG  
755  C CD1 . LEU A 105 ? 0.4506 0.9561 0.6033 -0.1296 -0.0471 0.0766  99  LEU A CD1 
756  C CD2 . LEU A 105 ? 0.4205 0.8407 0.5549 -0.0856 -0.0193 0.0931  99  LEU A CD2 
757  N N   . ALA A 106 ? 0.3080 0.7966 0.5477 -0.0418 0.0082  0.1543  100 ALA A N   
758  C CA  . ALA A 106 ? 0.2937 0.7395 0.5309 -0.0308 0.0313  0.1503  100 ALA A CA  
759  C C   . ALA A 106 ? 0.2847 0.7680 0.5649 -0.0345 0.0410  0.1600  100 ALA A C   
760  O O   . ALA A 106 ? 0.2719 0.7313 0.5499 -0.0418 0.0555  0.1509  100 ALA A O   
761  C CB  . ALA A 106 ? 0.3091 0.7197 0.5349 -0.0006 0.0446  0.1604  100 ALA A CB  
762  N N   . LEU A 107 ? 0.2953 0.8257 0.6076 -0.0284 0.0323  0.1770  101 LEU A N   
763  C CA  . LEU A 107 ? 0.3415 0.8974 0.6878 -0.0339 0.0375  0.1804  101 LEU A CA  
764  C C   . LEU A 107 ? 0.3543 0.9178 0.7024 -0.0668 0.0288  0.1604  101 LEU A C   
765  O O   . LEU A 107 ? 0.4242 0.9819 0.7895 -0.0751 0.0429  0.1561  101 LEU A O   
766  C CB  . LEU A 107 ? 0.3410 0.9432 0.7168 -0.0231 0.0256  0.2001  101 LEU A CB  
767  C CG  . LEU A 107 ? 0.3273 0.9288 0.7239 0.0093  0.0406  0.2220  101 LEU A CG  
768  C CD1 . LEU A 107 ? 0.3186 0.9718 0.7487 0.0130  0.0266  0.2402  101 LEU A CD1 
769  C CD2 . LEU A 107 ? 0.3307 0.9076 0.7375 0.0189  0.0686  0.2190  101 LEU A CD2 
770  N N   . GLU A 108 ? 0.3061 0.8794 0.6354 -0.0857 0.0073  0.1471  102 GLU A N   
771  C CA  . GLU A 108 ? 0.3307 0.9059 0.6617 -0.1166 -0.0005 0.1243  102 GLU A CA  
772  C C   . GLU A 108 ? 0.3762 0.9019 0.6906 -0.1265 0.0155  0.1090  102 GLU A C   
773  O O   . GLU A 108 ? 0.4244 0.9434 0.7538 -0.1464 0.0204  0.0965  102 GLU A O   
774  C CB  . GLU A 108 ? 0.3303 0.9232 0.6387 -0.1321 -0.0253 0.1112  102 GLU A CB  
775  N N   . ASN A 109 ? 0.2642 0.7544 0.5495 -0.1127 0.0244  0.1108  103 ASN A N   
776  C CA  . ASN A 109 ? 0.2940 0.7289 0.5561 -0.1173 0.0391  0.0982  103 ASN A CA  
777  C C   . ASN A 109 ? 0.3283 0.7431 0.5998 -0.1028 0.0643  0.1114  103 ASN A C   
778  O O   . ASN A 109 ? 0.3604 0.7229 0.6053 -0.1007 0.0768  0.1043  103 ASN A O   
779  C CB  . ASN A 109 ? 0.2871 0.6732 0.5014 -0.1044 0.0355  0.0885  103 ASN A CB  
780  C CG  . ASN A 109 ? 0.3235 0.7128 0.5206 -0.1246 0.0167  0.0679  103 ASN A CG  
781  O OD1 . ASN A 109 ? 0.4632 0.8658 0.6738 -0.1507 0.0110  0.0526  103 ASN A OD1 
782  N ND2 . ASN A 109 ? 0.3271 0.7033 0.4951 -0.1134 0.0087  0.0662  103 ASN A ND2 
783  N N   . GLY A 110 ? 0.2782 0.7296 0.5830 -0.0908 0.0720  0.1296  104 GLY A N   
784  C CA  . GLY A 110 ? 0.3384 0.7730 0.6515 -0.0796 0.0972  0.1392  104 GLY A CA  
785  C C   . GLY A 110 ? 0.3402 0.7395 0.6252 -0.0507 0.1155  0.1474  104 GLY A C   
786  O O   . GLY A 110 ? 0.3446 0.7137 0.6166 -0.0446 0.1364  0.1494  104 GLY A O   
787  N N   . VAL A 111 ? 0.2571 0.6519 0.5266 -0.0321 0.1069  0.1494  105 VAL A N   
788  C CA  . VAL A 111 ? 0.3194 0.6732 0.5597 -0.0044 0.1222  0.1510  105 VAL A CA  
789  C C   . VAL A 111 ? 0.2929 0.6648 0.5597 0.0136  0.1438  0.1654  105 VAL A C   
790  O O   . VAL A 111 ? 0.3180 0.7320 0.6232 0.0138  0.1380  0.1752  105 VAL A O   
791  C CB  . VAL A 111 ? 0.2897 0.6346 0.5141 0.0090  0.1079  0.1498  105 VAL A CB  
792  C CG1 . VAL A 111 ? 0.3244 0.6313 0.5274 0.0369  0.1245  0.1504  105 VAL A CG1 
793  C CG2 . VAL A 111 ? 0.2359 0.5540 0.4271 -0.0075 0.0895  0.1322  105 VAL A CG2 
794  N N   . ASP A 112 ? 0.3287 0.6605 0.5668 0.0290  0.1652  0.1621  106 ASP A N   
795  C CA  . ASP A 112 ? 0.3481 0.6817 0.5974 0.0479  0.1847  0.1685  106 ASP A CA  
796  C C   . ASP A 112 ? 0.3380 0.6584 0.5814 0.0750  0.1882  0.1696  106 ASP A C   
797  O O   . ASP A 112 ? 0.3533 0.6300 0.5575 0.0882  0.1978  0.1591  106 ASP A O   
798  C CB  . ASP A 112 ? 0.3855 0.6838 0.6025 0.0481  0.2047  0.1628  106 ASP A CB  
799  C CG  . ASP A 112 ? 0.5231 0.8263 0.7502 0.0648  0.2261  0.1677  106 ASP A CG  
800  O OD1 . ASP A 112 ? 0.5809 0.9176 0.8472 0.0742  0.2259  0.1765  106 ASP A OD1 
801  O OD2 . ASP A 112 ? 0.5438 0.8180 0.7384 0.0688  0.2429  0.1632  106 ASP A OD2 
802  N N   . PHE A 113 ? 0.3191 0.6754 0.6012 0.0831  0.1799  0.1820  107 PHE A N   
803  C CA  . PHE A 113 ? 0.3134 0.6555 0.5970 0.1090  0.1845  0.1856  107 PHE A CA  
804  C C   . PHE A 113 ? 0.3462 0.6720 0.6303 0.1283  0.2094  0.1838  107 PHE A C   
805  O O   . PHE A 113 ? 0.3578 0.7110 0.6685 0.1254  0.2179  0.1907  107 PHE A O   
806  C CB  . PHE A 113 ? 0.3024 0.6872 0.6258 0.1115  0.1662  0.2030  107 PHE A CB  
807  C CG  . PHE A 113 ? 0.4050 0.8023 0.7211 0.0965  0.1417  0.2037  107 PHE A CG  
808  C CD1 . PHE A 113 ? 0.2716 0.6422 0.5684 0.1078  0.1377  0.2021  107 PHE A CD1 
809  C CD2 . PHE A 113 ? 0.3561 0.7913 0.6848 0.0701  0.1230  0.2040  107 PHE A CD2 
810  C CE1 . PHE A 113 ? 0.2536 0.6328 0.5382 0.0925  0.1144  0.2011  107 PHE A CE1 
811  C CE2 . PHE A 113 ? 0.2986 0.7457 0.6164 0.0549  0.1005  0.2018  107 PHE A CE2 
812  C CZ  . PHE A 113 ? 0.2630 0.6822 0.5572 0.0663  0.0962  0.2009  107 PHE A CZ  
813  N N   . VAL A 114 ? 0.3726 0.6541 0.6277 0.1469  0.2211  0.1726  108 VAL A N   
814  C CA  . VAL A 114 ? 0.4014 0.6637 0.6524 0.1652  0.2444  0.1667  108 VAL A CA  
815  C C   . VAL A 114 ? 0.4142 0.6586 0.6758 0.1862  0.2458  0.1674  108 VAL A C   
816  O O   . VAL A 114 ? 0.4376 0.6465 0.6726 0.1898  0.2401  0.1568  108 VAL A O   
817  C CB  . VAL A 114 ? 0.4447 0.6642 0.6419 0.1644  0.2585  0.1469  108 VAL A CB  
818  C CG1 . VAL A 114 ? 0.4985 0.7065 0.6925 0.1805  0.2824  0.1401  108 VAL A CG1 
819  C CG2 . VAL A 114 ? 0.4129 0.6440 0.5980 0.1423  0.2551  0.1487  108 VAL A CG2 
820  N N   . GLU A 115 ? 0.4309 0.6984 0.7330 0.1992  0.2534  0.1800  109 GLU A N   
821  C CA  . GLU A 115 ? 0.4449 0.6994 0.7656 0.2173  0.2530  0.1859  109 GLU A CA  
822  C C   . GLU A 115 ? 0.4864 0.6940 0.7848 0.2339  0.2751  0.1658  109 GLU A C   
823  O O   . GLU A 115 ? 0.5114 0.7143 0.7975 0.2366  0.2940  0.1546  109 GLU A O   
824  C CB  . GLU A 115 ? 0.5063 0.8092 0.8829 0.2234  0.2487  0.2107  109 GLU A CB  
825  C CG  . GLU A 115 ? 0.5157 0.8700 0.9135 0.2040  0.2251  0.2272  109 GLU A CG  
826  C CD  . GLU A 115 ? 0.5576 0.9570 1.0049 0.2102  0.2137  0.2524  109 GLU A CD  
827  O OE1 . GLU A 115 ? 0.5843 0.9685 1.0450 0.2288  0.2174  0.2609  109 GLU A OE1 
828  O OE2 . GLU A 115 ? 0.5864 1.0360 1.0590 0.1955  0.2004  0.2634  109 GLU A OE2 
829  N N   . ASN A 116 ? 0.4969 0.6705 0.7902 0.2436  0.2720  0.1607  110 ASN A N   
830  C CA  . ASN A 116 ? 0.5386 0.6644 0.8108 0.2566  0.2891  0.1378  110 ASN A CA  
831  C C   . ASN A 116 ? 0.5821 0.7202 0.8972 0.2749  0.3049  0.1472  110 ASN A C   
832  O O   . ASN A 116 ? 0.6644 0.7851 0.9999 0.2868  0.3056  0.1513  110 ASN A O   
833  C CB  . ASN A 116 ? 0.5364 0.6218 0.7896 0.2558  0.2778  0.1281  110 ASN A CB  
834  C CG  . ASN A 116 ? 0.6563 0.6912 0.8835 0.2640  0.2918  0.0989  110 ASN A CG  
835  O OD1 . ASN A 116 ? 0.6413 0.6679 0.8481 0.2673  0.3082  0.0807  110 ASN A OD1 
836  N ND2 . ASN A 116 ? 0.5882 0.5905 0.8161 0.2661  0.2848  0.0938  110 ASN A ND2 
837  N N   . ILE A 117 ? 0.5814 0.7505 0.9117 0.2766  0.3183  0.1515  111 ILE A N   
838  C CA  . ILE A 117 ? 0.6112 0.8026 0.9892 0.2935  0.3327  0.1638  111 ILE A CA  
839  C C   . ILE A 117 ? 0.7108 0.8583 1.0824 0.3107  0.3514  0.1435  111 ILE A C   
840  O O   . ILE A 117 ? 0.7450 0.8944 1.1566 0.3264  0.3564  0.1552  111 ILE A O   
841  C CB  . ILE A 117 ? 0.6142 0.8447 1.0061 0.2903  0.3457  0.1682  111 ILE A CB  
842  C CG1 . ILE A 117 ? 0.6503 0.8554 0.9893 0.2831  0.3602  0.1422  111 ILE A CG1 
843  C CG2 . ILE A 117 ? 0.5714 0.8536 0.9888 0.2745  0.3257  0.1922  111 ILE A CG2 
844  C CD1 . ILE A 117 ? 0.6871 0.9216 1.0385 0.2843  0.3811  0.1432  111 ILE A CD1 
845  N N   . HIS A 118 ? 0.7539 0.8622 1.0757 0.3076  0.3611  0.1126  112 HIS A N   
846  C CA  . HIS A 118 ? 0.8264 0.8932 1.1383 0.3212  0.3777  0.0876  112 HIS A CA  
847  C C   . HIS A 118 ? 0.8220 0.8483 1.1270 0.3210  0.3647  0.0810  112 HIS A C   
848  O O   . HIS A 118 ? 0.8479 0.8335 1.1353 0.3273  0.3746  0.0542  112 HIS A O   
849  C CB  . HIS A 118 ? 0.8194 0.8668 1.0793 0.3168  0.3921  0.0562  112 HIS A CB  
850  C CG  . HIS A 118 ? 0.8613 0.9449 1.1294 0.3186  0.4100  0.0616  112 HIS A CG  
851  N ND1 . HIS A 118 ? 0.8450 0.9416 1.0772 0.3038  0.4095  0.0590  112 HIS A ND1 
852  C CD2 . HIS A 118 ? 0.8872 0.9973 1.1975 0.3333  0.4294  0.0707  112 HIS A CD2 
853  C CE1 . HIS A 118 ? 0.8585 0.9878 1.1100 0.3080  0.4282  0.0663  112 HIS A CE1 
854  N NE2 . HIS A 118 ? 0.8936 1.0328 1.1929 0.3261  0.4406  0.0727  112 HIS A NE2 
855  N N   . SER A 119 ? 0.7642 0.8033 1.0837 0.3131  0.3429  0.1044  113 SER A N   
856  C CA  . SER A 119 ? 0.7252 0.7322 1.0441 0.3115  0.3297  0.1045  113 SER A CA  
857  C C   . SER A 119 ? 0.7597 0.7158 1.0306 0.3049  0.3306  0.0679  113 SER A C   
858  O O   . SER A 119 ? 0.8119 0.7319 1.0879 0.3096  0.3316  0.0573  113 SER A O   
859  C CB  . SER A 119 ? 0.7188 0.7229 1.0869 0.3290  0.3373  0.1207  113 SER A CB  
860  N N   . LEU A 120 ? 0.7381 0.6923 0.9633 0.2934  0.3295  0.0490  114 LEU A N   
861  C CA  . LEU A 120 ? 0.7616 0.6743 0.9386 0.2859  0.3276  0.0138  114 LEU A CA  
862  C C   . LEU A 120 ? 0.7780 0.6750 0.9373 0.2711  0.3044  0.0147  114 LEU A C   
863  O O   . LEU A 120 ? 0.7745 0.6921 0.9572 0.2674  0.2914  0.0420  114 LEU A O   
864  C CB  . LEU A 120 ? 0.7503 0.6705 0.8847 0.2806  0.3364  -0.0046 114 LEU A CB  
865  N N   . SER A 121 ? 0.8156 0.6784 0.9337 0.2624  0.2985  -0.0161 115 SER A N   
866  C CA  . SER A 121 ? 0.7400 0.5886 0.8383 0.2473  0.2770  -0.0184 115 SER A CA  
867  C C   . SER A 121 ? 0.6797 0.5587 0.7634 0.2371  0.2670  -0.0018 115 SER A C   
868  O O   . SER A 121 ? 0.6553 0.5434 0.7072 0.2330  0.2712  -0.0112 115 SER A O   
869  C CB  . SER A 121 ? 0.8106 0.6237 0.8673 0.2393  0.2716  -0.0562 115 SER A CB  
870  N N   . LEU A 122 ? 0.6498 0.5452 0.7567 0.2329  0.2539  0.0234  116 LEU A N   
871  C CA  . LEU A 122 ? 0.6465 0.5771 0.7500 0.2250  0.2456  0.0419  116 LEU A CA  
872  C C   . LEU A 122 ? 0.6096 0.5264 0.6626 0.2115  0.2368  0.0223  116 LEU A C   
873  O O   . LEU A 122 ? 0.6253 0.5653 0.6641 0.2063  0.2383  0.0284  116 LEU A O   
874  C CB  . LEU A 122 ? 0.6265 0.5775 0.7622 0.2225  0.2314  0.0693  116 LEU A CB  
875  C CG  . LEU A 122 ? 0.5955 0.5947 0.7428 0.2162  0.2241  0.0918  116 LEU A CG  
876  C CD1 . LEU A 122 ? 0.5464 0.5787 0.7181 0.2240  0.2380  0.1039  116 LEU A CD1 
877  C CD2 . LEU A 122 ? 0.5853 0.6085 0.7616 0.2131  0.2076  0.1173  116 LEU A CD2 
878  N N   . LYS A 123 ? 0.6196 0.5003 0.6467 0.2046  0.2270  -0.0006 117 LYS A N   
879  C CA  . LYS A 123 ? 0.5914 0.4602 0.5708 0.1921  0.2164  -0.0190 117 LYS A CA  
880  C C   . LYS A 123 ? 0.6554 0.5239 0.6022 0.1942  0.2280  -0.0348 117 LYS A C   
881  O O   . LYS A 123 ? 0.6093 0.4890 0.5267 0.1872  0.2254  -0.0328 117 LYS A O   
882  C CB  . LYS A 123 ? 0.6326 0.4678 0.5972 0.1835  0.2015  -0.0404 117 LYS A CB  
883  C CG  . LYS A 123 ? 0.6634 0.4878 0.5795 0.1717  0.1895  -0.0618 117 LYS A CG  
884  C CD  . LYS A 123 ? 0.6558 0.4552 0.5643 0.1609  0.1717  -0.0808 117 LYS A CD  
885  C CE  . LYS A 123 ? 0.7247 0.5226 0.5910 0.1489  0.1562  -0.0952 117 LYS A CE  
886  N NZ  . LYS A 123 ? 0.7657 0.5468 0.6325 0.1369  0.1370  -0.1112 117 LYS A NZ  
887  N N   . GLN A 124 ? 0.6533 0.5085 0.6042 0.2036  0.2412  -0.0507 118 GLN A N   
888  C CA  . GLN A 124 ? 0.7037 0.5620 0.6245 0.2067  0.2546  -0.0655 118 GLN A CA  
889  C C   . GLN A 124 ? 0.6411 0.5340 0.5735 0.2106  0.2681  -0.0415 118 GLN A C   
890  O O   . GLN A 124 ? 0.6566 0.5592 0.5562 0.2055  0.2715  -0.0428 118 GLN A O   
891  C CB  . GLN A 124 ? 0.7102 0.5507 0.6398 0.2177  0.2683  -0.0872 118 GLN A CB  
892  N N   . PHE A 125 ? 0.6821 0.5962 0.6637 0.2190  0.2752  -0.0181 119 PHE A N   
893  C CA  . PHE A 125 ? 0.6522 0.6056 0.6549 0.2202  0.2846  0.0066  119 PHE A CA  
894  C C   . PHE A 125 ? 0.6140 0.5812 0.5950 0.2055  0.2722  0.0170  119 PHE A C   
895  O O   . PHE A 125 ? 0.5799 0.5621 0.5430 0.2008  0.2797  0.0210  119 PHE A O   
896  C CB  . PHE A 125 ? 0.6138 0.5913 0.6756 0.2288  0.2859  0.0317  119 PHE A CB  
897  C CG  . PHE A 125 ? 0.6298 0.6536 0.7221 0.2285  0.2927  0.0567  119 PHE A CG  
898  C CD1 . PHE A 125 ? 0.5643 0.6208 0.6861 0.2210  0.2787  0.0812  119 PHE A CD1 
899  C CD2 . PHE A 125 ? 0.6499 0.6871 0.7431 0.2344  0.3127  0.0546  119 PHE A CD2 
900  C CE1 . PHE A 125 ? 0.5086 0.6108 0.6621 0.2177  0.2824  0.1021  119 PHE A CE1 
901  C CE2 . PHE A 125 ? 0.6542 0.7353 0.7796 0.2322  0.3183  0.0770  119 PHE A CE2 
902  C CZ  . PHE A 125 ? 0.5381 0.6517 0.6947 0.2231  0.3022  0.1002  119 PHE A CZ  
903  N N   . ALA A 126 ? 0.5840 0.5454 0.5666 0.1977  0.2536  0.0212  120 ALA A N   
904  C CA  . ALA A 126 ? 0.5391 0.5129 0.5045 0.1838  0.2418  0.0300  120 ALA A CA  
905  C C   . ALA A 126 ? 0.5357 0.4889 0.4455 0.1766  0.2397  0.0130  120 ALA A C   
906  O O   . ALA A 126 ? 0.5333 0.5021 0.4300 0.1686  0.2414  0.0233  120 ALA A O   
907  C CB  . ALA A 126 ? 0.4931 0.4616 0.4682 0.1782  0.2236  0.0334  120 ALA A CB  
908  N N   . LEU A 127 ? 0.6105 0.5305 0.4896 0.1781  0.2343  -0.0121 121 LEU A N   
909  C CA  . LEU A 127 ? 0.5860 0.4910 0.4129 0.1714  0.2287  -0.0276 121 LEU A CA  
910  C C   . LEU A 127 ? 0.6511 0.5713 0.4635 0.1749  0.2472  -0.0234 121 LEU A C   
911  O O   . LEU A 127 ? 0.7208 0.6426 0.4983 0.1679  0.2444  -0.0206 121 LEU A O   
912  C CB  . LEU A 127 ? 0.7785 0.6535 0.5838 0.1718  0.2200  -0.0569 121 LEU A CB  
913  C CG  . LEU A 127 ? 0.7342 0.5893 0.5338 0.1628  0.1969  -0.0678 121 LEU A CG  
914  C CD1 . LEU A 127 ? 0.8068 0.6390 0.6054 0.1645  0.1944  -0.0957 121 LEU A CD1 
915  C CD2 . LEU A 127 ? 0.7252 0.5786 0.4851 0.1520  0.1807  -0.0688 121 LEU A CD2 
916  N N   . SER A 128 ? 0.6982 0.6296 0.5383 0.1861  0.2667  -0.0218 122 SER A N   
917  C CA  . SER A 128 ? 0.7107 0.6575 0.5390 0.1898  0.2866  -0.0193 122 SER A CA  
918  C C   . SER A 128 ? 0.6872 0.6629 0.5284 0.1820  0.2904  0.0080  122 SER A C   
919  O O   . SER A 128 ? 0.7033 0.6870 0.5199 0.1789  0.3005  0.0118  122 SER A O   
920  C CB  . SER A 128 ? 0.7248 0.6777 0.5855 0.2043  0.3068  -0.0244 122 SER A CB  
921  O OG  . SER A 128 ? 0.7244 0.6492 0.5715 0.2101  0.3052  -0.0528 122 SER A OG  
922  N N   . LEU A 129 ? 0.6346 0.6278 0.5152 0.1773  0.2822  0.0268  123 LEU A N   
923  C CA  . LEU A 129 ? 0.6451 0.6669 0.5429 0.1661  0.2834  0.0502  123 LEU A CA  
924  C C   . LEU A 129 ? 0.6936 0.7026 0.5528 0.1525  0.2700  0.0519  123 LEU A C   
925  O O   . LEU A 129 ? 0.7140 0.7416 0.5839 0.1411  0.2714  0.0698  123 LEU A O   
926  C CB  . LEU A 129 ? 0.5774 0.6262 0.5296 0.1631  0.2761  0.0675  123 LEU A CB  
927  C CG  . LEU A 129 ? 0.6175 0.6788 0.6134 0.1776  0.2842  0.0698  123 LEU A CG  
928  C CD1 . LEU A 129 ? 0.5517 0.6450 0.5973 0.1724  0.2720  0.0895  123 LEU A CD1 
929  C CD2 . LEU A 129 ? 0.6711 0.7497 0.6812 0.1860  0.3069  0.0728  123 LEU A CD2 
930  N N   . CYS A 130 ? 0.6644 0.6425 0.4824 0.1528  0.2562  0.0340  124 CYS A N   
931  C CA  . CYS A 130 ? 0.6442 0.6096 0.4314 0.1413  0.2396  0.0367  124 CYS A CA  
932  C C   . CYS A 130 ? 0.7567 0.7159 0.5005 0.1406  0.2458  0.0360  124 CYS A C   
933  O O   . CYS A 130 ? 0.8381 0.7807 0.5458 0.1468  0.2446  0.0169  124 CYS A O   
934  C CB  . CYS A 130 ? 0.7950 0.7347 0.5660 0.1414  0.2194  0.0190  124 CYS A CB  
935  S SG  . CYS A 130 ? 0.7738 0.7034 0.5264 0.1278  0.1974  0.0255  124 CYS A SG  
936  N N   . LYS A 131 ? 0.7044 0.6789 0.4534 0.1318  0.2525  0.0570  125 LYS A N   
937  C CA  . LYS A 131 ? 0.7740 0.7455 0.4845 0.1308  0.2600  0.0619  125 LYS A CA  
938  C C   . LYS A 131 ? 0.7474 0.6968 0.4161 0.1262  0.2394  0.0594  125 LYS A C   
939  O O   . LYS A 131 ? 0.7218 0.6580 0.3929 0.1234  0.2202  0.0531  125 LYS A O   
940  C CB  . LYS A 131 ? 0.7698 0.7643 0.5060 0.1220  0.2750  0.0867  125 LYS A CB  
941  C CG  . LYS A 131 ? 0.7688 0.7892 0.5409 0.1275  0.2974  0.0900  125 LYS A CG  
942  N N   . LYS A 132 ? 0.8052 0.7523 0.4357 0.1260  0.2435  0.0654  126 LYS A N   
943  C CA  . LYS A 132 ? 0.8581 0.7900 0.4570 0.1211  0.2250  0.0722  126 LYS A CA  
944  C C   . LYS A 132 ? 0.8553 0.7893 0.4863 0.1096  0.2214  0.0947  126 LYS A C   
945  O O   . LYS A 132 ? 0.9614 0.9126 0.6265 0.1031  0.2373  0.1105  126 LYS A O   
946  C CB  . LYS A 132 ? 0.8829 0.8163 0.4367 0.1231  0.2319  0.0789  126 LYS A CB  
947  N N   . ASP A 133 ? 0.7323 0.6496 0.3551 0.1062  0.2001  0.0944  127 ASP A N   
948  C CA  . ASP A 133 ? 0.7430 0.6559 0.3930 0.0949  0.1931  0.1105  127 ASP A CA  
949  C C   . ASP A 133 ? 0.6912 0.6122 0.3841 0.0896  0.1916  0.1036  127 ASP A C   
950  O O   . ASP A 133 ? 0.7000 0.6164 0.4142 0.0791  0.1841  0.1119  127 ASP A O   
951  C CB  . ASP A 133 ? 0.7238 0.6452 0.3902 0.0851  0.2080  0.1370  127 ASP A CB  
952  C CG  . ASP A 133 ? 0.8749 0.7877 0.4996 0.0889  0.2084  0.1495  127 ASP A CG  
953  O OD1 . ASP A 133 ? 0.9497 0.8499 0.5351 0.0972  0.1920  0.1395  127 ASP A OD1 
954  O OD2 . ASP A 133 ? 0.9109 0.8314 0.5432 0.0829  0.2243  0.1698  127 ASP A OD2 
955  N N   . ASP A 134 ? 0.6355 0.5684 0.3429 0.0963  0.1988  0.0897  128 ASP A N   
956  C CA  . ASP A 134 ? 0.5623 0.5035 0.3064 0.0929  0.1943  0.0838  128 ASP A CA  
957  C C   . ASP A 134 ? 0.5300 0.4501 0.2540 0.0974  0.1745  0.0646  128 ASP A C   
958  O O   . ASP A 134 ? 0.6599 0.5637 0.3474 0.1056  0.1661  0.0502  128 ASP A O   
959  C CB  . ASP A 134 ? 0.5712 0.5343 0.3444 0.0999  0.2097  0.0799  128 ASP A CB  
960  C CG  . ASP A 134 ? 0.6259 0.6147 0.4269 0.0946  0.2287  0.0978  128 ASP A CG  
961  O OD1 . ASP A 134 ? 0.6783 0.6717 0.4911 0.0811  0.2292  0.1141  128 ASP A OD1 
962  O OD2 . ASP A 134 ? 0.6561 0.6600 0.4704 0.1036  0.2436  0.0949  128 ASP A OD2 
963  N N   . VAL A 135 ? 0.4888 0.4137 0.2473 0.0879  0.1607  0.0615  129 VAL A N   
964  C CA  . VAL A 135 ? 0.4713 0.3812 0.2267 0.0880  0.1385  0.0425  129 VAL A CA  
965  C C   . VAL A 135 ? 0.4620 0.3823 0.2441 0.0931  0.1419  0.0332  129 VAL A C   
966  O O   . VAL A 135 ? 0.5008 0.4444 0.3231 0.0869  0.1457  0.0430  129 VAL A O   
967  C CB  . VAL A 135 ? 0.5185 0.4256 0.2939 0.0730  0.1193  0.0448  129 VAL A CB  
968  C CG1 . VAL A 135 ? 0.5376 0.4334 0.3147 0.0726  0.0991  0.0261  129 VAL A CG1 
969  C CG2 . VAL A 135 ? 0.5518 0.4447 0.3041 0.0704  0.1169  0.0565  129 VAL A CG2 
970  N N   . PHE A 136 ? 0.5218 0.4251 0.2829 0.1042  0.1400  0.0147  130 PHE A N   
971  C CA  . PHE A 136 ? 0.4991 0.4050 0.2857 0.1105  0.1432  0.0062  130 PHE A CA  
972  C C   . PHE A 136 ? 0.4426 0.3425 0.2467 0.1014  0.1215  -0.0013 130 PHE A C   
973  O O   . PHE A 136 ? 0.5076 0.3894 0.2901 0.0977  0.1055  -0.0135 130 PHE A O   
974  C CB  . PHE A 136 ? 0.5905 0.4774 0.3490 0.1258  0.1543  -0.0125 130 PHE A CB  
975  C CG  . PHE A 136 ? 0.5936 0.4771 0.3812 0.1338  0.1599  -0.0207 130 PHE A CG  
976  C CD1 . PHE A 136 ? 0.6082 0.4695 0.3937 0.1322  0.1455  -0.0397 130 PHE A CD1 
977  C CD2 . PHE A 136 ? 0.6189 0.5232 0.4415 0.1417  0.1782  -0.0075 130 PHE A CD2 
978  C CE1 . PHE A 136 ? 0.5712 0.4268 0.3872 0.1384  0.1507  -0.0442 130 PHE A CE1 
979  C CE2 . PHE A 136 ? 0.5603 0.4604 0.4132 0.1502  0.1825  -0.0114 130 PHE A CE2 
980  C CZ  . PHE A 136 ? 0.6249 0.4984 0.4735 0.1485  0.1694  -0.0292 130 PHE A CZ  
981  N N   . ILE A 137 ? 0.4362 0.3540 0.2796 0.0980  0.1210  0.0071  131 ILE A N   
982  C CA  . ILE A 137 ? 0.3810 0.2967 0.2418 0.0896  0.1039  0.0025  131 ILE A CA  
983  C C   . ILE A 137 ? 0.4380 0.3523 0.3205 0.0995  0.1107  0.0012  131 ILE A C   
984  O O   . ILE A 137 ? 0.4572 0.3938 0.3678 0.1049  0.1218  0.0161  131 ILE A O   
985  C CB  . ILE A 137 ? 0.3403 0.2804 0.2252 0.0740  0.0947  0.0154  131 ILE A CB  
986  C CG1 . ILE A 137 ? 0.3797 0.3138 0.2459 0.0652  0.0896  0.0160  131 ILE A CG1 
987  C CG2 . ILE A 137 ? 0.3521 0.2920 0.2517 0.0662  0.0797  0.0105  131 ILE A CG2 
988  C CD1 . ILE A 137 ? 0.3931 0.3447 0.2811 0.0483  0.0808  0.0229  131 ILE A CD1 
989  N N   . GLU A 138 ? 0.4380 0.3265 0.3108 0.1020  0.1043  -0.0157 132 GLU A N   
990  C CA  . GLU A 138 ? 0.4627 0.3416 0.3570 0.1110  0.1112  -0.0178 132 GLU A CA  
991  C C   . GLU A 138 ? 0.4567 0.3616 0.3893 0.1071  0.1084  0.0034  132 GLU A C   
992  O O   . GLU A 138 ? 0.4343 0.3591 0.3727 0.0934  0.0958  0.0119  132 GLU A O   
993  C CB  . GLU A 138 ? 0.5618 0.4106 0.4437 0.1076  0.1005  -0.0393 132 GLU A CB  
994  C CG  . GLU A 138 ? 0.6504 0.4816 0.5560 0.1148  0.1077  -0.0429 132 GLU A CG  
995  C CD  . GLU A 138 ? 0.7423 0.5532 0.6399 0.1294  0.1250  -0.0573 132 GLU A CD  
996  O OE1 . GLU A 138 ? 0.8386 0.6536 0.7090 0.1313  0.1286  -0.0646 132 GLU A OE1 
997  O OE2 . GLU A 138 ? 0.8126 0.6114 0.7357 0.1332  0.1301  -0.0591 132 GLU A OE2 
998  N N   . GLN A 139 ? 0.4712 0.3766 0.4299 0.1199  0.1205  0.0118  133 GLN A N   
999  C CA  . GLN A 139 ? 0.3558 0.2870 0.3499 0.1186  0.1169  0.0346  133 GLN A CA  
1000 C C   . GLN A 139 ? 0.3646 0.2944 0.3573 0.1034  0.0994  0.0338  133 GLN A C   
1001 O O   . GLN A 139 ? 0.3554 0.2554 0.3370 0.1008  0.0953  0.0175  133 GLN A O   
1002 C CB  . GLN A 139 ? 0.4313 0.3516 0.4529 0.1368  0.1319  0.0420  133 GLN A CB  
1003 C CG  . GLN A 139 ? 0.4197 0.3686 0.4779 0.1384  0.1279  0.0702  133 GLN A CG  
1004 C CD  . GLN A 139 ? 0.5032 0.4369 0.5920 0.1584  0.1434  0.0798  133 GLN A CD  
1005 O OE1 . GLN A 139 ? 0.5853 0.4790 0.6669 0.1676  0.1555  0.0601  133 GLN A OE1 
1006 N NE2 . GLN A 139 ? 0.5595 0.5257 0.6840 0.1654  0.1430  0.1099  133 GLN A NE2 
1007 N N   . GLY A 140 ? 0.3380 0.3026 0.3431 0.0926  0.0896  0.0502  134 GLY A N   
1008 C CA  . GLY A 140 ? 0.3408 0.3092 0.3436 0.0779  0.0753  0.0497  134 GLY A CA  
1009 C C   . GLY A 140 ? 0.4071 0.3585 0.3834 0.0657  0.0655  0.0285  134 GLY A C   
1010 O O   . GLY A 140 ? 0.4091 0.3583 0.3838 0.0550  0.0562  0.0240  134 GLY A O   
1011 N N   . ILE A 141 ? 0.3524 0.2940 0.3091 0.0677  0.0682  0.0174  135 ILE A N   
1012 C CA  . ILE A 141 ? 0.3419 0.2645 0.2736 0.0605  0.0593  -0.0011 135 ILE A CA  
1013 C C   . ILE A 141 ? 0.3664 0.2619 0.2940 0.0609  0.0547  -0.0165 135 ILE A C   
1014 O O   . ILE A 141 ? 0.3554 0.2444 0.2754 0.0515  0.0434  -0.0278 135 ILE A O   
1015 C CB  . ILE A 141 ? 0.3383 0.2795 0.2704 0.0448  0.0484  0.0005  135 ILE A CB  
1016 C CG1 . ILE A 141 ? 0.4055 0.3803 0.3537 0.0407  0.0519  0.0174  135 ILE A CG1 
1017 C CG2 . ILE A 141 ? 0.3769 0.3023 0.2863 0.0419  0.0432  -0.0121 135 ILE A CG2 
1018 C CD1 . ILE A 141 ? 0.3883 0.3811 0.3387 0.0238  0.0426  0.0160  135 ILE A CD1 
1019 N N   . ALA A 142 ? 0.3459 0.2248 0.2817 0.0719  0.0644  -0.0179 136 ALA A N   
1020 C CA  . ALA A 142 ? 0.3871 0.2383 0.3242 0.0712  0.0619  -0.0336 136 ALA A CA  
1021 C C   . ALA A 142 ? 0.4084 0.2368 0.3170 0.0746  0.0594  -0.0573 136 ALA A C   
1022 O O   . ALA A 142 ? 0.4727 0.2801 0.3749 0.0846  0.0689  -0.0692 136 ALA A O   
1023 C CB  . ALA A 142 ? 0.4328 0.2729 0.3942 0.0810  0.0746  -0.0249 136 ALA A CB  
1024 N N   . ASN A 143 ? 0.4054 0.2391 0.2960 0.0667  0.0465  -0.0642 137 ASN A N   
1025 C CA  . ASN A 143 ? 0.4645 0.2838 0.3242 0.0703  0.0413  -0.0821 137 ASN A CA  
1026 C C   . ASN A 143 ? 0.4074 0.2270 0.2631 0.0600  0.0230  -0.0925 137 ASN A C   
1027 O O   . ASN A 143 ? 0.3956 0.2261 0.2720 0.0504  0.0170  -0.0867 137 ASN A O   
1028 C CB  . ASN A 143 ? 0.4540 0.2832 0.2924 0.0772  0.0489  -0.0727 137 ASN A CB  
1029 C CG  . ASN A 143 ? 0.4241 0.2752 0.2691 0.0689  0.0441  -0.0563 137 ASN A CG  
1030 O OD1 . ASN A 143 ? 0.3792 0.2362 0.2357 0.0586  0.0326  -0.0566 137 ASN A OD1 
1031 N ND2 . ASN A 143 ? 0.4501 0.3133 0.2895 0.0730  0.0546  -0.0431 137 ASN A ND2 
1032 N N   . LEU A 144 ? 0.3757 0.3488 0.2128 0.0585  0.0642  -0.0102 138 LEU A N   
1033 C CA  . LEU A 144 ? 0.3401 0.3087 0.1666 0.0556  0.0526  -0.0088 138 LEU A CA  
1034 C C   . LEU A 144 ? 0.3582 0.3289 0.1980 0.0495  0.0552  0.0060  138 LEU A C   
1035 O O   . LEU A 144 ? 0.3568 0.3240 0.1996 0.0452  0.0448  0.0071  138 LEU A O   
1036 C CB  . LEU A 144 ? 0.3765 0.3439 0.1685 0.0651  0.0518  -0.0121 138 LEU A CB  
1037 C CG  . LEU A 144 ? 0.4116 0.3739 0.1879 0.0703  0.0456  -0.0303 138 LEU A CG  
1038 C CD1 . LEU A 144 ? 0.4969 0.4600 0.2371 0.0799  0.0428  -0.0341 138 LEU A CD1 
1039 C CD2 . LEU A 144 ? 0.4042 0.3602 0.1959 0.0622  0.0306  -0.0414 138 LEU A CD2 
1040 N N   . GLU A 145 ? 0.3620 0.3381 0.2111 0.0490  0.0693  0.0171  139 GLU A N   
1041 C CA  . GLU A 145 ? 0.3122 0.2876 0.1762 0.0421  0.0725  0.0302  139 GLU A CA  
1042 C C   . GLU A 145 ? 0.3168 0.2912 0.2073 0.0326  0.0631  0.0266  139 GLU A C   
1043 O O   . GLU A 145 ? 0.2968 0.2662 0.1948 0.0274  0.0594  0.0327  139 GLU A O   
1044 C CB  . GLU A 145 ? 0.3215 0.3041 0.1954 0.0416  0.0904  0.0415  139 GLU A CB  
1045 C CG  . GLU A 145 ? 0.3809 0.3635 0.2265 0.0510  0.1024  0.0504  139 GLU A CG  
1046 C CD  . GLU A 145 ? 0.4632 0.4495 0.2852 0.0621  0.1048  0.0399  139 GLU A CD  
1047 O OE1 . GLU A 145 ? 0.5414 0.5264 0.3316 0.0719  0.1099  0.0438  139 GLU A OE1 
1048 O OE2 . GLU A 145 ? 0.4048 0.3947 0.2384 0.0620  0.1020  0.0280  139 GLU A OE2 
1049 N N   . ALA A 146 ? 0.3062 0.2841 0.2092 0.0314  0.0592  0.0169  140 ALA A N   
1050 C CA  . ALA A 146 ? 0.2827 0.2607 0.2080 0.0240  0.0510  0.0140  140 ALA A CA  
1051 C C   . ALA A 146 ? 0.2873 0.2577 0.2065 0.0219  0.0383  0.0106  140 ALA A C   
1052 O O   . ALA A 146 ? 0.2837 0.2535 0.2181 0.0162  0.0324  0.0104  140 ALA A O   
1053 C CB  . ALA A 146 ? 0.2990 0.2814 0.2352 0.0257  0.0498  0.0057  140 ALA A CB  
1054 N N   . GLN A 147 ? 0.2982 0.2646 0.1959 0.0268  0.0337  0.0075  141 GLN A N   
1055 C CA  . GLN A 147 ? 0.2902 0.2531 0.1862 0.0247  0.0215  0.0036  141 GLN A CA  
1056 C C   . GLN A 147 ? 0.2945 0.2550 0.1945 0.0224  0.0200  0.0122  141 GLN A C   
1057 O O   . GLN A 147 ? 0.2877 0.2473 0.1935 0.0199  0.0114  0.0096  141 GLN A O   
1058 C CB  . GLN A 147 ? 0.2849 0.2470 0.1595 0.0301  0.0154  -0.0034 141 GLN A CB  
1059 C CG  . GLN A 147 ? 0.3259 0.2885 0.1793 0.0366  0.0175  0.0036  141 GLN A CG  
1060 C CD  . GLN A 147 ? 0.3831 0.3470 0.2149 0.0424  0.0099  -0.0063 141 GLN A CD  
1061 O OE1 . GLN A 147 ? 0.3561 0.3219 0.1885 0.0408  -0.0021 -0.0124 141 GLN A OE1 
1062 N NE2 . GLN A 147 ? 0.3603 0.3244 0.1737 0.0492  0.0169  -0.0089 141 GLN A NE2 
1063 N N   . TYR A 148 ? 0.2913 0.2500 0.1883 0.0236  0.0290  0.0226  142 TYR A N   
1064 C CA  . TYR A 148 ? 0.2643 0.2168 0.1630 0.0227  0.0277  0.0308  142 TYR A CA  
1065 C C   . TYR A 148 ? 0.2844 0.2350 0.2058 0.0151  0.0250  0.0292  142 TYR A C   
1066 O O   . TYR A 148 ? 0.2666 0.2126 0.1901 0.0150  0.0189  0.0297  142 TYR A O   
1067 C CB  . TYR A 148 ? 0.2808 0.2291 0.1704 0.0258  0.0394  0.0437  142 TYR A CB  
1068 C CG  . TYR A 148 ? 0.3093 0.2600 0.1709 0.0354  0.0393  0.0440  142 TYR A CG  
1069 C CD1 . TYR A 148 ? 0.3424 0.2923 0.1886 0.0415  0.0291  0.0434  142 TYR A CD1 
1070 C CD2 . TYR A 148 ? 0.3550 0.3109 0.2061 0.0392  0.0477  0.0426  142 TYR A CD2 
1071 C CE1 . TYR A 148 ? 0.4164 0.3705 0.2363 0.0506  0.0261  0.0414  142 TYR A CE1 
1072 C CE2 . TYR A 148 ? 0.3865 0.3447 0.2087 0.0490  0.0460  0.0402  142 TYR A CE2 
1073 C CZ  . TYR A 148 ? 0.4174 0.3748 0.2240 0.0542  0.0343  0.0392  142 TYR A CZ  
1074 O OH  . TYR A 148 ? 0.4476 0.4088 0.2248 0.0642  0.0302  0.0354  142 TYR A OH  
1075 N N   . GLY A 149 ? 0.2535 0.2087 0.1911 0.0100  0.0287  0.0264  143 GLY A N   
1076 C CA  . GLY A 149 ? 0.2401 0.1952 0.1963 0.0038  0.0241  0.0228  143 GLY A CA  
1077 C C   . GLY A 149 ? 0.2376 0.1941 0.1931 0.0045  0.0140  0.0149  143 GLY A C   
1078 O O   . GLY A 149 ? 0.2353 0.1898 0.1991 0.0019  0.0093  0.0129  143 GLY A O   
1079 N N   . TYR A 150 ? 0.2415 0.2010 0.1873 0.0079  0.0112  0.0102  144 TYR A N   
1080 C CA  . TYR A 150 ? 0.2257 0.1863 0.1727 0.0075  0.0030  0.0040  144 TYR A CA  
1081 C C   . TYR A 150 ? 0.2467 0.2062 0.1855 0.0100  -0.0025 0.0049  144 TYR A C   
1082 O O   . TYR A 150 ? 0.2454 0.2066 0.1900 0.0088  -0.0078 0.0021  144 TYR A O   
1083 C CB  . TYR A 150 ? 0.2153 0.1777 0.1596 0.0087  0.0024  -0.0022 144 TYR A CB  
1084 C CG  . TYR A 150 ? 0.2318 0.1971 0.1890 0.0070  0.0055  -0.0028 144 TYR A CG  
1085 C CD1 . TYR A 150 ? 0.2307 0.1970 0.1976 0.0048  0.0012  -0.0044 144 TYR A CD1 
1086 C CD2 . TYR A 150 ? 0.2607 0.2296 0.2208 0.0084  0.0130  -0.0007 144 TYR A CD2 
1087 C CE1 . TYR A 150 ? 0.2219 0.1930 0.2000 0.0046  0.0025  -0.0045 144 TYR A CE1 
1088 C CE2 . TYR A 150 ? 0.2265 0.2016 0.2013 0.0075  0.0148  -0.0011 144 TYR A CE2 
1089 C CZ  . TYR A 150 ? 0.2108 0.1869 0.1940 0.0058  0.0086  -0.0032 144 TYR A CZ  
1090 O OH  . TYR A 150 ? 0.2136 0.1978 0.2105 0.0062  0.0087  -0.0035 144 TYR A OH  
1091 N N   . MET A 151 ? 0.2458 0.2038 0.1715 0.0145  -0.0010 0.0094  145 MET A N   
1092 C CA  . MET A 151 ? 0.2604 0.2182 0.1809 0.0182  -0.0062 0.0124  145 MET A CA  
1093 C C   . MET A 151 ? 0.2566 0.2088 0.1879 0.0167  -0.0050 0.0163  145 MET A C   
1094 O O   . MET A 151 ? 0.2428 0.1970 0.1787 0.0179  -0.0102 0.0145  145 MET A O   
1095 C CB  . MET A 151 ? 0.2668 0.2232 0.1693 0.0250  -0.0041 0.0186  145 MET A CB  
1096 C CG  . MET A 151 ? 0.2939 0.2525 0.1900 0.0312  -0.0111 0.0217  145 MET A CG  
1097 S SD  . MET A 151 ? 0.3190 0.2735 0.1922 0.0411  -0.0073 0.0331  145 MET A SD  
1098 C CE  . MET A 151 ? 0.3249 0.2869 0.1804 0.0432  -0.0086 0.0254  145 MET A CE  
1099 N N   . GLU A 152 ? 0.2376 0.1832 0.1744 0.0136  0.0020  0.0206  146 GLU A N   
1100 C CA  . GLU A 152 ? 0.2500 0.1881 0.1974 0.0112  0.0026  0.0218  146 GLU A CA  
1101 C C   . GLU A 152 ? 0.2336 0.1763 0.1911 0.0081  -0.0025 0.0138  146 GLU A C   
1102 O O   . GLU A 152 ? 0.2313 0.1713 0.1916 0.0099  -0.0056 0.0123  146 GLU A O   
1103 C CB  . GLU A 152 ? 0.2517 0.1833 0.2066 0.0064  0.0107  0.0265  146 GLU A CB  
1104 C CG  . GLU A 152 ? 0.3363 0.2566 0.3021 0.0031  0.0114  0.0269  146 GLU A CG  
1105 C CD  . GLU A 152 ? 0.4253 0.3388 0.4009 -0.0030 0.0200  0.0325  146 GLU A CD  
1106 O OE1 . GLU A 152 ? 0.4400 0.3404 0.4240 -0.0062 0.0215  0.0336  146 GLU A OE1 
1107 O OE2 . GLU A 152 ? 0.3209 0.2417 0.2964 -0.0046 0.0260  0.0357  146 GLU A OE2 
1108 N N   . LEU A 153 ? 0.2176 0.1672 0.1797 0.0048  -0.0028 0.0092  147 LEU A N   
1109 C CA  . LEU A 153 ? 0.2426 0.1964 0.2114 0.0031  -0.0069 0.0034  147 LEU A CA  
1110 C C   . LEU A 153 ? 0.2212 0.1790 0.1866 0.0062  -0.0114 0.0018  147 LEU A C   
1111 O O   . LEU A 153 ? 0.2146 0.1733 0.1835 0.0070  -0.0133 -0.0003 147 LEU A O   
1112 C CB  . LEU A 153 ? 0.2368 0.1963 0.2096 0.0010  -0.0061 0.0007  147 LEU A CB  
1113 C CG  . LEU A 153 ? 0.1958 0.1595 0.1727 0.0007  -0.0098 -0.0032 147 LEU A CG  
1114 C CD1 . LEU A 153 ? 0.2177 0.1802 0.1993 -0.0001 -0.0119 -0.0054 147 LEU A CD1 
1115 C CD2 . LEU A 153 ? 0.2187 0.1865 0.1992 0.0004  -0.0087 -0.0044 147 LEU A CD2 
1116 N N   . ALA A 154 ? 0.2225 0.1839 0.1814 0.0079  -0.0130 0.0021  148 ALA A N   
1117 C CA  . ALA A 154 ? 0.1837 0.1517 0.1434 0.0097  -0.0176 0.0004  148 ALA A CA  
1118 C C   . ALA A 154 ? 0.2242 0.1914 0.1845 0.0143  -0.0186 0.0032  148 ALA A C   
1119 O O   . ALA A 154 ? 0.2411 0.2142 0.2073 0.0157  -0.0204 0.0017  148 ALA A O   
1120 C CB  . ALA A 154 ? 0.2160 0.1885 0.1690 0.0105  -0.0208 -0.0014 148 ALA A CB  
1121 N N   . GLN A 155 ? 0.2057 0.1650 0.1602 0.0175  -0.0165 0.0082  149 GLN A N   
1122 C CA  . GLN A 155 ? 0.2408 0.1962 0.1956 0.0235  -0.0171 0.0115  149 GLN A CA  
1123 C C   . GLN A 155 ? 0.2286 0.1781 0.1905 0.0225  -0.0153 0.0083  149 GLN A C   
1124 O O   . GLN A 155 ? 0.2286 0.1802 0.1934 0.0275  -0.0166 0.0072  149 GLN A O   
1125 C CB  . GLN A 155 ? 0.2237 0.1689 0.1697 0.0275  -0.0141 0.0193  149 GLN A CB  
1126 C CG  . GLN A 155 ? 0.2536 0.2071 0.1886 0.0314  -0.0176 0.0216  149 GLN A CG  
1127 C CD  . GLN A 155 ? 0.3329 0.2778 0.2551 0.0375  -0.0143 0.0312  149 GLN A CD  
1128 O OE1 . GLN A 155 ? 0.4050 0.3356 0.3284 0.0383  -0.0086 0.0375  149 GLN A OE1 
1129 N NE2 . GLN A 155 ? 0.2888 0.2416 0.1980 0.0419  -0.0180 0.0325  149 GLN A NE2 
1130 N N   . GLU A 156 ? 0.2140 0.1576 0.1789 0.0167  -0.0127 0.0059  150 GLU A N   
1131 C CA  . GLU A 156 ? 0.1970 0.1368 0.1668 0.0157  -0.0128 0.0005  150 GLU A CA  
1132 C C   . GLU A 156 ? 0.2199 0.1709 0.1909 0.0173  -0.0149 -0.0034 150 GLU A C   
1133 O O   . GLU A 156 ? 0.2266 0.1768 0.1979 0.0215  -0.0148 -0.0064 150 GLU A O   
1134 C CB  . GLU A 156 ? 0.2388 0.1755 0.2133 0.0089  -0.0116 -0.0023 150 GLU A CB  
1135 C CG  . GLU A 156 ? 0.2632 0.1883 0.2405 0.0059  -0.0077 0.0018  150 GLU A CG  
1136 C CD  . GLU A 156 ? 0.2941 0.2208 0.2807 -0.0016 -0.0067 -0.0012 150 GLU A CD  
1137 O OE1 . GLU A 156 ? 0.2506 0.1721 0.2421 -0.0056 -0.0018 0.0035  150 GLU A OE1 
1138 O OE2 . GLU A 156 ? 0.2316 0.1660 0.2214 -0.0031 -0.0106 -0.0077 150 GLU A OE2 
1139 N N   . ILE A 157 ? 0.2166 0.1768 0.1883 0.0141  -0.0157 -0.0033 151 ILE A N   
1140 C CA  . ILE A 157 ? 0.2313 0.2008 0.2051 0.0146  -0.0159 -0.0051 151 ILE A CA  
1141 C C   . ILE A 157 ? 0.2354 0.2126 0.2123 0.0193  -0.0163 -0.0036 151 ILE A C   
1142 O O   . ILE A 157 ? 0.2221 0.2056 0.2015 0.0221  -0.0145 -0.0047 151 ILE A O   
1143 C CB  . ILE A 157 ? 0.2176 0.1916 0.1927 0.0100  -0.0160 -0.0046 151 ILE A CB  
1144 C CG1 . ILE A 157 ? 0.1886 0.1583 0.1629 0.0073  -0.0156 -0.0059 151 ILE A CG1 
1145 C CG2 . ILE A 157 ? 0.2315 0.2139 0.2104 0.0097  -0.0149 -0.0041 151 ILE A CG2 
1146 C CD1 . ILE A 157 ? 0.2278 0.1990 0.2028 0.0045  -0.0152 -0.0052 151 ILE A CD1 
1147 N N   . GLN A 158 ? 0.1994 0.1778 0.1758 0.0213  -0.0185 -0.0009 152 GLN A N   
1148 C CA  . GLN A 158 ? 0.2079 0.1966 0.1894 0.0269  -0.0202 0.0004  152 GLN A CA  
1149 C C   . GLN A 158 ? 0.2277 0.2118 0.2094 0.0342  -0.0177 -0.0001 152 GLN A C   
1150 O O   . GLN A 158 ? 0.2287 0.2234 0.2167 0.0383  -0.0161 -0.0010 152 GLN A O   
1151 C CB  . GLN A 158 ? 0.1993 0.1898 0.1774 0.0294  -0.0244 0.0036  152 GLN A CB  
1152 C CG  . GLN A 158 ? 0.2295 0.2333 0.2141 0.0367  -0.0279 0.0051  152 GLN A CG  
1153 C CD  . GLN A 158 ? 0.2285 0.2384 0.2085 0.0389  -0.0342 0.0071  152 GLN A CD  
1154 O OE1 . GLN A 158 ? 0.2752 0.2746 0.2440 0.0437  -0.0343 0.0118  152 GLN A OE1 
1155 N NE2 . GLN A 158 ? 0.2346 0.2611 0.2228 0.0351  -0.0393 0.0035  152 GLN A NE2 
1156 N N   . MET A 159 ? 0.2217 0.1893 0.1973 0.0357  -0.0166 0.0000  153 MET A N   
1157 C CA  . MET A 159 ? 0.2218 0.1808 0.1968 0.0427  -0.0143 -0.0024 153 MET A CA  
1158 C C   . MET A 159 ? 0.2358 0.1974 0.2102 0.0420  -0.0120 -0.0087 153 MET A C   
1159 O O   . MET A 159 ? 0.2466 0.2122 0.2220 0.0493  -0.0096 -0.0110 153 MET A O   
1160 C CB  . MET A 159 ? 0.2558 0.1940 0.2264 0.0422  -0.0133 -0.0015 153 MET A CB  
1161 C CG  . MET A 159 ? 0.4857 0.4190 0.4532 0.0432  -0.0140 0.0065  153 MET A CG  
1162 S SD  . MET A 159 ? 0.7081 0.6167 0.6735 0.0388  -0.0101 0.0085  153 MET A SD  
1163 C CE  . MET A 159 ? 0.7129 0.6259 0.6738 0.0333  -0.0093 0.0159  153 MET A CE  
1164 N N   . GLN A 160 ? 0.2136 0.1740 0.1854 0.0346  -0.0126 -0.0111 154 GLN A N   
1165 C CA  . GLN A 160 ? 0.2348 0.1967 0.2024 0.0353  -0.0112 -0.0167 154 GLN A CA  
1166 C C   . GLN A 160 ? 0.2414 0.2195 0.2111 0.0375  -0.0080 -0.0144 154 GLN A C   
1167 O O   . GLN A 160 ? 0.2431 0.2244 0.2082 0.0431  -0.0047 -0.0176 154 GLN A O   
1168 C CB  . GLN A 160 ? 0.2274 0.1854 0.1926 0.0280  -0.0137 -0.0190 154 GLN A CB  
1169 C CG  . GLN A 160 ? 0.2512 0.1941 0.2171 0.0252  -0.0157 -0.0226 154 GLN A CG  
1170 C CD  . GLN A 160 ? 0.2564 0.1998 0.2245 0.0178  -0.0183 -0.0244 154 GLN A CD  
1171 O OE1 . GLN A 160 ? 0.2487 0.1982 0.2195 0.0140  -0.0180 -0.0195 154 GLN A OE1 
1172 N NE2 . GLN A 160 ? 0.2914 0.2288 0.2591 0.0162  -0.0214 -0.0324 154 GLN A NE2 
1173 N N   . SER A 161 ? 0.2059 0.1939 0.1824 0.0328  -0.0084 -0.0093 155 SER A N   
1174 C CA  A SER A 161 ? 0.2249 0.2282 0.2079 0.0331  -0.0045 -0.0061 155 SER A CA  
1175 C CA  B SER A 161 ? 0.2221 0.2254 0.2050 0.0331  -0.0044 -0.0062 155 SER A CA  
1176 C C   . SER A 161 ? 0.2554 0.2678 0.2442 0.0414  -0.0014 -0.0061 155 SER A C   
1177 O O   . SER A 161 ? 0.2579 0.2799 0.2475 0.0453  0.0046  -0.0056 155 SER A O   
1178 C CB  A SER A 161 ? 0.2585 0.2687 0.2504 0.0258  -0.0067 -0.0025 155 SER A CB  
1179 C CB  B SER A 161 ? 0.2625 0.2725 0.2541 0.0257  -0.0066 -0.0025 155 SER A CB  
1180 O OG  A SER A 161 ? 0.2345 0.2605 0.2381 0.0252  -0.0031 0.0005  155 SER A OG  
1181 O OG  B SER A 161 ? 0.2815 0.2823 0.2676 0.0199  -0.0087 -0.0029 155 SER A OG  
1182 N N   . GLN A 162 ? 0.2191 0.2293 0.2114 0.0455  -0.0047 -0.0057 156 GLN A N   
1183 C CA  . GLN A 162 ? 0.2086 0.2284 0.2079 0.0554  -0.0022 -0.0053 156 GLN A CA  
1184 C C   . GLN A 162 ? 0.2259 0.2364 0.2157 0.0639  0.0025  -0.0106 156 GLN A C   
1185 O O   . GLN A 162 ? 0.2435 0.2658 0.2376 0.0719  0.0082  -0.0111 156 GLN A O   
1186 C CB  . GLN A 162 ? 0.2347 0.2518 0.2372 0.0596  -0.0076 -0.0027 156 GLN A CB  
1187 C CG  . GLN A 162 ? 0.2164 0.2406 0.2255 0.0725  -0.0058 -0.0021 156 GLN A CG  
1188 C CD  . GLN A 162 ? 0.2475 0.2985 0.2725 0.0747  -0.0018 -0.0006 156 GLN A CD  
1189 O OE1 . GLN A 162 ? 0.2524 0.3178 0.2867 0.0654  -0.0024 0.0013  156 GLN A OE1 
1190 N NE2 . GLN A 162 ? 0.2436 0.3012 0.2734 0.0871  0.0028  -0.0014 156 GLN A NE2 
1191 N N   . SER A 163 ? 0.2250 0.2156 0.2029 0.0622  0.0002  -0.0156 157 SER A N   
1192 C CA  A SER A 163 ? 0.2682 0.2476 0.2360 0.0697  0.0029  -0.0234 157 SER A CA  
1193 C CA  B SER A 163 ? 0.2687 0.2483 0.2366 0.0698  0.0030  -0.0234 157 SER A CA  
1194 C C   . SER A 163 ? 0.2839 0.2739 0.2448 0.0713  0.0081  -0.0257 157 SER A C   
1195 O O   . SER A 163 ? 0.2600 0.2487 0.2132 0.0809  0.0125  -0.0315 157 SER A O   
1196 C CB  A SER A 163 ? 0.2930 0.2502 0.2528 0.0650  -0.0018 -0.0292 157 SER A CB  
1197 C CB  B SER A 163 ? 0.2959 0.2532 0.2558 0.0653  -0.0017 -0.0292 157 SER A CB  
1198 O OG  A SER A 163 ? 0.2425 0.1869 0.2067 0.0658  -0.0040 -0.0262 157 SER A OG  
1199 O OG  B SER A 163 ? 0.3167 0.2757 0.2720 0.0565  -0.0041 -0.0303 157 SER A OG  
1200 N N   . LEU A 164 ? 0.2410 0.2400 0.2029 0.0630  0.0081  -0.0209 158 LEU A N   
1201 C CA  . LEU A 164 ? 0.2185 0.2276 0.1732 0.0644  0.0138  -0.0196 158 LEU A CA  
1202 C C   . LEU A 164 ? 0.3227 0.3524 0.2905 0.0650  0.0214  -0.0114 158 LEU A C   
1203 O O   . LEU A 164 ? 0.3287 0.3677 0.2914 0.0672  0.0290  -0.0082 158 LEU A O   
1204 C CB  . LEU A 164 ? 0.2525 0.2576 0.2012 0.0557  0.0100  -0.0178 158 LEU A CB  
1205 C CG  . LEU A 164 ? 0.2844 0.2741 0.2216 0.0545  0.0029  -0.0262 158 LEU A CG  
1206 C CD1 . LEU A 164 ? 0.3143 0.3028 0.2522 0.0458  -0.0016 -0.0229 158 LEU A CD1 
1207 C CD2 . LEU A 164 ? 0.2817 0.2701 0.2015 0.0630  0.0045  -0.0340 158 LEU A CD2 
1208 N N   . LYS A 165 ? 0.2845 0.3226 0.2697 0.0628  0.0196  -0.0077 159 LYS A N   
1209 C CA  . LYS A 165 ? 0.2460 0.3057 0.2494 0.0600  0.0247  -0.0006 159 LYS A CA  
1210 C C   . LYS A 165 ? 0.2963 0.3592 0.3004 0.0504  0.0280  0.0053  159 LYS A C   
1211 O O   . LYS A 165 ? 0.3244 0.4012 0.3348 0.0505  0.0373  0.0110  159 LYS A O   
1212 C CB  . LYS A 165 ? 0.2767 0.3516 0.2853 0.0712  0.0340  -0.0004 159 LYS A CB  
1213 C CG  . LYS A 165 ? 0.3082 0.3832 0.3234 0.0808  0.0306  -0.0039 159 LYS A CG  
1214 C CD  . LYS A 165 ? 0.4588 0.5474 0.4775 0.0944  0.0405  -0.0050 159 LYS A CD  
1215 N N   . LEU A 166 ? 0.2543 0.3038 0.2523 0.0426  0.0211  0.0046  160 LEU A N   
1216 C CA  . LEU A 166 ? 0.2712 0.3195 0.2696 0.0342  0.0230  0.0101  160 LEU A CA  
1217 C C   . LEU A 166 ? 0.3235 0.3703 0.3342 0.0245  0.0164  0.0105  160 LEU A C   
1218 O O   . LEU A 166 ? 0.4222 0.4604 0.4297 0.0241  0.0086  0.0061  160 LEU A O   
1219 C CB  . LEU A 166 ? 0.3119 0.3458 0.2904 0.0355  0.0210  0.0083  160 LEU A CB  
1220 C CG  . LEU A 166 ? 0.4326 0.4661 0.3932 0.0451  0.0258  0.0063  160 LEU A CG  
1221 C CD1 . LEU A 166 ? 0.4469 0.4677 0.3910 0.0452  0.0193  0.0024  160 LEU A CD1 
1222 C CD2 . LEU A 166 ? 0.3908 0.4364 0.3524 0.0469  0.0374  0.0153  160 LEU A CD2 
1223 N N   . ASP A 167 ? 0.2745 0.3288 0.2987 0.0168  0.0200  0.0158  161 ASP A N   
1224 C CA  . ASP A 167 ? 0.3121 0.3649 0.3478 0.0071  0.0140  0.0147  161 ASP A CA  
1225 C C   . ASP A 167 ? 0.3295 0.3666 0.3557 0.0023  0.0142  0.0168  161 ASP A C   
1226 O O   . ASP A 167 ? 0.3253 0.3622 0.3564 -0.0020 0.0210  0.0230  161 ASP A O   
1227 C CB  . ASP A 167 ? 0.3996 0.4705 0.4592 0.0009  0.0179  0.0178  161 ASP A CB  
1228 C CG  . ASP A 167 ? 0.5021 0.5719 0.5745 -0.0099 0.0112  0.0147  161 ASP A CG  
1229 O OD1 . ASP A 167 ? 0.4668 0.5258 0.5298 -0.0103 0.0025  0.0092  161 ASP A OD1 
1230 O OD2 . ASP A 167 ? 0.4704 0.5505 0.5631 -0.0183 0.0151  0.0174  161 ASP A OD2 
1231 N N   . PHE A 168 ? 0.2451 0.2695 0.2595 0.0034  0.0076  0.0124  162 PHE A N   
1232 C CA  . PHE A 168 ? 0.2160 0.2275 0.2212 0.0017  0.0081  0.0146  162 PHE A CA  
1233 C C   . PHE A 168 ? 0.2507 0.2551 0.2636 -0.0063 0.0060  0.0141  162 PHE A C   
1234 O O   . PHE A 168 ? 0.2520 0.2594 0.2728 -0.0104 0.0010  0.0094  162 PHE A O   
1235 C CB  . PHE A 168 ? 0.2467 0.2491 0.2393 0.0054  0.0021  0.0096  162 PHE A CB  
1236 C CG  . PHE A 168 ? 0.2664 0.2692 0.2480 0.0129  0.0021  0.0074  162 PHE A CG  
1237 C CD1 . PHE A 168 ? 0.2632 0.2665 0.2351 0.0175  0.0061  0.0104  162 PHE A CD1 
1238 C CD2 . PHE A 168 ? 0.2887 0.2897 0.2684 0.0156  -0.0021 0.0021  162 PHE A CD2 
1239 C CE1 . PHE A 168 ? 0.3303 0.3333 0.2907 0.0244  0.0050  0.0059  162 PHE A CE1 
1240 C CE2 . PHE A 168 ? 0.3091 0.3076 0.2796 0.0217  -0.0024 -0.0016 162 PHE A CE2 
1241 C CZ  . PHE A 168 ? 0.2965 0.2964 0.2572 0.0259  0.0006  -0.0008 162 PHE A CZ  
1242 N N   . ASP A 169 ? 0.2228 0.2176 0.2312 -0.0069 0.0098  0.0191  163 ASP A N   
1243 C CA  . ASP A 169 ? 0.2407 0.2225 0.2503 -0.0112 0.0076  0.0177  163 ASP A CA  
1244 C C   . ASP A 169 ? 0.2676 0.2432 0.2632 -0.0049 0.0035  0.0153  163 ASP A C   
1245 O O   . ASP A 169 ? 0.2604 0.2380 0.2468 0.0010  0.0047  0.0181  163 ASP A O   
1246 C CB  . ASP A 169 ? 0.2345 0.2076 0.2480 -0.0141 0.0147  0.0257  163 ASP A CB  
1247 C CG  . ASP A 169 ? 0.2923 0.2692 0.3248 -0.0236 0.0186  0.0271  163 ASP A CG  
1248 O OD1 . ASP A 169 ? 0.2821 0.2656 0.3246 -0.0288 0.0129  0.0193  163 ASP A OD1 
1249 O OD2 . ASP A 169 ? 0.3058 0.2792 0.3428 -0.0256 0.0270  0.0361  163 ASP A OD2 
1250 N N   . ILE A 170 ? 0.2145 0.1843 0.2096 -0.0064 -0.0012 0.0096  164 ILE A N   
1251 C CA  . ILE A 170 ? 0.2320 0.1988 0.2184 -0.0017 -0.0045 0.0071  164 ILE A CA  
1252 C C   . ILE A 170 ? 0.2578 0.2144 0.2432 -0.0006 -0.0034 0.0085  164 ILE A C   
1253 O O   . ILE A 170 ? 0.2583 0.2071 0.2487 -0.0046 -0.0025 0.0068  164 ILE A O   
1254 C CB  . ILE A 170 ? 0.2441 0.2132 0.2298 -0.0026 -0.0088 0.0010  164 ILE A CB  
1255 C CG1 . ILE A 170 ? 0.2046 0.1824 0.1915 -0.0019 -0.0099 0.0003  164 ILE A CG1 
1256 C CG2 . ILE A 170 ? 0.2534 0.2200 0.2340 0.0007  -0.0103 -0.0006 164 ILE A CG2 
1257 C CD1 . ILE A 170 ? 0.2435 0.2225 0.2290 -0.0020 -0.0138 -0.0036 164 ILE A CD1 
1258 N N   . PHE A 171 ? 0.2319 0.1886 0.2116 0.0053  -0.0041 0.0107  165 PHE A N   
1259 C CA  . PHE A 171 ? 0.2191 0.1678 0.1987 0.0086  -0.0034 0.0121  165 PHE A CA  
1260 C C   . PHE A 171 ? 0.2367 0.1908 0.2154 0.0124  -0.0069 0.0083  165 PHE A C   
1261 O O   . PHE A 171 ? 0.2101 0.1733 0.1869 0.0141  -0.0099 0.0074  165 PHE A O   
1262 C CB  . PHE A 171 ? 0.2382 0.1827 0.2140 0.0138  -0.0003 0.0211  165 PHE A CB  
1263 C CG  . PHE A 171 ? 0.2558 0.1905 0.2325 0.0188  0.0008  0.0234  165 PHE A CG  
1264 C CD1 . PHE A 171 ? 0.2692 0.2104 0.2446 0.0258  -0.0030 0.0222  165 PHE A CD1 
1265 C CD2 . PHE A 171 ? 0.3112 0.2302 0.2920 0.0164  0.0054  0.0258  165 PHE A CD2 
1266 C CE1 . PHE A 171 ? 0.2782 0.2119 0.2558 0.0321  -0.0018 0.0243  165 PHE A CE1 
1267 C CE2 . PHE A 171 ? 0.3221 0.2297 0.3035 0.0225  0.0068  0.0276  165 PHE A CE2 
1268 C CZ  . PHE A 171 ? 0.2936 0.2094 0.2731 0.0311  0.0034  0.0270  165 PHE A CZ  
1269 N N   . LEU A 172 ? 0.2117 0.1605 0.1931 0.0133  -0.0060 0.0055  166 LEU A N   
1270 C CA  . LEU A 172 ? 0.2151 0.1706 0.1990 0.0176  -0.0074 0.0036  166 LEU A CA  
1271 C C   . LEU A 172 ? 0.2610 0.2081 0.2471 0.0223  -0.0044 0.0036  166 LEU A C   
1272 O O   . LEU A 172 ? 0.2471 0.1820 0.2318 0.0199  -0.0018 0.0012  166 LEU A O   
1273 C CB  . LEU A 172 ? 0.2100 0.1715 0.1951 0.0138  -0.0079 -0.0014 166 LEU A CB  
1274 C CG  . LEU A 172 ? 0.2586 0.2143 0.2412 0.0114  -0.0055 -0.0058 166 LEU A CG  
1275 C CD1 . LEU A 172 ? 0.2396 0.2024 0.2222 0.0097  -0.0051 -0.0074 166 LEU A CD1 
1276 C CD2 . LEU A 172 ? 0.2626 0.2120 0.2421 0.0068  -0.0064 -0.0071 166 LEU A CD2 
1277 N N   . PRO A 173 ? 0.2169 0.1704 0.2071 0.0294  -0.0051 0.0054  167 PRO A N   
1278 C CA  . PRO A 173 ? 0.2371 0.1825 0.2299 0.0364  -0.0017 0.0058  167 PRO A CA  
1279 C C   . PRO A 173 ? 0.2364 0.1832 0.2315 0.0362  0.0017  -0.0010 167 PRO A C   
1280 O O   . PRO A 173 ? 0.2498 0.2078 0.2468 0.0324  0.0013  -0.0037 167 PRO A O   
1281 C CB  . PRO A 173 ? 0.2347 0.1918 0.2323 0.0452  -0.0048 0.0108  167 PRO A CB  
1282 C CG  . PRO A 173 ? 0.2456 0.2209 0.2471 0.0407  -0.0097 0.0080  167 PRO A CG  
1283 C CD  . PRO A 173 ? 0.2375 0.2070 0.2315 0.0318  -0.0098 0.0065  167 PRO A CD  
1284 N N   . SER A 174 ? 0.2134 0.1474 0.2075 0.0412  0.0058  -0.0034 168 SER A N   
1285 C CA  . SER A 174 ? 0.2541 0.1878 0.2467 0.0426  0.0102  -0.0105 168 SER A CA  
1286 C C   . SER A 174 ? 0.2860 0.2233 0.2855 0.0538  0.0144  -0.0103 168 SER A C   
1287 O O   . SER A 174 ? 0.2634 0.1937 0.2662 0.0615  0.0145  -0.0062 168 SER A O   
1288 C CB  . SER A 174 ? 0.2648 0.1797 0.2482 0.0388  0.0116  -0.0176 168 SER A CB  
1289 O OG  . SER A 174 ? 0.2706 0.1878 0.2490 0.0292  0.0080  -0.0194 168 SER A OG  
1290 N N   . GLY A 175 ? 0.2381 0.1870 0.2399 0.0553  0.0188  -0.0140 169 GLY A N   
1291 C CA  . GLY A 175 ? 0.2356 0.1872 0.2423 0.0661  0.0254  -0.0164 169 GLY A CA  
1292 C C   . GLY A 175 ? 0.2660 0.2034 0.2590 0.0665  0.0308  -0.0254 169 GLY A C   
1293 O O   . GLY A 175 ? 0.2906 0.2074 0.2771 0.0705  0.0317  -0.0303 169 GLY A O   
1294 N N   . THR A 176 ? 0.2901 0.2370 0.2774 0.0623  0.0339  -0.0279 170 THR A N   
1295 C CA  . THR A 176 ? 0.3104 0.2460 0.2802 0.0627  0.0374  -0.0369 170 THR A CA  
1296 C C   . THR A 176 ? 0.3056 0.2284 0.2638 0.0531  0.0300  -0.0407 170 THR A C   
1297 O O   . THR A 176 ? 0.3300 0.2406 0.2737 0.0534  0.0300  -0.0503 170 THR A O   
1298 C CB  . THR A 176 ? 0.2766 0.2281 0.2427 0.0634  0.0446  -0.0360 170 THR A CB  
1299 O OG1 . THR A 176 ? 0.2722 0.2321 0.2386 0.0533  0.0404  -0.0304 170 THR A OG1 
1300 C CG2 . THR A 176 ? 0.3080 0.2776 0.2908 0.0714  0.0527  -0.0314 170 THR A CG2 
1301 N N   . GLY A 177 ? 0.2489 0.1759 0.2134 0.0450  0.0236  -0.0343 171 GLY A N   
1302 C CA  . GLY A 177 ? 0.2700 0.1897 0.2275 0.0360  0.0169  -0.0367 171 GLY A CA  
1303 C C   . GLY A 177 ? 0.2723 0.2018 0.2213 0.0315  0.0158  -0.0365 171 GLY A C   
1304 O O   . GLY A 177 ? 0.2955 0.2220 0.2397 0.0251  0.0097  -0.0383 171 GLY A O   
1305 N N   . THR A 178 ? 0.2807 0.2221 0.2291 0.0350  0.0219  -0.0333 172 THR A N   
1306 C CA  . THR A 178 ? 0.2674 0.2156 0.2059 0.0322  0.0225  -0.0313 172 THR A CA  
1307 C C   . THR A 178 ? 0.2528 0.2049 0.1970 0.0246  0.0161  -0.0255 172 THR A C   
1308 O O   . THR A 178 ? 0.2546 0.2046 0.1895 0.0213  0.0112  -0.0269 172 THR A O   
1309 C CB  . THR A 178 ? 0.2933 0.2536 0.2346 0.0366  0.0323  -0.0263 172 THR A CB  
1310 O OG1 . THR A 178 ? 0.2766 0.2340 0.2112 0.0454  0.0393  -0.0324 172 THR A OG1 
1311 C CG2 . THR A 178 ? 0.2745 0.2395 0.2050 0.0342  0.0343  -0.0216 172 THR A CG2 
1312 N N   . SER A 179 ? 0.2436 0.2022 0.2028 0.0226  0.0156  -0.0197 173 SER A N   
1313 C CA  . SER A 179 ? 0.2213 0.1831 0.1853 0.0166  0.0104  -0.0153 173 SER A CA  
1314 C C   . SER A 179 ? 0.2665 0.2208 0.2271 0.0132  0.0037  -0.0180 173 SER A C   
1315 O O   . SER A 179 ? 0.2773 0.2326 0.2340 0.0099  0.0000  -0.0171 173 SER A O   
1316 C CB  . SER A 179 ? 0.2393 0.2094 0.2187 0.0161  0.0100  -0.0112 173 SER A CB  
1317 O OG  . SER A 179 ? 0.2386 0.2185 0.2251 0.0167  0.0160  -0.0083 173 SER A OG  
1318 N N   . ALA A 180 ? 0.2282 0.1750 0.1917 0.0143  0.0026  -0.0205 174 ALA A N   
1319 C CA  . ALA A 180 ? 0.2398 0.1803 0.2037 0.0097  -0.0022 -0.0221 174 ALA A CA  
1320 C C   . ALA A 180 ? 0.2571 0.1944 0.2118 0.0073  -0.0053 -0.0288 174 ALA A C   
1321 O O   . ALA A 180 ? 0.2878 0.2281 0.2438 0.0027  -0.0101 -0.0289 174 ALA A O   
1322 C CB  . ALA A 180 ? 0.2323 0.1626 0.2016 0.0114  -0.0011 -0.0221 174 ALA A CB  
1323 N N   . ALA A 181 ? 0.2919 0.2246 0.2372 0.0112  -0.0031 -0.0352 175 ALA A N   
1324 C CA  . ALA A 181 ? 0.2825 0.2134 0.2164 0.0100  -0.0076 -0.0432 175 ALA A CA  
1325 C C   . ALA A 181 ? 0.2658 0.2076 0.1940 0.0093  -0.0106 -0.0390 175 ALA A C   
1326 O O   . ALA A 181 ? 0.3086 0.2534 0.2352 0.0060  -0.0177 -0.0424 175 ALA A O   
1327 C CB  . ALA A 181 ? 0.2644 0.1895 0.1853 0.0164  -0.0037 -0.0510 175 ALA A CB  
1328 N N   . PHE A 182 ? 0.2890 0.2369 0.2159 0.0123  -0.0054 -0.0313 176 PHE A N   
1329 C CA  . PHE A 182 ? 0.2743 0.2288 0.1946 0.0128  -0.0072 -0.0264 176 PHE A CA  
1330 C C   . PHE A 182 ? 0.2527 0.2109 0.1841 0.0086  -0.0114 -0.0217 176 PHE A C   
1331 O O   . PHE A 182 ? 0.2662 0.2288 0.1936 0.0090  -0.0157 -0.0200 176 PHE A O   
1332 C CB  . PHE A 182 ? 0.2814 0.2388 0.1971 0.0167  0.0012  -0.0194 176 PHE A CB  
1333 C CG  . PHE A 182 ? 0.2595 0.2156 0.1598 0.0226  0.0063  -0.0232 176 PHE A CG  
1334 C CD1 . PHE A 182 ? 0.2877 0.2421 0.1708 0.0255  0.0008  -0.0307 176 PHE A CD1 
1335 C CD2 . PHE A 182 ? 0.2733 0.2315 0.1762 0.0259  0.0164  -0.0200 176 PHE A CD2 
1336 C CE1 . PHE A 182 ? 0.3070 0.2599 0.1720 0.0324  0.0057  -0.0354 176 PHE A CE1 
1337 C CE2 . PHE A 182 ? 0.3375 0.2954 0.2248 0.0328  0.0227  -0.0234 176 PHE A CE2 
1338 C CZ  . PHE A 182 ? 0.3617 0.3159 0.2282 0.0365  0.0176  -0.0314 176 PHE A CZ  
1339 N N   . LEU A 183 ? 0.2393 0.1966 0.1836 0.0059  -0.0100 -0.0194 177 LEU A N   
1340 C CA  . LEU A 183 ? 0.2357 0.1966 0.1881 0.0030  -0.0135 -0.0162 177 LEU A CA  
1341 C C   . LEU A 183 ? 0.2580 0.2206 0.2128 -0.0001 -0.0192 -0.0206 177 LEU A C   
1342 O O   . LEU A 183 ? 0.2577 0.2270 0.2147 -0.0004 -0.0229 -0.0190 177 LEU A O   
1343 C CB  . LEU A 183 ? 0.2270 0.1874 0.1894 0.0019  -0.0112 -0.0132 177 LEU A CB  
1344 C CG  . LEU A 183 ? 0.2054 0.1697 0.1733 0.0005  -0.0134 -0.0101 177 LEU A CG  
1345 C CD1 . LEU A 183 ? 0.2230 0.1895 0.1880 0.0020  -0.0138 -0.0073 177 LEU A CD1 
1346 C CD2 . LEU A 183 ? 0.2471 0.2114 0.2206 0.0009  -0.0120 -0.0079 177 LEU A CD2 
1347 N N   . ALA A 184 ? 0.2422 0.1991 0.1984 -0.0024 -0.0200 -0.0266 178 ALA A N   
1348 C CA  . ALA A 184 ? 0.2503 0.2091 0.2123 -0.0074 -0.0256 -0.0320 178 ALA A CA  
1349 C C   . ALA A 184 ? 0.2703 0.2363 0.2233 -0.0058 -0.0322 -0.0369 178 ALA A C   
1350 O O   . ALA A 184 ? 0.2663 0.2412 0.2270 -0.0091 -0.0384 -0.0393 178 ALA A O   
1351 C CB  . ALA A 184 ? 0.2477 0.1948 0.2132 -0.0106 -0.0246 -0.0382 178 ALA A CB  
1352 N N   . LYS A 185 ? 0.2366 0.2005 0.1737 -0.0001 -0.0308 -0.0380 179 LYS A N   
1353 C CA  . LYS A 185 ? 0.2384 0.2095 0.1626 0.0037  -0.0371 -0.0412 179 LYS A CA  
1354 C C   . LYS A 185 ? 0.2536 0.2350 0.1810 0.0059  -0.0399 -0.0335 179 LYS A C   
1355 O O   . LYS A 185 ? 0.2781 0.2696 0.2043 0.0071  -0.0483 -0.0365 179 LYS A O   
1356 C CB  . LYS A 185 ? 0.2704 0.2369 0.1750 0.0107  -0.0321 -0.0409 179 LYS A CB  
1357 C CG  . LYS A 185 ? 0.2784 0.2516 0.1638 0.0170  -0.0378 -0.0427 179 LYS A CG  
1358 C CD  . LYS A 185 ? 0.3005 0.2688 0.1655 0.0244  -0.0300 -0.0411 179 LYS A CD  
1359 C CE  . LYS A 185 ? 0.3505 0.3253 0.1926 0.0323  -0.0352 -0.0415 179 LYS A CE  
1360 N NZ  . LYS A 185 ? 0.3759 0.3463 0.1957 0.0400  -0.0263 -0.0409 179 LYS A NZ  
1361 N N   . TYR A 186 ? 0.2349 0.2142 0.1672 0.0071  -0.0338 -0.0244 180 TYR A N   
1362 C CA  . TYR A 186 ? 0.2373 0.2225 0.1700 0.0111  -0.0352 -0.0173 180 TYR A CA  
1363 C C   . TYR A 186 ? 0.2356 0.2261 0.1850 0.0081  -0.0359 -0.0153 180 TYR A C   
1364 O O   . TYR A 186 ? 0.2506 0.2479 0.2020 0.0122  -0.0387 -0.0116 180 TYR A O   
1365 C CB  . TYR A 186 ? 0.2625 0.2403 0.1871 0.0152  -0.0278 -0.0090 180 TYR A CB  
1366 C CG  . TYR A 186 ? 0.2930 0.2683 0.1992 0.0201  -0.0257 -0.0085 180 TYR A CG  
1367 C CD1 . TYR A 186 ? 0.2812 0.2625 0.1737 0.0260  -0.0320 -0.0087 180 TYR A CD1 
1368 C CD2 . TYR A 186 ? 0.2727 0.2415 0.1746 0.0198  -0.0174 -0.0076 180 TYR A CD2 
1369 C CE1 . TYR A 186 ? 0.2888 0.2683 0.1604 0.0321  -0.0298 -0.0078 180 TYR A CE1 
1370 C CE2 . TYR A 186 ? 0.2873 0.2550 0.1707 0.0254  -0.0138 -0.0066 180 TYR A CE2 
1371 C CZ  . TYR A 186 ? 0.2991 0.2714 0.1658 0.0317  -0.0199 -0.0066 180 TYR A CZ  
1372 O OH  . TYR A 186 ? 0.3298 0.3016 0.1739 0.0388  -0.0164 -0.0053 180 TYR A OH  
1373 N N   . SER A 187 ? 0.2101 0.1976 0.1702 0.0026  -0.0328 -0.0168 181 SER A N   
1374 C CA  . SER A 187 ? 0.2244 0.2176 0.1978 0.0010  -0.0319 -0.0142 181 SER A CA  
1375 C C   . SER A 187 ? 0.1948 0.2002 0.1803 -0.0028 -0.0373 -0.0182 181 SER A C   
1376 O O   . SER A 187 ? 0.2187 0.2239 0.2062 -0.0076 -0.0408 -0.0246 181 SER A O   
1377 C CB  . SER A 187 ? 0.2051 0.1914 0.1833 -0.0022 -0.0262 -0.0128 181 SER A CB  
1378 O OG  . SER A 187 ? 0.2205 0.2123 0.2072 -0.0020 -0.0242 -0.0096 181 SER A OG  
1379 N N   . LYS A 188 ? 0.1854 0.2017 0.1805 -0.0005 -0.0377 -0.0150 182 LYS A N   
1380 C CA  . LYS A 188 ? 0.2163 0.2471 0.2290 -0.0053 -0.0407 -0.0176 182 LYS A CA  
1381 C C   . LYS A 188 ? 0.2297 0.2564 0.2530 -0.0126 -0.0342 -0.0166 182 LYS A C   
1382 O O   . LYS A 188 ? 0.2343 0.2697 0.2738 -0.0195 -0.0354 -0.0190 182 LYS A O   
1383 C CB  . LYS A 188 ? 0.2153 0.2605 0.2363 0.0008  -0.0414 -0.0136 182 LYS A CB  
1384 C CG  . LYS A 188 ? 0.2492 0.3004 0.2620 0.0093  -0.0485 -0.0131 182 LYS A CG  
1385 C CD  . LYS A 188 ? 0.2773 0.3462 0.2994 0.0072  -0.0586 -0.0190 182 LYS A CD  
1386 C CE  . LYS A 188 ? 0.2417 0.3324 0.2880 0.0064  -0.0594 -0.0184 182 LYS A CE  
1387 N NZ  . LYS A 188 ? 0.2562 0.3679 0.3141 0.0046  -0.0713 -0.0250 182 LYS A NZ  
1388 N N   . PHE A 189 ? 0.1990 0.2133 0.2144 -0.0110 -0.0276 -0.0125 183 PHE A N   
1389 C CA  . PHE A 189 ? 0.1863 0.1962 0.2084 -0.0154 -0.0210 -0.0092 183 PHE A CA  
1390 C C   . PHE A 189 ? 0.2219 0.2186 0.2415 -0.0204 -0.0210 -0.0126 183 PHE A C   
1391 O O   . PHE A 189 ? 0.2237 0.2130 0.2323 -0.0184 -0.0242 -0.0167 183 PHE A O   
1392 C CB  . PHE A 189 ? 0.2058 0.2107 0.2192 -0.0097 -0.0154 -0.0039 183 PHE A CB  
1393 C CG  . PHE A 189 ? 0.2075 0.2218 0.2214 -0.0035 -0.0150 -0.0022 183 PHE A CG  
1394 C CD1 . PHE A 189 ? 0.2410 0.2691 0.2675 -0.0036 -0.0120 0.0001  183 PHE A CD1 
1395 C CD2 . PHE A 189 ? 0.2321 0.2412 0.2353 0.0024  -0.0171 -0.0029 183 PHE A CD2 
1396 C CE1 . PHE A 189 ? 0.2303 0.2668 0.2574 0.0038  -0.0112 0.0010  183 PHE A CE1 
1397 C CE2 . PHE A 189 ? 0.2356 0.2500 0.2392 0.0090  -0.0166 -0.0018 183 PHE A CE2 
1398 C CZ  . PHE A 189 ? 0.2183 0.2466 0.2333 0.0105  -0.0138 -0.0003 183 PHE A CZ  
1399 N N   . LYS A 190 ? 0.2172 0.2102 0.2470 -0.0263 -0.0165 -0.0104 184 LYS A N   
1400 C CA  . LYS A 190 ? 0.2227 0.1999 0.2509 -0.0301 -0.0158 -0.0134 184 LYS A CA  
1401 C C   . LYS A 190 ? 0.2516 0.2172 0.2660 -0.0235 -0.0121 -0.0095 184 LYS A C   
1402 O O   . LYS A 190 ? 0.2482 0.2161 0.2593 -0.0192 -0.0080 -0.0026 184 LYS A O   
1403 C CB  . LYS A 190 ? 0.2359 0.2096 0.2800 -0.0383 -0.0108 -0.0104 184 LYS A CB  
1404 C CG  . LYS A 190 ? 0.2738 0.2279 0.3180 -0.0424 -0.0102 -0.0145 184 LYS A CG  
1405 C CD  . LYS A 190 ? 0.3127 0.2660 0.3589 -0.0473 -0.0189 -0.0277 184 LYS A CD  
1406 C CE  . LYS A 190 ? 0.3911 0.3566 0.4590 -0.0579 -0.0222 -0.0317 184 LYS A CE  
1407 N NZ  . LYS A 190 ? 0.6086 0.5765 0.6766 -0.0617 -0.0333 -0.0464 184 LYS A NZ  
1408 N N   . VAL A 191 ? 0.2081 0.1630 0.2149 -0.0222 -0.0139 -0.0146 185 VAL A N   
1409 C CA  . VAL A 191 ? 0.2549 0.2021 0.2518 -0.0157 -0.0112 -0.0120 185 VAL A CA  
1410 C C   . VAL A 191 ? 0.2405 0.1725 0.2399 -0.0164 -0.0074 -0.0110 185 VAL A C   
1411 O O   . VAL A 191 ? 0.2785 0.2014 0.2819 -0.0212 -0.0086 -0.0174 185 VAL A O   
1412 C CB  . VAL A 191 ? 0.2504 0.1985 0.2371 -0.0118 -0.0141 -0.0172 185 VAL A CB  
1413 C CG1 . VAL A 191 ? 0.2623 0.2054 0.2437 -0.0060 -0.0108 -0.0146 185 VAL A CG1 
1414 C CG2 . VAL A 191 ? 0.2213 0.1813 0.2051 -0.0100 -0.0169 -0.0159 185 VAL A CG2 
1415 N N   . PHE A 192 ? 0.2390 0.1676 0.2357 -0.0112 -0.0033 -0.0033 186 PHE A N   
1416 C CA  . PHE A 192 ? 0.3012 0.2147 0.2991 -0.0092 0.0009  0.0005  186 PHE A CA  
1417 C C   . PHE A 192 ? 0.2740 0.1858 0.2647 -0.0003 0.0009  0.0007  186 PHE A C   
1418 O O   . PHE A 192 ? 0.2582 0.1820 0.2448 0.0037  -0.0011 0.0020  186 PHE A O   
1419 C CB  . PHE A 192 ? 0.2624 0.1753 0.2631 -0.0089 0.0061  0.0116  186 PHE A CB  
1420 C CG  . PHE A 192 ? 0.2445 0.1601 0.2565 -0.0181 0.0084  0.0128  186 PHE A CG  
1421 C CD1 . PHE A 192 ? 0.2621 0.1632 0.2838 -0.0240 0.0133  0.0159  186 PHE A CD1 
1422 C CD2 . PHE A 192 ? 0.2404 0.1731 0.2553 -0.0208 0.0060  0.0112  186 PHE A CD2 
1423 C CE1 . PHE A 192 ? 0.3587 0.2646 0.3953 -0.0339 0.0160  0.0172  186 PHE A CE1 
1424 C CE2 . PHE A 192 ? 0.2542 0.1930 0.2830 -0.0288 0.0084  0.0125  186 PHE A CE2 
1425 C CZ  . PHE A 192 ? 0.2924 0.2192 0.3331 -0.0361 0.0134  0.0154  186 PHE A CZ  
1426 N N   . THR A 193 ? 0.2387 0.1358 0.2296 0.0029  0.0032  -0.0008 187 THR A N   
1427 C CA  . THR A 193 ? 0.2800 0.1783 0.2671 0.0122  0.0037  -0.0006 187 THR A CA  
1428 C C   . THR A 193 ? 0.3057 0.1866 0.2945 0.0180  0.0078  0.0035  187 THR A C   
1429 O O   . THR A 193 ? 0.2956 0.1617 0.2881 0.0139  0.0108  0.0066  187 THR A O   
1430 C CB  . THR A 193 ? 0.2596 0.1620 0.2430 0.0129  0.0022  -0.0102 187 THR A CB  
1431 O OG1 . THR A 193 ? 0.2493 0.1601 0.2325 0.0211  0.0032  -0.0083 187 THR A OG1 
1432 C CG2 . THR A 193 ? 0.2545 0.1403 0.2367 0.0114  0.0034  -0.0191 187 THR A CG2 
1433 N N   . CYS A 194 ? 0.2994 0.1827 0.2870 0.0280  0.0084  0.0043  188 CYS A N   
1434 C CA  . CYS A 194 ? 0.2918 0.1592 0.2807 0.0368  0.0122  0.0084  188 CYS A CA  
1435 C C   . CYS A 194 ? 0.2722 0.1426 0.2615 0.0449  0.0132  0.0016  188 CYS A C   
1436 O O   . CYS A 194 ? 0.2980 0.1863 0.2872 0.0446  0.0113  -0.0026 188 CYS A O   
1437 C CB  . CYS A 194 ? 0.2761 0.1478 0.2641 0.0449  0.0122  0.0217  188 CYS A CB  
1438 S SG  . CYS A 194 ? 0.2968 0.1975 0.2851 0.0525  0.0064  0.0231  188 CYS A SG  
1439 N N   . ALA A 195 ? 0.2897 0.1417 0.2800 0.0524  0.0173  0.0009  189 ALA A N   
1440 C CA  . ALA A 195 ? 0.3022 0.1562 0.2933 0.0622  0.0199  -0.0055 189 ALA A CA  
1441 C C   . ALA A 195 ? 0.3203 0.1873 0.3173 0.0752  0.0196  0.0039  189 ALA A C   
1442 O O   . ALA A 195 ? 0.3678 0.2214 0.3661 0.0837  0.0214  0.0118  189 ALA A O   
1443 C CB  . ALA A 195 ? 0.3358 0.1618 0.3248 0.0647  0.0244  -0.0132 189 ALA A CB  
1444 N N   . CYS A 196 ? 0.2870 0.1806 0.2887 0.0766  0.0171  0.0034  190 CYS A N   
1445 C CA  . CYS A 196 ? 0.2736 0.1832 0.2840 0.0890  0.0155  0.0104  190 CYS A CA  
1446 C C   . CYS A 196 ? 0.2941 0.2023 0.3106 0.1015  0.0211  0.0063  190 CYS A C   
1447 O O   . CYS A 196 ? 0.3260 0.2406 0.3503 0.1148  0.0206  0.0127  190 CYS A O   
1448 C CB  . CYS A 196 ? 0.2883 0.2279 0.3055 0.0850  0.0100  0.0109  190 CYS A CB  
1449 S SG  . CYS A 196 ? 0.2783 0.2216 0.2879 0.0725  0.0037  0.0143  190 CYS A SG  
1450 N N   . VAL A 197 ? 0.3424 0.2436 0.3549 0.0985  0.0264  -0.0042 191 VAL A N   
1451 C CA  . VAL A 197 ? 0.3790 0.2776 0.3946 0.1104  0.0335  -0.0101 191 VAL A CA  
1452 C C   . VAL A 197 ? 0.4296 0.2941 0.4340 0.1103  0.0376  -0.0180 191 VAL A C   
1453 O O   . VAL A 197 ? 0.4420 0.2966 0.4363 0.0984  0.0365  -0.0258 191 VAL A O   
1454 C CB  . VAL A 197 ? 0.3143 0.2350 0.3325 0.1078  0.0374  -0.0165 191 VAL A CB  
1455 C CG1 . VAL A 197 ? 0.3880 0.3078 0.4089 0.1216  0.0464  -0.0225 191 VAL A CG1 
1456 C CG2 . VAL A 197 ? 0.3114 0.2638 0.3436 0.1052  0.0329  -0.0097 191 VAL A CG2 
1457 N N   . GLY A 198 ? 0.4477 0.2938 0.4544 0.1234  0.0414  -0.0164 192 GLY A N   
1458 C CA  . GLY A 198 ? 0.5089 0.3196 0.5064 0.1223  0.0450  -0.0254 192 GLY A CA  
1459 C C   . GLY A 198 ? 0.5985 0.3892 0.5926 0.1096  0.0408  -0.0208 192 GLY A C   
1460 O O   . GLY A 198 ? 0.6673 0.4665 0.6653 0.1074  0.0370  -0.0077 192 GLY A O   
1461 N N   . ASP A 199 ? 0.5172 0.2823 0.5043 0.1010  0.0417  -0.0321 193 ASP A N   
1462 C CA  . ASP A 199 ? 0.4420 0.1892 0.4295 0.0870  0.0388  -0.0288 193 ASP A CA  
1463 C C   . ASP A 199 ? 0.4705 0.2261 0.4526 0.0706  0.0338  -0.0395 193 ASP A C   
1464 O O   . ASP A 199 ? 0.4828 0.2567 0.4586 0.0706  0.0326  -0.0479 193 ASP A O   
1465 C CB  . ASP A 199 ? 0.4789 0.1867 0.4680 0.0896  0.0432  -0.0312 193 ASP A CB  
1466 C CG  . ASP A 199 ? 0.5427 0.2382 0.5269 0.0902  0.0434  -0.0507 193 ASP A CG  
1467 O OD1 . ASP A 199 ? 0.5305 0.2379 0.5054 0.0893  0.0432  -0.0630 193 ASP A OD1 
1468 O OD2 . ASP A 199 ? 0.6031 0.2764 0.5915 0.0926  0.0438  -0.0534 193 ASP A OD2 
1469 N N   . ILE A 200 ? 0.4393 0.2122 0.4990 0.1030  0.0453  0.0299  194 ILE A N   
1470 C CA  . ILE A 200 ? 0.3903 0.1652 0.4460 0.0704  0.0346  0.0073  194 ILE A CA  
1471 C C   . ILE A 200 ? 0.4316 0.1767 0.4705 0.0646  0.0430  -0.0194 194 ILE A C   
1472 O O   . ILE A 200 ? 0.4073 0.1783 0.4426 0.0502  0.0316  -0.0349 194 ILE A O   
1473 C CB  . ILE A 200 ? 0.4629 0.2133 0.5152 0.0480  0.0332  0.0079  194 ILE A CB  
1474 C CG1 . ILE A 200 ? 0.4402 0.2272 0.5006 0.0510  0.0221  0.0307  194 ILE A CG1 
1475 C CG2 . ILE A 200 ? 0.3959 0.1542 0.4475 0.0171  0.0228  -0.0165 194 ILE A CG2 
1476 C CD1 . ILE A 200 ? 0.5063 0.2699 0.5625 0.0340  0.0265  0.0363  194 ILE A CD1 
1477 N N   . LYS A 201 ? 0.5064 0.2090 0.5266 0.0734  0.0575  -0.0244 195 LYS A N   
1478 C CA  . LYS A 201 ? 0.5559 0.2346 0.5532 0.0681  0.0635  -0.0501 195 LYS A CA  
1479 C C   . LYS A 201 ? 0.5468 0.2570 0.5478 0.0866  0.0673  -0.0514 195 LYS A C   
1480 O O   . LYS A 201 ? 0.4982 0.2104 0.4820 0.0743  0.0630  -0.0722 195 LYS A O   
1481 C CB  . LYS A 201 ? 0.5646 0.1931 0.5425 0.0780  0.0814  -0.0522 195 LYS A CB  
1482 N N   . TYR A 202 ? 0.5453 0.2874 0.5690 0.1160  0.0750  -0.0280 196 TYR A N   
1483 C CA  . TYR A 202 ? 0.5145 0.2978 0.5502 0.1329  0.0818  -0.0256 196 TYR A CA  
1484 C C   . TYR A 202 ? 0.4469 0.2803 0.4899 0.1068  0.0597  -0.0288 196 TYR A C   
1485 O O   . TYR A 202 ? 0.4349 0.2834 0.4669 0.1031  0.0624  -0.0392 196 TYR A O   
1486 C CB  . TYR A 202 ? 0.4889 0.3187 0.5576 0.1634  0.0874  0.0027  196 TYR A CB  
1487 C CG  . TYR A 202 ? 0.5188 0.4114 0.6129 0.1754  0.0931  0.0088  196 TYR A CG  
1488 C CD1 . TYR A 202 ? 0.5377 0.5040 0.6642 0.1621  0.0740  0.0228  196 TYR A CD1 
1489 C CD2 . TYR A 202 ? 0.6546 0.5370 0.7348 0.1885  0.1140  -0.0020 196 TYR A CD2 
1490 C CE1 . TYR A 202 ? 0.5393 0.5662 0.6907 0.1632  0.0796  0.0269  196 TYR A CE1 
1491 C CE2 . TYR A 202 ? 0.6733 0.6157 0.7791 0.1972  0.1236  0.0047  196 TYR A CE2 
1492 C CZ  . TYR A 202 ? 0.6232 0.6400 0.7674 0.1821  0.1060  0.0193  196 TYR A CZ  
1493 O OH  . TYR A 202 ? 0.7220 0.8008 0.8935 0.1815  0.1160  0.0248  196 TYR A OH  
1494 N N   . LEU A 203 ? 0.3466 0.1993 0.4024 0.0904  0.0411  -0.0192 197 LEU A N   
1495 C CA  . LEU A 203 ? 0.3224 0.2125 0.3805 0.0692  0.0239  -0.0206 197 LEU A CA  
1496 C C   . LEU A 203 ? 0.3335 0.2016 0.3637 0.0517  0.0184  -0.0426 197 LEU A C   
1497 O O   . LEU A 203 ? 0.3434 0.2299 0.3624 0.0470  0.0161  -0.0470 197 LEU A O   
1498 C CB  . LEU A 203 ? 0.3105 0.2168 0.3816 0.0592  0.0093  -0.0064 197 LEU A CB  
1499 C CG  . LEU A 203 ? 0.2598 0.1916 0.3276 0.0392  -0.0052 -0.0070 197 LEU A CG  
1500 C CD1 . LEU A 203 ? 0.2470 0.2171 0.3222 0.0379  -0.0041 -0.0029 197 LEU A CD1 
1501 C CD2 . LEU A 203 ? 0.2432 0.1809 0.3169 0.0336  -0.0147 0.0064  197 LEU A CD2 
1502 N N   . LYS A 204 ? 0.3690 0.1987 0.3865 0.0417  0.0170  -0.0562 198 LYS A N   
1503 C CA  . LYS A 204 ? 0.3649 0.1834 0.3572 0.0257  0.0085  -0.0787 198 LYS A CA  
1504 C C   . LYS A 204 ? 0.4090 0.2152 0.3726 0.0366  0.0196  -0.0921 198 LYS A C   
1505 O O   . LYS A 204 ? 0.4234 0.2431 0.3647 0.0313  0.0112  -0.1008 198 LYS A O   
1506 C CB  . LYS A 204 ? 0.4078 0.1903 0.3958 0.0083  0.0069  -0.0936 198 LYS A CB  
1507 C CG  . LYS A 204 ? 0.4077 0.2077 0.4202 -0.0073 -0.0039 -0.0830 198 LYS A CG  
1508 C CD  . LYS A 204 ? 0.5966 0.3610 0.6084 -0.0292 -0.0006 -0.0976 198 LYS A CD  
1509 C CE  . LYS A 204 ? 0.5578 0.3406 0.5954 -0.0430 -0.0052 -0.0840 198 LYS A CE  
1510 N NZ  . LYS A 204 ? 0.6530 0.4087 0.6861 -0.0638 0.0008  -0.0886 198 LYS A NZ  
1511 N N   . LYS A 205 ? 0.4624 0.2417 0.4226 0.0558  0.0408  -0.0919 199 LYS A N   
1512 C CA  . LYS A 205 ? 0.5224 0.2871 0.4522 0.0693  0.0570  -0.1042 199 LYS A CA  
1513 C C   . LYS A 205 ? 0.5176 0.3292 0.4534 0.0747  0.0578  -0.0916 199 LYS A C   
1514 O O   . LYS A 205 ? 0.4801 0.2874 0.3809 0.0738  0.0604  -0.1030 199 LYS A O   
1515 C CB  . LYS A 205 ? 0.5831 0.3155 0.5145 0.0949  0.0835  -0.1009 199 LYS A CB  
1516 C CG  . LYS A 205 ? 0.6743 0.4020 0.5808 0.1104  0.1021  -0.1090 199 LYS A CG  
1517 C CD  . LYS A 205 ? 0.7302 0.4460 0.6502 0.1364  0.1237  -0.0973 199 LYS A CD  
1518 C CE  . LYS A 205 ? 0.7882 0.5153 0.6965 0.1568  0.1466  -0.0975 199 LYS A CE  
1519 N NZ  . LYS A 205 ? 0.8588 0.5949 0.7933 0.1874  0.1672  -0.0782 199 LYS A NZ  
1520 N N   . GLN A 206 ? 0.4324 0.2870 0.4081 0.0782  0.0563  -0.0684 200 GLN A N   
1521 C CA  . GLN A 206 ? 0.3960 0.2907 0.3783 0.0753  0.0589  -0.0577 200 GLN A CA  
1522 C C   . GLN A 206 ? 0.3562 0.2488 0.3113 0.0577  0.0429  -0.0635 200 GLN A C   
1523 O O   . GLN A 206 ? 0.3527 0.2472 0.2822 0.0583  0.0508  -0.0643 200 GLN A O   
1524 C CB  . GLN A 206 ? 0.3687 0.3104 0.3968 0.0740  0.0550  -0.0359 200 GLN A CB  
1525 C CG  . GLN A 206 ? 0.4148 0.3723 0.4755 0.0968  0.0669  -0.0238 200 GLN A CG  
1526 C CD  . GLN A 206 ? 0.5895 0.5416 0.6441 0.1202  0.0944  -0.0277 200 GLN A CD  
1527 O OE1 . GLN A 206 ? 0.6466 0.6390 0.7163 0.1220  0.1075  -0.0207 200 GLN A OE1 
1528 N NE2 . GLN A 206 ? 0.6206 0.5188 0.6507 0.1370  0.1066  -0.0396 200 GLN A NE2 
1529 N N   . ILE A 207 ? 0.3450 0.2346 0.3052 0.0449  0.0228  -0.0646 201 ILE A N   
1530 C CA  . ILE A 207 ? 0.3459 0.2392 0.2845 0.0349  0.0086  -0.0663 201 ILE A CA  
1531 C C   . ILE A 207 ? 0.3930 0.2673 0.2879 0.0383  0.0066  -0.0838 201 ILE A C   
1532 O O   . ILE A 207 ? 0.4134 0.2908 0.2783 0.0412  0.0056  -0.0809 201 ILE A O   
1533 C CB  . ILE A 207 ? 0.3195 0.2186 0.2766 0.0239  -0.0091 -0.0637 201 ILE A CB  
1534 C CG1 . ILE A 207 ? 0.2867 0.2043 0.2731 0.0204  -0.0083 -0.0461 201 ILE A CG1 
1535 C CG2 . ILE A 207 ? 0.2913 0.1968 0.2266 0.0205  -0.0231 -0.0664 201 ILE A CG2 
1536 C CD1 . ILE A 207 ? 0.2638 0.1820 0.2681 0.0128  -0.0194 -0.0424 201 ILE A CD1 
1537 N N   . LEU A 208 ? 0.4011 0.2509 0.2856 0.0377  0.0067  -0.1024 202 LEU A N   
1538 C CA  . LEU A 208 ? 0.4256 0.2567 0.2618 0.0379  0.0028  -0.1235 202 LEU A CA  
1539 C C   . LEU A 208 ? 0.5537 0.3734 0.3561 0.0540  0.0250  -0.1230 202 LEU A C   
1540 O O   . LEU A 208 ? 0.5772 0.3881 0.3299 0.0571  0.0214  -0.1338 202 LEU A O   
1541 C CB  . LEU A 208 ? 0.4697 0.2682 0.2993 0.0276  0.0005  -0.1471 202 LEU A CB  
1542 C CG  . LEU A 208 ? 0.5549 0.3688 0.4058 0.0057  -0.0236 -0.1532 202 LEU A CG  
1543 C CD1 . LEU A 208 ? 0.6188 0.3950 0.4707 -0.0107 -0.0188 -0.1734 202 LEU A CD1 
1544 C CD2 . LEU A 208 ? 0.5956 0.4396 0.4203 0.0005  -0.0472 -0.1610 202 LEU A CD2 
1545 N N   . THR A 209 ? 0.5251 0.3494 0.3533 0.0652  0.0485  -0.1099 203 THR A N   
1546 C CA  . THR A 209 ? 0.5490 0.3721 0.3527 0.0791  0.0736  -0.1056 203 THR A CA  
1547 C C   . THR A 209 ? 0.5734 0.4164 0.3661 0.0746  0.0720  -0.0892 203 THR A C   
1548 O O   . THR A 209 ? 0.6558 0.4859 0.4006 0.0820  0.0830  -0.0906 203 THR A O   
1549 C CB  . THR A 209 ? 0.6388 0.4763 0.4834 0.0928  0.0992  -0.0938 203 THR A CB  
1550 O OG1 . THR A 209 ? 0.6662 0.4693 0.5063 0.1042  0.1078  -0.1084 203 THR A OG1 
1551 C CG2 . THR A 209 ? 0.6680 0.5158 0.4974 0.1044  0.1284  -0.0863 203 THR A CG2 
1552 N N   . LEU A 210 ? 0.4702 0.3370 0.3000 0.0632  0.0608  -0.0736 204 LEU A N   
1553 C CA  . LEU A 210 ? 0.5037 0.3757 0.3188 0.0575  0.0610  -0.0587 204 LEU A CA  
1554 C C   . LEU A 210 ? 0.5924 0.4480 0.3562 0.0631  0.0446  -0.0644 204 LEU A C   
1555 O O   . LEU A 210 ? 0.5688 0.4110 0.2888 0.0709  0.0555  -0.0563 204 LEU A O   
1556 C CB  . LEU A 210 ? 0.4648 0.3561 0.3224 0.0436  0.0504  -0.0463 204 LEU A CB  
1557 C CG  . LEU A 210 ? 0.4614 0.3461 0.3039 0.0354  0.0513  -0.0322 204 LEU A CG  
1558 C CD1 . LEU A 210 ? 0.6852 0.5693 0.5216 0.0290  0.0791  -0.0215 204 LEU A CD1 
1559 C CD2 . LEU A 210 ? 0.4730 0.3696 0.3496 0.0226  0.0377  -0.0267 204 LEU A CD2 
1560 N N   . ASP A 211 ? 0.5302 0.3907 0.2998 0.0597  0.0188  -0.0764 205 ASP A N   
1561 C CA  . ASP A 211 ? 0.5265 0.3899 0.2586 0.0653  -0.0027 -0.0811 205 ASP A CA  
1562 C C   . ASP A 211 ? 0.5155 0.3802 0.2444 0.0579  -0.0211 -0.1070 205 ASP A C   
1563 O O   . ASP A 211 ? 0.5088 0.3876 0.2764 0.0450  -0.0364 -0.1126 205 ASP A O   
1564 C CB  . ASP A 211 ? 0.5094 0.3893 0.2614 0.0642  -0.0164 -0.0657 205 ASP A CB  
1565 C CG  . ASP A 211 ? 0.6308 0.5296 0.3577 0.0737  -0.0418 -0.0691 205 ASP A CG  
1566 O OD1 . ASP A 211 ? 0.6799 0.5773 0.3615 0.0820  -0.0490 -0.0799 205 ASP A OD1 
1567 O OD2 . ASP A 211 ? 0.5942 0.5138 0.3467 0.0742  -0.0547 -0.0606 205 ASP A OD2 
1568 N N   . PRO A 212 ? 0.5341 0.3801 0.2141 0.0633  -0.0176 -0.1243 206 PRO A N   
1569 C CA  . PRO A 212 ? 0.5794 0.4243 0.2608 0.0471  -0.0313 -0.1495 206 PRO A CA  
1570 C C   . PRO A 212 ? 0.5689 0.4500 0.2629 0.0337  -0.0638 -0.1551 206 PRO A C   
1571 O O   . PRO A 212 ? 0.6070 0.4889 0.3151 0.0116  -0.0736 -0.1750 206 PRO A O   
1572 C CB  . PRO A 212 ? 0.6494 0.4781 0.2813 0.0530  -0.0188 -0.1585 206 PRO A CB  
1573 C CG  . PRO A 212 ? 0.6787 0.4931 0.3016 0.0711  0.0110  -0.1390 206 PRO A CG  
1574 C CD  . PRO A 212 ? 0.5874 0.4169 0.2290 0.0762  0.0072  -0.1161 206 PRO A CD  
1575 N N   . SER A 213 ? 0.5645 0.4755 0.2545 0.0461  -0.0775 -0.1367 207 SER A N   
1576 C CA  . SER A 213 ? 0.5921 0.5497 0.3026 0.0384  -0.1063 -0.1370 207 SER A CA  
1577 C C   . SER A 213 ? 0.5677 0.5450 0.3299 0.0364  -0.1123 -0.1269 207 SER A C   
1578 O O   . SER A 213 ? 0.5982 0.6205 0.3835 0.0368  -0.1311 -0.1198 207 SER A O   
1579 C CB  . SER A 213 ? 0.7227 0.7036 0.3986 0.0594  -0.1159 -0.1200 207 SER A CB  
1580 O OG  . SER A 213 ? 0.8415 0.8091 0.5116 0.0826  -0.1010 -0.0935 207 SER A OG  
1581 N N   . TYR A 214 ? 0.4685 0.4176 0.2567 0.0333  -0.0923 -0.1208 208 TYR A N   
1582 C CA  . TYR A 214 ? 0.4209 0.3858 0.2574 0.0307  -0.0911 -0.1036 208 TYR A CA  
1583 C C   . TYR A 214 ? 0.4851 0.4819 0.3610 0.0113  -0.1094 -0.1157 208 TYR A C   
1584 O O   . TYR A 214 ? 0.5327 0.5187 0.4134 -0.0093 -0.1129 -0.1382 208 TYR A O   
1585 C CB  . TYR A 214 ? 0.3606 0.2964 0.2204 0.0269  -0.0679 -0.0945 208 TYR A CB  
1586 C CG  . TYR A 214 ? 0.3696 0.3173 0.2639 0.0263  -0.0662 -0.0762 208 TYR A CG  
1587 C CD1 . TYR A 214 ? 0.3195 0.2724 0.2540 0.0122  -0.0678 -0.0778 208 TYR A CD1 
1588 C CD2 . TYR A 214 ? 0.3524 0.2990 0.2312 0.0401  -0.0606 -0.0576 208 TYR A CD2 
1589 C CE1 . TYR A 214 ? 0.2912 0.2526 0.2484 0.0128  -0.0651 -0.0621 208 TYR A CE1 
1590 C CE2 . TYR A 214 ? 0.3290 0.2785 0.2294 0.0395  -0.0571 -0.0440 208 TYR A CE2 
1591 C CZ  . TYR A 214 ? 0.2880 0.2471 0.2268 0.0263  -0.0600 -0.0467 208 TYR A CZ  
1592 O OH  . TYR A 214 ? 0.2772 0.2364 0.2296 0.0270  -0.0551 -0.0339 208 TYR A OH  
1593 N N   . ASP A 215 ? 0.5111 0.5438 0.4133 0.0179  -0.1177 -0.1004 209 ASP A N   
1594 C CA  . ASP A 215 ? 0.5378 0.6113 0.4860 0.0008  -0.1310 -0.1062 209 ASP A CA  
1595 C C   . ASP A 215 ? 0.4843 0.5402 0.4684 -0.0046 -0.1133 -0.0925 209 ASP A C   
1596 O O   . ASP A 215 ? 0.4621 0.5177 0.4478 0.0124  -0.1046 -0.0718 209 ASP A O   
1597 C CB  . ASP A 215 ? 0.6214 0.7542 0.5740 0.0186  -0.1497 -0.0956 209 ASP A CB  
1598 C CG  . ASP A 215 ? 0.6596 0.8456 0.6673 0.0010  -0.1595 -0.0977 209 ASP A CG  
1599 O OD1 . ASP A 215 ? 0.6572 0.8302 0.6966 -0.0264 -0.1523 -0.1084 209 ASP A OD1 
1600 O OD2 . ASP A 215 ? 0.6576 0.8947 0.6764 0.0154  -0.1700 -0.0849 209 ASP A OD2 
1601 N N   . PHE A 216 ? 0.3520 0.3878 0.3583 -0.0276 -0.1068 -0.1040 210 PHE A N   
1602 C CA  . PHE A 216 ? 0.3142 0.3326 0.3485 -0.0320 -0.0911 -0.0904 210 PHE A CA  
1603 C C   . PHE A 216 ? 0.2951 0.3542 0.3677 -0.0378 -0.0944 -0.0820 210 PHE A C   
1604 O O   . PHE A 216 ? 0.3682 0.4126 0.4615 -0.0451 -0.0811 -0.0730 210 PHE A O   
1605 C CB  . PHE A 216 ? 0.3532 0.3300 0.3922 -0.0493 -0.0799 -0.1017 210 PHE A CB  
1606 C CG  . PHE A 216 ? 0.3618 0.2990 0.3703 -0.0379 -0.0693 -0.1047 210 PHE A CG  
1607 C CD1 . PHE A 216 ? 0.3156 0.2381 0.3239 -0.0232 -0.0560 -0.0866 210 PHE A CD1 
1608 C CD2 . PHE A 216 ? 0.4590 0.3777 0.4390 -0.0427 -0.0720 -0.1266 210 PHE A CD2 
1609 C CE1 . PHE A 216 ? 0.4007 0.2994 0.3902 -0.0120 -0.0446 -0.0875 210 PHE A CE1 
1610 C CE2 . PHE A 216 ? 0.5169 0.4015 0.4704 -0.0287 -0.0574 -0.1279 210 PHE A CE2 
1611 C CZ  . PHE A 216 ? 0.4366 0.3157 0.3996 -0.0126 -0.0432 -0.1069 210 PHE A CZ  
1612 N N   . SER A 217 ? 0.2726 0.3850 0.3541 -0.0312 -0.1102 -0.0823 211 SER A N   
1613 C CA  . SER A 217 ? 0.2681 0.4302 0.3946 -0.0374 -0.1116 -0.0757 211 SER A CA  
1614 C C   . SER A 217 ? 0.2492 0.3981 0.3808 -0.0201 -0.0927 -0.0524 211 SER A C   
1615 O O   . SER A 217 ? 0.2770 0.4491 0.4443 -0.0288 -0.0842 -0.0462 211 SER A O   
1616 C CB  . SER A 217 ? 0.3879 0.6213 0.5246 -0.0264 -0.1336 -0.0774 211 SER A CB  
1617 O OG  . SER A 217 ? 0.4563 0.6816 0.5532 0.0094  -0.1350 -0.0629 211 SER A OG  
1618 N N   . ASN A 218 ? 0.2259 0.3364 0.3202 0.0013  -0.0841 -0.0408 212 ASN A N   
1619 C CA  . ASN A 218 ? 0.1994 0.2914 0.2878 0.0155  -0.0671 -0.0227 212 ASN A CA  
1620 C C   . ASN A 218 ? 0.2234 0.2630 0.2932 0.0074  -0.0549 -0.0201 212 ASN A C   
1621 O O   . ASN A 218 ? 0.2089 0.2248 0.2597 0.0168  -0.0433 -0.0087 212 ASN A O   
1622 C CB  . ASN A 218 ? 0.2088 0.2997 0.2670 0.0460  -0.0650 -0.0102 212 ASN A CB  
1623 C CG  . ASN A 218 ? 0.2333 0.3129 0.2882 0.0614  -0.0466 0.0056  212 ASN A CG  
1624 O OD1 . ASN A 218 ? 0.2096 0.3169 0.2980 0.0566  -0.0406 0.0089  212 ASN A OD1 
1625 N ND2 . ASN A 218 ? 0.2600 0.2936 0.2706 0.0781  -0.0344 0.0145  212 ASN A ND2 
1626 N N   . LEU A 219 ? 0.2306 0.2524 0.3040 -0.0089 -0.0573 -0.0306 213 LEU A N   
1627 C CA  . LEU A 219 ? 0.2530 0.2375 0.3141 -0.0120 -0.0481 -0.0258 213 LEU A CA  
1628 C C   . LEU A 219 ? 0.2504 0.2238 0.3327 -0.0275 -0.0428 -0.0278 213 LEU A C   
1629 O O   . LEU A 219 ? 0.2629 0.2342 0.3549 -0.0396 -0.0466 -0.0415 213 LEU A O   
1630 C CB  . LEU A 219 ? 0.2479 0.2148 0.2863 -0.0076 -0.0503 -0.0318 213 LEU A CB  
1631 C CG  . LEU A 219 ? 0.2557 0.2002 0.2890 -0.0084 -0.0427 -0.0259 213 LEU A CG  
1632 C CD1 . LEU A 219 ? 0.2835 0.2235 0.3058 -0.0063 -0.0378 -0.0131 213 LEU A CD1 
1633 C CD2 . LEU A 219 ? 0.3346 0.2717 0.3522 -0.0034 -0.0415 -0.0321 213 LEU A CD2 
1634 N N   . GLU A 220 ? 0.2489 0.2089 0.3318 -0.0274 -0.0328 -0.0145 214 GLU A N   
1635 C CA  . GLU A 220 ? 0.2578 0.1987 0.3534 -0.0381 -0.0236 -0.0108 214 GLU A CA  
1636 C C   . GLU A 220 ? 0.2121 0.1263 0.2909 -0.0290 -0.0203 -0.0013 214 GLU A C   
1637 O O   . GLU A 220 ? 0.2776 0.1963 0.3398 -0.0199 -0.0239 0.0053  214 GLU A O   
1638 C CB  . GLU A 220 ? 0.2991 0.2493 0.4068 -0.0426 -0.0126 0.0006  214 GLU A CB  
1639 C CG  . GLU A 220 ? 0.3276 0.3193 0.4620 -0.0488 -0.0149 -0.0058 214 GLU A CG  
1640 C CD  . GLU A 220 ? 0.4454 0.4470 0.6087 -0.0724 -0.0168 -0.0201 214 GLU A CD  
1641 O OE1 . GLU A 220 ? 0.4519 0.4136 0.6098 -0.0835 -0.0099 -0.0230 214 GLU A OE1 
1642 O OE2 . GLU A 220 ? 0.5000 0.5496 0.6903 -0.0800 -0.0247 -0.0285 214 GLU A OE2 
1643 N N   . PHE A 221 ? 0.2931 0.1803 0.3764 -0.0320 -0.0129 -0.0009 215 PHE A N   
1644 C CA  . PHE A 221 ? 0.2775 0.1462 0.3496 -0.0172 -0.0097 0.0105  215 PHE A CA  
1645 C C   . PHE A 221 ? 0.2694 0.1160 0.3372 -0.0144 0.0018  0.0292  215 PHE A C   
1646 O O   . PHE A 221 ? 0.3556 0.1757 0.4306 -0.0258 0.0145  0.0284  215 PHE A O   
1647 C CB  . PHE A 221 ? 0.3190 0.1656 0.3910 -0.0132 -0.0061 -0.0011 215 PHE A CB  
1648 C CG  . PHE A 221 ? 0.3012 0.1664 0.3691 -0.0136 -0.0154 -0.0176 215 PHE A CG  
1649 C CD1 . PHE A 221 ? 0.3073 0.1901 0.3690 -0.0007 -0.0191 -0.0130 215 PHE A CD1 
1650 C CD2 . PHE A 221 ? 0.3289 0.1979 0.3985 -0.0282 -0.0206 -0.0368 215 PHE A CD2 
1651 C CE1 . PHE A 221 ? 0.3027 0.1971 0.3553 -0.0004 -0.0234 -0.0252 215 PHE A CE1 
1652 C CE2 . PHE A 221 ? 0.3126 0.1969 0.3699 -0.0249 -0.0292 -0.0492 215 PHE A CE2 
1653 C CZ  . PHE A 221 ? 0.3095 0.2014 0.3559 -0.0102 -0.0284 -0.0425 215 PHE A CZ  
1654 N N   . LEU A 222 ? 0.2742 0.2147 0.4008 -0.0169 -0.0315 -0.0352 216 LEU A N   
1655 C CA  . LEU A 222 ? 0.2702 0.2065 0.4159 -0.0205 -0.0192 -0.0203 216 LEU A CA  
1656 C C   . LEU A 222 ? 0.2841 0.2025 0.4201 -0.0158 -0.0130 -0.0189 216 LEU A C   
1657 O O   . LEU A 222 ? 0.3109 0.2263 0.4210 -0.0078 -0.0130 -0.0232 216 LEU A O   
1658 C CB  . LEU A 222 ? 0.2512 0.2026 0.3905 -0.0177 -0.0097 -0.0043 216 LEU A CB  
1659 C CG  . LEU A 222 ? 0.2667 0.2368 0.4184 -0.0211 -0.0133 -0.0035 216 LEU A CG  
1660 C CD1 . LEU A 222 ? 0.2857 0.2675 0.4257 -0.0161 -0.0030 0.0104  216 LEU A CD1 
1661 C CD2 . LEU A 222 ? 0.3254 0.2980 0.5170 -0.0313 -0.0143 -0.0033 216 LEU A CD2 
1662 N N   . THR A 223 ? 0.4164 0.3229 0.5756 -0.0203 -0.0068 -0.0119 217 THR A N   
1663 C CA  . THR A 223 ? 0.4881 0.3766 0.6433 -0.0154 -0.0007 -0.0086 217 THR A CA  
1664 C C   . THR A 223 ? 0.4552 0.3474 0.6057 -0.0108 0.0114  0.0124  217 THR A C   
1665 O O   . THR A 223 ? 0.4988 0.4011 0.6590 -0.0142 0.0174  0.0252  217 THR A O   
1666 C CB  . THR A 223 ? 0.4933 0.3625 0.6780 -0.0224 -0.0020 -0.0141 217 THR A CB  
1667 O OG1 . THR A 223 ? 0.5774 0.4504 0.7916 -0.0308 0.0049  0.0000  217 THR A OG1 
1668 C CG2 . THR A 223 ? 0.5118 0.3768 0.7011 -0.0267 -0.0168 -0.0379 217 THR A CG2 
1669 N N   . SER A 224 ? 0.3467 0.2309 0.4824 -0.0021 0.0150  0.0158  218 SER A N   
1670 C CA  . SER A 224 ? 0.3962 0.2818 0.5277 0.0035  0.0241  0.0348  218 SER A CA  
1671 C C   . SER A 224 ? 0.3461 0.2129 0.5000 0.0014  0.0305  0.0444  218 SER A C   
1672 O O   . SER A 224 ? 0.4059 0.2557 0.5744 -0.0016 0.0274  0.0338  218 SER A O   
1673 C CB  . SER A 224 ? 0.4447 0.3328 0.5545 0.0142  0.0238  0.0350  218 SER A CB  
1674 O OG  . SER A 224 ? 0.5758 0.4481 0.6891 0.0178  0.0223  0.0259  218 SER A OG  
1675 N N   . ASP A 225 ? 0.3590 0.2278 0.5149 0.0033  0.0398  0.0645  219 ASP A N   
1676 C CA  . ASP A 225 ? 0.3921 0.2416 0.5683 0.0025  0.0480  0.0775  219 ASP A CA  
1677 C C   . ASP A 225 ? 0.3501 0.1860 0.5171 0.0136  0.0483  0.0813  219 ASP A C   
1678 O O   . ASP A 225 ? 0.3719 0.1883 0.5552 0.0147  0.0544  0.0914  219 ASP A O   
1679 C CB  . ASP A 225 ? 0.4689 0.3244 0.6486 0.0019  0.0600  0.0998  219 ASP A CB  
1680 C CG  . ASP A 225 ? 0.5927 0.4612 0.7406 0.0137  0.0624  0.1118  219 ASP A CG  
1681 O OD1 . ASP A 225 ? 0.6660 0.5364 0.8101 0.0168  0.0731  0.1313  219 ASP A OD1 
1682 O OD2 . ASP A 225 ? 0.6203 0.4967 0.7474 0.0201  0.0537  0.1017  219 ASP A OD2 
1683 N N   . LYS A 226 ? 0.4002 0.2457 0.5449 0.0217  0.0422  0.0735  220 LYS A N   
1684 C CA  . LYS A 226 ? 0.4489 0.2852 0.5884 0.0326  0.0412  0.0743  220 LYS A CA  
1685 C C   . LYS A 226 ? 0.4463 0.2858 0.5782 0.0338  0.0342  0.0531  220 LYS A C   
1686 O O   . LYS A 226 ? 0.4036 0.2590 0.5231 0.0304  0.0299  0.0438  220 LYS A O   
1687 C CB  . LYS A 226 ? 0.4576 0.3061 0.5779 0.0435  0.0421  0.0897  220 LYS A CB  
1688 C CG  . LYS A 226 ? 0.5113 0.3562 0.6281 0.0555  0.0391  0.0897  220 LYS A CG  
1689 C CD  . LYS A 226 ? 0.5348 0.3923 0.6347 0.0661  0.0374  0.1049  220 LYS A CD  
1690 C CE  . LYS A 226 ? 0.5336 0.3918 0.6342 0.0784  0.0325  0.1039  220 LYS A CE  
1691 N NZ  . LYS A 226 ? 0.5765 0.4493 0.6606 0.0889  0.0274  0.1164  220 LYS A NZ  
1692 N N   . LYS A 227 ? 0.4692 0.2927 0.6085 0.0392  0.0342  0.0460  221 LYS A N   
1693 C CA  . LYS A 227 ? 0.4394 0.2658 0.5691 0.0432  0.0304  0.0279  221 LYS A CA  
1694 C C   . LYS A 227 ? 0.4076 0.2514 0.5234 0.0530  0.0302  0.0336  221 LYS A C   
1695 O O   . LYS A 227 ? 0.4222 0.2631 0.5427 0.0622  0.0320  0.0445  221 LYS A O   
1696 C CB  . LYS A 227 ? 0.5078 0.3106 0.6506 0.0470  0.0319  0.0176  221 LYS A CB  
1697 C CG  . LYS A 227 ? 0.5062 0.3113 0.6383 0.0562  0.0320  0.0038  221 LYS A CG  
1698 C CD  . LYS A 227 ? 0.5273 0.3416 0.6426 0.0517  0.0281  -0.0135 221 LYS A CD  
1699 C CE  . LYS A 227 ? 0.6137 0.4294 0.7178 0.0618  0.0316  -0.0253 221 LYS A CE  
1700 N NZ  . LYS A 227 ? 0.7405 0.5616 0.8247 0.0590  0.0286  -0.0415 221 LYS A NZ  
1701 N N   . TYR A 228 ? 0.3691 0.2308 0.4701 0.0509  0.0274  0.0264  222 TYR A N   
1702 C CA  . TYR A 228 ? 0.3515 0.2304 0.4440 0.0582  0.0267  0.0287  222 TYR A CA  
1703 C C   . TYR A 228 ? 0.3445 0.2232 0.4340 0.0621  0.0288  0.0139  222 TYR A C   
1704 O O   . TYR A 228 ? 0.3818 0.2570 0.4632 0.0572  0.0284  0.0013  222 TYR A O   
1705 C CB  . TYR A 228 ? 0.3477 0.2457 0.4279 0.0535  0.0237  0.0324  222 TYR A CB  
1706 C CG  . TYR A 228 ? 0.3062 0.2064 0.3853 0.0520  0.0234  0.0473  222 TYR A CG  
1707 C CD1 . TYR A 228 ? 0.3570 0.2629 0.4337 0.0604  0.0219  0.0597  222 TYR A CD1 
1708 C CD2 . TYR A 228 ? 0.3547 0.2523 0.4352 0.0432  0.0248  0.0493  222 TYR A CD2 
1709 C CE1 . TYR A 228 ? 0.4351 0.3422 0.5054 0.0612  0.0229  0.0740  222 TYR A CE1 
1710 C CE2 . TYR A 228 ? 0.3502 0.2500 0.4287 0.0431  0.0276  0.0643  222 TYR A CE2 
1711 C CZ  . TYR A 228 ? 0.4706 0.3744 0.5414 0.0526  0.0271  0.0767  222 TYR A CZ  
1712 O OH  . TYR A 228 ? 0.5156 0.4211 0.5789 0.0545  0.0309  0.0922  222 TYR A OH  
1713 N N   . HIS A 229 ? 0.3219 0.2045 0.4180 0.0718  0.0313  0.0157  223 HIS A N   
1714 C CA  . HIS A 229 ? 0.3049 0.1888 0.3992 0.0770  0.0364  0.0036  223 HIS A CA  
1715 C C   . HIS A 229 ? 0.3369 0.2426 0.4244 0.0762  0.0369  0.0038  223 HIS A C   
1716 O O   . HIS A 229 ? 0.3144 0.2348 0.4077 0.0775  0.0332  0.0133  223 HIS A O   
1717 C CB  . HIS A 229 ? 0.3218 0.1992 0.4321 0.0885  0.0405  0.0053  223 HIS A CB  
1718 C CG  . HIS A 229 ? 0.3500 0.2029 0.4694 0.0898  0.0410  0.0050  223 HIS A CG  
1719 N ND1 . HIS A 229 ? 0.4163 0.2501 0.5334 0.0896  0.0442  -0.0104 223 HIS A ND1 
1720 C CD2 . HIS A 229 ? 0.3491 0.1921 0.4799 0.0917  0.0388  0.0184  223 HIS A CD2 
1721 C CE1 . HIS A 229 ? 0.4482 0.2607 0.5789 0.0902  0.0438  -0.0074 223 HIS A CE1 
1722 N NE2 . HIS A 229 ? 0.4399 0.2573 0.5790 0.0915  0.0414  0.0114  223 HIS A NE2 
1723 N N   . PHE A 230 ? 0.3032 0.2096 0.3780 0.0745  0.0411  -0.0068 224 PHE A N   
1724 C CA  . PHE A 230 ? 0.2903 0.2142 0.3593 0.0729  0.0433  -0.0059 224 PHE A CA  
1725 C C   . PHE A 230 ? 0.2906 0.2289 0.3777 0.0797  0.0470  -0.0007 224 PHE A C   
1726 O O   . PHE A 230 ? 0.3228 0.2574 0.4216 0.0881  0.0531  -0.0032 224 PHE A O   
1727 C CB  . PHE A 230 ? 0.3110 0.2304 0.3620 0.0731  0.0493  -0.0168 224 PHE A CB  
1728 C CG  . PHE A 230 ? 0.3457 0.2799 0.3897 0.0708  0.0526  -0.0141 224 PHE A CG  
1729 C CD1 . PHE A 230 ? 0.4221 0.3636 0.4698 0.0768  0.0638  -0.0146 224 PHE A CD1 
1730 C CD2 . PHE A 230 ? 0.3114 0.2516 0.3476 0.0629  0.0458  -0.0104 224 PHE A CD2 
1731 C CE1 . PHE A 230 ? 0.4187 0.3720 0.4630 0.0741  0.0682  -0.0106 224 PHE A CE1 
1732 C CE2 . PHE A 230 ? 0.3375 0.2888 0.3692 0.0610  0.0492  -0.0074 224 PHE A CE2 
1733 C CZ  . PHE A 230 ? 0.3440 0.3010 0.3800 0.0662  0.0604  -0.0072 224 PHE A CZ  
1734 N N   . ALA A 231 ? 0.2721 0.2271 0.3639 0.0761  0.0427  0.0056  225 ALA A N   
1735 C CA  . ALA A 231 ? 0.2678 0.2405 0.3804 0.0801  0.0433  0.0095  225 ALA A CA  
1736 C C   . ALA A 231 ? 0.3197 0.2948 0.4499 0.0873  0.0369  0.0158  225 ALA A C   
1737 O O   . ALA A 231 ? 0.3111 0.3014 0.4633 0.0923  0.0361  0.0178  225 ALA A O   
1738 C CB  . ALA A 231 ? 0.3603 0.3376 0.4808 0.0846  0.0566  0.0046  225 ALA A CB  
1739 N N   . LYS A 232 ? 0.2896 0.2504 0.4127 0.0883  0.0322  0.0196  226 LYS A N   
1740 C CA  . LYS A 232 ? 0.2854 0.2492 0.4219 0.0961  0.0248  0.0286  226 LYS A CA  
1741 C C   . LYS A 232 ? 0.2779 0.2502 0.4051 0.0927  0.0138  0.0362  226 LYS A C   
1742 O O   . LYS A 232 ? 0.2793 0.2463 0.3885 0.0847  0.0132  0.0363  226 LYS A O   
1743 C CB  . LYS A 232 ? 0.3165 0.2589 0.4528 0.1008  0.0270  0.0313  226 LYS A CB  
1744 C CG  . LYS A 232 ? 0.3651 0.2972 0.5113 0.1072  0.0372  0.0227  226 LYS A CG  
1745 C CD  . LYS A 232 ? 0.3801 0.3216 0.5512 0.1194  0.0369  0.0270  226 LYS A CD  
1746 C CE  . LYS A 232 ? 0.4480 0.3762 0.6290 0.1278  0.0482  0.0189  226 LYS A CE  
1747 N NZ  . LYS A 232 ? 0.5349 0.4700 0.7127 0.1264  0.0596  0.0078  226 LYS A NZ  
1748 N N   . PRO A 233 ? 0.2816 0.2676 0.4203 0.0995  0.0045  0.0420  227 PRO A N   
1749 C CA  . PRO A 233 ? 0.2954 0.2890 0.4208 0.0984  -0.0066 0.0479  227 PRO A CA  
1750 C C   . PRO A 233 ? 0.2794 0.2575 0.3887 0.1013  -0.0078 0.0590  227 PRO A C   
1751 O O   . PRO A 233 ? 0.2958 0.2615 0.4122 0.1081  -0.0050 0.0650  227 PRO A O   
1752 C CB  . PRO A 233 ? 0.2918 0.3049 0.4365 0.1066  -0.0176 0.0489  227 PRO A CB  
1753 C CG  . PRO A 233 ? 0.2781 0.2876 0.4446 0.1156  -0.0124 0.0501  227 PRO A CG  
1754 C CD  . PRO A 233 ? 0.2564 0.2535 0.4215 0.1094  0.0031  0.0422  227 PRO A CD  
1755 N N   . TYR A 234 ? 0.2816 0.2599 0.3706 0.0963  -0.0106 0.0623  228 TYR A N   
1756 C CA  . TYR A 234 ? 0.3018 0.2674 0.3751 0.0988  -0.0097 0.0750  228 TYR A CA  
1757 C C   . TYR A 234 ? 0.2885 0.2655 0.3432 0.1024  -0.0189 0.0802  228 TYR A C   
1758 O O   . TYR A 234 ? 0.2981 0.2855 0.3456 0.0962  -0.0214 0.0720  228 TYR A O   
1759 C CB  . TYR A 234 ? 0.2797 0.2306 0.3463 0.0884  0.0004  0.0738  228 TYR A CB  
1760 C CG  . TYR A 234 ? 0.2841 0.2196 0.3650 0.0866  0.0080  0.0686  228 TYR A CG  
1761 C CD1 . TYR A 234 ? 0.3025 0.2201 0.3901 0.0912  0.0117  0.0775  228 TYR A CD1 
1762 C CD2 . TYR A 234 ? 0.2882 0.2259 0.3747 0.0813  0.0117  0.0546  228 TYR A CD2 
1763 C CE1 . TYR A 234 ? 0.3161 0.2177 0.4167 0.0902  0.0178  0.0703  228 TYR A CE1 
1764 C CE2 . TYR A 234 ? 0.2885 0.2113 0.3840 0.0813  0.0181  0.0479  228 TYR A CE2 
1765 C CZ  . TYR A 234 ? 0.2975 0.2022 0.4006 0.0855  0.0206  0.0545  228 TYR A CZ  
1766 O OH  . TYR A 234 ? 0.3301 0.2180 0.4423 0.0861  0.0262  0.0455  228 TYR A OH  
1767 N N   . LYS A 235 ? 0.3192 0.2929 0.3646 0.1134  -0.0237 0.0937  229 LYS A N   
1768 C CA  . LYS A 235 ? 0.3651 0.3486 0.3874 0.1198  -0.0331 0.0986  229 LYS A CA  
1769 C C   . LYS A 235 ? 0.3702 0.3527 0.3732 0.1110  -0.0270 0.0964  229 LYS A C   
1770 O O   . LYS A 235 ? 0.3719 0.3670 0.3629 0.1108  -0.0345 0.0888  229 LYS A O   
1771 C CB  . LYS A 235 ? 0.3998 0.3746 0.4089 0.1334  -0.0351 0.1171  229 LYS A CB  
1772 C CG  . LYS A 235 ? 0.4765 0.4592 0.4540 0.1417  -0.0435 0.1228  229 LYS A CG  
1773 N N   . GLU A 236 ? 0.3706 0.3384 0.3731 0.1039  -0.0136 0.1022  230 GLU A N   
1774 C CA  . GLU A 236 ? 0.3979 0.3660 0.3853 0.0968  -0.0070 0.1018  230 GLU A CA  
1775 C C   . GLU A 236 ? 0.4045 0.3829 0.3977 0.0872  -0.0090 0.0850  230 GLU A C   
1776 O O   . GLU A 236 ? 0.3800 0.3647 0.3590 0.0849  -0.0088 0.0818  230 GLU A O   
1777 C CB  . GLU A 236 ? 0.4761 0.4279 0.4694 0.0905  0.0070  0.1112  230 GLU A CB  
1778 C CG  . GLU A 236 ? 0.4708 0.4133 0.4881 0.0818  0.0112  0.1028  230 GLU A CG  
1779 C CD  . GLU A 236 ? 0.5854 0.5128 0.6161 0.0876  0.0134  0.1113  230 GLU A CD  
1780 O OE1 . GLU A 236 ? 0.6110 0.5227 0.6548 0.0812  0.0218  0.1132  230 GLU A OE1 
1781 O OE2 . GLU A 236 ? 0.5706 0.5014 0.6006 0.0987  0.0060  0.1155  230 GLU A OE2 
1782 N N   . PHE A 237 ? 0.3210 0.3006 0.3342 0.0826  -0.0098 0.0749  231 PHE A N   
1783 C CA  . PHE A 237 ? 0.2831 0.2716 0.3018 0.0747  -0.0108 0.0612  231 PHE A CA  
1784 C C   . PHE A 237 ? 0.2929 0.2964 0.3085 0.0786  -0.0222 0.0546  231 PHE A C   
1785 O O   . PHE A 237 ? 0.2815 0.2908 0.2915 0.0738  -0.0233 0.0470  231 PHE A O   
1786 C CB  . PHE A 237 ? 0.2997 0.2851 0.3377 0.0706  -0.0070 0.0538  231 PHE A CB  
1787 C CG  . PHE A 237 ? 0.3213 0.2922 0.3623 0.0648  0.0022  0.0545  231 PHE A CG  
1788 C CD1 . PHE A 237 ? 0.3763 0.3393 0.4091 0.0616  0.0069  0.0616  231 PHE A CD1 
1789 C CD2 . PHE A 237 ? 0.3972 0.3629 0.4504 0.0630  0.0062  0.0472  231 PHE A CD2 
1790 C CE1 . PHE A 237 ? 0.3638 0.3144 0.4042 0.0554  0.0132  0.0603  231 PHE A CE1 
1791 C CE2 . PHE A 237 ? 0.4040 0.3560 0.4592 0.0581  0.0121  0.0449  231 PHE A CE2 
1792 C CZ  . PHE A 237 ? 0.3746 0.3193 0.4252 0.0537  0.0145  0.0509  231 PHE A CZ  
1793 N N   . TYR A 238 ? 0.2905 0.3004 0.3123 0.0875  -0.0316 0.0565  232 TYR A N   
1794 C CA  . TYR A 238 ? 0.3337 0.3587 0.3559 0.0911  -0.0452 0.0483  232 TYR A CA  
1795 C C   . TYR A 238 ? 0.3531 0.3791 0.3465 0.0950  -0.0495 0.0497  232 TYR A C   
1796 O O   . TYR A 238 ? 0.3255 0.3595 0.3157 0.0925  -0.0560 0.0387  232 TYR A O   
1797 C CB  . TYR A 238 ? 0.3482 0.3814 0.3840 0.1013  -0.0564 0.0508  232 TYR A CB  
1798 C CG  . TYR A 238 ? 0.3638 0.4146 0.4079 0.1037  -0.0727 0.0396  232 TYR A CG  
1799 C CD1 . TYR A 238 ? 0.4366 0.4938 0.4613 0.1145  -0.0877 0.0409  232 TYR A CD1 
1800 C CD2 . TYR A 238 ? 0.3838 0.4440 0.4552 0.0954  -0.0729 0.0275  232 TYR A CD2 
1801 C CE1 . TYR A 238 ? 0.4856 0.5590 0.5200 0.1163  -0.1051 0.0278  232 TYR A CE1 
1802 C CE2 . TYR A 238 ? 0.4098 0.4857 0.4950 0.0960  -0.0880 0.0162  232 TYR A CE2 
1803 C CZ  . TYR A 238 ? 0.5005 0.5831 0.5681 0.1061  -0.1053 0.0151  232 TYR A CZ  
1804 O OH  . TYR A 238 ? 0.5681 0.6665 0.6516 0.1062  -0.1227 0.0012  232 TYR A OH  
1805 N N   . GLU A 239 ? 0.3236 0.3404 0.2963 0.1012  -0.0444 0.0634  233 GLU A N   
1806 C CA  . GLU A 239 ? 0.3930 0.4104 0.3348 0.1070  -0.0459 0.0664  233 GLU A CA  
1807 C C   . GLU A 239 ? 0.3881 0.4039 0.3249 0.0976  -0.0367 0.0599  233 GLU A C   
1808 O O   . GLU A 239 ? 0.4081 0.4296 0.3287 0.0999  -0.0418 0.0519  233 GLU A O   
1809 C CB  . GLU A 239 ? 0.4603 0.4672 0.3833 0.1160  -0.0390 0.0856  233 GLU A CB  
1810 C CG  . GLU A 239 ? 0.5589 0.5679 0.4823 0.1287  -0.0503 0.0931  233 GLU A CG  
1811 C CD  . GLU A 239 ? 0.6485 0.6444 0.5540 0.1382  -0.0419 0.1148  233 GLU A CD  
1812 O OE1 . GLU A 239 ? 0.7182 0.7158 0.6144 0.1521  -0.0522 0.1233  233 GLU A OE1 
1813 O OE2 . GLU A 239 ? 0.7139 0.6981 0.6168 0.1321  -0.0252 0.1240  233 GLU A OE2 
1814 N N   . LEU A 240 ? 0.3398 0.3478 0.2904 0.0878  -0.0241 0.0622  234 LEU A N   
1815 C CA  . LEU A 240 ? 0.3534 0.3613 0.3028 0.0794  -0.0165 0.0563  234 LEU A CA  
1816 C C   . LEU A 240 ? 0.3163 0.3322 0.2762 0.0746  -0.0239 0.0406  234 LEU A C   
1817 O O   . LEU A 240 ? 0.2888 0.3075 0.2392 0.0736  -0.0240 0.0338  234 LEU A O   
1818 C CB  . LEU A 240 ? 0.3120 0.3112 0.2764 0.0706  -0.0049 0.0608  234 LEU A CB  
1819 C CG  . LEU A 240 ? 0.3224 0.3221 0.2891 0.0624  0.0021  0.0558  234 LEU A CG  
1820 C CD1 . LEU A 240 ? 0.3000 0.3018 0.2472 0.0669  0.0073  0.0610  234 LEU A CD1 
1821 C CD2 . LEU A 240 ? 0.3454 0.3371 0.3279 0.0548  0.0100  0.0592  234 LEU A CD2 
1822 N N   . TYR A 241 ? 0.2861 0.3051 0.2674 0.0719  -0.0286 0.0355  235 TYR A N   
1823 C CA  . TYR A 241 ? 0.2680 0.2942 0.2642 0.0671  -0.0342 0.0226  235 TYR A CA  
1824 C C   . TYR A 241 ? 0.2487 0.2827 0.2345 0.0725  -0.0468 0.0142  235 TYR A C   
1825 O O   . TYR A 241 ? 0.2958 0.3310 0.2818 0.0687  -0.0481 0.0044  235 TYR A O   
1826 C CB  . TYR A 241 ? 0.2543 0.2840 0.2757 0.0657  -0.0359 0.0212  235 TYR A CB  
1827 C CG  . TYR A 241 ? 0.2418 0.2813 0.2845 0.0624  -0.0427 0.0101  235 TYR A CG  
1828 C CD1 . TYR A 241 ? 0.2814 0.3320 0.3338 0.0680  -0.0568 0.0053  235 TYR A CD1 
1829 C CD2 . TYR A 241 ? 0.2685 0.3062 0.3238 0.0539  -0.0351 0.0052  235 TYR A CD2 
1830 C CE1 . TYR A 241 ? 0.3628 0.4232 0.4416 0.0636  -0.0629 -0.0051 235 TYR A CE1 
1831 C CE2 . TYR A 241 ? 0.2675 0.3131 0.3463 0.0502  -0.0392 -0.0031 235 TYR A CE2 
1832 C CZ  . TYR A 241 ? 0.4030 0.4601 0.4958 0.0543  -0.0529 -0.0086 235 TYR A CZ  
1833 O OH  . TYR A 241 ? 0.4028 0.4684 0.5253 0.0493  -0.0569 -0.0173 235 TYR A OH  
1834 N N   . MET A 242 ? 0.2676 0.3059 0.2433 0.0825  -0.0571 0.0174  236 MET A N   
1835 C CA  . MET A 242 ? 0.3018 0.3480 0.2659 0.0890  -0.0723 0.0070  236 MET A CA  
1836 C C   . MET A 242 ? 0.3462 0.3875 0.2789 0.0927  -0.0684 0.0059  236 MET A C   
1837 O O   . MET A 242 ? 0.3708 0.4153 0.2982 0.0934  -0.0767 -0.0080 236 MET A O   
1838 C CB  . MET A 242 ? 0.3821 0.4346 0.3401 0.1008  -0.0856 0.0116  236 MET A CB  
1839 C CG  . MET A 242 ? 0.3752 0.4362 0.3680 0.0988  -0.0920 0.0098  236 MET A CG  
1840 S SD  . MET A 242 ? 0.4245 0.4979 0.4504 0.0905  -0.1035 -0.0102 236 MET A SD  
1841 C CE  . MET A 242 ? 0.5262 0.6077 0.5283 0.1015  -0.1265 -0.0221 236 MET A CE  
1842 N N   . ASP A 243 ? 0.3386 0.3722 0.2524 0.0955  -0.0554 0.0200  237 ASP A N   
1843 C CA  . ASP A 243 ? 0.3956 0.4256 0.2827 0.0991  -0.0478 0.0205  237 ASP A CA  
1844 C C   . ASP A 243 ? 0.3583 0.3870 0.2577 0.0896  -0.0419 0.0101  237 ASP A C   
1845 O O   . ASP A 243 ? 0.3898 0.4189 0.2745 0.0929  -0.0442 0.0001  237 ASP A O   
1846 C CB  . ASP A 243 ? 0.4608 0.4835 0.3355 0.1015  -0.0320 0.0393  237 ASP A CB  
1847 C CG  . ASP A 243 ? 0.5855 0.6071 0.4373 0.1146  -0.0356 0.0519  237 ASP A CG  
1848 O OD1 . ASP A 243 ? 0.6004 0.6282 0.4423 0.1233  -0.0523 0.0451  237 ASP A OD1 
1849 O OD2 . ASP A 243 ? 0.5959 0.6101 0.4414 0.1163  -0.0220 0.0690  237 ASP A OD2 
1850 N N   . LEU A 244 ? 0.3396 0.3657 0.2639 0.0788  -0.0342 0.0123  238 LEU A N   
1851 C CA  . LEU A 244 ? 0.3211 0.3454 0.2559 0.0713  -0.0289 0.0044  238 LEU A CA  
1852 C C   . LEU A 244 ? 0.3374 0.3649 0.2828 0.0696  -0.0405 -0.0115 238 LEU A C   
1853 O O   . LEU A 244 ? 0.3218 0.3469 0.2640 0.0689  -0.0398 -0.0205 238 LEU A O   
1854 C CB  . LEU A 244 ? 0.2966 0.3174 0.2522 0.0619  -0.0200 0.0101  238 LEU A CB  
1855 C CG  . LEU A 244 ? 0.3776 0.3945 0.3270 0.0616  -0.0084 0.0228  238 LEU A CG  
1856 C CD1 . LEU A 244 ? 0.3056 0.3187 0.2738 0.0539  -0.0035 0.0267  238 LEU A CD1 
1857 C CD2 . LEU A 244 ? 0.3726 0.3897 0.3123 0.0623  -0.0007 0.0221  238 LEU A CD2 
1858 N N   . LYS A 245 ? 0.3052 0.3380 0.2665 0.0691  -0.0512 -0.0152 239 LYS A N   
1859 C CA  . LYS A 245 ? 0.3127 0.3497 0.2909 0.0665  -0.0631 -0.0304 239 LYS A CA  
1860 C C   . LYS A 245 ? 0.3602 0.3987 0.3161 0.0751  -0.0752 -0.0423 239 LYS A C   
1861 O O   . LYS A 245 ? 0.3979 0.4333 0.3573 0.0729  -0.0784 -0.0556 239 LYS A O   
1862 C CB  . LYS A 245 ? 0.3976 0.4428 0.4012 0.0649  -0.0712 -0.0303 239 LYS A CB  
1863 C CG  . LYS A 245 ? 0.4830 0.5331 0.5183 0.0582  -0.0791 -0.0431 239 LYS A CG  
1864 C CD  . LYS A 245 ? 0.5118 0.5696 0.5770 0.0550  -0.0788 -0.0381 239 LYS A CD  
1865 C CE  . LYS A 245 ? 0.5270 0.5965 0.6213 0.0539  -0.0946 -0.0506 239 LYS A CE  
1866 N NZ  . LYS A 245 ? 0.5772 0.6574 0.6962 0.0552  -0.0963 -0.0446 239 LYS A NZ  
1867 N N   . LEU A 246 ? 0.3586 0.4007 0.2897 0.0860  -0.0822 -0.0380 240 LEU A N   
1868 C CA  . LEU A 246 ? 0.3943 0.4384 0.3003 0.0961  -0.0961 -0.0509 240 LEU A CA  
1869 C C   . LEU A 246 ? 0.4087 0.4452 0.2848 0.1011  -0.0856 -0.0522 240 LEU A C   
1870 O O   . LEU A 246 ? 0.4698 0.5042 0.3352 0.1048  -0.0937 -0.0689 240 LEU A O   
1871 C CB  . LEU A 246 ? 0.3989 0.4494 0.2846 0.1084  -0.1075 -0.0444 240 LEU A CB  
1872 C CG  . LEU A 246 ? 0.5542 0.6145 0.4722 0.1053  -0.1193 -0.0442 240 LEU A CG  
1873 C CD1 . LEU A 246 ? 0.5718 0.6382 0.4693 0.1193  -0.1313 -0.0363 240 LEU A CD1 
1874 C CD2 . LEU A 246 ? 0.5731 0.6402 0.5234 0.0981  -0.1341 -0.0642 240 LEU A CD2 
1875 N N   . LYS A 247 ? 0.4078 0.4400 0.2724 0.1015  -0.0675 -0.0356 241 LYS A N   
1876 C CA  . LYS A 247 ? 0.4135 0.4408 0.2510 0.1078  -0.0558 -0.0350 241 LYS A CA  
1877 C C   . LYS A 247 ? 0.4080 0.4305 0.2637 0.0990  -0.0454 -0.0400 241 LYS A C   
1878 O O   . LYS A 247 ? 0.4516 0.4706 0.2902 0.1047  -0.0402 -0.0470 241 LYS A O   
1879 C CB  . LYS A 247 ? 0.4183 0.4446 0.2372 0.1131  -0.0408 -0.0138 241 LYS A CB  
1880 C CG  . LYS A 247 ? 0.5488 0.5779 0.3452 0.1243  -0.0498 -0.0062 241 LYS A CG  
1881 C CD  . LYS A 247 ? 0.5715 0.5973 0.3541 0.1286  -0.0333 0.0169  241 LYS A CD  
1882 C CE  . LYS A 247 ? 0.6787 0.7057 0.4364 0.1417  -0.0426 0.0258  241 LYS A CE  
1883 N NZ  . LYS A 247 ? 0.6646 0.6871 0.3906 0.1523  -0.0259 0.0444  241 LYS A NZ  
1884 N N   . CYS A 248 ? 0.3841 0.4060 0.2724 0.0869  -0.0420 -0.0366 242 CYS A N   
1885 C CA  . CYS A 248 ? 0.3682 0.3854 0.2734 0.0796  -0.0325 -0.0386 242 CYS A CA  
1886 C C   . CYS A 248 ? 0.3375 0.3522 0.2716 0.0709  -0.0398 -0.0493 242 CYS A C   
1887 O O   . CYS A 248 ? 0.3510 0.3603 0.2979 0.0661  -0.0328 -0.0509 242 CYS A O   
1888 C CB  . CYS A 248 ? 0.3932 0.4107 0.3086 0.0738  -0.0186 -0.0222 242 CYS A CB  
1889 S SG  . CYS A 248 ? 0.4618 0.4812 0.3529 0.0816  -0.0052 -0.0080 242 CYS A SG  
1890 N N   . ASN A 249 ? 0.3066 0.3253 0.2532 0.0691  -0.0530 -0.0557 243 ASN A N   
1891 C CA  . ASN A 249 ? 0.2943 0.3118 0.2743 0.0597  -0.0576 -0.0631 243 ASN A CA  
1892 C C   . ASN A 249 ? 0.2794 0.2937 0.2778 0.0513  -0.0443 -0.0512 243 ASN A C   
1893 O O   . ASN A 249 ? 0.3014 0.3098 0.3190 0.0453  -0.0408 -0.0545 243 ASN A O   
1894 C CB  . ASN A 249 ? 0.3058 0.3165 0.2912 0.0595  -0.0639 -0.0805 243 ASN A CB  
1895 C CG  . ASN A 249 ? 0.3912 0.4010 0.4151 0.0497  -0.0697 -0.0879 243 ASN A CG  
1896 O OD1 . ASN A 249 ? 0.3650 0.3835 0.4066 0.0466  -0.0771 -0.0871 243 ASN A OD1 
1897 N ND2 . ASN A 249 ? 0.4889 0.4884 0.5283 0.0449  -0.0649 -0.0937 243 ASN A ND2 
1898 N N   . ILE A 250 ? 0.2396 0.2566 0.2314 0.0515  -0.0370 -0.0374 244 ILE A N   
1899 C CA  . ILE A 250 ? 0.2693 0.2840 0.2761 0.0447  -0.0270 -0.0277 244 ILE A CA  
1900 C C   . ILE A 250 ? 0.2487 0.2686 0.2648 0.0435  -0.0290 -0.0217 244 ILE A C   
1901 O O   . ILE A 250 ? 0.2997 0.3220 0.3025 0.0479  -0.0290 -0.0148 244 ILE A O   
1902 C CB  . ILE A 250 ? 0.2414 0.2535 0.2354 0.0456  -0.0162 -0.0184 244 ILE A CB  
1903 C CG1 . ILE A 250 ? 0.2764 0.2848 0.2621 0.0488  -0.0137 -0.0243 244 ILE A CG1 
1904 C CG2 . ILE A 250 ? 0.2355 0.2448 0.2428 0.0395  -0.0088 -0.0111 244 ILE A CG2 
1905 C CD1 . ILE A 250 ? 0.2542 0.2629 0.2322 0.0501  -0.0035 -0.0157 244 ILE A CD1 
1906 N N   . GLU A 251 ? 0.2518 0.2729 0.2922 0.0380  -0.0292 -0.0234 245 GLU A N   
1907 C CA  . GLU A 251 ? 0.2071 0.2331 0.2594 0.0373  -0.0286 -0.0177 245 GLU A CA  
1908 C C   . GLU A 251 ? 0.2306 0.2512 0.2811 0.0345  -0.0163 -0.0082 245 GLU A C   
1909 O O   . GLU A 251 ? 0.2303 0.2453 0.2827 0.0310  -0.0093 -0.0072 245 GLU A O   
1910 C CB  . GLU A 251 ? 0.2550 0.2868 0.3372 0.0335  -0.0331 -0.0238 245 GLU A CB  
1911 C CG  . GLU A 251 ? 0.3019 0.3403 0.3988 0.0342  -0.0315 -0.0182 245 GLU A CG  
1912 C CD  . GLU A 251 ? 0.3408 0.3894 0.4712 0.0317  -0.0379 -0.0244 245 GLU A CD  
1913 O OE1 . GLU A 251 ? 0.2732 0.3283 0.4189 0.0331  -0.0352 -0.0198 245 GLU A OE1 
1914 O OE2 . GLU A 251 ? 0.3512 0.4015 0.4954 0.0284  -0.0454 -0.0343 245 GLU A OE2 
1915 N N   . PHE A 252 ? 0.2545 0.2758 0.3001 0.0370  -0.0146 -0.0017 246 PHE A N   
1916 C CA  . PHE A 252 ? 0.2354 0.2512 0.2789 0.0350  -0.0052 0.0047  246 PHE A CA  
1917 C C   . PHE A 252 ? 0.2420 0.2601 0.3004 0.0355  -0.0029 0.0062  246 PHE A C   
1918 O O   . PHE A 252 ? 0.2662 0.2909 0.3344 0.0387  -0.0093 0.0051  246 PHE A O   
1919 C CB  . PHE A 252 ? 0.2503 0.2623 0.2774 0.0372  -0.0037 0.0104  246 PHE A CB  
1920 C CG  . PHE A 252 ? 0.2402 0.2502 0.2556 0.0364  -0.0016 0.0105  246 PHE A CG  
1921 C CD1 . PHE A 252 ? 0.2253 0.2314 0.2400 0.0331  0.0039  0.0118  246 PHE A CD1 
1922 C CD2 . PHE A 252 ? 0.2699 0.2825 0.2741 0.0402  -0.0053 0.0092  246 PHE A CD2 
1923 C CE1 . PHE A 252 ? 0.2552 0.2614 0.2632 0.0331  0.0055  0.0122  246 PHE A CE1 
1924 C CE2 . PHE A 252 ? 0.2795 0.2912 0.2751 0.0404  -0.0016 0.0095  246 PHE A CE2 
1925 C CZ  . PHE A 252 ? 0.2917 0.3009 0.2916 0.0365  0.0038  0.0112  246 PHE A CZ  
1926 N N   . ASP A 253 ? 0.2340 0.2471 0.2932 0.0336  0.0062  0.0087  247 ASP A N   
1927 C CA  . ASP A 253 ? 0.1953 0.2087 0.2646 0.0355  0.0113  0.0102  247 ASP A CA  
1928 C C   . ASP A 253 ? 0.2183 0.2291 0.2814 0.0396  0.0085  0.0130  247 ASP A C   
1929 O O   . ASP A 253 ? 0.2695 0.2739 0.3178 0.0392  0.0081  0.0152  247 ASP A O   
1930 C CB  . ASP A 253 ? 0.2372 0.2438 0.3003 0.0343  0.0217  0.0117  247 ASP A CB  
1931 C CG  . ASP A 253 ? 0.2689 0.2714 0.3307 0.0379  0.0271  0.0124  247 ASP A CG  
1932 O OD1 . ASP A 253 ? 0.3078 0.3153 0.3861 0.0404  0.0311  0.0124  247 ASP A OD1 
1933 O OD2 . ASP A 253 ? 0.2954 0.2898 0.3419 0.0385  0.0272  0.0120  247 ASP A OD2 
1934 N N   . LEU A 254 ? 0.2395 0.2553 0.3173 0.0436  0.0071  0.0134  248 LEU A N   
1935 C CA  . LEU A 254 ? 0.2048 0.2171 0.2798 0.0487  0.0044  0.0171  248 LEU A CA  
1936 C C   . LEU A 254 ? 0.2602 0.2620 0.3325 0.0500  0.0127  0.0176  248 LEU A C   
1937 O O   . LEU A 254 ? 0.3183 0.3132 0.3877 0.0533  0.0114  0.0209  248 LEU A O   
1938 C CB  . LEU A 254 ? 0.1921 0.2151 0.2855 0.0540  -0.0026 0.0172  248 LEU A CB  
1939 C CG  . LEU A 254 ? 0.2239 0.2558 0.3152 0.0553  -0.0151 0.0156  248 LEU A CG  
1940 C CD1 . LEU A 254 ? 0.2185 0.2646 0.3352 0.0588  -0.0230 0.0123  248 LEU A CD1 
1941 C CD2 . LEU A 254 ? 0.2295 0.2560 0.3016 0.0606  -0.0200 0.0221  248 LEU A CD2 
1942 N N   . LEU A 255 ? 0.2448 0.2442 0.3172 0.0482  0.0214  0.0143  249 LEU A N   
1943 C CA  . LEU A 255 ? 0.2374 0.2262 0.3040 0.0507  0.0286  0.0121  249 LEU A CA  
1944 C C   . LEU A 255 ? 0.2807 0.2586 0.3287 0.0471  0.0273  0.0104  249 LEU A C   
1945 O O   . LEU A 255 ? 0.2834 0.2508 0.3284 0.0486  0.0275  0.0087  249 LEU A O   
1946 C CB  . LEU A 255 ? 0.2827 0.2732 0.3530 0.0522  0.0394  0.0095  249 LEU A CB  
1947 C CG  . LEU A 255 ? 0.3828 0.3830 0.4769 0.0568  0.0447  0.0103  249 LEU A CG  
1948 C CD1 . LEU A 255 ? 0.4247 0.4264 0.5196 0.0572  0.0582  0.0101  249 LEU A CD1 
1949 C CD2 . LEU A 255 ? 0.4288 0.4231 0.5281 0.0638  0.0461  0.0092  249 LEU A CD2 
1950 N N   . TYR A 256 ? 0.2467 0.2268 0.2852 0.0425  0.0256  0.0104  250 TYR A N   
1951 C CA  . TYR A 256 ? 0.2462 0.2194 0.2712 0.0391  0.0235  0.0084  250 TYR A CA  
1952 C C   . TYR A 256 ? 0.2508 0.2279 0.2744 0.0354  0.0178  0.0122  250 TYR A C   
1953 O O   . TYR A 256 ? 0.2476 0.2200 0.2700 0.0332  0.0155  0.0132  250 TYR A O   
1954 C CB  . TYR A 256 ? 0.2552 0.2274 0.2686 0.0388  0.0273  0.0054  250 TYR A CB  
1955 C CG  . TYR A 256 ? 0.2457 0.2137 0.2549 0.0438  0.0356  0.0022  250 TYR A CG  
1956 C CD1 . TYR A 256 ? 0.2432 0.2009 0.2396 0.0465  0.0362  -0.0045 250 TYR A CD1 
1957 C CD2 . TYR A 256 ? 0.2874 0.2619 0.3057 0.0460  0.0434  0.0053  250 TYR A CD2 
1958 C CE1 . TYR A 256 ? 0.2830 0.2364 0.2711 0.0528  0.0452  -0.0080 250 TYR A CE1 
1959 C CE2 . TYR A 256 ? 0.3129 0.2844 0.3271 0.0513  0.0539  0.0037  250 TYR A CE2 
1960 C CZ  . TYR A 256 ? 0.3535 0.3141 0.3501 0.0555  0.0552  -0.0030 250 TYR A CZ  
1961 O OH  . TYR A 256 ? 0.3997 0.3567 0.3882 0.0626  0.0672  -0.0051 250 TYR A OH  
1962 N N   . ASP A 257 ? 0.2333 0.2187 0.2583 0.0345  0.0165  0.0140  251 ASP A N   
1963 C CA  . ASP A 257 ? 0.2482 0.2367 0.2686 0.0321  0.0129  0.0162  251 ASP A CA  
1964 C C   . ASP A 257 ? 0.2543 0.2433 0.2755 0.0337  0.0103  0.0210  251 ASP A C   
1965 O O   . ASP A 257 ? 0.2654 0.2541 0.2829 0.0320  0.0103  0.0242  251 ASP A O   
1966 C CB  . ASP A 257 ? 0.2581 0.2529 0.2794 0.0316  0.0122  0.0151  251 ASP A CB  
1967 C CG  . ASP A 257 ? 0.2282 0.2219 0.2430 0.0295  0.0135  0.0142  251 ASP A CG  
1968 O OD1 . ASP A 257 ? 0.2113 0.2019 0.2210 0.0283  0.0129  0.0141  251 ASP A OD1 
1969 O OD2 . ASP A 257 ? 0.2014 0.1972 0.2184 0.0293  0.0144  0.0135  251 ASP A OD2 
1970 N N   . ILE A 258 ? 0.2383 0.2287 0.2649 0.0378  0.0085  0.0229  252 ILE A N   
1971 C CA  . ILE A 258 ? 0.2672 0.2574 0.2903 0.0412  0.0060  0.0296  252 ILE A CA  
1972 C C   . ILE A 258 ? 0.2818 0.2618 0.3064 0.0399  0.0097  0.0343  252 ILE A C   
1973 O O   . ILE A 258 ? 0.2855 0.2638 0.3062 0.0397  0.0113  0.0412  252 ILE A O   
1974 C CB  . ILE A 258 ? 0.2751 0.2706 0.3035 0.0473  0.0008  0.0307  252 ILE A CB  
1975 C CG1 . ILE A 258 ? 0.3786 0.3844 0.4069 0.0476  -0.0048 0.0255  252 ILE A CG1 
1976 C CG2 . ILE A 258 ? 0.3708 0.3638 0.3921 0.0528  -0.0013 0.0396  252 ILE A CG2 
1977 C CD1 . ILE A 258 ? 0.3356 0.3437 0.3483 0.0494  -0.0078 0.0274  252 ILE A CD1 
1978 N N   . LEU A 259 ? 0.2462 0.2186 0.2773 0.0388  0.0119  0.0300  253 LEU A N   
1979 C CA  . LEU A 259 ? 0.2314 0.1924 0.2668 0.0359  0.0143  0.0312  253 LEU A CA  
1980 C C   . LEU A 259 ? 0.2492 0.2118 0.2833 0.0294  0.0145  0.0296  253 LEU A C   
1981 O O   . LEU A 259 ? 0.2570 0.2158 0.2971 0.0264  0.0165  0.0350  253 LEU A O   
1982 C CB  . LEU A 259 ? 0.2804 0.2323 0.3204 0.0370  0.0158  0.0235  253 LEU A CB  
1983 C CG  . LEU A 259 ? 0.3549 0.2937 0.4008 0.0328  0.0163  0.0202  253 LEU A CG  
1984 C CD1 . LEU A 259 ? 0.3556 0.2861 0.4111 0.0337  0.0182  0.0304  253 LEU A CD1 
1985 C CD2 . LEU A 259 ? 0.4353 0.3644 0.4808 0.0349  0.0172  0.0093  253 LEU A CD2 
1986 N N   . GLY A 260 ? 0.2583 0.2267 0.2868 0.0276  0.0130  0.0231  254 GLY A N   
1987 C CA  . GLY A 260 ? 0.2400 0.2117 0.2690 0.0228  0.0118  0.0214  254 GLY A CA  
1988 C C   . GLY A 260 ? 0.2407 0.2191 0.2708 0.0222  0.0140  0.0293  254 GLY A C   
1989 O O   . GLY A 260 ? 0.2290 0.2076 0.2682 0.0182  0.0156  0.0320  254 GLY A O   
1990 N N   . LEU A 261 ? 0.2365 0.2208 0.2585 0.0265  0.0144  0.0324  255 LEU A N   
1991 C CA  . LEU A 261 ? 0.2361 0.2259 0.2541 0.0282  0.0175  0.0393  255 LEU A CA  
1992 C C   . LEU A 261 ? 0.2519 0.2359 0.2742 0.0288  0.0222  0.0493  255 LEU A C   
1993 O O   . LEU A 261 ? 0.2702 0.2567 0.2960 0.0274  0.0280  0.0559  255 LEU A O   
1994 C CB  . LEU A 261 ? 0.3028 0.2980 0.3091 0.0339  0.0148  0.0385  255 LEU A CB  
1995 C CG  . LEU A 261 ? 0.2863 0.2868 0.2904 0.0331  0.0124  0.0309  255 LEU A CG  
1996 C CD1 . LEU A 261 ? 0.3790 0.3826 0.3787 0.0371  0.0076  0.0272  255 LEU A CD1 
1997 C CD2 . LEU A 261 ? 0.2834 0.2891 0.2850 0.0330  0.0160  0.0324  255 LEU A CD2 
1998 N N   . SER A 262 ? 0.2321 0.2082 0.2558 0.0316  0.0210  0.0516  256 SER A N   
1999 C CA  . SER A 262 ? 0.2562 0.2244 0.2837 0.0334  0.0261  0.0632  256 SER A CA  
2000 C C   . SER A 262 ? 0.3044 0.2667 0.3497 0.0255  0.0308  0.0647  256 SER A C   
2001 O O   . SER A 262 ? 0.3240 0.2846 0.3750 0.0248  0.0386  0.0761  256 SER A O   
2002 C CB  . SER A 262 ? 0.3283 0.2882 0.3573 0.0384  0.0232  0.0644  256 SER A CB  
2003 O OG  . SER A 262 ? 0.4333 0.4009 0.4510 0.0454  0.0175  0.0628  256 SER A OG  
2004 N N   . ILE A 263 ? 0.2679 0.2279 0.3226 0.0198  0.0262  0.0532  257 ILE A N   
2005 C CA  . ILE A 263 ? 0.2522 0.2081 0.3266 0.0117  0.0272  0.0511  257 ILE A CA  
2006 C C   . ILE A 263 ? 0.2623 0.2310 0.3425 0.0080  0.0298  0.0531  257 ILE A C   
2007 O O   . ILE A 263 ? 0.3091 0.2779 0.4077 0.0032  0.0359  0.0602  257 ILE A O   
2008 C CB  . ILE A 263 ? 0.2756 0.2256 0.3532 0.0087  0.0194  0.0362  257 ILE A CB  
2009 C CG1 . ILE A 263 ? 0.2873 0.2232 0.3646 0.0125  0.0194  0.0350  257 ILE A CG1 
2010 C CG2 . ILE A 263 ? 0.3197 0.2690 0.4176 0.0001  0.0163  0.0304  257 ILE A CG2 
2011 C CD1 . ILE A 263 ? 0.2818 0.2110 0.3564 0.0124  0.0136  0.0200  257 ILE A CD1 
2012 N N   . ALA A 264 ? 0.2327 0.2121 0.3008 0.0102  0.0259  0.0470  258 ALA A N   
2013 C CA  . ALA A 264 ? 0.2143 0.2061 0.2890 0.0081  0.0280  0.0479  258 ALA A CA  
2014 C C   . ALA A 264 ? 0.2762 0.2724 0.3511 0.0108  0.0393  0.0612  258 ALA A C   
2015 O O   . ALA A 264 ? 0.2909 0.2942 0.3833 0.0071  0.0453  0.0657  258 ALA A O   
2016 C CB  . ALA A 264 ? 0.2314 0.2308 0.2911 0.0119  0.0230  0.0406  258 ALA A CB  
2017 N N   . LEU A 265 ? 0.2782 0.2707 0.3337 0.0181  0.0423  0.0677  259 LEU A N   
2018 C CA  . LEU A 265 ? 0.3011 0.2969 0.3487 0.0233  0.0532  0.0806  259 LEU A CA  
2019 C C   . LEU A 265 ? 0.3762 0.3647 0.4409 0.0200  0.0633  0.0939  259 LEU A C   
2020 O O   . LEU A 265 ? 0.4050 0.3970 0.4667 0.0237  0.0756  0.1066  259 LEU A O   
2021 C CB  . LEU A 265 ? 0.3344 0.3285 0.3542 0.0333  0.0506  0.0823  259 LEU A CB  
2022 C CG  . LEU A 265 ? 0.3742 0.3760 0.3801 0.0364  0.0430  0.0704  259 LEU A CG  
2023 C CD1 . LEU A 265 ? 0.4083 0.4089 0.3921 0.0450  0.0374  0.0697  259 LEU A CD1 
2024 C CD2 . LEU A 265 ? 0.4845 0.4963 0.4899 0.0375  0.0495  0.0704  259 LEU A CD2 
2025 N N   . LYS A 266 ? 0.3566 0.3342 0.4395 0.0136  0.0596  0.0916  260 LYS A N   
2026 C CA  . LYS A 266 ? 0.4031 0.3716 0.5083 0.0090  0.0693  0.1038  260 LYS A CA  
2027 C C   . LYS A 266 ? 0.4028 0.3767 0.5429 -0.0023 0.0707  0.1000  260 LYS A C   
2028 O O   . LYS A 266 ? 0.4945 0.4627 0.6597 -0.0077 0.0806  0.1108  260 LYS A O   
2029 C CB  . LYS A 266 ? 0.4701 0.4208 0.5776 0.0093  0.0650  0.1036  260 LYS A CB  
2030 C CG  . LYS A 266 ? 0.4625 0.4084 0.5420 0.0212  0.0650  0.1117  260 LYS A CG  
2031 C CD  . LYS A 266 ? 0.5614 0.4896 0.6478 0.0226  0.0629  0.1143  260 LYS A CD  
2032 N N   . GLN A 267 ? 0.3576 0.2701 0.4094 -0.0121 0.0119  0.1316  261 GLN A N   
2033 C CA  . GLN A 267 ? 0.4267 0.3397 0.4895 -0.0255 0.0138  0.1238  261 GLN A CA  
2034 C C   . GLN A 267 ? 0.4247 0.3742 0.4805 -0.0305 0.0192  0.1348  261 GLN A C   
2035 O O   . GLN A 267 ? 0.4983 0.4730 0.5324 -0.0213 0.0211  0.1359  261 GLN A O   
2036 C CB  . GLN A 267 ? 0.4455 0.3529 0.5010 -0.0239 0.0105  0.0945  261 GLN A CB  
2037 C CG  . GLN A 267 ? 0.4834 0.3621 0.5417 -0.0173 0.0075  0.0802  261 GLN A CG  
2038 C CD  . GLN A 267 ? 0.5349 0.3815 0.6179 -0.0240 0.0067  0.0836  261 GLN A CD  
2039 O OE1 . GLN A 267 ? 0.4887 0.3278 0.5854 -0.0378 0.0056  0.0807  261 GLN A OE1 
2040 N NE2 . GLN A 267 ? 0.5938 0.4260 0.6799 -0.0139 0.0060  0.0861  261 GLN A NE2 
2041 N N   . GLU A 268 ? 0.3229 0.2764 0.3985 -0.0454 0.0219  0.1411  262 GLU A N   
2042 C CA  . GLU A 268 ? 0.3469 0.3390 0.4214 -0.0506 0.0281  0.1461  262 GLU A CA  
2043 C C   . GLU A 268 ? 0.4445 0.4442 0.5161 -0.0493 0.0241  0.1198  262 GLU A C   
2044 O O   . GLU A 268 ? 0.5998 0.5824 0.6875 -0.0589 0.0187  0.1079  262 GLU A O   
2045 C CB  . GLU A 268 ? 0.4089 0.4062 0.5104 -0.0688 0.0328  0.1672  262 GLU A CB  
2046 C CG  . GLU A 268 ? 0.4974 0.4920 0.5940 -0.0664 0.0348  0.1861  262 GLU A CG  
2047 C CD  . GLU A 268 ? 0.5895 0.5942 0.7063 -0.0819 0.0392  0.2008  262 GLU A CD  
2048 O OE1 . GLU A 268 ? 0.7107 0.7292 0.8205 -0.0808 0.0438  0.2197  262 GLU A OE1 
2049 O OE2 . GLU A 268 ? 0.6002 0.6000 0.7397 -0.0956 0.0372  0.1930  262 GLU A OE2 
2050 N N   . TRP A 269 ? 0.3215 0.3455 0.3722 -0.0372 0.0257  0.1106  263 TRP A N   
2051 C CA  . TRP A 269 ? 0.2656 0.2956 0.3120 -0.0334 0.0207  0.0883  263 TRP A CA  
2052 C C   . TRP A 269 ? 0.2962 0.3636 0.3558 -0.0380 0.0256  0.0917  263 TRP A C   
2053 O O   . TRP A 269 ? 0.3651 0.4620 0.4211 -0.0347 0.0348  0.1049  263 TRP A O   
2054 C CB  . TRP A 269 ? 0.3057 0.3346 0.3245 -0.0171 0.0181  0.0754  263 TRP A CB  
2055 C CG  . TRP A 269 ? 0.2765 0.2742 0.2871 -0.0133 0.0137  0.0714  263 TRP A CG  
2056 C CD1 . TRP A 269 ? 0.3346 0.3273 0.3366 -0.0074 0.0148  0.0824  263 TRP A CD1 
2057 C CD2 . TRP A 269 ? 0.2700 0.2413 0.2819 -0.0148 0.0077  0.0558  263 TRP A CD2 
2058 N NE1 . TRP A 269 ? 0.3038 0.2698 0.3054 -0.0044 0.0103  0.0744  263 TRP A NE1 
2059 C CE2 . TRP A 269 ? 0.2661 0.2188 0.2726 -0.0088 0.0070  0.0575  263 TRP A CE2 
2060 C CE3 . TRP A 269 ? 0.2856 0.2504 0.3016 -0.0202 0.0026  0.0404  263 TRP A CE3 
2061 C CZ2 . TRP A 269 ? 0.2653 0.1943 0.2714 -0.0077 0.0039  0.0438  263 TRP A CZ2 
2062 C CZ3 . TRP A 269 ? 0.2900 0.2297 0.3011 -0.0198 -0.0012 0.0269  263 TRP A CZ3 
2063 C CH2 . TRP A 269 ? 0.3252 0.2478 0.3318 -0.0133 0.0006  0.0283  263 TRP A CH2 
2064 N N   . LYS A 270 ? 0.2713 0.3404 0.3472 -0.0457 0.0195  0.0802  264 LYS A N   
2065 C CA  . LYS A 270 ? 0.3184 0.4268 0.4122 -0.0492 0.0227  0.0822  264 LYS A CA  
2066 C C   . LYS A 270 ? 0.2736 0.3998 0.3533 -0.0325 0.0201  0.0664  264 LYS A C   
2067 O O   . LYS A 270 ? 0.3603 0.5230 0.4548 -0.0305 0.0235  0.0669  264 LYS A O   
2068 C CB  . LYS A 270 ? 0.4497 0.5550 0.5728 -0.0675 0.0153  0.0792  264 LYS A CB  
2069 N N   . LYS A 271 ? 0.2451 0.3466 0.2995 -0.0208 0.0143  0.0535  265 LYS A N   
2070 C CA  . LYS A 271 ? 0.2503 0.3581 0.2888 -0.0046 0.0105  0.0396  265 LYS A CA  
2071 C C   . LYS A 271 ? 0.2767 0.3694 0.2877 0.0069  0.0128  0.0379  265 LYS A C   
2072 O O   . LYS A 271 ? 0.2986 0.3718 0.3033 0.0023  0.0141  0.0451  265 LYS A O   
2073 C CB  . LYS A 271 ? 0.2576 0.3458 0.2938 -0.0057 -0.0023 0.0252  265 LYS A CB  
2074 C CG  . LYS A 271 ? 0.2774 0.3823 0.3390 -0.0166 -0.0086 0.0237  265 LYS A CG  
2075 C CD  . LYS A 271 ? 0.2811 0.3677 0.3323 -0.0156 -0.0222 0.0098  265 LYS A CD  
2076 C CE  . LYS A 271 ? 0.4004 0.5046 0.4747 -0.0267 -0.0317 0.0068  265 LYS A CE  
2077 N NZ  . LYS A 271 ? 0.4716 0.5638 0.5303 -0.0224 -0.0455 -0.0051 265 LYS A NZ  
2078 N N   . PRO A 272 ? 0.2618 0.3625 0.2579 0.0221  0.0123  0.0280  266 PRO A N   
2079 C CA  . PRO A 272 ? 0.2516 0.3341 0.2221 0.0310  0.0109  0.0232  266 PRO A CA  
2080 C C   . PRO A 272 ? 0.2618 0.3095 0.2258 0.0256  0.0030  0.0189  266 PRO A C   
2081 O O   . PRO A 272 ? 0.2948 0.3310 0.2645 0.0213  -0.0035 0.0125  266 PRO A O   
2082 C CB  . PRO A 272 ? 0.3239 0.4142 0.2848 0.0466  0.0084  0.0094  266 PRO A CB  
2083 C CG  . PRO A 272 ? 0.3700 0.4781 0.3519 0.0469  0.0063  0.0068  266 PRO A CG  
2084 C CD  . PRO A 272 ? 0.3037 0.4303 0.3081 0.0323  0.0122  0.0205  266 PRO A CD  
2085 N N   . LEU A 273 ? 0.2495 0.2838 0.2016 0.0259  0.0038  0.0228  267 LEU A N   
2086 C CA  . LEU A 273 ? 0.2823 0.2887 0.2310 0.0217  -0.0011 0.0198  267 LEU A CA  
2087 C C   . LEU A 273 ? 0.2534 0.2473 0.1848 0.0292  -0.0068 0.0089  267 LEU A C   
2088 O O   . LEU A 273 ? 0.2716 0.2719 0.1909 0.0364  -0.0069 0.0075  267 LEU A O   
2089 C CB  . LEU A 273 ? 0.3133 0.3143 0.2652 0.0180  0.0025  0.0324  267 LEU A CB  
2090 C CG  . LEU A 273 ? 0.2656 0.2432 0.2149 0.0175  -0.0010 0.0291  267 LEU A CG  
2091 C CD1 . LEU A 273 ? 0.2766 0.2366 0.2356 0.0104  -0.0026 0.0217  267 LEU A CD1 
2092 C CD2 . LEU A 273 ? 0.3377 0.3151 0.2911 0.0178  0.0014  0.0436  267 LEU A CD2 
2093 N N   . LEU A 274 ? 0.2338 0.2103 0.1634 0.0264  -0.0120 0.0014  268 LEU A N   
2094 C CA  . LEU A 274 ? 0.2452 0.2065 0.1614 0.0296  -0.0169 -0.0055 268 LEU A CA  
2095 C C   . LEU A 274 ? 0.2335 0.1811 0.1520 0.0237  -0.0154 -0.0036 268 LEU A C   
2096 O O   . LEU A 274 ? 0.2709 0.2103 0.1943 0.0180  -0.0146 -0.0056 268 LEU A O   
2097 C CB  . LEU A 274 ? 0.2681 0.2222 0.1794 0.0313  -0.0230 -0.0126 268 LEU A CB  
2098 C CG  . LEU A 274 ? 0.2501 0.1870 0.1491 0.0324  -0.0282 -0.0169 268 LEU A CG  
2099 C CD1 . LEU A 274 ? 0.2602 0.1989 0.1524 0.0398  -0.0300 -0.0204 268 LEU A CD1 
2100 C CD2 . LEU A 274 ? 0.2841 0.2123 0.1783 0.0331  -0.0347 -0.0196 268 LEU A CD2 
2101 N N   . TYR A 275 ? 0.2462 0.1934 0.1616 0.0259  -0.0155 -0.0010 269 TYR A N   
2102 C CA  . TYR A 275 ? 0.2452 0.1839 0.1659 0.0230  -0.0140 0.0006  269 TYR A CA  
2103 C C   . TYR A 275 ? 0.2612 0.1912 0.1739 0.0214  -0.0174 -0.0060 269 TYR A C   
2104 O O   . TYR A 275 ? 0.2923 0.2228 0.1967 0.0238  -0.0226 -0.0087 269 TYR A O   
2105 C CB  . TYR A 275 ? 0.2513 0.1989 0.1761 0.0261  -0.0138 0.0092  269 TYR A CB  
2106 C CG  . TYR A 275 ? 0.2476 0.1891 0.1850 0.0251  -0.0113 0.0120  269 TYR A CG  
2107 C CD1 . TYR A 275 ? 0.2564 0.1962 0.1942 0.0244  -0.0130 0.0074  269 TYR A CD1 
2108 C CD2 . TYR A 275 ? 0.2557 0.1929 0.2071 0.0248  -0.0070 0.0190  269 TYR A CD2 
2109 C CE1 . TYR A 275 ? 0.2341 0.1724 0.1865 0.0252  -0.0090 0.0088  269 TYR A CE1 
2110 C CE2 . TYR A 275 ? 0.2583 0.1885 0.2236 0.0266  -0.0042 0.0194  269 TYR A CE2 
2111 C CZ  . TYR A 275 ? 0.2452 0.1780 0.2109 0.0276  -0.0046 0.0137  269 TYR A CZ  
2112 O OH  . TYR A 275 ? 0.2518 0.1821 0.2339 0.0312  -0.0003 0.0131  269 TYR A OH  
2113 N N   . ILE A 276 ? 0.2516 0.1733 0.1664 0.0170  -0.0143 -0.0087 270 ILE A N   
2114 C CA  . ILE A 276 ? 0.2676 0.1834 0.1753 0.0136  -0.0160 -0.0117 270 ILE A CA  
2115 C C   . ILE A 276 ? 0.2502 0.1718 0.1677 0.0128  -0.0140 -0.0091 270 ILE A C   
2116 O O   . ILE A 276 ? 0.2537 0.1783 0.1827 0.0136  -0.0078 -0.0083 270 ILE A O   
2117 C CB  . ILE A 276 ? 0.2746 0.1835 0.1759 0.0090  -0.0127 -0.0155 270 ILE A CB  
2118 C CG1 . ILE A 276 ? 0.2683 0.1755 0.1640 0.0093  -0.0161 -0.0179 270 ILE A CG1 
2119 C CG2 . ILE A 276 ? 0.3028 0.2066 0.1945 0.0042  -0.0145 -0.0146 270 ILE A CG2 
2120 C CD1 . ILE A 276 ? 0.2816 0.1886 0.1706 0.0134  -0.0240 -0.0169 270 ILE A CD1 
2121 N N   . HIS A 277 ? 0.2428 0.1664 0.1582 0.0117  -0.0202 -0.0086 271 HIS A N   
2122 C CA  . HIS A 277 ? 0.2337 0.1669 0.1614 0.0094  -0.0202 -0.0060 271 HIS A CA  
2123 C C   . HIS A 277 ? 0.2694 0.2025 0.2014 0.0034  -0.0130 -0.0064 271 HIS A C   
2124 O O   . HIS A 277 ? 0.2803 0.2040 0.2008 -0.0022 -0.0134 -0.0073 271 HIS A O   
2125 C CB  . HIS A 277 ? 0.2659 0.1997 0.1896 0.0070  -0.0304 -0.0077 271 HIS A CB  
2126 C CG  . HIS A 277 ? 0.2450 0.1946 0.1832 0.0057  -0.0341 -0.0046 271 HIS A CG  
2127 N ND1 . HIS A 277 ? 0.2403 0.2005 0.1959 0.0014  -0.0292 -0.0014 271 HIS A ND1 
2128 C CD2 . HIS A 277 ? 0.2553 0.2151 0.1930 0.0085  -0.0429 -0.0045 271 HIS A CD2 
2129 C CE1 . HIS A 277 ? 0.2453 0.2222 0.2142 0.0016  -0.0358 0.0014  271 HIS A CE1 
2130 N NE2 . HIS A 277 ? 0.2649 0.2411 0.2214 0.0054  -0.0450 -0.0004 271 HIS A NE2 
2131 N N   . GLN A 278 ? 0.2255 0.1701 0.1741 0.0054  -0.0060 -0.0049 272 GLN A N   
2132 C CA  . GLN A 278 ? 0.2381 0.1880 0.1911 0.0014  0.0038  -0.0066 272 GLN A CA  
2133 C C   . GLN A 278 ? 0.2487 0.2123 0.2135 -0.0061 0.0032  -0.0024 272 GLN A C   
2134 O O   . GLN A 278 ? 0.2335 0.2056 0.2017 -0.0110 0.0128  -0.0021 272 GLN A O   
2135 C CB  . GLN A 278 ? 0.2401 0.1955 0.2075 0.0093  0.0136  -0.0097 272 GLN A CB  
2136 C CG  . GLN A 278 ? 0.2354 0.1756 0.1939 0.0135  0.0148  -0.0146 272 GLN A CG  
2137 C CD  . GLN A 278 ? 0.2724 0.2020 0.2080 0.0074  0.0145  -0.0191 272 GLN A CD  
2138 O OE1 . GLN A 278 ? 0.2941 0.2261 0.2219 0.0036  0.0216  -0.0231 272 GLN A OE1 
2139 N NE2 . GLN A 278 ? 0.3006 0.2215 0.2252 0.0068  0.0062  -0.0175 272 GLN A NE2 
2140 N N   . GLY A 279 ? 0.2501 0.2177 0.2208 -0.0082 -0.0078 0.0003  273 GLY A N   
2141 C CA  . GLY A 279 ? 0.2616 0.2437 0.2477 -0.0174 -0.0103 0.0040  273 GLY A CA  
2142 C C   . GLY A 279 ? 0.2612 0.2692 0.2743 -0.0136 -0.0016 0.0063  273 GLY A C   
2143 O O   . GLY A 279 ? 0.2328 0.2466 0.2561 -0.0019 0.0004  0.0060  273 GLY A O   
2144 N N   . GLY A 280 ? 0.2592 0.2836 0.2866 -0.0235 0.0036  0.0098  274 GLY A N   
2145 C CA  . GLY A 280 ? 0.2662 0.3205 0.3232 -0.0193 0.0136  0.0116  274 GLY A CA  
2146 C C   . GLY A 280 ? 0.2656 0.3411 0.3492 -0.0142 0.0031  0.0150  274 GLY A C   
2147 O O   . GLY A 280 ? 0.2999 0.3968 0.4087 -0.0037 0.0100  0.0160  274 GLY A O   
2148 N N   . ILE A 281 ? 0.2783 0.3490 0.3568 -0.0205 -0.0140 0.0162  275 ILE A N   
2149 C CA  . ILE A 281 ? 0.3232 0.4153 0.4224 -0.0146 -0.0260 0.0196  275 ILE A CA  
2150 C C   . ILE A 281 ? 0.2759 0.4044 0.4120 -0.0217 -0.0256 0.0243  275 ILE A C   
2151 O O   . ILE A 281 ? 0.2684 0.4223 0.4293 -0.0141 -0.0330 0.0286  275 ILE A O   
2152 C CB  . ILE A 281 ? 0.3729 0.4522 0.4526 -0.0181 -0.0448 0.0171  275 ILE A CB  
2153 C CG1 . ILE A 281 ? 0.4550 0.5319 0.5346 -0.0364 -0.0543 0.0141  275 ILE A CG1 
2154 C CG2 . ILE A 281 ? 0.3309 0.3795 0.3774 -0.0111 -0.0434 0.0129  275 ILE A CG2 
2155 C CD1 . ILE A 281 ? 0.5158 0.5825 0.5779 -0.0387 -0.0736 0.0077  275 ILE A CD1 
2156 N N   . LEU A 282 ? 0.2560 0.3903 0.3982 -0.0364 -0.0174 0.0254  276 LEU A N   
2157 C CA  . LEU A 282 ? 0.2634 0.4380 0.4454 -0.0436 -0.0141 0.0309  276 LEU A CA  
2158 C C   . LEU A 282 ? 0.2394 0.4400 0.4469 -0.0266 0.0021  0.0317  276 LEU A C   
2159 O O   . LEU A 282 ? 0.3073 0.5476 0.5545 -0.0255 0.0025  0.0363  276 LEU A O   
2160 C CB  . LEU A 282 ? 0.3756 0.5508 0.5580 -0.0646 -0.0068 0.0346  276 LEU A CB  
2161 N N   . GLY A 283 ? 0.3199 0.4992 0.5078 -0.0128 0.0146  0.0264  277 GLY A N   
2162 C CA  . GLY A 283 ? 0.3424 0.5389 0.5533 0.0061  0.0280  0.0241  277 GLY A CA  
2163 C C   . GLY A 283 ? 0.3672 0.5698 0.5962 0.0227  0.0156  0.0280  277 GLY A C   
2164 O O   . GLY A 283 ? 0.4061 0.6226 0.6602 0.0401  0.0246  0.0272  277 GLY A O   
2165 N N   . ASN A 284 ? 0.2607 0.4531 0.4769 0.0186  -0.0050 0.0325  278 ASN A N   
2166 C CA  . ASN A 284 ? 0.2296 0.4283 0.4584 0.0338  -0.0176 0.0395  278 ASN A CA  
2167 C C   . ASN A 284 ? 0.3040 0.5483 0.5792 0.0385  -0.0237 0.0469  278 ASN A C   
2168 O O   . ASN A 284 ? 0.2777 0.5310 0.5692 0.0544  -0.0325 0.0549  278 ASN A O   
2169 C CB  . ASN A 284 ? 0.2088 0.3887 0.4073 0.0279  -0.0369 0.0418  278 ASN A CB  
2170 C CG  . ASN A 284 ? 0.2296 0.3704 0.3923 0.0329  -0.0324 0.0384  278 ASN A CG  
2171 O OD1 . ASN A 284 ? 0.2407 0.3679 0.4045 0.0429  -0.0182 0.0358  278 ASN A OD1 
2172 N ND2 . ASN A 284 ? 0.2233 0.3470 0.3553 0.0259  -0.0444 0.0372  278 ASN A ND2 
2173 N N   . SER A 285 ? 0.3614 0.6359 0.6597 0.0247  -0.0199 0.0462  279 SER A N   
2174 C CA  . SER A 285 ? 0.3541 0.6784 0.7021 0.0282  -0.0256 0.0533  279 SER A CA  
2175 C C   . SER A 285 ? 0.3178 0.6560 0.6964 0.0544  -0.0146 0.0555  279 SER A C   
2176 O O   . SER A 285 ? 0.3666 0.7235 0.7682 0.0671  -0.0279 0.0632  279 SER A O   
2177 C CB  . SER A 285 ? 0.3699 0.7248 0.7410 0.0092  -0.0159 0.0523  279 SER A CB  
2178 N N   . THR A 286 ? 0.3247 0.6476 0.6970 0.0629  0.0089  0.0465  280 THR A N   
2179 C CA  . THR A 286 ? 0.3808 0.7143 0.7837 0.0884  0.0213  0.0446  280 THR A CA  
2180 C C   . THR A 286 ? 0.3637 0.6626 0.7512 0.1054  0.0094  0.0488  280 THR A C   
2181 O O   . THR A 286 ? 0.3893 0.6951 0.7941 0.1206  0.0029  0.0518  280 THR A O   
2182 C CB  . THR A 286 ? 0.4498 0.7736 0.8437 0.0918  0.0491  0.0303  280 THR A CB  
2183 N N   . MET A 287 ? 0.3417 0.5991 0.6892 0.1003  0.0057  0.0484  281 MET A N   
2184 C CA  . MET A 287 ? 0.3390 0.5670 0.6766 0.1150  -0.0038 0.0561  281 MET A CA  
2185 C C   . MET A 287 ? 0.3316 0.5734 0.6704 0.1147  -0.0277 0.0699  281 MET A C   
2186 O O   . MET A 287 ? 0.3103 0.5428 0.6528 0.1287  -0.0340 0.0760  281 MET A O   
2187 C CB  . MET A 287 ? 0.3411 0.5228 0.6298 0.1057  -0.0027 0.0512  281 MET A CB  
2188 C CG  . MET A 287 ? 0.4130 0.5640 0.6908 0.1124  0.0166  0.0374  281 MET A CG  
2189 S SD  . MET A 287 ? 0.4180 0.5593 0.7241 0.1377  0.0238  0.0347  281 MET A SD  
2190 C CE  . MET A 287 ? 0.5015 0.6271 0.7998 0.1428  0.0010  0.0546  281 MET A CE  
2191 N N   . LEU A 288 ? 0.3219 0.5843 0.6552 0.0980  -0.0419 0.0740  282 LEU A N   
2192 C CA  . LEU A 288 ? 0.2953 0.5693 0.6225 0.0967  -0.0648 0.0836  282 LEU A CA  
2193 C C   . LEU A 288 ? 0.4058 0.7076 0.7672 0.1089  -0.0685 0.0868  282 LEU A C   
2194 O O   . LEU A 288 ? 0.4046 0.7055 0.7611 0.1170  -0.0833 0.0963  282 LEU A O   
2195 C CB  . LEU A 288 ? 0.2873 0.5781 0.6031 0.0752  -0.0791 0.0818  282 LEU A CB  
2196 C CG  . LEU A 288 ? 0.3918 0.6493 0.6622 0.0640  -0.0816 0.0779  282 LEU A CG  
2197 C CD1 . LEU A 288 ? 0.4322 0.6952 0.6904 0.0407  -0.0876 0.0678  282 LEU A CD1 
2198 C CD2 . LEU A 288 ? 0.4258 0.6689 0.6674 0.0703  -0.0968 0.0871  282 LEU A CD2 
2199 N N   . GLU A 289 ? 0.3570 0.6854 0.7526 0.1108  -0.0546 0.0793  283 GLU A N   
2200 C CA  . GLU A 289 ? 0.3413 0.6968 0.7722 0.1254  -0.0563 0.0811  283 GLU A CA  
2201 C C   . GLU A 289 ? 0.3927 0.7193 0.8207 0.1478  -0.0540 0.0850  283 GLU A C   
2202 O O   . GLU A 289 ? 0.4247 0.7624 0.8678 0.1602  -0.0661 0.0934  283 GLU A O   
2203 C CB  . GLU A 289 ? 0.3125 0.7000 0.7772 0.1242  -0.0375 0.0705  283 GLU A CB  
2204 N N   . ARG A 290 ? 0.3548 0.6430 0.7635 0.1524  -0.0394 0.0792  284 ARG A N   
2205 C CA  . ARG A 290 ? 0.3857 0.6410 0.7902 0.1706  -0.0379 0.0823  284 ARG A CA  
2206 C C   . ARG A 290 ? 0.4175 0.6501 0.7953 0.1695  -0.0560 0.0984  284 ARG A C   
2207 O O   . ARG A 290 ? 0.5122 0.7208 0.8893 0.1830  -0.0580 0.1052  284 ARG A O   
2208 C CB  . ARG A 290 ? 0.4340 0.6536 0.8238 0.1730  -0.0182 0.0691  284 ARG A CB  
2209 C CG  . ARG A 290 ? 0.4555 0.6921 0.8697 0.1816  0.0017  0.0524  284 ARG A CG  
2210 C CD  . ARG A 290 ? 0.4969 0.7060 0.8882 0.1759  0.0201  0.0373  284 ARG A CD  
2211 N NE  . ARG A 290 ? 0.5488 0.7724 0.9564 0.1852  0.0401  0.0197  284 ARG A NE  
2212 C CZ  . ARG A 290 ? 0.5408 0.7594 0.9327 0.1779  0.0585  0.0045  284 ARG A CZ  
2213 N NH1 . ARG A 290 ? 0.5611 0.7965 0.9643 0.1874  0.0764  -0.0114 284 ARG A NH1 
2214 N NH2 . ARG A 290 ? 0.5076 0.7063 0.8709 0.1616  0.0589  0.0052  284 ARG A NH2 
2215 N N   . TYR A 291 ? 0.3574 0.5968 0.7120 0.1534  -0.0686 0.1041  285 TYR A N   
2216 C CA  . TYR A 291 ? 0.3851 0.6068 0.7092 0.1511  -0.0840 0.1180  285 TYR A CA  
2217 C C   . TYR A 291 ? 0.4754 0.7277 0.8091 0.1533  -0.1040 0.1283  285 TYR A C   
2218 O O   . TYR A 291 ? 0.5343 0.7752 0.8552 0.1600  -0.1148 0.1419  285 TYR A O   
2219 C CB  . TYR A 291 ? 0.3411 0.5494 0.6279 0.1337  -0.0856 0.1156  285 TYR A CB  
2220 C CG  . TYR A 291 ? 0.3465 0.5146 0.6135 0.1336  -0.0715 0.1119  285 TYR A CG  
2221 C CD1 . TYR A 291 ? 0.3309 0.4684 0.5794 0.1386  -0.0730 0.1220  285 TYR A CD1 
2222 C CD2 . TYR A 291 ? 0.3356 0.4974 0.6032 0.1275  -0.0567 0.0986  285 TYR A CD2 
2223 C CE1 . TYR A 291 ? 0.2793 0.3812 0.5114 0.1365  -0.0612 0.1179  285 TYR A CE1 
2224 C CE2 . TYR A 291 ? 0.3637 0.4887 0.6127 0.1271  -0.0450 0.0940  285 TYR A CE2 
2225 C CZ  . TYR A 291 ? 0.2566 0.3521 0.4889 0.1312  -0.0478 0.1031  285 TYR A CZ  
2226 O OH  . TYR A 291 ? 0.2571 0.3176 0.4730 0.1286  -0.0375 0.0981  285 TYR A OH  
# 
