data_9DGW
# 
_entry.id   9DGW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DGW         pdb_00009dgw 10.2210/pdb9dgw/pdb 
WWPDB D_1000288016 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-12 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DGW 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9DFW unspecified 
PDB . 9DFN unspecified 
PDB . 9DFU unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tyler.grove@einsteinmed.edu 
_pdbx_contact_author.name_first         Tyler 
_pdbx_contact_author.name_last          Grove 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4763-0646 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lachowicz, J.C.' 1 ? 
'Bonanno, J.B.'   2 ? 
'Grove, T.L.'     3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structural Insights from Active Site Variants and B-8 Loop Interactions in Viperin-like Enzymes' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lachowicz, J.C.' 1 ? 
primary 'Grudman, S.'     2 ? 
primary 'Bonanno, J.B.'   3 ? 
primary 'Fiser, A.'       4 ? 
primary 'Grove, T.L.'     5 ? 
# 
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 'Radical SAM core domain-containing protein' 36192.859 3   ? ? ? ? 
2 non-polymer syn "CYTIDINE-5'-TRIPHOSPHATE"                   483.156   3   ? ? ? ? 
3 non-polymer syn 'IRON/SULFUR CLUSTER'                        351.640   3   ? ? ? ? 
4 non-polymer syn S-ADENOSYLMETHIONINE                         398.437   3   ? ? ? ? 
5 water       nat water                                        18.015    299 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MHHHHHHSSGVDLGTENLYFQSMGQVPVSVNYHFSRKCNKECLFCFHTATTSHVEKPENAKRGLTLLKQAGMKKINFAGG
EPFLYPKFLGEMIDFCKETLQLESVSIVTNGSLVKEQFLQKHGRNIDILAVSCDSFNEATNIKIGRGSGDNVQKLYEIGS
WCQKYDIKFKLNTVVNKFNHLEDMNDHLNALQPFRWKCFQVLIVTGENDSDKTLRNAHSLTISDDEFDRFCERHSSQTCL
VPEPNRLMAKSYLILDEYMRFLDRNGQQPSKSILEVGVQQALQAVFWDEEAFVERGGIYDWNKSSCSSDSKDLEW
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHSSGVDLGTENLYFQSMGQVPVSVNYHFSRKCNKECLFCFHTATTSHVEKPENAKRGLTLLKQAGMKKINFAGG
EPFLYPKFLGEMIDFCKETLQLESVSIVTNGSLVKEQFLQKHGRNIDILAVSCDSFNEATNIKIGRGSGDNVQKLYEIGS
WCQKYDIKFKLNTVVNKFNHLEDMNDHLNALQPFRWKCFQVLIVTGENDSDKTLRNAHSLTISDDEFDRFCERHSSQTCL
VPEPNRLMAKSYLILDEYMRFLDRNGQQPSKSILEVGVQQALQAVFWDEEAFVERGGIYDWNKSSCSSDSKDLEW
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "CYTIDINE-5'-TRIPHOSPHATE" CTP 
3 'IRON/SULFUR CLUSTER'      SF4 
4 S-ADENOSYLMETHIONINE       SAM 
5 water                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   SER n 
1 9   SER n 
1 10  GLY n 
1 11  VAL n 
1 12  ASP n 
1 13  LEU n 
1 14  GLY n 
1 15  THR n 
1 16  GLU n 
1 17  ASN n 
1 18  LEU n 
1 19  TYR n 
1 20  PHE n 
1 21  GLN n 
1 22  SER n 
1 23  MET n 
1 24  GLY n 
1 25  GLN n 
1 26  VAL n 
1 27  PRO n 
1 28  VAL n 
1 29  SER n 
1 30  VAL n 
1 31  ASN n 
1 32  TYR n 
1 33  HIS n 
1 34  PHE n 
1 35  SER n 
1 36  ARG n 
1 37  LYS n 
1 38  CYS n 
1 39  ASN n 
1 40  LYS n 
1 41  GLU n 
1 42  CYS n 
1 43  LEU n 
1 44  PHE n 
1 45  CYS n 
1 46  PHE n 
1 47  HIS n 
1 48  THR n 
1 49  ALA n 
1 50  THR n 
1 51  THR n 
1 52  SER n 
1 53  HIS n 
1 54  VAL n 
1 55  GLU n 
1 56  LYS n 
1 57  PRO n 
1 58  GLU n 
1 59  ASN n 
1 60  ALA n 
1 61  LYS n 
1 62  ARG n 
1 63  GLY n 
1 64  LEU n 
1 65  THR n 
1 66  LEU n 
1 67  LEU n 
1 68  LYS n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  MET n 
1 73  LYS n 
1 74  LYS n 
1 75  ILE n 
1 76  ASN n 
1 77  PHE n 
1 78  ALA n 
1 79  GLY n 
1 80  GLY n 
1 81  GLU n 
1 82  PRO n 
1 83  PHE n 
1 84  LEU n 
1 85  TYR n 
1 86  PRO n 
1 87  LYS n 
1 88  PHE n 
1 89  LEU n 
1 90  GLY n 
1 91  GLU n 
1 92  MET n 
1 93  ILE n 
1 94  ASP n 
1 95  PHE n 
1 96  CYS n 
1 97  LYS n 
1 98  GLU n 
1 99  THR n 
1 100 LEU n 
1 101 GLN n 
1 102 LEU n 
1 103 GLU n 
1 104 SER n 
1 105 VAL n 
1 106 SER n 
1 107 ILE n 
1 108 VAL n 
1 109 THR n 
1 110 ASN n 
1 111 GLY n 
1 112 SER n 
1 113 LEU n 
1 114 VAL n 
1 115 LYS n 
1 116 GLU n 
1 117 GLN n 
1 118 PHE n 
1 119 LEU n 
1 120 GLN n 
1 121 LYS n 
1 122 HIS n 
1 123 GLY n 
1 124 ARG n 
1 125 ASN n 
1 126 ILE n 
1 127 ASP n 
1 128 ILE n 
1 129 LEU n 
1 130 ALA n 
1 131 VAL n 
1 132 SER n 
1 133 CYS n 
1 134 ASP n 
1 135 SER n 
1 136 PHE n 
1 137 ASN n 
1 138 GLU n 
1 139 ALA n 
1 140 THR n 
1 141 ASN n 
1 142 ILE n 
1 143 LYS n 
1 144 ILE n 
1 145 GLY n 
1 146 ARG n 
1 147 GLY n 
1 148 SER n 
1 149 GLY n 
1 150 ASP n 
1 151 ASN n 
1 152 VAL n 
1 153 GLN n 
1 154 LYS n 
1 155 LEU n 
1 156 TYR n 
1 157 GLU n 
1 158 ILE n 
1 159 GLY n 
1 160 SER n 
1 161 TRP n 
1 162 CYS n 
1 163 GLN n 
1 164 LYS n 
1 165 TYR n 
1 166 ASP n 
1 167 ILE n 
1 168 LYS n 
1 169 PHE n 
1 170 LYS n 
1 171 LEU n 
1 172 ASN n 
1 173 THR n 
1 174 VAL n 
1 175 VAL n 
1 176 ASN n 
1 177 LYS n 
1 178 PHE n 
1 179 ASN n 
1 180 HIS n 
1 181 LEU n 
1 182 GLU n 
1 183 ASP n 
1 184 MET n 
1 185 ASN n 
1 186 ASP n 
1 187 HIS n 
1 188 LEU n 
1 189 ASN n 
1 190 ALA n 
1 191 LEU n 
1 192 GLN n 
1 193 PRO n 
1 194 PHE n 
1 195 ARG n 
1 196 TRP n 
1 197 LYS n 
1 198 CYS n 
1 199 PHE n 
1 200 GLN n 
1 201 VAL n 
1 202 LEU n 
1 203 ILE n 
1 204 VAL n 
1 205 THR n 
1 206 GLY n 
1 207 GLU n 
1 208 ASN n 
1 209 ASP n 
1 210 SER n 
1 211 ASP n 
1 212 LYS n 
1 213 THR n 
1 214 LEU n 
1 215 ARG n 
1 216 ASN n 
1 217 ALA n 
1 218 HIS n 
1 219 SER n 
1 220 LEU n 
1 221 THR n 
1 222 ILE n 
1 223 SER n 
1 224 ASP n 
1 225 ASP n 
1 226 GLU n 
1 227 PHE n 
1 228 ASP n 
1 229 ARG n 
1 230 PHE n 
1 231 CYS n 
1 232 GLU n 
1 233 ARG n 
1 234 HIS n 
1 235 SER n 
1 236 SER n 
1 237 GLN n 
1 238 THR n 
1 239 CYS n 
1 240 LEU n 
1 241 VAL n 
1 242 PRO n 
1 243 GLU n 
1 244 PRO n 
1 245 ASN n 
1 246 ARG n 
1 247 LEU n 
1 248 MET n 
1 249 ALA n 
1 250 LYS n 
1 251 SER n 
1 252 TYR n 
1 253 LEU n 
1 254 ILE n 
1 255 LEU n 
1 256 ASP n 
1 257 GLU n 
1 258 TYR n 
1 259 MET n 
1 260 ARG n 
1 261 PHE n 
1 262 LEU n 
1 263 ASP n 
1 264 ARG n 
1 265 ASN n 
1 266 GLY n 
1 267 GLN n 
1 268 GLN n 
1 269 PRO n 
1 270 SER n 
1 271 LYS n 
1 272 SER n 
1 273 ILE n 
1 274 LEU n 
1 275 GLU n 
1 276 VAL n 
1 277 GLY n 
1 278 VAL n 
1 279 GLN n 
1 280 GLN n 
1 281 ALA n 
1 282 LEU n 
1 283 GLN n 
1 284 ALA n 
1 285 VAL n 
1 286 PHE n 
1 287 TRP n 
1 288 ASP n 
1 289 GLU n 
1 290 GLU n 
1 291 ALA n 
1 292 PHE n 
1 293 VAL n 
1 294 GLU n 
1 295 ARG n 
1 296 GLY n 
1 297 GLY n 
1 298 ILE n 
1 299 TYR n 
1 300 ASP n 
1 301 TRP n 
1 302 ASN n 
1 303 LYS n 
1 304 SER n 
1 305 SER n 
1 306 CYS n 
1 307 SER n 
1 308 SER n 
1 309 ASP n 
1 310 SER n 
1 311 LYS n 
1 312 ASP n 
1 313 LEU n 
1 314 GLU n 
1 315 TRP 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                   315 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 TRIVIDRAFT_58105 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    Gv29-8 
_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      'Trichoderma virens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     413071 
_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 
CTP non-polymer         . "CYTIDINE-5'-TRIPHOSPHATE" ? 'C9 H16 N3 O14 P3' 483.156 
CYS 'L-peptide linking' y CYSTEINE                   ? 'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                  ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'            ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                    ? 'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE                  ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                      ? 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                 ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                    ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                     ? 'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                 ? 'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE              ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                    ? 'C5 H9 N O2'       115.130 
SAM non-polymer         . S-ADENOSYLMETHIONINE       ? 'C15 H22 N6 O5 S'  398.437 
SER 'L-peptide linking' y SERINE                     ? 'C3 H7 N O3'       105.093 
SF4 non-polymer         . 'IRON/SULFUR CLUSTER'      ? 'Fe4 S4'           351.640 
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   MET 1   -6  ?   ?   ?   A . n 
A 1 2   HIS 2   -5  ?   ?   ?   A . n 
A 1 3   HIS 3   -4  ?   ?   ?   A . n 
A 1 4   HIS 4   -3  ?   ?   ?   A . n 
A 1 5   HIS 5   -2  ?   ?   ?   A . n 
A 1 6   HIS 6   -1  ?   ?   ?   A . n 
A 1 7   HIS 7   0   ?   ?   ?   A . n 
A 1 8   SER 8   1   ?   ?   ?   A . n 
A 1 9   SER 9   2   ?   ?   ?   A . n 
A 1 10  GLY 10  3   ?   ?   ?   A . n 
A 1 11  VAL 11  4   ?   ?   ?   A . n 
A 1 12  ASP 12  5   ?   ?   ?   A . n 
A 1 13  LEU 13  6   ?   ?   ?   A . n 
A 1 14  GLY 14  7   ?   ?   ?   A . n 
A 1 15  THR 15  8   ?   ?   ?   A . n 
A 1 16  GLU 16  9   ?   ?   ?   A . n 
A 1 17  ASN 17  10  ?   ?   ?   A . n 
A 1 18  LEU 18  11  ?   ?   ?   A . n 
A 1 19  TYR 19  12  ?   ?   ?   A . n 
A 1 20  PHE 20  13  ?   ?   ?   A . n 
A 1 21  GLN 21  14  ?   ?   ?   A . n 
A 1 22  SER 22  15  ?   ?   ?   A . n 
A 1 23  MET 23  16  ?   ?   ?   A . n 
A 1 24  GLY 24  17  17  GLY GLY A . n 
A 1 25  GLN 25  18  18  GLN GLN A . n 
A 1 26  VAL 26  19  19  VAL VAL A . n 
A 1 27  PRO 27  20  20  PRO PRO A . n 
A 1 28  VAL 28  21  21  VAL VAL A . n 
A 1 29  SER 29  22  22  SER SER A . n 
A 1 30  VAL 30  23  23  VAL VAL A . n 
A 1 31  ASN 31  24  24  ASN ASN A . n 
A 1 32  TYR 32  25  25  TYR TYR A . n 
A 1 33  HIS 33  26  26  HIS HIS A . n 
A 1 34  PHE 34  27  27  PHE PHE A . n 
A 1 35  SER 35  28  28  SER SER A . n 
A 1 36  ARG 36  29  29  ARG ARG A . n 
A 1 37  LYS 37  30  30  LYS LYS A . n 
A 1 38  CYS 38  31  31  CYS CYS A . n 
A 1 39  ASN 39  32  32  ASN ASN A . n 
A 1 40  LYS 40  33  33  LYS LYS A . n 
A 1 41  GLU 41  34  34  GLU GLU A . n 
A 1 42  CYS 42  35  35  CYS CYS A . n 
A 1 43  LEU 43  36  36  LEU LEU A . n 
A 1 44  PHE 44  37  37  PHE PHE A . n 
A 1 45  CYS 45  38  38  CYS CYS A . n 
A 1 46  PHE 46  39  39  PHE PHE A . n 
A 1 47  HIS 47  40  40  HIS HIS A . n 
A 1 48  THR 48  41  41  THR THR A . n 
A 1 49  ALA 49  42  42  ALA ALA A . n 
A 1 50  THR 50  43  43  THR THR A . n 
A 1 51  THR 51  44  44  THR THR A . n 
A 1 52  SER 52  45  45  SER SER A . n 
A 1 53  HIS 53  46  46  HIS HIS A . n 
A 1 54  VAL 54  47  47  VAL VAL A . n 
A 1 55  GLU 55  48  48  GLU GLU A . n 
A 1 56  LYS 56  49  49  LYS LYS A . n 
A 1 57  PRO 57  50  50  PRO PRO A . n 
A 1 58  GLU 58  51  51  GLU GLU A . n 
A 1 59  ASN 59  52  52  ASN ASN A . n 
A 1 60  ALA 60  53  53  ALA ALA A . n 
A 1 61  LYS 61  54  54  LYS LYS A . n 
A 1 62  ARG 62  55  55  ARG ARG A . n 
A 1 63  GLY 63  56  56  GLY GLY A . n 
A 1 64  LEU 64  57  57  LEU LEU A . n 
A 1 65  THR 65  58  58  THR THR A . n 
A 1 66  LEU 66  59  59  LEU LEU A . n 
A 1 67  LEU 67  60  60  LEU LEU A . n 
A 1 68  LYS 68  61  61  LYS LYS A . n 
A 1 69  GLN 69  62  62  GLN GLN A . n 
A 1 70  ALA 70  63  63  ALA ALA A . n 
A 1 71  GLY 71  64  64  GLY GLY A . n 
A 1 72  MET 72  65  65  MET MET A . n 
A 1 73  LYS 73  66  66  LYS LYS A . n 
A 1 74  LYS 74  67  67  LYS LYS A . n 
A 1 75  ILE 75  68  68  ILE ILE A . n 
A 1 76  ASN 76  69  69  ASN ASN A . n 
A 1 77  PHE 77  70  70  PHE PHE A . n 
A 1 78  ALA 78  71  71  ALA ALA A . n 
A 1 79  GLY 79  72  72  GLY GLY A . n 
A 1 80  GLY 80  73  73  GLY GLY A . n 
A 1 81  GLU 81  74  74  GLU GLU A . n 
A 1 82  PRO 82  75  75  PRO PRO A . n 
A 1 83  PHE 83  76  76  PHE PHE A . n 
A 1 84  LEU 84  77  77  LEU LEU A . n 
A 1 85  TYR 85  78  78  TYR TYR A . n 
A 1 86  PRO 86  79  79  PRO PRO A . n 
A 1 87  LYS 87  80  80  LYS LYS A . n 
A 1 88  PHE 88  81  81  PHE PHE A . n 
A 1 89  LEU 89  82  82  LEU LEU A . n 
A 1 90  GLY 90  83  83  GLY GLY A . n 
A 1 91  GLU 91  84  84  GLU GLU A . n 
A 1 92  MET 92  85  85  MET MET A . n 
A 1 93  ILE 93  86  86  ILE ILE A . n 
A 1 94  ASP 94  87  87  ASP ASP A . n 
A 1 95  PHE 95  88  88  PHE PHE A . n 
A 1 96  CYS 96  89  89  CYS CYS A . n 
A 1 97  LYS 97  90  90  LYS LYS A . n 
A 1 98  GLU 98  91  91  GLU GLU A . n 
A 1 99  THR 99  92  92  THR THR A . n 
A 1 100 LEU 100 93  93  LEU LEU A . n 
A 1 101 GLN 101 94  94  GLN GLN A . n 
A 1 102 LEU 102 95  95  LEU LEU A . n 
A 1 103 GLU 103 96  96  GLU GLU A . n 
A 1 104 SER 104 97  97  SER SER A . n 
A 1 105 VAL 105 98  98  VAL VAL A . n 
A 1 106 SER 106 99  99  SER SER A . n 
A 1 107 ILE 107 100 100 ILE ILE A . n 
A 1 108 VAL 108 101 101 VAL VAL A . n 
A 1 109 THR 109 102 102 THR THR A . n 
A 1 110 ASN 110 103 103 ASN ASN A . n 
A 1 111 GLY 111 104 104 GLY GLY A . n 
A 1 112 SER 112 105 105 SER SER A . n 
A 1 113 LEU 113 106 106 LEU LEU A . n 
A 1 114 VAL 114 107 107 VAL VAL A . n 
A 1 115 LYS 115 108 108 LYS LYS A . n 
A 1 116 GLU 116 109 109 GLU GLU A . n 
A 1 117 GLN 117 110 110 GLN GLN A . n 
A 1 118 PHE 118 111 111 PHE PHE A . n 
A 1 119 LEU 119 112 112 LEU LEU A . n 
A 1 120 GLN 120 113 113 GLN GLN A . n 
A 1 121 LYS 121 114 114 LYS LYS A . n 
A 1 122 HIS 122 115 115 HIS HIS A . n 
A 1 123 GLY 123 116 116 GLY GLY A . n 
A 1 124 ARG 124 117 117 ARG ARG A . n 
A 1 125 ASN 125 118 118 ASN ASN A . n 
A 1 126 ILE 126 119 119 ILE ILE A . n 
A 1 127 ASP 127 120 120 ASP ASP A . n 
A 1 128 ILE 128 121 121 ILE ILE A . n 
A 1 129 LEU 129 122 122 LEU LEU A . n 
A 1 130 ALA 130 123 123 ALA ALA A . n 
A 1 131 VAL 131 124 124 VAL VAL A . n 
A 1 132 SER 132 125 125 SER SER A . n 
A 1 133 CYS 133 126 126 CYS CYS A . n 
A 1 134 ASP 134 127 127 ASP ASP A . n 
A 1 135 SER 135 128 128 SER SER A . n 
A 1 136 PHE 136 129 129 PHE PHE A . n 
A 1 137 ASN 137 130 130 ASN ASN A . n 
A 1 138 GLU 138 131 131 GLU GLU A . n 
A 1 139 ALA 139 132 132 ALA ALA A . n 
A 1 140 THR 140 133 133 THR THR A . n 
A 1 141 ASN 141 134 134 ASN ASN A . n 
A 1 142 ILE 142 135 135 ILE ILE A . n 
A 1 143 LYS 143 136 136 LYS LYS A . n 
A 1 144 ILE 144 137 137 ILE ILE A . n 
A 1 145 GLY 145 138 138 GLY GLY A . n 
A 1 146 ARG 146 139 139 ARG ARG A . n 
A 1 147 GLY 147 140 140 GLY GLY A . n 
A 1 148 SER 148 141 141 SER SER A . n 
A 1 149 GLY 149 142 142 GLY GLY A . n 
A 1 150 ASP 150 143 143 ASP ASP A . n 
A 1 151 ASN 151 144 144 ASN ASN A . n 
A 1 152 VAL 152 145 145 VAL VAL A . n 
A 1 153 GLN 153 146 146 GLN GLN A . n 
A 1 154 LYS 154 147 147 LYS LYS A . n 
A 1 155 LEU 155 148 148 LEU LEU A . n 
A 1 156 TYR 156 149 149 TYR TYR A . n 
A 1 157 GLU 157 150 150 GLU GLU A . n 
A 1 158 ILE 158 151 151 ILE ILE A . n 
A 1 159 GLY 159 152 152 GLY GLY A . n 
A 1 160 SER 160 153 153 SER SER A . n 
A 1 161 TRP 161 154 154 TRP TRP A . n 
A 1 162 CYS 162 155 155 CYS CYS A . n 
A 1 163 GLN 163 156 156 GLN GLN A . n 
A 1 164 LYS 164 157 157 LYS LYS A . n 
A 1 165 TYR 165 158 158 TYR TYR A . n 
A 1 166 ASP 166 159 159 ASP ASP A . n 
A 1 167 ILE 167 160 160 ILE ILE A . n 
A 1 168 LYS 168 161 161 LYS LYS A . n 
A 1 169 PHE 169 162 162 PHE PHE A . n 
A 1 170 LYS 170 163 163 LYS LYS A . n 
A 1 171 LEU 171 164 164 LEU LEU A . n 
A 1 172 ASN 172 165 165 ASN ASN A . n 
A 1 173 THR 173 166 166 THR THR A . n 
A 1 174 VAL 174 167 167 VAL VAL A . n 
A 1 175 VAL 175 168 168 VAL VAL A . n 
A 1 176 ASN 176 169 169 ASN ASN A . n 
A 1 177 LYS 177 170 170 LYS LYS A . n 
A 1 178 PHE 178 171 171 PHE PHE A . n 
A 1 179 ASN 179 172 172 ASN ASN A . n 
A 1 180 HIS 180 173 173 HIS HIS A . n 
A 1 181 LEU 181 174 174 LEU LEU A . n 
A 1 182 GLU 182 175 175 GLU GLU A . n 
A 1 183 ASP 183 176 176 ASP ASP A . n 
A 1 184 MET 184 177 177 MET MET A . n 
A 1 185 ASN 185 178 178 ASN ASN A . n 
A 1 186 ASP 186 179 179 ASP ASP A . n 
A 1 187 HIS 187 180 180 HIS HIS A . n 
A 1 188 LEU 188 181 181 LEU LEU A . n 
A 1 189 ASN 189 182 182 ASN ASN A . n 
A 1 190 ALA 190 183 183 ALA ALA A . n 
A 1 191 LEU 191 184 184 LEU LEU A . n 
A 1 192 GLN 192 185 185 GLN GLN A . n 
A 1 193 PRO 193 186 186 PRO PRO A . n 
A 1 194 PHE 194 187 187 PHE PHE A . n 
A 1 195 ARG 195 188 188 ARG ARG A . n 
A 1 196 TRP 196 189 189 TRP TRP A . n 
A 1 197 LYS 197 190 190 LYS LYS A . n 
A 1 198 CYS 198 191 191 CYS CYS A . n 
A 1 199 PHE 199 192 192 PHE PHE A . n 
A 1 200 GLN 200 193 193 GLN GLN A . n 
A 1 201 VAL 201 194 194 VAL VAL A . n 
A 1 202 LEU 202 195 195 LEU LEU A . n 
A 1 203 ILE 203 196 196 ILE ILE A . n 
A 1 204 VAL 204 197 197 VAL VAL A . n 
A 1 205 THR 205 198 198 THR THR A . n 
A 1 206 GLY 206 199 199 GLY GLY A . n 
A 1 207 GLU 207 200 200 GLU GLU A . n 
A 1 208 ASN 208 201 201 ASN ASN A . n 
A 1 209 ASP 209 202 202 ASP ASP A . n 
A 1 210 SER 210 203 203 SER SER A . n 
A 1 211 ASP 211 204 204 ASP ASP A . n 
A 1 212 LYS 212 205 205 LYS LYS A . n 
A 1 213 THR 213 206 206 THR THR A . n 
A 1 214 LEU 214 207 207 LEU LEU A . n 
A 1 215 ARG 215 208 208 ARG ARG A . n 
A 1 216 ASN 216 209 209 ASN ASN A . n 
A 1 217 ALA 217 210 210 ALA ALA A . n 
A 1 218 HIS 218 211 211 HIS HIS A . n 
A 1 219 SER 219 212 212 SER SER A . n 
A 1 220 LEU 220 213 213 LEU LEU A . n 
A 1 221 THR 221 214 214 THR THR A . n 
A 1 222 ILE 222 215 215 ILE ILE A . n 
A 1 223 SER 223 216 216 SER SER A . n 
A 1 224 ASP 224 217 217 ASP ASP A . n 
A 1 225 ASP 225 218 218 ASP ASP A . n 
A 1 226 GLU 226 219 219 GLU GLU A . n 
A 1 227 PHE 227 220 220 PHE PHE A . n 
A 1 228 ASP 228 221 221 ASP ASP A . n 
A 1 229 ARG 229 222 222 ARG ARG A . n 
A 1 230 PHE 230 223 223 PHE PHE A . n 
A 1 231 CYS 231 224 224 CYS CYS A . n 
A 1 232 GLU 232 225 225 GLU GLU A . n 
A 1 233 ARG 233 226 226 ARG ARG A . n 
A 1 234 HIS 234 227 227 HIS HIS A . n 
A 1 235 SER 235 228 228 SER SER A . n 
A 1 236 SER 236 229 229 SER SER A . n 
A 1 237 GLN 237 230 230 GLN GLN A . n 
A 1 238 THR 238 231 231 THR THR A . n 
A 1 239 CYS 239 232 232 CYS CYS A . n 
A 1 240 LEU 240 233 233 LEU LEU A . n 
A 1 241 VAL 241 234 234 VAL VAL A . n 
A 1 242 PRO 242 235 235 PRO PRO A . n 
A 1 243 GLU 243 236 236 GLU GLU A . n 
A 1 244 PRO 244 237 237 PRO PRO A . n 
A 1 245 ASN 245 238 238 ASN ASN A . n 
A 1 246 ARG 246 239 239 ARG ARG A . n 
A 1 247 LEU 247 240 240 LEU LEU A . n 
A 1 248 MET 248 241 241 MET MET A . n 
A 1 249 ALA 249 242 242 ALA ALA A . n 
A 1 250 LYS 250 243 243 LYS LYS A . n 
A 1 251 SER 251 244 244 SER SER A . n 
A 1 252 TYR 252 245 245 TYR TYR A . n 
A 1 253 LEU 253 246 246 LEU LEU A . n 
A 1 254 ILE 254 247 247 ILE ILE A . n 
A 1 255 LEU 255 248 248 LEU LEU A . n 
A 1 256 ASP 256 249 249 ASP ASP A . n 
A 1 257 GLU 257 250 250 GLU GLU A . n 
A 1 258 TYR 258 251 251 TYR TYR A . n 
A 1 259 MET 259 252 252 MET MET A . n 
A 1 260 ARG 260 253 253 ARG ARG A . n 
A 1 261 PHE 261 254 254 PHE PHE A . n 
A 1 262 LEU 262 255 255 LEU LEU A . n 
A 1 263 ASP 263 256 256 ASP ASP A . n 
A 1 264 ARG 264 257 257 ARG ARG A . n 
A 1 265 ASN 265 258 258 ASN ASN A . n 
A 1 266 GLY 266 259 259 GLY GLY A . n 
A 1 267 GLN 267 260 260 GLN GLN A . n 
A 1 268 GLN 268 261 261 GLN GLN A . n 
A 1 269 PRO 269 262 262 PRO PRO A . n 
A 1 270 SER 270 263 263 SER SER A . n 
A 1 271 LYS 271 264 264 LYS LYS A . n 
A 1 272 SER 272 265 265 SER SER A . n 
A 1 273 ILE 273 266 266 ILE ILE A . n 
A 1 274 LEU 274 267 267 LEU LEU A . n 
A 1 275 GLU 275 268 268 GLU GLU A . n 
A 1 276 VAL 276 269 269 VAL VAL A . n 
A 1 277 GLY 277 270 270 GLY GLY A . n 
A 1 278 VAL 278 271 271 VAL VAL A . n 
A 1 279 GLN 279 272 272 GLN GLN A . n 
A 1 280 GLN 280 273 273 GLN GLN A . n 
A 1 281 ALA 281 274 274 ALA ALA A . n 
A 1 282 LEU 282 275 275 LEU LEU A . n 
A 1 283 GLN 283 276 276 GLN GLN A . n 
A 1 284 ALA 284 277 277 ALA ALA A . n 
A 1 285 VAL 285 278 278 VAL VAL A . n 
A 1 286 PHE 286 279 279 PHE PHE A . n 
A 1 287 TRP 287 280 280 TRP TRP A . n 
A 1 288 ASP 288 281 281 ASP ASP A . n 
A 1 289 GLU 289 282 282 GLU GLU A . n 
A 1 290 GLU 290 283 283 GLU GLU A . n 
A 1 291 ALA 291 284 284 ALA ALA A . n 
A 1 292 PHE 292 285 285 PHE PHE A . n 
A 1 293 VAL 293 286 286 VAL VAL A . n 
A 1 294 GLU 294 287 287 GLU GLU A . n 
A 1 295 ARG 295 288 288 ARG ARG A . n 
A 1 296 GLY 296 289 289 GLY GLY A . n 
A 1 297 GLY 297 290 290 GLY GLY A . n 
A 1 298 ILE 298 291 291 ILE ILE A . n 
A 1 299 TYR 299 292 292 TYR TYR A . n 
A 1 300 ASP 300 293 293 ASP ASP A . n 
A 1 301 TRP 301 294 294 TRP TRP A . n 
A 1 302 ASN 302 295 295 ASN ASN A . n 
A 1 303 LYS 303 296 ?   ?   ?   A . n 
A 1 304 SER 304 297 ?   ?   ?   A . n 
A 1 305 SER 305 298 ?   ?   ?   A . n 
A 1 306 CYS 306 299 ?   ?   ?   A . n 
A 1 307 SER 307 300 ?   ?   ?   A . n 
A 1 308 SER 308 301 ?   ?   ?   A . n 
A 1 309 ASP 309 302 ?   ?   ?   A . n 
A 1 310 SER 310 303 ?   ?   ?   A . n 
A 1 311 LYS 311 304 ?   ?   ?   A . n 
A 1 312 ASP 312 305 ?   ?   ?   A . n 
A 1 313 LEU 313 306 ?   ?   ?   A . n 
A 1 314 GLU 314 307 ?   ?   ?   A . n 
A 1 315 TRP 315 308 ?   ?   ?   A . n 
B 1 1   MET 1   -6  ?   ?   ?   B . n 
B 1 2   HIS 2   -5  ?   ?   ?   B . n 
B 1 3   HIS 3   -4  ?   ?   ?   B . n 
B 1 4   HIS 4   -3  ?   ?   ?   B . n 
B 1 5   HIS 5   -2  ?   ?   ?   B . n 
B 1 6   HIS 6   -1  ?   ?   ?   B . n 
B 1 7   HIS 7   0   ?   ?   ?   B . n 
B 1 8   SER 8   1   ?   ?   ?   B . n 
B 1 9   SER 9   2   ?   ?   ?   B . n 
B 1 10  GLY 10  3   ?   ?   ?   B . n 
B 1 11  VAL 11  4   ?   ?   ?   B . n 
B 1 12  ASP 12  5   ?   ?   ?   B . n 
B 1 13  LEU 13  6   ?   ?   ?   B . n 
B 1 14  GLY 14  7   ?   ?   ?   B . n 
B 1 15  THR 15  8   ?   ?   ?   B . n 
B 1 16  GLU 16  9   ?   ?   ?   B . n 
B 1 17  ASN 17  10  ?   ?   ?   B . n 
B 1 18  LEU 18  11  ?   ?   ?   B . n 
B 1 19  TYR 19  12  ?   ?   ?   B . n 
B 1 20  PHE 20  13  ?   ?   ?   B . n 
B 1 21  GLN 21  14  ?   ?   ?   B . n 
B 1 22  SER 22  15  ?   ?   ?   B . n 
B 1 23  MET 23  16  ?   ?   ?   B . n 
B 1 24  GLY 24  17  17  GLY GLY B . n 
B 1 25  GLN 25  18  18  GLN GLN B . n 
B 1 26  VAL 26  19  19  VAL VAL B . n 
B 1 27  PRO 27  20  20  PRO PRO B . n 
B 1 28  VAL 28  21  21  VAL VAL B . n 
B 1 29  SER 29  22  22  SER SER B . n 
B 1 30  VAL 30  23  23  VAL VAL B . n 
B 1 31  ASN 31  24  24  ASN ASN B . n 
B 1 32  TYR 32  25  25  TYR TYR B . n 
B 1 33  HIS 33  26  26  HIS HIS B . n 
B 1 34  PHE 34  27  27  PHE PHE B . n 
B 1 35  SER 35  28  28  SER SER B . n 
B 1 36  ARG 36  29  29  ARG ARG B . n 
B 1 37  LYS 37  30  30  LYS LYS B . n 
B 1 38  CYS 38  31  31  CYS CYS B . n 
B 1 39  ASN 39  32  32  ASN ASN B . n 
B 1 40  LYS 40  33  33  LYS LYS B . n 
B 1 41  GLU 41  34  34  GLU GLU B . n 
B 1 42  CYS 42  35  35  CYS CYS B . n 
B 1 43  LEU 43  36  36  LEU LEU B . n 
B 1 44  PHE 44  37  37  PHE PHE B . n 
B 1 45  CYS 45  38  38  CYS CYS B . n 
B 1 46  PHE 46  39  39  PHE PHE B . n 
B 1 47  HIS 47  40  40  HIS HIS B . n 
B 1 48  THR 48  41  41  THR THR B . n 
B 1 49  ALA 49  42  42  ALA ALA B . n 
B 1 50  THR 50  43  43  THR THR B . n 
B 1 51  THR 51  44  44  THR THR B . n 
B 1 52  SER 52  45  45  SER SER B . n 
B 1 53  HIS 53  46  46  HIS HIS B . n 
B 1 54  VAL 54  47  47  VAL VAL B . n 
B 1 55  GLU 55  48  48  GLU GLU B . n 
B 1 56  LYS 56  49  49  LYS LYS B . n 
B 1 57  PRO 57  50  50  PRO PRO B . n 
B 1 58  GLU 58  51  51  GLU GLU B . n 
B 1 59  ASN 59  52  52  ASN ASN B . n 
B 1 60  ALA 60  53  53  ALA ALA B . n 
B 1 61  LYS 61  54  54  LYS LYS B . n 
B 1 62  ARG 62  55  55  ARG ARG B . n 
B 1 63  GLY 63  56  56  GLY GLY B . n 
B 1 64  LEU 64  57  57  LEU LEU B . n 
B 1 65  THR 65  58  58  THR THR B . n 
B 1 66  LEU 66  59  59  LEU LEU B . n 
B 1 67  LEU 67  60  60  LEU LEU B . n 
B 1 68  LYS 68  61  61  LYS LYS B . n 
B 1 69  GLN 69  62  62  GLN GLN B . n 
B 1 70  ALA 70  63  63  ALA ALA B . n 
B 1 71  GLY 71  64  64  GLY GLY B . n 
B 1 72  MET 72  65  65  MET MET B . n 
B 1 73  LYS 73  66  66  LYS LYS B . n 
B 1 74  LYS 74  67  67  LYS LYS B . n 
B 1 75  ILE 75  68  68  ILE ILE B . n 
B 1 76  ASN 76  69  69  ASN ASN B . n 
B 1 77  PHE 77  70  70  PHE PHE B . n 
B 1 78  ALA 78  71  71  ALA ALA B . n 
B 1 79  GLY 79  72  72  GLY GLY B . n 
B 1 80  GLY 80  73  73  GLY GLY B . n 
B 1 81  GLU 81  74  74  GLU GLU B . n 
B 1 82  PRO 82  75  75  PRO PRO B . n 
B 1 83  PHE 83  76  76  PHE PHE B . n 
B 1 84  LEU 84  77  77  LEU LEU B . n 
B 1 85  TYR 85  78  78  TYR TYR B . n 
B 1 86  PRO 86  79  79  PRO PRO B . n 
B 1 87  LYS 87  80  80  LYS LYS B . n 
B 1 88  PHE 88  81  81  PHE PHE B . n 
B 1 89  LEU 89  82  82  LEU LEU B . n 
B 1 90  GLY 90  83  83  GLY GLY B . n 
B 1 91  GLU 91  84  84  GLU GLU B . n 
B 1 92  MET 92  85  85  MET MET B . n 
B 1 93  ILE 93  86  86  ILE ILE B . n 
B 1 94  ASP 94  87  87  ASP ASP B . n 
B 1 95  PHE 95  88  88  PHE PHE B . n 
B 1 96  CYS 96  89  89  CYS CYS B . n 
B 1 97  LYS 97  90  90  LYS LYS B . n 
B 1 98  GLU 98  91  91  GLU GLU B . n 
B 1 99  THR 99  92  92  THR THR B . n 
B 1 100 LEU 100 93  93  LEU LEU B . n 
B 1 101 GLN 101 94  94  GLN GLN B . n 
B 1 102 LEU 102 95  95  LEU LEU B . n 
B 1 103 GLU 103 96  96  GLU GLU B . n 
B 1 104 SER 104 97  97  SER SER B . n 
B 1 105 VAL 105 98  98  VAL VAL B . n 
B 1 106 SER 106 99  99  SER SER B . n 
B 1 107 ILE 107 100 100 ILE ILE B . n 
B 1 108 VAL 108 101 101 VAL VAL B . n 
B 1 109 THR 109 102 102 THR THR B . n 
B 1 110 ASN 110 103 103 ASN ASN B . n 
B 1 111 GLY 111 104 104 GLY GLY B . n 
B 1 112 SER 112 105 105 SER SER B . n 
B 1 113 LEU 113 106 106 LEU LEU B . n 
B 1 114 VAL 114 107 107 VAL VAL B . n 
B 1 115 LYS 115 108 108 LYS LYS B . n 
B 1 116 GLU 116 109 109 GLU GLU B . n 
B 1 117 GLN 117 110 110 GLN GLN B . n 
B 1 118 PHE 118 111 111 PHE PHE B . n 
B 1 119 LEU 119 112 112 LEU LEU B . n 
B 1 120 GLN 120 113 113 GLN GLN B . n 
B 1 121 LYS 121 114 114 LYS LYS B . n 
B 1 122 HIS 122 115 115 HIS HIS B . n 
B 1 123 GLY 123 116 116 GLY GLY B . n 
B 1 124 ARG 124 117 117 ARG ARG B . n 
B 1 125 ASN 125 118 118 ASN ASN B . n 
B 1 126 ILE 126 119 119 ILE ILE B . n 
B 1 127 ASP 127 120 120 ASP ASP B . n 
B 1 128 ILE 128 121 121 ILE ILE B . n 
B 1 129 LEU 129 122 122 LEU LEU B . n 
B 1 130 ALA 130 123 123 ALA ALA B . n 
B 1 131 VAL 131 124 124 VAL VAL B . n 
B 1 132 SER 132 125 125 SER SER B . n 
B 1 133 CYS 133 126 126 CYS CYS B . n 
B 1 134 ASP 134 127 127 ASP ASP B . n 
B 1 135 SER 135 128 128 SER SER B . n 
B 1 136 PHE 136 129 129 PHE PHE B . n 
B 1 137 ASN 137 130 130 ASN ASN B . n 
B 1 138 GLU 138 131 131 GLU GLU B . n 
B 1 139 ALA 139 132 132 ALA ALA B . n 
B 1 140 THR 140 133 133 THR THR B . n 
B 1 141 ASN 141 134 134 ASN ASN B . n 
B 1 142 ILE 142 135 135 ILE ILE B . n 
B 1 143 LYS 143 136 136 LYS LYS B . n 
B 1 144 ILE 144 137 137 ILE ILE B . n 
B 1 145 GLY 145 138 138 GLY GLY B . n 
B 1 146 ARG 146 139 139 ARG ARG B . n 
B 1 147 GLY 147 140 140 GLY GLY B . n 
B 1 148 SER 148 141 141 SER SER B . n 
B 1 149 GLY 149 142 142 GLY GLY B . n 
B 1 150 ASP 150 143 143 ASP ASP B . n 
B 1 151 ASN 151 144 144 ASN ASN B . n 
B 1 152 VAL 152 145 145 VAL VAL B . n 
B 1 153 GLN 153 146 146 GLN GLN B . n 
B 1 154 LYS 154 147 147 LYS LYS B . n 
B 1 155 LEU 155 148 148 LEU LEU B . n 
B 1 156 TYR 156 149 149 TYR TYR B . n 
B 1 157 GLU 157 150 150 GLU GLU B . n 
B 1 158 ILE 158 151 151 ILE ILE B . n 
B 1 159 GLY 159 152 152 GLY GLY B . n 
B 1 160 SER 160 153 153 SER SER B . n 
B 1 161 TRP 161 154 154 TRP TRP B . n 
B 1 162 CYS 162 155 155 CYS CYS B . n 
B 1 163 GLN 163 156 156 GLN GLN B . n 
B 1 164 LYS 164 157 157 LYS LYS B . n 
B 1 165 TYR 165 158 158 TYR TYR B . n 
B 1 166 ASP 166 159 159 ASP ASP B . n 
B 1 167 ILE 167 160 160 ILE ILE B . n 
B 1 168 LYS 168 161 161 LYS LYS B . n 
B 1 169 PHE 169 162 162 PHE PHE B . n 
B 1 170 LYS 170 163 163 LYS LYS B . n 
B 1 171 LEU 171 164 164 LEU LEU B . n 
B 1 172 ASN 172 165 165 ASN ASN B . n 
B 1 173 THR 173 166 166 THR THR B . n 
B 1 174 VAL 174 167 167 VAL VAL B . n 
B 1 175 VAL 175 168 168 VAL VAL B . n 
B 1 176 ASN 176 169 169 ASN ASN B . n 
B 1 177 LYS 177 170 170 LYS LYS B . n 
B 1 178 PHE 178 171 171 PHE PHE B . n 
B 1 179 ASN 179 172 172 ASN ASN B . n 
B 1 180 HIS 180 173 173 HIS HIS B . n 
B 1 181 LEU 181 174 174 LEU LEU B . n 
B 1 182 GLU 182 175 175 GLU GLU B . n 
B 1 183 ASP 183 176 176 ASP ASP B . n 
B 1 184 MET 184 177 177 MET MET B . n 
B 1 185 ASN 185 178 178 ASN ASN B . n 
B 1 186 ASP 186 179 179 ASP ASP B . n 
B 1 187 HIS 187 180 180 HIS HIS B . n 
B 1 188 LEU 188 181 181 LEU LEU B . n 
B 1 189 ASN 189 182 182 ASN ASN B . n 
B 1 190 ALA 190 183 183 ALA ALA B . n 
B 1 191 LEU 191 184 184 LEU LEU B . n 
B 1 192 GLN 192 185 185 GLN GLN B . n 
B 1 193 PRO 193 186 186 PRO PRO B . n 
B 1 194 PHE 194 187 187 PHE PHE B . n 
B 1 195 ARG 195 188 188 ARG ARG B . n 
B 1 196 TRP 196 189 189 TRP TRP B . n 
B 1 197 LYS 197 190 190 LYS LYS B . n 
B 1 198 CYS 198 191 191 CYS CYS B . n 
B 1 199 PHE 199 192 192 PHE PHE B . n 
B 1 200 GLN 200 193 193 GLN GLN B . n 
B 1 201 VAL 201 194 194 VAL VAL B . n 
B 1 202 LEU 202 195 195 LEU LEU B . n 
B 1 203 ILE 203 196 196 ILE ILE B . n 
B 1 204 VAL 204 197 197 VAL VAL B . n 
B 1 205 THR 205 198 198 THR THR B . n 
B 1 206 GLY 206 199 199 GLY GLY B . n 
B 1 207 GLU 207 200 200 GLU GLU B . n 
B 1 208 ASN 208 201 201 ASN ASN B . n 
B 1 209 ASP 209 202 202 ASP ASP B . n 
B 1 210 SER 210 203 203 SER SER B . n 
B 1 211 ASP 211 204 204 ASP ASP B . n 
B 1 212 LYS 212 205 205 LYS LYS B . n 
B 1 213 THR 213 206 206 THR THR B . n 
B 1 214 LEU 214 207 207 LEU LEU B . n 
B 1 215 ARG 215 208 208 ARG ARG B . n 
B 1 216 ASN 216 209 209 ASN ASN B . n 
B 1 217 ALA 217 210 210 ALA ALA B . n 
B 1 218 HIS 218 211 211 HIS HIS B . n 
B 1 219 SER 219 212 212 SER SER B . n 
B 1 220 LEU 220 213 213 LEU LEU B . n 
B 1 221 THR 221 214 214 THR THR B . n 
B 1 222 ILE 222 215 215 ILE ILE B . n 
B 1 223 SER 223 216 216 SER SER B . n 
B 1 224 ASP 224 217 217 ASP ASP B . n 
B 1 225 ASP 225 218 218 ASP ASP B . n 
B 1 226 GLU 226 219 219 GLU GLU B . n 
B 1 227 PHE 227 220 220 PHE PHE B . n 
B 1 228 ASP 228 221 221 ASP ASP B . n 
B 1 229 ARG 229 222 222 ARG ARG B . n 
B 1 230 PHE 230 223 223 PHE PHE B . n 
B 1 231 CYS 231 224 224 CYS CYS B . n 
B 1 232 GLU 232 225 225 GLU GLU B . n 
B 1 233 ARG 233 226 226 ARG ARG B . n 
B 1 234 HIS 234 227 227 HIS HIS B . n 
B 1 235 SER 235 228 228 SER SER B . n 
B 1 236 SER 236 229 229 SER SER B . n 
B 1 237 GLN 237 230 230 GLN GLN B . n 
B 1 238 THR 238 231 231 THR THR B . n 
B 1 239 CYS 239 232 232 CYS CYS B . n 
B 1 240 LEU 240 233 233 LEU LEU B . n 
B 1 241 VAL 241 234 234 VAL VAL B . n 
B 1 242 PRO 242 235 235 PRO PRO B . n 
B 1 243 GLU 243 236 236 GLU GLU B . n 
B 1 244 PRO 244 237 237 PRO PRO B . n 
B 1 245 ASN 245 238 238 ASN ASN B . n 
B 1 246 ARG 246 239 239 ARG ARG B . n 
B 1 247 LEU 247 240 240 LEU LEU B . n 
B 1 248 MET 248 241 241 MET MET B . n 
B 1 249 ALA 249 242 242 ALA ALA B . n 
B 1 250 LYS 250 243 243 LYS LYS B . n 
B 1 251 SER 251 244 244 SER SER B . n 
B 1 252 TYR 252 245 245 TYR TYR B . n 
B 1 253 LEU 253 246 246 LEU LEU B . n 
B 1 254 ILE 254 247 247 ILE ILE B . n 
B 1 255 LEU 255 248 248 LEU LEU B . n 
B 1 256 ASP 256 249 249 ASP ASP B . n 
B 1 257 GLU 257 250 250 GLU GLU B . n 
B 1 258 TYR 258 251 251 TYR TYR B . n 
B 1 259 MET 259 252 252 MET MET B . n 
B 1 260 ARG 260 253 253 ARG ARG B . n 
B 1 261 PHE 261 254 254 PHE PHE B . n 
B 1 262 LEU 262 255 255 LEU LEU B . n 
B 1 263 ASP 263 256 256 ASP ASP B . n 
B 1 264 ARG 264 257 257 ARG ARG B . n 
B 1 265 ASN 265 258 258 ASN ASN B . n 
B 1 266 GLY 266 259 259 GLY GLY B . n 
B 1 267 GLN 267 260 260 GLN GLN B . n 
B 1 268 GLN 268 261 261 GLN GLN B . n 
B 1 269 PRO 269 262 262 PRO PRO B . n 
B 1 270 SER 270 263 263 SER SER B . n 
B 1 271 LYS 271 264 264 LYS LYS B . n 
B 1 272 SER 272 265 265 SER SER B . n 
B 1 273 ILE 273 266 266 ILE ILE B . n 
B 1 274 LEU 274 267 267 LEU LEU B . n 
B 1 275 GLU 275 268 268 GLU GLU B . n 
B 1 276 VAL 276 269 269 VAL VAL B . n 
B 1 277 GLY 277 270 270 GLY GLY B . n 
B 1 278 VAL 278 271 271 VAL VAL B . n 
B 1 279 GLN 279 272 272 GLN GLN B . n 
B 1 280 GLN 280 273 273 GLN GLN B . n 
B 1 281 ALA 281 274 274 ALA ALA B . n 
B 1 282 LEU 282 275 275 LEU LEU B . n 
B 1 283 GLN 283 276 276 GLN GLN B . n 
B 1 284 ALA 284 277 277 ALA ALA B . n 
B 1 285 VAL 285 278 278 VAL VAL B . n 
B 1 286 PHE 286 279 279 PHE PHE B . n 
B 1 287 TRP 287 280 280 TRP TRP B . n 
B 1 288 ASP 288 281 281 ASP ASP B . n 
B 1 289 GLU 289 282 282 GLU GLU B . n 
B 1 290 GLU 290 283 283 GLU GLU B . n 
B 1 291 ALA 291 284 284 ALA ALA B . n 
B 1 292 PHE 292 285 285 PHE PHE B . n 
B 1 293 VAL 293 286 286 VAL VAL B . n 
B 1 294 GLU 294 287 287 GLU GLU B . n 
B 1 295 ARG 295 288 288 ARG ARG B . n 
B 1 296 GLY 296 289 289 GLY GLY B . n 
B 1 297 GLY 297 290 290 GLY GLY B . n 
B 1 298 ILE 298 291 291 ILE ILE B . n 
B 1 299 TYR 299 292 292 TYR TYR B . n 
B 1 300 ASP 300 293 293 ASP ASP B . n 
B 1 301 TRP 301 294 294 TRP TRP B . n 
B 1 302 ASN 302 295 295 ASN ASN B . n 
B 1 303 LYS 303 296 296 LYS LYS B . n 
B 1 304 SER 304 297 297 SER SER B . n 
B 1 305 SER 305 298 298 SER SER B . n 
B 1 306 CYS 306 299 ?   ?   ?   B . n 
B 1 307 SER 307 300 ?   ?   ?   B . n 
B 1 308 SER 308 301 ?   ?   ?   B . n 
B 1 309 ASP 309 302 ?   ?   ?   B . n 
B 1 310 SER 310 303 ?   ?   ?   B . n 
B 1 311 LYS 311 304 ?   ?   ?   B . n 
B 1 312 ASP 312 305 ?   ?   ?   B . n 
B 1 313 LEU 313 306 ?   ?   ?   B . n 
B 1 314 GLU 314 307 ?   ?   ?   B . n 
B 1 315 TRP 315 308 ?   ?   ?   B . n 
C 1 1   MET 1   -6  ?   ?   ?   C . n 
C 1 2   HIS 2   -5  ?   ?   ?   C . n 
C 1 3   HIS 3   -4  ?   ?   ?   C . n 
C 1 4   HIS 4   -3  ?   ?   ?   C . n 
C 1 5   HIS 5   -2  ?   ?   ?   C . n 
C 1 6   HIS 6   -1  ?   ?   ?   C . n 
C 1 7   HIS 7   0   ?   ?   ?   C . n 
C 1 8   SER 8   1   ?   ?   ?   C . n 
C 1 9   SER 9   2   ?   ?   ?   C . n 
C 1 10  GLY 10  3   ?   ?   ?   C . n 
C 1 11  VAL 11  4   ?   ?   ?   C . n 
C 1 12  ASP 12  5   ?   ?   ?   C . n 
C 1 13  LEU 13  6   ?   ?   ?   C . n 
C 1 14  GLY 14  7   ?   ?   ?   C . n 
C 1 15  THR 15  8   ?   ?   ?   C . n 
C 1 16  GLU 16  9   ?   ?   ?   C . n 
C 1 17  ASN 17  10  ?   ?   ?   C . n 
C 1 18  LEU 18  11  ?   ?   ?   C . n 
C 1 19  TYR 19  12  ?   ?   ?   C . n 
C 1 20  PHE 20  13  ?   ?   ?   C . n 
C 1 21  GLN 21  14  ?   ?   ?   C . n 
C 1 22  SER 22  15  ?   ?   ?   C . n 
C 1 23  MET 23  16  ?   ?   ?   C . n 
C 1 24  GLY 24  17  ?   ?   ?   C . n 
C 1 25  GLN 25  18  18  GLN GLN C . n 
C 1 26  VAL 26  19  19  VAL VAL C . n 
C 1 27  PRO 27  20  20  PRO PRO C . n 
C 1 28  VAL 28  21  21  VAL VAL C . n 
C 1 29  SER 29  22  22  SER SER C . n 
C 1 30  VAL 30  23  23  VAL VAL C . n 
C 1 31  ASN 31  24  24  ASN ASN C . n 
C 1 32  TYR 32  25  25  TYR TYR C . n 
C 1 33  HIS 33  26  26  HIS HIS C . n 
C 1 34  PHE 34  27  27  PHE PHE C . n 
C 1 35  SER 35  28  28  SER SER C . n 
C 1 36  ARG 36  29  29  ARG ARG C . n 
C 1 37  LYS 37  30  30  LYS LYS C . n 
C 1 38  CYS 38  31  31  CYS CYS C . n 
C 1 39  ASN 39  32  32  ASN ASN C . n 
C 1 40  LYS 40  33  33  LYS LYS C . n 
C 1 41  GLU 41  34  34  GLU GLU C . n 
C 1 42  CYS 42  35  35  CYS CYS C . n 
C 1 43  LEU 43  36  36  LEU LEU C . n 
C 1 44  PHE 44  37  37  PHE PHE C . n 
C 1 45  CYS 45  38  38  CYS CYS C . n 
C 1 46  PHE 46  39  39  PHE PHE C . n 
C 1 47  HIS 47  40  40  HIS HIS C . n 
C 1 48  THR 48  41  41  THR THR C . n 
C 1 49  ALA 49  42  42  ALA ALA C . n 
C 1 50  THR 50  43  43  THR THR C . n 
C 1 51  THR 51  44  44  THR THR C . n 
C 1 52  SER 52  45  45  SER SER C . n 
C 1 53  HIS 53  46  46  HIS HIS C . n 
C 1 54  VAL 54  47  47  VAL VAL C . n 
C 1 55  GLU 55  48  48  GLU GLU C . n 
C 1 56  LYS 56  49  49  LYS LYS C . n 
C 1 57  PRO 57  50  50  PRO PRO C . n 
C 1 58  GLU 58  51  51  GLU GLU C . n 
C 1 59  ASN 59  52  52  ASN ASN C . n 
C 1 60  ALA 60  53  53  ALA ALA C . n 
C 1 61  LYS 61  54  54  LYS LYS C . n 
C 1 62  ARG 62  55  55  ARG ARG C . n 
C 1 63  GLY 63  56  56  GLY GLY C . n 
C 1 64  LEU 64  57  57  LEU LEU C . n 
C 1 65  THR 65  58  58  THR THR C . n 
C 1 66  LEU 66  59  59  LEU LEU C . n 
C 1 67  LEU 67  60  60  LEU LEU C . n 
C 1 68  LYS 68  61  61  LYS LYS C . n 
C 1 69  GLN 69  62  62  GLN GLN C . n 
C 1 70  ALA 70  63  63  ALA ALA C . n 
C 1 71  GLY 71  64  64  GLY GLY C . n 
C 1 72  MET 72  65  65  MET MET C . n 
C 1 73  LYS 73  66  66  LYS LYS C . n 
C 1 74  LYS 74  67  67  LYS LYS C . n 
C 1 75  ILE 75  68  68  ILE ILE C . n 
C 1 76  ASN 76  69  69  ASN ASN C . n 
C 1 77  PHE 77  70  70  PHE PHE C . n 
C 1 78  ALA 78  71  71  ALA ALA C . n 
C 1 79  GLY 79  72  72  GLY GLY C . n 
C 1 80  GLY 80  73  73  GLY GLY C . n 
C 1 81  GLU 81  74  74  GLU GLU C . n 
C 1 82  PRO 82  75  75  PRO PRO C . n 
C 1 83  PHE 83  76  76  PHE PHE C . n 
C 1 84  LEU 84  77  77  LEU LEU C . n 
C 1 85  TYR 85  78  78  TYR TYR C . n 
C 1 86  PRO 86  79  79  PRO PRO C . n 
C 1 87  LYS 87  80  80  LYS LYS C . n 
C 1 88  PHE 88  81  81  PHE PHE C . n 
C 1 89  LEU 89  82  82  LEU LEU C . n 
C 1 90  GLY 90  83  83  GLY GLY C . n 
C 1 91  GLU 91  84  84  GLU GLU C . n 
C 1 92  MET 92  85  85  MET MET C . n 
C 1 93  ILE 93  86  86  ILE ILE C . n 
C 1 94  ASP 94  87  87  ASP ASP C . n 
C 1 95  PHE 95  88  88  PHE PHE C . n 
C 1 96  CYS 96  89  89  CYS CYS C . n 
C 1 97  LYS 97  90  90  LYS LYS C . n 
C 1 98  GLU 98  91  91  GLU GLU C . n 
C 1 99  THR 99  92  92  THR THR C . n 
C 1 100 LEU 100 93  93  LEU LEU C . n 
C 1 101 GLN 101 94  94  GLN GLN C . n 
C 1 102 LEU 102 95  95  LEU LEU C . n 
C 1 103 GLU 103 96  96  GLU GLU C . n 
C 1 104 SER 104 97  97  SER SER C . n 
C 1 105 VAL 105 98  98  VAL VAL C . n 
C 1 106 SER 106 99  99  SER SER C . n 
C 1 107 ILE 107 100 100 ILE ILE C . n 
C 1 108 VAL 108 101 101 VAL VAL C . n 
C 1 109 THR 109 102 102 THR THR C . n 
C 1 110 ASN 110 103 103 ASN ASN C . n 
C 1 111 GLY 111 104 104 GLY GLY C . n 
C 1 112 SER 112 105 105 SER SER C . n 
C 1 113 LEU 113 106 106 LEU LEU C . n 
C 1 114 VAL 114 107 107 VAL VAL C . n 
C 1 115 LYS 115 108 108 LYS LYS C . n 
C 1 116 GLU 116 109 109 GLU GLU C . n 
C 1 117 GLN 117 110 110 GLN GLN C . n 
C 1 118 PHE 118 111 111 PHE PHE C . n 
C 1 119 LEU 119 112 112 LEU LEU C . n 
C 1 120 GLN 120 113 113 GLN GLN C . n 
C 1 121 LYS 121 114 114 LYS LYS C . n 
C 1 122 HIS 122 115 115 HIS HIS C . n 
C 1 123 GLY 123 116 116 GLY GLY C . n 
C 1 124 ARG 124 117 117 ARG ARG C . n 
C 1 125 ASN 125 118 118 ASN ASN C . n 
C 1 126 ILE 126 119 119 ILE ILE C . n 
C 1 127 ASP 127 120 120 ASP ASP C . n 
C 1 128 ILE 128 121 121 ILE ILE C . n 
C 1 129 LEU 129 122 122 LEU LEU C . n 
C 1 130 ALA 130 123 123 ALA ALA C . n 
C 1 131 VAL 131 124 124 VAL VAL C . n 
C 1 132 SER 132 125 125 SER SER C . n 
C 1 133 CYS 133 126 126 CYS CYS C . n 
C 1 134 ASP 134 127 127 ASP ASP C . n 
C 1 135 SER 135 128 128 SER SER C . n 
C 1 136 PHE 136 129 129 PHE PHE C . n 
C 1 137 ASN 137 130 130 ASN ASN C . n 
C 1 138 GLU 138 131 131 GLU GLU C . n 
C 1 139 ALA 139 132 132 ALA ALA C . n 
C 1 140 THR 140 133 133 THR THR C . n 
C 1 141 ASN 141 134 134 ASN ASN C . n 
C 1 142 ILE 142 135 135 ILE ILE C . n 
C 1 143 LYS 143 136 136 LYS LYS C . n 
C 1 144 ILE 144 137 137 ILE ILE C . n 
C 1 145 GLY 145 138 138 GLY GLY C . n 
C 1 146 ARG 146 139 139 ARG ARG C . n 
C 1 147 GLY 147 140 140 GLY GLY C . n 
C 1 148 SER 148 141 141 SER SER C . n 
C 1 149 GLY 149 142 142 GLY GLY C . n 
C 1 150 ASP 150 143 143 ASP ASP C . n 
C 1 151 ASN 151 144 144 ASN ASN C . n 
C 1 152 VAL 152 145 145 VAL VAL C . n 
C 1 153 GLN 153 146 146 GLN GLN C . n 
C 1 154 LYS 154 147 147 LYS LYS C . n 
C 1 155 LEU 155 148 148 LEU LEU C . n 
C 1 156 TYR 156 149 149 TYR TYR C . n 
C 1 157 GLU 157 150 150 GLU GLU C . n 
C 1 158 ILE 158 151 151 ILE ILE C . n 
C 1 159 GLY 159 152 152 GLY GLY C . n 
C 1 160 SER 160 153 153 SER SER C . n 
C 1 161 TRP 161 154 154 TRP TRP C . n 
C 1 162 CYS 162 155 155 CYS CYS C . n 
C 1 163 GLN 163 156 156 GLN GLN C . n 
C 1 164 LYS 164 157 157 LYS LYS C . n 
C 1 165 TYR 165 158 158 TYR TYR C . n 
C 1 166 ASP 166 159 159 ASP ASP C . n 
C 1 167 ILE 167 160 160 ILE ILE C . n 
C 1 168 LYS 168 161 161 LYS LYS C . n 
C 1 169 PHE 169 162 162 PHE PHE C . n 
C 1 170 LYS 170 163 163 LYS LYS C . n 
C 1 171 LEU 171 164 164 LEU LEU C . n 
C 1 172 ASN 172 165 165 ASN ASN C . n 
C 1 173 THR 173 166 166 THR THR C . n 
C 1 174 VAL 174 167 167 VAL VAL C . n 
C 1 175 VAL 175 168 168 VAL VAL C . n 
C 1 176 ASN 176 169 169 ASN ASN C . n 
C 1 177 LYS 177 170 170 LYS LYS C . n 
C 1 178 PHE 178 171 171 PHE PHE C . n 
C 1 179 ASN 179 172 172 ASN ASN C . n 
C 1 180 HIS 180 173 173 HIS HIS C . n 
C 1 181 LEU 181 174 174 LEU LEU C . n 
C 1 182 GLU 182 175 175 GLU GLU C . n 
C 1 183 ASP 183 176 176 ASP ASP C . n 
C 1 184 MET 184 177 177 MET MET C . n 
C 1 185 ASN 185 178 178 ASN ASN C . n 
C 1 186 ASP 186 179 179 ASP ASP C . n 
C 1 187 HIS 187 180 180 HIS HIS C . n 
C 1 188 LEU 188 181 181 LEU LEU C . n 
C 1 189 ASN 189 182 182 ASN ASN C . n 
C 1 190 ALA 190 183 183 ALA ALA C . n 
C 1 191 LEU 191 184 184 LEU LEU C . n 
C 1 192 GLN 192 185 185 GLN GLN C . n 
C 1 193 PRO 193 186 186 PRO PRO C . n 
C 1 194 PHE 194 187 187 PHE PHE C . n 
C 1 195 ARG 195 188 188 ARG ARG C . n 
C 1 196 TRP 196 189 189 TRP TRP C . n 
C 1 197 LYS 197 190 190 LYS LYS C . n 
C 1 198 CYS 198 191 191 CYS CYS C . n 
C 1 199 PHE 199 192 192 PHE PHE C . n 
C 1 200 GLN 200 193 193 GLN GLN C . n 
C 1 201 VAL 201 194 194 VAL VAL C . n 
C 1 202 LEU 202 195 195 LEU LEU C . n 
C 1 203 ILE 203 196 196 ILE ILE C . n 
C 1 204 VAL 204 197 197 VAL VAL C . n 
C 1 205 THR 205 198 198 THR THR C . n 
C 1 206 GLY 206 199 199 GLY GLY C . n 
C 1 207 GLU 207 200 200 GLU GLU C . n 
C 1 208 ASN 208 201 201 ASN ASN C . n 
C 1 209 ASP 209 202 202 ASP ASP C . n 
C 1 210 SER 210 203 203 SER SER C . n 
C 1 211 ASP 211 204 204 ASP ASP C . n 
C 1 212 LYS 212 205 205 LYS LYS C . n 
C 1 213 THR 213 206 206 THR THR C . n 
C 1 214 LEU 214 207 207 LEU LEU C . n 
C 1 215 ARG 215 208 208 ARG ARG C . n 
C 1 216 ASN 216 209 209 ASN ASN C . n 
C 1 217 ALA 217 210 210 ALA ALA C . n 
C 1 218 HIS 218 211 211 HIS HIS C . n 
C 1 219 SER 219 212 212 SER SER C . n 
C 1 220 LEU 220 213 213 LEU LEU C . n 
C 1 221 THR 221 214 214 THR THR C . n 
C 1 222 ILE 222 215 215 ILE ILE C . n 
C 1 223 SER 223 216 216 SER SER C . n 
C 1 224 ASP 224 217 217 ASP ASP C . n 
C 1 225 ASP 225 218 218 ASP ASP C . n 
C 1 226 GLU 226 219 219 GLU GLU C . n 
C 1 227 PHE 227 220 220 PHE PHE C . n 
C 1 228 ASP 228 221 221 ASP ASP C . n 
C 1 229 ARG 229 222 222 ARG ARG C . n 
C 1 230 PHE 230 223 223 PHE PHE C . n 
C 1 231 CYS 231 224 224 CYS CYS C . n 
C 1 232 GLU 232 225 225 GLU GLU C . n 
C 1 233 ARG 233 226 226 ARG ARG C . n 
C 1 234 HIS 234 227 227 HIS HIS C . n 
C 1 235 SER 235 228 228 SER SER C . n 
C 1 236 SER 236 229 229 SER SER C . n 
C 1 237 GLN 237 230 230 GLN GLN C . n 
C 1 238 THR 238 231 231 THR THR C . n 
C 1 239 CYS 239 232 232 CYS CYS C . n 
C 1 240 LEU 240 233 233 LEU LEU C . n 
C 1 241 VAL 241 234 234 VAL VAL C . n 
C 1 242 PRO 242 235 235 PRO PRO C . n 
C 1 243 GLU 243 236 236 GLU GLU C . n 
C 1 244 PRO 244 237 237 PRO PRO C . n 
C 1 245 ASN 245 238 238 ASN ASN C . n 
C 1 246 ARG 246 239 239 ARG ARG C . n 
C 1 247 LEU 247 240 240 LEU LEU C . n 
C 1 248 MET 248 241 241 MET MET C . n 
C 1 249 ALA 249 242 242 ALA ALA C . n 
C 1 250 LYS 250 243 243 LYS LYS C . n 
C 1 251 SER 251 244 244 SER SER C . n 
C 1 252 TYR 252 245 245 TYR TYR C . n 
C 1 253 LEU 253 246 246 LEU LEU C . n 
C 1 254 ILE 254 247 247 ILE ILE C . n 
C 1 255 LEU 255 248 248 LEU LEU C . n 
C 1 256 ASP 256 249 249 ASP ASP C . n 
C 1 257 GLU 257 250 250 GLU GLU C . n 
C 1 258 TYR 258 251 251 TYR TYR C . n 
C 1 259 MET 259 252 252 MET MET C . n 
C 1 260 ARG 260 253 253 ARG ARG C . n 
C 1 261 PHE 261 254 254 PHE PHE C . n 
C 1 262 LEU 262 255 255 LEU LEU C . n 
C 1 263 ASP 263 256 256 ASP ASP C . n 
C 1 264 ARG 264 257 257 ARG ARG C . n 
C 1 265 ASN 265 258 ?   ?   ?   C . n 
C 1 266 GLY 266 259 ?   ?   ?   C . n 
C 1 267 GLN 267 260 ?   ?   ?   C . n 
C 1 268 GLN 268 261 ?   ?   ?   C . n 
C 1 269 PRO 269 262 262 PRO PRO C . n 
C 1 270 SER 270 263 263 SER SER C . n 
C 1 271 LYS 271 264 264 LYS LYS C . n 
C 1 272 SER 272 265 265 SER SER C . n 
C 1 273 ILE 273 266 266 ILE ILE C . n 
C 1 274 LEU 274 267 267 LEU LEU C . n 
C 1 275 GLU 275 268 268 GLU GLU C . n 
C 1 276 VAL 276 269 269 VAL VAL C . n 
C 1 277 GLY 277 270 270 GLY GLY C . n 
C 1 278 VAL 278 271 271 VAL VAL C . n 
C 1 279 GLN 279 272 272 GLN GLN C . n 
C 1 280 GLN 280 273 273 GLN GLN C . n 
C 1 281 ALA 281 274 274 ALA ALA C . n 
C 1 282 LEU 282 275 275 LEU LEU C . n 
C 1 283 GLN 283 276 276 GLN GLN C . n 
C 1 284 ALA 284 277 277 ALA ALA C . n 
C 1 285 VAL 285 278 278 VAL VAL C . n 
C 1 286 PHE 286 279 279 PHE PHE C . n 
C 1 287 TRP 287 280 280 TRP TRP C . n 
C 1 288 ASP 288 281 281 ASP ASP C . n 
C 1 289 GLU 289 282 282 GLU GLU C . n 
C 1 290 GLU 290 283 283 GLU GLU C . n 
C 1 291 ALA 291 284 284 ALA ALA C . n 
C 1 292 PHE 292 285 285 PHE PHE C . n 
C 1 293 VAL 293 286 286 VAL VAL C . n 
C 1 294 GLU 294 287 287 GLU GLU C . n 
C 1 295 ARG 295 288 288 ARG ARG C . n 
C 1 296 GLY 296 289 289 GLY GLY C . n 
C 1 297 GLY 297 290 290 GLY GLY C . n 
C 1 298 ILE 298 291 291 ILE ILE C . n 
C 1 299 TYR 299 292 292 TYR TYR C . n 
C 1 300 ASP 300 293 293 ASP ASP C . n 
C 1 301 TRP 301 294 294 TRP TRP C . n 
C 1 302 ASN 302 295 295 ASN ASN C . n 
C 1 303 LYS 303 296 296 LYS LYS C . n 
C 1 304 SER 304 297 297 SER SER C . n 
C 1 305 SER 305 298 ?   ?   ?   C . n 
C 1 306 CYS 306 299 ?   ?   ?   C . n 
C 1 307 SER 307 300 ?   ?   ?   C . n 
C 1 308 SER 308 301 ?   ?   ?   C . n 
C 1 309 ASP 309 302 ?   ?   ?   C . n 
C 1 310 SER 310 303 ?   ?   ?   C . n 
C 1 311 LYS 311 304 ?   ?   ?   C . n 
C 1 312 ASP 312 305 ?   ?   ?   C . n 
C 1 313 LEU 313 306 ?   ?   ?   C . n 
C 1 314 GLU 314 307 ?   ?   ?   C . n 
C 1 315 TRP 315 308 ?   ?   ?   C . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CTP ? ? CTP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SAM ? ? SAM ? ? 'SUBJECT OF INVESTIGATION' ? 
3 SF4 ? ? SF4 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 CTP 1   401 301 CTP CTP A . 
E 3 SF4 1   402 302 SF4 SF4 A . 
F 4 SAM 1   403 303 SAM SAM A . 
G 3 SF4 1   401 301 SF4 SF4 B . 
H 4 SAM 1   402 302 SAM SAM B . 
I 2 CTP 1   403 303 CTP CTP B . 
J 4 SAM 1   401 302 SAM SAM C . 
K 2 CTP 1   402 303 CTP CTP C . 
L 3 SF4 1   403 304 SF4 SF4 C . 
M 5 HOH 1   501 288 HOH HOH A . 
M 5 HOH 2   502 303 HOH HOH A . 
M 5 HOH 3   503 27  HOH HOH A . 
M 5 HOH 4   504 292 HOH HOH A . 
M 5 HOH 5   505 237 HOH HOH A . 
M 5 HOH 6   506 259 HOH HOH A . 
M 5 HOH 7   507 227 HOH HOH A . 
M 5 HOH 8   508 188 HOH HOH A . 
M 5 HOH 9   509 76  HOH HOH A . 
M 5 HOH 10  510 280 HOH HOH A . 
M 5 HOH 11  511 98  HOH HOH A . 
M 5 HOH 12  512 89  HOH HOH A . 
M 5 HOH 13  513 294 HOH HOH A . 
M 5 HOH 14  514 101 HOH HOH A . 
M 5 HOH 15  515 266 HOH HOH A . 
M 5 HOH 16  516 61  HOH HOH A . 
M 5 HOH 17  517 251 HOH HOH A . 
M 5 HOH 18  518 108 HOH HOH A . 
M 5 HOH 19  519 1   HOH HOH A . 
M 5 HOH 20  520 7   HOH HOH A . 
M 5 HOH 21  521 162 HOH HOH A . 
M 5 HOH 22  522 252 HOH HOH A . 
M 5 HOH 23  523 13  HOH HOH A . 
M 5 HOH 24  524 277 HOH HOH A . 
M 5 HOH 25  525 64  HOH HOH A . 
M 5 HOH 26  526 3   HOH HOH A . 
M 5 HOH 27  527 34  HOH HOH A . 
M 5 HOH 28  528 57  HOH HOH A . 
M 5 HOH 29  529 184 HOH HOH A . 
M 5 HOH 30  530 79  HOH HOH A . 
M 5 HOH 31  531 45  HOH HOH A . 
M 5 HOH 32  532 123 HOH HOH A . 
M 5 HOH 33  533 16  HOH HOH A . 
M 5 HOH 34  534 170 HOH HOH A . 
M 5 HOH 35  535 15  HOH HOH A . 
M 5 HOH 36  536 32  HOH HOH A . 
M 5 HOH 37  537 159 HOH HOH A . 
M 5 HOH 38  538 117 HOH HOH A . 
M 5 HOH 39  539 112 HOH HOH A . 
M 5 HOH 40  540 95  HOH HOH A . 
M 5 HOH 41  541 215 HOH HOH A . 
M 5 HOH 42  542 100 HOH HOH A . 
M 5 HOH 43  543 121 HOH HOH A . 
M 5 HOH 44  544 36  HOH HOH A . 
M 5 HOH 45  545 139 HOH HOH A . 
M 5 HOH 46  546 73  HOH HOH A . 
M 5 HOH 47  547 239 HOH HOH A . 
M 5 HOH 48  548 176 HOH HOH A . 
M 5 HOH 49  549 116 HOH HOH A . 
M 5 HOH 50  550 271 HOH HOH A . 
M 5 HOH 51  551 172 HOH HOH A . 
M 5 HOH 52  552 18  HOH HOH A . 
M 5 HOH 53  553 124 HOH HOH A . 
M 5 HOH 54  554 96  HOH HOH A . 
M 5 HOH 55  555 88  HOH HOH A . 
M 5 HOH 56  556 28  HOH HOH A . 
M 5 HOH 57  557 190 HOH HOH A . 
M 5 HOH 58  558 168 HOH HOH A . 
M 5 HOH 59  559 210 HOH HOH A . 
M 5 HOH 60  560 148 HOH HOH A . 
M 5 HOH 61  561 105 HOH HOH A . 
M 5 HOH 62  562 192 HOH HOH A . 
M 5 HOH 63  563 93  HOH HOH A . 
M 5 HOH 64  564 48  HOH HOH A . 
M 5 HOH 65  565 19  HOH HOH A . 
M 5 HOH 66  566 9   HOH HOH A . 
M 5 HOH 67  567 38  HOH HOH A . 
M 5 HOH 68  568 243 HOH HOH A . 
M 5 HOH 69  569 131 HOH HOH A . 
M 5 HOH 70  570 267 HOH HOH A . 
M 5 HOH 71  571 55  HOH HOH A . 
M 5 HOH 72  572 80  HOH HOH A . 
M 5 HOH 73  573 56  HOH HOH A . 
M 5 HOH 74  574 12  HOH HOH A . 
M 5 HOH 75  575 8   HOH HOH A . 
M 5 HOH 76  576 257 HOH HOH A . 
M 5 HOH 77  577 138 HOH HOH A . 
M 5 HOH 78  578 306 HOH HOH A . 
M 5 HOH 79  579 193 HOH HOH A . 
M 5 HOH 80  580 17  HOH HOH A . 
M 5 HOH 81  581 14  HOH HOH A . 
M 5 HOH 82  582 136 HOH HOH A . 
M 5 HOH 83  583 21  HOH HOH A . 
M 5 HOH 84  584 77  HOH HOH A . 
M 5 HOH 85  585 42  HOH HOH A . 
M 5 HOH 86  586 115 HOH HOH A . 
M 5 HOH 87  587 49  HOH HOH A . 
M 5 HOH 88  588 107 HOH HOH A . 
M 5 HOH 89  589 111 HOH HOH A . 
M 5 HOH 90  590 70  HOH HOH A . 
M 5 HOH 91  591 182 HOH HOH A . 
M 5 HOH 92  592 109 HOH HOH A . 
M 5 HOH 93  593 26  HOH HOH A . 
M 5 HOH 94  594 31  HOH HOH A . 
M 5 HOH 95  595 103 HOH HOH A . 
M 5 HOH 96  596 283 HOH HOH A . 
M 5 HOH 97  597 218 HOH HOH A . 
M 5 HOH 98  598 40  HOH HOH A . 
M 5 HOH 99  599 54  HOH HOH A . 
M 5 HOH 100 600 270 HOH HOH A . 
M 5 HOH 101 601 195 HOH HOH A . 
M 5 HOH 102 602 204 HOH HOH A . 
M 5 HOH 103 603 300 HOH HOH A . 
M 5 HOH 104 604 293 HOH HOH A . 
M 5 HOH 105 605 187 HOH HOH A . 
M 5 HOH 106 606 269 HOH HOH A . 
M 5 HOH 107 607 142 HOH HOH A . 
M 5 HOH 108 608 217 HOH HOH A . 
M 5 HOH 109 609 92  HOH HOH A . 
M 5 HOH 110 610 221 HOH HOH A . 
M 5 HOH 111 611 226 HOH HOH A . 
M 5 HOH 112 612 285 HOH HOH A . 
M 5 HOH 113 613 278 HOH HOH A . 
M 5 HOH 114 614 282 HOH HOH A . 
M 5 HOH 115 615 198 HOH HOH A . 
M 5 HOH 116 616 232 HOH HOH A . 
M 5 HOH 117 617 214 HOH HOH A . 
M 5 HOH 118 618 275 HOH HOH A . 
M 5 HOH 119 619 180 HOH HOH A . 
M 5 HOH 120 620 202 HOH HOH A . 
M 5 HOH 121 621 173 HOH HOH A . 
N 5 HOH 1   501 297 HOH HOH B . 
N 5 HOH 2   502 241 HOH HOH B . 
N 5 HOH 3   503 305 HOH HOH B . 
N 5 HOH 4   504 296 HOH HOH B . 
N 5 HOH 5   505 201 HOH HOH B . 
N 5 HOH 6   506 289 HOH HOH B . 
N 5 HOH 7   507 229 HOH HOH B . 
N 5 HOH 8   508 265 HOH HOH B . 
N 5 HOH 9   509 233 HOH HOH B . 
N 5 HOH 10  510 97  HOH HOH B . 
N 5 HOH 11  511 203 HOH HOH B . 
N 5 HOH 12  512 58  HOH HOH B . 
N 5 HOH 13  513 44  HOH HOH B . 
N 5 HOH 14  514 137 HOH HOH B . 
N 5 HOH 15  515 39  HOH HOH B . 
N 5 HOH 16  516 24  HOH HOH B . 
N 5 HOH 17  517 128 HOH HOH B . 
N 5 HOH 18  518 177 HOH HOH B . 
N 5 HOH 19  519 132 HOH HOH B . 
N 5 HOH 20  520 213 HOH HOH B . 
N 5 HOH 21  521 53  HOH HOH B . 
N 5 HOH 22  522 169 HOH HOH B . 
N 5 HOH 23  523 254 HOH HOH B . 
N 5 HOH 24  524 72  HOH HOH B . 
N 5 HOH 25  525 290 HOH HOH B . 
N 5 HOH 26  526 286 HOH HOH B . 
N 5 HOH 27  527 2   HOH HOH B . 
N 5 HOH 28  528 129 HOH HOH B . 
N 5 HOH 29  529 87  HOH HOH B . 
N 5 HOH 30  530 236 HOH HOH B . 
N 5 HOH 31  531 268 HOH HOH B . 
N 5 HOH 32  532 156 HOH HOH B . 
N 5 HOH 33  533 158 HOH HOH B . 
N 5 HOH 34  534 85  HOH HOH B . 
N 5 HOH 35  535 298 HOH HOH B . 
N 5 HOH 36  536 50  HOH HOH B . 
N 5 HOH 37  537 260 HOH HOH B . 
N 5 HOH 38  538 118 HOH HOH B . 
N 5 HOH 39  539 261 HOH HOH B . 
N 5 HOH 40  540 84  HOH HOH B . 
N 5 HOH 41  541 240 HOH HOH B . 
N 5 HOH 42  542 249 HOH HOH B . 
N 5 HOH 43  543 43  HOH HOH B . 
N 5 HOH 44  544 83  HOH HOH B . 
N 5 HOH 45  545 91  HOH HOH B . 
N 5 HOH 46  546 41  HOH HOH B . 
N 5 HOH 47  547 185 HOH HOH B . 
N 5 HOH 48  548 171 HOH HOH B . 
N 5 HOH 49  549 47  HOH HOH B . 
N 5 HOH 50  550 106 HOH HOH B . 
N 5 HOH 51  551 149 HOH HOH B . 
N 5 HOH 52  552 52  HOH HOH B . 
N 5 HOH 53  553 299 HOH HOH B . 
N 5 HOH 54  554 5   HOH HOH B . 
N 5 HOH 55  555 133 HOH HOH B . 
N 5 HOH 56  556 178 HOH HOH B . 
N 5 HOH 57  557 205 HOH HOH B . 
N 5 HOH 58  558 164 HOH HOH B . 
N 5 HOH 59  559 75  HOH HOH B . 
N 5 HOH 60  560 110 HOH HOH B . 
N 5 HOH 61  561 114 HOH HOH B . 
N 5 HOH 62  562 63  HOH HOH B . 
N 5 HOH 63  563 6   HOH HOH B . 
N 5 HOH 64  564 29  HOH HOH B . 
N 5 HOH 65  565 250 HOH HOH B . 
N 5 HOH 66  566 161 HOH HOH B . 
N 5 HOH 67  567 150 HOH HOH B . 
N 5 HOH 68  568 160 HOH HOH B . 
N 5 HOH 69  569 175 HOH HOH B . 
N 5 HOH 70  570 200 HOH HOH B . 
N 5 HOH 71  571 246 HOH HOH B . 
N 5 HOH 72  572 222 HOH HOH B . 
N 5 HOH 73  573 60  HOH HOH B . 
N 5 HOH 74  574 25  HOH HOH B . 
N 5 HOH 75  575 67  HOH HOH B . 
N 5 HOH 76  576 235 HOH HOH B . 
N 5 HOH 77  577 22  HOH HOH B . 
N 5 HOH 78  578 23  HOH HOH B . 
N 5 HOH 79  579 247 HOH HOH B . 
N 5 HOH 80  580 207 HOH HOH B . 
N 5 HOH 81  581 255 HOH HOH B . 
N 5 HOH 82  582 11  HOH HOH B . 
N 5 HOH 83  583 189 HOH HOH B . 
N 5 HOH 84  584 37  HOH HOH B . 
N 5 HOH 85  585 225 HOH HOH B . 
N 5 HOH 86  586 167 HOH HOH B . 
N 5 HOH 87  587 166 HOH HOH B . 
N 5 HOH 88  588 197 HOH HOH B . 
N 5 HOH 89  589 74  HOH HOH B . 
N 5 HOH 90  590 219 HOH HOH B . 
N 5 HOH 91  591 126 HOH HOH B . 
N 5 HOH 92  592 304 HOH HOH B . 
N 5 HOH 93  593 230 HOH HOH B . 
N 5 HOH 94  594 90  HOH HOH B . 
N 5 HOH 95  595 81  HOH HOH B . 
N 5 HOH 96  596 143 HOH HOH B . 
N 5 HOH 97  597 119 HOH HOH B . 
N 5 HOH 98  598 33  HOH HOH B . 
N 5 HOH 99  599 113 HOH HOH B . 
N 5 HOH 100 600 165 HOH HOH B . 
N 5 HOH 101 601 141 HOH HOH B . 
N 5 HOH 102 602 199 HOH HOH B . 
N 5 HOH 103 603 65  HOH HOH B . 
N 5 HOH 104 604 216 HOH HOH B . 
N 5 HOH 105 605 127 HOH HOH B . 
N 5 HOH 106 606 10  HOH HOH B . 
N 5 HOH 107 607 68  HOH HOH B . 
N 5 HOH 108 608 263 HOH HOH B . 
N 5 HOH 109 609 238 HOH HOH B . 
N 5 HOH 110 610 35  HOH HOH B . 
N 5 HOH 111 611 94  HOH HOH B . 
N 5 HOH 112 612 20  HOH HOH B . 
N 5 HOH 113 613 244 HOH HOH B . 
N 5 HOH 114 614 262 HOH HOH B . 
N 5 HOH 115 615 258 HOH HOH B . 
N 5 HOH 116 616 287 HOH HOH B . 
N 5 HOH 117 617 209 HOH HOH B . 
N 5 HOH 118 618 208 HOH HOH B . 
N 5 HOH 119 619 144 HOH HOH B . 
N 5 HOH 120 620 82  HOH HOH B . 
N 5 HOH 121 621 302 HOH HOH B . 
N 5 HOH 122 622 272 HOH HOH B . 
N 5 HOH 123 623 276 HOH HOH B . 
N 5 HOH 124 624 242 HOH HOH B . 
N 5 HOH 125 625 295 HOH HOH B . 
N 5 HOH 126 626 134 HOH HOH B . 
N 5 HOH 127 627 135 HOH HOH B . 
N 5 HOH 128 628 274 HOH HOH B . 
N 5 HOH 129 629 154 HOH HOH B . 
N 5 HOH 130 630 140 HOH HOH B . 
N 5 HOH 131 631 174 HOH HOH B . 
N 5 HOH 132 632 279 HOH HOH B . 
N 5 HOH 133 633 273 HOH HOH B . 
N 5 HOH 134 634 284 HOH HOH B . 
O 5 HOH 1   501 4   HOH HOH C . 
O 5 HOH 2   502 234 HOH HOH C . 
O 5 HOH 3   503 125 HOH HOH C . 
O 5 HOH 4   504 220 HOH HOH C . 
O 5 HOH 5   505 228 HOH HOH C . 
O 5 HOH 6   506 66  HOH HOH C . 
O 5 HOH 7   507 145 HOH HOH C . 
O 5 HOH 8   508 196 HOH HOH C . 
O 5 HOH 9   509 71  HOH HOH C . 
O 5 HOH 10  510 78  HOH HOH C . 
O 5 HOH 11  511 179 HOH HOH C . 
O 5 HOH 12  512 59  HOH HOH C . 
O 5 HOH 13  513 301 HOH HOH C . 
O 5 HOH 14  514 62  HOH HOH C . 
O 5 HOH 15  515 291 HOH HOH C . 
O 5 HOH 16  516 155 HOH HOH C . 
O 5 HOH 17  517 99  HOH HOH C . 
O 5 HOH 18  518 122 HOH HOH C . 
O 5 HOH 19  519 223 HOH HOH C . 
O 5 HOH 20  520 211 HOH HOH C . 
O 5 HOH 21  521 51  HOH HOH C . 
O 5 HOH 22  522 151 HOH HOH C . 
O 5 HOH 23  523 194 HOH HOH C . 
O 5 HOH 24  524 152 HOH HOH C . 
O 5 HOH 25  525 69  HOH HOH C . 
O 5 HOH 26  526 146 HOH HOH C . 
O 5 HOH 27  527 104 HOH HOH C . 
O 5 HOH 28  528 245 HOH HOH C . 
O 5 HOH 29  529 153 HOH HOH C . 
O 5 HOH 30  530 147 HOH HOH C . 
O 5 HOH 31  531 181 HOH HOH C . 
O 5 HOH 32  532 120 HOH HOH C . 
O 5 HOH 33  533 256 HOH HOH C . 
O 5 HOH 34  534 183 HOH HOH C . 
O 5 HOH 35  535 102 HOH HOH C . 
O 5 HOH 36  536 248 HOH HOH C . 
O 5 HOH 37  537 253 HOH HOH C . 
O 5 HOH 38  538 264 HOH HOH C . 
O 5 HOH 39  539 191 HOH HOH C . 
O 5 HOH 40  540 157 HOH HOH C . 
O 5 HOH 41  541 206 HOH HOH C . 
O 5 HOH 42  542 130 HOH HOH C . 
O 5 HOH 43  543 231 HOH HOH C . 
O 5 HOH 44  544 281 HOH HOH C . 
# 
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 C SER 128 ? OG  ? C SER 135 OG  
2 1 Y 1 C GLN 146 ? CG  ? C GLN 153 CG  
3 1 Y 1 C GLN 146 ? CD  ? C GLN 153 CD  
4 1 Y 1 C GLN 146 ? OE1 ? C GLN 153 OE1 
5 1 Y 1 C GLN 146 ? NE2 ? C GLN 153 NE2 
6 1 Y 1 C GLU 175 ? CG  ? C GLU 182 CG  
7 1 Y 1 C GLU 175 ? CD  ? C GLU 182 CD  
8 1 Y 1 C GLU 175 ? OE1 ? C GLU 182 OE1 
9 1 Y 1 C GLU 175 ? OE2 ? C GLU 182 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       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0425 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.71 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DGW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.569 
_cell.length_a_esd                 ? 
_cell.length_b                     80.309 
_cell.length_b_esd                 ? 
_cell.length_c                     105.613 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DGW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DGW 
_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             2.00 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.51 
_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              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Bis-Tris pH 6.5, 0.2 M NaCl, 25% (w/v) PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-02-22 
_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   0.9201 
_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                        'NSLS-II BEAMLINE 17-ID-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9201 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-2 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DGW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.72 
_reflns.d_resolution_low                               28.59 
_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                                     354684 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.095 
_reflns.pdbx_Rpim_I_all                                0.063 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.992 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.07 
_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                                    1.72 
_reflns_shell.d_res_low                                     1.75 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             17788 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.587 
_reflns_shell.pdbx_Rpim_I_all                               0.377 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.87 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.445 
_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]                            0.93 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -1.58 
_refine.aniso_B[2][2]                            0.34 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.88 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               52.117 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.934 
_refine.correlation_coeff_Fo_to_Fc_free          0.912 
_refine.details                                  
;HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Chain C of the final TvVip1 with CTP structure demonstrated significant static disorder. Therefore, chain C of TvVip1 with CTP was modeled as an NCS copy of chains A and B and refinement was performed utilizing TLS restraints.
;
_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                                 9DGW 
_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                            1.72 
_refine.ls_d_res_low                             28.59 
_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                     85544 
_refine.ls_number_reflns_R_free                  4454 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.10 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.26284 
_refine.ls_R_factor_R_free                       0.29231 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.26133 
_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                    MASK 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.164 
_refine.pdbx_overall_ESU_R_Free                  0.149 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                            ? 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.72 
_refine_hist.d_res_low                        28.59 
_refine_hist.number_atoms_solvent             299 
_refine_hist.number_atoms_total               7234 
_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        6743 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         192 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  0.012  7136  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.016  6576  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.511  1.826  9674  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.772  1.777  15156 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.104  5.000  841   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 6.542  5.000  36    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.212 10.000 1248  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.103  0.200  1055  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  8288  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  1692  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.141  3.786  3373  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.140  3.786  3373  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.964  6.813  4211  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.964  6.814  4212  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.260  3.779  3763  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.256  3.776  3752  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.101  6.939  5416  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.054  35.64  7842  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 3.061  35.61  7806  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.720 
_refine_ls_shell.d_res_low                        1.765 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             328 
_refine_ls_shell.number_reflns_R_work             6239 
_refine_ls_shell.percent_reflns_obs               98.83 
_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                  0.375 
_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   20 
_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                  0.380 
# 
_struct.entry_id                     9DGW 
_struct.title                        'X-ray crystal structure of the Viperin-like enzyme from T. virens with bound CTP and SAM' 
_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        9DGW 
_struct_keywords.text            'viperin-like enzyme, CTP, SAM, 4Fe-4S cluster, ANTIVIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'ANTIVIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 3 ? 
H N N 4 ? 
I N N 2 ? 
J N N 4 ? 
K N N 2 ? 
L N N 3 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    G9MQB8_HYPVG 
_struct_ref.pdbx_db_accession          G9MQB8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GQVPVSVNYHFSRKCNKECLFCFHTATTSHVEKPENAKRGLTLLKQAGMKKINFAGGEPFLYPKFLGEMIDFCKETLQLE
SVSIVTNGSLVKEQFLQKHGRNIDILAVSCDSFNEATNIKIGRGSGDNVQKLYEIGSWCQKYDIKFKLNTVVNKFNHLED
MNDHLNALQPFRWKCFQVLIVTGENDSDKTLRNAHSLTISDDEFDRFCERHSSQTCLVPEPNRLMAKSYLILDEYMRFLD
RNGQQPSKSILEVGVQQALQAVFWDEEAFVERGGIYDWNKSSCSSDSKDLEW
;
_struct_ref.pdbx_align_begin           17 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9DGW A 24 ? 315 ? G9MQB8 17 ? 308 ? 17 308 
2 1 9DGW B 24 ? 315 ? G9MQB8 17 ? 308 ? 17 308 
3 1 9DGW C 24 ? 315 ? G9MQB8 17 ? 308 ? 17 308 
# 
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 9DGW MET A 1  ? UNP G9MQB8 ? ? 'initiating methionine' -6 1  
1 9DGW HIS A 2  ? UNP G9MQB8 ? ? 'expression tag'        -5 2  
1 9DGW HIS A 3  ? UNP G9MQB8 ? ? 'expression tag'        -4 3  
1 9DGW HIS A 4  ? UNP G9MQB8 ? ? 'expression tag'        -3 4  
1 9DGW HIS A 5  ? UNP G9MQB8 ? ? 'expression tag'        -2 5  
1 9DGW HIS A 6  ? UNP G9MQB8 ? ? 'expression tag'        -1 6  
1 9DGW HIS A 7  ? UNP G9MQB8 ? ? 'expression tag'        0  7  
1 9DGW SER A 8  ? UNP G9MQB8 ? ? 'expression tag'        1  8  
1 9DGW SER A 9  ? UNP G9MQB8 ? ? 'expression tag'        2  9  
1 9DGW GLY A 10 ? UNP G9MQB8 ? ? 'expression tag'        3  10 
1 9DGW VAL A 11 ? UNP G9MQB8 ? ? 'expression tag'        4  11 
1 9DGW ASP A 12 ? UNP G9MQB8 ? ? 'expression tag'        5  12 
1 9DGW LEU A 13 ? UNP G9MQB8 ? ? 'expression tag'        6  13 
1 9DGW GLY A 14 ? UNP G9MQB8 ? ? 'expression tag'        7  14 
1 9DGW THR A 15 ? UNP G9MQB8 ? ? 'expression tag'        8  15 
1 9DGW GLU A 16 ? UNP G9MQB8 ? ? 'expression tag'        9  16 
1 9DGW ASN A 17 ? UNP G9MQB8 ? ? 'expression tag'        10 17 
1 9DGW LEU A 18 ? UNP G9MQB8 ? ? 'expression tag'        11 18 
1 9DGW TYR A 19 ? UNP G9MQB8 ? ? 'expression tag'        12 19 
1 9DGW PHE A 20 ? UNP G9MQB8 ? ? 'expression tag'        13 20 
1 9DGW GLN A 21 ? UNP G9MQB8 ? ? 'expression tag'        14 21 
1 9DGW SER A 22 ? UNP G9MQB8 ? ? 'expression tag'        15 22 
1 9DGW MET A 23 ? UNP G9MQB8 ? ? 'expression tag'        16 23 
2 9DGW MET B 1  ? UNP G9MQB8 ? ? 'initiating methionine' -6 24 
2 9DGW HIS B 2  ? UNP G9MQB8 ? ? 'expression tag'        -5 25 
2 9DGW HIS B 3  ? UNP G9MQB8 ? ? 'expression tag'        -4 26 
2 9DGW HIS B 4  ? UNP G9MQB8 ? ? 'expression tag'        -3 27 
2 9DGW HIS B 5  ? UNP G9MQB8 ? ? 'expression tag'        -2 28 
2 9DGW HIS B 6  ? UNP G9MQB8 ? ? 'expression tag'        -1 29 
2 9DGW HIS B 7  ? UNP G9MQB8 ? ? 'expression tag'        0  30 
2 9DGW SER B 8  ? UNP G9MQB8 ? ? 'expression tag'        1  31 
2 9DGW SER B 9  ? UNP G9MQB8 ? ? 'expression tag'        2  32 
2 9DGW GLY B 10 ? UNP G9MQB8 ? ? 'expression tag'        3  33 
2 9DGW VAL B 11 ? UNP G9MQB8 ? ? 'expression tag'        4  34 
2 9DGW ASP B 12 ? UNP G9MQB8 ? ? 'expression tag'        5  35 
2 9DGW LEU B 13 ? UNP G9MQB8 ? ? 'expression tag'        6  36 
2 9DGW GLY B 14 ? UNP G9MQB8 ? ? 'expression tag'        7  37 
2 9DGW THR B 15 ? UNP G9MQB8 ? ? 'expression tag'        8  38 
2 9DGW GLU B 16 ? UNP G9MQB8 ? ? 'expression tag'        9  39 
2 9DGW ASN B 17 ? UNP G9MQB8 ? ? 'expression tag'        10 40 
2 9DGW LEU B 18 ? UNP G9MQB8 ? ? 'expression tag'        11 41 
2 9DGW TYR B 19 ? UNP G9MQB8 ? ? 'expression tag'        12 42 
2 9DGW PHE B 20 ? UNP G9MQB8 ? ? 'expression tag'        13 43 
2 9DGW GLN B 21 ? UNP G9MQB8 ? ? 'expression tag'        14 44 
2 9DGW SER B 22 ? UNP G9MQB8 ? ? 'expression tag'        15 45 
2 9DGW MET B 23 ? UNP G9MQB8 ? ? 'expression tag'        16 46 
3 9DGW MET C 1  ? UNP G9MQB8 ? ? 'initiating methionine' -6 47 
3 9DGW HIS C 2  ? UNP G9MQB8 ? ? 'expression tag'        -5 48 
3 9DGW HIS C 3  ? UNP G9MQB8 ? ? 'expression tag'        -4 49 
3 9DGW HIS C 4  ? UNP G9MQB8 ? ? 'expression tag'        -3 50 
3 9DGW HIS C 5  ? UNP G9MQB8 ? ? 'expression tag'        -2 51 
3 9DGW HIS C 6  ? UNP G9MQB8 ? ? 'expression tag'        -1 52 
3 9DGW HIS C 7  ? UNP G9MQB8 ? ? 'expression tag'        0  53 
3 9DGW SER C 8  ? UNP G9MQB8 ? ? 'expression tag'        1  54 
3 9DGW SER C 9  ? UNP G9MQB8 ? ? 'expression tag'        2  55 
3 9DGW GLY C 10 ? UNP G9MQB8 ? ? 'expression tag'        3  56 
3 9DGW VAL C 11 ? UNP G9MQB8 ? ? 'expression tag'        4  57 
3 9DGW ASP C 12 ? UNP G9MQB8 ? ? 'expression tag'        5  58 
3 9DGW LEU C 13 ? UNP G9MQB8 ? ? 'expression tag'        6  59 
3 9DGW GLY C 14 ? UNP G9MQB8 ? ? 'expression tag'        7  60 
3 9DGW THR C 15 ? UNP G9MQB8 ? ? 'expression tag'        8  61 
3 9DGW GLU C 16 ? UNP G9MQB8 ? ? 'expression tag'        9  62 
3 9DGW ASN C 17 ? UNP G9MQB8 ? ? 'expression tag'        10 63 
3 9DGW LEU C 18 ? UNP G9MQB8 ? ? 'expression tag'        11 64 
3 9DGW TYR C 19 ? UNP G9MQB8 ? ? 'expression tag'        12 65 
3 9DGW PHE C 20 ? UNP G9MQB8 ? ? 'expression tag'        13 66 
3 9DGW GLN C 21 ? UNP G9MQB8 ? ? 'expression tag'        14 67 
3 9DGW SER C 22 ? UNP G9MQB8 ? ? 'expression tag'        15 68 
3 9DGW MET C 23 ? UNP G9MQB8 ? ? 'expression tag'        16 69 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,M 
2 1 B,G,H,I,N 
3 1 C,J,K,L,O 
# 
_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 LYS A 56  ? ALA A 70  ? LYS A 49  ALA A 63  1 ? 15 
HELX_P HELX_P2  AA2 GLU A 81  ? LEU A 84  ? GLU A 74  LEU A 77  5 ? 4  
HELX_P HELX_P3  AA3 TYR A 85  ? THR A 99  ? TYR A 78  THR A 92  1 ? 15 
HELX_P HELX_P4  AA4 LYS A 115 ? GLY A 123 ? LYS A 108 GLY A 116 1 ? 9  
HELX_P HELX_P5  AA5 ARG A 124 ? ILE A 126 ? ARG A 117 ILE A 119 5 ? 3  
HELX_P HELX_P6  AA6 ASN A 137 ? GLY A 145 ? ASN A 130 GLY A 138 1 ? 9  
HELX_P HELX_P7  AA7 ASP A 150 ? ASP A 166 ? ASP A 143 ASP A 159 1 ? 17 
HELX_P HELX_P8  AA8 MET A 184 ? GLN A 192 ? MET A 177 GLN A 185 1 ? 9  
HELX_P HELX_P9  AA9 ALA A 217 ? THR A 221 ? ALA A 210 THR A 214 5 ? 5  
HELX_P HELX_P10 AB1 SER A 223 ? HIS A 234 ? SER A 216 HIS A 227 1 ? 12 
HELX_P HELX_P11 AB2 PRO A 244 ? ALA A 249 ? PRO A 237 ALA A 242 1 ? 6  
HELX_P HELX_P12 AB3 SER A 272 ? GLY A 277 ? SER A 265 GLY A 270 1 ? 6  
HELX_P HELX_P13 AB4 GLY A 277 ? ALA A 284 ? GLY A 270 ALA A 277 1 ? 8  
HELX_P HELX_P14 AB5 ASP A 288 ? ARG A 295 ? ASP A 281 ARG A 288 1 ? 8  
HELX_P HELX_P15 AB6 LYS B 56  ? GLY B 71  ? LYS B 49  GLY B 64  1 ? 16 
HELX_P HELX_P16 AB7 GLU B 81  ? LEU B 84  ? GLU B 74  LEU B 77  5 ? 4  
HELX_P HELX_P17 AB8 TYR B 85  ? THR B 99  ? TYR B 78  THR B 92  1 ? 15 
HELX_P HELX_P18 AB9 LYS B 115 ? GLY B 123 ? LYS B 108 GLY B 116 1 ? 9  
HELX_P HELX_P19 AC1 ARG B 124 ? ILE B 126 ? ARG B 117 ILE B 119 5 ? 3  
HELX_P HELX_P20 AC2 ASN B 137 ? ILE B 144 ? ASN B 130 ILE B 137 1 ? 8  
HELX_P HELX_P21 AC3 ASP B 150 ? ASP B 166 ? ASP B 143 ASP B 159 1 ? 17 
HELX_P HELX_P22 AC4 MET B 184 ? GLN B 192 ? MET B 177 GLN B 185 1 ? 9  
HELX_P HELX_P23 AC5 ALA B 217 ? THR B 221 ? ALA B 210 THR B 214 5 ? 5  
HELX_P HELX_P24 AC6 SER B 223 ? ARG B 233 ? SER B 216 ARG B 226 1 ? 11 
HELX_P HELX_P25 AC7 PRO B 244 ? ALA B 249 ? PRO B 237 ALA B 242 1 ? 6  
HELX_P HELX_P26 AC8 SER B 272 ? GLN B 283 ? SER B 265 GLN B 276 1 ? 12 
HELX_P HELX_P27 AC9 ASP B 288 ? ARG B 295 ? ASP B 281 ARG B 288 1 ? 8  
HELX_P HELX_P28 AD1 LYS C 56  ? ALA C 70  ? LYS C 49  ALA C 63  1 ? 15 
HELX_P HELX_P29 AD2 GLU C 81  ? LEU C 84  ? GLU C 74  LEU C 77  5 ? 4  
HELX_P HELX_P30 AD3 TYR C 85  ? THR C 99  ? TYR C 78  THR C 92  1 ? 15 
HELX_P HELX_P31 AD4 LYS C 115 ? GLY C 123 ? LYS C 108 GLY C 116 1 ? 9  
HELX_P HELX_P32 AD5 ARG C 124 ? ILE C 126 ? ARG C 117 ILE C 119 5 ? 3  
HELX_P HELX_P33 AD6 ASN C 137 ? GLY C 145 ? ASN C 130 GLY C 138 1 ? 9  
HELX_P HELX_P34 AD7 ASP C 150 ? TYR C 165 ? ASP C 143 TYR C 158 1 ? 16 
HELX_P HELX_P35 AD8 MET C 184 ? GLN C 192 ? MET C 177 GLN C 185 1 ? 9  
HELX_P HELX_P36 AD9 ASN C 216 ? LEU C 220 ? ASN C 209 LEU C 213 5 ? 5  
HELX_P HELX_P37 AE1 SER C 223 ? ARG C 233 ? SER C 216 ARG C 226 1 ? 11 
HELX_P HELX_P38 AE2 PRO C 244 ? ALA C 249 ? PRO C 237 ALA C 242 1 ? 6  
HELX_P HELX_P39 AE3 SER C 272 ? GLY C 277 ? SER C 265 GLY C 270 1 ? 6  
HELX_P HELX_P40 AE4 GLY C 277 ? GLN C 283 ? GLY C 270 GLN C 276 1 ? 7  
HELX_P HELX_P41 AE5 ASP C 288 ? ARG C 295 ? ASP C 281 ARG C 288 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A CYS 38 SG  ? ? ? 1_555 E SF4 . FE2 ? ? A CYS 31  A SF4 402 1_555 ? ? ? ? ? ? ? 2.207 ? ? 
metalc2  metalc ? ? A CYS 42 SG  ? ? ? 1_555 E SF4 . FE1 ? ? A CYS 35  A SF4 402 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc3  metalc ? ? A CYS 45 SG  ? ? ? 1_555 E SF4 . FE4 ? ? A CYS 38  A SF4 402 1_555 ? ? ? ? ? ? ? 2.265 ? ? 
metalc4  metalc ? ? E SF4 .  FE3 ? ? ? 1_555 F SAM . OXT ? ? A SF4 402 A SAM 403 1_555 ? ? ? ? ? ? ? 2.237 ? ? 
metalc5  metalc ? ? E SF4 .  FE3 ? ? ? 1_555 F SAM . N   ? ? A SF4 402 A SAM 403 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc6  metalc ? ? B CYS 38 SG  ? ? ? 1_555 G SF4 . FE1 ? ? B CYS 31  B SF4 401 1_555 ? ? ? ? ? ? ? 2.216 ? ? 
metalc7  metalc ? ? B CYS 42 SG  ? ? ? 1_555 G SF4 . FE2 ? ? B CYS 35  B SF4 401 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc8  metalc ? ? B CYS 45 SG  ? ? ? 1_555 G SF4 . FE3 ? ? B CYS 38  B SF4 401 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc9  metalc ? ? G SF4 .  FE4 ? ? ? 1_555 H SAM . O   ? ? B SF4 401 B SAM 402 1_555 ? ? ? ? ? ? ? 2.215 ? ? 
metalc10 metalc ? ? G SF4 .  FE4 ? ? ? 1_555 H SAM . N   ? ? B SF4 401 B SAM 402 1_555 ? ? ? ? ? ? ? 2.347 ? ? 
metalc11 metalc ? ? C CYS 38 SG  ? ? ? 1_555 L SF4 . FE3 ? ? C CYS 31  C SF4 403 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc12 metalc ? ? C CYS 42 SG  ? ? ? 1_555 L SF4 . FE2 ? ? C CYS 35  C SF4 403 1_555 ? ? ? ? ? ? ? 2.485 ? ? 
metalc13 metalc ? ? C CYS 45 SG  ? ? ? 1_555 L SF4 . FE4 ? ? C CYS 38  C SF4 403 1_555 ? ? ? ? ? ? ? 2.383 ? ? 
metalc14 metalc ? ? J SAM .  N   ? ? ? 1_555 L SF4 . FE1 ? ? C SAM 401 C SF4 403 1_555 ? ? ? ? ? ? ? 2.502 ? ? 
metalc15 metalc ? ? J SAM .  O   ? ? ? 1_555 L SF4 . FE1 ? ? C SAM 401 C SF4 403 1_555 ? ? ? ? ? ? ? 1.907 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 38 ? A CYS 31  ? 1_555 FE2 ? E SF4 . ? A SF4 402 ? 1_555 S1 ? E SF4 . ? A SF4 402 ? 1_555 112.0 ? 
2  SG  ? A CYS 38 ? A CYS 31  ? 1_555 FE2 ? E SF4 . ? A SF4 402 ? 1_555 S3 ? E SF4 . ? A SF4 402 ? 1_555 123.5 ? 
3  S1  ? E SF4 .  ? A SF4 402 ? 1_555 FE2 ? E SF4 . ? A SF4 402 ? 1_555 S3 ? E SF4 . ? A SF4 402 ? 1_555 103.4 ? 
4  SG  ? A CYS 38 ? A CYS 31  ? 1_555 FE2 ? E SF4 . ? A SF4 402 ? 1_555 S4 ? E SF4 . ? A SF4 402 ? 1_555 103.2 ? 
5  S1  ? E SF4 .  ? A SF4 402 ? 1_555 FE2 ? E SF4 . ? A SF4 402 ? 1_555 S4 ? E SF4 . ? A SF4 402 ? 1_555 110.3 ? 
6  S3  ? E SF4 .  ? A SF4 402 ? 1_555 FE2 ? E SF4 . ? A SF4 402 ? 1_555 S4 ? E SF4 . ? A SF4 402 ? 1_555 103.8 ? 
7  SG  ? A CYS 42 ? A CYS 35  ? 1_555 FE1 ? E SF4 . ? A SF4 402 ? 1_555 S2 ? E SF4 . ? A SF4 402 ? 1_555 117.3 ? 
8  SG  ? A CYS 42 ? A CYS 35  ? 1_555 FE1 ? E SF4 . ? A SF4 402 ? 1_555 S3 ? E SF4 . ? A SF4 402 ? 1_555 109.7 ? 
9  S2  ? E SF4 .  ? A SF4 402 ? 1_555 FE1 ? E SF4 . ? A SF4 402 ? 1_555 S3 ? E SF4 . ? A SF4 402 ? 1_555 104.8 ? 
10 SG  ? A CYS 42 ? A CYS 35  ? 1_555 FE1 ? E SF4 . ? A SF4 402 ? 1_555 S4 ? E SF4 . ? A SF4 402 ? 1_555 115.5 ? 
11 S2  ? E SF4 .  ? A SF4 402 ? 1_555 FE1 ? E SF4 . ? A SF4 402 ? 1_555 S4 ? E SF4 . ? A SF4 402 ? 1_555 104.7 ? 
12 S3  ? E SF4 .  ? A SF4 402 ? 1_555 FE1 ? E SF4 . ? A SF4 402 ? 1_555 S4 ? E SF4 . ? A SF4 402 ? 1_555 103.4 ? 
13 SG  ? A CYS 45 ? A CYS 38  ? 1_555 FE4 ? E SF4 . ? A SF4 402 ? 1_555 S1 ? E SF4 . ? A SF4 402 ? 1_555 115.8 ? 
14 SG  ? A CYS 45 ? A CYS 38  ? 1_555 FE4 ? E SF4 . ? A SF4 402 ? 1_555 S2 ? E SF4 . ? A SF4 402 ? 1_555 121.4 ? 
15 S1  ? E SF4 .  ? A SF4 402 ? 1_555 FE4 ? E SF4 . ? A SF4 402 ? 1_555 S2 ? E SF4 . ? A SF4 402 ? 1_555 103.1 ? 
16 SG  ? A CYS 45 ? A CYS 38  ? 1_555 FE4 ? E SF4 . ? A SF4 402 ? 1_555 S3 ? E SF4 . ? A SF4 402 ? 1_555 103.5 ? 
17 S1  ? E SF4 .  ? A SF4 402 ? 1_555 FE4 ? E SF4 . ? A SF4 402 ? 1_555 S3 ? E SF4 . ? A SF4 402 ? 1_555 104.9 ? 
18 S2  ? E SF4 .  ? A SF4 402 ? 1_555 FE4 ? E SF4 . ? A SF4 402 ? 1_555 S3 ? E SF4 . ? A SF4 402 ? 1_555 106.8 ? 
19 OXT ? F SAM .  ? A SAM 403 ? 1_555 FE3 ? E SF4 . ? A SF4 402 ? 1_555 S1 ? E SF4 . ? A SF4 402 ? 1_555 147.4 ? 
20 OXT ? F SAM .  ? A SAM 403 ? 1_555 FE3 ? E SF4 . ? A SF4 402 ? 1_555 S2 ? E SF4 . ? A SF4 402 ? 1_555 98.2  ? 
21 S1  ? E SF4 .  ? A SF4 402 ? 1_555 FE3 ? E SF4 . ? A SF4 402 ? 1_555 S2 ? E SF4 . ? A SF4 402 ? 1_555 99.2  ? 
22 OXT ? F SAM .  ? A SAM 403 ? 1_555 FE3 ? E SF4 . ? A SF4 402 ? 1_555 S4 ? E SF4 . ? A SF4 402 ? 1_555 98.8  ? 
23 S1  ? E SF4 .  ? A SF4 402 ? 1_555 FE3 ? E SF4 . ? A SF4 402 ? 1_555 S4 ? E SF4 . ? A SF4 402 ? 1_555 104.4 ? 
24 S2  ? E SF4 .  ? A SF4 402 ? 1_555 FE3 ? E SF4 . ? A SF4 402 ? 1_555 S4 ? E SF4 . ? A SF4 402 ? 1_555 101.4 ? 
25 OXT ? F SAM .  ? A SAM 403 ? 1_555 FE3 ? E SF4 . ? A SF4 402 ? 1_555 N  ? F SAM . ? A SAM 403 ? 1_555 69.6  ? 
26 S1  ? E SF4 .  ? A SF4 402 ? 1_555 FE3 ? E SF4 . ? A SF4 402 ? 1_555 N  ? F SAM . ? A SAM 403 ? 1_555 83.9  ? 
27 S2  ? E SF4 .  ? A SF4 402 ? 1_555 FE3 ? E SF4 . ? A SF4 402 ? 1_555 N  ? F SAM . ? A SAM 403 ? 1_555 156.7 ? 
28 S4  ? E SF4 .  ? A SF4 402 ? 1_555 FE3 ? E SF4 . ? A SF4 402 ? 1_555 N  ? F SAM . ? A SAM 403 ? 1_555 100.1 ? 
29 SG  ? B CYS 38 ? B CYS 31  ? 1_555 FE1 ? G SF4 . ? B SF4 401 ? 1_555 S2 ? G SF4 . ? B SF4 401 ? 1_555 113.9 ? 
30 SG  ? B CYS 38 ? B CYS 31  ? 1_555 FE1 ? G SF4 . ? B SF4 401 ? 1_555 S3 ? G SF4 . ? B SF4 401 ? 1_555 105.4 ? 
31 S2  ? G SF4 .  ? B SF4 401 ? 1_555 FE1 ? G SF4 . ? B SF4 401 ? 1_555 S3 ? G SF4 . ? B SF4 401 ? 1_555 108.4 ? 
32 SG  ? B CYS 38 ? B CYS 31  ? 1_555 FE1 ? G SF4 . ? B SF4 401 ? 1_555 S4 ? G SF4 . ? B SF4 401 ? 1_555 122.1 ? 
33 S2  ? G SF4 .  ? B SF4 401 ? 1_555 FE1 ? G SF4 . ? B SF4 401 ? 1_555 S4 ? G SF4 . ? B SF4 401 ? 1_555 104.4 ? 
34 S3  ? G SF4 .  ? B SF4 401 ? 1_555 FE1 ? G SF4 . ? B SF4 401 ? 1_555 S4 ? G SF4 . ? B SF4 401 ? 1_555 101.3 ? 
35 SG  ? B CYS 42 ? B CYS 35  ? 1_555 FE2 ? G SF4 . ? B SF4 401 ? 1_555 S1 ? G SF4 . ? B SF4 401 ? 1_555 116.3 ? 
36 SG  ? B CYS 42 ? B CYS 35  ? 1_555 FE2 ? G SF4 . ? B SF4 401 ? 1_555 S3 ? G SF4 . ? B SF4 401 ? 1_555 119.0 ? 
37 S1  ? G SF4 .  ? B SF4 401 ? 1_555 FE2 ? G SF4 . ? B SF4 401 ? 1_555 S3 ? G SF4 . ? B SF4 401 ? 1_555 103.3 ? 
38 SG  ? B CYS 42 ? B CYS 35  ? 1_555 FE2 ? G SF4 . ? B SF4 401 ? 1_555 S4 ? G SF4 . ? B SF4 401 ? 1_555 107.3 ? 
39 S1  ? G SF4 .  ? B SF4 401 ? 1_555 FE2 ? G SF4 . ? B SF4 401 ? 1_555 S4 ? G SF4 . ? B SF4 401 ? 1_555 105.9 ? 
40 S3  ? G SF4 .  ? B SF4 401 ? 1_555 FE2 ? G SF4 . ? B SF4 401 ? 1_555 S4 ? G SF4 . ? B SF4 401 ? 1_555 103.8 ? 
41 SG  ? B CYS 45 ? B CYS 38  ? 1_555 FE3 ? G SF4 . ? B SF4 401 ? 1_555 S1 ? G SF4 . ? B SF4 401 ? 1_555 121.5 ? 
42 SG  ? B CYS 45 ? B CYS 38  ? 1_555 FE3 ? G SF4 . ? B SF4 401 ? 1_555 S2 ? G SF4 . ? B SF4 401 ? 1_555 117.4 ? 
43 S1  ? G SF4 .  ? B SF4 401 ? 1_555 FE3 ? G SF4 . ? B SF4 401 ? 1_555 S2 ? G SF4 . ? B SF4 401 ? 1_555 101.3 ? 
44 SG  ? B CYS 45 ? B CYS 38  ? 1_555 FE3 ? G SF4 . ? B SF4 401 ? 1_555 S4 ? G SF4 . ? B SF4 401 ? 1_555 106.1 ? 
45 S1  ? G SF4 .  ? B SF4 401 ? 1_555 FE3 ? G SF4 . ? B SF4 401 ? 1_555 S4 ? G SF4 . ? B SF4 401 ? 1_555 104.8 ? 
46 S2  ? G SF4 .  ? B SF4 401 ? 1_555 FE3 ? G SF4 . ? B SF4 401 ? 1_555 S4 ? G SF4 . ? B SF4 401 ? 1_555 103.9 ? 
47 O   ? H SAM .  ? B SAM 402 ? 1_555 FE4 ? G SF4 . ? B SF4 401 ? 1_555 S1 ? G SF4 . ? B SF4 401 ? 1_555 96.2  ? 
48 O   ? H SAM .  ? B SAM 402 ? 1_555 FE4 ? G SF4 . ? B SF4 401 ? 1_555 S2 ? G SF4 . ? B SF4 401 ? 1_555 150.0 ? 
49 S1  ? G SF4 .  ? B SF4 401 ? 1_555 FE4 ? G SF4 . ? B SF4 401 ? 1_555 S2 ? G SF4 . ? B SF4 401 ? 1_555 97.7  ? 
50 O   ? H SAM .  ? B SAM 402 ? 1_555 FE4 ? G SF4 . ? B SF4 401 ? 1_555 S3 ? G SF4 . ? B SF4 401 ? 1_555 96.5  ? 
51 S1  ? G SF4 .  ? B SF4 401 ? 1_555 FE4 ? G SF4 . ? B SF4 401 ? 1_555 S3 ? G SF4 . ? B SF4 401 ? 1_555 100.4 ? 
52 S2  ? G SF4 .  ? B SF4 401 ? 1_555 FE4 ? G SF4 . ? B SF4 401 ? 1_555 S3 ? G SF4 . ? B SF4 401 ? 1_555 106.9 ? 
53 O   ? H SAM .  ? B SAM 402 ? 1_555 FE4 ? G SF4 . ? B SF4 401 ? 1_555 N  ? H SAM . ? B SAM 402 ? 1_555 72.5  ? 
54 S1  ? G SF4 .  ? B SF4 401 ? 1_555 FE4 ? G SF4 . ? B SF4 401 ? 1_555 N  ? H SAM . ? B SAM 402 ? 1_555 157.1 ? 
55 S2  ? G SF4 .  ? B SF4 401 ? 1_555 FE4 ? G SF4 . ? B SF4 401 ? 1_555 N  ? H SAM . ? B SAM 402 ? 1_555 84.7  ? 
56 S3  ? G SF4 .  ? B SF4 401 ? 1_555 FE4 ? G SF4 . ? B SF4 401 ? 1_555 N  ? H SAM . ? B SAM 402 ? 1_555 100.6 ? 
57 SG  ? C CYS 38 ? C CYS 31  ? 1_555 FE3 ? L SF4 . ? C SF4 403 ? 1_555 S1 ? L SF4 . ? C SF4 403 ? 1_555 121.5 ? 
58 SG  ? C CYS 38 ? C CYS 31  ? 1_555 FE3 ? L SF4 . ? C SF4 403 ? 1_555 S2 ? L SF4 . ? C SF4 403 ? 1_555 121.0 ? 
59 S1  ? L SF4 .  ? C SF4 403 ? 1_555 FE3 ? L SF4 . ? C SF4 403 ? 1_555 S2 ? L SF4 . ? C SF4 403 ? 1_555 101.0 ? 
60 SG  ? C CYS 38 ? C CYS 31  ? 1_555 FE3 ? L SF4 . ? C SF4 403 ? 1_555 S4 ? L SF4 . ? C SF4 403 ? 1_555 104.8 ? 
61 S1  ? L SF4 .  ? C SF4 403 ? 1_555 FE3 ? L SF4 . ? C SF4 403 ? 1_555 S4 ? L SF4 . ? C SF4 403 ? 1_555 103.9 ? 
62 S2  ? L SF4 .  ? C SF4 403 ? 1_555 FE3 ? L SF4 . ? C SF4 403 ? 1_555 S4 ? L SF4 . ? C SF4 403 ? 1_555 101.8 ? 
63 SG  ? C CYS 42 ? C CYS 35  ? 1_555 FE2 ? L SF4 . ? C SF4 403 ? 1_555 S1 ? L SF4 . ? C SF4 403 ? 1_555 110.8 ? 
64 SG  ? C CYS 42 ? C CYS 35  ? 1_555 FE2 ? L SF4 . ? C SF4 403 ? 1_555 S3 ? L SF4 . ? C SF4 403 ? 1_555 114.3 ? 
65 S1  ? L SF4 .  ? C SF4 403 ? 1_555 FE2 ? L SF4 . ? C SF4 403 ? 1_555 S3 ? L SF4 . ? C SF4 403 ? 1_555 102.7 ? 
66 SG  ? C CYS 42 ? C CYS 35  ? 1_555 FE2 ? L SF4 . ? C SF4 403 ? 1_555 S4 ? L SF4 . ? C SF4 403 ? 1_555 117.8 ? 
67 S1  ? L SF4 .  ? C SF4 403 ? 1_555 FE2 ? L SF4 . ? C SF4 403 ? 1_555 S4 ? L SF4 . ? C SF4 403 ? 1_555 100.4 ? 
68 S3  ? L SF4 .  ? C SF4 403 ? 1_555 FE2 ? L SF4 . ? C SF4 403 ? 1_555 S4 ? L SF4 . ? C SF4 403 ? 1_555 108.9 ? 
69 SG  ? C CYS 45 ? C CYS 38  ? 1_555 FE4 ? L SF4 . ? C SF4 403 ? 1_555 S1 ? L SF4 . ? C SF4 403 ? 1_555 111.5 ? 
70 SG  ? C CYS 45 ? C CYS 38  ? 1_555 FE4 ? L SF4 . ? C SF4 403 ? 1_555 S2 ? L SF4 . ? C SF4 403 ? 1_555 112.7 ? 
71 S1  ? L SF4 .  ? C SF4 403 ? 1_555 FE4 ? L SF4 . ? C SF4 403 ? 1_555 S2 ? L SF4 . ? C SF4 403 ? 1_555 112.8 ? 
72 SG  ? C CYS 45 ? C CYS 38  ? 1_555 FE4 ? L SF4 . ? C SF4 403 ? 1_555 S3 ? L SF4 . ? C SF4 403 ? 1_555 118.7 ? 
73 S1  ? L SF4 .  ? C SF4 403 ? 1_555 FE4 ? L SF4 . ? C SF4 403 ? 1_555 S3 ? L SF4 . ? C SF4 403 ? 1_555 110.8 ? 
74 S2  ? L SF4 .  ? C SF4 403 ? 1_555 FE4 ? L SF4 . ? C SF4 403 ? 1_555 S3 ? L SF4 . ? C SF4 403 ? 1_555 88.4  ? 
75 N   ? J SAM .  ? C SAM 401 ? 1_555 FE1 ? L SF4 . ? C SF4 403 ? 1_555 S2 ? L SF4 . ? C SF4 403 ? 1_555 75.0  ? 
76 N   ? J SAM .  ? C SAM 401 ? 1_555 FE1 ? L SF4 . ? C SF4 403 ? 1_555 S3 ? L SF4 . ? C SF4 403 ? 1_555 155.6 ? 
77 S2  ? L SF4 .  ? C SF4 403 ? 1_555 FE1 ? L SF4 . ? C SF4 403 ? 1_555 S3 ? L SF4 . ? C SF4 403 ? 1_555 97.5  ? 
78 N   ? J SAM .  ? C SAM 401 ? 1_555 FE1 ? L SF4 . ? C SF4 403 ? 1_555 S4 ? L SF4 . ? C SF4 403 ? 1_555 102.9 ? 
79 S2  ? L SF4 .  ? C SF4 403 ? 1_555 FE1 ? L SF4 . ? C SF4 403 ? 1_555 S4 ? L SF4 . ? C SF4 403 ? 1_555 109.6 ? 
80 S3  ? L SF4 .  ? C SF4 403 ? 1_555 FE1 ? L SF4 . ? C SF4 403 ? 1_555 S4 ? L SF4 . ? C SF4 403 ? 1_555 101.5 ? 
81 N   ? J SAM .  ? C SAM 401 ? 1_555 FE1 ? L SF4 . ? C SF4 403 ? 1_555 O  ? J SAM . ? C SAM 401 ? 1_555 73.6  ? 
82 S2  ? L SF4 .  ? C SF4 403 ? 1_555 FE1 ? L SF4 . ? C SF4 403 ? 1_555 O  ? J SAM . ? C SAM 401 ? 1_555 134.8 ? 
83 S3  ? L SF4 .  ? C SF4 403 ? 1_555 FE1 ? L SF4 . ? C SF4 403 ? 1_555 O  ? J SAM . ? C SAM 401 ? 1_555 97.9  ? 
84 S4  ? L SF4 .  ? C SF4 403 ? 1_555 FE1 ? L SF4 . ? C SF4 403 ? 1_555 O  ? J SAM . ? C SAM 401 ? 1_555 108.4 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 79 A . ? GLY 72 A GLY 80 A ? GLY 73 A 1 17.39 
2 GLY 79 B . ? GLY 72 B GLY 80 B ? GLY 73 B 1 19.35 
3 GLY 79 C . ? GLY 72 C GLY 80 C ? GLY 73 C 1 10.61 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? parallel 
AA1 7 8 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? parallel 
AA2 5 6 ? parallel 
AA2 6 7 ? parallel 
AA2 7 8 ? parallel 
AA3 1 2 ? parallel 
AA3 2 3 ? parallel 
AA3 3 4 ? parallel 
AA3 4 5 ? parallel 
AA3 5 6 ? parallel 
AA3 6 7 ? parallel 
AA3 7 8 ? parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 240 ? GLU A 243 ? LEU A 233 GLU A 236 
AA1 2 ARG A 195 ? GLN A 200 ? ARG A 188 GLN A 193 
AA1 3 LYS A 168 ? VAL A 175 ? LYS A 161 VAL A 168 
AA1 4 ILE A 128 ? SER A 132 ? ILE A 121 SER A 125 
AA1 5 SER A 104 ? THR A 109 ? SER A 97  THR A 102 
AA1 6 LYS A 74  ? ALA A 78  ? LYS A 67  ALA A 71  
AA1 7 SER A 29  ? HIS A 33  ? SER A 22  HIS A 26  
AA1 8 ILE A 254 ? LEU A 255 ? ILE A 247 LEU A 248 
AA2 1 LEU B 240 ? GLU B 243 ? LEU B 233 GLU B 236 
AA2 2 ARG B 195 ? GLN B 200 ? ARG B 188 GLN B 193 
AA2 3 LYS B 168 ? VAL B 175 ? LYS B 161 VAL B 168 
AA2 4 ILE B 128 ? SER B 132 ? ILE B 121 SER B 125 
AA2 5 SER B 104 ? THR B 109 ? SER B 97  THR B 102 
AA2 6 LYS B 74  ? ALA B 78  ? LYS B 67  ALA B 71  
AA2 7 SER B 29  ? HIS B 33  ? SER B 22  HIS B 26  
AA2 8 ILE B 254 ? LEU B 255 ? ILE B 247 LEU B 248 
AA3 1 LEU C 240 ? GLU C 243 ? LEU C 233 GLU C 236 
AA3 2 ARG C 195 ? GLN C 200 ? ARG C 188 GLN C 193 
AA3 3 LYS C 168 ? VAL C 175 ? LYS C 161 VAL C 168 
AA3 4 ILE C 128 ? SER C 132 ? ILE C 121 SER C 125 
AA3 5 SER C 104 ? THR C 109 ? SER C 97  THR C 102 
AA3 6 LYS C 74  ? ALA C 78  ? LYS C 67  ALA C 71  
AA3 7 SER C 29  ? HIS C 33  ? SER C 22  HIS C 26  
AA3 8 LEU C 253 ? LEU C 255 ? LEU C 246 LEU C 248 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 241 ? O VAL A 234 N TRP A 196 ? N TRP A 189 
AA1 2 3 O LYS A 197 ? O LYS A 190 N THR A 173 ? N THR A 166 
AA1 3 4 O LYS A 168 ? O LYS A 161 N LEU A 129 ? N LEU A 122 
AA1 4 5 O ALA A 130 ? O ALA A 123 N ILE A 107 ? N ILE A 100 
AA1 5 6 O SER A 106 ? O SER A 99  N ILE A 75  ? N ILE A 68  
AA1 6 7 O ASN A 76  ? O ASN A 69  N TYR A 32  ? N TYR A 25  
AA1 7 8 N ASN A 31  ? N ASN A 24  O LEU A 255 ? O LEU A 248 
AA2 1 2 O GLU B 243 ? O GLU B 236 N CYS B 198 ? N CYS B 191 
AA2 2 3 O PHE B 199 ? O PHE B 192 N VAL B 175 ? N VAL B 168 
AA2 3 4 O ASN B 172 ? O ASN B 165 N VAL B 131 ? N VAL B 124 
AA2 4 5 O ALA B 130 ? O ALA B 123 N ILE B 107 ? N ILE B 100 
AA2 5 6 O SER B 106 ? O SER B 99  N PHE B 77  ? N PHE B 70  
AA2 6 7 O ASN B 76  ? O ASN B 69  N TYR B 32  ? N TYR B 25  
AA2 7 8 N ASN B 31  ? N ASN B 24  O LEU B 255 ? O LEU B 248 
AA3 1 2 O VAL C 241 ? O VAL C 234 N TRP C 196 ? N TRP C 189 
AA3 2 3 O LYS C 197 ? O LYS C 190 N THR C 173 ? N THR C 166 
AA3 3 4 O LYS C 170 ? O LYS C 163 N LEU C 129 ? N LEU C 122 
AA3 4 5 O ALA C 130 ? O ALA C 123 N ILE C 107 ? N ILE C 100 
AA3 5 6 O SER C 106 ? O SER C 99  N PHE C 77  ? N PHE C 70  
AA3 6 7 O ALA C 78  ? O ALA C 71  N TYR C 32  ? N TYR C 25  
AA3 7 8 N ASN C 31  ? N ASN C 24  O LEU C 255 ? O LEU C 248 
# 
_pdbx_entry_details.entry_id                   9DGW 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 34  ? ? -142.91 35.29   
2 1 ASN A 201 ? ? -143.14 28.69   
3 1 ASN A 258 ? ? -153.58 7.43    
4 1 ALA B 71  ? ? -141.31 -158.57 
5 1 ASN B 201 ? ? -144.68 30.65   
6 1 ASN B 258 ? ? -153.02 29.93   
7 1 TYR C 78  ? ? -118.58 65.56   
8 1 ASP C 159 ? ? 61.10   61.66   
9 1 ASN C 201 ? ? -142.51 32.50   
# 
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[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 18.433 16.457 11.460  0.0677 0.0248 0.0256 -0.0316 0.0241 0.0012  1.8095 1.6264 2.6276 -0.0393 
0.7699 -0.1554 -0.0760 0.0067  0.0694  0.1603 0.1150  -0.0594 -0.0339 -0.1974 0.1754 
'X-RAY DIFFRACTION' 2 ? refined 7.826  14.371 -24.583 0.0481 0.0445 0.0392 0.0368  0.0048 -0.0155 1.6867 1.6748 2.4854 -0.2747 
0.3126 0.3087  0.1180  -0.0684 -0.0497 0.1928 -0.1056 -0.0803 -0.0509 0.1558  0.0557 
'X-RAY DIFFRACTION' 3 ? refined 20.358 52.350 -46.315 0.1279 0.1817 0.1064 -0.0128 0.0240 -0.0046 1.8102 3.4241 3.9268 -0.4017 
0.6881 -1.3634 -0.0096 -0.0164 0.0261  0.0946 -0.0685 -0.2623 -0.1547 0.2494  0.2378 
# 
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.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 17  A 295 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 1 A 401 A 403 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 3 2 B 17  B 298 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 4 2 B 401 B 403 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 5 3 C 18  C 297 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 6 3 C 401 C 403 ? ? ? ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET -6  ? A MET 1   
2   1 Y 1 A HIS -5  ? A HIS 2   
3   1 Y 1 A HIS -4  ? A HIS 3   
4   1 Y 1 A HIS -3  ? A HIS 4   
5   1 Y 1 A HIS -2  ? A HIS 5   
6   1 Y 1 A HIS -1  ? A HIS 6   
7   1 Y 1 A HIS 0   ? A HIS 7   
8   1 Y 1 A SER 1   ? A SER 8   
9   1 Y 1 A SER 2   ? A SER 9   
10  1 Y 1 A GLY 3   ? A GLY 10  
11  1 Y 1 A VAL 4   ? A VAL 11  
12  1 Y 1 A ASP 5   ? A ASP 12  
13  1 Y 1 A LEU 6   ? A LEU 13  
14  1 Y 1 A GLY 7   ? A GLY 14  
15  1 Y 1 A THR 8   ? A THR 15  
16  1 Y 1 A GLU 9   ? A GLU 16  
17  1 Y 1 A ASN 10  ? A ASN 17  
18  1 Y 1 A LEU 11  ? A LEU 18  
19  1 Y 1 A TYR 12  ? A TYR 19  
20  1 Y 1 A PHE 13  ? A PHE 20  
21  1 Y 1 A GLN 14  ? A GLN 21  
22  1 Y 1 A SER 15  ? A SER 22  
23  1 Y 1 A MET 16  ? A MET 23  
24  1 Y 1 A LYS 296 ? A LYS 303 
25  1 Y 1 A SER 297 ? A SER 304 
26  1 Y 1 A SER 298 ? A SER 305 
27  1 Y 1 A CYS 299 ? A CYS 306 
28  1 Y 1 A SER 300 ? A SER 307 
29  1 Y 1 A SER 301 ? A SER 308 
30  1 Y 1 A ASP 302 ? A ASP 309 
31  1 Y 1 A SER 303 ? A SER 310 
32  1 Y 1 A LYS 304 ? A LYS 311 
33  1 Y 1 A ASP 305 ? A ASP 312 
34  1 Y 1 A LEU 306 ? A LEU 313 
35  1 Y 1 A GLU 307 ? A GLU 314 
36  1 Y 1 A TRP 308 ? A TRP 315 
37  1 Y 1 B MET -6  ? B MET 1   
38  1 Y 1 B HIS -5  ? B HIS 2   
39  1 Y 1 B HIS -4  ? B HIS 3   
40  1 Y 1 B HIS -3  ? B HIS 4   
41  1 Y 1 B HIS -2  ? B HIS 5   
42  1 Y 1 B HIS -1  ? B HIS 6   
43  1 Y 1 B HIS 0   ? B HIS 7   
44  1 Y 1 B SER 1   ? B SER 8   
45  1 Y 1 B SER 2   ? B SER 9   
46  1 Y 1 B GLY 3   ? B GLY 10  
47  1 Y 1 B VAL 4   ? B VAL 11  
48  1 Y 1 B ASP 5   ? B ASP 12  
49  1 Y 1 B LEU 6   ? B LEU 13  
50  1 Y 1 B GLY 7   ? B GLY 14  
51  1 Y 1 B THR 8   ? B THR 15  
52  1 Y 1 B GLU 9   ? B GLU 16  
53  1 Y 1 B ASN 10  ? B ASN 17  
54  1 Y 1 B LEU 11  ? B LEU 18  
55  1 Y 1 B TYR 12  ? B TYR 19  
56  1 Y 1 B PHE 13  ? B PHE 20  
57  1 Y 1 B GLN 14  ? B GLN 21  
58  1 Y 1 B SER 15  ? B SER 22  
59  1 Y 1 B MET 16  ? B MET 23  
60  1 Y 1 B CYS 299 ? B CYS 306 
61  1 Y 1 B SER 300 ? B SER 307 
62  1 Y 1 B SER 301 ? B SER 308 
63  1 Y 1 B ASP 302 ? B ASP 309 
64  1 Y 1 B SER 303 ? B SER 310 
65  1 Y 1 B LYS 304 ? B LYS 311 
66  1 Y 1 B ASP 305 ? B ASP 312 
67  1 Y 1 B LEU 306 ? B LEU 313 
68  1 Y 1 B GLU 307 ? B GLU 314 
69  1 Y 1 B TRP 308 ? B TRP 315 
70  1 Y 1 C MET -6  ? C MET 1   
71  1 Y 1 C HIS -5  ? C HIS 2   
72  1 Y 1 C HIS -4  ? C HIS 3   
73  1 Y 1 C HIS -3  ? C HIS 4   
74  1 Y 1 C HIS -2  ? C HIS 5   
75  1 Y 1 C HIS -1  ? C HIS 6   
76  1 Y 1 C HIS 0   ? C HIS 7   
77  1 Y 1 C SER 1   ? C SER 8   
78  1 Y 1 C SER 2   ? C SER 9   
79  1 Y 1 C GLY 3   ? C GLY 10  
80  1 Y 1 C VAL 4   ? C VAL 11  
81  1 Y 1 C ASP 5   ? C ASP 12  
82  1 Y 1 C LEU 6   ? C LEU 13  
83  1 Y 1 C GLY 7   ? C GLY 14  
84  1 Y 1 C THR 8   ? C THR 15  
85  1 Y 1 C GLU 9   ? C GLU 16  
86  1 Y 1 C ASN 10  ? C ASN 17  
87  1 Y 1 C LEU 11  ? C LEU 18  
88  1 Y 1 C TYR 12  ? C TYR 19  
89  1 Y 1 C PHE 13  ? C PHE 20  
90  1 Y 1 C GLN 14  ? C GLN 21  
91  1 Y 1 C SER 15  ? C SER 22  
92  1 Y 1 C MET 16  ? C MET 23  
93  1 Y 1 C GLY 17  ? C GLY 24  
94  1 Y 1 C ASN 258 ? C ASN 265 
95  1 Y 1 C GLY 259 ? C GLY 266 
96  1 Y 1 C GLN 260 ? C GLN 267 
97  1 Y 1 C GLN 261 ? C GLN 268 
98  1 Y 1 C SER 298 ? C SER 305 
99  1 Y 1 C CYS 299 ? C CYS 306 
100 1 Y 1 C SER 300 ? C SER 307 
101 1 Y 1 C SER 301 ? C SER 308 
102 1 Y 1 C ASP 302 ? C ASP 309 
103 1 Y 1 C SER 303 ? C SER 310 
104 1 Y 1 C LYS 304 ? C LYS 311 
105 1 Y 1 C ASP 305 ? C ASP 312 
106 1 Y 1 C LEU 306 ? C LEU 313 
107 1 Y 1 C GLU 307 ? C GLU 314 
108 1 Y 1 C TRP 308 ? C TRP 315 
# 
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  
CTP N1     N  N N 74  
CTP C2     C  N N 75  
CTP N3     N  N N 76  
CTP C4     C  N N 77  
CTP C5     C  N N 78  
CTP C6     C  N N 79  
CTP O2     O  N N 80  
CTP N4     N  N N 81  
CTP "C1'"  C  N R 82  
CTP "C2'"  C  N R 83  
CTP "O2'"  O  N N 84  
CTP "C3'"  C  N S 85  
CTP "C4'"  C  N R 86  
CTP "O4'"  O  N N 87  
CTP "O3'"  O  N N 88  
CTP "C5'"  C  N N 89  
CTP "O5'"  O  N N 90  
CTP PA     P  N S 91  
CTP O1A    O  N N 92  
CTP O2A    O  N N 93  
CTP O3A    O  N N 94  
CTP PB     P  N R 95  
CTP O1B    O  N N 96  
CTP O2B    O  N N 97  
CTP O3B    O  N N 98  
CTP PG     P  N N 99  
CTP O1G    O  N N 100 
CTP O2G    O  N N 101 
CTP O3G    O  N N 102 
CTP H5     H  N N 103 
CTP H6     H  N N 104 
CTP HN41   H  N N 105 
CTP HN42   H  N N 106 
CTP "H1'"  H  N N 107 
CTP "H2'"  H  N N 108 
CTP "HO2'" H  N N 109 
CTP "H3'"  H  N N 110 
CTP "H4'"  H  N N 111 
CTP "HO3'" H  N N 112 
CTP "H5'1" H  N N 113 
CTP "H5'2" H  N N 114 
CTP HOA2   H  N N 115 
CTP HOB2   H  N N 116 
CTP HOG2   H  N N 117 
CTP HOG3   H  N N 118 
CYS N      N  N N 119 
CYS CA     C  N R 120 
CYS C      C  N N 121 
CYS O      O  N N 122 
CYS CB     C  N N 123 
CYS SG     S  N N 124 
CYS OXT    O  N N 125 
CYS H      H  N N 126 
CYS H2     H  N N 127 
CYS HA     H  N N 128 
CYS HB2    H  N N 129 
CYS HB3    H  N N 130 
CYS HG     H  N N 131 
CYS HXT    H  N N 132 
GLN N      N  N N 133 
GLN CA     C  N S 134 
GLN C      C  N N 135 
GLN O      O  N N 136 
GLN CB     C  N N 137 
GLN CG     C  N N 138 
GLN CD     C  N N 139 
GLN OE1    O  N N 140 
GLN NE2    N  N N 141 
GLN OXT    O  N N 142 
GLN H      H  N N 143 
GLN H2     H  N N 144 
GLN HA     H  N N 145 
GLN HB2    H  N N 146 
GLN HB3    H  N N 147 
GLN HG2    H  N N 148 
GLN HG3    H  N N 149 
GLN HE21   H  N N 150 
GLN HE22   H  N N 151 
GLN HXT    H  N N 152 
GLU N      N  N N 153 
GLU CA     C  N S 154 
GLU C      C  N N 155 
GLU O      O  N N 156 
GLU CB     C  N N 157 
GLU CG     C  N N 158 
GLU CD     C  N N 159 
GLU OE1    O  N N 160 
GLU OE2    O  N N 161 
GLU OXT    O  N N 162 
GLU H      H  N N 163 
GLU H2     H  N N 164 
GLU HA     H  N N 165 
GLU HB2    H  N N 166 
GLU HB3    H  N N 167 
GLU HG2    H  N N 168 
GLU HG3    H  N N 169 
GLU HE2    H  N N 170 
GLU HXT    H  N N 171 
GLY N      N  N N 172 
GLY CA     C  N N 173 
GLY C      C  N N 174 
GLY O      O  N N 175 
GLY OXT    O  N N 176 
GLY H      H  N N 177 
GLY H2     H  N N 178 
GLY HA2    H  N N 179 
GLY HA3    H  N N 180 
GLY HXT    H  N N 181 
HIS N      N  N N 182 
HIS CA     C  N S 183 
HIS C      C  N N 184 
HIS O      O  N N 185 
HIS CB     C  N N 186 
HIS CG     C  Y N 187 
HIS ND1    N  Y N 188 
HIS CD2    C  Y N 189 
HIS CE1    C  Y N 190 
HIS NE2    N  Y N 191 
HIS OXT    O  N N 192 
HIS H      H  N N 193 
HIS H2     H  N N 194 
HIS HA     H  N N 195 
HIS HB2    H  N N 196 
HIS HB3    H  N N 197 
HIS HD1    H  N N 198 
HIS HD2    H  N N 199 
HIS HE1    H  N N 200 
HIS HE2    H  N N 201 
HIS HXT    H  N N 202 
HOH O      O  N N 203 
HOH H1     H  N N 204 
HOH H2     H  N N 205 
ILE N      N  N N 206 
ILE CA     C  N S 207 
ILE C      C  N N 208 
ILE O      O  N N 209 
ILE CB     C  N S 210 
ILE CG1    C  N N 211 
ILE CG2    C  N N 212 
ILE CD1    C  N N 213 
ILE OXT    O  N N 214 
ILE H      H  N N 215 
ILE H2     H  N N 216 
ILE HA     H  N N 217 
ILE HB     H  N N 218 
ILE HG12   H  N N 219 
ILE HG13   H  N N 220 
ILE HG21   H  N N 221 
ILE HG22   H  N N 222 
ILE HG23   H  N N 223 
ILE HD11   H  N N 224 
ILE HD12   H  N N 225 
ILE HD13   H  N N 226 
ILE HXT    H  N N 227 
LEU N      N  N N 228 
LEU CA     C  N S 229 
LEU C      C  N N 230 
LEU O      O  N N 231 
LEU CB     C  N N 232 
LEU CG     C  N N 233 
LEU CD1    C  N N 234 
LEU CD2    C  N N 235 
LEU OXT    O  N N 236 
LEU H      H  N N 237 
LEU H2     H  N N 238 
LEU HA     H  N N 239 
LEU HB2    H  N N 240 
LEU HB3    H  N N 241 
LEU HG     H  N N 242 
LEU HD11   H  N N 243 
LEU HD12   H  N N 244 
LEU HD13   H  N N 245 
LEU HD21   H  N N 246 
LEU HD22   H  N N 247 
LEU HD23   H  N N 248 
LEU HXT    H  N N 249 
LYS N      N  N N 250 
LYS CA     C  N S 251 
LYS C      C  N N 252 
LYS O      O  N N 253 
LYS CB     C  N N 254 
LYS CG     C  N N 255 
LYS CD     C  N N 256 
LYS CE     C  N N 257 
LYS NZ     N  N N 258 
LYS OXT    O  N N 259 
LYS H      H  N N 260 
LYS H2     H  N N 261 
LYS HA     H  N N 262 
LYS HB2    H  N N 263 
LYS HB3    H  N N 264 
LYS HG2    H  N N 265 
LYS HG3    H  N N 266 
LYS HD2    H  N N 267 
LYS HD3    H  N N 268 
LYS HE2    H  N N 269 
LYS HE3    H  N N 270 
LYS HZ1    H  N N 271 
LYS HZ2    H  N N 272 
LYS HZ3    H  N N 273 
LYS HXT    H  N N 274 
MET N      N  N N 275 
MET CA     C  N S 276 
MET C      C  N N 277 
MET O      O  N N 278 
MET CB     C  N N 279 
MET CG     C  N N 280 
MET SD     S  N N 281 
MET CE     C  N N 282 
MET OXT    O  N N 283 
MET H      H  N N 284 
MET H2     H  N N 285 
MET HA     H  N N 286 
MET HB2    H  N N 287 
MET HB3    H  N N 288 
MET HG2    H  N N 289 
MET HG3    H  N N 290 
MET HE1    H  N N 291 
MET HE2    H  N N 292 
MET HE3    H  N N 293 
MET HXT    H  N N 294 
PHE N      N  N N 295 
PHE CA     C  N S 296 
PHE C      C  N N 297 
PHE O      O  N N 298 
PHE CB     C  N N 299 
PHE CG     C  Y N 300 
PHE CD1    C  Y N 301 
PHE CD2    C  Y N 302 
PHE CE1    C  Y N 303 
PHE CE2    C  Y N 304 
PHE CZ     C  Y N 305 
PHE OXT    O  N N 306 
PHE H      H  N N 307 
PHE H2     H  N N 308 
PHE HA     H  N N 309 
PHE HB2    H  N N 310 
PHE HB3    H  N N 311 
PHE HD1    H  N N 312 
PHE HD2    H  N N 313 
PHE HE1    H  N N 314 
PHE HE2    H  N N 315 
PHE HZ     H  N N 316 
PHE HXT    H  N N 317 
PRO N      N  N N 318 
PRO CA     C  N S 319 
PRO C      C  N N 320 
PRO O      O  N N 321 
PRO CB     C  N N 322 
PRO CG     C  N N 323 
PRO CD     C  N N 324 
PRO OXT    O  N N 325 
PRO H      H  N N 326 
PRO HA     H  N N 327 
PRO HB2    H  N N 328 
PRO HB3    H  N N 329 
PRO HG2    H  N N 330 
PRO HG3    H  N N 331 
PRO HD2    H  N N 332 
PRO HD3    H  N N 333 
PRO HXT    H  N N 334 
SAM N      N  N N 335 
SAM CA     C  N S 336 
SAM C      C  N N 337 
SAM O      O  N N 338 
SAM OXT    O  N N 339 
SAM CB     C  N N 340 
SAM CG     C  N N 341 
SAM SD     S  N S 342 
SAM CE     C  N N 343 
SAM "C5'"  C  N N 344 
SAM "C4'"  C  N S 345 
SAM "O4'"  O  N N 346 
SAM "C3'"  C  N S 347 
SAM "O3'"  O  N N 348 
SAM "C2'"  C  N R 349 
SAM "O2'"  O  N N 350 
SAM "C1'"  C  N R 351 
SAM N9     N  Y N 352 
SAM C8     C  Y N 353 
SAM N7     N  Y N 354 
SAM C5     C  Y N 355 
SAM C6     C  Y N 356 
SAM N6     N  N N 357 
SAM N1     N  Y N 358 
SAM C2     C  Y N 359 
SAM N3     N  Y N 360 
SAM C4     C  Y N 361 
SAM HN1    H  N N 362 
SAM HN2    H  N N 363 
SAM HA     H  N N 364 
SAM HB1    H  N N 365 
SAM HB2    H  N N 366 
SAM HG1    H  N N 367 
SAM HG2    H  N N 368 
SAM HE1    H  N N 369 
SAM HE2    H  N N 370 
SAM HE3    H  N N 371 
SAM "H5'1" H  N N 372 
SAM "H5'2" H  N N 373 
SAM "H4'"  H  N N 374 
SAM "H3'"  H  N N 375 
SAM "HO3'" H  N N 376 
SAM "H2'"  H  N N 377 
SAM "HO2'" H  N N 378 
SAM "H1'"  H  N N 379 
SAM H8     H  N N 380 
SAM HN61   H  N N 381 
SAM HN62   H  N N 382 
SAM H2     H  N N 383 
SER N      N  N N 384 
SER CA     C  N S 385 
SER C      C  N N 386 
SER O      O  N N 387 
SER CB     C  N N 388 
SER OG     O  N N 389 
SER OXT    O  N N 390 
SER H      H  N N 391 
SER H2     H  N N 392 
SER HA     H  N N 393 
SER HB2    H  N N 394 
SER HB3    H  N N 395 
SER HG     H  N N 396 
SER HXT    H  N N 397 
SF4 FE1    FE N N 398 
SF4 FE2    FE N N 399 
SF4 FE3    FE N N 400 
SF4 FE4    FE N N 401 
SF4 S1     S  N N 402 
SF4 S2     S  N N 403 
SF4 S3     S  N N 404 
SF4 S4     S  N N 405 
THR N      N  N N 406 
THR CA     C  N S 407 
THR C      C  N N 408 
THR O      O  N N 409 
THR CB     C  N R 410 
THR OG1    O  N N 411 
THR CG2    C  N N 412 
THR OXT    O  N N 413 
THR H      H  N N 414 
THR H2     H  N N 415 
THR HA     H  N N 416 
THR HB     H  N N 417 
THR HG1    H  N N 418 
THR HG21   H  N N 419 
THR HG22   H  N N 420 
THR HG23   H  N N 421 
THR HXT    H  N N 422 
TRP N      N  N N 423 
TRP CA     C  N S 424 
TRP C      C  N N 425 
TRP O      O  N N 426 
TRP CB     C  N N 427 
TRP CG     C  Y N 428 
TRP CD1    C  Y N 429 
TRP CD2    C  Y N 430 
TRP NE1    N  Y N 431 
TRP CE2    C  Y N 432 
TRP CE3    C  Y N 433 
TRP CZ2    C  Y N 434 
TRP CZ3    C  Y N 435 
TRP CH2    C  Y N 436 
TRP OXT    O  N N 437 
TRP H      H  N N 438 
TRP H2     H  N N 439 
TRP HA     H  N N 440 
TRP HB2    H  N N 441 
TRP HB3    H  N N 442 
TRP HD1    H  N N 443 
TRP HE1    H  N N 444 
TRP HE3    H  N N 445 
TRP HZ2    H  N N 446 
TRP HZ3    H  N N 447 
TRP HH2    H  N N 448 
TRP HXT    H  N N 449 
TYR N      N  N N 450 
TYR CA     C  N S 451 
TYR C      C  N N 452 
TYR O      O  N N 453 
TYR CB     C  N N 454 
TYR CG     C  Y N 455 
TYR CD1    C  Y N 456 
TYR CD2    C  Y N 457 
TYR CE1    C  Y N 458 
TYR CE2    C  Y N 459 
TYR CZ     C  Y N 460 
TYR OH     O  N N 461 
TYR OXT    O  N N 462 
TYR H      H  N N 463 
TYR H2     H  N N 464 
TYR HA     H  N N 465 
TYR HB2    H  N N 466 
TYR HB3    H  N N 467 
TYR HD1    H  N N 468 
TYR HD2    H  N N 469 
TYR HE1    H  N N 470 
TYR HE2    H  N N 471 
TYR HH     H  N N 472 
TYR HXT    H  N N 473 
VAL N      N  N N 474 
VAL CA     C  N S 475 
VAL C      C  N N 476 
VAL O      O  N N 477 
VAL CB     C  N N 478 
VAL CG1    C  N N 479 
VAL CG2    C  N N 480 
VAL OXT    O  N N 481 
VAL H      H  N N 482 
VAL H2     H  N N 483 
VAL HA     H  N N 484 
VAL HB     H  N N 485 
VAL HG11   H  N N 486 
VAL HG12   H  N N 487 
VAL HG13   H  N N 488 
VAL HG21   H  N N 489 
VAL HG22   H  N N 490 
VAL HG23   H  N N 491 
VAL HXT    H  N N 492 
# 
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  
CTP N1    C2     sing N N 70  
CTP N1    C6     sing N N 71  
CTP N1    "C1'"  sing N N 72  
CTP C2    N3     sing N N 73  
CTP C2    O2     doub N N 74  
CTP N3    C4     doub N N 75  
CTP C4    C5     sing N N 76  
CTP C4    N4     sing N N 77  
CTP C5    C6     doub N N 78  
CTP C5    H5     sing N N 79  
CTP C6    H6     sing N N 80  
CTP N4    HN41   sing N N 81  
CTP N4    HN42   sing N N 82  
CTP "C1'" "C2'"  sing N N 83  
CTP "C1'" "O4'"  sing N N 84  
CTP "C1'" "H1'"  sing N N 85  
CTP "C2'" "O2'"  sing N N 86  
CTP "C2'" "C3'"  sing N N 87  
CTP "C2'" "H2'"  sing N N 88  
CTP "O2'" "HO2'" sing N N 89  
CTP "C3'" "C4'"  sing N N 90  
CTP "C3'" "O3'"  sing N N 91  
CTP "C3'" "H3'"  sing N N 92  
CTP "C4'" "O4'"  sing N N 93  
CTP "C4'" "C5'"  sing N N 94  
CTP "C4'" "H4'"  sing N N 95  
CTP "O3'" "HO3'" sing N N 96  
CTP "C5'" "O5'"  sing N N 97  
CTP "C5'" "H5'1" sing N N 98  
CTP "C5'" "H5'2" sing N N 99  
CTP "O5'" PA     sing N N 100 
CTP PA    O1A    doub N N 101 
CTP PA    O2A    sing N N 102 
CTP PA    O3A    sing N N 103 
CTP O2A   HOA2   sing N N 104 
CTP O3A   PB     sing N N 105 
CTP PB    O1B    doub N N 106 
CTP PB    O2B    sing N N 107 
CTP PB    O3B    sing N N 108 
CTP O2B   HOB2   sing N N 109 
CTP O3B   PG     sing N N 110 
CTP PG    O1G    doub N N 111 
CTP PG    O2G    sing N N 112 
CTP PG    O3G    sing N N 113 
CTP O2G   HOG2   sing N N 114 
CTP O3G   HOG3   sing N N 115 
CYS N     CA     sing N N 116 
CYS N     H      sing N N 117 
CYS N     H2     sing N N 118 
CYS CA    C      sing N N 119 
CYS CA    CB     sing N N 120 
CYS CA    HA     sing N N 121 
CYS C     O      doub N N 122 
CYS C     OXT    sing N N 123 
CYS CB    SG     sing N N 124 
CYS CB    HB2    sing N N 125 
CYS CB    HB3    sing N N 126 
CYS SG    HG     sing N N 127 
CYS OXT   HXT    sing N N 128 
GLN N     CA     sing N N 129 
GLN N     H      sing N N 130 
GLN N     H2     sing N N 131 
GLN CA    C      sing N N 132 
GLN CA    CB     sing N N 133 
GLN CA    HA     sing N N 134 
GLN C     O      doub N N 135 
GLN C     OXT    sing N N 136 
GLN CB    CG     sing N N 137 
GLN CB    HB2    sing N N 138 
GLN CB    HB3    sing N N 139 
GLN CG    CD     sing N N 140 
GLN CG    HG2    sing N N 141 
GLN CG    HG3    sing N N 142 
GLN CD    OE1    doub N N 143 
GLN CD    NE2    sing N N 144 
GLN NE2   HE21   sing N N 145 
GLN NE2   HE22   sing N N 146 
GLN OXT   HXT    sing N N 147 
GLU N     CA     sing N N 148 
GLU N     H      sing N N 149 
GLU N     H2     sing N N 150 
GLU CA    C      sing N N 151 
GLU CA    CB     sing N N 152 
GLU CA    HA     sing N N 153 
GLU C     O      doub N N 154 
GLU C     OXT    sing N N 155 
GLU CB    CG     sing N N 156 
GLU CB    HB2    sing N N 157 
GLU CB    HB3    sing N N 158 
GLU CG    CD     sing N N 159 
GLU CG    HG2    sing N N 160 
GLU CG    HG3    sing N N 161 
GLU CD    OE1    doub N N 162 
GLU CD    OE2    sing N N 163 
GLU OE2   HE2    sing N N 164 
GLU OXT   HXT    sing N N 165 
GLY N     CA     sing N N 166 
GLY N     H      sing N N 167 
GLY N     H2     sing N N 168 
GLY CA    C      sing N N 169 
GLY CA    HA2    sing N N 170 
GLY CA    HA3    sing N N 171 
GLY C     O      doub N N 172 
GLY C     OXT    sing N N 173 
GLY OXT   HXT    sing N N 174 
HIS N     CA     sing N N 175 
HIS N     H      sing N N 176 
HIS N     H2     sing N N 177 
HIS CA    C      sing N N 178 
HIS CA    CB     sing N N 179 
HIS CA    HA     sing N N 180 
HIS C     O      doub N N 181 
HIS C     OXT    sing N N 182 
HIS CB    CG     sing N N 183 
HIS CB    HB2    sing N N 184 
HIS CB    HB3    sing N N 185 
HIS CG    ND1    sing Y N 186 
HIS CG    CD2    doub Y N 187 
HIS ND1   CE1    doub Y N 188 
HIS ND1   HD1    sing N N 189 
HIS CD2   NE2    sing Y N 190 
HIS CD2   HD2    sing N N 191 
HIS CE1   NE2    sing Y N 192 
HIS CE1   HE1    sing N N 193 
HIS NE2   HE2    sing N N 194 
HIS OXT   HXT    sing N N 195 
HOH O     H1     sing N N 196 
HOH O     H2     sing N N 197 
ILE N     CA     sing N N 198 
ILE N     H      sing N N 199 
ILE N     H2     sing N N 200 
ILE CA    C      sing N N 201 
ILE CA    CB     sing N N 202 
ILE CA    HA     sing N N 203 
ILE C     O      doub N N 204 
ILE C     OXT    sing N N 205 
ILE CB    CG1    sing N N 206 
ILE CB    CG2    sing N N 207 
ILE CB    HB     sing N N 208 
ILE CG1   CD1    sing N N 209 
ILE CG1   HG12   sing N N 210 
ILE CG1   HG13   sing N N 211 
ILE CG2   HG21   sing N N 212 
ILE CG2   HG22   sing N N 213 
ILE CG2   HG23   sing N N 214 
ILE CD1   HD11   sing N N 215 
ILE CD1   HD12   sing N N 216 
ILE CD1   HD13   sing N N 217 
ILE OXT   HXT    sing N N 218 
LEU N     CA     sing N N 219 
LEU N     H      sing N N 220 
LEU N     H2     sing N N 221 
LEU CA    C      sing N N 222 
LEU CA    CB     sing N N 223 
LEU CA    HA     sing N N 224 
LEU C     O      doub N N 225 
LEU C     OXT    sing N N 226 
LEU CB    CG     sing N N 227 
LEU CB    HB2    sing N N 228 
LEU CB    HB3    sing N N 229 
LEU CG    CD1    sing N N 230 
LEU CG    CD2    sing N N 231 
LEU CG    HG     sing N N 232 
LEU CD1   HD11   sing N N 233 
LEU CD1   HD12   sing N N 234 
LEU CD1   HD13   sing N N 235 
LEU CD2   HD21   sing N N 236 
LEU CD2   HD22   sing N N 237 
LEU CD2   HD23   sing N N 238 
LEU OXT   HXT    sing N N 239 
LYS N     CA     sing N N 240 
LYS N     H      sing N N 241 
LYS N     H2     sing N N 242 
LYS CA    C      sing N N 243 
LYS CA    CB     sing N N 244 
LYS CA    HA     sing N N 245 
LYS C     O      doub N N 246 
LYS C     OXT    sing N N 247 
LYS CB    CG     sing N N 248 
LYS CB    HB2    sing N N 249 
LYS CB    HB3    sing N N 250 
LYS CG    CD     sing N N 251 
LYS CG    HG2    sing N N 252 
LYS CG    HG3    sing N N 253 
LYS CD    CE     sing N N 254 
LYS CD    HD2    sing N N 255 
LYS CD    HD3    sing N N 256 
LYS CE    NZ     sing N N 257 
LYS CE    HE2    sing N N 258 
LYS CE    HE3    sing N N 259 
LYS NZ    HZ1    sing N N 260 
LYS NZ    HZ2    sing N N 261 
LYS NZ    HZ3    sing N N 262 
LYS OXT   HXT    sing N N 263 
MET N     CA     sing N N 264 
MET N     H      sing N N 265 
MET N     H2     sing N N 266 
MET CA    C      sing N N 267 
MET CA    CB     sing N N 268 
MET CA    HA     sing N N 269 
MET C     O      doub N N 270 
MET C     OXT    sing N N 271 
MET CB    CG     sing N N 272 
MET CB    HB2    sing N N 273 
MET CB    HB3    sing N N 274 
MET CG    SD     sing N N 275 
MET CG    HG2    sing N N 276 
MET CG    HG3    sing N N 277 
MET SD    CE     sing N N 278 
MET CE    HE1    sing N N 279 
MET CE    HE2    sing N N 280 
MET CE    HE3    sing N N 281 
MET OXT   HXT    sing N N 282 
PHE N     CA     sing N N 283 
PHE N     H      sing N N 284 
PHE N     H2     sing N N 285 
PHE CA    C      sing N N 286 
PHE CA    CB     sing N N 287 
PHE CA    HA     sing N N 288 
PHE C     O      doub N N 289 
PHE C     OXT    sing N N 290 
PHE CB    CG     sing N N 291 
PHE CB    HB2    sing N N 292 
PHE CB    HB3    sing N N 293 
PHE CG    CD1    doub Y N 294 
PHE CG    CD2    sing Y N 295 
PHE CD1   CE1    sing Y N 296 
PHE CD1   HD1    sing N N 297 
PHE CD2   CE2    doub Y N 298 
PHE CD2   HD2    sing N N 299 
PHE CE1   CZ     doub Y N 300 
PHE CE1   HE1    sing N N 301 
PHE CE2   CZ     sing Y N 302 
PHE CE2   HE2    sing N N 303 
PHE CZ    HZ     sing N N 304 
PHE OXT   HXT    sing N N 305 
PRO N     CA     sing N N 306 
PRO N     CD     sing N N 307 
PRO N     H      sing N N 308 
PRO CA    C      sing N N 309 
PRO CA    CB     sing N N 310 
PRO CA    HA     sing N N 311 
PRO C     O      doub N N 312 
PRO C     OXT    sing N N 313 
PRO CB    CG     sing N N 314 
PRO CB    HB2    sing N N 315 
PRO CB    HB3    sing N N 316 
PRO CG    CD     sing N N 317 
PRO CG    HG2    sing N N 318 
PRO CG    HG3    sing N N 319 
PRO CD    HD2    sing N N 320 
PRO CD    HD3    sing N N 321 
PRO OXT   HXT    sing N N 322 
SAM N     CA     sing N N 323 
SAM N     HN1    sing N N 324 
SAM N     HN2    sing N N 325 
SAM CA    C      sing N N 326 
SAM CA    CB     sing N N 327 
SAM CA    HA     sing N N 328 
SAM C     O      doub N N 329 
SAM C     OXT    sing N N 330 
SAM CB    CG     sing N N 331 
SAM CB    HB1    sing N N 332 
SAM CB    HB2    sing N N 333 
SAM CG    SD     sing N N 334 
SAM CG    HG1    sing N N 335 
SAM CG    HG2    sing N N 336 
SAM SD    CE     sing N N 337 
SAM SD    "C5'"  sing N N 338 
SAM CE    HE1    sing N N 339 
SAM CE    HE2    sing N N 340 
SAM CE    HE3    sing N N 341 
SAM "C5'" "C4'"  sing N N 342 
SAM "C5'" "H5'1" sing N N 343 
SAM "C5'" "H5'2" sing N N 344 
SAM "C4'" "O4'"  sing N N 345 
SAM "C4'" "C3'"  sing N N 346 
SAM "C4'" "H4'"  sing N N 347 
SAM "O4'" "C1'"  sing N N 348 
SAM "C3'" "O3'"  sing N N 349 
SAM "C3'" "C2'"  sing N N 350 
SAM "C3'" "H3'"  sing N N 351 
SAM "O3'" "HO3'" sing N N 352 
SAM "C2'" "O2'"  sing N N 353 
SAM "C2'" "C1'"  sing N N 354 
SAM "C2'" "H2'"  sing N N 355 
SAM "O2'" "HO2'" sing N N 356 
SAM "C1'" N9     sing N N 357 
SAM "C1'" "H1'"  sing N N 358 
SAM N9    C8     sing Y N 359 
SAM N9    C4     sing Y N 360 
SAM C8    N7     doub Y N 361 
SAM C8    H8     sing N N 362 
SAM N7    C5     sing Y N 363 
SAM C5    C6     sing Y N 364 
SAM C5    C4     doub Y N 365 
SAM C6    N6     sing N N 366 
SAM C6    N1     doub Y N 367 
SAM N6    HN61   sing N N 368 
SAM N6    HN62   sing N N 369 
SAM N1    C2     sing Y N 370 
SAM C2    N3     doub Y N 371 
SAM C2    H2     sing N N 372 
SAM N3    C4     sing Y N 373 
SER N     CA     sing N N 374 
SER N     H      sing N N 375 
SER N     H2     sing N N 376 
SER CA    C      sing N N 377 
SER CA    CB     sing N N 378 
SER CA    HA     sing N N 379 
SER C     O      doub N N 380 
SER C     OXT    sing N N 381 
SER CB    OG     sing N N 382 
SER CB    HB2    sing N N 383 
SER CB    HB3    sing N N 384 
SER OG    HG     sing N N 385 
SER OXT   HXT    sing N N 386 
SF4 FE1   S2     sing N N 387 
SF4 FE1   S3     sing N N 388 
SF4 FE1   S4     sing N N 389 
SF4 FE2   S1     sing N N 390 
SF4 FE2   S3     sing N N 391 
SF4 FE2   S4     sing N N 392 
SF4 FE3   S1     sing N N 393 
SF4 FE3   S2     sing N N 394 
SF4 FE3   S4     sing N N 395 
SF4 FE4   S1     sing N N 396 
SF4 FE4   S2     sing N N 397 
SF4 FE4   S3     sing N N 398 
THR N     CA     sing N N 399 
THR N     H      sing N N 400 
THR N     H2     sing N N 401 
THR CA    C      sing N N 402 
THR CA    CB     sing N N 403 
THR CA    HA     sing N N 404 
THR C     O      doub N N 405 
THR C     OXT    sing N N 406 
THR CB    OG1    sing N N 407 
THR CB    CG2    sing N N 408 
THR CB    HB     sing N N 409 
THR OG1   HG1    sing N N 410 
THR CG2   HG21   sing N N 411 
THR CG2   HG22   sing N N 412 
THR CG2   HG23   sing N N 413 
THR OXT   HXT    sing N N 414 
TRP N     CA     sing N N 415 
TRP N     H      sing N N 416 
TRP N     H2     sing N N 417 
TRP CA    C      sing N N 418 
TRP CA    CB     sing N N 419 
TRP CA    HA     sing N N 420 
TRP C     O      doub N N 421 
TRP C     OXT    sing N N 422 
TRP CB    CG     sing N N 423 
TRP CB    HB2    sing N N 424 
TRP CB    HB3    sing N N 425 
TRP CG    CD1    doub Y N 426 
TRP CG    CD2    sing Y N 427 
TRP CD1   NE1    sing Y N 428 
TRP CD1   HD1    sing N N 429 
TRP CD2   CE2    doub Y N 430 
TRP CD2   CE3    sing Y N 431 
TRP NE1   CE2    sing Y N 432 
TRP NE1   HE1    sing N N 433 
TRP CE2   CZ2    sing Y N 434 
TRP CE3   CZ3    doub Y N 435 
TRP CE3   HE3    sing N N 436 
TRP CZ2   CH2    doub Y N 437 
TRP CZ2   HZ2    sing N N 438 
TRP CZ3   CH2    sing Y N 439 
TRP CZ3   HZ3    sing N N 440 
TRP CH2   HH2    sing N N 441 
TRP OXT   HXT    sing N N 442 
TYR N     CA     sing N N 443 
TYR N     H      sing N N 444 
TYR N     H2     sing N N 445 
TYR CA    C      sing N N 446 
TYR CA    CB     sing N N 447 
TYR CA    HA     sing N N 448 
TYR C     O      doub N N 449 
TYR C     OXT    sing N N 450 
TYR CB    CG     sing N N 451 
TYR CB    HB2    sing N N 452 
TYR CB    HB3    sing N N 453 
TYR CG    CD1    doub Y N 454 
TYR CG    CD2    sing Y N 455 
TYR CD1   CE1    sing Y N 456 
TYR CD1   HD1    sing N N 457 
TYR CD2   CE2    doub Y N 458 
TYR CD2   HD2    sing N N 459 
TYR CE1   CZ     doub Y N 460 
TYR CE1   HE1    sing N N 461 
TYR CE2   CZ     sing Y N 462 
TYR CE2   HE2    sing N N 463 
TYR CZ    OH     sing N N 464 
TYR OH    HH     sing N N 465 
TYR OXT   HXT    sing N N 466 
VAL N     CA     sing N N 467 
VAL N     H      sing N N 468 
VAL N     H2     sing N N 469 
VAL CA    C      sing N N 470 
VAL CA    CB     sing N N 471 
VAL CA    HA     sing N N 472 
VAL C     O      doub N N 473 
VAL C     OXT    sing N N 474 
VAL CB    CG1    sing N N 475 
VAL CB    CG2    sing N N 476 
VAL CB    HB     sing N N 477 
VAL CG1   HG11   sing N N 478 
VAL CG1   HG12   sing N N 479 
VAL CG1   HG13   sing N N 480 
VAL CG2   HG21   sing N N 481 
VAL CG2   HG22   sing N N 482 
VAL CG2   HG23   sing N N 483 
VAL OXT   HXT    sing N N 484 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM007491 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7N7I 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DGW 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.019391 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002283 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012452 
_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]   0.009534 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . GLY A 1 24  ? 1.435   -1.106  2.852   1.00 55.12  ?  17  GLY A N     1 
ATOM   2    C  CA    . GLY A 1 24  ? 1.982   -0.029  3.704   1.00 51.36  ?  17  GLY A CA    1 
ATOM   3    C  C     . GLY A 1 24  ? 3.246   0.587   3.096   1.00 48.87  ?  17  GLY A C     1 
ATOM   4    O  O     . GLY A 1 24  ? 3.834   0.045   2.167   1.00 49.98  ?  17  GLY A O     1 
ATOM   5    N  N     . GLN A 1 25  ? 3.626   1.763   3.606   1.00 45.88  ?  18  GLN A N     1 
ATOM   6    C  CA    . GLN A 1 25  ? 4.774   2.485   3.079   1.00 43.77  ?  18  GLN A CA    1 
ATOM   7    C  C     . GLN A 1 25  ? 6.057   1.797   3.532   1.00 42.87  ?  18  GLN A C     1 
ATOM   8    O  O     . GLN A 1 25  ? 6.075   1.125   4.555   1.00 42.97  ?  18  GLN A O     1 
ATOM   9    C  CB    . GLN A 1 25  ? 4.673   3.952   3.503   1.00 41.47  ?  18  GLN A CB    1 
ATOM   10   C  CG    . GLN A 1 25  ? 3.561   4.674   2.769   1.00 42.80  ?  18  GLN A CG    1 
ATOM   11   C  CD    . GLN A 1 25  ? 3.373   6.088   3.248   1.00 41.09  ?  18  GLN A CD    1 
ATOM   12   O  OE1   . GLN A 1 25  ? 3.215   6.334   4.436   1.00 40.05  ?  18  GLN A OE1   1 
ATOM   13   N  NE2   . GLN A 1 25  ? 3.347   7.037   2.330   1.00 41.19  ?  18  GLN A NE2   1 
ATOM   14   N  N     . VAL A 1 26  ? 7.127   1.922   2.745   1.00 42.44  ?  19  VAL A N     1 
ATOM   15   C  CA    . VAL A 1 26  ? 8.398   1.377   3.166   1.00 41.78  ?  19  VAL A CA    1 
ATOM   16   C  C     . VAL A 1 26  ? 9.211   2.507   3.803   1.00 38.78  ?  19  VAL A C     1 
ATOM   17   O  O     . VAL A 1 26  ? 9.527   3.481   3.108   1.00 37.98  ?  19  VAL A O     1 
ATOM   18   C  CB    . VAL A 1 26  ? 9.188   0.736   2.015   1.00 43.66  ?  19  VAL A CB    1 
ATOM   19   C  CG1   . VAL A 1 26  ? 10.584  0.356   2.481   1.00 43.01  ?  19  VAL A CG1   1 
ATOM   20   C  CG2   . VAL A 1 26  ? 8.455   -0.479  1.443   1.00 47.07  ?  19  VAL A CG2   1 
ATOM   21   N  N     . PRO A 1 27  ? 9.619   2.389   5.089   1.00 37.44  ?  20  PRO A N     1 
ATOM   22   C  CA    . PRO A 1 27  ? 10.298  3.487   5.779   1.00 34.90  ?  20  PRO A CA    1 
ATOM   23   C  C     . PRO A 1 27  ? 11.776  3.533   5.448   1.00 34.47  ?  20  PRO A C     1 
ATOM   24   O  O     . PRO A 1 27  ? 12.625  3.178   6.280   1.00 33.95  ?  20  PRO A O     1 
ATOM   25   C  CB    . PRO A 1 27  ? 10.121  3.161   7.253   1.00 34.31  ?  20  PRO A CB    1 
ATOM   26   C  CG    . PRO A 1 27  ? 10.107  1.648   7.296   1.00 36.50  ?  20  PRO A CG    1 
ATOM   27   C  CD    . PRO A 1 27  ? 9.382   1.268   6.010   1.00 38.54  ?  20  PRO A CD    1 
ATOM   28   N  N     . VAL A 1 28  ? 12.063  4.029   4.245   1.00 34.94  ?  21  VAL A N     1 
ATOM   29   C  CA    . VAL A 1 28  ? 13.386  3.883   3.653   1.00 35.54  ?  21  VAL A CA    1 
ATOM   30   C  C     . VAL A 1 28  ? 14.431  4.738   4.380   1.00 33.68  ?  21  VAL A C     1 
ATOM   31   O  O     . VAL A 1 28  ? 15.601  4.344   4.458   1.00 34.20  ?  21  VAL A O     1 
ATOM   32   C  CB    . VAL A 1 28  ? 13.347  4.153   2.132   1.00 37.09  ?  21  VAL A CB    1 
ATOM   33   C  CG1   . VAL A 1 28  ? 12.984  5.588   1.783   1.00 35.96  ?  21  VAL A CG1   1 
ATOM   34   C  CG2   . VAL A 1 28  ? 14.648  3.780   1.475   1.00 38.52  ?  21  VAL A CG2   1 
ATOM   35   N  N     . SER A 1 29  ? 14.021  5.914   4.884   1.00 31.91  ?  22  SER A N     1 
ATOM   36   C  CA    . SER A 1 29  ? 14.944  6.879   5.465   1.00 30.50  ?  22  SER A CA    1 
ATOM   37   C  C     . SER A 1 29  ? 14.260  7.513   6.676   1.00 28.89  ?  22  SER A C     1 
ATOM   38   O  O     . SER A 1 29  ? 13.182  8.091   6.535   1.00 28.72  ?  22  SER A O     1 
ATOM   39   C  CB    . SER A 1 29  ? 15.345  7.938   4.472   1.00 30.78  ?  22  SER A CB    1 
ATOM   40   O  OG    . SER A 1 29  ? 16.324  8.820   5.002   1.00 29.90  ?  22  SER A OG    1 
ATOM   41   N  N     . VAL A 1 30  ? 14.827  7.308   7.866   1.00 28.12  ?  23  VAL A N     1 
ATOM   42   C  CA    . VAL A 1 30  ? 14.107  7.592   9.114   1.00 27.16  ?  23  VAL A CA    1 
ATOM   43   C  C     . VAL A 1 30  ? 14.951  8.484   10.007  1.00 26.08  ?  23  VAL A C     1 
ATOM   44   O  O     . VAL A 1 30  ? 16.141  8.244   10.137  1.00 26.24  ?  23  VAL A O     1 
ATOM   45   C  CB    . VAL A 1 30  ? 13.795  6.289   9.860   1.00 27.86  ?  23  VAL A CB    1 
ATOM   46   C  CG1   . VAL A 1 30  ? 13.239  6.490   11.246  1.00 27.28  ?  23  VAL A CG1   1 
ATOM   47   C  CG2   . VAL A 1 30  ? 12.830  5.421   9.056   1.00 29.32  ?  23  VAL A CG2   1 
ATOM   48   N  N     . ASN A 1 31  ? 14.326  9.511   10.567  1.00 25.37  ?  24  ASN A N     1 
ATOM   49   C  CA    . ASN A 1 31  ? 14.952  10.322  11.592  1.00 24.68  ?  24  ASN A CA    1 
ATOM   50   C  C     . ASN A 1 31  ? 14.546  9.840   12.976  1.00 24.59  ?  24  ASN A C     1 
ATOM   51   O  O     . ASN A 1 31  ? 13.352  9.685   13.258  1.00 24.90  ?  24  ASN A O     1 
ATOM   52   C  CB    . ASN A 1 31  ? 14.517  11.771  11.456  1.00 24.46  ?  24  ASN A CB    1 
ATOM   53   C  CG    . ASN A 1 31  ? 15.358  12.505  10.434  1.00 24.75  ?  24  ASN A CG    1 
ATOM   54   O  OD1   . ASN A 1 31  ? 16.334  13.164  10.809  1.00 24.73  ?  24  ASN A OD1   1 
ATOM   55   N  ND2   . ASN A 1 31  ? 15.026  12.347  9.184   1.00 25.34  ?  24  ASN A ND2   1 
ATOM   56   N  N     . TYR A 1 32  ? 15.538  9.534   13.790  1.00 24.55  ?  25  TYR A N     1 
ATOM   57   C  CA    . TYR A 1 32  ? 15.278  9.129   15.165  1.00 24.76  ?  25  TYR A CA    1 
ATOM   58   C  C     . TYR A 1 32  ? 15.711  10.286  16.082  1.00 24.42  ?  25  TYR A C     1 
ATOM   59   O  O     . TYR A 1 32  ? 16.886  10.421  16.349  1.00 24.46  ?  25  TYR A O     1 
ATOM   60   C  CB    . TYR A 1 32  ? 16.015  7.817   15.425  1.00 25.46  ?  25  TYR A CB    1 
ATOM   61   C  CG    . TYR A 1 32  ? 15.910  7.234   16.836  1.00 26.10  ?  25  TYR A CG    1 
ATOM   62   C  CD1   . TYR A 1 32  ? 14.886  7.572   17.734  1.00 26.30  ?  25  TYR A CD1   1 
ATOM   63   C  CD2   . TYR A 1 32  ? 16.857  6.311   17.262  1.00 26.93  ?  25  TYR A CD2   1 
ATOM   64   C  CE1   . TYR A 1 32  ? 14.818  6.985   18.995  1.00 27.29  ?  25  TYR A CE1   1 
ATOM   65   C  CE2   . TYR A 1 32  ? 16.797  5.729   18.507  1.00 27.87  ?  25  TYR A CE2   1 
ATOM   66   C  CZ    . TYR A 1 32  ? 15.795  6.083   19.389  1.00 28.02  ?  25  TYR A CZ    1 
ATOM   67   O  OH    . TYR A 1 32  ? 15.786  5.541   20.639  1.00 29.26  ?  25  TYR A OH    1 
ATOM   68   N  N     . HIS A 1 33  ? 14.722  11.028  16.600  1.00 24.51  ?  26  HIS A N     1 
ATOM   69   C  CA    . HIS A 1 33  ? 14.935  12.068  17.600  1.00 24.69  ?  26  HIS A CA    1 
ATOM   70   C  C     . HIS A 1 33  ? 14.979  11.412  18.976  1.00 25.35  ?  26  HIS A C     1 
ATOM   71   O  O     . HIS A 1 33  ? 13.967  11.387  19.688  1.00 26.08  ?  26  HIS A O     1 
ATOM   72   C  CB    . HIS A 1 33  ? 13.851  13.110  17.456  1.00 24.98  ?  26  HIS A CB    1 
ATOM   73   C  CG    . HIS A 1 33  ? 13.960  13.849  16.143  1.00 24.64  ?  26  HIS A CG    1 
ATOM   74   N  ND1   . HIS A 1 33  ? 14.385  15.157  16.061  1.00 24.92  ?  26  HIS A ND1   1 
ATOM   75   C  CD2   . HIS A 1 33  ? 13.795  13.423  14.873  1.00 24.37  ?  26  HIS A CD2   1 
ATOM   76   C  CE1   . HIS A 1 33  ? 14.355  15.530  14.777  1.00 24.86  ?  26  HIS A CE1   1 
ATOM   77   N  NE2   . HIS A 1 33  ? 13.916  14.536  14.053  1.00 24.53  ?  26  HIS A NE2   1 
ATOM   78   N  N     . PHE A 1 34  ? 16.120  10.822  19.289  1.00 25.42  ?  27  PHE A N     1 
ATOM   79   C  CA    . PHE A 1 34  ? 16.215  9.875   20.401  1.00 26.32  ?  27  PHE A CA    1 
ATOM   80   C  C     . PHE A 1 34  ? 16.204  10.514  21.774  1.00 27.15  ?  27  PHE A C     1 
ATOM   81   O  O     . PHE A 1 34  ? 15.892  9.829   22.759  1.00 28.23  ?  27  PHE A O     1 
ATOM   82   C  CB    . PHE A 1 34  ? 17.416  8.978   20.218  1.00 26.53  ?  27  PHE A CB    1 
ATOM   83   C  CG    . PHE A 1 34  ? 18.753  9.632   20.406  1.00 26.59  ?  27  PHE A CG    1 
ATOM   84   C  CD1   . PHE A 1 34  ? 19.305  9.722   21.663  1.00 27.52  ?  27  PHE A CD1   1 
ATOM   85   C  CD2   . PHE A 1 34  ? 19.487  10.075  19.310  1.00 26.10  ?  27  PHE A CD2   1 
ATOM   86   C  CE1   . PHE A 1 34  ? 20.545  10.319  21.838  1.00 27.93  ?  27  PHE A CE1   1 
ATOM   87   C  CE2   . PHE A 1 34  ? 20.728  10.670  19.492  1.00 26.60  ?  27  PHE A CE2   1 
ATOM   88   C  CZ    . PHE A 1 34  ? 21.267  10.749  20.745  1.00 27.52  ?  27  PHE A CZ    1 
ATOM   89   N  N     . SER A 1 35  ? 16.473  11.819  21.809  1.00 26.97  ?  28  SER A N     1 
ATOM   90   C  CA    . SER A 1 35  ? 16.420  12.613  23.022  1.00 28.06  ?  28  SER A CA    1 
ATOM   91   C  C     . SER A 1 35  ? 15.875  13.993  22.671  1.00 28.07  ?  28  SER A C     1 
ATOM   92   O  O     . SER A 1 35  ? 16.017  14.439  21.546  1.00 27.21  ?  28  SER A O     1 
ATOM   93   C  CB    . SER A 1 35  ? 17.797  12.706  23.688  1.00 28.65  ?  28  SER A CB    1 
ATOM   94   O  OG    . SER A 1 35  ? 18.761  13.415  22.890  1.00 28.12  ?  28  SER A OG    1 
ATOM   95   N  N     . ARG A 1 36  ? 15.283  14.682  23.637  1.00 29.40  ?  29  ARG A N     1 
ATOM   96   C  CA    . ARG A 1 36  ? 14.860  16.053  23.410  1.00 29.95  ?  29  ARG A CA    1 
ATOM   97   C  C     . ARG A 1 36  ? 15.701  17.054  24.180  1.00 31.18  ?  29  ARG A C     1 
ATOM   98   O  O     . ARG A 1 36  ? 15.472  18.249  24.015  1.00 32.01  ?  29  ARG A O     1 
ATOM   99   C  CB    . ARG A 1 36  ? 13.406  16.217  23.839  1.00 31.18  ?  29  ARG A CB    1 
ATOM   100  C  CG    . ARG A 1 36  ? 12.402  15.642  22.861  1.00 30.42  ?  29  ARG A CG    1 
ATOM   101  C  CD    . ARG A 1 36  ? 10.964  15.781  23.320  1.00 32.10  ?  29  ARG A CD    1 
ATOM   102  N  NE    . ARG A 1 36  ? 10.047  15.193  22.346  1.00 31.62  ?  29  ARG A NE    1 
ATOM   103  C  CZ    . ARG A 1 36  ? 9.362   15.913  21.469  1.00 31.78  ?  29  ARG A CZ    1 
ATOM   104  N  NH1   . ARG A 1 36  ? 9.684   17.187  21.276  1.00 32.07  ?  29  ARG A NH1   1 
ATOM   105  N  NH2   . ARG A 1 36  ? 8.440   15.354  20.701  1.00 31.81  ?  29  ARG A NH2   1 
ATOM   106  N  N     . LYS A 1 37  ? 16.705  16.615  24.939  1.00 31.54  ?  30  LYS A N     1 
ATOM   107  C  CA    . LYS A 1 37  ? 17.519  17.585  25.676  1.00 33.07  ?  30  LYS A CA    1 
ATOM   108  C  C     . LYS A 1 37  ? 18.403  18.376  24.715  1.00 32.65  ?  30  LYS A C     1 
ATOM   109  O  O     . LYS A 1 37  ? 18.916  17.821  23.740  1.00 31.21  ?  30  LYS A O     1 
ATOM   110  C  CB    . LYS A 1 37  ? 18.397  16.880  26.713  1.00 33.87  ?  30  LYS A CB    1 
ATOM   111  C  CG    . LYS A 1 37  ? 18.994  17.795  27.779  1.00 36.10  ?  30  LYS A CG    1 
ATOM   112  C  CD    . LYS A 1 37  ? 19.572  17.046  28.992  1.00 37.39  ?  30  LYS A CD    1 
ATOM   113  C  CE    . LYS A 1 37  ? 20.375  15.823  28.608  1.00 36.17  ?  30  LYS A CE    1 
ATOM   114  N  NZ    . LYS A 1 37  ? 20.848  15.044  29.790  1.00 37.72  ?  30  LYS A NZ    1 
ATOM   115  N  N     . CYS A 1 38  ? 18.621  19.674  25.003  1.00 34.30  ?  31  CYS A N     1 
ATOM   116  C  CA    . CYS A 1 38  ? 19.561  20.444  24.214  1.00 34.51  ?  31  CYS A CA    1 
ATOM   117  C  C     . CYS A 1 38  ? 20.195  21.574  25.031  1.00 37.05  ?  31  CYS A C     1 
ATOM   118  O  O     . CYS A 1 38  ? 19.531  22.132  25.874  1.00 38.64  ?  31  CYS A O     1 
ATOM   119  C  CB    . CYS A 1 38  ? 18.877  21.065  23.000  1.00 33.93  ?  31  CYS A CB    1 
ATOM   120  S  SG    . CYS A 1 38  ? 20.057  21.931  21.941  1.00 34.55  ?  31  CYS A SG    1 
ATOM   121  N  N     . ASN A 1 39  ? 21.451  21.870  24.669  1.00 37.62  ?  32  ASN A N     1 
ATOM   122  C  CA    . ASN A 1 39  ? 22.351  22.812  25.316  1.00 40.23  ?  32  ASN A CA    1 
ATOM   123  C  C     . ASN A 1 39  ? 22.171  24.234  24.757  1.00 41.86  ?  32  ASN A C     1 
ATOM   124  O  O     . ASN A 1 39  ? 22.768  25.171  25.293  1.00 44.54  ?  32  ASN A O     1 
ATOM   125  C  CB    . ASN A 1 39  ? 23.800  22.285  25.233  1.00 40.40  ?  32  ASN A CB    1 
ATOM   126  C  CG    . ASN A 1 39  ? 24.355  22.039  23.831  1.00 39.17  ?  32  ASN A CG    1 
ATOM   127  O  OD1   . ASN A 1 39  ? 23.676  21.501  22.962  1.00 37.07  ?  32  ASN A OD1   1 
ATOM   128  N  ND2   . ASN A 1 39  ? 25.602  22.427  23.592  1.00 40.82  ?  32  ASN A ND2   1 
ATOM   129  N  N     . LYS A 1 40  ? 21.286  24.423  23.770  1.00 40.69  ?  33  LYS A N     1 
ATOM   130  C  CA    . LYS A 1 40  ? 21.175  25.692  23.056  1.00 42.33  ?  33  LYS A CA    1 
ATOM   131  C  C     . LYS A 1 40  ? 19.740  26.193  23.167  1.00 42.80  ?  33  LYS A C     1 
ATOM   132  O  O     . LYS A 1 40  ? 18.971  25.610  23.913  1.00 42.18  ?  33  LYS A O     1 
ATOM   133  C  CB    . LYS A 1 40  ? 21.706  25.513  21.636  1.00 41.14  ?  33  LYS A CB    1 
ATOM   134  C  CG    . LYS A 1 40  ? 23.176  25.124  21.548  1.00 41.42  ?  33  LYS A CG    1 
ATOM   135  C  CD    . LYS A 1 40  ? 24.063  25.996  22.450  1.00 44.54  ?  33  LYS A CD    1 
ATOM   136  C  CE    . LYS A 1 40  ? 25.529  25.992  22.078  1.00 45.80  ?  33  LYS A CE    1 
ATOM   137  N  NZ    . LYS A 1 40  ? 26.373  25.962  23.291  1.00 47.64  ?  33  LYS A NZ    1 
ATOM   138  N  N     . GLU A 1 41  ? 19.445  27.341  22.532  1.00 44.53  ?  34  GLU A N     1 
ATOM   139  C  CA    . GLU A 1 41  ? 18.194  28.060  22.693  1.00 46.00  ?  34  GLU A CA    1 
ATOM   140  C  C     . GLU A 1 41  ? 17.732  28.680  21.374  1.00 46.23  ?  34  GLU A C     1 
ATOM   141  O  O     . GLU A 1 41  ? 17.106  29.739  21.367  1.00 48.76  ?  34  GLU A O     1 
ATOM   142  C  CB    . GLU A 1 41  ? 18.382  29.161  23.745  1.00 49.69  ?  34  GLU A CB    1 
ATOM   143  C  CG    . GLU A 1 41  ? 19.184  28.701  24.955  1.00 50.07  ?  34  GLU A CG    1 
ATOM   144  C  CD    . GLU A 1 41  ? 19.202  29.691  26.106  1.00 53.93  ?  34  GLU A CD    1 
ATOM   145  O  OE1   . GLU A 1 41  ? 18.945  29.268  27.258  1.00 54.41  ?  34  GLU A OE1   1 
ATOM   146  O  OE2   . GLU A 1 41  ? 19.443  30.881  25.843  1.00 56.76  ?  34  GLU A OE2   1 
ATOM   147  N  N     . CYS A 1 42  ? 17.978  27.999  20.247  1.00 43.85  ?  35  CYS A N     1 
ATOM   148  C  CA    . CYS A 1 42  ? 17.541  28.471  18.944  1.00 44.06  ?  35  CYS A CA    1 
ATOM   149  C  C     . CYS A 1 42  ? 16.075  28.912  18.988  1.00 45.06  ?  35  CYS A C     1 
ATOM   150  O  O     . CYS A 1 42  ? 15.188  28.157  19.359  1.00 43.65  ?  35  CYS A O     1 
ATOM   151  C  CB    . CYS A 1 42  ? 17.791  27.358  17.923  1.00 41.11  ?  35  CYS A CB    1 
ATOM   152  S  SG    . CYS A 1 42  ? 19.469  26.707  17.797  1.00 40.21  ?  35  CYS A SG    1 
ATOM   153  N  N     . LEU A 1 43  ? 15.787  30.171  18.607  1.00 47.97  ?  36  LEU A N     1 
ATOM   154  C  CA    . LEU A 1 43  ? 14.456  30.734  18.818  1.00 49.80  ?  36  LEU A CA    1 
ATOM   155  C  C     . LEU A 1 43  ? 13.386  30.033  17.980  1.00 47.86  ?  36  LEU A C     1 
ATOM   156  O  O     . LEU A 1 43  ? 12.224  30.052  18.364  1.00 48.69  ?  36  LEU A O     1 
ATOM   157  C  CB    . LEU A 1 43  ? 14.463  32.235  18.481  1.00 53.71  ?  36  LEU A CB    1 
ATOM   158  C  CG    . LEU A 1 43  ? 15.177  33.164  19.460  1.00 56.89  ?  36  LEU A CG    1 
ATOM   159  C  CD1   . LEU A 1 43  ? 15.243  34.573  18.885  1.00 60.84  ?  36  LEU A CD1   1 
ATOM   160  C  CD2   . LEU A 1 43  ? 14.475  33.167  20.813  1.00 58.12  ?  36  LEU A CD2   1 
ATOM   161  N  N     . PHE A 1 44  ? 13.784  29.339  16.909  1.00 45.47  ?  37  PHE A N     1 
ATOM   162  C  CA    . PHE A 1 44  ? 12.820  28.721  16.014  1.00 44.02  ?  37  PHE A CA    1 
ATOM   163  C  C     . PHE A 1 44  ? 12.603  27.222  16.292  1.00 40.87  ?  37  PHE A C     1 
ATOM   164  O  O     . PHE A 1 44  ? 11.736  26.594  15.659  1.00 39.80  ?  37  PHE A O     1 
ATOM   165  C  CB    . PHE A 1 44  ? 13.222  28.959  14.559  1.00 44.04  ?  37  PHE A CB    1 
ATOM   166  C  CG    . PHE A 1 44  ? 14.659  28.692  14.200  1.00 43.02  ?  37  PHE A CG    1 
ATOM   167  C  CD1   . PHE A 1 44  ? 15.198  27.420  14.317  1.00 40.14  ?  37  PHE A CD1   1 
ATOM   168  C  CD2   . PHE A 1 44  ? 15.497  29.720  13.785  1.00 45.40  ?  37  PHE A CD2   1 
ATOM   169  C  CE1   . PHE A 1 44  ? 16.528  27.183  14.033  1.00 39.66  ?  37  PHE A CE1   1 
ATOM   170  C  CE2   . PHE A 1 44  ? 16.812  29.471  13.456  1.00 44.90  ?  37  PHE A CE2   1 
ATOM   171  C  CZ    . PHE A 1 44  ? 17.342  28.216  13.592  1.00 42.06  ?  37  PHE A CZ    1 
ATOM   172  N  N     . CYS A 1 45  ? 13.391  26.655  17.206  1.00 39.73  ?  38  CYS A N     1 
ATOM   173  C  CA    . CYS A 1 45  ? 13.487  25.196  17.312  1.00 36.91  ?  38  CYS A CA    1 
ATOM   174  C  C     . CYS A 1 45  ? 12.113  24.516  17.269  1.00 36.31  ?  38  CYS A C     1 
ATOM   175  O  O     . CYS A 1 45  ? 11.198  24.786  18.069  1.00 37.80  ?  38  CYS A O     1 
ATOM   176  C  CB    . CYS A 1 45  ? 14.277  24.870  18.569  1.00 36.69  ?  38  CYS A CB    1 
ATOM   177  S  SG    . CYS A 1 45  ? 14.519  23.091  18.816  1.00 33.78  ?  38  CYS A SG    1 
ATOM   178  N  N     . PHE A 1 46  ? 11.990  23.509  16.374  1.00 34.32  ?  39  PHE A N     1 
ATOM   179  C  CA    . PHE A 1 46  ? 10.715  22.833  16.225  1.00 34.04  ?  39  PHE A CA    1 
ATOM   180  C  C     . PHE A 1 46  ? 10.725  21.437  16.857  1.00 32.35  ?  39  PHE A C     1 
ATOM   181  O  O     . PHE A 1 46  ? 9.756   20.721  16.663  1.00 32.15  ?  39  PHE A O     1 
ATOM   182  C  CB    . PHE A 1 46  ? 10.268  22.761  14.765  1.00 33.81  ?  39  PHE A CB    1 
ATOM   183  C  CG    . PHE A 1 46  ? 11.147  22.039  13.767  1.00 32.01  ?  39  PHE A CG    1 
ATOM   184  C  CD1   . PHE A 1 46  ? 12.253  21.287  14.130  1.00 30.45  ?  39  PHE A CD1   1 
ATOM   185  C  CD2   . PHE A 1 46  ? 10.850  22.163  12.418  1.00 32.31  ?  39  PHE A CD2   1 
ATOM   186  C  CE1   . PHE A 1 46  ? 13.011  20.616  13.180  1.00 29.28  ?  39  PHE A CE1   1 
ATOM   187  C  CE2   . PHE A 1 46  ? 11.651  21.547  11.469  1.00 31.14  ?  39  PHE A CE2   1 
ATOM   188  C  CZ    . PHE A 1 46  ? 12.701  20.754  11.861  1.00 29.66  ?  39  PHE A CZ    1 
ATOM   189  N  N     . HIS A 1 47  ? 11.750  21.087  17.653  1.00 31.58  ?  40  HIS A N     1 
ATOM   190  C  CA    . HIS A 1 47  ? 11.742  19.806  18.346  1.00 30.48  ?  40  HIS A CA    1 
ATOM   191  C  C     . HIS A 1 47  ? 12.272  20.009  19.767  1.00 31.30  ?  40  HIS A C     1 
ATOM   192  O  O     . HIS A 1 47  ? 13.442  19.771  20.019  1.00 30.59  ?  40  HIS A O     1 
ATOM   193  C  CB    . HIS A 1 47  ? 12.463  18.739  17.512  1.00 28.55  ?  40  HIS A CB    1 
ATOM   194  C  CG    . HIS A 1 47  ? 12.115  17.378  17.967  1.00 27.84  ?  40  HIS A CG    1 
ATOM   195  N  ND1   . HIS A 1 47  ? 10.985  16.736  17.534  1.00 27.93  ?  40  HIS A ND1   1 
ATOM   196  C  CD2   . HIS A 1 47  ? 12.620  16.636  18.944  1.00 27.61  ?  40  HIS A CD2   1 
ATOM   197  C  CE1   . HIS A 1 47  ? 10.883  15.575  18.180  1.00 27.71  ?  40  HIS A CE1   1 
ATOM   198  N  NE2   . HIS A 1 47  ? 11.878  15.497  19.032  1.00 27.48  ?  40  HIS A NE2   1 
ATOM   199  N  N     . THR A 1 48  ? 11.394  20.506  20.646  1.00 33.16  ?  41  THR A N     1 
ATOM   200  C  CA    . THR A 1 48  ? 11.774  21.161  21.884  1.00 34.82  ?  41  THR A CA    1 
ATOM   201  C  C     . THR A 1 48  ? 11.948  20.179  23.042  1.00 34.70  ?  41  THR A C     1 
ATOM   202  O  O     . THR A 1 48  ? 11.520  19.016  22.982  1.00 33.71  ?  41  THR A O     1 
ATOM   203  C  CB    . THR A 1 48  ? 10.744  22.253  22.212  1.00 37.47  ?  41  THR A CB    1 
ATOM   204  O  OG1   . THR A 1 48  ? 9.448   21.692  22.432  1.00 38.17  ?  41  THR A OG1   1 
ATOM   205  C  CG2   . THR A 1 48  ? 10.719  23.275  21.103  1.00 37.94  ?  41  THR A CG2   1 
ATOM   206  N  N     . ALA A 1 49  ? 12.484  20.711  24.141  1.00 36.22  ?  42  ALA A N     1 
ATOM   207  C  CA    . ALA A 1 49  ? 12.909  19.894  25.269  1.00 36.39  ?  42  ALA A CA    1 
ATOM   208  C  C     . ALA A 1 49  ? 11.764  19.649  26.261  1.00 38.36  ?  42  ALA A C     1 
ATOM   209  O  O     . ALA A 1 49  ? 11.844  20.044  27.426  1.00 40.50  ?  42  ALA A O     1 
ATOM   210  C  CB    . ALA A 1 49  ? 14.098  20.543  25.922  1.00 37.33  ?  42  ALA A CB    1 
ATOM   211  N  N     . THR A 1 50  ? 10.724  18.949  25.802  1.00 37.91  ?  43  THR A N     1 
ATOM   212  C  CA    . THR A 1 50  ? 9.523   18.680  26.589  1.00 40.09  ?  43  THR A CA    1 
ATOM   213  C  C     . THR A 1 50  ? 9.667   17.480  27.532  1.00 40.37  ?  43  THR A C     1 
ATOM   214  O  O     . THR A 1 50  ? 8.844   17.335  28.442  1.00 42.81  ?  43  THR A O     1 
ATOM   215  C  CB    . THR A 1 50  ? 8.326   18.514  25.647  1.00 39.98  ?  43  THR A CB    1 
ATOM   216  O  OG1   . THR A 1 50  ? 8.697   17.571  24.635  1.00 37.29  ?  43  THR A OG1   1 
ATOM   217  C  CG2   . THR A 1 50  ? 7.915   19.819  25.004  1.00 40.92  ?  43  THR A CG2   1 
ATOM   218  N  N     . THR A 1 51  ? 10.638  16.582  27.298  1.00 38.29  ?  44  THR A N     1 
ATOM   219  C  CA    . THR A 1 51  ? 10.935  15.450  28.181  1.00 38.76  ?  44  THR A CA    1 
ATOM   220  C  C     . THR A 1 51  ? 12.439  15.215  28.196  1.00 37.31  ?  44  THR A C     1 
ATOM   221  O  O     . THR A 1 51  ? 13.178  15.819  27.419  1.00 35.85  ?  44  THR A O     1 
ATOM   222  C  CB    . THR A 1 51  ? 10.261  14.116  27.788  1.00 38.27  ?  44  THR A CB    1 
ATOM   223  O  OG1   . THR A 1 51  ? 11.032  13.432  26.798  1.00 35.75  ?  44  THR A OG1   1 
ATOM   224  C  CG2   . THR A 1 51  ? 8.869   14.240  27.211  1.00 39.02  ?  44  THR A CG2   1 
ATOM   225  N  N     . SER A 1 52  ? 12.878  14.315  29.090  1.00 38.09  ?  45  SER A N     1 
ATOM   226  C  CA    . SER A 1 52  ? 14.252  13.863  29.158  1.00 37.14  ?  45  SER A CA    1 
ATOM   227  C  C     . SER A 1 52  ? 14.323  12.342  28.955  1.00 36.49  ?  45  SER A C     1 
ATOM   228  O  O     . SER A 1 52  ? 15.376  11.774  29.155  1.00 36.27  ?  45  SER A O     1 
ATOM   229  C  CB    . SER A 1 52  ? 14.890  14.296  30.475  1.00 39.23  ?  45  SER A CB    1 
ATOM   230  O  OG    . SER A 1 52  ? 14.145  13.797  31.581  1.00 41.59  ?  45  SER A OG    1 
ATOM   231  N  N     . HIS A 1 53  ? 13.225  11.683  28.543  1.00 36.49  ?  46  HIS A N     1 
ATOM   232  C  CA    . HIS A 1 53  ? 13.252  10.246  28.302  1.00 36.28  ?  46  HIS A CA    1 
ATOM   233  C  C     . HIS A 1 53  ? 14.169  9.918   27.127  1.00 34.01  ?  46  HIS A C     1 
ATOM   234  O  O     . HIS A 1 53  ? 14.091  10.614  26.108  1.00 32.47  ?  46  HIS A O     1 
ATOM   235  C  CB    . HIS A 1 53  ? 11.873  9.697   27.938  1.00 36.93  ?  46  HIS A CB    1 
ATOM   236  C  CG    . HIS A 1 53  ? 11.910  8.247   27.641  1.00 37.04  ?  46  HIS A CG    1 
ATOM   237  N  ND1   . HIS A 1 53  ? 11.966  7.253   28.606  1.00 39.12  ?  46  HIS A ND1   1 
ATOM   238  C  CD2   . HIS A 1 53  ? 11.966  7.630   26.462  1.00 35.60  ?  46  HIS A CD2   1 
ATOM   239  C  CE1   . HIS A 1 53  ? 12.034  6.070   28.002  1.00 38.97  ?  46  HIS A CE1   1 
ATOM   240  N  NE2   . HIS A 1 53  ? 11.989  6.277   26.687  1.00 36.86  ?  46  HIS A NE2   1 
ATOM   241  N  N     . VAL A 1 54  ? 14.976  8.845   27.295  1.00 34.23  ?  47  VAL A N     1 
ATOM   242  C  CA    . VAL A 1 54  ? 15.697  8.151   26.240  1.00 32.86  ?  47  VAL A CA    1 
ATOM   243  C  C     . VAL A 1 54  ? 15.496  6.649   26.422  1.00 34.13  ?  47  VAL A C     1 
ATOM   244  O  O     . VAL A 1 54  ? 15.572  6.157   27.552  1.00 36.04  ?  47  VAL A O     1 
ATOM   245  C  CB    . VAL A 1 54  ? 17.195  8.523   26.275  1.00 32.39  ?  47  VAL A CB    1 
ATOM   246  C  CG1   . VAL A 1 54  ? 17.960  7.854   25.156  1.00 31.37  ?  47  VAL A CG1   1 
ATOM   247  C  CG2   . VAL A 1 54  ? 17.417  10.037  26.256  1.00 31.78  ?  47  VAL A CG2   1 
ATOM   248  N  N     . GLU A 1 55  ? 15.314  5.907   25.321  1.00 33.41  ?  48  GLU A N     1 
ATOM   249  C  CA    . GLU A 1 55  ? 15.230  4.453   25.410  1.00 34.95  ?  48  GLU A CA    1 
ATOM   250  C  C     . GLU A 1 55  ? 16.535  3.875   25.942  1.00 35.86  ?  48  GLU A C     1 
ATOM   251  O  O     . GLU A 1 55  ? 17.614  4.376   25.701  1.00 34.88  ?  48  GLU A O     1 
ATOM   252  C  CB    . GLU A 1 55  ? 14.924  3.842   24.044  1.00 34.21  ?  48  GLU A CB    1 
ATOM   253  C  CG    . GLU A 1 55  ? 13.505  4.089   23.594  1.00 34.11  ?  48  GLU A CG    1 
ATOM   254  C  CD    . GLU A 1 55  ? 12.442  3.404   24.424  1.00 36.51  ?  48  GLU A CD    1 
ATOM   255  O  OE1   . GLU A 1 55  ? 12.629  2.202   24.683  1.00 38.25  ?  48  GLU A OE1   1 
ATOM   256  O  OE2   . GLU A 1 55  ? 11.447  4.072   24.844  1.00 37.01  ?  48  GLU A OE2   1 
ATOM   257  N  N     . LYS A 1 56  ? 16.417  2.765   26.685  1.00 38.19  ?  49  LYS A N     1 
ATOM   258  C  CA    . LYS A 1 56  ? 17.566  1.949   27.001  1.00 39.52  ?  49  LYS A CA    1 
ATOM   259  C  C     . LYS A 1 56  ? 18.203  1.439   25.720  1.00 38.67  ?  49  LYS A C     1 
ATOM   260  O  O     . LYS A 1 56  ? 17.510  1.109   24.766  1.00 38.13  ?  49  LYS A O     1 
ATOM   261  C  CB    . LYS A 1 56  ? 17.138  0.783   27.892  1.00 42.53  ?  49  LYS A CB    1 
ATOM   262  C  CG    . LYS A 1 56  ? 16.584  1.202   29.235  1.00 44.00  ?  49  LYS A CG    1 
ATOM   263  C  CD    . LYS A 1 56  ? 16.065  0.038   30.059  1.00 47.36  ?  49  LYS A CD    1 
ATOM   264  C  CE    . LYS A 1 56  ? 14.757  -0.520  29.541  1.00 48.05  ?  49  LYS A CE    1 
ATOM   265  N  NZ    . LYS A 1 56  ? 13.959  -1.110  30.641  1.00 51.48  ?  49  LYS A NZ    1 
ATOM   266  N  N     . PRO A 1 57  ? 19.544  1.322   25.655  1.00 38.94  ?  50  PRO A N     1 
ATOM   267  C  CA    . PRO A 1 57  ? 20.233  0.843   24.458  1.00 38.64  ?  50  PRO A CA    1 
ATOM   268  C  C     . PRO A 1 57  ? 19.669  -0.437  23.852  1.00 40.04  ?  50  PRO A C     1 
ATOM   269  O  O     . PRO A 1 57  ? 19.453  -0.489  22.645  1.00 39.08  ?  50  PRO A O     1 
ATOM   270  C  CB    . PRO A 1 57  ? 21.661  0.600   24.943  1.00 40.10  ?  50  PRO A CB    1 
ATOM   271  C  CG    . PRO A 1 57  ? 21.824  1.598   26.025  1.00 39.76  ?  50  PRO A CG    1 
ATOM   272  C  CD    . PRO A 1 57  ? 20.491  1.670   26.720  1.00 39.90  ?  50  PRO A CD    1 
ATOM   273  N  N     . GLU A 1 58  ? 19.452  -1.461  24.694  1.00 42.67  ?  51  GLU A N     1 
ATOM   274  C  CA    . GLU A 1 58  ? 18.895  -2.727  24.235  1.00 44.65  ?  51  GLU A CA    1 
ATOM   275  C  C     . GLU A 1 58  ? 17.572  -2.539  23.493  1.00 43.48  ?  51  GLU A C     1 
ATOM   276  O  O     . GLU A 1 58  ? 17.357  -3.184  22.460  1.00 43.98  ?  51  GLU A O     1 
ATOM   277  C  CB    . GLU A 1 58  ? 18.757  -3.733  25.389  1.00 47.97  ?  51  GLU A CB    1 
ATOM   278  C  CG    . GLU A 1 58  ? 20.090  -4.332  25.813  1.00 50.04  ?  51  GLU A CG    1 
ATOM   279  C  CD    . GLU A 1 58  ? 21.041  -4.671  24.670  1.00 50.02  ?  51  GLU A CD    1 
ATOM   280  O  OE1   . GLU A 1 58  ? 20.717  -5.604  23.877  1.00 51.45  ?  51  GLU A OE1   1 
ATOM   281  O  OE2   . GLU A 1 58  ? 22.084  -3.978  24.545  1.00 48.83  ?  51  GLU A OE2   1 
ATOM   282  N  N     . ASN A 1 59  ? 16.710  -1.632  23.957  1.00 42.15  ?  52  ASN A N     1 
ATOM   283  C  CA    . ASN A 1 59  ? 15.418  -1.394  23.332  1.00 41.38  ?  52  ASN A CA    1 
ATOM   284  C  C     . ASN A 1 59  ? 15.569  -0.594  22.038  1.00 38.73  ?  52  ASN A C     1 
ATOM   285  O  O     . ASN A 1 59  ? 14.968  -0.933  21.028  1.00 38.76  ?  52  ASN A O     1 
ATOM   286  C  CB    . ASN A 1 59  ? 14.443  -0.710  24.294  1.00 41.43  ?  52  ASN A CB    1 
ATOM   287  C  CG    . ASN A 1 59  ? 13.951  -1.627  25.401  1.00 44.65  ?  52  ASN A CG    1 
ATOM   288  O  OD1   . ASN A 1 59  ? 14.159  -2.837  25.342  1.00 46.92  ?  52  ASN A OD1   1 
ATOM   289  N  ND2   . ASN A 1 59  ? 13.302  -1.069  26.410  1.00 45.26  ?  52  ASN A ND2   1 
ATOM   290  N  N     . ALA A 1 60  ? 16.400  0.457   22.042  1.00 36.77  ?  53  ALA A N     1 
ATOM   291  C  CA    . ALA A 1 60  ? 16.670  1.157   20.796  1.00 34.73  ?  53  ALA A CA    1 
ATOM   292  C  C     . ALA A 1 60  ? 17.217  0.215   19.712  1.00 35.64  ?  53  ALA A C     1 
ATOM   293  O  O     . ALA A 1 60  ? 16.829  0.287   18.539  1.00 34.99  ?  53  ALA A O     1 
ATOM   294  C  CB    . ALA A 1 60  ? 17.599  2.332   21.048  1.00 33.16  ?  53  ALA A CB    1 
ATOM   295  N  N     . LYS A 1 61  ? 18.131  -0.698  20.059  1.00 37.51  ?  54  LYS A N     1 
ATOM   296  C  CA    . LYS A 1 61  ? 18.681  -1.602  19.063  1.00 38.89  ?  54  LYS A CA    1 
ATOM   297  C  C     . LYS A 1 61  ? 17.609  -2.524  18.485  1.00 40.35  ?  54  LYS A C     1 
ATOM   298  O  O     . LYS A 1 61  ? 17.691  -2.867  17.307  1.00 40.76  ?  54  LYS A O     1 
ATOM   299  C  CB    . LYS A 1 61  ? 19.782  -2.472  19.664  1.00 41.24  ?  54  LYS A CB    1 
ATOM   300  C  CG    . LYS A 1 61  ? 21.092  -1.760  19.955  1.00 40.55  ?  54  LYS A CG    1 
ATOM   301  C  CD    . LYS A 1 61  ? 22.076  -2.659  20.703  1.00 43.32  ?  54  LYS A CD    1 
ATOM   302  C  CE    . LYS A 1 61  ? 23.342  -1.906  21.042  1.00 42.91  ?  54  LYS A CE    1 
ATOM   303  N  NZ    . LYS A 1 61  ? 24.440  -2.813  21.439  1.00 45.96  ?  54  LYS A NZ    1 
ATOM   304  N  N     . ARG A 1 62  ? 16.654  -2.901  19.333  1.00 41.50  ?  55  ARG A N     1 
ATOM   305  C  CA    . ARG A 1 62  ? 15.528  -3.765  18.900  1.00 43.27  ?  55  ARG A CA    1 
ATOM   306  C  C     . ARG A 1 62  ? 14.678  -2.984  17.903  1.00 41.34  ?  55  ARG A C     1 
ATOM   307  O  O     . ARG A 1 62  ? 14.338  -3.520  16.854  1.00 42.29  ?  55  ARG A O     1 
ATOM   308  C  CB    . ARG A 1 62  ? 14.631  -4.123  20.084  1.00 44.86  ?  55  ARG A CB    1 
ATOM   309  C  CG    . ARG A 1 62  ? 13.674  -5.265  19.786  1.00 48.15  ?  55  ARG A CG    1 
ATOM   310  C  CD    . ARG A 1 62  ? 13.181  -5.901  21.073  1.00 50.66  ?  55  ARG A CD    1 
ATOM   311  N  NE    . ARG A 1 62  ? 12.203  -5.098  21.813  1.00 49.71  ?  55  ARG A NE    1 
ATOM   312  C  CZ    . ARG A 1 62  ? 10.962  -4.857  21.426  1.00 49.83  ?  55  ARG A CZ    1 
ATOM   313  N  NH1   . ARG A 1 62  ? 10.499  -5.386  20.312  1.00 50.66  ?  55  ARG A NH1   1 
ATOM   314  N  NH2   . ARG A 1 62  ? 10.184  -4.096  22.168  1.00 49.41  ?  55  ARG A NH2   1 
ATOM   315  N  N     . GLY A 1 63  ? 14.393  -1.734  18.251  1.00 38.95  ?  56  GLY A N     1 
ATOM   316  C  CA    . GLY A 1 63  ? 13.613  -0.922  17.347  1.00 37.33  ?  56  GLY A CA    1 
ATOM   317  C  C     . GLY A 1 63  ? 14.305  -0.703  16.002  1.00 36.37  ?  56  GLY A C     1 
ATOM   318  O  O     . GLY A 1 63  ? 13.663  -0.786  14.964  1.00 36.60  ?  56  GLY A O     1 
ATOM   319  N  N     . LEU A 1 64  ? 15.614  -0.414  16.024  1.00 35.61  ?  57  LEU A N     1 
ATOM   320  C  CA    . LEU A 1 64  ? 16.378  -0.199  14.807  1.00 35.14  ?  57  LEU A CA    1 
ATOM   321  C  C     . LEU A 1 64  ? 16.381  -1.485  13.958  1.00 37.62  ?  57  LEU A C     1 
ATOM   322  O  O     . LEU A 1 64  ? 16.248  -1.398  12.750  1.00 37.66  ?  57  LEU A O     1 
ATOM   323  C  CB    . LEU A 1 64  ? 17.769  0.273   15.207  1.00 34.51  ?  57  LEU A CB    1 
ATOM   324  C  CG    . LEU A 1 64  ? 17.784  1.695   15.774  1.00 32.24  ?  57  LEU A CG    1 
ATOM   325  C  CD1   . LEU A 1 64  ? 19.087  1.998   16.505  1.00 32.24  ?  57  LEU A CD1   1 
ATOM   326  C  CD2   . LEU A 1 64  ? 17.512  2.666   14.659  1.00 30.78  ?  57  LEU A CD2   1 
ATOM   327  N  N     . THR A 1 65  ? 16.410  -2.655  14.617  1.00 39.96  ?  58  THR A N     1 
ATOM   328  C  CA    . THR A 1 65  ? 16.350  -3.942  13.933  1.00 42.88  ?  58  THR A CA    1 
ATOM   329  C  C     . THR A 1 65  ? 15.030  -4.124  13.184  1.00 43.46  ?  58  THR A C     1 
ATOM   330  O  O     . THR A 1 65  ? 15.040  -4.532  12.016  1.00 44.72  ?  58  THR A O     1 
ATOM   331  C  CB    . THR A 1 65  ? 16.651  -5.106  14.891  1.00 45.61  ?  58  THR A CB    1 
ATOM   332  O  OG1   . THR A 1 65  ? 17.945  -4.960  15.480  1.00 45.44  ?  58  THR A OG1   1 
ATOM   333  C  CG2   . THR A 1 65  ? 16.639  -6.462  14.214  1.00 49.16  ?  58  THR A CG2   1 
ATOM   334  N  N     . LEU A 1 66  ? 13.903  -3.819  13.832  1.00 42.87  ?  59  LEU A N     1 
ATOM   335  C  CA    . LEU A 1 66  ? 12.584  -3.876  13.214  1.00 43.53  ?  59  LEU A CA    1 
ATOM   336  C  C     . LEU A 1 66  ? 12.516  -2.936  12.002  1.00 41.67  ?  59  LEU A C     1 
ATOM   337  O  O     . LEU A 1 66  ? 11.974  -3.308  10.958  1.00 43.04  ?  59  LEU A O     1 
ATOM   338  C  CB    . LEU A 1 66  ? 11.520  -3.486  14.246  1.00 43.14  ?  59  LEU A CB    1 
ATOM   339  C  CG    . LEU A 1 66  ? 11.361  -4.393  15.470  1.00 45.46  ?  59  LEU A CG    1 
ATOM   340  C  CD1   . LEU A 1 66  ? 10.236  -3.885  16.354  1.00 45.30  ?  59  LEU A CD1   1 
ATOM   341  C  CD2   . LEU A 1 66  ? 11.123  -5.838  15.026  1.00 49.15  ?  59  LEU A CD2   1 
ATOM   342  N  N     . LEU A 1 67  ? 13.047  -1.697  12.131  1.00 38.83  ?  60  LEU A N     1 
ATOM   343  C  CA    . LEU A 1 67  ? 13.067  -0.786  10.988  1.00 37.39  ?  60  LEU A CA    1 
ATOM   344  C  C     . LEU A 1 67  ? 13.897  -1.352  9.848   1.00 38.78  ?  60  LEU A C     1 
ATOM   345  O  O     . LEU A 1 67  ? 13.452  -1.269  8.723   1.00 39.34  ?  60  LEU A O     1 
ATOM   346  C  CB    . LEU A 1 67  ? 13.614  0.591   11.368  1.00 34.64  ?  60  LEU A CB    1 
ATOM   347  C  CG    . LEU A 1 67  ? 12.739  1.393   12.320  1.00 33.36  ?  60  LEU A CG    1 
ATOM   348  C  CD1   . LEU A 1 67  ? 13.572  2.447   13.012  1.00 31.39  ?  60  LEU A CD1   1 
ATOM   349  C  CD2   . LEU A 1 67  ? 11.543  2.034   11.631  1.00 33.08  ?  60  LEU A CD2   1 
ATOM   350  N  N     . LYS A 1 68  ? 15.076  -1.933  10.118  1.00 39.70  ?  61  LYS A N     1 
ATOM   351  C  CA    . LYS A 1 68  ? 15.894  -2.549  9.083   1.00 41.64  ?  61  LYS A CA    1 
ATOM   352  C  C     . LYS A 1 68  ? 15.108  -3.613  8.319   1.00 44.47  ?  61  LYS A C     1 
ATOM   353  O  O     . LYS A 1 68  ? 15.136  -3.662  7.075   1.00 45.57  ?  61  LYS A O     1 
ATOM   354  C  CB    . LYS A 1 68  ? 17.145  -3.185  9.689   1.00 42.89  ?  61  LYS A CB    1 
ATOM   355  C  CG    . LYS A 1 68  ? 17.941  -4.070  8.736   1.00 45.85  ?  61  LYS A CG    1 
ATOM   356  C  CD    . LYS A 1 68  ? 18.804  -3.343  7.754   1.00 45.38  ?  61  LYS A CD    1 
ATOM   357  C  CE    . LYS A 1 68  ? 19.248  -4.256  6.624   1.00 48.83  ?  61  LYS A CE    1 
ATOM   358  N  NZ    . LYS A 1 68  ? 20.140  -3.567  5.676   1.00 48.86  ?  61  LYS A NZ    1 
ATOM   359  N  N     . GLN A 1 69  ? 14.448  -4.472  9.088   1.00 46.00  ?  62  GLN A N     1 
ATOM   360  C  CA    . GLN A 1 69  ? 13.647  -5.568  8.559   1.00 49.18  ?  62  GLN A CA    1 
ATOM   361  C  C     . GLN A 1 69  ? 12.461  -5.043  7.757   1.00 48.70  ?  62  GLN A C     1 
ATOM   362  O  O     . GLN A 1 69  ? 12.034  -5.704  6.813   1.00 51.27  ?  62  GLN A O     1 
ATOM   363  C  CB    . GLN A 1 69  ? 13.177  -6.455  9.706   1.00 50.94  ?  62  GLN A CB    1 
ATOM   364  C  CG    . GLN A 1 69  ? 14.324  -7.236  10.339  1.00 52.54  ?  62  GLN A CG    1 
ATOM   365  C  CD    . GLN A 1 69  ? 14.029  -8.038  11.586  1.00 54.35  ?  62  GLN A CD    1 
ATOM   366  O  OE1   . GLN A 1 69  ? 14.832  -8.891  11.974  1.00 56.63  ?  62  GLN A OE1   1 
ATOM   367  N  NE2   . GLN A 1 69  ? 12.901  -7.789  12.228  1.00 53.76  ?  62  GLN A NE2   1 
ATOM   368  N  N     . ALA A 1 70  ? 11.960  -3.837  8.073   1.00 45.73  ?  63  ALA A N     1 
ATOM   369  C  CA    . ALA A 1 70  ? 10.894  -3.233  7.287   1.00 45.38  ?  63  ALA A CA    1 
ATOM   370  C  C     . ALA A 1 70  ? 11.400  -2.513  6.028   1.00 44.56  ?  63  ALA A C     1 
ATOM   371  O  O     . ALA A 1 70  ? 10.589  -2.041  5.247   1.00 44.64  ?  63  ALA A O     1 
ATOM   372  C  CB    . ALA A 1 70  ? 10.091  -2.334  8.175   1.00 43.28  ?  63  ALA A CB    1 
ATOM   373  N  N     . GLY A 1 71  ? 12.714  -2.429  5.811   1.00 44.15  ?  64  GLY A N     1 
ATOM   374  C  CA    . GLY A 1 71  ? 13.291  -1.875  4.590   1.00 44.11  ?  64  GLY A CA    1 
ATOM   375  C  C     . GLY A 1 71  ? 14.000  -0.532  4.760   1.00 41.21  ?  64  GLY A C     1 
ATOM   376  O  O     . GLY A 1 71  ? 14.304  0.140   3.774   1.00 41.09  ?  64  GLY A O     1 
ATOM   377  N  N     . MET A 1 72  ? 14.301  -0.152  6.004   1.00 39.25  ?  65  MET A N     1 
ATOM   378  C  CA    . MET A 1 72  ? 15.058  1.053   6.255   1.00 36.95  ?  65  MET A CA    1 
ATOM   379  C  C     . MET A 1 72  ? 16.458  0.865   5.689   1.00 38.07  ?  65  MET A C     1 
ATOM   380  O  O     . MET A 1 72  ? 17.108  -0.147  5.955   1.00 39.78  ?  65  MET A O     1 
ATOM   381  C  CB    . MET A 1 72  ? 15.120  1.382   7.749   1.00 35.16  ?  65  MET A CB    1 
ATOM   382  C  CG    . MET A 1 72  ? 15.868  2.657   8.060   1.00 33.09  ?  65  MET A CG    1 
ATOM   383  S  SD    . MET A 1 72  ? 15.840  3.133   9.842   1.00 31.30  ?  65  MET A SD    1 
ATOM   384  C  CE    . MET A 1 72  ? 16.807  1.812   10.538  1.00 32.98  ?  65  MET A CE    1 
ATOM   385  N  N     . LYS A 1 73  ? 16.907  1.877   4.948   1.00 37.38  ?  66  LYS A N     1 
ATOM   386  C  CA    . LYS A 1 73  ? 18.214  1.947   4.328   1.00 38.60  ?  66  LYS A CA    1 
ATOM   387  C  C     . LYS A 1 73  ? 19.090  3.002   4.992   1.00 36.82  ?  66  LYS A C     1 
ATOM   388  O  O     . LYS A 1 73  ? 20.314  2.826   5.070   1.00 37.88  ?  66  LYS A O     1 
ATOM   389  C  CB    . LYS A 1 73  ? 18.034  2.290   2.855   1.00 39.88  ?  66  LYS A CB    1 
ATOM   390  C  CG    . LYS A 1 73  ? 17.241  1.241   2.077   1.00 42.19  ?  66  LYS A CG    1 
ATOM   391  C  CD    . LYS A 1 73  ? 17.239  1.478   0.596   1.00 44.05  ?  66  LYS A CD    1 
ATOM   392  C  CE    . LYS A 1 73  ? 16.509  0.400   -0.176  1.00 46.79  ?  66  LYS A CE    1 
ATOM   393  N  NZ    . LYS A 1 73  ? 16.349  0.800   -1.591  1.00 48.49  ?  66  LYS A NZ    1 
ATOM   394  N  N     . LYS A 1 74  ? 18.439  4.068   5.484   1.00 34.49  ?  67  LYS A N     1 
ATOM   395  C  CA    . LYS A 1 74  ? 19.150  5.202   6.036   1.00 33.05  ?  67  LYS A CA    1 
ATOM   396  C  C     . LYS A 1 74  ? 18.522  5.599   7.365   1.00 31.02  ?  67  LYS A C     1 
ATOM   397  O  O     . LYS A 1 74  ? 17.312  5.735   7.432   1.00 30.28  ?  67  LYS A O     1 
ATOM   398  C  CB    . LYS A 1 74  ? 19.116  6.395   5.100   1.00 32.88  ?  67  LYS A CB    1 
ATOM   399  C  CG    . LYS A 1 74  ? 19.822  7.646   5.628   1.00 31.80  ?  67  LYS A CG    1 
ATOM   400  C  CD    . LYS A 1 74  ? 20.054  8.720   4.575   1.00 32.50  ?  67  LYS A CD    1 
ATOM   401  C  CE    . LYS A 1 74  ? 20.831  9.916   5.090   1.00 32.00  ?  67  LYS A CE    1 
ATOM   402  N  NZ    . LYS A 1 74  ? 19.944  10.888  5.777   1.00 30.19  ?  67  LYS A NZ    1 
ATOM   403  N  N     . ILE A 1 75  ? 19.404  5.880   8.342   1.00 30.45  ?  68  ILE A N     1 
ATOM   404  C  CA    . ILE A 1 75  ? 19.014  6.369   9.666   1.00 28.86  ?  68  ILE A CA    1 
ATOM   405  C  C     . ILE A 1 75  ? 19.753  7.683   9.949   1.00 28.10  ?  68  ILE A C     1 
ATOM   406  O  O     . ILE A 1 75  ? 20.952  7.795   9.743   1.00 29.02  ?  68  ILE A O     1 
ATOM   407  C  CB    . ILE A 1 75  ? 19.255  5.296   10.742  1.00 29.39  ?  68  ILE A CB    1 
ATOM   408  C  CG1   . ILE A 1 75  ? 18.813  5.747   12.131  1.00 28.14  ?  68  ILE A CG1   1 
ATOM   409  C  CG2   . ILE A 1 75  ? 20.691  4.841   10.818  1.00 30.75  ?  68  ILE A CG2   1 
ATOM   410  C  CD1   . ILE A 1 75  ? 17.340  5.852   12.308  1.00 27.46  ?  68  ILE A CD1   1 
ATOM   411  N  N     . ASN A 1 76  ? 19.003  8.693   10.408  1.00 26.80  ?  69  ASN A N     1 
ATOM   412  C  CA    . ASN A 1 76  ? 19.578  9.951   10.840  1.00 26.34  ?  69  ASN A CA    1 
ATOM   413  C  C     . ASN A 1 76  ? 19.280  10.064  12.332  1.00 25.54  ?  69  ASN A C     1 
ATOM   414  O  O     . ASN A 1 76  ? 18.108  10.089  12.737  1.00 24.91  ?  69  ASN A O     1 
ATOM   415  C  CB    . ASN A 1 76  ? 19.003  11.114  10.049  1.00 26.11  ?  69  ASN A CB    1 
ATOM   416  C  CG    . ASN A 1 76  ? 19.710  12.434  10.317  1.00 26.25  ?  69  ASN A CG    1 
ATOM   417  O  OD1   . ASN A 1 76  ? 20.931  12.507  10.208  1.00 27.18  ?  69  ASN A OD1   1 
ATOM   418  N  ND2   . ASN A 1 76  ? 18.965  13.497  10.596  1.00 25.76  ?  69  ASN A ND2   1 
ATOM   419  N  N     . PHE A 1 77  ? 20.336  10.196  13.129  1.00 25.88  ?  70  PHE A N     1 
ATOM   420  C  CA    . PHE A 1 77  ? 20.233  10.514  14.551  1.00 25.49  ?  70  PHE A CA    1 
ATOM   421  C  C     . PHE A 1 77  ? 20.127  12.021  14.788  1.00 25.19  ?  70  PHE A C     1 
ATOM   422  O  O     . PHE A 1 77  ? 20.972  12.797  14.339  1.00 25.78  ?  70  PHE A O     1 
ATOM   423  C  CB    . PHE A 1 77  ? 21.378  9.849   15.321  1.00 26.40  ?  70  PHE A CB    1 
ATOM   424  C  CG    . PHE A 1 77  ? 21.356  8.346   15.268  1.00 27.06  ?  70  PHE A CG    1 
ATOM   425  C  CD1   . PHE A 1 77  ? 20.571  7.628   16.153  1.00 26.98  ?  70  PHE A CD1   1 
ATOM   426  C  CD2   . PHE A 1 77  ? 22.160  7.646   14.384  1.00 28.22  ?  70  PHE A CD2   1 
ATOM   427  C  CE1   . PHE A 1 77  ? 20.565  6.244   16.128  1.00 28.02  ?  70  PHE A CE1   1 
ATOM   428  C  CE2   . PHE A 1 77  ? 22.116  6.259   14.339  1.00 29.24  ?  70  PHE A CE2   1 
ATOM   429  C  CZ    . PHE A 1 77  ? 21.305  5.565   15.194  1.00 29.13  ?  70  PHE A CZ    1 
ATOM   430  N  N     . ALA A 1 78  ? 19.015  12.416  15.427  1.00 24.64  ?  71  ALA A N     1 
ATOM   431  C  CA    . ALA A 1 78  ? 18.680  13.819  15.690  1.00 24.70  ?  71  ALA A CA    1 
ATOM   432  C  C     . ALA A 1 78  ? 18.099  13.957  17.092  1.00 24.80  ?  71  ALA A C     1 
ATOM   433  O  O     . ALA A 1 78  ? 18.313  13.102  17.951  1.00 24.95  ?  71  ALA A O     1 
ATOM   434  C  CB    . ALA A 1 78  ? 17.756  14.340  14.629  1.00 24.50  ?  71  ALA A CB    1 
ATOM   435  N  N     . GLY A 1 79  ? 17.412  15.065  17.355  1.00 25.10  ?  72  GLY A N     1 
ATOM   436  C  CA    . GLY A 1 79  ? 16.883  15.380  18.671  1.00 25.70  ?  72  GLY A CA    1 
ATOM   437  C  C     . GLY A 1 79  ? 16.213  16.751  18.653  1.00 26.45  ?  72  GLY A C     1 
ATOM   438  O  O     . GLY A 1 79  ? 15.626  17.125  17.673  1.00 26.31  ?  72  GLY A O     1 
ATOM   439  N  N     . GLY A 1 80  ? 16.402  17.509  19.729  1.00 27.57  ?  73  GLY A N     1 
ATOM   440  C  CA    . GLY A 1 80  ? 17.452  17.277  20.695  1.00 28.04  ?  73  GLY A CA    1 
ATOM   441  C  C     . GLY A 1 80  ? 18.870  17.398  20.115  1.00 28.00  ?  73  GLY A C     1 
ATOM   442  O  O     . GLY A 1 80  ? 19.059  17.394  18.905  1.00 27.42  ?  73  GLY A O     1 
ATOM   443  N  N     . GLU A 1 81  ? 19.862  17.539  20.993  1.00 28.99  ?  74  GLU A N     1 
ATOM   444  C  CA    . GLU A 1 81  ? 21.258  17.541  20.577  1.00 29.42  ?  74  GLU A CA    1 
ATOM   445  C  C     . GLU A 1 81  ? 21.843  16.164  20.804  1.00 28.99  ?  74  GLU A C     1 
ATOM   446  O  O     . GLU A 1 81  ? 22.023  15.744  21.972  1.00 29.63  ?  74  GLU A O     1 
ATOM   447  C  CB    . GLU A 1 81  ? 22.149  18.545  21.337  1.00 31.32  ?  74  GLU A CB    1 
ATOM   448  C  CG    . GLU A 1 81  ? 23.631  18.507  20.935  1.00 32.23  ?  74  GLU A CG    1 
ATOM   449  C  CD    . GLU A 1 81  ? 23.966  18.388  19.458  1.00 31.73  ?  74  GLU A CD    1 
ATOM   450  O  OE1   . GLU A 1 81  ? 23.329  19.119  18.658  1.00 31.51  ?  74  GLU A OE1   1 
ATOM   451  O  OE2   . GLU A 1 81  ? 24.837  17.534  19.103  1.00 31.80  ?  74  GLU A OE2   1 
ATOM   452  N  N     . PRO A 1 82  ? 22.156  15.400  19.726  1.00 28.24  ?  75  PRO A N     1 
ATOM   453  C  CA    . PRO A 1 82  ? 22.714  14.062  19.916  1.00 28.25  ?  75  PRO A CA    1 
ATOM   454  C  C     . PRO A 1 82  ? 24.000  13.922  20.711  1.00 29.73  ?  75  PRO A C     1 
ATOM   455  O  O     . PRO A 1 82  ? 24.177  12.943  21.436  1.00 30.11  ?  75  PRO A O     1 
ATOM   456  C  CB    . PRO A 1 82  ? 23.014  13.565  18.486  1.00 27.85  ?  75  PRO A CB    1 
ATOM   457  C  CG    . PRO A 1 82  ? 21.997  14.298  17.656  1.00 26.99  ?  75  PRO A CG    1 
ATOM   458  C  CD    . PRO A 1 82  ? 21.804  15.659  18.321  1.00 27.57  ?  75  PRO A CD    1 
ATOM   459  N  N     . PHE A 1 83  ? 24.885  14.915  20.619  1.00 30.93  ?  76  PHE A N     1 
ATOM   460  C  CA    . PHE A 1 83  ? 26.198  14.815  21.249  1.00 32.73  ?  76  PHE A CA    1 
ATOM   461  C  C     . PHE A 1 83  ? 26.153  15.087  22.756  1.00 33.71  ?  76  PHE A C     1 
ATOM   462  O  O     . PHE A 1 83  ? 27.206  14.976  23.418  1.00 35.47  ?  76  PHE A O     1 
ATOM   463  C  CB    . PHE A 1 83  ? 27.225  15.648  20.481  1.00 34.12  ?  76  PHE A CB    1 
ATOM   464  C  CG    . PHE A 1 83  ? 27.761  14.907  19.277  1.00 34.15  ?  76  PHE A CG    1 
ATOM   465  C  CD1   . PHE A 1 83  ? 28.769  13.971  19.413  1.00 35.45  ?  76  PHE A CD1   1 
ATOM   466  C  CD2   . PHE A 1 83  ? 27.194  15.077  18.016  1.00 33.12  ?  76  PHE A CD2   1 
ATOM   467  C  CE1   . PHE A 1 83  ? 29.258  13.273  18.320  1.00 35.92  ?  76  PHE A CE1   1 
ATOM   468  C  CE2   . PHE A 1 83  ? 27.679  14.370  16.931  1.00 33.51  ?  76  PHE A CE2   1 
ATOM   469  C  CZ    . PHE A 1 83  ? 28.681  13.441  17.085  1.00 34.90  ?  76  PHE A CZ    1 
ATOM   470  N  N     . LEU A 1 84  ? 24.957  15.318  23.319  1.00 32.90  ?  77  LEU A N     1 
ATOM   471  C  CA    . LEU A 1 84  ? 24.788  15.250  24.771  1.00 33.95  ?  77  LEU A CA    1 
ATOM   472  C  C     . LEU A 1 84  ? 24.771  13.800  25.267  1.00 33.87  ?  77  LEU A C     1 
ATOM   473  O  O     . LEU A 1 84  ? 24.938  13.589  26.470  1.00 35.25  ?  77  LEU A O     1 
ATOM   474  C  CB    . LEU A 1 84  ? 23.501  15.949  25.196  1.00 33.61  ?  77  LEU A CB    1 
ATOM   475  C  CG    . LEU A 1 84  ? 23.511  17.474  25.119  1.00 34.58  ?  77  LEU A CG    1 
ATOM   476  C  CD1   . LEU A 1 84  ? 22.092  17.980  25.324  1.00 34.24  ?  77  LEU A CD1   1 
ATOM   477  C  CD2   . LEU A 1 84  ? 24.450  18.071  26.166  1.00 37.00  ?  77  LEU A CD2   1 
ATOM   478  N  N     . TYR A 1 85  ? 24.588  12.829  24.351  1.00 32.64  ?  78  TYR A N     1 
ATOM   479  C  CA    . TYR A 1 85  ? 24.553  11.420  24.693  1.00 32.87  ?  78  TYR A CA    1 
ATOM   480  C  C     . TYR A 1 85  ? 25.551  10.640  23.849  1.00 33.25  ?  78  TYR A C     1 
ATOM   481  O  O     . TYR A 1 85  ? 25.139  9.785   23.056  1.00 32.42  ?  78  TYR A O     1 
ATOM   482  C  CB    . TYR A 1 85  ? 23.145  10.864  24.472  1.00 31.55  ?  78  TYR A CB    1 
ATOM   483  C  CG    . TYR A 1 85  ? 22.096  11.434  25.408  1.00 31.72  ?  78  TYR A CG    1 
ATOM   484  C  CD1   . TYR A 1 85  ? 21.423  12.624  25.108  1.00 31.06  ?  78  TYR A CD1   1 
ATOM   485  C  CD2   . TYR A 1 85  ? 21.691  10.739  26.534  1.00 32.86  ?  78  TYR A CD2   1 
ATOM   486  C  CE1   . TYR A 1 85  ? 20.433  13.119  25.936  1.00 31.64  ?  78  TYR A CE1   1 
ATOM   487  C  CE2   . TYR A 1 85  ? 20.706  11.232  27.374  1.00 33.44  ?  78  TYR A CE2   1 
ATOM   488  C  CZ    . TYR A 1 85  ? 20.075  12.427  27.072  1.00 32.85  ?  78  TYR A CZ    1 
ATOM   489  O  OH    . TYR A 1 85  ? 19.110  12.950  27.888  1.00 33.83  ?  78  TYR A OH    1 
ATOM   490  N  N     . PRO A 1 86  ? 26.879  10.905  23.957  1.00 34.86  ?  79  PRO A N     1 
ATOM   491  C  CA    . PRO A 1 86  ? 27.857  10.243  23.087  1.00 35.67  ?  79  PRO A CA    1 
ATOM   492  C  C     . PRO A 1 86  ? 28.008  8.737   23.292  1.00 36.55  ?  79  PRO A C     1 
ATOM   493  O  O     . PRO A 1 86  ? 28.343  8.008   22.349  1.00 36.83  ?  79  PRO A O     1 
ATOM   494  C  CB    . PRO A 1 86  ? 29.165  10.956  23.408  1.00 37.72  ?  79  PRO A CB    1 
ATOM   495  C  CG    . PRO A 1 86  ? 28.955  11.512  24.800  1.00 38.39  ?  79  PRO A CG    1 
ATOM   496  C  CD    . PRO A 1 86  ? 27.507  11.935  24.811  1.00 36.31  ?  79  PRO A CD    1 
ATOM   497  N  N     . LYS A 1 87  ? 27.729  8.251   24.507  1.00 37.29  ?  80  LYS A N     1 
ATOM   498  C  CA    . LYS A 1 87  ? 27.852  6.834   24.758  1.00 38.54  ?  80  LYS A CA    1 
ATOM   499  C  C     . LYS A 1 87  ? 26.748  6.115   23.995  1.00 37.04  ?  80  LYS A C     1 
ATOM   500  O  O     . LYS A 1 87  ? 27.016  5.180   23.252  1.00 37.68  ?  80  LYS A O     1 
ATOM   501  C  CB    . LYS A 1 87  ? 27.762  6.491   26.248  1.00 40.03  ?  80  LYS A CB    1 
ATOM   502  C  CG    . LYS A 1 87  ? 28.037  5.024   26.530  1.00 41.94  ?  80  LYS A CG    1 
ATOM   503  C  CD    . LYS A 1 87  ? 28.188  4.702   27.977  1.00 44.04  ?  80  LYS A CD    1 
ATOM   504  C  CE    . LYS A 1 87  ? 28.380  3.205   28.159  1.00 46.17  ?  80  LYS A CE    1 
ATOM   505  N  NZ    . LYS A 1 87  ? 29.583  2.741   27.437  1.00 47.69  ?  80  LYS A NZ    1 
ATOM   506  N  N     . PHE A 1 88  ? 25.511  6.561   24.213  1.00 35.43  ?  81  PHE A N     1 
ATOM   507  C  CA    . PHE A 1 88  ? 24.361  6.009   23.517  1.00 34.17  ?  81  PHE A CA    1 
ATOM   508  C  C     . PHE A 1 88  ? 24.504  6.164   22.003  1.00 33.13  ?  81  PHE A C     1 
ATOM   509  O  O     . PHE A 1 88  ? 24.269  5.218   21.256  1.00 33.33  ?  81  PHE A O     1 
ATOM   510  C  CB    . PHE A 1 88  ? 23.081  6.702   23.991  1.00 32.94  ?  81  PHE A CB    1 
ATOM   511  C  CG    . PHE A 1 88  ? 21.821  6.255   23.294  1.00 31.86  ?  81  PHE A CG    1 
ATOM   512  C  CD1   . PHE A 1 88  ? 21.404  6.861   22.114  1.00 30.26  ?  81  PHE A CD1   1 
ATOM   513  C  CD2   . PHE A 1 88  ? 21.036  5.249   23.835  1.00 32.79  ?  81  PHE A CD2   1 
ATOM   514  C  CE1   . PHE A 1 88  ? 20.227  6.483   21.502  1.00 29.56  ?  81  PHE A CE1   1 
ATOM   515  C  CE2   . PHE A 1 88  ? 19.870  4.851   23.202  1.00 32.18  ?  81  PHE A CE2   1 
ATOM   516  C  CZ    . PHE A 1 88  ? 19.459  5.470   22.043  1.00 30.54  ?  81  PHE A CZ    1 
ATOM   517  N  N     . LEU A 1 89  ? 24.833  7.382   21.531  1.00 32.29  ?  82  LEU A N     1 
ATOM   518  C  CA    . LEU A 1 89  ? 24.994  7.643   20.096  1.00 31.62  ?  82  LEU A CA    1 
ATOM   519  C  C     . LEU A 1 89  ? 26.061  6.726   19.465  1.00 33.31  ?  82  LEU A C     1 
ATOM   520  O  O     . LEU A 1 89  ? 25.852  6.116   18.407  1.00 33.29  ?  82  LEU A O     1 
ATOM   521  C  CB    . LEU A 1 89  ? 25.399  9.109   19.919  1.00 31.24  ?  82  LEU A CB    1 
ATOM   522  C  CG    . LEU A 1 89  ? 25.525  9.615   18.474  1.00 30.78  ?  82  LEU A CG    1 
ATOM   523  C  CD1   . LEU A 1 89  ? 24.209  9.538   17.726  1.00 29.18  ?  82  LEU A CD1   1 
ATOM   524  C  CD2   . LEU A 1 89  ? 26.037  11.042  18.453  1.00 31.06  ?  82  LEU A CD2   1 
ATOM   525  N  N     . GLY A 1 90  ? 27.232  6.644   20.089  1.00 35.12  ?  83  GLY A N     1 
ATOM   526  C  CA    . GLY A 1 90  ? 28.265  5.751   19.578  1.00 37.25  ?  83  GLY A CA    1 
ATOM   527  C  C     . GLY A 1 90  ? 27.812  4.298   19.515  1.00 38.00  ?  83  GLY A C     1 
ATOM   528  O  O     . GLY A 1 90  ? 28.135  3.590   18.561  1.00 39.14  ?  83  GLY A O     1 
ATOM   529  N  N     . GLU A 1 91  ? 27.032  3.854   20.510  1.00 37.69  ?  84  GLU A N     1 
ATOM   530  C  CA    . GLU A 1 91  ? 26.586  2.472   20.560  1.00 38.85  ?  84  GLU A CA    1 
ATOM   531  C  C     . GLU A 1 91  ? 25.664  2.220   19.374  1.00 37.67  ?  84  GLU A C     1 
ATOM   532  O  O     . GLU A 1 91  ? 25.684  1.145   18.770  1.00 39.14  ?  84  GLU A O     1 
ATOM   533  C  CB    . GLU A 1 91  ? 25.871  2.157   21.875  1.00 39.00  ?  84  GLU A CB    1 
ATOM   534  C  CG    . GLU A 1 91  ? 26.775  2.005   23.066  1.00 41.02  ?  84  GLU A CG    1 
ATOM   535  C  CD    . GLU A 1 91  ? 25.992  1.608   24.306  1.00 41.55  ?  84  GLU A CD    1 
ATOM   536  O  OE1   . GLU A 1 91  ? 25.532  0.444   24.337  1.00 42.87  ?  84  GLU A OE1   1 
ATOM   537  O  OE2   . GLU A 1 91  ? 25.772  2.484   25.186  1.00 40.83  ?  84  GLU A OE2   1 
ATOM   538  N  N     . MET A 1 92  ? 24.831  3.212   19.043  1.00 35.30  ?  85  MET A N     1 
ATOM   539  C  CA    . MET A 1 92  ? 23.784  2.993   18.064  1.00 34.28  ?  85  MET A CA    1 
ATOM   540  C  C     . MET A 1 92  ? 24.373  3.051   16.660  1.00 34.69  ?  85  MET A C     1 
ATOM   541  O  O     . MET A 1 92  ? 23.950  2.278   15.797  1.00 35.32  ?  85  MET A O     1 
ATOM   542  C  CB    . MET A 1 92  ? 22.662  4.026   18.172  1.00 32.02  ?  85  MET A CB    1 
ATOM   543  C  CG    . MET A 1 92  ? 21.821  3.902   19.429  1.00 31.90  ?  85  MET A CG    1 
ATOM   544  S  SD    . MET A 1 92  ? 21.214  2.233   19.824  1.00 33.82  ?  85  MET A SD    1 
ATOM   545  C  CE    . MET A 1 92  ? 22.293  1.799   21.171  1.00 35.78  ?  85  MET A CE    1 
ATOM   546  N  N     . ILE A 1 93  ? 25.345  3.959   16.456  1.00 34.71  ?  86  ILE A N     1 
ATOM   547  C  CA    . ILE A 1 93  ? 26.049  4.095   15.193  1.00 35.62  ?  86  ILE A CA    1 
ATOM   548  C  C     . ILE A 1 93  ? 26.818  2.806   14.908  1.00 38.38  ?  86  ILE A C     1 
ATOM   549  O  O     . ILE A 1 93  ? 26.657  2.263   13.824  1.00 39.23  ?  86  ILE A O     1 
ATOM   550  C  CB    . ILE A 1 93  ? 26.958  5.324   15.208  1.00 35.59  ?  86  ILE A CB    1 
ATOM   551  C  CG1   . ILE A 1 93  ? 26.124  6.600   15.082  1.00 33.29  ?  86  ILE A CG1   1 
ATOM   552  C  CG2   . ILE A 1 93  ? 28.030  5.230   14.133  1.00 37.68  ?  86  ILE A CG2   1 
ATOM   553  C  CD1   . ILE A 1 93  ? 26.885  7.819   15.581  1.00 33.41  ?  86  ILE A CD1   1 
ATOM   554  N  N     . ASP A 1 94  ? 27.573  2.289   15.891  1.00 40.02  ?  87  ASP A N     1 
ATOM   555  C  CA    . ASP A 1 94  ? 28.342  1.059   15.697  1.00 43.13  ?  87  ASP A CA    1 
ATOM   556  C  C     . ASP A 1 94  ? 27.408  -0.101  15.345  1.00 43.65  ?  87  ASP A C     1 
ATOM   557  O  O     . ASP A 1 94  ? 27.666  -0.881  14.413  1.00 45.74  ?  87  ASP A O     1 
ATOM   558  C  CB    . ASP A 1 94  ? 29.193  0.709   16.930  1.00 44.95  ?  87  ASP A CB    1 
ATOM   559  C  CG    . ASP A 1 94  ? 30.264  1.730   17.282  1.00 45.28  ?  87  ASP A CG    1 
ATOM   560  O  OD1   . ASP A 1 94  ? 30.480  2.666   16.479  1.00 44.47  ?  87  ASP A OD1   1 
ATOM   561  O  OD2   . ASP A 1 94  ? 30.867  1.596   18.382  1.00 46.60  ?  87  ASP A OD2   1 
ATOM   562  N  N     . PHE A 1 95  ? 26.312  -0.223  16.097  1.00 42.14  ?  88  PHE A N     1 
ATOM   563  C  CA    . PHE A 1 95  ? 25.305  -1.244  15.852  1.00 42.74  ?  88  PHE A CA    1 
ATOM   564  C  C     . PHE A 1 95  ? 24.708  -1.155  14.443  1.00 42.12  ?  88  PHE A C     1 
ATOM   565  O  O     . PHE A 1 95  ? 24.558  -2.181  13.777  1.00 44.19  ?  88  PHE A O     1 
ATOM   566  C  CB    . PHE A 1 95  ? 24.180  -1.157  16.884  1.00 41.22  ?  88  PHE A CB    1 
ATOM   567  C  CG    . PHE A 1 95  ? 23.139  -2.229  16.756  1.00 42.30  ?  88  PHE A CG    1 
ATOM   568  C  CD1   . PHE A 1 95  ? 23.442  -3.532  17.093  1.00 45.39  ?  88  PHE A CD1   1 
ATOM   569  C  CD2   . PHE A 1 95  ? 21.871  -1.955  16.266  1.00 40.68  ?  88  PHE A CD2   1 
ATOM   570  C  CE1   . PHE A 1 95  ? 22.504  -4.539  16.941  1.00 46.87  ?  88  PHE A CE1   1 
ATOM   571  C  CE2   . PHE A 1 95  ? 20.912  -2.960  16.148  1.00 42.11  ?  88  PHE A CE2   1 
ATOM   572  C  CZ    . PHE A 1 95  ? 21.241  -4.257  16.468  1.00 45.25  ?  88  PHE A CZ    1 
ATOM   573  N  N     . CYS A 1 96  ? 24.301  0.054   14.029  1.00 39.56  ?  89  CYS A N     1 
ATOM   574  C  CA    . CYS A 1 96  ? 23.600  0.243   12.779  1.00 38.90  ?  89  CYS A CA    1 
ATOM   575  C  C     . CYS A 1 96  ? 24.506  -0.114  11.593  1.00 41.17  ?  89  CYS A C     1 
ATOM   576  O  O     . CYS A 1 96  ? 24.013  -0.623  10.582  1.00 42.13  ?  89  CYS A O     1 
ATOM   577  C  CB    . CYS A 1 96  ? 23.083  1.673   12.653  1.00 36.09  ?  89  CYS A CB    1 
ATOM   578  S  SG    . CYS A 1 96  ? 21.576  2.001   13.629  1.00 33.91  ?  89  CYS A SG    1 
ATOM   579  N  N     . LYS A 1 97  ? 25.813  0.148   11.688  1.00 42.38  ?  90  LYS A N     1 
ATOM   580  C  CA    . LYS A 1 97  ? 26.683  -0.179  10.570  1.00 44.99  ?  90  LYS A CA    1 
ATOM   581  C  C     . LYS A 1 97  ? 27.172  -1.618  10.698  1.00 48.39  ?  90  LYS A C     1 
ATOM   582  O  O     . LYS A 1 97  ? 26.994  -2.397  9.773   1.00 50.44  ?  90  LYS A O     1 
ATOM   583  C  CB    . LYS A 1 97  ? 27.888  0.748   10.437  1.00 45.48  ?  90  LYS A CB    1 
ATOM   584  C  CG    . LYS A 1 97  ? 28.448  0.828   9.021   1.00 47.57  ?  90  LYS A CG    1 
ATOM   585  C  CD    . LYS A 1 97  ? 27.546  1.613   8.096   1.00 45.62  ?  90  LYS A CD    1 
ATOM   586  C  CE    . LYS A 1 97  ? 28.111  1.796   6.710   1.00 47.89  ?  90  LYS A CE    1 
ATOM   587  N  NZ    . LYS A 1 97  ? 27.034  2.061   5.731   1.00 46.77  ?  90  LYS A NZ    1 
ATOM   588  N  N     . GLU A 1 98  ? 27.782  -1.964  11.833  1.00 49.31  ?  91  GLU A N     1 
ATOM   589  C  CA    . GLU A 1 98  ? 28.485  -3.224  11.976  1.00 53.10  ?  91  GLU A CA    1 
ATOM   590  C  C     . GLU A 1 98  ? 27.508  -4.398  12.023  1.00 54.11  ?  91  GLU A C     1 
ATOM   591  O  O     . GLU A 1 98  ? 27.832  -5.455  11.485  1.00 57.59  ?  91  GLU A O     1 
ATOM   592  C  CB    . GLU A 1 98  ? 29.385  -3.214  13.213  1.00 53.98  ?  91  GLU A CB    1 
ATOM   593  C  CG    . GLU A 1 98  ? 30.563  -2.256  13.110  1.00 54.28  ?  91  GLU A CG    1 
ATOM   594  C  CD    . GLU A 1 98  ? 31.384  -2.097  14.382  1.00 55.00  ?  91  GLU A CD    1 
ATOM   595  O  OE1   . GLU A 1 98  ? 32.343  -1.291  14.381  1.00 55.49  ?  91  GLU A OE1   1 
ATOM   596  O  OE2   . GLU A 1 98  ? 31.053  -2.764  15.389  1.00 55.31  ?  91  GLU A OE2   1 
ATOM   597  N  N     . THR A 1 99  ? 26.337  -4.237  12.670  1.00 51.55  ?  92  THR A N     1 
ATOM   598  C  CA    . THR A 1 99  ? 25.411  -5.340  12.844  1.00 52.86  ?  92  THR A CA    1 
ATOM   599  C  C     . THR A 1 99  ? 24.341  -5.284  11.757  1.00 51.95  ?  92  THR A C     1 
ATOM   600  O  O     . THR A 1 99  ? 24.184  -6.242  11.007  1.00 54.70  ?  92  THR A O     1 
ATOM   601  C  CB    . THR A 1 99  ? 24.853  -5.391  14.272  1.00 51.71  ?  92  THR A CB    1 
ATOM   602  O  OG1   . THR A 1 99  ? 25.931  -5.662  15.166  1.00 53.52  ?  92  THR A OG1   1 
ATOM   603  C  CG2   . THR A 1 99  ? 23.804  -6.459  14.488  1.00 53.22  ?  92  THR A CG2   1 
ATOM   604  N  N     . LEU A 1 100 ? 23.645  -4.148  11.646  1.00 48.45  ?  93  LEU A N     1 
ATOM   605  C  CA    . LEU A 1 100 ? 22.490  -4.035  10.775  1.00 47.50  ?  93  LEU A CA    1 
ATOM   606  C  C     . LEU A 1 100 ? 22.920  -3.819  9.325   1.00 48.48  ?  93  LEU A C     1 
ATOM   607  O  O     . LEU A 1 100 ? 22.120  -4.039  8.431   1.00 48.93  ?  93  LEU A O     1 
ATOM   608  C  CB    . LEU A 1 100 ? 21.569  -2.901  11.250  1.00 43.82  ?  93  LEU A CB    1 
ATOM   609  C  CG    . LEU A 1 100 ? 20.819  -3.097  12.568  1.00 43.05  ?  93  LEU A CG    1 
ATOM   610  C  CD1   . LEU A 1 100 ? 19.843  -1.951  12.793  1.00 39.92  ?  93  LEU A CD1   1 
ATOM   611  C  CD2   . LEU A 1 100 ? 20.063  -4.424  12.621  1.00 45.58  ?  93  LEU A CD2   1 
ATOM   612  N  N     . GLN A 1 101 ? 24.140  -3.331  9.098   1.00 48.97  ?  94  GLN A N     1 
ATOM   613  C  CA    . GLN A 1 101 ? 24.652  -3.050  7.764   1.00 50.25  ?  94  GLN A CA    1 
ATOM   614  C  C     . GLN A 1 101 ? 23.736  -2.072  7.039   1.00 47.72  ?  94  GLN A C     1 
ATOM   615  O  O     . GLN A 1 101 ? 23.424  -2.249  5.858   1.00 49.04  ?  94  GLN A O     1 
ATOM   616  C  CB    . GLN A 1 101 ? 24.821  -4.344  6.951   1.00 54.33  ?  94  GLN A CB    1 
ATOM   617  C  CG    . GLN A 1 101 ? 25.980  -5.204  7.419   1.00 57.62  ?  94  GLN A CG    1 
ATOM   618  C  CD    . GLN A 1 101 ? 27.293  -4.468  7.289   1.00 58.09  ?  94  GLN A CD    1 
ATOM   619  O  OE1   . GLN A 1 101 ? 27.574  -3.827  6.274   1.00 58.28  ?  94  GLN A OE1   1 
ATOM   620  N  NE2   . GLN A 1 101 ? 28.099  -4.518  8.337   1.00 58.48  ?  94  GLN A NE2   1 
ATOM   621  N  N     . LEU A 1 102 ? 23.267  -1.023  7.734   1.00 44.35  ?  95  LEU A N     1 
ATOM   622  C  CA    . LEU A 1 102 ? 22.486  -0.003  7.062   1.00 42.26  ?  95  LEU A CA    1 
ATOM   623  C  C     . LEU A 1 102 ? 23.336  0.659   5.986   1.00 43.25  ?  95  LEU A C     1 
ATOM   624  O  O     . LEU A 1 102 ? 24.550  0.764   6.140   1.00 44.47  ?  95  LEU A O     1 
ATOM   625  C  CB    . LEU A 1 102 ? 21.981  1.016   8.094   1.00 39.01  ?  95  LEU A CB    1 
ATOM   626  C  CG    . LEU A 1 102 ? 20.957  0.460   9.080   1.00 38.20  ?  95  LEU A CG    1 
ATOM   627  C  CD1   . LEU A 1 102 ? 20.474  1.521   10.062  1.00 35.41  ?  95  LEU A CD1   1 
ATOM   628  C  CD2   . LEU A 1 102 ? 19.770  -0.131  8.352   1.00 38.93  ?  95  LEU A CD2   1 
ATOM   629  N  N     . GLU A 1 103 ? 22.687  1.076   4.892   1.00 43.11  ?  96  GLU A N     1 
ATOM   630  C  CA    . GLU A 1 103 ? 23.376  1.709   3.782   1.00 44.41  ?  96  GLU A CA    1 
ATOM   631  C  C     . GLU A 1 103 ? 23.954  3.059   4.206   1.00 42.62  ?  96  GLU A C     1 
ATOM   632  O  O     . GLU A 1 103 ? 25.012  3.465   3.730   1.00 44.25  ?  96  GLU A O     1 
ATOM   633  C  CB    . GLU A 1 103 ? 22.443  1.977   2.605   1.00 44.56  ?  96  GLU A CB    1 
ATOM   634  C  CG    . GLU A 1 103 ? 21.905  0.733   1.951   1.00 46.96  ?  96  GLU A CG    1 
ATOM   635  C  CD    . GLU A 1 103 ? 21.141  1.000   0.668   1.00 47.77  ?  96  GLU A CD    1 
ATOM   636  O  OE1   . GLU A 1 103 ? 21.072  2.171   0.227   1.00 46.59  ?  96  GLU A OE1   1 
ATOM   637  O  OE2   . GLU A 1 103 ? 20.629  0.023   0.112   1.00 49.91  ?  96  GLU A OE2   1 
ATOM   638  N  N     . SER A 1 104 ? 23.237  3.790   5.053   1.00 39.63  ?  97  SER A N     1 
ATOM   639  C  CA    . SER A 1 104 ? 23.681  5.127   5.427   1.00 38.19  ?  97  SER A CA    1 
ATOM   640  C  C     . SER A 1 104 ? 23.293  5.380   6.882   1.00 35.81  ?  97  SER A C     1 
ATOM   641  O  O     . SER A 1 104 ? 22.118  5.215   7.233   1.00 34.33  ?  97  SER A O     1 
ATOM   642  C  CB    . SER A 1 104 ? 23.118  6.190   4.520   1.00 37.56  ?  97  SER A CB    1 
ATOM   643  O  OG    . SER A 1 104 ? 23.518  7.481   4.928   1.00 36.48  ?  97  SER A OG    1 
ATOM   644  N  N     . VAL A 1 105 ? 24.311  5.714   7.677   1.00 35.96  ?  98  VAL A N     1 
ATOM   645  C  CA    . VAL A 1 105 ? 24.180  6.145   9.057   1.00 34.15  ?  98  VAL A CA    1 
ATOM   646  C  C     . VAL A 1 105 ? 24.590  7.609   9.130   1.00 33.46  ?  98  VAL A C     1 
ATOM   647  O  O     . VAL A 1 105 ? 25.739  7.957   8.799   1.00 35.12  ?  98  VAL A O     1 
ATOM   648  C  CB    . VAL A 1 105 ? 25.057  5.255   9.972   1.00 35.44  ?  98  VAL A CB    1 
ATOM   649  C  CG1   . VAL A 1 105 ? 25.134  5.816   11.381  1.00 34.07  ?  98  VAL A CG1   1 
ATOM   650  C  CG2   . VAL A 1 105 ? 24.606  3.807   9.974   1.00 36.47  ?  98  VAL A CG2   1 
ATOM   651  N  N     . SER A 1 106 ? 23.651  8.477   9.531   1.00 31.43  ?  99  SER A N     1 
ATOM   652  C  CA    . SER A 1 106 ? 23.909  9.907   9.592   1.00 31.03  ?  99  SER A CA    1 
ATOM   653  C  C     . SER A 1 106 ? 23.579  10.445  10.977  1.00 29.58  ?  99  SER A C     1 
ATOM   654  O  O     . SER A 1 106 ? 22.821  9.836   11.748  1.00 28.56  ?  99  SER A O     1 
ATOM   655  C  CB    . SER A 1 106 ? 23.222  10.725  8.486   1.00 30.84  ?  99  SER A CB    1 
ATOM   656  O  OG    . SER A 1 106 ? 21.785  10.774  8.544   1.00 29.26  ?  99  SER A OG    1 
ATOM   657  N  N     . ILE A 1 107 ? 24.165  11.600  11.283  1.00 29.87  ?  100 ILE A N     1 
ATOM   658  C  CA    . ILE A 1 107 ? 23.866  12.358  12.497  1.00 28.91  ?  100 ILE A CA    1 
ATOM   659  C  C     . ILE A 1 107 ? 23.703  13.830  12.105  1.00 29.04  ?  100 ILE A C     1 
ATOM   660  O  O     . ILE A 1 107 ? 24.432  14.336  11.259  1.00 30.44  ?  100 ILE A O     1 
ATOM   661  C  CB    . ILE A 1 107 ? 24.991  12.224  13.542  1.00 29.90  ?  100 ILE A CB    1 
ATOM   662  C  CG1   . ILE A 1 107 ? 25.519  10.791  13.716  1.00 30.69  ?  100 ILE A CG1   1 
ATOM   663  C  CG2   . ILE A 1 107 ? 24.578  12.853  14.855  1.00 29.11  ?  100 ILE A CG2   1 
ATOM   664  C  CD1   . ILE A 1 107 ? 26.982  10.731  14.071  1.00 32.69  ?  100 ILE A CD1   1 
ATOM   665  N  N     . VAL A 1 108 ? 22.806  14.556  12.763  1.00 28.03  ?  101 VAL A N     1 
ATOM   666  C  CA    . VAL A 1 108 ? 22.720  15.998  12.622  1.00 28.60  ?  101 VAL A CA    1 
ATOM   667  C  C     . VAL A 1 108 ? 22.975  16.630  13.991  1.00 28.85  ?  101 VAL A C     1 
ATOM   668  O  O     . VAL A 1 108 ? 22.387  16.185  14.974  1.00 27.91  ?  101 VAL A O     1 
ATOM   669  C  CB    . VAL A 1 108 ? 21.377  16.426  11.999  1.00 27.84  ?  101 VAL A CB    1 
ATOM   670  C  CG1   . VAL A 1 108 ? 20.182  15.857  12.772  1.00 26.42  ?  101 VAL A CG1   1 
ATOM   671  C  CG2   . VAL A 1 108 ? 21.279  17.938  11.823  1.00 28.86  ?  101 VAL A CG2   1 
ATOM   672  N  N     . THR A 1 109 ? 23.906  17.611  14.069  1.00 30.49  ?  102 THR A N     1 
ATOM   673  C  CA    . THR A 1 109 ? 24.357  18.126  15.350  1.00 31.24  ?  102 THR A CA    1 
ATOM   674  C  C     . THR A 1 109 ? 24.597  19.632  15.234  1.00 32.95  ?  102 THR A C     1 
ATOM   675  O  O     . THR A 1 109 ? 24.808  20.111  14.128  1.00 33.88  ?  102 THR A O     1 
ATOM   676  C  CB    . THR A 1 109 ? 25.678  17.484  15.778  1.00 32.33  ?  102 THR A CB    1 
ATOM   677  O  OG1   . THR A 1 109 ? 26.174  18.054  16.997  1.00 33.45  ?  102 THR A OG1   1 
ATOM   678  C  CG2   . THR A 1 109 ? 26.757  17.630  14.718  1.00 34.08  ?  102 THR A CG2   1 
ATOM   679  N  N     . ASN A 1 110 ? 24.473  20.347  16.350  1.00 33.58  ?  103 ASN A N     1 
ATOM   680  C  CA    . ASN A 1 110 ? 24.858  21.764  16.399  1.00 35.82  ?  103 ASN A CA    1 
ATOM   681  C  C     . ASN A 1 110 ? 26.383  21.931  16.428  1.00 38.03  ?  103 ASN A C     1 
ATOM   682  O  O     . ASN A 1 110 ? 26.893  23.059  16.240  1.00 40.42  ?  103 ASN A O     1 
ATOM   683  C  CB    . ASN A 1 110 ? 24.123  22.495  17.525  1.00 36.17  ?  103 ASN A CB    1 
ATOM   684  C  CG    . ASN A 1 110 ? 24.560  22.097  18.924  1.00 36.44  ?  103 ASN A CG    1 
ATOM   685  O  OD1   . ASN A 1 110 ? 25.706  21.707  19.166  1.00 37.32  ?  103 ASN A OD1   1 
ATOM   686  N  ND2   . ASN A 1 110 ? 23.630  22.145  19.868  1.00 35.95  ?  103 ASN A ND2   1 
ATOM   687  N  N     . GLY A 1 111 ? 27.120  20.835  16.643  1.00 37.66  ?  104 GLY A N     1 
ATOM   688  C  CA    . GLY A 1 111 ? 28.553  20.779  16.396  1.00 39.88  ?  104 GLY A CA    1 
ATOM   689  C  C     . GLY A 1 111 ? 29.407  21.127  17.624  1.00 41.82  ?  104 GLY A C     1 
ATOM   690  O  O     . GLY A 1 111 ? 30.615  20.858  17.639  1.00 43.73  ?  104 GLY A O     1 
ATOM   691  N  N     . SER A 1 112 ? 28.791  21.756  18.623  1.00 41.73  ?  105 SER A N     1 
ATOM   692  C  CA    . SER A 1 112 ? 29.518  22.328  19.756  1.00 44.08  ?  105 SER A CA    1 
ATOM   693  C  C     . SER A 1 112 ? 30.233  21.258  20.585  1.00 44.16  ?  105 SER A C     1 
ATOM   694  O  O     . SER A 1 112 ? 31.317  21.526  21.084  1.00 46.76  ?  105 SER A O     1 
ATOM   695  C  CB    . SER A 1 112 ? 28.606  23.199  20.604  1.00 44.20  ?  105 SER A CB    1 
ATOM   696  O  OG    . SER A 1 112 ? 27.507  22.479  21.146  1.00 41.68  ?  105 SER A OG    1 
ATOM   697  N  N     . LEU A 1 113 ? 29.622  20.069  20.757  1.00 41.67  ?  106 LEU A N     1 
ATOM   698  C  CA    . LEU A 1 113 ? 30.101  19.034  21.662  1.00 41.81  ?  106 LEU A CA    1 
ATOM   699  C  C     . LEU A 1 113 ? 30.820  17.908  20.924  1.00 41.76  ?  106 LEU A C     1 
ATOM   700  O  O     . LEU A 1 113 ? 31.232  16.939  21.551  1.00 42.05  ?  106 LEU A O     1 
ATOM   701  C  CB    . LEU A 1 113 ? 28.894  18.457  22.415  1.00 39.63  ?  106 LEU A CB    1 
ATOM   702  C  CG    . LEU A 1 113 ? 28.086  19.457  23.239  1.00 39.94  ?  106 LEU A CG    1 
ATOM   703  C  CD1   . LEU A 1 113 ? 26.846  18.795  23.836  1.00 38.02  ?  106 LEU A CD1   1 
ATOM   704  C  CD2   . LEU A 1 113 ? 28.940  20.039  24.346  1.00 42.73  ?  106 LEU A CD2   1 
ATOM   705  N  N     . VAL A 1 114 ? 30.978  18.024  19.602  1.00 41.74  ?  107 VAL A N     1 
ATOM   706  C  CA    . VAL A 1 114 ? 31.681  17.017  18.818  1.00 42.22  ?  107 VAL A CA    1 
ATOM   707  C  C     . VAL A 1 114 ? 33.173  17.089  19.150  1.00 45.53  ?  107 VAL A C     1 
ATOM   708  O  O     . VAL A 1 114 ? 33.769  18.152  19.031  1.00 47.73  ?  107 VAL A O     1 
ATOM   709  C  CB    . VAL A 1 114 ? 31.496  17.251  17.299  1.00 41.93  ?  107 VAL A CB    1 
ATOM   710  C  CG1   . VAL A 1 114 ? 32.111  16.120  16.482  1.00 42.57  ?  107 VAL A CG1   1 
ATOM   711  C  CG2   . VAL A 1 114 ? 30.040  17.443  16.909  1.00 39.21  ?  107 VAL A CG2   1 
ATOM   712  N  N     . LYS A 1 115 ? 33.785  15.965  19.525  1.00 46.26  ?  108 LYS A N     1 
ATOM   713  C  CA    . LYS A 1 115 ? 35.224  15.923  19.735  1.00 49.75  ?  108 LYS A CA    1 
ATOM   714  C  C     . LYS A 1 115 ? 35.859  14.980  18.717  1.00 50.85  ?  108 LYS A C     1 
ATOM   715  O  O     . LYS A 1 115 ? 35.259  13.977  18.288  1.00 48.95  ?  108 LYS A O     1 
ATOM   716  C  CB    . LYS A 1 115 ? 35.554  15.452  21.154  1.00 50.64  ?  108 LYS A CB    1 
ATOM   717  C  CG    . LYS A 1 115 ? 35.135  16.413  22.258  1.00 50.54  ?  108 LYS A CG    1 
ATOM   718  C  CD    . LYS A 1 115 ? 35.711  16.026  23.606  1.00 52.37  ?  108 LYS A CD    1 
ATOM   719  C  CE    . LYS A 1 115 ? 35.368  17.003  24.711  1.00 52.87  ?  108 LYS A CE    1 
ATOM   720  N  NZ    . LYS A 1 115 ? 33.904  17.037  24.974  1.00 49.69  ?  108 LYS A NZ    1 
ATOM   721  N  N     . GLU A 1 116 ? 37.115  15.298  18.354  1.00 54.42  ?  109 GLU A N     1 
ATOM   722  C  CA    . GLU A 1 116 ? 37.813  14.553  17.332  1.00 56.25  ?  109 GLU A CA    1 
ATOM   723  C  C     . GLU A 1 116 ? 37.846  13.076  17.698  1.00 55.90  ?  109 GLU A C     1 
ATOM   724  O  O     . GLU A 1 116 ? 37.657  12.227  16.826  1.00 55.47  ?  109 GLU A O     1 
ATOM   725  C  CB    . GLU A 1 116 ? 39.229  15.088  17.096  1.00 60.80  ?  109 GLU A CB    1 
ATOM   726  C  CG    . GLU A 1 116 ? 39.954  14.323  16.013  1.00 63.18  ?  109 GLU A CG    1 
ATOM   727  C  CD    . GLU A 1 116 ? 41.260  14.944  15.535  1.00 67.98  ?  109 GLU A CD    1 
ATOM   728  O  OE1   . GLU A 1 116 ? 41.663  15.992  16.096  1.00 69.64  ?  109 GLU A OE1   1 
ATOM   729  O  OE2   . GLU A 1 116 ? 41.867  14.365  14.599  1.00 70.40  ?  109 GLU A OE2   1 
ATOM   730  N  N     . GLN A 1 117 ? 38.013  12.767  18.992  1.00 56.22  ?  110 GLN A N     1 
ATOM   731  C  CA    . GLN A 1 117 ? 38.115  11.393  19.473  1.00 56.50  ?  110 GLN A CA    1 
ATOM   732  C  C     . GLN A 1 117 ? 36.891  10.579  19.062  1.00 53.14  ?  110 GLN A C     1 
ATOM   733  O  O     . GLN A 1 117 ? 36.999  9.378   18.857  1.00 53.79  ?  110 GLN A O     1 
ATOM   734  C  CB    . GLN A 1 117 ? 38.302  11.294  20.995  1.00 57.20  ?  110 GLN A CB    1 
ATOM   735  C  CG    . GLN A 1 117 ? 37.205  11.973  21.817  1.00 54.28  ?  110 GLN A CG    1 
ATOM   736  C  CD    . GLN A 1 117 ? 37.313  11.818  23.321  1.00 55.14  ?  110 GLN A CD    1 
ATOM   737  O  OE1   . GLN A 1 117 ? 38.072  11.001  23.845  1.00 57.53  ?  110 GLN A OE1   1 
ATOM   738  N  NE2   . GLN A 1 117 ? 36.499  12.587  24.036  1.00 53.40  ?  110 GLN A NE2   1 
ATOM   739  N  N     . PHE A 1 118 ? 35.721  11.220  18.977  1.00 49.91  ?  111 PHE A N     1 
ATOM   740  C  CA    . PHE A 1 118 ? 34.507  10.485  18.665  1.00 46.97  ?  111 PHE A CA    1 
ATOM   741  C  C     . PHE A 1 118 ? 34.584  10.000  17.222  1.00 47.39  ?  111 PHE A C     1 
ATOM   742  O  O     . PHE A 1 118 ? 34.166  8.885   16.906  1.00 46.83  ?  111 PHE A O     1 
ATOM   743  C  CB    . PHE A 1 118 ? 33.277  11.362  18.927  1.00 43.95  ?  111 PHE A CB    1 
ATOM   744  C  CG    . PHE A 1 118 ? 31.965  10.636  18.807  1.00 41.19  ?  111 PHE A CG    1 
ATOM   745  C  CD1   . PHE A 1 118 ? 31.366  10.459  17.580  1.00 39.96  ?  111 PHE A CD1   1 
ATOM   746  C  CD2   . PHE A 1 118 ? 31.354  10.103  19.932  1.00 40.25  ?  111 PHE A CD2   1 
ATOM   747  C  CE1   . PHE A 1 118 ? 30.159  9.794   17.465  1.00 37.79  ?  111 PHE A CE1   1 
ATOM   748  C  CE2   . PHE A 1 118 ? 30.153  9.411   19.808  1.00 38.17  ?  111 PHE A CE2   1 
ATOM   749  C  CZ    . PHE A 1 118 ? 29.554  9.275   18.583  1.00 36.93  ?  111 PHE A CZ    1 
ATOM   750  N  N     . LEU A 1 119 ? 35.059  10.876  16.335  1.00 48.57  ?  112 LEU A N     1 
ATOM   751  C  CA    . LEU A 1 119 ? 35.123  10.539  14.925  1.00 49.28  ?  112 LEU A CA    1 
ATOM   752  C  C     . LEU A 1 119 ? 36.221  9.508   14.685  1.00 52.65  ?  112 LEU A C     1 
ATOM   753  O  O     . LEU A 1 119 ? 36.091  8.667   13.796  1.00 53.13  ?  112 LEU A O     1 
ATOM   754  C  CB    . LEU A 1 119 ? 35.332  11.802  14.089  1.00 50.03  ?  112 LEU A CB    1 
ATOM   755  C  CG    . LEU A 1 119 ? 34.280  12.903  14.269  1.00 47.25  ?  112 LEU A CG    1 
ATOM   756  C  CD1   . LEU A 1 119 ? 34.530  14.033  13.293  1.00 48.59  ?  112 LEU A CD1   1 
ATOM   757  C  CD2   . LEU A 1 119 ? 32.865  12.368  14.090  1.00 43.86  ?  112 LEU A CD2   1 
ATOM   758  N  N     . GLN A 1 120 ? 37.292  9.561   15.492  1.00 55.31  ?  113 GLN A N     1 
ATOM   759  C  CA    . GLN A 1 120 ? 38.365  8.589   15.377  1.00 58.96  ?  113 GLN A CA    1 
ATOM   760  C  C     . GLN A 1 120 ? 37.841  7.218   15.819  1.00 58.02  ?  113 GLN A C     1 
ATOM   761  O  O     . GLN A 1 120 ? 38.107  6.214   15.170  1.00 59.87  ?  113 GLN A O     1 
ATOM   762  C  CB    . GLN A 1 120 ? 39.594  9.056   16.166  1.00 62.24  ?  113 GLN A CB    1 
ATOM   763  C  CG    . GLN A 1 120 ? 40.764  8.083   16.103  1.00 66.58  ?  113 GLN A CG    1 
ATOM   764  C  CD    . GLN A 1 120 ? 41.999  8.600   16.802  1.00 70.25  ?  113 GLN A CD    1 
ATOM   765  O  OE1   . GLN A 1 120 ? 42.148  9.797   17.062  1.00 70.20  ?  113 GLN A OE1   1 
ATOM   766  N  NE2   . GLN A 1 120 ? 42.903  7.685   17.117  1.00 73.86  ?  113 GLN A NE2   1 
ATOM   767  N  N     . LYS A 1 121 ? 37.010  7.178   16.864  1.00 55.30  ?  114 LYS A N     1 
ATOM   768  C  CA    . LYS A 1 121 ? 36.562  5.904   17.395  1.00 54.93  ?  114 LYS A CA    1 
ATOM   769  C  C     . LYS A 1 121 ? 35.448  5.315   16.528  1.00 52.69  ?  114 LYS A C     1 
ATOM   770  O  O     . LYS A 1 121 ? 35.439  4.092   16.348  1.00 54.01  ?  114 LYS A O     1 
ATOM   771  C  CB    . LYS A 1 121 ? 36.116  6.025   18.856  1.00 53.45  ?  114 LYS A CB    1 
ATOM   772  C  CG    . LYS A 1 121 ? 35.574  4.734   19.458  1.00 53.26  ?  114 LYS A CG    1 
ATOM   773  C  CD    . LYS A 1 121 ? 35.089  4.851   20.880  1.00 52.10  ?  114 LYS A CD    1 
ATOM   774  C  CE    . LYS A 1 121 ? 34.591  3.522   21.408  1.00 52.49  ?  114 LYS A CE    1 
ATOM   775  N  NZ    . LYS A 1 121 ? 33.625  3.725   22.505  1.00 50.42  ?  114 LYS A NZ    1 
ATOM   776  N  N     . HIS A 1 122 ? 34.519  6.159   16.022  1.00 49.70  ?  115 HIS A N     1 
ATOM   777  C  CA    . HIS A 1 122 ? 33.272  5.674   15.417  1.00 47.30  ?  115 HIS A CA    1 
ATOM   778  C  C     . HIS A 1 122 ? 33.142  6.008   13.928  1.00 47.32  ?  115 HIS A C     1 
ATOM   779  O  O     . HIS A 1 122 ? 32.135  5.639   13.308  1.00 45.66  ?  115 HIS A O     1 
ATOM   780  C  CB    . HIS A 1 122 ? 32.036  6.240   16.138  1.00 43.81  ?  115 HIS A CB    1 
ATOM   781  C  CG    . HIS A 1 122 ? 31.937  5.853   17.566  1.00 43.72  ?  115 HIS A CG    1 
ATOM   782  N  ND1   . HIS A 1 122 ? 31.591  4.607   18.058  1.00 44.20  ?  115 HIS A ND1   1 
ATOM   783  C  CD2   . HIS A 1 122 ? 32.095  6.646   18.631  1.00 43.39  ?  115 HIS A CD2   1 
ATOM   784  C  CE1   . HIS A 1 122 ? 31.582  4.668   19.378  1.00 44.20  ?  115 HIS A CE1   1 
ATOM   785  N  NE2   . HIS A 1 122 ? 31.908  5.902   19.743  1.00 43.73  ?  115 HIS A NE2   1 
ATOM   786  N  N     . GLY A 1 123 ? 34.165  6.679   13.366  1.00 49.56  ?  116 GLY A N     1 
ATOM   787  C  CA    . GLY A 1 123 ? 34.170  7.205   12.013  1.00 50.07  ?  116 GLY A CA    1 
ATOM   788  C  C     . GLY A 1 123 ? 33.960  6.158   10.924  1.00 51.22  ?  116 GLY A C     1 
ATOM   789  O  O     . GLY A 1 123 ? 33.302  6.451   9.937   1.00 50.20  ?  116 GLY A O     1 
ATOM   790  N  N     . ARG A 1 124 ? 34.427  4.925   11.124  1.00 53.45  ?  117 ARG A N     1 
ATOM   791  C  CA    . ARG A 1 124 ? 34.193  3.879   10.127  1.00 54.91  ?  117 ARG A CA    1 
ATOM   792  C  C     . ARG A 1 124 ? 32.689  3.599   9.984   1.00 51.63  ?  117 ARG A C     1 
ATOM   793  O  O     . ARG A 1 124 ? 32.238  3.148   8.929   1.00 52.18  ?  117 ARG A O     1 
ATOM   794  C  CB    . ARG A 1 124 ? 34.993  2.620   10.479  1.00 58.32  ?  117 ARG A CB    1 
ATOM   795  C  CG    . ARG A 1 124 ? 34.535  1.913   11.745  1.00 57.02  ?  117 ARG A CG    1 
ATOM   796  C  CD    . ARG A 1 124 ? 35.382  0.713   12.128  1.00 60.83  ?  117 ARG A CD    1 
ATOM   797  N  NE    . ARG A 1 124 ? 34.833  0.010   13.283  1.00 59.74  ?  117 ARG A NE    1 
ATOM   798  C  CZ    . ARG A 1 124 ? 34.894  0.430   14.545  1.00 58.46  ?  117 ARG A CZ    1 
ATOM   799  N  NH1   . ARG A 1 124 ? 35.515  1.557   14.847  1.00 58.14  ?  117 ARG A NH1   1 
ATOM   800  N  NH2   . ARG A 1 124 ? 34.337  -0.288  15.508  1.00 57.86  ?  117 ARG A NH2   1 
ATOM   801  N  N     . ASN A 1 125 ? 31.894  3.932   11.024  1.00 48.47  ?  118 ASN A N     1 
ATOM   802  C  CA    . ASN A 1 125 ? 30.480  3.593   11.070  1.00 45.79  ?  118 ASN A CA    1 
ATOM   803  C  C     . ASN A 1 125 ? 29.578  4.814   10.800  1.00 42.77  ?  118 ASN A C     1 
ATOM   804  O  O     . ASN A 1 125 ? 28.363  4.679   10.813  1.00 40.63  ?  118 ASN A O     1 
ATOM   805  C  CB    . ASN A 1 125 ? 30.164  2.930   12.407  1.00 45.09  ?  118 ASN A CB    1 
ATOM   806  C  CG    . ASN A 1 125 ? 30.891  1.612   12.588  1.00 48.33  ?  118 ASN A CG    1 
ATOM   807  O  OD1   . ASN A 1 125 ? 30.947  0.787   11.662  1.00 50.37  ?  118 ASN A OD1   1 
ATOM   808  N  ND2   . ASN A 1 125 ? 31.455  1.395   13.767  1.00 49.19  ?  118 ASN A ND2   1 
ATOM   809  N  N     . ILE A 1 126 ? 30.169  5.978   10.526  1.00 43.01  ?  119 ILE A N     1 
ATOM   810  C  CA    . ILE A 1 126 ? 29.429  7.193   10.211  1.00 40.79  ?  119 ILE A CA    1 
ATOM   811  C  C     . ILE A 1 126 ? 29.575  7.459   8.723   1.00 42.22  ?  119 ILE A C     1 
ATOM   812  O  O     . ILE A 1 126 ? 30.678  7.746   8.250   1.00 44.81  ?  119 ILE A O     1 
ATOM   813  C  CB    . ILE A 1 126 ? 29.894  8.397   11.050  1.00 40.28  ?  119 ILE A CB    1 
ATOM   814  C  CG1   . ILE A 1 126 ? 29.760  8.102   12.549  1.00 39.23  ?  119 ILE A CG1   1 
ATOM   815  C  CG2   . ILE A 1 126 ? 29.156  9.675   10.635  1.00 38.54  ?  119 ILE A CG2   1 
ATOM   816  C  CD1   . ILE A 1 126 ? 30.498  9.056   13.459  1.00 39.72  ?  119 ILE A CD1   1 
ATOM   817  N  N     . ASP A 1 127 ? 28.450  7.444   8.008   1.00 40.76  ?  120 ASP A N     1 
ATOM   818  C  CA    . ASP A 1 127 ? 28.471  7.773   6.598   1.00 42.14  ?  120 ASP A CA    1 
ATOM   819  C  C     . ASP A 1 127 ? 28.489  9.275   6.412   1.00 41.54  ?  120 ASP A C     1 
ATOM   820  O  O     . ASP A 1 127 ? 29.237  9.785   5.585   1.00 43.84  ?  120 ASP A O     1 
ATOM   821  C  CB    . ASP A 1 127 ? 27.327  7.056   5.883   1.00 41.42  ?  120 ASP A CB    1 
ATOM   822  C  CG    . ASP A 1 127 ? 27.584  5.567   5.883   1.00 43.20  ?  120 ASP A CG    1 
ATOM   823  O  OD1   . ASP A 1 127 ? 28.604  5.164   5.280   1.00 46.31  ?  120 ASP A OD1   1 
ATOM   824  O  OD2   . ASP A 1 127 ? 26.857  4.844   6.580   1.00 41.84  ?  120 ASP A OD2   1 
ATOM   825  N  N     . ILE A 1 128 ? 27.582  9.975   7.114   1.00 38.77  ?  121 ILE A N     1 
ATOM   826  C  CA    . ILE A 1 128 ? 27.372  11.391  6.940   1.00 38.23  ?  121 ILE A CA    1 
ATOM   827  C  C     . ILE A 1 128 ? 27.306  12.093  8.297   1.00 36.65  ?  121 ILE A C     1 
ATOM   828  O  O     . ILE A 1 128 ? 26.659  11.593  9.225   1.00 34.80  ?  121 ILE A O     1 
ATOM   829  C  CB    . ILE A 1 128 ? 26.047  11.645  6.204   1.00 36.80  ?  121 ILE A CB    1 
ATOM   830  C  CG1   . ILE A 1 128 ? 25.973  10.995  4.814   1.00 38.49  ?  121 ILE A CG1   1 
ATOM   831  C  CG2   . ILE A 1 128 ? 25.772  13.125  6.173   1.00 36.37  ?  121 ILE A CG2   1 
ATOM   832  C  CD1   . ILE A 1 128 ? 24.560  10.876  4.273   1.00 37.08  ?  121 ILE A CD1   1 
ATOM   833  N  N     . LEU A 1 129 ? 27.982  13.243  8.398   1.00 37.78  ?  122 LEU A N     1 
ATOM   834  C  CA    . LEU A 1 129 ? 27.875  14.089  9.578   1.00 36.70  ?  122 LEU A CA    1 
ATOM   835  C  C     . LEU A 1 129 ? 27.357  15.454  9.135   1.00 36.63  ?  122 LEU A C     1 
ATOM   836  O  O     . LEU A 1 129 ? 28.039  16.165  8.388   1.00 38.83  ?  122 LEU A O     1 
ATOM   837  C  CB    . LEU A 1 129 ? 29.211  14.200  10.317  1.00 38.62  ?  122 LEU A CB    1 
ATOM   838  C  CG    . LEU A 1 129 ? 29.201  15.172  11.493  1.00 38.11  ?  122 LEU A CG    1 
ATOM   839  C  CD1   . LEU A 1 129 ? 28.238  14.693  12.571  1.00 35.58  ?  122 LEU A CD1   1 
ATOM   840  C  CD2   . LEU A 1 129 ? 30.598  15.339  12.077  1.00 40.59  ?  122 LEU A CD2   1 
ATOM   841  N  N     . ALA A 1 130 ? 26.119  15.787  9.535   1.00 34.46  ?  123 ALA A N     1 
ATOM   842  C  CA    . ALA A 1 130 ? 25.539  17.094  9.269   1.00 34.54  ?  123 ALA A CA    1 
ATOM   843  C  C     . ALA A 1 130 ? 25.733  18.035  10.443  1.00 34.69  ?  123 ALA A C     1 
ATOM   844  O  O     . ALA A 1 130 ? 25.386  17.727  11.587  1.00 33.30  ?  123 ALA A O     1 
ATOM   845  C  CB    . ALA A 1 130 ? 24.057  17.012  8.900   1.00 32.76  ?  123 ALA A CB    1 
ATOM   846  N  N     . VAL A 1 131 ? 26.258  19.229  10.150  1.00 36.72  ?  124 VAL A N     1 
ATOM   847  C  CA    . VAL A 1 131 ? 26.423  20.247  11.174  1.00 37.40  ?  124 VAL A CA    1 
ATOM   848  C  C     . VAL A 1 131 ? 25.482  21.412  10.865  1.00 37.60  ?  124 VAL A C     1 
ATOM   849  O  O     . VAL A 1 131 ? 25.422  21.856  9.724   1.00 38.81  ?  124 VAL A O     1 
ATOM   850  C  CB    . VAL A 1 131 ? 27.896  20.700  11.294  1.00 40.26  ?  124 VAL A CB    1 
ATOM   851  C  CG1   . VAL A 1 131 ? 28.092  21.740  12.371  1.00 41.35  ?  124 VAL A CG1   1 
ATOM   852  C  CG2   . VAL A 1 131 ? 28.825  19.527  11.526  1.00 40.49  ?  124 VAL A CG2   1 
ATOM   853  N  N     . SER A 1 132 ? 24.722  21.862  11.869  1.00 36.65  ?  125 SER A N     1 
ATOM   854  C  CA    . SER A 1 132 ? 23.759  22.929  11.736  1.00 37.06  ?  125 SER A CA    1 
ATOM   855  C  C     . SER A 1 132 ? 24.406  24.267  12.087  1.00 39.83  ?  125 SER A C     1 
ATOM   856  O  O     . SER A 1 132 ? 24.721  24.509  13.247  1.00 40.25  ?  125 SER A O     1 
ATOM   857  C  CB    . SER A 1 132 ? 22.537  22.731  12.618  1.00 35.14  ?  125 SER A CB    1 
ATOM   858  O  OG    . SER A 1 132 ? 21.822  21.547  12.273  1.00 32.94  ?  125 SER A OG    1 
ATOM   859  N  N     . CYS A 1 133 ? 24.448  25.150  11.097  1.00 41.88  ?  126 CYS A N     1 
ATOM   860  C  CA    . CYS A 1 133 ? 25.016  26.487  11.253  1.00 45.10  ?  126 CYS A CA    1 
ATOM   861  C  C     . CYS A 1 133 ? 24.274  27.415  10.303  1.00 46.56  ?  126 CYS A C     1 
ATOM   862  O  O     . CYS A 1 133 ? 24.303  27.220  9.097   1.00 46.96  ?  126 CYS A O     1 
ATOM   863  C  CB    . CYS A 1 133 ? 26.494  26.448  10.918  1.00 47.35  ?  126 CYS A CB    1 
ATOM   864  S  SG    . CYS A 1 133 ? 27.345  27.967  11.429  1.00 51.65  ?  126 CYS A SG    1 
ATOM   865  N  N     . ASP A 1 134 ? 23.545  28.384  10.845  1.00 47.52  ?  127 ASP A N     1 
ATOM   866  C  CA    . ASP A 1 134 ? 22.585  29.088  10.033  1.00 48.52  ?  127 ASP A CA    1 
ATOM   867  C  C     . ASP A 1 134 ? 23.206  30.341  9.418   1.00 52.65  ?  127 ASP A C     1 
ATOM   868  O  O     . ASP A 1 134 ? 22.583  30.938  8.546   1.00 54.08  ?  127 ASP A O     1 
ATOM   869  C  CB    . ASP A 1 134 ? 21.357  29.492  10.832  1.00 47.92  ?  127 ASP A CB    1 
ATOM   870  C  CG    . ASP A 1 134 ? 20.768  28.289  11.560  1.00 44.34  ?  127 ASP A CG    1 
ATOM   871  O  OD1   . ASP A 1 134 ? 20.570  27.236  10.887  1.00 42.15  ?  127 ASP A OD1   1 
ATOM   872  O  OD2   . ASP A 1 134 ? 20.643  28.382  12.780  1.00 44.12  ?  127 ASP A OD2   1 
ATOM   873  N  N     . SER A 1 135 ? 24.399  30.722  9.884   1.00 54.81  ?  128 SER A N     1 
ATOM   874  C  CA    . SER A 1 135 ? 25.036  31.947  9.405   1.00 59.27  ?  128 SER A CA    1 
ATOM   875  C  C     . SER A 1 135 ? 26.543  31.908  9.600   1.00 61.29  ?  128 SER A C     1 
ATOM   876  O  O     . SER A 1 135 ? 27.050  31.180  10.452  1.00 59.58  ?  128 SER A O     1 
ATOM   877  C  CB    . SER A 1 135 ? 24.476  33.147  10.105  1.00 61.51  ?  128 SER A CB    1 
ATOM   878  O  OG    . SER A 1 135 ? 25.120  34.333  9.633   1.00 66.27  ?  128 SER A OG    1 
ATOM   879  N  N     . PHE A 1 136 ? 27.236  32.800  8.872   1.00 65.50  ?  129 PHE A N     1 
ATOM   880  C  CA    . PHE A 1 136 ? 28.669  32.951  9.022   1.00 68.42  ?  129 PHE A CA    1 
ATOM   881  C  C     . PHE A 1 136 ? 28.999  34.338  9.579   1.00 72.82  ?  129 PHE A C     1 
ATOM   882  O  O     . PHE A 1 136 ? 30.166  34.742  9.571   1.00 76.46  ?  129 PHE A O     1 
ATOM   883  C  CB    . PHE A 1 136 ? 29.339  32.676  7.673   1.00 70.13  ?  129 PHE A CB    1 
ATOM   884  C  CG    . PHE A 1 136 ? 29.201  31.264  7.173   1.00 66.42  ?  129 PHE A CG    1 
ATOM   885  C  CD1   . PHE A 1 136 ? 30.129  30.296  7.524   1.00 65.48  ?  129 PHE A CD1   1 
ATOM   886  C  CD2   . PHE A 1 136 ? 28.106  30.884  6.410   1.00 64.08  ?  129 PHE A CD2   1 
ATOM   887  C  CE1   . PHE A 1 136 ? 30.005  28.988  7.079   1.00 62.48  ?  129 PHE A CE1   1 
ATOM   888  C  CE2   . PHE A 1 136 ? 27.991  29.576  5.957   1.00 61.07  ?  129 PHE A CE2   1 
ATOM   889  C  CZ    . PHE A 1 136 ? 28.931  28.633  6.292   1.00 60.29  ?  129 PHE A CZ    1 
ATOM   890  N  N     . ASN A 1 137 ? 27.973  35.048  10.064  1.00 72.82  ?  130 ASN A N     1 
ATOM   891  C  CA    . ASN A 1 137 ? 28.148  36.192  10.938  1.00 76.39  ?  130 ASN A CA    1 
ATOM   892  C  C     . ASN A 1 137 ? 27.860  35.768  12.374  1.00 73.78  ?  130 ASN A C     1 
ATOM   893  O  O     . ASN A 1 137 ? 26.704  35.526  12.724  1.00 70.96  ?  130 ASN A O     1 
ATOM   894  C  CB    . ASN A 1 137 ? 27.214  37.326  10.513  1.00 78.94  ?  130 ASN A CB    1 
ATOM   895  C  CG    . ASN A 1 137 ? 27.310  38.556  11.389  1.00 83.13  ?  130 ASN A CG    1 
ATOM   896  O  OD1   . ASN A 1 137 ? 26.957  38.524  12.570  1.00 81.95  ?  130 ASN A OD1   1 
ATOM   897  N  ND2   . ASN A 1 137 ? 27.762  39.658  10.809  1.00 88.39  ?  130 ASN A ND2   1 
ATOM   898  N  N     . GLU A 1 138 ? 28.886  35.766  13.238  1.00 75.29  ?  131 GLU A N     1 
ATOM   899  C  CA    . GLU A 1 138 ? 28.743  35.173  14.557  1.00 72.74  ?  131 GLU A CA    1 
ATOM   900  C  C     . GLU A 1 138 ? 27.698  35.911  15.385  1.00 73.31  ?  131 GLU A C     1 
ATOM   901  O  O     . GLU A 1 138 ? 27.083  35.291  16.250  1.00 70.28  ?  131 GLU A O     1 
ATOM   902  C  CB    . GLU A 1 138 ? 30.088  35.061  15.271  1.00 74.78  ?  131 GLU A CB    1 
ATOM   903  C  CG    . GLU A 1 138 ? 30.968  33.968  14.689  1.00 73.18  ?  131 GLU A CG    1 
ATOM   904  C  CD    . GLU A 1 138 ? 30.512  32.526  14.895  1.00 67.89  ?  131 GLU A CD    1 
ATOM   905  O  OE1   . GLU A 1 138 ? 29.355  32.312  15.298  1.00 64.97  ?  131 GLU A OE1   1 
ATOM   906  O  OE2   . GLU A 1 138 ? 31.337  31.616  14.658  1.00 67.07  ?  131 GLU A OE2   1 
ATOM   907  N  N     . ALA A 1 139 ? 27.460  37.206  15.095  1.00 77.43  ?  132 ALA A N     1 
ATOM   908  C  CA    . ALA A 1 139 ? 26.393  37.935  15.758  1.00 78.43  ?  132 ALA A CA    1 
ATOM   909  C  C     . ALA A 1 139 ? 25.046  37.287  15.448  1.00 74.26  ?  132 ALA A C     1 
ATOM   910  O  O     . ALA A 1 139 ? 24.179  37.245  16.322  1.00 73.15  ?  132 ALA A O     1 
ATOM   911  C  CB    . ALA A 1 139 ? 26.407  39.399  15.367  1.00 83.96  ?  132 ALA A CB    1 
ATOM   912  N  N     . THR A 1 140 ? 24.874  36.835  14.194  1.00 72.50  ?  133 THR A N     1 
ATOM   913  C  CA    . THR A 1 140 ? 23.635  36.210  13.751  1.00 68.93  ?  133 THR A CA    1 
ATOM   914  C  C     . THR A 1 140 ? 23.406  34.907  14.517  1.00 64.30  ?  133 THR A C     1 
ATOM   915  O  O     . THR A 1 140 ? 22.310  34.661  15.008  1.00 62.43  ?  133 THR A O     1 
ATOM   916  C  CB    . THR A 1 140 ? 23.619  35.960  12.235  1.00 68.40  ?  133 THR A CB    1 
ATOM   917  O  OG1   . THR A 1 140 ? 24.028  37.145  11.546  1.00 73.20  ?  133 THR A OG1   1 
ATOM   918  C  CG2   . THR A 1 140 ? 22.251  35.550  11.726  1.00 65.75  ?  133 THR A CG2   1 
ATOM   919  N  N     . ASN A 1 141 ? 24.436  34.065  14.629  1.00 62.79  ?  134 ASN A N     1 
ATOM   920  C  CA    . ASN A 1 141 ? 24.271  32.807  15.346  1.00 58.78  ?  134 ASN A CA    1 
ATOM   921  C  C     . ASN A 1 141 ? 23.969  33.064  16.822  1.00 59.34  ?  134 ASN A C     1 
ATOM   922  O  O     . ASN A 1 141 ? 23.252  32.303  17.463  1.00 56.53  ?  134 ASN A O     1 
ATOM   923  C  CB    . ASN A 1 141 ? 25.497  31.906  15.214  1.00 57.72  ?  134 ASN A CB    1 
ATOM   924  C  CG    . ASN A 1 141 ? 25.775  31.475  13.798  1.00 57.08  ?  134 ASN A CG    1 
ATOM   925  O  OD1   . ASN A 1 141 ? 24.858  31.174  13.034  1.00 55.21  ?  134 ASN A OD1   1 
ATOM   926  N  ND2   . ASN A 1 141 ? 27.047  31.411  13.447  1.00 58.88  ?  134 ASN A ND2   1 
ATOM   927  N  N     . ILE A 1 142 ? 24.518  34.144  17.400  1.00 63.36  ?  135 ILE A N     1 
ATOM   928  C  CA    . ILE A 1 142 ? 24.234  34.441  18.789  1.00 64.42  ?  135 ILE A CA    1 
ATOM   929  C  C     . ILE A 1 142 ? 22.793  34.914  18.957  1.00 64.62  ?  135 ILE A C     1 
ATOM   930  O  O     . ILE A 1 142 ? 22.133  34.484  19.896  1.00 63.19  ?  135 ILE A O     1 
ATOM   931  C  CB    . ILE A 1 142 ? 25.232  35.460  19.378  1.00 69.11  ?  135 ILE A CB    1 
ATOM   932  C  CG1   . ILE A 1 142 ? 26.620  34.827  19.521  1.00 68.87  ?  135 ILE A CG1   1 
ATOM   933  C  CG2   . ILE A 1 142 ? 24.692  36.012  20.693  1.00 71.04  ?  135 ILE A CG2   1 
ATOM   934  C  CD1   . ILE A 1 142 ? 27.720  35.792  19.958  1.00 73.84  ?  135 ILE A CD1   1 
ATOM   935  N  N     . LYS A 1 143 ? 22.297  35.777  18.061  1.00 66.69  ?  136 LYS A N     1 
ATOM   936  C  CA    . LYS A 1 143 ? 20.947  36.309  18.184  1.00 67.56  ?  136 LYS A CA    1 
ATOM   937  C  C     . LYS A 1 143 ? 19.914  35.187  17.985  1.00 63.13  ?  136 LYS A C     1 
ATOM   938  O  O     . LYS A 1 143 ? 18.896  35.148  18.676  1.00 62.90  ?  136 LYS A O     1 
ATOM   939  C  CB    . LYS A 1 143 ? 20.752  37.458  17.186  1.00 71.10  ?  136 LYS A CB    1 
ATOM   940  C  CG    . LYS A 1 143 ? 19.758  38.541  17.604  1.00 74.68  ?  136 LYS A CG    1 
ATOM   941  C  CD    . LYS A 1 143 ? 18.398  38.025  18.033  1.00 72.42  ?  136 LYS A CD    1 
ATOM   942  C  CE    . LYS A 1 143 ? 17.359  39.116  18.197  1.00 76.36  ?  136 LYS A CE    1 
ATOM   943  N  NZ    . LYS A 1 143 ? 16.041  38.560  18.585  1.00 74.41  ?  136 LYS A NZ    1 
ATOM   944  N  N     . ILE A 1 144 ? 20.181  34.282  17.031  1.00 60.02  ?  137 ILE A N     1 
ATOM   945  C  CA    . ILE A 1 144 ? 19.365  33.078  16.830  1.00 55.88  ?  137 ILE A CA    1 
ATOM   946  C  C     . ILE A 1 144 ? 19.262  32.274  18.130  1.00 53.97  ?  137 ILE A C     1 
ATOM   947  O  O     . ILE A 1 144 ? 18.198  31.758  18.457  1.00 52.32  ?  137 ILE A O     1 
ATOM   948  C  CB    . ILE A 1 144 ? 19.916  32.244  15.656  1.00 53.47  ?  137 ILE A CB    1 
ATOM   949  C  CG1   . ILE A 1 144 ? 19.557  32.880  14.310  1.00 55.01  ?  137 ILE A CG1   1 
ATOM   950  C  CG2   . ILE A 1 144 ? 19.428  30.799  15.717  1.00 49.27  ?  137 ILE A CG2   1 
ATOM   951  C  CD1   . ILE A 1 144 ? 20.313  32.284  13.145  1.00 53.81  ?  137 ILE A CD1   1 
ATOM   952  N  N     . GLY A 1 145 ? 20.370  32.161  18.868  1.00 54.51  ?  138 GLY A N     1 
ATOM   953  C  CA    . GLY A 1 145 ? 20.402  31.450  20.130  1.00 53.23  ?  138 GLY A CA    1 
ATOM   954  C  C     . GLY A 1 145 ? 21.080  30.094  20.002  1.00 49.93  ?  138 GLY A C     1 
ATOM   955  O  O     . GLY A 1 145 ? 21.023  29.291  20.924  1.00 48.47  ?  138 GLY A O     1 
ATOM   956  N  N     . ARG A 1 146 ? 21.802  29.869  18.898  1.00 49.26  ?  139 ARG A N     1 
ATOM   957  C  CA    . ARG A 1 146 ? 22.488  28.607  18.726  1.00 46.65  ?  139 ARG A CA    1 
ATOM   958  C  C     . ARG A 1 146 ? 23.898  28.650  19.314  1.00 48.28  ?  139 ARG A C     1 
ATOM   959  O  O     . ARG A 1 146 ? 24.440  27.608  19.669  1.00 46.61  ?  139 ARG A O     1 
ATOM   960  C  CB    . ARG A 1 146 ? 22.569  28.228  17.245  1.00 45.36  ?  139 ARG A CB    1 
ATOM   961  C  CG    . ARG A 1 146 ? 23.007  26.788  17.016  1.00 42.57  ?  139 ARG A CG    1 
ATOM   962  C  CD    . ARG A 1 146 ? 23.210  26.480  15.558  1.00 41.97  ?  139 ARG A CD    1 
ATOM   963  N  NE    . ARG A 1 146 ? 21.974  26.507  14.795  1.00 40.89  ?  139 ARG A NE    1 
ATOM   964  C  CZ    . ARG A 1 146 ? 21.111  25.501  14.681  1.00 38.25  ?  139 ARG A CZ    1 
ATOM   965  N  NH1   . ARG A 1 146 ? 21.216  24.426  15.451  1.00 36.40  ?  139 ARG A NH1   1 
ATOM   966  N  NH2   . ARG A 1 146 ? 20.129  25.594  13.804  1.00 37.82  ?  139 ARG A NH2   1 
ATOM   967  N  N     . GLY A 1 147 ? 24.490  29.845  19.417  1.00 51.85  ?  140 GLY A N     1 
ATOM   968  C  CA    . GLY A 1 147 ? 25.932  29.938  19.567  1.00 53.85  ?  140 GLY A CA    1 
ATOM   969  C  C     . GLY A 1 147 ? 26.371  30.951  20.616  1.00 57.56  ?  140 GLY A C     1 
ATOM   970  O  O     . GLY A 1 147 ? 25.575  31.767  21.064  1.00 59.06  ?  140 GLY A O     1 
ATOM   971  N  N     . SER A 1 148 ? 27.652  30.858  20.993  1.00 59.29  ?  141 SER A N     1 
ATOM   972  C  CA    . SER A 1 148 ? 28.293  31.878  21.805  1.00 63.54  ?  141 SER A CA    1 
ATOM   973  C  C     . SER A 1 148 ? 29.523  32.409  21.066  1.00 66.65  ?  141 SER A C     1 
ATOM   974  O  O     . SER A 1 148 ? 30.433  32.964  21.675  1.00 70.24  ?  141 SER A O     1 
ATOM   975  C  CB    . SER A 1 148 ? 28.622  31.338  23.170  1.00 63.47  ?  141 SER A CB    1 
ATOM   976  O  OG    . SER A 1 148 ? 29.455  30.201  23.074  1.00 61.69  ?  141 SER A OG    1 
ATOM   977  N  N     . GLY A 1 149 ? 29.547  32.232  19.742  1.00 65.61  ?  142 GLY A N     1 
ATOM   978  C  CA    . GLY A 1 149 ? 30.439  32.977  18.883  1.00 69.17  ?  142 GLY A CA    1 
ATOM   979  C  C     . GLY A 1 149 ? 31.525  32.116  18.265  1.00 68.70  ?  142 GLY A C     1 
ATOM   980  O  O     . GLY A 1 149 ? 32.418  32.662  17.642  1.00 72.12  ?  142 GLY A O     1 
ATOM   981  N  N     . ASP A 1 150 ? 31.451  30.788  18.434  1.00 64.91  ?  143 ASP A N     1 
ATOM   982  C  CA    . ASP A 1 150 ? 32.485  29.903  17.912  1.00 64.74  ?  143 ASP A CA    1 
ATOM   983  C  C     . ASP A 1 150 ? 31.938  28.902  16.887  1.00 61.06  ?  143 ASP A C     1 
ATOM   984  O  O     . ASP A 1 150 ? 32.685  28.044  16.433  1.00 60.75  ?  143 ASP A O     1 
ATOM   985  C  CB    . ASP A 1 150 ? 33.183  29.138  19.043  1.00 64.55  ?  143 ASP A CB    1 
ATOM   986  C  CG    . ASP A 1 150 ? 34.089  29.977  19.935  1.00 68.94  ?  143 ASP A CG    1 
ATOM   987  O  OD1   . ASP A 1 150 ? 34.782  30.873  19.396  1.00 72.86  ?  143 ASP A OD1   1 
ATOM   988  O  OD2   . ASP A 1 150 ? 34.133  29.693  21.164  1.00 68.72  ?  143 ASP A OD2   1 
ATOM   989  N  N     . ASN A 1 151 ? 30.696  29.058  16.422  1.00 58.88  ?  144 ASN A N     1 
ATOM   990  C  CA    . ASN A 1 151 ? 30.094  28.047  15.538  1.00 55.42  ?  144 ASN A CA    1 
ATOM   991  C  C     . ASN A 1 151 ? 30.840  27.893  14.204  1.00 56.86  ?  144 ASN A C     1 
ATOM   992  O  O     . ASN A 1 151 ? 31.024  26.773  13.700  1.00 55.01  ?  144 ASN A O     1 
ATOM   993  C  CB    . ASN A 1 151 ? 28.638  28.379  15.243  1.00 53.53  ?  144 ASN A CB    1 
ATOM   994  C  CG    . ASN A 1 151 ? 27.741  28.248  16.455  1.00 51.67  ?  144 ASN A CG    1 
ATOM   995  O  OD1   . ASN A 1 151 ? 27.360  29.248  17.050  1.00 53.47  ?  144 ASN A OD1   1 
ATOM   996  N  ND2   . ASN A 1 151 ? 27.391  27.028  16.830  1.00 48.45  ?  144 ASN A ND2   1 
ATOM   997  N  N     . VAL A 1 152 ? 31.288  29.019  13.617  1.00 60.60  ?  145 VAL A N     1 
ATOM   998  C  CA    . VAL A 1 152 ? 31.909  28.991  12.307  1.00 62.50  ?  145 VAL A CA    1 
ATOM   999  C  C     . VAL A 1 152 ? 33.277  28.328  12.405  1.00 64.13  ?  145 VAL A C     1 
ATOM   1000 O  O     . VAL A 1 152 ? 33.642  27.460  11.604  1.00 63.59  ?  145 VAL A O     1 
ATOM   1001 C  CB    . VAL A 1 152 ? 31.984  30.406  11.695  1.00 66.53  ?  145 VAL A CB    1 
ATOM   1002 C  CG1   . VAL A 1 152 ? 32.689  30.379  10.353  1.00 69.03  ?  145 VAL A CG1   1 
ATOM   1003 C  CG2   . VAL A 1 152 ? 30.604  31.062  11.582  1.00 65.28  ?  145 VAL A CG2   1 
ATOM   1004 N  N     . GLN A 1 153 ? 34.023  28.723  13.437  1.00 66.37  ?  146 GLN A N     1 
ATOM   1005 C  CA    . GLN A 1 153 ? 35.312  28.126  13.729  1.00 68.22  ?  146 GLN A CA    1 
ATOM   1006 C  C     . GLN A 1 153 ? 35.150  26.618  13.897  1.00 64.45  ?  146 GLN A C     1 
ATOM   1007 O  O     . GLN A 1 153 ? 35.872  25.849  13.278  1.00 65.19  ?  146 GLN A O     1 
ATOM   1008 C  CB    . GLN A 1 153 ? 35.893  28.836  14.958  1.00 70.95  ?  146 GLN A CB    1 
ATOM   1009 C  CG    . GLN A 1 153 ? 37.288  28.392  15.346  1.00 73.73  ?  146 GLN A CG    1 
ATOM   1010 C  CD    . GLN A 1 153 ? 37.930  29.400  16.270  1.00 77.77  ?  146 GLN A CD    1 
ATOM   1011 O  OE1   . GLN A 1 153 ? 37.339  30.424  16.621  1.00 78.55  ?  146 GLN A OE1   1 
ATOM   1012 N  NE2   . GLN A 1 153 ? 39.162  29.122  16.657  1.00 80.78  ?  146 GLN A NE2   1 
ATOM   1013 N  N     . LYS A 1 154 ? 34.169  26.201  14.709  1.00 60.75  ?  147 LYS A N     1 
ATOM   1014 C  CA    . LYS A 1 154 ? 33.959  24.784  14.971  1.00 57.45  ?  147 LYS A CA    1 
ATOM   1015 C  C     . LYS A 1 154 ? 33.546  24.056  13.686  1.00 55.66  ?  147 LYS A C     1 
ATOM   1016 O  O     . LYS A 1 154 ? 33.938  22.926  13.464  1.00 54.92  ?  147 LYS A O     1 
ATOM   1017 C  CB    . LYS A 1 154 ? 32.893  24.582  16.056  1.00 54.29  ?  147 LYS A CB    1 
ATOM   1018 C  CG    . LYS A 1 154 ? 32.753  23.143  16.557  1.00 51.49  ?  147 LYS A CG    1 
ATOM   1019 C  CD    . LYS A 1 154 ? 33.972  22.692  17.322  1.00 53.59  ?  147 LYS A CD    1 
ATOM   1020 C  CE    . LYS A 1 154 ? 34.122  21.198  17.524  1.00 51.84  ?  147 LYS A CE    1 
ATOM   1021 N  NZ    . LYS A 1 154 ? 33.406  20.753  18.733  1.00 49.61  ?  147 LYS A NZ    1 
ATOM   1022 N  N     . LEU A 1 155 ? 32.739  24.693  12.845  1.00 55.22  ?  148 LEU A N     1 
ATOM   1023 C  CA    . LEU A 1 155 ? 32.290  24.088  11.588  1.00 53.86  ?  148 LEU A CA    1 
ATOM   1024 C  C     . LEU A 1 155 ? 33.457  23.707  10.676  1.00 56.71  ?  148 LEU A C     1 
ATOM   1025 O  O     . LEU A 1 155 ? 33.548  22.576  10.180  1.00 55.59  ?  148 LEU A O     1 
ATOM   1026 C  CB    . LEU A 1 155 ? 31.345  25.093  10.926  1.00 53.91  ?  148 LEU A CB    1 
ATOM   1027 C  CG    . LEU A 1 155 ? 30.730  24.655  9.603   1.00 52.79  ?  148 LEU A CG    1 
ATOM   1028 C  CD1   . LEU A 1 155 ? 29.807  23.447  9.839   1.00 48.65  ?  148 LEU A CD1   1 
ATOM   1029 C  CD2   . LEU A 1 155 ? 29.966  25.793  8.953   1.00 53.79  ?  148 LEU A CD2   1 
ATOM   1030 N  N     . TYR A 1 156 ? 34.391  24.664  10.466  1.00 60.89  ?  149 TYR A N     1 
ATOM   1031 C  CA    . TYR A 1 156 ? 35.576  24.421  9.663   1.00 64.42  ?  149 TYR A CA    1 
ATOM   1032 C  C     . TYR A 1 156 ? 36.405  23.276  10.234  1.00 64.39  ?  149 TYR A C     1 
ATOM   1033 O  O     . TYR A 1 156 ? 36.921  22.463  9.478   1.00 65.42  ?  149 TYR A O     1 
ATOM   1034 C  CB    . TYR A 1 156 ? 36.406  25.713  9.553   1.00 69.26  ?  149 TYR A CB    1 
ATOM   1035 C  CG    . TYR A 1 156 ? 36.006  26.640  8.417   1.00 71.06  ?  149 TYR A CG    1 
ATOM   1036 C  CD1   . TYR A 1 156 ? 36.572  26.508  7.148   1.00 73.94  ?  149 TYR A CD1   1 
ATOM   1037 C  CD2   . TYR A 1 156 ? 35.056  27.635  8.597   1.00 70.26  ?  149 TYR A CD2   1 
ATOM   1038 C  CE1   . TYR A 1 156 ? 36.211  27.362  6.116   1.00 75.94  ?  149 TYR A CE1   1 
ATOM   1039 C  CE2   . TYR A 1 156 ? 34.688  28.497  7.574   1.00 72.26  ?  149 TYR A CE2   1 
ATOM   1040 C  CZ    . TYR A 1 156 ? 35.273  28.361  6.329   1.00 75.10  ?  149 TYR A CZ    1 
ATOM   1041 O  OH    . TYR A 1 156 ? 34.884  29.180  5.310   1.00 77.24  ?  149 TYR A OH    1 
ATOM   1042 N  N     . GLU A 1 157 ? 36.514  23.208  11.563  1.00 63.50  ?  150 GLU A N     1 
ATOM   1043 C  CA    . GLU A 1 157 ? 37.238  22.142  12.233  1.00 63.56  ?  150 GLU A CA    1 
ATOM   1044 C  C     . GLU A 1 157 ? 36.596  20.782  11.923  1.00 60.11  ?  150 GLU A C     1 
ATOM   1045 O  O     . GLU A 1 157 ? 37.297  19.838  11.533  1.00 61.40  ?  150 GLU A O     1 
ATOM   1046 C  CB    . GLU A 1 157 ? 37.345  22.486  13.723  1.00 63.44  ?  150 GLU A CB    1 
ATOM   1047 C  CG    . GLU A 1 157 ? 38.117  21.469  14.533  1.00 63.93  ?  150 GLU A CG    1 
ATOM   1048 C  CD    . GLU A 1 157 ? 38.540  21.862  15.939  1.00 65.18  ?  150 GLU A CD    1 
ATOM   1049 O  OE1   . GLU A 1 157 ? 37.741  22.468  16.671  1.00 63.44  ?  150 GLU A OE1   1 
ATOM   1050 O  OE2   . GLU A 1 157 ? 39.665  21.525  16.309  1.00 68.14  ?  150 GLU A OE2   1 
ATOM   1051 N  N     . ILE A 1 158 ? 35.266  20.680  12.079  1.00 56.14  ?  151 ILE A N     1 
ATOM   1052 C  CA    . ILE A 1 158 ? 34.551  19.426  11.835  1.00 53.00  ?  151 ILE A CA    1 
ATOM   1053 C  C     . ILE A 1 158 ? 34.681  19.024  10.362  1.00 54.10  ?  151 ILE A C     1 
ATOM   1054 O  O     . ILE A 1 158 ? 34.884  17.840  10.028  1.00 53.92  ?  151 ILE A O     1 
ATOM   1055 C  CB    . ILE A 1 158 ? 33.073  19.541  12.279  1.00 49.11  ?  151 ILE A CB    1 
ATOM   1056 C  CG1   . ILE A 1 158 ? 32.972  19.680  13.799  1.00 48.21  ?  151 ILE A CG1   1 
ATOM   1057 C  CG2   . ILE A 1 158 ? 32.262  18.363  11.746  1.00 46.41  ?  151 ILE A CG2   1 
ATOM   1058 C  CD1   . ILE A 1 158 ? 31.595  20.055  14.294  1.00 45.31  ?  151 ILE A CD1   1 
ATOM   1059 N  N     . GLY A 1 159 ? 34.598  20.021  9.476   1.00 55.71  ?  152 GLY A N     1 
ATOM   1060 C  CA    . GLY A 1 159 ? 34.863  19.820  8.058   1.00 57.69  ?  152 GLY A CA    1 
ATOM   1061 C  C     . GLY A 1 159 ? 36.192  19.099  7.835   1.00 61.01  ?  152 GLY A C     1 
ATOM   1062 O  O     . GLY A 1 159 ? 36.250  18.121  7.093   1.00 61.23  ?  152 GLY A O     1 
ATOM   1063 N  N     . SER A 1 160 ? 37.253  19.548  8.528   1.00 63.85  ?  153 SER A N     1 
ATOM   1064 C  CA    . SER A 1 160 ? 38.567  18.968  8.318   1.00 67.69  ?  153 SER A CA    1 
ATOM   1065 C  C     . SER A 1 160 ? 38.627  17.554  8.879   1.00 66.04  ?  153 SER A C     1 
ATOM   1066 O  O     . SER A 1 160 ? 39.263  16.695  8.274   1.00 68.27  ?  153 SER A O     1 
ATOM   1067 C  CB    . SER A 1 160 ? 39.709  19.834  8.833   1.00 71.76  ?  153 SER A CB    1 
ATOM   1068 O  OG    . SER A 1 160 ? 39.476  20.316  10.144  1.00 70.09  ?  153 SER A OG    1 
ATOM   1069 N  N     . TRP A 1 161 ? 37.962  17.314  10.025  1.00 62.53  ?  154 TRP A N     1 
ATOM   1070 C  CA    . TRP A 1 161 ? 37.903  15.979  10.602  1.00 60.96  ?  154 TRP A CA    1 
ATOM   1071 C  C     . TRP A 1 161 ? 37.183  14.999  9.678   1.00 59.21  ?  154 TRP A C     1 
ATOM   1072 O  O     . TRP A 1 161 ? 37.571  13.845  9.591   1.00 60.14  ?  154 TRP A O     1 
ATOM   1073 C  CB    . TRP A 1 161 ? 37.207  16.018  11.967  1.00 57.70  ?  154 TRP A CB    1 
ATOM   1074 C  CG    . TRP A 1 161 ? 37.971  16.699  13.075  1.00 59.62  ?  154 TRP A CG    1 
ATOM   1075 C  CD1   . TRP A 1 161 ? 39.313  16.948  13.188  1.00 63.93  ?  154 TRP A CD1   1 
ATOM   1076 C  CD2   . TRP A 1 161 ? 37.368  17.237  14.275  1.00 57.47  ?  154 TRP A CD2   1 
ATOM   1077 N  NE1   . TRP A 1 161 ? 39.584  17.592  14.372  1.00 64.54  ?  154 TRP A NE1   1 
ATOM   1078 C  CE2   . TRP A 1 161 ? 38.409  17.785  15.057  1.00 60.65  ?  154 TRP A CE2   1 
ATOM   1079 C  CE3   . TRP A 1 161 ? 36.055  17.312  14.747  1.00 53.56  ?  154 TRP A CE3   1 
ATOM   1080 C  CZ2   . TRP A 1 161 ? 38.168  18.394  16.285  1.00 59.97  ?  154 TRP A CZ2   1 
ATOM   1081 C  CZ3   . TRP A 1 161 ? 35.822  17.922  15.955  1.00 52.98  ?  154 TRP A CZ3   1 
ATOM   1082 C  CH2   . TRP A 1 161 ? 36.864  18.454  16.714  1.00 56.12  ?  154 TRP A CH2   1 
ATOM   1083 N  N     . CYS A 1 162 ? 36.107  15.427  9.014   1.00 56.89  ?  155 CYS A N     1 
ATOM   1084 C  CA    . CYS A 1 162 ? 35.388  14.536  8.109   1.00 55.50  ?  155 CYS A CA    1 
ATOM   1085 C  C     . CYS A 1 162 ? 36.323  14.115  6.964   1.00 59.51  ?  155 CYS A C     1 
ATOM   1086 O  O     . CYS A 1 162 ? 36.374  12.948  6.598   1.00 59.96  ?  155 CYS A O     1 
ATOM   1087 C  CB    . CYS A 1 162 ? 34.096  15.179  7.604   1.00 52.77  ?  155 CYS A CB    1 
ATOM   1088 S  SG    . CYS A 1 162 ? 32.801  15.331  8.873   1.00 48.14  ?  155 CYS A SG    1 
ATOM   1089 N  N     . GLN A 1 163 ? 37.109  15.075  6.481   1.00 62.84  ?  156 GLN A N     1 
ATOM   1090 C  CA    . GLN A 1 163 ? 38.134  14.860  5.467   1.00 67.49  ?  156 GLN A CA    1 
ATOM   1091 C  C     . GLN A 1 163 ? 39.092  13.776  5.951   1.00 69.66  ?  156 GLN A C     1 
ATOM   1092 O  O     . GLN A 1 163 ? 39.334  12.790  5.265   1.00 71.41  ?  156 GLN A O     1 
ATOM   1093 C  CB    . GLN A 1 163 ? 38.860  16.188  5.217   1.00 70.86  ?  156 GLN A CB    1 
ATOM   1094 C  CG    . GLN A 1 163 ? 38.881  16.641  3.764   1.00 73.55  ?  156 GLN A CG    1 
ATOM   1095 C  CD    . GLN A 1 163 ? 39.964  15.976  2.950   1.00 78.41  ?  156 GLN A CD    1 
ATOM   1096 O  OE1   . GLN A 1 163 ? 41.109  16.422  2.929   1.00 82.88  ?  156 GLN A OE1   1 
ATOM   1097 N  NE2   . GLN A 1 163 ? 39.602  14.918  2.243   1.00 78.01  ?  156 GLN A NE2   1 
ATOM   1098 N  N     . LYS A 1 164 ? 39.593  13.956  7.173   1.00 69.66  ?  157 LYS A N     1 
ATOM   1099 C  CA    . LYS A 1 164 ? 40.559  13.069  7.790   1.00 72.04  ?  157 LYS A CA    1 
ATOM   1100 C  C     . LYS A 1 164 ? 40.008  11.662  8.023   1.00 69.81  ?  157 LYS A C     1 
ATOM   1101 O  O     . LYS A 1 164 ? 40.764  10.713  7.843   1.00 72.86  ?  157 LYS A O     1 
ATOM   1102 C  CB    . LYS A 1 164 ? 41.000  13.664  9.128   1.00 72.02  ?  157 LYS A CB    1 
ATOM   1103 C  CG    . LYS A 1 164 ? 42.064  12.898  9.901   1.00 74.87  ?  157 LYS A CG    1 
ATOM   1104 C  CD    . LYS A 1 164 ? 42.533  13.691  11.104  1.00 75.45  ?  157 LYS A CD    1 
ATOM   1105 C  CE    . LYS A 1 164 ? 43.496  12.958  12.015  1.00 78.09  ?  157 LYS A CE    1 
ATOM   1106 N  NZ    . LYS A 1 164 ? 44.434  12.084  11.271  1.00 82.44  ?  157 LYS A NZ    1 
ATOM   1107 N  N     . TYR A 1 165 ? 38.731  11.524  8.450   1.00 65.00  ?  158 TYR A N     1 
ATOM   1108 C  CA    . TYR A 1 165 ? 38.206  10.240  8.915   1.00 63.02  ?  158 TYR A CA    1 
ATOM   1109 C  C     . TYR A 1 165 ? 37.220  9.638   7.907   1.00 61.35  ?  158 TYR A C     1 
ATOM   1110 O  O     . TYR A 1 165 ? 36.568  8.644   8.217   1.00 59.46  ?  158 TYR A O     1 
ATOM   1111 C  CB    . TYR A 1 165 ? 37.586  10.388  10.317  1.00 59.54  ?  158 TYR A CB    1 
ATOM   1112 C  CG    . TYR A 1 165 ? 38.627  10.729  11.380  1.00 61.71  ?  158 TYR A CG    1 
ATOM   1113 C  CD1   . TYR A 1 165 ? 39.542  9.783   11.830  1.00 64.54  ?  158 TYR A CD1   1 
ATOM   1114 C  CD2   . TYR A 1 165 ? 38.738  12.017  11.880  1.00 61.47  ?  158 TYR A CD2   1 
ATOM   1115 C  CE1   . TYR A 1 165 ? 40.528  10.107  12.751  1.00 66.97  ?  158 TYR A CE1   1 
ATOM   1116 C  CE2   . TYR A 1 165 ? 39.712  12.355  12.804  1.00 63.89  ?  158 TYR A CE2   1 
ATOM   1117 C  CZ    . TYR A 1 165 ? 40.614  11.399  13.232  1.00 66.64  ?  158 TYR A CZ    1 
ATOM   1118 O  OH    . TYR A 1 165 ? 41.554  11.759  14.152  1.00 69.22  ?  158 TYR A OH    1 
ATOM   1119 N  N     . ASP A 1 166 ? 37.179  10.176  6.680   1.00 62.64  ?  159 ASP A N     1 
ATOM   1120 C  CA    . ASP A 1 166 ? 36.435  9.580   5.586   1.00 62.15  ?  159 ASP A CA    1 
ATOM   1121 C  C     . ASP A 1 166 ? 34.941  9.626   5.915   1.00 57.30  ?  159 ASP A C     1 
ATOM   1122 O  O     . ASP A 1 166 ? 34.270  8.611   5.833   1.00 56.04  ?  159 ASP A O     1 
ATOM   1123 C  CB    . ASP A 1 166 ? 36.867  8.128   5.321   1.00 64.62  ?  159 ASP A CB    1 
ATOM   1124 C  CG    . ASP A 1 166 ? 36.384  7.568   3.995   1.00 65.62  ?  159 ASP A CG    1 
ATOM   1125 O  OD1   . ASP A 1 166 ? 36.094  8.381   3.095   1.00 65.75  ?  159 ASP A OD1   1 
ATOM   1126 O  OD2   . ASP A 1 166 ? 36.278  6.321   3.881   1.00 66.48  ?  159 ASP A OD2   1 
ATOM   1127 N  N     . ILE A 1 167 ? 34.453  10.798  6.318   1.00 55.01  ?  160 ILE A N     1 
ATOM   1128 C  CA    . ILE A 1 167 ? 33.033  10.996  6.581   1.00 50.88  ?  160 ILE A CA    1 
ATOM   1129 C  C     . ILE A 1 167 ? 32.509  12.049  5.618   1.00 50.70  ?  160 ILE A C     1 
ATOM   1130 O  O     . ILE A 1 167 ? 33.089  13.128  5.460   1.00 52.39  ?  160 ILE A O     1 
ATOM   1131 C  CB    . ILE A 1 167 ? 32.757  11.405  8.041   1.00 48.37  ?  160 ILE A CB    1 
ATOM   1132 C  CG1   . ILE A 1 167 ? 33.292  10.376  9.036   1.00 48.86  ?  160 ILE A CG1   1 
ATOM   1133 C  CG2   . ILE A 1 167 ? 31.252  11.647  8.204   1.00 44.61  ?  160 ILE A CG2   1 
ATOM   1134 C  CD1   . ILE A 1 167 ? 33.375  10.882  10.452  1.00 47.60  ?  160 ILE A CD1   1 
ATOM   1135 N  N     . LYS A 1 168 ? 31.360  11.772  5.004   1.00 48.79  ?  161 LYS A N     1 
ATOM   1136 C  CA    . LYS A 1 168 ? 30.731  12.783  4.166   1.00 48.51  ?  161 LYS A CA    1 
ATOM   1137 C  C     . LYS A 1 168 ? 30.235  13.973  4.987   1.00 46.36  ?  161 LYS A C     1 
ATOM   1138 O  O     . LYS A 1 168 ? 29.606  13.796  6.041   1.00 43.60  ?  161 LYS A O     1 
ATOM   1139 C  CB    . LYS A 1 168 ? 29.613  12.148  3.331   1.00 47.31  ?  161 LYS A CB    1 
ATOM   1140 C  CG    . LYS A 1 168 ? 30.067  11.033  2.397   1.00 49.97  ?  161 LYS A CG    1 
ATOM   1141 C  CD    . LYS A 1 168 ? 28.910  10.405  1.669   1.00 48.87  ?  161 LYS A CD    1 
ATOM   1142 C  CE    . LYS A 1 168 ? 28.219  11.353  0.714   1.00 48.89  ?  161 LYS A CE    1 
ATOM   1143 N  NZ    . LYS A 1 168 ? 28.838  11.308  -0.634  1.00 52.74  ?  161 LYS A NZ    1 
ATOM   1144 N  N     . PHE A 1 169 ? 30.601  15.194  4.534   1.00 48.17  ?  162 PHE A N     1 
ATOM   1145 C  CA    . PHE A 1 169 ? 30.403  16.434  5.276   1.00 47.27  ?  162 PHE A CA    1 
ATOM   1146 C  C     . PHE A 1 169 ? 29.225  17.240  4.731   1.00 45.97  ?  162 PHE A C     1 
ATOM   1147 O  O     . PHE A 1 169 ? 29.165  17.625  3.558   1.00 47.78  ?  162 PHE A O     1 
ATOM   1148 C  CB    . PHE A 1 169 ? 31.693  17.273  5.323   1.00 50.70  ?  162 PHE A CB    1 
ATOM   1149 C  CG    . PHE A 1 169 ? 31.576  18.640  5.958   1.00 50.65  ?  162 PHE A CG    1 
ATOM   1150 C  CD1   . PHE A 1 169 ? 31.039  18.805  7.227   1.00 48.03  ?  162 PHE A CD1   1 
ATOM   1151 C  CD2   . PHE A 1 169 ? 32.058  19.769  5.307   1.00 53.74  ?  162 PHE A CD2   1 
ATOM   1152 C  CE1   . PHE A 1 169 ? 30.951  20.054  7.815   1.00 48.43  ?  162 PHE A CE1   1 
ATOM   1153 C  CE2   . PHE A 1 169 ? 31.987  21.020  5.901   1.00 54.18  ?  162 PHE A CE2   1 
ATOM   1154 C  CZ    . PHE A 1 169 ? 31.442  21.167  7.158   1.00 51.56  ?  162 PHE A CZ    1 
ATOM   1155 N  N     . LYS A 1 170 ? 28.246  17.471  5.616   1.00 43.03  ?  163 LYS A N     1 
ATOM   1156 C  CA    . LYS A 1 170 ? 26.954  18.017  5.237   1.00 41.54  ?  163 LYS A CA    1 
ATOM   1157 C  C     . LYS A 1 170 ? 26.665  19.205  6.124   1.00 41.01  ?  163 LYS A C     1 
ATOM   1158 O  O     . LYS A 1 170 ? 27.054  19.214  7.286   1.00 40.43  ?  163 LYS A O     1 
ATOM   1159 C  CB    . LYS A 1 170 ? 25.852  16.946  5.345   1.00 38.81  ?  163 LYS A CB    1 
ATOM   1160 C  CG    . LYS A 1 170 ? 24.409  17.454  5.274   1.00 37.07  ?  163 LYS A CG    1 
ATOM   1161 C  CD    . LYS A 1 170 ? 23.388  16.313  5.264   1.00 35.03  ?  163 LYS A CD    1 
ATOM   1162 C  CE    . LYS A 1 170 ? 21.983  16.740  5.625   1.00 33.23  ?  163 LYS A CE    1 
ATOM   1163 N  NZ    . LYS A 1 170 ? 21.227  15.620  6.236   1.00 31.26  ?  163 LYS A NZ    1 
ATOM   1164 N  N     . LEU A 1 171 ? 26.042  20.232  5.539   1.00 41.70  ?  164 LEU A N     1 
ATOM   1165 C  CA    . LEU A 1 171 ? 25.735  21.466  6.223   1.00 41.90  ?  164 LEU A CA    1 
ATOM   1166 C  C     . LEU A 1 171 ? 24.232  21.698  6.164   1.00 40.06  ?  164 LEU A C     1 
ATOM   1167 O  O     . LEU A 1 171 ? 23.615  21.553  5.105   1.00 40.23  ?  164 LEU A O     1 
ATOM   1168 C  CB    . LEU A 1 171 ? 26.488  22.642  5.579   1.00 45.44  ?  164 LEU A CB    1 
ATOM   1169 C  CG    . LEU A 1 171 ? 26.086  24.013  6.121   1.00 46.26  ?  164 LEU A CG    1 
ATOM   1170 C  CD1   . LEU A 1 171 ? 26.471  24.165  7.580   1.00 45.65  ?  164 LEU A CD1   1 
ATOM   1171 C  CD2   . LEU A 1 171 ? 26.733  25.120  5.282   1.00 50.20  ?  164 LEU A CD2   1 
ATOM   1172 N  N     . ASN A 1 172 ? 23.630  22.053  7.308   1.00 38.62  ?  165 ASN A N     1 
ATOM   1173 C  CA    . ASN A 1 172 ? 22.216  22.367  7.393   1.00 37.34  ?  165 ASN A CA    1 
ATOM   1174 C  C     . ASN A 1 172 ? 22.031  23.789  7.862   1.00 38.90  ?  165 ASN A C     1 
ATOM   1175 O  O     . ASN A 1 172 ? 22.623  24.188  8.870   1.00 39.40  ?  165 ASN A O     1 
ATOM   1176 C  CB    . ASN A 1 172 ? 21.419  21.558  8.419   1.00 34.64  ?  165 ASN A CB    1 
ATOM   1177 C  CG    . ASN A 1 172 ? 21.206  20.124  8.003   1.00 33.07  ?  165 ASN A CG    1 
ATOM   1178 O  OD1   . ASN A 1 172 ? 21.788  19.692  7.013   1.00 34.01  ?  165 ASN A OD1   1 
ATOM   1179 N  ND2   . ASN A 1 172 ? 20.426  19.379  8.788   1.00 31.07  ?  165 ASN A ND2   1 
ATOM   1180 N  N     . THR A 1 173 ? 21.259  24.547  7.086   1.00 40.04  ?  166 THR A N     1 
ATOM   1181 C  CA    . THR A 1 173 ? 21.020  25.950  7.346   1.00 42.14  ?  166 THR A CA    1 
ATOM   1182 C  C     . THR A 1 173 ? 19.527  26.246  7.388   1.00 41.49  ?  166 THR A C     1 
ATOM   1183 O  O     . THR A 1 173 ? 18.794  25.917  6.447   1.00 41.16  ?  166 THR A O     1 
ATOM   1184 C  CB    . THR A 1 173 ? 21.697  26.810  6.270   1.00 45.44  ?  166 THR A CB    1 
ATOM   1185 O  OG1   . THR A 1 173 ? 23.106  26.613  6.346   1.00 46.54  ?  166 THR A OG1   1 
ATOM   1186 C  CG2   . THR A 1 173 ? 21.381  28.280  6.399   1.00 48.14  ?  166 THR A CG2   1 
ATOM   1187 N  N     . VAL A 1 174 ? 19.088  26.928  8.443   1.00 41.81  ?  167 VAL A N     1 
ATOM   1188 C  CA    . VAL A 1 174 ? 17.731  27.429  8.542   1.00 42.09  ?  167 VAL A CA    1 
ATOM   1189 C  C     . VAL A 1 174 ? 17.675  28.883  8.071   1.00 45.60  ?  167 VAL A C     1 
ATOM   1190 O  O     . VAL A 1 174 ? 18.178  29.771  8.768   1.00 47.52  ?  167 VAL A O     1 
ATOM   1191 C  CB    . VAL A 1 174 ? 17.143  27.319  9.957   1.00 40.91  ?  167 VAL A CB    1 
ATOM   1192 C  CG1   . VAL A 1 174 ? 15.740  27.869  10.020  1.00 41.77  ?  167 VAL A CG1   1 
ATOM   1193 C  CG2   . VAL A 1 174 ? 17.138  25.875  10.455  1.00 37.80  ?  167 VAL A CG2   1 
ATOM   1194 N  N     . VAL A 1 175 ? 16.910  29.099  6.997   1.00 46.55  ?  168 VAL A N     1 
ATOM   1195 C  CA    . VAL A 1 175 ? 16.679  30.413  6.411   1.00 50.14  ?  168 VAL A CA    1 
ATOM   1196 C  C     . VAL A 1 175 ? 15.506  31.102  7.117   1.00 51.10  ?  168 VAL A C     1 
ATOM   1197 O  O     . VAL A 1 175 ? 14.377  30.617  7.129   1.00 49.74  ?  168 VAL A O     1 
ATOM   1198 C  CB    . VAL A 1 175 ? 16.474  30.301  4.886   1.00 51.13  ?  168 VAL A CB    1 
ATOM   1199 C  CG1   . VAL A 1 175 ? 16.401  31.678  4.230   1.00 55.34  ?  168 VAL A CG1   1 
ATOM   1200 C  CG2   . VAL A 1 175 ? 17.545  29.464  4.211   1.00 50.22  ?  168 VAL A CG2   1 
ATOM   1201 N  N     . ASN A 1 176 ? 15.780  32.248  7.748   1.00 53.85  ?  169 ASN A N     1 
ATOM   1202 C  CA    . ASN A 1 176 ? 14.853  32.897  8.660   1.00 55.09  ?  169 ASN A CA    1 
ATOM   1203 C  C     . ASN A 1 176 ? 14.998  34.415  8.517   1.00 59.72  ?  169 ASN A C     1 
ATOM   1204 O  O     . ASN A 1 176 ? 15.791  34.876  7.695   1.00 61.73  ?  169 ASN A O     1 
ATOM   1205 C  CB    . ASN A 1 176 ? 15.079  32.409  10.099  1.00 53.09  ?  169 ASN A CB    1 
ATOM   1206 C  CG    . ASN A 1 176 ? 16.454  32.753  10.638  1.00 54.05  ?  169 ASN A CG    1 
ATOM   1207 O  OD1   . ASN A 1 176 ? 16.702  33.884  11.033  1.00 57.35  ?  169 ASN A OD1   1 
ATOM   1208 N  ND2   . ASN A 1 176 ? 17.371  31.798  10.659  1.00 51.60  ?  169 ASN A ND2   1 
ATOM   1209 N  N     . LYS A 1 177 ? 14.206  35.163  9.294   1.00 61.74  ?  170 LYS A N     1 
ATOM   1210 C  CA    . LYS A 1 177 ? 14.214  36.625  9.256   1.00 66.61  ?  170 LYS A CA    1 
ATOM   1211 C  C     . LYS A 1 177 ? 15.619  37.208  9.409   1.00 68.62  ?  170 LYS A C     1 
ATOM   1212 O  O     . LYS A 1 177 ? 15.960  38.192  8.758   1.00 72.49  ?  170 LYS A O     1 
ATOM   1213 C  CB    . LYS A 1 177 ? 13.362  37.202  10.387  1.00 68.37  ?  170 LYS A CB    1 
ATOM   1214 C  CG    . LYS A 1 177 ? 11.888  37.413  10.087  1.00 69.64  ?  170 LYS A CG    1 
ATOM   1215 C  CD    . LYS A 1 177 ? 11.568  38.799  9.549   1.00 74.95  ?  170 LYS A CD    1 
ATOM   1216 C  CE    . LYS A 1 177 ? 11.920  38.979  8.086   1.00 76.04  ?  170 LYS A CE    1 
ATOM   1217 N  NZ    . LYS A 1 177 ? 11.483  40.298  7.567   1.00 81.51  ?  170 LYS A NZ    1 
ATOM   1218 N  N     . PHE A 1 178 ? 16.428  36.629  10.295  1.00 66.41  ?  171 PHE A N     1 
ATOM   1219 C  CA    . PHE A 1 178 ? 17.725  37.199  10.641  1.00 68.66  ?  171 PHE A CA    1 
ATOM   1220 C  C     . PHE A 1 178 ? 18.833  36.933  9.614   1.00 68.66  ?  171 PHE A C     1 
ATOM   1221 O  O     . PHE A 1 178 ? 19.865  37.584  9.700   1.00 71.56  ?  171 PHE A O     1 
ATOM   1222 C  CB    . PHE A 1 178 ? 18.160  36.699  12.020  1.00 66.74  ?  171 PHE A CB    1 
ATOM   1223 C  CG    . PHE A 1 178 ? 17.200  37.024  13.138  1.00 67.43  ?  171 PHE A CG    1 
ATOM   1224 C  CD1   . PHE A 1 178 ? 16.477  38.212  13.141  1.00 71.55  ?  171 PHE A CD1   1 
ATOM   1225 C  CD2   . PHE A 1 178 ? 17.035  36.159  14.203  1.00 64.43  ?  171 PHE A CD2   1 
ATOM   1226 C  CE1   . PHE A 1 178 ? 15.611  38.520  14.176  1.00 72.68  ?  171 PHE A CE1   1 
ATOM   1227 C  CE2   . PHE A 1 178 ? 16.161  36.467  15.235  1.00 65.52  ?  171 PHE A CE2   1 
ATOM   1228 C  CZ    . PHE A 1 178 ? 15.453  37.644  15.221  1.00 69.66  ?  171 PHE A CZ    1 
ATOM   1229 N  N     . ASN A 1 179 ? 18.676  36.011  8.647   1.00 65.94  ?  172 ASN A N     1 
ATOM   1230 C  CA    . ASN A 1 179 ? 19.811  35.678  7.788   1.00 66.11  ?  172 ASN A CA    1 
ATOM   1231 C  C     . ASN A 1 179 ? 19.438  35.588  6.311   1.00 66.69  ?  172 ASN A C     1 
ATOM   1232 O  O     . ASN A 1 179 ? 20.245  35.150  5.485   1.00 66.66  ?  172 ASN A O     1 
ATOM   1233 C  CB    . ASN A 1 179 ? 20.476  34.361  8.206   1.00 62.12  ?  172 ASN A CB    1 
ATOM   1234 C  CG    . ASN A 1 179 ? 19.567  33.167  7.995   1.00 57.98  ?  172 ASN A CG    1 
ATOM   1235 O  OD1   . ASN A 1 179 ? 18.401  33.323  7.642   1.00 57.96  ?  172 ASN A OD1   1 
ATOM   1236 N  ND2   . ASN A 1 179 ? 20.101  31.972  8.183   1.00 54.83  ?  172 ASN A ND2   1 
ATOM   1237 N  N     . HIS A 1 180 ? 18.228  35.995  5.952   1.00 67.56  ?  173 HIS A N     1 
ATOM   1238 C  CA    . HIS A 1 180 ? 17.735  35.682  4.621   1.00 67.50  ?  173 HIS A CA    1 
ATOM   1239 C  C     . HIS A 1 180 ? 18.427  36.544  3.551   1.00 71.92  ?  173 HIS A C     1 
ATOM   1240 O  O     . HIS A 1 180 ? 18.347  36.223  2.368   1.00 72.20  ?  173 HIS A O     1 
ATOM   1241 C  CB    . HIS A 1 180 ? 16.200  35.720  4.594   1.00 67.00  ?  173 HIS A CB    1 
ATOM   1242 C  CG    . HIS A 1 180 ? 15.614  37.083  4.559   1.00 71.47  ?  173 HIS A CG    1 
ATOM   1243 N  ND1   . HIS A 1 180 ? 15.361  37.837  5.684   1.00 73.08  ?  173 HIS A ND1   1 
ATOM   1244 C  CD2   . HIS A 1 180 ? 15.197  37.813  3.507   1.00 74.99  ?  173 HIS A CD2   1 
ATOM   1245 C  CE1   . HIS A 1 180 ? 14.839  39.003  5.310   1.00 77.59  ?  173 HIS A CE1   1 
ATOM   1246 N  NE2   . HIS A 1 180 ? 14.724  38.999  3.999   1.00 78.74  ?  173 HIS A NE2   1 
ATOM   1247 N  N     . LEU A 1 181 ? 19.136  37.607  3.957   1.00 75.65  ?  174 LEU A N     1 
ATOM   1248 C  CA    . LEU A 1 181 ? 19.815  38.484  3.007   1.00 80.45  ?  174 LEU A CA    1 
ATOM   1249 C  C     . LEU A 1 181 ? 21.307  38.156  2.905   1.00 80.81  ?  174 LEU A C     1 
ATOM   1250 O  O     . LEU A 1 181 ? 22.023  38.672  2.050   1.00 84.63  ?  174 LEU A O     1 
ATOM   1251 C  CB    . LEU A 1 181 ? 19.594  39.935  3.445   1.00 85.22  ?  174 LEU A CB    1 
ATOM   1252 C  CG    . LEU A 1 181 ? 18.168  40.466  3.291   1.00 86.44  ?  174 LEU A CG    1 
ATOM   1253 C  CD1   . LEU A 1 181 ? 18.053  41.880  3.848   1.00 91.49  ?  174 LEU A CD1   1 
ATOM   1254 C  CD2   . LEU A 1 181 ? 17.722  40.442  1.837   1.00 87.83  ?  174 LEU A CD2   1 
ATOM   1255 N  N     . GLU A 1 182 ? 21.792  37.258  3.760   1.00 77.09  ?  175 GLU A N     1 
ATOM   1256 C  CA    . GLU A 1 182 ? 23.211  36.964  3.815   1.00 77.71  ?  175 GLU A CA    1 
ATOM   1257 C  C     . GLU A 1 182 ? 23.682  36.276  2.535   1.00 77.65  ?  175 GLU A C     1 
ATOM   1258 O  O     . GLU A 1 182 ? 22.915  35.550  1.913   1.00 75.09  ?  175 GLU A O     1 
ATOM   1259 C  CB    . GLU A 1 182 ? 23.446  36.077  5.034   1.00 73.59  ?  175 GLU A CB    1 
ATOM   1260 C  CG    . GLU A 1 182 ? 24.896  35.700  5.251   1.00 74.13  ?  175 GLU A CG    1 
ATOM   1261 C  CD    . GLU A 1 182 ? 25.152  35.009  6.581   1.00 70.89  ?  175 GLU A CD    1 
ATOM   1262 O  OE1   . GLU A 1 182 ? 24.296  35.126  7.479   1.00 69.23  ?  175 GLU A OE1   1 
ATOM   1263 O  OE2   . GLU A 1 182 ? 26.197  34.350  6.698   1.00 70.33  ?  175 GLU A OE2   1 
ATOM   1264 N  N     . ASP A 1 183 ? 24.963  36.492  2.184   1.00 80.78  ?  176 ASP A N     1 
ATOM   1265 C  CA    . ASP A 1 183 ? 25.654  35.779  1.118   1.00 81.14  ?  176 ASP A CA    1 
ATOM   1266 C  C     . ASP A 1 183 ? 26.751  34.884  1.698   1.00 79.29  ?  176 ASP A C     1 
ATOM   1267 O  O     . ASP A 1 183 ? 27.745  35.363  2.251   1.00 81.85  ?  176 ASP A O     1 
ATOM   1268 C  CB    . ASP A 1 183 ? 26.295  36.742  0.113   1.00 87.13  ?  176 ASP A CB    1 
ATOM   1269 C  CG    . ASP A 1 183 ? 26.974  36.019  -1.036  1.00 88.02  ?  176 ASP A CG    1 
ATOM   1270 O  OD1   . ASP A 1 183 ? 28.072  35.451  -0.818  1.00 87.95  ?  176 ASP A OD1   1 
ATOM   1271 O  OD2   . ASP A 1 183 ? 26.375  35.982  -2.132  1.00 88.83  ?  176 ASP A OD2   1 
ATOM   1272 N  N     . MET A 1 184 ? 26.622  33.573  1.467   1.00 75.40  ?  177 MET A N     1 
ATOM   1273 C  CA    . MET A 1 184 ? 27.410  32.586  2.179   1.00 72.90  ?  177 MET A CA    1 
ATOM   1274 C  C     . MET A 1 184 ? 28.315  31.848  1.199   1.00 74.19  ?  177 MET A C     1 
ATOM   1275 O  O     . MET A 1 184 ? 28.931  30.848  1.548   1.00 72.25  ?  177 MET A O     1 
ATOM   1276 C  CB    . MET A 1 184 ? 26.454  31.603  2.870   1.00 67.41  ?  177 MET A CB    1 
ATOM   1277 C  CG    . MET A 1 184 ? 25.516  32.271  3.832   1.00 66.36  ?  177 MET A CG    1 
ATOM   1278 S  SD    . MET A 1 184 ? 24.567  30.986  4.745   1.00 60.30  ?  177 MET A SD    1 
ATOM   1279 C  CE    . MET A 1 184 ? 23.242  31.961  5.421   1.00 60.37  ?  177 MET A CE    1 
ATOM   1280 N  N     . ASN A 1 185 ? 28.430  32.392  -0.031  1.00 78.05  ?  178 ASN A N     1 
ATOM   1281 C  CA    . ASN A 1 185 ? 29.039  31.680  -1.140  1.00 79.47  ?  178 ASN A CA    1 
ATOM   1282 C  C     . ASN A 1 185 ? 30.514  31.412  -0.861  1.00 81.62  ?  178 ASN A C     1 
ATOM   1283 O  O     . ASN A 1 185 ? 31.011  30.319  -1.119  1.00 80.52  ?  178 ASN A O     1 
ATOM   1284 C  CB    . ASN A 1 185 ? 28.820  32.429  -2.463  1.00 83.69  ?  178 ASN A CB    1 
ATOM   1285 C  CG    . ASN A 1 185 ? 27.490  32.118  -3.117  1.00 81.36  ?  178 ASN A CG    1 
ATOM   1286 O  OD1   . ASN A 1 185 ? 27.260  30.997  -3.565  1.00 78.86  ?  178 ASN A OD1   1 
ATOM   1287 N  ND2   . ASN A 1 185 ? 26.629  33.115  -3.220  1.00 82.66  ?  178 ASN A ND2   1 
ATOM   1288 N  N     . ASP A 1 186 ? 31.231  32.402  -0.331  1.00 85.06  ?  179 ASP A N     1 
ATOM   1289 C  CA    . ASP A 1 186 ? 32.672  32.261  -0.189  1.00 88.12  ?  179 ASP A CA    1 
ATOM   1290 C  C     . ASP A 1 186 ? 32.965  31.156  0.833   1.00 84.01  ?  179 ASP A C     1 
ATOM   1291 O  O     . ASP A 1 186 ? 33.829  30.311  0.609   1.00 84.63  ?  179 ASP A O     1 
ATOM   1292 C  CB    . ASP A 1 186 ? 33.321  33.616  0.116   1.00 93.21  ?  179 ASP A CB    1 
ATOM   1293 C  CG    . ASP A 1 186 ? 33.214  34.631  -1.018  1.00 98.21  ?  179 ASP A CG    1 
ATOM   1294 O  OD1   . ASP A 1 186 ? 32.889  34.242  -2.164  1.00 98.48  ?  179 ASP A OD1   1 
ATOM   1295 O  OD2   . ASP A 1 186 ? 33.414  35.815  -0.736  1.00 102.00 ?  179 ASP A OD2   1 
ATOM   1296 N  N     . HIS A 1 187 ? 32.201  31.140  1.932   1.00 80.04  ?  180 HIS A N     1 
ATOM   1297 C  CA    . HIS A 1 187 ? 32.280  30.087  2.940   1.00 75.91  ?  180 HIS A CA    1 
ATOM   1298 C  C     . HIS A 1 187 ? 31.977  28.709  2.347   1.00 72.80  ?  180 HIS A C     1 
ATOM   1299 O  O     . HIS A 1 187 ? 32.749  27.764  2.552   1.00 72.35  ?  180 HIS A O     1 
ATOM   1300 C  CB    . HIS A 1 187 ? 31.389  30.446  4.134   1.00 72.83  ?  180 HIS A CB    1 
ATOM   1301 C  CG    . HIS A 1 187 ? 31.986  31.509  5.003   1.00 75.88  ?  180 HIS A CG    1 
ATOM   1302 N  ND1   . HIS A 1 187 ? 33.195  31.357  5.648   1.00 77.69  ?  180 HIS A ND1   1 
ATOM   1303 C  CD2   . HIS A 1 187 ? 31.532  32.720  5.336   1.00 77.72  ?  180 HIS A CD2   1 
ATOM   1304 C  CE1   . HIS A 1 187 ? 33.456  32.461  6.335   1.00 80.56  ?  180 HIS A CE1   1 
ATOM   1305 N  NE2   . HIS A 1 187 ? 32.453  33.299  6.168   1.00 80.63  ?  180 HIS A NE2   1 
ATOM   1306 N  N     . LEU A 1 188 ? 30.861  28.605  1.606   1.00 71.06  ?  181 LEU A N     1 
ATOM   1307 C  CA    . LEU A 1 188 ? 30.432  27.350  1.001   1.00 68.35  ?  181 LEU A CA    1 
ATOM   1308 C  C     . LEU A 1 188 ? 31.485  26.848  0.021   1.00 71.66  ?  181 LEU A C     1 
ATOM   1309 O  O     . LEU A 1 188 ? 31.715  25.647  -0.086  1.00 70.13  ?  181 LEU A O     1 
ATOM   1310 C  CB    . LEU A 1 188 ? 29.058  27.533  0.338   1.00 66.81  ?  181 LEU A CB    1 
ATOM   1311 C  CG    . LEU A 1 188 ? 27.839  27.101  1.177   1.00 61.94  ?  181 LEU A CG    1 
ATOM   1312 C  CD1   . LEU A 1 188 ? 27.799  25.594  1.345   1.00 58.65  ?  181 LEU A CD1   1 
ATOM   1313 C  CD2   . LEU A 1 188 ? 27.836  27.782  2.532   1.00 61.20  ?  181 LEU A CD2   1 
ATOM   1314 N  N     . ASN A 1 189 ? 32.153  27.782  -0.683  1.00 76.67  ?  182 ASN A N     1 
ATOM   1315 C  CA    . ASN A 1 189 ? 33.219  27.418  -1.602  1.00 80.66  ?  182 ASN A CA    1 
ATOM   1316 C  C     . ASN A 1 189 ? 34.450  26.918  -0.851  1.00 81.59  ?  182 ASN A C     1 
ATOM   1317 O  O     . ASN A 1 189 ? 35.212  26.123  -1.392  1.00 83.44  ?  182 ASN A O     1 
ATOM   1318 C  CB    . ASN A 1 189 ? 33.587  28.603  -2.502  1.00 86.21  ?  182 ASN A CB    1 
ATOM   1319 C  CG    . ASN A 1 189 ? 32.510  28.922  -3.516  1.00 86.20  ?  182 ASN A CG    1 
ATOM   1320 O  OD1   . ASN A 1 189 ? 31.738  28.050  -3.922  1.00 83.12  ?  182 ASN A OD1   1 
ATOM   1321 N  ND2   . ASN A 1 189 ? 32.471  30.170  -3.949  1.00 90.07  ?  182 ASN A ND2   1 
ATOM   1322 N  N     . ALA A 1 190 ? 34.673  27.428  0.363   1.00 80.88  ?  183 ALA A N     1 
ATOM   1323 C  CA    . ALA A 1 190 ? 35.778  26.993  1.201   1.00 81.70  ?  183 ALA A CA    1 
ATOM   1324 C  C     . ALA A 1 190 ? 35.459  25.655  1.870   1.00 76.90  ?  183 ALA A C     1 
ATOM   1325 O  O     . ALA A 1 190 ? 36.342  24.799  1.963   1.00 77.90  ?  183 ALA A O     1 
ATOM   1326 C  CB    . ALA A 1 190 ? 36.079  28.060  2.220   1.00 83.05  ?  183 ALA A CB    1 
ATOM   1327 N  N     . LEU A 1 191 ? 34.203  25.487  2.337   1.00 72.12  ?  184 LEU A N     1 
ATOM   1328 C  CA    . LEU A 1 191 ? 33.788  24.311  3.099   1.00 67.64  ?  184 LEU A CA    1 
ATOM   1329 C  C     . LEU A 1 191 ? 33.520  23.105  2.202   1.00 66.50  ?  184 LEU A C     1 
ATOM   1330 O  O     . LEU A 1 191 ? 33.922  21.993  2.541   1.00 65.45  ?  184 LEU A O     1 
ATOM   1331 C  CB    . LEU A 1 191 ? 32.529  24.651  3.907   1.00 63.63  ?  184 LEU A CB    1 
ATOM   1332 C  CG    . LEU A 1 191 ? 32.734  25.638  5.055   1.00 64.27  ?  184 LEU A CG    1 
ATOM   1333 C  CD1   . LEU A 1 191 ? 31.417  26.223  5.532   1.00 61.52  ?  184 LEU A CD1   1 
ATOM   1334 C  CD2   . LEU A 1 191 ? 33.477  25.003  6.211   1.00 63.52  ?  184 LEU A CD2   1 
ATOM   1335 N  N     . GLN A 1 192 ? 32.802  23.311  1.086   1.00 66.85  ?  185 GLN A N     1 
ATOM   1336 C  CA    . GLN A 1 192 ? 32.591  22.273  0.086   1.00 66.67  ?  185 GLN A CA    1 
ATOM   1337 C  C     . GLN A 1 192 ? 31.927  21.052  0.728   1.00 62.17  ?  185 GLN A C     1 
ATOM   1338 O  O     . GLN A 1 192 ? 32.378  19.905  0.586   1.00 62.33  ?  185 GLN A O     1 
ATOM   1339 C  CB    . GLN A 1 192 ? 33.893  21.883  -0.611  1.00 71.11  ?  185 GLN A CB    1 
ATOM   1340 C  CG    . GLN A 1 192 ? 34.558  23.057  -1.312  1.00 76.13  ?  185 GLN A CG    1 
ATOM   1341 C  CD    . GLN A 1 192 ? 35.312  22.582  -2.529  1.00 80.42  ?  185 GLN A CD    1 
ATOM   1342 O  OE1   . GLN A 1 192 ? 36.205  21.743  -2.429  1.00 81.87  ?  185 GLN A OE1   1 
ATOM   1343 N  NE2   . GLN A 1 192 ? 34.938  23.102  -3.688  1.00 82.72  ?  185 GLN A NE2   1 
ATOM   1344 N  N     . PRO A 1 193 ? 30.781  21.250  1.406   1.00 58.38  ?  186 PRO A N     1 
ATOM   1345 C  CA    . PRO A 1 193 ? 29.970  20.109  1.843   1.00 54.45  ?  186 PRO A CA    1 
ATOM   1346 C  C     . PRO A 1 193 ? 29.390  19.449  0.602   1.00 54.67  ?  186 PRO A C     1 
ATOM   1347 O  O     . PRO A 1 193 ? 29.119  20.141  -0.375  1.00 56.58  ?  186 PRO A O     1 
ATOM   1348 C  CB    . PRO A 1 193 ? 28.895  20.780  2.696   1.00 51.49  ?  186 PRO A CB    1 
ATOM   1349 C  CG    . PRO A 1 193 ? 28.730  22.133  2.078   1.00 53.82  ?  186 PRO A CG    1 
ATOM   1350 C  CD    . PRO A 1 193 ? 30.137  22.539  1.667   1.00 58.12  ?  186 PRO A CD    1 
ATOM   1351 N  N     . PHE A 1 194 ? 29.171  18.129  0.647   1.00 52.97  ?  187 PHE A N     1 
ATOM   1352 C  CA    . PHE A 1 194 ? 28.585  17.414  -0.481  1.00 53.30  ?  187 PHE A CA    1 
ATOM   1353 C  C     . PHE A 1 194 ? 27.085  17.716  -0.586  1.00 50.69  ?  187 PHE A C     1 
ATOM   1354 O  O     . PHE A 1 194 ? 26.492  17.466  -1.630  1.00 51.43  ?  187 PHE A O     1 
ATOM   1355 C  CB    . PHE A 1 194 ? 28.876  15.912  -0.410  1.00 52.95  ?  187 PHE A CB    1 
ATOM   1356 C  CG    . PHE A 1 194 ? 27.870  15.097  0.376   1.00 49.07  ?  187 PHE A CG    1 
ATOM   1357 C  CD1   . PHE A 1 194 ? 27.846  15.148  1.759   1.00 46.63  ?  187 PHE A CD1   1 
ATOM   1358 C  CD2   . PHE A 1 194 ? 26.861  14.400  -0.275  1.00 48.12  ?  187 PHE A CD2   1 
ATOM   1359 C  CE1   . PHE A 1 194 ? 26.905  14.431  2.481   1.00 43.48  ?  187 PHE A CE1   1 
ATOM   1360 C  CE2   . PHE A 1 194 ? 25.894  13.703  0.439   1.00 44.96  ?  187 PHE A CE2   1 
ATOM   1361 C  CZ    . PHE A 1 194 ? 25.928  13.710  1.819   1.00 42.69  ?  187 PHE A CZ    1 
ATOM   1362 N  N     . ARG A 1 195 ? 26.495  18.301  0.473   1.00 48.09  ?  188 ARG A N     1 
ATOM   1363 C  CA    . ARG A 1 195 ? 25.053  18.453  0.619   1.00 45.51  ?  188 ARG A CA    1 
ATOM   1364 C  C     . ARG A 1 195 ? 24.831  19.613  1.577   1.00 44.62  ?  188 ARG A C     1 
ATOM   1365 O  O     . ARG A 1 195 ? 25.372  19.626  2.685   1.00 43.79  ?  188 ARG A O     1 
ATOM   1366 C  CB    . ARG A 1 195 ? 24.432  17.139  1.123   1.00 42.75  ?  188 ARG A CB    1 
ATOM   1367 C  CG    . ARG A 1 195 ? 22.906  17.116  1.209   1.00 40.46  ?  188 ARG A CG    1 
ATOM   1368 C  CD    . ARG A 1 195 ? 22.391  15.684  1.396   1.00 38.77  ?  188 ARG A CD    1 
ATOM   1369 N  NE    . ARG A 1 195 ? 20.942  15.510  1.405   1.00 37.07  ?  188 ARG A NE    1 
ATOM   1370 C  CZ    . ARG A 1 195 ? 20.179  15.400  0.323   1.00 37.99  ?  188 ARG A CZ    1 
ATOM   1371 N  NH1   . ARG A 1 195 ? 20.726  15.483  -0.883  1.00 40.62  ?  188 ARG A NH1   1 
ATOM   1372 N  NH2   . ARG A 1 195 ? 18.885  15.138  0.447   1.00 36.59  ?  188 ARG A NH2   1 
ATOM   1373 N  N     . TRP A 1 196 ? 24.062  20.600  1.137   1.00 45.20  ?  189 TRP A N     1 
ATOM   1374 C  CA    . TRP A 1 196 ? 23.793  21.802  1.902   1.00 45.07  ?  189 TRP A CA    1 
ATOM   1375 C  C     . TRP A 1 196 ? 22.288  21.995  1.963   1.00 43.27  ?  189 TRP A C     1 
ATOM   1376 O  O     . TRP A 1 196 ? 21.670  22.477  1.024   1.00 44.62  ?  189 TRP A O     1 
ATOM   1377 C  CB    . TRP A 1 196 ? 24.497  23.033  1.314   1.00 48.72  ?  189 TRP A CB    1 
ATOM   1378 C  CG    . TRP A 1 196 ? 24.214  24.319  2.037   1.00 49.18  ?  189 TRP A CG    1 
ATOM   1379 C  CD1   . TRP A 1 196 ? 24.001  24.460  3.375   1.00 47.21  ?  189 TRP A CD1   1 
ATOM   1380 C  CD2   . TRP A 1 196 ? 24.159  25.650  1.482   1.00 52.27  ?  189 TRP A CD2   1 
ATOM   1381 N  NE1   . TRP A 1 196 ? 23.773  25.766  3.692   1.00 48.79  ?  189 TRP A NE1   1 
ATOM   1382 C  CE2   . TRP A 1 196 ? 23.872  26.523  2.552   1.00 51.93  ?  189 TRP A CE2   1 
ATOM   1383 C  CE3   . TRP A 1 196 ? 24.320  26.187  0.195   1.00 55.61  ?  189 TRP A CE3   1 
ATOM   1384 C  CZ2   . TRP A 1 196 ? 23.745  27.899  2.377   1.00 54.84  ?  189 TRP A CZ2   1 
ATOM   1385 C  CZ3   . TRP A 1 196 ? 24.192  27.554  0.028   1.00 58.44  ?  189 TRP A CZ3   1 
ATOM   1386 C  CH2   . TRP A 1 196 ? 23.900  28.389  1.097   1.00 58.07  ?  189 TRP A CH2   1 
ATOM   1387 N  N     . LYS A 1 197 ? 21.677  21.589  3.080   1.00 40.48  ?  190 LYS A N     1 
ATOM   1388 C  CA    . LYS A 1 197 ? 20.236  21.697  3.199   1.00 39.04  ?  190 LYS A CA    1 
ATOM   1389 C  C     . LYS A 1 197 ? 19.897  23.119  3.604   1.00 40.21  ?  190 LYS A C     1 
ATOM   1390 O  O     . LYS A 1 197 ? 20.398  23.649  4.600   1.00 40.27  ?  190 LYS A O     1 
ATOM   1391 C  CB    . LYS A 1 197 ? 19.628  20.751  4.244   1.00 36.11  ?  190 LYS A CB    1 
ATOM   1392 C  CG    . LYS A 1 197 ? 19.969  19.275  4.154   1.00 34.94  ?  190 LYS A CG    1 
ATOM   1393 C  CD    . LYS A 1 197 ? 19.451  18.445  2.975   1.00 35.27  ?  190 LYS A CD    1 
ATOM   1394 C  CE    . LYS A 1 197 ? 17.965  18.196  2.886   1.00 34.17  ?  190 LYS A CE    1 
ATOM   1395 N  NZ    . LYS A 1 197 ? 17.378  17.212  3.841   1.00 31.99  ?  190 LYS A NZ    1 
ATOM   1396 N  N     . CYS A 1 198 ? 19.038  23.747  2.812   1.00 41.49  ?  191 CYS A N     1 
ATOM   1397 C  CA    . CYS A 1 198 ? 18.530  25.067  3.132   1.00 42.92  ?  191 CYS A CA    1 
ATOM   1398 C  C     . CYS A 1 198 ? 17.033  24.970  3.446   1.00 41.55  ?  191 CYS A C     1 
ATOM   1399 O  O     . CYS A 1 198 ? 16.237  24.776  2.529   1.00 41.99  ?  191 CYS A O     1 
ATOM   1400 C  CB    . CYS A 1 198 ? 18.875  26.035  2.007   1.00 46.39  ?  191 CYS A CB    1 
ATOM   1401 S  SG    . CYS A 1 198 ? 20.609  26.581  2.018   1.00 48.91  ?  191 CYS A SG    1 
ATOM   1402 N  N     . PHE A 1 199 ? 16.665  25.039  4.756   1.00 40.10  ?  192 PHE A N     1 
ATOM   1403 C  CA    . PHE A 1 199 ? 15.289  24.935  5.210   1.00 39.11  ?  192 PHE A CA    1 
ATOM   1404 C  C     . PHE A 1 199 ? 14.660  26.309  5.428   1.00 41.37  ?  192 PHE A C     1 
ATOM   1405 O  O     . PHE A 1 199 ? 15.159  27.135  6.187   1.00 42.43  ?  192 PHE A O     1 
ATOM   1406 C  CB    . PHE A 1 199 ? 15.153  24.232  6.567   1.00 36.74  ?  192 PHE A CB    1 
ATOM   1407 C  CG    . PHE A 1 199 ? 15.943  22.960  6.748   1.00 34.74  ?  192 PHE A CG    1 
ATOM   1408 C  CD1   . PHE A 1 199 ? 15.698  21.845  5.956   1.00 33.79  ?  192 PHE A CD1   1 
ATOM   1409 C  CD2   . PHE A 1 199 ? 16.918  22.877  7.721   1.00 34.16  ?  192 PHE A CD2   1 
ATOM   1410 C  CE1   . PHE A 1 199 ? 16.437  20.686  6.133   1.00 32.40  ?  192 PHE A CE1   1 
ATOM   1411 C  CE2   . PHE A 1 199 ? 17.664  21.717  7.885   1.00 32.72  ?  192 PHE A CE2   1 
ATOM   1412 C  CZ    . PHE A 1 199 ? 17.444  20.638  7.072   1.00 31.91  ?  192 PHE A CZ    1 
ATOM   1413 N  N     . GLN A 1 200 ? 13.524  26.553  4.780   1.00 42.42  ?  193 GLN A N     1 
ATOM   1414 C  CA    . GLN A 1 200 ? 12.687  27.669  5.190   1.00 44.44  ?  193 GLN A CA    1 
ATOM   1415 C  C     . GLN A 1 200 ? 12.178  27.401  6.603   1.00 42.91  ?  193 GLN A C     1 
ATOM   1416 O  O     . GLN A 1 200 ? 11.622  26.330  6.858   1.00 40.76  ?  193 GLN A O     1 
ATOM   1417 C  CB    . GLN A 1 200 ? 11.507  27.808  4.236   1.00 45.88  ?  193 GLN A CB    1 
ATOM   1418 C  CG    . GLN A 1 200 ? 10.657  29.042  4.501   1.00 48.73  ?  193 GLN A CG    1 
ATOM   1419 C  CD    . GLN A 1 200 ? 9.424   29.089  3.626   1.00 50.26  ?  193 GLN A CD    1 
ATOM   1420 O  OE1   . GLN A 1 200 ? 9.204   28.244  2.755   1.00 49.34  ?  193 GLN A OE1   1 
ATOM   1421 N  NE2   . GLN A 1 200 ? 8.590   30.094  3.875   1.00 52.98  ?  193 GLN A NE2   1 
ATOM   1422 N  N     . VAL A 1 201 ? 12.392  28.338  7.537   1.00 44.30  ?  194 VAL A N     1 
ATOM   1423 C  CA    . VAL A 1 201 ? 11.982  28.084  8.918   1.00 43.17  ?  194 VAL A CA    1 
ATOM   1424 C  C     . VAL A 1 201 ? 10.515  27.629  8.924   1.00 42.87  ?  194 VAL A C     1 
ATOM   1425 O  O     . VAL A 1 201 ? 9.645   28.230  8.271   1.00 44.99  ?  194 VAL A O     1 
ATOM   1426 C  CB    . VAL A 1 201 ? 12.254  29.288  9.845   1.00 45.50  ?  194 VAL A CB    1 
ATOM   1427 C  CG1   . VAL A 1 201 ? 11.522  30.535  9.400   1.00 49.02  ?  194 VAL A CG1   1 
ATOM   1428 C  CG2   . VAL A 1 201 ? 11.920  28.968  11.291  1.00 44.53  ?  194 VAL A CG2   1 
ATOM   1429 N  N     . LEU A 1 202 ? 10.259  26.502  9.605   1.00 40.47  ?  195 LEU A N     1 
ATOM   1430 C  CA    . LEU A 1 202 ? 8.971   25.827  9.573   1.00 40.09  ?  195 LEU A CA    1 
ATOM   1431 C  C     . LEU A 1 202 ? 8.284   25.924  10.937  1.00 40.59  ?  195 LEU A C     1 
ATOM   1432 O  O     . LEU A 1 202 ? 8.938   25.784  11.989  1.00 39.67  ?  195 LEU A O     1 
ATOM   1433 C  CB    . LEU A 1 202 ? 9.194   24.361  9.175   1.00 37.42  ?  195 LEU A CB    1 
ATOM   1434 C  CG    . LEU A 1 202 ? 7.944   23.478  9.099   1.00 37.09  ?  195 LEU A CG    1 
ATOM   1435 C  CD1   . LEU A 1 202 ? 7.115   23.796  7.870   1.00 38.86  ?  195 LEU A CD1   1 
ATOM   1436 C  CD2   . LEU A 1 202 ? 8.348   22.016  9.090   1.00 34.61  ?  195 LEU A CD2   1 
ATOM   1437 N  N     . ILE A 1 203 ? 6.982   26.242  10.910  1.00 42.53  ?  196 ILE A N     1 
ATOM   1438 C  CA    . ILE A 1 203 ? 6.118   26.168  12.090  1.00 43.39  ?  196 ILE A CA    1 
ATOM   1439 C  C     . ILE A 1 203 ? 5.551   24.762  12.245  1.00 41.55  ?  196 ILE A C     1 
ATOM   1440 O  O     . ILE A 1 203 ? 4.944   24.242  11.308  1.00 41.45  ?  196 ILE A O     1 
ATOM   1441 C  CB    . ILE A 1 203 ? 4.951   27.163  11.980  1.00 46.94  ?  196 ILE A CB    1 
ATOM   1442 C  CG1   . ILE A 1 203 ? 5.464   28.570  11.701  1.00 49.29  ?  196 ILE A CG1   1 
ATOM   1443 C  CG2   . ILE A 1 203 ? 4.088   27.080  13.237  1.00 48.26  ?  196 ILE A CG2   1 
ATOM   1444 C  CD1   . ILE A 1 203 ? 6.411   29.080  12.736  1.00 49.37  ?  196 ILE A CD1   1 
ATOM   1445 N  N     . VAL A 1 204 ? 5.699   24.179  13.446  1.00 40.54  ?  197 VAL A N     1 
ATOM   1446 C  CA    . VAL A 1 204 ? 5.151   22.869  13.741  1.00 39.30  ?  197 VAL A CA    1 
ATOM   1447 C  C     . VAL A 1 204 ? 4.190   23.014  14.907  1.00 41.36  ?  197 VAL A C     1 
ATOM   1448 O  O     . VAL A 1 204 ? 4.608   23.372  16.012  1.00 41.76  ?  197 VAL A O     1 
ATOM   1449 C  CB    . VAL A 1 204 ? 6.245   21.841  14.075  1.00 36.45  ?  197 VAL A CB    1 
ATOM   1450 C  CG1   . VAL A 1 204 ? 5.638   20.546  14.596  1.00 35.80  ?  197 VAL A CG1   1 
ATOM   1451 C  CG2   . VAL A 1 204 ? 7.158   21.592  12.883  1.00 34.80  ?  197 VAL A CG2   1 
ATOM   1452 N  N     . THR A 1 205 ? 2.913   22.724  14.638  1.00 42.95  ?  198 THR A N     1 
ATOM   1453 C  CA    . THR A 1 205 ? 1.887   22.770  15.661  1.00 45.39  ?  198 THR A CA    1 
ATOM   1454 C  C     . THR A 1 205 ? 2.307   21.963  16.901  1.00 44.20  ?  198 THR A C     1 
ATOM   1455 O  O     . THR A 1 205 ? 2.740   20.813  16.792  1.00 41.85  ?  198 THR A O     1 
ATOM   1456 C  CB    . THR A 1 205 ? 0.552   22.315  15.060  1.00 47.10  ?  198 THR A CB    1 
ATOM   1457 O  OG1   . THR A 1 205 ? 0.356   23.042  13.844  1.00 48.02  ?  198 THR A OG1   1 
ATOM   1458 C  CG2   . THR A 1 205 ? -0.608  22.545  15.997  1.00 50.49  ?  198 THR A CG2   1 
ATOM   1459 N  N     . GLY A 1 206 ? 2.193   22.585  18.090  1.00 46.17  ?  199 GLY A N     1 
ATOM   1460 C  CA    . GLY A 1 206 ? 2.514   21.937  19.355  1.00 45.73  ?  199 GLY A CA    1 
ATOM   1461 C  C     . GLY A 1 206 ? 3.981   22.033  19.783  1.00 43.58  ?  199 GLY A C     1 
ATOM   1462 O  O     . GLY A 1 206 ? 4.322   21.586  20.874  1.00 43.47  ?  199 GLY A O     1 
ATOM   1463 N  N     . GLU A 1 207 ? 4.847   22.598  18.926  1.00 42.18  ?  200 GLU A N     1 
ATOM   1464 C  CA    . GLU A 1 207 ? 6.276   22.710  19.175  1.00 40.40  ?  200 GLU A CA    1 
ATOM   1465 C  C     . GLU A 1 207 ? 6.739   24.163  19.258  1.00 42.14  ?  200 GLU A C     1 
ATOM   1466 O  O     . GLU A 1 207 ? 7.414   24.530  20.211  1.00 42.72  ?  200 GLU A O     1 
ATOM   1467 C  CB    . GLU A 1 207 ? 7.054   21.994  18.066  1.00 37.50  ?  200 GLU A CB    1 
ATOM   1468 C  CG    . GLU A 1 207 ? 7.029   20.475  18.197  1.00 35.68  ?  200 GLU A CG    1 
ATOM   1469 C  CD    . GLU A 1 207 ? 7.941   19.907  19.278  1.00 34.71  ?  200 GLU A CD    1 
ATOM   1470 O  OE1   . GLU A 1 207 ? 8.574   20.689  20.019  1.00 35.48  ?  200 GLU A OE1   1 
ATOM   1471 O  OE2   . GLU A 1 207 ? 8.072   18.668  19.338  1.00 33.36  ?  200 GLU A OE2   1 
ATOM   1472 N  N     . ASN A 1 208 ? 6.409   24.991  18.257  1.00 43.26  ?  201 ASN A N     1 
ATOM   1473 C  CA    . ASN A 1 208 ? 6.986   26.329  18.155  1.00 44.97  ?  201 ASN A CA    1 
ATOM   1474 C  C     . ASN A 1 208 ? 5.947   27.332  17.635  1.00 48.08  ?  201 ASN A C     1 
ATOM   1475 O  O     . ASN A 1 208 ? 6.336   28.339  17.071  1.00 49.40  ?  201 ASN A O     1 
ATOM   1476 C  CB    . ASN A 1 208 ? 8.264   26.353  17.309  1.00 42.95  ?  201 ASN A CB    1 
ATOM   1477 C  CG    . ASN A 1 208 ? 8.012   26.015  15.849  1.00 41.81  ?  201 ASN A CG    1 
ATOM   1478 O  OD1   . ASN A 1 208 ? 6.920   25.610  15.511  1.00 42.16  ?  201 ASN A OD1   1 
ATOM   1479 N  ND2   . ASN A 1 208 ? 8.989   26.201  14.982  1.00 40.87  ?  201 ASN A ND2   1 
ATOM   1480 N  N     . ASP A 1 209 ? 4.656   27.096  17.898  1.00 49.70  ?  202 ASP A N     1 
ATOM   1481 C  CA    . ASP A 1 209 ? 3.596   27.829  17.210  1.00 52.54  ?  202 ASP A CA    1 
ATOM   1482 C  C     . ASP A 1 209 ? 2.835   28.799  18.122  1.00 56.80  ?  202 ASP A C     1 
ATOM   1483 O  O     . ASP A 1 209 ? 1.890   29.423  17.650  1.00 59.70  ?  202 ASP A O     1 
ATOM   1484 C  CB    . ASP A 1 209 ? 2.546   26.891  16.618  1.00 52.01  ?  202 ASP A CB    1 
ATOM   1485 C  CG    . ASP A 1 209 ? 1.924   25.952  17.633  1.00 52.05  ?  202 ASP A CG    1 
ATOM   1486 O  OD1   . ASP A 1 209 ? 2.588   25.676  18.654  1.00 51.08  ?  202 ASP A OD1   1 
ATOM   1487 O  OD2   . ASP A 1 209 ? 0.799   25.465  17.370  1.00 53.21  ?  202 ASP A OD2   1 
ATOM   1488 N  N     . SER A 1 210 ? 3.185   28.916  19.406  1.00 57.57  ?  203 SER A N     1 
ATOM   1489 C  CA    . SER A 1 210 ? 2.496   29.890  20.257  1.00 62.11  ?  203 SER A CA    1 
ATOM   1490 C  C     . SER A 1 210 ? 3.374   30.339  21.416  1.00 62.89  ?  203 SER A C     1 
ATOM   1491 O  O     . SER A 1 210 ? 4.570   30.053  21.445  1.00 60.08  ?  203 SER A O     1 
ATOM   1492 C  CB    . SER A 1 210 ? 1.182   29.342  20.767  1.00 64.01  ?  203 SER A CB    1 
ATOM   1493 O  OG    . SER A 1 210 ? 1.373   28.425  21.829  1.00 62.71  ?  203 SER A OG    1 
ATOM   1494 N  N     . ASP A 1 211 ? 2.762   31.056  22.376  1.00 67.14  ?  204 ASP A N     1 
ATOM   1495 C  CA    . ASP A 1 211 ? 3.479   31.420  23.586  1.00 68.40  ?  204 ASP A CA    1 
ATOM   1496 C  C     . ASP A 1 211 ? 3.241   30.392  24.684  1.00 67.74  ?  204 ASP A C     1 
ATOM   1497 O  O     . ASP A 1 211 ? 3.774   30.560  25.773  1.00 68.89  ?  204 ASP A O     1 
ATOM   1498 C  CB    . ASP A 1 211 ? 3.116   32.837  24.041  1.00 73.79  ?  204 ASP A CB    1 
ATOM   1499 C  CG    . ASP A 1 211 ? 3.402   33.861  22.961  1.00 74.79  ?  204 ASP A CG    1 
ATOM   1500 O  OD1   . ASP A 1 211 ? 4.579   33.926  22.500  1.00 72.27  ?  204 ASP A OD1   1 
ATOM   1501 O  OD2   . ASP A 1 211 ? 2.443   34.564  22.560  1.00 78.31  ?  204 ASP A OD2   1 
ATOM   1502 N  N     . LYS A 1 212 ? 2.422   29.363  24.424  1.00 66.38  ?  205 LYS A N     1 
ATOM   1503 C  CA    . LYS A 1 212 ? 2.256   28.258  25.357  1.00 65.57  ?  205 LYS A CA    1 
ATOM   1504 C  C     . LYS A 1 212 ? 3.379   27.235  25.162  1.00 60.70  ?  205 LYS A C     1 
ATOM   1505 O  O     . LYS A 1 212 ? 3.671   26.470  26.076  1.00 60.01  ?  205 LYS A O     1 
ATOM   1506 C  CB    . LYS A 1 212 ? 0.901   27.567  25.178  1.00 66.69  ?  205 LYS A CB    1 
ATOM   1507 C  CG    . LYS A 1 212 ? -0.315  28.360  25.646  1.00 72.16  ?  205 LYS A CG    1 
ATOM   1508 C  CD    . LYS A 1 212 ? -0.774  29.449  24.682  1.00 74.28  ?  205 LYS A CD    1 
ATOM   1509 C  CE    . LYS A 1 212 ? -2.052  30.147  25.108  1.00 80.06  ?  205 LYS A CE    1 
ATOM   1510 N  NZ    . LYS A 1 212 ? -3.226  29.243  25.009  1.00 80.87  ?  205 LYS A NZ    1 
ATOM   1511 N  N     . THR A 1 213 ? 4.015   27.236  23.986  1.00 57.73  ?  206 THR A N     1 
ATOM   1512 C  CA    . THR A 1 213 ? 5.071   26.277  23.674  1.00 53.44  ?  206 THR A CA    1 
ATOM   1513 C  C     . THR A 1 213 ? 6.415   26.815  24.156  1.00 53.07  ?  206 THR A C     1 
ATOM   1514 O  O     . THR A 1 213 ? 6.490   27.931  24.649  1.00 56.08  ?  206 THR A O     1 
ATOM   1515 C  CB    . THR A 1 213 ? 5.025   25.948  22.179  1.00 50.94  ?  206 THR A CB    1 
ATOM   1516 O  OG1   . THR A 1 213 ? 5.017   27.180  21.463  1.00 52.64  ?  206 THR A OG1   1 
ATOM   1517 C  CG2   . THR A 1 213 ? 3.812   25.124  21.810  1.00 51.03  ?  206 THR A CG2   1 
ATOM   1518 N  N     . LEU A 1 214 ? 7.484   26.005  24.062  1.00 49.76  ?  207 LEU A N     1 
ATOM   1519 C  CA    . LEU A 1 214 ? 8.781   26.386  24.610  1.00 49.61  ?  207 LEU A CA    1 
ATOM   1520 C  C     . LEU A 1 214 ? 9.477   27.385  23.685  1.00 49.70  ?  207 LEU A C     1 
ATOM   1521 O  O     . LEU A 1 214 ? 10.466  28.030  24.079  1.00 50.64  ?  207 LEU A O     1 
ATOM   1522 C  CB    . LEU A 1 214 ? 9.621   25.117  24.857  1.00 46.51  ?  207 LEU A CB    1 
ATOM   1523 C  CG    . LEU A 1 214 ? 9.116   24.209  25.984  1.00 47.08  ?  207 LEU A CG    1 
ATOM   1524 C  CD1   . LEU A 1 214 ? 9.762   22.828  25.938  1.00 44.01  ?  207 LEU A CD1   1 
ATOM   1525 C  CD2   . LEU A 1 214 ? 9.399   24.834  27.347  1.00 50.03  ?  207 LEU A CD2   1 
ATOM   1526 N  N     . ARG A 1 215 ? 8.953   27.501  22.455  1.00 49.05  ?  208 ARG A N     1 
ATOM   1527 C  CA    . ARG A 1 215 ? 9.409   28.488  21.491  1.00 49.74  ?  208 ARG A CA    1 
ATOM   1528 C  C     . ARG A 1 215 ? 8.212   29.078  20.751  1.00 51.71  ?  208 ARG A C     1 
ATOM   1529 O  O     . ARG A 1 215 ? 7.145   28.475  20.706  1.00 51.57  ?  208 ARG A O     1 
ATOM   1530 C  CB    . ARG A 1 215 ? 10.341  27.827  20.466  1.00 46.36  ?  208 ARG A CB    1 
ATOM   1531 C  CG    . ARG A 1 215 ? 11.562  27.158  21.077  1.00 44.47  ?  208 ARG A CG    1 
ATOM   1532 C  CD    . ARG A 1 215 ? 12.560  28.143  21.614  1.00 46.48  ?  208 ARG A CD    1 
ATOM   1533 N  NE    . ARG A 1 215 ? 13.884  27.548  21.541  1.00 44.40  ?  208 ARG A NE    1 
ATOM   1534 C  CZ    . ARG A 1 215 ? 14.388  26.716  22.433  1.00 43.28  ?  208 ARG A CZ    1 
ATOM   1535 N  NH1   . ARG A 1 215 ? 13.776  26.510  23.579  1.00 44.35  ?  208 ARG A NH1   1 
ATOM   1536 N  NH2   . ARG A 1 215 ? 15.529  26.110  22.188  1.00 41.46  ?  208 ARG A NH2   1 
ATOM   1537 N  N     . ASN A 1 216 ? 8.436   30.253  20.155  1.00 53.81  ?  209 ASN A N     1 
ATOM   1538 C  CA    . ASN A 1 216 ? 7.509   30.870  19.209  1.00 55.68  ?  209 ASN A CA    1 
ATOM   1539 C  C     . ASN A 1 216 ? 8.312   31.360  18.001  1.00 55.14  ?  209 ASN A C     1 
ATOM   1540 O  O     . ASN A 1 216 ? 9.064   32.345  18.075  1.00 57.15  ?  209 ASN A O     1 
ATOM   1541 C  CB    . ASN A 1 216 ? 6.697   32.008  19.843  1.00 60.40  ?  209 ASN A CB    1 
ATOM   1542 C  CG    . ASN A 1 216 ? 5.474   32.371  19.023  1.00 62.44  ?  209 ASN A CG    1 
ATOM   1543 O  OD1   . ASN A 1 216 ? 5.507   32.271  17.799  1.00 61.12  ?  209 ASN A OD1   1 
ATOM   1544 N  ND2   . ASN A 1 216 ? 4.382   32.737  19.678  1.00 65.83  ?  209 ASN A ND2   1 
ATOM   1545 N  N     . ALA A 1 217 ? 8.141   30.676  16.860  1.00 52.79  ?  210 ALA A N     1 
ATOM   1546 C  CA    . ALA A 1 217 ? 8.957   30.951  15.693  1.00 52.11  ?  210 ALA A CA    1 
ATOM   1547 C  C     . ALA A 1 217 ? 8.251   31.916  14.744  1.00 55.06  ?  210 ALA A C     1 
ATOM   1548 O  O     . ALA A 1 217 ? 8.842   32.278  13.737  1.00 55.24  ?  210 ALA A O     1 
ATOM   1549 C  CB    . ALA A 1 217 ? 9.292   29.673  14.972  1.00 48.28  ?  210 ALA A CB    1 
ATOM   1550 N  N     . HIS A 1 218 ? 7.020   32.318  15.077  1.00 57.68  ?  211 HIS A N     1 
ATOM   1551 C  CA    . HIS A 1 218 ? 6.189   33.126  14.185  1.00 60.72  ?  211 HIS A CA    1 
ATOM   1552 C  C     . HIS A 1 218 ? 6.855   34.448  13.808  1.00 63.80  ?  211 HIS A C     1 
ATOM   1553 O  O     . HIS A 1 218 ? 6.689   34.926  12.678  1.00 65.26  ?  211 HIS A O     1 
ATOM   1554 C  CB    . HIS A 1 218 ? 4.786   33.335  14.764  1.00 63.50  ?  211 HIS A CB    1 
ATOM   1555 C  CG    . HIS A 1 218 ? 3.850   32.185  14.619  1.00 61.57  ?  211 HIS A CG    1 
ATOM   1556 N  ND1   . HIS A 1 218 ? 3.344   31.745  13.412  1.00 60.73  ?  211 HIS A ND1   1 
ATOM   1557 C  CD2   . HIS A 1 218 ? 3.283   31.425  15.554  1.00 60.87  ?  211 HIS A CD2   1 
ATOM   1558 C  CE1   . HIS A 1 218 ? 2.503   30.739  13.636  1.00 59.56  ?  211 HIS A CE1   1 
ATOM   1559 N  NE2   . HIS A 1 218 ? 2.458   30.526  14.939  1.00 59.64  ?  211 HIS A NE2   1 
ATOM   1560 N  N     . SER A 1 219 ? 7.659   35.007  14.716  1.00 64.94  ?  212 SER A N     1 
ATOM   1561 C  CA    . SER A 1 219 ? 8.330   36.267  14.439  1.00 68.31  ?  212 SER A CA    1 
ATOM   1562 C  C     . SER A 1 219 ? 9.591   36.073  13.597  1.00 66.31  ?  212 SER A C     1 
ATOM   1563 O  O     . SER A 1 219 ? 10.240  37.057  13.236  1.00 69.14  ?  212 SER A O     1 
ATOM   1564 C  CB    . SER A 1 219 ? 8.601   37.012  15.732  1.00 71.12  ?  212 SER A CB    1 
ATOM   1565 O  OG    . SER A 1 219 ? 9.291   36.202  16.676  1.00 68.14  ?  212 SER A OG    1 
ATOM   1566 N  N     . LEU A 1 220 ? 9.949   34.817  13.245  1.00 61.86  ?  213 LEU A N     1 
ATOM   1567 C  CA    . LEU A 1 220 ? 11.139  34.573  12.451  1.00 60.24  ?  213 LEU A CA    1 
ATOM   1568 C  C     . LEU A 1 220 ? 10.838  34.033  11.056  1.00 58.81  ?  213 LEU A C     1 
ATOM   1569 O  O     . LEU A 1 220 ? 11.784  33.753  10.319  1.00 57.62  ?  213 LEU A O     1 
ATOM   1570 C  CB    . LEU A 1 220 ? 12.039  33.575  13.188  1.00 56.74  ?  213 LEU A CB    1 
ATOM   1571 C  CG    . LEU A 1 220 ? 12.813  34.181  14.352  1.00 58.42  ?  213 LEU A CG    1 
ATOM   1572 C  CD1   . LEU A 1 220 ? 11.927  34.283  15.579  1.00 59.47  ?  213 LEU A CD1   1 
ATOM   1573 C  CD2   . LEU A 1 220 ? 14.063  33.381  14.657  1.00 55.66  ?  213 LEU A CD2   1 
ATOM   1574 N  N     . THR A 1 221 ? 9.560   33.826  10.746  1.00 59.05  ?  214 THR A N     1 
ATOM   1575 C  CA    . THR A 1 221 ? 9.153   33.198  9.499   1.00 57.73  ?  214 THR A CA    1 
ATOM   1576 C  C     . THR A 1 221 ? 9.301   34.203  8.359   1.00 61.01  ?  214 THR A C     1 
ATOM   1577 O  O     . THR A 1 221 ? 9.231   35.401  8.607   1.00 64.75  ?  214 THR A O     1 
ATOM   1578 C  CB    . THR A 1 221 ? 7.717   32.660  9.591   1.00 57.39  ?  214 THR A CB    1 
ATOM   1579 O  OG1   . THR A 1 221 ? 6.831   33.669  10.074  1.00 61.17  ?  214 THR A OG1   1 
ATOM   1580 C  CG2   . THR A 1 221 ? 7.591   31.451  10.495  1.00 54.01  ?  214 THR A CG2   1 
ATOM   1581 N  N     . ILE A 1 222 ? 9.527   33.700  7.134   1.00 59.88  ?  215 ILE A N     1 
ATOM   1582 C  CA    . ILE A 1 222 ? 9.786   34.536  5.972   1.00 62.97  ?  215 ILE A CA    1 
ATOM   1583 C  C     . ILE A 1 222 ? 8.834   34.156  4.848   1.00 63.20  ?  215 ILE A C     1 
ATOM   1584 O  O     . ILE A 1 222 ? 8.305   33.043  4.819   1.00 60.31  ?  215 ILE A O     1 
ATOM   1585 C  CB    . ILE A 1 222 ? 11.234  34.399  5.470   1.00 62.19  ?  215 ILE A CB    1 
ATOM   1586 C  CG1   . ILE A 1 222 ? 11.575  32.928  5.198   1.00 57.89  ?  215 ILE A CG1   1 
ATOM   1587 C  CG2   . ILE A 1 222 ? 12.205  35.077  6.418   1.00 63.33  ?  215 ILE A CG2   1 
ATOM   1588 C  CD1   . ILE A 1 222 ? 12.960  32.718  4.626   1.00 57.46  ?  215 ILE A CD1   1 
ATOM   1589 N  N     . SER A 1 223 ? 8.679   35.092  3.905   1.00 66.98  ?  216 SER A N     1 
ATOM   1590 C  CA    . SER A 1 223 ? 7.865   34.894  2.720   1.00 68.03  ?  216 SER A CA    1 
ATOM   1591 C  C     . SER A 1 223 ? 8.512   33.875  1.787   1.00 65.41  ?  216 SER A C     1 
ATOM   1592 O  O     . SER A 1 223 ? 9.723   33.687  1.798   1.00 64.13  ?  216 SER A O     1 
ATOM   1593 C  CB    . SER A 1 223 ? 7.677   36.212  1.981   1.00 73.18  ?  216 SER A CB    1 
ATOM   1594 O  OG    . SER A 1 223 ? 8.877   36.584  1.305   1.00 74.34  ?  216 SER A OG    1 
ATOM   1595 N  N     . ASP A 1 224 ? 7.671   33.272  0.944   1.00 65.18  ?  217 ASP A N     1 
ATOM   1596 C  CA    . ASP A 1 224 ? 8.110   32.416  -0.140  1.00 63.77  ?  217 ASP A CA    1 
ATOM   1597 C  C     . ASP A 1 224 ? 9.139   33.146  -0.993  1.00 66.39  ?  217 ASP A C     1 
ATOM   1598 O  O     . ASP A 1 224 ? 10.139  32.551  -1.410  1.00 64.87  ?  217 ASP A O     1 
ATOM   1599 C  CB    . ASP A 1 224 ? 6.921   31.971  -0.993  1.00 64.57  ?  217 ASP A CB    1 
ATOM   1600 C  CG    . ASP A 1 224 ? 5.933   31.105  -0.235  1.00 62.16  ?  217 ASP A CG    1 
ATOM   1601 O  OD1   . ASP A 1 224 ? 6.210   29.901  -0.073  1.00 58.68  ?  217 ASP A OD1   1 
ATOM   1602 O  OD2   . ASP A 1 224 ? 4.900   31.653  0.205   1.00 64.14  ?  217 ASP A OD2   1 
ATOM   1603 N  N     . ASP A 1 225 ? 8.888   34.436  -1.255  1.00 70.72  ?  218 ASP A N     1 
ATOM   1604 C  CA    . ASP A 1 225 ? 9.754   35.192  -2.143  1.00 73.99  ?  218 ASP A CA    1 
ATOM   1605 C  C     . ASP A 1 225 ? 11.101  35.463  -1.467  1.00 73.40  ?  218 ASP A C     1 
ATOM   1606 O  O     . ASP A 1 225 ? 12.125  35.454  -2.139  1.00 74.27  ?  218 ASP A O     1 
ATOM   1607 C  CB    . ASP A 1 225 ? 9.005   36.405  -2.699  1.00 79.13  ?  218 ASP A CB    1 
ATOM   1608 C  CG    . ASP A 1 225 ? 7.958   36.010  -3.731  1.00 80.07  ?  218 ASP A CG    1 
ATOM   1609 O  OD1   . ASP A 1 225 ? 7.012   35.265  -3.378  1.00 77.72  ?  218 ASP A OD1   1 
ATOM   1610 O  OD2   . ASP A 1 225 ? 8.104   36.427  -4.890  1.00 83.37  ?  218 ASP A OD2   1 
ATOM   1611 N  N     . GLU A 1 226 ? 11.126  35.668  -0.144  1.00 72.16  ?  219 GLU A N     1 
ATOM   1612 C  CA    . GLU A 1 226 ? 12.393  35.847  0.559   1.00 71.58  ?  219 GLU A CA    1 
ATOM   1613 C  C     . GLU A 1 226 ? 13.224  34.570  0.469   1.00 67.60  ?  219 GLU A C     1 
ATOM   1614 O  O     . GLU A 1 226 ? 14.430  34.634  0.176   1.00 68.33  ?  219 GLU A O     1 
ATOM   1615 C  CB    . GLU A 1 226 ? 12.155  36.323  1.990   1.00 71.43  ?  219 GLU A CB    1 
ATOM   1616 C  CG    . GLU A 1 226 ? 11.707  37.783  2.055   1.00 76.48  ?  219 GLU A CG    1 
ATOM   1617 C  CD    . GLU A 1 226 ? 11.108  38.228  3.378   1.00 76.87  ?  219 GLU A CD    1 
ATOM   1618 O  OE1   . GLU A 1 226 ? 10.344  37.435  3.977   1.00 73.80  ?  219 GLU A OE1   1 
ATOM   1619 O  OE2   . GLU A 1 226 ? 11.378  39.375  3.786   1.00 80.65  ?  219 GLU A OE2   1 
ATOM   1620 N  N     . PHE A 1 227 ? 12.562  33.418  0.688   1.00 63.87  ?  220 PHE A N     1 
ATOM   1621 C  CA    . PHE A 1 227 ? 13.246  32.136  0.679   1.00 60.22  ?  220 PHE A CA    1 
ATOM   1622 C  C     . PHE A 1 227 ? 13.813  31.892  -0.712  1.00 61.57  ?  220 PHE A C     1 
ATOM   1623 O  O     . PHE A 1 227 ? 14.974  31.549  -0.853  1.00 61.10  ?  220 PHE A O     1 
ATOM   1624 C  CB    . PHE A 1 227 ? 12.351  30.974  1.134   1.00 56.58  ?  220 PHE A CB    1 
ATOM   1625 C  CG    . PHE A 1 227 ? 13.050  29.637  1.075   1.00 53.28  ?  220 PHE A CG    1 
ATOM   1626 C  CD1   . PHE A 1 227 ? 13.991  29.290  2.031   1.00 51.28  ?  220 PHE A CD1   1 
ATOM   1627 C  CD2   . PHE A 1 227 ? 12.807  28.734  0.051   1.00 52.58  ?  220 PHE A CD2   1 
ATOM   1628 C  CE1   . PHE A 1 227 ? 14.671  28.088  1.961   1.00 48.73  ?  220 PHE A CE1   1 
ATOM   1629 C  CE2   . PHE A 1 227 ? 13.495  27.530  -0.026  1.00 50.09  ?  220 PHE A CE2   1 
ATOM   1630 C  CZ    . PHE A 1 227 ? 14.411  27.195  0.944   1.00 48.13  ?  220 PHE A CZ    1 
ATOM   1631 N  N     . ASP A 1 228 ? 13.013  32.178  -1.743  1.00 63.89  ?  221 ASP A N     1 
ATOM   1632 C  CA    . ASP A 1 228 ? 13.438  31.981  -3.116  1.00 65.70  ?  221 ASP A CA    1 
ATOM   1633 C  C     . ASP A 1 228 ? 14.654  32.841  -3.459  1.00 68.96  ?  221 ASP A C     1 
ATOM   1634 O  O     . ASP A 1 228 ? 15.561  32.344  -4.128  1.00 69.16  ?  221 ASP A O     1 
ATOM   1635 C  CB    . ASP A 1 228 ? 12.285  32.259  -4.081  1.00 68.12  ?  221 ASP A CB    1 
ATOM   1636 C  CG    . ASP A 1 228 ? 11.137  31.279  -3.938  1.00 65.34  ?  221 ASP A CG    1 
ATOM   1637 O  OD1   . ASP A 1 228 ? 11.384  30.145  -3.467  1.00 61.61  ?  221 ASP A OD1   1 
ATOM   1638 O  OD2   . ASP A 1 228 ? 9.991   31.678  -4.236  1.00 67.20  ?  221 ASP A OD2   1 
ATOM   1639 N  N     . ARG A 1 229 ? 14.687  34.108  -3.011  1.00 71.85  ?  222 ARG A N     1 
ATOM   1640 C  CA    . ARG A 1 229 ? 15.788  35.010  -3.340  1.00 75.64  ?  222 ARG A CA    1 
ATOM   1641 C  C     . ARG A 1 229 ? 17.086  34.571  -2.659  1.00 73.74  ?  222 ARG A C     1 
ATOM   1642 O  O     . ARG A 1 229 ? 18.173  34.733  -3.220  1.00 76.03  ?  222 ARG A O     1 
ATOM   1643 C  CB    . ARG A 1 229 ? 15.455  36.462  -2.973  1.00 79.54  ?  222 ARG A CB    1 
ATOM   1644 C  CG    . ARG A 1 229 ? 14.468  37.134  -3.919  1.00 83.18  ?  222 ARG A CG    1 
ATOM   1645 C  CD    . ARG A 1 229 ? 14.317  38.613  -3.614  1.00 87.82  ?  222 ARG A CD    1 
ATOM   1646 N  NE    . ARG A 1 229 ? 13.675  38.871  -2.323  1.00 86.40  ?  222 ARG A NE    1 
ATOM   1647 C  CZ    . ARG A 1 229 ? 14.313  39.175  -1.190  1.00 85.84  ?  222 ARG A CZ    1 
ATOM   1648 N  NH1   . ARG A 1 229 ? 15.629  39.086  -1.108  1.00 85.78  ?  222 ARG A NH1   1 
ATOM   1649 N  NH2   . ARG A 1 229 ? 13.630  39.558  -0.124  1.00 85.62  ?  222 ARG A NH2   1 
ATOM   1650 N  N     . PHE A 1 230 ? 16.983  34.006  -1.446  1.00 69.87  ?  223 PHE A N     1 
ATOM   1651 C  CA    . PHE A 1 230 ? 18.124  33.355  -0.827  1.00 67.66  ?  223 PHE A CA    1 
ATOM   1652 C  C     . PHE A 1 230 ? 18.667  32.261  -1.749  1.00 66.52  ?  223 PHE A C     1 
ATOM   1653 O  O     . PHE A 1 230 ? 19.850  32.208  -2.056  1.00 67.98  ?  223 PHE A O     1 
ATOM   1654 C  CB    . PHE A 1 230 ? 17.741  32.808  0.561   1.00 63.69  ?  223 PHE A CB    1 
ATOM   1655 C  CG    . PHE A 1 230 ? 18.903  32.211  1.318   1.00 61.75  ?  223 PHE A CG    1 
ATOM   1656 C  CD1   . PHE A 1 230 ? 19.355  30.930  1.034   1.00 59.08  ?  223 PHE A CD1   1 
ATOM   1657 C  CD2   . PHE A 1 230 ? 19.583  32.957  2.268   1.00 63.10  ?  223 PHE A CD2   1 
ATOM   1658 C  CE1   . PHE A 1 230 ? 20.461  30.393  1.686   1.00 57.78  ?  223 PHE A CE1   1 
ATOM   1659 C  CE2   . PHE A 1 230 ? 20.680  32.422  2.926   1.00 61.72  ?  223 PHE A CE2   1 
ATOM   1660 C  CZ    . PHE A 1 230 ? 21.117  31.144  2.640   1.00 59.06  ?  223 PHE A CZ    1 
ATOM   1661 N  N     . CYS A 1 231 ? 17.814  31.312  -2.138  1.00 64.01  ?  224 CYS A N     1 
ATOM   1662 C  CA    . CYS A 1 231 ? 18.263  30.201  -2.953  1.00 63.00  ?  224 CYS A CA    1 
ATOM   1663 C  C     . CYS A 1 231 ? 18.860  30.680  -4.283  1.00 67.29  ?  224 CYS A C     1 
ATOM   1664 O  O     . CYS A 1 231 ? 19.820  30.074  -4.778  1.00 67.74  ?  224 CYS A O     1 
ATOM   1665 C  CB    . CYS A 1 231 ? 17.123  29.227  -3.159  1.00 60.26  ?  224 CYS A CB    1 
ATOM   1666 S  SG    . CYS A 1 231 ? 16.607  28.502  -1.579  1.00 55.50  ?  224 CYS A SG    1 
ATOM   1667 N  N     . GLU A 1 232 ? 18.273  31.740  -4.851  1.00 70.70  ?  225 GLU A N     1 
ATOM   1668 C  CA    . GLU A 1 232 ? 18.759  32.384  -6.067  1.00 75.48  ?  225 GLU A CA    1 
ATOM   1669 C  C     . GLU A 1 232 ? 20.171  32.948  -5.886  1.00 78.10  ?  225 GLU A C     1 
ATOM   1670 O  O     . GLU A 1 232 ? 21.019  32.761  -6.755  1.00 80.57  ?  225 GLU A O     1 
ATOM   1671 C  CB    . GLU A 1 232 ? 17.804  33.503  -6.488  1.00 78.76  ?  225 GLU A CB    1 
ATOM   1672 C  CG    . GLU A 1 232 ? 16.459  32.988  -6.977  1.00 77.40  ?  225 GLU A CG    1 
ATOM   1673 C  CD    . GLU A 1 232 ? 15.372  34.036  -7.157  1.00 80.24  ?  225 GLU A CD    1 
ATOM   1674 O  OE1   . GLU A 1 232 ? 14.213  33.636  -7.395  1.00 79.10  ?  225 GLU A OE1   1 
ATOM   1675 O  OE2   . GLU A 1 232 ? 15.685  35.249  -7.076  1.00 83.94  ?  225 GLU A OE2   1 
ATOM   1676 N  N     . ARG A 1 233 ? 20.412  33.632  -4.758  1.00 77.90  ?  226 ARG A N     1 
ATOM   1677 C  CA    . ARG A 1 233 ? 21.708  34.205  -4.413  1.00 80.45  ?  226 ARG A CA    1 
ATOM   1678 C  C     . ARG A 1 233 ? 22.799  33.125  -4.422  1.00 78.77  ?  226 ARG A C     1 
ATOM   1679 O  O     . ARG A 1 233 ? 23.963  33.423  -4.707  1.00 82.02  ?  226 ARG A O     1 
ATOM   1680 C  CB    . ARG A 1 233 ? 21.550  34.907  -3.059  1.00 79.67  ?  226 ARG A CB    1 
ATOM   1681 C  CG    . ARG A 1 233 ? 22.729  35.758  -2.608  1.00 83.07  ?  226 ARG A CG    1 
ATOM   1682 C  CD    . ARG A 1 233 ? 22.441  36.540  -1.330  1.00 82.92  ?  226 ARG A CD    1 
ATOM   1683 N  NE    . ARG A 1 233 ? 21.125  37.178  -1.303  1.00 83.43  ?  226 ARG A NE    1 
ATOM   1684 C  CZ    . ARG A 1 233 ? 20.119  36.844  -0.489  1.00 79.86  ?  226 ARG A CZ    1 
ATOM   1685 N  NH1   . ARG A 1 233 ? 20.265  35.889  0.416   1.00 75.38  ?  226 ARG A NH1   1 
ATOM   1686 N  NH2   . ARG A 1 233 ? 18.951  37.461  -0.585  1.00 81.09  ?  226 ARG A NH2   1 
ATOM   1687 N  N     . HIS A 1 234 ? 22.417  31.868  -4.122  1.00 74.10  ?  227 HIS A N     1 
ATOM   1688 C  CA    . HIS A 1 234 ? 23.350  30.755  -3.993  1.00 72.26  ?  227 HIS A CA    1 
ATOM   1689 C  C     . HIS A 1 234 ? 23.164  29.743  -5.128  1.00 71.96  ?  227 HIS A C     1 
ATOM   1690 O  O     . HIS A 1 234 ? 23.511  28.572  -4.973  1.00 69.44  ?  227 HIS A O     1 
ATOM   1691 C  CB    . HIS A 1 234 ? 23.199  30.115  -2.598  1.00 67.61  ?  227 HIS A CB    1 
ATOM   1692 C  CG    . HIS A 1 234 ? 23.404  31.109  -1.508  1.00 68.35  ?  227 HIS A CG    1 
ATOM   1693 N  ND1   . HIS A 1 234 ? 22.347  31.856  -1.049  1.00 68.06  ?  227 HIS A ND1   1 
ATOM   1694 C  CD2   . HIS A 1 234 ? 24.478  31.575  -0.870  1.00 70.05  ?  227 HIS A CD2   1 
ATOM   1695 C  CE1   . HIS A 1 234 ? 22.766  32.733  -0.163  1.00 69.53  ?  227 HIS A CE1   1 
ATOM   1696 N  NE2   . HIS A 1 234 ? 24.050  32.569  -0.021  1.00 70.64  ?  227 HIS A NE2   1 
ATOM   1697 N  N     . SER A 1 235 ? 22.696  30.200  -6.299  1.00 75.05  ?  228 SER A N     1 
ATOM   1698 C  CA    . SER A 1 235 ? 22.325  29.299  -7.382  1.00 74.98  ?  228 SER A CA    1 
ATOM   1699 C  C     . SER A 1 235 ? 23.539  28.572  -7.971  1.00 76.68  ?  228 SER A C     1 
ATOM   1700 O  O     . SER A 1 235 ? 23.387  27.503  -8.558  1.00 75.68  ?  228 SER A O     1 
ATOM   1701 C  CB    . SER A 1 235 ? 21.535  30.018  -8.448  1.00 78.24  ?  228 SER A CB    1 
ATOM   1702 O  OG    . SER A 1 235 ? 22.096  31.296  -8.724  1.00 82.94  ?  228 SER A OG    1 
ATOM   1703 N  N     . SER A 1 236 ? 24.753  29.092  -7.762  1.00 79.38  ?  229 SER A N     1 
ATOM   1704 C  CA    . SER A 1 236 ? 25.952  28.423  -8.248  1.00 81.39  ?  229 SER A CA    1 
ATOM   1705 C  C     . SER A 1 236 ? 26.428  27.302  -7.321  1.00 77.55  ?  229 SER A C     1 
ATOM   1706 O  O     . SER A 1 236 ? 27.455  26.689  -7.608  1.00 79.20  ?  229 SER A O     1 
ATOM   1707 C  CB    . SER A 1 236 ? 27.075  29.413  -8.439  1.00 86.43  ?  229 SER A CB    1 
ATOM   1708 O  OG    . SER A 1 236 ? 27.635  29.757  -7.180  1.00 85.12  ?  229 SER A OG    1 
ATOM   1709 N  N     . GLN A 1 237 ? 25.744  27.083  -6.180  1.00 72.93  ?  230 GLN A N     1 
ATOM   1710 C  CA    . GLN A 1 237 ? 26.082  25.981  -5.291  1.00 69.32  ?  230 GLN A CA    1 
ATOM   1711 C  C     . GLN A 1 237 ? 25.342  24.735  -5.768  1.00 66.87  ?  230 GLN A C     1 
ATOM   1712 O  O     . GLN A 1 237 ? 24.119  24.651  -5.647  1.00 64.34  ?  230 GLN A O     1 
ATOM   1713 C  CB    . GLN A 1 237 ? 25.711  26.316  -3.842  1.00 65.98  ?  230 GLN A CB    1 
ATOM   1714 C  CG    . GLN A 1 237 ? 26.360  27.589  -3.316  1.00 68.60  ?  230 GLN A CG    1 
ATOM   1715 C  CD    . GLN A 1 237 ? 27.868  27.533  -3.313  1.00 71.49  ?  230 GLN A CD    1 
ATOM   1716 O  OE1   . GLN A 1 237 ? 28.476  26.491  -3.532  1.00 71.17  ?  230 GLN A OE1   1 
ATOM   1717 N  NE2   . GLN A 1 237 ? 28.494  28.673  -3.076  1.00 74.79  ?  230 GLN A NE2   1 
ATOM   1718 N  N     . THR A 1 238 ? 26.091  23.783  -6.329  1.00 68.10  ?  231 THR A N     1 
ATOM   1719 C  CA    . THR A 1 238 ? 25.497  22.560  -6.819  1.00 66.43  ?  231 THR A CA    1 
ATOM   1720 C  C     . THR A 1 238 ? 25.169  21.634  -5.642  1.00 61.75  ?  231 THR A C     1 
ATOM   1721 O  O     . THR A 1 238 ? 24.505  20.629  -5.832  1.00 59.88  ?  231 THR A O     1 
ATOM   1722 C  CB    . THR A 1 238 ? 26.407  21.860  -7.832  1.00 69.89  ?  231 THR A CB    1 
ATOM   1723 O  OG1   . THR A 1 238 ? 27.503  21.323  -7.104  1.00 69.58  ?  231 THR A OG1   1 
ATOM   1724 C  CG2   . THR A 1 238 ? 26.895  22.782  -8.934  1.00 75.09  ?  231 THR A CG2   1 
ATOM   1725 N  N     . CYS A 1 239 ? 25.651  21.956  -4.439  1.00 60.23  ?  232 CYS A N     1 
ATOM   1726 C  CA    . CYS A 1 239 ? 25.330  21.144  -3.270  1.00 56.10  ?  232 CYS A CA    1 
ATOM   1727 C  C     . CYS A 1 239 ? 24.022  21.567  -2.591  1.00 53.05  ?  232 CYS A C     1 
ATOM   1728 O  O     . CYS A 1 239 ? 23.544  20.853  -1.698  1.00 49.73  ?  232 CYS A O     1 
ATOM   1729 C  CB    . CYS A 1 239 ? 26.457  21.185  -2.249  1.00 56.05  ?  232 CYS A CB    1 
ATOM   1730 S  SG    . CYS A 1 239 ? 26.815  22.833  -1.601  1.00 57.58  ?  232 CYS A SG    1 
ATOM   1731 N  N     . LEU A 1 240 ? 23.466  22.715  -2.988  1.00 54.53  ?  233 LEU A N     1 
ATOM   1732 C  CA    . LEU A 1 240 ? 22.258  23.266  -2.391  1.00 52.45  ?  233 LEU A CA    1 
ATOM   1733 C  C     . LEU A 1 240 ? 21.031  22.364  -2.577  1.00 50.03  ?  233 LEU A C     1 
ATOM   1734 O  O     . LEU A 1 240 ? 20.675  21.972  -3.691  1.00 51.34  ?  233 LEU A O     1 
ATOM   1735 C  CB    . LEU A 1 240 ? 21.991  24.645  -2.992  1.00 55.46  ?  233 LEU A CB    1 
ATOM   1736 C  CG    . LEU A 1 240 ? 20.643  25.267  -2.640  1.00 54.23  ?  233 LEU A CG    1 
ATOM   1737 C  CD1   . LEU A 1 240 ? 20.566  25.610  -1.168  1.00 52.06  ?  233 LEU A CD1   1 
ATOM   1738 C  CD2   . LEU A 1 240 ? 20.393  26.504  -3.492  1.00 57.92  ?  233 LEU A CD2   1 
ATOM   1739 N  N     . VAL A 1 241 ? 20.368  22.072  -1.450  1.00 46.82  ?  234 VAL A N     1 
ATOM   1740 C  CA    . VAL A 1 241 ? 19.120  21.329  -1.429  1.00 44.69  ?  234 VAL A CA    1 
ATOM   1741 C  C     . VAL A 1 241 ? 18.061  22.152  -0.708  1.00 43.67  ?  234 VAL A C     1 
ATOM   1742 O  O     . VAL A 1 241 ? 17.946  22.119  0.517   1.00 41.60  ?  234 VAL A O     1 
ATOM   1743 C  CB    . VAL A 1 241 ? 19.256  19.966  -0.740  1.00 42.09  ?  234 VAL A CB    1 
ATOM   1744 C  CG1   . VAL A 1 241 ? 17.892  19.280  -0.655  1.00 40.26  ?  234 VAL A CG1   1 
ATOM   1745 C  CG2   . VAL A 1 241 ? 20.276  19.069  -1.407  1.00 43.36  ?  234 VAL A CG2   1 
ATOM   1746 N  N     . PRO A 1 242 ? 17.223  22.918  -1.434  1.00 45.42  ?  235 PRO A N     1 
ATOM   1747 C  CA    . PRO A 1 242 ? 16.231  23.774  -0.794  1.00 45.11  ?  235 PRO A CA    1 
ATOM   1748 C  C     . PRO A 1 242 ? 14.980  23.040  -0.338  1.00 42.85  ?  235 PRO A C     1 
ATOM   1749 O  O     . PRO A 1 242 ? 14.500  22.155  -1.039  1.00 42.62  ?  235 PRO A O     1 
ATOM   1750 C  CB    . PRO A 1 242 ? 15.839  24.769  -1.887  1.00 48.38  ?  235 PRO A CB    1 
ATOM   1751 C  CG    . PRO A 1 242 ? 16.090  24.004  -3.169  1.00 49.55  ?  235 PRO A CG    1 
ATOM   1752 C  CD    . PRO A 1 242 ? 17.227  23.041  -2.906  1.00 48.24  ?  235 PRO A CD    1 
ATOM   1753 N  N     . GLU A 1 243 ? 14.445  23.486  0.811   1.00 41.71  ?  236 GLU A N     1 
ATOM   1754 C  CA    . GLU A 1 243 ? 13.236  22.928  1.373   1.00 40.05  ?  236 GLU A CA    1 
ATOM   1755 C  C     . GLU A 1 243 ? 12.289  24.020  1.845   1.00 41.19  ?  236 GLU A C     1 
ATOM   1756 O  O     . GLU A 1 243 ? 12.238  24.375  3.012   1.00 40.42  ?  236 GLU A O     1 
ATOM   1757 C  CB    . GLU A 1 243 ? 13.536  21.961  2.521   1.00 37.28  ?  236 GLU A CB    1 
ATOM   1758 C  CG    . GLU A 1 243 ? 14.357  20.798  2.061   1.00 36.47  ?  236 GLU A CG    1 
ATOM   1759 C  CD    . GLU A 1 243 ? 14.496  19.664  3.044   1.00 34.08  ?  236 GLU A CD    1 
ATOM   1760 O  OE1   . GLU A 1 243 ? 13.684  19.579  3.965   1.00 32.94  ?  236 GLU A OE1   1 
ATOM   1761 O  OE2   . GLU A 1 243 ? 15.372  18.845  2.821   1.00 33.73  ?  236 GLU A OE2   1 
ATOM   1762 N  N     . PRO A 1 244 ? 11.430  24.526  0.946   1.00 43.33  ?  237 PRO A N     1 
ATOM   1763 C  CA    . PRO A 1 244 ? 10.377  25.449  1.347   1.00 44.76  ?  237 PRO A CA    1 
ATOM   1764 C  C     . PRO A 1 244 ? 9.390   24.690  2.212   1.00 42.91  ?  237 PRO A C     1 
ATOM   1765 O  O     . PRO A 1 244 ? 9.415   23.457  2.205   1.00 40.93  ?  237 PRO A O     1 
ATOM   1766 C  CB    . PRO A 1 244 ? 9.780   25.944  0.025   1.00 47.63  ?  237 PRO A CB    1 
ATOM   1767 C  CG    . PRO A 1 244 ? 10.231  24.935  -1.023  1.00 47.14  ?  237 PRO A CG    1 
ATOM   1768 C  CD    . PRO A 1 244 ? 11.458  24.228  -0.500  1.00 44.83  ?  237 PRO A CD    1 
ATOM   1769 N  N     . ASN A 1 245 ? 8.524   25.420  2.926   1.00 43.97  ?  238 ASN A N     1 
ATOM   1770 C  CA    . ASN A 1 245 ? 7.599   24.795  3.852   1.00 42.71  ?  238 ASN A CA    1 
ATOM   1771 C  C     . ASN A 1 245 ? 6.825   23.670  3.155   1.00 42.21  ?  238 ASN A C     1 
ATOM   1772 O  O     . ASN A 1 245 ? 6.577   22.629  3.759   1.00 40.37  ?  238 ASN A O     1 
ATOM   1773 C  CB    . ASN A 1 245 ? 6.621   25.789  4.472   1.00 44.86  ?  238 ASN A CB    1 
ATOM   1774 C  CG    . ASN A 1 245 ? 7.204   26.714  5.535   1.00 45.30  ?  238 ASN A CG    1 
ATOM   1775 O  OD1   . ASN A 1 245 ? 8.355   26.597  5.966   1.00 43.77  ?  238 ASN A OD1   1 
ATOM   1776 N  ND2   . ASN A 1 245 ? 6.378   27.622  5.999   1.00 47.69  ?  238 ASN A ND2   1 
ATOM   1777 N  N     . ARG A 1 246 ? 6.421   23.880  1.882   1.00 44.21  ?  239 ARG A N     1 
ATOM   1778 C  CA    . ARG A 1 246 ? 5.611   22.917  1.166   1.00 44.38  ?  239 ARG A CA    1 
ATOM   1779 C  C     . ARG A 1 246 ? 6.266   21.533  1.095   1.00 41.97  ?  239 ARG A C     1 
ATOM   1780 O  O     . ARG A 1 246 ? 5.576   20.518  1.167   1.00 41.41  ?  239 ARG A O     1 
ATOM   1781 C  CB    . ARG A 1 246 ? 5.296   23.494  -0.222  1.00 47.25  ?  239 ARG A CB    1 
ATOM   1782 C  CG    . ARG A 1 246 ? 4.683   22.511  -1.203  1.00 47.83  ?  239 ARG A CG    1 
ATOM   1783 C  CD    . ARG A 1 246 ? 4.360   23.201  -2.520  1.00 51.06  ?  239 ARG A CD    1 
ATOM   1784 N  NE    . ARG A 1 246 ? 4.203   22.232  -3.596  1.00 51.60  ?  239 ARG A NE    1 
ATOM   1785 C  CZ    . ARG A 1 246 ? 5.181   21.681  -4.308  1.00 51.08  ?  239 ARG A CZ    1 
ATOM   1786 N  NH1   . ARG A 1 246 ? 6.440   21.994  -4.082  1.00 49.94  ?  239 ARG A NH1   1 
ATOM   1787 N  NH2   . ARG A 1 246 ? 4.886   20.842  -5.291  1.00 52.16  ?  239 ARG A NH2   1 
ATOM   1788 N  N     . LEU A 1 247 ? 7.580   21.493  0.926   1.00 40.97  ?  240 LEU A N     1 
ATOM   1789 C  CA    . LEU A 1 247 ? 8.293   20.241  0.773   1.00 39.22  ?  240 LEU A CA    1 
ATOM   1790 C  C     . LEU A 1 247 ? 8.786   19.693  2.121   1.00 36.72  ?  240 LEU A C     1 
ATOM   1791 O  O     . LEU A 1 247 ? 9.101   18.514  2.214   1.00 35.36  ?  240 LEU A O     1 
ATOM   1792 C  CB    . LEU A 1 247 ? 9.436   20.472  -0.202  1.00 40.09  ?  240 LEU A CB    1 
ATOM   1793 C  CG    . LEU A 1 247 ? 9.039   20.629  -1.674  1.00 42.63  ?  240 LEU A CG    1 
ATOM   1794 C  CD1   . LEU A 1 247 ? 10.267  20.766  -2.561  1.00 43.69  ?  240 LEU A CD1   1 
ATOM   1795 C  CD2   . LEU A 1 247 ? 8.207   19.445  -2.141  1.00 42.65  ?  240 LEU A CD2   1 
ATOM   1796 N  N     . MET A 1 248 ? 8.918   20.528  3.157   1.00 36.39  ?  241 MET A N     1 
ATOM   1797 C  CA    . MET A 1 248 ? 9.485   20.037  4.406   1.00 34.31  ?  241 MET A CA    1 
ATOM   1798 C  C     . MET A 1 248 ? 8.413   19.491  5.348   1.00 33.73  ?  241 MET A C     1 
ATOM   1799 O  O     . MET A 1 248 ? 8.715   18.669  6.216   1.00 32.12  ?  241 MET A O     1 
ATOM   1800 C  CB    . MET A 1 248 ? 10.246  21.154  5.121   1.00 34.51  ?  241 MET A CB    1 
ATOM   1801 C  CG    . MET A 1 248 ? 11.002  20.673  6.362   1.00 32.62  ?  241 MET A CG    1 
ATOM   1802 S  SD    . MET A 1 248 ? 12.062  21.962  7.095   1.00 33.30  ?  241 MET A SD    1 
ATOM   1803 C  CE    . MET A 1 248 ? 13.093  20.967  8.181   1.00 31.11  ?  241 MET A CE    1 
ATOM   1804 N  N     . ALA A 1 249 ? 7.193   20.006  5.257   1.00 35.36  ?  242 ALA A N     1 
ATOM   1805 C  CA    . ALA A 1 249 ? 6.206   19.824  6.318   1.00 35.47  ?  242 ALA A CA    1 
ATOM   1806 C  C     . ALA A 1 249 ? 5.946   18.348  6.628   1.00 34.24  ?  242 ALA A C     1 
ATOM   1807 O  O     . ALA A 1 249 ? 5.877   17.989  7.794   1.00 33.45  ?  242 ALA A O     1 
ATOM   1808 C  CB    . ALA A 1 249 ? 4.922   20.506  5.964   1.00 37.93  ?  242 ALA A CB    1 
ATOM   1809 N  N     . LYS A 1 250 ? 5.709   17.538  5.596   1.00 34.56  ?  243 LYS A N     1 
ATOM   1810 C  CA    . LYS A 1 250 ? 5.168   16.206  5.815   1.00 34.28  ?  243 LYS A CA    1 
ATOM   1811 C  C     . LYS A 1 250 ? 6.003   15.157  5.098   1.00 33.37  ?  243 LYS A C     1 
ATOM   1812 O  O     . LYS A 1 250 ? 5.549   14.042  4.946   1.00 33.71  ?  243 LYS A O     1 
ATOM   1813 C  CB    . LYS A 1 250 ? 3.725   16.095  5.322   1.00 36.48  ?  243 LYS A CB    1 
ATOM   1814 C  CG    . LYS A 1 250 ? 2.777   17.179  5.804   1.00 38.19  ?  243 LYS A CG    1 
ATOM   1815 C  CD    . LYS A 1 250 ? 1.949   16.855  6.992   1.00 38.73  ?  243 LYS A CD    1 
ATOM   1816 C  CE    . LYS A 1 250 ? 2.737   16.540  8.231   1.00 36.76  ?  243 LYS A CE    1 
ATOM   1817 N  NZ    . LYS A 1 250 ? 2.025   17.010  9.440   1.00 37.94  ?  243 LYS A NZ    1 
ATOM   1818 N  N     . SER A 1 251 ? 7.234   15.490  4.739   1.00 32.52  ?  244 SER A N     1 
ATOM   1819 C  CA    . SER A 1 251 ? 8.029   14.671  3.851   1.00 32.35  ?  244 SER A CA    1 
ATOM   1820 C  C     . SER A 1 251 ? 9.061   13.831  4.607   1.00 30.71  ?  244 SER A C     1 
ATOM   1821 O  O     . SER A 1 251 ? 9.875   13.190  3.963   1.00 30.74  ?  244 SER A O     1 
ATOM   1822 C  CB    . SER A 1 251 ? 8.686   15.552  2.838   1.00 33.17  ?  244 SER A CB    1 
ATOM   1823 O  OG    . SER A 1 251 ? 9.670   16.369  3.444   1.00 32.29  ?  244 SER A OG    1 
ATOM   1824 N  N     . TYR A 1 252 ? 9.000   13.805  5.951   1.00 29.65  ?  245 TYR A N     1 
ATOM   1825 C  CA    . TYR A 1 252 ? 9.944   13.047  6.762   1.00 28.35  ?  245 TYR A CA    1 
ATOM   1826 C  C     . TYR A 1 252 ? 9.251   11.948  7.560   1.00 28.34  ?  245 TYR A C     1 
ATOM   1827 O  O     . TYR A 1 252 ? 8.076   12.061  7.854   1.00 29.13  ?  245 TYR A O     1 
ATOM   1828 C  CB    . TYR A 1 252 ? 10.657  13.987  7.726   1.00 27.45  ?  245 TYR A CB    1 
ATOM   1829 C  CG    . TYR A 1 252 ? 11.686  14.922  7.106   1.00 27.61  ?  245 TYR A CG    1 
ATOM   1830 C  CD1   . TYR A 1 252 ? 11.272  16.029  6.374   1.00 28.74  ?  245 TYR A CD1   1 
ATOM   1831 C  CD2   . TYR A 1 252 ? 13.056  14.689  7.210   1.00 27.06  ?  245 TYR A CD2   1 
ATOM   1832 C  CE1   . TYR A 1 252 ? 12.202  16.884  5.804   1.00 29.32  ?  245 TYR A CE1   1 
ATOM   1833 C  CE2   . TYR A 1 252 ? 14.001  15.562  6.677   1.00 27.65  ?  245 TYR A CE2   1 
ATOM   1834 C  CZ    . TYR A 1 252 ? 13.553  16.655  5.950   1.00 28.81  ?  245 TYR A CZ    1 
ATOM   1835 O  OH    . TYR A 1 252 ? 14.439  17.508  5.371   1.00 29.83  ?  245 TYR A OH    1 
ATOM   1836 N  N     . LEU A 1 253 ? 10.002  10.884  7.830   1.00 27.86  ?  246 LEU A N     1 
ATOM   1837 C  CA    . LEU A 1 253 ? 9.637   9.849   8.796   1.00 27.93  ?  246 LEU A CA    1 
ATOM   1838 C  C     . LEU A 1 253 ? 10.383  10.104  10.089  1.00 26.81  ?  246 LEU A C     1 
ATOM   1839 O  O     . LEU A 1 253 ? 11.608  10.087  10.118  1.00 26.12  ?  246 LEU A O     1 
ATOM   1840 C  CB    . LEU A 1 253 ? 10.026  8.517   8.172   1.00 28.63  ?  246 LEU A CB    1 
ATOM   1841 C  CG    . LEU A 1 253 ? 9.154   8.102   6.995   1.00 30.20  ?  246 LEU A CG    1 
ATOM   1842 C  CD1   . LEU A 1 253 ? 9.718   6.888   6.284   1.00 31.21  ?  246 LEU A CD1   1 
ATOM   1843 C  CD2   . LEU A 1 253 ? 7.732   7.844   7.451   1.00 31.28  ?  246 LEU A CD2   1 
ATOM   1844 N  N     . ILE A 1 254 ? 9.617   10.393  11.144  1.00 26.97  ?  247 ILE A N     1 
ATOM   1845 C  CA    . ILE A 1 254 ? 10.172  10.949  12.369  1.00 26.24  ?  247 ILE A CA    1 
ATOM   1846 C  C     . ILE A 1 254 ? 9.739   10.074  13.529  1.00 26.80  ?  247 ILE A C     1 
ATOM   1847 O  O     . ILE A 1 254 ? 8.541   10.010  13.836  1.00 27.92  ?  247 ILE A O     1 
ATOM   1848 C  CB    . ILE A 1 254 ? 9.722   12.406  12.557  1.00 26.40  ?  247 ILE A CB    1 
ATOM   1849 C  CG1   . ILE A 1 254 ? 10.229  13.241  11.377  1.00 26.20  ?  247 ILE A CG1   1 
ATOM   1850 C  CG2   . ILE A 1 254 ? 10.243  12.935  13.879  1.00 26.05  ?  247 ILE A CG2   1 
ATOM   1851 C  CD1   . ILE A 1 254 ? 9.713   14.629  11.318  1.00 26.86  ?  247 ILE A CD1   1 
ATOM   1852 N  N     . LEU A 1 255 ? 10.737  9.461   14.187  1.00 26.32  ?  248 LEU A N     1 
ATOM   1853 C  CA    . LEU A 1 255 ? 10.515  8.766   15.442  1.00 27.02  ?  248 LEU A CA    1 
ATOM   1854 C  C     . LEU A 1 255 ? 10.888  9.658   16.624  1.00 26.70  ?  248 LEU A C     1 
ATOM   1855 O  O     . LEU A 1 255 ? 11.976  10.244  16.639  1.00 25.79  ?  248 LEU A O     1 
ATOM   1856 C  CB    . LEU A 1 255 ? 11.391  7.524   15.472  1.00 27.16  ?  248 LEU A CB    1 
ATOM   1857 C  CG    . LEU A 1 255 ? 10.931  6.371   14.598  1.00 28.20  ?  248 LEU A CG    1 
ATOM   1858 C  CD1   . LEU A 1 255 ? 11.946  5.274   14.684  1.00 28.61  ?  248 LEU A CD1   1 
ATOM   1859 C  CD2   . LEU A 1 255 ? 9.557   5.873   15.060  1.00 29.79  ?  248 LEU A CD2   1 
ATOM   1860 N  N     . ASP A 1 256 ? 10.039  9.647   17.664  1.00 27.84  ?  249 ASP A N     1 
ATOM   1861 C  CA    . ASP A 1 256 ? 10.365  10.342  18.894  1.00 28.03  ?  249 ASP A CA    1 
ATOM   1862 C  C     . ASP A 1 256 ? 11.192  9.468   19.847  1.00 28.28  ?  249 ASP A C     1 
ATOM   1863 O  O     . ASP A 1 256 ? 11.681  8.373   19.505  1.00 28.20  ?  249 ASP A O     1 
ATOM   1864 C  CB    . ASP A 1 256 ? 9.089   10.929  19.503  1.00 29.53  ?  249 ASP A CB    1 
ATOM   1865 C  CG    . ASP A 1 256 ? 8.224   9.892   20.222  1.00 31.32  ?  249 ASP A CG    1 
ATOM   1866 O  OD1   . ASP A 1 256 ? 8.612   8.708   20.226  1.00 31.36  ?  249 ASP A OD1   1 
ATOM   1867 O  OD2   . ASP A 1 256 ? 7.154   10.280  20.724  1.00 32.99  ?  249 ASP A OD2   1 
ATOM   1868 N  N     . GLU A 1 257 ? 11.338  9.977   21.084  1.00 28.95  ?  250 GLU A N     1 
ATOM   1869 C  CA    . GLU A 1 257 ? 12.213  9.407   22.079  1.00 29.39  ?  250 GLU A CA    1 
ATOM   1870 C  C     . GLU A 1 257 ? 11.618  8.087   22.597  1.00 30.96  ?  250 GLU A C     1 
ATOM   1871 O  O     . GLU A 1 257 ? 12.313  7.382   23.309  1.00 31.61  ?  250 GLU A O     1 
ATOM   1872 C  CB    . GLU A 1 257 ? 12.510  10.429  23.177  1.00 29.96  ?  250 GLU A CB    1 
ATOM   1873 C  CG    . GLU A 1 257 ? 11.318  10.807  24.062  1.00 31.78  ?  250 GLU A CG    1 
ATOM   1874 C  CD    . GLU A 1 257 ? 10.442  11.981  23.638  1.00 31.97  ?  250 GLU A CD    1 
ATOM   1875 O  OE1   . GLU A 1 257 ? 10.366  12.328  22.419  1.00 30.71  ?  250 GLU A OE1   1 
ATOM   1876 O  OE2   . GLU A 1 257 ? 9.782   12.548  24.526  1.00 33.75  ?  250 GLU A OE2   1 
ATOM   1877 N  N     . TYR A 1 258 ? 10.332  7.811   22.310  1.00 31.95  ?  251 TYR A N     1 
ATOM   1878 C  CA    . TYR A 1 258 ? 9.737   6.514   22.657  1.00 33.81  ?  251 TYR A CA    1 
ATOM   1879 C  C     . TYR A 1 258 ? 9.607   5.601   21.431  1.00 33.54  ?  251 TYR A C     1 
ATOM   1880 O  O     . TYR A 1 258 ? 8.929   4.549   21.503  1.00 35.40  ?  251 TYR A O     1 
ATOM   1881 C  CB    . TYR A 1 258 ? 8.332   6.744   23.219  1.00 35.86  ?  251 TYR A CB    1 
ATOM   1882 C  CG    . TYR A 1 258 ? 8.325   7.484   24.538  1.00 36.94  ?  251 TYR A CG    1 
ATOM   1883 C  CD1   . TYR A 1 258 ? 8.592   6.796   25.714  1.00 38.67  ?  251 TYR A CD1   1 
ATOM   1884 C  CD2   . TYR A 1 258 ? 8.084   8.863   24.601  1.00 36.58  ?  251 TYR A CD2   1 
ATOM   1885 C  CE1   . TYR A 1 258 ? 8.560   7.440   26.937  1.00 40.07  ?  251 TYR A CE1   1 
ATOM   1886 C  CE2   . TYR A 1 258 ? 8.104   9.517   25.814  1.00 37.95  ?  251 TYR A CE2   1 
ATOM   1887 C  CZ    . TYR A 1 258 ? 8.312   8.796   26.977  1.00 39.72  ?  251 TYR A CZ    1 
ATOM   1888 O  OH    . TYR A 1 258 ? 8.347   9.395   28.190  1.00 41.41  ?  251 TYR A OH    1 
ATOM   1889 N  N     . MET A 1 259 ? 10.236  6.016   20.309  1.00 31.61  ?  252 MET A N     1 
ATOM   1890 C  CA    . MET A 1 259 ? 10.171  5.371   18.993  1.00 31.35  ?  252 MET A CA    1 
ATOM   1891 C  C     . MET A 1 259 ? 8.728   5.233   18.503  1.00 32.62  ?  252 MET A C     1 
ATOM   1892 O  O     . MET A 1 259 ? 8.349   4.213   17.909  1.00 33.79  ?  252 MET A O     1 
ATOM   1893 C  CB    . MET A 1 259 ? 10.890  4.007   18.934  1.00 32.17  ?  252 MET A CB    1 
ATOM   1894 C  CG    . MET A 1 259 ? 12.233  3.998   19.583  1.00 31.62  ?  252 MET A CG    1 
ATOM   1895 S  SD    . MET A 1 259 ? 13.307  2.567   19.340  1.00 32.69  ?  252 MET A SD    1 
ATOM   1896 C  CE    . MET A 1 259 ? 14.099  2.989   17.797  1.00 31.07  ?  252 MET A CE    1 
ATOM   1897 N  N     . ARG A 1 260 ? 7.957   6.308   18.684  1.00 32.61  ?  253 ARG A N     1 
ATOM   1898 C  CA    . ARG A 1 260 ? 6.708   6.547   17.986  1.00 33.56  ?  253 ARG A CA    1 
ATOM   1899 C  C     . ARG A 1 260 ? 6.917   7.500   16.808  1.00 31.93  ?  253 ARG A C     1 
ATOM   1900 O  O     . ARG A 1 260 ? 7.620   8.520   16.936  1.00 30.50  ?  253 ARG A O     1 
ATOM   1901 C  CB    . ARG A 1 260 ? 5.721   7.244   18.926  1.00 35.05  ?  253 ARG A CB    1 
ATOM   1902 C  CG    . ARG A 1 260 ? 5.563   6.490   20.241  1.00 36.93  ?  253 ARG A CG    1 
ATOM   1903 C  CD    . ARG A 1 260 ? 4.709   7.200   21.265  1.00 38.75  ?  253 ARG A CD    1 
ATOM   1904 N  NE    . ARG A 1 260 ? 5.189   8.515   21.672  1.00 37.56  ?  253 ARG A NE    1 
ATOM   1905 C  CZ    . ARG A 1 260 ? 4.536   9.311   22.520  1.00 39.24  ?  253 ARG A CZ    1 
ATOM   1906 N  NH1   . ARG A 1 260 ? 3.379   8.923   23.040  1.00 42.15  ?  253 ARG A NH1   1 
ATOM   1907 N  NH2   . ARG A 1 260 ? 5.023   10.501  22.829  1.00 38.38  ?  253 ARG A NH2   1 
ATOM   1908 N  N     . PHE A 1 261 ? 6.175   7.245   15.730  1.00 32.64  ?  254 PHE A N     1 
ATOM   1909 C  CA    . PHE A 1 261 ? 6.124   8.152   14.587  1.00 31.75  ?  254 PHE A CA    1 
ATOM   1910 C  C     . PHE A 1 261 ? 5.294   9.394   14.911  1.00 32.35  ?  254 PHE A C     1 
ATOM   1911 O  O     . PHE A 1 261 ? 4.199   9.293   15.468  1.00 34.27  ?  254 PHE A O     1 
ATOM   1912 C  CB    . PHE A 1 261 ? 5.554   7.451   13.355  1.00 32.75  ?  254 PHE A CB    1 
ATOM   1913 C  CG    . PHE A 1 261 ? 6.504   6.476   12.713  1.00 32.23  ?  254 PHE A CG    1 
ATOM   1914 C  CD1   . PHE A 1 261 ? 7.674   6.914   12.123  1.00 30.53  ?  254 PHE A CD1   1 
ATOM   1915 C  CD2   . PHE A 1 261 ? 6.289   5.104   12.807  1.00 33.80  ?  254 PHE A CD2   1 
ATOM   1916 C  CE1   . PHE A 1 261 ? 8.540   6.024   11.510  1.00 30.49  ?  254 PHE A CE1   1 
ATOM   1917 C  CE2   . PHE A 1 261 ? 7.182   4.218   12.240  1.00 33.72  ?  254 PHE A CE2   1 
ATOM   1918 C  CZ    . PHE A 1 261 ? 8.304   4.673   11.587  1.00 32.08  ?  254 PHE A CZ    1 
ATOM   1919 N  N     . LEU A 1 262 ? 5.847   10.577  14.555  1.00 31.06  ?  255 LEU A N     1 
ATOM   1920 C  CA    . LEU A 1 262 ? 5.229   11.874  14.789  1.00 31.78  ?  255 LEU A CA    1 
ATOM   1921 C  C     . LEU A 1 262 ? 4.627   12.438  13.512  1.00 32.32  ?  255 LEU A C     1 
ATOM   1922 O  O     . LEU A 1 262 ? 5.251   12.438  12.461  1.00 31.29  ?  255 LEU A O     1 
ATOM   1923 C  CB    . LEU A 1 262 ? 6.271   12.876  15.284  1.00 30.48  ?  255 LEU A CB    1 
ATOM   1924 C  CG    . LEU A 1 262 ? 6.930   12.581  16.616  1.00 30.16  ?  255 LEU A CG    1 
ATOM   1925 C  CD1   . LEU A 1 262 ? 7.816   13.748  17.033  1.00 29.43  ?  255 LEU A CD1   1 
ATOM   1926 C  CD2   . LEU A 1 262 ? 5.916   12.269  17.695  1.00 32.12  ?  255 LEU A CD2   1 
ATOM   1927 N  N     . ASP A 1 263 ? 3.439   13.023  13.641  1.00 34.26  ?  256 ASP A N     1 
ATOM   1928 C  CA    . ASP A 1 263 ? 2.729   13.543  12.490  1.00 35.32  ?  256 ASP A CA    1 
ATOM   1929 C  C     . ASP A 1 263 ? 3.148   14.982  12.183  1.00 34.93  ?  256 ASP A C     1 
ATOM   1930 O  O     . ASP A 1 263 ? 2.951   15.422  11.067  1.00 35.38  ?  256 ASP A O     1 
ATOM   1931 C  CB    . ASP A 1 263 ? 1.220   13.414  12.668  1.00 38.11  ?  256 ASP A CB    1 
ATOM   1932 C  CG    . ASP A 1 263 ? 0.485   13.039  11.385  1.00 39.38  ?  256 ASP A CG    1 
ATOM   1933 O  OD1   . ASP A 1 263 ? 1.155   12.670  10.383  1.00 38.05  ?  256 ASP A OD1   1 
ATOM   1934 O  OD2   . ASP A 1 263 ? -0.758  13.134  11.386  1.00 42.00  ?  256 ASP A OD2   1 
ATOM   1935 N  N     . ARG A 1 264 ? 3.724   15.678  13.170  1.00 34.41  ?  257 ARG A N     1 
ATOM   1936 C  CA    . ARG A 1 264 ? 4.223   17.065  12.959  1.00 34.34  ?  257 ARG A CA    1 
ATOM   1937 C  C     . ARG A 1 264 ? 3.079   17.975  12.481  1.00 36.76  ?  257 ARG A C     1 
ATOM   1938 O  O     . ARG A 1 264 ? 3.318   18.778  11.552  1.00 37.00  ?  257 ARG A O     1 
ATOM   1939 C  CB    . ARG A 1 264 ? 5.396   17.073  11.971  1.00 32.60  ?  257 ARG A CB    1 
ATOM   1940 C  CG    . ARG A 1 264 ? 6.519   16.117  12.347  1.00 30.60  ?  257 ARG A CG    1 
ATOM   1941 C  CD    . ARG A 1 264 ? 7.175   16.486  13.668  1.00 30.11  ?  257 ARG A CD    1 
ATOM   1942 N  NE    . ARG A 1 264 ? 7.922   17.745  13.582  1.00 29.97  ?  257 ARG A NE    1 
ATOM   1943 C  CZ    . ARG A 1 264 ? 8.585   18.299  14.589  1.00 30.04  ?  257 ARG A CZ    1 
ATOM   1944 N  NH1   . ARG A 1 264 ? 8.396   17.866  15.823  1.00 30.57  ?  257 ARG A NH1   1 
ATOM   1945 N  NH2   . ARG A 1 264 ? 9.431   19.285  14.359  1.00 29.94  ?  257 ARG A NH2   1 
ATOM   1946 N  N     . ASN A 1 265 ? 1.894   17.859  13.088  1.00 38.89  ?  258 ASN A N     1 
ATOM   1947 C  CA    . ASN A 1 265 ? 0.778   18.729  12.740  1.00 41.68  ?  258 ASN A CA    1 
ATOM   1948 C  C     . ASN A 1 265 ? -0.218  18.912  13.884  1.00 44.27  ?  258 ASN A C     1 
ATOM   1949 O  O     . ASN A 1 265 ? -1.288  19.472  13.665  1.00 47.12  ?  258 ASN A O     1 
ATOM   1950 C  CB    . ASN A 1 265 ? -0.021  18.155  11.575  1.00 42.63  ?  258 ASN A CB    1 
ATOM   1951 C  CG    . ASN A 1 265 ? -0.454  16.734  11.864  1.00 42.60  ?  258 ASN A CG    1 
ATOM   1952 O  OD1   . ASN A 1 265 ? -0.268  16.250  12.977  1.00 42.17  ?  258 ASN A OD1   1 
ATOM   1953 N  ND2   . ASN A 1 265 ? -1.025  16.065  10.880  1.00 43.38  ?  258 ASN A ND2   1 
ATOM   1954 N  N     . GLY A 1 266 ? 0.090   18.413  15.084  1.00 43.70  ?  259 GLY A N     1 
ATOM   1955 C  CA    . GLY A 1 266 ? -0.827  18.518  16.208  1.00 46.49  ?  259 GLY A CA    1 
ATOM   1956 C  C     . GLY A 1 266 ? -1.604  17.228  16.480  1.00 47.51  ?  259 GLY A C     1 
ATOM   1957 O  O     . GLY A 1 266 ? -2.248  17.125  17.522  1.00 49.84  ?  259 GLY A O     1 
ATOM   1958 N  N     . GLN A 1 267 ? -1.553  16.260  15.549  1.00 46.20  ?  260 GLN A N     1 
ATOM   1959 C  CA    . GLN A 1 267 ? -2.120  14.937  15.783  1.00 47.13  ?  260 GLN A CA    1 
ATOM   1960 C  C     . GLN A 1 267 ? -1.255  14.165  16.780  1.00 45.46  ?  260 GLN A C     1 
ATOM   1961 O  O     . GLN A 1 267 ? -0.052  14.403  16.901  1.00 42.83  ?  260 GLN A O     1 
ATOM   1962 C  CB    . GLN A 1 267 ? -2.181  14.109  14.496  1.00 46.34  ?  260 GLN A CB    1 
ATOM   1963 C  CG    . GLN A 1 267 ? -2.929  14.772  13.349  1.00 47.90  ?  260 GLN A CG    1 
ATOM   1964 C  CD    . GLN A 1 267 ? -4.425  14.736  13.533  1.00 51.91  ?  260 GLN A CD    1 
ATOM   1965 O  OE1   . GLN A 1 267 ? -5.015  15.588  14.196  1.00 54.18  ?  260 GLN A OE1   1 
ATOM   1966 N  NE2   . GLN A 1 267 ? -5.050  13.750  12.913  1.00 53.16  ?  260 GLN A NE2   1 
ATOM   1967 N  N     . GLN A 1 268 ? -1.869  13.178  17.442  1.00 47.27  ?  261 GLN A N     1 
ATOM   1968 C  CA    . GLN A 1 268 ? -1.167  12.374  18.420  1.00 46.31  ?  261 GLN A CA    1 
ATOM   1969 C  C     . GLN A 1 268 ? -0.151  11.488  17.711  1.00 43.40  ?  261 GLN A C     1 
ATOM   1970 O  O     . GLN A 1 268 ? -0.317  11.122  16.557  1.00 43.02  ?  261 GLN A O     1 
ATOM   1971 C  CB    . GLN A 1 268 ? -2.121  11.506  19.251  1.00 49.51  ?  261 GLN A CB    1 
ATOM   1972 C  CG    . GLN A 1 268 ? -2.581  12.168  20.545  1.00 52.05  ?  261 GLN A CG    1 
ATOM   1973 C  CD    . GLN A 1 268 ? -1.521  12.121  21.621  1.00 50.56  ?  261 GLN A CD    1 
ATOM   1974 O  OE1   . GLN A 1 268 ? -1.311  11.093  22.266  1.00 50.94  ?  261 GLN A OE1   1 
ATOM   1975 N  NE2   . GLN A 1 268 ? -0.842  13.241  21.830  1.00 49.19  ?  261 GLN A NE2   1 
ATOM   1976 N  N     . PRO A 1 269 ? 0.929   11.115  18.409  1.00 41.64  ?  262 PRO A N     1 
ATOM   1977 C  CA    . PRO A 1 269 ? 1.910   10.183  17.862  1.00 39.42  ?  262 PRO A CA    1 
ATOM   1978 C  C     . PRO A 1 269 ? 1.271   8.822   17.611  1.00 41.09  ?  262 PRO A C     1 
ATOM   1979 O  O     . PRO A 1 269 ? 0.219   8.514   18.172  1.00 43.93  ?  262 PRO A O     1 
ATOM   1980 C  CB    . PRO A 1 269 ? 2.980   10.068  18.950  1.00 38.23  ?  262 PRO A CB    1 
ATOM   1981 C  CG    . PRO A 1 269 ? 2.763   11.247  19.879  1.00 39.18  ?  262 PRO A CG    1 
ATOM   1982 C  CD    . PRO A 1 269 ? 1.317   11.657  19.717  1.00 41.89  ?  262 PRO A CD    1 
ATOM   1983 N  N     . SER A 1 270 ? 1.931   8.014   16.792  1.00 39.68  ?  263 SER A N     1 
ATOM   1984 C  CA    . SER A 1 270 ? 1.607   6.603   16.699  1.00 41.28  ?  263 SER A CA    1 
ATOM   1985 C  C     . SER A 1 270 ? 1.905   5.914   18.023  1.00 42.15  ?  263 SER A C     1 
ATOM   1986 O  O     . SER A 1 270 ? 2.536   6.458   18.932  1.00 41.13  ?  263 SER A O     1 
ATOM   1987 C  CB    . SER A 1 270 ? 2.364   5.943   15.590  1.00 39.82  ?  263 SER A CB    1 
ATOM   1988 O  OG    . SER A 1 270 ? 3.711   5.636   15.955  1.00 37.86  ?  263 SER A OG    1 
ATOM   1989 N  N     . LYS A 1 271 ? 1.510   4.643   18.110  1.00 44.29  ?  264 LYS A N     1 
ATOM   1990 C  CA    . LYS A 1 271 ? 2.040   3.800   19.164  1.00 45.01  ?  264 LYS A CA    1 
ATOM   1991 C  C     . LYS A 1 271 ? 3.492   3.473   18.823  1.00 42.38  ?  264 LYS A C     1 
ATOM   1992 O  O     . LYS A 1 271 ? 3.886   3.523   17.646  1.00 40.81  ?  264 LYS A O     1 
ATOM   1993 C  CB    . LYS A 1 271 ? 1.222   2.505   19.256  1.00 48.47  ?  264 LYS A CB    1 
ATOM   1994 C  CG    . LYS A 1 271 ? -0.269  2.713   19.483  1.00 51.71  ?  264 LYS A CG    1 
ATOM   1995 C  CD    . LYS A 1 271 ? -0.625  3.520   20.699  1.00 52.71  ?  264 LYS A CD    1 
ATOM   1996 C  CE    . LYS A 1 271 ? -2.123  3.561   20.941  1.00 56.70  ?  264 LYS A CE    1 
ATOM   1997 N  NZ    . LYS A 1 271 ? -2.425  3.782   22.376  1.00 58.97  ?  264 LYS A NZ    1 
ATOM   1998 N  N     . SER A 1 272 ? 4.281   3.123   19.838  1.00 42.25  ?  265 SER A N     1 
ATOM   1999 C  CA    . SER A 1 272 ? 5.687   2.795   19.634  1.00 40.23  ?  265 SER A CA    1 
ATOM   2000 C  C     . SER A 1 272 ? 5.840   1.580   18.730  1.00 41.07  ?  265 SER A C     1 
ATOM   2001 O  O     . SER A 1 272 ? 5.124   0.575   18.873  1.00 43.88  ?  265 SER A O     1 
ATOM   2002 C  CB    . SER A 1 272 ? 6.413   2.574   20.937  1.00 40.56  ?  265 SER A CB    1 
ATOM   2003 O  OG    . SER A 1 272 ? 7.768   2.246   20.675  1.00 38.93  ?  265 SER A OG    1 
ATOM   2004 N  N     . ILE A 1 273 ? 6.797   1.661   17.805  1.00 39.03  ?  266 ILE A N     1 
ATOM   2005 C  CA    . ILE A 1 273 ? 7.212   0.472   17.071  1.00 40.03  ?  266 ILE A CA    1 
ATOM   2006 C  C     . ILE A 1 273 ? 7.581   -0.672  18.027  1.00 42.07  ?  266 ILE A C     1 
ATOM   2007 O  O     . ILE A 1 273 ? 7.461   -1.835  17.642  1.00 44.26  ?  266 ILE A O     1 
ATOM   2008 C  CB    . ILE A 1 273 ? 8.341   0.771   16.070  1.00 37.82  ?  266 ILE A CB    1 
ATOM   2009 C  CG1   . ILE A 1 273 ? 9.692   1.018   16.751  1.00 36.31  ?  266 ILE A CG1   1 
ATOM   2010 C  CG2   . ILE A 1 273 ? 7.922   1.910   15.155  1.00 36.24  ?  266 ILE A CG2   1 
ATOM   2011 C  CD1   . ILE A 1 273 ? 10.797  1.325   15.776  1.00 34.62  ?  266 ILE A CD1   1 
ATOM   2012 N  N     . LEU A 1 274 ? 8.017   -0.368  19.250  1.00 41.73  ?  267 LEU A N     1 
ATOM   2013 C  CA    . LEU A 1 274 ? 8.422   -1.397  20.193  1.00 43.85  ?  267 LEU A CA    1 
ATOM   2014 C  C     . LEU A 1 274 ? 7.203   -2.095  20.799  1.00 47.26  ?  267 LEU A C     1 
ATOM   2015 O  O     . LEU A 1 274 ? 7.374   -3.152  21.411  1.00 49.80  ?  267 LEU A O     1 
ATOM   2016 C  CB    . LEU A 1 274 ? 9.243   -0.793  21.328  1.00 42.71  ?  267 LEU A CB    1 
ATOM   2017 C  CG    . LEU A 1 274 ? 10.547  -0.097  20.934  1.00 39.83  ?  267 LEU A CG    1 
ATOM   2018 C  CD1   . LEU A 1 274 ? 11.114  0.620   22.145  1.00 39.17  ?  267 LEU A CD1   1 
ATOM   2019 C  CD2   . LEU A 1 274 ? 11.599  -1.067  20.387  1.00 40.32  ?  267 LEU A CD2   1 
ATOM   2020 N  N     . GLU A 1 275 ? 6.022   -1.493  20.641  1.00 47.62  ?  268 GLU A N     1 
ATOM   2021 C  CA    . GLU A 1 275 ? 4.769   -1.983  21.211  1.00 51.13  ?  268 GLU A CA    1 
ATOM   2022 C  C     . GLU A 1 275 ? 3.932   -2.666  20.127  1.00 53.01  ?  268 GLU A C     1 
ATOM   2023 O  O     . GLU A 1 275 ? 3.333   -3.707  20.409  1.00 56.64  ?  268 GLU A O     1 
ATOM   2024 C  CB    . GLU A 1 275 ? 4.024   -0.861  21.932  1.00 50.99  ?  268 GLU A CB    1 
ATOM   2025 C  CG    . GLU A 1 275 ? 4.744   -0.434  23.210  1.00 50.37  ?  268 GLU A CG    1 
ATOM   2026 C  CD    . GLU A 1 275 ? 4.196   0.766   23.972  1.00 50.26  ?  268 GLU A CD    1 
ATOM   2027 O  OE1   . GLU A 1 275 ? 3.146   1.327   23.559  1.00 50.85  ?  268 GLU A OE1   1 
ATOM   2028 O  OE2   . GLU A 1 275 ? 4.827   1.152   24.980  1.00 49.86  ?  268 GLU A OE2   1 
ATOM   2029 N  N     . VAL A 1 276 ? 3.881   -2.116  18.896  1.00 50.97  ?  269 VAL A N     1 
ATOM   2030 C  CA    . VAL A 1 276 ? 2.913   -2.602  17.912  1.00 53.07  ?  269 VAL A CA    1 
ATOM   2031 C  C     . VAL A 1 276 ? 3.583   -3.031  16.608  1.00 52.05  ?  269 VAL A C     1 
ATOM   2032 O  O     . VAL A 1 276 ? 2.953   -3.631  15.731  1.00 54.13  ?  269 VAL A O     1 
ATOM   2033 C  CB    . VAL A 1 276 ? 1.757   -1.608  17.659  1.00 53.11  ?  269 VAL A CB    1 
ATOM   2034 C  CG1   . VAL A 1 276 ? 0.970   -1.288  18.914  1.00 55.04  ?  269 VAL A CG1   1 
ATOM   2035 C  CG2   . VAL A 1 276 ? 2.188   -0.300  16.998  1.00 49.38  ?  269 VAL A CG2   1 
ATOM   2036 N  N     . GLY A 1 277 ? 4.879   -2.806  16.502  1.00 49.37  ?  270 GLY A N     1 
ATOM   2037 C  CA    . GLY A 1 277 ? 5.593   -3.127  15.289  1.00 48.56  ?  270 GLY A CA    1 
ATOM   2038 C  C     . GLY A 1 277 ? 5.574   -1.928  14.340  1.00 45.81  ?  270 GLY A C     1 
ATOM   2039 O  O     . GLY A 1 277 ? 4.775   -0.999  14.509  1.00 45.19  ?  270 GLY A O     1 
ATOM   2040 N  N     . VAL A 1 278 ? 6.422   -2.013  13.319  1.00 44.72  ?  271 VAL A N     1 
ATOM   2041 C  CA    . VAL A 1 278 ? 6.652   -0.891  12.410  1.00 42.21  ?  271 VAL A CA    1 
ATOM   2042 C  C     . VAL A 1 278 ? 5.414   -0.624  11.569  1.00 43.37  ?  271 VAL A C     1 
ATOM   2043 O  O     . VAL A 1 278 ? 4.977   0.524   11.418  1.00 41.94  ?  271 VAL A O     1 
ATOM   2044 C  CB    . VAL A 1 278 ? 7.881   -1.126  11.511  1.00 41.38  ?  271 VAL A CB    1 
ATOM   2045 C  CG1   . VAL A 1 278 ? 8.008   -0.012  10.481  1.00 39.41  ?  271 VAL A CG1   1 
ATOM   2046 C  CG2   . VAL A 1 278 ? 9.158   -1.239  12.332  1.00 40.26  ?  271 VAL A CG2   1 
ATOM   2047 N  N     . GLN A 1 279 ? 4.850   -1.687  11.009  1.00 46.35  ?  272 GLN A N     1 
ATOM   2048 C  CA    . GLN A 1 279 ? 3.722   -1.509  10.067  1.00 47.83  ?  272 GLN A CA    1 
ATOM   2049 C  C     . GLN A 1 279 ? 2.558   -0.786  10.738  1.00 48.21  ?  272 GLN A C     1 
ATOM   2050 O  O     . GLN A 1 279 ? 2.021   0.141   10.150  1.00 47.54  ?  272 GLN A O     1 
ATOM   2051 C  CB    . GLN A 1 279 ? 3.287   -2.868  9.519   1.00 51.55  ?  272 GLN A CB    1 
ATOM   2052 C  CG    . GLN A 1 279 ? 2.058   -2.783  8.619   1.00 53.42  ?  272 GLN A CG    1 
ATOM   2053 C  CD    . GLN A 1 279 ? 1.562   -4.126  8.126   1.00 57.60  ?  272 GLN A CD    1 
ATOM   2054 O  OE1   . GLN A 1 279 ? 2.228   -4.826  7.359   1.00 58.73  ?  272 GLN A OE1   1 
ATOM   2055 N  NE2   . GLN A 1 279 ? 0.363   -4.489  8.552   1.00 60.31  ?  272 GLN A NE2   1 
ATOM   2056 N  N     . GLN A 1 280 ? 2.179   -1.226  11.926  1.00 49.66  ?  273 GLN A N     1 
ATOM   2057 C  CA    . GLN A 1 280 ? 1.019   -0.644  12.569  1.00 50.80  ?  273 GLN A CA    1 
ATOM   2058 C  C     . GLN A 1 280 ? 1.326   0.791   13.023  1.00 47.71  ?  273 GLN A C     1 
ATOM   2059 O  O     . GLN A 1 280 ? 0.456   1.660   12.967  1.00 48.06  ?  273 GLN A O     1 
ATOM   2060 C  CB    . GLN A 1 280 ? 0.596   -1.524  13.742  1.00 53.58  ?  273 GLN A CB    1 
ATOM   2061 C  CG    . GLN A 1 280 ? -0.516  -0.908  14.545  1.00 55.03  ?  273 GLN A CG    1 
ATOM   2062 C  CD    . GLN A 1 280 ? -1.871  -0.990  13.889  1.00 58.12  ?  273 GLN A CD    1 
ATOM   2063 O  OE1   . GLN A 1 280 ? -2.087  -1.735  12.935  1.00 59.86  ?  273 GLN A OE1   1 
ATOM   2064 N  NE2   . GLN A 1 280 ? -2.783  -0.165  14.365  1.00 59.03  ?  273 GLN A NE2   1 
ATOM   2065 N  N     . ALA A 1 281 ? 2.562   1.039   13.466  1.00 45.05  ?  274 ALA A N     1 
ATOM   2066 C  CA    . ALA A 1 281 ? 2.957   2.393   13.847  1.00 42.35  ?  274 ALA A CA    1 
ATOM   2067 C  C     . ALA A 1 281 ? 2.924   3.362   12.658  1.00 40.89  ?  274 ALA A C     1 
ATOM   2068 O  O     . ALA A 1 281 ? 2.326   4.423   12.739  1.00 40.66  ?  274 ALA A O     1 
ATOM   2069 C  CB    . ALA A 1 281 ? 4.304   2.351   14.510  1.00 40.31  ?  274 ALA A CB    1 
ATOM   2070 N  N     . LEU A 1 282 ? 3.458   2.956   11.522  1.00 40.51  ?  275 LEU A N     1 
ATOM   2071 C  CA    . LEU A 1 282 ? 3.580   3.820   10.340  1.00 39.32  ?  275 LEU A CA    1 
ATOM   2072 C  C     . LEU A 1 282 ? 2.224   4.154   9.709   1.00 41.30  ?  275 LEU A C     1 
ATOM   2073 O  O     . LEU A 1 282 ? 2.046   5.260   9.160   1.00 40.49  ?  275 LEU A O     1 
ATOM   2074 C  CB    . LEU A 1 282 ? 4.500   3.081   9.364   1.00 39.14  ?  275 LEU A CB    1 
ATOM   2075 C  CG    . LEU A 1 282 ? 4.930   3.819   8.103   1.00 38.05  ?  275 LEU A CG    1 
ATOM   2076 C  CD1   . LEU A 1 282 ? 5.598   5.135   8.437   1.00 35.51  ?  275 LEU A CD1   1 
ATOM   2077 C  CD2   . LEU A 1 282 ? 5.861   2.933   7.291   1.00 38.46  ?  275 LEU A CD2   1 
ATOM   2078 N  N     . GLN A 1 283 ? 1.260   3.228   9.858   1.00 44.20  ?  276 GLN A N     1 
ATOM   2079 C  CA    . GLN A 1 283 ? -0.094  3.340   9.326   1.00 46.82  ?  276 GLN A CA    1 
ATOM   2080 C  C     . GLN A 1 283 ? -0.788  4.566   9.928   1.00 46.68  ?  276 GLN A C     1 
ATOM   2081 O  O     . GLN A 1 283 ? -1.621  5.192   9.282   1.00 47.92  ?  276 GLN A O     1 
ATOM   2082 C  CB    . GLN A 1 283 ? -0.813  1.994   9.579   1.00 50.21  ?  276 GLN A CB    1 
ATOM   2083 C  CG    . GLN A 1 283 ? -2.310  2.068   9.871   1.00 53.46  ?  276 GLN A CG    1 
ATOM   2084 C  CD    . GLN A 1 283 ? -2.718  2.503   11.262  1.00 53.80  ?  276 GLN A CD    1 
ATOM   2085 O  OE1   . GLN A 1 283 ? -3.808  3.039   11.467  1.00 55.84  ?  276 GLN A OE1   1 
ATOM   2086 N  NE2   . GLN A 1 283 ? -1.853  2.298   12.242  1.00 52.12  ?  276 GLN A NE2   1 
ATOM   2087 N  N     . ALA A 1 284 ? -0.381  4.952   11.143  1.00 45.31  ?  277 ALA A N     1 
ATOM   2088 C  CA    . ALA A 1 284 ? -1.028  5.995   11.918  1.00 45.73  ?  277 ALA A CA    1 
ATOM   2089 C  C     . ALA A 1 284 ? -0.546  7.409   11.565  1.00 43.45  ?  277 ALA A C     1 
ATOM   2090 O  O     . ALA A 1 284 ? -1.039  8.377   12.141  1.00 43.96  ?  277 ALA A O     1 
ATOM   2091 C  CB    . ALA A 1 284 ? -0.780  5.720   13.376  1.00 45.72  ?  277 ALA A CB    1 
ATOM   2092 N  N     . VAL A 1 285 ? 0.464   7.551   10.704  1.00 41.21  ?  278 VAL A N     1 
ATOM   2093 C  CA    . VAL A 1 285 ? 0.919   8.892   10.350  1.00 39.50  ?  278 VAL A CA    1 
ATOM   2094 C  C     . VAL A 1 285 ? 0.866   9.063   8.839   1.00 39.76  ?  278 VAL A C     1 
ATOM   2095 O  O     . VAL A 1 285 ? 0.890   8.095   8.089   1.00 40.50  ?  278 VAL A O     1 
ATOM   2096 C  CB    . VAL A 1 285 ? 2.332   9.221   10.879  1.00 36.68  ?  278 VAL A CB    1 
ATOM   2097 C  CG1   . VAL A 1 285 ? 2.421   9.189   12.399  1.00 36.57  ?  278 VAL A CG1   1 
ATOM   2098 C  CG2   . VAL A 1 285 ? 3.390   8.334   10.240  1.00 35.45  ?  278 VAL A CG2   1 
ATOM   2099 N  N     . PHE A 1 286 ? 0.806   10.321  8.409   1.00 39.46  ?  279 PHE A N     1 
ATOM   2100 C  CA    . PHE A 1 286 ? 0.907   10.657  6.998   1.00 39.68  ?  279 PHE A CA    1 
ATOM   2101 C  C     . PHE A 1 286 ? 2.357   10.979  6.666   1.00 37.21  ?  279 PHE A C     1 
ATOM   2102 O  O     . PHE A 1 286 ? 2.993   11.736  7.392   1.00 35.69  ?  279 PHE A O     1 
ATOM   2103 C  CB    . PHE A 1 286 ? -0.038  11.806  6.650   1.00 41.40  ?  279 PHE A CB    1 
ATOM   2104 C  CG    . PHE A 1 286 ? 0.105   12.300  5.234   1.00 41.82  ?  279 PHE A CG    1 
ATOM   2105 C  CD1   . PHE A 1 286 ? -0.238  11.494  4.162   1.00 43.31  ?  279 PHE A CD1   1 
ATOM   2106 C  CD2   . PHE A 1 286 ? 0.629   13.553  4.960   1.00 41.03  ?  279 PHE A CD2   1 
ATOM   2107 C  CE1   . PHE A 1 286 ? -0.077  11.948  2.858   1.00 43.97  ?  279 PHE A CE1   1 
ATOM   2108 C  CE2   . PHE A 1 286 ? 0.776   14.006  3.649   1.00 41.77  ?  279 PHE A CE2   1 
ATOM   2109 C  CZ    . PHE A 1 286 ? 0.415   13.208  2.604   1.00 43.22  ?  279 PHE A CZ    1 
ATOM   2110 N  N     . TRP A 1 287 ? 2.849   10.365  5.599   1.00 37.22  ?  280 TRP A N     1 
ATOM   2111 C  CA    . TRP A 1 287 ? 4.168   10.606  5.044   1.00 35.60  ?  280 TRP A CA    1 
ATOM   2112 C  C     . TRP A 1 287 ? 3.978   10.880  3.557   1.00 37.00  ?  280 TRP A C     1 
ATOM   2113 O  O     . TRP A 1 287 ? 3.505   10.009  2.801   1.00 38.65  ?  280 TRP A O     1 
ATOM   2114 C  CB    . TRP A 1 287 ? 5.115   9.448   5.313   1.00 34.62  ?  280 TRP A CB    1 
ATOM   2115 C  CG    . TRP A 1 287 ? 6.471   9.554   4.665   1.00 33.53  ?  280 TRP A CG    1 
ATOM   2116 C  CD1   . TRP A 1 287 ? 7.271   10.674  4.663   1.00 32.33  ?  280 TRP A CD1   1 
ATOM   2117 C  CD2   . TRP A 1 287 ? 7.213   8.522   3.972   1.00 33.98  ?  280 TRP A CD2   1 
ATOM   2118 N  NE1   . TRP A 1 287 ? 8.436   10.413  3.988   1.00 32.04  ?  280 TRP A NE1   1 
ATOM   2119 C  CE2   . TRP A 1 287 ? 8.435   9.108   3.551   1.00 33.04  ?  280 TRP A CE2   1 
ATOM   2120 C  CE3   . TRP A 1 287 ? 6.975   7.178   3.655   1.00 35.45  ?  280 TRP A CE3   1 
ATOM   2121 C  CZ2   . TRP A 1 287 ? 9.402   8.389   2.855   1.00 33.54  ?  280 TRP A CZ2   1 
ATOM   2122 C  CZ3   . TRP A 1 287 ? 7.931   6.477   2.964   1.00 35.92  ?  280 TRP A CZ3   1 
ATOM   2123 C  CH2   . TRP A 1 287 ? 9.118   7.070   2.557   1.00 35.02  ?  280 TRP A CH2   1 
ATOM   2124 N  N     . ASP A 1 288 ? 4.276   12.121  3.170   1.00 36.73  ?  281 ASP A N     1 
ATOM   2125 C  CA    . ASP A 1 288 ? 4.118   12.557  1.777   1.00 38.31  ?  281 ASP A CA    1 
ATOM   2126 C  C     . ASP A 1 288 ? 5.332   12.081  0.985   1.00 37.81  ?  281 ASP A C     1 
ATOM   2127 O  O     . ASP A 1 288 ? 6.371   12.767  0.941   1.00 36.75  ?  281 ASP A O     1 
ATOM   2128 C  CB    . ASP A 1 288 ? 3.988   14.076  1.708   1.00 38.65  ?  281 ASP A CB    1 
ATOM   2129 C  CG    . ASP A 1 288 ? 3.543   14.622  0.355   1.00 40.90  ?  281 ASP A CG    1 
ATOM   2130 O  OD1   . ASP A 1 288 ? 3.639   13.894  -0.605  1.00 41.87  ?  281 ASP A OD1   1 
ATOM   2131 O  OD2   . ASP A 1 288 ? 3.057   15.780  0.317   1.00 41.98  ?  281 ASP A OD2   1 
ATOM   2132 N  N     . GLU A 1 289 ? 5.197   10.891  0.406   1.00 38.92  ?  282 GLU A N     1 
ATOM   2133 C  CA    . GLU A 1 289 ? 6.273   10.265  -0.348  1.00 39.03  ?  282 GLU A CA    1 
ATOM   2134 C  C     . GLU A 1 289 ? 6.576   11.033  -1.632  1.00 40.38  ?  282 GLU A C     1 
ATOM   2135 O  O     . GLU A 1 289 ? 7.727   11.033  -2.062  1.00 40.15  ?  282 GLU A O     1 
ATOM   2136 C  CB    . GLU A 1 289 ? 5.924   8.802   -0.596  1.00 40.43  ?  282 GLU A CB    1 
ATOM   2137 C  CG    . GLU A 1 289 ? 7.127   7.968   -0.952  1.00 40.40  ?  282 GLU A CG    1 
ATOM   2138 C  CD    . GLU A 1 289 ? 7.005   6.473   -0.664  1.00 41.30  ?  282 GLU A CD    1 
ATOM   2139 O  OE1   . GLU A 1 289 ? 8.035   5.813   -0.845  1.00 41.41  ?  282 GLU A OE1   1 
ATOM   2140 O  OE2   . GLU A 1 289 ? 5.943   5.993   -0.183  1.00 42.05  ?  282 GLU A OE2   1 
ATOM   2141 N  N     . GLU A 1 290 ? 5.574   11.686  -2.226  1.00 42.08  ?  283 GLU A N     1 
ATOM   2142 C  CA    . GLU A 1 290 ? 5.798   12.503  -3.403  1.00 43.68  ?  283 GLU A CA    1 
ATOM   2143 C  C     . GLU A 1 290 ? 6.712   13.684  -3.042  1.00 42.28  ?  283 GLU A C     1 
ATOM   2144 O  O     . GLU A 1 290 ? 7.652   13.984  -3.770  1.00 42.88  ?  283 GLU A O     1 
ATOM   2145 C  CB    . GLU A 1 290 ? 4.505   13.041  -4.004  1.00 46.00  ?  283 GLU A CB    1 
ATOM   2146 C  CG    . GLU A 1 290 ? 3.644   11.960  -4.617  1.00 48.16  ?  283 GLU A CG    1 
ATOM   2147 C  CD    . GLU A 1 290 ? 2.327   12.494  -5.159  1.00 50.74  ?  283 GLU A CD    1 
ATOM   2148 O  OE1   . GLU A 1 290 ? 1.958   13.633  -4.813  1.00 50.63  ?  283 GLU A OE1   1 
ATOM   2149 O  OE2   . GLU A 1 290 ? 1.698   11.768  -5.965  1.00 53.22  ?  283 GLU A OE2   1 
ATOM   2150 N  N     . ALA A 1 291 ? 6.407   14.336  -1.912  1.00 40.81  ?  284 ALA A N     1 
ATOM   2151 C  CA    . ALA A 1 291 ? 7.238   15.394  -1.373  1.00 39.59  ?  284 ALA A CA    1 
ATOM   2152 C  C     . ALA A 1 291 ? 8.655   14.913  -1.049  1.00 37.98  ?  284 ALA A C     1 
ATOM   2153 O  O     . ALA A 1 291 ? 9.618   15.619  -1.336  1.00 38.14  ?  284 ALA A O     1 
ATOM   2154 C  CB    . ALA A 1 291 ? 6.573   16.052  -0.186  1.00 38.72  ?  284 ALA A CB    1 
ATOM   2155 N  N     . PHE A 1 292 ? 8.785   13.729  -0.469  1.00 36.81  ?  285 PHE A N     1 
ATOM   2156 C  CA    . PHE A 1 292 ? 10.058  13.140  -0.101  1.00 35.58  ?  285 PHE A CA    1 
ATOM   2157 C  C     . PHE A 1 292 ? 10.964  12.975  -1.307  1.00 37.09  ?  285 PHE A C     1 
ATOM   2158 O  O     . PHE A 1 292 ? 12.115  13.392  -1.289  1.00 36.85  ?  285 PHE A O     1 
ATOM   2159 C  CB    . PHE A 1 292 ? 9.818   11.782  0.543   1.00 34.87  ?  285 PHE A CB    1 
ATOM   2160 C  CG    . PHE A 1 292 ? 11.046  10.977  0.834   1.00 34.15  ?  285 PHE A CG    1 
ATOM   2161 C  CD1   . PHE A 1 292 ? 11.852  11.263  1.918   1.00 32.42  ?  285 PHE A CD1   1 
ATOM   2162 C  CD2   . PHE A 1 292 ? 11.358  9.862   0.065   1.00 35.54  ?  285 PHE A CD2   1 
ATOM   2163 C  CE1   . PHE A 1 292 ? 12.970  10.483  2.191   1.00 32.10  ?  285 PHE A CE1   1 
ATOM   2164 C  CE2   . PHE A 1 292 ? 12.438  9.051   0.385   1.00 35.26  ?  285 PHE A CE2   1 
ATOM   2165 C  CZ    . PHE A 1 292 ? 13.262  9.378   1.423   1.00 33.55  ?  285 PHE A CZ    1 
ATOM   2166 N  N     . VAL A 1 293 ? 10.409  12.438  -2.399  1.00 39.08  ?  286 VAL A N     1 
ATOM   2167 C  CA    . VAL A 1 293 ? 11.209  12.260  -3.597  1.00 41.03  ?  286 VAL A CA    1 
ATOM   2168 C  C     . VAL A 1 293 ? 11.598  13.612  -4.188  1.00 42.07  ?  286 VAL A C     1 
ATOM   2169 O  O     . VAL A 1 293 ? 12.742  13.848  -4.599  1.00 42.86  ?  286 VAL A O     1 
ATOM   2170 C  CB    . VAL A 1 293 ? 10.482  11.376  -4.635  1.00 43.32  ?  286 VAL A CB    1 
ATOM   2171 C  CG1   . VAL A 1 293 ? 11.107  11.468  -6.009  1.00 45.99  ?  286 VAL A CG1   1 
ATOM   2172 C  CG2   . VAL A 1 293 ? 10.409  9.931   -4.159  1.00 42.91  ?  286 VAL A CG2   1 
ATOM   2173 N  N     . GLU A 1 294 ? 10.622  14.490  -4.289  1.00 42.57  ?  287 GLU A N     1 
ATOM   2174 C  CA    . GLU A 1 294 ? 10.803  15.768  -4.944  1.00 44.18  ?  287 GLU A CA    1 
ATOM   2175 C  C     . GLU A 1 294 ? 11.875  16.613  -4.247  1.00 43.04  ?  287 GLU A C     1 
ATOM   2176 O  O     . GLU A 1 294 ? 12.552  17.367  -4.917  1.00 44.77  ?  287 GLU A O     1 
ATOM   2177 C  CB    . GLU A 1 294 ? 9.480   16.525  -4.976  1.00 44.96  ?  287 GLU A CB    1 
ATOM   2178 C  CG    . GLU A 1 294 ? 9.550   17.853  -5.744  1.00 47.24  ?  287 GLU A CG    1 
ATOM   2179 C  CD    . GLU A 1 294 ? 8.204   18.344  -6.273  1.00 49.25  ?  287 GLU A CD    1 
ATOM   2180 O  OE1   . GLU A 1 294 ? 7.488   17.530  -6.895  1.00 50.39  ?  287 GLU A OE1   1 
ATOM   2181 O  OE2   . GLU A 1 294 ? 7.819   19.554  -6.047  1.00 50.01  ?  287 GLU A OE2   1 
ATOM   2182 N  N     . ARG A 1 295 ? 12.004  16.512  -2.914  1.00 40.51  ?  288 ARG A N     1 
ATOM   2183 C  CA    . ARG A 1 295 ? 12.978  17.328  -2.211  1.00 39.71  ?  288 ARG A CA    1 
ATOM   2184 C  C     . ARG A 1 295 ? 14.367  16.703  -2.298  1.00 39.67  ?  288 ARG A C     1 
ATOM   2185 O  O     . ARG A 1 295 ? 15.337  17.338  -1.866  1.00 39.55  ?  288 ARG A O     1 
ATOM   2186 C  CB    . ARG A 1 295 ? 12.638  17.552  -0.725  1.00 37.42  ?  288 ARG A CB    1 
ATOM   2187 C  CG    . ARG A 1 295 ? 12.694  16.310  0.156   1.00 35.38  ?  288 ARG A CG    1 
ATOM   2188 C  CD    . ARG A 1 295 ? 12.518  16.697  1.618   1.00 33.58  ?  288 ARG A CD    1 
ATOM   2189 N  NE    . ARG A 1 295 ? 12.335  15.606  2.583   1.00 31.90  ?  288 ARG A NE    1 
ATOM   2190 C  CZ    . ARG A 1 295 ? 13.276  14.808  3.056   1.00 30.95  ?  288 ARG A CZ    1 
ATOM   2191 N  NH1   . ARG A 1 295 ? 14.534  14.931  2.686   1.00 31.45  ?  288 ARG A NH1   1 
ATOM   2192 N  NH2   . ARG A 1 295 ? 12.957  13.885  3.943   1.00 29.78  ?  288 ARG A NH2   1 
ATOM   2193 N  N     . GLY A 1 296 ? 14.478  15.480  -2.832  1.00 40.11  ?  289 GLY A N     1 
ATOM   2194 C  CA    . GLY A 1 296 ? 15.754  14.794  -2.975  1.00 40.59  ?  289 GLY A CA    1 
ATOM   2195 C  C     . GLY A 1 296 ? 16.070  13.818  -1.840  1.00 38.45  ?  289 GLY A C     1 
ATOM   2196 O  O     . GLY A 1 296 ? 17.243  13.555  -1.540  1.00 38.48  ?  289 GLY A O     1 
ATOM   2197 N  N     . GLY A 1 297 ? 15.023  13.253  -1.223  1.00 36.96  ?  290 GLY A N     1 
ATOM   2198 C  CA    . GLY A 1 297 ? 15.197  12.370  -0.085  1.00 35.16  ?  290 GLY A CA    1 
ATOM   2199 C  C     . GLY A 1 297 ? 15.990  11.102  -0.394  1.00 36.12  ?  290 GLY A C     1 
ATOM   2200 O  O     . GLY A 1 297 ? 16.531  10.519  0.539   1.00 35.03  ?  290 GLY A O     1 
ATOM   2201 N  N     . ILE A 1 298 ? 15.978  10.627  -1.666  1.00 38.41  ?  291 ILE A N     1 
ATOM   2202 C  CA    . ILE A 1 298 ? 16.830  9.514   -2.106  1.00 40.06  ?  291 ILE A CA    1 
ATOM   2203 C  C     . ILE A 1 298 ? 18.016  10.121  -2.848  1.00 41.95  ?  291 ILE A C     1 
ATOM   2204 O  O     . ILE A 1 298 ? 17.811  10.944  -3.741  1.00 43.31  ?  291 ILE A O     1 
ATOM   2205 C  CB    . ILE A 1 298 ? 16.084  8.532   -3.033  1.00 41.99  ?  291 ILE A CB    1 
ATOM   2206 C  CG1   . ILE A 1 298 ? 14.776  8.030   -2.424  1.00 40.70  ?  291 ILE A CG1   1 
ATOM   2207 C  CG2   . ILE A 1 298 ? 16.963  7.352   -3.455  1.00 44.12  ?  291 ILE A CG2   1 
ATOM   2208 C  CD1   . ILE A 1 298 ? 14.979  7.207   -1.232  1.00 39.26  ?  291 ILE A CD1   1 
ATOM   2209 N  N     . TYR A 1 299 ? 19.231  9.749   -2.424  1.00 42.25  ?  292 TYR A N     1 
ATOM   2210 C  CA    . TYR A 1 299 ? 20.475  10.236  -2.988  1.00 44.37  ?  292 TYR A CA    1 
ATOM   2211 C  C     . TYR A 1 299 ? 21.596  9.238   -2.682  1.00 45.47  ?  292 TYR A C     1 
ATOM   2212 O  O     . TYR A 1 299 ? 21.364  8.242   -2.010  1.00 44.44  ?  292 TYR A O     1 
ATOM   2213 C  CB    . TYR A 1 299 ? 20.736  11.649  -2.459  1.00 43.20  ?  292 TYR A CB    1 
ATOM   2214 C  CG    . TYR A 1 299 ? 21.031  11.851  -0.968  1.00 40.67  ?  292 TYR A CG    1 
ATOM   2215 C  CD1   . TYR A 1 299 ? 20.014  11.937  -0.020  1.00 37.98  ?  292 TYR A CD1   1 
ATOM   2216 C  CD2   . TYR A 1 299 ? 22.337  11.958  -0.494  1.00 41.33  ?  292 TYR A CD2   1 
ATOM   2217 C  CE1   . TYR A 1 299 ? 20.276  12.134  1.330   1.00 36.02  ?  292 TYR A CE1   1 
ATOM   2218 C  CE2   . TYR A 1 299 ? 22.608  12.155  0.861   1.00 39.31  ?  292 TYR A CE2   1 
ATOM   2219 C  CZ    . TYR A 1 299 ? 21.578  12.270  1.781   1.00 36.64  ?  292 TYR A CZ    1 
ATOM   2220 O  OH    . TYR A 1 299 ? 21.825  12.531  3.105   1.00 34.97  ?  292 TYR A OH    1 
ATOM   2221 N  N     . ASP A 1 300 ? 22.816  9.512   -3.185  1.00 47.95  ?  293 ASP A N     1 
ATOM   2222 C  CA    . ASP A 1 300 ? 23.964  8.649   -2.925  1.00 49.54  ?  293 ASP A CA    1 
ATOM   2223 C  C     . ASP A 1 300 ? 24.512  8.952   -1.533  1.00 47.36  ?  293 ASP A C     1 
ATOM   2224 O  O     . ASP A 1 300 ? 25.364  9.831   -1.352  1.00 47.97  ?  293 ASP A O     1 
ATOM   2225 C  CB    . ASP A 1 300 ? 25.070  8.810   -3.972  1.00 53.53  ?  293 ASP A CB    1 
ATOM   2226 C  CG    . ASP A 1 300 ? 24.580  8.617   -5.401  1.00 56.15  ?  293 ASP A CG    1 
ATOM   2227 O  OD1   . ASP A 1 300 ? 23.860  7.622   -5.652  1.00 56.26  ?  293 ASP A OD1   1 
ATOM   2228 O  OD2   . ASP A 1 300 ? 24.917  9.466   -6.252  1.00 58.34  ?  293 ASP A OD2   1 
ATOM   2229 N  N     . TRP A 1 301 ? 24.019  8.195   -0.558  1.00 45.20  ?  294 TRP A N     1 
ATOM   2230 C  CA    . TRP A 1 301 ? 24.147  8.592   0.838   1.00 42.65  ?  294 TRP A CA    1 
ATOM   2231 C  C     . TRP A 1 301 ? 25.234  7.800   1.574   1.00 43.59  ?  294 TRP A C     1 
ATOM   2232 O  O     . TRP A 1 301 ? 25.289  7.797   2.804   1.00 41.72  ?  294 TRP A O     1 
ATOM   2233 C  CB    . TRP A 1 301 ? 22.772  8.465   1.498   1.00 39.76  ?  294 TRP A CB    1 
ATOM   2234 C  CG    . TRP A 1 301 ? 22.010  7.212   1.174   1.00 40.24  ?  294 TRP A CG    1 
ATOM   2235 C  CD1   . TRP A 1 301 ? 22.473  5.940   0.988   1.00 42.21  ?  294 TRP A CD1   1 
ATOM   2236 C  CD2   . TRP A 1 301 ? 20.573  7.128   1.100   1.00 38.89  ?  294 TRP A CD2   1 
ATOM   2237 N  NE1   . TRP A 1 301 ? 21.421  5.078   0.824   1.00 42.16  ?  294 TRP A NE1   1 
ATOM   2238 C  CE2   . TRP A 1 301 ? 20.247  5.775   0.880   1.00 40.16  ?  294 TRP A CE2   1 
ATOM   2239 C  CE3   . TRP A 1 301 ? 19.544  8.064   1.216   1.00 37.10  ?  294 TRP A CE3   1 
ATOM   2240 C  CZ2   . TRP A 1 301 ? 18.928  5.352   0.759   1.00 39.68  ?  294 TRP A CZ2   1 
ATOM   2241 C  CZ3   . TRP A 1 301 ? 18.243  7.636   1.133   1.00 36.57  ?  294 TRP A CZ3   1 
ATOM   2242 C  CH2   . TRP A 1 301 ? 17.939  6.298   0.924   1.00 37.81  ?  294 TRP A CH2   1 
ATOM   2243 N  N     . ASN A 1 302 ? 26.119  7.135   0.810   1.00 46.86  ?  295 ASN A N     1 
ATOM   2244 C  CA    . ASN A 1 302 ? 27.350  6.564   1.356   1.00 48.60  ?  295 ASN A CA    1 
ATOM   2245 C  C     . ASN A 1 302 ? 28.499  6.824   0.376   1.00 52.42  ?  295 ASN A C     1 
ATOM   2246 O  O     . ASN A 1 302 ? 28.181  6.777   -0.833  1.00 54.15  ?  295 ASN A O     1 
ATOM   2247 C  CB    . ASN A 1 302 ? 27.237  5.067   1.650   1.00 49.35  ?  295 ASN A CB    1 
ATOM   2248 C  CG    . ASN A 1 302 ? 26.617  4.272   0.518   1.00 51.13  ?  295 ASN A CG    1 
ATOM   2249 O  OD1   . ASN A 1 302 ? 26.935  4.487   -0.649  1.00 53.66  ?  295 ASN A OD1   1 
ATOM   2250 N  ND2   . ASN A 1 302 ? 25.713  3.363   0.846   1.00 50.12  ?  295 ASN A ND2   1 
ATOM   2251 N  N     . GLY B 1 24  ? -2.116  34.469  -34.714 1.00 57.73  ?  17  GLY B N     1 
ATOM   2252 C  CA    . GLY B 1 24  ? -3.380  34.092  -34.053 1.00 56.97  ?  17  GLY B CA    1 
ATOM   2253 C  C     . GLY B 1 24  ? -3.618  32.582  -34.077 1.00 54.15  ?  17  GLY B C     1 
ATOM   2254 O  O     . GLY B 1 24  ? -4.752  32.130  -34.177 1.00 54.68  ?  17  GLY B O     1 
ATOM   2255 N  N     . GLN B 1 25  ? -2.544  31.788  -33.953 1.00 51.42  ?  18  GLN B N     1 
ATOM   2256 C  CA    . GLN B 1 25  ? -2.656  30.340  -33.919 1.00 48.93  ?  18  GLN B CA    1 
ATOM   2257 C  C     . GLN B 1 25  ? -3.320  29.905  -32.615 1.00 47.01  ?  18  GLN B C     1 
ATOM   2258 O  O     . GLN B 1 25  ? -3.191  30.585  -31.593 1.00 46.64  ?  18  GLN B O     1 
ATOM   2259 C  CB    . GLN B 1 25  ? -1.263  29.717  -34.071 1.00 47.01  ?  18  GLN B CB    1 
ATOM   2260 C  CG    . GLN B 1 25  ? -0.619  30.009  -35.428 1.00 49.23  ?  18  GLN B CG    1 
ATOM   2261 C  CD    . GLN B 1 25  ? 0.776   29.439  -35.579 1.00 47.81  ?  18  GLN B CD    1 
ATOM   2262 O  OE1   . GLN B 1 25  ? 1.720   29.860  -34.923 1.00 47.02  ?  18  GLN B OE1   1 
ATOM   2263 N  NE2   . GLN B 1 25  ? 0.931   28.499  -36.492 1.00 47.91  ?  18  GLN B NE2   1 
ATOM   2264 N  N     . VAL B 1 26  ? -4.028  28.774  -32.674 1.00 46.15  ?  19  VAL B N     1 
ATOM   2265 C  CA    . VAL B 1 26  ? -4.686  28.185  -31.527 1.00 44.65  ?  19  VAL B CA    1 
ATOM   2266 C  C     . VAL B 1 26  ? -3.778  27.098  -30.975 1.00 41.57  ?  19  VAL B C     1 
ATOM   2267 O  O     . VAL B 1 26  ? -3.590  26.085  -31.641 1.00 41.01  ?  19  VAL B O     1 
ATOM   2268 C  CB    . VAL B 1 26  ? -6.061  27.607  -31.896 1.00 46.17  ?  19  VAL B CB    1 
ATOM   2269 C  CG1   . VAL B 1 26  ? -6.699  26.806  -30.758 1.00 44.84  ?  19  VAL B CG1   1 
ATOM   2270 C  CG2   . VAL B 1 26  ? -6.997  28.713  -32.364 1.00 49.59  ?  19  VAL B CG2   1 
ATOM   2271 N  N     . PRO B 1 27  ? -3.235  27.267  -29.754 1.00 39.85  ?  20  PRO B N     1 
ATOM   2272 C  CA    . PRO B 1 27  ? -2.288  26.288  -29.214 1.00 37.26  ?  20  PRO B CA    1 
ATOM   2273 C  C     . PRO B 1 27  ? -2.977  25.012  -28.745 1.00 36.26  ?  20  PRO B C     1 
ATOM   2274 O  O     . PRO B 1 27  ? -3.112  24.758  -27.557 1.00 35.20  ?  20  PRO B O     1 
ATOM   2275 C  CB    . PRO B 1 27  ? -1.625  27.101  -28.098 1.00 36.55  ?  20  PRO B CB    1 
ATOM   2276 C  CG    . PRO B 1 27  ? -2.742  27.958  -27.576 1.00 38.22  ?  20  PRO B CG    1 
ATOM   2277 C  CD    . PRO B 1 27  ? -3.461  28.392  -28.831 1.00 40.62  ?  20  PRO B CD    1 
ATOM   2278 N  N     . VAL B 1 28  ? -3.350  24.139  -29.682 1.00 36.81  ?  21  VAL B N     1 
ATOM   2279 C  CA    . VAL B 1 28  ? -4.237  23.049  -29.350 1.00 36.77  ?  21  VAL B CA    1 
ATOM   2280 C  C     . VAL B 1 28  ? -3.544  21.976  -28.507 1.00 34.61  ?  21  VAL B C     1 
ATOM   2281 O  O     . VAL B 1 28  ? -4.206  21.341  -27.691 1.00 34.50  ?  21  VAL B O     1 
ATOM   2282 C  CB    . VAL B 1 28  ? -4.845  22.411  -30.608 1.00 38.42  ?  21  VAL B CB    1 
ATOM   2283 C  CG1   . VAL B 1 28  ? -3.751  21.858  -31.526 1.00 37.79  ?  21  VAL B CG1   1 
ATOM   2284 C  CG2   . VAL B 1 28  ? -5.835  21.335  -30.235 1.00 38.90  ?  21  VAL B CG2   1 
ATOM   2285 N  N     . SER B 1 29  ? -2.226  21.775  -28.745 1.00 33.30  ?  22  SER B N     1 
ATOM   2286 C  CA    . SER B 1 29  ? -1.462  20.717  -28.102 1.00 31.64  ?  22  SER B CA    1 
ATOM   2287 C  C     . SER B 1 29  ? -0.083  21.239  -27.697 1.00 30.39  ?  22  SER B C     1 
ATOM   2288 O  O     . SER B 1 29  ? 0.703   21.642  -28.553 1.00 30.76  ?  22  SER B O     1 
ATOM   2289 C  CB    . SER B 1 29  ? -1.346  19.525  -29.012 1.00 32.00  ?  22  SER B CB    1 
ATOM   2290 O  OG    . SER B 1 29  ? -0.605  18.503  -28.349 1.00 30.71  ?  22  SER B OG    1 
ATOM   2291 N  N     . VAL B 1 30  ? 0.203   21.279  -26.376 1.00 29.28  ?  23  VAL B N     1 
ATOM   2292 C  CA    . VAL B 1 30  ? 1.342   22.000  -25.865 1.00 28.59  ?  23  VAL B CA    1 
ATOM   2293 C  C     . VAL B 1 30  ? 2.188   21.084  -24.978 1.00 27.29  ?  23  VAL B C     1 
ATOM   2294 O  O     . VAL B 1 30  ? 1.655   20.345  -24.162 1.00 26.95  ?  23  VAL B O     1 
ATOM   2295 C  CB    . VAL B 1 30  ? 0.877   23.205  -25.030 1.00 29.08  ?  23  VAL B CB    1 
ATOM   2296 C  CG1   . VAL B 1 30  ? 2.023   23.917  -24.367 1.00 28.65  ?  23  VAL B CG1   1 
ATOM   2297 C  CG2   . VAL B 1 30  ? 0.025   24.176  -25.854 1.00 30.77  ?  23  VAL B CG2   1 
ATOM   2298 N  N     . ASN B 1 31  ? 3.497   21.207  -25.162 1.00 26.98  ?  24  ASN B N     1 
ATOM   2299 C  CA    . ASN B 1 31  ? 4.494   20.572  -24.317 1.00 26.13  ?  24  ASN B CA    1 
ATOM   2300 C  C     . ASN B 1 31  ? 4.956   21.571  -23.272 1.00 26.05  ?  24  ASN B C     1 
ATOM   2301 O  O     . ASN B 1 31  ? 5.519   22.607  -23.617 1.00 26.69  ?  24  ASN B O     1 
ATOM   2302 C  CB    . ASN B 1 31  ? 5.691   20.045  -25.130 1.00 26.31  ?  24  ASN B CB    1 
ATOM   2303 C  CG    . ASN B 1 31  ? 5.393   18.689  -25.725 1.00 26.41  ?  24  ASN B CG    1 
ATOM   2304 O  OD1   . ASN B 1 31  ? 5.787   17.695  -25.148 1.00 26.06  ?  24  ASN B OD1   1 
ATOM   2305 N  ND2   . ASN B 1 31  ? 4.612   18.634  -26.783 1.00 27.14  ?  24  ASN B ND2   1 
ATOM   2306 N  N     . TYR B 1 32  ? 4.832   21.191  -22.010 1.00 25.55  ?  25  TYR B N     1 
ATOM   2307 C  CA    . TYR B 1 32  ? 5.356   21.987  -20.917 1.00 25.68  ?  25  TYR B CA    1 
ATOM   2308 C  C     . TYR B 1 32  ? 6.573   21.264  -20.338 1.00 25.36  ?  25  TYR B C     1 
ATOM   2309 O  O     . TYR B 1 32  ? 6.435   20.335  -19.576 1.00 25.05  ?  25  TYR B O     1 
ATOM   2310 C  CB    . TYR B 1 32  ? 4.229   22.262  -19.910 1.00 25.91  ?  25  TYR B CB    1 
ATOM   2311 C  CG    . TYR B 1 32  ? 4.555   23.051  -18.653 1.00 26.38  ?  25  TYR B CG    1 
ATOM   2312 C  CD1   . TYR B 1 32  ? 5.640   23.912  -18.555 1.00 26.86  ?  25  TYR B CD1   1 
ATOM   2313 C  CD2   . TYR B 1 32  ? 3.773   22.888  -17.509 1.00 26.70  ?  25  TYR B CD2   1 
ATOM   2314 C  CE1   . TYR B 1 32  ? 5.897   24.613  -17.377 1.00 27.61  ?  25  TYR B CE1   1 
ATOM   2315 C  CE2   . TYR B 1 32  ? 4.034   23.575  -16.327 1.00 27.42  ?  25  TYR B CE2   1 
ATOM   2316 C  CZ    . TYR B 1 32  ? 5.116   24.432  -16.260 1.00 27.86  ?  25  TYR B CZ    1 
ATOM   2317 O  OH    . TYR B 1 32  ? 5.431   25.139  -15.114 1.00 28.89  ?  25  TYR B OH    1 
ATOM   2318 N  N     . HIS B 1 33  ? 7.768   21.765  -20.690 1.00 25.82  ?  26  HIS B N     1 
ATOM   2319 C  CA    . HIS B 1 33  ? 9.023   21.279  -20.143 1.00 26.00  ?  26  HIS B CA    1 
ATOM   2320 C  C     . HIS B 1 33  ? 9.251   21.986  -18.810 1.00 26.44  ?  26  HIS B C     1 
ATOM   2321 O  O     . HIS B 1 33  ? 9.938   22.995  -18.732 1.00 27.36  ?  26  HIS B O     1 
ATOM   2322 C  CB    . HIS B 1 33  ? 10.158  21.490  -21.163 1.00 26.78  ?  26  HIS B CB    1 
ATOM   2323 C  CG    . HIS B 1 33  ? 10.029  20.670  -22.383 1.00 26.65  ?  26  HIS B CG    1 
ATOM   2324 N  ND1   . HIS B 1 33  ? 10.875  19.601  -22.651 1.00 26.95  ?  26  HIS B ND1   1 
ATOM   2325 C  CD2   . HIS B 1 33  ? 9.107   20.667  -23.358 1.00 26.50  ?  26  HIS B CD2   1 
ATOM   2326 C  CE1   . HIS B 1 33  ? 10.493  19.038  -23.793 1.00 27.03  ?  26  HIS B CE1   1 
ATOM   2327 N  NE2   . HIS B 1 33  ? 9.430   19.686  -24.251 1.00 26.75  ?  26  HIS B NE2   1 
ATOM   2328 N  N     . PHE B 1 34  ? 8.582   21.505  -17.765 1.00 26.11  ?  27  PHE B N     1 
ATOM   2329 C  CA    . PHE B 1 34  ? 8.437   22.316  -16.544 1.00 26.76  ?  27  PHE B CA    1 
ATOM   2330 C  C     . PHE B 1 34  ? 9.684   22.368  -15.658 1.00 27.62  ?  27  PHE B C     1 
ATOM   2331 O  O     . PHE B 1 34  ? 9.770   23.198  -14.729 1.00 28.57  ?  27  PHE B O     1 
ATOM   2332 C  CB    . PHE B 1 34  ? 7.226   21.832  -15.766 1.00 26.55  ?  27  PHE B CB    1 
ATOM   2333 C  CG    . PHE B 1 34  ? 7.370   20.488  -15.099 1.00 26.45  ?  27  PHE B CG    1 
ATOM   2334 C  CD1   . PHE B 1 34  ? 7.972   20.374  -13.856 1.00 27.25  ?  27  PHE B CD1   1 
ATOM   2335 C  CD2   . PHE B 1 34  ? 6.919   19.334  -15.727 1.00 25.90  ?  27  PHE B CD2   1 
ATOM   2336 C  CE1   . PHE B 1 34  ? 8.067   19.149  -13.206 1.00 27.56  ?  27  PHE B CE1   1 
ATOM   2337 C  CE2   . PHE B 1 34  ? 7.024   18.101  -15.086 1.00 26.23  ?  27  PHE B CE2   1 
ATOM   2338 C  CZ    . PHE B 1 34  ? 7.591   18.007  -13.836 1.00 27.07  ?  27  PHE B CZ    1 
ATOM   2339 N  N     A SER B 1 35  ? 10.654  21.487  -15.946 0.54 27.62  ?  28  SER B N     1 
ATOM   2340 N  N     B SER B 1 35  ? 10.628  21.455  -15.910 0.46 27.61  ?  28  SER B N     1 
ATOM   2341 C  CA    A SER B 1 35  ? 11.918  21.403  -15.232 0.54 28.75  ?  28  SER B CA    1 
ATOM   2342 C  CA    B SER B 1 35  ? 11.952  21.523  -15.319 0.46 28.79  ?  28  SER B CA    1 
ATOM   2343 C  C     A SER B 1 35  ? 12.989  20.882  -16.188 0.54 29.07  ?  28  SER B C     1 
ATOM   2344 C  C     B SER B 1 35  ? 12.988  21.024  -16.312 0.46 29.08  ?  28  SER B C     1 
ATOM   2345 O  O     A SER B 1 35  ? 12.653  20.073  -17.048 0.54 28.27  ?  28  SER B O     1 
ATOM   2346 O  O     B SER B 1 35  ? 12.650  20.381  -17.298 0.46 28.29  ?  28  SER B O     1 
ATOM   2347 C  CB    A SER B 1 35  ? 11.791  20.516  -14.026 0.54 28.98  ?  28  SER B CB    1 
ATOM   2348 C  CB    B SER B 1 35  ? 12.059  20.747  -14.054 0.46 29.24  ?  28  SER B CB    1 
ATOM   2349 O  OG    A SER B 1 35  ? 11.461  19.179  -14.408 0.54 28.29  ?  28  SER B OG    1 
ATOM   2350 O  OG    B SER B 1 35  ? 13.426  20.597  -13.688 0.46 30.58  ?  28  SER B OG    1 
ATOM   2351 N  N     . ARG B 1 36  ? 14.251  21.323  -16.006 1.00 30.56  ?  29  ARG B N     1 
ATOM   2352 C  CA    . ARG B 1 36  ? 15.367  20.878  -16.819 1.00 31.44  ?  29  ARG B CA    1 
ATOM   2353 C  C     . ARG B 1 36  ? 16.218  19.834  -16.079 1.00 32.42  ?  29  ARG B C     1 
ATOM   2354 O  O     . ARG B 1 36  ? 17.117  19.272  -16.703 1.00 33.37  ?  29  ARG B O     1 
ATOM   2355 C  CB    . ARG B 1 36  ? 16.213  22.093  -17.238 1.00 33.02  ?  29  ARG B CB    1 
ATOM   2356 C  CG    . ARG B 1 36  ? 15.616  22.910  -18.378 1.00 32.58  ?  29  ARG B CG    1 
ATOM   2357 C  CD    . ARG B 1 36  ? 16.487  24.061  -18.856 1.00 34.63  ?  29  ARG B CD    1 
ATOM   2358 N  NE    . ARG B 1 36  ? 15.892  24.775  -19.979 1.00 34.51  ?  29  ARG B NE    1 
ATOM   2359 C  CZ    . ARG B 1 36  ? 16.191  24.570  -21.254 1.00 35.00  ?  29  ARG B CZ    1 
ATOM   2360 N  NH1   . ARG B 1 36  ? 16.981  23.565  -21.611 1.00 35.40  ?  29  ARG B NH1   1 
ATOM   2361 N  NH2   . ARG B 1 36  ? 15.663  25.336  -22.187 1.00 35.31  ?  29  ARG B NH2   1 
ATOM   2362 N  N     . LYS B 1 37  ? 15.946  19.515  -14.801 1.00 32.52  ?  30  LYS B N     1 
ATOM   2363 C  CA    . LYS B 1 37  ? 16.782  18.552  -14.070 1.00 33.89  ?  30  LYS B CA    1 
ATOM   2364 C  C     . LYS B 1 37  ? 16.613  17.145  -14.661 1.00 33.40  ?  30  LYS B C     1 
ATOM   2365 O  O     . LYS B 1 37  ? 15.528  16.764  -15.036 1.00 31.89  ?  30  LYS B O     1 
ATOM   2366 C  CB    . LYS B 1 37  ? 16.465  18.614  -12.572 1.00 34.42  ?  30  LYS B CB    1 
ATOM   2367 C  CG    . LYS B 1 37  ? 17.427  17.833  -11.689 1.00 36.42  ?  30  LYS B CG    1 
ATOM   2368 C  CD    . LYS B 1 37  ? 17.399  18.154  -10.219 1.00 37.67  ?  30  LYS B CD    1 
ATOM   2369 C  CE    . LYS B 1 37  ? 16.153  17.642  -9.526  1.00 36.76  ?  30  LYS B CE    1 
ATOM   2370 N  NZ    . LYS B 1 37  ? 16.001  18.232  -8.180  1.00 38.05  ?  30  LYS B NZ    1 
ATOM   2371 N  N     . CYS B 1 38  ? 17.688  16.340  -14.772 1.00 35.01  ?  31  CYS B N     1 
ATOM   2372 C  CA    . CYS B 1 38  ? 17.506  14.946  -15.117 1.00 35.02  ?  31  CYS B CA    1 
ATOM   2373 C  C     . CYS B 1 38  ? 18.526  14.020  -14.443 1.00 37.34  ?  31  CYS B C     1 
ATOM   2374 O  O     . CYS B 1 38  ? 19.646  14.434  -14.225 1.00 39.10  ?  31  CYS B O     1 
ATOM   2375 C  CB    . CYS B 1 38  ? 17.722  14.798  -16.608 1.00 34.82  ?  31  CYS B CB    1 
ATOM   2376 S  SG    . CYS B 1 38  ? 17.276  13.130  -17.130 1.00 34.89  ?  31  CYS B SG    1 
ATOM   2377 N  N     . ASN B 1 39  ? 18.134  12.759  -14.276 1.00 37.61  ?  32  ASN B N     1 
ATOM   2378 C  CA    . ASN B 1 39  ? 18.910  11.726  -13.597 1.00 40.03  ?  32  ASN B CA    1 
ATOM   2379 C  C     . ASN B 1 39  ? 19.747  10.891  -14.573 1.00 41.58  ?  32  ASN B C     1 
ATOM   2380 O  O     . ASN B 1 39  ? 20.398  9.931   -14.139 1.00 43.92  ?  32  ASN B O     1 
ATOM   2381 C  CB    . ASN B 1 39  ? 17.992  10.837  -12.739 1.00 40.05  ?  32  ASN B CB    1 
ATOM   2382 C  CG    . ASN B 1 39  ? 16.927  10.051  -13.492 1.00 38.84  ?  32  ASN B CG    1 
ATOM   2383 O  OD1   . ASN B 1 39  ? 16.280  10.559  -14.396 1.00 36.89  ?  32  ASN B OD1   1 
ATOM   2384 N  ND2   . ASN B 1 39  ? 16.701  8.805   -13.109 1.00 40.29  ?  32  ASN B ND2   1 
ATOM   2385 N  N     . LYS B 1 40  ? 19.761  11.250  -15.862 1.00 40.66  ?  33  LYS B N     1 
ATOM   2386 C  CA    . LYS B 1 40  ? 20.411  10.450  -16.900 1.00 42.19  ?  33  LYS B CA    1 
ATOM   2387 C  C     . LYS B 1 40  ? 21.356  11.306  -17.740 1.00 43.00  ?  33  LYS B C     1 
ATOM   2388 O  O     . LYS B 1 40  ? 21.522  12.495  -17.459 1.00 42.48  ?  33  LYS B O     1 
ATOM   2389 C  CB    . LYS B 1 40  ? 19.342  9.810   -17.786 1.00 40.75  ?  33  LYS B CB    1 
ATOM   2390 C  CG    . LYS B 1 40  ? 18.442  8.773   -17.135 1.00 40.64  ?  33  LYS B CG    1 
ATOM   2391 C  CD    . LYS B 1 40  ? 19.178  7.702   -16.332 1.00 43.46  ?  33  LYS B CD    1 
ATOM   2392 C  CE    . LYS B 1 40  ? 18.251  6.660   -15.746 1.00 43.77  ?  33  LYS B CE    1 
ATOM   2393 N  NZ    . LYS B 1 40  ? 17.994  5.561   -16.706 1.00 44.71  ?  33  LYS B NZ    1 
ATOM   2394 N  N     . GLU B 1 41  ? 22.008  10.690  -18.749 1.00 44.72  ?  34  GLU B N     1 
ATOM   2395 C  CA    . GLU B 1 41  ? 23.069  11.351  -19.502 1.00 46.39  ?  34  GLU B CA    1 
ATOM   2396 C  C     . GLU B 1 41  ? 22.980  11.095  -21.014 1.00 46.56  ?  34  GLU B C     1 
ATOM   2397 O  O     . GLU B 1 41  ? 24.015  10.955  -21.686 1.00 49.18  ?  34  GLU B O     1 
ATOM   2398 C  CB    . GLU B 1 41  ? 24.417  10.854  -18.952 1.00 49.89  ?  34  GLU B CB    1 
ATOM   2399 C  CG    . GLU B 1 41  ? 24.602  11.081  -17.454 1.00 50.30  ?  34  GLU B CG    1 
ATOM   2400 C  CD    . GLU B 1 41  ? 25.335  12.361  -17.085 1.00 51.19  ?  34  GLU B CD    1 
ATOM   2401 O  OE1   . GLU B 1 41  ? 26.540  12.267  -16.766 1.00 54.42  ?  34  GLU B OE1   1 
ATOM   2402 O  OE2   . GLU B 1 41  ? 24.702  13.443  -17.094 1.00 48.99  ?  34  GLU B OE2   1 
ATOM   2403 N  N     . CYS B 1 42  ? 21.763  11.066  -21.592 1.00 44.11  ?  35  CYS B N     1 
ATOM   2404 C  CA    . CYS B 1 42  ? 21.604  10.784  -23.015 1.00 44.46  ?  35  CYS B CA    1 
ATOM   2405 C  C     . CYS B 1 42  ? 22.473  11.718  -23.848 1.00 45.92  ?  35  CYS B C     1 
ATOM   2406 O  O     . CYS B 1 42  ? 22.373  12.932  -23.722 1.00 44.87  ?  35  CYS B O     1 
ATOM   2407 C  CB    . CYS B 1 42  ? 20.146  10.902  -23.423 1.00 41.68  ?  35  CYS B CB    1 
ATOM   2408 S  SG    . CYS B 1 42  ? 19.056  9.913   -22.381 1.00 40.31  ?  35  CYS B SG    1 
ATOM   2409 N  N     . LEU B 1 43  ? 23.336  11.142  -24.710 1.00 48.74  ?  36  LEU B N     1 
ATOM   2410 C  CA    . LEU B 1 43  ? 24.345  11.933  -25.412 1.00 51.00  ?  36  LEU B CA    1 
ATOM   2411 C  C     . LEU B 1 43  ? 23.724  12.911  -26.404 1.00 49.66  ?  36  LEU B C     1 
ATOM   2412 O  O     . LEU B 1 43  ? 24.337  13.913  -26.739 1.00 50.97  ?  36  LEU B O     1 
ATOM   2413 C  CB    . LEU B 1 43  ? 25.314  10.989  -26.133 1.00 54.62  ?  36  LEU B CB    1 
ATOM   2414 C  CG    . LEU B 1 43  ? 26.224  10.160  -25.230 1.00 57.04  ?  36  LEU B CG    1 
ATOM   2415 C  CD1   . LEU B 1 43  ? 26.812  9.002   -26.024 1.00 60.29  ?  36  LEU B CD1   1 
ATOM   2416 C  CD2   . LEU B 1 43  ? 27.324  11.020  -24.645 1.00 58.99  ?  36  LEU B CD2   1 
ATOM   2417 N  N     . PHE B 1 44  ? 22.486  12.657  -26.837 1.00 47.31  ?  37  PHE B N     1 
ATOM   2418 C  CA    . PHE B 1 44  ? 21.857  13.484  -27.848 1.00 46.41  ?  37  PHE B CA    1 
ATOM   2419 C  C     . PHE B 1 44  ? 20.861  14.491  -27.232 1.00 43.40  ?  37  PHE B C     1 
ATOM   2420 O  O     . PHE B 1 44  ? 20.263  15.257  -27.990 1.00 42.69  ?  37  PHE B O     1 
ATOM   2421 C  CB    . PHE B 1 44  ? 21.183  12.564  -28.875 1.00 46.46  ?  37  PHE B CB    1 
ATOM   2422 C  CG    . PHE B 1 44  ? 20.279  11.511  -28.304 1.00 44.77  ?  37  PHE B CG    1 
ATOM   2423 C  CD1   . PHE B 1 44  ? 19.204  11.853  -27.487 1.00 41.81  ?  37  PHE B CD1   1 
ATOM   2424 C  CD2   . PHE B 1 44  ? 20.542  10.163  -28.485 1.00 46.53  ?  37  PHE B CD2   1 
ATOM   2425 C  CE1   . PHE B 1 44  ? 18.380  10.889  -26.941 1.00 40.69  ?  37  PHE B CE1   1 
ATOM   2426 C  CE2   . PHE B 1 44  ? 19.710  9.197   -27.949 1.00 45.41  ?  37  PHE B CE2   1 
ATOM   2427 C  CZ    . PHE B 1 44  ? 18.634  9.556   -27.183 1.00 42.52  ?  37  PHE B CZ    1 
ATOM   2428 N  N     . CYS B 1 45  ? 20.712  14.503  -25.894 1.00 42.04  ?  38  CYS B N     1 
ATOM   2429 C  CA    . CYS B 1 45  ? 19.615  15.217  -25.230 1.00 39.27  ?  38  CYS B CA    1 
ATOM   2430 C  C     . CYS B 1 45  ? 19.482  16.635  -25.793 1.00 39.19  ?  38  CYS B C     1 
ATOM   2431 O  O     . CYS B 1 45  ? 20.455  17.388  -25.726 1.00 40.99  ?  38  CYS B O     1 
ATOM   2432 C  CB    . CYS B 1 45  ? 19.821  15.276  -23.718 1.00 38.79  ?  38  CYS B CB    1 
ATOM   2433 S  SG    . CYS B 1 45  ? 18.415  16.046  -22.858 1.00 35.78  ?  38  CYS B SG    1 
ATOM   2434 N  N     . PHE B 1 46  ? 18.281  17.017  -26.299 1.00 37.43  ?  39  PHE B N     1 
ATOM   2435 C  CA    . PHE B 1 46  ? 18.051  18.365  -26.821 1.00 37.56  ?  39  PHE B CA    1 
ATOM   2436 C  C     . PHE B 1 46  ? 17.310  19.279  -25.849 1.00 35.80  ?  39  PHE B C     1 
ATOM   2437 O  O     . PHE B 1 46  ? 16.955  20.403  -26.238 1.00 35.94  ?  39  PHE B O     1 
ATOM   2438 C  CB    . PHE B 1 46  ? 17.308  18.379  -28.164 1.00 37.56  ?  39  PHE B CB    1 
ATOM   2439 C  CG    . PHE B 1 46  ? 15.962  17.700  -28.262 1.00 35.56  ?  39  PHE B CG    1 
ATOM   2440 C  CD1   . PHE B 1 46  ? 15.201  17.330  -27.156 1.00 33.54  ?  39  PHE B CD1   1 
ATOM   2441 C  CD2   . PHE B 1 46  ? 15.434  17.443  -29.518 1.00 36.11  ?  39  PHE B CD2   1 
ATOM   2442 C  CE1   . PHE B 1 46  ? 13.954  16.736  -27.308 1.00 32.19  ?  39  PHE B CE1   1 
ATOM   2443 C  CE2   . PHE B 1 46  ? 14.207  16.819  -29.665 1.00 34.73  ?  39  PHE B CE2   1 
ATOM   2444 C  CZ    . PHE B 1 46  ? 13.458  16.484  -28.561 1.00 32.79  ?  39  PHE B CZ    1 
ATOM   2445 N  N     . HIS B 1 47  ? 17.167  18.847  -24.594 1.00 34.65  ?  40  HIS B N     1 
ATOM   2446 C  CA    . HIS B 1 47  ? 16.570  19.694  -23.576 1.00 33.43  ?  40  HIS B CA    1 
ATOM   2447 C  C     . HIS B 1 47  ? 17.362  19.545  -22.272 1.00 34.04  ?  40  HIS B C     1 
ATOM   2448 O  O     . HIS B 1 47  ? 16.955  18.835  -21.361 1.00 33.01  ?  40  HIS B O     1 
ATOM   2449 C  CB    . HIS B 1 47  ? 15.049  19.462  -23.574 1.00 31.31  ?  40  HIS B CB    1 
ATOM   2450 C  CG    . HIS B 1 47  ? 14.355  20.630  -22.981 1.00 30.60  ?  40  HIS B CG    1 
ATOM   2451 N  ND1   . HIS B 1 47  ? 13.966  21.716  -23.731 1.00 31.01  ?  40  HIS B ND1   1 
ATOM   2452 C  CD2   . HIS B 1 47  ? 14.160  20.958  -21.713 1.00 30.09  ?  40  HIS B CD2   1 
ATOM   2453 C  CE1   . HIS B 1 47  ? 13.459  22.629  -22.913 1.00 30.64  ?  40  HIS B CE1   1 
ATOM   2454 N  NE2   . HIS B 1 47  ? 13.566  22.184  -21.685 1.00 30.06  ?  40  HIS B NE2   1 
ATOM   2455 N  N     . THR B 1 48  ? 18.478  20.283  -22.195 1.00 36.06  ?  41  THR B N     1 
ATOM   2456 C  CA    . THR B 1 48  ? 19.545  20.042  -21.234 1.00 37.56  ?  41  THR B CA    1 
ATOM   2457 C  C     . THR B 1 48  ? 19.349  20.770  -19.898 1.00 37.24  ?  41  THR B C     1 
ATOM   2458 O  O     . THR B 1 48  ? 18.563  21.709  -19.797 1.00 36.31  ?  41  THR B O     1 
ATOM   2459 C  CB    . THR B 1 48  ? 20.909  20.394  -21.865 1.00 40.51  ?  41  THR B CB    1 
ATOM   2460 O  OG1   . THR B 1 48  ? 21.022  21.797  -22.109 1.00 41.55  ?  41  THR B OG1   1 
ATOM   2461 C  CG2   . THR B 1 48  ? 21.173  19.623  -23.143 1.00 41.29  ?  41  THR B CG2   1 
ATOM   2462 N  N     . ALA B 1 49  ? 20.137  20.352  -18.888 1.00 38.45  ?  42  ALA B N     1 
ATOM   2463 C  CA    . ALA B 1 49  ? 20.017  20.789  -17.507 1.00 38.48  ?  42  ALA B CA    1 
ATOM   2464 C  C     . ALA B 1 49  ? 20.764  22.092  -17.237 1.00 40.60  ?  42  ALA B C     1 
ATOM   2465 O  O     . ALA B 1 49  ? 21.687  22.135  -16.409 1.00 42.64  ?  42  ALA B O     1 
ATOM   2466 C  CB    . ALA B 1 49  ? 20.496  19.706  -16.586 1.00 39.18  ?  42  ALA B CB    1 
ATOM   2467 N  N     . THR B 1 50  ? 20.276  23.164  -17.870 1.00 40.30  ?  43  THR B N     1 
ATOM   2468 C  CA    . THR B 1 50  ? 20.897  24.470  -17.818 1.00 42.61  ?  43  THR B CA    1 
ATOM   2469 C  C     . THR B 1 50  ? 20.361  25.306  -16.661 1.00 42.48  ?  43  THR B C     1 
ATOM   2470 O  O     . THR B 1 50  ? 20.929  26.358  -16.372 1.00 44.80  ?  43  THR B O     1 
ATOM   2471 C  CB    . THR B 1 50  ? 20.719  25.213  -19.154 1.00 43.01  ?  43  THR B CB    1 
ATOM   2472 O  OG1   . THR B 1 50  ? 19.341  25.259  -19.530 1.00 40.45  ?  43  THR B OG1   1 
ATOM   2473 C  CG2   . THR B 1 50  ? 21.514  24.601  -20.288 1.00 44.22  ?  43  THR B CG2   1 
ATOM   2474 N  N     . THR B 1 51  ? 19.219  24.909  -16.060 1.00 40.10  ?  44  THR B N     1 
ATOM   2475 C  CA    . THR B 1 51  ? 18.706  25.578  -14.872 1.00 40.24  ?  44  THR B CA    1 
ATOM   2476 C  C     . THR B 1 51  ? 18.056  24.546  -13.971 1.00 38.59  ?  44  THR B C     1 
ATOM   2477 O  O     . THR B 1 51  ? 17.886  23.410  -14.396 1.00 37.22  ?  44  THR B O     1 
ATOM   2478 C  CB    . THR B 1 51  ? 17.673  26.682  -15.147 1.00 39.65  ?  44  THR B CB    1 
ATOM   2479 O  OG1   . THR B 1 51  ? 16.393  26.087  -15.424 1.00 36.98  ?  44  THR B OG1   1 
ATOM   2480 C  CG2   . THR B 1 51  ? 18.093  27.618  -16.256 1.00 41.17  ?  44  THR B CG2   1 
ATOM   2481 N  N     . SER B 1 52  ? 17.771  24.946  -12.726 1.00 39.19  ?  45  SER B N     1 
ATOM   2482 C  CA    . SER B 1 52  ? 16.971  24.143  -11.814 1.00 37.95  ?  45  SER B CA    1 
ATOM   2483 C  C     . SER B 1 52  ? 15.656  24.851  -11.444 1.00 37.04  ?  45  SER B C     1 
ATOM   2484 O  O     . SER B 1 52  ? 14.952  24.418  -10.529 1.00 36.62  ?  45  SER B O     1 
ATOM   2485 C  CB    . SER B 1 52  ? 17.799  23.782  -10.598 1.00 39.87  ?  45  SER B CB    1 
ATOM   2486 O  OG    . SER B 1 52  ? 18.019  24.928  -9.791  1.00 41.86  ?  45  SER B OG    1 
ATOM   2487 N  N     . HIS B 1 53  ? 15.304  25.935  -12.157 1.00 37.09  ?  46  HIS B N     1 
ATOM   2488 C  CA    . HIS B 1 53  ? 14.068  26.654  -11.882 1.00 36.63  ?  46  HIS B CA    1 
ATOM   2489 C  C     . HIS B 1 53  ? 12.830  25.813  -12.210 1.00 34.31  ?  46  HIS B C     1 
ATOM   2490 O  O     . HIS B 1 53  ? 12.753  25.205  -13.283 1.00 32.96  ?  46  HIS B O     1 
ATOM   2491 C  CB    . HIS B 1 53  ? 13.969  27.935  -12.716 1.00 37.47  ?  46  HIS B CB    1 
ATOM   2492 C  CG    . HIS B 1 53  ? 12.683  28.644  -12.485 1.00 37.28  ?  46  HIS B CG    1 
ATOM   2493 N  ND1   . HIS B 1 53  ? 12.382  29.410  -11.374 1.00 38.89  ?  46  HIS B ND1   1 
ATOM   2494 C  CD2   . HIS B 1 53  ? 11.589  28.649  -13.244 1.00 35.89  ?  46  HIS B CD2   1 
ATOM   2495 C  CE1   . HIS B 1 53  ? 11.148  29.860  -11.481 1.00 38.51  ?  46  HIS B CE1   1 
ATOM   2496 N  NE2   . HIS B 1 53  ? 10.643  29.411  -12.612 1.00 36.70  ?  46  HIS B NE2   1 
ATOM   2497 N  N     . VAL B 1 54  ? 11.854  25.831  -11.294 1.00 34.24  ?  47  VAL B N     1 
ATOM   2498 C  CA    . VAL B 1 54  ? 10.526  25.284  -11.556 1.00 32.64  ?  47  VAL B CA    1 
ATOM   2499 C  C     . VAL B 1 54  ? 9.504   26.284  -11.004 1.00 33.52  ?  47  VAL B C     1 
ATOM   2500 O  O     . VAL B 1 54  ? 9.684   26.811  -9.903  1.00 35.17  ?  47  VAL B O     1 
ATOM   2501 C  CB    . VAL B 1 54  ? 10.312  23.890  -10.961 1.00 31.95  ?  47  VAL B CB    1 
ATOM   2502 C  CG1   . VAL B 1 54  ? 8.923   23.376  -11.306 1.00 30.70  ?  47  VAL B CG1   1 
ATOM   2503 C  CG2   . VAL B 1 54  ? 11.401  22.915  -11.395 1.00 31.61  ?  47  VAL B CG2   1 
ATOM   2504 N  N     . GLU B 1 55  ? 8.428   26.517  -11.756 1.00 32.72  ?  48  GLU B N     1 
ATOM   2505 C  CA    . GLU B 1 55  ? 7.381   27.411  -11.286 1.00 33.82  ?  48  GLU B CA    1 
ATOM   2506 C  C     . GLU B 1 55  ? 6.759   26.855  -10.003 1.00 34.34  ?  48  GLU B C     1 
ATOM   2507 O  O     . GLU B 1 55  ? 6.613   25.654  -9.787  1.00 33.41  ?  48  GLU B O     1 
ATOM   2508 C  CB    . GLU B 1 55  ? 6.310   27.645  -12.354 1.00 33.11  ?  48  GLU B CB    1 
ATOM   2509 C  CG    . GLU B 1 55  ? 6.741   28.533  -13.502 1.00 33.45  ?  48  GLU B CG    1 
ATOM   2510 C  CD    . GLU B 1 55  ? 6.981   29.989  -13.145 1.00 35.73  ?  48  GLU B CD    1 
ATOM   2511 O  OE1   . GLU B 1 55  ? 6.094   30.640  -12.515 1.00 37.06  ?  48  GLU B OE1   1 
ATOM   2512 O  OE2   . GLU B 1 55  ? 8.046   30.467  -13.484 1.00 36.51  ?  48  GLU B OE2   1 
ATOM   2513 N  N     . LYS B 1 56  ? 6.304   27.771  -9.148  1.00 36.22  ?  49  LYS B N     1 
ATOM   2514 C  CA    . LYS B 1 56  ? 5.410   27.404  -8.062  1.00 37.13  ?  49  LYS B CA    1 
ATOM   2515 C  C     . LYS B 1 56  ? 4.105   26.859  -8.616  1.00 36.17  ?  49  LYS B C     1 
ATOM   2516 O  O     . LYS B 1 56  ? 3.607   27.367  -9.621  1.00 35.72  ?  49  LYS B O     1 
ATOM   2517 C  CB    . LYS B 1 56  ? 5.091   28.645  -7.221  1.00 39.68  ?  49  LYS B CB    1 
ATOM   2518 C  CG    . LYS B 1 56  ? 6.259   29.184  -6.410  1.00 41.35  ?  49  LYS B CG    1 
ATOM   2519 C  CD    . LYS B 1 56  ? 5.924   30.495  -5.728  1.00 44.15  ?  49  LYS B CD    1 
ATOM   2520 C  CE    . LYS B 1 56  ? 7.123   31.142  -5.077  1.00 46.12  ?  49  LYS B CE    1 
ATOM   2521 N  NZ    . LYS B 1 56  ? 7.750   30.244  -4.074  1.00 46.42  ?  49  LYS B NZ    1 
ATOM   2522 N  N     . PRO B 1 57  ? 3.529   25.803  -7.994  1.00 36.15  ?  50  PRO B N     1 
ATOM   2523 C  CA    . PRO B 1 57  ? 2.227   25.279  -8.384  1.00 35.86  ?  50  PRO B CA    1 
ATOM   2524 C  C     . PRO B 1 57  ? 1.191   26.358  -8.701  1.00 37.03  ?  50  PRO B C     1 
ATOM   2525 O  O     . PRO B 1 57  ? 0.507   26.254  -9.709  1.00 36.26  ?  50  PRO B O     1 
ATOM   2526 C  CB    . PRO B 1 57  ? 1.785   24.423  -7.192  1.00 37.10  ?  50  PRO B CB    1 
ATOM   2527 C  CG    . PRO B 1 57  ? 3.105   23.974  -6.585  1.00 36.94  ?  50  PRO B CG    1 
ATOM   2528 C  CD    . PRO B 1 57  ? 4.067   25.112  -6.808  1.00 36.99  ?  50  PRO B CD    1 
ATOM   2529 N  N     . GLU B 1 58  ? 1.084   27.413  -7.878  1.00 39.16  ?  51  GLU B N     1 
ATOM   2530 C  CA    . GLU B 1 58  ? -0.006  28.351  -8.111  1.00 40.73  ?  51  GLU B CA    1 
ATOM   2531 C  C     . GLU B 1 58  ? 0.243   29.165  -9.377  1.00 40.01  ?  51  GLU B C     1 
ATOM   2532 O  O     . GLU B 1 58  ? -0.713  29.483  -10.092 1.00 40.45  ?  51  GLU B O     1 
ATOM   2533 C  CB    . GLU B 1 58  ? -0.222  29.226  -6.876  1.00 43.62  ?  51  GLU B CB    1 
ATOM   2534 C  CG    . GLU B 1 58  ? -0.782  28.443  -5.701  1.00 44.91  ?  51  GLU B CG    1 
ATOM   2535 C  CD    . GLU B 1 58  ? -2.077  27.683  -5.954  1.00 45.06  ?  51  GLU B CD    1 
ATOM   2536 O  OE1   . GLU B 1 58  ? -3.116  28.355  -6.223  1.00 46.63  ?  51  GLU B OE1   1 
ATOM   2537 O  OE2   . GLU B 1 58  ? -2.045  26.410  -5.893  1.00 43.92  ?  51  GLU B OE2   1 
ATOM   2538 N  N     . ASN B 1 59  ? 1.519   29.407  -9.703  1.00 39.08  ?  52  ASN B N     1 
ATOM   2539 C  CA    . ASN B 1 59  ? 1.886   30.112  -10.926 1.00 38.62  ?  52  ASN B CA    1 
ATOM   2540 C  C     . ASN B 1 59  ? 1.687   29.218  -12.158 1.00 36.43  ?  52  ASN B C     1 
ATOM   2541 O  O     . ASN B 1 59  ? 1.097   29.644  -13.155 1.00 36.61  ?  52  ASN B O     1 
ATOM   2542 C  CB    . ASN B 1 59  ? 3.293   30.677  -10.771 1.00 38.97  ?  52  ASN B CB    1 
ATOM   2543 C  CG    . ASN B 1 59  ? 3.289   31.858  -9.804  1.00 41.80  ?  52  ASN B CG    1 
ATOM   2544 O  OD1   . ASN B 1 59  ? 2.233   32.379  -9.452  1.00 43.50  ?  52  ASN B OD1   1 
ATOM   2545 N  ND2   . ASN B 1 59  ? 4.448   32.327  -9.408  1.00 42.70  ?  52  ASN B ND2   1 
ATOM   2546 N  N     . ALA B 1 60  ? 2.123   27.957  -12.087 1.00 34.68  ?  53  ALA B N     1 
ATOM   2547 C  CA    . ALA B 1 60  ? 1.887   27.027  -13.193 1.00 32.92  ?  53  ALA B CA    1 
ATOM   2548 C  C     . ALA B 1 60  ? 0.385   26.849  -13.475 1.00 33.51  ?  53  ALA B C     1 
ATOM   2549 O  O     . ALA B 1 60  ? -0.049  26.831  -14.625 1.00 33.09  ?  53  ALA B O     1 
ATOM   2550 C  CB    . ALA B 1 60  ? 2.597   25.725  -12.923 1.00 31.51  ?  53  ALA B CB    1 
ATOM   2551 N  N     . LYS B 1 61  ? -0.441  26.742  -12.427 1.00 34.86  ?  54  LYS B N     1 
ATOM   2552 C  CA    . LYS B 1 61  ? -1.894  26.718  -12.594 1.00 36.10  ?  54  LYS B CA    1 
ATOM   2553 C  C     . LYS B 1 61  ? -2.424  27.956  -13.325 1.00 37.41  ?  54  LYS B C     1 
ATOM   2554 O  O     . LYS B 1 61  ? -3.287  27.834  -14.197 1.00 37.68  ?  54  LYS B O     1 
ATOM   2555 C  CB    . LYS B 1 61  ? -2.573  26.530  -11.234 1.00 37.90  ?  54  LYS B CB    1 
ATOM   2556 C  CG    . LYS B 1 61  ? -2.463  25.145  -10.620 1.00 37.25  ?  54  LYS B CG    1 
ATOM   2557 C  CD    . LYS B 1 61  ? -3.110  25.108  -9.266  1.00 39.54  ?  54  LYS B CD    1 
ATOM   2558 C  CE    . LYS B 1 61  ? -2.743  23.898  -8.436  1.00 39.37  ?  54  LYS B CE    1 
ATOM   2559 N  NZ    . LYS B 1 61  ? -3.644  23.878  -7.258  1.00 42.15  ?  54  LYS B NZ    1 
ATOM   2560 N  N     . ARG B 1 62  ? -1.916  29.134  -13.008 1.00 38.59  ?  55  ARG B N     1 
ATOM   2561 C  CA    . ARG B 1 62  ? -2.354  30.347  -13.748 1.00 40.14  ?  55  ARG B CA    1 
ATOM   2562 C  C     . ARG B 1 62  ? -2.023  30.182  -15.245 1.00 38.70  ?  55  ARG B C     1 
ATOM   2563 O  O     . ARG B 1 62  ? -2.894  30.426  -16.062 1.00 39.65  ?  55  ARG B O     1 
ATOM   2564 C  CB    . ARG B 1 62  ? -1.729  31.636  -13.208 1.00 41.74  ?  55  ARG B CB    1 
ATOM   2565 C  CG    . ARG B 1 62  ? -2.298  32.120  -11.884 1.00 44.20  ?  55  ARG B CG    1 
ATOM   2566 C  CD    . ARG B 1 62  ? -1.540  33.289  -11.269 1.00 46.05  ?  55  ARG B CD    1 
ATOM   2567 N  NE    . ARG B 1 62  ? -0.935  34.188  -12.257 1.00 47.16  ?  55  ARG B NE    1 
ATOM   2568 C  CZ    . ARG B 1 62  ? 0.355   34.498  -12.296 1.00 47.80  ?  55  ARG B CZ    1 
ATOM   2569 N  NH1   . ARG B 1 62  ? 1.197   33.911  -11.471 1.00 47.90  ?  55  ARG B NH1   1 
ATOM   2570 N  NH2   . ARG B 1 62  ? 0.802   35.394  -13.156 1.00 48.59  ?  55  ARG B NH2   1 
ATOM   2571 N  N     . GLY B 1 63  ? -0.801  29.752  -15.548 1.00 36.77  ?  56  GLY B N     1 
ATOM   2572 C  CA    . GLY B 1 63  ? -0.367  29.551  -16.932 1.00 35.60  ?  56  GLY B CA    1 
ATOM   2573 C  C     . GLY B 1 63  ? -1.228  28.549  -17.695 1.00 34.78  ?  56  GLY B C     1 
ATOM   2574 O  O     . GLY B 1 63  ? -1.649  28.822  -18.810 1.00 35.31  ?  56  GLY B O     1 
ATOM   2575 N  N     . LEU B 1 64  ? -1.508  27.394  -17.075 1.00 33.85  ?  57  LEU B N     1 
ATOM   2576 C  CA    . LEU B 1 64  ? -2.296  26.337  -17.700 1.00 33.36  ?  57  LEU B CA    1 
ATOM   2577 C  C     . LEU B 1 64  ? -3.728  26.817  -17.915 1.00 35.43  ?  57  LEU B C     1 
ATOM   2578 O  O     . LEU B 1 64  ? -4.325  26.500  -18.919 1.00 35.67  ?  57  LEU B O     1 
ATOM   2579 C  CB    . LEU B 1 64  ? -2.217  25.096  -16.812 1.00 32.48  ?  57  LEU B CB    1 
ATOM   2580 C  CG    . LEU B 1 64  ? -0.826  24.484  -16.681 1.00 30.70  ?  57  LEU B CG    1 
ATOM   2581 C  CD1   . LEU B 1 64  ? -0.808  23.451  -15.570 1.00 30.53  ?  57  LEU B CD1   1 
ATOM   2582 C  CD2   . LEU B 1 64  ? -0.412  23.842  -17.991 1.00 29.49  ?  57  LEU B CD2   1 
ATOM   2583 N  N     . THR B 1 65  ? -4.252  27.602  -16.961 1.00 37.24  ?  58  THR B N     1 
ATOM   2584 C  CA    . THR B 1 65  ? -5.547  28.239  -17.120 1.00 39.73  ?  58  THR B CA    1 
ATOM   2585 C  C     . THR B 1 65  ? -5.564  29.171  -18.339 1.00 40.58  ?  58  THR B C     1 
ATOM   2586 O  O     . THR B 1 65  ? -6.543  29.162  -19.081 1.00 41.94  ?  58  THR B O     1 
ATOM   2587 C  CB    . THR B 1 65  ? -5.945  28.982  -15.835 1.00 41.79  ?  58  THR B CB    1 
ATOM   2588 O  OG1   . THR B 1 65  ? -6.079  28.069  -14.737 1.00 41.51  ?  58  THR B OG1   1 
ATOM   2589 C  CG2   . THR B 1 65  ? -7.248  29.744  -16.012 1.00 44.82  ?  58  THR B CG2   1 
ATOM   2590 N  N     . LEU B 1 66  ? -4.525  29.994  -18.553 1.00 40.23  ?  59  LEU B N     1 
ATOM   2591 C  CA    . LEU B 1 66  ? -4.515  30.856  -19.731 1.00 41.39  ?  59  LEU B CA    1 
ATOM   2592 C  C     . LEU B 1 66  ? -4.518  30.043  -21.029 1.00 40.19  ?  59  LEU B C     1 
ATOM   2593 O  O     . LEU B 1 66  ? -5.199  30.382  -22.014 1.00 41.75  ?  59  LEU B O     1 
ATOM   2594 C  CB    . LEU B 1 66  ? -3.319  31.798  -19.694 1.00 41.48  ?  59  LEU B CB    1 
ATOM   2595 C  CG    . LEU B 1 66  ? -3.220  32.685  -18.457 1.00 43.02  ?  59  LEU B CG    1 
ATOM   2596 C  CD1   . LEU B 1 66  ? -1.948  33.491  -18.512 1.00 43.21  ?  59  LEU B CD1   1 
ATOM   2597 C  CD2   . LEU B 1 66  ? -4.457  33.575  -18.337 1.00 46.19  ?  59  LEU B CD2   1 
ATOM   2598 N  N     . LEU B 1 67  ? -3.781  28.928  -21.012 1.00 37.71  ?  60  LEU B N     1 
ATOM   2599 C  CA    . LEU B 1 67  ? -3.692  28.074  -22.189 1.00 36.69  ?  60  LEU B CA    1 
ATOM   2600 C  C     . LEU B 1 67  ? -5.025  27.388  -22.470 1.00 37.65  ?  60  LEU B C     1 
ATOM   2601 O  O     . LEU B 1 67  ? -5.445  27.291  -23.609 1.00 38.44  ?  60  LEU B O     1 
ATOM   2602 C  CB    . LEU B 1 67  ? -2.582  27.038  -21.966 1.00 34.19  ?  60  LEU B CB    1 
ATOM   2603 C  CG    . LEU B 1 67  ? -1.132  27.525  -22.048 1.00 33.38  ?  60  LEU B CG    1 
ATOM   2604 C  CD1   . LEU B 1 67  ? -0.230  26.447  -21.467 1.00 31.36  ?  60  LEU B CD1   1 
ATOM   2605 C  CD2   . LEU B 1 67  ? -0.704  27.905  -23.467 1.00 33.91  ?  60  LEU B CD2   1 
ATOM   2606 N  N     . LYS B 1 68  ? -5.744  26.961  -21.442 1.00 38.04  ?  61  LYS B N     1 
ATOM   2607 C  CA    . LYS B 1 68  ? -7.063  26.398  -21.644 1.00 39.57  ?  61  LYS B CA    1 
ATOM   2608 C  C     . LYS B 1 68  ? -7.964  27.416  -22.351 1.00 42.26  ?  61  LYS B C     1 
ATOM   2609 O  O     . LYS B 1 68  ? -8.696  27.074  -23.283 1.00 43.43  ?  61  LYS B O     1 
ATOM   2610 C  CB    . LYS B 1 68  ? -7.665  25.962  -20.303 1.00 40.16  ?  61  LYS B CB    1 
ATOM   2611 C  CG    . LYS B 1 68  ? -9.146  25.598  -20.314 1.00 42.60  ?  61  LYS B CG    1 
ATOM   2612 C  CD    . LYS B 1 68  ? -9.433  24.268  -20.960 1.00 42.14  ?  61  LYS B CD    1 
ATOM   2613 C  CE    . LYS B 1 68  ? -10.900 24.047  -21.245 1.00 45.08  ?  61  LYS B CE    1 
ATOM   2614 N  NZ    . LYS B 1 68  ? -11.153 22.615  -21.454 1.00 44.90  ?  61  LYS B NZ    1 
ATOM   2615 N  N     . GLN B 1 69  ? -7.939  28.647  -21.852 1.00 43.60  ?  62  GLN B N     1 
ATOM   2616 C  CA    . GLN B 1 69  ? -8.808  29.692  -22.379 1.00 46.64  ?  62  GLN B CA    1 
ATOM   2617 C  C     . GLN B 1 69  ? -8.519  29.958  -23.859 1.00 46.91  ?  62  GLN B C     1 
ATOM   2618 O  O     . GLN B 1 69  ? -9.442  30.229  -24.636 1.00 49.33  ?  62  GLN B O     1 
ATOM   2619 C  CB    . GLN B 1 69  ? -8.680  30.946  -21.519 1.00 48.13  ?  62  GLN B CB    1 
ATOM   2620 C  CG    . GLN B 1 69  ? -9.762  31.975  -21.841 1.00 51.91  ?  62  GLN B CG    1 
ATOM   2621 C  CD    . GLN B 1 69  ? -11.135 31.464  -21.470 1.00 53.86  ?  62  GLN B CD    1 
ATOM   2622 O  OE1   . GLN B 1 69  ? -11.911 31.060  -22.324 1.00 55.04  ?  62  GLN B OE1   1 
ATOM   2623 N  NE2   . GLN B 1 69  ? -11.429 31.434  -20.179 1.00 54.43  ?  62  GLN B NE2   1 
ATOM   2624 N  N     . ALA B 1 70  ? -7.234  29.856  -24.250 1.00 44.71  ?  63  ALA B N     1 
ATOM   2625 C  CA    . ALA B 1 70  ? -6.774  30.117  -25.608 1.00 45.03  ?  63  ALA B CA    1 
ATOM   2626 C  C     . ALA B 1 70  ? -7.084  28.947  -26.541 1.00 44.41  ?  63  ALA B C     1 
ATOM   2627 O  O     . ALA B 1 70  ? -6.937  29.063  -27.744 1.00 45.21  ?  63  ALA B O     1 
ATOM   2628 C  CB    . ALA B 1 70  ? -5.299  30.423  -25.577 1.00 43.34  ?  63  ALA B CB    1 
ATOM   2629 N  N     . GLY B 1 71  ? -7.503  27.819  -25.975 1.00 43.31  ?  64  GLY B N     1 
ATOM   2630 C  CA    . GLY B 1 71  ? -8.025  26.719  -26.755 1.00 43.43  ?  64  GLY B CA    1 
ATOM   2631 C  C     . GLY B 1 71  ? -7.141  25.475  -26.715 1.00 40.70  ?  64  GLY B C     1 
ATOM   2632 O  O     . GLY B 1 71  ? -7.331  24.558  -27.526 1.00 40.80  ?  64  GLY B O     1 
ATOM   2633 N  N     . MET B 1 72  ? -6.262  25.383  -25.715 1.00 38.65  ?  65  MET B N     1 
ATOM   2634 C  CA    . MET B 1 72  ? -5.522  24.143  -25.527 1.00 36.47  ?  65  MET B CA    1 
ATOM   2635 C  C     . MET B 1 72  ? -6.466  22.973  -25.198 1.00 36.99  ?  65  MET B C     1 
ATOM   2636 O  O     . MET B 1 72  ? -7.401  23.056  -24.395 1.00 38.24  ?  65  MET B O     1 
ATOM   2637 C  CB    . MET B 1 72  ? -4.430  24.310  -24.463 1.00 34.61  ?  65  MET B CB    1 
ATOM   2638 C  CG    . MET B 1 72  ? -3.607  23.061  -24.220 1.00 32.66  ?  65  MET B CG    1 
ATOM   2639 S  SD    . MET B 1 72  ? -2.298  23.383  -22.990 1.00 30.99  ?  65  MET B SD    1 
ATOM   2640 C  CE    . MET B 1 72  ? -3.192  23.437  -21.440 1.00 31.73  ?  65  MET B CE    1 
ATOM   2641 N  N     . LYS B 1 73  ? -6.227  21.830  -25.837 1.00 36.38  ?  66  LYS B N     1 
ATOM   2642 C  CA    . LYS B 1 73  ? -6.975  20.595  -25.608 1.00 37.07  ?  66  LYS B CA    1 
ATOM   2643 C  C     . LYS B 1 73  ? -6.109  19.485  -24.986 1.00 35.23  ?  66  LYS B C     1 
ATOM   2644 O  O     . LYS B 1 73  ? -6.610  18.609  -24.293 1.00 35.76  ?  66  LYS B O     1 
ATOM   2645 C  CB    . LYS B 1 73  ? -7.519  20.084  -26.954 1.00 38.61  ?  66  LYS B CB    1 
ATOM   2646 C  CG    . LYS B 1 73  ? -8.685  20.890  -27.516 1.00 41.24  ?  66  LYS B CG    1 
ATOM   2647 C  CD    . LYS B 1 73  ? -9.205  20.368  -28.854 1.00 43.08  ?  66  LYS B CD    1 
ATOM   2648 C  CE    . LYS B 1 73  ? -10.355 21.185  -29.416 1.00 46.05  ?  66  LYS B CE    1 
ATOM   2649 N  NZ    . LYS B 1 73  ? -10.837 20.598  -30.691 1.00 48.07  ?  66  LYS B NZ    1 
ATOM   2650 N  N     . LYS B 1 74  ? -4.821  19.470  -25.346 1.00 33.48  ?  67  LYS B N     1 
ATOM   2651 C  CA    . LYS B 1 74  ? -3.868  18.476  -24.868 1.00 31.98  ?  67  LYS B CA    1 
ATOM   2652 C  C     . LYS B 1 74  ? -2.612  19.124  -24.290 1.00 30.28  ?  67  LYS B C     1 
ATOM   2653 O  O     . LYS B 1 74  ? -2.052  20.037  -24.867 1.00 30.03  ?  67  LYS B O     1 
ATOM   2654 C  CB    . LYS B 1 74  ? -3.418  17.590  -26.034 1.00 32.04  ?  67  LYS B CB    1 
ATOM   2655 C  CG    . LYS B 1 74  ? -2.488  16.457  -25.610 1.00 30.99  ?  67  LYS B CG    1 
ATOM   2656 C  CD    . LYS B 1 74  ? -2.301  15.368  -26.644 1.00 31.71  ?  67  LYS B CD    1 
ATOM   2657 C  CE    . LYS B 1 74  ? -1.355  14.284  -26.149 1.00 31.00  ?  67  LYS B CE    1 
ATOM   2658 N  NZ    . LYS B 1 74  ? 0.062   14.698  -26.271 1.00 29.63  ?  67  LYS B NZ    1 
ATOM   2659 N  N     . ILE B 1 75  ? -2.175  18.630  -23.114 1.00 29.45  ?  68  ILE B N     1 
ATOM   2660 C  CA    . ILE B 1 75  ? -0.951  19.093  -22.453 1.00 28.12  ?  68  ILE B CA    1 
ATOM   2661 C  C     . ILE B 1 75  ? -0.049  17.879  -22.248 1.00 27.35  ?  68  ILE B C     1 
ATOM   2662 O  O     . ILE B 1 75  ? -0.549  16.855  -21.812 1.00 27.90  ?  68  ILE B O     1 
ATOM   2663 C  CB    . ILE B 1 75  ? -1.253  19.781  -21.091 1.00 28.32  ?  68  ILE B CB    1 
ATOM   2664 C  CG1   . ILE B 1 75  ? 0.002   20.306  -20.391 1.00 27.32  ?  68  ILE B CG1   1 
ATOM   2665 C  CG2   . ILE B 1 75  ? -1.977  18.867  -20.134 1.00 29.02  ?  68  ILE B CG2   1 
ATOM   2666 C  CD1   . ILE B 1 75  ? 0.704   21.432  -21.100 1.00 27.14  ?  68  ILE B CD1   1 
ATOM   2667 N  N     . ASN B 1 76  ? 1.242   17.983  -22.627 1.00 26.50  ?  69  ASN B N     1 
ATOM   2668 C  CA    . ASN B 1 76  ? 2.196   16.926  -22.368 1.00 26.07  ?  69  ASN B CA    1 
ATOM   2669 C  C     . ASN B 1 76  ? 3.184   17.489  -21.359 1.00 25.41  ?  69  ASN B C     1 
ATOM   2670 O  O     . ASN B 1 76  ? 3.807   18.523  -21.620 1.00 25.17  ?  69  ASN B O     1 
ATOM   2671 C  CB    . ASN B 1 76  ? 2.900   16.468  -23.645 1.00 26.17  ?  69  ASN B CB    1 
ATOM   2672 C  CG    . ASN B 1 76  ? 3.721   15.195  -23.514 1.00 26.27  ?  69  ASN B CG    1 
ATOM   2673 O  OD1   . ASN B 1 76  ? 3.249   14.195  -22.979 1.00 26.78  ?  69  ASN B OD1   1 
ATOM   2674 N  ND2   . ASN B 1 76  ? 4.932   15.216  -24.067 1.00 26.19  ?  69  ASN B ND2   1 
ATOM   2675 N  N     . PHE B 1 77  ? 3.352   16.790  -20.238 1.00 25.45  ?  70  PHE B N     1 
ATOM   2676 C  CA    . PHE B 1 77  ? 4.345   17.181  -19.257 1.00 25.15  ?  70  PHE B CA    1 
ATOM   2677 C  C     . PHE B 1 77  ? 5.682   16.520  -19.591 1.00 25.06  ?  70  PHE B C     1 
ATOM   2678 O  O     . PHE B 1 77  ? 5.749   15.296  -19.724 1.00 25.46  ?  70  PHE B O     1 
ATOM   2679 C  CB    . PHE B 1 77  ? 3.861   16.828  -17.846 1.00 25.67  ?  70  PHE B CB    1 
ATOM   2680 C  CG    . PHE B 1 77  ? 2.718   17.699  -17.375 1.00 26.10  ?  70  PHE B CG    1 
ATOM   2681 C  CD1   . PHE B 1 77  ? 2.985   18.923  -16.788 1.00 26.11  ?  70  PHE B CD1   1 
ATOM   2682 C  CD2   . PHE B 1 77  ? 1.394   17.319  -17.526 1.00 26.86  ?  70  PHE B CD2   1 
ATOM   2683 C  CE1   . PHE B 1 77  ? 1.952   19.756  -16.389 1.00 26.84  ?  70  PHE B CE1   1 
ATOM   2684 C  CE2   . PHE B 1 77  ? 0.359   18.159  -17.116 1.00 27.62  ?  70  PHE B CE2   1 
ATOM   2685 C  CZ    . PHE B 1 77  ? 0.644   19.354  -16.514 1.00 27.62  ?  70  PHE B CZ    1 
ATOM   2686 N  N     . ALA B 1 78  ? 6.725   17.325  -19.773 1.00 24.89  ?  71  ALA B N     1 
ATOM   2687 C  CA    . ALA B 1 78  ? 8.039   16.844  -20.194 1.00 25.17  ?  71  ALA B CA    1 
ATOM   2688 C  C     . ALA B 1 78  ? 9.120   17.614  -19.456 1.00 25.44  ?  71  ALA B C     1 
ATOM   2689 O  O     . ALA B 1 78  ? 8.857   18.196  -18.408 1.00 25.43  ?  71  ALA B O     1 
ATOM   2690 C  CB    . ALA B 1 78  ? 8.177   16.959  -21.703 1.00 25.32  ?  71  ALA B CB    1 
ATOM   2691 N  N     . GLY B 1 79  ? 10.348  17.641  -20.000 1.00 26.03  ?  72  GLY B N     1 
ATOM   2692 C  CA    . GLY B 1 79  ? 11.459  18.243  -19.296 1.00 26.74  ?  72  GLY B CA    1 
ATOM   2693 C  C     . GLY B 1 79  ? 12.771  18.014  -20.058 1.00 27.79  ?  72  GLY B C     1 
ATOM   2694 O  O     . GLY B 1 79  ? 12.762  17.995  -21.275 1.00 27.92  ?  72  GLY B O     1 
ATOM   2695 N  N     . GLY B 1 80  ? 13.860  17.755  -19.340 1.00 28.84  ?  73  GLY B N     1 
ATOM   2696 C  CA    . GLY B 1 80  ? 13.906  17.280  -17.962 1.00 29.05  ?  73  GLY B CA    1 
ATOM   2697 C  C     . GLY B 1 80  ? 13.160  15.959  -17.744 1.00 28.64  ?  73  GLY B C     1 
ATOM   2698 O  O     . GLY B 1 80  ? 12.384  15.503  -18.597 1.00 27.96  ?  73  GLY B O     1 
ATOM   2699 N  N     . GLU B 1 81  ? 13.328  15.384  -16.541 1.00 29.32  ?  74  GLU B N     1 
ATOM   2700 C  CA    . GLU B 1 81  ? 12.638  14.162  -16.171 1.00 29.44  ?  74  GLU B CA    1 
ATOM   2701 C  C     . GLU B 1 81  ? 11.478  14.463  -15.225 1.00 28.88  ?  74  GLU B C     1 
ATOM   2702 O  O     . GLU B 1 81  ? 11.672  14.876  -14.074 1.00 29.47  ?  74  GLU B O     1 
ATOM   2703 C  CB    . GLU B 1 81  ? 13.566  13.143  -15.528 1.00 31.15  ?  74  GLU B CB    1 
ATOM   2704 C  CG    . GLU B 1 81  ? 12.839  11.924  -14.997 1.00 31.74  ?  74  GLU B CG    1 
ATOM   2705 C  CD    . GLU B 1 81  ? 11.818  11.324  -15.964 1.00 31.03  ?  74  GLU B CD    1 
ATOM   2706 O  OE1   . GLU B 1 81  ? 12.157  11.163  -17.166 1.00 30.93  ?  74  GLU B OE1   1 
ATOM   2707 O  OE2   . GLU B 1 81  ? 10.703  11.031  -15.528 1.00 30.88  ?  74  GLU B OE2   1 
ATOM   2708 N  N     . PRO B 1 82  ? 10.225  14.357  -15.686 1.00 28.00  ?  75  PRO B N     1 
ATOM   2709 C  CA    . PRO B 1 82  ? 9.091   14.761  -14.845 1.00 27.78  ?  75  PRO B CA    1 
ATOM   2710 C  C     . PRO B 1 82  ? 8.994   14.070  -13.491 1.00 29.03  ?  75  PRO B C     1 
ATOM   2711 O  O     . PRO B 1 82  ? 8.637   14.683  -12.507 1.00 29.36  ?  75  PRO B O     1 
ATOM   2712 C  CB    . PRO B 1 82  ? 7.866   14.450  -15.703 1.00 27.17  ?  75  PRO B CB    1 
ATOM   2713 C  CG    . PRO B 1 82  ? 8.399   14.623  -17.100 1.00 26.59  ?  75  PRO B CG    1 
ATOM   2714 C  CD    . PRO B 1 82  ? 9.812   14.100  -17.075 1.00 27.37  ?  75  PRO B CD    1 
ATOM   2715 N  N     . PHE B 1 83  ? 9.398   12.816  -13.402 1.00 30.11  ?  76  PHE B N     1 
ATOM   2716 C  CA    . PHE B 1 83  ? 9.199   12.077  -12.158 1.00 31.70  ?  76  PHE B CA    1 
ATOM   2717 C  C     . PHE B 1 83  ? 10.251  12.417  -11.095 1.00 32.79  ?  76  PHE B C     1 
ATOM   2718 O  O     . PHE B 1 83  ? 10.174  11.891  -9.986  1.00 34.41  ?  76  PHE B O     1 
ATOM   2719 C  CB    . PHE B 1 83  ? 9.120   10.585  -12.512 1.00 32.85  ?  76  PHE B CB    1 
ATOM   2720 C  CG    . PHE B 1 83  ? 7.729   10.238  -12.958 1.00 32.61  ?  76  PHE B CG    1 
ATOM   2721 C  CD1   . PHE B 1 83  ? 6.750   10.026  -12.003 1.00 33.71  ?  76  PHE B CD1   1 
ATOM   2722 C  CD2   . PHE B 1 83  ? 7.359   10.243  -14.300 1.00 31.54  ?  76  PHE B CD2   1 
ATOM   2723 C  CE1   . PHE B 1 83  ? 5.444   9.762   -12.384 1.00 33.86  ?  76  PHE B CE1   1 
ATOM   2724 C  CE2   . PHE B 1 83  ? 6.060   9.976   -14.677 1.00 31.63  ?  76  PHE B CE2   1 
ATOM   2725 C  CZ    . PHE B 1 83  ? 5.102   9.707   -13.710 1.00 32.86  ?  76  PHE B CZ    1 
ATOM   2726 N  N     . LEU B 1 84  ? 11.194  13.336  -11.394 1.00 32.24  ?  77  LEU B N     1 
ATOM   2727 C  CA    . LEU B 1 84  ? 11.996  13.939  -10.331 1.00 33.37  ?  77  LEU B CA    1 
ATOM   2728 C  C     . LEU B 1 84  ? 11.143  14.864  -9.447  1.00 33.29  ?  77  LEU B C     1 
ATOM   2729 O  O     . LEU B 1 84  ? 11.607  15.194  -8.349  1.00 34.70  ?  77  LEU B O     1 
ATOM   2730 C  CB    . LEU B 1 84  ? 13.206  14.690  -10.898 1.00 33.27  ?  77  LEU B CB    1 
ATOM   2731 C  CG    . LEU B 1 84  ? 14.362  13.816  -11.417 1.00 34.33  ?  77  LEU B CG    1 
ATOM   2732 C  CD1   . LEU B 1 84  ? 15.413  14.664  -12.113 1.00 34.37  ?  77  LEU B CD1   1 
ATOM   2733 C  CD2   . LEU B 1 84  ? 14.980  13.033  -10.257 1.00 36.63  ?  77  LEU B CD2   1 
ATOM   2734 N  N     . TYR B 1 85  ? 9.951   15.280  -9.900  1.00 32.01  ?  78  TYR B N     1 
ATOM   2735 C  CA    . TYR B 1 85  ? 9.089   16.224  -9.199  1.00 32.11  ?  78  TYR B CA    1 
ATOM   2736 C  C     . TYR B 1 85  ? 7.679   15.651  -9.133  1.00 32.17  ?  78  TYR B C     1 
ATOM   2737 O  O     . TYR B 1 85  ? 6.712   16.242  -9.620  1.00 31.32  ?  78  TYR B O     1 
ATOM   2738 C  CB    . TYR B 1 85  ? 9.001   17.583  -9.901  1.00 30.91  ?  78  TYR B CB    1 
ATOM   2739 C  CG    . TYR B 1 85  ? 10.317  18.322  -10.003 1.00 31.20  ?  78  TYR B CG    1 
ATOM   2740 C  CD1   . TYR B 1 85  ? 11.270  17.959  -10.947 1.00 30.80  ?  78  TYR B CD1   1 
ATOM   2741 C  CD2   . TYR B 1 85  ? 10.600  19.373  -9.146  1.00 32.27  ?  78  TYR B CD2   1 
ATOM   2742 C  CE1   . TYR B 1 85  ? 12.467  18.644  -11.047 1.00 31.49  ?  78  TYR B CE1   1 
ATOM   2743 C  CE2   . TYR B 1 85  ? 11.813  20.021  -9.200  1.00 33.00  ?  78  TYR B CE2   1 
ATOM   2744 C  CZ    . TYR B 1 85  ? 12.736  19.669  -10.164 1.00 32.62  ?  78  TYR B CZ    1 
ATOM   2745 O  OH    . TYR B 1 85  ? 13.930  20.315  -10.269 1.00 33.69  ?  78  TYR B OH    1 
ATOM   2746 N  N     . PRO B 1 86  ? 7.469   14.490  -8.484  1.00 33.60  ?  79  PRO B N     1 
ATOM   2747 C  CA    . PRO B 1 86  ? 6.150   13.867  -8.509  1.00 34.05  ?  79  PRO B CA    1 
ATOM   2748 C  C     . PRO B 1 86  ? 5.051   14.649  -7.770  1.00 34.75  ?  79  PRO B C     1 
ATOM   2749 O  O     . PRO B 1 86  ? 3.871   14.510  -8.097  1.00 34.82  ?  79  PRO B O     1 
ATOM   2750 C  CB    . PRO B 1 86  ? 6.432   12.479  -7.900  1.00 35.97  ?  79  PRO B CB    1 
ATOM   2751 C  CG    . PRO B 1 86  ? 7.652   12.671  -7.030  1.00 36.98  ?  79  PRO B CG    1 
ATOM   2752 C  CD    . PRO B 1 86  ? 8.477   13.677  -7.792  1.00 35.17  ?  79  PRO B CD    1 
ATOM   2753 N  N     . LYS B 1 87  ? 5.414   15.516  -6.803  1.00 35.54  ?  80  LYS B N     1 
ATOM   2754 C  CA    . LYS B 1 87  ? 4.358   16.236  -6.107  1.00 36.58  ?  80  LYS B CA    1 
ATOM   2755 C  C     . LYS B 1 87  ? 3.814   17.314  -7.035  1.00 35.01  ?  80  LYS B C     1 
ATOM   2756 O  O     . LYS B 1 87  ? 2.592   17.426  -7.175  1.00 35.40  ?  80  LYS B O     1 
ATOM   2757 C  CB    . LYS B 1 87  ? 4.838   16.803  -4.763  1.00 38.36  ?  80  LYS B CB    1 
ATOM   2758 C  CG    . LYS B 1 87  ? 3.739   17.500  -3.976  1.00 39.94  ?  80  LYS B CG    1 
ATOM   2759 C  CD    . LYS B 1 87  ? 4.149   17.995  -2.612  1.00 42.14  ?  80  LYS B CD    1 
ATOM   2760 C  CE    . LYS B 1 87  ? 2.986   18.609  -1.858  1.00 44.08  ?  80  LYS B CE    1 
ATOM   2761 N  NZ    . LYS B 1 87  ? 1.969   17.587  -1.508  1.00 45.73  ?  80  LYS B NZ    1 
ATOM   2762 N  N     . PHE B 1 88  ? 4.742   18.068  -7.656  1.00 33.61  ?  81  PHE B N     1 
ATOM   2763 C  CA    . PHE B 1 88  ? 4.373   19.074  -8.646  1.00 32.31  ?  81  PHE B CA    1 
ATOM   2764 C  C     . PHE B 1 88  ? 3.562   18.417  -9.759  1.00 31.33  ?  81  PHE B C     1 
ATOM   2765 O  O     . PHE B 1 88  ? 2.502   18.901  -10.116 1.00 31.41  ?  81  PHE B O     1 
ATOM   2766 C  CB    . PHE B 1 88  ? 5.615   19.710  -9.259  1.00 31.28  ?  81  PHE B CB    1 
ATOM   2767 C  CG    . PHE B 1 88  ? 5.331   20.827  -10.232 1.00 30.39  ?  81  PHE B CG    1 
ATOM   2768 C  CD1   . PHE B 1 88  ? 5.177   22.125  -9.812  1.00 31.26  ?  81  PHE B CD1   1 
ATOM   2769 C  CD2   . PHE B 1 88  ? 5.248   20.561  -11.590 1.00 29.01  ?  81  PHE B CD2   1 
ATOM   2770 C  CE1   . PHE B 1 88  ? 4.952   23.134  -10.731 1.00 30.81  ?  81  PHE B CE1   1 
ATOM   2771 C  CE2   . PHE B 1 88  ? 5.042   21.565  -12.516 1.00 28.51  ?  81  PHE B CE2   1 
ATOM   2772 C  CZ    . PHE B 1 88  ? 4.879   22.856  -12.076 1.00 29.45  ?  81  PHE B CZ    1 
ATOM   2773 N  N     . LEU B 1 89  ? 4.100   17.319  -10.304 1.00 30.71  ?  82  LEU B N     1 
ATOM   2774 C  CA    . LEU B 1 89  ? 3.523   16.658  -11.464 1.00 29.93  ?  82  LEU B CA    1 
ATOM   2775 C  C     . LEU B 1 89  ? 2.097   16.199  -11.146 1.00 31.19  ?  82  LEU B C     1 
ATOM   2776 O  O     . LEU B 1 89  ? 1.178   16.457  -11.920 1.00 30.94  ?  82  LEU B O     1 
ATOM   2777 C  CB    . LEU B 1 89  ? 4.434   15.493  -11.868 1.00 29.68  ?  82  LEU B CB    1 
ATOM   2778 C  CG    . LEU B 1 89  ? 3.971   14.645  -13.051 1.00 29.25  ?  82  LEU B CG    1 
ATOM   2779 C  CD1   . LEU B 1 89  ? 3.859   15.452  -14.333 1.00 27.89  ?  82  LEU B CD1   1 
ATOM   2780 C  CD2   . LEU B 1 89  ? 4.932   13.512  -13.235 1.00 29.54  ?  82  LEU B CD2   1 
ATOM   2781 N  N     . GLY B 1 90  ? 1.920   15.566  -9.986  1.00 32.89  ?  83  GLY B N     1 
ATOM   2782 C  CA    . GLY B 1 90  ? 0.620   15.111  -9.509  1.00 34.71  ?  83  GLY B CA    1 
ATOM   2783 C  C     . GLY B 1 90  ? -0.397  16.239  -9.366  1.00 35.24  ?  83  GLY B C     1 
ATOM   2784 O  O     . GLY B 1 90  ? -1.558  16.081  -9.781  1.00 36.02  ?  83  GLY B O     1 
ATOM   2785 N  N     . GLU B 1 91  ? 0.039   17.363  -8.781  1.00 35.14  ?  84  GLU B N     1 
ATOM   2786 C  CA    . GLU B 1 91  ? -0.843  18.496  -8.605  1.00 35.97  ?  84  GLU B CA    1 
ATOM   2787 C  C     . GLU B 1 91  ? -1.276  19.031  -9.963  1.00 34.66  ?  84  GLU B C     1 
ATOM   2788 O  O     . GLU B 1 91  ? -2.404  19.455  -10.103 1.00 35.76  ?  84  GLU B O     1 
ATOM   2789 C  CB    . GLU B 1 91  ? -0.146  19.607  -7.820  1.00 36.24  ?  84  GLU B CB    1 
ATOM   2790 C  CG    . GLU B 1 91  ? 0.005   19.301  -6.357  1.00 38.26  ?  84  GLU B CG    1 
ATOM   2791 C  CD    . GLU B 1 91  ? 0.583   20.473  -5.585  1.00 38.98  ?  84  GLU B CD    1 
ATOM   2792 O  OE1   . GLU B 1 91  ? 0.054   21.617  -5.741  1.00 39.37  ?  84  GLU B OE1   1 
ATOM   2793 O  OE2   . GLU B 1 91  ? 1.524   20.238  -4.831  1.00 39.45  ?  84  GLU B OE2   1 
ATOM   2794 N  N     . MET B 1 92  ? -0.347  19.118  -10.934 1.00 32.64  ?  85  MET B N     1 
ATOM   2795 C  CA    . MET B 1 92  ? -0.663  19.732  -12.212 1.00 31.67  ?  85  MET B CA    1 
ATOM   2796 C  C     . MET B 1 92  ? -1.540  18.795  -13.049 1.00 31.85  ?  85  MET B C     1 
ATOM   2797 O  O     . MET B 1 92  ? -2.447  19.260  -13.730 1.00 32.30  ?  85  MET B O     1 
ATOM   2798 C  CB    . MET B 1 92  ? 0.603   20.087  -12.999 1.00 29.92  ?  85  MET B CB    1 
ATOM   2799 C  CG    . MET B 1 92  ? 1.475   21.153  -12.354 1.00 30.02  ?  85  MET B CG    1 
ATOM   2800 S  SD    . MET B 1 92  ? 0.546   22.681  -11.874 1.00 31.64  ?  85  MET B SD    1 
ATOM   2801 C  CE    . MET B 1 92  ? 0.377   22.461  -10.106 1.00 33.47  ?  85  MET B CE    1 
ATOM   2802 N  N     . ILE B 1 93  ? -1.289  17.480  -12.989 1.00 31.86  ?  86  ILE B N     1 
ATOM   2803 C  CA    . ILE B 1 93  ? -2.131  16.502  -13.673 1.00 32.55  ?  86  ILE B CA    1 
ATOM   2804 C  C     . ILE B 1 93  ? -3.559  16.593  -13.148 1.00 34.76  ?  86  ILE B C     1 
ATOM   2805 O  O     . ILE B 1 93  ? -4.512  16.621  -13.911 1.00 35.46  ?  86  ILE B O     1 
ATOM   2806 C  CB    . ILE B 1 93  ? -1.574  15.082  -13.494 1.00 32.74  ?  86  ILE B CB    1 
ATOM   2807 C  CG1   . ILE B 1 93  ? -0.371  14.876  -14.421 1.00 30.91  ?  86  ILE B CG1   1 
ATOM   2808 C  CG2   . ILE B 1 93  ? -2.621  13.991  -13.673 1.00 34.55  ?  86  ILE B CG2   1 
ATOM   2809 C  CD1   . ILE B 1 93  ? 0.471   13.679  -13.982 1.00 31.28  ?  86  ILE B CD1   1 
ATOM   2810 N  N     . ASP B 1 94  ? -3.692  16.592  -11.827 1.00 36.20  ?  87  ASP B N     1 
ATOM   2811 C  CA    . ASP B 1 94  ? -5.001  16.590  -11.192 1.00 38.82  ?  87  ASP B CA    1 
ATOM   2812 C  C     . ASP B 1 94  ? -5.726  17.870  -11.585 1.00 39.12  ?  87  ASP B C     1 
ATOM   2813 O  O     . ASP B 1 94  ? -6.881  17.817  -12.011 1.00 40.70  ?  87  ASP B O     1 
ATOM   2814 C  CB    . ASP B 1 94  ? -4.882  16.399  -9.676  1.00 40.51  ?  87  ASP B CB    1 
ATOM   2815 C  CG    . ASP B 1 94  ? -4.412  15.030  -9.213  1.00 41.15  ?  87  ASP B CG    1 
ATOM   2816 O  OD1   . ASP B 1 94  ? -4.347  14.089  -10.033 1.00 40.66  ?  87  ASP B OD1   1 
ATOM   2817 O  OD2   . ASP B 1 94  ? -4.068  14.921  -8.017  1.00 42.36  ?  87  ASP B OD2   1 
ATOM   2818 N  N     . PHE B 1 95  ? -5.040  19.016  -11.504 1.00 37.90  ?  88  PHE B N     1 
ATOM   2819 C  CA    . PHE B 1 95  ? -5.649  20.282  -11.870 1.00 38.47  ?  88  PHE B CA    1 
ATOM   2820 C  C     . PHE B 1 95  ? -6.105  20.299  -13.335 1.00 37.87  ?  88  PHE B C     1 
ATOM   2821 O  O     . PHE B 1 95  ? -7.202  20.770  -13.661 1.00 39.56  ?  88  PHE B O     1 
ATOM   2822 C  CB    . PHE B 1 95  ? -4.651  21.405  -11.632 1.00 37.32  ?  88  PHE B CB    1 
ATOM   2823 C  CG    . PHE B 1 95  ? -5.113  22.798  -11.983 1.00 38.11  ?  88  PHE B CG    1 
ATOM   2824 C  CD1   . PHE B 1 95  ? -5.942  23.498  -11.126 1.00 40.60  ?  88  PHE B CD1   1 
ATOM   2825 C  CD2   . PHE B 1 95  ? -4.696  23.420  -13.149 1.00 36.74  ?  88  PHE B CD2   1 
ATOM   2826 C  CE1   . PHE B 1 95  ? -6.308  24.801  -11.415 1.00 41.66  ?  88  PHE B CE1   1 
ATOM   2827 C  CE2   . PHE B 1 95  ? -5.111  24.705  -13.463 1.00 37.86  ?  88  PHE B CE2   1 
ATOM   2828 C  CZ    . PHE B 1 95  ? -5.919  25.397  -12.583 1.00 40.34  ?  88  PHE B CZ    1 
ATOM   2829 N  N     . CYS B 1 96  ? -5.257  19.802  -14.236 1.00 35.76  ?  89  CYS B N     1 
ATOM   2830 C  CA    . CYS B 1 96  ? -5.558  19.895  -15.659 1.00 35.28  ?  89  CYS B CA    1 
ATOM   2831 C  C     . CYS B 1 96  ? -6.808  19.102  -16.013 1.00 37.16  ?  89  CYS B C     1 
ATOM   2832 O  O     . CYS B 1 96  ? -7.578  19.541  -16.860 1.00 38.07  ?  89  CYS B O     1 
ATOM   2833 C  CB    . CYS B 1 96  ? -4.416  19.388  -16.533 1.00 33.09  ?  89  CYS B CB    1 
ATOM   2834 S  SG    . CYS B 1 96  ? -3.076  20.593  -16.630 1.00 31.37  ?  89  CYS B SG    1 
ATOM   2835 N  N     . LYS B 1 97  ? -6.943  17.900  -15.451 1.00 37.91  ?  90  LYS B N     1 
ATOM   2836 C  CA    . LYS B 1 97  ? -8.068  17.045  -15.787 1.00 40.03  ?  90  LYS B CA    1 
ATOM   2837 C  C     . LYS B 1 97  ? -9.317  17.445  -15.000 1.00 42.97  ?  90  LYS B C     1 
ATOM   2838 O  O     . LYS B 1 97  ? -10.382 17.549  -15.592 1.00 44.83  ?  90  LYS B O     1 
ATOM   2839 C  CB    . LYS B 1 97  ? -7.752  15.568  -15.574 1.00 40.23  ?  90  LYS B CB    1 
ATOM   2840 C  CG    . LYS B 1 97  ? -8.672  14.642  -16.360 1.00 42.11  ?  90  LYS B CG    1 
ATOM   2841 C  CD    . LYS B 1 97  ? -8.281  14.588  -17.819 1.00 40.60  ?  90  LYS B CD    1 
ATOM   2842 C  CE    . LYS B 1 97  ? -9.187  13.750  -18.685 1.00 42.69  ?  90  LYS B CE    1 
ATOM   2843 N  NZ    . LYS B 1 97  ? -8.934  14.057  -20.104 1.00 41.54  ?  90  LYS B NZ    1 
ATOM   2844 N  N     . GLU B 1 98  ? -9.181  17.735  -13.704 1.00 43.62  ?  91  GLU B N     1 
ATOM   2845 C  CA    . GLU B 1 98  ? -10.334 17.992  -12.848 1.00 46.84  ?  91  GLU B CA    1 
ATOM   2846 C  C     . GLU B 1 98  ? -10.848 19.425  -12.963 1.00 47.65  ?  91  GLU B C     1 
ATOM   2847 O  O     . GLU B 1 98  ? -12.066 19.620  -13.040 1.00 50.48  ?  91  GLU B O     1 
ATOM   2848 C  CB    . GLU B 1 98  ? -10.021 17.648  -11.393 1.00 47.76  ?  91  GLU B CB    1 
ATOM   2849 C  CG    . GLU B 1 98  ? -9.856  16.158  -11.164 1.00 48.29  ?  91  GLU B CG    1 
ATOM   2850 C  CD    . GLU B 1 98  ? -9.504  15.795  -9.729  1.00 49.49  ?  91  GLU B CD    1 
ATOM   2851 O  OE1   . GLU B 1 98  ? -9.015  14.674  -9.501  1.00 49.47  ?  91  GLU B OE1   1 
ATOM   2852 O  OE2   . GLU B 1 98  ? -9.757  16.629  -8.831  1.00 50.82  ?  91  GLU B OE2   1 
ATOM   2853 N  N     . THR B 1 99  ? -9.964  20.430  -12.914 1.00 45.70  ?  92  THR B N     1 
ATOM   2854 C  CA    . THR B 1 99  ? -10.400 21.821  -12.976 1.00 46.81  ?  92  THR B CA    1 
ATOM   2855 C  C     . THR B 1 99  ? -10.501 22.303  -14.426 1.00 45.96  ?  92  THR B C     1 
ATOM   2856 O  O     . THR B 1 99  ? -11.510 22.863  -14.845 1.00 48.16  ?  92  THR B O     1 
ATOM   2857 C  CB    . THR B 1 99  ? -9.485  22.719  -12.141 1.00 45.89  ?  92  THR B CB    1 
ATOM   2858 O  OG1   . THR B 1 99  ? -9.548  22.258  -10.791 1.00 47.30  ?  92  THR B OG1   1 
ATOM   2859 C  CG2   . THR B 1 99  ? -9.857  24.182  -12.197 1.00 47.29  ?  92  THR B CG2   1 
ATOM   2860 N  N     . LEU B 1 100 ? -9.442  22.137  -15.223 1.00 43.07  ?  93  LEU B N     1 
ATOM   2861 C  CA    . LEU B 1 100 ? -9.463  22.708  -16.564 1.00 42.54  ?  93  LEU B CA    1 
ATOM   2862 C  C     . LEU B 1 100 ? -10.256 21.837  -17.534 1.00 43.46  ?  93  LEU B C     1 
ATOM   2863 O  O     . LEU B 1 100 ? -10.621 22.334  -18.594 1.00 44.04  ?  93  LEU B O     1 
ATOM   2864 C  CB    . LEU B 1 100 ? -8.021  22.906  -17.060 1.00 39.55  ?  93  LEU B CB    1 
ATOM   2865 C  CG    . LEU B 1 100 ? -7.173  23.879  -16.246 1.00 38.90  ?  93  LEU B CG    1 
ATOM   2866 C  CD1   . LEU B 1 100 ? -5.811  24.073  -16.905 1.00 36.46  ?  93  LEU B CD1   1 
ATOM   2867 C  CD2   . LEU B 1 100 ? -7.837  25.234  -16.069 1.00 41.08  ?  93  LEU B CD2   1 
ATOM   2868 N  N     . GLN B 1 101 ? -10.517 20.573  -17.172 1.00 43.94  ?  94  GLN B N     1 
ATOM   2869 C  CA    . GLN B 1 101 ? -11.262 19.650  -18.016 1.00 45.21  ?  94  GLN B CA    1 
ATOM   2870 C  C     . GLN B 1 101 ? -10.630 19.511  -19.404 1.00 43.33  ?  94  GLN B C     1 
ATOM   2871 O  O     . GLN B 1 101 ? -11.342 19.455  -20.411 1.00 44.75  ?  94  GLN B O     1 
ATOM   2872 C  CB    . GLN B 1 101 ? -12.713 20.118  -18.120 1.00 48.68  ?  94  GLN B CB    1 
ATOM   2873 C  CG    . GLN B 1 101 ? -13.412 20.087  -16.770 1.00 51.10  ?  94  GLN B CG    1 
ATOM   2874 C  CD    . GLN B 1 101 ? -14.907 20.179  -16.949 1.00 55.06  ?  94  GLN B CD    1 
ATOM   2875 O  OE1   . GLN B 1 101 ? -15.457 21.248  -17.207 1.00 56.58  ?  94  GLN B OE1   1 
ATOM   2876 N  NE2   . GLN B 1 101 ? -15.565 19.037  -16.851 1.00 57.06  ?  94  GLN B NE2   1 
ATOM   2877 N  N     . LEU B 1 102 ? -9.301  19.325  -19.435 1.00 40.49  ?  95  LEU B N     1 
ATOM   2878 C  CA    . LEU B 1 102 ? -8.597  19.161  -20.699 1.00 38.89  ?  95  LEU B CA    1 
ATOM   2879 C  C     . LEU B 1 102 ? -8.943  17.813  -21.309 1.00 39.69  ?  95  LEU B C     1 
ATOM   2880 O  O     . LEU B 1 102 ? -9.193  16.844  -20.605 1.00 40.51  ?  95  LEU B O     1 
ATOM   2881 C  CB    . LEU B 1 102 ? -7.077  19.309  -20.483 1.00 36.12  ?  95  LEU B CB    1 
ATOM   2882 C  CG    . LEU B 1 102 ? -6.623  20.727  -20.134 1.00 35.53  ?  95  LEU B CG    1 
ATOM   2883 C  CD1   . LEU B 1 102 ? -5.145  20.801  -19.788 1.00 33.27  ?  95  LEU B CD1   1 
ATOM   2884 C  CD2   . LEU B 1 102 ? -6.924  21.660  -21.280 1.00 36.23  ?  95  LEU B CD2   1 
ATOM   2885 N  N     . GLU B 1 103 ? -8.894  17.744  -22.642 1.00 39.64  ?  96  GLU B N     1 
ATOM   2886 C  CA    . GLU B 1 103 ? -9.209  16.520  -23.357 1.00 40.71  ?  96  GLU B CA    1 
ATOM   2887 C  C     . GLU B 1 103 ? -8.169  15.437  -23.091 1.00 39.10  ?  96  GLU B C     1 
ATOM   2888 O  O     . GLU B 1 103 ? -8.494  14.263  -22.980 1.00 40.38  ?  96  GLU B O     1 
ATOM   2889 C  CB    . GLU B 1 103 ? -9.293  16.756  -24.862 1.00 41.17  ?  96  GLU B CB    1 
ATOM   2890 C  CG    . GLU B 1 103 ? -10.472 17.610  -25.291 1.00 43.56  ?  96  GLU B CG    1 
ATOM   2891 C  CD    . GLU B 1 103 ? -10.635 17.762  -26.799 1.00 44.57  ?  96  GLU B CD    1 
ATOM   2892 O  OE1   . GLU B 1 103 ? -10.090 16.920  -27.552 1.00 44.03  ?  96  GLU B OE1   1 
ATOM   2893 O  OE2   . GLU B 1 103 ? -11.301 18.729  -27.220 1.00 46.17  ?  96  GLU B OE2   1 
ATOM   2894 N  N     . SER B 1 104 ? -6.894  15.824  -23.027 1.00 36.61  ?  97  SER B N     1 
ATOM   2895 C  CA    . SER B 1 104 ? -5.828  14.856  -22.947 1.00 35.31  ?  97  SER B CA    1 
ATOM   2896 C  C     . SER B 1 104 ? -4.686  15.408  -22.097 1.00 33.22  ?  97  SER B C     1 
ATOM   2897 O  O     . SER B 1 104 ? -4.142  16.473  -22.390 1.00 32.06  ?  97  SER B O     1 
ATOM   2898 C  CB    . SER B 1 104 ? -5.329  14.479  -24.339 1.00 35.06  ?  97  SER B CB    1 
ATOM   2899 O  OG    . SER B 1 104 ? -4.242  13.554  -24.249 1.00 34.06  ?  97  SER B OG    1 
ATOM   2900 N  N     . VAL B 1 105 ? -4.346  14.651  -21.062 1.00 33.13  ?  98  VAL B N     1 
ATOM   2901 C  CA    . VAL B 1 105 ? -3.214  14.952  -20.207 1.00 31.53  ?  98  VAL B CA    1 
ATOM   2902 C  C     . VAL B 1 105 ? -2.218  13.821  -20.407 1.00 31.00  ?  98  VAL B C     1 
ATOM   2903 O  O     . VAL B 1 105 ? -2.564  12.688  -20.139 1.00 32.31  ?  98  VAL B O     1 
ATOM   2904 C  CB    . VAL B 1 105 ? -3.674  15.067  -18.746 1.00 32.37  ?  98  VAL B CB    1 
ATOM   2905 C  CG1   . VAL B 1 105 ? -2.511  15.238  -17.777 1.00 31.13  ?  98  VAL B CG1   1 
ATOM   2906 C  CG2   . VAL B 1 105 ? -4.655  16.211  -18.566 1.00 33.25  ?  98  VAL B CG2   1 
ATOM   2907 N  N     . SER B 1 106 ? -0.981  14.151  -20.840 1.00 29.45  ?  99  SER B N     1 
ATOM   2908 C  CA    . SER B 1 106 ? 0.029   13.139  -21.110 1.00 29.23  ?  99  SER B CA    1 
ATOM   2909 C  C     . SER B 1 106 ? 1.323   13.495  -20.384 1.00 28.04  ?  99  SER B C     1 
ATOM   2910 O  O     . SER B 1 106 ? 1.537   14.643  -20.019 1.00 27.22  ?  99  SER B O     1 
ATOM   2911 C  CB    . SER B 1 106 ? 0.240   12.922  -22.608 1.00 29.32  ?  99  SER B CB    1 
ATOM   2912 O  OG    . SER B 1 106 ? 0.690   14.079  -23.314 1.00 28.33  ?  99  SER B OG    1 
ATOM   2913 N  N     . ILE B 1 107 ? 2.208   12.501  -20.201 1.00 28.26  ?  100 ILE B N     1 
ATOM   2914 C  CA    . ILE B 1 107 ? 3.508   12.649  -19.571 1.00 27.60  ?  100 ILE B CA    1 
ATOM   2915 C  C     . ILE B 1 107 ? 4.471   11.841  -20.425 1.00 27.88  ?  100 ILE B C     1 
ATOM   2916 O  O     . ILE B 1 107 ? 4.058   10.787  -20.900 1.00 28.99  ?  100 ILE B O     1 
ATOM   2917 C  CB    . ILE B 1 107 ? 3.556   12.120  -18.121 1.00 28.37  ?  100 ILE B CB    1 
ATOM   2918 C  CG1   . ILE B 1 107 ? 2.312   12.501  -17.302 1.00 28.94  ?  100 ILE B CG1   1 
ATOM   2919 C  CG2   . ILE B 1 107 ? 4.862   12.572  -17.479 1.00 27.79  ?  100 ILE B CG2   1 
ATOM   2920 C  CD1   . ILE B 1 107 ? 2.125   11.641  -16.074 1.00 30.44  ?  100 ILE B CD1   1 
ATOM   2921 N  N     . VAL B 1 108 ? 5.679   12.383  -20.666 1.00 27.20  ?  101 VAL B N     1 
ATOM   2922 C  CA    . VAL B 1 108 ? 6.793   11.646  -21.255 1.00 27.81  ?  101 VAL B CA    1 
ATOM   2923 C  C     . VAL B 1 108 ? 7.907   11.511  -20.215 1.00 28.07  ?  101 VAL B C     1 
ATOM   2924 O  O     . VAL B 1 108 ? 8.294   12.482  -19.530 1.00 27.39  ?  101 VAL B O     1 
ATOM   2925 C  CB    . VAL B 1 108 ? 7.285   12.314  -22.555 1.00 27.47  ?  101 VAL B CB    1 
ATOM   2926 C  CG1   . VAL B 1 108 ? 7.701   13.744  -22.352 1.00 26.52  ?  101 VAL B CG1   1 
ATOM   2927 C  CG2   . VAL B 1 108 ? 8.438   11.515  -23.179 1.00 28.53  ?  101 VAL B CG2   1 
ATOM   2928 N  N     . THR B 1 109 ? 8.415   10.269  -20.057 1.00 29.42  ?  102 THR B N     1 
ATOM   2929 C  CA    . THR B 1 109 ? 9.324   9.968   -18.954 1.00 30.16  ?  102 THR B CA    1 
ATOM   2930 C  C     . THR B 1 109 ? 10.346  8.936   -19.416 1.00 31.73  ?  102 THR B C     1 
ATOM   2931 O  O     . THR B 1 109 ? 9.992   8.071   -20.247 1.00 32.60  ?  102 THR B O     1 
ATOM   2932 C  CB    . THR B 1 109 ? 8.586   9.408   -17.724 1.00 30.91  ?  102 THR B CB    1 
ATOM   2933 O  OG1   . THR B 1 109 ? 9.511   9.068   -16.669 1.00 32.01  ?  102 THR B OG1   1 
ATOM   2934 C  CG2   . THR B 1 109 ? 7.766   8.172   -18.053 1.00 32.25  ?  102 THR B CG2   1 
ATOM   2935 N  N     . ASN B 1 110 ? 11.566  8.994   -18.838 1.00 32.44  ?  103 ASN B N     1 
ATOM   2936 C  CA    . ASN B 1 110 ? 12.551  7.925   -19.017 1.00 34.48  ?  103 ASN B CA    1 
ATOM   2937 C  C     . ASN B 1 110 ? 12.157  6.652   -18.260 1.00 36.20  ?  103 ASN B C     1 
ATOM   2938 O  O     . ASN B 1 110 ? 12.783  5.605   -18.460 1.00 38.29  ?  103 ASN B O     1 
ATOM   2939 C  CB    . ASN B 1 110 ? 13.987  8.364   -18.686 1.00 35.20  ?  103 ASN B CB    1 
ATOM   2940 C  CG    . ASN B 1 110 ? 14.273  8.697   -17.237 1.00 35.44  ?  103 ASN B CG    1 
ATOM   2941 O  OD1   . ASN B 1 110 ? 13.735  8.051   -16.340 1.00 36.12  ?  103 ASN B OD1   1 
ATOM   2942 N  ND2   . ASN B 1 110 ? 15.048  9.760   -16.993 1.00 35.07  ?  103 ASN B ND2   1 
ATOM   2943 N  N     . GLY B 1 111 ? 11.177  6.722   -17.350 1.00 35.77  ?  104 GLY B N     1 
ATOM   2944 C  CA    . GLY B 1 111 ? 10.574  5.540   -16.758 1.00 37.64  ?  104 GLY B CA    1 
ATOM   2945 C  C     . GLY B 1 111 ? 11.253  5.047   -15.480 1.00 39.50  ?  104 GLY B C     1 
ATOM   2946 O  O     . GLY B 1 111 ? 10.594  4.395   -14.672 1.00 40.90  ?  104 GLY B O     1 
ATOM   2947 N  N     . SER B 1 112 ? 12.498  5.471   -15.236 1.00 39.68  ?  105 SER B N     1 
ATOM   2948 C  CA    . SER B 1 112 ? 13.276  4.903   -14.131 1.00 41.99  ?  105 SER B CA    1 
ATOM   2949 C  C     . SER B 1 112 ? 12.611  5.157   -12.773 1.00 42.12  ?  105 SER B C     1 
ATOM   2950 O  O     . SER B 1 112 ? 12.561  4.246   -11.942 1.00 44.53  ?  105 SER B O     1 
ATOM   2951 C  CB    . SER B 1 112 ? 14.710  5.360   -14.151 1.00 42.44  ?  105 SER B CB    1 
ATOM   2952 O  OG    . SER B 1 112 ? 14.804  6.766   -14.280 1.00 40.14  ?  105 SER B OG    1 
ATOM   2953 N  N     . LEU B 1 113 ? 12.083  6.370   -12.524 1.00 39.91  ?  106 LEU B N     1 
ATOM   2954 C  CA    . LEU B 1 113 ? 11.588  6.701   -11.194 1.00 40.36  ?  106 LEU B CA    1 
ATOM   2955 C  C     . LEU B 1 113 ? 10.087  6.457   -11.018 1.00 40.28  ?  106 LEU B C     1 
ATOM   2956 O  O     . LEU B 1 113 ? 9.585   6.562   -9.903  1.00 41.21  ?  106 LEU B O     1 
ATOM   2957 C  CB    . LEU B 1 113 ? 11.923  8.168   -10.889 1.00 38.66  ?  106 LEU B CB    1 
ATOM   2958 C  CG    . LEU B 1 113 ? 13.407  8.548   -10.896 1.00 39.18  ?  106 LEU B CG    1 
ATOM   2959 C  CD1   . LEU B 1 113 ? 13.565  10.071  -10.895 1.00 37.42  ?  106 LEU B CD1   1 
ATOM   2960 C  CD2   . LEU B 1 113 ? 14.147  7.962   -9.700  1.00 41.93  ?  106 LEU B CD2   1 
ATOM   2961 N  N     . VAL B 1 114 ? 9.354   6.131   -12.085 1.00 39.51  ?  107 VAL B N     1 
ATOM   2962 C  CA    . VAL B 1 114 ? 7.904   5.959   -11.992 1.00 39.67  ?  107 VAL B CA    1 
ATOM   2963 C  C     . VAL B 1 114 ? 7.554   4.828   -11.022 1.00 42.73  ?  107 VAL B C     1 
ATOM   2964 O  O     . VAL B 1 114 ? 8.088   3.737   -11.184 1.00 44.71  ?  107 VAL B O     1 
ATOM   2965 C  CB    . VAL B 1 114 ? 7.297   5.591   -13.368 1.00 39.03  ?  107 VAL B CB    1 
ATOM   2966 C  CG1   . VAL B 1 114 ? 5.795   5.376   -13.244 1.00 39.69  ?  107 VAL B CG1   1 
ATOM   2967 C  CG2   . VAL B 1 114 ? 7.585   6.604   -14.473 1.00 36.45  ?  107 VAL B CG2   1 
ATOM   2968 N  N     . LYS B 1 115 ? 6.577   5.031   -10.119 1.00 43.47  ?  108 LYS B N     1 
ATOM   2969 C  CA    . LYS B 1 115 ? 6.155   3.955   -9.230  1.00 46.79  ?  108 LYS B CA    1 
ATOM   2970 C  C     . LYS B 1 115 ? 4.658   3.675   -9.401  1.00 47.62  ?  108 LYS B C     1 
ATOM   2971 O  O     . LYS B 1 115 ? 3.876   4.566   -9.729  1.00 45.74  ?  108 LYS B O     1 
ATOM   2972 C  CB    . LYS B 1 115 ? 6.483   4.302   -7.774  1.00 48.06  ?  108 LYS B CB    1 
ATOM   2973 C  CG    . LYS B 1 115 ? 7.956   4.313   -7.415  1.00 48.44  ?  108 LYS B CG    1 
ATOM   2974 C  CD    . LYS B 1 115 ? 8.160   4.366   -5.918  1.00 50.71  ?  108 LYS B CD    1 
ATOM   2975 C  CE    . LYS B 1 115 ? 9.609   4.546   -5.516  1.00 51.19  ?  108 LYS B CE    1 
ATOM   2976 N  NZ    . LYS B 1 115 ? 9.718   5.060   -4.126  1.00 52.66  ?  108 LYS B NZ    1 
ATOM   2977 N  N     . GLU B 1 116 ? 4.253   2.424   -9.131  1.00 50.89  ?  109 GLU B N     1 
ATOM   2978 C  CA    . GLU B 1 116 ? 2.863   2.020   -9.272  1.00 52.43  ?  109 GLU B CA    1 
ATOM   2979 C  C     . GLU B 1 116 ? 1.946   2.940   -8.477  1.00 52.14  ?  109 GLU B C     1 
ATOM   2980 O  O     . GLU B 1 116 ? 0.876   3.302   -8.954  1.00 51.58  ?  109 GLU B O     1 
ATOM   2981 C  CB    . GLU B 1 116 ? 2.672   0.561   -8.835  1.00 56.72  ?  109 GLU B CB    1 
ATOM   2982 C  CG    . GLU B 1 116 ? 1.354   -0.034  -9.289  1.00 58.67  ?  109 GLU B CG    1 
ATOM   2983 C  CD    . GLU B 1 116 ? 1.240   -1.519  -8.982  1.00 63.25  ?  109 GLU B CD    1 
ATOM   2984 O  OE1   . GLU B 1 116 ? 2.209   -2.072  -8.449  1.00 64.78  ?  109 GLU B OE1   1 
ATOM   2985 O  OE2   . GLU B 1 116 ? 0.188   -2.087  -9.262  1.00 65.51  ?  109 GLU B OE2   1 
ATOM   2986 N  N     . GLN B 1 117 ? 2.377   3.335   -7.273  1.00 52.77  ?  110 GLN B N     1 
ATOM   2987 C  CA    . GLN B 1 117 ? 1.571   4.147   -6.384  1.00 53.14  ?  110 GLN B CA    1 
ATOM   2988 C  C     . GLN B 1 117 ? 1.135   5.455   -7.070  1.00 49.79  ?  110 GLN B C     1 
ATOM   2989 O  O     . GLN B 1 117 ? 0.044   5.943   -6.810  1.00 50.35  ?  110 GLN B O     1 
ATOM   2990 C  CB    . GLN B 1 117 ? 2.321   4.406   -5.071  1.00 54.28  ?  110 GLN B CB    1 
ATOM   2991 C  CG    . GLN B 1 117 ? 3.594   5.224   -5.267  1.00 51.43  ?  110 GLN B CG    1 
ATOM   2992 C  CD    . GLN B 1 117 ? 4.625   5.116   -4.168  1.00 53.10  ?  110 GLN B CD    1 
ATOM   2993 O  OE1   . GLN B 1 117 ? 5.008   4.020   -3.762  1.00 55.92  ?  110 GLN B OE1   1 
ATOM   2994 N  NE2   . GLN B 1 117 ? 5.145   6.258   -3.740  1.00 51.56  ?  110 GLN B NE2   1 
ATOM   2995 N  N     . PHE B 1 118 ? 1.983   6.035   -7.927  1.00 46.68  ?  111 PHE B N     1 
ATOM   2996 C  CA    . PHE B 1 118 ? 1.618   7.282   -8.598  1.00 43.84  ?  111 PHE B CA    1 
ATOM   2997 C  C     . PHE B 1 118 ? 0.463   7.049   -9.583  1.00 43.90  ?  111 PHE B C     1 
ATOM   2998 O  O     . PHE B 1 118 ? -0.459  7.851   -9.731  1.00 43.33  ?  111 PHE B O     1 
ATOM   2999 C  CB    . PHE B 1 118 ? 2.841   7.852   -9.318  1.00 41.08  ?  111 PHE B CB    1 
ATOM   3000 C  CG    . PHE B 1 118 ? 2.674   9.245   -9.877  1.00 38.45  ?  111 PHE B CG    1 
ATOM   3001 C  CD1   . PHE B 1 118 ? 2.093   9.464   -11.115 1.00 37.09  ?  111 PHE B CD1   1 
ATOM   3002 C  CD2   . PHE B 1 118 ? 3.126   10.357  -9.181  1.00 37.64  ?  111 PHE B CD2   1 
ATOM   3003 C  CE1   . PHE B 1 118 ? 1.980   10.737  -11.647 1.00 35.02  ?  111 PHE B CE1   1 
ATOM   3004 C  CE2   . PHE B 1 118 ? 2.948   11.638  -9.689  1.00 35.65  ?  111 PHE B CE2   1 
ATOM   3005 C  CZ    . PHE B 1 118 ? 2.389   11.829  -10.931 1.00 34.34  ?  111 PHE B CZ    1 
ATOM   3006 N  N     . LEU B 1 119 ? 0.521   5.942   -10.310 1.00 44.84  ?  112 LEU B N     1 
ATOM   3007 C  CA    . LEU B 1 119 ? -0.463  5.685   -11.347 1.00 45.06  ?  112 LEU B CA    1 
ATOM   3008 C  C     . LEU B 1 119 ? -1.798  5.291   -10.707 1.00 48.11  ?  112 LEU B C     1 
ATOM   3009 O  O     . LEU B 1 119 ? -2.861  5.629   -11.225 1.00 48.24  ?  112 LEU B O     1 
ATOM   3010 C  CB    . LEU B 1 119 ? 0.084   4.623   -12.311 1.00 45.46  ?  112 LEU B CB    1 
ATOM   3011 C  CG    . LEU B 1 119 ? 1.393   4.976   -13.019 1.00 42.89  ?  112 LEU B CG    1 
ATOM   3012 C  CD1   . LEU B 1 119 ? 1.778   3.880   -14.014 1.00 43.85  ?  112 LEU B CD1   1 
ATOM   3013 C  CD2   . LEU B 1 119 ? 1.315   6.321   -13.723 1.00 39.87  ?  112 LEU B CD2   1 
ATOM   3014 N  N     . GLN B 1 120 ? -1.743  4.635   -9.546  1.00 50.84  ?  113 GLN B N     1 
ATOM   3015 C  CA    . GLN B 1 120 ? -2.928  4.347   -8.748  1.00 54.15  ?  113 GLN B CA    1 
ATOM   3016 C  C     . GLN B 1 120 ? -3.551  5.627   -8.207  1.00 53.32  ?  113 GLN B C     1 
ATOM   3017 O  O     . GLN B 1 120 ? -4.774  5.784   -8.199  1.00 54.99  ?  113 GLN B O     1 
ATOM   3018 C  CB    . GLN B 1 120 ? -2.523  3.412   -7.611  1.00 57.32  ?  113 GLN B CB    1 
ATOM   3019 C  CG    . GLN B 1 120 ? -3.685  2.869   -6.802  1.00 61.59  ?  113 GLN B CG    1 
ATOM   3020 C  CD    . GLN B 1 120 ? -3.204  1.766   -5.894  1.00 65.06  ?  113 GLN B CD    1 
ATOM   3021 O  OE1   . GLN B 1 120 ? -2.013  1.668   -5.593  1.00 64.13  ?  113 GLN B OE1   1 
ATOM   3022 N  NE2   . GLN B 1 120 ? -4.129  0.927   -5.452  1.00 69.45  ?  113 GLN B NE2   1 
ATOM   3023 N  N     . LYS B 1 121 ? -2.723  6.541   -7.697  1.00 51.22  ?  114 LYS B N     1 
ATOM   3024 C  CA    . LYS B 1 121 ? -3.262  7.779   -7.140  1.00 50.75  ?  114 LYS B CA    1 
ATOM   3025 C  C     . LYS B 1 121 ? -3.793  8.714   -8.232  1.00 48.39  ?  114 LYS B C     1 
ATOM   3026 O  O     . LYS B 1 121 ? -4.849  9.328   -8.044  1.00 49.44  ?  114 LYS B O     1 
ATOM   3027 C  CB    . LYS B 1 121 ? -2.198  8.473   -6.280  1.00 49.59  ?  114 LYS B CB    1 
ATOM   3028 C  CG    . LYS B 1 121 ? -2.562  9.844   -5.714  1.00 49.05  ?  114 LYS B CG    1 
ATOM   3029 C  CD    . LYS B 1 121 ? -1.886  10.111  -4.357  1.00 50.24  ?  114 LYS B CD    1 
ATOM   3030 C  CE    . LYS B 1 121 ? -1.451  11.543  -4.110  1.00 48.39  ?  114 LYS B CE    1 
ATOM   3031 N  NZ    . LYS B 1 121 ? -2.525  12.525  -4.394  1.00 48.17  ?  114 LYS B NZ    1 
ATOM   3032 N  N     . HIS B 1 122 ? -3.060  8.876   -9.345  1.00 45.49  ?  115 HIS B N     1 
ATOM   3033 C  CA    . HIS B 1 122 ? -3.339  9.934   -10.324 1.00 43.14  ?  115 HIS B CA    1 
ATOM   3034 C  C     . HIS B 1 122 ? -3.867  9.403   -11.667 1.00 43.04  ?  115 HIS B C     1 
ATOM   3035 O  O     . HIS B 1 122 ? -4.153  10.192  -12.569 1.00 41.47  ?  115 HIS B O     1 
ATOM   3036 C  CB    . HIS B 1 122 ? -2.064  10.766  -10.618 1.00 40.05  ?  115 HIS B CB    1 
ATOM   3037 C  CG    . HIS B 1 122 ? -1.521  11.455  -9.405  1.00 40.12  ?  115 HIS B CG    1 
ATOM   3038 N  ND1   . HIS B 1 122 ? -2.172  12.525  -8.847  1.00 40.55  ?  115 HIS B ND1   1 
ATOM   3039 C  CD2   . HIS B 1 122 ? -0.461  11.209  -8.607  1.00 40.30  ?  115 HIS B CD2   1 
ATOM   3040 C  CE1   . HIS B 1 122 ? -1.495  12.941  -7.779  1.00 40.85  ?  115 HIS B CE1   1 
ATOM   3041 N  NE2   . HIS B 1 122 ? -0.493  12.131  -7.584  1.00 40.81  ?  115 HIS B NE2   1 
ATOM   3042 N  N     . GLY B 1 123 ? -3.989  8.074   -11.827 1.00 44.99  ?  116 GLY B N     1 
ATOM   3043 C  CA    . GLY B 1 123 ? -4.275  7.455   -13.114 1.00 45.07  ?  116 GLY B CA    1 
ATOM   3044 C  C     . GLY B 1 123 ? -5.563  7.908   -13.798 1.00 45.79  ?  116 GLY B C     1 
ATOM   3045 O  O     . GLY B 1 123 ? -5.624  8.031   -15.017 1.00 44.67  ?  116 GLY B O     1 
ATOM   3046 N  N     . ARG B 1 124 ? -6.600  8.201   -13.025 1.00 47.91  ?  117 ARG B N     1 
ATOM   3047 C  CA    . ARG B 1 124 ? -7.840  8.696   -13.597 1.00 48.99  ?  117 ARG B CA    1 
ATOM   3048 C  C     . ARG B 1 124 ? -7.627  10.012  -14.349 1.00 46.05  ?  117 ARG B C     1 
ATOM   3049 O  O     . ARG B 1 124 ? -8.445  10.365  -15.206 1.00 46.54  ?  117 ARG B O     1 
ATOM   3050 C  CB    . ARG B 1 124 ? -8.889  8.905   -12.498 1.00 51.97  ?  117 ARG B CB    1 
ATOM   3051 C  CG    . ARG B 1 124 ? -8.551  10.009  -11.506 1.00 50.81  ?  117 ARG B CG    1 
ATOM   3052 C  CD    . ARG B 1 124 ? -9.536  10.094  -10.352 1.00 54.26  ?  117 ARG B CD    1 
ATOM   3053 N  NE    . ARG B 1 124 ? -9.264  11.235  -9.484  1.00 53.37  ?  117 ARG B NE    1 
ATOM   3054 C  CZ    . ARG B 1 124 ? -8.205  11.357  -8.692  1.00 52.08  ?  117 ARG B CZ    1 
ATOM   3055 N  NH1   . ARG B 1 124 ? -7.328  10.375  -8.589  1.00 51.68  ?  117 ARG B NH1   1 
ATOM   3056 N  NH2   . ARG B 1 124 ? -8.031  12.464  -7.992  1.00 51.53  ?  117 ARG B NH2   1 
ATOM   3057 N  N     . ASN B 1 125 ? -6.536  10.734  -14.013 1.00 43.39  ?  118 ASN B N     1 
ATOM   3058 C  CA    . ASN B 1 125 ? -6.264  12.033  -14.598 1.00 40.98  ?  118 ASN B CA    1 
ATOM   3059 C  C     . ASN B 1 125 ? -5.159  11.987  -15.649 1.00 38.41  ?  118 ASN B C     1 
ATOM   3060 O  O     . ASN B 1 125 ? -4.840  13.036  -16.171 1.00 36.61  ?  118 ASN B O     1 
ATOM   3061 C  CB    . ASN B 1 125 ? -5.933  13.073  -13.536 1.00 40.32  ?  118 ASN B CB    1 
ATOM   3062 C  CG    . ASN B 1 125 ? -7.116  13.306  -12.619 1.00 43.10  ?  118 ASN B CG    1 
ATOM   3063 O  OD1   . ASN B 1 125 ? -8.250  13.315  -13.088 1.00 44.84  ?  118 ASN B OD1   1 
ATOM   3064 N  ND2   . ASN B 1 125 ? -6.881  13.438  -11.327 1.00 43.93  ?  118 ASN B ND2   1 
ATOM   3065 N  N     . ILE B 1 126 ? -4.600  10.809  -15.934 1.00 38.62  ?  119 ILE B N     1 
ATOM   3066 C  CA    . ILE B 1 126 ? -3.569  10.640  -16.950 1.00 36.73  ?  119 ILE B CA    1 
ATOM   3067 C  C     . ILE B 1 126 ? -4.186  9.868   -18.114 1.00 37.98  ?  119 ILE B C     1 
ATOM   3068 O  O     . ILE B 1 126 ? -4.598  8.721   -17.954 1.00 40.19  ?  119 ILE B O     1 
ATOM   3069 C  CB    . ILE B 1 126 ? -2.361  9.854   -16.398 1.00 36.40  ?  119 ILE B CB    1 
ATOM   3070 C  CG1   . ILE B 1 126 ? -1.821  10.476  -15.102 1.00 35.83  ?  119 ILE B CG1   1 
ATOM   3071 C  CG2   . ILE B 1 126 ? -1.276  9.667   -17.451 1.00 34.84  ?  119 ILE B CG2   1 
ATOM   3072 C  CD1   . ILE B 1 126 ? -0.832  9.613   -14.391 1.00 36.34  ?  119 ILE B CD1   1 
ATOM   3073 N  N     . ASP B 1 127 ? -4.169  10.475  -19.290 1.00 36.82  ?  120 ASP B N     1 
ATOM   3074 C  CA    . ASP B 1 127 ? -4.752  9.864   -20.470 1.00 38.14  ?  120 ASP B CA    1 
ATOM   3075 C  C     . ASP B 1 127 ? -3.694  8.986   -21.109 1.00 37.66  ?  120 ASP B C     1 
ATOM   3076 O  O     . ASP B 1 127 ? -4.010  7.893   -21.560 1.00 39.61  ?  120 ASP B O     1 
ATOM   3077 C  CB    . ASP B 1 127 ? -5.304  10.955  -21.384 1.00 37.62  ?  120 ASP B CB    1 
ATOM   3078 C  CG    . ASP B 1 127 ? -6.511  11.649  -20.765 1.00 38.94  ?  120 ASP B CG    1 
ATOM   3079 O  OD1   . ASP B 1 127 ? -7.518  10.954  -20.573 1.00 41.51  ?  120 ASP B OD1   1 
ATOM   3080 O  OD2   . ASP B 1 127 ? -6.440  12.859  -20.450 1.00 37.74  ?  120 ASP B OD2   1 
ATOM   3081 N  N     . ILE B 1 128 ? -2.461  9.509   -21.192 1.00 35.40  ?  121 ILE B N     1 
ATOM   3082 C  CA    . ILE B 1 128 ? -1.367  8.866   -21.904 1.00 34.98  ?  121 ILE B CA    1 
ATOM   3083 C  C     . ILE B 1 128 ? -0.111  8.964   -21.065 1.00 33.65  ?  121 ILE B C     1 
ATOM   3084 O  O     . ILE B 1 128 ? 0.185   10.038  -20.555 1.00 32.10  ?  121 ILE B O     1 
ATOM   3085 C  CB    . ILE B 1 128 ? -1.149  9.559   -23.256 1.00 33.99  ?  121 ILE B CB    1 
ATOM   3086 C  CG1   . ILE B 1 128 ? -2.400  9.478   -24.136 1.00 35.63  ?  121 ILE B CG1   1 
ATOM   3087 C  CG2   . ILE B 1 128 ? 0.067   9.025   -23.984 1.00 33.69  ?  121 ILE B CG2   1 
ATOM   3088 C  CD1   . ILE B 1 128 ? -2.421  10.514  -25.210 1.00 34.79  ?  121 ILE B CD1   1 
ATOM   3089 N  N     . LEU B 1 129 ? 0.626   7.854   -21.008 1.00 34.56  ?  122 LEU B N     1 
ATOM   3090 C  CA    . LEU B 1 129 ? 1.962   7.823   -20.428 1.00 33.70  ?  122 LEU B CA    1 
ATOM   3091 C  C     . LEU B 1 129 ? 2.935   7.295   -21.479 1.00 33.87  ?  122 LEU B C     1 
ATOM   3092 O  O     . LEU B 1 129 ? 2.767   6.183   -21.994 1.00 35.71  ?  122 LEU B O     1 
ATOM   3093 C  CB    . LEU B 1 129 ? 1.924   6.939   -19.185 1.00 35.31  ?  122 LEU B CB    1 
ATOM   3094 C  CG    . LEU B 1 129 ? 3.253   6.777   -18.458 1.00 35.02  ?  122 LEU B CG    1 
ATOM   3095 C  CD1   . LEU B 1 129 ? 3.792   8.103   -17.983 1.00 32.95  ?  122 LEU B CD1   1 
ATOM   3096 C  CD2   . LEU B 1 129 ? 3.126   5.863   -17.257 1.00 37.09  ?  122 LEU B CD2   1 
ATOM   3097 N  N     . ALA B 1 130 ? 3.883   8.152   -21.874 1.00 32.23  ?  123 ALA B N     1 
ATOM   3098 C  CA    . ALA B 1 130 ? 4.929   7.806   -22.822 1.00 32.52  ?  123 ALA B CA    1 
ATOM   3099 C  C     . ALA B 1 130 ? 6.257   7.509   -22.105 1.00 32.68  ?  123 ALA B C     1 
ATOM   3100 O  O     . ALA B 1 130 ? 6.748   8.270   -21.268 1.00 31.57  ?  123 ALA B O     1 
ATOM   3101 C  CB    . ALA B 1 130 ? 5.079   8.929   -23.812 1.00 31.23  ?  123 ALA B CB    1 
ATOM   3102 N  N     . VAL B 1 131 ? 6.879   6.381   -22.467 1.00 34.42  ?  124 VAL B N     1 
ATOM   3103 C  CA    . VAL B 1 131 ? 8.146   5.954   -21.894 1.00 35.18  ?  124 VAL B CA    1 
ATOM   3104 C  C     . VAL B 1 131 ? 9.191   5.994   -23.000 1.00 35.56  ?  124 VAL B C     1 
ATOM   3105 O  O     . VAL B 1 131 ? 8.941   5.528   -24.112 1.00 36.52  ?  124 VAL B O     1 
ATOM   3106 C  CB    . VAL B 1 131 ? 8.042   4.564   -21.241 1.00 37.54  ?  124 VAL B CB    1 
ATOM   3107 C  CG1   . VAL B 1 131 ? 9.333   4.201   -20.548 1.00 38.55  ?  124 VAL B CG1   1 
ATOM   3108 C  CG2   . VAL B 1 131 ? 6.886   4.433   -20.275 1.00 37.76  ?  124 VAL B CG2   1 
ATOM   3109 N  N     . SER B 1 132 ? 10.326  6.626   -22.725 1.00 34.99  ?  125 SER B N     1 
ATOM   3110 C  CA    . SER B 1 132 ? 11.385  6.783   -23.693 1.00 35.61  ?  125 SER B CA    1 
ATOM   3111 C  C     . SER B 1 132 ? 12.384  5.643   -23.528 1.00 38.03  ?  125 SER B C     1 
ATOM   3112 O  O     . SER B 1 132 ? 13.028  5.570   -22.492 1.00 38.42  ?  125 SER B O     1 
ATOM   3113 C  CB    . SER B 1 132 ? 12.083  8.074   -23.491 1.00 34.25  ?  125 SER B CB    1 
ATOM   3114 O  OG    . SER B 1 132 ? 11.274  9.175   -23.854 1.00 32.45  ?  125 SER B OG    1 
ATOM   3115 N  N     . CYS B 1 133 ? 12.497  4.799   -24.548 1.00 39.88  ?  126 CYS B N     1 
ATOM   3116 C  CA    . CYS B 1 133 ? 13.428  3.685   -24.530 1.00 42.65  ?  126 CYS B CA    1 
ATOM   3117 C  C     . CYS B 1 133 ? 13.882  3.441   -25.957 1.00 44.20  ?  126 CYS B C     1 
ATOM   3118 O  O     . CYS B 1 133 ? 13.065  3.137   -26.823 1.00 44.54  ?  126 CYS B O     1 
ATOM   3119 C  CB    . CYS B 1 133 ? 12.785  2.441   -23.956 1.00 44.33  ?  126 CYS B CB    1 
ATOM   3120 S  SG    . CYS B 1 133 ? 13.965  1.078   -23.665 1.00 48.17  ?  126 CYS B SG    1 
ATOM   3121 N  N     . ASP B 1 134 ? 15.162  3.670   -26.195 1.00 45.28  ?  127 ASP B N     1 
ATOM   3122 C  CA    . ASP B 1 134 ? 15.674  3.822   -27.543 1.00 46.51  ?  127 ASP B CA    1 
ATOM   3123 C  C     . ASP B 1 134 ? 16.106  2.462   -28.100 1.00 50.04  ?  127 ASP B C     1 
ATOM   3124 O  O     . ASP B 1 134 ? 16.289  2.345   -29.308 1.00 51.54  ?  127 ASP B O     1 
ATOM   3125 C  CB    . ASP B 1 134 ? 16.854  4.787   -27.607 1.00 46.45  ?  127 ASP B CB    1 
ATOM   3126 C  CG    . ASP B 1 134 ? 16.527  6.151   -27.011 1.00 43.42  ?  127 ASP B CG    1 
ATOM   3127 O  OD1   . ASP B 1 134 ? 15.478  6.748   -27.391 1.00 41.48  ?  127 ASP B OD1   1 
ATOM   3128 O  OD2   . ASP B 1 134 ? 17.268  6.556   -26.116 1.00 43.27  ?  127 ASP B OD2   1 
ATOM   3129 N  N     . SER B 1 135 ? 16.338  1.482   -27.227 1.00 51.68  ?  128 SER B N     1 
ATOM   3130 C  CA    . SER B 1 135 ? 16.824  0.178   -27.696 1.00 55.51  ?  128 SER B CA    1 
ATOM   3131 C  C     . SER B 1 135 ? 16.352  -0.947  -26.787 1.00 56.92  ?  128 SER B C     1 
ATOM   3132 O  O     . SER B 1 135 ? 16.152  -0.764  -25.586 1.00 55.56  ?  128 SER B O     1 
ATOM   3133 C  CB    . SER B 1 135 ? 18.325  0.167   -27.811 1.00 57.81  ?  128 SER B CB    1 
ATOM   3134 O  OG    . SER B 1 135 ? 18.810  -1.110  -28.233 1.00 61.89  ?  128 SER B OG    1 
ATOM   3135 N  N     . PHE B 1 136 ? 16.260  -2.162  -27.352 1.00 60.22  ?  129 PHE B N     1 
ATOM   3136 C  CA    . PHE B 1 136 ? 15.962  -3.316  -26.521 1.00 62.43  ?  129 PHE B CA    1 
ATOM   3137 C  C     . PHE B 1 136 ? 17.232  -4.105  -26.228 1.00 66.10  ?  129 PHE B C     1 
ATOM   3138 O  O     . PHE B 1 136 ? 17.166  -5.183  -25.638 1.00 68.88  ?  129 PHE B O     1 
ATOM   3139 C  CB    . PHE B 1 136 ? 14.852  -4.133  -27.163 1.00 63.85  ?  129 PHE B CB    1 
ATOM   3140 C  CG    . PHE B 1 136 ? 13.537  -3.411  -27.140 1.00 60.53  ?  129 PHE B CG    1 
ATOM   3141 C  CD1   . PHE B 1 136 ? 12.728  -3.455  -26.018 1.00 59.39  ?  129 PHE B CD1   1 
ATOM   3142 C  CD2   . PHE B 1 136 ? 13.132  -2.657  -28.225 1.00 58.84  ?  129 PHE B CD2   1 
ATOM   3143 C  CE1   . PHE B 1 136 ? 11.522  -2.777  -25.993 1.00 56.67  ?  129 PHE B CE1   1 
ATOM   3144 C  CE2   . PHE B 1 136 ? 11.931  -1.966  -28.186 1.00 56.08  ?  129 PHE B CE2   1 
ATOM   3145 C  CZ    . PHE B 1 136 ? 11.130  -2.032  -27.073 1.00 55.02  ?  129 PHE B CZ    1 
ATOM   3146 N  N     . ASN B 1 137 ? 18.370  -3.529  -26.640 1.00 66.36  ?  130 ASN B N     1 
ATOM   3147 C  CA    . ASN B 1 137 ? 19.667  -3.992  -26.200 1.00 69.47  ?  130 ASN B CA    1 
ATOM   3148 C  C     . ASN B 1 137 ? 20.189  -3.064  -25.106 1.00 67.26  ?  130 ASN B C     1 
ATOM   3149 O  O     . ASN B 1 137 ? 20.560  -1.934  -25.383 1.00 65.09  ?  130 ASN B O     1 
ATOM   3150 C  CB    . ASN B 1 137 ? 20.662  -4.047  -27.357 1.00 72.10  ?  130 ASN B CB    1 
ATOM   3151 C  CG    . ASN B 1 137 ? 21.876  -4.873  -27.001 1.00 76.53  ?  130 ASN B CG    1 
ATOM   3152 O  OD1   . ASN B 1 137 ? 22.940  -4.328  -26.719 1.00 76.96  ?  130 ASN B OD1   1 
ATOM   3153 N  ND2   . ASN B 1 137 ? 21.705  -6.184  -26.956 1.00 80.09  ?  130 ASN B ND2   1 
ATOM   3154 N  N     . GLU B 1 138 ? 20.362  -3.600  -23.896 1.00 68.55  ?  131 GLU B N     1 
ATOM   3155 C  CA    . GLU B 1 138 ? 20.729  -2.774  -22.753 1.00 66.65  ?  131 GLU B CA    1 
ATOM   3156 C  C     . GLU B 1 138 ? 22.121  -2.164  -22.930 1.00 67.73  ?  131 GLU B C     1 
ATOM   3157 O  O     . GLU B 1 138 ? 22.387  -1.086  -22.404 1.00 65.44  ?  131 GLU B O     1 
ATOM   3158 C  CB    . GLU B 1 138 ? 20.566  -3.576  -21.463 1.00 68.39  ?  131 GLU B CB    1 
ATOM   3159 C  CG    . GLU B 1 138 ? 19.119  -3.932  -21.103 1.00 66.98  ?  131 GLU B CG    1 
ATOM   3160 C  CD    . GLU B 1 138 ? 18.216  -2.742  -20.781 1.00 62.30  ?  131 GLU B CD    1 
ATOM   3161 O  OE1   . GLU B 1 138 ? 18.630  -1.598  -21.073 1.00 59.90  ?  131 GLU B OE1   1 
ATOM   3162 O  OE2   . GLU B 1 138 ? 17.125  -2.954  -20.215 1.00 61.42  ?  131 GLU B OE2   1 
ATOM   3163 N  N     . ALA B 1 139 ? 23.024  -2.826  -23.670 1.00 71.53  ?  132 ALA B N     1 
ATOM   3164 C  CA    . ALA B 1 139 ? 24.351  -2.261  -23.911 1.00 73.08  ?  132 ALA B CA    1 
ATOM   3165 C  C     . ALA B 1 139 ? 24.261  -1.031  -24.811 1.00 70.21  ?  132 ALA B C     1 
ATOM   3166 O  O     . ALA B 1 139 ? 25.089  -0.117  -24.730 1.00 70.00  ?  132 ALA B O     1 
ATOM   3167 C  CB    . ALA B 1 139 ? 25.267  -3.285  -24.536 1.00 78.19  ?  132 ALA B CB    1 
ATOM   3168 N  N     . THR B 1 140 ? 23.275  -1.024  -25.716 1.00 68.45  ?  133 THR B N     1 
ATOM   3169 C  CA    . THR B 1 140 ? 23.030  0.156   -26.531 1.00 65.69  ?  133 THR B CA    1 
ATOM   3170 C  C     . THR B 1 140 ? 22.492  1.285   -25.654 1.00 61.56  ?  133 THR B C     1 
ATOM   3171 O  O     . THR B 1 140 ? 22.886  2.442   -25.818 1.00 60.17  ?  133 THR B O     1 
ATOM   3172 C  CB    . THR B 1 140 ? 22.073  -0.109  -27.699 1.00 65.11  ?  133 THR B CB    1 
ATOM   3173 O  OG1   . THR B 1 140 ? 22.571  -1.177  -28.510 1.00 69.31  ?  133 THR B OG1   1 
ATOM   3174 C  CG2   . THR B 1 140 ? 21.887  1.124   -28.551 1.00 62.76  ?  133 THR B CG2   1 
ATOM   3175 N  N     . ASN B 1 141 ? 21.594  0.956   -24.726 1.00 59.94  ?  134 ASN B N     1 
ATOM   3176 C  CA    . ASN B 1 141 ? 21.008  1.981   -23.880 1.00 56.31  ?  134 ASN B CA    1 
ATOM   3177 C  C     . ASN B 1 141 ? 22.078  2.614   -23.002 1.00 56.85  ?  134 ASN B C     1 
ATOM   3178 O  O     . ASN B 1 141 ? 22.030  3.812   -22.729 1.00 54.44  ?  134 ASN B O     1 
ATOM   3179 C  CB    . ASN B 1 141 ? 19.861  1.449   -23.035 1.00 55.06  ?  134 ASN B CB    1 
ATOM   3180 C  CG    . ASN B 1 141 ? 18.614  1.223   -23.857 1.00 53.74  ?  134 ASN B CG    1 
ATOM   3181 O  OD1   . ASN B 1 141 ? 18.340  1.989   -24.793 1.00 52.09  ?  134 ASN B OD1   1 
ATOM   3182 N  ND2   . ASN B 1 141 ? 17.903  0.146   -23.553 1.00 54.97  ?  134 ASN B ND2   1 
ATOM   3183 N  N     . ILE B 1 142 ? 23.024  1.790   -22.527 1.00 60.34  ?  135 ILE B N     1 
ATOM   3184 C  CA    . ILE B 1 142 ? 24.109  2.303   -21.710 1.00 61.53  ?  135 ILE B CA    1 
ATOM   3185 C  C     . ILE B 1 142 ? 25.013  3.206   -22.543 1.00 62.13  ?  135 ILE B C     1 
ATOM   3186 O  O     . ILE B 1 142 ? 25.416  4.276   -22.076 1.00 61.10  ?  135 ILE B O     1 
ATOM   3187 C  CB    . ILE B 1 142 ? 24.879  1.150   -21.031 1.00 65.60  ?  135 ILE B CB    1 
ATOM   3188 C  CG1   . ILE B 1 142 ? 24.024  0.524   -19.922 1.00 64.95  ?  135 ILE B CG1   1 
ATOM   3189 C  CG2   . ILE B 1 142 ? 26.221  1.655   -20.516 1.00 67.80  ?  135 ILE B CG2   1 
ATOM   3190 C  CD1   . ILE B 1 142 ? 24.418  -0.879  -19.536 1.00 69.14  ?  135 ILE B CD1   1 
ATOM   3191 N  N     . LYS B 1 143 ? 25.293  2.810   -23.780 1.00 63.99  ?  136 LYS B N     1 
ATOM   3192 C  CA    . LYS B 1 143 ? 26.159  3.607   -24.629 1.00 65.14  ?  136 LYS B CA    1 
ATOM   3193 C  C     . LYS B 1 143 ? 25.502  4.961   -24.918 1.00 61.35  ?  136 LYS B C     1 
ATOM   3194 O  O     . LYS B 1 143 ? 26.200  5.975   -25.015 1.00 61.68  ?  136 LYS B O     1 
ATOM   3195 C  CB    . LYS B 1 143 ? 26.507  2.883   -25.934 1.00 68.14  ?  136 LYS B CB    1 
ATOM   3196 C  CG    . LYS B 1 143 ? 27.328  3.710   -26.916 1.00 69.62  ?  136 LYS B CG    1 
ATOM   3197 C  CD    . LYS B 1 143 ? 28.566  4.386   -26.295 1.00 71.56  ?  136 LYS B CD    1 
ATOM   3198 C  CE    . LYS B 1 143 ? 28.956  5.684   -26.970 1.00 71.28  ?  136 LYS B CE    1 
ATOM   3199 N  NZ    . LYS B 1 143 ? 29.563  6.649   -26.023 1.00 71.06  ?  136 LYS B NZ    1 
ATOM   3200 N  N     . ILE B 1 144 ? 24.173  4.949   -25.081 1.00 58.23  ?  137 ILE B N     1 
ATOM   3201 C  CA    . ILE B 1 144 ? 23.432  6.171   -25.386 1.00 54.85  ?  137 ILE B CA    1 
ATOM   3202 C  C     . ILE B 1 144 ? 23.495  7.088   -24.168 1.00 53.05  ?  137 ILE B C     1 
ATOM   3203 O  O     . ILE B 1 144 ? 23.544  8.306   -24.314 1.00 51.73  ?  137 ILE B O     1 
ATOM   3204 C  CB    . ILE B 1 144 ? 21.973  5.855   -25.778 1.00 52.38  ?  137 ILE B CB    1 
ATOM   3205 C  CG1   . ILE B 1 144 ? 21.854  5.292   -27.193 1.00 53.99  ?  137 ILE B CG1   1 
ATOM   3206 C  CG2   . ILE B 1 144 ? 21.073  7.083   -25.600 1.00 48.73  ?  137 ILE B CG2   1 
ATOM   3207 C  CD1   . ILE B 1 144 ? 20.552  4.531   -27.426 1.00 52.81  ?  137 ILE B CD1   1 
ATOM   3208 N  N     . GLY B 1 145 ? 23.510  6.484   -22.978 1.00 53.42  ?  138 GLY B N     1 
ATOM   3209 C  CA    . GLY B 1 145 ? 23.636  7.198   -21.719 1.00 52.36  ?  138 GLY B CA    1 
ATOM   3210 C  C     . GLY B 1 145 ? 22.304  7.319   -20.964 1.00 49.16  ?  138 GLY B C     1 
ATOM   3211 O  O     . GLY B 1 145 ? 22.248  8.049   -19.988 1.00 48.03  ?  138 GLY B O     1 
ATOM   3212 N  N     . ARG B 1 146 ? 21.288  6.553   -21.375 1.00 48.24  ?  139 ARG B N     1 
ATOM   3213 C  CA    . ARG B 1 146 ? 20.029  6.425   -20.653 1.00 46.00  ?  139 ARG B CA    1 
ATOM   3214 C  C     . ARG B 1 146 ? 19.989  5.147   -19.831 1.00 47.92  ?  139 ARG B C     1 
ATOM   3215 O  O     . ARG B 1 146 ? 19.086  4.956   -19.006 1.00 46.79  ?  139 ARG B O     1 
ATOM   3216 C  CB    . ARG B 1 146 ? 18.864  6.356   -21.646 1.00 44.25  ?  139 ARG B CB    1 
ATOM   3217 C  CG    . ARG B 1 146 ? 17.505  6.630   -21.008 1.00 41.69  ?  139 ARG B CG    1 
ATOM   3218 C  CD    . ARG B 1 146 ? 16.361  6.451   -21.970 1.00 40.51  ?  139 ARG B CD    1 
ATOM   3219 N  NE    . ARG B 1 146 ? 16.497  7.172   -23.241 1.00 39.97  ?  139 ARG B NE    1 
ATOM   3220 C  CZ    . ARG B 1 146 ? 15.883  8.326   -23.523 1.00 37.76  ?  139 ARG B CZ    1 
ATOM   3221 N  NH1   . ARG B 1 146 ? 15.332  9.039   -22.557 1.00 35.95  ?  139 ARG B NH1   1 
ATOM   3222 N  NH2   . ARG B 1 146 ? 15.823  8.755   -24.767 1.00 37.70  ?  139 ARG B NH2   1 
ATOM   3223 N  N     . GLY B 1 147 ? 20.911  4.236   -20.156 1.00 51.14  ?  140 GLY B N     1 
ATOM   3224 C  CA    . GLY B 1 147 ? 20.842  2.863   -19.680 1.00 53.58  ?  140 GLY B CA    1 
ATOM   3225 C  C     . GLY B 1 147 ? 21.386  2.712   -18.258 1.00 55.08  ?  140 GLY B C     1 
ATOM   3226 O  O     . GLY B 1 147 ? 22.412  3.292   -17.933 1.00 56.04  ?  140 GLY B O     1 
ATOM   3227 N  N     . SER B 1 148 ? 20.625  1.978   -17.447 1.00 55.40  ?  141 SER B N     1 
ATOM   3228 C  CA    . SER B 1 148 ? 21.049  1.412   -16.184 1.00 57.86  ?  141 SER B CA    1 
ATOM   3229 C  C     . SER B 1 148 ? 21.068  -0.117  -16.268 1.00 61.35  ?  141 SER B C     1 
ATOM   3230 O  O     . SER B 1 148 ? 21.293  -0.785  -15.262 1.00 63.90  ?  141 SER B O     1 
ATOM   3231 C  CB    . SER B 1 148 ? 20.089  1.838   -15.125 1.00 55.80  ?  141 SER B CB    1 
ATOM   3232 O  OG    . SER B 1 148 ? 18.803  1.316   -15.441 1.00 54.71  ?  141 SER B OG    1 
ATOM   3233 N  N     . GLY B 1 149 ? 20.736  -0.668  -17.439 1.00 61.61  ?  142 GLY B N     1 
ATOM   3234 C  CA    . GLY B 1 149 ? 20.615  -2.108  -17.622 1.00 65.00  ?  142 GLY B CA    1 
ATOM   3235 C  C     . GLY B 1 149 ? 19.232  -2.666  -17.290 1.00 64.35  ?  142 GLY B C     1 
ATOM   3236 O  O     . GLY B 1 149 ? 19.009  -3.868  -17.449 1.00 67.33  ?  142 GLY B O     1 
ATOM   3237 N  N     . ASP B 1 150 ? 18.301  -1.809  -16.830 1.00 60.86  ?  143 ASP B N     1 
ATOM   3238 C  CA    . ASP B 1 150 ? 16.973  -2.260  -16.439 1.00 60.47  ?  143 ASP B CA    1 
ATOM   3239 C  C     . ASP B 1 150 ? 15.882  -1.520  -17.214 1.00 56.87  ?  143 ASP B C     1 
ATOM   3240 O  O     . ASP B 1 150 ? 14.712  -1.701  -16.904 1.00 56.28  ?  143 ASP B O     1 
ATOM   3241 C  CB    . ASP B 1 150 ? 16.720  -2.123  -14.935 1.00 60.68  ?  143 ASP B CB    1 
ATOM   3242 C  CG    . ASP B 1 150 ? 17.343  -3.230  -14.082 1.00 65.13  ?  143 ASP B CG    1 
ATOM   3243 O  OD1   . ASP B 1 150 ? 16.954  -4.414  -14.248 1.00 68.00  ?  143 ASP B OD1   1 
ATOM   3244 O  OD2   . ASP B 1 150 ? 18.217  -2.901  -13.251 1.00 66.01  ?  143 ASP B OD2   1 
ATOM   3245 N  N     . ASN B 1 151 ? 16.251  -0.763  -18.248 1.00 54.98  ?  144 ASN B N     1 
ATOM   3246 C  CA    . ASN B 1 151 ? 15.274  0.037   -18.992 1.00 51.74  ?  144 ASN B CA    1 
ATOM   3247 C  C     . ASN B 1 151 ? 14.173  -0.847  -19.579 1.00 52.70  ?  144 ASN B C     1 
ATOM   3248 O  O     . ASN B 1 151 ? 12.990  -0.520  -19.468 1.00 50.92  ?  144 ASN B O     1 
ATOM   3249 C  CB    . ASN B 1 151 ? 15.956  0.840   -20.100 1.00 50.46  ?  144 ASN B CB    1 
ATOM   3250 C  CG    . ASN B 1 151 ? 16.895  1.879   -19.528 1.00 49.41  ?  144 ASN B CG    1 
ATOM   3251 O  OD1   . ASN B 1 151 ? 17.768  1.560   -18.722 1.00 51.41  ?  144 ASN B OD1   1 
ATOM   3252 N  ND2   . ASN B 1 151 ? 16.696  3.133   -19.900 1.00 46.56  ?  144 ASN B ND2   1 
ATOM   3253 N  N     . VAL B 1 152 ? 14.556  -1.986  -20.183 1.00 55.92  ?  145 VAL B N     1 
ATOM   3254 C  CA    . VAL B 1 152 ? 13.600  -2.824  -20.884 1.00 57.26  ?  145 VAL B CA    1 
ATOM   3255 C  C     . VAL B 1 152 ? 12.660  -3.494  -19.889 1.00 58.56  ?  145 VAL B C     1 
ATOM   3256 O  O     . VAL B 1 152 ? 11.458  -3.544  -20.119 1.00 57.93  ?  145 VAL B O     1 
ATOM   3257 C  CB    . VAL B 1 152 ? 14.278  -3.840  -21.824 1.00 60.72  ?  145 VAL B CB    1 
ATOM   3258 C  CG1   . VAL B 1 152 ? 13.250  -4.776  -22.429 1.00 62.64  ?  145 VAL B CG1   1 
ATOM   3259 C  CG2   . VAL B 1 152 ? 15.104  -3.156  -22.904 1.00 59.70  ?  145 VAL B CG2   1 
ATOM   3260 N  N     . GLN B 1 153 ? 13.198  -4.022  -18.783 1.00 60.76  ?  146 GLN B N     1 
ATOM   3261 C  CA    . GLN B 1 153 ? 12.375  -4.647  -17.758 1.00 62.45  ?  146 GLN B CA    1 
ATOM   3262 C  C     . GLN B 1 153 ? 11.368  -3.639  -17.202 1.00 59.13  ?  146 GLN B C     1 
ATOM   3263 O  O     . GLN B 1 153 ? 10.182  -3.935  -17.026 1.00 59.61  ?  146 GLN B O     1 
ATOM   3264 C  CB    . GLN B 1 153 ? 13.287  -5.232  -16.669 1.00 65.41  ?  146 GLN B CB    1 
ATOM   3265 C  CG    . GLN B 1 153 ? 12.525  -5.909  -15.539 1.00 67.75  ?  146 GLN B CG    1 
ATOM   3266 C  CD    . GLN B 1 153 ? 13.423  -6.633  -14.558 1.00 71.44  ?  146 GLN B CD    1 
ATOM   3267 O  OE1   . GLN B 1 153 ? 14.634  -6.765  -14.746 1.00 72.70  ?  146 GLN B OE1   1 
ATOM   3268 N  NE2   . GLN B 1 153 ? 12.822  -7.108  -13.481 1.00 73.56  ?  146 GLN B NE2   1 
ATOM   3269 N  N     . LYS B 1 154 ? 11.836  -2.415  -16.947 1.00 56.02  ?  147 LYS B N     1 
ATOM   3270 C  CA    . LYS B 1 154 ? 10.961  -1.389  -16.387 1.00 53.10  ?  147 LYS B CA    1 
ATOM   3271 C  C     . LYS B 1 154 ? 9.891   -1.018  -17.413 1.00 51.20  ?  147 LYS B C     1 
ATOM   3272 O  O     . LYS B 1 154 ? 8.770   -0.727  -17.014 1.00 50.36  ?  147 LYS B O     1 
ATOM   3273 C  CB    . LYS B 1 154 ? 11.781  -0.184  -15.904 1.00 50.71  ?  147 LYS B CB    1 
ATOM   3274 C  CG    . LYS B 1 154 ? 10.992  0.854   -15.104 1.00 48.30  ?  147 LYS B CG    1 
ATOM   3275 C  CD    . LYS B 1 154 ? 10.186  0.326   -13.899 1.00 50.15  ?  147 LYS B CD    1 
ATOM   3276 C  CE    . LYS B 1 154 ? 9.279   1.343   -13.227 1.00 48.05  ?  147 LYS B CE    1 
ATOM   3277 N  NZ    . LYS B 1 154 ? 10.038  2.466   -12.643 1.00 46.27  ?  147 LYS B NZ    1 
ATOM   3278 N  N     . LEU B 1 155 ? 10.244  -1.020  -18.706 1.00 50.82  ?  148 LEU B N     1 
ATOM   3279 C  CA    . LEU B 1 155 ? 9.288   -0.656  -19.751 1.00 49.32  ?  148 LEU B CA    1 
ATOM   3280 C  C     . LEU B 1 155 ? 8.096   -1.610  -19.758 1.00 51.58  ?  148 LEU B C     1 
ATOM   3281 O  O     . LEU B 1 155 ? 6.955   -1.179  -19.753 1.00 50.41  ?  148 LEU B O     1 
ATOM   3282 C  CB    . LEU B 1 155 ? 9.992   -0.615  -21.114 1.00 49.26  ?  148 LEU B CB    1 
ATOM   3283 C  CG    . LEU B 1 155 ? 9.102   -0.386  -22.337 1.00 48.42  ?  148 LEU B CG    1 
ATOM   3284 C  CD1   . LEU B 1 155 ? 8.453   1.000   -22.305 1.00 44.98  ?  148 LEU B CD1   1 
ATOM   3285 C  CD2   . LEU B 1 155 ? 9.921   -0.527  -23.605 1.00 49.22  ?  148 LEU B CD2   1 
ATOM   3286 N  N     . TYR B 1 156 ? 8.360   -2.922  -19.735 1.00 55.22  ?  149 TYR B N     1 
ATOM   3287 C  CA    . TYR B 1 156 ? 7.307   -3.922  -19.665 1.00 58.10  ?  149 TYR B CA    1 
ATOM   3288 C  C     . TYR B 1 156 ? 6.436   -3.730  -18.431 1.00 58.03  ?  149 TYR B C     1 
ATOM   3289 O  O     . TYR B 1 156 ? 5.228   -3.878  -18.500 1.00 58.73  ?  149 TYR B O     1 
ATOM   3290 C  CB    . TYR B 1 156 ? 7.932   -5.330  -19.686 1.00 62.42  ?  149 TYR B CB    1 
ATOM   3291 C  CG    . TYR B 1 156 ? 8.226   -5.845  -21.089 1.00 63.80  ?  149 TYR B CG    1 
ATOM   3292 C  CD1   . TYR B 1 156 ? 9.354   -5.422  -21.785 1.00 62.60  ?  149 TYR B CD1   1 
ATOM   3293 C  CD2   . TYR B 1 156 ? 7.341   -6.681  -21.752 1.00 66.45  ?  149 TYR B CD2   1 
ATOM   3294 C  CE1   . TYR B 1 156 ? 9.619   -5.860  -23.073 1.00 64.10  ?  149 TYR B CE1   1 
ATOM   3295 C  CE2   . TYR B 1 156 ? 7.589   -7.122  -23.044 1.00 67.92  ?  149 TYR B CE2   1 
ATOM   3296 C  CZ    . TYR B 1 156 ? 8.742   -6.725  -23.700 1.00 66.78  ?  149 TYR B CZ    1 
ATOM   3297 O  OH    . TYR B 1 156 ? 9.043   -7.116  -24.971 1.00 68.42  ?  149 TYR B OH    1 
ATOM   3298 N  N     . GLU B 1 157 ? 7.048   -3.406  -17.280 1.00 57.53  ?  150 GLU B N     1 
ATOM   3299 C  CA    . GLU B 1 157 ? 6.311   -3.254  -16.041 1.00 57.92  ?  150 GLU B CA    1 
ATOM   3300 C  C     . GLU B 1 157 ? 5.358   -2.063  -16.160 1.00 54.68  ?  150 GLU B C     1 
ATOM   3301 O  O     . GLU B 1 157 ? 4.222   -2.114  -15.693 1.00 55.57  ?  150 GLU B O     1 
ATOM   3302 C  CB    . GLU B 1 157 ? 7.295   -3.065  -14.881 1.00 58.07  ?  150 GLU B CB    1 
ATOM   3303 C  CG    . GLU B 1 157 ? 6.669   -3.162  -13.511 1.00 59.60  ?  150 GLU B CG    1 
ATOM   3304 C  CD    . GLU B 1 157 ? 7.632   -2.895  -12.364 1.00 59.85  ?  150 GLU B CD    1 
ATOM   3305 O  OE1   . GLU B 1 157 ? 8.681   -2.267  -12.602 1.00 57.83  ?  150 GLU B OE1   1 
ATOM   3306 O  OE2   . GLU B 1 157 ? 7.325   -3.315  -11.241 1.00 62.35  ?  150 GLU B OE2   1 
ATOM   3307 N  N     . ILE B 1 158 ? 5.852   -0.977  -16.754 1.00 51.24  ?  151 ILE B N     1 
ATOM   3308 C  CA    . ILE B 1 158 ? 5.030   0.217   -16.851 1.00 48.37  ?  151 ILE B CA    1 
ATOM   3309 C  C     . ILE B 1 158 ? 3.840   -0.068  -17.758 1.00 49.09  ?  151 ILE B C     1 
ATOM   3310 O  O     . ILE B 1 158 ? 2.733   0.377   -17.483 1.00 48.73  ?  151 ILE B O     1 
ATOM   3311 C  CB    . ILE B 1 158 ? 5.824   1.439   -17.340 1.00 44.99  ?  151 ILE B CB    1 
ATOM   3312 C  CG1   . ILE B 1 158 ? 6.853   1.859   -16.296 1.00 44.44  ?  151 ILE B CG1   1 
ATOM   3313 C  CG2   . ILE B 1 158 ? 4.858   2.566   -17.679 1.00 42.57  ?  151 ILE B CG2   1 
ATOM   3314 C  CD1   . ILE B 1 158 ? 7.866   2.885   -16.773 1.00 41.96  ?  151 ILE B CD1   1 
ATOM   3315 N  N     . GLY B 1 159 ? 4.096   -0.796  -18.844 1.00 50.39  ?  152 GLY B N     1 
ATOM   3316 C  CA    . GLY B 1 159 ? 3.042   -1.185  -19.764 1.00 51.65  ?  152 GLY B CA    1 
ATOM   3317 C  C     . GLY B 1 159 ? 1.935   -1.961  -19.054 1.00 54.71  ?  152 GLY B C     1 
ATOM   3318 O  O     . GLY B 1 159 ? 0.748   -1.710  -19.273 1.00 54.90  ?  152 GLY B O     1 
ATOM   3319 N  N     . SER B 1 160 ? 2.315   -2.921  -18.202 1.00 57.52  ?  153 SER B N     1 
ATOM   3320 C  CA    . SER B 1 160 ? 1.327   -3.674  -17.442 1.00 60.90  ?  153 SER B CA    1 
ATOM   3321 C  C     . SER B 1 160 ? 0.570   -2.761  -16.477 1.00 59.47  ?  153 SER B C     1 
ATOM   3322 O  O     . SER B 1 160 ? -0.600  -2.978  -16.206 1.00 61.50  ?  153 SER B O     1 
ATOM   3323 C  CB    . SER B 1 160 ? 1.957   -4.828  -16.710 1.00 64.42  ?  153 SER B CB    1 
ATOM   3324 O  OG    . SER B 1 160 ? 2.857   -4.343  -15.711 1.00 62.93  ?  153 SER B OG    1 
ATOM   3325 N  N     . TRP B 1 161 ? 1.243   -1.753  -15.906 1.00 56.39  ?  154 TRP B N     1 
ATOM   3326 C  CA    . TRP B 1 161 ? 0.551   -0.810  -15.040 1.00 55.09  ?  154 TRP B CA    1 
ATOM   3327 C  C     . TRP B 1 161 ? -0.519  -0.024  -15.796 1.00 53.55  ?  154 TRP B C     1 
ATOM   3328 O  O     . TRP B 1 161 ? -1.587  0.267   -15.248 1.00 54.45  ?  154 TRP B O     1 
ATOM   3329 C  CB    . TRP B 1 161 ? 1.568   0.145   -14.383 1.00 52.26  ?  154 TRP B CB    1 
ATOM   3330 C  CG    . TRP B 1 161 ? 2.463   -0.490  -13.362 1.00 54.15  ?  154 TRP B CG    1 
ATOM   3331 C  CD1   . TRP B 1 161 ? 2.285   -1.697  -12.748 1.00 58.17  ?  154 TRP B CD1   1 
ATOM   3332 C  CD2   . TRP B 1 161 ? 3.675   0.061   -12.800 1.00 52.51  ?  154 TRP B CD2   1 
ATOM   3333 N  NE1   . TRP B 1 161 ? 3.297   -1.935  -11.860 1.00 59.10  ?  154 TRP B NE1   1 
ATOM   3334 C  CE2   . TRP B 1 161 ? 4.165   -0.876  -11.870 1.00 55.69  ?  154 TRP B CE2   1 
ATOM   3335 C  CE3   . TRP B 1 161 ? 4.401   1.243   -13.001 1.00 49.04  ?  154 TRP B CE3   1 
ATOM   3336 C  CZ2   . TRP B 1 161 ? 5.328   -0.658  -11.135 1.00 55.45  ?  154 TRP B CZ2   1 
ATOM   3337 C  CZ3   . TRP B 1 161 ? 5.550   1.455   -12.275 1.00 48.84  ?  154 TRP B CZ3   1 
ATOM   3338 C  CH2   . TRP B 1 161 ? 6.004   0.521   -11.351 1.00 51.98  ?  154 TRP B CH2   1 
ATOM   3339 N  N     . CYS B 1 162 ? -0.205  0.389   -17.030 1.00 51.36  ?  155 CYS B N     1 
ATOM   3340 C  CA    . CYS B 1 162 ? -1.125  1.214   -17.793 1.00 49.92  ?  155 CYS B CA    1 
ATOM   3341 C  C     . CYS B 1 162 ? -2.392  0.416   -18.086 1.00 53.26  ?  155 CYS B C     1 
ATOM   3342 O  O     . CYS B 1 162 ? -3.499  0.930   -18.030 1.00 53.54  ?  155 CYS B O     1 
ATOM   3343 C  CB    . CYS B 1 162 ? -0.510  1.704   -19.098 1.00 47.55  ?  155 CYS B CB    1 
ATOM   3344 S  SG    . CYS B 1 162 ? 0.813   2.933   -18.881 1.00 43.66  ?  155 CYS B SG    1 
ATOM   3345 N  N     . GLN B 1 163 ? -2.219  -0.879  -18.317 1.00 56.28  ?  156 GLN B N     1 
ATOM   3346 C  CA    . GLN B 1 163 ? -3.363  -1.731  -18.596 1.00 60.03  ?  156 GLN B CA    1 
ATOM   3347 C  C     . GLN B 1 163 ? -4.261  -1.758  -17.351 1.00 62.14  ?  156 GLN B C     1 
ATOM   3348 O  O     . GLN B 1 163 ? -5.462  -1.531  -17.449 1.00 63.43  ?  156 GLN B O     1 
ATOM   3349 C  CB    . GLN B 1 163 ? -2.821  -3.074  -19.100 1.00 62.91  ?  156 GLN B CB    1 
ATOM   3350 C  CG    . GLN B 1 163 ? -3.838  -3.909  -19.862 1.00 66.60  ?  156 GLN B CG    1 
ATOM   3351 C  CD    . GLN B 1 163 ? -4.954  -4.349  -18.948 1.00 70.14  ?  156 GLN B CD    1 
ATOM   3352 O  OE1   . GLN B 1 163 ? -4.745  -4.557  -17.751 1.00 71.09  ?  156 GLN B OE1   1 
ATOM   3353 N  NE2   . GLN B 1 163 ? -6.161  -4.422  -19.487 1.00 72.24  ?  156 GLN B NE2   1 
ATOM   3354 N  N     . LYS B 1 164 ? -3.658  -1.966  -16.175 1.00 62.59  ?  157 LYS B N     1 
ATOM   3355 C  CA    . LYS B 1 164 ? -4.350  -2.077  -14.898 1.00 65.02  ?  157 LYS B CA    1 
ATOM   3356 C  C     . LYS B 1 164 ? -5.085  -0.801  -14.499 1.00 63.03  ?  157 LYS B C     1 
ATOM   3357 O  O     . LYS B 1 164 ? -6.192  -0.868  -13.963 1.00 65.70  ?  157 LYS B O     1 
ATOM   3358 C  CB    . LYS B 1 164 ? -3.311  -2.404  -13.823 1.00 65.37  ?  157 LYS B CB    1 
ATOM   3359 C  CG    . LYS B 1 164 ? -3.841  -2.818  -12.457 1.00 68.87  ?  157 LYS B CG    1 
ATOM   3360 C  CD    . LYS B 1 164 ? -2.698  -3.280  -11.584 1.00 69.58  ?  157 LYS B CD    1 
ATOM   3361 C  CE    . LYS B 1 164 ? -3.089  -4.137  -10.400 1.00 74.38  ?  157 LYS B CE    1 
ATOM   3362 N  NZ    . LYS B 1 164 ? -1.882  -4.541  -9.636  1.00 75.03  ?  157 LYS B NZ    1 
ATOM   3363 N  N     . TYR B 1 165 ? -4.449  0.365   -14.728 1.00 58.68  ?  158 TYR B N     1 
ATOM   3364 C  CA    . TYR B 1 165 ? -4.970  1.640   -14.253 1.00 56.81  ?  158 TYR B CA    1 
ATOM   3365 C  C     . TYR B 1 165 ? -5.604  2.453   -15.377 1.00 55.02  ?  158 TYR B C     1 
ATOM   3366 O  O     . TYR B 1 165 ? -5.854  3.651   -15.205 1.00 52.95  ?  158 TYR B O     1 
ATOM   3367 C  CB    . TYR B 1 165 ? -3.817  2.374   -13.540 1.00 53.92  ?  158 TYR B CB    1 
ATOM   3368 C  CG    . TYR B 1 165 ? -3.346  1.615   -12.310 1.00 56.29  ?  158 TYR B CG    1 
ATOM   3369 C  CD1   . TYR B 1 165 ? -4.171  1.498   -11.204 1.00 59.14  ?  158 TYR B CD1   1 
ATOM   3370 C  CD2   . TYR B 1 165 ? -2.137  0.926   -12.288 1.00 56.30  ?  158 TYR B CD2   1 
ATOM   3371 C  CE1   . TYR B 1 165 ? -3.802  0.757   -10.096 1.00 61.85  ?  158 TYR B CE1   1 
ATOM   3372 C  CE2   . TYR B 1 165 ? -1.749  0.196   -11.174 1.00 58.96  ?  158 TYR B CE2   1 
ATOM   3373 C  CZ    . TYR B 1 165 ? -2.604  0.083   -10.089 1.00 61.82  ?  158 TYR B CZ    1 
ATOM   3374 O  OH    . TYR B 1 165 ? -2.268  -0.619  -8.959  1.00 64.84  ?  158 TYR B OH    1 
ATOM   3375 N  N     . ASP B 1 166 ? -5.872  1.809   -16.520 1.00 56.14  ?  159 ASP B N     1 
ATOM   3376 C  CA    . ASP B 1 166 ? -6.608  2.424   -17.613 1.00 55.36  ?  159 ASP B CA    1 
ATOM   3377 C  C     . ASP B 1 166 ? -5.935  3.714   -18.096 1.00 51.08  ?  159 ASP B C     1 
ATOM   3378 O  O     . ASP B 1 166 ? -6.581  4.757   -18.169 1.00 50.09  ?  159 ASP B O     1 
ATOM   3379 C  CB    . ASP B 1 166 ? -8.069  2.655   -17.206 1.00 57.93  ?  159 ASP B CB    1 
ATOM   3380 C  CG    . ASP B 1 166 ? -8.913  3.218   -18.331 1.00 57.81  ?  159 ASP B CG    1 
ATOM   3381 O  OD1   . ASP B 1 166 ? -8.706  2.774   -19.484 1.00 57.84  ?  159 ASP B OD1   1 
ATOM   3382 O  OD2   . ASP B 1 166 ? -9.764  4.094   -18.050 1.00 57.97  ?  159 ASP B OD2   1 
ATOM   3383 N  N     . ILE B 1 167 ? -4.679  3.582   -18.539 1.00 49.07  ?  160 ILE B N     1 
ATOM   3384 C  CA    . ILE B 1 167 ? -3.924  4.649   -19.188 1.00 45.52  ?  160 ILE B CA    1 
ATOM   3385 C  C     . ILE B 1 167 ? -3.442  4.122   -20.534 1.00 45.50  ?  160 ILE B C     1 
ATOM   3386 O  O     . ILE B 1 167 ? -2.958  2.998   -20.617 1.00 47.14  ?  160 ILE B O     1 
ATOM   3387 C  CB    . ILE B 1 167 ? -2.732  5.063   -18.301 1.00 43.42  ?  160 ILE B CB    1 
ATOM   3388 C  CG1   . ILE B 1 167 ? -3.184  5.576   -16.934 1.00 43.76  ?  160 ILE B CG1   1 
ATOM   3389 C  CG2   . ILE B 1 167 ? -1.864  6.091   -19.023 1.00 40.22  ?  160 ILE B CG2   1 
ATOM   3390 C  CD1   . ILE B 1 167 ? -2.083  5.575   -15.887 1.00 42.98  ?  160 ILE B CD1   1 
ATOM   3391 N  N     . LYS B 1 168 ? -3.463  4.957   -21.564 1.00 43.77  ?  161 LYS B N     1 
ATOM   3392 C  CA    . LYS B 1 168 ? -2.894  4.611   -22.856 1.00 43.65  ?  161 LYS B CA    1 
ATOM   3393 C  C     . LYS B 1 168 ? -1.369  4.606   -22.782 1.00 41.85  ?  161 LYS B C     1 
ATOM   3394 O  O     . LYS B 1 168 ? -0.779  5.553   -22.257 1.00 39.49  ?  161 LYS B O     1 
ATOM   3395 C  CB    . LYS B 1 168 ? -3.475  5.578   -23.890 1.00 42.76  ?  161 LYS B CB    1 
ATOM   3396 C  CG    . LYS B 1 168 ? -5.003  5.601   -23.912 1.00 44.93  ?  161 LYS B CG    1 
ATOM   3397 C  CD    . LYS B 1 168 ? -5.612  6.782   -24.661 1.00 44.04  ?  161 LYS B CD    1 
ATOM   3398 C  CE    . LYS B 1 168 ? -5.398  6.736   -26.158 1.00 44.26  ?  161 LYS B CE    1 
ATOM   3399 N  NZ    . LYS B 1 168 ? -6.044  5.540   -26.761 1.00 47.58  ?  161 LYS B NZ    1 
ATOM   3400 N  N     . PHE B 1 169 ? -0.749  3.526   -23.310 1.00 43.36  ?  162 PHE B N     1 
ATOM   3401 C  CA    . PHE B 1 169 ? 0.680   3.265   -23.225 1.00 42.58  ?  162 PHE B CA    1 
ATOM   3402 C  C     . PHE B 1 169 ? 1.364   3.627   -24.547 1.00 41.59  ?  162 PHE B C     1 
ATOM   3403 O  O     . PHE B 1 169 ? 1.036   3.085   -25.613 1.00 43.27  ?  162 PHE B O     1 
ATOM   3404 C  CB    . PHE B 1 169 ? 0.901   1.792   -22.833 1.00 45.52  ?  162 PHE B CB    1 
ATOM   3405 C  CG    . PHE B 1 169 ? 2.337   1.311   -22.765 1.00 45.59  ?  162 PHE B CG    1 
ATOM   3406 C  CD1   . PHE B 1 169 ? 3.272   1.929   -21.947 1.00 43.65  ?  162 PHE B CD1   1 
ATOM   3407 C  CD2   . PHE B 1 169 ? 2.734   0.184   -23.461 1.00 48.09  ?  162 PHE B CD2   1 
ATOM   3408 C  CE1   . PHE B 1 169 ? 4.590   1.493   -21.900 1.00 44.09  ?  162 PHE B CE1   1 
ATOM   3409 C  CE2   . PHE B 1 169 ? 4.043   -0.275  -23.397 1.00 48.58  ?  162 PHE B CE2   1 
ATOM   3410 C  CZ    . PHE B 1 169 ? 4.972   0.375   -22.609 1.00 46.60  ?  162 PHE B CZ    1 
ATOM   3411 N  N     . LYS B 1 170 ? 2.369   4.507   -24.452 1.00 39.24  ?  163 LYS B N     1 
ATOM   3412 C  CA    . LYS B 1 170 ? 3.086   5.056   -25.591 1.00 38.28  ?  163 LYS B CA    1 
ATOM   3413 C  C     . LYS B 1 170 ? 4.573   4.815   -25.382 1.00 38.09  ?  163 LYS B C     1 
ATOM   3414 O  O     . LYS B 1 170 ? 5.071   4.866   -24.248 1.00 37.49  ?  163 LYS B O     1 
ATOM   3415 C  CB    . LYS B 1 170 ? 2.698   6.538   -25.730 1.00 36.07  ?  163 LYS B CB    1 
ATOM   3416 C  CG    . LYS B 1 170 ? 3.473   7.395   -26.726 1.00 34.95  ?  163 LYS B CG    1 
ATOM   3417 C  CD    . LYS B 1 170 ? 2.894   8.805   -26.815 1.00 33.35  ?  163 LYS B CD    1 
ATOM   3418 C  CE    . LYS B 1 170 ? 3.822   9.818   -27.460 1.00 32.23  ?  163 LYS B CE    1 
ATOM   3419 N  NZ    . LYS B 1 170 ? 3.455   11.233  -27.152 1.00 30.72  ?  163 LYS B NZ    1 
ATOM   3420 N  N     . LEU B 1 171 ? 5.255   4.486   -26.493 1.00 39.06  ?  164 LEU B N     1 
ATOM   3421 C  CA    . LEU B 1 171 ? 6.698   4.354   -26.530 1.00 39.22  ?  164 LEU B CA    1 
ATOM   3422 C  C     . LEU B 1 171 ? 7.315   5.434   -27.428 1.00 37.94  ?  164 LEU B C     1 
ATOM   3423 O  O     . LEU B 1 171 ? 6.916   5.632   -28.582 1.00 38.41  ?  164 LEU B O     1 
ATOM   3424 C  CB    . LEU B 1 171 ? 7.001   2.919   -27.020 1.00 42.25  ?  164 LEU B CB    1 
ATOM   3425 C  CG    . LEU B 1 171 ? 8.470   2.563   -27.256 1.00 43.34  ?  164 LEU B CG    1 
ATOM   3426 C  CD1   . LEU B 1 171 ? 9.308   2.557   -25.979 1.00 42.90  ?  164 LEU B CD1   1 
ATOM   3427 C  CD2   . LEU B 1 171 ? 8.577   1.206   -27.928 1.00 46.68  ?  164 LEU B CD2   1 
ATOM   3428 N  N     . ASN B 1 172 ? 8.390   6.061   -26.932 1.00 36.84  ?  165 ASN B N     1 
ATOM   3429 C  CA    . ASN B 1 172 ? 9.176   7.040   -27.656 1.00 36.13  ?  165 ASN B CA    1 
ATOM   3430 C  C     . ASN B 1 172 ? 10.581  6.470   -27.854 1.00 37.79  ?  165 ASN B C     1 
ATOM   3431 O  O     . ASN B 1 172 ? 11.217  6.055   -26.880 1.00 38.12  ?  165 ASN B O     1 
ATOM   3432 C  CB    . ASN B 1 172 ? 9.282   8.375   -26.918 1.00 33.88  ?  165 ASN B CB    1 
ATOM   3433 C  CG    . ASN B 1 172 ? 7.991   9.204   -26.880 1.00 32.44  ?  165 ASN B CG    1 
ATOM   3434 O  OD1   . ASN B 1 172 ? 6.916   8.731   -27.237 1.00 33.04  ?  165 ASN B OD1   1 
ATOM   3435 N  ND2   . ASN B 1 172 ? 8.082   10.466  -26.478 1.00 30.86  ?  165 ASN B ND2   1 
ATOM   3436 N  N     . THR B 1 173 ? 11.047  6.477   -29.110 1.00 39.09  ?  166 THR B N     1 
ATOM   3437 C  CA    . THR B 1 173 ? 12.358  5.975   -29.518 1.00 41.19  ?  166 THR B CA    1 
ATOM   3438 C  C     . THR B 1 173 ? 13.080  7.019   -30.362 1.00 41.17  ?  166 THR B C     1 
ATOM   3439 O  O     . THR B 1 173 ? 12.523  7.560   -31.324 1.00 41.01  ?  166 THR B O     1 
ATOM   3440 C  CB    . THR B 1 173 ? 12.180  4.686   -30.324 1.00 43.89  ?  166 THR B CB    1 
ATOM   3441 O  OG1   . THR B 1 173 ? 11.563  3.679   -29.519 1.00 44.42  ?  166 THR B OG1   1 
ATOM   3442 C  CG2   . THR B 1 173 ? 13.481  4.206   -30.922 1.00 46.50  ?  166 THR B CG2   1 
ATOM   3443 N  N     . VAL B 1 174 ? 14.310  7.350   -29.988 1.00 41.60  ?  167 VAL B N     1 
ATOM   3444 C  CA    . VAL B 1 174 ? 15.181  8.223   -30.753 1.00 42.36  ?  167 VAL B CA    1 
ATOM   3445 C  C     . VAL B 1 174 ? 16.094  7.370   -31.647 1.00 45.64  ?  167 VAL B C     1 
ATOM   3446 O  O     . VAL B 1 174 ? 16.886  6.601   -31.120 1.00 47.15  ?  167 VAL B O     1 
ATOM   3447 C  CB    . VAL B 1 174 ? 16.009  9.115   -29.816 1.00 41.42  ?  167 VAL B CB    1 
ATOM   3448 C  CG1   . VAL B 1 174 ? 17.011  9.946   -30.582 1.00 42.85  ?  167 VAL B CG1   1 
ATOM   3449 C  CG2   . VAL B 1 174 ? 15.138  10.046  -28.969 1.00 38.52  ?  167 VAL B CG2   1 
ATOM   3450 N  N     . VAL B 1 175 ? 15.968  7.509   -32.971 1.00 47.01  ?  168 VAL B N     1 
ATOM   3451 C  CA    . VAL B 1 175 ? 16.744  6.714   -33.930 1.00 50.49  ?  168 VAL B CA    1 
ATOM   3452 C  C     . VAL B 1 175 ? 18.044  7.461   -34.180 1.00 51.93  ?  168 VAL B C     1 
ATOM   3453 O  O     . VAL B 1 175 ? 18.022  8.605   -34.611 1.00 51.26  ?  168 VAL B O     1 
ATOM   3454 C  CB    . VAL B 1 175 ? 15.978  6.481   -35.245 1.00 51.73  ?  168 VAL B CB    1 
ATOM   3455 C  CG1   . VAL B 1 175 ? 16.726  5.512   -36.172 1.00 55.70  ?  168 VAL B CG1   1 
ATOM   3456 C  CG2   . VAL B 1 175 ? 14.548  6.026   -35.007 1.00 50.17  ?  168 VAL B CG2   1 
ATOM   3457 N  N     . ASN B 1 176 ? 19.188  6.817   -33.872 1.00 54.25  ?  169 ASN B N     1 
ATOM   3458 C  CA    . ASN B 1 176 ? 20.477  7.484   -33.875 1.00 55.84  ?  169 ASN B CA    1 
ATOM   3459 C  C     . ASN B 1 176 ? 21.551  6.497   -34.359 1.00 60.02  ?  169 ASN B C     1 
ATOM   3460 O  O     . ASN B 1 176 ? 21.250  5.336   -34.597 1.00 61.38  ?  169 ASN B O     1 
ATOM   3461 C  CB    . ASN B 1 176 ? 20.843  7.993   -32.483 1.00 53.98  ?  169 ASN B CB    1 
ATOM   3462 C  CG    . ASN B 1 176 ? 20.917  6.881   -31.466 1.00 54.15  ?  169 ASN B CG    1 
ATOM   3463 O  OD1   . ASN B 1 176 ? 21.961  6.236   -31.313 1.00 56.98  ?  169 ASN B OD1   1 
ATOM   3464 N  ND2   . ASN B 1 176 ? 19.823  6.643   -30.763 1.00 51.52  ?  169 ASN B ND2   1 
ATOM   3465 N  N     . LYS B 1 177 ? 22.796  6.954   -34.427 1.00 62.27  ?  170 LYS B N     1 
ATOM   3466 C  CA    . LYS B 1 177 ? 23.870  6.116   -34.951 1.00 66.73  ?  170 LYS B CA    1 
ATOM   3467 C  C     . LYS B 1 177 ? 23.919  4.761   -34.248 1.00 67.67  ?  170 LYS B C     1 
ATOM   3468 O  O     . LYS B 1 177 ? 24.193  3.757   -34.892 1.00 70.95  ?  170 LYS B O     1 
ATOM   3469 C  CB    . LYS B 1 177 ? 25.217  6.833   -34.829 1.00 68.99  ?  170 LYS B CB    1 
ATOM   3470 C  CG    . LYS B 1 177 ? 26.384  6.121   -35.496 1.00 74.16  ?  170 LYS B CG    1 
ATOM   3471 C  CD    . LYS B 1 177 ? 26.121  5.695   -36.929 1.00 76.58  ?  170 LYS B CD    1 
ATOM   3472 C  CE    . LYS B 1 177 ? 25.591  6.797   -37.824 1.00 75.46  ?  170 LYS B CE    1 
ATOM   3473 N  NZ    . LYS B 1 177 ? 25.426  6.321   -39.220 1.00 78.46  ?  170 LYS B NZ    1 
ATOM   3474 N  N     . PHE B 1 178 ? 23.662  4.708   -32.934 1.00 65.19  ?  171 PHE B N     1 
ATOM   3475 C  CA    . PHE B 1 178 ? 23.845  3.471   -32.184 1.00 66.62  ?  171 PHE B CA    1 
ATOM   3476 C  C     . PHE B 1 178 ? 22.698  2.470   -32.362 1.00 66.03  ?  171 PHE B C     1 
ATOM   3477 O  O     . PHE B 1 178 ? 22.868  1.296   -32.019 1.00 68.24  ?  171 PHE B O     1 
ATOM   3478 C  CB    . PHE B 1 178 ? 24.092  3.755   -30.695 1.00 64.87  ?  171 PHE B CB    1 
ATOM   3479 C  CG    . PHE B 1 178 ? 25.345  4.544   -30.387 1.00 66.32  ?  171 PHE B CG    1 
ATOM   3480 C  CD1   . PHE B 1 178 ? 26.562  4.198   -30.957 1.00 70.76  ?  171 PHE B CD1   1 
ATOM   3481 C  CD2   . PHE B 1 178 ? 25.315  5.627   -29.519 1.00 63.64  ?  171 PHE B CD2   1 
ATOM   3482 C  CE1   . PHE B 1 178 ? 27.710  4.924   -30.689 1.00 72.52  ?  171 PHE B CE1   1 
ATOM   3483 C  CE2   . PHE B 1 178 ? 26.467  6.351   -29.249 1.00 65.37  ?  171 PHE B CE2   1 
ATOM   3484 C  CZ    . PHE B 1 178 ? 27.662  6.002   -29.841 1.00 69.83  ?  171 PHE B CZ    1 
ATOM   3485 N  N     . ASN B 1 179 ? 21.543  2.858   -32.927 1.00 63.61  ?  172 ASN B N     1 
ATOM   3486 C  CA    . ASN B 1 179 ? 20.459  1.884   -32.993 1.00 63.38  ?  172 ASN B CA    1 
ATOM   3487 C  C     . ASN B 1 179 ? 19.780  1.799   -34.369 1.00 64.24  ?  172 ASN B C     1 
ATOM   3488 O  O     . ASN B 1 179 ? 18.806  1.061   -34.516 1.00 64.23  ?  172 ASN B O     1 
ATOM   3489 C  CB    . ASN B 1 179 ? 19.453  2.132   -31.867 1.00 59.59  ?  172 ASN B CB    1 
ATOM   3490 C  CG    . ASN B 1 179 ? 18.736  3.451   -32.045 1.00 56.12  ?  172 ASN B CG    1 
ATOM   3491 O  OD1   . ASN B 1 179 ? 19.066  4.207   -32.947 1.00 56.57  ?  172 ASN B OD1   1 
ATOM   3492 N  ND2   . ASN B 1 179 ? 17.775  3.749   -31.182 1.00 53.01  ?  172 ASN B ND2   1 
ATOM   3493 N  N     . HIS B 1 180 ? 20.287  2.499   -35.389 1.00 65.44  ?  173 HIS B N     1 
ATOM   3494 C  CA    . HIS B 1 180 ? 19.514  2.679   -36.610 1.00 65.72  ?  173 HIS B CA    1 
ATOM   3495 C  C     . HIS B 1 180 ? 19.383  1.367   -37.392 1.00 69.38  ?  173 HIS B C     1 
ATOM   3496 O  O     . HIS B 1 180 ? 18.547  1.290   -38.280 1.00 69.72  ?  173 HIS B O     1 
ATOM   3497 C  CB    . HIS B 1 180 ? 20.056  3.831   -37.463 1.00 66.27  ?  173 HIS B CB    1 
ATOM   3498 C  CG    . HIS B 1 180 ? 21.295  3.493   -38.228 1.00 70.77  ?  173 HIS B CG    1 
ATOM   3499 N  ND1   . HIS B 1 180 ? 22.545  3.460   -37.644 1.00 72.41  ?  173 HIS B ND1   1 
ATOM   3500 C  CD2   . HIS B 1 180 ? 21.473  3.160   -39.521 1.00 74.31  ?  173 HIS B CD2   1 
ATOM   3501 C  CE1   . HIS B 1 180 ? 23.448  3.120   -38.559 1.00 76.86  ?  173 HIS B CE1   1 
ATOM   3502 N  NE2   . HIS B 1 180 ? 22.820  2.935   -39.706 1.00 78.07  ?  173 HIS B NE2   1 
ATOM   3503 N  N     . LEU B 1 181 ? 20.159  0.325   -37.036 1.00 72.32  ?  174 LEU B N     1 
ATOM   3504 C  CA    . LEU B 1 181 ? 20.081  -0.972  -37.703 1.00 76.25  ?  174 LEU B CA    1 
ATOM   3505 C  C     . LEU B 1 181 ? 19.248  -1.990  -36.925 1.00 75.76  ?  174 LEU B C     1 
ATOM   3506 O  O     . LEU B 1 181 ? 18.945  -3.048  -37.459 1.00 78.84  ?  174 LEU B O     1 
ATOM   3507 C  CB    . LEU B 1 181 ? 21.503  -1.522  -37.891 1.00 80.68  ?  174 LEU B CB    1 
ATOM   3508 C  CG    . LEU B 1 181 ? 22.338  -0.874  -38.990 1.00 83.09  ?  174 LEU B CG    1 
ATOM   3509 C  CD1   . LEU B 1 181 ? 23.696  -1.564  -39.100 1.00 87.99  ?  174 LEU B CD1   1 
ATOM   3510 C  CD2   . LEU B 1 181 ? 21.611  -0.912  -40.327 1.00 84.37  ?  174 LEU B CD2   1 
ATOM   3511 N  N     . GLU B 1 182 ? 18.892  -1.688  -35.670 1.00 72.32  ?  175 GLU B N     1 
ATOM   3512 C  CA    . GLU B 1 182 ? 18.243  -2.649  -34.789 1.00 72.30  ?  175 GLU B CA    1 
ATOM   3513 C  C     . GLU B 1 182 ? 16.853  -3.022  -35.307 1.00 71.96  ?  175 GLU B C     1 
ATOM   3514 O  O     . GLU B 1 182 ? 16.178  -2.246  -35.990 1.00 70.11  ?  175 GLU B O     1 
ATOM   3515 C  CB    . GLU B 1 182 ? 18.154  -2.058  -33.377 1.00 68.67  ?  175 GLU B CB    1 
ATOM   3516 C  CG    . GLU B 1 182 ? 17.525  -2.972  -32.334 1.00 68.73  ?  175 GLU B CG    1 
ATOM   3517 C  CD    . GLU B 1 182 ? 17.554  -2.404  -30.922 1.00 65.69  ?  175 GLU B CD    1 
ATOM   3518 O  OE1   . GLU B 1 182 ? 18.379  -1.511  -30.663 1.00 64.43  ?  175 GLU B OE1   1 
ATOM   3519 O  OE2   . GLU B 1 182 ? 16.720  -2.821  -30.115 1.00 64.80  ?  175 GLU B OE2   1 
ATOM   3520 N  N     . ASP B 1 183 ? 16.426  -4.229  -34.933 1.00 74.08  ?  176 ASP B N     1 
ATOM   3521 C  CA    . ASP B 1 183 ? 15.114  -4.742  -35.263 1.00 74.38  ?  176 ASP B CA    1 
ATOM   3522 C  C     . ASP B 1 183 ? 14.384  -5.016  -33.956 1.00 72.53  ?  176 ASP B C     1 
ATOM   3523 O  O     . ASP B 1 183 ? 14.835  -5.837  -33.158 1.00 74.43  ?  176 ASP B O     1 
ATOM   3524 C  CB    . ASP B 1 183 ? 15.246  -5.988  -36.142 1.00 79.54  ?  176 ASP B CB    1 
ATOM   3525 C  CG    . ASP B 1 183 ? 13.929  -6.474  -36.721 1.00 80.52  ?  176 ASP B CG    1 
ATOM   3526 O  OD1   . ASP B 1 183 ? 13.022  -6.787  -35.922 1.00 79.40  ?  176 ASP B OD1   1 
ATOM   3527 O  OD2   . ASP B 1 183 ? 13.827  -6.548  -37.972 1.00 82.74  ?  176 ASP B OD2   1 
ATOM   3528 N  N     . MET B 1 184 ? 13.282  -4.278  -33.731 1.00 69.03  ?  177 MET B N     1 
ATOM   3529 C  CA    . MET B 1 184 ? 12.564  -4.266  -32.465 1.00 66.83  ?  177 MET B CA    1 
ATOM   3530 C  C     . MET B 1 184 ? 11.198  -4.922  -32.608 1.00 67.94  ?  177 MET B C     1 
ATOM   3531 O  O     . MET B 1 184 ? 10.376  -4.886  -31.680 1.00 66.35  ?  177 MET B O     1 
ATOM   3532 C  CB    . MET B 1 184 ? 12.330  -2.824  -32.008 1.00 62.14  ?  177 MET B CB    1 
ATOM   3533 C  CG    . MET B 1 184 ? 13.559  -1.965  -32.155 1.00 61.13  ?  177 MET B CG    1 
ATOM   3534 S  SD    . MET B 1 184 ? 13.388  -0.345  -31.349 1.00 56.11  ?  177 MET B SD    1 
ATOM   3535 C  CE    . MET B 1 184 ? 14.972  0.377   -31.765 1.00 56.58  ?  177 MET B CE    1 
ATOM   3536 N  N     . ASN B 1 185 ? 10.953  -5.508  -33.783 1.00 70.96  ?  178 ASN B N     1 
ATOM   3537 C  CA    . ASN B 1 185 ? 9.613   -5.928  -34.153 1.00 72.06  ?  178 ASN B CA    1 
ATOM   3538 C  C     . ASN B 1 185 ? 9.029   -6.855  -33.091 1.00 73.47  ?  178 ASN B C     1 
ATOM   3539 O  O     . ASN B 1 185 ? 7.856   -6.728  -32.763 1.00 72.41  ?  178 ASN B O     1 
ATOM   3540 C  CB    . ASN B 1 185 ? 9.605   -6.520  -35.577 1.00 75.86  ?  178 ASN B CB    1 
ATOM   3541 C  CG    . ASN B 1 185 ? 9.555   -5.449  -36.648 1.00 74.16  ?  178 ASN B CG    1 
ATOM   3542 O  OD1   . ASN B 1 185 ? 8.554   -4.748  -36.775 1.00 71.92  ?  178 ASN B OD1   1 
ATOM   3543 N  ND2   . ASN B 1 185 ? 10.618  -5.302  -37.424 1.00 75.51  ?  178 ASN B ND2   1 
ATOM   3544 N  N     . ASP B 1 186 ? 9.828   -7.796  -32.564 1.00 76.25  ?  179 ASP B N     1 
ATOM   3545 C  CA    . ASP B 1 186 ? 9.347   -8.769  -31.593 1.00 78.38  ?  179 ASP B CA    1 
ATOM   3546 C  C     . ASP B 1 186 ? 8.898   -8.070  -30.307 1.00 74.66  ?  179 ASP B C     1 
ATOM   3547 O  O     . ASP B 1 186 ? 7.792   -8.284  -29.834 1.00 74.81  ?  179 ASP B O     1 
ATOM   3548 C  CB    . ASP B 1 186 ? 10.415  -9.829  -31.302 1.00 82.29  ?  179 ASP B CB    1 
ATOM   3549 C  CG    . ASP B 1 186 ? 10.685  -10.769 -32.471 1.00 87.07  ?  179 ASP B CG    1 
ATOM   3550 O  OD1   . ASP B 1 186 ? 10.043  -10.600 -33.538 1.00 87.36  ?  179 ASP B OD1   1 
ATOM   3551 O  OD2   . ASP B 1 186 ? 11.539  -11.674 -32.312 1.00 90.79  ?  179 ASP B OD2   1 
ATOM   3552 N  N     . HIS B 1 187 ? 9.753   -7.199  -29.762 1.00 71.55  ?  180 HIS B N     1 
ATOM   3553 C  CA    . HIS B 1 187 ? 9.394   -6.466  -28.555 1.00 68.13  ?  180 HIS B CA    1 
ATOM   3554 C  C     . HIS B 1 187 ? 8.152   -5.596  -28.792 1.00 65.25  ?  180 HIS B C     1 
ATOM   3555 O  O     . HIS B 1 187 ? 7.250   -5.580  -27.950 1.00 64.56  ?  180 HIS B O     1 
ATOM   3556 C  CB    . HIS B 1 187 ? 10.597  -5.674  -28.039 1.00 65.76  ?  180 HIS B CB    1 
ATOM   3557 C  CG    . HIS B 1 187 ? 11.696  -6.481  -27.418 1.00 68.52  ?  180 HIS B CG    1 
ATOM   3558 N  ND1   . HIS B 1 187 ? 11.568  -7.094  -26.194 1.00 69.81  ?  180 HIS B ND1   1 
ATOM   3559 C  CD2   . HIS B 1 187 ? 12.949  -6.703  -27.819 1.00 70.35  ?  180 HIS B CD2   1 
ATOM   3560 C  CE1   . HIS B 1 187 ? 12.714  -7.680  -25.888 1.00 72.38  ?  180 HIS B CE1   1 
ATOM   3561 N  NE2   . HIS B 1 187 ? 13.565  -7.449  -26.859 1.00 72.73  ?  180 HIS B NE2   1 
ATOM   3562 N  N     . LEU B 1 188 ? 8.093   -4.888  -29.932 1.00 63.95  ?  181 LEU B N     1 
ATOM   3563 C  CA    . LEU B 1 188 ? 6.952   -4.028  -30.244 1.00 61.57  ?  181 LEU B CA    1 
ATOM   3564 C  C     . LEU B 1 188 ? 5.672   -4.853  -30.364 1.00 64.19  ?  181 LEU B C     1 
ATOM   3565 O  O     . LEU B 1 188 ? 4.578   -4.402  -30.010 1.00 62.79  ?  181 LEU B O     1 
ATOM   3566 C  CB    . LEU B 1 188 ? 7.219   -3.229  -31.527 1.00 60.54  ?  181 LEU B CB    1 
ATOM   3567 C  CG    . LEU B 1 188 ? 7.693   -1.794  -31.310 1.00 56.53  ?  181 LEU B CG    1 
ATOM   3568 C  CD1   . LEU B 1 188 ? 6.601   -0.942  -30.681 1.00 53.67  ?  181 LEU B CD1   1 
ATOM   3569 C  CD2   . LEU B 1 188 ? 8.941   -1.779  -30.447 1.00 55.95  ?  181 LEU B CD2   1 
ATOM   3570 N  N     . ASN B 1 189 ? 5.788   -6.085  -30.874 1.00 68.44  ?  182 ASN B N     1 
ATOM   3571 C  CA    . ASN B 1 189 ? 4.604   -6.929  -30.981 1.00 71.53  ?  182 ASN B CA    1 
ATOM   3572 C  C     . ASN B 1 189 ? 4.089   -7.336  -29.604 1.00 71.94  ?  182 ASN B C     1 
ATOM   3573 O  O     . ASN B 1 189 ? 2.886   -7.531  -29.435 1.00 73.04  ?  182 ASN B O     1 
ATOM   3574 C  CB    . ASN B 1 189 ? 4.881   -8.164  -31.832 1.00 76.41  ?  182 ASN B CB    1 
ATOM   3575 C  CG    . ASN B 1 189 ? 4.868   -7.846  -33.307 1.00 76.88  ?  182 ASN B CG    1 
ATOM   3576 O  OD1   . ASN B 1 189 ? 4.415   -6.786  -33.727 1.00 73.97  ?  182 ASN B OD1   1 
ATOM   3577 N  ND2   . ASN B 1 189 ? 5.304   -8.795  -34.108 1.00 81.00  ?  182 ASN B ND2   1 
ATOM   3578 N  N     . ALA B 1 190 ? 5.013   -7.475  -28.639 1.00 71.43  ?  183 ALA B N     1 
ATOM   3579 C  CA    . ALA B 1 190 ? 4.685   -7.907  -27.290 1.00 72.25  ?  183 ALA B CA    1 
ATOM   3580 C  C     . ALA B 1 190 ? 4.111   -6.756  -26.457 1.00 68.19  ?  183 ALA B C     1 
ATOM   3581 O  O     . ALA B 1 190 ? 3.114   -6.927  -25.754 1.00 69.00  ?  183 ALA B O     1 
ATOM   3582 C  CB    . ALA B 1 190 ? 5.920   -8.507  -26.654 1.00 73.74  ?  183 ALA B CB    1 
ATOM   3583 N  N     . LEU B 1 191 ? 4.734   -5.576  -26.549 1.00 64.19  ?  184 LEU B N     1 
ATOM   3584 C  CA    . LEU B 1 191 ? 4.329   -4.434  -25.737 1.00 60.48  ?  184 LEU B CA    1 
ATOM   3585 C  C     . LEU B 1 191 ? 3.009   -3.849  -26.237 1.00 59.52  ?  184 LEU B C     1 
ATOM   3586 O  O     . LEU B 1 191 ? 2.168   -3.447  -25.434 1.00 58.56  ?  184 LEU B O     1 
ATOM   3587 C  CB    . LEU B 1 191 ? 5.428   -3.368  -25.785 1.00 57.04  ?  184 LEU B CB    1 
ATOM   3588 C  CG    . LEU B 1 191 ? 6.685   -3.669  -24.978 1.00 57.47  ?  184 LEU B CG    1 
ATOM   3589 C  CD1   . LEU B 1 191 ? 7.837   -2.780  -25.433 1.00 55.13  ?  184 LEU B CD1   1 
ATOM   3590 C  CD2   . LEU B 1 191 ? 6.426   -3.504  -23.489 1.00 56.68  ?  184 LEU B CD2   1 
ATOM   3591 N  N     . GLN B 1 192 ? 2.859   -3.755  -27.563 1.00 59.95  ?  185 GLN B N     1 
ATOM   3592 C  CA    . GLN B 1 192 ? 1.644   -3.253  -28.194 1.00 59.61  ?  185 GLN B CA    1 
ATOM   3593 C  C     . GLN B 1 192 ? 1.286   -1.852  -27.695 1.00 55.70  ?  185 GLN B C     1 
ATOM   3594 O  O     . GLN B 1 192 ? 0.157   -1.602  -27.267 1.00 55.72  ?  185 GLN B O     1 
ATOM   3595 C  CB    . GLN B 1 192 ? 0.464   -4.195  -27.942 1.00 63.14  ?  185 GLN B CB    1 
ATOM   3596 C  CG    . GLN B 1 192 ? 0.624   -5.546  -28.614 1.00 67.56  ?  185 GLN B CG    1 
ATOM   3597 C  CD    . GLN B 1 192 ? -0.721  -6.211  -28.810 1.00 71.08  ?  185 GLN B CD    1 
ATOM   3598 O  OE1   . GLN B 1 192 ? -1.414  -6.570  -27.854 1.00 72.48  ?  185 GLN B OE1   1 
ATOM   3599 N  NE2   . GLN B 1 192 ? -1.110  -6.361  -30.068 1.00 72.83  ?  185 GLN B NE2   1 
ATOM   3600 N  N     . PRO B 1 193 ? 2.218   -0.879  -27.758 1.00 52.58  ?  186 PRO B N     1 
ATOM   3601 C  CA    . PRO B 1 193 ? 1.863   0.517   -27.482 1.00 49.22  ?  186 PRO B CA    1 
ATOM   3602 C  C     . PRO B 1 193 ? 0.860   0.983   -28.529 1.00 49.48  ?  186 PRO B C     1 
ATOM   3603 O  O     . PRO B 1 193 ? 0.932   0.506   -29.669 1.00 51.37  ?  186 PRO B O     1 
ATOM   3604 C  CB    . PRO B 1 193 ? 3.194   1.239   -27.677 1.00 46.95  ?  186 PRO B CB    1 
ATOM   3605 C  CG    . PRO B 1 193 ? 3.945   0.373   -28.644 1.00 49.27  ?  186 PRO B CG    1 
ATOM   3606 C  CD    . PRO B 1 193 ? 3.606   -1.033  -28.213 1.00 52.54  ?  186 PRO B CD    1 
ATOM   3607 N  N     . PHE B 1 194 ? -0.041  1.911   -28.163 1.00 47.90  ?  187 PHE B N     1 
ATOM   3608 C  CA    . PHE B 1 194 ? -1.016  2.441   -29.120 1.00 48.33  ?  187 PHE B CA    1 
ATOM   3609 C  C     . PHE B 1 194 ? -0.325  3.391   -30.094 1.00 46.51  ?  187 PHE B C     1 
ATOM   3610 O  O     . PHE B 1 194 ? -0.751  3.581   -31.235 1.00 47.57  ?  187 PHE B O     1 
ATOM   3611 C  CB    . PHE B 1 194 ? -2.213  3.116   -28.432 1.00 47.73  ?  187 PHE B CB    1 
ATOM   3612 C  CG    . PHE B 1 194 ? -2.080  4.593   -28.143 1.00 44.53  ?  187 PHE B CG    1 
ATOM   3613 C  CD1   . PHE B 1 194 ? -1.371  5.033   -27.035 1.00 42.33  ?  187 PHE B CD1   1 
ATOM   3614 C  CD2   . PHE B 1 194 ? -2.689  5.537   -28.946 1.00 44.11  ?  187 PHE B CD2   1 
ATOM   3615 C  CE1   . PHE B 1 194 ? -1.256  6.388   -26.758 1.00 39.76  ?  187 PHE B CE1   1 
ATOM   3616 C  CE2   . PHE B 1 194 ? -2.578  6.897   -28.676 1.00 41.58  ?  187 PHE B CE2   1 
ATOM   3617 C  CZ    . PHE B 1 194 ? -1.865  7.316   -27.572 1.00 39.42  ?  187 PHE B CZ    1 
ATOM   3618 N  N     . ARG B 1 195 ? 0.782   3.960   -29.642 1.00 44.15  ?  188 ARG B N     1 
ATOM   3619 C  CA    . ARG B 1 195 ? 1.518   4.959   -30.370 1.00 42.48  ?  188 ARG B CA    1 
ATOM   3620 C  C     . ARG B 1 195 ? 3.011   4.770   -30.088 1.00 41.77  ?  188 ARG B C     1 
ATOM   3621 O  O     . ARG B 1 195 ? 3.442   4.697   -28.950 1.00 40.78  ?  188 ARG B O     1 
ATOM   3622 C  CB    . ARG B 1 195 ? 0.961   6.299   -29.880 1.00 40.19  ?  188 ARG B CB    1 
ATOM   3623 C  CG    . ARG B 1 195 ? 1.501   7.542   -30.558 1.00 38.62  ?  188 ARG B CG    1 
ATOM   3624 C  CD    . ARG B 1 195 ? 0.596   8.729   -30.207 1.00 37.32  ?  188 ARG B CD    1 
ATOM   3625 N  NE    . ARG B 1 195 ? 0.997   9.966   -30.876 1.00 36.27  ?  188 ARG B NE    1 
ATOM   3626 C  CZ    . ARG B 1 195 ? 0.511   10.387  -32.034 1.00 37.40  ?  188 ARG B CZ    1 
ATOM   3627 N  NH1   . ARG B 1 195 ? -0.321  9.613   -32.709 1.00 39.62  ?  188 ARG B NH1   1 
ATOM   3628 N  NH2   . ARG B 1 195 ? 0.895   11.545  -32.539 1.00 36.67  ?  188 ARG B NH2   1 
ATOM   3629 N  N     . TRP B 1 196 ? 3.794   4.729   -31.142 1.00 42.57  ?  189 TRP B N     1 
ATOM   3630 C  CA    . TRP B 1 196 ? 5.215   4.501   -31.054 1.00 42.58  ?  189 TRP B CA    1 
ATOM   3631 C  C     . TRP B 1 196 ? 5.943   5.590   -31.830 1.00 41.53  ?  189 TRP B C     1 
ATOM   3632 O  O     . TRP B 1 196 ? 6.074   5.525   -33.054 1.00 43.09  ?  189 TRP B O     1 
ATOM   3633 C  CB    . TRP B 1 196 ? 5.554   3.099   -31.590 1.00 45.69  ?  189 TRP B CB    1 
ATOM   3634 C  CG    . TRP B 1 196 ? 7.035   2.833   -31.622 1.00 46.27  ?  189 TRP B CG    1 
ATOM   3635 C  CD1   . TRP B 1 196 ? 7.960   3.254   -30.719 1.00 44.68  ?  189 TRP B CD1   1 
ATOM   3636 C  CD2   . TRP B 1 196 ? 7.750   1.992   -32.557 1.00 49.14  ?  189 TRP B CD2   1 
ATOM   3637 N  NE1   . TRP B 1 196 ? 9.213   2.811   -31.071 1.00 46.28  ?  189 TRP B NE1   1 
ATOM   3638 C  CE2   . TRP B 1 196 ? 9.108   2.022   -32.183 1.00 49.04  ?  189 TRP B CE2   1 
ATOM   3639 C  CE3   . TRP B 1 196 ? 7.375   1.260   -33.691 1.00 52.01  ?  189 TRP B CE3   1 
ATOM   3640 C  CZ2   . TRP B 1 196 ? 10.094  1.326   -32.884 1.00 51.78  ?  189 TRP B CZ2   1 
ATOM   3641 C  CZ3   . TRP B 1 196 ? 8.347   0.562   -34.377 1.00 54.68  ?  189 TRP B CZ3   1 
ATOM   3642 C  CH2   . TRP B 1 196 ? 9.686   0.597   -33.977 1.00 54.57  ?  189 TRP B CH2   1 
ATOM   3643 N  N     . LYS B 1 197 ? 6.377   6.659   -31.161 1.00 39.18  ?  190 LYS B N     1 
ATOM   3644 C  CA    . LYS B 1 197 ? 7.079   7.721   -31.862 1.00 38.56  ?  190 LYS B CA    1 
ATOM   3645 C  C     . LYS B 1 197 ? 8.511   7.274   -32.167 1.00 39.89  ?  190 LYS B C     1 
ATOM   3646 O  O     . LYS B 1 197 ? 9.229   6.851   -31.255 1.00 39.71  ?  190 LYS B O     1 
ATOM   3647 C  CB    . LYS B 1 197 ? 7.239   8.999   -31.034 1.00 36.10  ?  190 LYS B CB    1 
ATOM   3648 C  CG    . LYS B 1 197 ? 5.985   9.569   -30.389 1.00 34.66  ?  190 LYS B CG    1 
ATOM   3649 C  CD    . LYS B 1 197 ? 4.847   10.009  -31.286 1.00 35.20  ?  190 LYS B CD    1 
ATOM   3650 C  CE    . LYS B 1 197 ? 5.060   11.286  -32.049 1.00 34.86  ?  190 LYS B CE    1 
ATOM   3651 N  NZ    . LYS B 1 197 ? 4.818   12.540  -31.284 1.00 33.04  ?  190 LYS B NZ    1 
ATOM   3652 N  N     . CYS B 1 198 ? 8.885   7.386   -33.442 1.00 41.51  ?  191 CYS B N     1 
ATOM   3653 C  CA    . CYS B 1 198 ? 10.263  7.191   -33.859 1.00 43.04  ?  191 CYS B CA    1 
ATOM   3654 C  C     . CYS B 1 198 ? 10.853  8.492   -34.372 1.00 42.56  ?  191 CYS B C     1 
ATOM   3655 O  O     . CYS B 1 198 ? 10.563  8.935   -35.476 1.00 43.56  ?  191 CYS B O     1 
ATOM   3656 C  CB    . CYS B 1 198 ? 10.359  6.107   -34.922 1.00 46.16  ?  191 CYS B CB    1 
ATOM   3657 S  SG    . CYS B 1 198 ? 9.995   4.480   -34.240 1.00 47.52  ?  191 CYS B SG    1 
ATOM   3658 N  N     . PHE B 1 199 ? 11.628  9.146   -33.516 1.00 41.19  ?  192 PHE B N     1 
ATOM   3659 C  CA    . PHE B 1 199 ? 12.218  10.415  -33.867 1.00 40.96  ?  192 PHE B CA    1 
ATOM   3660 C  C     . PHE B 1 199 ? 13.598  10.219  -34.493 1.00 43.43  ?  192 PHE B C     1 
ATOM   3661 O  O     . PHE B 1 199 ? 14.462  9.602   -33.886 1.00 44.07  ?  192 PHE B O     1 
ATOM   3662 C  CB    . PHE B 1 199 ? 12.475  11.263  -32.622 1.00 38.76  ?  192 PHE B CB    1 
ATOM   3663 C  CG    . PHE B 1 199 ? 11.310  11.393  -31.672 1.00 36.47  ?  192 PHE B CG    1 
ATOM   3664 C  CD1   . PHE B 1 199 ? 10.149  12.042  -32.074 1.00 35.69  ?  192 PHE B CD1   1 
ATOM   3665 C  CD2   . PHE B 1 199 ? 11.399  10.908  -30.383 1.00 35.46  ?  192 PHE B CD2   1 
ATOM   3666 C  CE1   . PHE B 1 199 ? 9.083   12.158  -31.200 1.00 33.98  ?  192 PHE B CE1   1 
ATOM   3667 C  CE2   . PHE B 1 199 ? 10.353  11.088  -29.482 1.00 33.67  ?  192 PHE B CE2   1 
ATOM   3668 C  CZ    . PHE B 1 199 ? 9.196   11.696  -29.908 1.00 32.98  ?  192 PHE B CZ    1 
ATOM   3669 N  N     . GLN B 1 200 ? 13.819  10.832  -35.647 1.00 45.01  ?  193 GLN B N     1 
ATOM   3670 C  CA    . GLN B 1 200 ? 15.187  11.035  -36.101 1.00 47.30  ?  193 GLN B CA    1 
ATOM   3671 C  C     . GLN B 1 200 ? 15.928  11.969  -35.149 1.00 46.06  ?  193 GLN B C     1 
ATOM   3672 O  O     . GLN B 1 200 ? 15.467  13.057  -34.819 1.00 44.28  ?  193 GLN B O     1 
ATOM   3673 C  CB    . GLN B 1 200 ? 15.194  11.633  -37.495 1.00 49.41  ?  193 GLN B CB    1 
ATOM   3674 C  CG    . GLN B 1 200 ? 16.601  11.643  -38.111 1.00 52.61  ?  193 GLN B CG    1 
ATOM   3675 C  CD    . GLN B 1 200 ? 16.627  12.278  -39.479 1.00 55.07  ?  193 GLN B CD    1 
ATOM   3676 O  OE1   . GLN B 1 200 ? 15.635  12.813  -39.985 1.00 54.41  ?  193 GLN B OE1   1 
ATOM   3677 N  NE2   . GLN B 1 200 ? 17.815  12.269  -40.065 1.00 58.29  ?  193 GLN B NE2   1 
ATOM   3678 N  N     . VAL B 1 201 ? 17.116  11.573  -34.710 1.00 47.38  ?  194 VAL B N     1 
ATOM   3679 C  CA    . VAL B 1 201 ? 17.792  12.360  -33.700 1.00 46.40  ?  194 VAL B CA    1 
ATOM   3680 C  C     . VAL B 1 201 ? 17.981  13.771  -34.270 1.00 46.93  ?  194 VAL B C     1 
ATOM   3681 O  O     . VAL B 1 201 ? 18.327  13.967  -35.451 1.00 49.42  ?  194 VAL B O     1 
ATOM   3682 C  CB    . VAL B 1 201 ? 19.086  11.676  -33.218 1.00 48.35  ?  194 VAL B CB    1 
ATOM   3683 C  CG1   . VAL B 1 201 ? 20.134  11.660  -34.305 1.00 52.00  ?  194 VAL B CG1   1 
ATOM   3684 C  CG2   . VAL B 1 201 ? 19.621  12.294  -31.929 1.00 47.15  ?  194 VAL B CG2   1 
ATOM   3685 N  N     . LEU B 1 202 ? 17.638  14.777  -33.454 1.00 44.78  ?  195 LEU B N     1 
ATOM   3686 C  CA    . LEU B 1 202 ? 17.545  16.149  -33.924 1.00 45.13  ?  195 LEU B CA    1 
ATOM   3687 C  C     . LEU B 1 202 ? 18.568  17.034  -33.222 1.00 45.81  ?  195 LEU B C     1 
ATOM   3688 O  O     . LEU B 1 202 ? 18.785  16.928  -32.012 1.00 44.45  ?  195 LEU B O     1 
ATOM   3689 C  CB    . LEU B 1 202 ? 16.100  16.637  -33.719 1.00 42.54  ?  195 LEU B CB    1 
ATOM   3690 C  CG    . LEU B 1 202 ? 15.795  18.077  -34.099 1.00 42.81  ?  195 LEU B CG    1 
ATOM   3691 C  CD1   . LEU B 1 202 ? 15.633  18.242  -35.615 1.00 45.15  ?  195 LEU B CD1   1 
ATOM   3692 C  CD2   . LEU B 1 202 ? 14.536  18.574  -33.371 1.00 40.08  ?  195 LEU B CD2   1 
ATOM   3693 N  N     . ILE B 1 203 ? 19.193  17.903  -34.026 1.00 48.33  ?  196 ILE B N     1 
ATOM   3694 C  CA    . ILE B 1 203 ? 20.111  18.935  -33.566 1.00 49.65  ?  196 ILE B CA    1 
ATOM   3695 C  C     . ILE B 1 203 ? 19.321  20.220  -33.345 1.00 48.27  ?  196 ILE B C     1 
ATOM   3696 O  O     . ILE B 1 203 ? 18.658  20.723  -34.260 1.00 48.76  ?  196 ILE B O     1 
ATOM   3697 C  CB    . ILE B 1 203 ? 21.277  19.175  -34.560 1.00 53.82  ?  196 ILE B CB    1 
ATOM   3698 C  CG1   . ILE B 1 203 ? 22.119  17.917  -34.766 1.00 55.68  ?  196 ILE B CG1   1 
ATOM   3699 C  CG2   . ILE B 1 203 ? 22.125  20.356  -34.140 1.00 55.56  ?  196 ILE B CG2   1 
ATOM   3700 C  CD1   . ILE B 1 203 ? 22.681  17.316  -33.497 1.00 54.78  ?  196 ILE B CD1   1 
ATOM   3701 N  N     . VAL B 1 204 ? 19.390  20.712  -32.104 1.00 46.79  ?  197 VAL B N     1 
ATOM   3702 C  CA    . VAL B 1 204 ? 18.779  21.964  -31.702 1.00 45.85  ?  197 VAL B CA    1 
ATOM   3703 C  C     . VAL B 1 204 ? 19.868  22.960  -31.317 1.00 48.18  ?  197 VAL B C     1 
ATOM   3704 O  O     . VAL B 1 204 ? 20.651  22.698  -30.398 1.00 48.34  ?  197 VAL B O     1 
ATOM   3705 C  CB    . VAL B 1 204 ? 17.808  21.710  -30.527 1.00 42.39  ?  197 VAL B CB    1 
ATOM   3706 C  CG1   . VAL B 1 204 ? 17.260  23.009  -29.973 1.00 41.74  ?  197 VAL B CG1   1 
ATOM   3707 C  CG2   . VAL B 1 204 ? 16.689  20.759  -30.914 1.00 40.51  ?  197 VAL B CG2   1 
ATOM   3708 N  N     . THR B 1 205 ? 19.839  24.134  -31.965 1.00 50.13  ?  198 THR B N     1 
ATOM   3709 C  CA    . THR B 1 205 ? 20.821  25.186  -31.749 1.00 52.99  ?  198 THR B CA    1 
ATOM   3710 C  C     . THR B 1 205 ? 20.740  25.649  -30.296 1.00 51.36  ?  198 THR B C     1 
ATOM   3711 O  O     . THR B 1 205 ? 19.657  25.881  -29.784 1.00 48.76  ?  198 THR B O     1 
ATOM   3712 C  CB    . THR B 1 205 ? 20.602  26.342  -32.741 1.00 55.45  ?  198 THR B CB    1 
ATOM   3713 O  OG1   . THR B 1 205 ? 19.662  25.918  -33.726 1.00 54.54  ?  198 THR B OG1   1 
ATOM   3714 C  CG2   . THR B 1 205 ? 21.862  26.795  -33.443 1.00 60.01  ?  198 THR B CG2   1 
ATOM   3715 N  N     . GLY B 1 206 ? 21.893  25.745  -29.614 1.00 53.15  ?  199 GLY B N     1 
ATOM   3716 C  CA    . GLY B 1 206 ? 21.951  26.221  -28.246 1.00 52.26  ?  199 GLY B CA    1 
ATOM   3717 C  C     . GLY B 1 206 ? 21.770  25.116  -27.208 1.00 49.46  ?  199 GLY B C     1 
ATOM   3718 O  O     . GLY B 1 206 ? 21.959  25.385  -26.034 1.00 49.11  ?  199 GLY B O     1 
ATOM   3719 N  N     . GLU B 1 207 ? 21.436  23.883  -27.633 1.00 47.89  ?  200 GLU B N     1 
ATOM   3720 C  CA    . GLU B 1 207 ? 21.181  22.786  -26.708 1.00 45.51  ?  200 GLU B CA    1 
ATOM   3721 C  C     . GLU B 1 207 ? 22.197  21.647  -26.858 1.00 47.06  ?  200 GLU B C     1 
ATOM   3722 O  O     . GLU B 1 207 ? 22.695  21.135  -25.857 1.00 47.03  ?  200 GLU B O     1 
ATOM   3723 C  CB    . GLU B 1 207 ? 19.776  22.215  -26.933 1.00 42.44  ?  200 GLU B CB    1 
ATOM   3724 C  CG    . GLU B 1 207 ? 18.641  23.098  -26.414 1.00 40.53  ?  200 GLU B CG    1 
ATOM   3725 C  CD    . GLU B 1 207 ? 18.326  23.003  -24.923 1.00 38.78  ?  200 GLU B CD    1 
ATOM   3726 O  OE1   . GLU B 1 207 ? 19.078  22.340  -24.197 1.00 39.16  ?  200 GLU B OE1   1 
ATOM   3727 O  OE2   . GLU B 1 207 ? 17.276  23.568  -24.491 1.00 37.20  ?  200 GLU B OE2   1 
ATOM   3728 N  N     . ASN B 1 208 ? 22.418  21.186  -28.095 1.00 48.49  ?  201 ASN B N     1 
ATOM   3729 C  CA    . ASN B 1 208 ? 23.189  19.969  -28.325 1.00 49.90  ?  201 ASN B CA    1 
ATOM   3730 C  C     . ASN B 1 208 ? 24.023  20.079  -29.604 1.00 53.44  ?  201 ASN B C     1 
ATOM   3731 O  O     . ASN B 1 208 ? 24.292  19.070  -30.221 1.00 54.47  ?  201 ASN B O     1 
ATOM   3732 C  CB    . ASN B 1 208 ? 22.307  18.718  -28.343 1.00 47.43  ?  201 ASN B CB    1 
ATOM   3733 C  CG    . ASN B 1 208 ? 21.363  18.620  -29.522 1.00 46.62  ?  201 ASN B CG    1 
ATOM   3734 O  OD1   . ASN B 1 208 ? 21.231  19.575  -30.288 1.00 47.56  ?  201 ASN B OD1   1 
ATOM   3735 N  ND2   . ASN B 1 208 ? 20.695  17.494  -29.669 1.00 45.19  ?  201 ASN B ND2   1 
ATOM   3736 N  N     . ASP B 1 209 ? 24.462  21.285  -29.971 1.00 55.69  ?  202 ASP B N     1 
ATOM   3737 C  CA    . ASP B 1 209 ? 24.985  21.505  -31.310 1.00 59.00  ?  202 ASP B CA    1 
ATOM   3738 C  C     . ASP B 1 209 ? 26.502  21.731  -31.308 1.00 63.36  ?  202 ASP B C     1 
ATOM   3739 O  O     . ASP B 1 209 ? 27.079  21.870  -32.389 1.00 66.77  ?  202 ASP B O     1 
ATOM   3740 C  CB    . ASP B 1 209 ? 24.239  22.645  -31.992 1.00 58.91  ?  202 ASP B CB    1 
ATOM   3741 C  CG    . ASP B 1 209 ? 24.398  24.007  -31.347 1.00 59.65  ?  202 ASP B CG    1 
ATOM   3742 O  OD1   . ASP B 1 209 ? 24.362  24.091  -30.104 1.00 57.93  ?  202 ASP B OD1   1 
ATOM   3743 O  OD2   . ASP B 1 209 ? 24.474  24.982  -32.099 1.00 62.03  ?  202 ASP B OD2   1 
ATOM   3744 N  N     . SER B 1 210 ? 27.136  21.777  -30.121 1.00 63.62  ?  203 SER B N     1 
ATOM   3745 C  CA    . SER B 1 210 ? 28.579  21.996  -30.042 1.00 68.07  ?  203 SER B CA    1 
ATOM   3746 C  C     . SER B 1 210 ? 29.191  21.463  -28.739 1.00 67.99  ?  203 SER B C     1 
ATOM   3747 O  O     . SER B 1 210 ? 28.565  20.728  -27.967 1.00 64.67  ?  203 SER B O     1 
ATOM   3748 C  CB    . SER B 1 210 ? 28.897  23.469  -30.253 1.00 70.65  ?  203 SER B CB    1 
ATOM   3749 O  OG    . SER B 1 210 ? 28.672  24.216  -29.066 1.00 69.16  ?  203 SER B OG    1 
ATOM   3750 N  N     . ASP B 1 211 ? 30.472  21.810  -28.525 1.00 72.20  ?  204 ASP B N     1 
ATOM   3751 C  CA    . ASP B 1 211 ? 31.214  21.423  -27.335 1.00 73.14  ?  204 ASP B CA    1 
ATOM   3752 C  C     . ASP B 1 211 ? 31.094  22.542  -26.304 1.00 72.55  ?  204 ASP B C     1 
ATOM   3753 O  O     . ASP B 1 211 ? 31.517  22.389  -25.160 1.00 72.88  ?  204 ASP B O     1 
ATOM   3754 C  CB    . ASP B 1 211 ? 32.671  21.096  -27.685 1.00 78.47  ?  204 ASP B CB    1 
ATOM   3755 C  CG    . ASP B 1 211 ? 32.811  20.175  -28.887 1.00 79.81  ?  204 ASP B CG    1 
ATOM   3756 O  OD1   . ASP B 1 211 ? 32.366  19.015  -28.797 1.00 77.53  ?  204 ASP B OD1   1 
ATOM   3757 O  OD2   . ASP B 1 211 ? 33.333  20.639  -29.922 1.00 83.36  ?  204 ASP B OD2   1 
ATOM   3758 N  N     . LYS B 1 212 ? 30.527  23.673  -26.736 1.00 72.07  ?  205 LYS B N     1 
ATOM   3759 C  CA    . LYS B 1 212 ? 30.090  24.715  -25.824 1.00 70.82  ?  205 LYS B CA    1 
ATOM   3760 C  C     . LYS B 1 212 ? 28.872  24.254  -25.024 1.00 65.70  ?  205 LYS B C     1 
ATOM   3761 O  O     . LYS B 1 212 ? 28.727  24.642  -23.873 1.00 64.80  ?  205 LYS B O     1 
ATOM   3762 C  CB    . LYS B 1 212 ? 29.761  26.006  -26.578 1.00 72.01  ?  205 LYS B CB    1 
ATOM   3763 C  CG    . LYS B 1 212 ? 30.937  26.939  -26.827 1.00 77.50  ?  205 LYS B CG    1 
ATOM   3764 C  CD    . LYS B 1 212 ? 31.941  26.447  -27.846 1.00 81.49  ?  205 LYS B CD    1 
ATOM   3765 C  CE    . LYS B 1 212 ? 33.150  27.357  -27.933 1.00 87.37  ?  205 LYS B CE    1 
ATOM   3766 N  NZ    . LYS B 1 212 ? 32.759  28.764  -28.198 1.00 88.48  ?  205 LYS B NZ    1 
ATOM   3767 N  N     . THR B 1 213 ? 27.991  23.440  -25.617 1.00 62.68  ?  206 THR B N     1 
ATOM   3768 C  CA    . THR B 1 213 ? 26.737  23.072  -24.959 1.00 58.13  ?  206 THR B CA    1 
ATOM   3769 C  C     . THR B 1 213 ? 26.964  21.871  -24.035 1.00 57.20  ?  206 THR B C     1 
ATOM   3770 O  O     . THR B 1 213 ? 28.034  21.267  -24.054 1.00 59.95  ?  206 THR B O     1 
ATOM   3771 C  CB    . THR B 1 213 ? 25.644  22.834  -26.008 1.00 55.74  ?  206 THR B CB    1 
ATOM   3772 O  OG1   . THR B 1 213 ? 26.139  21.930  -26.995 1.00 57.31  ?  206 THR B OG1   1 
ATOM   3773 C  CG2   . THR B 1 213 ? 25.197  24.096  -26.713 1.00 56.32  ?  206 THR B CG2   1 
ATOM   3774 N  N     . LEU B 1 214 ? 25.946  21.509  -23.236 1.00 53.64  ?  207 LEU B N     1 
ATOM   3775 C  CA    . LEU B 1 214 ? 26.061  20.421  -22.272 1.00 52.88  ?  207 LEU B CA    1 
ATOM   3776 C  C     . LEU B 1 214 ? 26.036  19.069  -22.990 1.00 52.64  ?  207 LEU B C     1 
ATOM   3777 O  O     . LEU B 1 214 ? 26.399  18.036  -22.406 1.00 53.12  ?  207 LEU B O     1 
ATOM   3778 C  CB    . LEU B 1 214 ? 24.925  20.513  -21.240 1.00 49.54  ?  207 LEU B CB    1 
ATOM   3779 C  CG    . LEU B 1 214 ? 24.931  21.746  -20.334 1.00 49.97  ?  207 LEU B CG    1 
ATOM   3780 C  CD1   . LEU B 1 214 ? 23.636  21.828  -19.530 1.00 46.67  ?  207 LEU B CD1   1 
ATOM   3781 C  CD2   . LEU B 1 214 ? 26.134  21.730  -19.388 1.00 52.94  ?  207 LEU B CD2   1 
ATOM   3782 N  N     . ARG B 1 215 ? 25.611  19.083  -24.255 1.00 52.22  ?  208 ARG B N     1 
ATOM   3783 C  CA    . ARG B 1 215 ? 25.695  17.920  -25.124 1.00 52.77  ?  208 ARG B CA    1 
ATOM   3784 C  C     . ARG B 1 215 ? 26.117  18.346  -26.528 1.00 55.12  ?  208 ARG B C     1 
ATOM   3785 O  O     . ARG B 1 215 ? 25.907  19.490  -26.932 1.00 55.26  ?  208 ARG B O     1 
ATOM   3786 C  CB    . ARG B 1 215 ? 24.339  17.212  -25.247 1.00 49.29  ?  208 ARG B CB    1 
ATOM   3787 C  CG    . ARG B 1 215 ? 23.761  16.685  -23.946 1.00 47.05  ?  208 ARG B CG    1 
ATOM   3788 C  CD    . ARG B 1 215 ? 24.565  15.516  -23.423 1.00 48.86  ?  208 ARG B CD    1 
ATOM   3789 N  NE    . ARG B 1 215 ? 23.826  14.854  -22.367 1.00 46.76  ?  208 ARG B NE    1 
ATOM   3790 C  CZ    . ARG B 1 215 ? 23.700  15.292  -21.124 1.00 45.97  ?  208 ARG B CZ    1 
ATOM   3791 N  NH1   . ARG B 1 215 ? 24.418  16.311  -20.700 1.00 47.40  ?  208 ARG B NH1   1 
ATOM   3792 N  NH2   . ARG B 1 215 ? 22.876  14.677  -20.293 1.00 44.12  ?  208 ARG B NH2   1 
ATOM   3793 N  N     . ASN B 1 216 ? 26.698  17.381  -27.256 1.00 57.23  ?  209 ASN B N     1 
ATOM   3794 C  CA    . ASN B 1 216 ? 26.992  17.491  -28.679 1.00 59.56  ?  209 ASN B CA    1 
ATOM   3795 C  C     . ASN B 1 216 ? 26.504  16.215  -29.350 1.00 58.86  ?  209 ASN B C     1 
ATOM   3796 O  O     . ASN B 1 216 ? 27.116  15.164  -29.197 1.00 60.51  ?  209 ASN B O     1 
ATOM   3797 C  CB    . ASN B 1 216 ? 28.494  17.664  -28.934 1.00 64.35  ?  209 ASN B CB    1 
ATOM   3798 C  CG    . ASN B 1 216 ? 28.853  17.941  -30.379 1.00 67.31  ?  209 ASN B CG    1 
ATOM   3799 O  OD1   . ASN B 1 216 ? 28.139  17.554  -31.304 1.00 66.28  ?  209 ASN B OD1   1 
ATOM   3800 N  ND2   . ASN B 1 216 ? 29.977  18.612  -30.582 1.00 71.40  ?  209 ASN B ND2   1 
ATOM   3801 N  N     . ALA B 1 217 ? 25.427  16.307  -30.132 1.00 56.85  ?  210 ALA B N     1 
ATOM   3802 C  CA    . ALA B 1 217 ? 24.760  15.114  -30.642 1.00 55.85  ?  210 ALA B CA    1 
ATOM   3803 C  C     . ALA B 1 217 ? 25.273  14.751  -32.037 1.00 59.15  ?  210 ALA B C     1 
ATOM   3804 O  O     . ALA B 1 217 ? 24.841  13.758  -32.618 1.00 59.12  ?  210 ALA B O     1 
ATOM   3805 C  CB    . ALA B 1 217 ? 23.280  15.385  -30.687 1.00 52.20  ?  210 ALA B CB    1 
ATOM   3806 N  N     . HIS B 1 218 ? 26.173  15.585  -32.572 1.00 62.27  ?  211 HIS B N     1 
ATOM   3807 C  CA    . HIS B 1 218 ? 26.526  15.555  -33.985 1.00 65.50  ?  211 HIS B CA    1 
ATOM   3808 C  C     . HIS B 1 218 ? 26.996  14.183  -34.462 1.00 67.86  ?  211 HIS B C     1 
ATOM   3809 O  O     . HIS B 1 218 ? 26.722  13.833  -35.608 1.00 69.18  ?  211 HIS B O     1 
ATOM   3810 C  CB    . HIS B 1 218 ? 27.574  16.618  -34.302 1.00 69.12  ?  211 HIS B CB    1 
ATOM   3811 C  CG    . HIS B 1 218 ? 26.942  17.914  -34.614 1.00 68.01  ?  211 HIS B CG    1 
ATOM   3812 N  ND1   . HIS B 1 218 ? 26.172  18.045  -35.747 1.00 67.88  ?  211 HIS B ND1   1 
ATOM   3813 C  CD2   . HIS B 1 218 ? 26.936  19.090  -34.004 1.00 67.34  ?  211 HIS B CD2   1 
ATOM   3814 C  CE1   . HIS B 1 218 ? 25.739  19.291  -35.824 1.00 67.26  ?  211 HIS B CE1   1 
ATOM   3815 N  NE2   . HIS B 1 218 ? 26.180  19.943  -34.769 1.00 66.88  ?  211 HIS B NE2   1 
ATOM   3816 N  N     . SER B 1 219 ? 27.617  13.399  -33.570 1.00 68.44  ?  212 SER B N     1 
ATOM   3817 C  CA    . SER B 1 219 ? 28.219  12.125  -33.931 1.00 71.39  ?  212 SER B CA    1 
ATOM   3818 C  C     . SER B 1 219 ? 27.178  11.008  -33.912 1.00 68.92  ?  212 SER B C     1 
ATOM   3819 O  O     . SER B 1 219 ? 27.482  9.877   -34.293 1.00 71.26  ?  212 SER B O     1 
ATOM   3820 C  CB    . SER B 1 219 ? 29.374  11.807  -33.022 1.00 73.70  ?  212 SER B CB    1 
ATOM   3821 O  OG    . SER B 1 219 ? 28.931  11.445  -31.715 1.00 70.59  ?  212 SER B OG    1 
ATOM   3822 N  N     . LEU B 1 220 ? 25.956  11.325  -33.453 1.00 64.54  ?  213 LEU B N     1 
ATOM   3823 C  CA    . LEU B 1 220 ? 24.879  10.346  -33.409 1.00 62.32  ?  213 LEU B CA    1 
ATOM   3824 C  C     . LEU B 1 220 ? 23.876  10.589  -34.541 1.00 61.40  ?  213 LEU B C     1 
ATOM   3825 O  O     . LEU B 1 220 ? 22.971  9.774   -34.736 1.00 60.21  ?  213 LEU B O     1 
ATOM   3826 C  CB    . LEU B 1 220 ? 24.176  10.402  -32.046 1.00 58.51  ?  213 LEU B CB    1 
ATOM   3827 C  CG    . LEU B 1 220 ? 25.028  10.064  -30.821 1.00 59.33  ?  213 LEU B CG    1 
ATOM   3828 C  CD1   . LEU B 1 220 ? 25.626  11.322  -30.228 1.00 59.21  ?  213 LEU B CD1   1 
ATOM   3829 C  CD2   . LEU B 1 220 ? 24.214  9.341   -29.768 1.00 56.69  ?  213 LEU B CD2   1 
ATOM   3830 N  N     . THR B 1 221 ? 24.015  11.703  -35.270 1.00 62.23  ?  214 THR B N     1 
ATOM   3831 C  CA    . THR B 1 221 ? 23.083  12.027  -36.342 1.00 61.70  ?  214 THR B CA    1 
ATOM   3832 C  C     . THR B 1 221 ? 23.151  10.986  -37.452 1.00 64.60  ?  214 THR B C     1 
ATOM   3833 O  O     . THR B 1 221 ? 24.224  10.433  -37.713 1.00 68.14  ?  214 THR B O     1 
ATOM   3834 C  CB    . THR B 1 221 ? 23.336  13.422  -36.923 1.00 62.78  ?  214 THR B CB    1 
ATOM   3835 O  OG1   . THR B 1 221 ? 24.663  13.453  -37.460 1.00 67.17  ?  214 THR B OG1   1 
ATOM   3836 C  CG2   . THR B 1 221 ? 23.110  14.520  -35.907 1.00 60.02  ?  214 THR B CG2   1 
ATOM   3837 N  N     . ILE B 1 222 ? 21.996  10.733  -38.094 1.00 63.37  ?  215 ILE B N     1 
ATOM   3838 C  CA    . ILE B 1 222 ? 21.887  9.765   -39.175 1.00 66.10  ?  215 ILE B CA    1 
ATOM   3839 C  C     . ILE B 1 222 ? 21.348  10.458  -40.426 1.00 67.10  ?  215 ILE B C     1 
ATOM   3840 O  O     . ILE B 1 222 ? 20.956  11.630  -40.389 1.00 65.41  ?  215 ILE B O     1 
ATOM   3841 C  CB    . ILE B 1 222 ? 21.030  8.553   -38.742 1.00 64.45  ?  215 ILE B CB    1 
ATOM   3842 C  CG1   . ILE B 1 222 ? 19.607  8.967   -38.352 1.00 60.40  ?  215 ILE B CG1   1 
ATOM   3843 C  CG2   . ILE B 1 222 ? 21.715  7.799   -37.622 1.00 64.48  ?  215 ILE B CG2   1 
ATOM   3844 C  CD1   . ILE B 1 222 ? 18.652  7.814   -38.202 1.00 59.55  ?  215 ILE B CD1   1 
ATOM   3845 N  N     . SER B 1 223 ? 21.425  9.746   -41.565 1.00 70.45  ?  216 SER B N     1 
ATOM   3846 C  CA    . SER B 1 223 ? 20.984  10.272  -42.846 1.00 72.21  ?  216 SER B CA    1 
ATOM   3847 C  C     . SER B 1 223 ? 19.489  10.033  -43.023 1.00 69.77  ?  216 SER B C     1 
ATOM   3848 O  O     . SER B 1 223 ? 18.942  9.097   -42.444 1.00 68.08  ?  216 SER B O     1 
ATOM   3849 C  CB    . SER B 1 223 ? 21.719  9.631   -43.990 1.00 77.26  ?  216 SER B CB    1 
ATOM   3850 O  OG    . SER B 1 223 ? 21.378  8.252   -44.068 1.00 77.94  ?  216 SER B OG    1 
ATOM   3851 N  N     . ASP B 1 224 ? 18.879  10.855  -43.892 1.00 70.23  ?  217 ASP B N     1 
ATOM   3852 C  CA    . ASP B 1 224 ? 17.498  10.668  -44.304 1.00 68.95  ?  217 ASP B CA    1 
ATOM   3853 C  C     . ASP B 1 224 ? 17.283  9.201   -44.681 1.00 70.75  ?  217 ASP B C     1 
ATOM   3854 O  O     . ASP B 1 224 ? 16.330  8.591   -44.211 1.00 68.57  ?  217 ASP B O     1 
ATOM   3855 C  CB    . ASP B 1 224 ? 17.104  11.599  -45.460 1.00 70.82  ?  217 ASP B CB    1 
ATOM   3856 C  CG    . ASP B 1 224 ? 17.354  13.080  -45.222 1.00 69.90  ?  217 ASP B CG    1 
ATOM   3857 O  OD1   . ASP B 1 224 ? 17.156  13.545  -44.079 1.00 66.33  ?  217 ASP B OD1   1 
ATOM   3858 O  OD2   . ASP B 1 224 ? 17.722  13.774  -46.198 1.00 73.08  ?  217 ASP B OD2   1 
ATOM   3859 N  N     . ASP B 1 225 ? 18.187  8.636   -45.508 1.00 75.07  ?  218 ASP B N     1 
ATOM   3860 C  CA    . ASP B 1 225 ? 18.067  7.258   -45.964 1.00 77.55  ?  218 ASP B CA    1 
ATOM   3861 C  C     . ASP B 1 225 ? 18.149  6.257   -44.810 1.00 75.76  ?  218 ASP B C     1 
ATOM   3862 O  O     . ASP B 1 225 ? 17.363  5.309   -44.769 1.00 75.59  ?  218 ASP B O     1 
ATOM   3863 C  CB    . ASP B 1 225 ? 19.129  6.934   -47.020 1.00 82.88  ?  218 ASP B CB    1 
ATOM   3864 C  CG    . ASP B 1 225 ? 18.802  7.471   -48.404 1.00 85.79  ?  218 ASP B CG    1 
ATOM   3865 O  OD1   . ASP B 1 225 ? 18.151  8.537   -48.490 1.00 83.78  ?  218 ASP B OD1   1 
ATOM   3866 O  OD2   . ASP B 1 225 ? 19.202  6.821   -49.387 1.00 90.34  ?  218 ASP B OD2   1 
ATOM   3867 N  N     . GLU B 1 226 ? 19.127  6.426   -43.909 1.00 74.98  ?  219 GLU B N     1 
ATOM   3868 C  CA    . GLU B 1 226 ? 19.247  5.565   -42.741 1.00 73.42  ?  219 GLU B CA    1 
ATOM   3869 C  C     . GLU B 1 226 ? 17.942  5.583   -41.932 1.00 69.13  ?  219 GLU B C     1 
ATOM   3870 O  O     . GLU B 1 226 ? 17.433  4.534   -41.546 1.00 68.94  ?  219 GLU B O     1 
ATOM   3871 C  CB    . GLU B 1 226 ? 20.439  5.977   -41.869 1.00 73.11  ?  219 GLU B CB    1 
ATOM   3872 C  CG    . GLU B 1 226 ? 21.784  5.424   -42.340 1.00 77.83  ?  219 GLU B CG    1 
ATOM   3873 C  CD    . GLU B 1 226 ? 23.017  6.187   -41.865 1.00 78.51  ?  219 GLU B CD    1 
ATOM   3874 O  OE1   . GLU B 1 226 ? 22.874  7.297   -41.324 1.00 75.56  ?  219 GLU B OE1   1 
ATOM   3875 O  OE2   . GLU B 1 226 ? 24.134  5.667   -42.037 1.00 82.33  ?  219 GLU B OE2   1 
ATOM   3876 N  N     . PHE B 1 227 ? 17.391  6.776   -41.676 1.00 66.05  ?  220 PHE B N     1 
ATOM   3877 C  CA    . PHE B 1 227 ? 16.154  6.867   -40.901 1.00 62.27  ?  220 PHE B CA    1 
ATOM   3878 C  C     . PHE B 1 227 ? 15.019  6.102   -41.591 1.00 63.25  ?  220 PHE B C     1 
ATOM   3879 O  O     . PHE B 1 227 ? 14.328  5.296   -40.961 1.00 62.11  ?  220 PHE B O     1 
ATOM   3880 C  CB    . PHE B 1 227 ? 15.757  8.324   -40.682 1.00 59.53  ?  220 PHE B CB    1 
ATOM   3881 C  CG    . PHE B 1 227 ? 14.519  8.461   -39.833 1.00 55.92  ?  220 PHE B CG    1 
ATOM   3882 C  CD1   . PHE B 1 227 ? 14.550  8.137   -38.483 1.00 53.57  ?  220 PHE B CD1   1 
ATOM   3883 C  CD2   . PHE B 1 227 ? 13.309  8.811   -40.407 1.00 55.36  ?  220 PHE B CD2   1 
ATOM   3884 C  CE1   . PHE B 1 227 ? 13.391  8.210   -37.719 1.00 50.70  ?  220 PHE B CE1   1 
ATOM   3885 C  CE2   . PHE B 1 227 ? 12.156  8.894   -39.638 1.00 52.49  ?  220 PHE B CE2   1 
ATOM   3886 C  CZ    . PHE B 1 227 ? 12.211  8.608   -38.295 1.00 50.17  ?  220 PHE B CZ    1 
ATOM   3887 N  N     . ASP B 1 228 ? 14.855  6.342   -42.900 1.00 65.78  ?  221 ASP B N     1 
ATOM   3888 C  CA    . ASP B 1 228 ? 13.787  5.728   -43.680 1.00 67.20  ?  221 ASP B CA    1 
ATOM   3889 C  C     . ASP B 1 228 ? 13.897  4.204   -43.645 1.00 69.53  ?  221 ASP B C     1 
ATOM   3890 O  O     . ASP B 1 228 ? 12.893  3.526   -43.485 1.00 69.16  ?  221 ASP B O     1 
ATOM   3891 C  CB    . ASP B 1 228 ? 13.773  6.243   -45.124 1.00 70.19  ?  221 ASP B CB    1 
ATOM   3892 C  CG    . ASP B 1 228 ? 13.325  7.688   -45.267 1.00 68.29  ?  221 ASP B CG    1 
ATOM   3893 O  OD1   . ASP B 1 228 ? 12.578  8.166   -44.386 1.00 64.66  ?  221 ASP B OD1   1 
ATOM   3894 O  OD2   . ASP B 1 228 ? 13.742  8.334   -46.246 1.00 70.76  ?  221 ASP B OD2   1 
ATOM   3895 N  N     . ARG B 1 229 ? 15.122  3.691   -43.793 1.00 72.24  ?  222 ARG B N     1 
ATOM   3896 C  CA    . ARG B 1 229 ? 15.339  2.222   -43.731 1.00 74.93  ?  222 ARG B CA    1 
ATOM   3897 C  C     . ARG B 1 229 ? 14.825  1.697   -42.383 1.00 72.13  ?  222 ARG B C     1 
ATOM   3898 O  O     . ARG B 1 229 ? 14.113  0.669   -42.381 1.00 73.44  ?  222 ARG B O     1 
ATOM   3899 C  CB    . ARG B 1 229 ? 16.820  1.878   -43.920 1.00 78.22  ?  222 ARG B CB    1 
ATOM   3900 C  CG    . ARG B 1 229 ? 17.257  1.834   -45.376 1.00 82.75  ?  222 ARG B CG    1 
ATOM   3901 C  CD    . ARG B 1 229 ? 18.671  1.292   -45.522 1.00 86.64  ?  222 ARG B CD    1 
ATOM   3902 N  NE    . ARG B 1 229 ? 19.720  2.267   -45.201 1.00 87.83  ?  222 ARG B NE    1 
ATOM   3903 C  CZ    . ARG B 1 229 ? 19.977  3.369   -45.896 1.00 87.52  ?  222 ARG B CZ    1 
ATOM   3904 N  NH1   . ARG B 1 229 ? 19.337  3.607   -47.027 1.00 86.56  ?  222 ARG B NH1   1 
ATOM   3905 N  NH2   . ARG B 1 229 ? 20.889  4.222   -45.466 1.00 88.65  ?  222 ARG B NH2   1 
ATOM   3906 N  N     . PHE B 1 230 ? 15.170  2.378   -41.286 1.00 68.74  ?  223 PHE B N     1 
ATOM   3907 C  CA    . PHE B 1 230 ? 14.740  1.926   -39.974 1.00 66.26  ?  223 PHE B CA    1 
ATOM   3908 C  C     . PHE B 1 230 ? 13.224  1.772   -39.944 1.00 64.81  ?  223 PHE B C     1 
ATOM   3909 O  O     . PHE B 1 230 ? 12.703  0.792   -39.413 1.00 65.24  ?  223 PHE B O     1 
ATOM   3910 C  CB    . PHE B 1 230 ? 15.165  2.905   -38.872 1.00 62.75  ?  223 PHE B CB    1 
ATOM   3911 C  CG    . PHE B 1 230 ? 14.648  2.518   -37.510 1.00 60.29  ?  223 PHE B CG    1 
ATOM   3912 C  CD1   . PHE B 1 230 ? 13.386  2.916   -37.091 1.00 57.42  ?  223 PHE B CD1   1 
ATOM   3913 C  CD2   . PHE B 1 230 ? 15.394  1.709   -36.673 1.00 61.30  ?  223 PHE B CD2   1 
ATOM   3914 C  CE1   . PHE B 1 230 ? 12.907  2.552   -35.845 1.00 55.56  ?  223 PHE B CE1   1 
ATOM   3915 C  CE2   . PHE B 1 230 ? 14.912  1.341   -35.429 1.00 59.42  ?  223 PHE B CE2   1 
ATOM   3916 C  CZ    . PHE B 1 230 ? 13.664  1.755   -35.021 1.00 56.58  ?  223 PHE B CZ    1 
ATOM   3917 N  N     . CYS B 1 231 ? 12.531  2.802   -40.443 1.00 63.21  ?  224 CYS B N     1 
ATOM   3918 C  CA    . CYS B 1 231 ? 11.078  2.812   -40.446 1.00 61.98  ?  224 CYS B CA    1 
ATOM   3919 C  C     . CYS B 1 231 ? 10.544  1.675   -41.331 1.00 65.66  ?  224 CYS B C     1 
ATOM   3920 O  O     . CYS B 1 231 ? 9.621   0.956   -40.935 1.00 65.72  ?  224 CYS B O     1 
ATOM   3921 C  CB    . CYS B 1 231 ? 10.563  4.182   -40.884 1.00 60.14  ?  224 CYS B CB    1 
ATOM   3922 S  SG    . CYS B 1 231 ? 10.931  5.525   -39.706 1.00 55.84  ?  224 CYS B SG    1 
ATOM   3923 N  N     . GLU B 1 232 ? 11.130  1.512   -42.525 1.00 69.05  ?  225 GLU B N     1 
ATOM   3924 C  CA    . GLU B 1 232 ? 10.697  0.470   -43.450 1.00 73.04  ?  225 GLU B CA    1 
ATOM   3925 C  C     . GLU B 1 232 ? 10.780  -0.887  -42.758 1.00 74.50  ?  225 GLU B C     1 
ATOM   3926 O  O     . GLU B 1 232 ? 9.865   -1.702  -42.885 1.00 76.15  ?  225 GLU B O     1 
ATOM   3927 C  CB    . GLU B 1 232 ? 11.537  0.459   -44.730 1.00 76.83  ?  225 GLU B CB    1 
ATOM   3928 C  CG    . GLU B 1 232 ? 11.344  1.677   -45.623 1.00 76.50  ?  225 GLU B CG    1 
ATOM   3929 C  CD    . GLU B 1 232 ? 12.486  1.956   -46.592 1.00 79.60  ?  225 GLU B CD    1 
ATOM   3930 O  OE1   . GLU B 1 232 ? 12.622  3.130   -47.020 1.00 78.81  ?  225 GLU B OE1   1 
ATOM   3931 O  OE2   . GLU B 1 232 ? 13.236  1.006   -46.929 1.00 83.15  ?  225 GLU B OE2   1 
ATOM   3932 N  N     . ARG B 1 233 ? 11.885  -1.102  -42.021 1.00 74.18  ?  226 ARG B N     1 
ATOM   3933 C  CA    . ARG B 1 233 ? 12.179  -2.348  -41.329 1.00 75.95  ?  226 ARG B CA    1 
ATOM   3934 C  C     . ARG B 1 233 ? 11.067  -2.680  -40.338 1.00 73.89  ?  226 ARG B C     1 
ATOM   3935 O  O     . ARG B 1 233 ? 10.976  -3.831  -39.920 1.00 76.05  ?  226 ARG B O     1 
ATOM   3936 C  CB    . ARG B 1 233 ? 13.548  -2.247  -40.632 1.00 75.51  ?  226 ARG B CB    1 
ATOM   3937 C  CG    . ARG B 1 233 ? 14.099  -3.549  -40.058 1.00 78.29  ?  226 ARG B CG    1 
ATOM   3938 C  CD    . ARG B 1 233 ? 15.326  -3.331  -39.195 1.00 77.45  ?  226 ARG B CD    1 
ATOM   3939 N  NE    . ARG B 1 233 ? 16.316  -2.587  -39.959 1.00 78.33  ?  226 ARG B NE    1 
ATOM   3940 C  CZ    . ARG B 1 233 ? 16.854  -1.428  -39.614 1.00 75.57  ?  226 ARG B CZ    1 
ATOM   3941 N  NH1   . ARG B 1 233 ? 16.766  -0.980  -38.369 1.00 71.99  ?  226 ARG B NH1   1 
ATOM   3942 N  NH2   . ARG B 1 233 ? 17.519  -0.737  -40.525 1.00 76.86  ?  226 ARG B NH2   1 
ATOM   3943 N  N     . HIS B 1 234 ? 10.240  -1.675  -39.961 1.00 70.08  ?  227 HIS B N     1 
ATOM   3944 C  CA    . HIS B 1 234 ? 9.203   -1.827  -38.944 1.00 67.99  ?  227 HIS B CA    1 
ATOM   3945 C  C     . HIS B 1 234 ? 7.819   -1.482  -39.497 1.00 67.69  ?  227 HIS B C     1 
ATOM   3946 O  O     . HIS B 1 234 ? 6.934   -1.040  -38.750 1.00 65.05  ?  227 HIS B O     1 
ATOM   3947 C  CB    . HIS B 1 234 ? 9.501   -0.921  -37.742 1.00 63.76  ?  227 HIS B CB    1 
ATOM   3948 C  CG    . HIS B 1 234 ? 10.716  -1.372  -37.016 1.00 64.28  ?  227 HIS B CG    1 
ATOM   3949 N  ND1   . HIS B 1 234 ? 11.949  -0.832  -37.304 1.00 64.34  ?  227 HIS B ND1   1 
ATOM   3950 C  CD2   . HIS B 1 234 ? 10.922  -2.336  -36.115 1.00 65.37  ?  227 HIS B CD2   1 
ATOM   3951 C  CE1   . HIS B 1 234 ? 12.865  -1.447  -36.574 1.00 65.37  ?  227 HIS B CE1   1 
ATOM   3952 N  NE2   . HIS B 1 234 ? 12.262  -2.359  -35.846 1.00 65.98  ?  227 HIS B NE2   1 
ATOM   3953 N  N     . SER B 1 235 ? 7.627   -1.723  -40.798 1.00 70.79  ?  228 SER B N     1 
ATOM   3954 C  CA    . SER B 1 235 ? 6.450   -1.257  -41.518 1.00 70.94  ?  228 SER B CA    1 
ATOM   3955 C  C     . SER B 1 235 ? 5.191   -1.998  -41.075 1.00 71.84  ?  228 SER B C     1 
ATOM   3956 O  O     . SER B 1 235 ? 4.090   -1.526  -41.329 1.00 71.35  ?  228 SER B O     1 
ATOM   3957 C  CB    . SER B 1 235 ? 6.675   -1.395  -43.009 1.00 74.56  ?  228 SER B CB    1 
ATOM   3958 O  OG    . SER B 1 235 ? 7.279   -2.651  -43.302 1.00 78.47  ?  228 SER B OG    1 
ATOM   3959 N  N     . SER B 1 236 ? 5.335   -3.132  -40.384 1.00 73.41  ?  229 SER B N     1 
ATOM   3960 C  CA    . SER B 1 236 ? 4.169   -3.860  -39.911 1.00 74.69  ?  229 SER B CA    1 
ATOM   3961 C  C     . SER B 1 236 ? 3.674   -3.344  -38.559 1.00 70.96  ?  229 SER B C     1 
ATOM   3962 O  O     . SER B 1 236 ? 2.728   -3.907  -38.004 1.00 71.95  ?  229 SER B O     1 
ATOM   3963 C  CB    . SER B 1 236 ? 4.453   -5.343  -39.850 1.00 78.81  ?  229 SER B CB    1 
ATOM   3964 O  OG    . SER B 1 236 ? 5.381   -5.651  -38.817 1.00 77.71  ?  229 SER B OG    1 
ATOM   3965 N  N     . GLN B 1 237 ? 4.334   -2.313  -38.007 1.00 67.06  ?  230 GLN B N     1 
ATOM   3966 C  CA    . GLN B 1 237 ? 3.881   -1.697  -36.773 1.00 63.58  ?  230 GLN B CA    1 
ATOM   3967 C  C     . GLN B 1 237 ? 2.966   -0.533  -37.140 1.00 61.61  ?  230 GLN B C     1 
ATOM   3968 O  O     . GLN B 1 237 ? 3.420   0.505   -37.613 1.00 59.81  ?  230 GLN B O     1 
ATOM   3969 C  CB    . GLN B 1 237 ? 5.070   -1.255  -35.911 1.00 60.90  ?  230 GLN B CB    1 
ATOM   3970 C  CG    . GLN B 1 237 ? 6.063   -2.368  -35.600 1.00 63.20  ?  230 GLN B CG    1 
ATOM   3971 C  CD    . GLN B 1 237 ? 5.436   -3.481  -34.803 1.00 65.15  ?  230 GLN B CD    1 
ATOM   3972 O  OE1   . GLN B 1 237 ? 4.372   -3.330  -34.207 1.00 64.15  ?  230 GLN B OE1   1 
ATOM   3973 N  NE2   . GLN B 1 237 ? 6.102   -4.623  -34.784 1.00 68.33  ?  230 GLN B NE2   1 
ATOM   3974 N  N     . THR B 1 238 ? 1.662   -0.742  -36.936 1.00 62.43  ?  231 THR B N     1 
ATOM   3975 C  CA    . THR B 1 238 ? 0.639   0.216   -37.320 1.00 61.43  ?  231 THR B CA    1 
ATOM   3976 C  C     . THR B 1 238 ? 0.619   1.354   -36.299 1.00 57.30  ?  231 THR B C     1 
ATOM   3977 O  O     . THR B 1 238 ? -0.090  2.338   -36.478 1.00 56.04  ?  231 THR B O     1 
ATOM   3978 C  CB    . THR B 1 238 ? -0.740  -0.454  -37.378 1.00 64.21  ?  231 THR B CB    1 
ATOM   3979 O  OG1   . THR B 1 238 ? -1.096  -0.775  -36.041 1.00 63.29  ?  231 THR B OG1   1 
ATOM   3980 C  CG2   . THR B 1 238 ? -0.787  -1.730  -38.200 1.00 68.77  ?  231 THR B CG2   1 
ATOM   3981 N  N     . CYS B 1 239 ? 1.387   1.190   -35.212 1.00 55.57  ?  232 CYS B N     1 
ATOM   3982 C  CA    . CYS B 1 239 ? 1.474   2.215   -34.179 1.00 51.94  ?  232 CYS B CA    1 
ATOM   3983 C  C     . CYS B 1 239 ? 2.646   3.160   -34.429 1.00 49.77  ?  232 CYS B C     1 
ATOM   3984 O  O     . CYS B 1 239 ? 2.782   4.182   -33.738 1.00 46.89  ?  232 CYS B O     1 
ATOM   3985 C  CB    . CYS B 1 239 ? 1.605   1.561   -32.812 1.00 51.57  ?  232 CYS B CB    1 
ATOM   3986 S  SG    . CYS B 1 239 ? 3.136   0.622   -32.612 1.00 52.65  ?  232 CYS B SG    1 
ATOM   3987 N  N     . LEU B 1 240 ? 3.437   2.893   -35.473 1.00 51.45  ?  233 LEU B N     1 
ATOM   3988 C  CA    . LEU B 1 240 ? 4.632   3.687   -35.710 1.00 50.01  ?  233 LEU B CA    1 
ATOM   3989 C  C     . LEU B 1 240 ? 4.261   5.068   -36.245 1.00 48.50  ?  233 LEU B C     1 
ATOM   3990 O  O     . LEU B 1 240 ? 3.562   5.182   -37.253 1.00 50.12  ?  233 LEU B O     1 
ATOM   3991 C  CB    . LEU B 1 240 ? 5.550   2.920   -36.679 1.00 52.87  ?  233 LEU B CB    1 
ATOM   3992 C  CG    . LEU B 1 240 ? 6.574   3.762   -37.434 1.00 52.61  ?  233 LEU B CG    1 
ATOM   3993 C  CD1   . LEU B 1 240 ? 7.683   4.177   -36.513 1.00 50.56  ?  233 LEU B CD1   1 
ATOM   3994 C  CD2   . LEU B 1 240 ? 7.142   2.998   -38.620 1.00 56.21  ?  233 LEU B CD2   1 
ATOM   3995 N  N     . VAL B 1 241 ? 4.797   6.114   -35.586 1.00 45.76  ?  234 VAL B N     1 
ATOM   3996 C  CA    . VAL B 1 241 ? 4.671   7.504   -35.988 1.00 44.44  ?  234 VAL B CA    1 
ATOM   3997 C  C     . VAL B 1 241 ? 6.068   8.057   -36.249 1.00 44.13  ?  234 VAL B C     1 
ATOM   3998 O  O     . VAL B 1 241 ? 6.771   8.393   -35.305 1.00 42.31  ?  234 VAL B O     1 
ATOM   3999 C  CB    . VAL B 1 241 ? 3.967   8.343   -34.897 1.00 41.83  ?  234 VAL B CB    1 
ATOM   4000 C  CG1   . VAL B 1 241 ? 3.862   9.803   -35.324 1.00 40.86  ?  234 VAL B CG1   1 
ATOM   4001 C  CG2   . VAL B 1 241 ? 2.608   7.767   -34.550 1.00 42.49  ?  234 VAL B CG2   1 
ATOM   4002 N  N     . PRO B 1 242 ? 6.539   8.149   -37.514 1.00 46.21  ?  235 PRO B N     1 
ATOM   4003 C  CA    . PRO B 1 242 ? 7.889   8.629   -37.788 1.00 46.48  ?  235 PRO B CA    1 
ATOM   4004 C  C     . PRO B 1 242 ? 7.976   10.146  -37.800 1.00 44.99  ?  235 PRO B C     1 
ATOM   4005 O  O     . PRO B 1 242 ? 7.128   10.819  -38.392 1.00 45.25  ?  235 PRO B O     1 
ATOM   4006 C  CB    . PRO B 1 242 ? 8.169   8.073   -39.205 1.00 49.90  ?  235 PRO B CB    1 
ATOM   4007 C  CG    . PRO B 1 242 ? 6.809   8.107   -39.864 1.00 50.77  ?  235 PRO B CG    1 
ATOM   4008 C  CD    . PRO B 1 242 ? 5.820   7.800   -38.751 1.00 48.82  ?  235 PRO B CD    1 
ATOM   4009 N  N     . GLU B 1 243 ? 9.057   10.659  -37.213 1.00 43.95  ?  236 GLU B N     1 
ATOM   4010 C  CA    . GLU B 1 243 ? 9.371   12.057  -37.220 1.00 43.09  ?  236 GLU B CA    1 
ATOM   4011 C  C     . GLU B 1 243 ? 10.794  12.254  -37.700 1.00 44.79  ?  236 GLU B C     1 
ATOM   4012 O  O     . GLU B 1 243 ? 11.735  12.391  -36.930 1.00 44.07  ?  236 GLU B O     1 
ATOM   4013 C  CB    . GLU B 1 243 ? 9.179   12.670  -35.837 1.00 40.22  ?  236 GLU B CB    1 
ATOM   4014 C  CG    . GLU B 1 243 ? 7.821   12.340  -35.299 1.00 38.96  ?  236 GLU B CG    1 
ATOM   4015 C  CD    . GLU B 1 243 ? 7.346   13.257  -34.201 1.00 36.60  ?  236 GLU B CD    1 
ATOM   4016 O  OE1   . GLU B 1 243 ? 8.000   14.289  -33.955 1.00 35.96  ?  236 GLU B OE1   1 
ATOM   4017 O  OE2   . GLU B 1 243 ? 6.302   12.920  -33.635 1.00 35.77  ?  236 GLU B OE2   1 
ATOM   4018 N  N     . PRO B 1 244 ? 10.970  12.359  -39.019 1.00 47.42  ?  237 PRO B N     1 
ATOM   4019 C  CA    . PRO B 1 244 ? 12.222  12.895  -39.542 1.00 49.32  ?  237 PRO B CA    1 
ATOM   4020 C  C     . PRO B 1 244 ? 12.455  14.333  -39.117 1.00 48.10  ?  237 PRO B C     1 
ATOM   4021 O  O     . PRO B 1 244 ? 11.511  15.050  -38.743 1.00 46.26  ?  237 PRO B O     1 
ATOM   4022 C  CB    . PRO B 1 244 ? 12.046  12.737  -41.061 1.00 52.52  ?  237 PRO B CB    1 
ATOM   4023 C  CG    . PRO B 1 244 ? 10.536  12.665  -41.270 1.00 51.73  ?  237 PRO B CG    1 
ATOM   4024 C  CD    . PRO B 1 244 ? 9.999   11.959  -40.052 1.00 49.09  ?  237 PRO B CD    1 
ATOM   4025 N  N     . ASN B 1 245 ? 13.710  14.784  -39.220 1.00 49.57  ?  238 ASN B N     1 
ATOM   4026 C  CA    . ASN B 1 245 ? 14.031  16.146  -38.821 1.00 48.95  ?  238 ASN B CA    1 
ATOM   4027 C  C     . ASN B 1 245 ? 13.025  17.160  -39.381 1.00 48.96  ?  238 ASN B C     1 
ATOM   4028 O  O     . ASN B 1 245 ? 12.602  18.069  -38.658 1.00 47.11  ?  238 ASN B O     1 
ATOM   4029 C  CB    . ASN B 1 245 ? 15.467  16.519  -39.184 1.00 51.62  ?  238 ASN B CB    1 
ATOM   4030 C  CG    . ASN B 1 245 ? 16.535  15.798  -38.387 1.00 51.58  ?  238 ASN B CG    1 
ATOM   4031 O  OD1   . ASN B 1 245 ? 17.708  15.972  -38.696 1.00 54.14  ?  238 ASN B OD1   1 
ATOM   4032 N  ND2   . ASN B 1 245 ? 16.181  14.974  -37.407 1.00 49.22  ?  238 ASN B ND2   1 
ATOM   4033 N  N     . ARG B 1 246 ? 12.662  17.043  -40.677 1.00 51.38  ?  239 ARG B N     1 
ATOM   4034 C  CA    . ARG B 1 246 ? 11.824  18.013  -41.363 1.00 52.23  ?  239 ARG B CA    1 
ATOM   4035 C  C     . ARG B 1 246 ? 10.497  18.221  -40.617 1.00 49.39  ?  239 ARG B C     1 
ATOM   4036 O  O     . ARG B 1 246 ? 10.015  19.348  -40.546 1.00 49.18  ?  239 ARG B O     1 
ATOM   4037 C  CB    . ARG B 1 246 ? 11.613  17.511  -42.802 1.00 55.40  ?  239 ARG B CB    1 
ATOM   4038 C  CG    . ARG B 1 246 ? 10.669  18.327  -43.670 1.00 56.91  ?  239 ARG B CG    1 
ATOM   4039 C  CD    . ARG B 1 246 ? 10.421  17.622  -44.998 1.00 60.04  ?  239 ARG B CD    1 
ATOM   4040 N  NE    . ARG B 1 246 ? 9.201   18.128  -45.617 1.00 60.93  ?  239 ARG B NE    1 
ATOM   4041 C  CZ    . ARG B 1 246 ? 8.005   17.552  -45.530 1.00 59.86  ?  239 ARG B CZ    1 
ATOM   4042 N  NH1   . ARG B 1 246 ? 7.844   16.416  -44.867 1.00 57.91  ?  239 ARG B NH1   1 
ATOM   4043 N  NH2   . ARG B 1 246 ? 6.970   18.121  -46.118 1.00 61.14  ?  239 ARG B NH2   1 
ATOM   4044 N  N     . LEU B 1 247 ? 9.942   17.138  -40.052 1.00 47.58  ?  240 LEU B N     1 
ATOM   4045 C  CA    . LEU B 1 247 ? 8.644   17.180  -39.397 1.00 45.38  ?  240 LEU B CA    1 
ATOM   4046 C  C     . LEU B 1 247 ? 8.781   17.530  -37.917 1.00 42.51  ?  240 LEU B C     1 
ATOM   4047 O  O     . LEU B 1 247 ? 7.901   18.165  -37.355 1.00 41.10  ?  240 LEU B O     1 
ATOM   4048 C  CB    . LEU B 1 247 ? 7.939   15.830  -39.560 1.00 45.44  ?  240 LEU B CB    1 
ATOM   4049 C  CG    . LEU B 1 247 ? 7.436   15.528  -40.968 1.00 48.31  ?  240 LEU B CG    1 
ATOM   4050 C  CD1   . LEU B 1 247 ? 6.593   14.271  -40.993 1.00 48.42  ?  240 LEU B CD1   1 
ATOM   4051 C  CD2   . LEU B 1 247 ? 6.676   16.721  -41.540 1.00 49.24  ?  240 LEU B CD2   1 
ATOM   4052 N  N     . MET B 1 248 ? 9.873   17.120  -37.277 1.00 41.94  ?  241 MET B N     1 
ATOM   4053 C  CA    . MET B 1 248 ? 10.029  17.356  -35.849 1.00 39.50  ?  241 MET B CA    1 
ATOM   4054 C  C     . MET B 1 248 ? 10.525  18.763  -35.536 1.00 39.52  ?  241 MET B C     1 
ATOM   4055 O  O     . MET B 1 248 ? 10.188  19.271  -34.469 1.00 37.66  ?  241 MET B O     1 
ATOM   4056 C  CB    . MET B 1 248 ? 10.982  16.311  -35.259 1.00 39.23  ?  241 MET B CB    1 
ATOM   4057 C  CG    . MET B 1 248 ? 11.005  16.328  -33.746 1.00 36.87  ?  241 MET B CG    1 
ATOM   4058 S  SD    . MET B 1 248 ? 12.006  14.992  -33.044 1.00 36.95  ?  241 MET B SD    1 
ATOM   4059 C  CE    . MET B 1 248 ? 11.333  15.037  -31.380 1.00 34.18  ?  241 MET B CE    1 
ATOM   4060 N  N     . ALA B 1 249 ? 11.328  19.410  -36.397 1.00 41.88  ?  242 ALA B N     1 
ATOM   4061 C  CA    . ALA B 1 249 ? 12.042  20.624  -36.010 1.00 42.37  ?  242 ALA B CA    1 
ATOM   4062 C  C     . ALA B 1 249 ? 11.110  21.685  -35.416 1.00 41.07  ?  242 ALA B C     1 
ATOM   4063 O  O     . ALA B 1 249 ? 11.418  22.236  -34.359 1.00 39.94  ?  242 ALA B O     1 
ATOM   4064 C  CB    . ALA B 1 249 ? 12.827  21.206  -37.165 1.00 45.65  ?  242 ALA B CB    1 
ATOM   4065 N  N     . LYS B 1 250 ? 10.016  21.994  -36.122 1.00 41.64  ?  243 LYS B N     1 
ATOM   4066 C  CA    . LYS B 1 250 ? 9.268   23.213  -35.855 1.00 41.58  ?  243 LYS B CA    1 
ATOM   4067 C  C     . LYS B 1 250 ? 7.773   22.958  -35.660 1.00 40.24  ?  243 LYS B C     1 
ATOM   4068 O  O     . LYS B 1 250 ? 7.004   23.921  -35.707 1.00 40.83  ?  243 LYS B O     1 
ATOM   4069 C  CB    . LYS B 1 250 ? 9.486   24.213  -36.997 1.00 44.71  ?  243 LYS B CB    1 
ATOM   4070 C  CG    . LYS B 1 250 ? 10.908  24.238  -37.538 1.00 46.89  ?  243 LYS B CG    1 
ATOM   4071 C  CD    . LYS B 1 250 ? 11.436  25.571  -38.014 1.00 49.79  ?  243 LYS B CD    1 
ATOM   4072 C  CE    . LYS B 1 250 ? 12.392  26.197  -37.019 1.00 49.55  ?  243 LYS B CE    1 
ATOM   4073 N  NZ    . LYS B 1 250 ? 13.524  26.877  -37.696 1.00 53.12  ?  243 LYS B NZ    1 
ATOM   4074 N  N     . SER B 1 251 ? 7.380   21.717  -35.363 1.00 38.71  ?  244 SER B N     1 
ATOM   4075 C  CA    . SER B 1 251 ? 5.996   21.252  -35.384 1.00 38.11  ?  244 SER B CA    1 
ATOM   4076 C  C     . SER B 1 251 ? 5.433   21.122  -33.973 1.00 35.74  ?  244 SER B C     1 
ATOM   4077 O  O     . SER B 1 251 ? 4.323   20.637  -33.803 1.00 35.26  ?  244 SER B O     1 
ATOM   4078 C  CB    . SER B 1 251 ? 5.873   19.950  -36.117 1.00 38.75  ?  244 SER B CB    1 
ATOM   4079 O  OG    . SER B 1 251 ? 6.467   18.872  -35.405 1.00 37.35  ?  244 SER B OG    1 
ATOM   4080 N  N     . TYR B 1 252 ? 6.202   21.566  -32.973 1.00 34.62  ?  245 TYR B N     1 
ATOM   4081 C  CA    . TYR B 1 252 ? 5.732   21.517  -31.589 1.00 32.69  ?  245 TYR B CA    1 
ATOM   4082 C  C     . TYR B 1 252 ? 5.588   22.904  -30.971 1.00 32.77  ?  245 TYR B C     1 
ATOM   4083 O  O     . TYR B 1 252 ? 6.235   23.876  -31.347 1.00 34.08  ?  245 TYR B O     1 
ATOM   4084 C  CB    . TYR B 1 252 ? 6.675   20.748  -30.664 1.00 31.36  ?  245 TYR B CB    1 
ATOM   4085 C  CG    . TYR B 1 252 ? 6.731   19.267  -30.952 1.00 31.23  ?  245 TYR B CG    1 
ATOM   4086 C  CD1   . TYR B 1 252 ? 7.365   18.776  -32.105 1.00 32.71  ?  245 TYR B CD1   1 
ATOM   4087 C  CD2   . TYR B 1 252 ? 6.150   18.348  -30.082 1.00 30.01  ?  245 TYR B CD2   1 
ATOM   4088 C  CE1   . TYR B 1 252 ? 7.404   17.422  -32.360 1.00 32.93  ?  245 TYR B CE1   1 
ATOM   4089 C  CE2   . TYR B 1 252 ? 6.194   16.990  -30.338 1.00 30.29  ?  245 TYR B CE2   1 
ATOM   4090 C  CZ    . TYR B 1 252 ? 6.806   16.532  -31.488 1.00 31.74  ?  245 TYR B CZ    1 
ATOM   4091 O  OH    . TYR B 1 252 ? 6.845   15.196  -31.633 1.00 32.22  ?  245 TYR B OH    1 
ATOM   4092 N  N     . LEU B 1 253 ? 4.638   22.993  -30.027 1.00 31.73  ?  246 LEU B N     1 
ATOM   4093 C  CA    . LEU B 1 253 ? 4.527   24.152  -29.168 1.00 31.74  ?  246 LEU B CA    1 
ATOM   4094 C  C     . LEU B 1 253 ? 5.163   23.789  -27.835 1.00 30.18  ?  246 LEU B C     1 
ATOM   4095 O  O     . LEU B 1 253 ? 4.672   22.884  -27.165 1.00 28.99  ?  246 LEU B O     1 
ATOM   4096 C  CB    . LEU B 1 253 ? 3.039   24.463  -28.979 1.00 32.05  ?  246 LEU B CB    1 
ATOM   4097 C  CG    . LEU B 1 253 ? 2.365   25.081  -30.191 1.00 34.07  ?  246 LEU B CG    1 
ATOM   4098 C  CD1   . LEU B 1 253 ? 0.853   25.178  -29.981 1.00 34.58  ?  246 LEU B CD1   1 
ATOM   4099 C  CD2   . LEU B 1 253 ? 2.995   26.421  -30.506 1.00 35.66  ?  246 LEU B CD2   1 
ATOM   4100 N  N     . ILE B 1 254 ? 6.229   24.494  -27.501 1.00 30.57  ?  247 ILE B N     1 
ATOM   4101 C  CA    . ILE B 1 254 ? 7.063   24.128  -26.367 1.00 29.53  ?  247 ILE B CA    1 
ATOM   4102 C  C     . ILE B 1 254 ? 7.133   25.297  -25.388 1.00 29.95  ?  247 ILE B C     1 
ATOM   4103 O  O     . ILE B 1 254 ? 7.666   26.355  -25.713 1.00 31.44  ?  247 ILE B O     1 
ATOM   4104 C  CB    . ILE B 1 254 ? 8.467   23.710  -26.842 1.00 30.03  ?  247 ILE B CB    1 
ATOM   4105 C  CG1   . ILE B 1 254 ? 8.380   22.562  -27.831 1.00 29.99  ?  247 ILE B CG1   1 
ATOM   4106 C  CG2   . ILE B 1 254 ? 9.388   23.391  -25.654 1.00 29.38  ?  247 ILE B CG2   1 
ATOM   4107 C  CD1   . ILE B 1 254 ? 9.654   22.256  -28.629 1.00 31.20  ?  247 ILE B CD1   1 
ATOM   4108 N  N     . LEU B 1 255 ? 6.660   25.055  -24.160 1.00 28.91  ?  248 LEU B N     1 
ATOM   4109 C  CA    . LEU B 1 255 ? 6.885   25.956  -23.034 1.00 29.35  ?  248 LEU B CA    1 
ATOM   4110 C  C     . LEU B 1 255 ? 8.058   25.493  -22.183 1.00 28.92  ?  248 LEU B C     1 
ATOM   4111 O  O     . LEU B 1 255 ? 8.140   24.313  -21.849 1.00 27.79  ?  248 LEU B O     1 
ATOM   4112 C  CB    . LEU B 1 255 ? 5.642   25.976  -22.158 1.00 28.93  ?  248 LEU B CB    1 
ATOM   4113 C  CG    . LEU B 1 255 ? 4.439   26.713  -22.726 1.00 29.94  ?  248 LEU B CG    1 
ATOM   4114 C  CD1   . LEU B 1 255 ? 3.288   26.539  -21.761 1.00 29.70  ?  248 LEU B CD1   1 
ATOM   4115 C  CD2   . LEU B 1 255 ? 4.748   28.191  -22.977 1.00 31.81  ?  248 LEU B CD2   1 
ATOM   4116 N  N     . ASP B 1 256 ? 8.883   26.446  -21.762 1.00 30.14  ?  249 ASP B N     1 
ATOM   4117 C  CA    . ASP B 1 256 ? 10.018  26.154  -20.909 1.00 30.24  ?  249 ASP B CA    1 
ATOM   4118 C  C     . ASP B 1 256 ? 9.586   26.273  -19.448 1.00 29.95  ?  249 ASP B C     1 
ATOM   4119 O  O     . ASP B 1 256 ? 8.388   26.339  -19.137 1.00 29.47  ?  249 ASP B O     1 
ATOM   4120 C  CB    . ASP B 1 256 ? 11.223  27.034  -21.290 1.00 32.16  ?  249 ASP B CB    1 
ATOM   4121 C  CG    . ASP B 1 256 ? 11.177  28.474  -20.776 1.00 33.89  ?  249 ASP B CG    1 
ATOM   4122 O  OD1   . ASP B 1 256 ? 10.148  28.859  -20.144 1.00 33.59  ?  249 ASP B OD1   1 
ATOM   4123 O  OD2   . ASP B 1 256 ? 12.179  29.217  -20.999 1.00 35.88  ?  249 ASP B OD2   1 
ATOM   4124 N  N     . GLU B 1 257 ? 10.583  26.251  -18.543 1.00 30.54  ?  250 GLU B N     1 
ATOM   4125 C  CA    . GLU B 1 257 ? 10.364  26.203  -17.113 1.00 30.54  ?  250 GLU B CA    1 
ATOM   4126 C  C     . GLU B 1 257 ? 9.837   27.522  -16.552 1.00 31.87  ?  250 GLU B C     1 
ATOM   4127 O  O     . GLU B 1 257 ? 9.393   27.547  -15.394 1.00 32.05  ?  250 GLU B O     1 
ATOM   4128 C  CB    . GLU B 1 257 ? 11.632  25.738  -16.366 1.00 31.14  ?  250 GLU B CB    1 
ATOM   4129 C  CG    . GLU B 1 257 ? 12.886  26.624  -16.423 1.00 33.14  ?  250 GLU B CG    1 
ATOM   4130 C  CD    . GLU B 1 257 ? 13.831  26.551  -17.627 1.00 33.80  ?  250 GLU B CD    1 
ATOM   4131 O  OE1   . GLU B 1 257 ? 13.419  26.076  -18.734 1.00 32.76  ?  250 GLU B OE1   1 
ATOM   4132 O  OE2   . GLU B 1 257 ? 15.018  26.892  -17.441 1.00 35.60  ?  250 GLU B OE2   1 
ATOM   4133 N  N     . TYR B 1 258 ? 9.932   28.589  -17.360 1.00 33.12  ?  251 TYR B N     1 
ATOM   4134 C  CA    . TYR B 1 258 ? 9.391   29.902  -17.044 1.00 34.79  ?  251 TYR B CA    1 
ATOM   4135 C  C     . TYR B 1 258 ? 8.086   30.178  -17.795 1.00 34.53  ?  251 TYR B C     1 
ATOM   4136 O  O     . TYR B 1 258 ? 7.563   31.297  -17.743 1.00 36.20  ?  251 TYR B O     1 
ATOM   4137 C  CB    . TYR B 1 258 ? 10.465  30.942  -17.412 1.00 37.05  ?  251 TYR B CB    1 
ATOM   4138 C  CG    . TYR B 1 258 ? 11.703  30.948  -16.523 1.00 38.15  ?  251 TYR B CG    1 
ATOM   4139 C  CD1   . TYR B 1 258 ? 11.692  31.544  -15.263 1.00 39.53  ?  251 TYR B CD1   1 
ATOM   4140 C  CD2   . TYR B 1 258 ? 12.879  30.305  -16.940 1.00 38.08  ?  251 TYR B CD2   1 
ATOM   4141 C  CE1   . TYR B 1 258 ? 12.825  31.529  -14.457 1.00 40.82  ?  251 TYR B CE1   1 
ATOM   4142 C  CE2   . TYR B 1 258 ? 13.999  30.277  -16.130 1.00 39.38  ?  251 TYR B CE2   1 
ATOM   4143 C  CZ    . TYR B 1 258 ? 13.971  30.893  -14.894 1.00 40.75  ?  251 TYR B CZ    1 
ATOM   4144 O  OH    . TYR B 1 258 ? 15.058  30.855  -14.073 1.00 42.31  ?  251 TYR B OH    1 
ATOM   4145 N  N     . MET B 1 259 ? 7.523   29.155  -18.465 1.00 32.75  ?  252 MET B N     1 
ATOM   4146 C  CA    . MET B 1 259 ? 6.330   29.225  -19.311 1.00 32.58  ?  252 MET B CA    1 
ATOM   4147 C  C     . MET B 1 259 ? 6.494   30.290  -20.412 1.00 34.31  ?  252 MET B C     1 
ATOM   4148 O  O     . MET B 1 259 ? 5.543   30.991  -20.783 1.00 35.41  ?  252 MET B O     1 
ATOM   4149 C  CB    . MET B 1 259 ? 5.060   29.466  -18.482 1.00 32.91  ?  252 MET B CB    1 
ATOM   4150 C  CG    . MET B 1 259 ? 4.931   28.517  -17.304 1.00 31.79  ?  252 MET B CG    1 
ATOM   4151 S  SD    . MET B 1 259 ? 3.323   28.456  -16.524 1.00 32.24  ?  252 MET B SD    1 
ATOM   4152 C  CE    . MET B 1 259 ? 2.496   27.192  -17.465 1.00 30.76  ?  252 MET B CE    1 
ATOM   4153 N  N     . ARG B 1 260 ? 7.683   30.287  -21.018 1.00 34.72  ?  253 ARG B N     1 
ATOM   4154 C  CA    . ARG B 1 260 ? 7.999   30.963  -22.270 1.00 36.32  ?  253 ARG B CA    1 
ATOM   4155 C  C     . ARG B 1 260 ? 7.993   29.950  -23.421 1.00 35.13  ?  253 ARG B C     1 
ATOM   4156 O  O     . ARG B 1 260 ? 8.472   28.826  -23.277 1.00 33.55  ?  253 ARG B O     1 
ATOM   4157 C  CB    . ARG B 1 260 ? 9.392   31.573  -22.163 1.00 38.04  ?  253 ARG B CB    1 
ATOM   4158 C  CG    . ARG B 1 260 ? 9.599   32.448  -20.947 1.00 39.42  ?  253 ARG B CG    1 
ATOM   4159 C  CD    . ARG B 1 260 ? 10.966  33.099  -20.917 1.00 41.65  ?  253 ARG B CD    1 
ATOM   4160 N  NE    . ARG B 1 260 ? 12.033  32.131  -20.726 1.00 40.63  ?  253 ARG B NE    1 
ATOM   4161 C  CZ    . ARG B 1 260 ? 13.327  32.393  -20.769 1.00 42.46  ?  253 ARG B CZ    1 
ATOM   4162 N  NH1   . ARG B 1 260 ? 13.748  33.637  -20.922 1.00 45.51  ?  253 ARG B NH1   1 
ATOM   4163 N  NH2   . ARG B 1 260 ? 14.199  31.417  -20.580 1.00 41.59  ?  253 ARG B NH2   1 
ATOM   4164 N  N     . PHE B 1 261 ? 7.463   30.348  -24.583 1.00 36.21  ?  254 PHE B N     1 
ATOM   4165 C  CA    . PHE B 1 261 ? 7.517   29.503  -25.767 1.00 35.65  ?  254 PHE B CA    1 
ATOM   4166 C  C     . PHE B 1 261 ? 8.940   29.526  -26.349 1.00 36.78  ?  254 PHE B C     1 
ATOM   4167 O  O     . PHE B 1 261 ? 9.551   30.578  -26.464 1.00 38.97  ?  254 PHE B O     1 
ATOM   4168 C  CB    . PHE B 1 261 ? 6.515   29.999  -26.821 1.00 36.96  ?  254 PHE B CB    1 
ATOM   4169 C  CG    . PHE B 1 261 ? 5.076   29.626  -26.575 1.00 35.98  ?  254 PHE B CG    1 
ATOM   4170 C  CD1   . PHE B 1 261 ? 4.666   28.293  -26.591 1.00 34.03  ?  254 PHE B CD1   1 
ATOM   4171 C  CD2   . PHE B 1 261 ? 4.151   30.587  -26.199 1.00 37.26  ?  254 PHE B CD2   1 
ATOM   4172 C  CE1   . PHE B 1 261 ? 3.345   27.956  -26.335 1.00 33.55  ?  254 PHE B CE1   1 
ATOM   4173 C  CE2   . PHE B 1 261 ? 2.835   30.245  -25.953 1.00 36.75  ?  254 PHE B CE2   1 
ATOM   4174 C  CZ    . PHE B 1 261 ? 2.430   28.936  -26.014 1.00 34.92  ?  254 PHE B CZ    1 
ATOM   4175 N  N     . LEU B 1 262 ? 9.460   28.357  -26.741 1.00 35.64  ?  255 LEU B N     1 
ATOM   4176 C  CA    . LEU B 1 262 ? 10.811  28.257  -27.289 1.00 36.93  ?  255 LEU B CA    1 
ATOM   4177 C  C     . LEU B 1 262 ? 10.739  28.087  -28.805 1.00 38.13  ?  255 LEU B C     1 
ATOM   4178 O  O     . LEU B 1 262 ? 9.914   27.348  -29.314 1.00 37.05  ?  255 LEU B O     1 
ATOM   4179 C  CB    . LEU B 1 262 ? 11.550  27.056  -26.682 1.00 35.40  ?  255 LEU B CB    1 
ATOM   4180 C  CG    . LEU B 1 262 ? 11.730  27.032  -25.160 1.00 34.38  ?  255 LEU B CG    1 
ATOM   4181 C  CD1   . LEU B 1 262 ? 12.383  25.716  -24.723 1.00 33.16  ?  255 LEU B CD1   1 
ATOM   4182 C  CD2   . LEU B 1 262 ? 12.485  28.233  -24.670 1.00 36.37  ?  255 LEU B CD2   1 
ATOM   4183 N  N     . ASP B 1 263 ? 11.679  28.715  -29.516 1.00 40.66  ?  256 ASP B N     1 
ATOM   4184 C  CA    . ASP B 1 263 ? 11.660  28.666  -30.968 1.00 42.37  ?  256 ASP B CA    1 
ATOM   4185 C  C     . ASP B 1 263 ? 12.407  27.428  -31.468 1.00 41.99  ?  256 ASP B C     1 
ATOM   4186 O  O     . ASP B 1 263 ? 12.176  26.997  -32.587 1.00 42.76  ?  256 ASP B O     1 
ATOM   4187 C  CB    . ASP B 1 263 ? 12.192  29.974  -31.563 1.00 45.83  ?  256 ASP B CB    1 
ATOM   4188 C  CG    . ASP B 1 263 ? 11.527  30.415  -32.866 1.00 47.84  ?  256 ASP B CG    1 
ATOM   4189 O  OD1   . ASP B 1 263 ? 10.543  29.759  -33.309 1.00 46.50  ?  256 ASP B OD1   1 
ATOM   4190 O  OD2   . ASP B 1 263 ? 11.981  31.440  -33.425 1.00 51.08  ?  256 ASP B OD2   1 
ATOM   4191 N  N     . ARG B 1 264 ? 13.304  26.869  -30.650 1.00 41.14  ?  257 ARG B N     1 
ATOM   4192 C  CA    . ARG B 1 264 ? 14.090  25.679  -30.979 1.00 41.05  ?  257 ARG B CA    1 
ATOM   4193 C  C     . ARG B 1 264 ? 15.043  25.930  -32.156 1.00 44.23  ?  257 ARG B C     1 
ATOM   4194 O  O     . ARG B 1 264 ? 15.327  25.015  -32.904 1.00 44.69  ?  257 ARG B O     1 
ATOM   4195 C  CB    . ARG B 1 264 ? 13.187  24.467  -31.260 1.00 39.06  ?  257 ARG B CB    1 
ATOM   4196 C  CG    . ARG B 1 264 ? 12.206  24.144  -30.132 1.00 36.30  ?  257 ARG B CG    1 
ATOM   4197 C  CD    . ARG B 1 264 ? 12.805  23.987  -28.738 1.00 35.21  ?  257 ARG B CD    1 
ATOM   4198 N  NE    . ARG B 1 264 ? 13.399  22.666  -28.539 1.00 34.59  ?  257 ARG B NE    1 
ATOM   4199 C  CZ    . ARG B 1 264 ? 14.285  22.363  -27.586 1.00 34.49  ?  257 ARG B CZ    1 
ATOM   4200 N  NH1   . ARG B 1 264 ? 14.919  23.318  -26.932 1.00 35.41  ?  257 ARG B NH1   1 
ATOM   4201 N  NH2   . ARG B 1 264 ? 14.575  21.093  -27.321 1.00 33.85  ?  257 ARG B NH2   1 
ATOM   4202 N  N     . ASN B 1 265 ? 15.559  27.153  -32.313 1.00 46.78  ?  258 ASN B N     1 
ATOM   4203 C  CA    . ASN B 1 265 ? 16.434  27.447  -33.445 1.00 50.29  ?  258 ASN B CA    1 
ATOM   4204 C  C     . ASN B 1 265 ? 17.409  28.585  -33.130 1.00 53.13  ?  258 ASN B C     1 
ATOM   4205 O  O     . ASN B 1 265 ? 17.817  29.319  -34.035 1.00 56.57  ?  258 ASN B O     1 
ATOM   4206 C  CB    . ASN B 1 265 ? 15.621  27.763  -34.705 1.00 51.61  ?  258 ASN B CB    1 
ATOM   4207 C  CG    . ASN B 1 265 ? 14.863  29.072  -34.618 1.00 52.39  ?  258 ASN B CG    1 
ATOM   4208 O  OD1   . ASN B 1 265 ? 15.194  29.952  -33.824 1.00 53.01  ?  258 ASN B OD1   1 
ATOM   4209 N  ND2   . ASN B 1 265 ? 13.843  29.213  -35.447 1.00 52.73  ?  258 ASN B ND2   1 
ATOM   4210 N  N     . GLY B 1 266 ? 17.791  28.728  -31.852 1.00 52.07  ?  259 GLY B N     1 
ATOM   4211 C  CA    . GLY B 1 266 ? 18.787  29.709  -31.442 1.00 54.94  ?  259 GLY B CA    1 
ATOM   4212 C  C     . GLY B 1 266 ? 18.212  31.098  -31.155 1.00 55.98  ?  259 GLY B C     1 
ATOM   4213 O  O     . GLY B 1 266 ? 18.854  31.892  -30.466 1.00 57.80  ?  259 GLY B O     1 
ATOM   4214 N  N     . GLN B 1 267 ? 17.023  31.402  -31.695 1.00 55.25  ?  260 GLN B N     1 
ATOM   4215 C  CA    . GLN B 1 267 ? 16.347  32.664  -31.419 1.00 56.28  ?  260 GLN B CA    1 
ATOM   4216 C  C     . GLN B 1 267 ? 15.952  32.722  -29.942 1.00 53.76  ?  260 GLN B C     1 
ATOM   4217 O  O     . GLN B 1 267 ? 16.022  31.725  -29.225 1.00 50.95  ?  260 GLN B O     1 
ATOM   4218 C  CB    . GLN B 1 267 ? 15.102  32.800  -32.300 1.00 55.97  ?  260 GLN B CB    1 
ATOM   4219 C  CG    . GLN B 1 267 ? 15.391  32.777  -33.795 1.00 58.77  ?  260 GLN B CG    1 
ATOM   4220 C  CD    . GLN B 1 267 ? 15.561  34.149  -34.401 1.00 63.15  ?  260 GLN B CD    1 
ATOM   4221 O  OE1   . GLN B 1 267 ? 16.466  34.903  -34.047 1.00 65.79  ?  260 GLN B OE1   1 
ATOM   4222 N  NE2   . GLN B 1 267 ? 14.695  34.479  -35.347 1.00 64.35  ?  260 GLN B NE2   1 
ATOM   4223 N  N     . GLN B 1 268 ? 15.499  33.894  -29.499 1.00 55.05  ?  261 GLN B N     1 
ATOM   4224 C  CA    . GLN B 1 268 ? 15.210  34.115  -28.091 1.00 53.48  ?  261 GLN B CA    1 
ATOM   4225 C  C     . GLN B 1 268 ? 13.850  33.515  -27.730 1.00 49.93  ?  261 GLN B C     1 
ATOM   4226 O  O     . GLN B 1 268 ? 12.952  33.445  -28.561 1.00 49.60  ?  261 GLN B O     1 
ATOM   4227 C  CB    . GLN B 1 268 ? 15.275  35.608  -27.757 1.00 56.73  ?  261 GLN B CB    1 
ATOM   4228 C  CG    . GLN B 1 268 ? 16.702  36.111  -27.574 1.00 60.02  ?  261 GLN B CG    1 
ATOM   4229 C  CD    . GLN B 1 268 ? 17.297  35.681  -26.253 1.00 58.62  ?  261 GLN B CD    1 
ATOM   4230 O  OE1   . GLN B 1 268 ? 16.860  36.114  -25.188 1.00 58.02  ?  261 GLN B OE1   1 
ATOM   4231 N  NE2   . GLN B 1 268 ? 18.318  34.838  -26.303 1.00 58.44  ?  261 GLN B NE2   1 
ATOM   4232 N  N     . PRO B 1 269 ? 13.643  33.049  -26.480 1.00 47.47  ?  262 PRO B N     1 
ATOM   4233 C  CA    . PRO B 1 269 ? 12.310  32.601  -26.064 1.00 44.71  ?  262 PRO B CA    1 
ATOM   4234 C  C     . PRO B 1 269 ? 11.325  33.770  -26.032 1.00 46.18  ?  262 PRO B C     1 
ATOM   4235 O  O     . PRO B 1 269 ? 11.739  34.917  -25.919 1.00 49.03  ?  262 PRO B O     1 
ATOM   4236 C  CB    . PRO B 1 269 ? 12.535  32.021  -24.659 1.00 42.74  ?  262 PRO B CB    1 
ATOM   4237 C  CG    . PRO B 1 269 ? 14.036  31.820  -24.552 1.00 43.98  ?  262 PRO B CG    1 
ATOM   4238 C  CD    . PRO B 1 269 ? 14.640  32.903  -25.416 1.00 47.54  ?  262 PRO B CD    1 
ATOM   4239 N  N     . SER B 1 270 ? 10.021  33.485  -26.144 1.00 44.60  ?  263 SER B N     1 
ATOM   4240 C  CA    . SER B 1 270 ? 9.023   34.512  -25.920 1.00 45.98  ?  263 SER B CA    1 
ATOM   4241 C  C     . SER B 1 270 ? 9.188   35.061  -24.498 1.00 46.29  ?  263 SER B C     1 
ATOM   4242 O  O     . SER B 1 270 ? 9.899   34.490  -23.663 1.00 44.96  ?  263 SER B O     1 
ATOM   4243 C  CB    . SER B 1 270 ? 7.626   34.003  -26.186 1.00 44.37  ?  263 SER B CB    1 
ATOM   4244 O  OG    . SER B 1 270 ? 7.175   33.159  -25.123 1.00 41.64  ?  263 SER B OG    1 
ATOM   4245 N  N     . LYS B 1 271 ? 8.505   36.166  -24.195 1.00 48.32  ?  264 LYS B N     1 
ATOM   4246 C  CA    . LYS B 1 271 ? 8.252   36.477  -22.807 1.00 48.19  ?  264 LYS B CA    1 
ATOM   4247 C  C     . LYS B 1 271 ? 7.264   35.435  -22.303 1.00 45.07  ?  264 LYS B C     1 
ATOM   4248 O  O     . LYS B 1 271 ? 6.535   34.836  -23.087 1.00 43.85  ?  264 LYS B O     1 
ATOM   4249 C  CB    . LYS B 1 271 ? 7.700   37.891  -22.638 1.00 51.47  ?  264 LYS B CB    1 
ATOM   4250 C  CG    . LYS B 1 271 ? 8.551   38.946  -23.322 1.00 55.11  ?  264 LYS B CG    1 
ATOM   4251 C  CD    . LYS B 1 271 ? 8.575   40.302  -22.652 1.00 58.68  ?  264 LYS B CD    1 
ATOM   4252 C  CE    . LYS B 1 271 ? 9.249   41.359  -23.506 1.00 62.80  ?  264 LYS B CE    1 
ATOM   4253 N  NZ    . LYS B 1 271 ? 10.458  40.851  -24.200 1.00 62.59  ?  264 LYS B NZ    1 
ATOM   4254 N  N     . SER B 1 272 ? 7.205   35.296  -20.983 1.00 44.30  ?  265 SER B N     1 
ATOM   4255 C  CA    . SER B 1 272 ? 6.356   34.322  -20.340 1.00 41.80  ?  265 SER B CA    1 
ATOM   4256 C  C     . SER B 1 272 ? 4.889   34.614  -20.656 1.00 42.35  ?  265 SER B C     1 
ATOM   4257 O  O     . SER B 1 272 ? 4.467   35.771  -20.646 1.00 44.94  ?  265 SER B O     1 
ATOM   4258 C  CB    . SER B 1 272 ? 6.595   34.282  -18.855 1.00 41.62  ?  265 SER B CB    1 
ATOM   4259 O  OG    . SER B 1 272 ? 5.754   33.312  -18.222 1.00 39.53  ?  265 SER B OG    1 
ATOM   4260 N  N     . ILE B 1 273 ? 4.125   33.555  -20.895 1.00 40.22  ?  266 ILE B N     1 
ATOM   4261 C  CA    . ILE B 1 273 ? 2.684   33.687  -21.002 1.00 40.81  ?  266 ILE B CA    1 
ATOM   4262 C  C     . ILE B 1 273 ? 2.121   34.350  -19.741 1.00 42.20  ?  266 ILE B C     1 
ATOM   4263 O  O     . ILE B 1 273 ? 1.073   34.989  -19.838 1.00 44.04  ?  266 ILE B O     1 
ATOM   4264 C  CB    . ILE B 1 273 ? 1.943   32.371  -21.318 1.00 38.59  ?  266 ILE B CB    1 
ATOM   4265 C  CG1   . ILE B 1 273 ? 2.019   31.334  -20.199 1.00 36.56  ?  266 ILE B CG1   1 
ATOM   4266 C  CG2   . ILE B 1 273 ? 2.424   31.798  -22.644 1.00 37.76  ?  266 ILE B CG2   1 
ATOM   4267 C  CD1   . ILE B 1 273 ? 1.254   30.087  -20.494 1.00 34.94  ?  266 ILE B CD1   1 
ATOM   4268 N  N     . LEU B 1 274 ? 2.788   34.163  -18.599 1.00 41.57  ?  267 LEU B N     1 
ATOM   4269 C  CA    . LEU B 1 274 ? 2.351   34.693  -17.321 1.00 42.98  ?  267 LEU B CA    1 
ATOM   4270 C  C     . LEU B 1 274 ? 2.446   36.226  -17.306 1.00 46.36  ?  267 LEU B C     1 
ATOM   4271 O  O     . LEU B 1 274 ? 1.646   36.869  -16.615 1.00 48.34  ?  267 LEU B O     1 
ATOM   4272 C  CB    . LEU B 1 274 ? 3.160   34.073  -16.175 1.00 41.71  ?  267 LEU B CB    1 
ATOM   4273 C  CG    . LEU B 1 274 ? 3.025   32.560  -15.976 1.00 38.90  ?  267 LEU B CG    1 
ATOM   4274 C  CD1   . LEU B 1 274 ? 4.064   32.051  -14.980 1.00 38.13  ?  267 LEU B CD1   1 
ATOM   4275 C  CD2   . LEU B 1 274 ? 1.616   32.145  -15.561 1.00 38.91  ?  267 LEU B CD2   1 
ATOM   4276 N  N     . GLU B 1 275 ? 3.343   36.774  -18.124 1.00 47.30  ?  268 GLU B N     1 
ATOM   4277 C  CA    . GLU B 1 275 ? 3.642   38.199  -18.179 1.00 50.82  ?  268 GLU B CA    1 
ATOM   4278 C  C     . GLU B 1 275 ? 2.898   38.900  -19.323 1.00 52.85  ?  268 GLU B C     1 
ATOM   4279 O  O     . GLU B 1 275 ? 2.549   40.075  -19.199 1.00 56.20  ?  268 GLU B O     1 
ATOM   4280 C  CB    . GLU B 1 275 ? 5.153   38.366  -18.329 1.00 51.16  ?  268 GLU B CB    1 
ATOM   4281 C  CG    . GLU B 1 275 ? 5.652   39.799  -18.415 1.00 55.13  ?  268 GLU B CG    1 
ATOM   4282 C  CD    . GLU B 1 275 ? 7.169   39.888  -18.352 1.00 55.72  ?  268 GLU B CD    1 
ATOM   4283 O  OE1   . GLU B 1 275 ? 7.833   39.580  -19.366 1.00 55.17  ?  268 GLU B OE1   1 
ATOM   4284 O  OE2   . GLU B 1 275 ? 7.686   40.216  -17.267 1.00 56.89  ?  268 GLU B OE2   1 
ATOM   4285 N  N     . VAL B 1 276 ? 2.697   38.225  -20.461 1.00 51.25  ?  269 VAL B N     1 
ATOM   4286 C  CA    . VAL B 1 276 ? 2.155   38.905  -21.634 1.00 53.52  ?  269 VAL B CA    1 
ATOM   4287 C  C     . VAL B 1 276 ? 0.922   38.185  -22.192 1.00 52.28  ?  269 VAL B C     1 
ATOM   4288 O  O     . VAL B 1 276 ? 0.250   38.682  -23.097 1.00 54.32  ?  269 VAL B O     1 
ATOM   4289 C  CB    . VAL B 1 276 ? 3.234   39.113  -22.714 1.00 54.24  ?  269 VAL B CB    1 
ATOM   4290 C  CG1   . VAL B 1 276 ? 4.437   39.893  -22.193 1.00 56.13  ?  269 VAL B CG1   1 
ATOM   4291 C  CG2   . VAL B 1 276 ? 3.687   37.790  -23.332 1.00 50.92  ?  269 VAL B CG2   1 
ATOM   4292 N  N     . GLY B 1 277 ? 0.606   36.995  -21.673 1.00 49.26  ?  270 GLY B N     1 
ATOM   4293 C  CA    . GLY B 1 277 ? -0.503  36.233  -22.194 1.00 48.27  ?  270 GLY B CA    1 
ATOM   4294 C  C     . GLY B 1 277 ? -0.091  35.320  -23.345 1.00 46.34  ?  270 GLY B C     1 
ATOM   4295 O  O     . GLY B 1 277 ? 0.979   35.480  -23.933 1.00 46.39  ?  270 GLY B O     1 
ATOM   4296 N  N     . VAL B 1 278 ? -1.015  34.428  -23.688 1.00 45.20  ?  271 VAL B N     1 
ATOM   4297 C  CA    . VAL B 1 278 ? -0.747  33.399  -24.677 1.00 43.40  ?  271 VAL B CA    1 
ATOM   4298 C  C     . VAL B 1 278 ? -0.591  33.999  -26.073 1.00 45.40  ?  271 VAL B C     1 
ATOM   4299 O  O     . VAL B 1 278 ? 0.394   33.714  -26.757 1.00 44.72  ?  271 VAL B O     1 
ATOM   4300 C  CB    . VAL B 1 278 ? -1.834  32.322  -24.601 1.00 42.16  ?  271 VAL B CB    1 
ATOM   4301 C  CG1   . VAL B 1 278 ? -1.805  31.386  -25.816 1.00 41.19  ?  271 VAL B CG1   1 
ATOM   4302 C  CG2   . VAL B 1 278 ? -1.695  31.534  -23.299 1.00 40.05  ?  271 VAL B CG2   1 
ATOM   4303 N  N     . GLN B 1 279 ? -1.523  34.877  -26.481 1.00 48.28  ?  272 GLN B N     1 
ATOM   4304 C  CA    . GLN B 1 279 ? -1.493  35.437  -27.834 1.00 50.64  ?  272 GLN B CA    1 
ATOM   4305 C  C     . GLN B 1 279 ? -0.166  36.148  -28.141 1.00 51.69  ?  272 GLN B C     1 
ATOM   4306 O  O     . GLN B 1 279 ? 0.422   35.909  -29.192 1.00 51.88  ?  272 GLN B O     1 
ATOM   4307 C  CB    . GLN B 1 279 ? -2.695  36.362  -28.064 1.00 54.05  ?  272 GLN B CB    1 
ATOM   4308 C  CG    . GLN B 1 279 ? -2.661  37.055  -29.425 1.00 57.10  ?  272 GLN B CG    1 
ATOM   4309 C  CD    . GLN B 1 279 ? -3.709  38.136  -29.575 1.00 61.06  ?  272 GLN B CD    1 
ATOM   4310 O  OE1   . GLN B 1 279 ? -4.431  38.464  -28.638 1.00 61.73  ?  272 GLN B OE1   1 
ATOM   4311 N  NE2   . GLN B 1 279 ? -3.797  38.702  -30.769 1.00 64.07  ?  272 GLN B NE2   1 
ATOM   4312 N  N     . GLN B 1 280 ? 0.322   37.027  -27.250 1.00 52.75  ?  273 GLN B N     1 
ATOM   4313 C  CA    . GLN B 1 280 ? 1.510   37.833  -27.508 1.00 54.53  ?  273 GLN B CA    1 
ATOM   4314 C  C     . GLN B 1 280 ? 2.740   36.923  -27.512 1.00 51.85  ?  273 GLN B C     1 
ATOM   4315 O  O     . GLN B 1 280 ? 3.654   37.070  -28.348 1.00 52.92  ?  273 GLN B O     1 
ATOM   4316 C  CB    . GLN B 1 280 ? 1.559   38.960  -26.465 1.00 56.64  ?  273 GLN B CB    1 
ATOM   4317 C  CG    . GLN B 1 280 ? 2.785   39.858  -26.548 1.00 58.94  ?  273 GLN B CG    1 
ATOM   4318 C  CD    . GLN B 1 280 ? 2.820   40.729  -27.780 1.00 62.67  ?  273 GLN B CD    1 
ATOM   4319 O  OE1   . GLN B 1 280 ? 1.783   41.177  -28.279 1.00 64.78  ?  273 GLN B OE1   1 
ATOM   4320 N  NE2   . GLN B 1 280 ? 4.023   40.968  -28.286 1.00 63.84  ?  273 GLN B NE2   1 
ATOM   4321 N  N     . ALA B 1 281 ? 2.746   35.937  -26.596 1.00 48.62  ?  274 ALA B N     1 
ATOM   4322 C  CA    . ALA B 1 281 ? 3.904   35.068  -26.462 1.00 46.32  ?  274 ALA B CA    1 
ATOM   4323 C  C     . ALA B 1 281 ? 4.055   34.226  -27.733 1.00 45.57  ?  274 ALA B C     1 
ATOM   4324 O  O     . ALA B 1 281 ? 5.161   34.075  -28.246 1.00 45.77  ?  274 ALA B O     1 
ATOM   4325 C  CB    . ALA B 1 281 ? 3.772   34.201  -25.229 1.00 43.50  ?  274 ALA B CB    1 
ATOM   4326 N  N     . LEU B 1 282 ? 2.928   33.704  -28.229 1.00 45.07  ?  275 LEU B N     1 
ATOM   4327 C  CA    . LEU B 1 282 ? 2.907   32.767  -29.347 1.00 44.32  ?  275 LEU B CA    1 
ATOM   4328 C  C     . LEU B 1 282 ? 3.324   33.461  -30.640 1.00 47.18  ?  275 LEU B C     1 
ATOM   4329 O  O     . LEU B 1 282 ? 3.790   32.816  -31.579 1.00 47.02  ?  275 LEU B O     1 
ATOM   4330 C  CB    . LEU B 1 282 ? 1.506   32.158  -29.477 1.00 43.69  ?  275 LEU B CB    1 
ATOM   4331 C  CG    . LEU B 1 282 ? 1.408   30.823  -30.215 1.00 42.14  ?  275 LEU B CG    1 
ATOM   4332 C  CD1   . LEU B 1 282 ? 2.157   29.731  -29.484 1.00 39.26  ?  275 LEU B CD1   1 
ATOM   4333 C  CD2   . LEU B 1 282 ? -0.037  30.396  -30.396 1.00 42.36  ?  275 LEU B CD2   1 
ATOM   4334 N  N     . GLN B 1 283 ? 3.189   34.791  -30.689 1.00 50.16  ?  276 GLN B N     1 
ATOM   4335 C  CA    . GLN B 1 283 ? 3.426   35.463  -31.950 1.00 53.38  ?  276 GLN B CA    1 
ATOM   4336 C  C     . GLN B 1 283 ? 4.933   35.656  -32.098 1.00 54.09  ?  276 GLN B C     1 
ATOM   4337 O  O     . GLN B 1 283 ? 5.416   35.982  -33.182 1.00 56.59  ?  276 GLN B O     1 
ATOM   4338 C  CB    . GLN B 1 283 ? 2.521   36.696  -32.049 1.00 56.66  ?  276 GLN B CB    1 
ATOM   4339 C  CG    . GLN B 1 283 ? 3.220   38.026  -31.852 1.00 59.78  ?  276 GLN B CG    1 
ATOM   4340 C  CD    . GLN B 1 283 ? 2.266   39.167  -32.111 1.00 63.47  ?  276 GLN B CD    1 
ATOM   4341 O  OE1   . GLN B 1 283 ? 1.631   39.251  -33.164 1.00 65.44  ?  276 GLN B OE1   1 
ATOM   4342 N  NE2   . GLN B 1 283 ? 2.154   40.054  -31.136 1.00 64.72  ?  276 GLN B NE2   1 
ATOM   4343 N  N     . ALA B 1 284 ? 5.680   35.351  -31.026 1.00 52.00  ?  277 ALA B N     1 
ATOM   4344 C  CA    . ALA B 1 284 ? 7.124   35.481  -30.985 1.00 52.70  ?  277 ALA B CA    1 
ATOM   4345 C  C     . ALA B 1 284 ? 7.847   34.220  -31.453 1.00 50.74  ?  277 ALA B C     1 
ATOM   4346 O  O     . ALA B 1 284 ? 9.076   34.188  -31.508 1.00 51.45  ?  277 ALA B O     1 
ATOM   4347 C  CB    . ALA B 1 284 ? 7.524   35.830  -29.582 1.00 51.94  ?  277 ALA B CB    1 
ATOM   4348 N  N     . VAL B 1 285 ? 7.101   33.163  -31.790 1.00 48.58  ?  278 VAL B N     1 
ATOM   4349 C  CA    . VAL B 1 285 ? 7.731   31.931  -32.218 1.00 46.97  ?  278 VAL B CA    1 
ATOM   4350 C  C     . VAL B 1 285 ? 7.054   31.464  -33.492 1.00 47.71  ?  278 VAL B C     1 
ATOM   4351 O  O     . VAL B 1 285 ? 5.923   31.849  -33.785 1.00 48.55  ?  278 VAL B O     1 
ATOM   4352 C  CB    . VAL B 1 285 ? 7.666   30.844  -31.128 1.00 43.41  ?  278 VAL B CB    1 
ATOM   4353 C  CG1   . VAL B 1 285 ? 8.461   31.242  -29.907 1.00 42.99  ?  278 VAL B CG1   1 
ATOM   4354 C  CG2   . VAL B 1 285 ? 6.239   30.517  -30.743 1.00 41.86  ?  278 VAL B CG2   1 
ATOM   4355 N  N     . PHE B 1 286 ? 7.768   30.622  -34.234 1.00 47.66  ?  279 PHE B N     1 
ATOM   4356 C  CA    . PHE B 1 286 ? 7.170   29.931  -35.358 1.00 48.11  ?  279 PHE B CA    1 
ATOM   4357 C  C     . PHE B 1 286 ? 6.665   28.568  -34.905 1.00 44.95  ?  279 PHE B C     1 
ATOM   4358 O  O     . PHE B 1 286 ? 7.383   27.832  -34.228 1.00 43.02  ?  279 PHE B O     1 
ATOM   4359 C  CB    . PHE B 1 286 ? 8.193   29.753  -36.489 1.00 50.36  ?  279 PHE B CB    1 
ATOM   4360 C  CG    . PHE B 1 286 ? 7.659   29.047  -37.709 1.00 51.28  ?  279 PHE B CG    1 
ATOM   4361 C  CD1   . PHE B 1 286 ? 6.494   29.481  -38.316 1.00 52.75  ?  279 PHE B CD1   1 
ATOM   4362 C  CD2   . PHE B 1 286 ? 8.329   27.969  -38.261 1.00 51.09  ?  279 PHE B CD2   1 
ATOM   4363 C  CE1   . PHE B 1 286 ? 6.001   28.839  -39.446 1.00 53.94  ?  279 PHE B CE1   1 
ATOM   4364 C  CE2   . PHE B 1 286 ? 7.845   27.337  -39.395 1.00 52.32  ?  279 PHE B CE2   1 
ATOM   4365 C  CZ    . PHE B 1 286 ? 6.682   27.770  -39.986 1.00 53.73  ?  279 PHE B CZ    1 
ATOM   4366 N  N     . TRP B 1 287 ? 5.446   28.245  -35.323 1.00 44.88  ?  280 TRP B N     1 
ATOM   4367 C  CA    . TRP B 1 287 ? 4.879   26.920  -35.198 1.00 42.79  ?  280 TRP B CA    1 
ATOM   4368 C  C     . TRP B 1 287 ? 4.372   26.484  -36.555 1.00 44.61  ?  280 TRP B C     1 
ATOM   4369 O  O     . TRP B 1 287 ? 3.471   27.124  -37.080 1.00 46.42  ?  280 TRP B O     1 
ATOM   4370 C  CB    . TRP B 1 287 ? 3.734   26.906  -34.174 1.00 41.12  ?  280 TRP B CB    1 
ATOM   4371 C  CG    . TRP B 1 287 ? 3.098   25.554  -33.973 1.00 39.33  ?  280 TRP B CG    1 
ATOM   4372 C  CD1   . TRP B 1 287 ? 3.699   24.325  -33.871 1.00 37.87  ?  280 TRP B CD1   1 
ATOM   4373 C  CD2   . TRP B 1 287 ? 1.685   25.301  -33.822 1.00 39.24  ?  280 TRP B CD2   1 
ATOM   4374 N  NE1   . TRP B 1 287 ? 2.762   23.342  -33.670 1.00 36.92  ?  280 TRP B NE1   1 
ATOM   4375 C  CE2   . TRP B 1 287 ? 1.515   23.911  -33.650 1.00 37.77  ?  280 TRP B CE2   1 
ATOM   4376 C  CE3   . TRP B 1 287 ? 0.554   26.125  -33.821 1.00 40.63  ?  280 TRP B CE3   1 
ATOM   4377 C  CZ2   . TRP B 1 287 ? 0.264   23.327  -33.479 1.00 37.69  ?  280 TRP B CZ2   1 
ATOM   4378 C  CZ3   . TRP B 1 287 ? -0.679  25.546  -33.616 1.00 40.46  ?  280 TRP B CZ3   1 
ATOM   4379 C  CH2   . TRP B 1 287 ? -0.828  24.165  -33.497 1.00 39.10  ?  280 TRP B CH2   1 
ATOM   4380 N  N     . ASP B 1 288 ? 4.937   25.393  -37.086 1.00 44.35  ?  281 ASP B N     1 
ATOM   4381 C  CA    . ASP B 1 288 ? 4.562   24.893  -38.400 1.00 46.35  ?  281 ASP B CA    1 
ATOM   4382 C  C     . ASP B 1 288 ? 3.363   23.975  -38.228 1.00 45.16  ?  281 ASP B C     1 
ATOM   4383 O  O     . ASP B 1 288 ? 3.523   22.792  -37.950 1.00 43.63  ?  281 ASP B O     1 
ATOM   4384 C  CB    . ASP B 1 288 ? 5.743   24.182  -39.064 1.00 47.14  ?  281 ASP B CB    1 
ATOM   4385 C  CG    . ASP B 1 288 ? 5.518   23.833  -40.525 1.00 49.93  ?  281 ASP B CG    1 
ATOM   4386 O  OD1   . ASP B 1 288 ? 4.363   23.654  -40.910 1.00 50.51  ?  281 ASP B OD1   1 
ATOM   4387 O  OD2   . ASP B 1 288 ? 6.529   23.768  -41.269 1.00 51.82  ?  281 ASP B OD2   1 
ATOM   4388 N  N     . GLU B 1 289 ? 2.156   24.537  -38.344 1.00 46.16  ?  282 GLU B N     1 
ATOM   4389 C  CA    . GLU B 1 289 ? 0.969   23.748  -38.042 1.00 45.29  ?  282 GLU B CA    1 
ATOM   4390 C  C     . GLU B 1 289 ? 0.715   22.723  -39.141 1.00 46.77  ?  282 GLU B C     1 
ATOM   4391 O  O     . GLU B 1 289 ? 0.099   21.713  -38.871 1.00 45.90  ?  282 GLU B O     1 
ATOM   4392 C  CB    . GLU B 1 289 ? -0.223  24.691  -37.798 1.00 46.30  ?  282 GLU B CB    1 
ATOM   4393 C  CG    . GLU B 1 289 ? -1.407  24.012  -37.125 1.00 45.25  ?  282 GLU B CG    1 
ATOM   4394 C  CD    . GLU B 1 289 ? -2.598  24.908  -36.779 1.00 46.46  ?  282 GLU B CD    1 
ATOM   4395 O  OE1   . GLU B 1 289 ? -3.613  24.361  -36.306 1.00 46.15  ?  282 GLU B OE1   1 
ATOM   4396 O  OE2   . GLU B 1 289 ? -2.497  26.125  -36.946 1.00 47.93  ?  282 GLU B OE2   1 
ATOM   4397 N  N     . GLU B 1 290 ? 1.181   22.954  -40.379 1.00 49.34  ?  283 GLU B N     1 
ATOM   4398 C  CA    . GLU B 1 290 ? 1.087   21.936  -41.417 1.00 50.96  ?  283 GLU B CA    1 
ATOM   4399 C  C     . GLU B 1 290 ? 1.964   20.722  -41.072 1.00 49.19  ?  283 GLU B C     1 
ATOM   4400 O  O     . GLU B 1 290 ? 1.521   19.586  -41.239 1.00 49.26  ?  283 GLU B O     1 
ATOM   4401 C  CB    . GLU B 1 290 ? 1.481   22.505  -42.780 1.00 54.41  ?  283 GLU B CB    1 
ATOM   4402 C  CG    . GLU B 1 290 ? 0.464   23.512  -43.321 1.00 56.95  ?  283 GLU B CG    1 
ATOM   4403 C  CD    . GLU B 1 290 ? 0.876   24.197  -44.618 1.00 60.72  ?  283 GLU B CD    1 
ATOM   4404 O  OE1   . GLU B 1 290 ? 2.082   24.147  -44.985 1.00 61.28  ?  283 GLU B OE1   1 
ATOM   4405 O  OE2   . GLU B 1 290 ? -0.022  24.757  -45.274 1.00 63.43  ?  283 GLU B OE2   1 
ATOM   4406 N  N     . ALA B 1 291 ? 3.203   20.958  -40.607 1.00 47.99  ?  284 ALA B N     1 
ATOM   4407 C  CA    . ALA B 1 291 ? 4.057   19.862  -40.164 1.00 46.46  ?  284 ALA B CA    1 
ATOM   4408 C  C     . ALA B 1 291 ? 3.414   19.093  -39.009 1.00 43.89  ?  284 ALA B C     1 
ATOM   4409 O  O     . ALA B 1 291 ? 3.414   17.858  -38.944 1.00 43.54  ?  284 ALA B O     1 
ATOM   4410 C  CB    . ALA B 1 291 ? 5.411   20.397  -39.768 1.00 45.90  ?  284 ALA B CB    1 
ATOM   4411 N  N     . PHE B 1 292 ? 2.837   19.857  -38.082 1.00 42.41  ?  285 PHE B N     1 
ATOM   4412 C  CA    . PHE B 1 292 ? 2.152   19.314  -36.924 1.00 40.31  ?  285 PHE B CA    1 
ATOM   4413 C  C     . PHE B 1 292 ? 1.094   18.329  -37.383 1.00 41.39  ?  285 PHE B C     1 
ATOM   4414 O  O     . PHE B 1 292 ? 1.034   17.232  -36.874 1.00 40.48  ?  285 PHE B O     1 
ATOM   4415 C  CB    . PHE B 1 292 ? 1.535   20.454  -36.100 1.00 39.50  ?  285 PHE B CB    1 
ATOM   4416 C  CG    . PHE B 1 292 ? 0.603   20.044  -34.988 1.00 38.00  ?  285 PHE B CG    1 
ATOM   4417 C  CD1   . PHE B 1 292 ? 1.065   19.539  -33.788 1.00 35.83  ?  285 PHE B CD1   1 
ATOM   4418 C  CD2   . PHE B 1 292 ? -0.774  20.215  -35.132 1.00 39.18  ?  285 PHE B CD2   1 
ATOM   4419 C  CE1   . PHE B 1 292 ? 0.192   19.148  -32.779 1.00 34.88  ?  285 PHE B CE1   1 
ATOM   4420 C  CE2   . PHE B 1 292 ? -1.644  19.848  -34.118 1.00 38.25  ?  285 PHE B CE2   1 
ATOM   4421 C  CZ    . PHE B 1 292 ? -1.169  19.311  -32.950 1.00 36.13  ?  285 PHE B CZ    1 
ATOM   4422 N  N     . VAL B 1 293 ? 0.243   18.737  -38.338 1.00 43.67  ?  286 VAL B N     1 
ATOM   4423 C  CA    . VAL B 1 293 ? -0.792  17.847  -38.839 1.00 45.21  ?  286 VAL B CA    1 
ATOM   4424 C  C     . VAL B 1 293 ? -0.170  16.646  -39.571 1.00 46.25  ?  286 VAL B C     1 
ATOM   4425 O  O     . VAL B 1 293 ? -0.619  15.512  -39.397 1.00 46.41  ?  286 VAL B O     1 
ATOM   4426 C  CB    . VAL B 1 293 ? -1.817  18.646  -39.692 1.00 47.79  ?  286 VAL B CB    1 
ATOM   4427 C  CG1   . VAL B 1 293 ? -2.798  17.719  -40.403 1.00 50.05  ?  286 VAL B CG1   1 
ATOM   4428 C  CG2   . VAL B 1 293 ? -2.577  19.620  -38.783 1.00 46.88  ?  286 VAL B CG2   1 
ATOM   4429 N  N     . GLU B 1 294 ? 0.828   16.908  -40.405 1.00 47.38  ?  287 GLU B N     1 
ATOM   4430 C  CA    . GLU B 1 294 ? 1.431   15.867  -41.220 1.00 48.96  ?  287 GLU B CA    1 
ATOM   4431 C  C     . GLU B 1 294 ? 2.053   14.772  -40.361 1.00 47.15  ?  287 GLU B C     1 
ATOM   4432 O  O     . GLU B 1 294 ? 2.023   13.622  -40.747 1.00 48.43  ?  287 GLU B O     1 
ATOM   4433 C  CB    . GLU B 1 294 ? 2.449   16.456  -42.183 1.00 50.70  ?  287 GLU B CB    1 
ATOM   4434 C  CG    . GLU B 1 294 ? 3.005   15.421  -43.145 1.00 52.99  ?  287 GLU B CG    1 
ATOM   4435 C  CD    . GLU B 1 294 ? 3.634   16.028  -44.389 1.00 55.89  ?  287 GLU B CD    1 
ATOM   4436 O  OE1   . GLU B 1 294 ? 3.004   16.961  -44.985 1.00 57.48  ?  287 GLU B OE1   1 
ATOM   4437 O  OE2   . GLU B 1 294 ? 4.731   15.559  -44.785 1.00 56.95  ?  287 GLU B OE2   1 
ATOM   4438 N  N     . ARG B 1 295 ? 2.622   15.107  -39.196 1.00 44.49  ?  288 ARG B N     1 
ATOM   4439 C  CA    . ARG B 1 295 ? 3.254   14.083  -38.366 1.00 43.08  ?  288 ARG B CA    1 
ATOM   4440 C  C     . ARG B 1 295 ? 2.259   13.356  -37.478 1.00 42.11  ?  288 ARG B C     1 
ATOM   4441 O  O     . ARG B 1 295 ? 2.652   12.429  -36.761 1.00 41.28  ?  288 ARG B O     1 
ATOM   4442 C  CB    . ARG B 1 295 ? 4.375   14.657  -37.491 1.00 41.08  ?  288 ARG B CB    1 
ATOM   4443 C  CG    . ARG B 1 295 ? 3.908   15.602  -36.384 1.00 38.92  ?  288 ARG B CG    1 
ATOM   4444 C  CD    . ARG B 1 295 ? 5.014   15.911  -35.414 1.00 37.17  ?  288 ARG B CD    1 
ATOM   4445 N  NE    . ARG B 1 295 ? 4.649   16.960  -34.433 1.00 35.52  ?  288 ARG B NE    1 
ATOM   4446 C  CZ    . ARG B 1 295 ? 3.932   16.785  -33.331 1.00 34.03  ?  288 ARG B CZ    1 
ATOM   4447 N  NH1   . ARG B 1 295 ? 3.303   15.654  -33.087 1.00 34.04  ?  288 ARG B NH1   1 
ATOM   4448 N  NH2   . ARG B 1 295 ? 3.854   17.785  -32.470 1.00 32.85  ?  288 ARG B NH2   1 
ATOM   4449 N  N     . GLY B 1 296 ? 0.987   13.783  -37.518 1.00 42.54  ?  289 GLY B N     1 
ATOM   4450 C  CA    . GLY B 1 296 ? -0.096  13.109  -36.822 1.00 42.37  ?  289 GLY B CA    1 
ATOM   4451 C  C     . GLY B 1 296 ? -0.331  13.724  -35.439 1.00 39.98  ?  289 GLY B C     1 
ATOM   4452 O  O     . GLY B 1 296 ? -0.720  13.018  -34.508 1.00 39.31  ?  289 GLY B O     1 
ATOM   4453 N  N     . GLY B 1 297 ? -0.101  15.023  -35.331 1.00 39.07  ?  290 GLY B N     1 
ATOM   4454 C  CA    . GLY B 1 297 ? -0.219  15.742  -34.072 1.00 37.08  ?  290 GLY B CA    1 
ATOM   4455 C  C     . GLY B 1 297 ? -1.653  15.735  -33.528 1.00 37.51  ?  290 GLY B C     1 
ATOM   4456 O  O     . GLY B 1 297 ? -1.849  15.896  -32.325 1.00 36.12  ?  290 GLY B O     1 
ATOM   4457 N  N     . ILE B 1 298 ? -2.644  15.639  -34.436 1.00 39.75  ?  291 ILE B N     1 
ATOM   4458 C  CA    . ILE B 1 298 ? -4.049  15.476  -34.060 1.00 40.87  ?  291 ILE B CA    1 
ATOM   4459 C  C     . ILE B 1 298 ? -4.413  14.005  -34.162 1.00 42.12  ?  291 ILE B C     1 
ATOM   4460 O  O     . ILE B 1 298 ? -4.407  13.459  -35.265 1.00 43.98  ?  291 ILE B O     1 
ATOM   4461 C  CB    . ILE B 1 298 ? -5.010  16.308  -34.940 1.00 43.11  ?  291 ILE B CB    1 
ATOM   4462 C  CG1   . ILE B 1 298 ? -4.753  17.811  -34.867 1.00 42.47  ?  291 ILE B CG1   1 
ATOM   4463 C  CG2   . ILE B 1 298 ? -6.454  15.960  -34.553 1.00 44.73  ?  291 ILE B CG2   1 
ATOM   4464 C  CD1   . ILE B 1 298 ? -4.994  18.426  -33.514 1.00 40.90  ?  291 ILE B CD1   1 
ATOM   4465 N  N     . TYR B 1 299 ? -4.716  13.365  -33.027 1.00 41.43  ?  292 TYR B N     1 
ATOM   4466 C  CA    . TYR B 1 299 ? -5.117  11.968  -33.012 1.00 43.00  ?  292 TYR B CA    1 
ATOM   4467 C  C     . TYR B 1 299 ? -6.107  11.717  -31.877 1.00 43.40  ?  292 TYR B C     1 
ATOM   4468 O  O     . TYR B 1 299 ? -6.504  12.636  -31.178 1.00 42.55  ?  292 TYR B O     1 
ATOM   4469 C  CB    . TYR B 1 299 ? -3.857  11.123  -32.856 1.00 41.88  ?  292 TYR B CB    1 
ATOM   4470 C  CG    . TYR B 1 299 ? -3.096  11.271  -31.540 1.00 39.35  ?  292 TYR B CG    1 
ATOM   4471 C  CD1   . TYR B 1 299 ? -2.167  12.288  -31.372 1.00 37.28  ?  292 TYR B CD1   1 
ATOM   4472 C  CD2   . TYR B 1 299 ? -3.200  10.319  -30.534 1.00 39.41  ?  292 TYR B CD2   1 
ATOM   4473 C  CE1   . TYR B 1 299 ? -1.389  12.373  -30.228 1.00 35.30  ?  292 TYR B CE1   1 
ATOM   4474 C  CE2   . TYR B 1 299 ? -2.446  10.411  -29.370 1.00 37.42  ?  292 TYR B CE2   1 
ATOM   4475 C  CZ    . TYR B 1 299 ? -1.550  11.451  -29.206 1.00 35.33  ?  292 TYR B CZ    1 
ATOM   4476 O  OH    . TYR B 1 299 ? -0.767  11.506  -28.059 1.00 33.67  ?  292 TYR B OH    1 
ATOM   4477 N  N     . ASP B 1 300 ? -6.491  10.456  -31.707 1.00 45.06  ?  293 ASP B N     1 
ATOM   4478 C  CA    . ASP B 1 300 ? -7.434  10.043  -30.677 1.00 46.11  ?  293 ASP B CA    1 
ATOM   4479 C  C     . ASP B 1 300 ? -6.683  9.941   -29.353 1.00 43.82  ?  293 ASP B C     1 
ATOM   4480 O  O     . ASP B 1 300 ? -6.143  8.895   -29.010 1.00 43.95  ?  293 ASP B O     1 
ATOM   4481 C  CB    . ASP B 1 300 ? -8.100  8.719   -31.049 1.00 49.28  ?  293 ASP B CB    1 
ATOM   4482 C  CG    . ASP B 1 300 ? -8.992  8.857   -32.270 1.00 52.02  ?  293 ASP B CG    1 
ATOM   4483 O  OD1   . ASP B 1 300 ? -9.342  10.006  -32.616 1.00 51.69  ?  293 ASP B OD1   1 
ATOM   4484 O  OD2   . ASP B 1 300 ? -9.298  7.821   -32.884 1.00 54.69  ?  293 ASP B OD2   1 
ATOM   4485 N  N     . TRP B 1 301 ? -6.677  11.050  -28.625 1.00 42.07  ?  294 TRP B N     1 
ATOM   4486 C  CA    . TRP B 1 301 ? -5.740  11.243  -27.526 1.00 39.65  ?  294 TRP B CA    1 
ATOM   4487 C  C     . TRP B 1 301 ? -6.392  11.051  -26.152 1.00 40.18  ?  294 TRP B C     1 
ATOM   4488 O  O     . TRP B 1 301 ? -5.838  11.426  -25.113 1.00 38.49  ?  294 TRP B O     1 
ATOM   4489 C  CB    . TRP B 1 301 ? -5.059  12.610  -27.697 1.00 37.51  ?  294 TRP B CB    1 
ATOM   4490 C  CG    . TRP B 1 301 ? -5.941  13.801  -27.965 1.00 38.15  ?  294 TRP B CG    1 
ATOM   4491 C  CD1   . TRP B 1 301 ? -7.172  14.072  -27.430 1.00 39.66  ?  294 TRP B CD1   1 
ATOM   4492 C  CD2   . TRP B 1 301 ? -5.583  14.963  -28.751 1.00 37.52  ?  294 TRP B CD2   1 
ATOM   4493 N  NE1   . TRP B 1 301 ? -7.605  15.301  -27.845 1.00 40.01  ?  294 TRP B NE1   1 
ATOM   4494 C  CE2   . TRP B 1 301 ? -6.660  15.877  -28.651 1.00 38.74  ?  294 TRP B CE2   1 
ATOM   4495 C  CE3   . TRP B 1 301 ? -4.477  15.315  -29.536 1.00 36.44  ?  294 TRP B CE3   1 
ATOM   4496 C  CZ2   . TRP B 1 301 ? -6.648  17.106  -29.302 1.00 38.89  ?  294 TRP B CZ2   1 
ATOM   4497 C  CZ3   . TRP B 1 301 ? -4.467  16.538  -30.171 1.00 36.60  ?  294 TRP B CZ3   1 
ATOM   4498 C  CH2   . TRP B 1 301 ? -5.532  17.435  -30.021 1.00 37.76  ?  294 TRP B CH2   1 
ATOM   4499 N  N     . ASN B 1 302 ? -7.553  10.385  -26.122 1.00 42.91  ?  295 ASN B N     1 
ATOM   4500 C  CA    . ASN B 1 302 ? -8.084  9.888   -24.864 1.00 44.04  ?  295 ASN B CA    1 
ATOM   4501 C  C     . ASN B 1 302 ? -8.944  8.674   -25.196 1.00 47.41  ?  295 ASN B C     1 
ATOM   4502 O  O     . ASN B 1 302 ? -9.116  8.365   -26.375 1.00 48.61  ?  295 ASN B O     1 
ATOM   4503 C  CB    . ASN B 1 302 ? -8.837  10.985  -24.102 1.00 44.08  ?  295 ASN B CB    1 
ATOM   4504 C  CG    . ASN B 1 302 ? -9.974  11.546  -24.926 1.00 46.05  ?  295 ASN B CG    1 
ATOM   4505 O  OD1   . ASN B 1 302 ? -10.570 10.821  -25.717 1.00 48.37  ?  295 ASN B OD1   1 
ATOM   4506 N  ND2   . ASN B 1 302 ? -10.236 12.838  -24.814 1.00 45.38  ?  295 ASN B ND2   1 
ATOM   4507 N  N     . LYS B 1 303 ? -9.470  7.993   -24.170 1.00 49.25  ?  296 LYS B N     1 
ATOM   4508 C  CA    . LYS B 1 303 ? -10.156 6.726   -24.400 1.00 52.77  ?  296 LYS B CA    1 
ATOM   4509 C  C     . LYS B 1 303 ? -11.562 6.967   -24.947 1.00 55.73  ?  296 LYS B C     1 
ATOM   4510 O  O     . LYS B 1 303 ? -12.092 6.113   -25.655 1.00 58.64  ?  296 LYS B O     1 
ATOM   4511 C  CB    . LYS B 1 303 ? -10.206 5.859   -23.139 1.00 54.26  ?  296 LYS B CB    1 
ATOM   4512 C  CG    . LYS B 1 303 ? -11.059 6.389   -21.994 1.00 55.33  ?  296 LYS B CG    1 
ATOM   4513 C  CD    . LYS B 1 303 ? -11.181 5.408   -20.833 1.00 57.59  ?  296 LYS B CD    1 
ATOM   4514 C  CE    . LYS B 1 303 ? -11.463 3.985   -21.280 1.00 60.99  ?  296 LYS B CE    1 
ATOM   4515 N  NZ    . LYS B 1 303 ? -11.886 3.113   -20.156 1.00 64.21  ?  296 LYS B NZ    1 
ATOM   4516 N  N     . SER B 1 304 ? -12.169 8.108   -24.583 1.00 55.35  ?  297 SER B N     1 
ATOM   4517 C  CA    . SER B 1 304 ? -13.404 8.574   -25.204 1.00 57.95  ?  297 SER B CA    1 
ATOM   4518 C  C     . SER B 1 304 ? -13.251 8.657   -26.726 1.00 57.93  ?  297 SER B C     1 
ATOM   4519 O  O     . SER B 1 304 ? -14.186 8.333   -27.459 1.00 61.19  ?  297 SER B O     1 
ATOM   4520 C  CB    . SER B 1 304 ? -13.843 9.907   -24.634 1.00 57.18  ?  297 SER B CB    1 
ATOM   4521 O  OG    . SER B 1 304 ? -14.539 9.733   -23.408 1.00 59.16  ?  297 SER B OG    1 
ATOM   4522 N  N     . SER B 1 305 ? -12.074 9.099   -27.193 1.00 54.58  ?  298 SER B N     1 
ATOM   4523 C  CA    . SER B 1 305 ? -11.796 9.214   -28.616 1.00 54.55  ?  298 SER B CA    1 
ATOM   4524 C  C     . SER B 1 305 ? -11.713 7.816   -29.241 1.00 56.72  ?  298 SER B C     1 
ATOM   4525 O  O     . SER B 1 305 ? -11.798 7.749   -30.481 1.00 57.95  ?  298 SER B O     1 
ATOM   4526 C  CB    . SER B 1 305 ? -10.530 9.996   -28.869 1.00 50.85  ?  298 SER B CB    1 
ATOM   4527 O  OG    . SER B 1 305 ? -10.570 11.262  -28.229 1.00 49.13  ?  298 SER B OG    1 
ATOM   4528 N  N     . GLN C 1 25  ? 7.083   50.209  -28.241 1.00 75.24  ?  18  GLN C N     1 
ATOM   4529 C  CA    . GLN C 1 25  ? 8.352   50.864  -28.664 1.00 70.75  ?  18  GLN C CA    1 
ATOM   4530 C  C     . GLN C 1 25  ? 8.001   52.010  -29.611 1.00 68.88  ?  18  GLN C C     1 
ATOM   4531 O  O     . GLN C 1 25  ? 7.108   51.873  -30.443 1.00 68.97  ?  18  GLN C O     1 
ATOM   4532 C  CB    . GLN C 1 25  ? 9.290   49.840  -29.323 1.00 67.30  ?  18  GLN C CB    1 
ATOM   4533 C  CG    . GLN C 1 25  ? 9.572   48.627  -28.442 1.00 69.63  ?  18  GLN C CG    1 
ATOM   4534 C  CD    . GLN C 1 25  ? 10.476  47.582  -29.053 1.00 67.07  ?  18  GLN C CD    1 
ATOM   4535 O  OE1   . GLN C 1 25  ? 10.080  46.813  -29.921 1.00 66.48  ?  18  GLN C OE1   1 
ATOM   4536 N  NE2   . GLN C 1 25  ? 11.704  47.513  -28.569 1.00 66.22  ?  18  GLN C NE2   1 
ATOM   4537 N  N     . VAL C 1 26  ? 8.684   53.148  -29.454 1.00 67.77  ?  19  VAL C N     1 
ATOM   4538 C  CA    . VAL C 1 26  ? 8.452   54.296  -30.313 1.00 66.30  ?  19  VAL C CA    1 
ATOM   4539 C  C     . VAL C 1 26  ? 9.310   54.138  -31.574 1.00 61.36  ?  19  VAL C C     1 
ATOM   4540 O  O     . VAL C 1 26  ? 10.533  54.066  -31.469 1.00 59.32  ?  19  VAL C O     1 
ATOM   4541 C  CB    . VAL C 1 26  ? 8.780   55.597  -29.560 1.00 68.19  ?  19  VAL C CB    1 
ATOM   4542 C  CG1   . VAL C 1 26  ? 8.664   56.819  -30.452 1.00 66.87  ?  19  VAL C CG1   1 
ATOM   4543 C  CG2   . VAL C 1 26  ? 7.907   55.746  -28.324 1.00 73.80  ?  19  VAL C CG2   1 
ATOM   4544 N  N     . PRO C 1 27  ? 8.724   54.109  -32.791 1.00 59.82  ?  20  PRO C N     1 
ATOM   4545 C  CA    . PRO C 1 27  ? 9.515   53.894  -34.009 1.00 55.74  ?  20  PRO C CA    1 
ATOM   4546 C  C     . PRO C 1 27  ? 10.171  55.167  -34.533 1.00 53.83  ?  20  PRO C C     1 
ATOM   4547 O  O     . PRO C 1 27  ? 9.756   55.718  -35.545 1.00 52.93  ?  20  PRO C O     1 
ATOM   4548 C  CB    . PRO C 1 27  ? 8.454   53.357  -34.985 1.00 56.07  ?  20  PRO C CB    1 
ATOM   4549 C  CG    . PRO C 1 27  ? 7.196   54.123  -34.594 1.00 59.64  ?  20  PRO C CG    1 
ATOM   4550 C  CD    . PRO C 1 27  ? 7.281   54.238  -33.082 1.00 62.49  ?  20  PRO C CD    1 
ATOM   4551 N  N     . VAL C 1 28  ? 11.248  55.589  -33.878 1.00 53.54  ?  21  VAL C N     1 
ATOM   4552 C  CA    . VAL C 1 28  ? 11.802  56.916  -34.094 1.00 53.09  ?  21  VAL C CA    1 
ATOM   4553 C  C     . VAL C 1 28  ? 12.551  57.004  -35.431 1.00 49.76  ?  21  VAL C C     1 
ATOM   4554 O  O     . VAL C 1 28  ? 12.626  58.091  -35.979 1.00 49.53  ?  21  VAL C O     1 
ATOM   4555 C  CB    . VAL C 1 28  ? 12.739  57.329  -32.949 1.00 54.65  ?  21  VAL C CB    1 
ATOM   4556 C  CG1   . VAL C 1 28  ? 13.913  56.369  -32.765 1.00 53.18  ?  21  VAL C CG1   1 
ATOM   4557 C  CG2   . VAL C 1 28  ? 13.257  58.738  -33.135 1.00 55.04  ?  21  VAL C CG2   1 
ATOM   4558 N  N     . SER C 1 29  ? 13.205  55.916  -35.865 1.00 47.77  ?  22  SER C N     1 
ATOM   4559 C  CA    . SER C 1 29  ? 14.028  55.916  -37.085 1.00 45.24  ?  22  SER C CA    1 
ATOM   4560 C  C     . SER C 1 29  ? 13.718  54.664  -37.857 1.00 44.16  ?  22  SER C C     1 
ATOM   4561 O  O     . SER C 1 29  ? 13.999  53.573  -37.361 1.00 44.50  ?  22  SER C O     1 
ATOM   4562 C  CB    . SER C 1 29  ? 15.501  55.978  -36.839 1.00 44.79  ?  22  SER C CB    1 
ATOM   4563 O  OG    . SER C 1 29  ? 16.189  56.160  -38.072 1.00 43.07  ?  22  SER C OG    1 
ATOM   4564 N  N     . VAL C 1 30  ? 13.112  54.851  -39.044 1.00 43.37  ?  23  VAL C N     1 
ATOM   4565 C  CA    . VAL C 1 30  ? 12.603  53.741  -39.806 1.00 43.17  ?  23  VAL C CA    1 
ATOM   4566 C  C     . VAL C 1 30  ? 13.252  53.748  -41.184 1.00 41.53  ?  23  VAL C C     1 
ATOM   4567 O  O     . VAL C 1 30  ? 13.471  54.816  -41.783 1.00 40.88  ?  23  VAL C O     1 
ATOM   4568 C  CB    . VAL C 1 30  ? 11.066  53.812  -39.916 1.00 44.93  ?  23  VAL C CB    1 
ATOM   4569 C  CG1   . VAL C 1 30  ? 10.518  52.691  -40.789 1.00 45.35  ?  23  VAL C CG1   1 
ATOM   4570 C  CG2   . VAL C 1 30  ? 10.440  53.808  -38.522 1.00 47.26  ?  23  VAL C CG2   1 
ATOM   4571 N  N     . ASN C 1 31  ? 13.543  52.529  -41.627 1.00 41.43  ?  24  ASN C N     1 
ATOM   4572 C  CA    . ASN C 1 31  ? 13.988  52.279  -42.987 1.00 40.73  ?  24  ASN C CA    1 
ATOM   4573 C  C     . ASN C 1 31  ? 12.809  51.766  -43.810 1.00 41.83  ?  24  ASN C C     1 
ATOM   4574 O  O     . ASN C 1 31  ? 12.223  50.726  -43.486 1.00 43.26  ?  24  ASN C O     1 
ATOM   4575 C  CB    . ASN C 1 31  ? 15.149  51.301  -42.980 1.00 40.72  ?  24  ASN C CB    1 
ATOM   4576 C  CG    . ASN C 1 31  ? 16.465  51.996  -42.695 1.00 40.03  ?  24  ASN C CG    1 
ATOM   4577 O  OD1   . ASN C 1 31  ? 17.182  52.326  -43.636 1.00 39.74  ?  24  ASN C OD1   1 
ATOM   4578 N  ND2   . ASN C 1 31  ? 16.746  52.279  -41.433 1.00 40.30  ?  24  ASN C ND2   1 
ATOM   4579 N  N     . TYR C 1 32  ? 12.488  52.488  -44.885 1.00 41.64  ?  25  TYR C N     1 
ATOM   4580 C  CA    . TYR C 1 32  ? 11.422  52.058  -45.779 1.00 43.18  ?  25  TYR C CA    1 
ATOM   4581 C  C     . TYR C 1 32  ? 12.046  51.610  -47.092 1.00 43.25  ?  25  TYR C C     1 
ATOM   4582 O  O     . TYR C 1 32  ? 12.532  52.454  -47.855 1.00 42.48  ?  25  TYR C O     1 
ATOM   4583 C  CB    . TYR C 1 32  ? 10.401  53.189  -45.851 1.00 43.82  ?  25  TYR C CB    1 
ATOM   4584 C  CG    . TYR C 1 32  ? 9.271   52.955  -46.842 1.00 45.91  ?  25  TYR C CG    1 
ATOM   4585 C  CD1   . TYR C 1 32  ? 8.913   51.667  -47.221 1.00 47.64  ?  25  TYR C CD1   1 
ATOM   4586 C  CD2   . TYR C 1 32  ? 8.620   54.020  -47.446 1.00 46.62  ?  25  TYR C CD2   1 
ATOM   4587 C  CE1   . TYR C 1 32  ? 7.910   51.447  -48.158 1.00 50.16  ?  25  TYR C CE1   1 
ATOM   4588 C  CE2   . TYR C 1 32  ? 7.622   53.815  -48.393 1.00 49.01  ?  25  TYR C CE2   1 
ATOM   4589 C  CZ    . TYR C 1 32  ? 7.257   52.518  -48.740 1.00 50.85  ?  25  TYR C CZ    1 
ATOM   4590 O  OH    . TYR C 1 32  ? 6.280   52.240  -49.683 1.00 53.87  ?  25  TYR C OH    1 
ATOM   4591 N  N     . HIS C 1 33  ? 12.107  50.286  -47.269 1.00 44.58  ?  26  HIS C N     1 
ATOM   4592 C  CA    . HIS C 1 33  ? 12.645  49.644  -48.449 1.00 45.59  ?  26  HIS C CA    1 
ATOM   4593 C  C     . HIS C 1 33  ? 11.496  49.459  -49.436 1.00 47.82  ?  26  HIS C C     1 
ATOM   4594 O  O     . HIS C 1 33  ? 10.947  48.354  -49.543 1.00 50.22  ?  26  HIS C O     1 
ATOM   4595 C  CB    . HIS C 1 33  ? 13.271  48.287  -48.116 1.00 46.70  ?  26  HIS C CB    1 
ATOM   4596 C  CG    . HIS C 1 33  ? 14.484  48.395  -47.238 1.00 45.14  ?  26  HIS C CG    1 
ATOM   4597 N  ND1   . HIS C 1 33  ? 15.757  48.200  -47.724 1.00 45.34  ?  26  HIS C ND1   1 
ATOM   4598 C  CD2   . HIS C 1 33  ? 14.622  48.743  -45.956 1.00 43.90  ?  26  HIS C CD2   1 
ATOM   4599 C  CE1   . HIS C 1 33  ? 16.625  48.347  -46.728 1.00 44.35  ?  26  HIS C CE1   1 
ATOM   4600 N  NE2   . HIS C 1 33  ? 15.957  48.700  -45.654 1.00 43.38  ?  26  HIS C NE2   1 
ATOM   4601 N  N     . PHE C 1 34  ? 11.192  50.555  -50.148 1.00 47.45  ?  27  PHE C N     1 
ATOM   4602 C  CA    . PHE C 1 34  ? 9.911   50.754  -50.811 1.00 49.57  ?  27  PHE C CA    1 
ATOM   4603 C  C     . PHE C 1 34  ? 9.788   49.911  -52.081 1.00 52.35  ?  27  PHE C C     1 
ATOM   4604 O  O     . PHE C 1 34  ? 8.664   49.661  -52.529 1.00 55.13  ?  27  PHE C O     1 
ATOM   4605 C  CB    . PHE C 1 34  ? 9.671   52.261  -50.957 1.00 48.46  ?  27  PHE C CB    1 
ATOM   4606 C  CG    . PHE C 1 34  ? 10.529  53.003  -51.959 1.00 47.70  ?  27  PHE C CG    1 
ATOM   4607 C  CD1   . PHE C 1 34  ? 10.214  52.991  -53.309 1.00 49.83  ?  27  PHE C CD1   1 
ATOM   4608 C  CD2   . PHE C 1 34  ? 11.621  53.749  -51.539 1.00 45.42  ?  27  PHE C CD2   1 
ATOM   4609 C  CE1   . PHE C 1 34  ? 10.985  53.698  -54.218 1.00 49.62  ?  27  PHE C CE1   1 
ATOM   4610 C  CE2   . PHE C 1 34  ? 12.386  54.455  -52.451 1.00 45.35  ?  27  PHE C CE2   1 
ATOM   4611 C  CZ    . PHE C 1 34  ? 12.069  54.417  -53.785 1.00 47.40  ?  27  PHE C CZ    1 
ATOM   4612 N  N     A SER C 1 35  ? 10.925  49.438  -52.611 0.36 52.25  ?  28  SER C N     1 
ATOM   4613 N  N     B SER C 1 35  ? 10.922  49.462  -52.632 0.64 52.25  ?  28  SER C N     1 
ATOM   4614 C  CA    A SER C 1 35  ? 10.957  48.591  -53.794 0.36 55.42  ?  28  SER C CA    1 
ATOM   4615 C  CA    B SER C 1 35  ? 10.933  48.561  -53.773 0.64 55.47  ?  28  SER C CA    1 
ATOM   4616 C  C     A SER C 1 35  ? 12.114  47.603  -53.680 0.36 55.79  ?  28  SER C C     1 
ATOM   4617 C  C     B SER C 1 35  ? 12.045  47.533  -53.598 0.64 55.85  ?  28  SER C C     1 
ATOM   4618 O  O     A SER C 1 35  ? 13.028  47.833  -52.893 0.36 53.31  ?  28  SER C O     1 
ATOM   4619 O  O     B SER C 1 35  ? 12.855  47.665  -52.684 0.64 53.42  ?  28  SER C O     1 
ATOM   4620 C  CB    A SER C 1 35  ? 11.090  49.454  -55.025 0.36 55.99  ?  28  SER C CB    1 
ATOM   4621 C  CB    B SER C 1 35  ? 11.111  49.355  -55.047 0.64 56.17  ?  28  SER C CB    1 
ATOM   4622 O  OG    A SER C 1 35  ? 12.297  50.200  -54.982 0.36 53.60  ?  28  SER C OG    1 
ATOM   4623 O  OG    B SER C 1 35  ? 11.149  48.499  -56.176 0.64 59.83  ?  28  SER C OG    1 
ATOM   4624 N  N     . ARG C 1 36  ? 12.088  46.528  -54.488 1.00 59.43  ?  29  ARG C N     1 
ATOM   4625 C  CA    . ARG C 1 36  ? 13.141  45.518  -54.475 1.00 60.78  ?  29  ARG C CA    1 
ATOM   4626 C  C     . ARG C 1 36  ? 13.960  45.476  -55.768 1.00 63.10  ?  29  ARG C C     1 
ATOM   4627 O  O     . ARG C 1 36  ? 14.934  44.722  -55.853 1.00 64.76  ?  29  ARG C O     1 
ATOM   4628 C  CB    . ARG C 1 36  ? 12.562  44.140  -54.158 1.00 63.93  ?  29  ARG C CB    1 
ATOM   4629 C  CG    . ARG C 1 36  ? 12.506  43.837  -52.665 1.00 62.00  ?  29  ARG C CG    1 
ATOM   4630 C  CD    . ARG C 1 36  ? 11.984  42.440  -52.356 1.00 65.69  ?  29  ARG C CD    1 
ATOM   4631 N  NE    . ARG C 1 36  ? 11.599  42.310  -50.955 1.00 64.23  ?  29  ARG C NE    1 
ATOM   4632 C  CZ    . ARG C 1 36  ? 12.367  41.813  -49.994 1.00 63.40  ?  29  ARG C CZ    1 
ATOM   4633 N  NH1   . ARG C 1 36  ? 13.624  41.475  -50.243 1.00 63.60  ?  29  ARG C NH1   1 
ATOM   4634 N  NH2   . ARG C 1 36  ? 11.876  41.685  -48.775 1.00 62.76  ?  29  ARG C NH2   1 
ATOM   4635 N  N     . LYS C 1 37  ? 13.615  46.295  -56.766 1.00 63.66  ?  30  LYS C N     1 
ATOM   4636 C  CA    . LYS C 1 37  ? 14.358  46.288  -58.014 1.00 66.41  ?  30  LYS C CA    1 
ATOM   4637 C  C     . LYS C 1 37  ? 15.694  47.003  -57.806 1.00 64.09  ?  30  LYS C C     1 
ATOM   4638 O  O     . LYS C 1 37  ? 15.753  47.987  -57.069 1.00 60.31  ?  30  LYS C O     1 
ATOM   4639 C  CB    . LYS C 1 37  ? 13.478  46.923  -59.098 1.00 68.17  ?  30  LYS C CB    1 
ATOM   4640 C  CG    . LYS C 1 37  ? 13.887  46.616  -60.534 1.00 72.75  ?  30  LYS C CG    1 
ATOM   4641 C  CD    . LYS C 1 37  ? 12.829  46.987  -61.562 1.00 75.49  ?  30  LYS C CD    1 
ATOM   4642 C  CE    . LYS C 1 37  ? 12.496  48.465  -61.562 1.00 72.44  ?  30  LYS C CE    1 
ATOM   4643 N  NZ    . LYS C 1 37  ? 11.541  48.810  -62.640 1.00 75.77  ?  30  LYS C NZ    1 
ATOM   4644 N  N     . CYS C 1 38  ? 16.769  46.486  -58.418 1.00 66.95  ?  31  CYS C N     1 
ATOM   4645 C  CA    . CYS C 1 38  ? 18.062  47.155  -58.402 1.00 66.01  ?  31  CYS C CA    1 
ATOM   4646 C  C     . CYS C 1 38  ? 18.763  47.004  -59.755 1.00 70.57  ?  31  CYS C C     1 
ATOM   4647 O  O     . CYS C 1 38  ? 18.543  46.035  -60.473 1.00 74.77  ?  31  CYS C O     1 
ATOM   4648 C  CB    . CYS C 1 38  ? 18.937  46.652  -57.251 1.00 64.67  ?  31  CYS C CB    1 
ATOM   4649 S  SG    . CYS C 1 38  ? 20.592  47.384  -57.283 1.00 64.82  ?  31  CYS C SG    1 
ATOM   4650 N  N     . ASN C 1 39  ? 19.645  47.962  -60.090 1.00 70.33  ?  32  ASN C N     1 
ATOM   4651 C  CA    . ASN C 1 39  ? 20.382  47.898  -61.347 1.00 75.12  ?  32  ASN C CA    1 
ATOM   4652 C  C     . ASN C 1 39  ? 21.641  47.031  -61.188 1.00 78.14  ?  32  ASN C C     1 
ATOM   4653 O  O     . ASN C 1 39  ? 22.186  46.568  -62.187 1.00 83.35  ?  32  ASN C O     1 
ATOM   4654 C  CB    . ASN C 1 39  ? 20.679  49.285  -61.943 1.00 74.70  ?  32  ASN C CB    1 
ATOM   4655 C  CG    . ASN C 1 39  ? 21.330  50.262  -60.982 1.00 70.92  ?  32  ASN C CG    1 
ATOM   4656 O  OD1   . ASN C 1 39  ? 20.993  50.282  -59.801 1.00 66.96  ?  32  ASN C OD1   1 
ATOM   4657 N  ND2   . ASN C 1 39  ? 22.251  51.091  -61.457 1.00 72.55  ?  32  ASN C ND2   1 
ATOM   4658 N  N     . LYS C 1 40  ? 22.095  46.790  -59.944 1.00 75.47  ?  33  LYS C N     1 
ATOM   4659 C  CA    . LYS C 1 40  ? 23.406  46.201  -59.692 1.00 78.25  ?  33  LYS C CA    1 
ATOM   4660 C  C     . LYS C 1 40  ? 23.270  44.739  -59.271 1.00 80.22  ?  33  LYS C C     1 
ATOM   4661 O  O     . LYS C 1 40  ? 22.153  44.224  -59.205 1.00 79.49  ?  33  LYS C O     1 
ATOM   4662 C  CB    . LYS C 1 40  ? 24.165  47.018  -58.635 1.00 74.85  ?  33  LYS C CB    1 
ATOM   4663 C  CG    . LYS C 1 40  ? 24.556  48.429  -59.056 1.00 74.14  ?  33  LYS C CG    1 
ATOM   4664 C  CD    . LYS C 1 40  ? 25.184  48.482  -60.437 1.00 79.56  ?  33  LYS C CD    1 
ATOM   4665 C  CE    . LYS C 1 40  ? 25.700  49.850  -60.838 1.00 79.68  ?  33  LYS C CE    1 
ATOM   4666 N  NZ    . LYS C 1 40  ? 27.110  50.070  -60.428 1.00 81.77  ?  33  LYS C NZ    1 
ATOM   4667 N  N     . GLU C 1 41  ? 24.433  44.098  -59.024 1.00 83.34  ?  34  GLU C N     1 
ATOM   4668 C  CA    . GLU C 1 41  ? 24.545  42.669  -58.740 1.00 86.61  ?  34  GLU C CA    1 
ATOM   4669 C  C     . GLU C 1 41  ? 25.531  42.399  -57.597 1.00 86.10  ?  34  GLU C C     1 
ATOM   4670 O  O     . GLU C 1 41  ? 26.327  41.456  -57.659 1.00 90.91  ?  34  GLU C O     1 
ATOM   4671 C  CB    . GLU C 1 41  ? 25.011  41.931  -60.000 1.00 93.79  ?  34  GLU C CB    1 
ATOM   4672 C  CG    . GLU C 1 41  ? 23.985  41.873  -61.125 1.00 95.66  ?  34  GLU C CG    1 
ATOM   4673 C  CD    . GLU C 1 41  ? 23.063  40.660  -61.096 1.00 97.77  ?  34  GLU C CD    1 
ATOM   4674 O  OE1   . GLU C 1 41  ? 23.149  39.826  -62.031 1.00 104.17 ?  34  GLU C OE1   1 
ATOM   4675 O  OE2   . GLU C 1 41  ? 22.263  40.542  -60.134 1.00 93.57  -1 34  GLU C OE2   1 
ATOM   4676 N  N     . CYS C 1 42  ? 25.470  43.210  -56.525 1.00 80.74  ?  35  CYS C N     1 
ATOM   4677 C  CA    . CYS C 1 42  ? 26.286  42.985  -55.341 1.00 80.15  ?  35  CYS C CA    1 
ATOM   4678 C  C     . CYS C 1 42  ? 26.037  41.561  -54.839 1.00 82.22  ?  35  CYS C C     1 
ATOM   4679 O  O     . CYS C 1 42  ? 24.887  41.144  -54.673 1.00 80.53  ?  35  CYS C O     1 
ATOM   4680 C  CB    . CYS C 1 42  ? 26.015  44.015  -54.243 1.00 74.29  ?  35  CYS C CB    1 
ATOM   4681 S  SG    . CYS C 1 42  ? 26.530  45.711  -54.655 1.00 72.67  ?  35  CYS C SG    1 
ATOM   4682 N  N     . LEU C 1 43  ? 27.136  40.828  -54.613 1.00 86.47  ?  36  LEU C N     1 
ATOM   4683 C  CA    . LEU C 1 43  ? 27.085  39.407  -54.310 1.00 89.99  ?  36  LEU C CA    1 
ATOM   4684 C  C     . LEU C 1 43  ? 26.499  39.189  -52.911 1.00 85.92  ?  36  LEU C C     1 
ATOM   4685 O  O     . LEU C 1 43  ? 25.838  38.180  -52.671 1.00 87.22  ?  36  LEU C O     1 
ATOM   4686 C  CB    . LEU C 1 43  ? 28.501  38.838  -54.443 1.00 95.98  ?  36  LEU C CB    1 
ATOM   4687 C  CG    . LEU C 1 43  ? 29.037  38.716  -55.872 1.00 101.85 ?  36  LEU C CG    1 
ATOM   4688 C  CD1   . LEU C 1 43  ? 30.540  38.529  -55.877 1.00 107.27 ?  36  LEU C CD1   1 
ATOM   4689 C  CD2   . LEU C 1 43  ? 28.385  37.553  -56.605 1.00 106.19 ?  36  LEU C CD2   1 
ATOM   4690 N  N     . PHE C 1 44  ? 26.706  40.170  -52.015 1.00 81.41  ?  37  PHE C N     1 
ATOM   4691 C  CA    . PHE C 1 44  ? 26.390  40.032  -50.601 1.00 78.30  ?  37  PHE C CA    1 
ATOM   4692 C  C     . PHE C 1 44  ? 24.994  40.548  -50.272 1.00 73.26  ?  37  PHE C C     1 
ATOM   4693 O  O     . PHE C 1 44  ? 24.597  40.411  -49.120 1.00 71.01  ?  37  PHE C O     1 
ATOM   4694 C  CB    . PHE C 1 44  ? 27.408  40.768  -49.721 1.00 77.06  ?  37  PHE C CB    1 
ATOM   4695 C  CG    . PHE C 1 44  ? 27.695  42.204  -50.097 1.00 74.63  ?  37  PHE C CG    1 
ATOM   4696 C  CD1   . PHE C 1 44  ? 26.696  43.171  -50.122 1.00 69.83  ?  37  PHE C CD1   1 
ATOM   4697 C  CD2   . PHE C 1 44  ? 28.990  42.599  -50.418 1.00 77.78  ?  37  PHE C CD2   1 
ATOM   4698 C  CE1   . PHE C 1 44  ? 26.990  44.488  -50.462 1.00 68.15  ?  37  PHE C CE1   1 
ATOM   4699 C  CE2   . PHE C 1 44  ? 29.278  43.916  -50.753 1.00 76.16  ?  37  PHE C CE2   1 
ATOM   4700 C  CZ    . PHE C 1 44  ? 28.274  44.858  -50.798 1.00 71.31  ?  37  PHE C CZ    1 
ATOM   4701 N  N     . CYS C 1 45  ? 24.271  41.090  -51.276 1.00 72.17  ?  38  CYS C N     1 
ATOM   4702 C  CA    . CYS C 1 45  ? 23.070  41.905  -51.073 1.00 67.56  ?  38  CYS C CA    1 
ATOM   4703 C  C     . CYS C 1 45  ? 22.063  41.165  -50.191 1.00 66.67  ?  38  CYS C C     1 
ATOM   4704 O  O     . CYS C 1 45  ? 21.665  40.046  -50.520 1.00 69.99  ?  38  CYS C O     1 
ATOM   4705 C  CB    . CYS C 1 45  ? 22.407  42.294  -52.397 1.00 68.02  ?  38  CYS C CB    1 
ATOM   4706 S  SG    . CYS C 1 45  ? 20.955  43.381  -52.251 1.00 63.13  ?  38  CYS C SG    1 
ATOM   4707 N  N     . PHE C 1 46  ? 21.675  41.815  -49.075 1.00 62.74  ?  39  PHE C N     1 
ATOM   4708 C  CA    . PHE C 1 46  ? 20.778  41.214  -48.096 1.00 62.11  ?  39  PHE C CA    1 
ATOM   4709 C  C     . PHE C 1 46  ? 19.356  41.746  -48.273 1.00 59.84  ?  39  PHE C C     1 
ATOM   4710 O  O     . PHE C 1 46  ? 18.510  41.577  -47.411 1.00 58.89  ?  39  PHE C O     1 
ATOM   4711 C  CB    . PHE C 1 46  ? 21.360  41.366  -46.678 1.00 60.66  ?  39  PHE C CB    1 
ATOM   4712 C  CG    . PHE C 1 46  ? 21.318  42.736  -46.034 1.00 56.63  ?  39  PHE C CG    1 
ATOM   4713 C  CD1   . PHE C 1 46  ? 20.728  43.834  -46.651 1.00 54.14  ?  39  PHE C CD1   1 
ATOM   4714 C  CD2   . PHE C 1 46  ? 21.840  42.912  -44.765 1.00 55.84  ?  39  PHE C CD2   1 
ATOM   4715 C  CE1   . PHE C 1 46  ? 20.681  45.073  -46.026 1.00 51.07  ?  39  PHE C CE1   1 
ATOM   4716 C  CE2   . PHE C 1 46  ? 21.807  44.151  -44.145 1.00 52.84  ?  39  PHE C CE2   1 
ATOM   4717 C  CZ    . PHE C 1 46  ? 21.231  45.230  -44.776 1.00 50.51  ?  39  PHE C CZ    1 
ATOM   4718 N  N     . HIS C 1 47  ? 19.084  42.422  -49.395 1.00 59.40  ?  40  HIS C N     1 
ATOM   4719 C  CA    . HIS C 1 47  ? 17.736  42.854  -49.723 1.00 58.21  ?  40  HIS C CA    1 
ATOM   4720 C  C     . HIS C 1 47  ? 17.590  42.676  -51.234 1.00 60.92  ?  40  HIS C C     1 
ATOM   4721 O  O     . HIS C 1 47  ? 17.955  43.564  -51.999 1.00 60.06  ?  40  HIS C O     1 
ATOM   4722 C  CB    . HIS C 1 47  ? 17.490  44.267  -49.174 1.00 54.08  ?  40  HIS C CB    1 
ATOM   4723 C  CG    . HIS C 1 47  ? 16.062  44.524  -48.849 1.00 53.08  ?  40  HIS C CG    1 
ATOM   4724 N  ND1   . HIS C 1 47  ? 15.616  44.599  -47.550 1.00 51.69  ?  40  HIS C ND1   1 
ATOM   4725 C  CD2   . HIS C 1 47  ? 14.983  44.673  -49.626 1.00 53.95  ?  40  HIS C CD2   1 
ATOM   4726 C  CE1   . HIS C 1 47  ? 14.303  44.795  -47.551 1.00 51.84  ?  40  HIS C CE1   1 
ATOM   4727 N  NE2   . HIS C 1 47  ? 13.898  44.855  -48.803 1.00 53.17  ?  40  HIS C NE2   1 
ATOM   4728 N  N     . THR C 1 48  ? 17.081  41.497  -51.630 1.00 64.72  ?  41  THR C N     1 
ATOM   4729 C  CA    . THR C 1 48  ? 17.210  40.959  -52.979 1.00 68.85  ?  41  THR C CA    1 
ATOM   4730 C  C     . THR C 1 48  ? 15.961  41.263  -53.799 1.00 69.57  ?  41  THR C C     1 
ATOM   4731 O  O     . THR C 1 48  ? 14.905  41.538  -53.238 1.00 67.85  ?  41  THR C O     1 
ATOM   4732 C  CB    . THR C 1 48  ? 17.450  39.436  -52.949 1.00 73.63  ?  41  THR C CB    1 
ATOM   4733 O  OG1   . THR C 1 48  ? 16.317  38.758  -52.393 1.00 74.70  ?  41  THR C OG1   1 
ATOM   4734 C  CG2   . THR C 1 48  ? 18.684  39.055  -52.156 1.00 73.71  ?  41  THR C CG2   1 
ATOM   4735 N  N     . ALA C 1 49  ? 16.089  41.146  -55.131 1.00 72.87  ?  42  ALA C N     1 
ATOM   4736 C  CA    . ALA C 1 49  ? 15.015  41.494  -56.050 1.00 74.16  ?  42  ALA C CA    1 
ATOM   4737 C  C     . ALA C 1 49  ? 14.042  40.325  -56.216 1.00 78.68  ?  42  ALA C C     1 
ATOM   4738 O  O     . ALA C 1 49  ? 14.030  39.683  -57.265 1.00 83.60  ?  42  ALA C O     1 
ATOM   4739 C  CB    . ALA C 1 49  ? 15.611  41.920  -57.371 1.00 76.13  ?  42  ALA C CB    1 
ATOM   4740 N  N     . THR C 1 50  ? 13.217  40.077  -55.184 1.00 77.52  ?  43  THR C N     1 
ATOM   4741 C  CA    . THR C 1 50  ? 12.285  38.953  -55.152 1.00 82.09  ?  43  THR C CA    1 
ATOM   4742 C  C     . THR C 1 50  ? 10.879  39.369  -55.591 1.00 83.24  ?  43  THR C C     1 
ATOM   4743 O  O     . THR C 1 50  ? 10.052  38.500  -55.870 1.00 88.17  ?  43  THR C O     1 
ATOM   4744 C  CB    . THR C 1 50  ? 12.178  38.317  -53.755 1.00 81.33  ?  43  THR C CB    1 
ATOM   4745 O  OG1   . THR C 1 50  ? 11.901  39.348  -52.804 1.00 76.10  ?  43  THR C OG1   1 
ATOM   4746 C  CG2   . THR C 1 50  ? 13.421  37.559  -53.343 1.00 82.11  ?  43  THR C CG2   1 
ATOM   4747 N  N     . THR C 1 51  ? 10.589  40.678  -55.600 1.00 79.21  ?  44  THR C N     1 
ATOM   4748 C  CA    . THR C 1 51  ? 9.349   41.191  -56.176 1.00 80.71  ?  44  THR C CA    1 
ATOM   4749 C  C     . THR C 1 51  ? 9.622   42.520  -56.878 1.00 77.85  ?  44  THR C C     1 
ATOM   4750 O  O     . THR C 1 51  ? 10.696  43.102  -56.720 1.00 74.28  ?  44  THR C O     1 
ATOM   4751 C  CB    . THR C 1 51  ? 8.232   41.406  -55.140 1.00 79.64  ?  44  THR C CB    1 
ATOM   4752 O  OG1   . THR C 1 51  ? 8.453   42.654  -54.483 1.00 74.12  ?  44  THR C OG1   1 
ATOM   4753 C  CG2   . THR C 1 51  ? 8.117   40.296  -54.118 1.00 81.30  ?  44  THR C CG2   1 
ATOM   4754 N  N     . SER C 1 52  ? 8.635   42.983  -57.655 1.00 79.97  ?  45  SER C N     1 
ATOM   4755 C  CA    . SER C 1 52  ? 8.685   44.288  -58.292 1.00 77.79  ?  45  SER C CA    1 
ATOM   4756 C  C     . SER C 1 52  ? 7.598   45.208  -57.727 1.00 75.91  ?  45  SER C C     1 
ATOM   4757 O  O     . SER C 1 52  ? 7.468   46.339  -58.185 1.00 74.47  ?  45  SER C O     1 
ATOM   4758 C  CB    . SER C 1 52  ? 8.590   44.164  -59.802 1.00 82.36  ?  45  SER C CB    1 
ATOM   4759 O  OG    . SER C 1 52  ? 7.416   43.470  -60.208 1.00 87.66  ?  45  SER C OG    1 
ATOM   4760 N  N     . HIS C 1 53  ? 6.851   44.746  -56.713 1.00 76.27  ?  46  HIS C N     1 
ATOM   4761 C  CA    . HIS C 1 53  ? 5.784   45.542  -56.132 1.00 75.41  ?  46  HIS C CA    1 
ATOM   4762 C  C     . HIS C 1 53  ? 6.335   46.823  -55.509 1.00 69.91  ?  46  HIS C C     1 
ATOM   4763 O  O     . HIS C 1 53  ? 7.392   46.807  -54.868 1.00 66.47  ?  46  HIS C O     1 
ATOM   4764 C  CB    . HIS C 1 53  ? 4.996   44.746  -55.083 1.00 77.27  ?  46  HIS C CB    1 
ATOM   4765 C  CG    . HIS C 1 53  ? 3.925   45.557  -54.440 1.00 77.01  ?  46  HIS C CG    1 
ATOM   4766 N  ND1   . HIS C 1 53  ? 2.653   45.692  -54.950 1.00 81.42  ?  46  HIS C ND1   1 
ATOM   4767 C  CD2   . HIS C 1 53  ? 3.953   46.297  -53.322 1.00 73.38  ?  46  HIS C CD2   1 
ATOM   4768 C  CE1   . HIS C 1 53  ? 1.949   46.489  -54.159 1.00 80.48  ?  46  HIS C CE1   1 
ATOM   4769 N  NE2   . HIS C 1 53  ? 2.725   46.874  -53.168 1.00 75.60  ?  46  HIS C NE2   1 
ATOM   4770 N  N     . VAL C 1 54  ? 5.583   47.918  -55.718 1.00 69.77  ?  47  VAL C N     1 
ATOM   4771 C  CA    . VAL C 1 54  ? 5.799   49.198  -55.066 1.00 65.68  ?  47  VAL C CA    1 
ATOM   4772 C  C     . VAL C 1 54  ? 4.440   49.786  -54.723 1.00 67.54  ?  47  VAL C C     1 
ATOM   4773 O  O     . VAL C 1 54  ? 3.567   49.849  -55.586 1.00 71.32  ?  47  VAL C O     1 
ATOM   4774 C  CB    . VAL C 1 54  ? 6.600   50.174  -55.957 1.00 63.86  ?  47  VAL C CB    1 
ATOM   4775 C  CG1   . VAL C 1 54  ? 6.687   51.576  -55.361 1.00 60.59  ?  47  VAL C CG1   1 
ATOM   4776 C  CG2   . VAL C 1 54  ? 7.976   49.624  -56.269 1.00 62.64  ?  47  VAL C CG2   1 
ATOM   4777 N  N     . GLU C 1 55  ? 4.278   50.235  -53.475 1.00 65.39  ?  48  GLU C N     1 
ATOM   4778 C  CA    . GLU C 1 55  ? 3.032   50.827  -53.017 1.00 67.53  ?  48  GLU C CA    1 
ATOM   4779 C  C     . GLU C 1 55  ? 2.608   51.952  -53.951 1.00 68.59  ?  48  GLU C C     1 
ATOM   4780 O  O     . GLU C 1 55  ? 3.438   52.539  -54.622 1.00 66.37  ?  48  GLU C O     1 
ATOM   4781 C  CB    . GLU C 1 55  ? 3.166   51.368  -51.593 1.00 64.80  ?  48  GLU C CB    1 
ATOM   4782 C  CG    . GLU C 1 55  ? 2.970   50.292  -50.553 1.00 65.81  ?  48  GLU C CG    1 
ATOM   4783 C  CD    . GLU C 1 55  ? 1.619   49.622  -50.698 1.00 71.33  ?  48  GLU C CD    1 
ATOM   4784 O  OE1   . GLU C 1 55  ? 0.621   50.269  -50.344 1.00 73.64  ?  48  GLU C OE1   1 
ATOM   4785 O  OE2   . GLU C 1 55  ? 1.570   48.504  -51.246 1.00 73.86  -1 48  GLU C OE2   1 
ATOM   4786 N  N     . LYS C 1 56  ? 1.302   52.252  -53.954 1.00 72.49  ?  49  LYS C N     1 
ATOM   4787 C  CA    . LYS C 1 56  ? 0.790   53.420  -54.656 1.00 73.93  ?  49  LYS C CA    1 
ATOM   4788 C  C     . LYS C 1 56  ? 1.184   54.640  -53.844 1.00 70.46  ?  49  LYS C C     1 
ATOM   4789 O  O     . LYS C 1 56  ? 1.226   54.538  -52.624 1.00 69.05  ?  49  LYS C O     1 
ATOM   4790 C  CB    . LYS C 1 56  ? -0.740  53.415  -54.791 1.00 79.74  ?  49  LYS C CB    1 
ATOM   4791 C  CG    . LYS C 1 56  ? -1.342  52.325  -55.667 1.00 84.64  ?  49  LYS C CG    1 
ATOM   4792 C  CD    . LYS C 1 56  ? -1.401  50.979  -54.997 1.00 85.72  ?  49  LYS C CD    1 
ATOM   4793 C  CE    . LYS C 1 56  ? -2.378  50.035  -55.662 1.00 92.33  ?  49  LYS C CE    1 
ATOM   4794 N  NZ    . LYS C 1 56  ? -2.258  48.670  -55.102 1.00 93.41  ?  49  LYS C NZ    1 
ATOM   4795 N  N     . PRO C 1 57  ? 1.458   55.811  -54.471 1.00 69.56  ?  50  PRO C N     1 
ATOM   4796 C  CA    . PRO C 1 57  ? 1.878   56.999  -53.729 1.00 66.81  ?  50  PRO C CA    1 
ATOM   4797 C  C     . PRO C 1 57  ? 0.980   57.259  -52.537 1.00 68.58  ?  50  PRO C C     1 
ATOM   4798 O  O     . PRO C 1 57  ? 1.462   57.409  -51.432 1.00 66.07  ?  50  PRO C O     1 
ATOM   4799 C  CB    . PRO C 1 57  ? 1.796   58.143  -54.745 1.00 68.01  ?  50  PRO C CB    1 
ATOM   4800 C  CG    . PRO C 1 57  ? 2.027   57.454  -56.063 1.00 69.19  ?  50  PRO C CG    1 
ATOM   4801 C  CD    . PRO C 1 57  ? 1.446   56.056  -55.921 1.00 71.45  ?  50  PRO C CD    1 
ATOM   4802 N  N     . GLU C 1 58  ? -0.338  57.292  -52.765 1.00 73.52  ?  51  GLU C N     1 
ATOM   4803 C  CA    . GLU C 1 58  ? -1.246  57.720  -51.713 1.00 76.16  ?  51  GLU C CA    1 
ATOM   4804 C  C     . GLU C 1 58  ? -1.158  56.734  -50.543 1.00 75.30  ?  51  GLU C C     1 
ATOM   4805 O  O     . GLU C 1 58  ? -1.232  57.154  -49.402 1.00 75.07  ?  51  GLU C O     1 
ATOM   4806 C  CB    . GLU C 1 58  ? -2.669  57.917  -52.261 1.00 82.41  ?  51  GLU C CB    1 
ATOM   4807 C  CG    . GLU C 1 58  ? -2.796  59.037  -53.304 1.00 83.71  ?  51  GLU C CG    1 
ATOM   4808 C  CD    . GLU C 1 58  ? -2.177  60.396  -52.981 1.00 81.09  ?  51  GLU C CD    1 
ATOM   4809 O  OE1   . GLU C 1 58  ? -2.574  61.013  -51.968 1.00 82.37  ?  51  GLU C OE1   1 
ATOM   4810 O  OE2   . GLU C 1 58  ? -1.293  60.848  -53.754 1.00 78.30  -1 51  GLU C OE2   1 
ATOM   4811 N  N     . ASN C 1 59  ? -0.949  55.445  -50.839 1.00 75.10  ?  52  ASN C N     1 
ATOM   4812 C  CA    . ASN C 1 59  ? -0.849  54.398  -49.825 1.00 74.74  ?  52  ASN C CA    1 
ATOM   4813 C  C     . ASN C 1 59  ? 0.456   54.491  -49.032 1.00 69.33  ?  52  ASN C C     1 
ATOM   4814 O  O     . ASN C 1 59  ? 0.481   54.229  -47.836 1.00 69.05  ?  52  ASN C O     1 
ATOM   4815 C  CB    . ASN C 1 59  ? -0.989  53.005  -50.446 1.00 76.73  ?  52  ASN C CB    1 
ATOM   4816 C  CG    . ASN C 1 59  ? -2.381  52.792  -51.004 1.00 83.13  ?  52  ASN C CG    1 
ATOM   4817 O  OD1   . ASN C 1 59  ? -3.244  53.645  -50.827 1.00 86.04  ?  52  ASN C OD1   1 
ATOM   4818 N  ND2   . ASN C 1 59  ? -2.606  51.680  -51.680 1.00 85.90  ?  52  ASN C ND2   1 
ATOM   4819 N  N     . ALA C 1 60  ? 1.553   54.859  -49.692 1.00 65.54  ?  53  ALA C N     1 
ATOM   4820 C  CA    . ALA C 1 60  ? 2.794   55.137  -48.980 1.00 61.03  ?  53  ALA C CA    1 
ATOM   4821 C  C     . ALA C 1 60  ? 2.646   56.376  -48.098 1.00 60.89  ?  53  ALA C C     1 
ATOM   4822 O  O     . ALA C 1 60  ? 3.075   56.393  -46.944 1.00 59.44  ?  53  ALA C O     1 
ATOM   4823 C  CB    . ALA C 1 60  ? 3.926   55.290  -49.985 1.00 58.09  ?  53  ALA C CB    1 
ATOM   4824 N  N     . LYS C 1 61  ? 2.027   57.437  -48.631 1.00 62.92  ?  54  LYS C N     1 
ATOM   4825 C  CA    . LYS C 1 61  ? 1.887   58.646  -47.839 1.00 63.46  ?  54  LYS C CA    1 
ATOM   4826 C  C     . LYS C 1 61  ? 1.071   58.317  -46.591 1.00 66.27  ?  54  LYS C C     1 
ATOM   4827 O  O     . LYS C 1 61  ? 1.362   58.804  -45.497 1.00 65.71  ?  54  LYS C O     1 
ATOM   4828 C  CB    . LYS C 1 61  ? 1.239   59.748  -48.673 1.00 66.09  ?  54  LYS C CB    1 
ATOM   4829 C  CG    . LYS C 1 61  ? 2.083   60.224  -49.846 1.00 63.75  ?  54  LYS C CG    1 
ATOM   4830 C  CD    . LYS C 1 61  ? 1.400   61.284  -50.675 1.00 66.85  ?  54  LYS C CD    1 
ATOM   4831 C  CE    . LYS C 1 61  ? 2.277   61.816  -51.786 1.00 64.90  ?  54  LYS C CE    1 
ATOM   4832 N  NZ    . LYS C 1 61  ? 1.685   63.025  -52.401 1.00 68.07  ?  54  LYS C NZ    1 
ATOM   4833 N  N     . ARG C 1 62  ? 0.049   57.472  -46.761 1.00 69.85  ?  55  ARG C N     1 
ATOM   4834 C  CA    . ARG C 1 62  ? -0.811  57.144  -45.633 1.00 73.46  ?  55  ARG C CA    1 
ATOM   4835 C  C     . ARG C 1 62  ? 0.029   56.401  -44.585 1.00 70.55  ?  55  ARG C C     1 
ATOM   4836 O  O     . ARG C 1 62  ? -0.013  56.747  -43.412 1.00 71.39  ?  55  ARG C O     1 
ATOM   4837 C  CB    . ARG C 1 62  ? -2.036  56.372  -46.130 1.00 78.45  ?  55  ARG C CB    1 
ATOM   4838 C  CG    . ARG C 1 62  ? -2.936  55.812  -45.042 1.00 82.89  ?  55  ARG C CG    1 
ATOM   4839 C  CD    . ARG C 1 62  ? -4.181  56.623  -44.769 1.00 88.78  ?  55  ARG C CD    1 
ATOM   4840 N  NE    . ARG C 1 62  ? -4.752  56.130  -43.528 1.00 92.41  ?  55  ARG C NE    1 
ATOM   4841 C  CZ    . ARG C 1 62  ? -4.701  56.765  -42.366 1.00 93.13  ?  55  ARG C CZ    1 
ATOM   4842 N  NH1   . ARG C 1 62  ? -4.237  58.001  -42.296 1.00 91.14  ?  55  ARG C NH1   1 
ATOM   4843 N  NH2   . ARG C 1 62  ? -5.159  56.169  -41.281 1.00 96.55  ?  55  ARG C NH2   1 
ATOM   4844 N  N     . GLY C 1 63  ? 0.825   55.415  -45.021 1.00 67.50  ?  56  GLY C N     1 
ATOM   4845 C  CA    . GLY C 1 63  ? 1.709   54.682  -44.121 1.00 64.86  ?  56  GLY C CA    1 
ATOM   4846 C  C     . GLY C 1 63  ? 2.742   55.561  -43.406 1.00 61.54  ?  56  GLY C C     1 
ATOM   4847 O  O     . GLY C 1 63  ? 3.039   55.340  -42.226 1.00 61.37  ?  56  GLY C O     1 
ATOM   4848 N  N     . LEU C 1 64  ? 3.337   56.517  -44.132 1.00 59.27  ?  57  LEU C N     1 
ATOM   4849 C  CA    . LEU C 1 64  ? 4.297   57.440  -43.540 1.00 56.87  ?  57  LEU C CA    1 
ATOM   4850 C  C     . LEU C 1 64  ? 3.587   58.350  -42.533 1.00 60.01  ?  57  LEU C C     1 
ATOM   4851 O  O     . LEU C 1 64  ? 4.112   58.663  -41.473 1.00 59.56  ?  57  LEU C O     1 
ATOM   4852 C  CB    . LEU C 1 64  ? 4.995   58.222  -44.665 1.00 54.64  ?  57  LEU C CB    1 
ATOM   4853 C  CG    . LEU C 1 64  ? 5.807   57.350  -45.627 1.00 52.02  ?  57  LEU C CG    1 
ATOM   4854 C  CD1   . LEU C 1 64  ? 6.146   58.095  -46.910 1.00 51.24  ?  57  LEU C CD1   1 
ATOM   4855 C  CD2   . LEU C 1 64  ? 7.085   56.859  -44.963 1.00 49.13  ?  57  LEU C CD2   1 
ATOM   4856 N  N     . THR C 1 65  ? 2.347   58.721  -42.821 1.00 63.90  ?  58  THR C N     1 
ATOM   4857 C  CA    . THR C 1 65  ? 1.551   59.486  -41.871 1.00 67.95  ?  58  THR C CA    1 
ATOM   4858 C  C     . THR C 1 65  ? 1.360   58.724  -40.552 1.00 69.60  ?  58  THR C C     1 
ATOM   4859 O  O     . THR C 1 65  ? 1.450   59.317  -39.464 1.00 71.11  ?  58  THR C O     1 
ATOM   4860 C  CB    . THR C 1 65  ? 0.208   59.818  -42.520 1.00 72.46  ?  58  THR C CB    1 
ATOM   4861 O  OG1   . THR C 1 65  ? 0.525   60.441  -43.762 1.00 70.66  ?  58  THR C OG1   1 
ATOM   4862 C  CG2   . THR C 1 65  ? -0.675  60.709  -41.669 1.00 77.53  ?  58  THR C CG2   1 
ATOM   4863 N  N     . LEU C 1 66  ? 1.052   57.420  -40.664 1.00 69.98  ?  59  LEU C N     1 
ATOM   4864 C  CA    . LEU C 1 66  ? 0.849   56.578  -39.491 1.00 71.92  ?  59  LEU C CA    1 
ATOM   4865 C  C     . LEU C 1 66  ? 2.125   56.567  -38.646 1.00 68.43  ?  59  LEU C C     1 
ATOM   4866 O  O     . LEU C 1 66  ? 2.068   56.583  -37.408 1.00 70.52  ?  59  LEU C O     1 
ATOM   4867 C  CB    . LEU C 1 66  ? 0.432   55.166  -39.926 1.00 72.84  ?  59  LEU C CB    1 
ATOM   4868 C  CG    . LEU C 1 66  ? -0.943  55.032  -40.596 1.00 77.65  ?  59  LEU C CG    1 
ATOM   4869 C  CD1   . LEU C 1 66  ? -1.247  53.577  -40.934 1.00 78.96  ?  59  LEU C CD1   1 
ATOM   4870 C  CD2   . LEU C 1 66  ? -2.051  55.617  -39.727 1.00 83.45  ?  59  LEU C CD2   1 
ATOM   4871 N  N     . LEU C 1 67  ? 3.284   56.572  -39.327 1.00 63.63  ?  60  LEU C N     1 
ATOM   4872 C  CA    . LEU C 1 67  ? 4.575   56.495  -38.646 1.00 60.56  ?  60  LEU C CA    1 
ATOM   4873 C  C     . LEU C 1 67  ? 4.876   57.812  -37.932 1.00 61.31  ?  60  LEU C C     1 
ATOM   4874 O  O     . LEU C 1 67  ? 5.272   57.791  -36.775 1.00 62.06  ?  60  LEU C O     1 
ATOM   4875 C  CB    . LEU C 1 67  ? 5.669   56.087  -39.650 1.00 56.15  ?  60  LEU C CB    1 
ATOM   4876 C  CG    . LEU C 1 67  ? 5.578   54.635  -40.140 1.00 55.77  ?  60  LEU C CG    1 
ATOM   4877 C  CD1   . LEU C 1 67  ? 6.426   54.373  -41.378 1.00 52.54  ?  60  LEU C CD1   1 
ATOM   4878 C  CD2   . LEU C 1 67  ? 5.969   53.666  -39.042 1.00 56.06  ?  60  LEU C CD2   1 
ATOM   4879 N  N     . LYS C 1 68  ? 4.664   58.952  -38.602 1.00 61.68  ?  61  LYS C N     1 
ATOM   4880 C  CA    . LYS C 1 68  ? 4.836   60.245  -37.973 1.00 63.33  ?  61  LYS C CA    1 
ATOM   4881 C  C     . LYS C 1 68  ? 3.946   60.304  -36.728 1.00 68.18  ?  61  LYS C C     1 
ATOM   4882 O  O     . LYS C 1 68  ? 4.387   60.739  -35.663 1.00 69.44  ?  61  LYS C O     1 
ATOM   4883 C  CB    . LYS C 1 68  ? 4.462   61.363  -38.951 1.00 64.10  ?  61  LYS C CB    1 
ATOM   4884 C  CG    . LYS C 1 68  ? 4.343   62.767  -38.366 1.00 67.25  ?  61  LYS C CG    1 
ATOM   4885 C  CD    . LYS C 1 68  ? 5.684   63.456  -38.148 1.00 65.02  ?  61  LYS C CD    1 
ATOM   4886 C  CE    . LYS C 1 68  ? 5.544   64.728  -37.339 1.00 69.10  ?  61  LYS C CE    1 
ATOM   4887 N  NZ    . LYS C 1 68  ? 6.728   65.597  -37.510 1.00 67.57  ?  61  LYS C NZ    1 
ATOM   4888 N  N     . GLN C 1 69  ? 2.708   59.819  -36.854 1.00 71.42  ?  62  GLN C N     1 
ATOM   4889 C  CA    . GLN C 1 69  ? 1.756   59.896  -35.742 1.00 76.98  ?  62  GLN C CA    1 
ATOM   4890 C  C     . GLN C 1 69  ? 2.243   59.043  -34.571 1.00 76.90  ?  62  GLN C C     1 
ATOM   4891 O  O     . GLN C 1 69  ? 2.031   59.408  -33.413 1.00 80.70  ?  62  GLN C O     1 
ATOM   4892 C  CB    . GLN C 1 69  ? 0.358   59.464  -36.187 1.00 80.92  ?  62  GLN C CB    1 
ATOM   4893 C  CG    . GLN C 1 69  ? -0.744  59.771  -35.173 1.00 87.82  ?  62  GLN C CG    1 
ATOM   4894 C  CD    . GLN C 1 69  ? -0.820  61.234  -34.802 1.00 90.65  ?  62  GLN C CD    1 
ATOM   4895 O  OE1   . GLN C 1 69  ? -0.089  61.713  -33.934 1.00 90.36  ?  62  GLN C OE1   1 
ATOM   4896 N  NE2   . GLN C 1 69  ? -1.728  61.955  -35.442 1.00 94.04  ?  62  GLN C NE2   1 
ATOM   4897 N  N     . ALA C 1 70  ? 2.938   57.935  -34.904 1.00 72.88  ?  63  ALA C N     1 
ATOM   4898 C  CA    . ALA C 1 70  ? 3.477   56.986  -33.942 1.00 72.53  ?  63  ALA C CA    1 
ATOM   4899 C  C     . ALA C 1 70  ? 4.788   57.467  -33.306 1.00 70.18  ?  63  ALA C C     1 
ATOM   4900 O  O     . ALA C 1 70  ? 5.278   56.796  -32.408 1.00 70.39  ?  63  ALA C O     1 
ATOM   4901 C  CB    . ALA C 1 70  ? 3.665   55.642  -34.612 1.00 69.89  ?  63  ALA C CB    1 
ATOM   4902 N  N     . GLY C 1 71  ? 5.366   58.593  -33.758 1.00 68.41  ?  64  GLY C N     1 
ATOM   4903 C  CA    . GLY C 1 71  ? 6.576   59.149  -33.164 1.00 67.09  ?  64  GLY C CA    1 
ATOM   4904 C  C     . GLY C 1 71  ? 7.834   59.011  -34.042 1.00 61.98  ?  64  GLY C C     1 
ATOM   4905 O  O     . GLY C 1 71  ? 8.940   59.258  -33.571 1.00 60.96  ?  64  GLY C O     1 
ATOM   4906 N  N     . MET C 1 72  ? 7.694   58.630  -35.320 1.00 59.30  ?  65  MET C N     1 
ATOM   4907 C  CA    . MET C 1 72  ? 8.845   58.617  -36.225 1.00 55.21  ?  65  MET C CA    1 
ATOM   4908 C  C     . MET C 1 72  ? 9.388   60.043  -36.411 1.00 55.29  ?  65  MET C C     1 
ATOM   4909 O  O     . MET C 1 72  ? 8.625   61.000  -36.530 1.00 57.65  ?  65  MET C O     1 
ATOM   4910 C  CB    . MET C 1 72  ? 8.483   57.985  -37.576 1.00 53.22  ?  65  MET C CB    1 
ATOM   4911 C  CG    . MET C 1 72  ? 9.666   57.891  -38.557 1.00 49.58  ?  65  MET C CG    1 
ATOM   4912 S  SD    . MET C 1 72  ? 9.188   57.055  -40.082 1.00 48.17  ?  65  MET C SD    1 
ATOM   4913 C  CE    . MET C 1 72  ? 8.237   58.327  -40.907 1.00 49.77  ?  65  MET C CE    1 
ATOM   4914 N  N     . LYS C 1 73  ? 10.722  60.166  -36.359 1.00 53.34  ?  66  LYS C N     1 
ATOM   4915 C  CA    . LYS C 1 73  ? 11.439  61.409  -36.607 1.00 53.51  ?  66  LYS C CA    1 
ATOM   4916 C  C     . LYS C 1 73  ? 12.387  61.310  -37.817 1.00 50.28  ?  66  LYS C C     1 
ATOM   4917 O  O     . LYS C 1 73  ? 12.654  62.338  -38.424 1.00 50.56  ?  66  LYS C O     1 
ATOM   4918 C  CB    . LYS C 1 73  ? 12.229  61.789  -35.357 1.00 55.45  ?  66  LYS C CB    1 
ATOM   4919 C  CG    . LYS C 1 73  ? 11.392  61.965  -34.084 1.00 59.42  ?  66  LYS C CG    1 
ATOM   4920 C  CD    . LYS C 1 73  ? 12.234  62.394  -32.900 1.00 61.82  ?  66  LYS C CD    1 
ATOM   4921 C  CE    . LYS C 1 73  ? 11.438  63.075  -31.803 1.00 66.85  ?  66  LYS C CE    1 
ATOM   4922 N  NZ    . LYS C 1 73  ? 12.331  63.543  -30.717 1.00 69.61  ?  66  LYS C NZ    1 
ATOM   4923 N  N     . LYS C 1 74  ? 12.931  60.112  -38.123 1.00 47.84  ?  67  LYS C N     1 
ATOM   4924 C  CA    . LYS C 1 74  ? 13.828  59.875  -39.267 1.00 45.37  ?  67  LYS C CA    1 
ATOM   4925 C  C     . LYS C 1 74  ? 13.254  58.782  -40.150 1.00 43.84  ?  67  LYS C C     1 
ATOM   4926 O  O     . LYS C 1 74  ? 12.815  57.737  -39.667 1.00 44.00  ?  67  LYS C O     1 
ATOM   4927 C  CB    . LYS C 1 74  ? 15.236  59.440  -38.836 1.00 44.73  ?  67  LYS C CB    1 
ATOM   4928 C  CG    . LYS C 1 74  ? 16.263  59.281  -39.964 1.00 43.09  ?  67  LYS C CG    1 
ATOM   4929 C  CD    . LYS C 1 74  ? 17.683  59.563  -39.532 1.00 43.89  ?  67  LYS C CD    1 
ATOM   4930 C  CE    . LYS C 1 74  ? 18.765  59.431  -40.587 1.00 43.16  ?  67  LYS C CE    1 
ATOM   4931 N  NZ    . LYS C 1 74  ? 18.858  58.048  -41.140 1.00 41.67  ?  67  LYS C NZ    1 
ATOM   4932 N  N     . ILE C 1 75  ? 13.298  59.026  -41.470 1.00 42.79  ?  68  ILE C N     1 
ATOM   4933 C  CA    . ILE C 1 75  ? 12.994  58.008  -42.443 1.00 41.69  ?  68  ILE C CA    1 
ATOM   4934 C  C     . ILE C 1 75  ? 14.227  57.967  -43.347 1.00 40.38  ?  68  ILE C C     1 
ATOM   4935 O  O     . ILE C 1 75  ? 14.787  59.010  -43.718 1.00 40.60  ?  68  ILE C O     1 
ATOM   4936 C  CB    . ILE C 1 75  ? 11.679  58.318  -43.197 1.00 42.72  ?  68  ILE C CB    1 
ATOM   4937 C  CG1   . ILE C 1 75  ? 11.226  57.210  -44.146 1.00 42.39  ?  68  ILE C CG1   1 
ATOM   4938 C  CG2   . ILE C 1 75  ? 11.786  59.632  -43.945 1.00 43.09  ?  68  ILE C CG2   1 
ATOM   4939 C  CD1   . ILE C 1 75  ? 10.772  55.951  -43.475 1.00 42.98  ?  68  ILE C CD1   1 
ATOM   4940 N  N     . ASN C 1 76  ? 14.640  56.751  -43.609 1.00 39.62  ?  69  ASN C N     1 
ATOM   4941 C  CA    . ASN C 1 76  ? 15.668  56.457  -44.592 1.00 39.03  ?  69  ASN C CA    1 
ATOM   4942 C  C     . ASN C 1 76  ? 14.994  55.702  -45.721 1.00 39.11  ?  69  ASN C C     1 
ATOM   4943 O  O     . ASN C 1 76  ? 14.447  54.601  -45.518 1.00 39.43  ?  69  ASN C O     1 
ATOM   4944 C  CB    . ASN C 1 76  ? 16.817  55.624  -44.018 1.00 38.94  ?  69  ASN C CB    1 
ATOM   4945 C  CG    . ASN C 1 76  ? 18.014  55.517  -44.955 1.00 39.15  ?  69  ASN C CG    1 
ATOM   4946 O  OD1   . ASN C 1 76  ? 18.513  56.517  -45.428 1.00 39.52  ?  69  ASN C OD1   1 
ATOM   4947 N  ND2   . ASN C 1 76  ? 18.517  54.323  -45.189 1.00 39.49  ?  69  ASN C ND2   1 
ATOM   4948 N  N     . PHE C 1 77  ? 15.085  56.294  -46.923 1.00 39.32  ?  70  PHE C N     1 
ATOM   4949 C  CA    . PHE C 1 77  ? 14.544  55.658  -48.107 1.00 39.96  ?  70  PHE C CA    1 
ATOM   4950 C  C     . PHE C 1 77  ? 15.569  54.711  -48.696 1.00 40.25  ?  70  PHE C C     1 
ATOM   4951 O  O     . PHE C 1 77  ? 16.695  55.116  -48.993 1.00 40.35  ?  70  PHE C O     1 
ATOM   4952 C  CB    . PHE C 1 77  ? 14.079  56.697  -49.122 1.00 40.64  ?  70  PHE C CB    1 
ATOM   4953 C  CG    . PHE C 1 77  ? 12.817  57.419  -48.752 1.00 41.25  ?  70  PHE C CG    1 
ATOM   4954 C  CD1   . PHE C 1 77  ? 11.578  56.805  -48.910 1.00 42.38  ?  70  PHE C CD1   1 
ATOM   4955 C  CD2   . PHE C 1 77  ? 12.885  58.660  -48.160 1.00 41.30  ?  70  PHE C CD2   1 
ATOM   4956 C  CE1   . PHE C 1 77  ? 10.424  57.462  -48.515 1.00 43.60  ?  70  PHE C CE1   1 
ATOM   4957 C  CE2   . PHE C 1 77  ? 11.723  59.311  -47.748 1.00 42.48  ?  70  PHE C CE2   1 
ATOM   4958 C  CZ    . PHE C 1 77  ? 10.508  58.723  -47.966 1.00 43.65  ?  70  PHE C CZ    1 
ATOM   4959 N  N     . ALA C 1 78  ? 15.170  53.437  -48.796 1.00 40.95  ?  71  ALA C N     1 
ATOM   4960 C  CA    . ALA C 1 78  ? 16.067  52.399  -49.247 1.00 41.87  ?  71  ALA C CA    1 
ATOM   4961 C  C     . ALA C 1 78  ? 15.284  51.436  -50.142 1.00 43.64  ?  71  ALA C C     1 
ATOM   4962 O  O     . ALA C 1 78  ? 14.206  51.792  -50.621 1.00 44.15  ?  71  ALA C O     1 
ATOM   4963 C  CB    . ALA C 1 78  ? 16.701  51.777  -48.049 1.00 41.45  ?  71  ALA C CB    1 
ATOM   4964 N  N     . GLY C 1 79  ? 15.865  50.276  -50.395 1.00 45.10  ?  72  GLY C N     1 
ATOM   4965 C  CA    . GLY C 1 79  ? 15.268  49.229  -51.212 1.00 47.57  ?  72  GLY C CA    1 
ATOM   4966 C  C     . GLY C 1 79  ? 16.169  47.993  -51.219 1.00 49.38  ?  72  GLY C C     1 
ATOM   4967 O  O     . GLY C 1 79  ? 16.668  47.616  -50.170 1.00 48.65  ?  72  GLY C O     1 
ATOM   4968 N  N     . GLY C 1 80  ? 16.452  47.399  -52.394 1.00 52.17  ?  73  GLY C N     1 
ATOM   4969 C  CA    . GLY C 1 80  ? 16.141  47.976  -53.702 1.00 53.36  ?  73  GLY C CA    1 
ATOM   4970 C  C     . GLY C 1 80  ? 16.939  49.249  -53.962 1.00 51.83  ?  73  GLY C C     1 
ATOM   4971 O  O     . GLY C 1 80  ? 17.587  49.756  -53.053 1.00 49.72  ?  73  GLY C O     1 
ATOM   4972 N  N     . GLU C 1 81  ? 16.880  49.752  -55.206 1.00 53.41  ?  74  GLU C N     1 
ATOM   4973 C  CA    . GLU C 1 81  ? 17.620  50.936  -55.592 1.00 52.80  ?  74  GLU C CA    1 
ATOM   4974 C  C     . GLU C 1 81  ? 16.659  52.098  -55.697 1.00 51.29  ?  74  GLU C C     1 
ATOM   4975 O  O     . GLU C 1 81  ? 15.815  52.135  -56.587 1.00 52.92  ?  74  GLU C O     1 
ATOM   4976 C  CB    . GLU C 1 81  ? 18.335  50.786  -56.936 1.00 56.28  ?  74  GLU C CB    1 
ATOM   4977 C  CG    . GLU C 1 81  ? 19.027  52.044  -57.363 1.00 56.20  ?  74  GLU C CG    1 
ATOM   4978 C  CD    . GLU C 1 81  ? 19.767  52.769  -56.258 1.00 53.70  ?  74  GLU C CD    1 
ATOM   4979 O  OE1   . GLU C 1 81  ? 20.492  52.095  -55.468 1.00 53.52  ?  74  GLU C OE1   1 
ATOM   4980 O  OE2   . GLU C 1 81  ? 19.669  53.974  -56.222 1.00 52.52  -1 74  GLU C OE2   1 
ATOM   4981 N  N     . PRO C 1 82  ? 16.710  53.079  -54.786 1.00 48.65  ?  75  PRO C N     1 
ATOM   4982 C  CA    . PRO C 1 82  ? 15.677  54.103  -54.779 1.00 47.69  ?  75  PRO C CA    1 
ATOM   4983 C  C     . PRO C 1 82  ? 15.620  54.909  -56.071 1.00 49.48  ?  75  PRO C C     1 
ATOM   4984 O  O     . PRO C 1 82  ? 14.540  55.326  -56.477 1.00 50.08  ?  75  PRO C O     1 
ATOM   4985 C  CB    . PRO C 1 82  ? 16.050  54.957  -53.571 1.00 45.30  ?  75  PRO C CB    1 
ATOM   4986 C  CG    . PRO C 1 82  ? 16.705  53.946  -52.680 1.00 44.70  ?  75  PRO C CG    1 
ATOM   4987 C  CD    . PRO C 1 82  ? 17.602  53.173  -53.622 1.00 46.93  ?  75  PRO C CD    1 
ATOM   4988 N  N     . PHE C 1 83  ? 16.767  55.060  -56.736 1.00 50.91  ?  76  PHE C N     1 
ATOM   4989 C  CA    . PHE C 1 83  ? 16.862  56.000  -57.852 1.00 52.78  ?  76  PHE C CA    1 
ATOM   4990 C  C     . PHE C 1 83  ? 16.351  55.363  -59.140 1.00 55.88  ?  76  PHE C C     1 
ATOM   4991 O  O     . PHE C 1 83  ? 16.319  56.017  -60.184 1.00 58.05  ?  76  PHE C O     1 
ATOM   4992 C  CB    . PHE C 1 83  ? 18.284  56.558  -57.946 1.00 53.56  ?  76  PHE C CB    1 
ATOM   4993 C  CG    . PHE C 1 83  ? 18.526  57.716  -57.021 1.00 51.57  ?  76  PHE C CG    1 
ATOM   4994 C  CD1   . PHE C 1 83  ? 18.163  58.997  -57.402 1.00 52.07  ?  76  PHE C CD1   1 
ATOM   4995 C  CD2   . PHE C 1 83  ? 19.038  57.524  -55.750 1.00 49.62  ?  76  PHE C CD2   1 
ATOM   4996 C  CE1   . PHE C 1 83  ? 18.367  60.080  -56.564 1.00 50.91  ?  76  PHE C CE1   1 
ATOM   4997 C  CE2   . PHE C 1 83  ? 19.251  58.611  -54.919 1.00 48.47  ?  76  PHE C CE2   1 
ATOM   4998 C  CZ    . PHE C 1 83  ? 18.881  59.875  -55.308 1.00 49.12  ?  76  PHE C CZ    1 
ATOM   4999 N  N     . LEU C 1 84  ? 15.873  54.120  -59.082 1.00 56.57  ?  77  LEU C N     1 
ATOM   5000 C  CA    . LEU C 1 84  ? 15.043  53.606  -60.169 1.00 59.73  ?  77  LEU C CA    1 
ATOM   5001 C  C     . LEU C 1 84  ? 13.677  54.290  -60.224 1.00 59.44  ?  77  LEU C C     1 
ATOM   5002 O  O     . LEU C 1 84  ? 13.039  54.285  -61.273 1.00 62.46  ?  77  LEU C O     1 
ATOM   5003 C  CB    . LEU C 1 84  ? 14.857  52.101  -59.997 1.00 61.04  ?  77  LEU C CB    1 
ATOM   5004 C  CG    . LEU C 1 84  ? 16.091  51.273  -60.316 1.00 63.12  ?  77  LEU C CG    1 
ATOM   5005 C  CD1   . LEU C 1 84  ? 15.893  49.858  -59.814 1.00 63.93  ?  77  LEU C CD1   1 
ATOM   5006 C  CD2   . LEU C 1 84  ? 16.386  51.290  -61.814 1.00 67.50  ?  77  LEU C CD2   1 
ATOM   5007 N  N     . TYR C 1 85  ? 13.216  54.830  -59.099 1.00 56.40  ?  78  TYR C N     1 
ATOM   5008 C  CA    . TYR C 1 85  ? 11.940  55.516  -59.042 1.00 56.54  ?  78  TYR C CA    1 
ATOM   5009 C  C     . TYR C 1 85  ? 12.114  56.975  -58.644 1.00 54.77  ?  78  TYR C C     1 
ATOM   5010 O  O     . TYR C 1 85  ? 11.608  57.389  -57.591 1.00 52.88  ?  78  TYR C O     1 
ATOM   5011 C  CB    . TYR C 1 85  ? 11.078  54.824  -57.982 1.00 55.46  ?  78  TYR C CB    1 
ATOM   5012 C  CG    . TYR C 1 85  ? 10.856  53.338  -58.158 1.00 57.40  ?  78  TYR C CG    1 
ATOM   5013 C  CD1   . TYR C 1 85  ? 11.789  52.413  -57.707 1.00 56.56  ?  78  TYR C CD1   1 
ATOM   5014 C  CD2   . TYR C 1 85  ? 9.716   52.867  -58.794 1.00 60.69  ?  78  TYR C CD2   1 
ATOM   5015 C  CE1   . TYR C 1 85  ? 11.596  51.053  -57.882 1.00 58.90  ?  78  TYR C CE1   1 
ATOM   5016 C  CE2   . TYR C 1 85  ? 9.518   51.511  -58.980 1.00 63.15  ?  78  TYR C CE2   1 
ATOM   5017 C  CZ    . TYR C 1 85  ? 10.457  50.603  -58.525 1.00 62.25  ?  78  TYR C CZ    1 
ATOM   5018 O  OH    . TYR C 1 85  ? 10.281  49.254  -58.660 1.00 65.06  ?  78  TYR C OH    1 
ATOM   5019 N  N     . PRO C 1 86  ? 12.770  57.839  -59.461 1.00 55.90  ?  79  PRO C N     1 
ATOM   5020 C  CA    . PRO C 1 86  ? 12.924  59.240  -59.081 1.00 54.84  ?  79  PRO C CA    1 
ATOM   5021 C  C     . PRO C 1 86  ? 11.610  59.998  -58.865 1.00 55.28  ?  79  PRO C C     1 
ATOM   5022 O  O     . PRO C 1 86  ? 11.590  60.950  -58.099 1.00 54.05  ?  79  PRO C O     1 
ATOM   5023 C  CB    . PRO C 1 86  ? 13.771  59.852  -60.214 1.00 57.11  ?  79  PRO C CB    1 
ATOM   5024 C  CG    . PRO C 1 86  ? 13.638  58.878  -61.370 1.00 59.97  ?  79  PRO C CG    1 
ATOM   5025 C  CD    . PRO C 1 86  ? 13.471  57.516  -60.718 1.00 58.70  ?  79  PRO C CD    1 
ATOM   5026 N  N     . LYS C 1 87  ? 10.502  59.588  -59.516 1.00 57.59  ?  80  LYS C N     1 
ATOM   5027 C  CA    . LYS C 1 87  ? 9.255   60.321  -59.345 1.00 58.76  ?  80  LYS C CA    1 
ATOM   5028 C  C     . LYS C 1 87  ? 8.626   59.941  -58.005 1.00 56.98  ?  80  LYS C C     1 
ATOM   5029 O  O     . LYS C 1 87  ? 8.313   60.831  -57.234 1.00 56.33  ?  80  LYS C O     1 
ATOM   5030 C  CB    . LYS C 1 87  ? 8.270   60.139  -60.505 1.00 62.61  ?  80  LYS C CB    1 
ATOM   5031 C  CG    . LYS C 1 87  ? 6.989   60.950  -60.360 1.00 64.54  ?  80  LYS C CG    1 
ATOM   5032 C  CD    . LYS C 1 87  ? 6.026   60.858  -61.500 1.00 68.92  ?  80  LYS C CD    1 
ATOM   5033 C  CE    . LYS C 1 87  ? 4.784   61.702  -61.279 1.00 71.27  ?  80  LYS C CE    1 
ATOM   5034 N  NZ    . LYS C 1 87  ? 5.096   63.139  -61.067 1.00 70.71  ?  80  LYS C NZ    1 
ATOM   5035 N  N     . PHE C 1 88  ? 8.494   58.641  -57.732 1.00 56.63  ?  81  PHE C N     1 
ATOM   5036 C  CA    . PHE C 1 88  ? 8.079   58.158  -56.424 1.00 55.08  ?  81  PHE C CA    1 
ATOM   5037 C  C     . PHE C 1 88  ? 8.958   58.747  -55.320 1.00 51.97  ?  81  PHE C C     1 
ATOM   5038 O  O     . PHE C 1 88  ? 8.439   59.324  -54.363 1.00 51.57  ?  81  PHE C O     1 
ATOM   5039 C  CB    . PHE C 1 88  ? 8.158   56.638  -56.370 1.00 55.24  ?  81  PHE C CB    1 
ATOM   5040 C  CG    . PHE C 1 88  ? 7.567   56.015  -55.127 1.00 54.57  ?  81  PHE C CG    1 
ATOM   5041 C  CD1   . PHE C 1 88  ? 6.212   55.727  -55.031 1.00 57.31  ?  81  PHE C CD1   1 
ATOM   5042 C  CD2   . PHE C 1 88  ? 8.386   55.737  -54.048 1.00 51.72  ?  81  PHE C CD2   1 
ATOM   5043 C  CE1   . PHE C 1 88  ? 5.694   55.157  -53.878 1.00 57.21  ?  81  PHE C CE1   1 
ATOM   5044 C  CE2   . PHE C 1 88  ? 7.876   55.147  -52.902 1.00 51.47  ?  81  PHE C CE2   1 
ATOM   5045 C  CZ    . PHE C 1 88  ? 6.529   54.845  -52.826 1.00 54.25  ?  81  PHE C CZ    1 
ATOM   5046 N  N     . LEU C 1 89  ? 10.286  58.591  -55.466 1.00 50.41  ?  82  LEU C N     1 
ATOM   5047 C  CA    . LEU C 1 89  ? 11.226  59.043  -54.433 1.00 47.99  ?  82  LEU C CA    1 
ATOM   5048 C  C     . LEU C 1 89  ? 11.073  60.545  -54.175 1.00 48.29  ?  82  LEU C C     1 
ATOM   5049 O  O     . LEU C 1 89  ? 10.924  60.962  -53.019 1.00 47.38  ?  82  LEU C O     1 
ATOM   5050 C  CB    . LEU C 1 89  ? 12.661  58.645  -54.837 1.00 47.35  ?  82  LEU C CB    1 
ATOM   5051 C  CG    . LEU C 1 89  ? 13.762  59.089  -53.870 1.00 45.56  ?  82  LEU C CG    1 
ATOM   5052 C  CD1   . LEU C 1 89  ? 13.667  58.311  -52.562 1.00 43.88  ?  82  LEU C CD1   1 
ATOM   5053 C  CD2   . LEU C 1 89  ? 15.155  58.904  -54.475 1.00 46.04  ?  82  LEU C CD2   1 
ATOM   5054 N  N     . GLY C 1 90  ? 11.100  61.373  -55.235 1.00 50.06  ?  83  GLY C N     1 
ATOM   5055 C  CA    . GLY C 1 90  ? 10.870  62.805  -55.137 1.00 51.15  ?  83  GLY C CA    1 
ATOM   5056 C  C     . GLY C 1 90  ? 9.559   63.172  -54.423 1.00 52.13  ?  83  GLY C C     1 
ATOM   5057 O  O     . GLY C 1 90  ? 9.543   64.035  -53.552 1.00 52.14  ?  83  GLY C O     1 
ATOM   5058 N  N     . GLU C 1 91  ? 8.462   62.499  -54.776 1.00 53.54  ?  84  GLU C N     1 
ATOM   5059 C  CA    . GLU C 1 91  ? 7.169   62.735  -54.143 1.00 55.27  ?  84  GLU C CA    1 
ATOM   5060 C  C     . GLU C 1 91  ? 7.191   62.384  -52.649 1.00 53.58  ?  84  GLU C C     1 
ATOM   5061 O  O     . GLU C 1 91  ? 6.540   63.055  -51.844 1.00 54.91  ?  84  GLU C O     1 
ATOM   5062 C  CB    . GLU C 1 91  ? 6.091   61.854  -54.772 1.00 57.49  ?  84  GLU C CB    1 
ATOM   5063 C  CG    . GLU C 1 91  ? 5.426   62.425  -56.008 1.00 60.83  ?  84  GLU C CG    1 
ATOM   5064 C  CD    . GLU C 1 91  ? 4.126   61.691  -56.300 1.00 63.94  ?  84  GLU C CD    1 
ATOM   5065 O  OE1   . GLU C 1 91  ? 3.192   61.796  -55.463 1.00 65.43  ?  84  GLU C OE1   1 
ATOM   5066 O  OE2   . GLU C 1 91  ? 4.071   60.962  -57.313 1.00 65.28  -1 84  GLU C OE2   1 
ATOM   5067 N  N     . MET C 1 92  ? 7.846   61.270  -52.291 1.00 51.27  ?  85  MET C N     1 
ATOM   5068 C  CA    . MET C 1 92  ? 7.829   60.805  -50.908 1.00 50.06  ?  85  MET C CA    1 
ATOM   5069 C  C     . MET C 1 92  ? 8.688   61.726  -50.043 1.00 48.81  ?  85  MET C C     1 
ATOM   5070 O  O     . MET C 1 92  ? 8.332   62.010  -48.904 1.00 49.30  ?  85  MET C O     1 
ATOM   5071 C  CB    . MET C 1 92  ? 8.306   59.363  -50.771 1.00 48.44  ?  85  MET C CB    1 
ATOM   5072 C  CG    . MET C 1 92  ? 7.369   58.338  -51.387 1.00 50.35  ?  85  MET C CG    1 
ATOM   5073 S  SD    . MET C 1 92  ? 5.661   58.448  -50.796 1.00 53.65  ?  85  MET C SD    1 
ATOM   5074 C  CE    . MET C 1 92  ? 4.901   59.355  -52.142 1.00 56.63  ?  85  MET C CE    1 
ATOM   5075 N  N     A ILE C 1 93  ? 9.818   62.226  -50.567 0.39 47.81  ?  86  ILE C N     1 
ATOM   5076 N  N     B ILE C 1 93  ? 9.817   62.172  -50.611 0.61 47.78  ?  86  ILE C N     1 
ATOM   5077 C  CA    A ILE C 1 93  ? 10.700  63.039  -49.741 0.39 47.17  ?  86  ILE C CA    1 
ATOM   5078 C  CA    B ILE C 1 93  ? 10.745  63.037  -49.909 0.61 47.18  ?  86  ILE C CA    1 
ATOM   5079 C  C     A ILE C 1 93  ? 10.097  64.425  -49.557 0.39 49.56  ?  86  ILE C C     1 
ATOM   5080 C  C     B ILE C 1 93  ? 10.036  64.336  -49.572 0.61 49.52  ?  86  ILE C C     1 
ATOM   5081 O  O     A ILE C 1 93  ? 10.274  65.032  -48.502 0.39 50.06  ?  86  ILE C O     1 
ATOM   5082 O  O     B ILE C 1 93  ? 10.075  64.778  -48.432 0.61 49.93  ?  86  ILE C O     1 
ATOM   5083 C  CB    A ILE C 1 93  ? 12.135  63.116  -50.304 0.39 46.10  ?  86  ILE C CB    1 
ATOM   5084 C  CB    B ILE C 1 93  ? 12.019  63.266  -50.750 0.61 46.59  ?  86  ILE C CB    1 
ATOM   5085 C  CG1   A ILE C 1 93  ? 12.158  63.637  -51.741 0.39 47.51  ?  86  ILE C CG1   1 
ATOM   5086 C  CG1   B ILE C 1 93  ? 12.985  62.084  -50.613 0.61 44.62  ?  86  ILE C CG1   1 
ATOM   5087 C  CG2   A ILE C 1 93  ? 12.838  61.773  -50.173 0.39 44.19  ?  86  ILE C CG2   1 
ATOM   5088 C  CG2   B ILE C 1 93  ? 12.702  64.572  -50.383 0.61 47.55  ?  86  ILE C CG2   1 
ATOM   5089 C  CD1   A ILE C 1 93  ? 13.520  63.568  -52.401 0.39 47.15  ?  86  ILE C CD1   1 
ATOM   5090 C  CD1   B ILE C 1 93  ? 14.041  62.049  -51.680 0.61 44.84  ?  86  ILE C CD1   1 
ATOM   5091 N  N     . ASP C 1 94  ? 9.444   64.951  -50.603 1.00 51.50  ?  87  ASP C N     1 
ATOM   5092 C  CA    . ASP C 1 94  ? 8.789   66.242  -50.498 1.00 54.38  ?  87  ASP C CA    1 
ATOM   5093 C  C     . ASP C 1 94  ? 7.660   66.136  -49.470 1.00 55.90  ?  87  ASP C C     1 
ATOM   5094 O  O     . ASP C 1 94  ? 7.513   67.026  -48.639 1.00 57.72  ?  87  ASP C O     1 
ATOM   5095 C  CB    . ASP C 1 94  ? 8.310   66.736  -51.875 1.00 56.50  ?  87  ASP C CB    1 
ATOM   5096 C  CG    . ASP C 1 94  ? 9.404   67.104  -52.879 1.00 56.10  ?  87  ASP C CG    1 
ATOM   5097 O  OD1   . ASP C 1 94  ? 10.550  67.332  -52.456 1.00 54.85  -1 87  ASP C OD1   1 
ATOM   5098 O  OD2   . ASP C 1 94  ? 9.094   67.189  -54.106 1.00 57.61  ?  87  ASP C OD2   1 
ATOM   5099 N  N     . PHE C 1 95  ? 6.890   65.039  -49.513 1.00 55.70  ?  88  PHE C N     1 
ATOM   5100 C  CA    . PHE C 1 95  ? 5.775   64.830  -48.604 1.00 57.76  ?  88  PHE C CA    1 
ATOM   5101 C  C     . PHE C 1 95  ? 6.298   64.663  -47.178 1.00 56.52  ?  88  PHE C C     1 
ATOM   5102 O  O     . PHE C 1 95  ? 5.707   65.183  -46.249 1.00 58.99  ?  88  PHE C O     1 
ATOM   5103 C  CB    . PHE C 1 95  ? 4.937   63.620  -49.049 1.00 58.22  ?  88  PHE C CB    1 
ATOM   5104 C  CG    . PHE C 1 95  ? 3.778   63.244  -48.152 1.00 60.87  ?  88  PHE C CG    1 
ATOM   5105 C  CD1   . PHE C 1 95  ? 2.587   63.955  -48.192 1.00 65.21  ?  88  PHE C CD1   1 
ATOM   5106 C  CD2   . PHE C 1 95  ? 3.870   62.169  -47.271 1.00 59.59  ?  88  PHE C CD2   1 
ATOM   5107 C  CE1   . PHE C 1 95  ? 1.524   63.609  -47.365 1.00 68.37  ?  88  PHE C CE1   1 
ATOM   5108 C  CE2   . PHE C 1 95  ? 2.803   61.823  -46.449 1.00 62.62  ?  88  PHE C CE2   1 
ATOM   5109 C  CZ    . PHE C 1 95  ? 1.633   62.548  -46.496 1.00 67.10  ?  88  PHE C CZ    1 
ATOM   5110 N  N     . CYS C 1 96  ? 7.418   63.941  -46.999 1.00 53.21  ?  89  CYS C N     1 
ATOM   5111 C  CA    . CYS C 1 96  ? 7.961   63.717  -45.665 1.00 52.29  ?  89  CYS C CA    1 
ATOM   5112 C  C     . CYS C 1 96  ? 8.446   65.013  -45.029 1.00 53.68  ?  89  CYS C C     1 
ATOM   5113 O  O     . CYS C 1 96  ? 8.102   65.323  -43.887 1.00 55.61  ?  89  CYS C O     1 
ATOM   5114 C  CB    . CYS C 1 96  ? 9.093   62.706  -45.687 1.00 49.00  ?  89  CYS C CB    1 
ATOM   5115 S  SG    . CYS C 1 96  ? 8.392   61.042  -45.706 1.00 48.46  ?  89  CYS C SG    1 
ATOM   5116 N  N     . LYS C 1 97  ? 9.265   65.762  -45.771 1.00 53.23  ?  90  LYS C N     1 
ATOM   5117 C  CA    . LYS C 1 97  ? 9.838   66.978  -45.217 1.00 54.98  ?  90  LYS C CA    1 
ATOM   5118 C  C     . LYS C 1 97  ? 8.757   68.054  -45.071 1.00 59.00  ?  90  LYS C C     1 
ATOM   5119 O  O     . LYS C 1 97  ? 8.672   68.678  -44.016 1.00 61.41  ?  90  LYS C O     1 
ATOM   5120 C  CB    . LYS C 1 97  ? 11.024  67.435  -46.082 1.00 53.99  ?  90  LYS C CB    1 
ATOM   5121 C  CG    . LYS C 1 97  ? 12.010  68.374  -45.391 1.00 55.44  ?  90  LYS C CG    1 
ATOM   5122 C  CD    . LYS C 1 97  ? 12.720  67.716  -44.226 1.00 54.15  ?  90  LYS C CD    1 
ATOM   5123 C  CE    . LYS C 1 97  ? 13.192  68.665  -43.141 1.00 56.97  ?  90  LYS C CE    1 
ATOM   5124 N  NZ    . LYS C 1 97  ? 13.638  67.935  -41.920 1.00 56.19  ?  90  LYS C NZ    1 
ATOM   5125 N  N     . GLU C 1 98  ? 7.928   68.281  -46.110 1.00 60.28  ?  91  GLU C N     1 
ATOM   5126 C  CA    . GLU C 1 98  ? 7.077   69.472  -46.142 1.00 64.62  ?  91  GLU C CA    1 
ATOM   5127 C  C     . GLU C 1 98  ? 5.774   69.269  -45.368 1.00 67.48  ?  91  GLU C C     1 
ATOM   5128 O  O     . GLU C 1 98  ? 5.382   70.150  -44.610 1.00 71.24  ?  91  GLU C O     1 
ATOM   5129 C  CB    . GLU C 1 98  ? 6.702   69.884  -47.569 1.00 65.65  ?  91  GLU C CB    1 
ATOM   5130 C  CG    . GLU C 1 98  ? 7.832   70.513  -48.365 1.00 64.78  ?  91  GLU C CG    1 
ATOM   5131 C  CD    . GLU C 1 98  ? 7.519   70.749  -49.839 1.00 65.70  ?  91  GLU C CD    1 
ATOM   5132 O  OE1   . GLU C 1 98  ? 8.367   71.357  -50.525 1.00 65.83  ?  91  GLU C OE1   1 
ATOM   5133 O  OE2   . GLU C 1 98  ? 6.440   70.314  -50.309 1.00 66.72  -1 91  GLU C OE2   1 
ATOM   5134 N  N     . THR C 1 99  ? 5.091   68.137  -45.608 1.00 66.38  ?  92  THR C N     1 
ATOM   5135 C  CA    . THR C 1 99  ? 3.785   67.850  -45.025 1.00 69.67  ?  92  THR C CA    1 
ATOM   5136 C  C     . THR C 1 99  ? 3.910   67.263  -43.615 1.00 69.37  ?  92  THR C C     1 
ATOM   5137 O  O     . THR C 1 99  ? 3.198   67.681  -42.699 1.00 73.35  ?  92  THR C O     1 
ATOM   5138 C  CB    . THR C 1 99  ? 2.977   66.887  -45.907 1.00 69.47  ?  92  THR C CB    1 
ATOM   5139 O  OG1   . THR C 1 99  ? 2.753   67.517  -47.170 1.00 70.67  ?  92  THR C OG1   1 
ATOM   5140 C  CG2   . THR C 1 99  ? 1.647   66.519  -45.290 1.00 73.42  ?  92  THR C CG2   1 
ATOM   5141 N  N     . LEU C 1 100 ? 4.769   66.247  -43.455 1.00 65.17  ?  93  LEU C N     1 
ATOM   5142 C  CA    . LEU C 1 100 ? 4.913   65.563  -42.179 1.00 64.87  ?  93  LEU C CA    1 
ATOM   5143 C  C     . LEU C 1 100 ? 5.949   66.267  -41.298 1.00 64.69  ?  93  LEU C C     1 
ATOM   5144 O  O     . LEU C 1 100 ? 6.024   65.969  -40.106 1.00 65.59  ?  93  LEU C O     1 
ATOM   5145 C  CB    . LEU C 1 100 ? 5.295   64.097  -42.433 1.00 61.12  ?  93  LEU C CB    1 
ATOM   5146 C  CG    . LEU C 1 100 ? 4.228   63.215  -43.088 1.00 62.07  ?  93  LEU C CG    1 
ATOM   5147 C  CD1   . LEU C 1 100 ? 4.711   61.775  -43.224 1.00 58.87  ?  93  LEU C CD1   1 
ATOM   5148 C  CD2   . LEU C 1 100 ? 2.917   63.247  -42.304 1.00 66.80  ?  93  LEU C CD2   1 
ATOM   5149 N  N     . GLN C 1 101 ? 6.769   67.166  -41.881 1.00 63.94  ?  94  GLN C N     1 
ATOM   5150 C  CA    . GLN C 1 101 ? 7.765   67.930  -41.129 1.00 64.57  ?  94  GLN C CA    1 
ATOM   5151 C  C     . GLN C 1 101 ? 8.597   66.997  -40.252 1.00 62.11  ?  94  GLN C C     1 
ATOM   5152 O  O     . GLN C 1 101 ? 8.869   67.311  -39.093 1.00 64.16  ?  94  GLN C O     1 
ATOM   5153 C  CB    . GLN C 1 101 ? 7.083   69.024  -40.301 1.00 69.88  ?  94  GLN C CB    1 
ATOM   5154 C  CG    . GLN C 1 101 ? 6.179   69.926  -41.137 1.00 72.98  ?  94  GLN C CG    1 
ATOM   5155 C  CD    . GLN C 1 101 ? 5.602   71.080  -40.357 1.00 78.84  ?  94  GLN C CD    1 
ATOM   5156 O  OE1   . GLN C 1 101 ? 4.407   71.128  -40.075 1.00 82.57  ?  94  GLN C OE1   1 
ATOM   5157 N  NE2   . GLN C 1 101 ? 6.455   72.028  -40.004 1.00 80.32  ?  94  GLN C NE2   1 
ATOM   5158 N  N     . LEU C 1 102 ? 9.024   65.858  -40.833 1.00 58.16  ?  95  LEU C N     1 
ATOM   5159 C  CA    . LEU C 1 102 ? 9.964   64.938  -40.198 1.00 55.72  ?  95  LEU C CA    1 
ATOM   5160 C  C     . LEU C 1 102 ? 11.290  65.637  -39.909 1.00 55.70  ?  95  LEU C C     1 
ATOM   5161 O  O     . LEU C 1 102 ? 11.681  66.550  -40.634 1.00 56.18  ?  95  LEU C O     1 
ATOM   5162 C  CB    . LEU C 1 102 ? 10.229  63.749  -41.131 1.00 52.11  ?  95  LEU C CB    1 
ATOM   5163 C  CG    . LEU C 1 102 ? 9.104   62.727  -41.278 1.00 52.18  ?  95  LEU C CG    1 
ATOM   5164 C  CD1   . LEU C 1 102 ? 9.601   61.526  -42.069 1.00 49.04  ?  95  LEU C CD1   1 
ATOM   5165 C  CD2   . LEU C 1 102 ? 8.558   62.275  -39.931 1.00 54.15  ?  95  LEU C CD2   1 
ATOM   5166 N  N     . GLU C 1 103 ? 12.001  65.154  -38.874 1.00 55.45  ?  96  GLU C N     1 
ATOM   5167 C  CA    . GLU C 1 103 ? 13.237  65.799  -38.461 1.00 56.31  ?  96  GLU C CA    1 
ATOM   5168 C  C     . GLU C 1 103 ? 14.327  65.483  -39.480 1.00 53.44  ?  96  GLU C C     1 
ATOM   5169 O  O     . GLU C 1 103 ? 15.107  66.378  -39.801 1.00 54.61  ?  96  GLU C O     1 
ATOM   5170 C  CB    . GLU C 1 103 ? 13.661  65.392  -37.043 1.00 57.55  ?  96  GLU C CB    1 
ATOM   5171 C  CG    . GLU C 1 103 ? 12.714  65.851  -35.941 1.00 61.46  ?  96  GLU C CG    1 
ATOM   5172 C  CD    . GLU C 1 103 ? 13.214  65.607  -34.522 1.00 63.51  ?  96  GLU C CD    1 
ATOM   5173 O  OE1   . GLU C 1 103 ? 14.418  65.266  -34.372 1.00 62.22  ?  96  GLU C OE1   1 
ATOM   5174 O  OE2   . GLU C 1 103 ? 12.401  65.775  -33.556 1.00 66.96  -1 96  GLU C OE2   1 
ATOM   5175 N  N     . SER C 1 104 ? 14.347  64.226  -39.990 1.00 50.33  ?  97  SER C N     1 
ATOM   5176 C  CA    . SER C 1 104 ? 15.419  63.743  -40.862 1.00 48.10  ?  97  SER C CA    1 
ATOM   5177 C  C     . SER C 1 104 ? 14.922  62.836  -41.994 1.00 45.72  ?  97  SER C C     1 
ATOM   5178 O  O     . SER C 1 104 ? 14.205  61.835  -41.774 1.00 44.83  ?  97  SER C O     1 
ATOM   5179 C  CB    . SER C 1 104 ? 16.470  63.019  -40.063 1.00 47.67  ?  97  SER C CB    1 
ATOM   5180 O  OG    . SER C 1 104 ? 17.465  62.477  -40.912 1.00 46.07  ?  97  SER C OG    1 
ATOM   5181 N  N     . VAL C 1 105 ? 15.334  63.197  -43.215 1.00 45.24  ?  98  VAL C N     1 
ATOM   5182 C  CA    . VAL C 1 105 ? 15.007  62.455  -44.427 1.00 43.63  ?  98  VAL C CA    1 
ATOM   5183 C  C     . VAL C 1 105 ? 16.311  62.087  -45.128 1.00 42.82  ?  98  VAL C C     1 
ATOM   5184 O  O     . VAL C 1 105 ? 17.091  62.949  -45.499 1.00 43.96  ?  98  VAL C O     1 
ATOM   5185 C  CB    . VAL C 1 105 ? 14.068  63.245  -45.360 1.00 44.68  ?  98  VAL C CB    1 
ATOM   5186 C  CG1   . VAL C 1 105 ? 13.789  62.473  -46.644 1.00 43.57  ?  98  VAL C CG1   1 
ATOM   5187 C  CG2   . VAL C 1 105 ? 12.774  63.623  -44.670 1.00 46.27  ?  98  VAL C CG2   1 
ATOM   5188 N  N     . SER C 1 106 ? 16.572  60.784  -45.249 1.00 41.40  ?  99  SER C N     1 
ATOM   5189 C  CA    . SER C 1 106 ? 17.823  60.307  -45.806 1.00 41.23  ?  99  SER C CA    1 
ATOM   5190 C  C     . SER C 1 106 ? 17.488  59.328  -46.913 1.00 40.45  ?  99  SER C C     1 
ATOM   5191 O  O     . SER C 1 106 ? 16.371  58.807  -46.952 1.00 39.93  ?  99  SER C O     1 
ATOM   5192 C  CB    . SER C 1 106 ? 18.762  59.659  -44.778 1.00 41.26  ?  99  SER C CB    1 
ATOM   5193 O  OG    . SER C 1 106 ? 18.161  58.547  -44.110 1.00 40.28  ?  99  SER C OG    1 
ATOM   5194 N  N     . ILE C 1 107 ? 18.461  59.108  -47.805 1.00 41.03  ?  100 ILE C N     1 
ATOM   5195 C  CA    . ILE C 1 107 ? 18.347  58.113  -48.871 1.00 41.02  ?  100 ILE C CA    1 
ATOM   5196 C  C     . ILE C 1 107 ? 19.629  57.291  -48.894 1.00 41.74  ?  100 ILE C C     1 
ATOM   5197 O  O     . ILE C 1 107 ? 20.693  57.839  -48.678 1.00 42.80  ?  100 ILE C O     1 
ATOM   5198 C  CB    . ILE C 1 107 ? 18.133  58.822  -50.220 1.00 42.09  ?  100 ILE C CB    1 
ATOM   5199 C  CG1   . ILE C 1 107 ? 17.011  59.856  -50.147 1.00 42.06  ?  100 ILE C CG1   1 
ATOM   5200 C  CG2   . ILE C 1 107 ? 17.929  57.856  -51.377 1.00 42.73  ?  100 ILE C CG2   1 
ATOM   5201 C  CD1   . ILE C 1 107 ? 17.115  60.847  -51.242 1.00 43.59  ?  100 ILE C CD1   1 
ATOM   5202 N  N     . VAL C 1 108 ? 19.524  55.993  -49.172 1.00 41.75  ?  101 VAL C N     1 
ATOM   5203 C  CA    . VAL C 1 108 ? 20.699  55.169  -49.413 1.00 43.18  ?  101 VAL C CA    1 
ATOM   5204 C  C     . VAL C 1 108 ? 20.653  54.648  -50.850 1.00 44.70  ?  101 VAL C C     1 
ATOM   5205 O  O     . VAL C 1 108 ? 19.662  54.078  -51.273 1.00 44.44  ?  101 VAL C O     1 
ATOM   5206 C  CB    . VAL C 1 108 ? 20.832  54.028  -48.393 1.00 42.82  ?  101 VAL C CB    1 
ATOM   5207 C  CG1   . VAL C 1 108 ? 19.592  53.178  -48.371 1.00 42.02  ?  101 VAL C CG1   1 
ATOM   5208 C  CG2   . VAL C 1 108 ? 22.078  53.166  -48.636 1.00 44.94  ?  101 VAL C CG2   1 
ATOM   5209 N  N     . THR C 1 109 ? 21.757  54.831  -51.591 1.00 46.91  ?  102 THR C N     1 
ATOM   5210 C  CA    . THR C 1 109 ? 21.820  54.503  -53.005 1.00 49.10  ?  102 THR C CA    1 
ATOM   5211 C  C     . THR C 1 109 ? 23.189  53.929  -53.378 1.00 52.18  ?  102 THR C C     1 
ATOM   5212 O  O     . THR C 1 109 ? 24.192  54.288  -52.776 1.00 52.92  ?  102 THR C O     1 
ATOM   5213 C  CB    . THR C 1 109 ? 21.637  55.764  -53.866 1.00 49.72  ?  102 THR C CB    1 
ATOM   5214 O  OG1   . THR C 1 109 ? 21.754  55.388  -55.238 1.00 52.39  ?  102 THR C OG1   1 
ATOM   5215 C  CG2   . THR C 1 109 ? 22.625  56.876  -53.576 1.00 50.63  ?  102 THR C CG2   1 
ATOM   5216 N  N     . ASN C 1 110 ? 23.215  53.159  -54.465 1.00 54.62  ?  103 ASN C N     1 
ATOM   5217 C  CA    . ASN C 1 110 ? 24.465  52.819  -55.139 1.00 58.62  ?  103 ASN C CA    1 
ATOM   5218 C  C     . ASN C 1 110 ? 25.080  54.014  -55.878 1.00 60.59  ?  103 ASN C C     1 
ATOM   5219 O  O     . ASN C 1 110 ? 26.278  54.015  -56.182 1.00 64.13  ?  103 ASN C O     1 
ATOM   5220 C  CB    . ASN C 1 110 ? 24.280  51.646  -56.098 1.00 61.39  ?  103 ASN C CB    1 
ATOM   5221 C  CG    . ASN C 1 110 ? 23.288  51.899  -57.216 1.00 61.74  ?  103 ASN C CG    1 
ATOM   5222 O  OD1   . ASN C 1 110 ? 23.343  52.932  -57.877 1.00 62.38  ?  103 ASN C OD1   1 
ATOM   5223 N  ND2   . ASN C 1 110 ? 22.408  50.947  -57.449 1.00 61.92  ?  103 ASN C ND2   1 
ATOM   5224 N  N     . GLY C 1 111 ? 24.284  55.027  -56.197 1.00 58.97  ?  104 GLY C N     1 
ATOM   5225 C  CA    . GLY C 1 111 ? 24.845  56.302  -56.624 1.00 60.62  ?  104 GLY C CA    1 
ATOM   5226 C  C     . GLY C 1 111 ? 24.994  56.400  -58.143 1.00 64.34  ?  104 GLY C C     1 
ATOM   5227 O  O     . GLY C 1 111 ? 25.271  57.477  -58.672 1.00 66.04  ?  104 GLY C O     1 
ATOM   5228 N  N     . SER C 1 112 ? 24.793  55.277  -58.840 1.00 66.05  ?  105 SER C N     1 
ATOM   5229 C  CA    . SER C 1 112 ? 25.059  55.236  -60.272 1.00 70.50  ?  105 SER C CA    1 
ATOM   5230 C  C     . SER C 1 112 ? 24.027  56.068  -61.034 1.00 69.85  ?  105 SER C C     1 
ATOM   5231 O  O     . SER C 1 112 ? 24.376  56.671  -62.043 1.00 73.29  ?  105 SER C O     1 
ATOM   5232 C  CB    . SER C 1 112 ? 25.101  53.818  -60.800 1.00 73.16  ?  105 SER C CB    1 
ATOM   5233 O  OG    . SER C 1 112 ? 23.843  53.179  -60.673 1.00 70.60  ?  105 SER C OG    1 
ATOM   5234 N  N     . LEU C 1 113 ? 22.779  56.100  -60.525 1.00 65.91  ?  106 LEU C N     1 
ATOM   5235 C  CA    . LEU C 1 113 ? 21.645  56.686  -61.228 1.00 65.63  ?  106 LEU C CA    1 
ATOM   5236 C  C     . LEU C 1 113 ? 21.231  58.032  -60.634 1.00 62.98  ?  106 LEU C C     1 
ATOM   5237 O  O     . LEU C 1 113 ? 20.191  58.558  -61.013 1.00 62.47  ?  106 LEU C O     1 
ATOM   5238 C  CB    . LEU C 1 113 ? 20.457  55.718  -61.167 1.00 64.22  ?  106 LEU C CB    1 
ATOM   5239 C  CG    . LEU C 1 113 ? 20.649  54.377  -61.863 1.00 67.50  ?  106 LEU C CG    1 
ATOM   5240 C  CD1   . LEU C 1 113 ? 19.506  53.428  -61.541 1.00 66.09  ?  106 LEU C CD1   1 
ATOM   5241 C  CD2   . LEU C 1 113 ? 20.762  54.571  -63.372 1.00 72.18  ?  106 LEU C CD2   1 
ATOM   5242 N  N     A VAL C 1 114 ? 22.025  58.604  -59.722 0.32 61.88  ?  107 VAL C N     1 
ATOM   5243 N  N     B VAL C 1 114 ? 22.045  58.566  -59.715 0.68 61.90  ?  107 VAL C N     1 
ATOM   5244 C  CA    A VAL C 1 114 ? 21.685  59.917  -59.197 0.32 60.24  ?  107 VAL C CA    1 
ATOM   5245 C  CA    B VAL C 1 114 ? 21.866  59.908  -59.182 0.68 60.50  ?  107 VAL C CA    1 
ATOM   5246 C  C     A VAL C 1 114 ? 22.244  60.984  -60.137 0.32 63.79  ?  107 VAL C C     1 
ATOM   5247 C  C     B VAL C 1 114 ? 22.190  60.906  -60.296 0.68 64.05  ?  107 VAL C C     1 
ATOM   5248 O  O     A VAL C 1 114 ? 23.383  60.892  -60.590 0.32 67.07  ?  107 VAL C O     1 
ATOM   5249 O  O     B VAL C 1 114 ? 23.123  60.659  -61.057 0.68 67.66  ?  107 VAL C O     1 
ATOM   5250 C  CB    A VAL C 1 114 ? 22.158  60.123  -57.745 0.32 57.89  ?  107 VAL C CB    1 
ATOM   5251 C  CB    B VAL C 1 114 ? 22.762  60.123  -57.942 0.68 59.38  ?  107 VAL C CB    1 
ATOM   5252 C  CG1   A VAL C 1 114 ? 23.670  60.169  -57.631 0.32 60.50  ?  107 VAL C CG1   1 
ATOM   5253 C  CG1   B VAL C 1 114 ? 22.600  61.514  -57.335 0.68 58.55  ?  107 VAL C CG1   1 
ATOM   5254 C  CG2   A VAL C 1 114 ? 21.543  61.377  -57.140 0.32 56.31  ?  107 VAL C CG2   1 
ATOM   5255 C  CG2   B VAL C 1 114 ? 22.525  59.052  -56.891 0.68 56.48  ?  107 VAL C CG2   1 
ATOM   5256 N  N     . LYS C 1 115 ? 21.419  62.005  -60.390 1.00 63.53  ?  108 LYS C N     1 
ATOM   5257 C  CA    . LYS C 1 115 ? 21.729  63.112  -61.286 1.00 67.00  ?  108 LYS C CA    1 
ATOM   5258 C  C     . LYS C 1 115 ? 21.594  64.438  -60.554 1.00 66.18  ?  108 LYS C C     1 
ATOM   5259 O  O     . LYS C 1 115 ? 20.787  64.566  -59.638 1.00 62.98  ?  108 LYS C O     1 
ATOM   5260 C  CB    . LYS C 1 115 ? 20.757  63.153  -62.470 1.00 68.57  ?  108 LYS C CB    1 
ATOM   5261 C  CG    . LYS C 1 115 ? 20.799  61.955  -63.407 1.00 70.59  ?  108 LYS C CG    1 
ATOM   5262 C  CD    . LYS C 1 115 ? 20.023  62.196  -64.690 1.00 73.43  ?  108 LYS C CD    1 
ATOM   5263 C  CE    . LYS C 1 115 ? 19.848  60.953  -65.536 1.00 75.54  ?  108 LYS C CE    1 
ATOM   5264 N  NZ    . LYS C 1 115 ? 19.086  61.242  -66.775 1.00 78.83  ?  108 LYS C NZ    1 
ATOM   5265 N  N     . GLU C 1 116 ? 22.343  65.448  -61.018 1.00 69.75  ?  109 GLU C N     1 
ATOM   5266 C  CA    . GLU C 1 116 ? 22.396  66.723  -60.335 1.00 69.98  ?  109 GLU C CA    1 
ATOM   5267 C  C     . GLU C 1 116 ? 20.998  67.334  -60.249 1.00 68.30  ?  109 GLU C C     1 
ATOM   5268 O  O     . GLU C 1 116 ? 20.622  67.895  -59.219 1.00 66.53  ?  109 GLU C O     1 
ATOM   5269 C  CB    . GLU C 1 116 ? 23.416  67.649  -61.012 1.00 75.02  ?  109 GLU C CB    1 
ATOM   5270 C  CG    . GLU C 1 116 ? 23.656  68.919  -60.229 1.00 76.04  ?  109 GLU C CG    1 
ATOM   5271 C  CD    . GLU C 1 116 ? 24.767  69.849  -60.697 1.00 81.52  ?  109 GLU C CD    1 
ATOM   5272 O  OE1   . GLU C 1 116 ? 25.510  69.480  -61.632 1.00 84.85  ?  109 GLU C OE1   1 
ATOM   5273 O  OE2   . GLU C 1 116 ? 24.908  70.917  -60.090 1.00 82.90  -1 109 GLU C OE2   1 
ATOM   5274 N  N     . GLN C 1 117 ? 20.229  67.204  -61.342 1.00 69.40  ?  110 GLN C N     1 
ATOM   5275 C  CA    . GLN C 1 117 ? 18.904  67.783  -61.429 1.00 68.82  ?  110 GLN C CA    1 
ATOM   5276 C  C     . GLN C 1 117 ? 18.034  67.261  -60.285 1.00 64.64  ?  110 GLN C C     1 
ATOM   5277 O  O     . GLN C 1 117 ? 17.190  67.992  -59.774 1.00 64.12  ?  110 GLN C O     1 
ATOM   5278 C  CB    . GLN C 1 117 ? 18.276  67.509  -62.802 1.00 71.05  ?  110 GLN C CB    1 
ATOM   5279 C  CG    . GLN C 1 117 ? 18.207  66.038  -63.183 1.00 70.03  ?  110 GLN C CG    1 
ATOM   5280 C  CD    . GLN C 1 117 ? 17.545  65.834  -64.527 1.00 72.91  ?  110 GLN C CD    1 
ATOM   5281 O  OE1   . GLN C 1 117 ? 17.845  66.521  -65.500 1.00 76.79  ?  110 GLN C OE1   1 
ATOM   5282 N  NE2   . GLN C 1 117 ? 16.615  64.895  -64.595 1.00 71.53  ?  110 GLN C NE2   1 
ATOM   5283 N  N     . PHE C 1 118 ? 18.234  65.995  -59.895 1.00 62.22  ?  111 PHE C N     1 
ATOM   5284 C  CA    . PHE C 1 118 ? 17.448  65.466  -58.801 1.00 58.73  ?  111 PHE C CA    1 
ATOM   5285 C  C     . PHE C 1 118 ? 17.797  66.199  -57.510 1.00 57.64  ?  111 PHE C C     1 
ATOM   5286 O  O     . PHE C 1 118 ? 16.900  66.548  -56.759 1.00 56.40  ?  111 PHE C O     1 
ATOM   5287 C  CB    . PHE C 1 118 ? 17.597  63.951  -58.679 1.00 56.91  ?  111 PHE C CB    1 
ATOM   5288 C  CG    . PHE C 1 118 ? 16.660  63.352  -57.665 1.00 53.91  ?  111 PHE C CG    1 
ATOM   5289 C  CD1   . PHE C 1 118 ? 16.954  63.386  -56.315 1.00 51.80  ?  111 PHE C CD1   1 
ATOM   5290 C  CD2   . PHE C 1 118 ? 15.441  62.823  -58.064 1.00 53.85  ?  111 PHE C CD2   1 
ATOM   5291 C  CE1   . PHE C 1 118 ? 16.079  62.829  -55.394 1.00 49.58  ?  111 PHE C CE1   1 
ATOM   5292 C  CE2   . PHE C 1 118 ? 14.575  62.258  -57.139 1.00 51.75  ?  111 PHE C CE2   1 
ATOM   5293 C  CZ    . PHE C 1 118 ? 14.898  62.264  -55.809 1.00 49.60  ?  111 PHE C CZ    1 
ATOM   5294 N  N     . LEU C 1 119 ? 19.080  66.494  -57.275 1.00 58.83  ?  112 LEU C N     1 
ATOM   5295 C  CA    . LEU C 1 119 ? 19.489  67.115  -56.013 1.00 58.33  ?  112 LEU C CA    1 
ATOM   5296 C  C     . LEU C 1 119 ? 19.099  68.597  -55.949 1.00 60.54  ?  112 LEU C C     1 
ATOM   5297 O  O     . LEU C 1 119 ? 18.692  69.100  -54.893 1.00 59.86  ?  112 LEU C O     1 
ATOM   5298 C  CB    . LEU C 1 119 ? 20.987  66.862  -55.834 1.00 59.59  ?  112 LEU C CB    1 
ATOM   5299 C  CG    . LEU C 1 119 ? 21.404  65.391  -55.862 1.00 57.98  ?  112 LEU C CG    1 
ATOM   5300 C  CD1   . LEU C 1 119 ? 22.906  65.237  -55.673 1.00 60.06  ?  112 LEU C CD1   1 
ATOM   5301 C  CD2   . LEU C 1 119 ? 20.668  64.589  -54.803 1.00 54.32  ?  112 LEU C CD2   1 
ATOM   5302 N  N     . GLN C 1 120 ? 19.114  69.267  -57.110 1.00 63.55  ?  113 GLN C N     1 
ATOM   5303 C  CA    . GLN C 1 120 ? 18.665  70.642  -57.229 1.00 66.23  ?  113 GLN C CA    1 
ATOM   5304 C  C     . GLN C 1 120 ? 17.170  70.748  -56.911 1.00 64.80  ?  113 GLN C C     1 
ATOM   5305 O  O     . GLN C 1 120 ? 16.767  71.618  -56.147 1.00 65.67  ?  113 GLN C O     1 
ATOM   5306 C  CB    . GLN C 1 120 ? 18.981  71.139  -58.637 1.00 69.91  ?  113 GLN C CB    1 
ATOM   5307 C  CG    . GLN C 1 120 ? 18.568  72.577  -58.906 1.00 73.42  ?  113 GLN C CG    1 
ATOM   5308 C  CD    . GLN C 1 120 ? 19.294  73.109  -60.120 1.00 77.74  ?  113 GLN C CD    1 
ATOM   5309 O  OE1   . GLN C 1 120 ? 19.460  72.410  -61.119 1.00 78.13  ?  113 GLN C OE1   1 
ATOM   5310 N  NE2   . GLN C 1 120 ? 19.780  74.337  -60.019 1.00 81.55  ?  113 GLN C NE2   1 
ATOM   5311 N  N     . LYS C 1 121 ? 16.358  69.864  -57.511 1.00 63.27  ?  114 LYS C N     1 
ATOM   5312 C  CA    . LYS C 1 121 ? 14.913  69.923  -57.361 1.00 62.78  ?  114 LYS C CA    1 
ATOM   5313 C  C     . LYS C 1 121 ? 14.511  69.575  -55.925 1.00 60.16  ?  114 LYS C C     1 
ATOM   5314 O  O     . LYS C 1 121 ? 13.573  70.178  -55.407 1.00 61.00  ?  114 LYS C O     1 
ATOM   5315 C  CB    . LYS C 1 121 ? 14.241  69.005  -58.392 1.00 62.51  ?  114 LYS C CB    1 
ATOM   5316 C  CG    . LYS C 1 121 ? 12.720  68.895  -58.323 1.00 62.53  ?  114 LYS C CG    1 
ATOM   5317 C  CD    . LYS C 1 121 ? 12.068  68.755  -59.695 1.00 64.91  ?  114 LYS C CD    1 
ATOM   5318 C  CE    . LYS C 1 121 ? 10.850  67.855  -59.763 1.00 64.37  ?  114 LYS C CE    1 
ATOM   5319 N  NZ    . LYS C 1 121 ? 9.922   68.040  -58.626 1.00 63.59  ?  114 LYS C NZ    1 
ATOM   5320 N  N     . HIS C 1 122 ? 15.221  68.629  -55.284 1.00 57.53  ?  115 HIS C N     1 
ATOM   5321 C  CA    . HIS C 1 122 ? 14.732  68.029  -54.040 1.00 55.07  ?  115 HIS C CA    1 
ATOM   5322 C  C     . HIS C 1 122 ? 15.658  68.241  -52.836 1.00 54.51  ?  115 HIS C C     1 
ATOM   5323 O  O     . HIS C 1 122 ? 15.270  67.944  -51.708 1.00 53.14  ?  115 HIS C O     1 
ATOM   5324 C  CB    . HIS C 1 122 ? 14.508  66.529  -54.242 1.00 52.66  ?  115 HIS C CB    1 
ATOM   5325 C  CG    . HIS C 1 122 ? 13.409  66.238  -55.203 1.00 53.53  ?  115 HIS C CG    1 
ATOM   5326 N  ND1   . HIS C 1 122 ? 12.061  66.301  -54.916 1.00 53.98  ?  115 HIS C ND1   1 
ATOM   5327 C  CD2   . HIS C 1 122 ? 13.505  65.788  -56.462 1.00 54.50  ?  115 HIS C CD2   1 
ATOM   5328 C  CE1   . HIS C 1 122 ? 11.376  65.970  -56.013 1.00 55.32  ?  115 HIS C CE1   1 
ATOM   5329 N  NE2   . HIS C 1 122 ? 12.231  65.647  -56.950 1.00 55.59  ?  115 HIS C NE2   1 
ATOM   5330 N  N     . GLY C 1 123 ? 16.864  68.773  -53.069 1.00 56.15  ?  116 GLY C N     1 
ATOM   5331 C  CA    . GLY C 1 123 ? 17.825  69.094  -52.019 1.00 56.63  ?  116 GLY C CA    1 
ATOM   5332 C  C     . GLY C 1 123 ? 17.263  69.716  -50.733 1.00 57.09  ?  116 GLY C C     1 
ATOM   5333 O  O     . GLY C 1 123 ? 17.708  69.344  -49.655 1.00 56.13  ?  116 GLY C O     1 
ATOM   5334 N  N     . ARG C 1 124 ? 16.311  70.650  -50.812 1.00 59.02  ?  117 ARG C N     1 
ATOM   5335 C  CA    . ARG C 1 124 ? 15.776  71.277  -49.604 1.00 60.30  ?  117 ARG C CA    1 
ATOM   5336 C  C     . ARG C 1 124 ? 15.130  70.229  -48.689 1.00 57.50  ?  117 ARG C C     1 
ATOM   5337 O  O     . ARG C 1 124 ? 15.016  70.431  -47.476 1.00 58.21  ?  117 ARG C O     1 
ATOM   5338 C  CB    . ARG C 1 124 ? 14.772  72.381  -49.948 1.00 63.35  ?  117 ARG C CB    1 
ATOM   5339 C  CG    . ARG C 1 124 ? 13.485  71.905  -50.603 1.00 62.36  ?  117 ARG C CG    1 
ATOM   5340 C  CD    . ARG C 1 124 ? 12.693  73.064  -51.207 1.00 66.09  ?  117 ARG C CD    1 
ATOM   5341 N  NE    . ARG C 1 124 ? 11.347  72.667  -51.624 1.00 65.96  ?  117 ARG C NE    1 
ATOM   5342 C  CZ    . ARG C 1 124 ? 11.075  71.790  -52.588 1.00 64.17  ?  117 ARG C CZ    1 
ATOM   5343 N  NH1   . ARG C 1 124 ? 12.040  71.313  -53.355 1.00 62.63  ?  117 ARG C NH1   1 
ATOM   5344 N  NH2   . ARG C 1 124 ? 9.827   71.422  -52.823 1.00 64.62  ?  117 ARG C NH2   1 
ATOM   5345 N  N     . ASN C 1 125 ? 14.695  69.112  -49.275 1.00 54.85  ?  118 ASN C N     1 
ATOM   5346 C  CA    . ASN C 1 125 ? 13.925  68.134  -48.533 1.00 52.83  ?  118 ASN C CA    1 
ATOM   5347 C  C     . ASN C 1 125 ? 14.759  66.898  -48.197 1.00 50.10  ?  118 ASN C C     1 
ATOM   5348 O  O     . ASN C 1 125 ? 14.203  65.944  -47.656 1.00 48.47  ?  118 ASN C O     1 
ATOM   5349 C  CB    . ASN C 1 125 ? 12.661  67.719  -49.285 1.00 52.63  ?  118 ASN C CB    1 
ATOM   5350 C  CG    . ASN C 1 125 ? 11.656  68.847  -49.387 1.00 55.77  ?  118 ASN C CG    1 
ATOM   5351 O  OD1   . ASN C 1 125 ? 11.421  69.573  -48.421 1.00 57.68  ?  118 ASN C OD1   1 
ATOM   5352 N  ND2   . ASN C 1 125 ? 11.053  68.978  -50.553 1.00 56.78  ?  118 ASN C ND2   1 
ATOM   5353 N  N     . ILE C 1 126 ? 16.042  66.879  -48.596 1.00 50.06  ?  119 ILE C N     1 
ATOM   5354 C  CA    . ILE C 1 126 ? 16.929  65.753  -48.349 1.00 48.17  ?  119 ILE C CA    1 
ATOM   5355 C  C     . ILE C 1 126 ? 17.939  66.166  -47.286 1.00 49.30  ?  119 ILE C C     1 
ATOM   5356 O  O     . ILE C 1 126 ? 18.937  66.825  -47.599 1.00 51.25  ?  119 ILE C O     1 
ATOM   5357 C  CB    . ILE C 1 126 ? 17.696  65.300  -49.609 1.00 48.06  ?  119 ILE C CB    1 
ATOM   5358 C  CG1   . ILE C 1 126 ? 16.786  65.042  -50.811 1.00 47.84  ?  119 ILE C CG1   1 
ATOM   5359 C  CG2   . ILE C 1 126 ? 18.568  64.076  -49.322 1.00 46.63  ?  119 ILE C CG2   1 
ATOM   5360 C  CD1   . ILE C 1 126 ? 17.549  64.795  -52.094 1.00 48.71  ?  119 ILE C CD1   1 
ATOM   5361 N  N     . ASP C 1 127 ? 17.741  65.684  -46.059 1.00 48.46  ?  120 ASP C N     1 
ATOM   5362 C  CA    . ASP C 1 127 ? 18.664  66.064  -45.005 1.00 50.04  ?  120 ASP C CA    1 
ATOM   5363 C  C     . ASP C 1 127 ? 20.002  65.378  -45.268 1.00 49.74  ?  120 ASP C C     1 
ATOM   5364 O  O     . ASP C 1 127 ? 21.026  66.051  -45.169 1.00 52.20  ?  120 ASP C O     1 
ATOM   5365 C  CB    . ASP C 1 127 ? 18.049  65.851  -43.625 1.00 49.98  ?  120 ASP C CB    1 
ATOM   5366 C  CG    . ASP C 1 127 ? 16.814  66.708  -43.411 1.00 51.47  ?  120 ASP C CG    1 
ATOM   5367 O  OD1   . ASP C 1 127 ? 16.945  67.964  -43.515 1.00 54.25  ?  120 ASP C OD1   1 
ATOM   5368 O  OD2   . ASP C 1 127 ? 15.721  66.124  -43.136 1.00 50.38  -1 120 ASP C OD2   1 
ATOM   5369 N  N     . ILE C 1 128 ? 19.983  64.079  -45.644 1.00 47.39  ?  121 ILE C N     1 
ATOM   5370 C  CA    . ILE C 1 128 ? 21.173  63.266  -45.806 1.00 47.44  ?  121 ILE C CA    1 
ATOM   5371 C  C     . ILE C 1 128 ? 21.102  62.370  -47.049 1.00 46.19  ?  121 ILE C C     1 
ATOM   5372 O  O     . ILE C 1 128 ? 20.086  61.721  -47.281 1.00 44.34  ?  121 ILE C O     1 
ATOM   5373 C  CB    . ILE C 1 128 ? 21.359  62.362  -44.563 1.00 46.61  ?  121 ILE C CB    1 
ATOM   5374 C  CG1   . ILE C 1 128 ? 21.464  63.153  -43.254 1.00 48.39  ?  121 ILE C CG1   1 
ATOM   5375 C  CG2   . ILE C 1 128 ? 22.547  61.439  -44.774 1.00 47.04  ?  121 ILE C CG2   1 
ATOM   5376 C  CD1   . ILE C 1 128 ? 21.242  62.321  -42.001 1.00 47.61  ?  121 ILE C CD1   1 
ATOM   5377 N  N     . LEU C 1 129 ? 22.240  62.223  -47.748 1.00 47.74  ?  122 LEU C N     1 
ATOM   5378 C  CA    . LEU C 1 129 ? 22.373  61.307  -48.869 1.00 47.43  ?  122 LEU C CA    1 
ATOM   5379 C  C     . LEU C 1 129 ? 23.552  60.364  -48.611 1.00 48.43  ?  122 LEU C C     1 
ATOM   5380 O  O     . LEU C 1 129 ? 24.669  60.825  -48.345 1.00 50.89  ?  122 LEU C O     1 
ATOM   5381 C  CB    . LEU C 1 129 ? 22.561  62.118  -50.162 1.00 49.39  ?  122 LEU C CB    1 
ATOM   5382 C  CG    . LEU C 1 129 ? 22.740  61.328  -51.459 1.00 50.02  ?  122 LEU C CG    1 
ATOM   5383 C  CD1   . LEU C 1 129 ? 21.630  60.325  -51.727 1.00 47.77  ?  122 LEU C CD1   1 
ATOM   5384 C  CD2   . LEU C 1 129 ? 22.812  62.278  -52.648 1.00 52.30  ?  122 LEU C CD2   1 
ATOM   5385 N  N     . ALA C 1 130 ? 23.259  59.049  -48.589 1.00 46.97  ?  123 ALA C N     1 
ATOM   5386 C  CA    . ALA C 1 130 ? 24.245  58.018  -48.346 1.00 48.12  ?  123 ALA C CA    1 
ATOM   5387 C  C     . ALA C 1 130 ? 24.533  57.312  -49.652 1.00 49.46  ?  123 ALA C C     1 
ATOM   5388 O  O     . ALA C 1 130 ? 23.657  56.762  -50.309 1.00 48.29  ?  123 ALA C O     1 
ATOM   5389 C  CB    . ALA C 1 130 ? 23.798  57.003  -47.319 1.00 46.34  ?  123 ALA C CB    1 
ATOM   5390 N  N     . VAL C 1 131 ? 25.808  57.269  -49.993 1.00 52.57  ?  124 VAL C N     1 
ATOM   5391 C  CA    . VAL C 1 131 ? 26.200  56.540  -51.174 1.00 54.70  ?  124 VAL C CA    1 
ATOM   5392 C  C     . VAL C 1 131 ? 26.985  55.340  -50.701 1.00 56.18  ?  124 VAL C C     1 
ATOM   5393 O  O     . VAL C 1 131 ? 27.836  55.465  -49.807 1.00 57.45  ?  124 VAL C O     1 
ATOM   5394 C  CB    . VAL C 1 131 ? 27.017  57.430  -52.128 1.00 58.14  ?  124 VAL C CB    1 
ATOM   5395 C  CG1   . VAL C 1 131 ? 27.164  56.760  -53.469 1.00 60.47  ?  124 VAL C CG1   1 
ATOM   5396 C  CG2   . VAL C 1 131 ? 26.396  58.814  -52.267 1.00 57.11  ?  124 VAL C CG2   1 
ATOM   5397 N  N     . SER C 1 132 ? 26.599  54.191  -51.252 1.00 56.19  ?  125 SER C N     1 
ATOM   5398 C  CA    . SER C 1 132 ? 27.211  52.914  -50.965 1.00 58.00  ?  125 SER C CA    1 
ATOM   5399 C  C     . SER C 1 132 ? 28.381  52.638  -51.908 1.00 62.82  ?  125 SER C C     1 
ATOM   5400 O  O     . SER C 1 132 ? 28.175  52.150  -53.024 1.00 64.44  ?  125 SER C O     1 
ATOM   5401 C  CB    . SER C 1 132 ? 26.214  51.817  -51.095 1.00 56.44  ?  125 SER C CB    1 
ATOM   5402 O  OG    . SER C 1 132 ? 25.201  51.901  -50.076 1.00 52.74  ?  125 SER C OG    1 
ATOM   5403 N  N     . CYS C 1 133 ? 29.593  52.826  -51.378 1.00 65.62  ?  126 CYS C N     1 
ATOM   5404 C  CA    . CYS C 1 133 ? 30.825  52.510  -52.081 1.00 71.07  ?  126 CYS C CA    1 
ATOM   5405 C  C     . CYS C 1 133 ? 31.730  51.703  -51.150 1.00 73.43  ?  126 CYS C C     1 
ATOM   5406 O  O     . CYS C 1 133 ? 32.176  52.214  -50.120 1.00 73.24  ?  126 CYS C O     1 
ATOM   5407 C  CB    . CYS C 1 133 ? 31.485  53.810  -52.522 1.00 73.46  ?  126 CYS C CB    1 
ATOM   5408 S  SG    . CYS C 1 133 ? 32.984  53.583  -53.519 1.00 81.17  ?  126 CYS C SG    1 
ATOM   5409 N  N     . ASP C 1 134 ? 31.987  50.435  -51.504 1.00 76.08  ?  127 ASP C N     1 
ATOM   5410 C  CA    . ASP C 1 134 ? 32.682  49.521  -50.611 1.00 78.27  ?  127 ASP C CA    1 
ATOM   5411 C  C     . ASP C 1 134 ? 34.203  49.534  -50.820 1.00 84.77  ?  127 ASP C C     1 
ATOM   5412 O  O     . ASP C 1 134 ? 34.931  49.051  -49.949 1.00 87.08  ?  127 ASP C O     1 
ATOM   5413 C  CB    . ASP C 1 134 ? 32.176  48.087  -50.768 1.00 78.41  ?  127 ASP C CB    1 
ATOM   5414 C  CG    . ASP C 1 134 ? 30.677  47.958  -50.912 1.00 73.48  ?  127 ASP C CG    1 
ATOM   5415 O  OD1   . ASP C 1 134 ? 29.929  48.261  -49.928 1.00 69.06  ?  127 ASP C OD1   1 
ATOM   5416 O  OD2   . ASP C 1 134 ? 30.276  47.526  -51.990 1.00 74.68  -1 127 ASP C OD2   1 
ATOM   5417 N  N     . SER C 1 135 ? 34.688  50.031  -51.972 1.00 88.32  ?  128 SER C N     1 
ATOM   5418 C  CA    . SER C 1 135 ? 36.125  50.124  -52.226 1.00 95.25  ?  128 SER C CA    1 
ATOM   5419 C  C     . SER C 1 135 ? 36.451  51.446  -52.924 1.00 96.91  ?  128 SER C C     1 
ATOM   5420 O  O     . SER C 1 135 ? 35.564  52.197  -53.319 1.00 92.89  ?  128 SER C O     1 
ATOM   5421 C  CB    . SER C 1 135 ? 36.634  48.935  -53.039 1.00 100.71 ?  128 SER C CB    1 
ATOM   5422 N  N     . PHE C 1 136 ? 37.749  51.728  -53.038 1.00 103.41 ?  129 PHE C N     1 
ATOM   5423 C  CA    . PHE C 1 136 ? 38.250  52.788  -53.898 1.00 107.07 ?  129 PHE C CA    1 
ATOM   5424 C  C     . PHE C 1 136 ? 39.129  52.160  -54.977 1.00 114.65 ?  129 PHE C C     1 
ATOM   5425 O  O     . PHE C 1 136 ? 39.917  52.859  -55.605 1.00 120.10 ?  129 PHE C O     1 
ATOM   5426 C  CB    . PHE C 1 136 ? 38.966  53.856  -53.065 1.00 108.73 ?  129 PHE C CB    1 
ATOM   5427 C  CG    . PHE C 1 136 ? 38.013  54.645  -52.207 1.00 101.83 ?  129 PHE C CG    1 
ATOM   5428 C  CD1   . PHE C 1 136 ? 37.260  55.674  -52.752 1.00 98.77  ?  129 PHE C CD1   1 
ATOM   5429 C  CD2   . PHE C 1 136 ? 37.787  54.294  -50.884 1.00 98.56  ?  129 PHE C CD2   1 
ATOM   5430 C  CE1   . PHE C 1 136 ? 36.337  56.367  -51.978 1.00 92.91  ?  129 PHE C CE1   1 
ATOM   5431 C  CE2   . PHE C 1 136 ? 36.863  54.987  -50.110 1.00 92.71  ?  129 PHE C CE2   1 
ATOM   5432 C  CZ    . PHE C 1 136 ? 36.148  56.025  -50.657 1.00 90.01  ?  129 PHE C CZ    1 
ATOM   5433 N  N     . ASN C 1 137 ? 38.966  50.838  -55.164 1.00 115.37 ?  130 ASN C N     1 
ATOM   5434 C  CA    . ASN C 1 137 ? 39.580  50.093  -56.253 1.00 122.36 ?  130 ASN C CA    1 
ATOM   5435 C  C     . ASN C 1 137 ? 38.476  49.449  -57.094 1.00 119.38 ?  130 ASN C C     1 
ATOM   5436 O  O     . ASN C 1 137 ? 37.725  48.589  -56.632 1.00 115.36 ?  130 ASN C O     1 
ATOM   5437 C  CB    . ASN C 1 137 ? 40.569  49.032  -55.761 1.00 128.09 ?  130 ASN C CB    1 
ATOM   5438 C  CG    . ASN C 1 137 ? 41.492  48.565  -56.865 1.00 137.28 ?  130 ASN C CG    1 
ATOM   5439 O  OD1   . ASN C 1 137 ? 41.390  47.440  -57.346 1.00 139.86 ?  130 ASN C OD1   1 
ATOM   5440 N  ND2   . ASN C 1 137 ? 42.387  49.441  -57.291 1.00 142.84 ?  130 ASN C ND2   1 
ATOM   5441 N  N     . GLU C 1 138 ? 38.435  49.846  -58.365 1.00 122.30 ?  131 GLU C N     1 
ATOM   5442 C  CA    . GLU C 1 138 ? 37.353  49.476  -59.258 1.00 119.82 ?  131 GLU C CA    1 
ATOM   5443 C  C     . GLU C 1 138 ? 37.436  47.984  -59.587 1.00 123.69 ?  131 GLU C C     1 
ATOM   5444 O  O     . GLU C 1 138 ? 36.418  47.355  -59.861 1.00 120.58 ?  131 GLU C O     1 
ATOM   5445 C  CB    . GLU C 1 138 ? 37.390  50.384  -60.491 1.00 122.70 ?  131 GLU C CB    1 
ATOM   5446 C  CG    . GLU C 1 138 ? 37.409  51.877  -60.160 1.00 119.94 ?  131 GLU C CG    1 
ATOM   5447 C  CD    . GLU C 1 138 ? 36.304  52.419  -59.255 1.00 110.97 ?  131 GLU C CD    1 
ATOM   5448 O  OE1   . GLU C 1 138 ? 35.498  51.620  -58.713 1.00 106.26 ?  131 GLU C OE1   1 
ATOM   5449 O  OE2   . GLU C 1 138 ? 36.241  53.657  -59.095 1.00 109.18 -1 131 GLU C OE2   1 
ATOM   5450 N  N     . ALA C 1 139 ? 38.648  47.412  -59.537 1.00 131.00 ?  132 ALA C N     1 
ATOM   5451 C  CA    . ALA C 1 139 ? 38.820  45.976  -59.713 1.00 135.36 ?  132 ALA C CA    1 
ATOM   5452 C  C     . ALA C 1 139 ? 38.016  45.211  -58.664 1.00 129.21 ?  132 ALA C C     1 
ATOM   5453 O  O     . ALA C 1 139 ? 37.414  44.187  -58.981 1.00 129.50 ?  132 ALA C O     1 
ATOM   5454 C  CB    . ALA C 1 139 ? 40.283  45.609  -59.649 1.00 144.19 ?  132 ALA C CB    1 
ATOM   5455 N  N     . THR C 1 140 ? 38.033  45.723  -57.425 1.00 124.35 ?  133 THR C N     1 
ATOM   5456 C  CA    . THR C 1 140 ? 37.337  45.121  -56.299 1.00 118.75 ?  133 THR C CA    1 
ATOM   5457 C  C     . THR C 1 140 ? 35.830  45.249  -56.500 1.00 111.70 ?  133 THR C C     1 
ATOM   5458 O  O     . THR C 1 140 ? 35.117  44.245  -56.476 1.00 110.59 ?  133 THR C O     1 
ATOM   5459 C  CB    . THR C 1 140 ? 37.780  45.769  -54.979 1.00 116.11 ?  133 THR C CB    1 
ATOM   5460 O  OG1   . THR C 1 140 ? 39.204  45.684  -54.938 1.00 123.72 ?  133 THR C OG1   1 
ATOM   5461 C  CG2   . THR C 1 140 ? 37.192  45.122  -53.742 1.00 111.35 ?  133 THR C CG2   1 
ATOM   5462 N  N     . ASN C 1 141 ? 35.364  46.494  -56.682 1.00 107.52 ?  134 ASN C N     1 
ATOM   5463 C  CA    . ASN C 1 141 ? 33.952  46.799  -56.865 1.00 101.16 ?  134 ASN C CA    1 
ATOM   5464 C  C     . ASN C 1 141 ? 33.362  45.903  -57.951 1.00 103.59 ?  134 ASN C C     1 
ATOM   5465 O  O     . ASN C 1 141 ? 32.248  45.415  -57.818 1.00 99.77  ?  134 ASN C O     1 
ATOM   5466 C  CB    . ASN C 1 141 ? 33.751  48.283  -57.181 1.00 98.56  ?  134 ASN C CB    1 
ATOM   5467 C  CG    . ASN C 1 141 ? 34.144  49.184  -56.027 1.00 95.83  ?  134 ASN C CG    1 
ATOM   5468 O  OD1   . ASN C 1 141 ? 34.272  48.722  -54.895 1.00 94.27  ?  134 ASN C OD1   1 
ATOM   5469 N  ND2   . ASN C 1 141 ? 34.337  50.466  -56.301 1.00 95.70  ?  134 ASN C ND2   1 
ATOM   5470 N  N     . ILE C 1 142 ? 34.148  45.662  -59.010 1.00 110.72 ?  135 ILE C N     1 
ATOM   5471 C  CA    . ILE C 1 142 ? 33.777  44.745  -60.079 1.00 114.74 ?  135 ILE C CA    1 
ATOM   5472 C  C     . ILE C 1 142 ? 33.529  43.359  -59.486 1.00 115.19 ?  135 ILE C C     1 
ATOM   5473 O  O     . ILE C 1 142 ? 32.425  42.806  -59.570 1.00 112.48 ?  135 ILE C O     1 
ATOM   5474 C  CB    . ILE C 1 142 ? 34.863  44.749  -61.179 1.00 123.39 ?  135 ILE C CB    1 
ATOM   5475 C  CG1   . ILE C 1 142 ? 34.747  46.012  -62.034 1.00 123.02 ?  135 ILE C CG1   1 
ATOM   5476 C  CG2   . ILE C 1 142 ? 34.799  43.491  -62.034 1.00 129.52 ?  135 ILE C CG2   1 
ATOM   5477 C  CD1   . ILE C 1 142 ? 35.957  46.322  -62.858 1.00 131.15 ?  135 ILE C CD1   1 
ATOM   5478 N  N     . LYS C 1 143 ? 34.560  42.817  -58.837 1.00 118.93 ?  136 LYS C N     1 
ATOM   5479 C  CA    . LYS C 1 143 ? 34.446  41.492  -58.258 1.00 120.26 ?  136 LYS C CA    1 
ATOM   5480 C  C     . LYS C 1 143 ? 33.255  41.433  -57.286 1.00 112.35 ?  136 LYS C C     1 
ATOM   5481 O  O     . LYS C 1 143 ? 32.555  40.423  -57.249 1.00 112.49 ?  136 LYS C O     1 
ATOM   5482 C  CB    . LYS C 1 143 ? 35.787  41.078  -57.646 1.00 125.56 ?  136 LYS C CB    1 
ATOM   5483 C  CG    . LYS C 1 143 ? 35.795  39.709  -56.975 1.00 127.67 ?  136 LYS C CG    1 
ATOM   5484 C  CD    . LYS C 1 143 ? 35.117  38.606  -57.779 1.00 130.82 ?  136 LYS C CD    1 
ATOM   5485 C  CE    . LYS C 1 143 ? 34.482  37.539  -56.908 1.00 128.94 ?  136 LYS C CE    1 
ATOM   5486 N  NZ    . LYS C 1 143 ? 33.076  37.256  -57.295 1.00 125.41 ?  136 LYS C NZ    1 
ATOM   5487 N  N     . ILE C 1 144 ? 32.996  42.505  -56.522 1.00 106.04 ?  137 ILE C N     1 
ATOM   5488 C  CA    . ILE C 1 144 ? 31.864  42.518  -55.590 1.00 99.05  ?  137 ILE C CA    1 
ATOM   5489 C  C     . ILE C 1 144 ? 30.543  42.437  -56.360 1.00 96.68  ?  137 ILE C C     1 
ATOM   5490 O  O     . ILE C 1 144 ? 29.602  41.788  -55.895 1.00 94.09  ?  137 ILE C O     1 
ATOM   5491 C  CB    . ILE C 1 144 ? 31.870  43.737  -54.638 1.00 93.54  ?  137 ILE C CB    1 
ATOM   5492 C  CG1   . ILE C 1 144 ? 33.027  43.694  -53.631 1.00 95.64  ?  137 ILE C CG1   1 
ATOM   5493 C  CG2   . ILE C 1 144 ? 30.530  43.853  -53.919 1.00 86.79  ?  137 ILE C CG2   1 
ATOM   5494 C  CD1   . ILE C 1 144 ? 33.174  44.943  -52.763 1.00 91.53  ?  137 ILE C CD1   1 
ATOM   5495 N  N     . GLY C 1 145 ? 30.472  43.123  -57.512 1.00 97.92  ?  138 GLY C N     1 
ATOM   5496 C  CA    . GLY C 1 145 ? 29.276  43.135  -58.344 1.00 96.46  ?  138 GLY C CA    1 
ATOM   5497 C  C     . GLY C 1 145 ? 28.508  44.461  -58.300 1.00 90.54  ?  138 GLY C C     1 
ATOM   5498 O  O     . GLY C 1 145 ? 27.467  44.594  -58.949 1.00 89.18  ?  138 GLY C O     1 
ATOM   5499 N  N     . ARG C 1 146 ? 29.023  45.438  -57.539 1.00 87.61  ?  139 ARG C N     1 
ATOM   5500 C  CA    . ARG C 1 146 ? 28.496  46.796  -57.568 1.00 83.21  ?  139 ARG C CA    1 
ATOM   5501 C  C     . ARG C 1 146 ? 29.083  47.555  -58.761 1.00 86.96  ?  139 ARG C C     1 
ATOM   5502 O  O     . ARG C 1 146 ? 28.407  48.390  -59.357 1.00 85.09  ?  139 ARG C O     1 
ATOM   5503 C  CB    . ARG C 1 146 ? 28.829  47.547  -56.271 1.00 79.36  ?  139 ARG C CB    1 
ATOM   5504 C  CG    . ARG C 1 146 ? 27.906  48.722  -55.981 1.00 73.93  ?  139 ARG C CG    1 
ATOM   5505 C  CD    . ARG C 1 146 ? 28.241  49.476  -54.704 1.00 70.86  ?  139 ARG C CD    1 
ATOM   5506 N  NE    . ARG C 1 146 ? 28.052  48.727  -53.462 1.00 68.81  ?  139 ARG C NE    1 
ATOM   5507 C  CZ    . ARG C 1 146 ? 26.899  48.586  -52.808 1.00 64.65  ?  139 ARG C CZ    1 
ATOM   5508 N  NH1   . ARG C 1 146 ? 25.780  49.100  -53.286 1.00 62.07  ?  139 ARG C NH1   1 
ATOM   5509 N  NH2   . ARG C 1 146 ? 26.868  47.933  -51.656 1.00 63.51  ?  139 ARG C NH2   1 
ATOM   5510 N  N     . GLY C 1 147 ? 30.335  47.231  -59.111 1.00 92.81  ?  140 GLY C N     1 
ATOM   5511 C  CA    . GLY C 1 147 ? 31.201  48.115  -59.878 1.00 96.65  ?  140 GLY C CA    1 
ATOM   5512 C  C     . GLY C 1 147 ? 31.005  48.012  -61.387 1.00 101.07 ?  140 GLY C C     1 
ATOM   5513 O  O     . GLY C 1 147 ? 30.927  46.915  -61.934 1.00 104.90 ?  140 GLY C O     1 
ATOM   5514 N  N     . SER C 1 148 ? 30.917  49.182  -62.036 1.00 100.86 ?  141 SER C N     1 
ATOM   5515 C  CA    . SER C 1 148 ? 31.029  49.309  -63.482 1.00 106.25 ?  141 SER C CA    1 
ATOM   5516 C  C     . SER C 1 148 ? 32.181  50.255  -63.815 1.00 110.42 ?  141 SER C C     1 
ATOM   5517 O  O     . SER C 1 148 ? 32.175  50.887  -64.868 1.00 113.44 ?  141 SER C O     1 
ATOM   5518 C  CB    . SER C 1 148 ? 29.735  49.798  -64.088 1.00 102.96 ?  141 SER C CB    1 
ATOM   5519 O  OG    . SER C 1 148 ? 29.564  51.192  -63.873 1.00 99.37  ?  141 SER C OG    1 
ATOM   5520 N  N     . GLY C 1 149 ? 33.135  50.383  -62.880 1.00 110.76 ?  142 GLY C N     1 
ATOM   5521 C  CA    . GLY C 1 149 ? 34.366  51.124  -63.101 1.00 115.94 ?  142 GLY C CA    1 
ATOM   5522 C  C     . GLY C 1 149 ? 34.304  52.591  -62.669 1.00 112.33 ?  142 GLY C C     1 
ATOM   5523 O  O     . GLY C 1 149 ? 35.350  53.199  -62.454 1.00 115.88 ?  142 GLY C O     1 
ATOM   5524 N  N     . ASP C 1 150 ? 33.091  53.153  -62.537 1.00 105.92 ?  143 ASP C N     1 
ATOM   5525 C  CA    . ASP C 1 150 ? 32.914  54.595  -62.404 1.00 103.49 ?  143 ASP C CA    1 
ATOM   5526 C  C     . ASP C 1 150 ? 32.476  54.980  -60.992 1.00 96.88  ?  143 ASP C C     1 
ATOM   5527 O  O     . ASP C 1 150 ? 32.148  56.143  -60.748 1.00 94.24  ?  143 ASP C O     1 
ATOM   5528 C  CB    . ASP C 1 150 ? 31.880  55.122  -63.405 1.00 102.24 ?  143 ASP C CB    1 
ATOM   5529 C  CG    . ASP C 1 150 ? 32.339  55.117  -64.852 1.00 109.32 ?  143 ASP C CG    1 
ATOM   5530 O  OD1   . ASP C 1 150 ? 33.405  55.711  -65.137 1.00 114.59 ?  143 ASP C OD1   1 
ATOM   5531 O  OD2   . ASP C 1 150 ? 31.609  54.544  -65.690 1.00 109.96 -1 143 ASP C OD2   1 
ATOM   5532 N  N     . ASN C 1 151 ? 32.471  54.005  -60.072 1.00 94.72  ?  144 ASN C N     1 
ATOM   5533 C  CA    . ASN C 1 151 ? 31.951  54.216  -58.732 1.00 88.68  ?  144 ASN C CA    1 
ATOM   5534 C  C     . ASN C 1 151 ? 32.602  55.454  -58.119 1.00 89.06  ?  144 ASN C C     1 
ATOM   5535 O  O     . ASN C 1 151 ? 31.900  56.335  -57.618 1.00 84.73  ?  144 ASN C O     1 
ATOM   5536 C  CB    . ASN C 1 151 ? 32.169  52.996  -57.831 1.00 88.02  ?  144 ASN C CB    1 
ATOM   5537 C  CG    . ASN C 1 151 ? 31.605  51.718  -58.413 1.00 88.61  ?  144 ASN C CG    1 
ATOM   5538 O  OD1   . ASN C 1 151 ? 32.021  51.293  -59.487 1.00 93.79  ?  144 ASN C OD1   1 
ATOM   5539 N  ND2   . ASN C 1 151 ? 30.660  51.104  -57.719 1.00 83.92  ?  144 ASN C ND2   1 
ATOM   5540 N  N     . VAL C 1 152 ? 33.944  55.520  -58.177 1.00 94.91  ?  145 VAL C N     1 
ATOM   5541 C  CA    . VAL C 1 152 ? 34.680  56.507  -57.402 1.00 96.03  ?  145 VAL C CA    1 
ATOM   5542 C  C     . VAL C 1 152 ? 34.482  57.892  -58.018 1.00 96.64  ?  145 VAL C C     1 
ATOM   5543 O  O     . VAL C 1 152 ? 34.200  58.847  -57.293 1.00 93.81  ?  145 VAL C O     1 
ATOM   5544 C  CB    . VAL C 1 152 ? 36.168  56.133  -57.234 1.00 102.76 ?  145 VAL C CB    1 
ATOM   5545 C  CG1   . VAL C 1 152 ? 36.977  57.255  -56.593 1.00 105.24 ?  145 VAL C CG1   1 
ATOM   5546 C  CG2   . VAL C 1 152 ? 36.323  54.846  -56.433 1.00 101.91 ?  145 VAL C CG2   1 
ATOM   5547 N  N     . GLN C 1 153 ? 34.584  58.000  -59.348 1.00 100.58 ?  146 GLN C N     1 
ATOM   5548 C  CA    . GLN C 1 153 ? 34.325  59.274  -60.005 1.00 101.40 ?  146 GLN C CA    1 
ATOM   5549 C  C     . GLN C 1 153 ? 32.925  59.758  -59.620 1.00 94.30  ?  146 GLN C C     1 
ATOM   5550 O  O     . GLN C 1 153 ? 32.730  60.926  -59.283 1.00 93.15  ?  146 GLN C O     1 
ATOM   5551 C  CB    . GLN C 1 153 ? 34.495  59.173  -61.524 1.00 106.56 ?  146 GLN C CB    1 
ATOM   5552 N  N     . LYS C 1 154 ? 31.957  58.836  -59.622 1.00 90.04  ?  147 LYS C N     1 
ATOM   5553 C  CA    . LYS C 1 154 ? 30.578  59.171  -59.287 1.00 83.90  ?  147 LYS C CA    1 
ATOM   5554 C  C     . LYS C 1 154 ? 30.464  59.600  -57.824 1.00 80.06  ?  147 LYS C C     1 
ATOM   5555 O  O     . LYS C 1 154 ? 29.783  60.578  -57.514 1.00 77.40  ?  147 LYS C O     1 
ATOM   5556 C  CB    . LYS C 1 154 ? 29.642  58.001  -59.606 1.00 81.24  ?  147 LYS C CB    1 
ATOM   5557 C  CG    . LYS C 1 154 ? 28.167  58.380  -59.716 1.00 76.67  ?  147 LYS C CG    1 
ATOM   5558 C  CD    . LYS C 1 154 ? 27.896  59.590  -60.603 1.00 78.34  ?  147 LYS C CD    1 
ATOM   5559 C  CE    . LYS C 1 154 ? 26.497  60.147  -60.449 1.00 73.97  ?  147 LYS C CE    1 
ATOM   5560 N  NZ    . LYS C 1 154 ? 25.477  59.194  -60.944 1.00 72.38  ?  147 LYS C NZ    1 
ATOM   5561 N  N     . LEU C 1 155 ? 31.194  58.921  -56.932 1.00 80.55  ?  148 LEU C N     1 
ATOM   5562 C  CA    . LEU C 1 155 ? 31.117  59.243  -55.517 1.00 77.45  ?  148 LEU C CA    1 
ATOM   5563 C  C     . LEU C 1 155 ? 31.558  60.689  -55.259 1.00 79.45  ?  148 LEU C C     1 
ATOM   5564 O  O     . LEU C 1 155 ? 30.830  61.452  -54.608 1.00 76.15  ?  148 LEU C O     1 
ATOM   5565 C  CB    . LEU C 1 155 ? 31.928  58.203  -54.742 1.00 78.71  ?  148 LEU C CB    1 
ATOM   5566 C  CG    . LEU C 1 155 ? 31.984  58.398  -53.226 1.00 76.36  ?  148 LEU C CG    1 
ATOM   5567 C  CD1   . LEU C 1 155 ? 30.599  58.269  -52.592 1.00 70.18  ?  148 LEU C CD1   1 
ATOM   5568 C  CD2   . LEU C 1 155 ? 32.949  57.411  -52.589 1.00 78.89  ?  148 LEU C CD2   1 
ATOM   5569 N  N     . TYR C 1 156 ? 32.719  61.095  -55.819 1.00 85.47  ?  149 TYR C N     1 
ATOM   5570 C  CA    . TYR C 1 156 ? 33.270  62.431  -55.593 1.00 88.57  ?  149 TYR C CA    1 
ATOM   5571 C  C     . TYR C 1 156 ? 32.283  63.487  -56.102 1.00 86.55  ?  149 TYR C C     1 
ATOM   5572 O  O     . TYR C 1 156 ? 32.043  64.508  -55.454 1.00 85.74  ?  149 TYR C O     1 
ATOM   5573 C  CB    . TYR C 1 156 ? 34.670  62.611  -56.211 1.00 96.20  ?  149 TYR C CB    1 
ATOM   5574 C  CG    . TYR C 1 156 ? 35.823  62.110  -55.351 1.00 99.51  ?  149 TYR C CG    1 
ATOM   5575 C  CD1   . TYR C 1 156 ? 36.178  60.765  -55.316 1.00 99.99  ?  149 TYR C CD1   1 
ATOM   5576 C  CD2   . TYR C 1 156 ? 36.546  62.985  -54.549 1.00 102.63 ?  149 TYR C CD2   1 
ATOM   5577 C  CE1   . TYR C 1 156 ? 37.226  60.309  -54.529 1.00 103.45 ?  149 TYR C CE1   1 
ATOM   5578 C  CE2   . TYR C 1 156 ? 37.588  62.544  -53.751 1.00 106.13 ?  149 TYR C CE2   1 
ATOM   5579 C  CZ    . TYR C 1 156 ? 37.936  61.202  -53.743 1.00 106.54 ?  149 TYR C CZ    1 
ATOM   5580 O  OH    . TYR C 1 156 ? 38.969  60.774  -52.955 1.00 110.46 ?  149 TYR C OH    1 
ATOM   5581 N  N     . GLU C 1 157 ? 31.691  63.211  -57.266 1.00 86.15  ?  150 GLU C N     1 
ATOM   5582 C  CA    . GLU C 1 157 ? 30.723  64.104  -57.894 1.00 84.74  ?  150 GLU C CA    1 
ATOM   5583 C  C     . GLU C 1 157 ? 29.581  64.397  -56.921 1.00 79.01  ?  150 GLU C C     1 
ATOM   5584 O  O     . GLU C 1 157 ? 29.220  65.559  -56.677 1.00 78.93  ?  150 GLU C O     1 
ATOM   5585 C  CB    . GLU C 1 157 ? 30.208  63.479  -59.195 1.00 85.03  ?  150 GLU C CB    1 
ATOM   5586 C  CG    . GLU C 1 157 ? 29.597  64.488  -60.159 1.00 86.25  ?  150 GLU C CG    1 
ATOM   5587 C  CD    . GLU C 1 157 ? 28.985  63.913  -61.428 1.00 86.74  ?  150 GLU C CD    1 
ATOM   5588 O  OE1   . GLU C 1 157 ? 28.643  62.719  -61.429 1.00 84.54  ?  150 GLU C OE1   1 
ATOM   5589 O  OE2   . GLU C 1 157 ? 28.876  64.661  -62.425 1.00 89.89  -1 150 GLU C OE2   1 
ATOM   5590 N  N     . ILE C 1 158 ? 29.042  63.319  -56.341 1.00 74.78  ?  151 ILE C N     1 
ATOM   5591 C  CA    . ILE C 1 158 ? 27.907  63.435  -55.444 1.00 69.72  ?  151 ILE C CA    1 
ATOM   5592 C  C     . ILE C 1 158 ? 28.313  64.269  -54.231 1.00 70.13  ?  151 ILE C C     1 
ATOM   5593 O  O     . ILE C 1 158 ? 27.622  65.226  -53.858 1.00 68.91  ?  151 ILE C O     1 
ATOM   5594 C  CB    . ILE C 1 158 ? 27.364  62.038  -55.086 1.00 66.07  ?  151 ILE C CB    1 
ATOM   5595 C  CG1   . ILE C 1 158 ? 26.870  61.313  -56.341 1.00 66.32  ?  151 ILE C CG1   1 
ATOM   5596 C  CG2   . ILE C 1 158 ? 26.265  62.146  -54.038 1.00 61.52  ?  151 ILE C CG2   1 
ATOM   5597 C  CD1   . ILE C 1 158 ? 26.629  59.851  -56.152 1.00 64.45  ?  151 ILE C CD1   1 
ATOM   5598 N  N     . GLY C 1 159 ? 29.469  63.920  -53.656 1.00 72.61  ?  152 GLY C N     1 
ATOM   5599 C  CA    . GLY C 1 159 ? 30.081  64.709  -52.602 1.00 74.49  ?  152 GLY C CA    1 
ATOM   5600 C  C     . GLY C 1 159 ? 29.979  66.205  -52.882 1.00 76.96  ?  152 GLY C C     1 
ATOM   5601 O  O     . GLY C 1 159 ? 29.444  66.963  -52.079 1.00 75.69  ?  152 GLY C O     1 
ATOM   5602 N  N     . SER C 1 160 ? 30.472  66.614  -54.051 1.00 80.95  ?  153 SER C N     1 
ATOM   5603 C  CA    . SER C 1 160 ? 30.500  68.016  -54.423 1.00 84.29  ?  153 SER C CA    1 
ATOM   5604 C  C     . SER C 1 160 ? 29.084  68.567  -54.561 1.00 80.65  ?  153 SER C C     1 
ATOM   5605 O  O     . SER C 1 160 ? 28.819  69.691  -54.125 1.00 81.76  ?  153 SER C O     1 
ATOM   5606 C  CB    . SER C 1 160 ? 31.261  68.196  -55.697 1.00 89.43  ?  153 SER C CB    1 
ATOM   5607 O  OG    . SER C 1 160 ? 30.623  67.472  -56.732 1.00 87.29  ?  153 SER C OG    1 
ATOM   5608 N  N     . TRP C 1 161 ? 28.199  67.768  -55.190 1.00 76.99  ?  154 TRP C N     1 
ATOM   5609 C  CA    . TRP C 1 161 ? 26.791  68.116  -55.321 1.00 73.64  ?  154 TRP C CA    1 
ATOM   5610 C  C     . TRP C 1 161 ? 26.186  68.390  -53.942 1.00 70.75  ?  154 TRP C C     1 
ATOM   5611 O  O     . TRP C 1 161 ? 25.465  69.370  -53.766 1.00 70.85  ?  154 TRP C O     1 
ATOM   5612 C  CB    . TRP C 1 161 ? 26.011  67.020  -56.074 1.00 70.56  ?  154 TRP C CB    1 
ATOM   5613 C  CG    . TRP C 1 161 ? 26.322  66.901  -57.546 1.00 73.72  ?  154 TRP C CG    1 
ATOM   5614 C  CD1   . TRP C 1 161 ? 26.955  67.827  -58.329 1.00 78.62  ?  154 TRP C CD1   1 
ATOM   5615 C  CD2   . TRP C 1 161 ? 26.010  65.795  -58.423 1.00 72.85  ?  154 TRP C CD2   1 
ATOM   5616 N  NE1   . TRP C 1 161 ? 27.061  67.377  -59.620 1.00 80.81  ?  154 TRP C NE1   1 
ATOM   5617 C  CE2   . TRP C 1 161 ? 26.494  66.134  -59.710 1.00 77.42  ?  154 TRP C CE2   1 
ATOM   5618 C  CE3   . TRP C 1 161 ? 25.375  64.556  -58.260 1.00 69.22  ?  154 TRP C CE3   1 
ATOM   5619 C  CZ2   . TRP C 1 161 ? 26.359  65.284  -60.809 1.00 78.47  ?  154 TRP C CZ2   1 
ATOM   5620 C  CZ3   . TRP C 1 161 ? 25.253  63.713  -59.347 1.00 70.32  ?  154 TRP C CZ3   1 
ATOM   5621 C  CH2   . TRP C 1 161 ? 25.742  64.072  -60.603 1.00 74.91  ?  154 TRP C CH2   1 
ATOM   5622 N  N     . CYS C 1 162 ? 26.488  67.530  -52.960 1.00 68.72  ?  155 CYS C N     1 
ATOM   5623 C  CA    . CYS C 1 162 ? 25.903  67.651  -51.629 1.00 66.20  ?  155 CYS C CA    1 
ATOM   5624 C  C     . CYS C 1 162 ? 26.264  68.978  -50.965 1.00 69.59  ?  155 CYS C C     1 
ATOM   5625 O  O     . CYS C 1 162 ? 25.498  69.506  -50.142 1.00 68.46  ?  155 CYS C O     1 
ATOM   5626 C  CB    . CYS C 1 162 ? 26.371  66.516  -50.728 1.00 64.47  ?  155 CYS C CB    1 
ATOM   5627 S  SG    . CYS C 1 162 ? 25.544  64.945  -51.078 1.00 59.91  ?  155 CYS C SG    1 
ATOM   5628 N  N     . GLN C 1 163 ? 27.473  69.454  -51.293 1.00 74.30  ?  156 GLN C N     1 
ATOM   5629 C  CA    . GLN C 1 163 ? 28.003  70.717  -50.800 1.00 78.81  ?  156 GLN C CA    1 
ATOM   5630 C  C     . GLN C 1 163 ? 27.242  71.858  -51.472 1.00 80.12  ?  156 GLN C C     1 
ATOM   5631 O  O     . GLN C 1 163 ? 26.735  72.780  -50.828 1.00 81.06  ?  156 GLN C O     1 
ATOM   5632 C  CB    . GLN C 1 163 ? 29.504  70.768  -51.110 1.00 84.00  ?  156 GLN C CB    1 
ATOM   5633 C  CG    . GLN C 1 163 ? 30.322  71.581  -50.114 1.00 88.60  ?  156 GLN C CG    1 
ATOM   5634 C  CD    . GLN C 1 163 ? 30.047  73.066  -50.187 1.00 92.17  ?  156 GLN C CD    1 
ATOM   5635 O  OE1   . GLN C 1 163 ? 30.264  73.712  -51.213 1.00 95.53  ?  156 GLN C OE1   1 
ATOM   5636 N  NE2   . GLN C 1 163 ? 29.574  73.625  -49.083 1.00 92.00  ?  156 GLN C NE2   1 
ATOM   5637 N  N     . LYS C 1 164 ? 27.166  71.760  -52.798 1.00 80.60  ?  157 LYS C N     1 
ATOM   5638 C  CA    . LYS C 1 164 ? 26.505  72.739  -53.643 1.00 82.26  ?  157 LYS C CA    1 
ATOM   5639 C  C     . LYS C 1 164 ? 25.026  72.898  -53.277 1.00 78.54  ?  157 LYS C C     1 
ATOM   5640 O  O     . LYS C 1 164 ? 24.499  74.011  -53.365 1.00 80.75  ?  157 LYS C O     1 
ATOM   5641 C  CB    . LYS C 1 164 ? 26.697  72.287  -55.090 1.00 83.06  ?  157 LYS C CB    1 
ATOM   5642 C  CG    . LYS C 1 164 ? 26.161  73.234  -56.149 1.00 85.57  ?  157 LYS C CG    1 
ATOM   5643 C  CD    . LYS C 1 164 ? 26.329  72.682  -57.528 1.00 86.49  ?  157 LYS C CD    1 
ATOM   5644 C  CE    . LYS C 1 164 ? 26.201  73.734  -58.604 1.00 90.86  ?  157 LYS C CE    1 
ATOM   5645 N  NZ    . LYS C 1 164 ? 26.484  73.161  -59.942 1.00 92.54  ?  157 LYS C NZ    1 
ATOM   5646 N  N     . TYR C 1 165 ? 24.347  71.804  -52.876 1.00 73.50  ?  158 TYR C N     1 
ATOM   5647 C  CA    . TYR C 1 165 ? 22.905  71.859  -52.647 1.00 70.47  ?  158 TYR C CA    1 
ATOM   5648 C  C     . TYR C 1 165 ? 22.541  71.646  -51.176 1.00 68.32  ?  158 TYR C C     1 
ATOM   5649 O  O     . TYR C 1 165 ? 21.370  71.420  -50.889 1.00 65.64  ?  158 TYR C O     1 
ATOM   5650 C  CB    . TYR C 1 165 ? 22.187  70.828  -53.524 1.00 67.15  ?  158 TYR C CB    1 
ATOM   5651 C  CG    . TYR C 1 165 ? 22.381  71.092  -55.007 1.00 69.67  ?  158 TYR C CG    1 
ATOM   5652 C  CD1   . TYR C 1 165 ? 21.803  72.207  -55.609 1.00 72.24  ?  158 TYR C CD1   1 
ATOM   5653 C  CD2   . TYR C 1 165 ? 23.206  70.284  -55.777 1.00 70.26  ?  158 TYR C CD2   1 
ATOM   5654 C  CE1   . TYR C 1 165 ? 22.002  72.487  -56.950 1.00 75.07  ?  158 TYR C CE1   1 
ATOM   5655 C  CE2   . TYR C 1 165 ? 23.403  70.546  -57.122 1.00 73.20  ?  158 TYR C CE2   1 
ATOM   5656 C  CZ    . TYR C 1 165 ? 22.802  71.647  -57.707 1.00 75.54  ?  158 TYR C CZ    1 
ATOM   5657 O  OH    . TYR C 1 165 ? 22.998  71.910  -59.031 1.00 78.83  ?  158 TYR C OH    1 
ATOM   5658 N  N     . ASP C 1 166 ? 23.510  71.754  -50.252 1.00 70.09  ?  159 ASP C N     1 
ATOM   5659 C  CA    . ASP C 1 166 ? 23.217  71.765  -48.825 1.00 69.23  ?  159 ASP C CA    1 
ATOM   5660 C  C     . ASP C 1 166 ? 22.542  70.445  -48.431 1.00 64.29  ?  159 ASP C C     1 
ATOM   5661 O  O     . ASP C 1 166 ? 21.399  70.404  -47.965 1.00 62.37  ?  159 ASP C O     1 
ATOM   5662 C  CB    . ASP C 1 166 ? 22.379  72.994  -48.459 1.00 71.44  ?  159 ASP C CB    1 
ATOM   5663 C  CG    . ASP C 1 166 ? 22.093  73.132  -46.973 1.00 71.66  ?  159 ASP C CG    1 
ATOM   5664 O  OD1   . ASP C 1 166 ? 22.981  72.774  -46.182 1.00 72.30  ?  159 ASP C OD1   1 
ATOM   5665 O  OD2   . ASP C 1 166 ? 20.992  73.630  -46.624 1.00 71.79  -1 159 ASP C OD2   1 
ATOM   5666 N  N     . ILE C 1 167 ? 23.282  69.355  -48.632 1.00 62.83  ?  160 ILE C N     1 
ATOM   5667 C  CA    . ILE C 1 167 ? 22.849  68.023  -48.236 1.00 58.84  ?  160 ILE C CA    1 
ATOM   5668 C  C     . ILE C 1 167 ? 23.982  67.350  -47.458 1.00 59.38  ?  160 ILE C C     1 
ATOM   5669 O  O     . ILE C 1 167 ? 25.105  67.253  -47.966 1.00 61.63  ?  160 ILE C O     1 
ATOM   5670 C  CB    . ILE C 1 167 ? 22.479  67.182  -49.474 1.00 56.73  ?  160 ILE C CB    1 
ATOM   5671 C  CG1   . ILE C 1 167 ? 21.331  67.787  -50.287 1.00 56.54  ?  160 ILE C CG1   1 
ATOM   5672 C  CG2   . ILE C 1 167 ? 22.171  65.751  -49.055 1.00 53.34  ?  160 ILE C CG2   1 
ATOM   5673 C  CD1   . ILE C 1 167 ? 21.125  67.114  -51.620 1.00 55.70  ?  160 ILE C CD1   1 
ATOM   5674 N  N     . LYS C 1 168 ? 23.693  66.849  -46.243 1.00 57.76  ?  161 LYS C N     1 
ATOM   5675 C  CA    . LYS C 1 168 ? 24.721  66.153  -45.483 1.00 58.48  ?  161 LYS C CA    1 
ATOM   5676 C  C     . LYS C 1 168 ? 25.131  64.910  -46.271 1.00 56.91  ?  161 LYS C C     1 
ATOM   5677 O  O     . LYS C 1 168 ? 24.287  64.138  -46.726 1.00 53.84  ?  161 LYS C O     1 
ATOM   5678 C  CB    . LYS C 1 168 ? 24.246  65.846  -44.054 1.00 57.33  ?  161 LYS C CB    1 
ATOM   5679 C  CG    . LYS C 1 168 ? 23.936  67.086  -43.220 1.00 59.87  ?  161 LYS C CG    1 
ATOM   5680 C  CD    . LYS C 1 168 ? 23.190  66.831  -41.936 1.00 58.90  ?  161 LYS C CD    1 
ATOM   5681 C  CE    . LYS C 1 168 ? 24.018  66.139  -40.870 1.00 59.75  ?  161 LYS C CE    1 
ATOM   5682 N  NZ    . LYS C 1 168 ? 25.149  66.981  -40.408 1.00 64.42  ?  161 LYS C NZ    1 
ATOM   5683 N  N     . PHE C 1 169 ? 26.443  64.718  -46.438 1.00 59.67  ?  162 PHE C N     1 
ATOM   5684 C  CA    . PHE C 1 169 ? 26.963  63.626  -47.251 1.00 59.35  ?  162 PHE C CA    1 
ATOM   5685 C  C     . PHE C 1 169 ? 27.471  62.510  -46.349 1.00 58.89  ?  162 PHE C C     1 
ATOM   5686 O  O     . PHE C 1 169 ? 28.380  62.721  -45.540 1.00 61.66  ?  162 PHE C O     1 
ATOM   5687 C  CB    . PHE C 1 169 ? 28.102  64.129  -48.137 1.00 63.62  ?  162 PHE C CB    1 
ATOM   5688 C  CG    . PHE C 1 169 ? 28.858  63.087  -48.924 1.00 64.76  ?  162 PHE C CG    1 
ATOM   5689 C  CD1   . PHE C 1 169 ? 28.206  62.234  -49.792 1.00 62.28  ?  162 PHE C CD1   1 
ATOM   5690 C  CD2   . PHE C 1 169 ? 30.243  63.006  -48.840 1.00 69.13  ?  162 PHE C CD2   1 
ATOM   5691 C  CE1   . PHE C 1 169 ? 28.912  61.306  -50.546 1.00 64.09  ?  162 PHE C CE1   1 
ATOM   5692 C  CE2   . PHE C 1 169 ? 30.947  62.077  -49.593 1.00 70.96  ?  162 PHE C CE2   1 
ATOM   5693 C  CZ    . PHE C 1 169 ? 30.282  61.225  -50.435 1.00 68.43  ?  162 PHE C CZ    1 
ATOM   5694 N  N     . LYS C 1 170 ? 26.884  61.320  -46.527 1.00 55.87  ?  163 LYS C N     1 
ATOM   5695 C  CA    . LYS C 1 170 ? 27.231  60.126  -45.769 1.00 55.36  ?  163 LYS C CA    1 
ATOM   5696 C  C     . LYS C 1 170 ? 27.725  59.058  -46.731 1.00 56.06  ?  163 LYS C C     1 
ATOM   5697 O  O     . LYS C 1 170 ? 27.313  59.043  -47.883 1.00 55.50  ?  163 LYS C O     1 
ATOM   5698 C  CB    . LYS C 1 170 ? 25.990  59.658  -45.010 1.00 51.78  ?  163 LYS C CB    1 
ATOM   5699 C  CG    . LYS C 1 170 ? 25.960  58.205  -44.558 1.00 50.58  ?  163 LYS C CG    1 
ATOM   5700 C  CD    . LYS C 1 170 ? 24.700  57.970  -43.757 1.00 47.80  ?  163 LYS C CD    1 
ATOM   5701 C  CE    . LYS C 1 170 ? 24.353  56.506  -43.576 1.00 46.45  ?  163 LYS C CE    1 
ATOM   5702 N  NZ    . LYS C 1 170 ? 22.977  56.391  -43.032 1.00 44.17  ?  163 LYS C NZ    1 
ATOM   5703 N  N     . LEU C 1 171 ? 28.625  58.191  -46.251 1.00 57.87  ?  164 LEU C N     1 
ATOM   5704 C  CA    . LEU C 1 171 ? 29.142  57.059  -47.018 1.00 59.23  ?  164 LEU C CA    1 
ATOM   5705 C  C     . LEU C 1 171 ? 28.902  55.756  -46.266 1.00 57.77  ?  164 LEU C C     1 
ATOM   5706 O  O     . LEU C 1 171 ? 29.065  55.699  -45.045 1.00 57.77  ?  164 LEU C O     1 
ATOM   5707 C  CB    . LEU C 1 171 ? 30.645  57.272  -47.271 1.00 64.35  ?  164 LEU C CB    1 
ATOM   5708 C  CG    . LEU C 1 171 ? 31.432  56.106  -47.883 1.00 67.21  ?  164 LEU C CG    1 
ATOM   5709 C  CD1   . LEU C 1 171 ? 31.100  55.895  -49.354 1.00 67.35  ?  164 LEU C CD1   1 
ATOM   5710 C  CD2   . LEU C 1 171 ? 32.939  56.348  -47.742 1.00 72.86  ?  164 LEU C CD2   1 
ATOM   5711 N  N     . ASN C 1 172 ? 28.576  54.710  -47.035 1.00 57.21  ?  165 ASN C N     1 
ATOM   5712 C  CA    . ASN C 1 172 ? 28.198  53.402  -46.527 1.00 56.06  ?  165 ASN C CA    1 
ATOM   5713 C  C     . ASN C 1 172 ? 29.094  52.351  -47.142 1.00 59.51  ?  165 ASN C C     1 
ATOM   5714 O  O     . ASN C 1 172 ? 29.051  52.128  -48.349 1.00 60.58  ?  165 ASN C O     1 
ATOM   5715 C  CB    . ASN C 1 172 ? 26.781  52.943  -46.893 1.00 52.75  ?  165 ASN C CB    1 
ATOM   5716 C  CG    . ASN C 1 172 ? 25.724  53.415  -45.923 1.00 49.57  ?  165 ASN C CG    1 
ATOM   5717 O  OD1   . ASN C 1 172 ? 25.936  54.392  -45.217 1.00 49.58  ?  165 ASN C OD1   1 
ATOM   5718 N  ND2   . ASN C 1 172 ? 24.566  52.767  -45.946 1.00 47.45  ?  165 ASN C ND2   1 
ATOM   5719 N  N     . THR C 1 173 ? 29.884  51.710  -46.278 1.00 61.64  ?  166 THR C N     1 
ATOM   5720 C  CA    . THR C 1 173 ? 30.829  50.682  -46.674 1.00 65.72  ?  166 THR C CA    1 
ATOM   5721 C  C     . THR C 1 173 ? 30.378  49.353  -46.079 1.00 64.93  ?  166 THR C C     1 
ATOM   5722 O  O     . THR C 1 173 ? 30.201  49.255  -44.867 1.00 63.65  ?  166 THR C O     1 
ATOM   5723 C  CB    . THR C 1 173 ? 32.239  50.996  -46.154 1.00 70.07  ?  166 THR C CB    1 
ATOM   5724 O  OG1   . THR C 1 173 ? 32.655  52.302  -46.566 1.00 71.22  ?  166 THR C OG1   1 
ATOM   5725 C  CG2   . THR C 1 173 ? 33.251  49.969  -46.610 1.00 75.10  ?  166 THR C CG2   1 
ATOM   5726 N  N     . VAL C 1 174 ? 30.260  48.319  -46.911 1.00 66.42  ?  167 VAL C N     1 
ATOM   5727 C  CA    . VAL C 1 174 ? 30.143  46.963  -46.382 1.00 67.36  ?  167 VAL C CA    1 
ATOM   5728 C  C     . VAL C 1 174 ? 31.539  46.315  -46.345 1.00 72.93  ?  167 VAL C C     1 
ATOM   5729 O  O     . VAL C 1 174 ? 32.175  46.161  -47.388 1.00 76.56  ?  167 VAL C O     1 
ATOM   5730 C  CB    . VAL C 1 174 ? 29.171  46.131  -47.226 1.00 66.53  ?  167 VAL C CB    1 
ATOM   5731 C  CG1   . VAL C 1 174 ? 29.086  44.707  -46.711 1.00 68.27  ?  167 VAL C CG1   1 
ATOM   5732 C  CG2   . VAL C 1 174 ? 27.787  46.766  -47.299 1.00 61.75  ?  167 VAL C CG2   1 
ATOM   5733 N  N     . VAL C 1 175 ? 31.997  45.932  -45.140 1.00 74.07  ?  168 VAL C N     1 
ATOM   5734 C  CA    . VAL C 1 175 ? 33.318  45.350  -44.921 1.00 79.72  ?  168 VAL C CA    1 
ATOM   5735 C  C     . VAL C 1 175 ? 33.197  43.839  -45.115 1.00 82.12  ?  168 VAL C C     1 
ATOM   5736 O  O     . VAL C 1 175 ? 32.397  43.210  -44.439 1.00 79.82  ?  168 VAL C O     1 
ATOM   5737 C  CB    . VAL C 1 175 ? 33.886  45.700  -43.527 1.00 80.42  ?  168 VAL C CB    1 
ATOM   5738 C  CG1   . VAL C 1 175 ? 35.351  45.298  -43.375 1.00 86.99  ?  168 VAL C CG1   1 
ATOM   5739 C  CG2   . VAL C 1 175 ? 33.736  47.184  -43.217 1.00 77.63  ?  168 VAL C CG2   1 
ATOM   5740 N  N     . ASN C 1 176 ? 34.011  43.289  -46.033 1.00 87.33  ?  169 ASN C N     1 
ATOM   5741 C  CA    . ASN C 1 176 ? 33.833  41.947  -46.566 1.00 90.20  ?  169 ASN C CA    1 
ATOM   5742 C  C     . ASN C 1 176 ? 35.192  41.286  -46.829 1.00 97.74  ?  169 ASN C C     1 
ATOM   5743 O  O     . ASN C 1 176 ? 36.256  41.905  -46.675 1.00 100.75 ?  169 ASN C O     1 
ATOM   5744 C  CB    . ASN C 1 176 ? 33.005  41.984  -47.853 1.00 88.64  ?  169 ASN C CB    1 
ATOM   5745 C  CG    . ASN C 1 176 ? 33.621  42.854  -48.929 1.00 90.65  ?  169 ASN C CG    1 
ATOM   5746 O  OD1   . ASN C 1 176 ? 34.556  42.451  -49.612 1.00 96.56  ?  169 ASN C OD1   1 
ATOM   5747 N  ND2   . ASN C 1 176 ? 33.080  44.049  -49.125 1.00 86.24  ?  169 ASN C ND2   1 
ATOM   5748 N  N     . LYS C 1 177 ? 35.142  40.017  -47.256 1.00 101.40 ?  170 LYS C N     1 
ATOM   5749 C  CA    . LYS C 1 177 ? 36.347  39.258  -47.551 1.00 109.27 ?  170 LYS C CA    1 
ATOM   5750 C  C     . LYS C 1 177 ? 37.201  40.014  -48.567 1.00 112.83 ?  170 LYS C C     1 
ATOM   5751 O  O     . LYS C 1 177 ? 38.428  40.023  -48.465 1.00 118.68 ?  170 LYS C O     1 
ATOM   5752 C  CB    . LYS C 1 177 ? 35.975  37.852  -48.042 1.00 112.60 ?  170 LYS C CB    1 
ATOM   5753 C  CG    . LYS C 1 177 ? 37.135  36.929  -48.402 1.00 121.53 ?  170 LYS C CG    1 
ATOM   5754 C  CD    . LYS C 1 177 ? 38.292  36.875  -47.399 1.00 125.52 ?  170 LYS C CD    1 
ATOM   5755 C  CE    . LYS C 1 177 ? 37.864  36.811  -45.946 1.00 121.33 ?  170 LYS C CE    1 
ATOM   5756 N  NZ    . LYS C 1 177 ? 38.970  36.414  -45.045 1.00 126.81 ?  170 LYS C NZ    1 
ATOM   5757 N  N     . PHE C 1 178 ? 36.546  40.672  -49.529 1.00 109.70 ?  171 PHE C N     1 
ATOM   5758 C  CA    . PHE C 1 178 ? 37.252  41.193  -50.687 1.00 113.95 ?  171 PHE C CA    1 
ATOM   5759 C  C     . PHE C 1 178 ? 37.904  42.548  -50.406 1.00 113.26 ?  171 PHE C C     1 
ATOM   5760 O  O     . PHE C 1 178 ? 38.769  42.971  -51.182 1.00 118.29 ?  171 PHE C O     1 
ATOM   5761 C  CB    . PHE C 1 178 ? 36.318  41.235  -51.897 1.00 112.00 ?  171 PHE C CB    1 
ATOM   5762 C  CG    . PHE C 1 178 ? 35.845  39.876  -52.347 1.00 114.66 ?  171 PHE C CG    1 
ATOM   5763 C  CD1   . PHE C 1 178 ? 36.756  38.890  -52.687 1.00 122.71 ?  171 PHE C CD1   1 
ATOM   5764 C  CD2   . PHE C 1 178 ? 34.494  39.579  -52.436 1.00 109.84 ?  171 PHE C CD2   1 
ATOM   5765 C  CE1   . PHE C 1 178 ? 36.328  37.637  -53.097 1.00 125.82 ?  171 PHE C CE1   1 
ATOM   5766 C  CE2   . PHE C 1 178 ? 34.068  38.326  -52.849 1.00 113.00 ?  171 PHE C CE2   1 
ATOM   5767 C  CZ    . PHE C 1 178 ? 34.984  37.358  -53.179 1.00 120.96 ?  171 PHE C CZ    1 
ATOM   5768 N  N     . ASN C 1 179 ? 37.511  43.245  -49.328 1.00 107.74 ?  172 ASN C N     1 
ATOM   5769 C  CA    . ASN C 1 179 ? 38.039  44.588  -49.121 1.00 107.28 ?  172 ASN C CA    1 
ATOM   5770 C  C     . ASN C 1 179 ? 38.487  44.827  -47.678 1.00 106.90 ?  172 ASN C C     1 
ATOM   5771 O  O     . ASN C 1 179 ? 38.793  45.977  -47.322 1.00 106.06 ?  172 ASN C O     1 
ATOM   5772 C  CB    . ASN C 1 179 ? 37.026  45.662  -49.533 1.00 101.00 ?  172 ASN C CB    1 
ATOM   5773 C  CG    . ASN C 1 179 ? 35.792  45.686  -48.659 1.00 93.81  ?  172 ASN C CG    1 
ATOM   5774 O  OD1   . ASN C 1 179 ? 35.535  44.739  -47.919 1.00 93.29  ?  172 ASN C OD1   1 
ATOM   5775 N  ND2   . ASN C 1 179 ? 35.025  46.763  -48.738 1.00 88.78  ?  172 ASN C ND2   1 
ATOM   5776 N  N     . HIS C 1 180 ? 38.572  43.764  -46.862 1.00 108.20 ?  173 HIS C N     1 
ATOM   5777 C  CA    . HIS C 1 180 ? 38.780  43.947  -45.432 1.00 107.20 ?  173 HIS C CA    1 
ATOM   5778 C  C     . HIS C 1 180 ? 40.214  44.357  -45.108 1.00 113.72 ?  173 HIS C C     1 
ATOM   5779 O  O     . HIS C 1 180 ? 40.464  44.813  -43.996 1.00 113.28 ?  173 HIS C O     1 
ATOM   5780 C  CB    . HIS C 1 180 ? 38.385  42.718  -44.606 1.00 106.74 ?  173 HIS C CB    1 
ATOM   5781 C  CG    . HIS C 1 180 ? 39.196  41.500  -44.863 1.00 113.78 ?  173 HIS C CG    1 
ATOM   5782 N  ND1   . HIS C 1 180 ? 39.221  40.849  -46.075 1.00 116.92 ?  173 HIS C ND1   1 
ATOM   5783 C  CD2   . HIS C 1 180 ? 40.000  40.807  -44.047 1.00 118.75 ?  173 HIS C CD2   1 
ATOM   5784 C  CE1   . HIS C 1 180 ? 40.021  39.798  -45.982 1.00 123.70 ?  173 HIS C CE1   1 
ATOM   5785 N  NE2   . HIS C 1 180 ? 40.499  39.755  -44.760 1.00 124.83 ?  173 HIS C NE2   1 
ATOM   5786 N  N     . LEU C 1 181 ? 41.151  44.173  -46.048 1.00 120.35 ?  174 LEU C N     1 
ATOM   5787 C  CA    . LEU C 1 181 ? 42.521  44.623  -45.849 1.00 127.36 ?  174 LEU C CA    1 
ATOM   5788 C  C     . LEU C 1 181 ? 42.746  46.021  -46.430 1.00 127.23 ?  174 LEU C C     1 
ATOM   5789 O  O     . LEU C 1 181 ? 43.789  46.613  -46.165 1.00 132.59 ?  174 LEU C O     1 
ATOM   5790 C  CB    . LEU C 1 181 ? 43.492  43.620  -46.485 1.00 135.96 ?  174 LEU C CB    1 
ATOM   5791 C  CG    . LEU C 1 181 ? 43.690  42.299  -45.740 1.00 138.84 ?  174 LEU C CG    1 
ATOM   5792 C  CD1   . LEU C 1 181 ? 44.829  41.503  -46.361 1.00 148.76 ?  174 LEU C CD1   1 
ATOM   5793 C  CD2   . LEU C 1 181 ? 43.957  42.526  -44.259 1.00 138.30 ?  174 LEU C CD2   1 
ATOM   5794 N  N     . GLU C 1 182 ? 41.789  46.563  -47.205 1.00 121.69 ?  175 GLU C N     1 
ATOM   5795 C  CA    . GLU C 1 182 ? 42.051  47.782  -47.958 1.00 122.69 ?  175 GLU C CA    1 
ATOM   5796 C  C     . GLU C 1 182 ? 42.262  48.958  -47.001 1.00 121.43 ?  175 GLU C C     1 
ATOM   5797 O  O     . GLU C 1 182 ? 41.792  48.931  -45.864 1.00 117.39 ?  175 GLU C O     1 
ATOM   5798 C  CB    . GLU C 1 182 ? 40.922  48.071  -48.948 1.00 117.15 ?  175 GLU C CB    1 
ATOM   5799 N  N     . ASP C 1 183 ? 43.004  49.971  -47.470 1.00 125.69 ?  176 ASP C N     1 
ATOM   5800 C  CA    . ASP C 1 183 ? 43.183  51.228  -46.760 1.00 125.17 ?  176 ASP C CA    1 
ATOM   5801 C  C     . ASP C 1 183 ? 42.423  52.318  -47.515 1.00 120.81 ?  176 ASP C C     1 
ATOM   5802 O  O     . ASP C 1 183 ? 42.693  52.563  -48.687 1.00 123.85 ?  176 ASP C O     1 
ATOM   5803 C  CB    . ASP C 1 183 ? 44.675  51.551  -46.629 1.00 134.53 ?  176 ASP C CB    1 
ATOM   5804 C  CG    . ASP C 1 183 ? 45.013  52.692  -45.682 1.00 135.52 ?  176 ASP C CG    1 
ATOM   5805 O  OD1   . ASP C 1 183 ? 44.066  53.316  -45.147 1.00 128.75 -1 176 ASP C OD1   1 
ATOM   5806 O  OD2   . ASP C 1 183 ? 46.231  52.941  -45.476 1.00 143.66 ?  176 ASP C OD2   1 
ATOM   5807 N  N     . MET C 1 184 ? 41.476  52.973  -46.837 1.00 114.19 ?  177 MET C N     1 
ATOM   5808 C  CA    . MET C 1 184 ? 40.614  53.957  -47.475 1.00 109.66 ?  177 MET C CA    1 
ATOM   5809 C  C     . MET C 1 184 ? 40.865  55.346  -46.884 1.00 110.63 ?  177 MET C C     1 
ATOM   5810 O  O     . MET C 1 184 ? 40.075  56.258  -47.116 1.00 106.57 ?  177 MET C O     1 
ATOM   5811 C  CB    . MET C 1 184 ? 39.142  53.594  -47.262 1.00 101.30 ?  177 MET C CB    1 
ATOM   5812 C  CG    . MET C 1 184 ? 38.711  52.301  -47.931 1.00 100.09 ?  177 MET C CG    1 
ATOM   5813 S  SD    . MET C 1 184 ? 36.937  52.028  -47.706 1.00 90.97  ?  177 MET C SD    1 
ATOM   5814 C  CE    . MET C 1 184 ? 36.834  50.246  -47.860 1.00 91.82  ?  177 MET C CE    1 
ATOM   5815 N  N     . ASN C 1 185 ? 41.983  55.525  -46.163 1.00 116.71 ?  178 ASN C N     1 
ATOM   5816 C  CA    . ASN C 1 185 ? 42.140  56.676  -45.279 1.00 117.54 ?  178 ASN C CA    1 
ATOM   5817 C  C     . ASN C 1 185 ? 42.290  57.976  -46.085 1.00 119.79 ?  178 ASN C C     1 
ATOM   5818 O  O     . ASN C 1 185 ? 41.693  59.039  -45.700 1.00 116.83 ?  178 ASN C O     1 
ATOM   5819 C  CB    . ASN C 1 185 ? 43.279  56.486  -44.266 1.00 124.00 ?  178 ASN C CB    1 
ATOM   5820 C  CG    . ASN C 1 185 ? 42.841  55.858  -42.953 1.00 120.48 ?  178 ASN C CG    1 
ATOM   5821 O  OD1   . ASN C 1 185 ? 41.981  56.400  -42.258 1.00 115.44 ?  178 ASN C OD1   1 
ATOM   5822 N  ND2   . ASN C 1 185 ? 43.447  54.739  -42.582 1.00 123.72 ?  178 ASN C ND2   1 
ATOM   5823 N  N     . ASP C 1 186 ? 43.081  57.919  -47.183 1.00 125.54 ?  179 ASP C N     1 
ATOM   5824 C  CA    . ASP C 1 186 ? 43.245  59.079  -48.049 1.00 128.28 ?  179 ASP C CA    1 
ATOM   5825 C  C     . ASP C 1 186 ? 41.885  59.440  -48.644 1.00 120.64 ?  179 ASP C C     1 
ATOM   5826 O  O     . ASP C 1 186 ? 41.414  60.572  -48.510 1.00 118.77 ?  179 ASP C O     1 
ATOM   5827 C  CB    . ASP C 1 186 ? 44.299  58.832  -49.140 1.00 136.17 ?  179 ASP C CB    1 
ATOM   5828 C  CG    . ASP C 1 186 ? 45.754  58.956  -48.707 1.00 145.78 ?  179 ASP C CG    1 
ATOM   5829 O  OD1   . ASP C 1 186 ? 46.022  59.562  -47.649 1.00 147.15 -1 179 ASP C OD1   1 
ATOM   5830 O  OD2   . ASP C 1 186 ? 46.617  58.441  -49.441 1.00 152.43 ?  179 ASP C OD2   1 
ATOM   5831 N  N     . HIS C 1 187 ? 41.233  58.452  -49.266 1.00 116.58 ?  180 HIS C N     1 
ATOM   5832 C  CA    . HIS C 1 187 ? 39.959  58.664  -49.937 1.00 110.08 ?  180 HIS C CA    1 
ATOM   5833 C  C     . HIS C 1 187 ? 38.923  59.275  -48.993 1.00 103.71 ?  180 HIS C C     1 
ATOM   5834 O  O     . HIS C 1 187 ? 38.179  60.158  -49.409 1.00 100.91 ?  180 HIS C O     1 
ATOM   5835 C  CB    . HIS C 1 187 ? 39.488  57.373  -50.612 1.00 107.61 ?  180 HIS C CB    1 
ATOM   5836 C  CG    . HIS C 1 187 ? 40.241  57.095  -51.871 1.00 113.68 ?  180 HIS C CG    1 
ATOM   5837 N  ND1   . HIS C 1 187 ? 39.954  57.746  -53.054 1.00 114.26 ?  180 HIS C ND1   1 
ATOM   5838 C  CD2   . HIS C 1 187 ? 41.249  56.258  -52.138 1.00 119.90 ?  180 HIS C CD2   1 
ATOM   5839 C  CE1   . HIS C 1 187 ? 40.778  57.309  -53.997 1.00 120.73 ?  180 HIS C CE1   1 
ATOM   5840 N  NE2   . HIS C 1 187 ? 41.569  56.407  -53.461 1.00 124.29 ?  180 HIS C NE2   1 
ATOM   5841 N  N     . LEU C 1 188 ? 38.906  58.831  -47.729 1.00 102.10 ?  181 LEU C N     1 
ATOM   5842 C  CA    . LEU C 1 188 ? 38.019  59.403  -46.724 1.00 97.17  ?  181 LEU C CA    1 
ATOM   5843 C  C     . LEU C 1 188 ? 38.425  60.835  -46.355 1.00 100.62 ?  181 LEU C C     1 
ATOM   5844 O  O     . LEU C 1 188 ? 37.552  61.676  -46.141 1.00 97.08  ?  181 LEU C O     1 
ATOM   5845 C  CB    . LEU C 1 188 ? 37.983  58.488  -45.491 1.00 95.55  ?  181 LEU C CB    1 
ATOM   5846 C  CG    . LEU C 1 188 ? 36.768  57.562  -45.383 1.00 88.78  ?  181 LEU C CG    1 
ATOM   5847 C  CD1   . LEU C 1 188 ? 35.504  58.348  -45.050 1.00 83.28  ?  181 LEU C CD1   1 
ATOM   5848 C  CD2   . LEU C 1 188 ? 36.561  56.758  -46.661 1.00 88.08  ?  181 LEU C CD2   1 
ATOM   5849 N  N     . ASN C 1 189 ? 39.737  61.115  -46.274 1.00 108.07 ?  182 ASN C N     1 
ATOM   5850 C  CA    . ASN C 1 189 ? 40.226  62.417  -45.830 1.00 112.48 ?  182 ASN C CA    1 
ATOM   5851 C  C     . ASN C 1 189 ? 39.875  63.509  -46.842 1.00 112.69 ?  182 ASN C C     1 
ATOM   5852 O  O     . ASN C 1 189 ? 39.655  64.656  -46.456 1.00 113.36 ?  182 ASN C O     1 
ATOM   5853 C  CB    . ASN C 1 189 ? 41.733  62.401  -45.546 1.00 121.24 ?  182 ASN C CB    1 
ATOM   5854 C  CG    . ASN C 1 189 ? 42.091  61.809  -44.197 1.00 122.15 ?  182 ASN C CG    1 
ATOM   5855 O  OD1   . ASN C 1 189 ? 41.241  61.652  -43.320 1.00 116.72 ?  182 ASN C OD1   1 
ATOM   5856 N  ND2   . ASN C 1 189 ? 43.361  61.496  -44.006 1.00 129.59 ?  182 ASN C ND2   1 
ATOM   5857 N  N     . ALA C 1 190 ? 39.833  63.151  -48.130 1.00 112.65 ?  183 ALA C N     1 
ATOM   5858 C  CA    . ALA C 1 190 ? 39.402  64.069  -49.174 1.00 112.53 ?  183 ALA C CA    1 
ATOM   5859 C  C     . ALA C 1 190 ? 37.890  64.293  -49.109 1.00 104.62 ?  183 ALA C C     1 
ATOM   5860 O  O     . ALA C 1 190 ? 37.438  65.434  -49.043 1.00 104.29 ?  183 ALA C O     1 
ATOM   5861 C  CB    . ALA C 1 190 ? 39.817  63.531  -50.521 1.00 115.33 ?  183 ALA C CB    1 
ATOM   5862 N  N     . LEU C 1 191 ? 37.123  63.192  -49.129 1.00 98.90  ?  184 LEU C N     1 
ATOM   5863 C  CA    . LEU C 1 191 ? 35.671  63.219  -49.302 1.00 91.96  ?  184 LEU C CA    1 
ATOM   5864 C  C     . LEU C 1 191 ? 34.984  63.881  -48.103 1.00 88.97  ?  184 LEU C C     1 
ATOM   5865 O  O     . LEU C 1 191 ? 33.979  64.572  -48.278 1.00 85.78  ?  184 LEU C O     1 
ATOM   5866 C  CB    . LEU C 1 191 ? 35.164  61.785  -49.505 1.00 87.85  ?  184 LEU C CB    1 
ATOM   5867 C  CG    . LEU C 1 191 ? 35.481  61.135  -50.853 1.00 90.00  ?  184 LEU C CG    1 
ATOM   5868 C  CD1   . LEU C 1 191 ? 35.307  59.622  -50.796 1.00 87.77  ?  184 LEU C CD1   1 
ATOM   5869 C  CD2   . LEU C 1 191 ? 34.585  61.714  -51.939 1.00 87.82  ?  184 LEU C CD2   1 
ATOM   5870 N  N     . GLN C 1 192 ? 35.531  63.647  -46.899 1.00 90.52  ?  185 GLN C N     1 
ATOM   5871 C  CA    . GLN C 1 192 ? 35.039  64.194  -45.639 1.00 88.87  ?  185 GLN C CA    1 
ATOM   5872 C  C     . GLN C 1 192 ? 33.528  64.006  -45.464 1.00 81.96  ?  185 GLN C C     1 
ATOM   5873 O  O     . GLN C 1 192 ? 32.805  64.965  -45.171 1.00 80.78  ?  185 GLN C O     1 
ATOM   5874 C  CB    . GLN C 1 192 ? 35.395  65.674  -45.496 1.00 93.37  ?  185 GLN C CB    1 
ATOM   5875 C  CG    . GLN C 1 192 ? 36.876  65.915  -45.245 1.00 100.96 ?  185 GLN C CG    1 
ATOM   5876 C  CD    . GLN C 1 192 ? 37.075  67.185  -44.456 1.00 104.92 ?  185 GLN C CD    1 
ATOM   5877 O  OE1   . GLN C 1 192 ? 36.631  68.260  -44.858 1.00 105.38 ?  185 GLN C OE1   1 
ATOM   5878 N  NE2   . GLN C 1 192 ? 37.713  67.061  -43.302 1.00 108.10 ?  185 GLN C NE2   1 
ATOM   5879 N  N     . PRO C 1 193 ? 33.001  62.762  -45.547 1.00 77.76  ?  186 PRO C N     1 
ATOM   5880 C  CA    . PRO C 1 193 ? 31.657  62.479  -45.023 1.00 72.11  ?  186 PRO C CA    1 
ATOM   5881 C  C     . PRO C 1 193 ? 31.515  62.805  -43.541 1.00 72.22  ?  186 PRO C C     1 
ATOM   5882 O  O     . PRO C 1 193 ? 32.458  62.612  -42.775 1.00 75.63  ?  186 PRO C O     1 
ATOM   5883 C  CB    . PRO C 1 193 ? 31.502  60.971  -45.219 1.00 69.55  ?  186 PRO C CB    1 
ATOM   5884 C  CG    . PRO C 1 193 ? 32.917  60.472  -45.380 1.00 74.37  ?  186 PRO C CG    1 
ATOM   5885 C  CD    . PRO C 1 193 ? 33.643  61.570  -46.127 1.00 78.85  ?  186 PRO C CD    1 
ATOM   5886 N  N     . PHE C 1 194 ? 30.346  63.336  -43.153 1.00 69.14  ?  187 PHE C N     1 
ATOM   5887 C  CA    . PHE C 1 194 ? 30.060  63.620  -41.761 1.00 69.33  ?  187 PHE C CA    1 
ATOM   5888 C  C     . PHE C 1 194 ? 29.786  62.314  -41.008 1.00 66.69  ?  187 PHE C C     1 
ATOM   5889 O  O     . PHE C 1 194 ? 29.906  62.253  -39.786 1.00 67.90  ?  187 PHE C O     1 
ATOM   5890 C  CB    . PHE C 1 194 ? 28.877  64.580  -41.618 1.00 67.56  ?  187 PHE C CB    1 
ATOM   5891 C  CG    . PHE C 1 194 ? 27.541  63.887  -41.539 1.00 62.52  ?  187 PHE C CG    1 
ATOM   5892 C  CD1   . PHE C 1 194 ? 26.928  63.395  -42.680 1.00 59.39  ?  187 PHE C CD1   1 
ATOM   5893 C  CD2   . PHE C 1 194 ? 26.927  63.673  -40.312 1.00 61.53  ?  187 PHE C CD2   1 
ATOM   5894 C  CE1   . PHE C 1 194 ? 25.711  62.737  -42.598 1.00 55.46  ?  187 PHE C CE1   1 
ATOM   5895 C  CE2   . PHE C 1 194 ? 25.699  63.033  -40.234 1.00 57.60  ?  187 PHE C CE2   1 
ATOM   5896 C  CZ    . PHE C 1 194 ? 25.102  62.557  -41.381 1.00 54.62  ?  187 PHE C CZ    1 
ATOM   5897 N  N     . ARG C 1 195 ? 29.417  61.265  -41.740 1.00 63.56  ?  188 ARG C N     1 
ATOM   5898 C  CA    . ARG C 1 195 ? 29.064  59.985  -41.137 1.00 61.19  ?  188 ARG C CA    1 
ATOM   5899 C  C     . ARG C 1 195 ? 29.486  58.876  -42.085 1.00 60.89  ?  188 ARG C C     1 
ATOM   5900 O  O     . ARG C 1 195 ? 29.102  58.927  -43.240 1.00 59.49  ?  188 ARG C O     1 
ATOM   5901 C  CB    . ARG C 1 195 ? 27.555  59.905  -40.941 1.00 57.03  ?  188 ARG C CB    1 
ATOM   5902 C  CG    . ARG C 1 195 ? 27.078  58.643  -40.237 1.00 54.98  ?  188 ARG C CG    1 
ATOM   5903 C  CD    . ARG C 1 195 ? 25.640  58.859  -39.881 1.00 52.18  ?  188 ARG C CD    1 
ATOM   5904 N  NE    . ARG C 1 195 ? 25.088  57.744  -39.137 1.00 50.71  ?  188 ARG C NE    1 
ATOM   5905 C  CZ    . ARG C 1 195 ? 25.361  57.484  -37.869 1.00 52.27  ?  188 ARG C CZ    1 
ATOM   5906 N  NH1   . ARG C 1 195 ? 26.172  58.271  -37.188 1.00 55.43  ?  188 ARG C NH1   1 
ATOM   5907 N  NH2   . ARG C 1 195 ? 24.831  56.419  -37.298 1.00 51.15  ?  188 ARG C NH2   1 
ATOM   5908 N  N     . TRP C 1 196 ? 30.282  57.913  -41.611 1.00 62.74  ?  189 TRP C N     1 
ATOM   5909 C  CA    . TRP C 1 196 ? 30.750  56.818  -42.458 1.00 63.34  ?  189 TRP C CA    1 
ATOM   5910 C  C     . TRP C 1 196 ? 30.355  55.480  -41.838 1.00 61.59  ?  189 TRP C C     1 
ATOM   5911 O  O     . TRP C 1 196 ? 30.917  55.112  -40.810 1.00 63.60  ?  189 TRP C O     1 
ATOM   5912 C  CB    . TRP C 1 196 ? 32.275  56.928  -42.641 1.00 68.76  ?  189 TRP C CB    1 
ATOM   5913 C  CG    . TRP C 1 196 ? 32.884  55.747  -43.361 1.00 70.52  ?  189 TRP C CG    1 
ATOM   5914 C  CD1   . TRP C 1 196 ? 32.259  55.000  -44.306 1.00 68.15  ?  189 TRP C CD1   1 
ATOM   5915 C  CD2   . TRP C 1 196 ? 34.207  55.178  -43.218 1.00 75.63  ?  189 TRP C CD2   1 
ATOM   5916 N  NE1   . TRP C 1 196 ? 33.077  53.996  -44.752 1.00 71.36  ?  189 TRP C NE1   1 
ATOM   5917 C  CE2   . TRP C 1 196 ? 34.282  54.087  -44.113 1.00 76.00  ?  189 TRP C CE2   1 
ATOM   5918 C  CE3   . TRP C 1 196 ? 35.330  55.483  -42.438 1.00 80.47  ?  189 TRP C CE3   1 
ATOM   5919 C  CZ2   . TRP C 1 196 ? 35.425  53.306  -44.245 1.00 81.01  ?  189 TRP C CZ2   1 
ATOM   5920 C  CZ3   . TRP C 1 196 ? 36.459  54.703  -42.563 1.00 85.37  ?  189 TRP C CZ3   1 
ATOM   5921 C  CH2   . TRP C 1 196 ? 36.498  53.623  -43.449 1.00 85.60  ?  189 TRP C CH2   1 
ATOM   5922 N  N     . LYS C 1 197 ? 29.411  54.739  -42.462 1.00 58.39  ?  190 LYS C N     1 
ATOM   5923 C  CA    . LYS C 1 197 ? 28.940  53.465  -41.931 1.00 57.03  ?  190 LYS C CA    1 
ATOM   5924 C  C     . LYS C 1 197 ? 29.784  52.328  -42.474 1.00 59.71  ?  190 LYS C C     1 
ATOM   5925 O  O     . LYS C 1 197 ? 29.885  52.155  -43.677 1.00 60.23  ?  190 LYS C O     1 
ATOM   5926 C  CB    . LYS C 1 197 ? 27.486  53.139  -42.311 1.00 53.11  ?  190 LYS C CB    1 
ATOM   5927 C  CG    . LYS C 1 197 ? 26.458  54.183  -41.909 1.00 50.63  ?  190 LYS C CG    1 
ATOM   5928 C  CD    . LYS C 1 197 ? 26.398  54.488  -40.439 1.00 51.05  ?  190 LYS C CD    1 
ATOM   5929 C  CE    . LYS C 1 197 ? 25.729  53.409  -39.621 1.00 49.99  ?  190 LYS C CE    1 
ATOM   5930 N  NZ    . LYS C 1 197 ? 24.251  53.352  -39.774 1.00 47.13  ?  190 LYS C NZ    1 
ATOM   5931 N  N     . CYS C 1 198 ? 30.381  51.543  -41.565 1.00 61.86  ?  191 CYS C N     1 
ATOM   5932 C  CA    . CYS C 1 198 ? 31.081  50.327  -41.950 1.00 64.75  ?  191 CYS C CA    1 
ATOM   5933 C  C     . CYS C 1 198 ? 30.394  49.107  -41.361 1.00 63.41  ?  191 CYS C C     1 
ATOM   5934 O  O     . CYS C 1 198 ? 30.464  48.883  -40.149 1.00 63.95  ?  191 CYS C O     1 
ATOM   5935 C  CB    . CYS C 1 198 ? 32.530  50.361  -41.476 1.00 69.78  ?  191 CYS C CB    1 
ATOM   5936 S  SG    . CYS C 1 198 ? 33.491  51.652  -42.302 1.00 72.85  ?  191 CYS C SG    1 
ATOM   5937 N  N     . PHE C 1 199 ? 29.740  48.327  -42.226 1.00 62.20  ?  192 PHE C N     1 
ATOM   5938 C  CA    . PHE C 1 199 ? 28.944  47.200  -41.781 1.00 61.11  ?  192 PHE C CA    1 
ATOM   5939 C  C     . PHE C 1 199 ? 29.792  45.963  -41.929 1.00 65.22  ?  192 PHE C C     1 
ATOM   5940 O  O     . PHE C 1 199 ? 30.308  45.727  -43.010 1.00 67.47  ?  192 PHE C O     1 
ATOM   5941 C  CB    . PHE C 1 199 ? 27.677  46.963  -42.614 1.00 58.22  ?  192 PHE C CB    1 
ATOM   5942 C  CG    . PHE C 1 199 ? 26.828  48.188  -42.849 1.00 54.74  ?  192 PHE C CG    1 
ATOM   5943 C  CD1   . PHE C 1 199 ? 26.124  48.779  -41.813 1.00 52.46  ?  192 PHE C CD1   1 
ATOM   5944 C  CD2   . PHE C 1 199 ? 26.727  48.747  -44.113 1.00 54.27  ?  192 PHE C CD2   1 
ATOM   5945 C  CE1   . PHE C 1 199 ? 25.373  49.924  -42.026 1.00 49.91  ?  192 PHE C CE1   1 
ATOM   5946 C  CE2   . PHE C 1 199 ? 25.946  49.874  -44.333 1.00 51.50  ?  192 PHE C CE2   1 
ATOM   5947 C  CZ    . PHE C 1 199 ? 25.277  50.464  -43.288 1.00 49.37  ?  192 PHE C CZ    1 
ATOM   5948 N  N     . GLN C 1 200 ? 29.935  45.202  -40.842 1.00 66.63  ?  193 GLN C N     1 
ATOM   5949 C  CA    . GLN C 1 200 ? 30.365  43.830  -40.986 1.00 70.22  ?  193 GLN C CA    1 
ATOM   5950 C  C     . GLN C 1 200 ? 29.329  43.177  -41.881 1.00 68.62  ?  193 GLN C C     1 
ATOM   5951 O  O     . GLN C 1 200 ? 28.155  43.184  -41.542 1.00 65.37  ?  193 GLN C O     1 
ATOM   5952 C  CB    . GLN C 1 200 ? 30.447  43.085  -39.652 1.00 71.75  ?  193 GLN C CB    1 
ATOM   5953 C  CG    . GLN C 1 200 ? 30.779  41.603  -39.825 1.00 75.74  ?  193 GLN C CG    1 
ATOM   5954 C  CD    . GLN C 1 200 ? 30.995  40.877  -38.519 1.00 78.03  ?  193 GLN C CD    1 
ATOM   5955 O  OE1   . GLN C 1 200 ? 30.641  41.358  -37.446 1.00 76.14  ?  193 GLN C OE1   1 
ATOM   5956 N  NE2   . GLN C 1 200 ? 31.566  39.686  -38.605 1.00 82.60  ?  193 GLN C NE2   1 
ATOM   5957 N  N     . VAL C 1 201 ? 29.768  42.658  -43.034 1.00 71.43  ?  194 VAL C N     1 
ATOM   5958 C  CA    . VAL C 1 201 ? 28.861  41.970  -43.935 1.00 70.92  ?  194 VAL C CA    1 
ATOM   5959 C  C     . VAL C 1 201 ? 28.010  41.001  -43.112 1.00 70.44  ?  194 VAL C C     1 
ATOM   5960 O  O     . VAL C 1 201 ? 28.496  40.400  -42.145 1.00 72.66  ?  194 VAL C O     1 
ATOM   5961 C  CB    . VAL C 1 201 ? 29.629  41.284  -45.080 1.00 75.66  ?  194 VAL C CB    1 
ATOM   5962 C  CG1   . VAL C 1 201 ? 30.535  40.172  -44.575 1.00 80.74  ?  194 VAL C CG1   1 
ATOM   5963 C  CG2   . VAL C 1 201 ? 28.676  40.772  -46.148 1.00 75.35  ?  194 VAL C CG2   1 
ATOM   5964 N  N     . LEU C 1 202 ? 26.724  40.880  -43.469 1.00 67.92  ?  195 LEU C N     1 
ATOM   5965 C  CA    . LEU C 1 202 ? 25.745  40.234  -42.598 1.00 67.04  ?  195 LEU C CA    1 
ATOM   5966 C  C     . LEU C 1 202 ? 24.907  39.193  -43.325 1.00 68.71  ?  195 LEU C C     1 
ATOM   5967 O  O     . LEU C 1 202 ? 24.322  39.479  -44.367 1.00 67.64  ?  195 LEU C O     1 
ATOM   5968 C  CB    . LEU C 1 202 ? 24.800  41.306  -42.042 1.00 62.43  ?  195 LEU C CB    1 
ATOM   5969 C  CG    . LEU C 1 202 ? 23.663  40.793  -41.155 1.00 61.65  ?  195 LEU C CG    1 
ATOM   5970 C  CD1   . LEU C 1 202 ? 24.194  40.411  -39.775 1.00 63.27  ?  195 LEU C CD1   1 
ATOM   5971 C  CD2   . LEU C 1 202 ? 22.560  41.828  -41.009 1.00 57.75  ?  195 LEU C CD2   1 
ATOM   5972 N  N     . ILE C 1 203 ? 24.761  38.009  -42.706 1.00 71.53  ?  196 ILE C N     1 
ATOM   5973 C  CA    . ILE C 1 203 ? 23.819  37.016  -43.197 1.00 73.44  ?  196 ILE C CA    1 
ATOM   5974 C  C     . ILE C 1 203 ? 22.446  37.333  -42.615 1.00 70.29  ?  196 ILE C C     1 
ATOM   5975 O  O     . ILE C 1 203 ? 22.312  37.549  -41.421 1.00 68.95  ?  196 ILE C O     1 
ATOM   5976 C  CB    . ILE C 1 203 ? 24.235  35.562  -42.872 1.00 78.71  ?  196 ILE C CB    1 
ATOM   5977 C  CG1   . ILE C 1 203 ? 25.666  35.224  -43.318 1.00 82.69  ?  196 ILE C CG1   1 
ATOM   5978 C  CG2   . ILE C 1 203 ? 23.221  34.575  -43.449 1.00 81.25  ?  196 ILE C CG2   1 
ATOM   5979 C  CD1   . ILE C 1 203 ? 25.893  35.282  -44.812 1.00 84.33  ?  196 ILE C CD1   1 
ATOM   5980 N  N     . VAL C 1 204 ? 21.449  37.330  -43.498 1.00 69.80  ?  197 VAL C N     1 
ATOM   5981 C  CA    . VAL C 1 204 ? 20.044  37.465  -43.163 1.00 68.11  ?  197 VAL C CA    1 
ATOM   5982 C  C     . VAL C 1 204 ? 19.351  36.258  -43.772 1.00 72.16  ?  197 VAL C C     1 
ATOM   5983 O  O     . VAL C 1 204 ? 19.341  36.143  -45.001 1.00 73.56  ?  197 VAL C O     1 
ATOM   5984 C  CB    . VAL C 1 204 ? 19.449  38.767  -43.740 1.00 64.12  ?  197 VAL C CB    1 
ATOM   5985 C  CG1   . VAL C 1 204 ? 17.945  38.877  -43.511 1.00 63.22  ?  197 VAL C CG1   1 
ATOM   5986 C  CG2   . VAL C 1 204 ? 20.162  39.999  -43.205 1.00 60.71  ?  197 VAL C CG2   1 
ATOM   5987 N  N     . THR C 1 205 ? 18.799  35.388  -42.910 1.00 74.46  ?  198 THR C N     1 
ATOM   5988 C  CA    . THR C 1 205 ? 18.042  34.223  -43.348 1.00 78.93  ?  198 THR C CA    1 
ATOM   5989 C  C     . THR C 1 205 ? 17.001  34.651  -44.377 1.00 78.12  ?  198 THR C C     1 
ATOM   5990 O  O     . THR C 1 205 ? 16.317  35.664  -44.183 1.00 74.37  ?  198 THR C O     1 
ATOM   5991 C  CB    . THR C 1 205 ? 17.373  33.495  -42.172 1.00 81.04  ?  198 THR C CB    1 
ATOM   5992 O  OG1   . THR C 1 205 ? 17.141  34.447  -41.133 1.00 77.03  ?  198 THR C OG1   1 
ATOM   5993 C  CG2   . THR C 1 205 ? 18.199  32.341  -41.642 1.00 85.36  ?  198 THR C CG2   1 
ATOM   5994 N  N     . GLY C 1 206 ? 16.923  33.878  -45.474 1.00 82.18  ?  199 GLY C N     1 
ATOM   5995 C  CA    . GLY C 1 206 ? 15.926  34.077  -46.516 1.00 82.80  ?  199 GLY C CA    1 
ATOM   5996 C  C     . GLY C 1 206 ? 16.294  35.181  -47.511 1.00 79.60  ?  199 GLY C C     1 
ATOM   5997 O  O     . GLY C 1 206 ? 15.525  35.459  -48.430 1.00 80.05  ?  199 GLY C O     1 
ATOM   5998 N  N     . GLU C 1 207 ? 17.460  35.816  -47.334 1.00 76.87  ?  200 GLU C N     1 
ATOM   5999 C  CA    . GLU C 1 207 ? 17.884  36.873  -48.239 1.00 74.30  ?  200 GLU C CA    1 
ATOM   6000 C  C     . GLU C 1 207 ? 19.157  36.437  -48.967 1.00 77.37  ?  200 GLU C C     1 
ATOM   6001 O  O     . GLU C 1 207 ? 19.178  36.437  -50.204 1.00 79.45  ?  200 GLU C O     1 
ATOM   6002 C  CB    . GLU C 1 207 ? 18.035  38.198  -47.478 1.00 68.81  ?  200 GLU C CB    1 
ATOM   6003 C  CG    . GLU C 1 207 ? 16.713  38.808  -47.005 1.00 66.23  ?  200 GLU C CG    1 
ATOM   6004 C  CD    . GLU C 1 207 ? 15.916  39.602  -48.033 1.00 65.09  ?  200 GLU C CD    1 
ATOM   6005 O  OE1   . GLU C 1 207 ? 16.390  39.726  -49.165 1.00 66.09  ?  200 GLU C OE1   1 
ATOM   6006 O  OE2   . GLU C 1 207 ? 14.812  40.100  -47.696 1.00 63.62  -1 200 GLU C OE2   1 
ATOM   6007 N  N     . ASN C 1 208 ? 20.206  36.056  -48.214 1.00 78.24  ?  201 ASN C N     1 
ATOM   6008 C  CA    . ASN C 1 208 ? 21.516  35.788  -48.800 1.00 81.29  ?  201 ASN C CA    1 
ATOM   6009 C  C     . ASN C 1 208 ? 22.242  34.606  -48.136 1.00 85.53  ?  201 ASN C C     1 
ATOM   6010 O  O     . ASN C 1 208 ? 23.480  34.601  -48.096 1.00 87.13  ?  201 ASN C O     1 
ATOM   6011 C  CB    . ASN C 1 208 ? 22.408  37.039  -48.730 1.00 77.69  ?  201 ASN C CB    1 
ATOM   6012 C  CG    . ASN C 1 208 ? 22.723  37.497  -47.315 1.00 74.48  ?  201 ASN C CG    1 
ATOM   6013 O  OD1   . ASN C 1 208 ? 22.344  36.850  -46.343 1.00 74.97  ?  201 ASN C OD1   1 
ATOM   6014 N  ND2   . ASN C 1 208 ? 23.428  38.611  -47.181 1.00 71.70  ?  201 ASN C ND2   1 
ATOM   6015 N  N     . ASP C 1 209 ? 21.487  33.600  -47.665 1.00 88.01  ?  202 ASP C N     1 
ATOM   6016 C  CA    . ASP C 1 209 ? 22.002  32.643  -46.690 1.00 91.06  ?  202 ASP C CA    1 
ATOM   6017 C  C     . ASP C 1 209 ? 22.165  31.226  -47.255 1.00 98.24  ?  202 ASP C C     1 
ATOM   6018 O  O     . ASP C 1 209 ? 22.590  30.334  -46.515 1.00 101.64 ?  202 ASP C O     1 
ATOM   6019 C  CB    . ASP C 1 209 ? 21.117  32.601  -45.434 1.00 88.76  ?  202 ASP C CB    1 
ATOM   6020 C  CG    . ASP C 1 209 ? 19.715  32.047  -45.640 1.00 90.44  ?  202 ASP C CG    1 
ATOM   6021 O  OD1   . ASP C 1 209 ? 18.906  32.743  -46.285 1.00 87.95  ?  202 ASP C OD1   1 
ATOM   6022 O  OD2   . ASP C 1 209 ? 19.431  30.936  -45.135 1.00 94.58  -1 202 ASP C OD2   1 
ATOM   6023 N  N     . SER C 1 210 ? 21.811  30.992  -48.529 1.00 101.08 ?  203 SER C N     1 
ATOM   6024 C  CA    . SER C 1 210 ? 21.964  29.669  -49.131 1.00 108.62 ?  203 SER C CA    1 
ATOM   6025 C  C     . SER C 1 210 ? 21.939  29.780  -50.653 1.00 111.22 ?  203 SER C C     1 
ATOM   6026 O  O     . SER C 1 210 ? 21.952  30.888  -51.186 1.00 107.09 ?  203 SER C O     1 
ATOM   6027 C  CB    . SER C 1 210 ? 20.913  28.696  -48.623 1.00 111.47 ?  203 SER C CB    1 
ATOM   6028 O  OG    . SER C 1 210 ? 19.616  29.012  -49.112 1.00 109.98 ?  203 SER C OG    1 
ATOM   6029 N  N     . ASP C 1 211 ? 21.909  28.623  -51.340 1.00 118.58 ?  204 ASP C N     1 
ATOM   6030 C  CA    . ASP C 1 211 ? 21.793  28.575  -52.792 1.00 122.32 ?  204 ASP C CA    1 
ATOM   6031 C  C     . ASP C 1 211 ? 20.324  28.559  -53.229 1.00 122.20 ?  204 ASP C C     1 
ATOM   6032 O  O     . ASP C 1 211 ? 20.043  28.563  -54.427 1.00 125.27 ?  204 ASP C O     1 
ATOM   6033 C  CB    . ASP C 1 211 ? 22.539  27.364  -53.365 1.00 131.22 ?  204 ASP C CB    1 
ATOM   6034 C  CG    . ASP C 1 211 ? 24.016  27.338  -53.006 1.00 132.49 ?  204 ASP C CG    1 
ATOM   6035 O  OD1   . ASP C 1 211 ? 24.707  28.361  -53.265 1.00 128.91 ?  204 ASP C OD1   1 
ATOM   6036 O  OD2   . ASP C 1 211 ? 24.465  26.299  -52.462 1.00 137.46 -1 204 ASP C OD2   1 
ATOM   6037 N  N     . LYS C 1 212 ? 19.392  28.507  -52.264 1.00 119.40 ?  205 LYS C N     1 
ATOM   6038 C  CA    . LYS C 1 212 ? 17.975  28.697  -52.545 1.00 118.61 ?  205 LYS C CA    1 
ATOM   6039 C  C     . LYS C 1 212 ? 17.694  30.180  -52.818 1.00 111.65 ?  205 LYS C C     1 
ATOM   6040 O  O     . LYS C 1 212 ? 16.942  30.510  -53.733 1.00 112.26 ?  205 LYS C O     1 
ATOM   6041 C  CB    . LYS C 1 212 ? 17.116  28.146  -51.396 1.00 118.70 ?  205 LYS C CB    1 
ATOM   6042 C  CG    . LYS C 1 212 ? 16.827  26.648  -51.441 1.00 126.98 ?  205 LYS C CG    1 
ATOM   6043 C  CD    . LYS C 1 212 ? 18.031  25.743  -51.232 1.00 131.60 ?  205 LYS C CD    1 
ATOM   6044 C  CE    . LYS C 1 212 ? 17.717  24.276  -51.459 1.00 140.73 ?  205 LYS C CE    1 
ATOM   6045 N  NZ    . LYS C 1 212 ? 16.712  23.764  -50.499 1.00 141.60 ?  205 LYS C NZ    1 
ATOM   6046 N  N     . THR C 1 213 ? 18.322  31.073  -52.042 1.00 105.59 ?  206 THR C N     1 
ATOM   6047 C  CA    . THR C 1 213 ? 18.107  32.509  -52.176 1.00 99.16  ?  206 THR C CA    1 
ATOM   6048 C  C     . THR C 1 213 ? 18.813  33.046  -53.423 1.00 99.95  ?  206 THR C C     1 
ATOM   6049 O  O     . THR C 1 213 ? 19.562  32.325  -54.084 1.00 105.32 ?  206 THR C O     1 
ATOM   6050 C  CB    . THR C 1 213 ? 18.553  33.254  -50.910 1.00 93.29  ?  206 THR C CB    1 
ATOM   6051 O  OG1   . THR C 1 213 ? 19.917  32.918  -50.655 1.00 94.92  ?  206 THR C OG1   1 
ATOM   6052 C  CG2   . THR C 1 213 ? 17.698  32.913  -49.707 1.00 92.26  ?  206 THR C CG2   1 
ATOM   6053 N  N     . LEU C 1 214 ? 18.546  34.322  -53.744 1.00 95.06  ?  207 LEU C N     1 
ATOM   6054 C  CA    . LEU C 1 214 ? 19.105  34.950  -54.931 1.00 95.71  ?  207 LEU C CA    1 
ATOM   6055 C  C     . LEU C 1 214 ? 20.597  35.232  -54.732 1.00 95.16  ?  207 LEU C C     1 
ATOM   6056 O  O     . LEU C 1 214 ? 21.328  35.320  -55.719 1.00 98.24  ?  207 LEU C O     1 
ATOM   6057 C  CB    . LEU C 1 214 ? 18.323  36.230  -55.255 1.00 90.95  ?  207 LEU C CB    1 
ATOM   6058 C  CG    . LEU C 1 214 ? 16.901  36.027  -55.782 1.00 92.79  ?  207 LEU C CG    1 
ATOM   6059 C  CD1   . LEU C 1 214 ? 16.209  37.364  -56.008 1.00 88.11  ?  207 LEU C CD1   1 
ATOM   6060 C  CD2   . LEU C 1 214 ? 16.894  35.214  -57.070 1.00 99.78  ?  207 LEU C CD2   1 
ATOM   6061 N  N     . ARG C 1 215 ? 21.031  35.356  -53.465 1.00 91.89  ?  208 ARG C N     1 
ATOM   6062 C  CA    . ARG C 1 215 ? 22.438  35.506  -53.105 1.00 92.09  ?  208 ARG C CA    1 
ATOM   6063 C  C     . ARG C 1 215 ? 22.845  34.443  -52.078 1.00 94.54  ?  208 ARG C C     1 
ATOM   6064 O  O     . ARG C 1 215 ? 21.990  33.858  -51.415 1.00 94.40  ?  208 ARG C O     1 
ATOM   6065 C  CB    . ARG C 1 215 ? 22.708  36.902  -52.521 1.00 85.80  ?  208 ARG C CB    1 
ATOM   6066 C  CG    . ARG C 1 215 ? 22.543  38.047  -53.515 1.00 83.73  ?  208 ARG C CG    1 
ATOM   6067 C  CD    . ARG C 1 215 ? 23.492  37.945  -54.698 1.00 88.44  ?  208 ARG C CD    1 
ATOM   6068 N  NE    . ARG C 1 215 ? 23.455  39.079  -55.614 1.00 86.84  ?  208 ARG C NE    1 
ATOM   6069 C  CZ    . ARG C 1 215 ? 22.481  39.333  -56.485 1.00 86.81  ?  208 ARG C CZ    1 
ATOM   6070 N  NH1   . ARG C 1 215 ? 21.376  38.609  -56.484 1.00 87.84  ?  208 ARG C NH1   1 
ATOM   6071 N  NH2   . ARG C 1 215 ? 22.602  40.340  -57.334 1.00 86.05  ?  208 ARG C NH2   1 
ATOM   6072 N  N     . ASN C 1 216 ? 24.166  34.215  -51.963 1.00 97.27  ?  209 ASN C N     1 
ATOM   6073 C  CA    . ASN C 1 216 ? 24.791  33.420  -50.908 1.00 99.34  ?  209 ASN C CA    1 
ATOM   6074 C  C     . ASN C 1 216 ? 26.074  34.122  -50.450 1.00 98.00  ?  209 ASN C C     1 
ATOM   6075 O  O     . ASN C 1 216 ? 27.109  33.994  -51.096 1.00 102.24 ?  209 ASN C O     1 
ATOM   6076 C  CB    . ASN C 1 216 ? 25.134  32.002  -51.378 1.00 107.20 ?  209 ASN C CB    1 
ATOM   6077 C  CG    . ASN C 1 216 ? 25.837  31.192  -50.309 1.00 109.85 ?  209 ASN C CG    1 
ATOM   6078 O  OD1   . ASN C 1 216 ? 26.155  31.715  -49.239 1.00 105.93 ?  209 ASN C OD1   1 
ATOM   6079 N  ND2   . ASN C 1 216 ? 26.080  29.919  -50.581 1.00 116.94 ?  209 ASN C ND2   1 
ATOM   6080 N  N     . ALA C 1 217 ? 26.030  34.853  -49.327 1.00 92.82  ?  210 ALA C N     1 
ATOM   6081 C  CA    . ALA C 1 217 ? 27.112  35.775  -48.995 1.00 91.15  ?  210 ALA C CA    1 
ATOM   6082 C  C     . ALA C 1 217 ? 28.206  35.089  -48.170 1.00 94.96  ?  210 ALA C C     1 
ATOM   6083 O  O     . ALA C 1 217 ? 29.031  35.759  -47.542 1.00 93.69  ?  210 ALA C O     1 
ATOM   6084 C  CB    . ALA C 1 217 ? 26.535  36.963  -48.266 1.00 84.40  ?  210 ALA C CB    1 
ATOM   6085 N  N     . HIS C 1 218 ? 28.227  33.751  -48.192 1.00 100.22 ?  211 HIS C N     1 
ATOM   6086 C  CA    . HIS C 1 218 ? 28.922  32.992  -47.165 1.00 103.37 ?  211 HIS C CA    1 
ATOM   6087 C  C     . HIS C 1 218 ? 30.432  32.963  -47.390 1.00 108.23 ?  211 HIS C C     1 
ATOM   6088 O  O     . HIS C 1 218 ? 31.182  32.856  -46.422 1.00 109.43 ?  211 HIS C O     1 
ATOM   6089 C  CB    . HIS C 1 218 ? 28.368  31.567  -47.045 1.00 107.71 ?  211 HIS C CB    1 
ATOM   6090 C  CG    . HIS C 1 218 ? 27.184  31.464  -46.153 1.00 103.90 ?  211 HIS C CG    1 
ATOM   6091 N  ND1   . HIS C 1 218 ? 27.180  32.003  -44.884 1.00 99.85  ?  211 HIS C ND1   1 
ATOM   6092 C  CD2   . HIS C 1 218 ? 25.987  30.892  -46.321 1.00 104.14 ?  211 HIS C CD2   1 
ATOM   6093 C  CE1   . HIS C 1 218 ? 26.012  31.751  -44.312 1.00 97.78  ?  211 HIS C CE1   1 
ATOM   6094 N  NE2   . HIS C 1 218 ? 25.275  31.067  -45.164 1.00 100.40 ?  211 HIS C NE2   1 
ATOM   6095 N  N     . SER C 1 219 ? 30.872  33.033  -48.652 1.00 111.62 ?  212 SER C N     1 
ATOM   6096 C  CA    . SER C 1 219 ? 32.293  33.070  -48.969 1.00 116.88 ?  212 SER C CA    1 
ATOM   6097 C  C     . SER C 1 219 ? 32.864  34.479  -48.800 1.00 113.03 ?  212 SER C C     1 
ATOM   6098 O  O     . SER C 1 219 ? 34.073  34.664  -48.963 1.00 117.29 ?  212 SER C O     1 
ATOM   6099 C  CB    . SER C 1 219 ? 32.533  32.572  -50.371 1.00 122.81 ?  212 SER C CB    1 
ATOM   6100 O  OG    . SER C 1 219 ? 31.968  33.487  -51.301 1.00 119.13 ?  212 SER C OG    1 
ATOM   6101 N  N     . LEU C 1 220 ? 31.984  35.452  -48.510 1.00 105.70 ?  213 LEU C N     1 
ATOM   6102 C  CA    . LEU C 1 220 ? 32.347  36.857  -48.378 1.00 101.83 ?  213 LEU C CA    1 
ATOM   6103 C  C     . LEU C 1 220 ? 32.430  37.300  -46.922 1.00 98.31  ?  213 LEU C C     1 
ATOM   6104 O  O     . LEU C 1 220 ? 33.011  38.363  -46.677 1.00 96.77  ?  213 LEU C O     1 
ATOM   6105 C  CB    . LEU C 1 220 ? 31.307  37.726  -49.089 1.00 96.59  ?  213 LEU C CB    1 
ATOM   6106 C  CG    . LEU C 1 220 ? 31.263  37.627  -50.612 1.00 99.71  ?  213 LEU C CG    1 
ATOM   6107 C  CD1   . LEU C 1 220 ? 30.106  36.744  -51.066 1.00 99.94  ?  213 LEU C CD1   1 
ATOM   6108 C  CD2   . LEU C 1 220 ? 31.168  39.011  -51.228 1.00 96.21  ?  213 LEU C CD2   1 
ATOM   6109 N  N     . THR C 1 221 ? 31.803  36.524  -46.008 1.00 97.37  ?  214 THR C N     1 
ATOM   6110 C  CA    . THR C 1 221 ? 31.784  36.789  -44.571 1.00 94.68  ?  214 THR C CA    1 
ATOM   6111 C  C     . THR C 1 221 ? 33.207  36.938  -44.034 1.00 98.66  ?  214 THR C C     1 
ATOM   6112 O  O     . THR C 1 221 ? 34.162  36.532  -44.684 1.00 104.32 ?  214 THR C O     1 
ATOM   6113 C  CB    . THR C 1 221 ? 31.053  35.695  -43.759 1.00 95.06  ?  214 THR C CB    1 
ATOM   6114 O  OG1   . THR C 1 221 ? 31.334  34.416  -44.321 1.00 101.07 ?  214 THR C OG1   1 
ATOM   6115 C  CG2   . THR C 1 221 ? 29.549  35.854  -43.717 1.00 89.98  ?  214 THR C CG2   1 
ATOM   6116 N  N     . ILE C 1 222 ? 33.319  37.498  -42.821 1.00 96.24  ?  215 ILE C N     1 
ATOM   6117 C  CA    . ILE C 1 222 ? 34.603  37.772  -42.195 1.00 99.90  ?  215 ILE C CA    1 
ATOM   6118 C  C     . ILE C 1 222 ? 34.483  37.539  -40.691 1.00 99.20  ?  215 ILE C C     1 
ATOM   6119 O  O     . ILE C 1 222 ? 33.395  37.601  -40.122 1.00 94.65  ?  215 ILE C O     1 
ATOM   6120 C  CB    . ILE C 1 222 ? 35.104  39.202  -42.512 1.00 98.20  ?  215 ILE C CB    1 
ATOM   6121 C  CG1   . ILE C 1 222 ? 34.116  40.290  -42.080 1.00 91.17  ?  215 ILE C CG1   1 
ATOM   6122 C  CG2   . ILE C 1 222 ? 35.461  39.347  -43.986 1.00 100.56 ?  215 ILE C CG2   1 
ATOM   6123 C  CD1   . ILE C 1 222 ? 34.733  41.670  -42.024 1.00 90.42  ?  215 ILE C CD1   1 
ATOM   6124 N  N     . SER C 1 223 ? 35.628  37.257  -40.064 1.00 104.38 ?  216 SER C N     1 
ATOM   6125 C  CA    . SER C 1 223 ? 35.708  37.091  -38.625 1.00 104.78 ?  216 SER C CA    1 
ATOM   6126 C  C     . SER C 1 223 ? 35.423  38.412  -37.918 1.00 99.95  ?  216 SER C C     1 
ATOM   6127 O  O     . SER C 1 223 ? 35.477  39.479  -38.528 1.00 97.51  ?  216 SER C O     1 
ATOM   6128 C  CB    . SER C 1 223 ? 37.068  36.592  -38.236 1.00 112.04 ?  216 SER C CB    1 
ATOM   6129 O  OG    . SER C 1 223 ? 38.010  37.645  -38.371 1.00 113.42 ?  216 SER C OG    1 
ATOM   6130 N  N     . ASP C 1 224 ? 35.181  38.303  -36.608 1.00 99.40  ?  217 ASP C N     1 
ATOM   6131 C  CA    . ASP C 1 224 ? 35.063  39.440  -35.714 1.00 96.47  ?  217 ASP C CA    1 
ATOM   6132 C  C     . ASP C 1 224 ? 36.415  40.148  -35.600 1.00 100.54 ?  217 ASP C C     1 
ATOM   6133 O  O     . ASP C 1 224 ? 36.468  41.365  -35.419 1.00 98.39  ?  217 ASP C O     1 
ATOM   6134 C  CB    . ASP C 1 224 ? 34.548  38.969  -34.352 1.00 96.29  ?  217 ASP C CB    1 
ATOM   6135 C  CG    . ASP C 1 224 ? 33.278  38.139  -34.449 1.00 93.57  ?  217 ASP C CG    1 
ATOM   6136 O  OD1   . ASP C 1 224 ? 32.188  38.733  -34.454 1.00 88.40  ?  217 ASP C OD1   1 
ATOM   6137 O  OD2   . ASP C 1 224 ? 33.392  36.905  -34.549 1.00 97.16  -1 217 ASP C OD2   1 
ATOM   6138 N  N     . ASP C 1 225 ? 37.503  39.372  -35.711 1.00 107.05 ?  218 ASP C N     1 
ATOM   6139 C  CA    . ASP C 1 225 ? 38.860  39.898  -35.643 1.00 112.31 ?  218 ASP C CA    1 
ATOM   6140 C  C     . ASP C 1 225 ? 39.174  40.704  -36.905 1.00 111.78 ?  218 ASP C C     1 
ATOM   6141 O  O     . ASP C 1 225 ? 39.689  41.815  -36.818 1.00 112.23 ?  218 ASP C O     1 
ATOM   6142 C  CB    . ASP C 1 225 ? 39.892  38.777  -35.464 1.00 120.07 ?  218 ASP C CB    1 
ATOM   6143 C  CG    . ASP C 1 225 ? 39.521  37.740  -34.417 1.00 121.14 ?  218 ASP C CG    1 
ATOM   6144 O  OD1   . ASP C 1 225 ? 38.443  37.128  -34.564 1.00 117.41 ?  218 ASP C OD1   1 
ATOM   6145 O  OD2   . ASP C 1 225 ? 40.320  37.532  -33.478 1.00 126.22 -1 218 ASP C OD2   1 
ATOM   6146 N  N     . GLU C 1 226 ? 38.876  40.120  -38.073 1.00 111.45 ?  219 GLU C N     1 
ATOM   6147 C  CA    . GLU C 1 226 ? 39.111  40.748  -39.366 1.00 111.39 ?  219 GLU C CA    1 
ATOM   6148 C  C     . GLU C 1 226 ? 38.393  42.091  -39.471 1.00 105.09 ?  219 GLU C C     1 
ATOM   6149 O  O     . GLU C 1 226 ? 38.952  43.058  -39.991 1.00 106.16 ?  219 GLU C O     1 
ATOM   6150 C  CB    . GLU C 1 226 ? 38.634  39.824  -40.488 1.00 111.49 ?  219 GLU C CB    1 
ATOM   6151 C  CG    . GLU C 1 226 ? 39.587  38.672  -40.755 1.00 119.31 ?  219 GLU C CG    1 
ATOM   6152 C  CD    . GLU C 1 226 ? 38.966  37.439  -41.393 1.00 119.93 ?  219 GLU C CD    1 
ATOM   6153 O  OE1   . GLU C 1 226 ? 37.722  37.362  -41.443 1.00 114.15 ?  219 GLU C OE1   1 
ATOM   6154 O  OE2   . GLU C 1 226 ? 39.734  36.552  -41.833 1.00 126.80 -1 219 GLU C OE2   1 
ATOM   6155 N  N     . PHE C 1 227 ? 37.137  42.127  -39.010 1.00 99.02  ?  220 PHE C N     1 
ATOM   6156 C  CA    . PHE C 1 227 ? 36.350  43.347  -39.038 1.00 93.26  ?  220 PHE C CA    1 
ATOM   6157 C  C     . PHE C 1 227 ? 37.047  44.420  -38.207 1.00 94.77  ?  220 PHE C C     1 
ATOM   6158 O  O     . PHE C 1 227 ? 37.146  45.567  -38.638 1.00 93.57  ?  220 PHE C O     1 
ATOM   6159 C  CB    . PHE C 1 227 ? 34.937  43.084  -38.512 1.00 87.77  ?  220 PHE C CB    1 
ATOM   6160 C  CG    . PHE C 1 227 ? 34.033  44.292  -38.530 1.00 82.18  ?  220 PHE C CG    1 
ATOM   6161 C  CD1   . PHE C 1 227 ? 33.575  44.812  -39.730 1.00 79.50  ?  220 PHE C CD1   1 
ATOM   6162 C  CD2   . PHE C 1 227 ? 33.672  44.930  -37.353 1.00 80.23  ?  220 PHE C CD2   1 
ATOM   6163 C  CE1   . PHE C 1 227 ? 32.750  45.922  -39.746 1.00 74.87  ?  220 PHE C CE1   1 
ATOM   6164 C  CE2   . PHE C 1 227 ? 32.848  46.043  -37.370 1.00 75.76  ?  220 PHE C CE2   1 
ATOM   6165 C  CZ    . PHE C 1 227 ? 32.390  46.539  -38.569 1.00 73.07  ?  220 PHE C CZ    1 
ATOM   6166 N  N     . ASP C 1 228 ? 37.558  44.014  -37.032 1.00 98.05  ?  221 ASP C N     1 
ATOM   6167 C  CA    . ASP C 1 228 ? 38.091  44.936  -36.039 1.00 99.74  ?  221 ASP C CA    1 
ATOM   6168 C  C     . ASP C 1 228 ? 39.380  45.590  -36.546 1.00 105.05 ?  221 ASP C C     1 
ATOM   6169 O  O     . ASP C 1 228 ? 39.564  46.792  -36.365 1.00 104.84 ?  221 ASP C O     1 
ATOM   6170 C  CB    . ASP C 1 228 ? 38.276  44.244  -34.679 1.00 102.41 ?  221 ASP C CB    1 
ATOM   6171 C  CG    . ASP C 1 228 ? 36.996  44.029  -33.880 1.00 97.44  ?  221 ASP C CG    1 
ATOM   6172 O  OD1   . ASP C 1 228 ? 35.974  44.665  -34.209 1.00 91.87  ?  221 ASP C OD1   1 
ATOM   6173 O  OD2   . ASP C 1 228 ? 37.027  43.213  -32.933 1.00 99.64  -1 221 ASP C OD2   1 
ATOM   6174 N  N     . ARG C 1 229 ? 40.272  44.815  -37.180 1.00 110.41 ?  222 ARG C N     1 
ATOM   6175 C  CA    . ARG C 1 229 ? 41.522  45.356  -37.702 1.00 116.43 ?  222 ARG C CA    1 
ATOM   6176 C  C     . ARG C 1 229 ? 41.229  46.460  -38.713 1.00 113.36 ?  222 ARG C C     1 
ATOM   6177 O  O     . ARG C 1 229 ? 41.934  47.465  -38.783 1.00 116.39 ?  222 ARG C O     1 
ATOM   6178 C  CB    . ARG C 1 229 ? 42.360  44.274  -38.388 1.00 122.58 ?  222 ARG C CB    1 
ATOM   6179 C  CG    . ARG C 1 229 ? 43.166  43.399  -37.441 1.00 128.73 ?  222 ARG C CG    1 
ATOM   6180 C  CD    . ARG C 1 229 ? 44.052  42.437  -38.209 1.00 135.68 ?  222 ARG C CD    1 
ATOM   6181 N  NE    . ARG C 1 229 ? 44.246  41.186  -37.487 1.00 139.18 ?  222 ARG C NE    1 
ATOM   6182 C  CZ    . ARG C 1 229 ? 43.318  40.244  -37.331 1.00 135.44 ?  222 ARG C CZ    1 
ATOM   6183 N  NH1   . ARG C 1 229 ? 42.141  40.361  -37.920 1.00 128.32 ?  222 ARG C NH1   1 
ATOM   6184 N  NH2   . ARG C 1 229 ? 43.579  39.168  -36.607 1.00 139.41 ?  222 ARG C NH2   1 
ATOM   6185 N  N     . PHE C 1 230 ? 40.182  46.240  -39.510 1.00 107.84 ?  223 PHE C N     1 
ATOM   6186 C  CA    . PHE C 1 230 ? 39.730  47.232  -40.468 1.00 104.42 ?  223 PHE C CA    1 
ATOM   6187 C  C     . PHE C 1 230 ? 39.398  48.524  -39.726 1.00 101.51 ?  223 PHE C C     1 
ATOM   6188 O  O     . PHE C 1 230 ? 39.786  49.604  -40.160 1.00 102.82 ?  223 PHE C O     1 
ATOM   6189 C  CB    . PHE C 1 230 ? 38.563  46.686  -41.292 1.00 99.16  ?  223 PHE C CB    1 
ATOM   6190 C  CG    . PHE C 1 230 ? 38.010  47.657  -42.303 1.00 95.66  ?  223 PHE C CG    1 
ATOM   6191 C  CD1   . PHE C 1 230 ? 37.020  48.565  -41.951 1.00 89.91  ?  223 PHE C CD1   1 
ATOM   6192 C  CD2   . PHE C 1 230 ? 38.506  47.694  -43.598 1.00 98.74  ?  223 PHE C CD2   1 
ATOM   6193 C  CE1   . PHE C 1 230 ? 36.516  49.463  -42.882 1.00 87.12  ?  223 PHE C CE1   1 
ATOM   6194 C  CE2   . PHE C 1 230 ? 38.001  48.588  -44.527 1.00 95.89  ?  223 PHE C CE2   1 
ATOM   6195 C  CZ    . PHE C 1 230 ? 37.011  49.473  -44.167 1.00 90.04  ?  223 PHE C CZ    1 
ATOM   6196 N  N     . CYS C 1 231 ? 38.710  48.400  -38.589 1.00 98.26  ?  224 CYS C N     1 
ATOM   6197 C  CA    . CYS C 1 231 ? 38.157  49.565  -37.911 1.00 95.04  ?  224 CYS C CA    1 
ATOM   6198 C  C     . CYS C 1 231 ? 39.256  50.303  -37.142 1.00 100.64 ?  224 CYS C C     1 
ATOM   6199 O  O     . CYS C 1 231 ? 39.187  51.527  -37.012 1.00 100.12 ?  224 CYS C O     1 
ATOM   6200 C  CB    . CYS C 1 231 ? 36.974  49.181  -37.021 1.00 90.09  ?  224 CYS C CB    1 
ATOM   6201 S  SG    . CYS C 1 231 ? 35.558  48.508  -37.940 1.00 83.77  ?  224 CYS C SG    1 
ATOM   6202 N  N     . GLU C 1 232 ? 40.270  49.551  -36.668 1.00 106.52 ?  225 GLU C N     1 
ATOM   6203 C  CA    . GLU C 1 232 ? 41.461  50.092  -36.022 1.00 113.31 ?  225 GLU C CA    1 
ATOM   6204 C  C     . GLU C 1 232 ? 42.370  50.753  -37.056 1.00 117.74 ?  225 GLU C C     1 
ATOM   6205 O  O     . GLU C 1 232 ? 43.024  51.748  -36.753 1.00 121.73 ?  225 GLU C O     1 
ATOM   6206 C  CB    . GLU C 1 232 ? 42.263  48.990  -35.319 1.00 118.80 ?  225 GLU C CB    1 
ATOM   6207 C  CG    . GLU C 1 232 ? 41.491  48.228  -34.254 1.00 115.68 ?  225 GLU C CG    1 
ATOM   6208 C  CD    . GLU C 1 232 ? 42.117  46.920  -33.789 1.00 120.49 ?  225 GLU C CD    1 
ATOM   6209 O  OE1   . GLU C 1 232 ? 41.351  46.039  -33.337 1.00 117.36 ?  225 GLU C OE1   1 
ATOM   6210 O  OE2   . GLU C 1 232 ? 43.371  46.794  -33.837 1.00 127.88 -1 225 GLU C OE2   1 
ATOM   6211 N  N     . ARG C 1 233 ? 42.426  50.161  -38.258 1.00 117.72 ?  226 ARG C N     1 
ATOM   6212 C  CA    . ARG C 1 233 ? 43.177  50.687  -39.392 1.00 121.83 ?  226 ARG C CA    1 
ATOM   6213 C  C     . ARG C 1 233 ? 42.725  52.103  -39.764 1.00 118.78 ?  226 ARG C C     1 
ATOM   6214 O  O     . ARG C 1 233 ? 43.440  52.824  -40.468 1.00 123.11 ?  226 ARG C O     1 
ATOM   6215 C  CB    . ARG C 1 233 ? 42.979  49.754  -40.593 1.00 120.98 ?  226 ARG C CB    1 
ATOM   6216 C  CG    . ARG C 1 233 ? 43.507  50.289  -41.917 1.00 124.26 ?  226 ARG C CG    1 
ATOM   6217 C  CD    . ARG C 1 233 ? 43.460  49.233  -43.001 1.00 125.07 ?  226 ARG C CD    1 
ATOM   6218 N  NE    . ARG C 1 233 ? 43.771  47.898  -42.499 1.00 127.85 ?  226 ARG C NE    1 
ATOM   6219 C  CZ    . ARG C 1 233 ? 42.980  46.834  -42.604 1.00 124.11 ?  226 ARG C CZ    1 
ATOM   6220 N  NH1   . ARG C 1 233 ? 41.852  46.900  -43.286 1.00 117.72 ?  226 ARG C NH1   1 
ATOM   6221 N  NH2   . ARG C 1 233 ? 43.340  45.685  -42.058 1.00 127.43 ?  226 ARG C NH2   1 
ATOM   6222 N  N     . HIS C 1 234 ? 41.515  52.469  -39.326 1.00 111.72 ?  227 HIS C N     1 
ATOM   6223 C  CA    . HIS C 1 234 ? 40.836  53.666  -39.799 1.00 107.88 ?  227 HIS C CA    1 
ATOM   6224 C  C     . HIS C 1 234 ? 40.498  54.573  -38.616 1.00 106.71 ?  227 HIS C C     1 
ATOM   6225 O  O     . HIS C 1 234 ? 39.535  55.330  -38.680 1.00 101.82 ?  227 HIS C O     1 
ATOM   6226 C  CB    . HIS C 1 234 ? 39.576  53.271  -40.574 1.00 100.78 ?  227 HIS C CB    1 
ATOM   6227 C  CG    . HIS C 1 234 ? 39.833  52.587  -41.876 1.00 102.17 ?  227 HIS C CG    1 
ATOM   6228 N  ND1   . HIS C 1 234 ? 39.735  51.220  -42.049 1.00 101.98 ?  227 HIS C ND1   1 
ATOM   6229 C  CD2   . HIS C 1 234 ? 40.213  53.090  -43.060 1.00 104.48 ?  227 HIS C CD2   1 
ATOM   6230 C  CE1   . HIS C 1 234 ? 40.030  50.917  -43.305 1.00 104.12 ?  227 HIS C CE1   1 
ATOM   6231 N  NE2   . HIS C 1 234 ? 40.327  52.038  -43.936 1.00 105.65 ?  227 HIS C NE2   1 
ATOM   6232 N  N     . SER C 1 235 ? 41.326  54.525  -37.559 1.00 111.93 ?  228 SER C N     1 
ATOM   6233 C  CA    . SER C 1 235 ? 40.947  55.060  -36.257 1.00 111.09 ?  228 SER C CA    1 
ATOM   6234 C  C     . SER C 1 235 ? 40.836  56.587  -36.259 1.00 111.62 ?  228 SER C C     1 
ATOM   6235 O  O     . SER C 1 235 ? 40.054  57.142  -35.490 1.00 108.68 ?  228 SER C O     1 
ATOM   6236 C  CB    . SER C 1 235 ? 41.913  54.602  -35.177 1.00 117.34 ?  228 SER C CB    1 
ATOM   6237 O  OG    . SER C 1 235 ? 43.216  55.120  -35.394 1.00 125.20 ?  228 SER C OG    1 
ATOM   6238 N  N     . SER C 1 236 ? 41.635  57.267  -37.092 1.00 116.06 ?  229 SER C N     1 
ATOM   6239 C  CA    . SER C 1 236 ? 41.686  58.724  -37.101 1.00 118.00 ?  229 SER C CA    1 
ATOM   6240 C  C     . SER C 1 236 ? 40.398  59.313  -37.684 1.00 110.93 ?  229 SER C C     1 
ATOM   6241 O  O     . SER C 1 236 ? 40.115  60.499  -37.516 1.00 111.24 ?  229 SER C O     1 
ATOM   6242 C  CB    . SER C 1 236 ? 42.914  59.219  -37.836 1.00 125.38 ?  229 SER C CB    1 
ATOM   6243 O  OG    . SER C 1 236 ? 42.958  58.717  -39.163 1.00 124.16 ?  229 SER C OG    1 
ATOM   6244 N  N     . GLN C 1 237 ? 39.616  58.468  -38.361 1.00 105.09 ?  230 GLN C N     1 
ATOM   6245 C  CA    . GLN C 1 237 ? 38.384  58.883  -39.012 1.00 98.69  ?  230 GLN C CA    1 
ATOM   6246 C  C     . GLN C 1 237 ? 37.283  59.031  -37.970 1.00 94.20  ?  230 GLN C C     1 
ATOM   6247 O  O     . GLN C 1 237 ? 36.587  58.070  -37.664 1.00 90.09  ?  230 GLN C O     1 
ATOM   6248 C  CB    . GLN C 1 237 ? 38.022  57.868  -40.095 1.00 95.20  ?  230 GLN C CB    1 
ATOM   6249 C  CG    . GLN C 1 237 ? 39.112  57.688  -41.143 1.00 100.31 ?  230 GLN C CG    1 
ATOM   6250 C  CD    . GLN C 1 237 ? 39.524  59.002  -41.761 1.00 103.67 ?  230 GLN C CD    1 
ATOM   6251 O  OE1   . GLN C 1 237 ? 38.794  59.989  -41.716 1.00 100.94 ?  230 GLN C OE1   1 
ATOM   6252 N  NE2   . GLN C 1 237 ? 40.706  59.023  -42.353 1.00 110.21 ?  230 GLN C NE2   1 
ATOM   6253 N  N     . THR C 1 238 ? 37.121  60.261  -37.469 1.00 95.55  ?  231 THR C N     1 
ATOM   6254 C  CA    . THR C 1 238 ? 36.158  60.584  -36.424 1.00 92.72  ?  231 THR C CA    1 
ATOM   6255 C  C     . THR C 1 238 ? 34.710  60.369  -36.882 1.00 85.53  ?  231 THR C C     1 
ATOM   6256 O  O     . THR C 1 238 ? 33.812  60.347  -36.046 1.00 82.87  ?  231 THR C O     1 
ATOM   6257 C  CB    . THR C 1 238 ? 36.289  62.042  -35.950 1.00 96.43  ?  231 THR C CB    1 
ATOM   6258 O  OG1   . THR C 1 238 ? 35.994  62.882  -37.065 1.00 95.26  ?  231 THR C OG1   1 
ATOM   6259 C  CG2   . THR C 1 238 ? 37.650  62.395  -35.387 1.00 104.32 ?  231 THR C CG2   1 
ATOM   6260 N  N     . CYS C 1 239 ? 34.481  60.232  -38.193 1.00 83.00  ?  232 CYS C N     1 
ATOM   6261 C  CA    . CYS C 1 239 ? 33.140  60.018  -38.729 1.00 76.84  ?  232 CYS C CA    1 
ATOM   6262 C  C     . CYS C 1 239 ? 32.742  58.534  -38.787 1.00 73.52  ?  232 CYS C C     1 
ATOM   6263 O  O     . CYS C 1 239 ? 31.586  58.220  -39.068 1.00 68.80  ?  232 CYS C O     1 
ATOM   6264 C  CB    . CYS C 1 239 ? 33.052  60.573  -40.143 1.00 76.17  ?  232 CYS C CB    1 
ATOM   6265 S  SG    . CYS C 1 239 ? 34.086  59.650  -41.309 1.00 78.54  ?  232 CYS C SG    1 
ATOM   6266 N  N     . LEU C 1 240 ? 33.692  57.617  -38.567 1.00 76.47  ?  233 LEU C N     1 
ATOM   6267 C  CA    . LEU C 1 240 ? 33.454  56.190  -38.751 1.00 74.32  ?  233 LEU C CA    1 
ATOM   6268 C  C     . LEU C 1 240 ? 32.472  55.670  -37.696 1.00 71.14  ?  233 LEU C C     1 
ATOM   6269 O  O     . LEU C 1 240 ? 32.511  56.072  -36.527 1.00 72.67  ?  233 LEU C O     1 
ATOM   6270 C  CB    . LEU C 1 240 ? 34.792  55.444  -38.687 1.00 79.35  ?  233 LEU C CB    1 
ATOM   6271 C  CG    . LEU C 1 240 ? 34.733  53.968  -38.296 1.00 78.79  ?  233 LEU C CG    1 
ATOM   6272 C  CD1   . LEU C 1 240 ? 34.382  53.098  -39.485 1.00 76.60  ?  233 LEU C CD1   1 
ATOM   6273 C  CD2   . LEU C 1 240 ? 36.054  53.516  -37.685 1.00 84.77  ?  233 LEU C CD2   1 
ATOM   6274 N  N     . VAL C 1 241 ? 31.575  54.784  -38.159 1.00 67.20  ?  234 VAL C N     1 
ATOM   6275 C  CA    . VAL C 1 241 ? 30.567  54.128  -37.341 1.00 64.36  ?  234 VAL C CA    1 
ATOM   6276 C  C     . VAL C 1 241 ? 30.574  52.631  -37.669 1.00 63.93  ?  234 VAL C C     1 
ATOM   6277 O  O     . VAL C 1 241 ? 30.004  52.211  -38.669 1.00 61.51  ?  234 VAL C O     1 
ATOM   6278 C  CB    . VAL C 1 241 ? 29.167  54.706  -37.617 1.00 60.10  ?  234 VAL C CB    1 
ATOM   6279 C  CG1   . VAL C 1 241 ? 28.095  53.942  -36.855 1.00 57.74  ?  234 VAL C CG1   1 
ATOM   6280 C  CG2   . VAL C 1 241 ? 29.078  56.193  -37.316 1.00 60.87  ?  234 VAL C CG2   1 
ATOM   6281 N  N     . PRO C 1 242 ? 31.136  51.743  -36.820 1.00 66.49  ?  235 PRO C N     1 
ATOM   6282 C  CA    . PRO C 1 242 ? 31.175  50.311  -37.120 1.00 66.78  ?  235 PRO C CA    1 
ATOM   6283 C  C     . PRO C 1 242 ? 29.941  49.524  -36.668 1.00 63.71  ?  235 PRO C C     1 
ATOM   6284 O  O     . PRO C 1 242 ? 29.350  49.861  -35.649 1.00 62.80  ?  235 PRO C O     1 
ATOM   6285 C  CB    . PRO C 1 242 ? 32.384  49.883  -36.269 1.00 71.72  ?  235 PRO C CB    1 
ATOM   6286 C  CG    . PRO C 1 242 ? 32.233  50.712  -35.021 1.00 72.14  ?  235 PRO C CG    1 
ATOM   6287 C  CD    . PRO C 1 242 ? 31.752  52.064  -35.519 1.00 69.78  ?  235 PRO C CD    1 
ATOM   6288 N  N     . GLU C 1 243 ? 29.569  48.485  -37.426 1.00 62.78  ?  236 GLU C N     1 
ATOM   6289 C  CA    . GLU C 1 243 ? 28.410  47.668  -37.094 1.00 60.58  ?  236 GLU C CA    1 
ATOM   6290 C  C     . GLU C 1 243 ? 28.692  46.184  -37.268 1.00 62.79  ?  236 GLU C C     1 
ATOM   6291 O  O     . GLU C 1 243 ? 28.235  45.548  -38.212 1.00 61.96  ?  236 GLU C O     1 
ATOM   6292 C  CB    . GLU C 1 243 ? 27.184  48.054  -37.921 1.00 56.71  ?  236 GLU C CB    1 
ATOM   6293 C  CG    . GLU C 1 243 ? 26.800  49.489  -37.748 1.00 54.83  ?  236 GLU C CG    1 
ATOM   6294 C  CD    . GLU C 1 243 ? 25.439  49.853  -38.319 1.00 51.40  ?  236 GLU C CD    1 
ATOM   6295 O  OE1   . GLU C 1 243 ? 25.253  51.011  -38.617 1.00 50.24  ?  236 GLU C OE1   1 
ATOM   6296 O  OE2   . GLU C 1 243 ? 24.570  48.985  -38.355 1.00 50.43  -1 236 GLU C OE2   1 
ATOM   6297 N  N     . PRO C 1 244 ? 29.296  45.532  -36.255 1.00 65.89  ?  237 PRO C N     1 
ATOM   6298 C  CA    . PRO C 1 244 ? 29.332  44.079  -36.222 1.00 68.07  ?  237 PRO C CA    1 
ATOM   6299 C  C     . PRO C 1 244 ? 27.929  43.477  -36.190 1.00 65.51  ?  237 PRO C C     1 
ATOM   6300 O  O     . PRO C 1 244 ? 26.949  44.128  -35.842 1.00 62.51  ?  237 PRO C O     1 
ATOM   6301 C  CB    . PRO C 1 244 ? 30.111  43.795  -34.919 1.00 71.68  ?  237 PRO C CB    1 
ATOM   6302 C  CG    . PRO C 1 244 ? 29.880  45.014  -34.067 1.00 70.14  ?  237 PRO C CG    1 
ATOM   6303 C  CD    . PRO C 1 244 ? 29.905  46.149  -35.067 1.00 67.85  ?  237 PRO C CD    1 
ATOM   6304 N  N     . ASN C 1 245 ? 27.846  42.204  -36.549 1.00 67.38  ?  238 ASN C N     1 
ATOM   6305 C  CA    . ASN C 1 245 ? 26.583  41.500  -36.636 1.00 65.98  ?  238 ASN C CA    1 
ATOM   6306 C  C     . ASN C 1 245 ? 25.769  41.717  -35.354 1.00 64.84  ?  238 ASN C C     1 
ATOM   6307 O  O     . ASN C 1 245 ? 24.565  41.948  -35.419 1.00 62.31  ?  238 ASN C O     1 
ATOM   6308 C  CB    . ASN C 1 245 ? 26.832  40.031  -36.996 1.00 69.57  ?  238 ASN C CB    1 
ATOM   6309 C  CG    . ASN C 1 245 ? 27.580  39.836  -38.307 1.00 71.28  ?  238 ASN C CG    1 
ATOM   6310 O  OD1   . ASN C 1 245 ? 28.232  38.811  -38.498 1.00 75.39  ?  238 ASN C OD1   1 
ATOM   6311 N  ND2   . ASN C 1 245 ? 27.529  40.803  -39.221 1.00 68.75  ?  238 ASN C ND2   1 
ATOM   6312 N  N     . ARG C 1 246 ? 26.443  41.692  -34.193 1.00 67.19  ?  239 ARG C N     1 
ATOM   6313 C  CA    . ARG C 1 246 ? 25.792  41.833  -32.896 1.00 67.13  ?  239 ARG C CA    1 
ATOM   6314 C  C     . ARG C 1 246 ? 24.943  43.109  -32.811 1.00 63.59  ?  239 ARG C C     1 
ATOM   6315 O  O     . ARG C 1 246 ? 23.860  43.108  -32.228 1.00 62.81  ?  239 ARG C O     1 
ATOM   6316 C  CB    . ARG C 1 246 ? 26.874  41.831  -31.809 1.00 70.58  ?  239 ARG C CB    1 
ATOM   6317 C  CG    . ARG C 1 246 ? 26.365  42.154  -30.414 1.00 71.13  ?  239 ARG C CG    1 
ATOM   6318 C  CD    . ARG C 1 246 ? 27.492  42.171  -29.392 1.00 75.07  ?  239 ARG C CD    1 
ATOM   6319 N  NE    . ARG C 1 246 ? 27.072  42.961  -28.242 1.00 75.19  ?  239 ARG C NE    1 
ATOM   6320 C  CZ    . ARG C 1 246 ? 27.434  44.221  -28.033 1.00 74.70  ?  239 ARG C CZ    1 
ATOM   6321 N  NH1   . ARG C 1 246 ? 28.319  44.795  -28.833 1.00 74.36  ?  239 ARG C NH1   1 
ATOM   6322 N  NH2   . ARG C 1 246 ? 26.931  44.896  -27.014 1.00 75.19  ?  239 ARG C NH2   1 
ATOM   6323 N  N     . LEU C 1 247 ? 25.443  44.197  -33.391 1.00 61.99  ?  240 LEU C N     1 
ATOM   6324 C  CA    . LEU C 1 247 ? 24.834  45.515  -33.281 1.00 59.36  ?  240 LEU C CA    1 
ATOM   6325 C  C     . LEU C 1 247 ? 23.827  45.741  -34.408 1.00 56.17  ?  240 LEU C C     1 
ATOM   6326 O  O     . LEU C 1 247 ? 22.891  46.502  -34.221 1.00 54.31  ?  240 LEU C O     1 
ATOM   6327 C  CB    . LEU C 1 247 ? 25.920  46.586  -33.347 1.00 59.97  ?  240 LEU C CB    1 
ATOM   6328 C  CG    . LEU C 1 247 ? 26.713  46.818  -32.065 1.00 63.15  ?  240 LEU C CG    1 
ATOM   6329 C  CD1   . LEU C 1 247 ? 27.579  48.040  -32.233 1.00 63.79  ?  240 LEU C CD1   1 
ATOM   6330 C  CD2   . LEU C 1 247 ? 25.794  46.963  -30.848 1.00 63.30  ?  240 LEU C CD2   1 
ATOM   6331 N  N     . MET C 1 248 ? 24.015  45.071  -35.551 1.00 56.11  ?  241 MET C N     1 
ATOM   6332 C  CA    . MET C 1 248 ? 23.245  45.399  -36.740 1.00 53.56  ?  241 MET C CA    1 
ATOM   6333 C  C     . MET C 1 248 ? 22.005  44.514  -36.834 1.00 53.39  ?  241 MET C C     1 
ATOM   6334 O  O     . MET C 1 248 ? 20.948  44.942  -37.317 1.00 51.44  ?  241 MET C O     1 
ATOM   6335 C  CB    . MET C 1 248 ? 24.105  45.239  -38.004 1.00 54.17  ?  241 MET C CB    1 
ATOM   6336 C  CG    . MET C 1 248 ? 23.420  45.811  -39.239 1.00 51.76  ?  241 MET C CG    1 
ATOM   6337 S  SD    . MET C 1 248 ? 24.326  45.454  -40.757 1.00 53.33  ?  241 MET C SD    1 
ATOM   6338 C  CE    . MET C 1 248 ? 23.529  46.588  -41.898 1.00 50.36  ?  241 MET C CE    1 
ATOM   6339 N  N     . ALA C 1 249 ? 22.124  43.276  -36.353 1.00 55.97  ?  242 ALA C N     1 
ATOM   6340 C  CA    . ALA C 1 249 ? 21.185  42.222  -36.705 1.00 56.89  ?  242 ALA C CA    1 
ATOM   6341 C  C     . ALA C 1 249 ? 19.757  42.648  -36.392 1.00 55.42  ?  242 ALA C C     1 
ATOM   6342 O  O     . ALA C 1 249 ? 18.863  42.442  -37.206 1.00 54.93  ?  242 ALA C O     1 
ATOM   6343 C  CB    . ALA C 1 249 ? 21.558  40.933  -36.012 1.00 60.42  ?  242 ALA C CB    1 
ATOM   6344 N  N     . LYS C 1 250 ? 19.528  43.262  -35.225 1.00 55.25  ?  243 LYS C N     1 
ATOM   6345 C  CA    . LYS C 1 250 ? 18.168  43.466  -34.762 1.00 55.13  ?  243 LYS C CA    1 
ATOM   6346 C  C     . LYS C 1 250 ? 17.915  44.870  -34.211 1.00 53.55  ?  243 LYS C C     1 
ATOM   6347 O  O     . LYS C 1 250 ? 16.991  45.023  -33.427 1.00 54.54  ?  243 LYS C O     1 
ATOM   6348 C  CB    . LYS C 1 250 ? 17.835  42.411  -33.692 1.00 58.34  ?  243 LYS C CB    1 
ATOM   6349 C  CG    . LYS C 1 250 ? 18.698  41.151  -33.715 1.00 60.85  ?  243 LYS C CG    1 
ATOM   6350 C  CD    . LYS C 1 250 ? 18.004  39.875  -33.280 1.00 64.22  ?  243 LYS C CD    1 
ATOM   6351 C  CE    . LYS C 1 250 ? 17.151  39.282  -34.383 1.00 64.55  ?  243 LYS C CE    1 
ATOM   6352 N  NZ    . LYS C 1 250 ? 16.870  37.848  -34.136 1.00 68.67  ?  243 LYS C NZ    1 
ATOM   6353 N  N     . SER C 1 251 ? 18.668  45.890  -34.653 1.00 51.64  ?  244 SER C N     1 
ATOM   6354 C  CA    . SER C 1 251 ? 18.687  47.239  -34.091 1.00 50.84  ?  244 SER C CA    1 
ATOM   6355 C  C     . SER C 1 251 ? 17.993  48.263  -34.994 1.00 48.56  ?  244 SER C C     1 
ATOM   6356 O  O     . SER C 1 251 ? 18.121  49.482  -34.797 1.00 47.92  ?  244 SER C O     1 
ATOM   6357 C  CB    . SER C 1 251 ? 20.142  47.709  -33.833 1.00 51.29  ?  244 SER C CB    1 
ATOM   6358 O  OG    . SER C 1 251 ? 20.882  47.801  -35.060 1.00 50.04  ?  244 SER C OG    1 
ATOM   6359 N  N     . TYR C 1 252 ? 17.318  47.745  -36.032 1.00 47.79  ?  245 TYR C N     1 
ATOM   6360 C  CA    . TYR C 1 252 ? 16.680  48.587  -37.024 1.00 46.00  ?  245 TYR C CA    1 
ATOM   6361 C  C     . TYR C 1 252 ? 15.195  48.225  -37.101 1.00 46.83  ?  245 TYR C C     1 
ATOM   6362 O  O     . TYR C 1 252 ? 14.773  47.110  -36.781 1.00 48.65  ?  245 TYR C O     1 
ATOM   6363 C  CB    . TYR C 1 252 ? 17.227  48.433  -38.443 1.00 44.82  ?  245 TYR C CB    1 
ATOM   6364 C  CG    . TYR C 1 252 ? 18.631  48.960  -38.711 1.00 44.30  ?  245 TYR C CG    1 
ATOM   6365 C  CD1   . TYR C 1 252 ? 19.757  48.306  -38.222 1.00 45.75  ?  245 TYR C CD1   1 
ATOM   6366 C  CD2   . TYR C 1 252 ? 18.824  50.099  -39.471 1.00 42.94  ?  245 TYR C CD2   1 
ATOM   6367 C  CE1   . TYR C 1 252 ? 21.029  48.782  -38.484 1.00 46.01  ?  245 TYR C CE1   1 
ATOM   6368 C  CE2   . TYR C 1 252 ? 20.088  50.588  -39.749 1.00 43.12  ?  245 TYR C CE2   1 
ATOM   6369 C  CZ    . TYR C 1 252 ? 21.198  49.908  -39.270 1.00 44.75  ?  245 TYR C CZ    1 
ATOM   6370 O  OH    . TYR C 1 252 ? 22.449  50.393  -39.553 1.00 45.62  ?  245 TYR C OH    1 
ATOM   6371 N  N     . LEU C 1 253 ? 14.433  49.227  -37.503 1.00 45.98  ?  246 LEU C N     1 
ATOM   6372 C  CA    . LEU C 1 253 ? 13.042  49.070  -37.877 1.00 46.96  ?  246 LEU C CA    1 
ATOM   6373 C  C     . LEU C 1 253 ? 12.956  49.133  -39.397 1.00 45.69  ?  246 LEU C C     1 
ATOM   6374 O  O     . LEU C 1 253 ? 13.335  50.168  -39.950 1.00 44.03  ?  246 LEU C O     1 
ATOM   6375 C  CB    . LEU C 1 253 ? 12.291  50.227  -37.231 1.00 47.56  ?  246 LEU C CB    1 
ATOM   6376 C  CG    . LEU C 1 253 ? 12.181  50.177  -35.708 1.00 49.68  ?  246 LEU C CG    1 
ATOM   6377 C  CD1   . LEU C 1 253 ? 11.597  51.470  -35.178 1.00 50.60  ?  246 LEU C CD1   1 
ATOM   6378 C  CD2   . LEU C 1 253 ? 11.314  49.006  -35.261 1.00 52.38  ?  246 LEU C CD2   1 
ATOM   6379 N  N     . ILE C 1 254 ? 12.533  48.019  -40.037 1.00 46.94  ?  247 ILE C N     1 
ATOM   6380 C  CA    . ILE C 1 254 ? 12.647  47.828  -41.477 1.00 46.40  ?  247 ILE C CA    1 
ATOM   6381 C  C     . ILE C 1 254 ? 11.276  47.487  -42.055 1.00 48.38  ?  247 ILE C C     1 
ATOM   6382 O  O     . ILE C 1 254 ? 10.709  46.452  -41.707 1.00 50.84  ?  247 ILE C O     1 
ATOM   6383 C  CB    . ILE C 1 254 ? 13.618  46.670  -41.768 1.00 47.03  ?  247 ILE C CB    1 
ATOM   6384 C  CG1   . ILE C 1 254 ? 15.011  46.943  -41.192 1.00 45.82  ?  247 ILE C CG1   1 
ATOM   6385 C  CG2   . ILE C 1 254 ? 13.679  46.360  -43.255 1.00 47.36  ?  247 ILE C CG2   1 
ATOM   6386 C  CD1   . ILE C 1 254 ? 15.802  45.708  -40.928 1.00 47.42  ?  247 ILE C CD1   1 
ATOM   6387 N  N     . LEU C 1 255 ? 10.799  48.331  -42.968 1.00 47.73  ?  248 LEU C N     1 
ATOM   6388 C  CA    . LEU C 1 255 ? 9.554   48.095  -43.670 1.00 49.98  ?  248 LEU C CA    1 
ATOM   6389 C  C     . LEU C 1 255 ? 9.862   47.574  -45.058 1.00 50.35  ?  248 LEU C C     1 
ATOM   6390 O  O     . LEU C 1 255 ? 10.749  48.105  -45.725 1.00 48.38  ?  248 LEU C O     1 
ATOM   6391 C  CB    . LEU C 1 255 ? 8.775   49.397  -43.807 1.00 49.73  ?  248 LEU C CB    1 
ATOM   6392 C  CG    . LEU C 1 255 ? 8.220   49.983  -42.522 1.00 50.47  ?  248 LEU C CG    1 
ATOM   6393 C  CD1   . LEU C 1 255 ? 7.770   51.425  -42.734 1.00 50.06  ?  248 LEU C CD1   1 
ATOM   6394 C  CD2   . LEU C 1 255 ? 7.081   49.117  -41.992 1.00 54.12  ?  248 LEU C CD2   1 
ATOM   6395 N  N     . ASP C 1 256 ? 9.009   46.663  -45.533 1.00 53.47  ?  249 ASP C N     1 
ATOM   6396 C  CA    . ASP C 1 256 ? 9.182   46.141  -46.874 1.00 54.71  ?  249 ASP C CA    1 
ATOM   6397 C  C     . ASP C 1 256 ? 8.292   46.919  -47.833 1.00 55.54  ?  249 ASP C C     1 
ATOM   6398 O  O     . ASP C 1 256 ? 7.721   47.973  -47.498 1.00 54.69  ?  249 ASP C O     1 
ATOM   6399 C  CB    . ASP C 1 256 ? 8.946   44.626  -46.913 1.00 58.25  ?  249 ASP C CB    1 
ATOM   6400 C  CG    . ASP C 1 256 ? 7.505   44.195  -46.706 1.00 62.01  ?  249 ASP C CG    1 
ATOM   6401 O  OD1   . ASP C 1 256 ? 6.637   45.072  -46.418 1.00 61.94  ?  249 ASP C OD1   1 
ATOM   6402 O  OD2   . ASP C 1 256 ? 7.265   42.981  -46.811 1.00 65.50  -1 249 ASP C OD2   1 
ATOM   6403 N  N     . GLU C 1 257 ? 8.172   46.348  -49.043 1.00 57.82  ?  250 GLU C N     1 
ATOM   6404 C  CA    . GLU C 1 257 ? 7.523   47.041  -50.139 1.00 58.87  ?  250 GLU C CA    1 
ATOM   6405 C  C     . GLU C 1 257 ? 6.007   47.062  -49.939 1.00 62.07  ?  250 GLU C C     1 
ATOM   6406 O  O     . GLU C 1 257 ? 5.347   47.802  -50.656 1.00 63.10  ?  250 GLU C O     1 
ATOM   6407 C  CB    . GLU C 1 257 ? 7.944   46.428  -51.476 1.00 60.81  ?  250 GLU C CB    1 
ATOM   6408 C  CG    . GLU C 1 257 ? 7.511   44.982  -51.664 1.00 65.12  ?  250 GLU C CG    1 
ATOM   6409 C  CD    . GLU C 1 257 ? 8.493   43.874  -51.298 1.00 65.35  ?  250 GLU C CD    1 
ATOM   6410 O  OE1   . GLU C 1 257 ? 8.268   42.757  -51.787 1.00 69.43  ?  250 GLU C OE1   1 
ATOM   6411 O  OE2   . GLU C 1 257 ? 9.458   44.101  -50.516 1.00 62.03  -1 250 GLU C OE2   1 
ATOM   6412 N  N     . TYR C 1 258 ? 5.461   46.298  -48.961 1.00 64.06  ?  251 TYR C N     1 
ATOM   6413 C  CA    . TYR C 1 258 ? 4.047   46.386  -48.582 1.00 67.52  ?  251 TYR C CA    1 
ATOM   6414 C  C     . TYR C 1 258 ? 3.866   47.131  -47.253 1.00 65.84  ?  251 TYR C C     1 
ATOM   6415 O  O     . TYR C 1 258 ? 2.752   47.218  -46.721 1.00 68.97  ?  251 TYR C O     1 
ATOM   6416 C  CB    . TYR C 1 258 ? 3.395   44.999  -48.500 1.00 72.38  ?  251 TYR C CB    1 
ATOM   6417 C  CG    . TYR C 1 258 ? 3.413   44.217  -49.806 1.00 75.34  ?  251 TYR C CG    1 
ATOM   6418 C  CD1   . TYR C 1 258 ? 2.392   44.335  -50.749 1.00 79.36  ?  251 TYR C CD1   1 
ATOM   6419 C  CD2   . TYR C 1 258 ? 4.482   43.384  -50.109 1.00 74.58  ?  251 TYR C CD2   1 
ATOM   6420 C  CE1   . TYR C 1 258 ? 2.427   43.624  -51.937 1.00 82.58  ?  251 TYR C CE1   1 
ATOM   6421 C  CE2   . TYR C 1 258 ? 4.534   42.680  -51.298 1.00 77.82  ?  251 TYR C CE2   1 
ATOM   6422 C  CZ    . TYR C 1 258 ? 3.501   42.796  -52.211 1.00 81.84  ?  251 TYR C CZ    1 
ATOM   6423 O  OH    . TYR C 1 258 ? 3.601   42.087  -53.375 1.00 85.47  ?  251 TYR C OH    1 
ATOM   6424 N  N     . MET C 1 259 ? 4.972   47.682  -46.733 1.00 61.47  ?  252 MET C N     1 
ATOM   6425 C  CA    . MET C 1 259 ? 5.014   48.448  -45.499 1.00 59.82  ?  252 MET C CA    1 
ATOM   6426 C  C     . MET C 1 259 ? 4.724   47.523  -44.303 1.00 61.96  ?  252 MET C C     1 
ATOM   6427 O  O     . MET C 1 259 ? 4.123   47.916  -43.302 1.00 63.25  ?  252 MET C O     1 
ATOM   6428 C  CB    . MET C 1 259 ? 4.073   49.662  -45.542 1.00 60.87  ?  252 MET C CB    1 
ATOM   6429 C  CG    . MET C 1 259 ? 4.327   50.611  -46.698 1.00 59.19  ?  252 MET C CG    1 
ATOM   6430 S  SD    . MET C 1 259 ? 3.623   52.275  -46.480 1.00 59.61  ?  252 MET C SD    1 
ATOM   6431 C  CE    . MET C 1 259 ? 4.866   53.107  -45.498 1.00 55.40  ?  252 MET C CE    1 
ATOM   6432 N  N     . ARG C 1 260 ? 5.244   46.295  -44.406 1.00 62.58  ?  253 ARG C N     1 
ATOM   6433 C  CA    . ARG C 1 260 ? 5.278   45.333  -43.317 1.00 64.29  ?  253 ARG C CA    1 
ATOM   6434 C  C     . ARG C 1 260 ? 6.653   45.384  -42.641 1.00 60.64  ?  253 ARG C C     1 
ATOM   6435 O  O     . ARG C 1 260 ? 7.669   45.435  -43.325 1.00 58.09  ?  253 ARG C O     1 
ATOM   6436 C  CB    . ARG C 1 260 ? 5.009   43.932  -43.872 1.00 67.97  ?  253 ARG C CB    1 
ATOM   6437 C  CG    . ARG C 1 260 ? 3.684   43.810  -44.617 1.00 72.33  ?  253 ARG C CG    1 
ATOM   6438 C  CD    . ARG C 1 260 ? 3.524   42.430  -45.215 1.00 76.36  ?  253 ARG C CD    1 
ATOM   6439 N  NE    . ARG C 1 260 ? 4.567   42.112  -46.181 1.00 74.41  ?  253 ARG C NE    1 
ATOM   6440 C  CZ    . ARG C 1 260 ? 4.852   40.879  -46.597 1.00 77.26  ?  253 ARG C CZ    1 
ATOM   6441 N  NH1   . ARG C 1 260 ? 4.100   39.861  -46.217 1.00 82.31  ?  253 ARG C NH1   1 
ATOM   6442 N  NH2   . ARG C 1 260 ? 5.866   40.670  -47.419 1.00 75.70  ?  253 ARG C NH2   1 
ATOM   6443 N  N     . PHE C 1 261 ? 6.681   45.329  -41.308 1.00 61.03  ?  254 PHE C N     1 
ATOM   6444 C  CA    . PHE C 1 261 ? 7.937   45.305  -40.563 1.00 58.42  ?  254 PHE C CA    1 
ATOM   6445 C  C     . PHE C 1 261 ? 8.610   43.952  -40.764 1.00 59.48  ?  254 PHE C C     1 
ATOM   6446 O  O     . PHE C 1 261 ? 7.937   42.929  -40.642 1.00 63.16  ?  254 PHE C O     1 
ATOM   6447 C  CB    . PHE C 1 261 ? 7.687   45.554  -39.073 1.00 59.46  ?  254 PHE C CB    1 
ATOM   6448 C  CG    . PHE C 1 261 ? 7.496   47.004  -38.708 1.00 57.97  ?  254 PHE C CG    1 
ATOM   6449 C  CD1   . PHE C 1 261 ? 8.533   47.918  -38.870 1.00 54.32  ?  254 PHE C CD1   1 
ATOM   6450 C  CD2   . PHE C 1 261 ? 6.294   47.458  -38.200 1.00 60.82  ?  254 PHE C CD2   1 
ATOM   6451 C  CE1   . PHE C 1 261 ? 8.354   49.255  -38.556 1.00 53.52  ?  254 PHE C CE1   1 
ATOM   6452 C  CE2   . PHE C 1 261 ? 6.115   48.800  -37.908 1.00 60.02  ?  254 PHE C CE2   1 
ATOM   6453 C  CZ    . PHE C 1 261 ? 7.143   49.692  -38.077 1.00 56.36  ?  254 PHE C CZ    1 
ATOM   6454 N  N     . LEU C 1 262 ? 9.915   43.946  -41.099 1.00 56.87  ?  255 LEU C N     1 
ATOM   6455 C  CA    . LEU C 1 262 ? 10.665  42.710  -41.262 1.00 58.22  ?  255 LEU C CA    1 
ATOM   6456 C  C     . LEU C 1 262 ? 11.460  42.375  -39.993 1.00 58.11  ?  255 LEU C C     1 
ATOM   6457 O  O     . LEU C 1 262 ? 11.968  43.281  -39.334 1.00 55.74  ?  255 LEU C O     1 
ATOM   6458 C  CB    . LEU C 1 262 ? 11.614  42.850  -42.456 1.00 56.41  ?  255 LEU C CB    1 
ATOM   6459 C  CG    . LEU C 1 262 ? 10.978  43.166  -43.813 1.00 56.77  ?  255 LEU C CG    1 
ATOM   6460 C  CD1   . LEU C 1 262 ? 12.051  43.198  -44.889 1.00 55.63  ?  255 LEU C CD1   1 
ATOM   6461 C  CD2   . LEU C 1 262 ? 9.891   42.162  -44.170 1.00 61.00  ?  255 LEU C CD2   1 
ATOM   6462 N  N     . ASP C 1 263 ? 11.608  41.070  -39.699 1.00 61.10  ?  256 ASP C N     1 
ATOM   6463 C  CA    . ASP C 1 263 ? 12.328  40.572  -38.527 1.00 61.87  ?  256 ASP C CA    1 
ATOM   6464 C  C     . ASP C 1 263 ? 13.745  40.118  -38.919 1.00 61.25  ?  256 ASP C C     1 
ATOM   6465 O  O     . ASP C 1 263 ? 14.598  39.878  -38.060 1.00 61.52  ?  256 ASP C O     1 
ATOM   6466 C  CB    . ASP C 1 263 ? 11.522  39.442  -37.865 1.00 66.31  ?  256 ASP C CB    1 
ATOM   6467 C  CG    . ASP C 1 263 ? 11.459  39.455  -36.337 1.00 67.48  ?  256 ASP C CG    1 
ATOM   6468 O  OD1   . ASP C 1 263 ? 11.787  40.507  -35.717 1.00 64.89  -1 256 ASP C OD1   1 
ATOM   6469 O  OD2   . ASP C 1 263 ? 11.068  38.404  -35.759 1.00 71.48  ?  256 ASP C OD2   1 
ATOM   6470 N  N     . ARG C 1 264 ? 14.011  40.009  -40.227 1.00 60.93  ?  257 ARG C N     1 
ATOM   6471 C  CA    . ARG C 1 264 ? 15.348  39.757  -40.748 1.00 60.60  ?  257 ARG C CA    1 
ATOM   6472 C  C     . ARG C 1 264 ? 15.919  38.446  -40.181 1.00 64.06  ?  257 ARG C C     1 
ATOM   6473 O  O     . ARG C 1 264 ? 17.144  38.426  -39.907 1.00 63.76  ?  257 ARG C O     1 
ATOM   6474 C  CB    . ARG C 1 264 ? 16.253  40.959  -40.447 1.00 57.11  ?  257 ARG C CB    1 
ATOM   6475 C  CG    . ARG C 1 264 ? 15.625  42.303  -40.794 1.00 54.13  ?  257 ARG C CG    1 
ATOM   6476 C  CD    . ARG C 1 264 ? 15.316  42.463  -42.271 1.00 53.88  ?  257 ARG C CD    1 
ATOM   6477 N  NE    . ARG C 1 264 ? 16.535  42.596  -43.059 1.00 53.32  ?  257 ARG C NE    1 
ATOM   6478 C  CZ    . ARG C 1 264 ? 16.663  42.256  -44.341 1.00 54.57  ?  257 ARG C CZ    1 
ATOM   6479 N  NH1   . ARG C 1 264 ? 15.717  41.548  -44.944 1.00 56.88  ?  257 ARG C NH1   1 
ATOM   6480 N  NH2   . ARG C 1 264 ? 17.781  42.555  -44.987 1.00 54.22  ?  257 ARG C NH2   1 
ATOM   6481 N  N     . PRO C 1 269 ? 7.181   38.222  -41.650 1.00 77.43  ?  262 PRO C N     1 
ATOM   6482 C  CA    . PRO C 1 269 ? 6.830   39.657  -41.605 1.00 73.98  ?  262 PRO C CA    1 
ATOM   6483 C  C     . PRO C 1 269 ? 5.531   39.899  -40.847 1.00 76.91  ?  262 PRO C C     1 
ATOM   6484 O  O     . PRO C 1 269 ? 4.703   38.998  -40.748 1.00 82.01  ?  262 PRO C O     1 
ATOM   6485 C  CB    . PRO C 1 269 ? 6.649   40.087  -43.068 1.00 73.25  ?  262 PRO C CB    1 
ATOM   6486 C  CG    . PRO C 1 269 ? 7.387   39.027  -43.856 1.00 74.80  ?  262 PRO C CG    1 
ATOM   6487 C  CD    . PRO C 1 269 ? 7.201   37.760  -43.049 1.00 79.05  ?  262 PRO C CD    1 
ATOM   6488 N  N     . SER C 1 270 ? 5.371   41.115  -40.317 1.00 74.25  ?  263 SER C N     1 
ATOM   6489 C  CA    . SER C 1 270 ? 4.137   41.515  -39.672 1.00 77.29  ?  263 SER C CA    1 
ATOM   6490 C  C     . SER C 1 270 ? 3.085   41.736  -40.751 1.00 79.70  ?  263 SER C C     1 
ATOM   6491 O  O     . SER C 1 270 ? 3.398   41.698  -41.940 1.00 78.40  ?  263 SER C O     1 
ATOM   6492 C  CB    . SER C 1 270 ? 4.321   42.738  -38.815 1.00 74.36  ?  263 SER C CB    1 
ATOM   6493 O  OG    . SER C 1 270 ? 4.357   43.933  -39.583 1.00 71.16  ?  263 SER C OG    1 
ATOM   6494 N  N     . LYS C 1 271 ? 1.844   41.958  -40.326 1.00 83.76  ?  264 LYS C N     1 
ATOM   6495 C  CA    . LYS C 1 271 ? 0.849   42.512  -41.226 1.00 85.80  ?  264 LYS C CA    1 
ATOM   6496 C  C     . LYS C 1 271 ? 1.251   43.956  -41.510 1.00 80.82  ?  264 LYS C C     1 
ATOM   6497 O  O     . LYS C 1 271 ? 1.940   44.590  -40.706 1.00 77.31  ?  264 LYS C O     1 
ATOM   6498 C  CB    . LYS C 1 271 ? -0.565  42.422  -40.637 1.00 92.07  ?  264 LYS C CB    1 
ATOM   6499 C  CG    . LYS C 1 271 ? -0.930  41.073  -40.026 1.00 97.42  ?  264 LYS C CG    1 
ATOM   6500 C  CD    . LYS C 1 271 ? -2.378  40.664  -40.231 1.00 105.01 ?  264 LYS C CD    1 
ATOM   6501 C  CE    . LYS C 1 271 ? -2.722  39.341  -39.575 1.00 110.84 ?  264 LYS C CE    1 
ATOM   6502 N  NZ    . LYS C 1 271 ? -1.828  38.244  -40.023 1.00 109.74 ?  264 LYS C NZ    1 
ATOM   6503 N  N     . SER C 1 272 ? 0.789   44.460  -42.657 1.00 81.14  ?  265 SER C N     1 
ATOM   6504 C  CA    . SER C 1 272 ? 1.091   45.808  -43.101 1.00 77.17  ?  265 SER C CA    1 
ATOM   6505 C  C     . SER C 1 272 ? 0.606   46.827  -42.073 1.00 77.56  ?  265 SER C C     1 
ATOM   6506 O  O     . SER C 1 272 ? -0.406  46.643  -41.400 1.00 82.29  ?  265 SER C O     1 
ATOM   6507 C  CB    . SER C 1 272 ? 0.494   46.042  -44.477 1.00 78.85  ?  265 SER C CB    1 
ATOM   6508 O  OG    . SER C 1 272 ? 0.463   47.425  -44.794 1.00 76.48  ?  265 SER C OG    1 
ATOM   6509 N  N     . ILE C 1 273 ? 1.329   47.937  -41.952 1.00 73.13  ?  266 ILE C N     1 
ATOM   6510 C  CA    . ILE C 1 273 ? 0.869   49.005  -41.087 1.00 73.96  ?  266 ILE C CA    1 
ATOM   6511 C  C     . ILE C 1 273 ? -0.441  49.574  -41.629 1.00 78.13  ?  266 ILE C C     1 
ATOM   6512 O  O     . ILE C 1 273 ? -1.199  50.147  -40.859 1.00 81.28  ?  266 ILE C O     1 
ATOM   6513 C  CB    . ILE C 1 273 ? 1.970   50.067  -40.879 1.00 68.86  ?  266 ILE C CB    1 
ATOM   6514 C  CG1   . ILE C 1 273 ? 2.453   50.702  -42.188 1.00 65.70  ?  266 ILE C CG1   1 
ATOM   6515 C  CG2   . ILE C 1 273 ? 3.136   49.452  -40.118 1.00 66.09  ?  266 ILE C CG2   1 
ATOM   6516 C  CD1   . ILE C 1 273 ? 3.370   51.873  -41.961 1.00 61.84  ?  266 ILE C CD1   1 
ATOM   6517 N  N     . LEU C 1 274 ? -0.672  49.410  -42.941 1.00 78.55  ?  267 LEU C N     1 
ATOM   6518 C  CA    . LEU C 1 274 ? -1.858  49.908  -43.637 1.00 82.73  ?  267 LEU C CA    1 
ATOM   6519 C  C     . LEU C 1 274 ? -3.079  49.019  -43.388 1.00 89.54  ?  267 LEU C C     1 
ATOM   6520 O  O     . LEU C 1 274 ? -4.184  49.382  -43.773 1.00 94.25  ?  267 LEU C O     1 
ATOM   6521 C  CB    . LEU C 1 274 ? -1.587  49.929  -45.144 1.00 81.15  ?  267 LEU C CB    1 
ATOM   6522 C  CG    . LEU C 1 274 ? -0.458  50.840  -45.627 1.00 75.33  ?  267 LEU C CG    1 
ATOM   6523 C  CD1   . LEU C 1 274 ? -0.167  50.588  -47.096 1.00 74.59  ?  267 LEU C CD1   1 
ATOM   6524 C  CD2   . LEU C 1 274 ? -0.793  52.304  -45.395 1.00 75.31  ?  267 LEU C CD2   1 
ATOM   6525 N  N     . GLU C 1 275 ? -2.859  47.830  -42.819 1.00 90.49  ?  268 GLU C N     1 
ATOM   6526 C  CA    . GLU C 1 275 ? -3.922  46.861  -42.600 1.00 97.32  ?  268 GLU C CA    1 
ATOM   6527 C  C     . GLU C 1 275 ? -4.282  46.782  -41.115 1.00 100.14 ?  268 GLU C C     1 
ATOM   6528 O  O     . GLU C 1 275 ? -5.442  46.551  -40.793 1.00 106.83 ?  268 GLU C O     1 
ATOM   6529 C  CB    . GLU C 1 275 ? -3.458  45.512  -43.153 1.00 97.37  ?  268 GLU C CB    1 
ATOM   6530 C  CG    . GLU C 1 275 ? -4.554  44.489  -43.351 1.00 104.95 ?  268 GLU C CG    1 
ATOM   6531 C  CD    . GLU C 1 275 ? -4.061  43.246  -44.078 1.00 105.26 ?  268 GLU C CD    1 
ATOM   6532 O  OE1   . GLU C 1 275 ? -4.000  42.172  -43.441 1.00 107.76 ?  268 GLU C OE1   1 
ATOM   6533 O  OE2   . GLU C 1 275 ? -3.720  43.359  -45.279 1.00 103.34 -1 268 GLU C OE2   1 
ATOM   6534 N  N     . VAL C 1 276 ? -3.295  46.962  -40.216 1.00 95.64  ?  269 VAL C N     1 
ATOM   6535 C  CA    . VAL C 1 276 ? -3.501  46.719  -38.792 1.00 98.42  ?  269 VAL C CA    1 
ATOM   6536 C  C     . VAL C 1 276 ? -3.162  47.936  -37.930 1.00 95.99  ?  269 VAL C C     1 
ATOM   6537 O  O     . VAL C 1 276 ? -3.580  47.973  -36.777 1.00 99.59  ?  269 VAL C O     1 
ATOM   6538 C  CB    . VAL C 1 276 ? -2.706  45.488  -38.306 1.00 97.17  ?  269 VAL C CB    1 
ATOM   6539 C  CG1   . VAL C 1 276 ? -3.213  44.191  -38.916 1.00 101.51 ?  269 VAL C CG1   1 
ATOM   6540 C  CG2   . VAL C 1 276 ? -1.212  45.638  -38.537 1.00 89.78  ?  269 VAL C CG2   1 
ATOM   6541 N  N     . GLY C 1 277 ? -2.372  48.897  -38.440 1.00 90.39  ?  270 GLY C N     1 
ATOM   6542 C  CA    . GLY C 1 277 ? -1.831  49.960  -37.607 1.00 87.88  ?  270 GLY C CA    1 
ATOM   6543 C  C     . GLY C 1 277 ? -0.375  49.692  -37.219 1.00 82.31  ?  270 GLY C C     1 
ATOM   6544 O  O     . GLY C 1 277 ? 0.106   48.571  -37.367 1.00 81.28  ?  270 GLY C O     1 
ATOM   6545 N  N     . VAL C 1 278 ? 0.315   50.734  -36.733 1.00 79.31  ?  271 VAL C N     1 
ATOM   6546 C  CA    . VAL C 1 278 ? 1.747   50.669  -36.454 1.00 74.24  ?  271 VAL C CA    1 
ATOM   6547 C  C     . VAL C 1 278 ? 1.974   49.862  -35.174 1.00 76.07  ?  271 VAL C C     1 
ATOM   6548 O  O     . VAL C 1 278 ? 2.927   49.091  -35.074 1.00 73.48  ?  271 VAL C O     1 
ATOM   6549 C  CB    . VAL C 1 278 ? 2.338   52.090  -36.348 1.00 71.45  ?  271 VAL C CB    1 
ATOM   6550 C  CG1   . VAL C 1 278 ? 3.758   52.103  -35.791 1.00 67.54  ?  271 VAL C CG1   1 
ATOM   6551 C  CG2   . VAL C 1 278 ? 2.271   52.813  -37.688 1.00 69.39  ?  271 VAL C CG2   1 
ATOM   6552 N  N     . GLN C 1 279 ? 1.087   50.057  -34.192 1.00 81.07  ?  272 GLN C N     1 
ATOM   6553 C  CA    . GLN C 1 279 ? 1.242   49.443  -32.887 1.00 83.53  ?  272 GLN C CA    1 
ATOM   6554 C  C     . GLN C 1 279 ? 1.144   47.933  -33.039 1.00 85.00  ?  272 GLN C C     1 
ATOM   6555 O  O     . GLN C 1 279 ? 1.907   47.189  -32.431 1.00 84.10  ?  272 GLN C O     1 
ATOM   6556 C  CB    . GLN C 1 279 ? 0.188   49.949  -31.898 1.00 89.61  ?  272 GLN C CB    1 
ATOM   6557 C  CG    . GLN C 1 279 ? 0.425   49.438  -30.476 1.00 92.39  ?  272 GLN C CG    1 
ATOM   6558 C  CD    . GLN C 1 279 ? -0.675  49.763  -29.492 1.00 99.49  ?  272 GLN C CD    1 
ATOM   6559 O  OE1   . GLN C 1 279 ? -1.739  50.264  -29.852 1.00 103.09 ?  272 GLN C OE1   1 
ATOM   6560 N  NE2   . GLN C 1 279 ? -0.423  49.457  -28.228 1.00 102.11 ?  272 GLN C NE2   1 
ATOM   6561 N  N     . GLN C 1 280 ? 0.173   47.495  -33.833 1.00 87.91  ?  273 GLN C N     1 
ATOM   6562 C  CA    . GLN C 1 280 ? -0.096  46.076  -33.995 1.00 90.63  ?  273 GLN C CA    1 
ATOM   6563 C  C     . GLN C 1 280 ? 1.040   45.426  -34.786 1.00 85.61  ?  273 GLN C C     1 
ATOM   6564 O  O     . GLN C 1 280 ? 1.524   44.359  -34.411 1.00 86.11  ?  273 GLN C O     1 
ATOM   6565 C  CB    . GLN C 1 280 ? -1.462  45.882  -34.657 1.00 95.79  ?  273 GLN C CB    1 
ATOM   6566 C  CG    . GLN C 1 280 ? -1.907  44.429  -34.759 1.00 100.13 ?  273 GLN C CG    1 
ATOM   6567 C  CD    . GLN C 1 280 ? -1.938  43.746  -33.412 1.00 103.86 ?  273 GLN C CD    1 
ATOM   6568 O  OE1   . GLN C 1 280 ? -2.434  44.295  -32.426 1.00 107.14 ?  273 GLN C OE1   1 
ATOM   6569 N  NE2   . GLN C 1 280 ? -1.380  42.546  -33.354 1.00 103.75 ?  273 GLN C NE2   1 
ATOM   6570 N  N     . ALA C 1 281 ? 1.464   46.083  -35.877 1.00 81.26  ?  274 ALA C N     1 
ATOM   6571 C  CA    . ALA C 1 281 ? 2.539   45.573  -36.720 1.00 76.95  ?  274 ALA C CA    1 
ATOM   6572 C  C     . ALA C 1 281 ? 3.839   45.499  -35.922 1.00 73.64  ?  274 ALA C C     1 
ATOM   6573 O  O     . ALA C 1 281 ? 4.579   44.534  -36.068 1.00 72.70  ?  274 ALA C O     1 
ATOM   6574 C  CB    . ALA C 1 281 ? 2.708   46.450  -37.940 1.00 73.54  ?  274 ALA C CB    1 
ATOM   6575 N  N     . LEU C 1 282 ? 4.083   46.499  -35.063 1.00 72.59  ?  275 LEU C N     1 
ATOM   6576 C  CA    . LEU C 1 282 ? 5.373   46.637  -34.397 1.00 69.46  ?  275 LEU C CA    1 
ATOM   6577 C  C     . LEU C 1 282 ? 5.544   45.578  -33.307 1.00 72.25  ?  275 LEU C C     1 
ATOM   6578 O  O     . LEU C 1 282 ? 6.625   45.019  -33.146 1.00 70.32  ?  275 LEU C O     1 
ATOM   6579 C  CB    . LEU C 1 282 ? 5.511   48.061  -33.845 1.00 68.34  ?  275 LEU C CB    1 
ATOM   6580 C  CG    . LEU C 1 282 ? 6.939   48.567  -33.639 1.00 64.30  ?  275 LEU C CG    1 
ATOM   6581 C  CD1   . LEU C 1 282 ? 7.718   48.592  -34.946 1.00 60.16  ?  275 LEU C CD1   1 
ATOM   6582 C  CD2   . LEU C 1 282 ? 6.926   49.956  -33.017 1.00 64.46  ?  275 LEU C CD2   1 
ATOM   6583 N  N     . GLN C 1 283 ? 4.464   45.228  -32.605 1.00 77.38  ?  276 GLN C N     1 
ATOM   6584 C  CA    . GLN C 1 283 ? 4.602   44.253  -31.533 1.00 80.55  ?  276 GLN C CA    1 
ATOM   6585 C  C     . GLN C 1 283 ? 4.870   42.857  -32.109 1.00 81.05  ?  276 GLN C C     1 
ATOM   6586 O  O     . GLN C 1 283 ? 5.187   41.940  -31.351 1.00 83.30  ?  276 GLN C O     1 
ATOM   6587 C  CB    . GLN C 1 283 ? 3.379   44.299  -30.612 1.00 86.55  ?  276 GLN C CB    1 
ATOM   6588 C  CG    . GLN C 1 283 ? 2.223   43.423  -31.072 1.00 91.29  ?  276 GLN C CG    1 
ATOM   6589 C  CD    . GLN C 1 283 ? 0.976   43.650  -30.256 1.00 97.62  ?  276 GLN C CD    1 
ATOM   6590 O  OE1   . GLN C 1 283 ? 0.994   44.337  -29.233 1.00 98.86  ?  276 GLN C OE1   1 
ATOM   6591 N  NE2   . GLN C 1 283 ? -0.121  43.064  -30.710 1.00 102.32 ?  276 GLN C NE2   1 
ATOM   6592 N  N     . ALA C 1 284 ? 4.769   42.692  -33.439 1.00 79.38  ?  277 ALA C N     1 
ATOM   6593 C  CA    . ALA C 1 284 ? 4.988   41.398  -34.074 1.00 80.47  ?  277 ALA C CA    1 
ATOM   6594 C  C     . ALA C 1 284 ? 6.457   41.163  -34.423 1.00 76.20  ?  277 ALA C C     1 
ATOM   6595 O  O     . ALA C 1 284 ? 6.754   40.122  -34.995 1.00 77.16  ?  277 ALA C O     1 
ATOM   6596 C  CB    . ALA C 1 284 ? 4.128   41.262  -35.310 1.00 81.86  ?  277 ALA C CB    1 
ATOM   6597 N  N     . VAL C 1 285 ? 7.355   42.120  -34.114 1.00 72.14  ?  278 VAL C N     1 
ATOM   6598 C  CA    . VAL C 1 285 ? 8.784   41.988  -34.413 1.00 68.61  ?  278 VAL C CA    1 
ATOM   6599 C  C     . VAL C 1 285 ? 9.615   42.409  -33.203 1.00 67.73  ?  278 VAL C C     1 
ATOM   6600 O  O     . VAL C 1 285 ? 9.176   43.194  -32.372 1.00 68.52  ?  278 VAL C O     1 
ATOM   6601 C  CB    . VAL C 1 285 ? 9.215   42.828  -35.634 1.00 64.42  ?  278 VAL C CB    1 
ATOM   6602 C  CG1   . VAL C 1 285 ? 8.689   42.250  -36.940 1.00 65.38  ?  278 VAL C CG1   1 
ATOM   6603 C  CG2   . VAL C 1 285 ? 8.829   44.298  -35.480 1.00 62.66  ?  278 VAL C CG2   1 
ATOM   6604 N  N     . PHE C 1 286 ? 10.854  41.916  -33.164 1.00 66.44  ?  279 PHE C N     1 
ATOM   6605 C  CA    . PHE C 1 286 ? 11.815  42.292  -32.148 1.00 65.73  ?  279 PHE C CA    1 
ATOM   6606 C  C     . PHE C 1 286 ? 12.646  43.460  -32.680 1.00 61.54  ?  279 PHE C C     1 
ATOM   6607 O  O     . PHE C 1 286 ? 13.104  43.416  -33.819 1.00 59.32  ?  279 PHE C O     1 
ATOM   6608 C  CB    . PHE C 1 286 ? 12.681  41.079  -31.785 1.00 67.53  ?  279 PHE C CB    1 
ATOM   6609 C  CG    . PHE C 1 286 ? 13.702  41.357  -30.711 1.00 67.56  ?  279 PHE C CG    1 
ATOM   6610 C  CD1   . PHE C 1 286 ? 13.306  41.592  -29.403 1.00 70.11  ?  279 PHE C CD1   1 
ATOM   6611 C  CD2   . PHE C 1 286 ? 15.053  41.416  -31.015 1.00 65.58  ?  279 PHE C CD2   1 
ATOM   6612 C  CE1   . PHE C 1 286 ? 14.243  41.871  -28.418 1.00 70.63  ?  279 PHE C CE1   1 
ATOM   6613 C  CE2   . PHE C 1 286 ? 15.989  41.696  -30.029 1.00 66.17  ?  279 PHE C CE2   1 
ATOM   6614 C  CZ    . PHE C 1 286 ? 15.583  41.920  -28.734 1.00 68.65  ?  279 PHE C CZ    1 
ATOM   6615 N  N     . TRP C 1 287 ? 12.800  44.493  -31.843 1.00 61.10  ?  280 TRP C N     1 
ATOM   6616 C  CA    . TRP C 1 287 ? 13.698  45.609  -32.083 1.00 58.07  ?  280 TRP C CA    1 
ATOM   6617 C  C     . TRP C 1 287 ? 14.550  45.853  -30.839 1.00 59.29  ?  280 TRP C C     1 
ATOM   6618 O  O     . TRP C 1 287 ? 14.015  46.178  -29.774 1.00 61.66  ?  280 TRP C O     1 
ATOM   6619 C  CB    . TRP C 1 287 ? 12.881  46.862  -32.431 1.00 56.89  ?  280 TRP C CB    1 
ATOM   6620 C  CG    . TRP C 1 287 ? 13.716  48.085  -32.701 1.00 54.29  ?  280 TRP C CG    1 
ATOM   6621 C  CD1   . TRP C 1 287 ? 14.852  48.181  -33.450 1.00 51.95  ?  280 TRP C CD1   1 
ATOM   6622 C  CD2   . TRP C 1 287 ? 13.446  49.418  -32.230 1.00 54.48  ?  280 TRP C CD2   1 
ATOM   6623 N  NE1   . TRP C 1 287 ? 15.303  49.473  -33.479 1.00 50.65  ?  280 TRP C NE1   1 
ATOM   6624 C  CE2   . TRP C 1 287 ? 14.477  50.251  -32.711 1.00 52.17  ?  280 TRP C CE2   1 
ATOM   6625 C  CE3   . TRP C 1 287 ? 12.446  49.977  -31.429 1.00 56.98  ?  280 TRP C CE3   1 
ATOM   6626 C  CZ2   . TRP C 1 287 ? 14.527  51.616  -32.425 1.00 52.25  ?  280 TRP C CZ2   1 
ATOM   6627 C  CZ3   . TRP C 1 287 ? 12.509  51.322  -31.138 1.00 57.07  ?  280 TRP C CZ3   1 
ATOM   6628 C  CH2   . TRP C 1 287 ? 13.540  52.122  -31.612 1.00 54.74  ?  280 TRP C CH2   1 
ATOM   6629 N  N     . ASP C 1 288 ? 15.874  45.707  -30.987 1.00 58.23  ?  281 ASP C N     1 
ATOM   6630 C  CA    . ASP C 1 288 ? 16.801  45.891  -29.878 1.00 59.81  ?  281 ASP C CA    1 
ATOM   6631 C  C     . ASP C 1 288 ? 17.195  47.366  -29.756 1.00 58.54  ?  281 ASP C C     1 
ATOM   6632 O  O     . ASP C 1 288 ? 18.088  47.882  -30.449 1.00 56.54  ?  281 ASP C O     1 
ATOM   6633 C  CB    . ASP C 1 288 ? 17.976  44.922  -30.027 1.00 60.38  ?  281 ASP C CB    1 
ATOM   6634 C  CG    . ASP C 1 288 ? 18.918  44.894  -28.835 1.00 62.91  ?  281 ASP C CG    1 
ATOM   6635 O  OD1   . ASP C 1 288 ? 18.791  45.755  -27.961 1.00 63.93  ?  281 ASP C OD1   1 
ATOM   6636 O  OD2   . ASP C 1 288 ? 19.759  44.007  -28.812 1.00 64.27  -1 281 ASP C OD2   1 
ATOM   6637 N  N     . GLU C 1 289 ? 16.524  48.059  -28.837 1.00 60.35  ?  282 GLU C N     1 
ATOM   6638 C  CA    . GLU C 1 289 ? 16.684  49.492  -28.680 1.00 59.91  ?  282 GLU C CA    1 
ATOM   6639 C  C     . GLU C 1 289 ? 18.001  49.868  -27.984 1.00 61.24  ?  282 GLU C C     1 
ATOM   6640 O  O     . GLU C 1 289 ? 18.508  50.972  -28.165 1.00 60.59  ?  282 GLU C O     1 
ATOM   6641 C  CB    . GLU C 1 289 ? 15.481  50.045  -27.918 1.00 62.30  ?  282 GLU C CB    1 
ATOM   6642 C  CG    . GLU C 1 289 ? 15.245  51.518  -28.228 1.00 61.43  ?  282 GLU C CG    1 
ATOM   6643 C  CD    . GLU C 1 289 ? 13.958  52.170  -27.735 1.00 63.90  ?  282 GLU C CD    1 
ATOM   6644 O  OE1   . GLU C 1 289 ? 13.805  53.386  -27.998 1.00 63.58  ?  282 GLU C OE1   1 
ATOM   6645 O  OE2   . GLU C 1 289 ? 13.135  51.490  -27.073 1.00 66.66  -1 282 GLU C OE2   1 
ATOM   6646 N  N     . GLU C 1 290 ? 18.550  48.979  -27.144 1.00 63.71  ?  283 GLU C N     1 
ATOM   6647 C  CA    . GLU C 1 290 ? 19.875  49.190  -26.582 1.00 65.38  ?  283 GLU C CA    1 
ATOM   6648 C  C     . GLU C 1 290 ? 20.932  49.113  -27.688 1.00 63.00  ?  283 GLU C C     1 
ATOM   6649 O  O     . GLU C 1 290 ? 21.804  49.979  -27.796 1.00 63.11  ?  283 GLU C O     1 
ATOM   6650 C  CB    . GLU C 1 290 ? 20.208  48.156  -25.500 1.00 68.91  ?  283 GLU C CB    1 
ATOM   6651 C  CG    . GLU C 1 290 ? 19.364  48.295  -24.238 1.00 72.39  ?  283 GLU C CG    1 
ATOM   6652 C  CD    . GLU C 1 290 ? 19.533  47.208  -23.186 1.00 76.23  ?  283 GLU C CD    1 
ATOM   6653 O  OE1   . GLU C 1 290 ? 20.039  46.091  -23.510 1.00 76.02  ?  283 GLU C OE1   1 
ATOM   6654 O  OE2   . GLU C 1 290 ? 19.146  47.469  -22.026 1.00 79.92  -1 283 GLU C OE2   1 
ATOM   6655 N  N     . ALA C 1 291 ? 20.797  48.118  -28.561 1.00 61.28  ?  284 ALA C N     1 
ATOM   6656 C  CA    . ALA C 1 291 ? 21.703  47.985  -29.691 1.00 59.48  ?  284 ALA C CA    1 
ATOM   6657 C  C     . ALA C 1 291 ? 21.613  49.224  -30.587 1.00 56.87  ?  284 ALA C C     1 
ATOM   6658 O  O     . ALA C 1 291 ? 22.606  49.732  -31.096 1.00 56.61  ?  284 ALA C O     1 
ATOM   6659 C  CB    . ALA C 1 291 ? 21.385  46.728  -30.452 1.00 58.67  ?  284 ALA C CB    1 
ATOM   6660 N  N     . PHE C 1 292 ? 20.387  49.720  -30.792 1.00 55.41  ?  285 PHE C N     1 
ATOM   6661 C  CA    . PHE C 1 292 ? 20.188  50.851  -31.679 1.00 53.20  ?  285 PHE C CA    1 
ATOM   6662 C  C     . PHE C 1 292 ? 20.939  52.073  -31.159 1.00 54.59  ?  285 PHE C C     1 
ATOM   6663 O  O     . PHE C 1 292 ? 21.616  52.786  -31.885 1.00 53.75  ?  285 PHE C O     1 
ATOM   6664 C  CB    . PHE C 1 292 ? 18.685  51.114  -31.765 1.00 52.43  ?  285 PHE C CB    1 
ATOM   6665 C  CG    . PHE C 1 292 ? 18.280  52.443  -32.326 1.00 51.15  ?  285 PHE C CG    1 
ATOM   6666 C  CD1   . PHE C 1 292 ? 18.360  52.685  -33.692 1.00 48.66  ?  285 PHE C CD1   1 
ATOM   6667 C  CD2   . PHE C 1 292 ? 17.765  53.435  -31.507 1.00 52.91  ?  285 PHE C CD2   1 
ATOM   6668 C  CE1   . PHE C 1 292 ? 17.966  53.902  -34.218 1.00 47.84  ?  285 PHE C CE1   1 
ATOM   6669 C  CE2   . PHE C 1 292 ? 17.358  54.648  -32.043 1.00 52.19  ?  285 PHE C CE2   1 
ATOM   6670 C  CZ    . PHE C 1 292 ? 17.445  54.872  -33.400 1.00 49.57  ?  285 PHE C CZ    1 
ATOM   6671 N  N     . VAL C 1 293 ? 20.852  52.319  -29.856 1.00 57.39  ?  286 VAL C N     1 
ATOM   6672 C  CA    . VAL C 1 293 ? 21.572  53.421  -29.256 1.00 59.63  ?  286 VAL C CA    1 
ATOM   6673 C  C     . VAL C 1 293 ? 23.088  53.199  -29.312 1.00 60.96  ?  286 VAL C C     1 
ATOM   6674 O  O     . VAL C 1 293 ? 23.845  54.115  -29.653 1.00 61.53  ?  286 VAL C O     1 
ATOM   6675 C  CB    . VAL C 1 293 ? 21.044  53.672  -27.829 1.00 62.98  ?  286 VAL C CB    1 
ATOM   6676 C  CG1   . VAL C 1 293 ? 22.006  54.535  -27.044 1.00 66.41  ?  286 VAL C CG1   1 
ATOM   6677 C  CG2   . VAL C 1 293 ? 19.633  54.263  -27.847 1.00 62.49  ?  286 VAL C CG2   1 
ATOM   6678 N  N     . GLU C 1 294 ? 23.533  51.983  -28.976 1.00 62.01  ?  287 GLU C N     1 
ATOM   6679 C  CA    . GLU C 1 294 ? 24.946  51.655  -28.911 1.00 64.15  ?  287 GLU C CA    1 
ATOM   6680 C  C     . GLU C 1 294 ? 25.637  51.910  -30.251 1.00 62.39  ?  287 GLU C C     1 
ATOM   6681 O  O     . GLU C 1 294 ? 26.766  52.414  -30.275 1.00 64.61  ?  287 GLU C O     1 
ATOM   6682 C  CB    . GLU C 1 294 ? 25.130  50.221  -28.403 1.00 65.66  ?  287 GLU C CB    1 
ATOM   6683 C  CG    . GLU C 1 294 ? 26.590  49.833  -28.281 1.00 68.61  ?  287 GLU C CG    1 
ATOM   6684 C  CD    . GLU C 1 294 ? 26.851  48.748  -27.248 1.00 71.87  ?  287 GLU C CD    1 
ATOM   6685 O  OE1   . GLU C 1 294 ? 26.240  48.851  -26.156 1.00 73.45  ?  287 GLU C OE1   1 
ATOM   6686 O  OE2   . GLU C 1 294 ? 27.691  47.840  -27.495 1.00 73.39  -1 287 GLU C OE2   1 
ATOM   6687 N  N     . ARG C 1 295 ? 24.961  51.602  -31.372 1.00 58.95  ?  288 ARG C N     1 
ATOM   6688 C  CA    . ARG C 1 295 ? 25.621  51.673  -32.665 1.00 57.78  ?  288 ARG C CA    1 
ATOM   6689 C  C     . ARG C 1 295 ? 25.630  53.105  -33.204 1.00 57.00  ?  288 ARG C C     1 
ATOM   6690 O  O     . ARG C 1 295 ? 26.166  53.331  -34.287 1.00 56.40  ?  288 ARG C O     1 
ATOM   6691 C  CB    . ARG C 1 295 ? 24.941  50.734  -33.667 1.00 55.13  ?  288 ARG C CB    1 
ATOM   6692 C  CG    . ARG C 1 295 ? 23.535  51.163  -34.066 1.00 52.26  ?  288 ARG C CG    1 
ATOM   6693 C  CD    . ARG C 1 295 ? 23.084  50.388  -35.289 1.00 50.24  ?  288 ARG C CD    1 
ATOM   6694 N  NE    . ARG C 1 295 ? 21.672  50.583  -35.579 1.00 48.21  ?  288 ARG C NE    1 
ATOM   6695 C  CZ    . ARG C 1 295 ? 21.168  51.609  -36.247 1.00 46.57  ?  288 ARG C CZ    1 
ATOM   6696 N  NH1   . ARG C 1 295 ? 21.925  52.587  -36.703 1.00 46.61  ?  288 ARG C NH1   1 
ATOM   6697 N  NH2   . ARG C 1 295 ? 19.864  51.615  -36.476 1.00 45.36  ?  288 ARG C NH2   1 
ATOM   6698 N  N     . GLY C 1 296 ? 24.992  54.029  -32.483 1.00 57.38  ?  289 GLY C N     1 
ATOM   6699 C  CA    . GLY C 1 296 ? 24.867  55.431  -32.838 1.00 57.23  ?  289 GLY C CA    1 
ATOM   6700 C  C     . GLY C 1 296 ? 23.640  55.751  -33.688 1.00 53.96  ?  289 GLY C C     1 
ATOM   6701 O  O     . GLY C 1 296 ? 23.712  56.660  -34.505 1.00 53.32  ?  289 GLY C O     1 
ATOM   6702 N  N     . GLY C 1 297 ? 22.491  55.139  -33.378 1.00 52.64  ?  290 GLY C N     1 
ATOM   6703 C  CA    . GLY C 1 297 ? 21.252  55.299  -34.136 1.00 50.12  ?  290 GLY C CA    1 
ATOM   6704 C  C     . GLY C 1 297 ? 20.543  56.635  -33.924 1.00 50.74  ?  290 GLY C C     1 
ATOM   6705 O  O     . GLY C 1 297 ? 19.786  57.077  -34.792 1.00 49.06  ?  290 GLY C O     1 
ATOM   6706 N  N     . ILE C 1 298 ? 20.758  57.258  -32.752 1.00 53.67  ?  291 ILE C N     1 
ATOM   6707 C  CA    . ILE C 1 298 ? 20.364  58.640  -32.526 1.00 55.29  ?  291 ILE C CA    1 
ATOM   6708 C  C     . ILE C 1 298 ? 21.589  59.528  -32.729 1.00 57.03  ?  291 ILE C C     1 
ATOM   6709 O  O     . ILE C 1 298 ? 22.614  59.319  -32.093 1.00 59.25  ?  291 ILE C O     1 
ATOM   6710 C  CB    . ILE C 1 298 ? 19.749  58.841  -31.125 1.00 58.33  ?  291 ILE C CB    1 
ATOM   6711 C  CG1   . ILE C 1 298 ? 18.585  57.885  -30.835 1.00 57.46  ?  291 ILE C CG1   1 
ATOM   6712 C  CG2   . ILE C 1 298 ? 19.335  60.290  -30.930 1.00 60.64  ?  291 ILE C CG2   1 
ATOM   6713 C  CD1   . ILE C 1 298 ? 17.316  58.189  -31.600 1.00 55.86  ?  291 ILE C CD1   1 
ATOM   6714 N  N     . TYR C 1 299 ? 21.467  60.546  -33.595 1.00 56.56  ?  292 TYR C N     1 
ATOM   6715 C  CA    . TYR C 1 299 ? 22.586  61.428  -33.897 1.00 58.63  ?  292 TYR C CA    1 
ATOM   6716 C  C     . TYR C 1 299 ? 22.086  62.722  -34.530 1.00 59.05  ?  292 TYR C C     1 
ATOM   6717 O  O     . TYR C 1 299 ? 20.881  62.930  -34.616 1.00 58.00  ?  292 TYR C O     1 
ATOM   6718 C  CB    . TYR C 1 299 ? 23.618  60.755  -34.796 1.00 57.34  ?  292 TYR C CB    1 
ATOM   6719 C  CG    . TYR C 1 299 ? 23.220  60.395  -36.228 1.00 53.87  ?  292 TYR C CG    1 
ATOM   6720 C  CD1   . TYR C 1 299 ? 22.496  59.242  -36.515 1.00 50.99  ?  292 TYR C CD1   1 
ATOM   6721 C  CD2   . TYR C 1 299 ? 23.616  61.189  -37.305 1.00 54.05  ?  292 TYR C CD2   1 
ATOM   6722 C  CE1   . TYR C 1 299 ? 22.177  58.900  -37.825 1.00 48.48  ?  292 TYR C CE1   1 
ATOM   6723 C  CE2   . TYR C 1 299 ? 23.295  60.859  -38.616 1.00 51.43  ?  292 TYR C CE2   1 
ATOM   6724 C  CZ    . TYR C 1 299 ? 22.577  59.707  -38.882 1.00 48.66  ?  292 TYR C CZ    1 
ATOM   6725 O  OH    . TYR C 1 299 ? 22.295  59.382  -40.188 1.00 46.69  ?  292 TYR C OH    1 
ATOM   6726 N  N     . ASP C 1 300 ? 23.029  63.606  -34.893 1.00 61.32  ?  293 ASP C N     1 
ATOM   6727 C  CA    . ASP C 1 300 ? 22.704  64.933  -35.403 1.00 62.72  ?  293 ASP C CA    1 
ATOM   6728 C  C     . ASP C 1 300 ? 22.397  64.793  -36.890 1.00 59.40  ?  293 ASP C C     1 
ATOM   6729 O  O     . ASP C 1 300 ? 23.273  64.786  -37.763 1.00 59.32  ?  293 ASP C O     1 
ATOM   6730 C  CB    . ASP C 1 300 ? 23.801  65.951  -35.078 1.00 67.41  ?  293 ASP C CB    1 
ATOM   6731 C  CG    . ASP C 1 300 ? 23.766  66.489  -33.651 1.00 71.68  ?  293 ASP C CG    1 
ATOM   6732 O  OD1   . ASP C 1 300 ? 22.705  66.350  -32.966 1.00 71.29  ?  293 ASP C OD1   1 
ATOM   6733 O  OD2   . ASP C 1 300 ? 24.804  67.034  -33.219 1.00 75.92  -1 293 ASP C OD2   1 
ATOM   6734 N  N     . TRP C 1 301 ? 21.113  64.597  -37.142 1.00 57.03  ?  294 TRP C N     1 
ATOM   6735 C  CA    . TRP C 1 301 ? 20.671  63.999  -38.380 1.00 53.55  ?  294 TRP C CA    1 
ATOM   6736 C  C     . TRP C 1 301 ? 19.943  65.037  -39.240 1.00 53.81  ?  294 TRP C C     1 
ATOM   6737 O  O     . TRP C 1 301 ? 19.253  64.713  -40.207 1.00 51.47  ?  294 TRP C O     1 
ATOM   6738 C  CB    . TRP C 1 301 ? 19.862  62.751  -38.018 1.00 51.12  ?  294 TRP C CB    1 
ATOM   6739 C  CG    . TRP C 1 301 ? 18.696  62.940  -37.082 1.00 52.13  ?  294 TRP C CG    1 
ATOM   6740 C  CD1   . TRP C 1 301 ? 17.954  64.058  -36.825 1.00 54.35  ?  294 TRP C CD1   1 
ATOM   6741 C  CD2   . TRP C 1 301 ? 18.115  61.882  -36.285 1.00 51.46  ?  294 TRP C CD2   1 
ATOM   6742 N  NE1   . TRP C 1 301 ? 16.922  63.756  -35.971 1.00 55.11  ?  294 TRP C NE1   1 
ATOM   6743 C  CE2   . TRP C 1 301 ? 17.010  62.433  -35.601 1.00 53.41  ?  294 TRP C CE2   1 
ATOM   6744 C  CE3   . TRP C 1 301 ? 18.433  60.531  -36.095 1.00 49.91  ?  294 TRP C CE3   1 
ATOM   6745 C  CZ2   . TRP C 1 301 ? 16.214  61.669  -34.743 1.00 53.87  ?  294 TRP C CZ2   1 
ATOM   6746 C  CZ3   . TRP C 1 301 ? 17.656  59.782  -35.240 1.00 50.23  ?  294 TRP C CZ3   1 
ATOM   6747 C  CH2   . TRP C 1 301 ? 16.543  60.339  -34.594 1.00 52.16  ?  294 TRP C CH2   1 
ATOM   6748 N  N     . ASN C 1 302 ? 20.139  66.318  -38.919 1.00 57.20  ?  295 ASN C N     1 
ATOM   6749 C  CA    . ASN C 1 302 ? 19.825  67.378  -39.862 1.00 58.18  ?  295 ASN C CA    1 
ATOM   6750 C  C     . ASN C 1 302 ? 20.799  68.519  -39.610 1.00 62.39  ?  295 ASN C C     1 
ATOM   6751 O  O     . ASN C 1 302 ? 21.590  68.464  -38.675 1.00 64.51  ?  295 ASN C O     1 
ATOM   6752 C  CB    . ASN C 1 302 ? 18.343  67.781  -39.829 1.00 58.23  ?  295 ASN C CB    1 
ATOM   6753 C  CG    . ASN C 1 302 ? 17.835  68.172  -38.455 1.00 61.06  ?  295 ASN C CG    1 
ATOM   6754 O  OD1   . ASN C 1 302 ? 18.437  69.007  -37.779 1.00 64.72  ?  295 ASN C OD1   1 
ATOM   6755 N  ND2   . ASN C 1 302 ? 16.718  67.582  -38.047 1.00 59.96  ?  295 ASN C ND2   1 
ATOM   6756 N  N     . LYS C 1 303 ? 20.770  69.545  -40.460 1.00 64.08  ?  296 LYS C N     1 
ATOM   6757 C  CA    . LYS C 1 303 ? 21.713  70.641  -40.295 1.00 68.68  ?  296 LYS C CA    1 
ATOM   6758 C  C     . LYS C 1 303 ? 21.373  71.474  -39.053 1.00 72.68  ?  296 LYS C C     1 
ATOM   6759 O  O     . LYS C 1 303 ? 22.258  72.113  -38.478 1.00 76.94  ?  296 LYS C O     1 
ATOM   6760 C  CB    . LYS C 1 303 ? 21.758  71.498  -41.561 1.00 69.85  ?  296 LYS C CB    1 
ATOM   6761 C  CG    . LYS C 1 303 ? 20.498  72.296  -41.867 1.00 70.49  ?  296 LYS C CG    1 
ATOM   6762 C  CD    . LYS C 1 303 ? 20.668  73.269  -43.014 1.00 72.71  ?  296 LYS C CD    1 
ATOM   6763 C  CE    . LYS C 1 303 ? 22.007  73.980  -43.002 1.00 77.00  ?  296 LYS C CE    1 
ATOM   6764 N  NZ    . LYS C 1 303 ? 22.028  75.140  -43.923 1.00 80.39  ?  296 LYS C NZ    1 
ATOM   6765 N  N     . SER C 1 304 ? 20.095  71.464  -38.640 1.00 71.92  ?  297 SER C N     1 
ATOM   6766 C  CA    . SER C 1 304 ? 19.664  72.134  -37.422 1.00 75.97  ?  297 SER C CA    1 
ATOM   6767 C  C     . SER C 1 304 ? 20.211  71.388  -36.197 1.00 76.36  ?  297 SER C C     1 
ATOM   6768 O  O     . SER C 1 304 ? 20.078  71.953  -35.092 1.00 80.59  ?  297 SER C O     1 
ATOM   6769 C  CB    . SER C 1 304 ? 18.155  72.249  -37.356 1.00 75.54  ?  297 SER C CB    1 
ATOM   6770 O  OG    . SER C 1 304 ? 17.653  73.057  -38.412 1.00 76.14  ?  297 SER C OG    1 
HETATM 6771 N  N1    . CTP D 2 .   ? 11.897  17.511  10.651  1.00 27.17  ?  401 CTP A N1    1 
HETATM 6772 C  C2    . CTP D 2 .   ? 10.987  17.833  11.652  1.00 27.66  ?  401 CTP A C2    1 
HETATM 6773 N  N3    . CTP D 2 .   ? 9.725   18.143  11.329  1.00 28.80  ?  401 CTP A N3    1 
HETATM 6774 C  C4    . CTP D 2 .   ? 9.372   18.177  10.030  1.00 29.37  ?  401 CTP A C4    1 
HETATM 6775 C  C5    . CTP D 2 .   ? 10.296  17.948  8.997   1.00 28.91  ?  401 CTP A C5    1 
HETATM 6776 C  C6    . CTP D 2 .   ? 11.534  17.594  9.341   1.00 27.85  ?  401 CTP A C6    1 
HETATM 6777 O  O2    . CTP D 2 .   ? 11.353  17.729  12.823  1.00 27.27  ?  401 CTP A O2    1 
HETATM 6778 N  N4    . CTP D 2 .   ? 8.135   18.515  9.750   1.00 30.77  ?  401 CTP A N4    1 
HETATM 6779 C  "C1'" . CTP D 2 .   ? 13.275  17.181  11.050  1.00 26.35  ?  401 CTP A "C1'" 1 
HETATM 6780 C  "C2'" . CTP D 2 .   ? 13.759  15.821  10.545  1.00 25.62  ?  401 CTP A "C2'" 1 
HETATM 6781 O  "O2'" . CTP D 2 .   ? 13.316  14.726  11.322  1.00 25.05  ?  401 CTP A "O2'" 1 
HETATM 6782 C  "C3'" . CTP D 2 .   ? 15.276  16.035  10.578  1.00 25.59  ?  401 CTP A "C3'" 1 
HETATM 6783 C  "C4'" . CTP D 2 .   ? 15.444  17.539  10.286  1.00 26.63  ?  401 CTP A "C4'" 1 
HETATM 6784 O  "O4'" . CTP D 2 .   ? 14.123  18.111  10.431  1.00 27.06  ?  401 CTP A "O4'" 1 
HETATM 6785 O  "O3'" . CTP D 2 .   ? 15.892  15.726  11.822  1.00 25.07  ?  401 CTP A "O3'" 1 
HETATM 6786 C  "C5'" . CTP D 2 .   ? 16.000  17.853  8.919   1.00 27.59  ?  401 CTP A "C5'" 1 
HETATM 6787 O  "O5'" . CTP D 2 .   ? 17.347  17.419  8.902   1.00 27.63  ?  401 CTP A "O5'" 1 
HETATM 6788 P  PA    . CTP D 2 .   ? 17.989  16.767  7.597   1.00 28.37  ?  401 CTP A PA    1 
HETATM 6789 O  O1A   . CTP D 2 .   ? 17.264  17.290  6.413   1.00 29.36  ?  401 CTP A O1A   1 
HETATM 6790 O  O2A   . CTP D 2 .   ? 19.452  16.688  7.767   1.00 29.02  ?  401 CTP A O2A   1 
HETATM 6791 O  O3A   . CTP D 2 .   ? 17.558  15.222  7.753   1.00 27.31  ?  401 CTP A O3A   1 
HETATM 6792 P  PB    . CTP D 2 .   ? 17.937  13.924  6.881   1.00 27.81  ?  401 CTP A PB    1 
HETATM 6793 O  O1B   . CTP D 2 .   ? 16.757  12.987  6.988   1.00 27.14  ?  401 CTP A O1B   1 
HETATM 6794 O  O2B   . CTP D 2 .   ? 19.293  13.444  7.260   1.00 28.17  ?  401 CTP A O2B   1 
HETATM 6795 O  O3B   . CTP D 2 .   ? 17.939  14.569  5.423   1.00 29.33  ?  401 CTP A O3B   1 
HETATM 6796 P  PG    . CTP D 2 .   ? 18.454  13.881  4.047   1.00 30.98  ?  401 CTP A PG    1 
HETATM 6797 O  O1G   . CTP D 2 .   ? 17.521  14.453  3.041   1.00 31.81  ?  401 CTP A O1G   1 
HETATM 6798 O  O2G   . CTP D 2 .   ? 19.878  14.398  3.867   1.00 32.33  ?  401 CTP A O2G   1 
HETATM 6799 O  O3G   . CTP D 2 .   ? 18.410  12.390  4.139   1.00 30.75  ?  401 CTP A O3G   1 
HETATM 6800 FE FE1   . SF4 E 3 .   ? 18.927  24.516  18.247  1.00 36.00  ?  402 SF4 A FE1   1 
HETATM 6801 FE FE2   . SF4 E 3 .   ? 18.972  22.620  20.147  1.00 33.92  ?  402 SF4 A FE2   1 
HETATM 6802 FE FE3   . SF4 E 3 .   ? 19.161  21.868  17.534  1.00 31.67  ?  402 SF4 A FE3   1 
HETATM 6803 FE FE4   . SF4 E 3 .   ? 16.767  22.922  18.596  1.00 33.13  ?  402 SF4 A FE4   1 
HETATM 6804 S  S1    . SF4 E 3 .   ? 17.677  20.915  19.194  1.00 30.74  ?  402 SF4 A S1    1 
HETATM 6805 S  S2    . SF4 E 3 .   ? 17.788  23.383  16.657  1.00 33.24  ?  402 SF4 A S2    1 
HETATM 6806 S  S3    . SF4 E 3 .   ? 17.571  24.415  20.139  1.00 36.53  ?  402 SF4 A S3    1 
HETATM 6807 S  S4    . SF4 E 3 .   ? 20.610  23.216  18.758  1.00 34.80  ?  402 SF4 A S4    1 
HETATM 6808 N  N     . SAM F 4 .   ? 20.262  19.823  17.705  1.00 29.71  ?  403 SAM A N     1 
HETATM 6809 C  CA    . SAM F 4 .   ? 20.749  19.270  16.425  1.00 29.13  ?  403 SAM A CA    1 
HETATM 6810 C  C     . SAM F 4 .   ? 20.944  20.418  15.431  1.00 30.41  ?  403 SAM A C     1 
HETATM 6811 O  O     . SAM F 4 .   ? 21.491  20.133  14.369  1.00 30.51  ?  403 SAM A O     1 
HETATM 6812 O  OXT   . SAM F 4 .   ? 20.449  21.525  15.737  1.00 31.48  ?  403 SAM A OXT   1 
HETATM 6813 C  CB    . SAM F 4 .   ? 19.795  18.224  15.831  1.00 27.54  ?  403 SAM A CB    1 
HETATM 6814 C  CG    . SAM F 4 .   ? 18.323  18.486  15.937  1.00 27.18  ?  403 SAM A CG    1 
HETATM 6815 S  SD    . SAM F 4 .   ? 17.614  19.940  15.089  1.00 28.33  ?  403 SAM A SD    1 
HETATM 6816 C  CE    . SAM F 4 .   ? 15.967  19.916  15.767  1.00 28.21  ?  403 SAM A CE    1 
HETATM 6817 C  "C5'" . SAM F 4 .   ? 17.378  19.128  13.444  1.00 27.45  ?  403 SAM A "C5'" 1 
HETATM 6818 C  "C4'" . SAM F 4 .   ? 17.518  20.092  12.278  1.00 28.67  ?  403 SAM A "C4'" 1 
HETATM 6819 O  "O4'" . SAM F 4 .   ? 16.306  20.871  12.173  1.00 29.33  ?  403 SAM A "O4'" 1 
HETATM 6820 C  "C3'" . SAM F 4 .   ? 18.660  21.110  12.415  1.00 30.25  ?  403 SAM A "C3'" 1 
HETATM 6821 O  "O3'" . SAM F 4 .   ? 19.389  21.255  11.200  1.00 31.18  ?  403 SAM A "O3'" 1 
HETATM 6822 C  "C2'" . SAM F 4 .   ? 17.913  22.377  12.853  1.00 31.56  ?  403 SAM A "C2'" 1 
HETATM 6823 O  "O2'" . SAM F 4 .   ? 18.622  23.569  12.546  1.00 33.69  ?  403 SAM A "O2'" 1 
HETATM 6824 C  "C1'" . SAM F 4 .   ? 16.630  22.230  12.038  1.00 31.18  ?  403 SAM A "C1'" 1 
HETATM 6825 N  N9    . SAM F 4 .   ? 15.498  23.035  12.484  1.00 32.16  ?  403 SAM A N9    1 
HETATM 6826 C  C8    . SAM F 4 .   ? 15.200  23.351  13.790  1.00 32.57  ?  403 SAM A C8    1 
HETATM 6827 N  N7    . SAM F 4 .   ? 14.143  24.099  13.913  1.00 33.92  ?  403 SAM A N7    1 
HETATM 6828 C  C5    . SAM F 4 .   ? 13.723  24.308  12.613  1.00 34.38  ?  403 SAM A C5    1 
HETATM 6829 C  C6    . SAM F 4 .   ? 12.623  25.002  12.099  1.00 35.95  ?  403 SAM A C6    1 
HETATM 6830 N  N6    . SAM F 4 .   ? 11.739  25.619  12.860  1.00 37.44  ?  403 SAM A N6    1 
HETATM 6831 N  N1    . SAM F 4 .   ? 12.435  24.977  10.756  1.00 36.21  ?  403 SAM A N1    1 
HETATM 6832 C  C2    . SAM F 4 .   ? 13.330  24.318  10.015  1.00 35.03  ?  403 SAM A C2    1 
HETATM 6833 N  N3    . SAM F 4 .   ? 14.403  23.606  10.384  1.00 33.58  ?  403 SAM A N3    1 
HETATM 6834 C  C4    . SAM F 4 .   ? 14.556  23.666  11.720  1.00 33.31  ?  403 SAM A C4    1 
HETATM 6835 FE FE1   . SF4 G 3 .   ? 17.178  13.107  -19.344 1.00 34.43  ?  401 SF4 B FE1   1 
HETATM 6836 FE FE2   . SF4 G 3 .   ? 17.705  11.571  -21.531 1.00 36.46  ?  401 SF4 B FE2   1 
HETATM 6837 FE FE3   . SF4 G 3 .   ? 17.394  14.280  -21.840 1.00 34.39  ?  401 SF4 B FE3   1 
HETATM 6838 FE FE4   . SF4 G 3 .   ? 15.150  12.621  -21.056 1.00 32.17  ?  401 SF4 B FE4   1 
HETATM 6839 S  S1    . SF4 G 3 .   ? 16.360  12.659  -23.039 1.00 34.15  ?  401 SF4 B S1    1 
HETATM 6840 S  S2    . SF4 G 3 .   ? 15.799  14.752  -20.246 1.00 31.73  ?  401 SF4 B S2    1 
HETATM 6841 S  S3    . SF4 G 3 .   ? 16.329  11.087  -19.886 1.00 34.78  ?  401 SF4 B S3    1 
HETATM 6842 S  S4    . SF4 G 3 .   ? 19.066  13.165  -20.649 1.00 37.40  ?  401 SF4 B S4    1 
HETATM 6843 N  N     . SAM H 4 .   ? 13.288  12.898  -19.654 1.00 29.98  ?  402 SAM B N     1 
HETATM 6844 C  CA    . SAM H 4 .   ? 12.045  12.426  -20.325 1.00 29.26  ?  402 SAM B CA    1 
HETATM 6845 C  C     . SAM H 4 .   ? 12.352  11.358  -21.384 1.00 30.44  ?  402 SAM B C     1 
HETATM 6846 O  O     . SAM H 4 .   ? 13.571  11.238  -21.764 1.00 31.67  ?  402 SAM B O     1 
HETATM 6847 O  OXT   . SAM H 4 .   ? 11.380  10.704  -21.791 1.00 30.38  ?  402 SAM B OXT   1 
HETATM 6848 C  CB    . SAM H 4 .   ? 11.293  13.593  -20.978 1.00 27.98  ?  402 SAM B CB    1 
HETATM 6849 C  CG    . SAM H 4 .   ? 12.142  14.658  -21.583 1.00 28.14  ?  402 SAM B CG    1 
HETATM 6850 S  SD    . SAM H 4 .   ? 12.871  14.172  -23.177 1.00 29.39  ?  402 SAM B SD    1 
HETATM 6851 C  CE    . SAM H 4 .   ? 13.785  15.655  -23.588 1.00 29.89  ?  402 SAM B CE    1 
HETATM 6852 C  "C5'" . SAM H 4 .   ? 11.405  14.270  -24.330 1.00 28.61  ?  402 SAM B "C5'" 1 
HETATM 6853 C  "C4'" . SAM H 4 .   ? 11.508  13.311  -25.522 1.00 29.80  ?  402 SAM B "C4'" 1 
HETATM 6854 O  "O4'" . SAM H 4 .   ? 12.492  13.808  -26.469 1.00 30.93  ?  402 SAM B "O4'" 1 
HETATM 6855 C  "C3'" . SAM H 4 .   ? 11.961  11.897  -25.147 1.00 30.90  ?  402 SAM B "C3'" 1 
HETATM 6856 O  "O3'" . SAM H 4 .   ? 11.176  10.892  -25.780 1.00 31.51  ?  402 SAM B "O3'" 1 
HETATM 6857 C  "C2'" . SAM H 4 .   ? 13.434  11.878  -25.583 1.00 32.46  ?  402 SAM B "C2'" 1 
HETATM 6858 O  "O2'" . SAM H 4 .   ? 13.940  10.582  -25.834 1.00 34.20  ?  402 SAM B "O2'" 1 
HETATM 6859 C  "C1'" . SAM H 4 .   ? 13.343  12.741  -26.837 1.00 32.60  ?  402 SAM B "C1'" 1 
HETATM 6860 N  N9    . SAM H 4 .   ? 14.601  13.280  -27.317 1.00 34.01  ?  402 SAM B N9    1 
HETATM 6861 C  C8    . SAM H 4 .   ? 15.646  13.704  -26.532 1.00 34.49  ?  402 SAM B C8    1 
HETATM 6862 N  N7    . SAM H 4 .   ? 16.632  14.225  -27.227 1.00 36.16  ?  402 SAM B N7    1 
HETATM 6863 C  C5    . SAM H 4 .   ? 16.244  14.062  -28.544 1.00 36.84  ?  402 SAM B C5    1 
HETATM 6864 C  C6    . SAM H 4 .   ? 16.889  14.359  -29.757 1.00 38.91  ?  402 SAM B C6    1 
HETATM 6865 N  N6    . SAM H 4 .   ? 18.067  14.966  -29.817 1.00 40.67  ?  402 SAM B N6    1 
HETATM 6866 N  N1    . SAM H 4 .   ? 16.190  14.166  -30.903 1.00 39.28  ?  402 SAM B N1    1 
HETATM 6867 C  C2    . SAM H 4 .   ? 14.975  13.616  -30.823 1.00 37.78  ?  402 SAM B C2    1 
HETATM 6868 N  N3    . SAM H 4 .   ? 14.276  13.289  -29.744 1.00 35.89  ?  402 SAM B N3    1 
HETATM 6869 C  C4    . SAM H 4 .   ? 14.975  13.517  -28.616 1.00 35.47  ?  402 SAM B C4    1 
HETATM 6870 N  N1    . CTP I 2 .   ? 10.600  18.683  -28.840 1.00 30.60  ?  403 CTP B N1    1 
HETATM 6871 C  C2    . CTP I 2 .   ? 11.702  19.516  -28.617 1.00 31.43  ?  403 CTP B C2    1 
HETATM 6872 N  N3    . CTP I 2 .   ? 12.245  20.190  -29.670 1.00 33.23  ?  403 CTP B N3    1 
HETATM 6873 C  C4    . CTP I 2 .   ? 11.711  20.075  -30.898 1.00 34.12  ?  403 CTP B C4    1 
HETATM 6874 C  C5    . CTP I 2 .   ? 10.595  19.224  -31.137 1.00 33.25  ?  403 CTP B C5    1 
HETATM 6875 C  C6    . CTP I 2 .   ? 10.088  18.557  -30.102 1.00 31.55  ?  403 CTP B C6    1 
HETATM 6876 O  O2    . CTP I 2 .   ? 12.182  19.602  -27.469 1.00 30.82  ?  403 CTP B O2    1 
HETATM 6877 N  N4    . CTP I 2 .   ? 12.250  20.753  -31.896 1.00 36.20  ?  403 CTP B N4    1 
HETATM 6878 C  "C1'" . CTP I 2 .   ? 10.002  17.870  -27.753 1.00 29.14  ?  403 CTP B "C1'" 1 
HETATM 6879 C  "C2'" . CTP I 2 .   ? 8.499   18.072  -27.519 1.00 28.20  ?  403 CTP B "C2'" 1 
HETATM 6880 O  "O2'" . CTP I 2 .   ? 8.334   19.303  -26.829 1.00 27.76  ?  403 CTP B "O2'" 1 
HETATM 6881 C  "C3'" . CTP I 2 .   ? 8.158   16.795  -26.750 1.00 27.55  ?  403 CTP B "C3'" 1 
HETATM 6882 C  "C4'" . CTP I 2 .   ? 9.122   15.763  -27.379 1.00 28.60  ?  403 CTP B "C4'" 1 
HETATM 6883 O  "O4'" . CTP I 2 .   ? 10.109  16.514  -28.119 1.00 29.59  ?  403 CTP B "O4'" 1 
HETATM 6884 O  "O3'" . CTP I 2 .   ? 8.392   16.835  -25.351 1.00 26.73  ?  403 CTP B "O3'" 1 
HETATM 6885 C  "C5'" . CTP I 2 .   ? 8.421   14.803  -28.267 1.00 29.34  ?  403 CTP B "C5'" 1 
HETATM 6886 O  "O5'" . CTP I 2 .   ? 7.672   13.958  -27.392 1.00 28.78  ?  403 CTP B "O5'" 1 
HETATM 6887 P  PA    . CTP I 2 .   ? 6.230   13.392  -27.778 1.00 29.16  ?  403 CTP B PA    1 
HETATM 6888 O  O1A   . CTP I 2 .   ? 6.153   13.147  -29.238 1.00 30.53  ?  403 CTP B O1A   1 
HETATM 6889 O  O2A   . CTP I 2 .   ? 5.832   12.468  -26.684 1.00 28.99  ?  403 CTP B O2A   1 
HETATM 6890 O  O3A   . CTP I 2 .   ? 5.345   14.733  -27.546 1.00 28.29  ?  403 CTP B O3A   1 
HETATM 6891 P  PB    . CTP I 2 .   ? 3.741   14.815  -27.565 1.00 28.52  ?  403 CTP B PB    1 
HETATM 6892 O  O1B   . CTP I 2 .   ? 3.431   16.281  -27.785 1.00 28.28  ?  403 CTP B O1B   1 
HETATM 6893 O  O2B   . CTP I 2 .   ? 3.147   14.077  -26.476 1.00 28.34  ?  403 CTP B O2B   1 
HETATM 6894 O  O3B   . CTP I 2 .   ? 3.391   13.979  -28.867 1.00 30.05  ?  403 CTP B O3B   1 
HETATM 6895 P  PG    . CTP I 2 .   ? 1.954   13.587  -29.530 1.00 31.43  ?  403 CTP B PG    1 
HETATM 6896 O  O1G   . CTP I 2 .   ? 1.737   12.280  -29.041 1.00 32.00  ?  403 CTP B O1G   1 
HETATM 6897 O  O2G   . CTP I 2 .   ? 0.908   14.555  -29.023 1.00 31.05  ?  403 CTP B O2G   1 
HETATM 6898 O  O3G   . CTP I 2 .   ? 2.166   13.610  -31.039 1.00 32.83  ?  403 CTP B O3G   1 
HETATM 6899 N  N     . SAM J 4 .   ? 20.509  49.814  -53.228 1.00 52.07  ?  401 SAM C N     1 
HETATM 6900 C  CA    . SAM J 4 .   ? 20.925  50.859  -52.255 1.00 49.65  ?  401 SAM C CA    1 
HETATM 6901 C  C     . SAM J 4 .   ? 22.405  50.686  -51.880 1.00 51.25  ?  401 SAM C C     1 
HETATM 6902 O  O     . SAM J 4 .   ? 22.884  49.577  -52.004 1.00 53.53  ?  401 SAM C O     1 
HETATM 6903 O  OXT   . SAM J 4 .   ? 23.000  51.651  -51.439 1.00 50.57  ?  401 SAM C OXT   1 
HETATM 6904 C  CB    . SAM J 4 .   ? 20.063  50.782  -50.988 1.00 47.04  ?  401 SAM C CB    1 
HETATM 6905 C  CG    . SAM J 4 .   ? 19.526  49.421  -50.649 1.00 47.77  ?  401 SAM C CG    1 
HETATM 6906 S  SD    . SAM J 4 .   ? 20.769  48.456  -49.793 1.00 49.17  ?  401 SAM C SD    1 
HETATM 6907 C  CE    . SAM J 4 .   ? 19.985  46.862  -49.566 1.00 50.70  ?  401 SAM C CE    1 
HETATM 6908 C  "C5'" . SAM J 4 .   ? 20.760  49.185  -48.106 1.00 46.38  ?  401 SAM C "C5'" 1 
HETATM 6909 C  "C4'" . SAM J 4 .   ? 22.164  49.189  -47.488 1.00 47.49  ?  401 SAM C "C4'" 1 
HETATM 6910 O  "O4'" . SAM J 4 .   ? 22.461  47.870  -46.971 1.00 49.18  ?  401 SAM C "O4'" 1 
HETATM 6911 C  "C3'" . SAM J 4 .   ? 23.330  49.527  -48.448 1.00 49.70  ?  401 SAM C "C3'" 1 
HETATM 6912 O  "O3'" . SAM J 4 .   ? 24.331  50.398  -47.971 1.00 50.07  ?  401 SAM C "O3'" 1 
HETATM 6913 C  "C2'" . SAM J 4 .   ? 24.082  48.214  -48.644 1.00 52.87  ?  401 SAM C "C2'" 1 
HETATM 6914 O  "O2'" . SAM J 4 .   ? 25.440  48.475  -48.963 1.00 55.54  ?  401 SAM C "O2'" 1 
HETATM 6915 C  "C1'" . SAM J 4 .   ? 23.801  47.555  -47.296 1.00 51.96  ?  401 SAM C "C1'" 1 
HETATM 6916 N  N9    . SAM J 4 .   ? 23.946  46.114  -47.366 1.00 54.58  ?  401 SAM C N9    1 
HETATM 6917 C  C8    . SAM J 4 .   ? 23.576  45.312  -48.417 1.00 56.57  ?  401 SAM C C8    1 
HETATM 6918 N  N7    . SAM J 4 .   ? 23.856  44.048  -48.232 1.00 59.39  ?  401 SAM C N7    1 
HETATM 6919 C  C5    . SAM J 4 .   ? 24.447  44.017  -46.978 1.00 59.08  ?  401 SAM C C5    1 
HETATM 6920 C  C6    . SAM J 4 .   ? 24.964  42.956  -46.220 1.00 61.58  ?  401 SAM C C6    1 
HETATM 6921 N  N6    . SAM J 4 .   ? 24.946  41.700  -46.649 1.00 64.96  ?  401 SAM C N6    1 
HETATM 6922 N  N1    . SAM J 4 .   ? 25.478  43.249  -45.000 1.00 60.89  ?  401 SAM C N1    1 
HETATM 6923 C  C2    . SAM J 4 .   ? 25.493  44.532  -44.609 1.00 58.07  ?  401 SAM C C2    1 
HETATM 6924 N  N3    . SAM J 4 .   ? 25.039  45.614  -45.240 1.00 55.65  ?  401 SAM C N3    1 
HETATM 6925 C  C4    . SAM J 4 .   ? 24.515  45.284  -46.432 1.00 56.19  ?  401 SAM C C4    1 
HETATM 6926 N  N1    . CTP K 2 .   ? 19.068  46.492  -42.416 1.00 46.18  ?  402 CTP C N1    1 
HETATM 6927 C  C2    . CTP K 2 .   ? 18.449  45.303  -42.831 1.00 47.92  ?  402 CTP C C2    1 
HETATM 6928 N  N3    . CTP K 2 .   ? 18.419  44.260  -41.968 1.00 49.74  ?  402 CTP C N3    1 
HETATM 6929 C  C4    . CTP K 2 .   ? 18.955  44.358  -40.742 1.00 49.80  ?  402 CTP C C4    1 
HETATM 6930 C  C5    . CTP K 2 .   ? 19.585  45.552  -40.303 1.00 48.14  ?  402 CTP C C5    1 
HETATM 6931 C  C6    . CTP K 2 .   ? 19.617  46.582  -41.162 1.00 46.41  ?  402 CTP C C6    1 
HETATM 6932 O  O2    . CTP K 2 .   ? 17.933  45.222  -43.957 1.00 48.19  ?  402 CTP C O2    1 
HETATM 6933 N  N4    . CTP K 2 .   ? 18.901  43.292  -39.959 1.00 51.97  ?  402 CTP C N4    1 
HETATM 6934 C  "C1'" . CTP K 2 .   ? 19.164  47.660  -43.326 1.00 44.64  ?  402 CTP C "C1'" 1 
HETATM 6935 C  "C2'" . CTP K 2 .   ? 18.439  48.912  -42.837 1.00 42.79  ?  402 CTP C "C2'" 1 
HETATM 6936 O  "O2'" . CTP K 2 .   ? 17.048  48.818  -43.097 1.00 42.64  ?  402 CTP C "O2'" 1 
HETATM 6937 C  "C3'" . CTP K 2 .   ? 19.193  50.009  -43.604 1.00 42.05  ?  402 CTP C "C3'" 1 
HETATM 6938 C  "C4'" . CTP K 2 .   ? 20.596  49.396  -43.816 1.00 43.68  ?  402 CTP C "C4'" 1 
HETATM 6939 O  "O4'" . CTP K 2 .   ? 20.522  48.030  -43.343 1.00 45.08  ?  402 CTP C "O4'" 1 
HETATM 6940 O  "O3'" . CTP K 2 .   ? 18.624  50.277  -44.893 1.00 41.75  ?  402 CTP C "O3'" 1 
HETATM 6941 C  "C5'" . CTP K 2 .   ? 21.738  50.109  -43.163 1.00 44.10  ?  402 CTP C "C5'" 1 
HETATM 6942 O  "O5'" . CTP K 2 .   ? 21.817  51.382  -43.781 1.00 43.31  ?  402 CTP C "O5'" 1 
HETATM 6943 P  PA    . CTP K 2 .   ? 22.133  52.713  -43.011 1.00 43.03  ?  402 CTP C PA    1 
HETATM 6944 O  O1A   . CTP K 2 .   ? 23.095  52.388  -41.948 1.00 44.61  -1 402 CTP C O1A   1 
HETATM 6945 O  O2A   . CTP K 2 .   ? 22.303  53.784  -44.029 1.00 42.95  ?  402 CTP C O2A   1 
HETATM 6946 O  O3A   . CTP K 2 .   ? 20.707  52.990  -42.273 1.00 41.49  ?  402 CTP C O3A   1 
HETATM 6947 P  PB    . CTP K 2 .   ? 20.214  54.347  -41.583 1.00 41.10  ?  402 CTP C PB    1 
HETATM 6948 O  O1B   . CTP K 2 .   ? 18.992  53.895  -40.788 1.00 40.72  -1 402 CTP C O1B   1 
HETATM 6949 O  O2B   . CTP K 2 .   ? 20.123  55.480  -42.543 1.00 40.75  ?  402 CTP C O2B   1 
HETATM 6950 O  O3B   . CTP K 2 .   ? 21.451  54.613  -40.646 1.00 42.74  ?  402 CTP C O3B   1 
HETATM 6951 P  PG    . CTP K 2 .   ? 21.809  55.818  -39.636 1.00 44.10  ?  402 CTP C PG    1 
HETATM 6952 O  O1G   . CTP K 2 .   ? 22.764  56.655  -40.369 1.00 45.15  ?  402 CTP C O1G   1 
HETATM 6953 O  O2G   . CTP K 2 .   ? 20.568  56.497  -39.249 1.00 43.46  -1 402 CTP C O2G   1 
HETATM 6954 O  O3G   . CTP K 2 .   ? 22.439  55.092  -38.482 1.00 45.62  ?  402 CTP C O3G   1 
HETATM 6955 FE FE1   . SF4 L 3 .   ? 22.324  48.099  -53.071 1.00 56.66  ?  403 SF4 C FE1   1 
HETATM 6956 FE FE2   . SF4 L 3 .   ? 24.176  46.377  -54.220 1.00 65.19  ?  403 SF4 C FE2   1 
HETATM 6957 FE FE3   . SF4 L 3 .   ? 21.731  46.830  -55.329 1.00 62.70  ?  403 SF4 C FE3   1 
HETATM 6958 FE FE4   . SF4 L 3 .   ? 22.023  45.260  -53.255 1.00 61.99  ?  403 SF4 C FE4   1 
HETATM 6959 S  S1    . SF4 L 3 .   ? 22.717  44.823  -55.072 1.00 67.88  ?  403 SF4 C S1    1 
HETATM 6960 S  S2    . SF4 L 3 .   ? 20.734  47.109  -53.234 1.00 56.64  ?  403 SF4 C S2    1 
HETATM 6961 S  S3    . SF4 L 3 .   ? 23.614  46.434  -52.023 1.00 59.80  ?  403 SF4 C S3    1 
HETATM 6962 S  S4    . SF4 L 3 .   ? 23.405  48.259  -55.227 1.00 62.49  ?  403 SF4 C S4    1 
HETATM 6963 O  O     . HOH M 5 .   ? 33.939  34.321  17.184  1.00 31.57  ?  501 HOH A O     1 
HETATM 6964 O  O     . HOH M 5 .   ? 19.866  15.348  23.644  1.00 31.57  ?  502 HOH A O     1 
HETATM 6965 O  O     . HOH M 5 .   ? 5.933   32.739  5.023   1.00 31.57  ?  503 HOH A O     1 
HETATM 6966 O  O     . HOH M 5 .   ? 3.329   3.515   22.558  1.00 31.57  ?  504 HOH A O     1 
HETATM 6967 O  O     . HOH M 5 .   ? 4.658   33.816  1.367   1.00 31.57  ?  505 HOH A O     1 
HETATM 6968 O  O     . HOH M 5 .   ? -0.060  30.953  17.614  1.00 31.57  ?  506 HOH A O     1 
HETATM 6969 O  O     . HOH M 5 .   ? 6.215   35.758  -1.075  1.00 31.57  ?  507 HOH A O     1 
HETATM 6970 O  O     . HOH M 5 .   ? 26.813  25.151  14.453  1.00 31.57  ?  508 HOH A O     1 
HETATM 6971 O  O     . HOH M 5 .   ? 14.093  13.107  25.739  1.00 31.57  ?  509 HOH A O     1 
HETATM 6972 O  O     . HOH M 5 .   ? 10.529  -7.555  11.402  1.00 31.57  ?  510 HOH A O     1 
HETATM 6973 O  O     . HOH M 5 .   ? 3.054   20.312  1.460   1.00 31.57  ?  511 HOH A O     1 
HETATM 6974 O  O     . HOH M 5 .   ? 19.332  13.903  20.448  1.00 31.57  ?  512 HOH A O     1 
HETATM 6975 O  O     . HOH M 5 .   ? 22.856  29.310  13.691  1.00 31.57  ?  513 HOH A O     1 
HETATM 6976 O  O     . HOH M 5 .   ? 10.503  24.662  5.257   1.00 31.57  ?  514 HOH A O     1 
HETATM 6977 O  O     . HOH M 5 .   ? 33.858  31.119  14.710  1.00 31.57  ?  515 HOH A O     1 
HETATM 6978 O  O     . HOH M 5 .   ? 7.378   13.288  23.995  1.00 31.57  ?  516 HOH A O     1 
HETATM 6979 O  O     . HOH M 5 .   ? 6.755   16.059  23.883  1.00 31.57  ?  517 HOH A O     1 
HETATM 6980 O  O     . HOH M 5 .   ? 13.807  -0.586  1.342   1.00 31.57  ?  518 HOH A O     1 
HETATM 6981 O  O     . HOH M 5 .   ? 32.768  6.661   7.176   1.00 31.57  ?  519 HOH A O     1 
HETATM 6982 O  O     . HOH M 5 .   ? 0.729   15.505  -6.116  1.00 31.57  ?  520 HOH A O     1 
HETATM 6983 O  O     . HOH M 5 .   ? 2.865   17.708  2.057   1.00 31.57  ?  521 HOH A O     1 
HETATM 6984 O  O     . HOH M 5 .   ? 26.837  11.683  -2.440  1.00 31.57  ?  522 HOH A O     1 
HETATM 6985 O  O     . HOH M 5 .   ? 16.459  10.885  3.244   1.00 31.57  ?  523 HOH A O     1 
HETATM 6986 O  O     . HOH M 5 .   ? 7.141   -4.386  18.191  1.00 31.57  ?  524 HOH A O     1 
HETATM 6987 O  O     . HOH M 5 .   ? 12.043  13.055  20.341  1.00 31.57  ?  525 HOH A O     1 
HETATM 6988 O  O     . HOH M 5 .   ? 3.577   -5.389  22.420  1.00 31.57  ?  526 HOH A O     1 
HETATM 6989 O  O     . HOH M 5 .   ? 13.759  1.520   26.975  1.00 31.57  ?  527 HOH A O     1 
HETATM 6990 O  O     . HOH M 5 .   ? 15.326  19.946  21.888  1.00 31.57  ?  528 HOH A O     1 
HETATM 6991 O  O     . HOH M 5 .   ? 25.835  15.294  28.307  1.00 31.57  ?  529 HOH A O     1 
HETATM 6992 O  O     . HOH M 5 .   ? 9.716   4.163   0.541   1.00 31.57  ?  530 HOH A O     1 
HETATM 6993 O  O     . HOH M 5 .   ? 20.487  24.576  10.716  1.00 31.57  ?  531 HOH A O     1 
HETATM 6994 O  O     . HOH M 5 .   ? 4.510   28.605  4.364   1.00 31.57  ?  532 HOH A O     1 
HETATM 6995 O  O     . HOH M 5 .   ? 2.313   13.202  16.360  1.00 31.57  ?  533 HOH A O     1 
HETATM 6996 O  O     . HOH M 5 .   ? 2.382   21.491  12.286  1.00 31.57  ?  534 HOH A O     1 
HETATM 6997 O  O     . HOH M 5 .   ? 15.091  7.241   22.716  1.00 31.57  ?  535 HOH A O     1 
HETATM 6998 O  O     . HOH M 5 .   ? 1.558   5.738   6.534   1.00 31.57  ?  536 HOH A O     1 
HETATM 6999 O  O     . HOH M 5 .   ? 41.114  17.961  17.893  1.00 31.57  ?  537 HOH A O     1 
HETATM 7000 O  O     . HOH M 5 .   ? 1.771   14.889  -2.317  1.00 31.57  ?  538 HOH A O     1 
HETATM 7001 O  O     . HOH M 5 .   ? 11.343  31.526  20.487  1.00 31.57  ?  539 HOH A O     1 
HETATM 7002 O  O     . HOH M 5 .   ? 2.151   9.071   -5.907  1.00 31.57  ?  540 HOH A O     1 
HETATM 7003 O  O     . HOH M 5 .   ? 20.522  5.728   -2.684  1.00 31.57  ?  541 HOH A O     1 
HETATM 7004 O  O     . HOH M 5 .   ? 29.638  24.489  14.312  1.00 31.57  ?  542 HOH A O     1 
HETATM 7005 O  O     . HOH M 5 .   ? -0.549  6.785   6.153   1.00 31.57  ?  543 HOH A O     1 
HETATM 7006 O  O     . HOH M 5 .   ? 5.474   11.353  8.510   1.00 31.57  ?  544 HOH A O     1 
HETATM 7007 O  O     . HOH M 5 .   ? 5.422   26.845  8.461   1.00 31.57  ?  545 HOH A O     1 
HETATM 7008 O  O     . HOH M 5 .   ? 2.141   0.548   7.427   1.00 31.57  ?  546 HOH A O     1 
HETATM 7009 O  O     . HOH M 5 .   ? 37.508  2.362   16.915  1.00 31.57  ?  547 HOH A O     1 
HETATM 7010 O  O     . HOH M 5 .   ? 4.350   22.225  9.521   1.00 31.57  ?  548 HOH A O     1 
HETATM 7011 O  O     . HOH M 5 .   ? 6.369   30.310  6.630   1.00 31.57  ?  549 HOH A O     1 
HETATM 7012 O  O     . HOH M 5 .   ? 9.866   -5.078  11.191  1.00 31.57  ?  550 HOH A O     1 
HETATM 7013 O  O     . HOH M 5 .   ? 35.223  17.616  4.574   1.00 31.57  ?  551 HOH A O     1 
HETATM 7014 O  O     . HOH M 5 .   ? 14.814  12.208  5.142   1.00 31.57  ?  552 HOH A O     1 
HETATM 7015 O  O     . HOH M 5 .   ? 15.896  16.854  0.809   1.00 31.57  ?  553 HOH A O     1 
HETATM 7016 O  O     . HOH M 5 .   ? 3.070   -3.731  12.953  1.00 31.57  ?  554 HOH A O     1 
HETATM 7017 O  O     . HOH M 5 .   ? 29.858  28.925  19.756  1.00 31.57  ?  555 HOH A O     1 
HETATM 7018 O  O     . HOH M 5 .   ? 6.915   13.010  21.272  1.00 31.57  ?  556 HOH A O     1 
HETATM 7019 O  O     . HOH M 5 .   ? 8.370   3.078   23.813  1.00 31.57  ?  557 HOH A O     1 
HETATM 7020 O  O     . HOH M 5 .   ? 19.853  5.085   27.231  1.00 31.57  ?  558 HOH A O     1 
HETATM 7021 O  O     . HOH M 5 .   ? 35.692  33.201  20.670  1.00 31.57  ?  559 HOH A O     1 
HETATM 7022 O  O     . HOH M 5 .   ? 5.262   19.937  9.725   1.00 31.57  ?  560 HOH A O     1 
HETATM 7023 O  O     . HOH M 5 .   ? 29.980  14.644  23.061  1.00 31.57  ?  561 HOH A O     1 
HETATM 7024 O  O     . HOH M 5 .   ? 16.708  14.066  26.911  1.00 31.57  ?  562 HOH A O     1 
HETATM 7025 O  O     . HOH M 5 .   ? 6.512   3.206   0.301   1.00 31.57  ?  563 HOH A O     1 
HETATM 7026 O  O     . HOH M 5 .   ? 16.574  24.098  23.882  1.00 31.57  ?  564 HOH A O     1 
HETATM 7027 O  O     . HOH M 5 .   ? 14.608  11.770  -4.092  1.00 31.57  ?  565 HOH A O     1 
HETATM 7028 O  O     . HOH M 5 .   ? 17.527  10.231  7.172   1.00 31.57  ?  566 HOH A O     1 
HETATM 7029 O  O     . HOH M 5 .   ? 1.162   8.327   4.461   1.00 31.57  ?  567 HOH A O     1 
HETATM 7030 O  O     . HOH M 5 .   ? 1.801   16.148  15.497  1.00 31.57  ?  568 HOH A O     1 
HETATM 7031 O  O     . HOH M 5 .   ? 9.429   29.507  -1.467  1.00 31.57  ?  569 HOH A O     1 
HETATM 7032 O  O     . HOH M 5 .   ? 10.941  28.394  26.889  1.00 31.57  ?  570 HOH A O     1 
HETATM 7033 O  O     . HOH M 5 .   ? 32.199  13.976  20.864  1.00 31.57  ?  571 HOH A O     1 
HETATM 7034 O  O     . HOH M 5 .   ? -2.276  1.396   16.728  1.00 31.57  ?  572 HOH A O     1 
HETATM 7035 O  O     . HOH M 5 .   ? 9.236   30.816  7.075   1.00 31.57  ?  573 HOH A O     1 
HETATM 7036 O  O     . HOH M 5 .   ? 5.457   18.118  2.766   1.00 31.57  ?  574 HOH A O     1 
HETATM 7037 O  O     . HOH M 5 .   ? 13.020  10.944  6.958   1.00 31.57  ?  575 HOH A O     1 
HETATM 7038 O  O     . HOH M 5 .   ? 26.507  11.887  -6.522  1.00 31.57  ?  576 HOH A O     1 
HETATM 7039 O  O     . HOH M 5 .   ? 5.529   13.713  9.846   1.00 31.57  ?  577 HOH A O     1 
HETATM 7040 O  O     . HOH M 5 .   ? 19.903  -1.685  27.587  1.00 31.57  ?  578 HOH A O     1 
HETATM 7041 O  O     . HOH M 5 .   ? 38.701  25.949  12.476  1.00 31.57  ?  579 HOH A O     1 
HETATM 7042 O  O     . HOH M 5 .   ? 19.266  15.268  -3.436  1.00 31.57  ?  580 HOH A O     1 
HETATM 7043 O  O     . HOH M 5 .   ? 6.668   10.300  10.979  1.00 31.57  ?  581 HOH A O     1 
HETATM 7044 O  O     . HOH M 5 .   ? 13.271  23.629  24.002  1.00 31.57  ?  582 HOH A O     1 
HETATM 7045 O  O     . HOH M 5 .   ? 7.473   15.329  8.009   1.00 31.57  ?  583 HOH A O     1 
HETATM 7046 O  O     . HOH M 5 .   ? 1.881   2.867   5.786   1.00 31.57  ?  584 HOH A O     1 
HETATM 7047 O  O     . HOH M 5 .   ? 39.075  14.566  21.173  1.00 31.57  ?  585 HOH A O     1 
HETATM 7048 O  O     . HOH M 5 .   ? 5.194   -4.560  11.900  1.00 31.57  ?  586 HOH A O     1 
HETATM 7049 O  O     . HOH M 5 .   ? 2.637   9.347   -0.085  1.00 31.57  ?  587 HOH A O     1 
HETATM 7050 O  O     . HOH M 5 .   ? 6.294   26.677  0.711   1.00 31.57  ?  588 HOH A O     1 
HETATM 7051 O  O     . HOH M 5 .   ? 4.532   -0.528  6.585   1.00 31.57  ?  589 HOH A O     1 
HETATM 7052 O  O     . HOH M 5 .   ? 23.493  15.831  -2.091  1.00 31.57  ?  590 HOH A O     1 
HETATM 7053 O  O     . HOH M 5 .   ? 1.039   33.693  13.853  1.00 31.57  ?  591 HOH A O     1 
HETATM 7054 O  O     . HOH M 5 .   ? 31.548  37.737  -2.203  1.00 31.57  ?  592 HOH A O     1 
HETATM 7055 O  O     . HOH M 5 .   ? 38.691  17.478  19.839  1.00 31.57  ?  593 HOH A O     1 
HETATM 7056 O  O     . HOH M 5 .   ? 32.086  15.500  1.853   1.00 31.57  ?  594 HOH A O     1 
HETATM 7057 O  O     . HOH M 5 .   ? 1.892   24.644  11.081  1.00 31.57  ?  595 HOH A O     1 
HETATM 7058 O  O     . HOH M 5 .   ? 23.101  11.926  -5.088  1.00 31.57  ?  596 HOH A O     1 
HETATM 7059 O  O     . HOH M 5 .   ? 1.672   33.438  18.364  1.00 31.57  ?  597 HOH A O     1 
HETATM 7060 O  O     . HOH M 5 .   ? 17.099  20.672  27.508  1.00 31.57  ?  598 HOH A O     1 
HETATM 7061 O  O     . HOH M 5 .   ? -0.345  3.213   16.074  1.00 31.57  ?  599 HOH A O     1 
HETATM 7062 O  O     . HOH M 5 .   ? 7.894   -4.761  13.111  1.00 31.57  ?  600 HOH A O     1 
HETATM 7063 O  O     . HOH M 5 .   ? 16.692  23.449  26.311  1.00 31.57  ?  601 HOH A O     1 
HETATM 7064 O  O     . HOH M 5 .   ? 6.913   9.269   -4.683  1.00 31.57  ?  602 HOH A O     1 
HETATM 7065 O  O     . HOH M 5 .   ? 33.693  11.705  22.585  1.00 31.57  ?  603 HOH A O     1 
HETATM 7066 O  O     . HOH M 5 .   ? 1.670   6.087   22.971  1.00 31.57  ?  604 HOH A O     1 
HETATM 7067 O  O     . HOH M 5 .   ? 13.822  24.595  26.415  1.00 31.57  ?  605 HOH A O     1 
HETATM 7068 O  O     . HOH M 5 .   ? 4.731   16.324  16.460  1.00 31.57  ?  606 HOH A O     1 
HETATM 7069 O  O     . HOH M 5 .   ? 0.225   8.617   1.688   1.00 31.57  ?  607 HOH A O     1 
HETATM 7070 O  O     . HOH M 5 .   ? 30.346  25.997  18.738  1.00 31.57  ?  608 HOH A O     1 
HETATM 7071 O  O     . HOH M 5 .   ? 15.192  22.463  22.011  1.00 31.57  ?  609 HOH A O     1 
HETATM 7072 O  O     . HOH M 5 .   ? 2.701   13.583  22.714  1.00 31.57  ?  610 HOH A O     1 
HETATM 7073 O  O     . HOH M 5 .   ? 3.811   -7.928  8.845   1.00 31.57  ?  611 HOH A O     1 
HETATM 7074 O  O     . HOH M 5 .   ? 8.158   -7.550  18.066  1.00 31.57  ?  612 HOH A O     1 
HETATM 7075 O  O     . HOH M 5 .   ? 18.409  3.883   -2.859  1.00 31.57  ?  613 HOH A O     1 
HETATM 7076 O  O     . HOH M 5 .   ? 24.949  13.329  -3.095  1.00 31.57  ?  614 HOH A O     1 
HETATM 7077 O  O     . HOH M 5 .   ? 18.248  17.420  -4.613  1.00 31.57  ?  615 HOH A O     1 
HETATM 7078 O  O     . HOH M 5 .   ? 32.792  25.310  19.517  1.00 31.57  ?  616 HOH A O     1 
HETATM 7079 O  O     . HOH M 5 .   ? 4.466   14.278  20.950  1.00 31.57  ?  617 HOH A O     1 
HETATM 7080 O  O     . HOH M 5 .   ? 7.201   -6.185  15.738  1.00 31.57  ?  618 HOH A O     1 
HETATM 7081 O  O     . HOH M 5 .   ? 12.282  31.698  23.189  1.00 31.57  ?  619 HOH A O     1 
HETATM 7082 O  O     . HOH M 5 .   ? 8.190   -5.714  8.969   1.00 31.57  ?  620 HOH A O     1 
HETATM 7083 O  O     . HOH M 5 .   ? 5.575   -6.704  10.305  1.00 31.57  ?  621 HOH A O     1 
HETATM 7084 O  O     . HOH N 5 .   ? 14.956  21.445  -12.308 1.00 31.57  ?  501 HOH B O     1 
HETATM 7085 O  O     . HOH N 5 .   ? 1.230   -8.989  -28.572 1.00 31.57  ?  502 HOH B O     1 
HETATM 7086 O  O     . HOH N 5 .   ? 2.806   32.081  -33.707 1.00 31.57  ?  503 HOH B O     1 
HETATM 7087 O  O     . HOH N 5 .   ? 1.521   22.247  -3.349  1.00 31.57  ?  504 HOH B O     1 
HETATM 7088 O  O     . HOH N 5 .   ? 16.339  -4.863  -18.782 1.00 31.57  ?  505 HOH B O     1 
HETATM 7089 O  O     . HOH N 5 .   ? 20.515  -0.202  -20.139 1.00 31.57  ?  506 HOH B O     1 
HETATM 7090 O  O     . HOH N 5 .   ? 26.035  9.428   -21.502 1.00 31.57  ?  507 HOH B O     1 
HETATM 7091 O  O     . HOH N 5 .   ? -2.446  2.357   -32.690 1.00 31.57  ?  508 HOH B O     1 
HETATM 7092 O  O     . HOH N 5 .   ? 21.694  28.083  -14.635 1.00 31.57  ?  509 HOH B O     1 
HETATM 7093 O  O     . HOH N 5 .   ? 13.691  14.400  -36.105 1.00 31.57  ?  510 HOH B O     1 
HETATM 7094 O  O     . HOH N 5 .   ? 18.508  27.541  -20.392 1.00 31.57  ?  511 HOH B O     1 
HETATM 7095 O  O     . HOH N 5 .   ? -9.308  24.683  -29.182 1.00 31.57  ?  512 HOH B O     1 
HETATM 7096 O  O     . HOH N 5 .   ? 16.188  28.299  -19.280 1.00 31.57  ?  513 HOH B O     1 
HETATM 7097 O  O     . HOH N 5 .   ? 8.936   23.181  -40.479 1.00 31.57  ?  514 HOH B O     1 
HETATM 7098 O  O     . HOH N 5 .   ? 12.284  1.984   -19.460 1.00 31.57  ?  515 HOH B O     1 
HETATM 7099 O  O     . HOH N 5 .   ? -0.216  16.504  -30.336 1.00 31.57  ?  516 HOH B O     1 
HETATM 7100 O  O     . HOH N 5 .   ? 12.086  8.528   -14.375 1.00 31.57  ?  517 HOH B O     1 
HETATM 7101 O  O     . HOH N 5 .   ? -0.421  -1.246  -21.560 1.00 31.57  ?  518 HOH B O     1 
HETATM 7102 O  O     . HOH N 5 .   ? 4.956   -4.350  -10.864 1.00 31.57  ?  519 HOH B O     1 
HETATM 7103 O  O     . HOH N 5 .   ? 17.391  4.415   -24.541 1.00 31.57  ?  520 HOH B O     1 
HETATM 7104 O  O     . HOH N 5 .   ? 10.497  17.533  -16.202 1.00 31.57  ?  521 HOH B O     1 
HETATM 7105 O  O     . HOH N 5 .   ? 29.105  19.487  -25.718 1.00 31.57  ?  522 HOH B O     1 
HETATM 7106 O  O     . HOH N 5 .   ? 13.612  17.356  -7.521  1.00 31.57  ?  523 HOH B O     1 
HETATM 7107 O  O     . HOH N 5 .   ? 17.431  17.805  -18.864 1.00 31.57  ?  524 HOH B O     1 
HETATM 7108 O  O     . HOH N 5 .   ? 3.107   11.815  -24.100 1.00 31.57  ?  525 HOH B O     1 
HETATM 7109 O  O     . HOH N 5 .   ? -4.048  27.605  -35.403 1.00 31.57  ?  526 HOH B O     1 
HETATM 7110 O  O     . HOH N 5 .   ? -6.783  7.330   -17.411 1.00 31.57  ?  527 HOH B O     1 
HETATM 7111 O  O     . HOH N 5 .   ? -8.320  8.620   -21.533 1.00 31.57  ?  528 HOH B O     1 
HETATM 7112 O  O     . HOH N 5 .   ? -2.057  -5.189  -16.170 1.00 31.57  ?  529 HOH B O     1 
HETATM 7113 O  O     . HOH N 5 .   ? 13.858  10.394  -43.745 1.00 31.57  ?  530 HOH B O     1 
HETATM 7114 O  O     . HOH N 5 .   ? 3.819   30.401  -36.464 1.00 31.57  ?  531 HOH B O     1 
HETATM 7115 O  O     . HOH N 5 .   ? -9.466  24.739  -24.423 1.00 31.57  ?  532 HOH B O     1 
HETATM 7116 O  O     . HOH N 5 .   ? 13.745  14.218  -7.093  1.00 31.57  ?  533 HOH B O     1 
HETATM 7117 O  O     . HOH N 5 .   ? -2.358  24.999  -44.011 1.00 31.57  ?  534 HOH B O     1 
HETATM 7118 O  O     . HOH N 5 .   ? 13.117  17.241  -13.625 1.00 31.57  ?  535 HOH B O     1 
HETATM 7119 O  O     . HOH N 5 .   ? 13.136  8.195   -26.711 1.00 31.57  ?  536 HOH B O     1 
HETATM 7120 O  O     . HOH N 5 .   ? 15.372  -5.484  -30.568 1.00 31.57  ?  537 HOH B O     1 
HETATM 7121 O  O     . HOH N 5 .   ? -4.462  24.664  -33.737 1.00 31.57  ?  538 HOH B O     1 
HETATM 7122 O  O     . HOH N 5 .   ? -3.984  19.805  -7.968  1.00 31.57  ?  539 HOH B O     1 
HETATM 7123 O  O     . HOH N 5 .   ? 21.105  15.052  -18.165 1.00 31.57  ?  540 HOH B O     1 
HETATM 7124 O  O     . HOH N 5 .   ? 0.861   -1.650  -31.274 1.00 31.57  ?  541 HOH B O     1 
HETATM 7125 O  O     . HOH N 5 .   ? 15.413  28.788  -30.183 1.00 31.57  ?  542 HOH B O     1 
HETATM 7126 O  O     . HOH N 5 .   ? 2.459   17.573  -29.937 1.00 31.57  ?  543 HOH B O     1 
HETATM 7127 O  O     . HOH N 5 .   ? 7.221   24.001  -7.730  1.00 31.57  ?  544 HOH B O     1 
HETATM 7128 O  O     . HOH N 5 .   ? 3.327   13.187  -34.205 1.00 31.57  ?  545 HOH B O     1 
HETATM 7129 O  O     . HOH N 5 .   ? 14.605  28.175  -21.614 1.00 31.57  ?  546 HOH B O     1 
HETATM 7130 O  O     . HOH N 5 .   ? 21.914  -0.060  -34.998 1.00 31.57  ?  547 HOH B O     1 
HETATM 7131 O  O     . HOH N 5 .   ? 26.829  12.119  -38.429 1.00 31.57  ?  548 HOH B O     1 
HETATM 7132 O  O     . HOH N 5 .   ? -3.316  29.643  -9.307  1.00 31.57  ?  549 HOH B O     1 
HETATM 7133 O  O     . HOH N 5 .   ? 12.411  23.711  -19.741 1.00 31.57  ?  550 HOH B O     1 
HETATM 7134 O  O     . HOH N 5 .   ? 13.969  3.798   -20.640 1.00 31.57  ?  551 HOH B O     1 
HETATM 7135 O  O     . HOH N 5 .   ? 8.093   25.370  -14.375 1.00 31.57  ?  552 HOH B O     1 
HETATM 7136 O  O     . HOH N 5 .   ? -5.808  33.026  -22.377 1.00 31.57  ?  553 HOH B O     1 
HETATM 7137 O  O     . HOH N 5 .   ? -1.463  38.043  -25.137 1.00 31.57  ?  554 HOH B O     1 
HETATM 7138 O  O     . HOH N 5 .   ? 23.175  22.719  -23.532 1.00 31.57  ?  555 HOH B O     1 
HETATM 7139 O  O     . HOH N 5 .   ? -0.115  17.672  -3.295  1.00 31.57  ?  556 HOH B O     1 
HETATM 7140 O  O     . HOH N 5 .   ? 27.242  -0.510  -23.056 1.00 31.57  ?  557 HOH B O     1 
HETATM 7141 O  O     . HOH N 5 .   ? -6.243  31.151  -29.423 1.00 31.57  ?  558 HOH B O     1 
HETATM 7142 O  O     . HOH N 5 .   ? 8.850   9.762   -8.807  1.00 31.57  ?  559 HOH B O     1 
HETATM 7143 O  O     . HOH N 5 .   ? -3.330  17.162  -6.557  1.00 31.57  ?  560 HOH B O     1 
HETATM 7144 O  O     . HOH N 5 .   ? 6.730   26.565  -31.828 1.00 31.57  ?  561 HOH B O     1 
HETATM 7145 O  O     . HOH N 5 .   ? 6.676   30.493  -9.799  1.00 31.57  ?  562 HOH B O     1 
HETATM 7146 O  O     . HOH N 5 .   ? 3.107   20.377  -29.177 1.00 31.57  ?  563 HOH B O     1 
HETATM 7147 O  O     . HOH N 5 .   ? 1.175   17.311  -26.493 1.00 31.57  ?  564 HOH B O     1 
HETATM 7148 O  O     . HOH N 5 .   ? -5.307  12.677  -6.895  1.00 31.57  ?  565 HOH B O     1 
HETATM 7149 O  O     . HOH N 5 .   ? 14.754  31.848  -11.471 1.00 31.57  ?  566 HOH B O     1 
HETATM 7150 O  O     . HOH N 5 .   ? 26.977  14.588  -26.050 1.00 31.57  ?  567 HOH B O     1 
HETATM 7151 O  O     . HOH N 5 .   ? 9.629   25.557  -31.469 1.00 31.57  ?  568 HOH B O     1 
HETATM 7152 O  O     . HOH N 5 .   ? 13.648  22.971  -8.491  1.00 31.57  ?  569 HOH B O     1 
HETATM 7153 O  O     . HOH N 5 .   ? 4.470   2.022   -5.680  1.00 31.57  ?  570 HOH B O     1 
HETATM 7154 O  O     . HOH N 5 .   ? 10.155  7.644   -7.351  1.00 31.57  ?  571 HOH B O     1 
HETATM 7155 O  O     . HOH N 5 .   ? -8.487  28.187  -13.245 1.00 31.57  ?  572 HOH B O     1 
HETATM 7156 O  O     . HOH N 5 .   ? 14.875  23.700  -14.426 1.00 31.57  ?  573 HOH B O     1 
HETATM 7157 O  O     . HOH N 5 .   ? -2.602  15.129  -37.380 1.00 31.57  ?  574 HOH B O     1 
HETATM 7158 O  O     . HOH N 5 .   ? 8.835   21.180  -38.701 1.00 31.57  ?  575 HOH B O     1 
HETATM 7159 O  O     . HOH N 5 .   ? 16.372  22.204  -35.129 1.00 31.57  ?  576 HOH B O     1 
HETATM 7160 O  O     . HOH N 5 .   ? 19.898  12.713  -37.486 1.00 31.57  ?  577 HOH B O     1 
HETATM 7161 O  O     . HOH N 5 .   ? 7.090   26.722  -29.076 1.00 31.57  ?  578 HOH B O     1 
HETATM 7162 O  O     . HOH N 5 .   ? -11.704 20.822  -25.287 1.00 31.57  ?  579 HOH B O     1 
HETATM 7163 O  O     . HOH N 5 .   ? 6.154   33.942  -35.747 1.00 31.57  ?  580 HOH B O     1 
HETATM 7164 O  O     . HOH N 5 .   ? 10.212  25.826  -7.249  1.00 31.57  ?  581 HOH B O     1 
HETATM 7165 O  O     . HOH N 5 .   ? 14.087  15.457  -42.622 1.00 31.57  ?  582 HOH B O     1 
HETATM 7166 O  O     . HOH N 5 .   ? 18.845  18.064  -37.026 1.00 31.57  ?  583 HOH B O     1 
HETATM 7167 O  O     . HOH N 5 .   ? -2.703  33.309  -30.660 1.00 31.57  ?  584 HOH B O     1 
HETATM 7168 O  O     . HOH N 5 .   ? -8.240  20.074  -9.351  1.00 31.57  ?  585 HOH B O     1 
HETATM 7169 O  O     . HOH N 5 .   ? -9.712  21.401  -23.700 1.00 31.57  ?  586 HOH B O     1 
HETATM 7170 O  O     . HOH N 5 .   ? -1.085  9.870   -35.526 1.00 31.57  ?  587 HOH B O     1 
HETATM 7171 O  O     . HOH N 5 .   ? -6.612  6.892   -20.657 1.00 31.57  ?  588 HOH B O     1 
HETATM 7172 O  O     . HOH N 5 .   ? 20.231  17.575  -13.882 1.00 31.57  ?  589 HOH B O     1 
HETATM 7173 O  O     . HOH N 5 .   ? 19.045  2.072   -41.147 1.00 31.57  ?  590 HOH B O     1 
HETATM 7174 O  O     . HOH N 5 .   ? 3.723   4.105   -40.024 1.00 31.57  ?  591 HOH B O     1 
HETATM 7175 O  O     . HOH N 5 .   ? 0.249   33.129  -33.488 1.00 31.57  ?  592 HOH B O     1 
HETATM 7176 O  O     . HOH N 5 .   ? 13.861  30.079  -27.992 1.00 31.57  ?  593 HOH B O     1 
HETATM 7177 O  O     . HOH N 5 .   ? 8.946   22.682  -32.541 1.00 31.57  ?  594 HOH B O     1 
HETATM 7178 O  O     . HOH N 5 .   ? 9.260   36.738  -19.350 1.00 31.57  ?  595 HOH B O     1 
HETATM 7179 O  O     . HOH N 5 .   ? 9.612   -4.569  -43.759 1.00 31.57  ?  596 HOH B O     1 
HETATM 7180 O  O     . HOH N 5 .   ? 20.627  15.816  -11.737 1.00 31.57  ?  597 HOH B O     1 
HETATM 7181 O  O     . HOH N 5 .   ? 6.407   7.824   -8.999  1.00 31.57  ?  598 HOH B O     1 
HETATM 7182 O  O     . HOH N 5 .   ? -4.781  32.557  -15.061 1.00 31.57  ?  599 HOH B O     1 
HETATM 7183 O  O     . HOH N 5 .   ? 2.267   27.700  -5.114  1.00 31.57  ?  600 HOH B O     1 
HETATM 7184 O  O     . HOH N 5 .   ? 21.994  18.069  -19.629 1.00 31.57  ?  601 HOH B O     1 
HETATM 7185 O  O     . HOH N 5 .   ? 20.808  -0.792  -12.263 1.00 31.57  ?  602 HOH B O     1 
HETATM 7186 O  O     . HOH N 5 .   ? -2.348  1.442   -24.885 1.00 31.57  ?  603 HOH B O     1 
HETATM 7187 O  O     . HOH N 5 .   ? -5.877  8.267   -33.763 1.00 31.57  ?  604 HOH B O     1 
HETATM 7188 O  O     . HOH N 5 .   ? -1.367  6.756   -32.324 1.00 31.57  ?  605 HOH B O     1 
HETATM 7189 O  O     . HOH N 5 .   ? 6.201   0.415   -7.842  1.00 31.57  ?  606 HOH B O     1 
HETATM 7190 O  O     . HOH N 5 .   ? -6.719  7.438   -9.976  1.00 31.57  ?  607 HOH B O     1 
HETATM 7191 O  O     . HOH N 5 .   ? -12.399 22.109  -9.546  1.00 31.57  ?  608 HOH B O     1 
HETATM 7192 O  O     . HOH N 5 .   ? 18.274  30.319  -27.574 1.00 31.57  ?  609 HOH B O     1 
HETATM 7193 O  O     . HOH N 5 .   ? 6.770   37.928  -26.165 1.00 31.57  ?  610 HOH B O     1 
HETATM 7194 O  O     . HOH N 5 .   ? 12.498  27.090  -8.410  1.00 31.57  ?  611 HOH B O     1 
HETATM 7195 O  O     . HOH N 5 .   ? 5.049   8.331   -6.192  1.00 31.57  ?  612 HOH B O     1 
HETATM 7196 O  O     . HOH N 5 .   ? 16.684  30.820  -18.602 1.00 31.57  ?  613 HOH B O     1 
HETATM 7197 O  O     . HOH N 5 .   ? 2.793   29.671  -38.976 1.00 31.57  ?  614 HOH B O     1 
HETATM 7198 O  O     . HOH N 5 .   ? 25.444  3.106   -16.745 1.00 31.57  ?  615 HOH B O     1 
HETATM 7199 O  O     . HOH N 5 .   ? 15.335  26.594  -27.709 1.00 31.57  ?  616 HOH B O     1 
HETATM 7200 O  O     . HOH N 5 .   ? 23.861  17.592  -17.541 1.00 31.57  ?  617 HOH B O     1 
HETATM 7201 O  O     . HOH N 5 .   ? 1.027   -4.837  -12.809 1.00 31.57  ?  618 HOH B O     1 
HETATM 7202 O  O     . HOH N 5 .   ? -5.163  29.206  -11.560 1.00 31.57  ?  619 HOH B O     1 
HETATM 7203 O  O     . HOH N 5 .   ? 19.398  16.723  -19.733 1.00 31.57  ?  620 HOH B O     1 
HETATM 7204 O  O     . HOH N 5 .   ? 11.761  36.670  -20.773 1.00 31.57  ?  621 HOH B O     1 
HETATM 7205 O  O     . HOH N 5 .   ? 22.138  16.707  -15.792 1.00 31.57  ?  622 HOH B O     1 
HETATM 7206 O  O     . HOH N 5 .   ? 19.069  13.308  -10.652 1.00 31.57  ?  623 HOH B O     1 
HETATM 7207 O  O     . HOH N 5 .   ? 24.252  24.946  -23.015 1.00 31.57  ?  624 HOH B O     1 
HETATM 7208 O  O     . HOH N 5 .   ? -1.404  16.040  -5.458  1.00 31.57  ?  625 HOH B O     1 
HETATM 7209 O  O     . HOH N 5 .   ? -5.319  15.383  -38.608 1.00 31.57  ?  626 HOH B O     1 
HETATM 7210 O  O     . HOH N 5 .   ? 16.235  28.987  -23.662 1.00 31.57  ?  627 HOH B O     1 
HETATM 7211 O  O     . HOH N 5 .   ? 12.503  7.403   -6.009  1.00 31.57  ?  628 HOH B O     1 
HETATM 7212 O  O     . HOH N 5 .   ? -5.852  31.766  -12.658 1.00 31.57  ?  629 HOH B O     1 
HETATM 7213 O  O     . HOH N 5 .   ? -4.202  6.658   -32.055 1.00 31.57  ?  630 HOH B O     1 
HETATM 7214 O  O     . HOH N 5 .   ? -7.028  24.369  -33.574 1.00 31.57  ?  631 HOH B O     1 
HETATM 7215 O  O     . HOH N 5 .   ? 25.454  25.201  -20.864 1.00 31.57  ?  632 HOH B O     1 
HETATM 7216 O  O     . HOH N 5 .   ? 9.868   35.064  -17.064 1.00 31.57  ?  633 HOH B O     1 
HETATM 7217 O  O     . HOH N 5 .   ? 24.976  24.838  -18.235 1.00 31.57  ?  634 HOH B O     1 
HETATM 7218 O  O     . HOH O 5 .   ? 19.105  69.671  -47.383 1.00 31.57  ?  501 HOH C O     1 
HETATM 7219 O  O     . HOH O 5 .   ? 15.184  62.852  -64.772 1.00 31.57  ?  502 HOH C O     1 
HETATM 7220 O  O     . HOH O 5 .   ? 15.869  52.130  -38.264 1.00 31.57  ?  503 HOH C O     1 
HETATM 7221 O  O     . HOH O 5 .   ? 16.013  67.105  -35.109 1.00 31.57  ?  504 HOH C O     1 
HETATM 7222 O  O     . HOH O 5 .   ? 23.187  69.514  -36.938 1.00 31.57  ?  505 HOH C O     1 
HETATM 7223 O  O     . HOH O 5 .   ? 16.900  55.832  -40.541 1.00 31.57  ?  506 HOH C O     1 
HETATM 7224 O  O     . HOH O 5 .   ? 19.721  44.634  -25.797 1.00 31.57  ?  507 HOH C O     1 
HETATM 7225 O  O     . HOH O 5 .   ? 13.786  53.689  -63.720 1.00 31.57  ?  508 HOH C O     1 
HETATM 7226 O  O     . HOH O 5 .   ? 11.449  45.647  -38.317 1.00 31.57  ?  509 HOH C O     1 
HETATM 7227 O  O     . HOH O 5 .   ? 21.942  44.660  -22.389 1.00 31.57  ?  510 HOH C O     1 
HETATM 7228 O  O     . HOH O 5 .   ? 26.267  43.129  -39.328 1.00 31.57  ?  511 HOH C O     1 
HETATM 7229 O  O     . HOH O 5 .   ? 12.986  45.381  -35.859 1.00 31.57  ?  512 HOH C O     1 
HETATM 7230 O  O     . HOH O 5 .   ? 17.107  49.151  -21.705 1.00 31.57  ?  513 HOH C O     1 
HETATM 7231 O  O     . HOH O 5 .   ? -0.176  55.756  -36.238 1.00 31.57  ?  514 HOH C O     1 
HETATM 7232 O  O     . HOH O 5 .   ? 14.185  51.383  -53.504 1.00 31.57  ?  515 HOH C O     1 
HETATM 7233 O  O     . HOH O 5 .   ? 24.545  53.210  -36.639 1.00 31.57  ?  516 HOH C O     1 
HETATM 7234 O  O     . HOH O 5 .   ? 18.833  56.054  -37.122 1.00 31.57  ?  517 HOH C O     1 
HETATM 7235 O  O     . HOH O 5 .   ? 28.489  53.712  -28.612 1.00 31.57  ?  518 HOH C O     1 
HETATM 7236 O  O     . HOH O 5 .   ? 23.373  75.792  -55.098 1.00 31.57  ?  519 HOH C O     1 
HETATM 7237 O  O     . HOH O 5 .   ? 9.365   40.994  -47.945 1.00 31.57  ?  520 HOH C O     1 
HETATM 7238 O  O     . HOH O 5 .   ? 18.491  53.361  -38.143 1.00 31.57  ?  521 HOH C O     1 
HETATM 7239 O  O     . HOH O 5 .   ? 3.828   48.101  -30.676 1.00 31.57  ?  522 HOH C O     1 
HETATM 7240 O  O     . HOH O 5 .   ? 17.199  69.367  -45.899 1.00 31.57  ?  523 HOH C O     1 
HETATM 7241 O  O     . HOH O 5 .   ? 29.754  66.789  -49.299 1.00 31.57  ?  524 HOH C O     1 
HETATM 7242 O  O     . HOH O 5 .   ? 20.967  43.783  -32.853 1.00 31.57  ?  525 HOH C O     1 
HETATM 7243 O  O     . HOH O 5 .   ? 18.556  74.191  -34.221 1.00 31.57  ?  526 HOH C O     1 
HETATM 7244 O  O     . HOH O 5 .   ? 22.358  56.705  -30.403 1.00 31.57  ?  527 HOH C O     1 
HETATM 7245 O  O     . HOH O 5 .   ? 30.766  38.675  -41.635 1.00 31.57  ?  528 HOH C O     1 
HETATM 7246 O  O     . HOH O 5 .   ? -3.942  50.954  -41.340 1.00 31.57  ?  529 HOH C O     1 
HETATM 7247 O  O     . HOH O 5 .   ? 26.805  57.985  -34.330 1.00 31.57  ?  530 HOH C O     1 
HETATM 7248 O  O     . HOH O 5 .   ? 21.171  64.380  -31.392 1.00 31.57  ?  531 HOH C O     1 
HETATM 7249 O  O     . HOH O 5 .   ? 2.270   63.907  -60.526 1.00 31.57  ?  532 HOH C O     1 
HETATM 7250 O  O     . HOH O 5 .   ? 18.477  57.914  -63.396 1.00 31.57  ?  533 HOH C O     1 
HETATM 7251 O  O     . HOH O 5 .   ? 4.502   65.218  -52.310 1.00 31.57  ?  534 HOH C O     1 
HETATM 7252 O  O     . HOH O 5 .   ? 29.314  40.799  -33.934 1.00 31.57  ?  535 HOH C O     1 
HETATM 7253 O  O     . HOH O 5 .   ? 28.216  60.537  -37.826 1.00 31.57  ?  536 HOH C O     1 
HETATM 7254 O  O     . HOH O 5 .   ? 3.281   67.430  -39.600 1.00 31.57  ?  537 HOH C O     1 
HETATM 7255 O  O     . HOH O 5 .   ? 18.423  31.077  -56.760 1.00 31.57  ?  538 HOH C O     1 
HETATM 7256 O  O     . HOH O 5 .   ? -1.715  53.108  -37.261 1.00 31.57  ?  539 HOH C O     1 
HETATM 7257 O  O     . HOH O 5 .   ? 3.567   62.579  -33.204 1.00 31.57  ?  540 HOH C O     1 
HETATM 7258 O  O     . HOH O 5 .   ? 18.485  64.092  -32.842 1.00 31.57  ?  541 HOH C O     1 
HETATM 7259 O  O     . HOH O 5 .   ? 15.562  62.565  -62.274 1.00 31.57  ?  542 HOH C O     1 
HETATM 7260 O  O     . HOH O 5 .   ? 29.020  70.659  -57.632 1.00 31.57  ?  543 HOH C O     1 
HETATM 7261 O  O     . HOH O 5 .   ? 16.536  54.451  -63.786 1.00 31.57  ?  544 HOH C 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     . GLY A 24  ? 0.7304 0.6480 0.7157 -0.1412 -0.0932 -0.0506 17  GLY A N     
2    C  CA    . GLY A 24  ? 0.6745 0.6092 0.6674 -0.1280 -0.0771 -0.0429 17  GLY A CA    
3    C  C     . GLY A 24  ? 0.6531 0.5783 0.6253 -0.1097 -0.0709 -0.0502 17  GLY A C     
4    O  O     . GLY A 24  ? 0.6815 0.5850 0.6322 -0.1058 -0.0768 -0.0614 17  GLY A O     
5    N  N     . GLN A 25  ? 0.6072 0.5502 0.5859 -0.0987 -0.0591 -0.0439 18  GLN A N     
6    C  CA    . GLN A 25  ? 0.5872 0.5262 0.5495 -0.0837 -0.0527 -0.0483 18  GLN A CA    
7    C  C     . GLN A 25  ? 0.5883 0.5026 0.5377 -0.0773 -0.0468 -0.0528 18  GLN A C     
8    O  O     . GLN A 25  ? 0.5907 0.4949 0.5468 -0.0823 -0.0448 -0.0490 18  GLN A O     
9    C  CB    . GLN A 25  ? 0.5461 0.5094 0.5201 -0.0762 -0.0443 -0.0397 18  GLN A CB    
10   C  CG    . GLN A 25  ? 0.5526 0.5380 0.5353 -0.0782 -0.0519 -0.0370 18  GLN A CG    
11   C  CD    . GLN A 25  ? 0.5203 0.5260 0.5149 -0.0698 -0.0449 -0.0288 18  GLN A CD    
12   O  OE1   . GLN A 25  ? 0.4997 0.5136 0.5085 -0.0694 -0.0370 -0.0230 18  GLN A OE1   
13   N  NE2   . GLN A 25  ? 0.5215 0.5344 0.5089 -0.0630 -0.0482 -0.0282 18  GLN A NE2   
14   N  N     . VAL A 26  ? 0.5919 0.4976 0.5228 -0.0663 -0.0443 -0.0607 19  VAL A N     
15   C  CA    . VAL A 26  ? 0.5927 0.4804 0.5142 -0.0577 -0.0382 -0.0650 19  VAL A CA    
16   C  C     . VAL A 26  ? 0.5478 0.4506 0.4751 -0.0487 -0.0260 -0.0580 19  VAL A C     
17   O  O     . VAL A 26  ? 0.5349 0.4511 0.4570 -0.0430 -0.0227 -0.0578 19  VAL A O     
18   C  CB    . VAL A 26  ? 0.6297 0.5007 0.5284 -0.0498 -0.0415 -0.0786 19  VAL A CB    
19   C  CG1   . VAL A 26  ? 0.6274 0.4866 0.5200 -0.0378 -0.0338 -0.0823 19  VAL A CG1   
20   C  CG2   . VAL A 26  ? 0.6829 0.5325 0.5730 -0.0588 -0.0552 -0.0873 19  VAL A CG2   
21   N  N     . PRO A 27  ? 0.5289 0.4283 0.4650 -0.0477 -0.0200 -0.0523 20  PRO A N     
22   C  CA    . PRO A 27  ? 0.4903 0.4034 0.4322 -0.0410 -0.0101 -0.0458 20  PRO A CA    
23   C  C     . PRO A 27  ? 0.4895 0.3991 0.4208 -0.0298 -0.0048 -0.0512 20  PRO A C     
24   O  O     . PRO A 27  ? 0.4848 0.3875 0.4175 -0.0251 -0.0010 -0.0504 20  PRO A O     
25   C  CB    . PRO A 27  ? 0.4805 0.3899 0.4331 -0.0451 -0.0074 -0.0387 20  PRO A CB    
26   C  CG    . PRO A 27  ? 0.5182 0.4036 0.4647 -0.0492 -0.0141 -0.0431 20  PRO A CG    
27   C  CD    . PRO A 27  ? 0.5473 0.4293 0.4874 -0.0543 -0.0231 -0.0503 20  PRO A CD    
28   N  N     . VAL A 28  ? 0.4963 0.4136 0.4174 -0.0259 -0.0044 -0.0555 21  VAL A N     
29   C  CA    . VAL A 28  ? 0.5080 0.4247 0.4175 -0.0158 0.0003  -0.0623 21  VAL A CA    
30   C  C     . VAL A 28  ? 0.4778 0.4069 0.3948 -0.0109 0.0093  -0.0560 21  VAL A C     
31   O  O     . VAL A 28  ? 0.4854 0.4139 0.3998 -0.0027 0.0135  -0.0602 21  VAL A O     
32   C  CB    . VAL A 28  ? 0.5305 0.4537 0.4248 -0.0142 -0.0013 -0.0679 21  VAL A CB    
33   C  CG1   . VAL A 28  ? 0.5095 0.4505 0.4062 -0.0176 0.0005  -0.0590 21  VAL A CG1   
34   C  CG2   . VAL A 28  ? 0.5527 0.4767 0.4342 -0.0034 0.0041  -0.0766 21  VAL A CG2   
35   N  N     . SER A 29  ? 0.4484 0.3890 0.3747 -0.0154 0.0115  -0.0466 22  SER A N     
36   C  CA    . SER A 29  ? 0.4252 0.3764 0.3569 -0.0127 0.0183  -0.0408 22  SER A CA    
37   C  C     . SER A 29  ? 0.4007 0.3527 0.3441 -0.0172 0.0183  -0.0330 22  SER A C     
38   O  O     . SER A 29  ? 0.3963 0.3519 0.3428 -0.0214 0.0155  -0.0294 22  SER A O     
39   C  CB    . SER A 29  ? 0.4267 0.3909 0.3518 -0.0125 0.0214  -0.0384 22  SER A CB    
40   O  OG    . SER A 29  ? 0.4106 0.3841 0.3411 -0.0117 0.0271  -0.0328 22  SER A OG    
41   N  N     . VAL A 30  ? 0.3901 0.3389 0.3394 -0.0155 0.0208  -0.0310 23  VAL A N     
42   C  CA    . VAL A 30  ? 0.3756 0.3233 0.3331 -0.0191 0.0209  -0.0253 23  VAL A CA    
43   C  C     . VAL A 30  ? 0.3592 0.3118 0.3198 -0.0170 0.0248  -0.0213 23  VAL A C     
44   O  O     . VAL A 30  ? 0.3613 0.3146 0.3208 -0.0131 0.0265  -0.0229 23  VAL A O     
45   C  CB    . VAL A 30  ? 0.3881 0.3235 0.3469 -0.0210 0.0184  -0.0260 23  VAL A CB    
46   C  CG1   . VAL A 30  ? 0.3783 0.3146 0.3435 -0.0244 0.0201  -0.0197 23  VAL A CG1   
47   C  CG2   . VAL A 30  ? 0.4096 0.3382 0.3660 -0.0258 0.0127  -0.0297 23  VAL A CG2   
48   N  N     . ASN A 31  ? 0.3477 0.3041 0.3120 -0.0190 0.0256  -0.0169 24  ASN A N     
49   C  CA    . ASN A 31  ? 0.3382 0.2955 0.3038 -0.0178 0.0278  -0.0140 24  ASN A CA    
50   C  C     . ASN A 31  ? 0.3379 0.2910 0.3055 -0.0183 0.0285  -0.0122 24  ASN A C     
51   O  O     . ASN A 31  ? 0.3403 0.2946 0.3110 -0.0206 0.0286  -0.0107 24  ASN A O     
52   C  CB    . ASN A 31  ? 0.3345 0.2946 0.3002 -0.0184 0.0276  -0.0111 24  ASN A CB    
53   C  CG    . ASN A 31  ? 0.3384 0.3017 0.3002 -0.0193 0.0274  -0.0101 24  ASN A CG    
54   O  OD1   . ASN A 31  ? 0.3380 0.3019 0.2995 -0.0203 0.0282  -0.0083 24  ASN A OD1   
55   N  ND2   . ASN A 31  ? 0.3461 0.3122 0.3044 -0.0198 0.0262  -0.0108 24  ASN A ND2   
56   N  N     . TYR A 32  ? 0.3388 0.2889 0.3048 -0.0165 0.0288  -0.0119 25  TYR A N     
57   C  CA    . TYR A 32  ? 0.3434 0.2891 0.3080 -0.0171 0.0293  -0.0091 25  TYR A CA    
58   C  C     . TYR A 32  ? 0.3393 0.2871 0.3014 -0.0159 0.0301  -0.0081 25  TYR A C     
59   O  O     . TYR A 32  ? 0.3400 0.2881 0.3011 -0.0144 0.0285  -0.0085 25  TYR A O     
60   C  CB    . TYR A 32  ? 0.3556 0.2934 0.3182 -0.0152 0.0271  -0.0093 25  TYR A CB    
61   C  CG    . TYR A 32  ? 0.3674 0.2985 0.3257 -0.0161 0.0266  -0.0048 25  TYR A CG    
62   C  CD1   . TYR A 32  ? 0.3696 0.3033 0.3261 -0.0199 0.0297  -0.0011 25  TYR A CD1   
63   C  CD2   . TYR A 32  ? 0.3816 0.3046 0.3370 -0.0125 0.0232  -0.0041 25  TYR A CD2   
64   C  CE1   . TYR A 32  ? 0.3861 0.3144 0.3361 -0.0214 0.0298  0.0039  25  TYR A CE1   
65   C  CE2   . TYR A 32  ? 0.3980 0.3133 0.3473 -0.0135 0.0218  0.0013  25  TYR A CE2   
66   C  CZ    . TYR A 32  ? 0.4003 0.3183 0.3458 -0.0187 0.0254  0.0057  25  TYR A CZ    
67   O  OH    . TYR A 32  ? 0.4211 0.3325 0.3579 -0.0202 0.0246  0.0119  25  TYR A OH    
68   N  N     . HIS A 33  ? 0.3400 0.2896 0.3014 -0.0162 0.0322  -0.0073 26  HIS A N     
69   C  CA    . HIS A 33  ? 0.3447 0.2926 0.3006 -0.0143 0.0324  -0.0079 26  HIS A CA    
70   C  C     . HIS A 33  ? 0.3559 0.3015 0.3056 -0.0143 0.0335  -0.0059 26  HIS A C     
71   O  O     . HIS A 33  ? 0.3650 0.3137 0.3123 -0.0141 0.0373  -0.0046 26  HIS A O     
72   C  CB    . HIS A 33  ? 0.3472 0.2974 0.3043 -0.0121 0.0341  -0.0092 26  HIS A CB    
73   C  CG    . HIS A 33  ? 0.3420 0.2918 0.3024 -0.0123 0.0315  -0.0097 26  HIS A CG    
74   N  ND1   . HIS A 33  ? 0.3489 0.2921 0.3055 -0.0115 0.0288  -0.0105 26  HIS A ND1   
75   C  CD2   . HIS A 33  ? 0.3358 0.2893 0.3007 -0.0142 0.0306  -0.0089 26  HIS A CD2   
76   C  CE1   . HIS A 33  ? 0.3472 0.2910 0.3062 -0.0129 0.0269  -0.0089 26  HIS A CE1   
77   N  NE2   . HIS A 33  ? 0.3391 0.2901 0.3027 -0.0138 0.0281  -0.0084 26  HIS A NE2   
78   N  N     . PHE A 34  ? 0.3588 0.3009 0.3062 -0.0142 0.0303  -0.0049 27  PHE A N     
79   C  CA    . PHE A 34  ? 0.3737 0.3117 0.3144 -0.0144 0.0298  -0.0012 27  PHE A CA    
80   C  C     . PHE A 34  ? 0.3882 0.3253 0.3178 -0.0134 0.0303  -0.0011 27  PHE A C     
81   O  O     . PHE A 34  ? 0.4053 0.3403 0.3268 -0.0144 0.0316  0.0030  27  PHE A O     
82   C  CB    . PHE A 34  ? 0.3770 0.3114 0.3195 -0.0126 0.0250  -0.0003 27  PHE A CB    
83   C  CG    . PHE A 34  ? 0.3762 0.3145 0.3194 -0.0106 0.0207  -0.0023 27  PHE A CG    
84   C  CD1   . PHE A 34  ? 0.3915 0.3277 0.3264 -0.0098 0.0171  -0.0007 27  PHE A CD1   
85   C  CD2   . PHE A 34  ? 0.3647 0.3102 0.3168 -0.0103 0.0200  -0.0052 27  PHE A CD2   
86   C  CE1   . PHE A 34  ? 0.3941 0.3358 0.3314 -0.0094 0.0118  -0.0024 27  PHE A CE1   
87   C  CE2   . PHE A 34  ? 0.3678 0.3201 0.3229 -0.0105 0.0159  -0.0060 27  PHE A CE2   
88   C  CZ    . PHE A 34  ? 0.3820 0.3327 0.3309 -0.0101 0.0113  -0.0048 27  PHE A CZ    
89   N  N     . SER A 35  ? 0.3866 0.3239 0.3142 -0.0120 0.0291  -0.0056 28  SER A N     
90   C  CA    . SER A 35  ? 0.4056 0.3399 0.3205 -0.0101 0.0288  -0.0081 28  SER A CA    
91   C  C     . SER A 35  ? 0.4063 0.3387 0.3214 -0.0077 0.0300  -0.0136 28  SER A C     
92   O  O     . SER A 35  ? 0.3925 0.3246 0.3165 -0.0088 0.0284  -0.0143 28  SER A O     
93   C  CB    . SER A 35  ? 0.4164 0.3469 0.3252 -0.0107 0.0215  -0.0085 28  SER A CB    
94   O  OG    . SER A 35  ? 0.4067 0.3378 0.3238 -0.0128 0.0165  -0.0109 28  SER A OG    
95   N  N     . ARG A 36  ? 0.4278 0.3578 0.3314 -0.0036 0.0323  -0.0174 29  ARG A N     
96   C  CA    . ARG A 36  ? 0.4374 0.3612 0.3392 0.0006  0.0317  -0.0237 29  ARG A CA    
97   C  C     . ARG A 36  ? 0.4620 0.3724 0.3502 0.0010  0.0248  -0.0294 29  ARG A C     
98   O  O     . ARG A 36  ? 0.4773 0.3770 0.3619 0.0044  0.0224  -0.0350 29  ARG A O     
99   C  CB    . ARG A 36  ? 0.4511 0.3826 0.3507 0.0074  0.0396  -0.0259 29  ARG A CB    
100  C  CG    . ARG A 36  ? 0.4318 0.3763 0.3475 0.0068  0.0445  -0.0217 29  ARG A CG    
101  C  CD    . ARG A 36  ? 0.4482 0.4063 0.3652 0.0132  0.0527  -0.0233 29  ARG A CD    
102  N  NE    . ARG A 36  ? 0.4316 0.4038 0.3658 0.0109  0.0555  -0.0188 29  ARG A NE    
103  C  CZ    . ARG A 36  ? 0.4293 0.4047 0.3734 0.0160  0.0544  -0.0211 29  ARG A CZ    
104  N  NH1   . ARG A 36  ? 0.4396 0.4006 0.3780 0.0224  0.0495  -0.0268 29  ARG A NH1   
105  N  NH2   . ARG A 36  ? 0.4195 0.4102 0.3788 0.0137  0.0564  -0.0173 29  ARG A NH2   
106  N  N     . LYS A 37  ? 0.4694 0.3786 0.3504 -0.0026 0.0201  -0.0281 30  LYS A N     
107  C  CA    . LYS A 37  ? 0.4973 0.3938 0.3652 -0.0037 0.0119  -0.0340 30  LYS A CA    
108  C  C     . LYS A 37  ? 0.4910 0.3808 0.3685 -0.0101 0.0044  -0.0340 30  LYS A C     
109  O  O     . LYS A 37  ? 0.4646 0.3638 0.3574 -0.0147 0.0045  -0.0282 30  LYS A O     
110  C  CB    . LYS A 37  ? 0.5096 0.4087 0.3683 -0.0064 0.0073  -0.0318 30  LYS A CB    
111  C  CG    . LYS A 37  ? 0.5482 0.4349 0.3884 -0.0068 -0.0011 -0.0391 30  LYS A CG    
112  C  CD    . LYS A 37  ? 0.5679 0.4581 0.3945 -0.0074 -0.0050 -0.0368 30  LYS A CD    
113  C  CE    . LYS A 37  ? 0.5436 0.4458 0.3847 -0.0112 -0.0073 -0.0273 30  LYS A CE    
114  N  NZ    . LYS A 37  ? 0.5673 0.4715 0.3942 -0.0105 -0.0118 -0.0236 30  LYS A NZ    
115  N  N     . CYS A 38  ? 0.5209 0.3939 0.3883 -0.0107 -0.0022 -0.0406 31  CYS A N     
116  C  CA    . CYS A 38  ? 0.5233 0.3894 0.3985 -0.0196 -0.0102 -0.0390 31  CYS A CA    
117  C  C     . CYS A 38  ? 0.5669 0.4137 0.4271 -0.0236 -0.0211 -0.0460 31  CYS A C     
118  O  O     . CYS A 38  ? 0.5975 0.4302 0.4404 -0.0160 -0.0212 -0.0544 31  CYS A O     
119  C  CB    . CYS A 38  ? 0.5152 0.3755 0.3982 -0.0183 -0.0075 -0.0374 31  CYS A CB    
120  S  SG    . CYS A 38  ? 0.5223 0.3762 0.4143 -0.0319 -0.0162 -0.0323 31  CYS A SG    
121  N  N     . ASN A 39  ? 0.5708 0.4189 0.4394 -0.0356 -0.0298 -0.0424 32  ASN A N     
122  C  CA    . ASN A 39  ? 0.6122 0.4452 0.4710 -0.0441 -0.0427 -0.0471 32  ASN A CA    
123  C  C     . ASN A 39  ? 0.6430 0.4503 0.4971 -0.0483 -0.0486 -0.0497 32  ASN A C     
124  O  O     . ASN A 39  ? 0.6870 0.4749 0.5302 -0.0557 -0.0605 -0.0548 32  ASN A O     
125  C  CB    . ASN A 39  ? 0.6028 0.4560 0.4763 -0.0554 -0.0488 -0.0406 32  ASN A CB    
126  C  CG    . ASN A 39  ? 0.5735 0.4445 0.4702 -0.0631 -0.0454 -0.0310 32  ASN A CG    
127  O  OD1   . ASN A 39  ? 0.5416 0.4205 0.4463 -0.0573 -0.0353 -0.0272 32  ASN A OD1   
128  N  ND2   . ASN A 39  ? 0.5878 0.4673 0.4956 -0.0766 -0.0537 -0.0270 32  ASN A ND2   
129  N  N     . LYS A 40  ? 0.6274 0.4312 0.4872 -0.0430 -0.0417 -0.0468 33  LYS A N     
130  C  CA    . LYS A 40  ? 0.6573 0.4365 0.5143 -0.0476 -0.0479 -0.0463 33  LYS A CA    
131  C  C     . LYS A 40  ? 0.6731 0.4346 0.5184 -0.0315 -0.0437 -0.0535 33  LYS A C     
132  O  O     . LYS A 40  ? 0.6644 0.4347 0.5035 -0.0191 -0.0363 -0.0593 33  LYS A O     
133  C  CB    . LYS A 40  ? 0.6308 0.4250 0.5070 -0.0583 -0.0457 -0.0340 33  LYS A CB    
134  C  CG    . LYS A 40  ? 0.6232 0.4379 0.5126 -0.0733 -0.0498 -0.0276 33  LYS A CG    
135  C  CD    . LYS A 40  ? 0.6717 0.4693 0.5513 -0.0842 -0.0639 -0.0324 33  LYS A CD    
136  C  CE    . LYS A 40  ? 0.6757 0.4926 0.5718 -0.1025 -0.0699 -0.0241 33  LYS A CE    
137  N  NZ    . LYS A 40  ? 0.6998 0.5190 0.5913 -0.1077 -0.0802 -0.0296 33  LYS A NZ    
138  N  N     . GLU A 41  ? 0.7051 0.4407 0.5460 -0.0320 -0.0497 -0.0533 34  GLU A N     
139  C  CA    . GLU A 41  ? 0.7349 0.4492 0.5637 -0.0156 -0.0488 -0.0615 34  GLU A CA    
140  C  C     . GLU A 41  ? 0.7393 0.4422 0.5749 -0.0155 -0.0502 -0.0539 34  GLU A C     
141  O  O     . GLU A 41  ? 0.7851 0.4582 0.6091 -0.0066 -0.0562 -0.0593 34  GLU A O     
142  C  CB    . GLU A 41  ? 0.8007 0.4804 0.6066 -0.0136 -0.0603 -0.0741 34  GLU A CB    
143  C  CG    . GLU A 41  ? 0.8056 0.4936 0.6030 -0.0191 -0.0631 -0.0798 34  GLU A CG    
144  C  CD    . GLU A 41  ? 0.8745 0.5291 0.6454 -0.0142 -0.0736 -0.0948 34  GLU A CD    
145  O  OE1   . GLU A 41  ? 0.8826 0.5446 0.6399 -0.0049 -0.0697 -0.1042 34  GLU A OE1   
146  O  OE2   . GLU A 41  ? 0.9247 0.5445 0.6871 -0.0196 -0.0860 -0.0972 34  GLU A OE2   
147  N  N     . CYS A 42  ? 0.6956 0.4217 0.5486 -0.0235 -0.0448 -0.0417 35  CYS A N     
148  C  CA    . CYS A 42  ? 0.6990 0.4177 0.5572 -0.0238 -0.0458 -0.0331 35  CYS A CA    
149  C  C     . CYS A 42  ? 0.7177 0.4242 0.5701 -0.0037 -0.0440 -0.0397 35  CYS A C     
150  O  O     . CYS A 42  ? 0.6912 0.4185 0.5485 0.0091  -0.0344 -0.0445 35  CYS A O     
151  C  CB    . CYS A 42  ? 0.6445 0.3969 0.5204 -0.0306 -0.0369 -0.0223 35  CYS A CB    
152  S  SG    . CYS A 42  ? 0.6222 0.3968 0.5088 -0.0504 -0.0370 -0.0150 35  CYS A SG    
153  N  N     . LEU A 43  ? 0.7692 0.4416 0.6117 -0.0006 -0.0538 -0.0396 36  LEU A N     
154  C  CA    . LEU A 43  ? 0.7992 0.4574 0.6354 0.0211  -0.0540 -0.0480 36  LEU A CA    
155  C  C     . LEU A 43  ? 0.7601 0.4463 0.6118 0.0313  -0.0448 -0.0426 36  LEU A C     
156  O  O     . LEU A 43  ? 0.7686 0.4603 0.6211 0.0503  -0.0404 -0.0506 36  LEU A O     
157  C  CB    . LEU A 43  ? 0.8690 0.4808 0.6909 0.0219  -0.0685 -0.0477 36  LEU A CB    
158  C  CG    . LEU A 43  ? 0.9280 0.5029 0.7305 0.0169  -0.0801 -0.0572 36  LEU A CG    
159  C  CD1   . LEU A 43  ? 0.9983 0.5252 0.7881 0.0142  -0.0955 -0.0534 36  LEU A CD1   
160  C  CD2   . LEU A 43  ? 0.9480 0.5210 0.7391 0.0367  -0.0762 -0.0756 36  LEU A CD2   
161  N  N     . PHE A 44  ? 0.7187 0.4259 0.5828 0.0187  -0.0413 -0.0301 37  PHE A N     
162  C  CA    . PHE A 44  ? 0.6881 0.4189 0.5653 0.0264  -0.0351 -0.0248 37  PHE A CA    
163  C  C     . PHE A 44  ? 0.6308 0.4007 0.5213 0.0265  -0.0225 -0.0262 37  PHE A C     
164  O  O     . PHE A 44  ? 0.6062 0.3977 0.5082 0.0323  -0.0174 -0.0231 37  PHE A O     
165  C  CB    . PHE A 44  ? 0.6892 0.4156 0.5685 0.0146  -0.0399 -0.0108 37  PHE A CB    
166  C  CG    . PHE A 44  ? 0.6745 0.4058 0.5543 -0.0066 -0.0402 -0.0027 37  PHE A CG    
167  C  CD1   . PHE A 44  ? 0.6238 0.3870 0.5142 -0.0136 -0.0309 -0.0023 37  PHE A CD1   
168  C  CD2   . PHE A 44  ? 0.7168 0.4209 0.5871 -0.0199 -0.0501 0.0047  37  PHE A CD2   
169  C  CE1   . PHE A 44  ? 0.6142 0.3853 0.5071 -0.0310 -0.0308 0.0041  37  PHE A CE1   
170  C  CE2   . PHE A 44  ? 0.7059 0.4204 0.5795 -0.0397 -0.0494 0.0127  37  PHE A CE2   
171  C  CZ    . PHE A 44  ? 0.6545 0.4037 0.5399 -0.0444 -0.0395 0.0118  37  PHE A CZ    
172  N  N     . CYS A 45  ? 0.6145 0.3921 0.5029 0.0195  -0.0190 -0.0301 38  CYS A N     
173  C  CA    . CYS A 45  ? 0.5642 0.3741 0.4638 0.0155  -0.0092 -0.0283 38  CYS A CA    
174  C  C     . CYS A 45  ? 0.5460 0.3779 0.4557 0.0277  -0.0013 -0.0302 38  CYS A C     
175  O  O     . CYS A 45  ? 0.5656 0.3978 0.4726 0.0412  0.0014  -0.0380 38  CYS A O     
176  C  CB    . CYS A 45  ? 0.5635 0.3740 0.4563 0.0112  -0.0081 -0.0340 38  CYS A CB    
177  S  SG    . CYS A 45  ? 0.5119 0.3558 0.4158 0.0064  0.0018  -0.0312 38  CYS A SG    
178  N  N     . PHE A 46  ? 0.5095 0.3632 0.4313 0.0223  0.0030  -0.0233 39  PHE A N     
179  C  CA    . PHE A 46  ? 0.4948 0.3705 0.4280 0.0308  0.0090  -0.0239 39  PHE A CA    
180  C  C     . PHE A 46  ? 0.4639 0.3620 0.4032 0.0268  0.0175  -0.0246 39  PHE A C     
181  O  O     . PHE A 46  ? 0.4512 0.3691 0.4013 0.0300  0.0223  -0.0236 39  PHE A O     
182  C  CB    . PHE A 46  ? 0.4871 0.3690 0.4283 0.0294  0.0060  -0.0168 39  PHE A CB    
183  C  CG    . PHE A 46  ? 0.4615 0.3498 0.4046 0.0161  0.0059  -0.0097 39  PHE A CG    
184  C  CD1   . PHE A 46  ? 0.4407 0.3337 0.3826 0.0065  0.0093  -0.0095 39  PHE A CD1   
185  C  CD2   . PHE A 46  ? 0.4641 0.3542 0.4093 0.0147  0.0020  -0.0034 39  PHE A CD2   
186  C  CE1   . PHE A 46  ? 0.4223 0.3235 0.3665 -0.0029 0.0100  -0.0042 39  PHE A CE1   
187  C  CE2   . PHE A 46  ? 0.4473 0.3438 0.3919 0.0038  0.0027  0.0020  39  PHE A CE2   
188  C  CZ    . PHE A 46  ? 0.4263 0.3293 0.3712 -0.0042 0.0073  0.0010  39  PHE A CZ    
189  N  N     . HIS A 47  ? 0.4577 0.3521 0.3901 0.0200  0.0185  -0.0260 40  HIS A N     
190  C  CA    . HIS A 47  ? 0.4368 0.3484 0.3725 0.0172  0.0254  -0.0258 40  HIS A CA    
191  C  C     . HIS A 47  ? 0.4542 0.3578 0.3770 0.0184  0.0258  -0.0312 40  HIS A C     
192  O  O     . HIS A 47  ? 0.4485 0.3470 0.3668 0.0105  0.0228  -0.0299 40  HIS A O     
193  C  CB    . HIS A 47  ? 0.4072 0.3274 0.3499 0.0070  0.0256  -0.0197 40  HIS A CB    
194  C  CG    . HIS A 47  ? 0.3915 0.3272 0.3391 0.0052  0.0316  -0.0184 40  HIS A CG    
195  N  ND1   . HIS A 47  ? 0.3844 0.3346 0.3422 0.0066  0.0351  -0.0166 40  HIS A ND1   
196  C  CD2   . HIS A 47  ? 0.3894 0.3270 0.3323 0.0025  0.0339  -0.0185 40  HIS A CD2   
197  C  CE1   . HIS A 47  ? 0.3781 0.3373 0.3372 0.0030  0.0395  -0.0148 40  HIS A CE1   
198  N  NE2   . HIS A 47  ? 0.3812 0.3322 0.3306 0.0011  0.0389  -0.0157 40  HIS A NE2   
199  N  N     . THR A 48  ? 0.4797 0.3833 0.3966 0.0291  0.0292  -0.0376 41  THR A N     
200  C  CA    . THR A 48  ? 0.5111 0.4007 0.4111 0.0331  0.0274  -0.0452 41  THR A CA    
201  C  C     . THR A 48  ? 0.5076 0.4094 0.4012 0.0306  0.0333  -0.0452 41  THR A C     
202  O  O     . THR A 48  ? 0.4856 0.4068 0.3884 0.0274  0.0399  -0.0395 41  THR A O     
203  C  CB    . THR A 48  ? 0.5488 0.4312 0.4434 0.0482  0.0281  -0.0535 41  THR A CB    
204  O  OG1   . THR A 48  ? 0.5461 0.4539 0.4502 0.0563  0.0380  -0.0536 41  THR A OG1   
205  C  CG2   . THR A 48  ? 0.5596 0.4242 0.4576 0.0501  0.0198  -0.0523 41  THR A CG2   
206  N  N     . ALA A 49  ? 0.5372 0.4257 0.4131 0.0325  0.0302  -0.0519 42  ALA A N     
207  C  CA    . ALA A 49  ? 0.5405 0.4360 0.4061 0.0290  0.0331  -0.0511 42  ALA A CA    
208  C  C     . ALA A 49  ? 0.5628 0.4732 0.4211 0.0383  0.0436  -0.0546 42  ALA A C     
209  O  O     . ALA A 49  ? 0.5986 0.5028 0.4374 0.0435  0.0440  -0.0618 42  ALA A O     
210  C  CB    . ALA A 49  ? 0.5643 0.4401 0.4140 0.0252  0.0234  -0.0562 42  ALA A CB    
211  N  N     . THR A 50  ? 0.5448 0.4768 0.4186 0.0394  0.0521  -0.0491 43  THR A N     
212  C  CA    . THR A 50  ? 0.5661 0.5189 0.4380 0.0469  0.0636  -0.0505 43  THR A CA    
213  C  C     . THR A 50  ? 0.5683 0.5334 0.4321 0.0394  0.0694  -0.0436 43  THR A C     
214  O  O     . THR A 50  ? 0.5963 0.5777 0.4527 0.0446  0.0792  -0.0448 43  THR A O     
215  C  CB    . THR A 50  ? 0.5507 0.5232 0.4450 0.0500  0.0688  -0.0469 43  THR A CB    
216  O  OG1   . THR A 50  ? 0.5109 0.4859 0.4199 0.0378  0.0654  -0.0373 43  THR A OG1   
217  C  CG2   . THR A 50  ? 0.5648 0.5268 0.4631 0.0618  0.0643  -0.0545 43  THR A CG2   
218  N  N     . THR A 51  ? 0.5433 0.5023 0.4090 0.0278  0.0639  -0.0357 44  THR A N     
219  C  CA    . THR A 51  ? 0.5507 0.5152 0.4065 0.0207  0.0665  -0.0281 44  THR A CA    
220  C  C     . THR A 51  ? 0.5402 0.4875 0.3898 0.0142  0.0555  -0.0263 44  THR A C     
221  O  O     . THR A 51  ? 0.5236 0.4587 0.3797 0.0134  0.0474  -0.0296 44  THR A O     
222  C  CB    . THR A 51  ? 0.5340 0.5153 0.4047 0.0125  0.0726  -0.0167 44  THR A CB    
223  O  OG1   . THR A 51  ? 0.5012 0.4734 0.3837 0.0046  0.0650  -0.0113 44  THR A OG1   
224  C  CG2   . THR A 51  ? 0.5310 0.5323 0.4190 0.0158  0.0806  -0.0167 44  THR A CG2   
225  N  N     . SER A 52  ? 0.5540 0.5019 0.3913 0.0095  0.0552  -0.0200 45  SER A N     
226  C  CA    . SER A 52  ? 0.5468 0.4832 0.3808 0.0040  0.0449  -0.0165 45  SER A CA    
227  C  C     . SER A 52  ? 0.5347 0.4753 0.3762 -0.0029 0.0456  -0.0046 45  SER A C     
228  O  O     . SER A 52  ? 0.5356 0.4688 0.3737 -0.0057 0.0377  -0.0006 45  SER A O     
229  C  CB    . SER A 52  ? 0.5843 0.5127 0.3935 0.0064  0.0401  -0.0210 45  SER A CB    
230  O  OG    . SER A 52  ? 0.6167 0.5543 0.4092 0.0076  0.0486  -0.0172 45  SER A OG    
231  N  N     . HIS A 53  ? 0.5274 0.4793 0.3798 -0.0057 0.0539  0.0009  46  HIS A N     
232  C  CA    . HIS A 53  ? 0.5228 0.4739 0.3815 -0.0131 0.0532  0.0118  46  HIS A CA    
233  C  C     . HIS A 53  ? 0.4922 0.4341 0.3656 -0.0145 0.0448  0.0114  46  HIS A C     
234  O  O     . HIS A 53  ? 0.4678 0.4116 0.3540 -0.0124 0.0444  0.0054  46  HIS A O     
235  C  CB    . HIS A 53  ? 0.5226 0.4877 0.3928 -0.0177 0.0623  0.0171  46  HIS A CB    
236  C  CG    . HIS A 53  ? 0.5242 0.4833 0.3997 -0.0265 0.0598  0.0276  46  HIS A CG    
237  N  ND1   . HIS A 53  ? 0.5568 0.5111 0.4183 -0.0322 0.0599  0.0382  46  HIS A ND1   
238  C  CD2   . HIS A 53  ? 0.5025 0.4563 0.3938 -0.0301 0.0557  0.0288  46  HIS A CD2   
239  C  CE1   . HIS A 53  ? 0.5555 0.4996 0.4253 -0.0390 0.0555  0.0454  46  HIS A CE1   
240  N  NE2   . HIS A 53  ? 0.5227 0.4672 0.4106 -0.0376 0.0533  0.0390  46  HIS A NE2   
241  N  N     . VAL A 54  ? 0.4991 0.4318 0.3697 -0.0172 0.0386  0.0181  47  VAL A N     
242  C  CA    . VAL A 54  ? 0.4794 0.4053 0.3634 -0.0178 0.0324  0.0191  47  VAL A CA    
243  C  C     . VAL A 54  ? 0.4991 0.4167 0.3807 -0.0225 0.0313  0.0290  47  VAL A C     
244  O  O     . VAL A 54  ? 0.5300 0.4429 0.3963 -0.0241 0.0303  0.0361  47  VAL A O     
245  C  CB    . VAL A 54  ? 0.4752 0.3968 0.3585 -0.0135 0.0233  0.0153  47  VAL A CB    
246  C  CG1   . VAL A 54  ? 0.4585 0.3771 0.3563 -0.0122 0.0184  0.0151  47  VAL A CG1   
247  C  CG2   . VAL A 54  ? 0.4662 0.3921 0.3488 -0.0112 0.0230  0.0065  47  VAL A CG2   
248  N  N     . GLU A 55  ? 0.4871 0.4002 0.3818 -0.0248 0.0301  0.0297  48  GLU A N     
249  C  CA    . GLU A 55  ? 0.5123 0.4115 0.4040 -0.0292 0.0267  0.0384  48  GLU A CA    
250  C  C     . GLU A 55  ? 0.5309 0.4172 0.4144 -0.0236 0.0174  0.0413  48  GLU A C     
251  O  O     . GLU A 55  ? 0.5161 0.4053 0.4038 -0.0165 0.0126  0.0352  48  GLU A O     
252  C  CB    . GLU A 55  ? 0.4999 0.3939 0.4057 -0.0314 0.0253  0.0358  48  GLU A CB    
253  C  CG    . GLU A 55  ? 0.4919 0.3979 0.4060 -0.0386 0.0326  0.0357  48  GLU A CG    
254  C  CD    . GLU A 55  ? 0.5238 0.4311 0.4320 -0.0488 0.0370  0.0463  48  GLU A CD    
255  O  OE1   . GLU A 55  ? 0.5541 0.4434 0.4558 -0.0535 0.0318  0.0542  48  GLU A OE1   
256  O  OE2   . GLU A 55  ? 0.5233 0.4497 0.4331 -0.0518 0.0457  0.0471  48  GLU A OE2   
257  N  N     . LYS A 56  ? 0.5689 0.4411 0.4408 -0.0275 0.0142  0.0520  49  LYS A N     
258  C  CA    . LYS A 56  ? 0.5930 0.4494 0.4590 -0.0211 0.0036  0.0559  49  LYS A CA    
259  C  C     . LYS A 56  ? 0.5798 0.4287 0.4607 -0.0146 -0.0016 0.0492  49  LYS A C     
260  O  O     . LYS A 56  ? 0.5711 0.4167 0.4606 -0.0187 0.0012  0.0466  49  LYS A O     
261  C  CB    . LYS A 56  ? 0.6421 0.4809 0.4925 -0.0278 0.0010  0.0700  49  LYS A CB    
262  C  CG    . LYS A 56  ? 0.6639 0.5115 0.4963 -0.0337 0.0068  0.0774  49  LYS A CG    
263  C  CD    . LYS A 56  ? 0.7173 0.5485 0.5335 -0.0428 0.0054  0.0935  49  LYS A CD    
264  C  CE    . LYS A 56  ? 0.7238 0.5542 0.5477 -0.0557 0.0122  0.0986  49  LYS A CE    
265  N  NZ    . LYS A 56  ? 0.7739 0.6017 0.5802 -0.0681 0.0165  0.1147  49  LYS A NZ    
266  N  N     . PRO A 57  ? 0.5826 0.4300 0.4667 -0.0038 -0.0097 0.0459  50  PRO A N     
267  C  CA    . PRO A 57  ? 0.5756 0.4191 0.4732 0.0045  -0.0137 0.0385  50  PRO A CA    
268  C  C     . PRO A 57  ? 0.6015 0.4218 0.4980 0.0024  -0.0162 0.0408  50  PRO A C     
269  O  O     . PRO A 57  ? 0.5856 0.4069 0.4920 0.0032  -0.0138 0.0327  50  PRO A O     
270  C  CB    . PRO A 57  ? 0.5941 0.4378 0.4916 0.0162  -0.0233 0.0391  50  PRO A CB    
271  C  CG    . PRO A 57  ? 0.5878 0.4454 0.4775 0.0130  -0.0225 0.0415  50  PRO A CG    
272  C  CD    . PRO A 57  ? 0.5960 0.4483 0.4716 0.0013  -0.0157 0.0485  50  PRO A CD    
273  N  N     . GLU A 58  ? 0.6466 0.4448 0.5295 -0.0006 -0.0218 0.0519  51  GLU A N     
274  C  CA    . GLU A 58  ? 0.6819 0.4528 0.5615 -0.0047 -0.0260 0.0553  51  GLU A CA    
275  C  C     . GLU A 58  ? 0.6634 0.4393 0.5491 -0.0175 -0.0182 0.0529  51  GLU A C     
276  O  O     . GLU A 58  ? 0.6727 0.4349 0.5633 -0.0174 -0.0211 0.0472  51  GLU A O     
277  C  CB    . GLU A 58  ? 0.7382 0.4841 0.6001 -0.0094 -0.0331 0.0705  51  GLU A CB    
278  C  CG    . GLU A 58  ? 0.7706 0.5026 0.6277 0.0059  -0.0450 0.0722  51  GLU A CG    
279  C  CD    . GLU A 58  ? 0.7671 0.4956 0.6375 0.0222  -0.0502 0.0592  51  GLU A CD    
280  O  OE1   . GLU A 58  ? 0.7934 0.4975 0.6637 0.0225  -0.0539 0.0561  51  GLU A OE1   
281  O  OE2   . GLU A 58  ? 0.7410 0.4924 0.6219 0.0340  -0.0503 0.0517  51  GLU A OE2   
282  N  N     . ASN A 59  ? 0.6397 0.4364 0.5255 -0.0273 -0.0088 0.0559  52  ASN A N     
283  C  CA    . ASN A 59  ? 0.6241 0.4302 0.5177 -0.0388 -0.0017 0.0544  52  ASN A CA    
284  C  C     . ASN A 59  ? 0.5806 0.4023 0.4885 -0.0328 0.0013  0.0407  52  ASN A C     
285  O  O     . ASN A 59  ? 0.5802 0.3977 0.4947 -0.0372 0.0008  0.0363  52  ASN A O     
286  C  CB    . ASN A 59  ? 0.6198 0.4451 0.5093 -0.0488 0.0076  0.0619  52  ASN A CB    
287  C  CG    . ASN A 59  ? 0.6701 0.4812 0.5452 -0.0593 0.0062  0.0773  52  ASN A CG    
288  O  OD1   . ASN A 59  ? 0.7101 0.4933 0.5791 -0.0614 -0.0024 0.0832  52  ASN A OD1   
289  N  ND2   . ASN A 59  ? 0.6742 0.5032 0.5422 -0.0658 0.0148  0.0842  52  ASN A ND2   
290  N  N     . ALA A 60  ? 0.5487 0.3876 0.4604 -0.0237 0.0036  0.0343  53  ALA A N     
291  C  CA    . ALA A 60  ? 0.5148 0.3665 0.4382 -0.0184 0.0058  0.0231  53  ALA A CA    
292  C  C     . ALA A 60  ? 0.5305 0.3669 0.4567 -0.0117 -0.0002 0.0165  53  ALA A C     
293  O  O     . ALA A 60  ? 0.5193 0.3585 0.4515 -0.0128 0.0012  0.0094  53  ALA A O     
294  C  CB    . ALA A 60  ? 0.4880 0.3576 0.4143 -0.0113 0.0077  0.0190  53  ALA A CB    
295  N  N     . LYS A 61  ? 0.5617 0.3810 0.4826 -0.0033 -0.0076 0.0181  54  LYS A N     
296  C  CA    . LYS A 61  ? 0.5838 0.3876 0.5061 0.0057  -0.0133 0.0103  54  LYS A CA    
297  C  C     . LYS A 61  ? 0.6109 0.3930 0.5290 -0.0034 -0.0163 0.0103  54  LYS A C     
298  O  O     . LYS A 61  ? 0.6175 0.3935 0.5376 0.0011  -0.0181 0.0003  54  LYS A O     
299  C  CB    . LYS A 61  ? 0.6207 0.4082 0.5379 0.0178  -0.0220 0.0128  54  LYS A CB    
300  C  CG    . LYS A 61  ? 0.6022 0.4117 0.5266 0.0295  -0.0218 0.0101  54  LYS A CG    
301  C  CD    . LYS A 61  ? 0.6440 0.4382 0.5636 0.0414  -0.0318 0.0144  54  LYS A CD    
302  C  CE    . LYS A 61  ? 0.6269 0.4474 0.5559 0.0512  -0.0323 0.0123  54  LYS A CE    
303  N  NZ    . LYS A 61  ? 0.6691 0.4790 0.5981 0.0670  -0.0428 0.0136  54  LYS A NZ    
304  N  N     . ARG A 62  ? 0.6309 0.4028 0.5428 -0.0167 -0.0167 0.0216  55  ARG A N     
305  C  CA    . ARG A 62  ? 0.6607 0.4134 0.5700 -0.0295 -0.0202 0.0238  55  ARG A CA    
306  C  C     . ARG A 62  ? 0.6257 0.3997 0.5452 -0.0360 -0.0141 0.0168  55  ARG A C     
307  O  O     . ARG A 62  ? 0.6416 0.4037 0.5614 -0.0379 -0.0184 0.0096  55  ARG A O     
308  C  CB    . ARG A 62  ? 0.6850 0.4315 0.5878 -0.0448 -0.0195 0.0394  55  ARG A CB    
309  C  CG    . ARG A 62  ? 0.7364 0.4573 0.6356 -0.0591 -0.0260 0.0439  55  ARG A CG    
310  C  CD    . ARG A 62  ? 0.7760 0.4837 0.6651 -0.0720 -0.0274 0.0615  55  ARG A CD    
311  N  NE    . ARG A 62  ? 0.7521 0.4904 0.6460 -0.0846 -0.0163 0.0704  55  ARG A NE    
312  C  CZ    . ARG A 62  ? 0.7442 0.5001 0.6488 -0.0987 -0.0112 0.0713  55  ARG A CZ    
313  N  NH1   . ARG A 62  ? 0.7567 0.5008 0.6673 -0.1044 -0.0173 0.0646  55  ARG A NH1   
314  N  NH2   . ARG A 62  ? 0.7274 0.5133 0.6364 -0.1065 -0.0004 0.0785  55  ARG A NH2   
315  N  N     . GLY A 63  ? 0.5836 0.3866 0.5096 -0.0381 -0.0052 0.0186  56  GLY A N     
316  C  CA    . GLY A 63  ? 0.5532 0.3763 0.4887 -0.0425 -0.0002 0.0129  56  GLY A CA    
317  C  C     . GLY A 63  ? 0.5395 0.3648 0.4774 -0.0321 -0.0017 0.0001  56  GLY A C     
318  O  O     . GLY A 63  ? 0.5414 0.3671 0.4819 -0.0363 -0.0032 -0.0054 56  GLY A O     
319  N  N     . LEU A 64  ? 0.5290 0.3580 0.4660 -0.0189 -0.0012 -0.0041 57  LEU A N     
320  C  CA    . LEU A 64  ? 0.5204 0.3554 0.4594 -0.0087 -0.0009 -0.0153 57  LEU A CA    
321  C  C     . LEU A 64  ? 0.5624 0.3722 0.4944 -0.0056 -0.0083 -0.0226 57  LEU A C     
322  O  O     . LEU A 64  ? 0.5620 0.3753 0.4934 -0.0040 -0.0081 -0.0316 57  LEU A O     
323  C  CB    . LEU A 64  ? 0.5077 0.3541 0.4491 0.0031  0.0008  -0.0163 57  LEU A CB    
324  C  CG    . LEU A 64  ? 0.4692 0.3393 0.4162 -0.0001 0.0072  -0.0120 57  LEU A CG    
325  C  CD1   . LEU A 64  ? 0.4658 0.3441 0.4148 0.0082  0.0065  -0.0106 57  LEU A CD1   
326  C  CD2   . LEU A 64  ? 0.4435 0.3304 0.3953 -0.0018 0.0119  -0.0174 57  LEU A CD2   
327  N  N     . THR A 65  ? 0.6035 0.3861 0.5285 -0.0062 -0.0155 -0.0182 58  THR A N     
328  C  CA    . THR A 65  ? 0.6537 0.4056 0.5700 -0.0039 -0.0244 -0.0250 58  THR A CA    
329  C  C     . THR A 65  ? 0.6628 0.4097 0.5785 -0.0184 -0.0268 -0.0269 58  THR A C     
330  O  O     . THR A 65  ? 0.6839 0.4210 0.5943 -0.0145 -0.0308 -0.0386 58  THR A O     
331  C  CB    . THR A 65  ? 0.7015 0.4220 0.6095 -0.0021 -0.0327 -0.0179 58  THR A CB    
332  O  OG1   . THR A 65  ? 0.6967 0.4237 0.6061 0.0131  -0.0321 -0.0173 58  THR A OG1   
333  C  CG2   . THR A 65  ? 0.7626 0.4454 0.6598 0.0013  -0.0436 -0.0257 58  THR A CG2   
334  N  N     . LEU A 66  ? 0.6505 0.4064 0.5718 -0.0347 -0.0244 -0.0160 59  LEU A N     
335  C  CA    . LEU A 66  ? 0.6568 0.4153 0.5817 -0.0497 -0.0266 -0.0163 59  LEU A CA    
336  C  C     . LEU A 66  ? 0.6240 0.4056 0.5532 -0.0452 -0.0226 -0.0262 59  LEU A C     
337  O  O     . LEU A 66  ? 0.6450 0.4192 0.5710 -0.0495 -0.0284 -0.0337 59  LEU A O     
338  C  CB    . LEU A 66  ? 0.6437 0.4182 0.5771 -0.0650 -0.0218 -0.0022 59  LEU A CB    
339  C  CG    . LEU A 66  ? 0.6817 0.4357 0.6095 -0.0737 -0.0252 0.0104  59  LEU A CG    
340  C  CD1   . LEU A 66  ? 0.6688 0.4464 0.6057 -0.0886 -0.0181 0.0231  59  LEU A CD1   
341  C  CD2   . LEU A 66  ? 0.7443 0.4599 0.6630 -0.0807 -0.0377 0.0085  59  LEU A CD2   
342  N  N     . LEU A 67  ? 0.5771 0.3857 0.5123 -0.0374 -0.0137 -0.0257 60  LEU A N     
343  C  CA    . LEU A 67  ? 0.5516 0.3799 0.4889 -0.0332 -0.0103 -0.0334 60  LEU A CA    
344  C  C     . LEU A 67  ? 0.5770 0.3927 0.5038 -0.0220 -0.0139 -0.0463 60  LEU A C     
345  O  O     . LEU A 67  ? 0.5843 0.4029 0.5073 -0.0239 -0.0162 -0.0533 60  LEU A O     
346  C  CB    . LEU A 67  ? 0.5060 0.3601 0.4499 -0.0274 -0.0013 -0.0300 60  LEU A CB    
347  C  CG    . LEU A 67  ? 0.4815 0.3516 0.4343 -0.0360 0.0033  -0.0200 60  LEU A CG    
348  C  CD1   . LEU A 67  ? 0.4509 0.3355 0.4061 -0.0289 0.0098  -0.0172 60  LEU A CD1   
349  C  CD2   . LEU A 67  ? 0.4705 0.3563 0.4300 -0.0435 0.0035  -0.0201 60  LEU A CD2   
350  N  N     . LYS A 68  ? 0.5945 0.3976 0.5162 -0.0094 -0.0146 -0.0498 61  LYS A N     
351  C  CA    . LYS A 68  ? 0.6260 0.4182 0.5377 0.0036  -0.0172 -0.0633 61  LYS A CA    
352  C  C     . LYS A 68  ? 0.6746 0.4396 0.5754 -0.0022 -0.0272 -0.0709 61  LYS A C     
353  O  O     . LYS A 68  ? 0.6913 0.4568 0.5832 0.0021  -0.0285 -0.0826 61  LYS A O     
354  C  CB    . LYS A 68  ? 0.6463 0.4270 0.5563 0.0182  -0.0182 -0.0647 61  LYS A CB    
355  C  CG    . LYS A 68  ? 0.6926 0.4576 0.5916 0.0340  -0.0219 -0.0797 61  LYS A CG    
356  C  CD    . LYS A 68  ? 0.6771 0.4701 0.5767 0.0457  -0.0134 -0.0884 61  LYS A CD    
357  C  CE    . LYS A 68  ? 0.7310 0.5079 0.6163 0.0594  -0.0169 -0.1052 61  LYS A CE    
358  N  NZ    . LYS A 68  ? 0.7210 0.5290 0.6063 0.0708  -0.0070 -0.1129 61  LYS A NZ    
359  N  N     . GLN A 69  ? 0.7022 0.4429 0.6024 -0.0127 -0.0346 -0.0641 62  GLN A N     
360  C  CA    . GLN A 69  ? 0.7559 0.4662 0.6465 -0.0218 -0.0462 -0.0694 62  GLN A CA    
361  C  C     . GLN A 69  ? 0.7433 0.4697 0.6374 -0.0355 -0.0474 -0.0703 62  GLN A C     
362  O  O     . GLN A 69  ? 0.7853 0.4936 0.6689 -0.0389 -0.0565 -0.0803 62  GLN A O     
363  C  CB    . GLN A 69  ? 0.7866 0.4711 0.6778 -0.0332 -0.0529 -0.0578 62  GLN A CB    
364  C  CG    . GLN A 69  ? 0.8175 0.4772 0.7013 -0.0184 -0.0559 -0.0583 62  GLN A CG    
365  C  CD    . GLN A 69  ? 0.8495 0.4837 0.7318 -0.0283 -0.0620 -0.0444 62  GLN A CD    
366  O  OE1   . GLN A 69  ? 0.8908 0.4965 0.7643 -0.0168 -0.0682 -0.0454 62  GLN A OE1   
367  N  NE2   . GLN A 69  ? 0.8358 0.4804 0.7261 -0.0487 -0.0603 -0.0310 62  GLN A NE2   
368  N  N     . ALA A 70  ? 0.6899 0.4498 0.5977 -0.0419 -0.0392 -0.0612 63  ALA A N     
369  C  CA    . ALA A 70  ? 0.6777 0.4563 0.5902 -0.0522 -0.0406 -0.0619 63  ALA A CA    
370  C  C     . ALA A 70  ? 0.6646 0.4588 0.5696 -0.0412 -0.0371 -0.0722 63  ALA A C     
371  O  O     . ALA A 70  ? 0.6608 0.4685 0.5669 -0.0479 -0.0398 -0.0736 63  ALA A O     
372  C  CB    . ALA A 70  ? 0.6366 0.4416 0.5663 -0.0622 -0.0343 -0.0481 63  ALA A CB    
373  N  N     . GLY A 71  ? 0.6618 0.4562 0.5594 -0.0248 -0.0315 -0.0788 64  GLY A N     
374  C  CA    . GLY A 71  ? 0.6597 0.4683 0.5478 -0.0147 -0.0276 -0.0884 64  GLY A CA    
375  C  C     . GLY A 71  ? 0.6102 0.4492 0.5063 -0.0084 -0.0158 -0.0822 64  GLY A C     
376  O  O     . GLY A 71  ? 0.6054 0.4606 0.4951 -0.0038 -0.0118 -0.0864 64  GLY A O     
377  N  N     . MET A 72  ? 0.5790 0.4246 0.4876 -0.0087 -0.0107 -0.0721 65  MET A N     
378  C  CA    . MET A 72  ? 0.5393 0.4097 0.4550 -0.0036 -0.0012 -0.0668 65  MET A CA    
379  C  C     . MET A 72  ? 0.5544 0.4288 0.4632 0.0109  0.0032  -0.0753 65  MET A C     
380  O  O     . MET A 72  ? 0.5826 0.4406 0.4880 0.0196  0.0007  -0.0808 65  MET A O     
381  C  CB    . MET A 72  ? 0.5115 0.3851 0.4393 -0.0066 0.0017  -0.0559 65  MET A CB    
382  C  CG    . MET A 72  ? 0.4754 0.3718 0.4100 -0.0030 0.0098  -0.0507 65  MET A CG    
383  S  SD    . MET A 72  ? 0.4480 0.3476 0.3935 -0.0069 0.0124  -0.0391 65  MET A SD    
384  C  CE    . MET A 72  ? 0.4766 0.3573 0.4189 0.0015  0.0088  -0.0414 65  MET A CE    
385  N  N     . LYS A 73  ? 0.5384 0.4358 0.4460 0.0133  0.0099  -0.0753 66  LYS A N     
386  C  CA    . LYS A 73  ? 0.5507 0.4617 0.4540 0.0255  0.0166  -0.0816 66  LYS A CA    
387  C  C     . LYS A 73  ? 0.5162 0.4501 0.4324 0.0261  0.0243  -0.0727 66  LYS A C     
388  O  O     . LYS A 73  ? 0.5250 0.4695 0.4447 0.0364  0.0289  -0.0757 66  LYS A O     
389  C  CB    . LYS A 73  ? 0.5682 0.4889 0.4578 0.0255  0.0182  -0.0875 66  LYS A CB    
390  C  CG    . LYS A 73  ? 0.6101 0.5081 0.4845 0.0250  0.0093  -0.0983 66  LYS A CG    
391  C  CD    . LYS A 73  ? 0.6363 0.5439 0.4932 0.0273  0.0107  -0.1057 66  LYS A CD    
392  C  CE    . LYS A 73  ? 0.6849 0.5681 0.5247 0.0270  0.0004  -0.1183 66  LYS A CE    
393  N  NZ    . LYS A 73  ? 0.7088 0.6033 0.5301 0.0272  0.0011  -0.1237 66  LYS A NZ    
394  N  N     . LYS A 74  ? 0.4820 0.4230 0.4054 0.0155  0.0248  -0.0622 67  LYS A N     
395  C  CA    . LYS A 74  ? 0.4542 0.4138 0.3876 0.0138  0.0305  -0.0540 67  LYS A CA    
396  C  C     . LYS A 74  ? 0.4276 0.3807 0.3701 0.0068  0.0279  -0.0455 67  LYS A C     
397  O  O     . LYS A 74  ? 0.4211 0.3666 0.3628 -0.0002 0.0245  -0.0429 67  LYS A O     
398  C  CB    . LYS A 74  ? 0.4478 0.4240 0.3772 0.0088  0.0345  -0.0502 67  LYS A CB    
399  C  CG    . LYS A 74  ? 0.4257 0.4180 0.3645 0.0048  0.0390  -0.0412 67  LYS A CG    
400  C  CD    . LYS A 74  ? 0.4313 0.4391 0.3642 0.0001  0.0432  -0.0368 67  LYS A CD    
401  C  CE    . LYS A 74  ? 0.4177 0.4385 0.3595 -0.0054 0.0464  -0.0278 67  LYS A CE    
402  N  NZ    . LYS A 74  ? 0.3976 0.4073 0.3421 -0.0130 0.0419  -0.0205 67  LYS A NZ    
403  N  N     . ILE A 75  ? 0.4154 0.3751 0.3664 0.0091  0.0300  -0.0415 68  ILE A N     
404  C  CA    . ILE A 75  ? 0.3944 0.3502 0.3517 0.0037  0.0285  -0.0341 68  ILE A CA    
405  C  C     . ILE A 75  ? 0.3776 0.3495 0.3406 0.0010  0.0320  -0.0287 68  ILE A C     
406  O  O     . ILE A 75  ? 0.3833 0.3689 0.3503 0.0049  0.0347  -0.0297 68  ILE A O     
407  C  CB    . ILE A 75  ? 0.4051 0.3477 0.3639 0.0079  0.0250  -0.0342 68  ILE A CB    
408  C  CG1   . ILE A 75  ? 0.3892 0.3284 0.3513 0.0024  0.0240  -0.0266 68  ILE A CG1   
409  C  CG2   . ILE A 75  ? 0.4186 0.3685 0.3812 0.0180  0.0257  -0.0375 68  ILE A CG2   
410  C  CD1   . ILE A 75  ? 0.3836 0.3156 0.3441 -0.0054 0.0231  -0.0236 68  ILE A CD1   
411  N  N     . ASN A 76  ? 0.3613 0.3316 0.3251 -0.0058 0.0314  -0.0232 69  ASN A N     
412  C  CA    . ASN A 76  ? 0.3515 0.3303 0.3190 -0.0095 0.0326  -0.0184 69  ASN A CA    
413  C  C     . ASN A 76  ? 0.3435 0.3140 0.3127 -0.0106 0.0302  -0.0156 69  ASN A C     
414  O  O     . ASN A 76  ? 0.3391 0.3012 0.3061 -0.0126 0.0294  -0.0145 69  ASN A O     
415  C  CB    . ASN A 76  ? 0.3490 0.3298 0.3130 -0.0149 0.0331  -0.0151 69  ASN A CB    
416  C  CG    . ASN A 76  ? 0.3482 0.3345 0.3144 -0.0200 0.0333  -0.0100 69  ASN A CG    
417  O  OD1   . ASN A 76  ? 0.3544 0.3531 0.3250 -0.0206 0.0351  -0.0093 69  ASN A OD1   
418  N  ND2   . ASN A 76  ? 0.3456 0.3234 0.3094 -0.0237 0.0310  -0.0065 69  ASN A ND2   
419  N  N     . PHE A 77  ? 0.3448 0.3205 0.3180 -0.0096 0.0292  -0.0144 70  PHE A N     
420  C  CA    . PHE A 77  ? 0.3424 0.3118 0.3142 -0.0110 0.0267  -0.0119 70  PHE A CA    
421  C  C     . PHE A 77  ? 0.3391 0.3084 0.3094 -0.0166 0.0260  -0.0095 70  PHE A C     
422  O  O     . PHE A 77  ? 0.3427 0.3204 0.3163 -0.0202 0.0256  -0.0081 70  PHE A O     
423  C  CB    . PHE A 77  ? 0.3513 0.3248 0.3267 -0.0067 0.0239  -0.0120 70  PHE A CB    
424  C  CG    . PHE A 77  ? 0.3621 0.3289 0.3369 0.0000  0.0229  -0.0141 70  PHE A CG    
425  C  CD1   . PHE A 77  ? 0.3682 0.3202 0.3368 0.0000  0.0210  -0.0120 70  PHE A CD1   
426  C  CD2   . PHE A 77  ? 0.3727 0.3472 0.3520 0.0065  0.0238  -0.0182 70  PHE A CD2   
427  C  CE1   . PHE A 77  ? 0.3856 0.3267 0.3522 0.0050  0.0186  -0.0131 70  PHE A CE1   
428  C  CE2   . PHE A 77  ? 0.3903 0.3534 0.3671 0.0138  0.0216  -0.0211 70  PHE A CE2   
429  C  CZ    . PHE A 77  ? 0.3973 0.3418 0.3676 0.0123  0.0183  -0.0182 70  PHE A CZ    
430  N  N     . ALA A 78  ? 0.3371 0.2966 0.3022 -0.0173 0.0258  -0.0091 71  ALA A N     
431  C  CA    . ALA A 78  ? 0.3409 0.2950 0.3023 -0.0202 0.0245  -0.0084 71  ALA A CA    
432  C  C     . ALA A 78  ? 0.3468 0.2933 0.3019 -0.0181 0.0239  -0.0094 71  ALA A C     
433  O  O     . ALA A 78  ? 0.3493 0.2959 0.3026 -0.0164 0.0237  -0.0092 71  ALA A O     
434  C  CB    . ALA A 78  ? 0.3390 0.2915 0.3001 -0.0207 0.0257  -0.0077 71  ALA A CB    
435  N  N     . GLY A 79  ? 0.3546 0.2939 0.3049 -0.0176 0.0234  -0.0106 72  GLY A N     
436  C  CA    . GLY A 79  ? 0.3670 0.3001 0.3092 -0.0145 0.0236  -0.0130 72  GLY A CA    
437  C  C     . GLY A 79  ? 0.3811 0.3049 0.3186 -0.0120 0.0224  -0.0157 72  GLY A C     
438  O  O     . GLY A 79  ? 0.3780 0.3018 0.3197 -0.0112 0.0228  -0.0146 72  GLY A O     
439  N  N     . GLY A 80  ? 0.4019 0.3161 0.3293 -0.0105 0.0196  -0.0195 73  GLY A N     
440  C  CA    . GLY A 80  ? 0.4101 0.3233 0.3318 -0.0135 0.0161  -0.0203 73  GLY A CA    
441  C  C     . GLY A 80  ? 0.4064 0.3226 0.3347 -0.0211 0.0107  -0.0174 73  GLY A C     
442  O  O     . GLY A 80  ? 0.3944 0.3159 0.3315 -0.0242 0.0117  -0.0141 73  GLY A O     
443  N  N     . GLU A 81  ? 0.4210 0.3357 0.3447 -0.0244 0.0050  -0.0187 74  GLU A N     
444  C  CA    . GLU A 81  ? 0.4203 0.3441 0.3533 -0.0318 0.0002  -0.0156 74  GLU A CA    
445  C  C     . GLU A 81  ? 0.4078 0.3460 0.3473 -0.0292 0.0014  -0.0131 74  GLU A C     
446  O  O     . GLU A 81  ? 0.4190 0.3557 0.3509 -0.0267 -0.0014 -0.0142 74  GLU A O     
447  C  CB    . GLU A 81  ? 0.4491 0.3648 0.3760 -0.0384 -0.0090 -0.0180 74  GLU A CB    
448  C  CG    . GLU A 81  ? 0.4510 0.3823 0.3912 -0.0473 -0.0139 -0.0139 74  GLU A CG    
449  C  CD    . GLU A 81  ? 0.4352 0.3804 0.3897 -0.0512 -0.0093 -0.0084 74  GLU A CD    
450  O  OE1   . GLU A 81  ? 0.4368 0.3718 0.3886 -0.0532 -0.0072 -0.0072 74  GLU A OE1   
451  O  OE2   . GLU A 81  ? 0.4247 0.3913 0.3922 -0.0511 -0.0077 -0.0056 74  GLU A OE2   
452  N  N     . PRO A 82  ? 0.3900 0.3411 0.3418 -0.0288 0.0051  -0.0100 75  PRO A N     
453  C  CA    . PRO A 82  ? 0.3848 0.3463 0.3423 -0.0242 0.0053  -0.0085 75  PRO A CA    
454  C  C     . PRO A 82  ? 0.3995 0.3698 0.3603 -0.0252 -0.0018 -0.0078 75  PRO A C     
455  O  O     . PRO A 82  ? 0.4048 0.3758 0.3633 -0.0198 -0.0038 -0.0068 75  PRO A O     
456  C  CB    . PRO A 82  ? 0.3717 0.3454 0.3411 -0.0234 0.0098  -0.0072 75  PRO A CB    
457  C  CG    . PRO A 82  ? 0.3645 0.3304 0.3304 -0.0258 0.0137  -0.0074 75  PRO A CG    
458  C  CD    . PRO A 82  ? 0.3786 0.3324 0.3364 -0.0305 0.0095  -0.0084 75  PRO A CD    
459  N  N     . PHE A 83  ? 0.4108 0.3873 0.3769 -0.0330 -0.0068 -0.0077 76  PHE A N     
460  C  CA    . PHE A 83  ? 0.4268 0.4168 0.4000 -0.0352 -0.0148 -0.0067 76  PHE A CA    
461  C  C     . PHE A 83  ? 0.4482 0.4260 0.4064 -0.0354 -0.0225 -0.0090 76  PHE A C     
462  O  O     . PHE A 83  ? 0.4655 0.4540 0.4280 -0.0370 -0.0310 -0.0082 76  PHE A O     
463  C  CB    . PHE A 83  ? 0.4342 0.4403 0.4216 -0.0451 -0.0170 -0.0044 76  PHE A CB    
464  C  CG    . PHE A 83  ? 0.4216 0.4501 0.4255 -0.0417 -0.0104 -0.0020 76  PHE A CG    
465  C  CD1   . PHE A 83  ? 0.4267 0.4765 0.4438 -0.0353 -0.0124 -0.0014 76  PHE A CD1   
466  C  CD2   . PHE A 83  ? 0.4087 0.4362 0.4132 -0.0427 -0.0022 -0.0011 76  PHE A CD2   
467  C  CE1   . PHE A 83  ? 0.4211 0.4916 0.4521 -0.0297 -0.0058 -0.0010 76  PHE A CE1   
468  C  CE2   . PHE A 83  ? 0.4028 0.4507 0.4194 -0.0384 0.0041  -0.0002 76  PHE A CE2   
469  C  CZ    . PHE A 83  ? 0.4092 0.4781 0.4385 -0.0311 0.0029  -0.0009 76  PHE A CZ    
470  N  N     . LEU A 84  ? 0.4502 0.4086 0.3910 -0.0326 -0.0195 -0.0118 77  LEU A N     
471  C  CA    . LEU A 84  ? 0.4727 0.4211 0.3961 -0.0301 -0.0245 -0.0139 77  LEU A CA    
472  C  C     . LEU A 84  ? 0.4708 0.4236 0.3925 -0.0223 -0.0235 -0.0098 77  LEU A C     
473  O  O     . LEU A 84  ? 0.4941 0.4426 0.4023 -0.0206 -0.0292 -0.0096 77  LEU A O     
474  C  CB    . LEU A 84  ? 0.4804 0.4103 0.3862 -0.0282 -0.0202 -0.0186 77  LEU A CB    
475  C  CG    . LEU A 84  ? 0.4987 0.4160 0.3992 -0.0344 -0.0246 -0.0238 77  LEU A CG    
476  C  CD1   . LEU A 84  ? 0.5043 0.4059 0.3907 -0.0284 -0.0181 -0.0286 77  LEU A CD1   
477  C  CD2   . LEU A 84  ? 0.5338 0.4469 0.4250 -0.0398 -0.0369 -0.0273 77  LEU A CD2   
478  N  N     . TYR A 85  ? 0.4491 0.4083 0.3825 -0.0179 -0.0172 -0.0066 78  TYR A N     
479  C  CA    . TYR A 85  ? 0.4529 0.4115 0.3846 -0.0108 -0.0170 -0.0024 78  TYR A CA    
480  C  C     . TYR A 85  ? 0.4464 0.4200 0.3969 -0.0065 -0.0186 -0.0007 78  TYR A C     
481  O  O     . TYR A 85  ? 0.4348 0.4065 0.3903 -0.0019 -0.0129 0.0000  78  TYR A O     
482  C  CB    . TYR A 85  ? 0.4421 0.3895 0.3668 -0.0087 -0.0080 -0.0011 78  TYR A CB    
483  C  CG    . TYR A 85  ? 0.4540 0.3906 0.3605 -0.0105 -0.0049 -0.0025 78  TYR A CG    
484  C  CD1   . TYR A 85  ? 0.4475 0.3807 0.3519 -0.0132 -0.0010 -0.0075 78  TYR A CD1   
485  C  CD2   . TYR A 85  ? 0.4757 0.4057 0.3668 -0.0084 -0.0052 0.0015  78  TYR A CD2   
486  C  CE1   . TYR A 85  ? 0.4627 0.3881 0.3512 -0.0122 0.0026  -0.0100 78  TYR A CE1   
487  C  CE2   . TYR A 85  ? 0.4906 0.4148 0.3649 -0.0091 -0.0005 0.0000  78  TYR A CE2   
488  C  CZ    . TYR A 85  ? 0.4839 0.4066 0.3575 -0.0101 0.0036  -0.0066 78  TYR A CZ    
489  O  OH    . TYR A 85  ? 0.5030 0.4217 0.3606 -0.0083 0.0087  -0.0097 78  TYR A OH    
490  N  N     . PRO A 86  ? 0.4575 0.4476 0.4193 -0.0075 -0.0262 -0.0008 79  PRO A N     
491  C  CA    . PRO A 86  ? 0.4547 0.4641 0.4365 -0.0019 -0.0263 -0.0002 79  PRO A CA    
492  C  C     . PRO A 86  ? 0.4669 0.4726 0.4489 0.0101  -0.0284 0.0023  79  PRO A C     
493  O  O     . PRO A 86  ? 0.4636 0.4777 0.4580 0.0175  -0.0250 0.0009  79  PRO A O     
494  C  CB    . PRO A 86  ? 0.4698 0.4998 0.4635 -0.0070 -0.0350 -0.0001 79  PRO A CB    
495  C  CG    . PRO A 86  ? 0.4890 0.5051 0.4643 -0.0117 -0.0430 -0.0001 79  PRO A CG    
496  C  CD    . PRO A 86  ? 0.4762 0.4695 0.4338 -0.0146 -0.0350 -0.0022 79  PRO A CD    
497  N  N     . LYS A 87  ? 0.4865 0.4775 0.4527 0.0125  -0.0341 0.0059  80  LYS A N     
498  C  CA    . LYS A 87  ? 0.5059 0.4884 0.4699 0.0233  -0.0376 0.0098  80  LYS A CA    
499  C  C     . LYS A 87  ? 0.4940 0.4598 0.4536 0.0248  -0.0288 0.0095  80  LYS A C     
500  O  O     . LYS A 87  ? 0.4993 0.4647 0.4675 0.0335  -0.0282 0.0082  80  LYS A O     
501  C  CB    . LYS A 87  ? 0.5355 0.5047 0.4806 0.0240  -0.0459 0.0157  80  LYS A CB    
502  C  CG    . LYS A 87  ? 0.5641 0.5225 0.5068 0.0354  -0.0519 0.0213  80  LYS A CG    
503  C  CD    . LYS A 87  ? 0.6000 0.5485 0.5246 0.0365  -0.0619 0.0285  80  LYS A CD    
504  C  CE    . LYS A 87  ? 0.6334 0.5662 0.5546 0.0478  -0.0683 0.0352  80  LYS A CE    
505  N  NZ    . LYS A 87  ? 0.6392 0.5889 0.5838 0.0606  -0.0736 0.0316  80  LYS A NZ    
506  N  N     . PHE A 88  ? 0.4824 0.4351 0.4285 0.0168  -0.0227 0.0100  81  PHE A N     
507  C  CA    . PHE A 88  ? 0.4719 0.4113 0.4149 0.0157  -0.0149 0.0099  81  PHE A CA    
508  C  C     . PHE A 88  ? 0.4503 0.4001 0.4084 0.0170  -0.0094 0.0040  81  PHE A C     
509  O  O     . PHE A 88  ? 0.4546 0.3967 0.4151 0.0219  -0.0076 0.0027  81  PHE A O     
510  C  CB    . PHE A 88  ? 0.4632 0.3948 0.3933 0.0070  -0.0089 0.0109  81  PHE A CB    
511  C  CG    . PHE A 88  ? 0.4530 0.3752 0.3822 0.0041  -0.0014 0.0111  81  PHE A CG    
512  C  CD1   . PHE A 88  ? 0.4274 0.3563 0.3658 0.0016  0.0044  0.0059  81  PHE A CD1   
513  C  CD2   . PHE A 88  ? 0.4733 0.3804 0.3921 0.0027  -0.0011 0.0174  81  PHE A CD2   
514  C  CE1   . PHE A 88  ? 0.4210 0.3431 0.3590 -0.0015 0.0098  0.0060  81  PHE A CE1   
515  C  CE2   . PHE A 88  ? 0.4675 0.3680 0.3872 -0.0018 0.0046  0.0178  81  PHE A CE2   
516  C  CZ    . PHE A 88  ? 0.4405 0.3493 0.3703 -0.0036 0.0098  0.0117  81  PHE A CZ    
517  N  N     . LEU A 89  ? 0.4318 0.3971 0.3977 0.0118  -0.0069 0.0005  82  LEU A N     
518  C  CA    . LEU A 89  ? 0.4155 0.3925 0.3934 0.0118  -0.0012 -0.0038 82  LEU A CA    
519  C  C     . LEU A 89  ? 0.4288 0.4174 0.4190 0.0224  -0.0030 -0.0061 82  LEU A C     
520  O  O     . LEU A 89  ? 0.4283 0.4152 0.4211 0.0272  0.0013  -0.0099 82  LEU A O     
521  C  CB    . LEU A 89  ? 0.4043 0.3952 0.3875 0.0035  -0.0006 -0.0048 82  LEU A CB    
522  C  CG    . LEU A 89  ? 0.3911 0.3945 0.3839 0.0008  0.0056  -0.0073 82  LEU A CG    
523  C  CD1   . LEU A 89  ? 0.3776 0.3678 0.3631 -0.0006 0.0118  -0.0087 82  LEU A CD1   
524  C  CD2   . LEU A 89  ? 0.3895 0.4038 0.3867 -0.0089 0.0042  -0.0063 82  LEU A CD2   
525  N  N     . GLY A 90  ? 0.4448 0.4467 0.4427 0.0271  -0.0098 -0.0047 83  GLY A N     
526  C  CA    . GLY A 90  ? 0.4630 0.4783 0.4740 0.0398  -0.0117 -0.0074 83  GLY A CA    
527  C  C     . GLY A 90  ? 0.4828 0.4751 0.4857 0.0504  -0.0134 -0.0082 83  GLY A C     
528  O  O     . GLY A 90  ? 0.4939 0.4897 0.5033 0.0604  -0.0108 -0.0137 83  GLY A O     
529  N  N     . GLU A 91  ? 0.4923 0.4599 0.4796 0.0477  -0.0175 -0.0027 84  GLU A N     
530  C  CA    . GLU A 91  ? 0.5187 0.4605 0.4969 0.0551  -0.0207 -0.0015 84  GLU A CA    
531  C  C     . GLU A 91  ? 0.5079 0.4394 0.4836 0.0525  -0.0133 -0.0068 84  GLU A C     
532  O  O     . GLU A 91  ? 0.5315 0.4494 0.5062 0.0615  -0.0150 -0.0108 84  GLU A O     
533  C  CB    . GLU A 91  ? 0.5337 0.4533 0.4947 0.0494  -0.0255 0.0072  84  GLU A CB    
534  C  CG    . GLU A 91  ? 0.5587 0.4818 0.5179 0.0548  -0.0355 0.0129  84  GLU A CG    
535  C  CD    . GLU A 91  ? 0.5801 0.4800 0.5185 0.0488  -0.0393 0.0225  84  GLU A CD    
536  O  OE1   . GLU A 91  ? 0.6081 0.4831 0.5376 0.0518  -0.0420 0.0266  84  GLU A OE1   
537  O  OE2   . GLU A 91  ? 0.5718 0.4778 0.5016 0.0402  -0.0389 0.0256  84  GLU A OE2   
538  N  N     . MET A 92  ? 0.4770 0.4133 0.4507 0.0405  -0.0063 -0.0072 85  MET A N     
539  C  CA    . MET A 92  ? 0.4690 0.3946 0.4386 0.0363  -0.0009 -0.0108 85  MET A CA    
540  C  C     . MET A 92  ? 0.4661 0.4070 0.4449 0.0427  0.0033  -0.0191 85  MET A C     
541  O  O     . MET A 92  ? 0.4795 0.4081 0.4543 0.0463  0.0042  -0.0244 85  MET A O     
542  C  CB    . MET A 92  ? 0.4415 0.3683 0.4065 0.0232  0.0043  -0.0082 85  MET A CB    
543  C  CG    . MET A 92  ? 0.4485 0.3610 0.4023 0.0167  0.0025  -0.0008 85  MET A CG    
544  S  SD    . MET A 92  ? 0.4859 0.3696 0.4293 0.0179  -0.0025 0.0040  85  MET A SD    
545  C  CE    . MET A 92  ? 0.5136 0.3936 0.4523 0.0252  -0.0110 0.0103  85  MET A CE    
546  N  N     . ILE A 93  ? 0.4535 0.4213 0.4438 0.0432  0.0057  -0.0202 86  ILE A N     
547  C  CA    . ILE A 93  ? 0.4551 0.4434 0.4546 0.0487  0.0111  -0.0267 86  ILE A CA    
548  C  C     . ILE A 93  ? 0.4898 0.4757 0.4926 0.0656  0.0080  -0.0326 86  ILE A C     
549  O  O     . ILE A 93  ? 0.5029 0.4850 0.5024 0.0716  0.0115  -0.0401 86  ILE A O     
550  C  CB    . ILE A 93  ? 0.4407 0.4589 0.4525 0.0433  0.0135  -0.0243 86  ILE A CB    
551  C  CG1   . ILE A 93  ? 0.4137 0.4305 0.4203 0.0284  0.0173  -0.0208 86  ILE A CG1   
552  C  CG2   . ILE A 93  ? 0.4540 0.4994 0.4781 0.0516  0.0186  -0.0297 86  ILE A CG2   
553  C  CD1   . ILE A 93  ? 0.4062 0.4418 0.4213 0.0203  0.0158  -0.0165 86  ILE A CD1   
554  N  N     . ASP A 94  ? 0.5093 0.4947 0.5166 0.0739  0.0005  -0.0296 87  ASP A N     
555  C  CA    . ASP A 94  ? 0.5488 0.5303 0.5597 0.0925  -0.0037 -0.0352 87  ASP A CA    
556  C  C     . ASP A 94  ? 0.5729 0.5175 0.5682 0.0961  -0.0063 -0.0390 87  ASP A C     
557  O  O     . ASP A 94  ? 0.6010 0.5412 0.5954 0.1088  -0.0053 -0.0487 87  ASP A O     
558  C  CB    . ASP A 94  ? 0.5691 0.5529 0.5859 0.1004  -0.0135 -0.0295 87  ASP A CB    
559  C  CG    . ASP A 94  ? 0.5549 0.5764 0.5890 0.0976  -0.0133 -0.0265 87  ASP A CG    
560  O  OD1   . ASP A 94  ? 0.5331 0.5803 0.5761 0.0905  -0.0048 -0.0289 87  ASP A OD1   
561  O  OD2   . ASP A 94  ? 0.5695 0.5936 0.6072 0.1013  -0.0224 -0.0210 87  ASP A OD2   
562  N  N     . PHE A 95  ? 0.5667 0.4849 0.5493 0.0845  -0.0099 -0.0318 88  PHE A N     
563  C  CA    . PHE A 95  ? 0.5907 0.4738 0.5591 0.0831  -0.0132 -0.0334 88  PHE A CA    
564  C  C     . PHE A 95  ? 0.5839 0.4675 0.5490 0.0803  -0.0067 -0.0425 88  PHE A C     
565  O  O     . PHE A 95  ? 0.6195 0.4821 0.5771 0.0883  -0.0099 -0.0502 88  PHE A O     
566  C  CB    . PHE A 95  ? 0.5814 0.4453 0.5393 0.0678  -0.0157 -0.0225 88  PHE A CB    
567  C  CG    . PHE A 95  ? 0.6111 0.4399 0.5561 0.0633  -0.0201 -0.0218 88  PHE A CG    
568  C  CD1   . PHE A 95  ? 0.6622 0.4623 0.6000 0.0732  -0.0296 -0.0211 88  PHE A CD1   
569  C  CD2   . PHE A 95  ? 0.5937 0.4176 0.5341 0.0492  -0.0157 -0.0219 88  PHE A CD2   
570  C  CE1   . PHE A 95  ? 0.6968 0.4618 0.6222 0.0672  -0.0349 -0.0201 88  PHE A CE1   
571  C  CE2   . PHE A 95  ? 0.6257 0.4186 0.5557 0.0429  -0.0208 -0.0207 88  PHE A CE2   
572  C  CZ    . PHE A 95  ? 0.6782 0.4406 0.6004 0.0512  -0.0304 -0.0199 88  PHE A CZ    
573  N  N     . CYS A 96  ? 0.5434 0.4476 0.5120 0.0686  0.0009  -0.0413 89  CYS A N     
574  C  CA    . CYS A 96  ? 0.5366 0.4411 0.5002 0.0638  0.0060  -0.0478 89  CYS A CA    
575  C  C     . CYS A 96  ? 0.5602 0.4776 0.5261 0.0783  0.0095  -0.0594 89  CYS A C     
576  O  O     . CYS A 96  ? 0.5797 0.4849 0.5359 0.0802  0.0099  -0.0677 89  CYS A O     
577  C  CB    . CYS A 96  ? 0.4935 0.4172 0.4605 0.0500  0.0125  -0.0429 89  CYS A CB    
578  S  SG    . CYS A 96  ? 0.4735 0.3805 0.4344 0.0337  0.0105  -0.0331 89  CYS A SG    
579  N  N     . LYS A 97  ? 0.5626 0.5065 0.5410 0.0886  0.0121  -0.0604 90  LYS A N     
580  C  CA    . LYS A 97  ? 0.5889 0.5501 0.5703 0.1033  0.0171  -0.0715 90  LYS A CA    
581  C  C     . LYS A 97  ? 0.6402 0.5802 0.6183 0.1225  0.0098  -0.0792 90  LYS A C     
582  O  O     . LYS A 97  ? 0.6747 0.5996 0.6420 0.1315  0.0097  -0.0905 90  LYS A O     
583  C  CB    . LYS A 97  ? 0.5748 0.5796 0.5734 0.1055  0.0243  -0.0696 90  LYS A CB    
584  C  CG    . LYS A 97  ? 0.5928 0.6226 0.5920 0.1136  0.0339  -0.0793 90  LYS A CG    
585  C  CD    . LYS A 97  ? 0.5716 0.6020 0.5597 0.0991  0.0399  -0.0785 90  LYS A CD    
586  C  CE    . LYS A 97  ? 0.5919 0.6494 0.5781 0.1054  0.0501  -0.0863 90  LYS A CE    
587  N  NZ    . LYS A 97  ? 0.5880 0.6327 0.5563 0.0957  0.0523  -0.0885 90  LYS A NZ    
588  N  N     . GLU A 98  ? 0.6502 0.5872 0.6361 0.1291  0.0028  -0.0733 91  GLU A N     
589  C  CA    . GLU A 98  ? 0.7035 0.6249 0.6891 0.1504  -0.0044 -0.0799 91  GLU A CA    
590  C  C     . GLU A 98  ? 0.7397 0.6101 0.7059 0.1502  -0.0136 -0.0824 91  GLU A C     
591  O  O     . GLU A 98  ? 0.7922 0.6441 0.7519 0.1678  -0.0177 -0.0936 91  GLU A O     
592  C  CB    . GLU A 98  ? 0.7065 0.6392 0.7053 0.1568  -0.0109 -0.0714 91  GLU A CB    
593  C  CG    . GLU A 98  ? 0.6858 0.6700 0.7063 0.1598  -0.0038 -0.0706 91  GLU A CG    
594  C  CD    . GLU A 98  ? 0.6859 0.6838 0.7199 0.1627  -0.0116 -0.0613 91  GLU A CD    
595  O  OE1   . GLU A 98  ? 0.6714 0.7121 0.7247 0.1626  -0.0073 -0.0597 91  GLU A OE1   
596  O  OE2   . GLU A 98  ? 0.7036 0.6696 0.7281 0.1637  -0.0225 -0.0549 91  GLU A OE2   
597  N  N     . THR A 99  ? 0.7178 0.5658 0.6750 0.1308  -0.0171 -0.0721 92  THR A N     
598  C  CA    . THR A 99  ? 0.7555 0.5566 0.6962 0.1273  -0.0265 -0.0717 92  THR A CA    
599  C  C     . THR A 99  ? 0.7508 0.5420 0.6808 0.1162  -0.0231 -0.0786 92  THR A C     
600  O  O     . THR A 99  ? 0.7983 0.5633 0.7166 0.1244  -0.0279 -0.0897 92  THR A O     
601  C  CB    . THR A 99  ? 0.7481 0.5313 0.6854 0.1143  -0.0331 -0.0558 92  THR A CB    
602  O  OG1   . THR A 99  ? 0.7670 0.5550 0.7113 0.1279  -0.0388 -0.0512 92  THR A OG1   
603  C  CG2   . THR A 99  ? 0.7881 0.5249 0.7091 0.1059  -0.0422 -0.0525 92  THR A CG2   
604  N  N     . LEU A 100 ? 0.6983 0.5103 0.6319 0.0988  -0.0156 -0.0729 93  LEU A N     
605  C  CA    . LEU A 100 ? 0.6923 0.4956 0.6167 0.0861  -0.0141 -0.0767 93  LEU A CA    
606  C  C     . LEU A 100 ? 0.6995 0.5209 0.6214 0.0954  -0.0074 -0.0904 93  LEU A C     
607  O  O     . LEU A 100 ? 0.7131 0.5219 0.6238 0.0897  -0.0087 -0.0971 93  LEU A O     
608  C  CB    . LEU A 100 ? 0.6390 0.4574 0.5684 0.0661  -0.0094 -0.0651 93  LEU A CB    
609  C  CG    . LEU A 100 ? 0.6354 0.4364 0.5636 0.0537  -0.0145 -0.0518 93  LEU A CG    
610  C  CD1   . LEU A 100 ? 0.5884 0.4070 0.5211 0.0367  -0.0086 -0.0439 93  LEU A CD1   
611  C  CD2   . LEU A 100 ? 0.6850 0.4454 0.6011 0.0498  -0.0244 -0.0522 93  LEU A CD2   
612  N  N     . GLN A 101 ? 0.6914 0.5451 0.6239 0.1079  -0.0002 -0.0937 94  GLN A N     
613  C  CA    . GLN A 101 ? 0.7006 0.5776 0.6309 0.1166  0.0081  -0.1052 94  GLN A CA    
614  C  C     . GLN A 101 ? 0.6663 0.5550 0.5917 0.0996  0.0135  -0.1025 94  GLN A C     
615  O  O     . GLN A 101 ? 0.6881 0.5742 0.6009 0.1013  0.0152  -0.1125 94  GLN A O     
616  C  CB    . GLN A 101 ? 0.7656 0.6171 0.6814 0.1335  0.0032  -0.1215 94  GLN A CB    
617  C  CG    . GLN A 101 ? 0.8067 0.6540 0.7287 0.1558  -0.0005 -0.1265 94  GLN A CG    
618  C  CD    . GLN A 101 ? 0.7902 0.6866 0.7301 0.1667  0.0100  -0.1267 94  GLN A CD    
619  O  OE1   . GLN A 101 ? 0.7823 0.7093 0.7224 0.1671  0.0208  -0.1320 94  GLN A OE1   
620  N  NE2   . GLN A 101 ? 0.7869 0.6927 0.7422 0.1739  0.0068  -0.1195 94  GLN A NE2   
621  N  N     . LEU A 102 ? 0.6167 0.5175 0.5508 0.0838  0.0156  -0.0893 95  LEU A N     
622  C  CA    . LEU A 102 ? 0.5869 0.5005 0.5179 0.0699  0.0203  -0.0861 95  LEU A CA    
623  C  C     . LEU A 102 ? 0.5886 0.5342 0.5204 0.0758  0.0301  -0.0910 95  LEU A C     
624  O  O     . LEU A 102 ? 0.5931 0.5610 0.5354 0.0859  0.0349  -0.0917 95  LEU A O     
625  C  CB    . LEU A 102 ? 0.5403 0.4609 0.4809 0.0553  0.0208  -0.0721 95  LEU A CB    
626  C  CG    . LEU A 102 ? 0.5400 0.4331 0.4783 0.0468  0.0130  -0.0660 95  LEU A CG    
627  C  CD1   . LEU A 102 ? 0.4988 0.4017 0.4449 0.0345  0.0149  -0.0539 95  LEU A CD1   
628  C  CD2   . LEU A 102 ? 0.5601 0.4322 0.4869 0.0402  0.0081  -0.0709 95  LEU A CD2   
629  N  N     . GLU A 103 ? 0.5894 0.5385 0.5100 0.0692  0.0326  -0.0938 96  GLU A N     
630  C  CA    . GLU A 103 ? 0.5970 0.5757 0.5147 0.0728  0.0422  -0.0971 96  GLU A CA    
631  C  C     . GLU A 103 ? 0.5593 0.5678 0.4919 0.0644  0.0489  -0.0846 96  GLU A C     
632  O  O     . GLU A 103 ? 0.5683 0.6065 0.5062 0.0694  0.0574  -0.0851 96  GLU A O     
633  C  CB    . GLU A 103 ? 0.6060 0.5804 0.5066 0.0652  0.0420  -0.1002 96  GLU A CB    
634  C  CG    . GLU A 103 ? 0.6514 0.5982 0.5345 0.0722  0.0350  -0.1141 96  GLU A CG    
635  C  CD    . GLU A 103 ? 0.6678 0.6146 0.5325 0.0662  0.0345  -0.1184 96  GLU A CD    
636  O  OE1   . GLU A 103 ? 0.6452 0.6144 0.5103 0.0575  0.0402  -0.1099 96  GLU A OE1   
637  O  OE2   . GLU A 103 ? 0.7081 0.6309 0.5571 0.0701  0.0273  -0.1303 96  GLU A OE2   
638  N  N     . SER A 104 ? 0.5220 0.5231 0.4606 0.0510  0.0452  -0.0736 97  SER A N     
639  C  CA    . SER A 104 ? 0.4924 0.5160 0.4423 0.0418  0.0497  -0.0625 97  SER A CA    
640  C  C     . SER A 104 ? 0.4636 0.4744 0.4226 0.0352  0.0439  -0.0544 97  SER A C     
641  O  O     . SER A 104 ? 0.4537 0.4430 0.4074 0.0292  0.0386  -0.0528 97  SER A O     
642  C  CB    . SER A 104 ? 0.4846 0.5161 0.4263 0.0309  0.0529  -0.0575 97  SER A CB    
643  O  OG    . SER A 104 ? 0.4624 0.5099 0.4138 0.0212  0.0556  -0.0466 97  SER A OG    
644  N  N     . VAL A 105 ? 0.4558 0.4822 0.4281 0.0368  0.0451  -0.0501 98  VAL A N     
645  C  CA    . VAL A 105 ? 0.4327 0.4524 0.4125 0.0306  0.0405  -0.0423 98  VAL A CA    
646  C  C     . VAL A 105 ? 0.4153 0.4540 0.4019 0.0200  0.0436  -0.0343 98  VAL A C     
647  O  O     . VAL A 105 ? 0.4247 0.4891 0.4203 0.0214  0.0480  -0.0335 98  VAL A O     
648  C  CB    . VAL A 105 ? 0.4464 0.4657 0.4345 0.0415  0.0367  -0.0442 98  VAL A CB    
649  C  CG1   . VAL A 105 ? 0.4275 0.4447 0.4220 0.0350  0.0321  -0.0361 98  VAL A CG1   
650  C  CG2   . VAL A 105 ? 0.4708 0.4644 0.4503 0.0510  0.0318  -0.0512 98  VAL A CG2   
651  N  N     . SER A 106 ? 0.3949 0.4217 0.3775 0.0095  0.0412  -0.0283 99  SER A N     
652  C  CA    . SER A 106 ? 0.3851 0.4226 0.3713 -0.0010 0.0424  -0.0209 99  SER A CA    
653  C  C     . SER A 106 ? 0.3700 0.3954 0.3582 -0.0060 0.0370  -0.0165 99  SER A C     
654  O  O     . SER A 106 ? 0.3641 0.3723 0.3485 -0.0032 0.0336  -0.0179 99  SER A O     
655  C  CB    . SER A 106 ? 0.3858 0.4225 0.3631 -0.0080 0.0449  -0.0182 99  SER A CB    
656  O  OG    . SER A 106 ? 0.3755 0.3918 0.3445 -0.0102 0.0414  -0.0181 99  SER A OG    
657  N  N     . ILE A 107 ? 0.3692 0.4034 0.3623 -0.0142 0.0362  -0.0111 100 ILE A N     
658  C  CA    . ILE A 107 ? 0.3615 0.3835 0.3534 -0.0197 0.0309  -0.0079 100 ILE A CA    
659  C  C     . ILE A 107 ? 0.3649 0.3848 0.3536 -0.0302 0.0305  -0.0027 100 ILE A C     
660  O  O     . ILE A 107 ? 0.3763 0.4114 0.3688 -0.0357 0.0333  0.0007  100 ILE A O     
661  C  CB    . ILE A 107 ? 0.3676 0.3996 0.3686 -0.0186 0.0269  -0.0074 100 ILE A CB    
662  C  CG1   . ILE A 107 ? 0.3739 0.4120 0.3800 -0.0069 0.0269  -0.0116 100 ILE A CG1   
663  C  CG2   . ILE A 107 ? 0.3647 0.3811 0.3601 -0.0228 0.0211  -0.0058 100 ILE A CG2   
664  C  CD1   . ILE A 107 ? 0.3869 0.4479 0.4070 -0.0050 0.0247  -0.0107 100 ILE A CD1   
665  N  N     . VAL A 108 ? 0.3607 0.3619 0.3423 -0.0331 0.0268  -0.0016 101 VAL A N     
666  C  CA    . VAL A 108 ? 0.3716 0.3653 0.3494 -0.0420 0.0241  0.0029  101 VAL A CA    
667  C  C     . VAL A 108 ? 0.3784 0.3623 0.3552 -0.0451 0.0179  0.0023  101 VAL A C     
668  O  O     . VAL A 108 ? 0.3711 0.3455 0.3437 -0.0391 0.0166  -0.0014 101 VAL A O     
669  C  CB    . VAL A 108 ? 0.3699 0.3490 0.3387 -0.0408 0.0245  0.0036  101 VAL A CB    
670  C  CG1   . VAL A 108 ? 0.3569 0.3243 0.3223 -0.0333 0.0241  -0.0008 101 VAL A CG1   
671  C  CG2   . VAL A 108 ? 0.3887 0.3556 0.3520 -0.0487 0.0203  0.0087  101 VAL A CG2   
672  N  N     . THR A 109 ? 0.3969 0.3844 0.3769 -0.0551 0.0139  0.0062  102 THR A N     
673  C  CA    . THR A 109 ? 0.4093 0.3893 0.3881 -0.0588 0.0066  0.0046  102 THR A CA    
674  C  C     . THR A 109 ? 0.4366 0.4040 0.4111 -0.0708 0.0007  0.0087  102 THR A C     
675  O  O     . THR A 109 ? 0.4460 0.4185 0.4226 -0.0779 0.0030  0.0148  102 THR A O     
676  C  CB    . THR A 109 ? 0.4115 0.4139 0.4027 -0.0596 0.0051  0.0047  102 THR A CB    
677  O  OG1   . THR A 109 ? 0.4286 0.4243 0.4178 -0.0646 -0.0036 0.0033  102 THR A OG1   
678  C  CG2   . THR A 109 ? 0.4211 0.4485 0.4253 -0.0672 0.0083  0.0101  102 THR A CG2   
679  N  N     . ASN A 110 ? 0.4537 0.4022 0.4199 -0.0727 -0.0068 0.0052  103 ASN A N     
680  C  CA    . ASN A 110 ? 0.4889 0.4215 0.4504 -0.0852 -0.0149 0.0082  103 ASN A CA    
681  C  C     . ASN A 110 ? 0.5057 0.4587 0.4803 -0.0986 -0.0192 0.0129  103 ASN A C     
682  O  O     . ASN A 110 ? 0.5393 0.4833 0.5129 -0.1130 -0.0259 0.0179  103 ASN A O     
683  C  CB    . ASN A 110 ? 0.5086 0.4113 0.4541 -0.0810 -0.0218 0.0011  103 ASN A CB    
684  C  CG    . ASN A 110 ? 0.5121 0.4172 0.4552 -0.0784 -0.0266 -0.0051 103 ASN A CG    
685  O  OD1   . ASN A 110 ? 0.5130 0.4379 0.4669 -0.0846 -0.0294 -0.0031 103 ASN A OD1   
686  N  ND2   . ASN A 110 ? 0.5166 0.4039 0.4453 -0.0684 -0.0272 -0.0127 103 ASN A ND2   
687  N  N     . GLY A 111 ? 0.4876 0.4681 0.4750 -0.0943 -0.0161 0.0120  104 GLY A N     
688  C  CA    . GLY A 111 ? 0.4998 0.5102 0.5051 -0.1046 -0.0174 0.0172  104 GLY A CA    
689  C  C     . GLY A 111 ? 0.5230 0.5345 0.5313 -0.1118 -0.0290 0.0149  104 GLY A C     
690  O  O     . GLY A 111 ? 0.5312 0.5728 0.5575 -0.1177 -0.0309 0.0181  104 GLY A O     
691  N  N     . SER A 112 ? 0.5381 0.5183 0.5291 -0.1110 -0.0370 0.0091  105 SER A N     
692  C  CA    . SER A 112 ? 0.5704 0.5451 0.5593 -0.1199 -0.0501 0.0062  105 SER A CA    
693  C  C     . SER A 112 ? 0.5601 0.5590 0.5586 -0.1129 -0.0525 0.0036  105 SER A C     
694  O  O     . SER A 112 ? 0.5850 0.5982 0.5932 -0.1232 -0.0622 0.0049  105 SER A O     
695  C  CB    . SER A 112 ? 0.5934 0.5277 0.5581 -0.1179 -0.0572 -0.0012 105 SER A CB    
696  O  OG    . SER A 112 ? 0.5693 0.4931 0.5211 -0.1004 -0.0512 -0.0079 105 SER A OG    
697  N  N     . LEU A 113 ? 0.5285 0.5308 0.5239 -0.0961 -0.0450 0.0005  106 LEU A N     
698  C  CA    . LEU A 113 ? 0.5241 0.5410 0.5232 -0.0872 -0.0484 -0.0017 106 LEU A CA    
699  C  C     . LEU A 113 ? 0.5049 0.5559 0.5256 -0.0807 -0.0416 0.0023  106 LEU A C     
700  O  O     . LEU A 113 ? 0.5030 0.5662 0.5283 -0.0713 -0.0444 0.0012  106 LEU A O     
701  C  CB    . LEU A 113 ? 0.5108 0.5051 0.4897 -0.0735 -0.0451 -0.0071 106 LEU A CB    
702  C  CG    . LEU A 113 ? 0.5332 0.4952 0.4889 -0.0756 -0.0502 -0.0131 106 LEU A CG    
703  C  CD1   . LEU A 113 ? 0.5195 0.4666 0.4582 -0.0619 -0.0438 -0.0171 106 LEU A CD1   
704  C  CD2   . LEU A 113 ? 0.5712 0.5306 0.5215 -0.0838 -0.0645 -0.0161 106 LEU A CD2   
705  N  N     . VAL A 114 ? 0.4958 0.5616 0.5286 -0.0846 -0.0331 0.0067  107 VAL A N     
706  C  CA    . VAL A 114 ? 0.4842 0.5833 0.5365 -0.0772 -0.0259 0.0091  107 VAL A CA    
707  C  C     . VAL A 114 ? 0.5080 0.6403 0.5817 -0.0841 -0.0335 0.0121  107 VAL A C     
708  O  O     . VAL A 114 ? 0.5312 0.6706 0.6117 -0.1013 -0.0385 0.0162  107 VAL A O     
709  C  CB    . VAL A 114 ? 0.4762 0.5838 0.5330 -0.0810 -0.0147 0.0130  107 VAL A CB    
710  C  CG1   . VAL A 114 ? 0.4680 0.6080 0.5413 -0.0701 -0.0060 0.0130  107 VAL A CG1   
711  C  CG2   . VAL A 114 ? 0.4589 0.5348 0.4960 -0.0772 -0.0093 0.0110  107 VAL A CG2   
712  N  N     . LYS A 115 ? 0.5063 0.6596 0.5916 -0.0713 -0.0349 0.0105  108 LYS A N     
713  C  CA    . LYS A 115 ? 0.5296 0.7212 0.6395 -0.0754 -0.0416 0.0134  108 LYS A CA    
714  C  C     . LYS A 115 ? 0.5244 0.7522 0.6554 -0.0639 -0.0312 0.0143  108 LYS A C     
715  O  O     . LYS A 115 ? 0.5055 0.7246 0.6297 -0.0475 -0.0229 0.0105  108 LYS A O     
716  C  CB    . LYS A 115 ? 0.5430 0.7312 0.6496 -0.0687 -0.0548 0.0108  108 LYS A CB    
717  C  CG    . LYS A 115 ? 0.5590 0.7162 0.6448 -0.0800 -0.0664 0.0088  108 LYS A CG    
718  C  CD    . LYS A 115 ? 0.5813 0.7426 0.6657 -0.0757 -0.0808 0.0072  108 LYS A CD    
719  C  CE    . LYS A 115 ? 0.6051 0.7368 0.6667 -0.0867 -0.0928 0.0037  108 LYS A CE    
720  N  NZ    . LYS A 115 ? 0.5885 0.6793 0.6202 -0.0802 -0.0864 -0.0007 108 LYS A NZ    
721  N  N     . GLU A 116 ? 0.5466 0.8169 0.7039 -0.0725 -0.0320 0.0188  109 GLU A N     
722  C  CA    . GLU A 116 ? 0.5493 0.8596 0.7280 -0.0621 -0.0210 0.0192  109 GLU A CA    
723  C  C     . GLU A 116 ? 0.5441 0.8556 0.7243 -0.0368 -0.0216 0.0130  109 GLU A C     
724  O  O     . GLU A 116 ? 0.5365 0.8536 0.7173 -0.0219 -0.0105 0.0093  109 GLU A O     
725  C  CB    . GLU A 116 ? 0.5797 0.9408 0.7893 -0.0751 -0.0230 0.0254  109 GLU A CB    
726  C  CG    . GLU A 116 ? 0.5872 0.9939 0.8191 -0.0625 -0.0098 0.0249  109 GLU A CG    
727  C  CD    . GLU A 116 ? 0.6190 1.0814 0.8825 -0.0777 -0.0077 0.0326  109 GLU A CD    
728  O  OE1   . GLU A 116 ? 0.6372 1.1019 0.9066 -0.1002 -0.0186 0.0389  109 GLU A OE1   
729  O  OE2   . GLU A 116 ? 0.6297 1.1336 0.9114 -0.0670 0.0049  0.0319  109 GLU A OE2   
730  N  N     . GLN A 117 ? 0.5524 0.8541 0.7297 -0.0318 -0.0352 0.0119  110 GLN A N     
731  C  CA    . GLN A 117 ? 0.5562 0.8563 0.7340 -0.0087 -0.0386 0.0079  110 GLN A CA    
732  C  C     . GLN A 117 ? 0.5334 0.7971 0.6886 0.0041  -0.0299 0.0033  110 GLN A C     
733  O  O     . GLN A 117 ? 0.5396 0.8059 0.6981 0.0238  -0.0275 -0.0004 110 GLN A O     
734  C  CB    . GLN A 117 ? 0.5714 0.8591 0.7426 -0.0078 -0.0556 0.0088  110 GLN A CB    
735  C  CG    . GLN A 117 ? 0.5597 0.8021 0.7004 -0.0190 -0.0606 0.0086  110 GLN A CG    
736  C  CD    . GLN A 117 ? 0.5792 0.8076 0.7082 -0.0170 -0.0764 0.0090  110 GLN A CD    
737  O  OE1   . GLN A 117 ? 0.5998 0.8458 0.7402 -0.0044 -0.0849 0.0100  110 GLN A OE1   
738  N  NE2   . GLN A 117 ? 0.5766 0.7716 0.6805 -0.0281 -0.0806 0.0080  110 GLN A NE2   
739  N  N     . PHE A 118 ? 0.5116 0.7406 0.6440 -0.0065 -0.0262 0.0034  111 PHE A N     
740  C  CA    . PHE A 118 ? 0.4922 0.6880 0.6043 0.0035  -0.0194 -0.0003 111 PHE A CA    
741  C  C     . PHE A 118 ? 0.4894 0.7015 0.6095 0.0115  -0.0064 -0.0034 111 PHE A C     
742  O  O     . PHE A 118 ? 0.4889 0.6881 0.6023 0.0272  -0.0028 -0.0082 111 PHE A O     
743  C  CB    . PHE A 118 ? 0.4735 0.6339 0.5625 -0.0093 -0.0189 0.0005  111 PHE A CB    
744  C  CG    . PHE A 118 ? 0.4561 0.5836 0.5252 -0.0008 -0.0137 -0.0024 111 PHE A CG    
745  C  CD1   . PHE A 118 ? 0.4426 0.5668 0.5087 0.0012  -0.0029 -0.0046 111 PHE A CD1   
746  C  CD2   . PHE A 118 ? 0.4582 0.5598 0.5113 0.0043  -0.0201 -0.0024 111 PHE A CD2   
747  C  CE1   . PHE A 118 ? 0.4302 0.5257 0.4797 0.0073  0.0005  -0.0072 111 PHE A CE1   
748  C  CE2   . PHE A 118 ? 0.4463 0.5206 0.4833 0.0101  -0.0152 -0.0040 111 PHE A CE2   
749  C  CZ    . PHE A 118 ? 0.4318 0.5033 0.4680 0.0111  -0.0054 -0.0066 111 PHE A CZ    
750  N  N     . LEU A 119 ? 0.4917 0.7298 0.6236 -0.0004 0.0002  -0.0006 112 LEU A N     
751  C  CA    . LEU A 119 ? 0.4935 0.7487 0.6300 0.0056  0.0134  -0.0034 112 LEU A CA    
752  C  C     . LEU A 119 ? 0.5177 0.8077 0.6749 0.0241  0.0152  -0.0075 112 LEU A C     
753  O  O     . LEU A 119 ? 0.5238 0.8161 0.6785 0.0387  0.0239  -0.0139 112 LEU A O     
754  C  CB    . LEU A 119 ? 0.4956 0.7685 0.6369 -0.0137 0.0199  0.0026  112 LEU A CB    
755  C  CG    . LEU A 119 ? 0.4787 0.7163 0.5999 -0.0305 0.0173  0.0066  112 LEU A CG    
756  C  CD1   . LEU A 119 ? 0.4890 0.7428 0.6141 -0.0481 0.0237  0.0135  112 LEU A CD1   
757  C  CD2   . LEU A 119 ? 0.4565 0.6555 0.5544 -0.0220 0.0204  0.0017  112 LEU A CD2   
758  N  N     . GLN A 120 ? 0.5357 0.8525 0.7131 0.0245  0.0062  -0.0047 113 GLN A N     
759  C  CA    . GLN A 120 ? 0.5630 0.9147 0.7624 0.0442  0.0063  -0.0087 113 GLN A CA    
760  C  C     . GLN A 120 ? 0.5668 0.8855 0.7521 0.0664  0.0015  -0.0151 113 GLN A C     
761  O  O     . GLN A 120 ? 0.5856 0.9133 0.7757 0.0864  0.0070  -0.0222 113 GLN A O     
762  C  CB    . GLN A 120 ? 0.5834 0.9727 0.8088 0.0376  -0.0038 -0.0033 113 GLN A CB    
763  C  CG    . GLN A 120 ? 0.6158 1.0461 0.8677 0.0597  -0.0047 -0.0071 113 GLN A CG    
764  C  CD    . GLN A 120 ? 0.6382 1.1118 0.9190 0.0517  -0.0151 -0.0012 113 GLN A CD    
765  O  OE1   . GLN A 120 ? 0.6338 1.1149 0.9184 0.0269  -0.0191 0.0058  113 GLN A OE1   
766  N  NE2   . GLN A 120 ? 0.6676 1.1692 0.9693 0.0731  -0.0209 -0.0042 113 GLN A NE2   
767  N  N     . LYS A 121 ? 0.5528 0.8303 0.7179 0.0624  -0.0081 -0.0129 114 LYS A N     
768  C  CA    . LYS A 121 ? 0.5630 0.8090 0.7148 0.0805  -0.0141 -0.0164 114 LYS A CA    
769  C  C     . LYS A 121 ? 0.5519 0.7663 0.6837 0.0859  -0.0050 -0.0221 114 LYS A C     
770  O  O     . LYS A 121 ? 0.5738 0.7758 0.7022 0.1052  -0.0059 -0.0278 114 LYS A O     
771  C  CB    . LYS A 121 ? 0.5590 0.7758 0.6959 0.0741  -0.0273 -0.0109 114 LYS A CB    
772  C  CG    . LYS A 121 ? 0.5741 0.7550 0.6944 0.0898  -0.0338 -0.0120 114 LYS A CG    
773  C  CD    . LYS A 121 ? 0.5745 0.7280 0.6771 0.0828  -0.0452 -0.0057 114 LYS A CD    
774  C  CE    . LYS A 121 ? 0.5966 0.7152 0.6827 0.0973  -0.0512 -0.0049 114 LYS A CE    
775  N  NZ    . LYS A 121 ? 0.5897 0.6752 0.6509 0.0863  -0.0563 0.0011  114 LYS A NZ    
776  N  N     . HIS A 122 ? 0.5234 0.7232 0.6415 0.0694  0.0021  -0.0207 115 HIS A N     
777  C  CA    . HIS A 122 ? 0.5116 0.6769 0.6085 0.0714  0.0078  -0.0249 115 HIS A CA    
778  C  C     . HIS A 122 ? 0.5070 0.6868 0.6040 0.0685  0.0207  -0.0289 115 HIS A C     
779  O  O     . HIS A 122 ? 0.5002 0.6544 0.5803 0.0697  0.0249  -0.0329 115 HIS A O     
780  C  CB    . HIS A 122 ? 0.4857 0.6163 0.5626 0.0568  0.0043  -0.0201 115 HIS A CB    
781  C  CG    . HIS A 122 ? 0.4932 0.6046 0.5633 0.0591  -0.0070 -0.0161 115 HIS A CG    
782  N  ND1   . HIS A 122 ? 0.5113 0.5967 0.5712 0.0717  -0.0125 -0.0171 115 HIS A ND1   
783  C  CD2   . HIS A 122 ? 0.4888 0.6015 0.5582 0.0484  -0.0143 -0.0106 115 HIS A CD2   
784  C  CE1   . HIS A 122 ? 0.5170 0.5916 0.5705 0.0686  -0.0221 -0.0112 115 HIS A CE1   
785  N  NE2   . HIS A 122 ? 0.5036 0.5952 0.5626 0.0551  -0.0234 -0.0081 115 HIS A NE2   
786  N  N     . GLY A 123 ? 0.5150 0.7369 0.6309 0.0642  0.0264  -0.0272 116 GLY A N     
787  C  CA    . GLY A 123 ? 0.5151 0.7560 0.6310 0.0582  0.0388  -0.0282 116 GLY A CA    
788  C  C     . GLY A 123 ? 0.5339 0.7708 0.6414 0.0753  0.0467  -0.0385 116 GLY A C     
789  O  O     . GLY A 123 ? 0.5278 0.7577 0.6219 0.0693  0.0544  -0.0400 116 GLY A O     
790  N  N     . ARG A 124 ? 0.5605 0.7970 0.6731 0.0969  0.0433  -0.0461 117 ARG A N     
791  C  CA    . ARG A 124 ? 0.5860 0.8127 0.6875 0.1142  0.0491  -0.0577 117 ARG A CA    
792  C  C     . ARG A 124 ? 0.5696 0.7476 0.6445 0.1087  0.0467  -0.0597 117 ARG A C     
793  O  O     . ARG A 124 ? 0.5842 0.7530 0.6454 0.1146  0.0527  -0.0680 117 ARG A O     
794  C  CB    . ARG A 124 ? 0.6244 0.8552 0.7361 0.1396  0.0438  -0.0654 117 ARG A CB    
795  C  CG    . ARG A 124 ? 0.6237 0.8148 0.7276 0.1441  0.0294  -0.0628 117 ARG A CG    
796  C  CD    . ARG A 124 ? 0.6679 0.8615 0.7819 0.1697  0.0223  -0.0689 117 ARG A CD    
797  N  NE    . ARG A 124 ? 0.6724 0.8229 0.7743 0.1723  0.0084  -0.0648 117 ARG A NE    
798  C  CZ    . ARG A 124 ? 0.6560 0.8034 0.7616 0.1624  -0.0010 -0.0542 117 ARG A CZ    
799  N  NH1   . ARG A 124 ? 0.6344 0.8179 0.7568 0.1493  0.0004  -0.0473 117 ARG A NH1   
800  N  NH2   . ARG A 124 ? 0.6666 0.7738 0.7578 0.1651  -0.0124 -0.0502 117 ARG A NH2   
801  N  N     . ASN A 125 ? 0.5416 0.6911 0.6089 0.0962  0.0383  -0.0521 118 ASN A N     
802  C  CA    . ASN A 125 ? 0.5290 0.6357 0.5748 0.0911  0.0350  -0.0530 118 ASN A CA    
803  C  C     . ASN A 125 ? 0.4951 0.5972 0.5325 0.0707  0.0387  -0.0465 118 ASN A C     
804  O  O     . ASN A 125 ? 0.4831 0.5552 0.5052 0.0650  0.0366  -0.0464 118 ASN A O     
805  C  CB    . ASN A 125 ? 0.5312 0.6088 0.5729 0.0942  0.0236  -0.0494 118 ASN A CB    
806  C  CG    . ASN A 125 ? 0.5721 0.6457 0.6183 0.1160  0.0182  -0.0559 118 ASN A CG    
807  O  OD1   . ASN A 125 ? 0.6013 0.6700 0.6424 0.1296  0.0215  -0.0662 118 ASN A OD1   
808  N  ND2   . ASN A 125 ? 0.5802 0.6543 0.6345 0.1204  0.0092  -0.0504 118 ASN A ND2   
809  N  N     . ILE A 126 ? 0.4848 0.6167 0.5326 0.0599  0.0439  -0.0409 119 ILE A N     
810  C  CA    . ILE A 126 ? 0.4608 0.5880 0.5008 0.0419  0.0467  -0.0345 119 ILE A CA    
811  C  C     . ILE A 126 ? 0.4737 0.6200 0.5102 0.0411  0.0569  -0.0371 119 ILE A C     
812  O  O     . ILE A 126 ? 0.4903 0.6722 0.5398 0.0421  0.0631  -0.0361 119 ILE A O     
813  C  CB    . ILE A 126 ? 0.4467 0.5864 0.4973 0.0279  0.0431  -0.0251 119 ILE A CB    
814  C  CG1   . ILE A 126 ? 0.4394 0.5606 0.4903 0.0295  0.0329  -0.0232 119 ILE A CG1   
815  C  CG2   . ILE A 126 ? 0.4303 0.5623 0.4718 0.0109  0.0454  -0.0189 119 ILE A CG2   
816  C  CD1   . ILE A 126 ? 0.4369 0.5730 0.4991 0.0192  0.0275  -0.0164 119 ILE A CD1   
817  N  N     . ASP A 127 ? 0.4683 0.5933 0.4872 0.0378  0.0584  -0.0392 120 ASP A N     
818  C  CA    . ASP A 127 ? 0.4831 0.6234 0.4943 0.0356  0.0672  -0.0407 120 ASP A CA    
819  C  C     . ASP A 127 ? 0.4711 0.6230 0.4840 0.0174  0.0695  -0.0292 120 ASP A C     
820  O  O     . ASP A 127 ? 0.4893 0.6702 0.5060 0.0134  0.0774  -0.0260 120 ASP A O     
821  C  CB    . ASP A 127 ? 0.4895 0.6030 0.4810 0.0404  0.0661  -0.0483 120 ASP A CB    
822  C  CG    . ASP A 127 ? 0.5155 0.6203 0.5054 0.0589  0.0643  -0.0603 120 ASP A CG    
823  O  OD1   . ASP A 127 ? 0.5446 0.6748 0.5399 0.0707  0.0709  -0.0666 120 ASP A OD1   
824  O  OD2   . ASP A 127 ? 0.5101 0.5844 0.4951 0.0617  0.0562  -0.0626 120 ASP A OD2   
825  N  N     . ILE A 128 ? 0.4459 0.5733 0.4538 0.0066  0.0627  -0.0231 121 ILE A N     
826  C  CA    . ILE A 128 ? 0.4396 0.5676 0.4450 -0.0096 0.0627  -0.0130 121 ILE A CA    
827  C  C     . ILE A 128 ? 0.4216 0.5372 0.4337 -0.0176 0.0547  -0.0075 121 ILE A C     
828  O  O     . ILE A 128 ? 0.4062 0.5001 0.4156 -0.0127 0.0489  -0.0108 121 ILE A O     
829  C  CB    . ILE A 128 ? 0.4350 0.5408 0.4222 -0.0132 0.0620  -0.0126 121 ILE A CB    
830  C  CG1   . ILE A 128 ? 0.4575 0.5718 0.4332 -0.0060 0.0686  -0.0188 121 ILE A CG1   
831  C  CG2   . ILE A 128 ? 0.4323 0.5329 0.4165 -0.0284 0.0599  -0.0019 121 ILE A CG2   
832  C  CD1   . ILE A 128 ? 0.4534 0.5431 0.4121 -0.0065 0.0649  -0.0211 121 ILE A CD1   
833  N  N     . LEU A 129 ? 0.4288 0.5580 0.4484 -0.0307 0.0544  0.0008  122 LEU A N     
834  C  CA    . LEU A 129 ? 0.4193 0.5338 0.4413 -0.0397 0.0461  0.0054  122 LEU A CA    
835  C  C     . LEU A 129 ? 0.4258 0.5274 0.4383 -0.0538 0.0447  0.0134  122 LEU A C     
836  O  O     . LEU A 129 ? 0.4466 0.5662 0.4625 -0.0642 0.0484  0.0206  122 LEU A O     
837  C  CB    . LEU A 129 ? 0.4296 0.5678 0.4697 -0.0428 0.0433  0.0074  122 LEU A CB    
838  C  CG    . LEU A 129 ? 0.4280 0.5511 0.4686 -0.0536 0.0337  0.0115  122 LEU A CG    
839  C  CD1   . LEU A 129 ? 0.4090 0.5030 0.4396 -0.0454 0.0279  0.0062  122 LEU A CD1   
840  C  CD2   . LEU A 129 ? 0.4440 0.5946 0.5036 -0.0588 0.0301  0.0142  122 LEU A CD2   
841  N  N     . ALA A 130 ? 0.4124 0.4836 0.4129 -0.0536 0.0397  0.0126  123 ALA A N     
842  C  CA    . ALA A 130 ? 0.4226 0.4762 0.4135 -0.0643 0.0363  0.0195  123 ALA A CA    
843  C  C     . ALA A 130 ? 0.4284 0.4681 0.4213 -0.0722 0.0280  0.0218  123 ALA A C     
844  O  O     . ALA A 130 ? 0.4150 0.4424 0.4075 -0.0663 0.0235  0.0163  123 ALA A O     
845  C  CB    . ALA A 130 ? 0.4119 0.4433 0.3894 -0.0584 0.0355  0.0172  123 ALA A CB    
846  N  N     . VAL A 131 ? 0.4541 0.4939 0.4471 -0.0866 0.0253  0.0302  124 VAL A N     
847  C  CA    . VAL A 131 ? 0.4690 0.4910 0.4610 -0.0955 0.0158  0.0318  124 VAL A CA    
848  C  C     . VAL A 131 ? 0.4868 0.4779 0.4637 -0.1003 0.0109  0.0361  124 VAL A C     
849  O  O     . VAL A 131 ? 0.5033 0.4961 0.4752 -0.1065 0.0138  0.0439  124 VAL A O     
850  C  CB    . VAL A 131 ? 0.4930 0.5376 0.4990 -0.1096 0.0137  0.0378  124 VAL A CB    
851  C  CG1   . VAL A 131 ? 0.5147 0.5383 0.5181 -0.1198 0.0020  0.0383  124 VAL A CG1   
852  C  CG2   . VAL A 131 ? 0.4793 0.5572 0.5019 -0.1022 0.0183  0.0335  124 VAL A CG2   
853  N  N     . SER A 132 ? 0.4868 0.4502 0.4555 -0.0960 0.0038  0.0309  125 SER A N     
854  C  CA    . SER A 132 ? 0.5070 0.4392 0.4618 -0.0966 -0.0016 0.0330  125 SER A CA    
855  C  C     . SER A 132 ? 0.5491 0.4637 0.5005 -0.1115 -0.0112 0.0382  125 SER A C     
856  O  O     . SER A 132 ? 0.5574 0.4629 0.5089 -0.1129 -0.0178 0.0327  125 SER A O     
857  C  CB    . SER A 132 ? 0.4916 0.4046 0.4390 -0.0823 -0.0035 0.0236  125 SER A CB    
858  O  OG    . SER A 132 ? 0.4584 0.3844 0.4085 -0.0706 0.0040  0.0197  125 SER A OG    
859  N  N     . CYS A 133 ? 0.5801 0.4855 0.5255 -0.1219 -0.0131 0.0485  126 CYS A N     
860  C  CA    . CYS A 133 ? 0.6296 0.5138 0.5701 -0.1385 -0.0232 0.0555  126 CYS A CA    
861  C  C     . CYS A 133 ? 0.6616 0.5197 0.5877 -0.1408 -0.0267 0.0642  126 CYS A C     
862  O  O     . CYS A 133 ? 0.6617 0.5351 0.5873 -0.1439 -0.0202 0.0731  126 CYS A O     
863  C  CB    . CYS A 133 ? 0.6431 0.5578 0.5979 -0.1562 -0.0209 0.0640  126 CYS A CB    
864  S  SG    . CYS A 133 ? 0.7067 0.5969 0.6587 -0.1797 -0.0356 0.0712  126 CYS A SG    
865  N  N     . ASP A 134 ? 0.6915 0.5097 0.6044 -0.1369 -0.0371 0.0610  127 ASP A N     
866  C  CA    . ASP A 134 ? 0.7173 0.5097 0.6164 -0.1325 -0.0407 0.0670  127 ASP A CA    
867  C  C     . ASP A 134 ? 0.7794 0.5505 0.6703 -0.1526 -0.0493 0.0817  127 ASP A C     
868  O  O     . ASP A 134 ? 0.8080 0.5597 0.6869 -0.1517 -0.0527 0.0904  127 ASP A O     
869  C  CB    . ASP A 134 ? 0.7237 0.4842 0.6128 -0.1148 -0.0472 0.0560  127 ASP A CB    
870  C  CG    . ASP A 134 ? 0.6686 0.4501 0.5658 -0.0975 -0.0389 0.0427  127 ASP A CG    
871  O  OD1   . ASP A 134 ? 0.6287 0.4390 0.5336 -0.0926 -0.0290 0.0438  127 ASP A OD1   
872  O  OD2   . ASP A 134 ? 0.6705 0.4404 0.5654 -0.0913 -0.0424 0.0320  127 ASP A OD2   
873  N  N     . SER A 135 ? 0.8035 0.5781 0.7007 -0.1710 -0.0537 0.0849  128 SER A N     
874  C  CA    . SER A 135 ? 0.8699 0.6222 0.7596 -0.1933 -0.0632 0.0996  128 SER A CA    
875  C  C     . SER A 135 ? 0.8811 0.6612 0.7862 -0.2158 -0.0625 0.1055  128 SER A C     
876  O  O     . SER A 135 ? 0.8468 0.6511 0.7657 -0.2124 -0.0595 0.0954  128 SER A O     
877  C  CB    . SER A 135 ? 0.9221 0.6195 0.7952 -0.1910 -0.0790 0.0951  128 SER A CB    
878  O  OG    . SER A 135 ? 0.9936 0.6655 0.8585 -0.2147 -0.0895 0.1105  128 SER A OG    
879  N  N     . PHE A 136 ? 0.9378 0.7109 0.8398 -0.2396 -0.0671 0.1227  129 PHE A N     
880  C  CA    . PHE A 136 ? 0.9610 0.7598 0.8787 -0.2641 -0.0681 0.1304  129 PHE A CA    
881  C  C     . PHE A 136 ? 1.0354 0.7884 0.9430 -0.2835 -0.0867 0.1349  129 PHE A C     
882  O  O     . PHE A 136 ? 1.0728 0.8405 0.9917 -0.3094 -0.0906 0.1451  129 PHE A O     
883  C  CB    . PHE A 136 ? 0.9665 0.8059 0.8921 -0.2781 -0.0555 0.1475  129 PHE A CB    
884  C  CG    . PHE A 136 ? 0.9006 0.7865 0.8366 -0.2603 -0.0380 0.1414  129 PHE A CG    
885  C  CD1   . PHE A 136 ? 0.8648 0.7993 0.8238 -0.2599 -0.0291 0.1356  129 PHE A CD1   
886  C  CD2   . PHE A 136 ? 0.8778 0.7565 0.8003 -0.2425 -0.0319 0.1401  129 PHE A CD2   
887  C  CE1   . PHE A 136 ? 0.8115 0.7839 0.7784 -0.2424 -0.0142 0.1289  129 PHE A CE1   
888  C  CE2   . PHE A 136 ? 0.8238 0.7419 0.7544 -0.2270 -0.0172 0.1335  129 PHE A CE2   
889  C  CZ    . PHE A 136 ? 0.7921 0.7548 0.7440 -0.2266 -0.0084 0.1276  129 PHE A CZ    
890  N  N     . ASN A 137 ? 1.0603 0.7589 0.9475 -0.2707 -0.0985 0.1268  130 ASN A N     
891  C  CA    . ASN A 137 ? 1.1256 0.7756 1.0013 -0.2818 -0.1174 0.1232  130 ASN A CA    
892  C  C     . ASN A 137 ? 1.0940 0.7387 0.9703 -0.2638 -0.1208 0.1007  130 ASN A C     
893  O  O     . ASN A 137 ? 1.0677 0.6950 0.9333 -0.2377 -0.1189 0.0878  130 ASN A O     
894  C  CB    . ASN A 137 ? 1.1863 0.7765 1.0367 -0.2780 -0.1291 0.1287  130 ASN A CB    
895  C  CG    . ASN A 137 ? 1.2638 0.7959 1.0986 -0.2872 -0.1501 0.1234  130 ASN A CG    
896  O  OD1   . ASN A 137 ? 1.2567 0.7707 1.0862 -0.2721 -0.1561 0.1039  130 ASN A OD1   
897  N  ND2   . ASN A 137 ? 1.3443 0.8446 1.1693 -0.3122 -0.1619 0.1409  130 ASN A ND2   
898  N  N     . GLU A 138 ? 1.1052 0.7627 0.9925 -0.2785 -0.1271 0.0964  131 GLU A N     
899  C  CA    . GLU A 138 ? 1.0708 0.7332 0.9596 -0.2622 -0.1283 0.0765  131 GLU A CA    
900  C  C     . GLU A 138 ? 1.1057 0.7105 0.9691 -0.2453 -0.1401 0.0617  131 GLU A C     
901  O  O     . GLU A 138 ? 1.0673 0.6757 0.9272 -0.2230 -0.1360 0.0452  131 GLU A O     
902  C  CB    . GLU A 138 ? 1.0825 0.7709 0.9878 -0.2820 -0.1344 0.0760  131 GLU A CB    
903  C  CG    . GLU A 138 ? 1.0305 0.7860 0.9640 -0.2879 -0.1193 0.0846  131 GLU A CG    
904  C  CD    . GLU A 138 ? 0.9486 0.7398 0.8908 -0.2616 -0.1040 0.0739  131 GLU A CD    
905  O  OE1   . GLU A 138 ? 0.9247 0.6922 0.8517 -0.2383 -0.1023 0.0620  131 GLU A OE1   
906  O  OE2   . GLU A 138 ? 0.9133 0.7568 0.8783 -0.2648 -0.0942 0.0778  131 GLU A OE2   
907  N  N     . ALA A 139 ? 1.1816 0.7338 1.0266 -0.2545 -0.1540 0.0676  132 ALA A N     
908  C  CA    . ALA A 139 ? 1.2210 0.7176 1.0413 -0.2351 -0.1645 0.0531  132 ALA A CA    
909  C  C     . ALA A 139 ? 1.1664 0.6712 0.9838 -0.2042 -0.1513 0.0469  132 ALA A C     
910  O  O     . ALA A 139 ? 1.1622 0.6489 0.9681 -0.1809 -0.1523 0.0294  132 ALA A O     
911  C  CB    . ALA A 139 ? 1.3168 0.7547 1.1184 -0.2503 -0.1820 0.0624  132 ALA A CB    
912  N  N     . THR A 140 ? 1.1319 0.6637 0.9590 -0.2049 -0.1396 0.0616  133 THR A N     
913  C  CA    . THR A 140 ? 1.0834 0.6258 0.9096 -0.1788 -0.1281 0.0578  133 THR A CA    
914  C  C     . THR A 140 ? 1.0074 0.5897 0.8457 -0.1616 -0.1153 0.0435  133 THR A C     
915  O  O     . THR A 140 ? 0.9885 0.5631 0.8204 -0.1374 -0.1121 0.0307  133 THR A O     
916  C  CB    . THR A 140 ? 1.0670 0.6319 0.8997 -0.1856 -0.1193 0.0765  133 THR A CB    
917  O  OG1   . THR A 140 ? 1.1430 0.6735 0.9645 -0.2063 -0.1313 0.0926  133 THR A OG1   
918  C  CG2   . THR A 140 ? 1.0342 0.6008 0.8629 -0.1600 -0.1119 0.0732  133 THR A CG2   
919  N  N     . ASN A 141 ? 0.9679 0.5935 0.8241 -0.1739 -0.1081 0.0461  134 ASN A N     
920  C  CA    . ASN A 141 ? 0.9020 0.5625 0.7686 -0.1585 -0.0972 0.0342  134 ASN A CA    
921  C  C     . ASN A 141 ? 0.9216 0.5575 0.7754 -0.1475 -0.1051 0.0165  134 ASN A C     
922  O  O     . ASN A 141 ? 0.8822 0.5301 0.7354 -0.1278 -0.0974 0.0049  134 ASN A O     
923  C  CB    . ASN A 141 ? 0.8653 0.5744 0.7532 -0.1726 -0.0898 0.0402  134 ASN A CB    
924  C  CG    . ASN A 141 ? 0.8430 0.5828 0.7427 -0.1802 -0.0791 0.0554  134 ASN A CG    
925  O  OD1   . ASN A 141 ? 0.8203 0.5612 0.7163 -0.1672 -0.0716 0.0574  134 ASN A OD1   
926  N  ND2   . ASN A 141 ? 0.8516 0.6194 0.7660 -0.2010 -0.0782 0.0656  134 ASN A ND2   
927  N  N     . ILE A 142 ? 0.9882 0.5888 0.8303 -0.1609 -0.1209 0.0140  135 ILE A N     
928  C  CA    . ILE A 142 ? 1.0154 0.5904 0.8417 -0.1500 -0.1291 -0.0039 135 ILE A CA    
929  C  C     . ILE A 142 ? 1.0354 0.5762 0.8436 -0.1251 -0.1295 -0.0143 135 ILE A C     
930  O  O     . ILE A 142 ? 1.0184 0.5625 0.8198 -0.1057 -0.1248 -0.0291 135 ILE A O     
931  C  CB    . ILE A 142 ? 1.0878 0.6326 0.9052 -0.1716 -0.1476 -0.0051 135 ILE A CB    
932  C  CG1   . ILE A 142 ? 1.0638 0.6510 0.9018 -0.1924 -0.1467 0.0014  135 ILE A CG1   
933  C  CG2   . ILE A 142 ? 1.1334 0.6391 0.9266 -0.1570 -0.1576 -0.0254 135 ILE A CG2   
934  C  CD1   . ILE A 142 ? 1.1356 0.7001 0.9697 -0.2185 -0.1655 0.0030  135 ILE A CD1   
935  N  N     . LYS A 143 ? 1.0743 0.5844 0.8749 -0.1250 -0.1347 -0.0061 136 LYS A N     
936  C  CA    . LYS A 143 ? 1.1014 0.5790 0.8864 -0.1002 -0.1365 -0.0157 136 LYS A CA    
937  C  C     . LYS A 143 ? 1.0289 0.5444 0.8253 -0.0781 -0.1191 -0.0187 136 LYS A C     
938  O  O     . LYS A 143 ? 1.0310 0.5394 0.8193 -0.0548 -0.1161 -0.0328 136 LYS A O     
939  C  CB    . LYS A 143 ? 1.1631 0.5999 0.9384 -0.1066 -0.1475 -0.0037 136 LYS A CB    
940  C  CG    . LYS A 143 ? 1.2340 0.6164 0.9868 -0.0864 -0.1589 -0.0158 136 LYS A CG    
941  C  CD    . LYS A 143 ? 1.2009 0.5969 0.9536 -0.0536 -0.1481 -0.0300 136 LYS A CD    
942  C  CE    . LYS A 143 ? 1.2739 0.6200 1.0074 -0.0313 -0.1585 -0.0398 136 LYS A CE    
943  N  NZ    . LYS A 143 ? 1.2404 0.6086 0.9779 0.0000  -0.1463 -0.0526 136 LYS A NZ    
944  N  N     . ILE A 144 ? 0.9697 0.5260 0.7848 -0.0858 -0.1079 -0.0055 137 ILE A N     
945  C  CA    . ILE A 144 ? 0.9002 0.4951 0.7277 -0.0693 -0.0921 -0.0076 137 ILE A CA    
946  C  C     . ILE A 144 ? 0.8694 0.4833 0.6976 -0.0587 -0.0857 -0.0221 137 ILE A C     
947  O  O     . ILE A 144 ? 0.8445 0.4699 0.6734 -0.0388 -0.0773 -0.0301 137 ILE A O     
948  C  CB    . ILE A 144 ? 0.8512 0.4841 0.6962 -0.0822 -0.0828 0.0075  137 ILE A CB    
949  C  CG1   . ILE A 144 ? 0.8768 0.4946 0.7185 -0.0854 -0.0861 0.0212  137 ILE A CG1   
950  C  CG2   . ILE A 144 ? 0.7794 0.4544 0.6379 -0.0698 -0.0678 0.0035  137 ILE A CG2   
951  C  CD1   . ILE A 144 ? 0.8465 0.4971 0.7008 -0.1017 -0.0787 0.0365  137 ILE A CD1   
952  N  N     . GLY A 145 ? 0.8745 0.4935 0.7029 -0.0727 -0.0900 -0.0245 138 GLY A N     
953  C  CA    . GLY A 145 ? 0.8539 0.4886 0.6800 -0.0648 -0.0859 -0.0368 138 GLY A CA    
954  C  C     . GLY A 145 ? 0.7904 0.4712 0.6354 -0.0719 -0.0757 -0.0305 138 GLY A C     
955  O  O     . GLY A 145 ? 0.7662 0.4645 0.6109 -0.0643 -0.0705 -0.0381 138 GLY A O     
956  N  N     . ARG A 146 ? 0.7707 0.4702 0.6308 -0.0868 -0.0736 -0.0166 139 ARG A N     
957  C  CA    . ARG A 146 ? 0.7175 0.4594 0.5954 -0.0917 -0.0644 -0.0116 139 ARG A CA    
958  C  C     . ARG A 146 ? 0.7333 0.4844 0.6164 -0.1085 -0.0722 -0.0107 139 ARG A C     
959  O  O     . ARG A 146 ? 0.6982 0.4803 0.5925 -0.1082 -0.0670 -0.0111 139 ARG A O     
960  C  CB    . ARG A 146 ? 0.6897 0.4525 0.5812 -0.0972 -0.0568 0.0014  139 ARG A CB    
961  C  CG    . ARG A 146 ? 0.6346 0.4397 0.5430 -0.0961 -0.0457 0.0040  139 ARG A CG    
962  C  CD    . ARG A 146 ? 0.6169 0.4418 0.5359 -0.1022 -0.0388 0.0156  139 ARG A CD    
963  N  NE    . ARG A 146 ? 0.6081 0.4240 0.5215 -0.0908 -0.0344 0.0168  139 ARG A NE    
964  C  CZ    . ARG A 146 ? 0.5684 0.3994 0.4854 -0.0767 -0.0255 0.0128  139 ARG A CZ    
965  N  NH1   . ARG A 146 ? 0.5367 0.3863 0.4597 -0.0704 -0.0204 0.0064  139 ARG A NH1   
966  N  NH2   . ARG A 146 ? 0.5655 0.3916 0.4796 -0.0695 -0.0230 0.0158  139 ARG A NH2   
967  N  N     . GLY A 147 ? 0.7904 0.5140 0.6657 -0.1234 -0.0855 -0.0092 140 GLY A N     
968  C  CA    . GLY A 147 ? 0.8069 0.5456 0.6932 -0.1443 -0.0929 -0.0037 140 GLY A CA    
969  C  C     . GLY A 147 ? 0.8701 0.5758 0.7410 -0.1535 -0.1098 -0.0119 140 GLY A C     
970  O  O     . GLY A 147 ? 0.9097 0.5749 0.7595 -0.1443 -0.1163 -0.0212 140 GLY A O     
971  N  N     . SER A 148 ? 0.8817 0.6068 0.7641 -0.1708 -0.1170 -0.0091 141 SER A N     
972  C  CA    . SER A 148 ? 0.9491 0.6452 0.8197 -0.1856 -0.1353 -0.0145 141 SER A CA    
973  C  C     . SER A 148 ? 0.9788 0.6869 0.8667 -0.2143 -0.1424 0.0002  141 SER A C     
974  O  O     . SER A 148 ? 1.0265 0.7277 0.9143 -0.2322 -0.1573 -0.0011 141 SER A O     
975  C  CB    . SER A 148 ? 0.9466 0.6529 0.8121 -0.1798 -0.1401 -0.0265 141 SER A CB    
976  O  OG    . SER A 148 ? 0.8991 0.6561 0.7888 -0.1831 -0.1331 -0.0198 141 SER A OG    
977  N  N     . GLY A 149 ? 0.9542 0.6821 0.8565 -0.2194 -0.1317 0.0147  142 GLY A N     
978  C  CA    . GLY A 149 ? 0.9947 0.7253 0.9079 -0.2463 -0.1374 0.0303  142 GLY A CA    
979  C  C     . GLY A 149 ? 0.9584 0.7494 0.9021 -0.2575 -0.1275 0.0420  142 GLY A C     
980  O  O     . GLY A 149 ? 0.9939 0.7961 0.9499 -0.2820 -0.1315 0.0555  142 GLY A O     
981  N  N     . ASP A 150 ? 0.8937 0.7229 0.8493 -0.2398 -0.1149 0.0371  143 ASP A N     
982  C  CA    . ASP A 150 ? 0.8628 0.7498 0.8472 -0.2465 -0.1057 0.0460  143 ASP A CA    
983  C  C     . ASP A 150 ? 0.8052 0.7182 0.7965 -0.2301 -0.0865 0.0498  143 ASP A C     
984  O  O     . ASP A 150 ? 0.7781 0.7385 0.7915 -0.2307 -0.0771 0.0549  143 ASP A O     
985  C  CB    . ASP A 150 ? 0.8478 0.7614 0.8433 -0.2420 -0.1103 0.0374  143 ASP A CB    
986  C  CG    . ASP A 150 ? 0.9067 0.8099 0.9027 -0.2626 -0.1297 0.0356  143 ASP A CG    
987  O  OD1   . ASP A 150 ? 0.9540 0.8562 0.9579 -0.2878 -0.1366 0.0468  143 ASP A OD1   
988  O  OD2   . ASP A 150 ? 0.9082 0.8061 0.8966 -0.2544 -0.1382 0.0237  143 ASP A OD2   
989  N  N     . ASN A 151 ? 0.7933 0.6769 0.7667 -0.2168 -0.0812 0.0480  144 ASN A N     
990  C  CA    . ASN A 151 ? 0.7405 0.6466 0.7184 -0.2005 -0.0646 0.0497  144 ASN A CA    
991  C  C     . ASN A 151 ? 0.7413 0.6835 0.7356 -0.2131 -0.0550 0.0641  144 ASN A C     
992  O  O     . ASN A 151 ? 0.7009 0.6807 0.7083 -0.2031 -0.0423 0.0642  144 ASN A O     
993  C  CB    . ASN A 151 ? 0.7361 0.6048 0.6930 -0.1862 -0.0628 0.0462  144 ASN A CB    
994  C  CG    . ASN A 151 ? 0.7260 0.5689 0.6681 -0.1684 -0.0670 0.0311  144 ASN A CG    
995  O  OD1   . ASN A 151 ? 0.7676 0.5710 0.6930 -0.1700 -0.0782 0.0260  144 ASN A OD1   
996  N  ND2   . ASN A 151 ? 0.6767 0.5405 0.6236 -0.1514 -0.0582 0.0239  144 ASN A ND2   
997  N  N     . VAL A 152 ? 0.7932 0.7236 0.7857 -0.2353 -0.0611 0.0765  145 VAL A N     
998  C  CA    . VAL A 152 ? 0.8026 0.7654 0.8068 -0.2484 -0.0512 0.0915  145 VAL A CA    
999  C  C     . VAL A 152 ? 0.7953 0.8133 0.8277 -0.2567 -0.0467 0.0941  145 VAL A C     
1000 O  O     . VAL A 152 ? 0.7697 0.8305 0.8159 -0.2511 -0.0324 0.0976  145 VAL A O     
1001 C  CB    . VAL A 152 ? 0.8675 0.7998 0.8602 -0.2713 -0.0597 0.1057  145 VAL A CB    
1002 C  CG1   . VAL A 152 ? 0.8830 0.8527 0.8870 -0.2866 -0.0485 0.1228  145 VAL A CG1   
1003 C  CG2   . VAL A 152 ? 0.8791 0.7565 0.8446 -0.2600 -0.0651 0.1028  145 VAL A CG2   
1004 N  N     . GLN A 153 ? 0.8214 0.8383 0.8619 -0.2687 -0.0597 0.0912  146 GLN A N     
1005 C  CA    . GLN A 153 ? 0.8180 0.8869 0.8869 -0.2753 -0.0584 0.0923  146 GLN A CA    
1006 C  C     . GLN A 153 ? 0.7575 0.8561 0.8351 -0.2487 -0.0470 0.0819  146 GLN A C     
1007 O  O     . GLN A 153 ? 0.7435 0.8912 0.8420 -0.2463 -0.0356 0.0859  146 GLN A O     
1008 C  CB    . GLN A 153 ? 0.8576 0.9101 0.9280 -0.2901 -0.0775 0.0884  146 GLN A CB    
1009 C  CG    . GLN A 153 ? 0.8647 0.9705 0.9661 -0.3000 -0.0800 0.0905  146 GLN A CG    
1010 C  CD    . GLN A 153 ? 0.9217 1.0093 1.0237 -0.3230 -0.1006 0.0908  146 GLN A CD    
1011 O  OE1   . GLN A 153 ? 0.9580 0.9907 1.0357 -0.3307 -0.1129 0.0885  146 GLN A OE1   
1012 N  NE2   . GLN A 153 ? 0.9349 1.0690 1.0651 -0.3337 -0.1053 0.0932  146 GLN A NE2   
1013 N  N     . LYS A 154 ? 0.7265 0.7943 0.7873 -0.2285 -0.0499 0.0687  147 LYS A N     
1014 C  CA    . LYS A 154 ? 0.6757 0.7647 0.7423 -0.2045 -0.0412 0.0594  147 LYS A CA    
1015 C  C     . LYS A 154 ? 0.6467 0.7537 0.7141 -0.1932 -0.0244 0.0625  147 LYS A C     
1016 O  O     . LYS A 154 ? 0.6210 0.7629 0.7026 -0.1805 -0.0153 0.0596  147 LYS A O     
1017 C  CB    . LYS A 154 ? 0.6555 0.7058 0.7013 -0.1878 -0.0471 0.0466  147 LYS A CB    
1018 C  CG    . LYS A 154 ? 0.6123 0.6808 0.6633 -0.1658 -0.0412 0.0378  147 LYS A CG    
1019 C  CD    . LYS A 154 ? 0.6213 0.7225 0.6921 -0.1686 -0.0479 0.0368  147 LYS A CD    
1020 C  CE    . LYS A 154 ? 0.5870 0.7144 0.6681 -0.1482 -0.0412 0.0315  147 LYS A CE    
1021 N  NZ    . LYS A 154 ? 0.5734 0.6740 0.6373 -0.1345 -0.0472 0.0221  147 LYS A NZ    
1022 N  N     . LEU A 155 ? 0.6554 0.7365 0.7062 -0.1966 -0.0212 0.0679  148 LEU A N     
1023 C  CA    . LEU A 155 ? 0.6345 0.7294 0.6823 -0.1870 -0.0067 0.0707  148 LEU A CA    
1024 C  C     . LEU A 155 ? 0.6461 0.7934 0.7149 -0.1946 0.0037  0.0790  148 LEU A C     
1025 O  O     . LEU A 155 ? 0.6200 0.7960 0.6961 -0.1791 0.0153  0.0744  148 LEU A O     
1026 C  CB    . LEU A 155 ? 0.6552 0.7116 0.6813 -0.1932 -0.0089 0.0772  148 LEU A CB    
1027 C  CG    . LEU A 155 ? 0.6413 0.7050 0.6592 -0.1848 0.0034  0.0807  148 LEU A CG    
1028 C  CD1   . LEU A 155 ? 0.5918 0.6518 0.6048 -0.1599 0.0087  0.0676  148 LEU A CD1   
1029 C  CD2   . LEU A 155 ? 0.6729 0.7001 0.6707 -0.1937 -0.0011 0.0897  148 LEU A CD2   
1030 N  N     . TYR A 156 ? 0.6912 0.8520 0.7702 -0.2191 -0.0003 0.0910  149 TYR A N     
1031 C  CA    . TYR A 156 ? 0.7102 0.9258 0.8114 -0.2287 0.0099  0.1000  149 TYR A CA    
1032 C  C     . TYR A 156 ? 0.6876 0.9457 0.8131 -0.2151 0.0129  0.0913  149 TYR A C     
1033 O  O     . TYR A 156 ? 0.6820 0.9829 0.8208 -0.2064 0.0264  0.0914  149 TYR A O     
1034 C  CB    . TYR A 156 ? 0.7676 0.9873 0.8764 -0.2602 0.0024  0.1150  149 TYR A CB    
1035 C  CG    . TYR A 156 ? 0.8027 1.0034 0.8939 -0.2755 0.0058  0.1293  149 TYR A CG    
1036 C  CD1   . TYR A 156 ? 0.8229 1.0651 0.9214 -0.2832 0.0207  0.1409  149 TYR A CD1   
1037 C  CD2   . TYR A 156 ? 0.8206 0.9621 0.8866 -0.2811 -0.0056 0.1312  149 TYR A CD2   
1038 C  CE1   . TYR A 156 ? 0.8604 1.0843 0.9404 -0.2979 0.0231  0.1555  149 TYR A CE1   
1039 C  CE2   . TYR A 156 ? 0.8585 0.9797 0.9073 -0.2945 -0.0042 0.1454  149 TYR A CE2   
1040 C  CZ    . TYR A 156 ? 0.8786 1.0408 0.9338 -0.3038 0.0099  0.1583  149 TYR A CZ    
1041 O  OH    . TYR A 156 ? 0.9192 1.0605 0.9547 -0.3167 0.0110  0.1733  149 TYR A OH    
1042 N  N     . GLU A 157 ? 0.6794 0.9244 0.8089 -0.2120 0.0001  0.0833  150 GLU A N     
1043 C  CA    . GLU A 157 ? 0.6616 0.9413 0.8120 -0.1978 0.0000  0.0753  150 GLU A CA    
1044 C  C     . GLU A 157 ? 0.6195 0.9009 0.7634 -0.1695 0.0110  0.0650  150 GLU A C     
1045 O  O     . GLU A 157 ? 0.6155 0.9394 0.7777 -0.1578 0.0201  0.0628  150 GLU A O     
1046 C  CB    . GLU A 157 ? 0.6678 0.9253 0.8172 -0.2019 -0.0176 0.0698  150 GLU A CB    
1047 C  CG    . GLU A 157 ? 0.6562 0.9465 0.8260 -0.1884 -0.0208 0.0628  150 GLU A CG    
1048 C  CD    . GLU A 157 ? 0.6746 0.9546 0.8473 -0.1962 -0.0392 0.0595  150 GLU A CD    
1049 O  OE1   . GLU A 157 ? 0.6766 0.9083 0.8254 -0.1989 -0.0493 0.0550  150 GLU A OE1   
1050 O  OE2   . GLU A 157 ? 0.6895 1.0112 0.8880 -0.1982 -0.0436 0.0606  150 GLU A OE2   
1051 N  N     . ILE A 158 ? 0.5929 0.8286 0.7114 -0.1584 0.0099  0.0587  151 ILE A N     
1052 C  CA    . ILE A 158 ? 0.5572 0.7888 0.6678 -0.1340 0.0183  0.0492  151 ILE A CA    
1053 C  C     . ILE A 158 ? 0.5615 0.8199 0.6741 -0.1302 0.0336  0.0524  151 ILE A C     
1054 O  O     . ILE A 158 ? 0.5493 0.8304 0.6689 -0.1121 0.0419  0.0454  151 ILE A O     
1055 C  CB    . ILE A 158 ? 0.5337 0.7137 0.6183 -0.1264 0.0137  0.0434  151 ILE A CB    
1056 C  CG1   . ILE A 158 ? 0.5307 0.6888 0.6121 -0.1254 0.0004  0.0378  151 ILE A CG1   
1057 C  CG2   . ILE A 158 ? 0.5040 0.6796 0.5797 -0.1058 0.0230  0.0359  151 ILE A CG2   
1058 C  CD1   . ILE A 158 ? 0.5180 0.6286 0.5749 -0.1210 -0.0040 0.0332  151 ILE A CD1   
1059 N  N     . GLY A 159 ? 0.5855 0.8406 0.6906 -0.1472 0.0369  0.0630  152 GLY A N     
1060 C  CA    . GLY A 159 ? 0.6005 0.8850 0.7063 -0.1475 0.0513  0.0681  152 GLY A CA    
1061 C  C     . GLY A 159 ? 0.6143 0.9566 0.7471 -0.1427 0.0597  0.0672  152 GLY A C     
1062 O  O     . GLY A 159 ? 0.6096 0.9737 0.7430 -0.1259 0.0715  0.0610  152 GLY A O     
1063 N  N     . SER A 160 ? 0.6344 1.0015 0.7900 -0.1561 0.0528  0.0723  153 SER A N     
1064 C  CA    . SER A 160 ? 0.6531 1.0804 0.8381 -0.1523 0.0604  0.0727  153 SER A CA    
1065 C  C     . SER A 160 ? 0.6271 1.0622 0.8198 -0.1241 0.0604  0.0582  153 SER A C     
1066 O  O     . SER A 160 ? 0.6370 1.1130 0.8437 -0.1095 0.0717  0.0539  153 SER A O     
1067 C  CB    . SER A 160 ? 0.6868 1.1431 0.8965 -0.1758 0.0525  0.0830  153 SER A CB    
1068 O  OG    . SER A 160 ? 0.6786 1.0998 0.8846 -0.1826 0.0345  0.0808  153 SER A OG    
1069 N  N     . TRP A 161 ? 0.5993 0.9945 0.7818 -0.1159 0.0478  0.0508  154 TRP A N     
1070 C  CA    . TRP A 161 ? 0.5786 0.9731 0.7643 -0.0901 0.0463  0.0386  154 TRP A CA    
1071 C  C     . TRP A 161 ? 0.5648 0.9499 0.7347 -0.0701 0.0580  0.0304  154 TRP A C     
1072 O  O     . TRP A 161 ? 0.5670 0.9717 0.7462 -0.0493 0.0623  0.0219  154 TRP A O     
1073 C  CB    . TRP A 161 ? 0.5563 0.9067 0.7292 -0.0881 0.0314  0.0342  154 TRP A CB    
1074 C  CG    . TRP A 161 ? 0.5729 0.9317 0.7604 -0.1024 0.0174  0.0386  154 TRP A CG    
1075 C  CD1   . TRP A 161 ? 0.6022 1.0080 0.8186 -0.1122 0.0149  0.0441  154 TRP A CD1   
1076 C  CD2   . TRP A 161 ? 0.5649 0.8818 0.7368 -0.1088 0.0031  0.0370  154 TRP A CD2   
1077 N  NE1   . TRP A 161 ? 0.6129 1.0071 0.8322 -0.1249 -0.0013 0.0459  154 TRP A NE1   
1078 C  CE2   . TRP A 161 ? 0.5915 0.9304 0.7822 -0.1226 -0.0085 0.0411  154 TRP A CE2   
1079 C  CE3   . TRP A 161 ? 0.5417 0.8074 0.6859 -0.1042 -0.0006 0.0322  154 TRP A CE3   
1080 C  CZ2   . TRP A 161 ? 0.5971 0.9049 0.7765 -0.1311 -0.0241 0.0396  154 TRP A CZ2   
1081 C  CZ3   . TRP A 161 ? 0.5469 0.7847 0.6811 -0.1118 -0.0145 0.0310  154 TRP A CZ3   
1082 C  CH2   . TRP A 161 ? 0.5750 0.8319 0.7251 -0.1248 -0.0263 0.0341  154 TRP A CH2   
1083 N  N     . CYS A 162 ? 0.5544 0.9071 0.6998 -0.0755 0.0616  0.0322  155 CYS A N     
1084 C  CA    . CYS A 162 ? 0.5456 0.8883 0.6747 -0.0585 0.0712  0.0242  155 CYS A CA    
1085 C  C     . CYS A 162 ? 0.5757 0.9679 0.7172 -0.0525 0.0856  0.0237  155 CYS A C     
1086 O  O     . CYS A 162 ? 0.5788 0.9797 0.7197 -0.0308 0.0917  0.0128  155 CYS A O     
1087 C  CB    . CYS A 162 ? 0.5333 0.8359 0.6356 -0.0670 0.0710  0.0274  155 CYS A CB    
1088 S  SG    . CYS A 162 ? 0.4990 0.7450 0.5848 -0.0659 0.0569  0.0237  155 CYS A SG    
1089 N  N     . GLN A 163 ? 0.6031 1.0280 0.7565 -0.0719 0.0905  0.0355  156 GLN A N     
1090 C  CA    . GLN A 163 ? 0.6385 1.1187 0.8069 -0.0697 0.1052  0.0374  156 GLN A CA    
1091 C  C     . GLN A 163 ? 0.6456 1.1615 0.8394 -0.0489 0.1059  0.0278  156 GLN A C     
1092 O  O     . GLN A 163 ? 0.6605 1.1978 0.8550 -0.0280 0.1165  0.0179  156 GLN A O     
1093 C  CB    . GLN A 163 ? 0.6681 1.1754 0.8487 -0.0988 0.1067  0.0543  156 GLN A CB    
1094 C  CG    . GLN A 163 ? 0.6996 1.2265 0.8683 -0.1089 0.1214  0.0628  156 GLN A CG    
1095 C  CD    . GLN A 163 ? 0.7340 1.3243 0.9209 -0.0978 0.1380  0.0599  156 GLN A CD    
1096 O  OE1   . GLN A 163 ? 0.7650 1.4052 0.9785 -0.1111 0.1422  0.0693  156 GLN A OE1   
1097 N  NE2   . GLN A 163 ? 0.7339 1.3236 0.9064 -0.0734 0.1475  0.0466  156 GLN A NE2   
1098 N  N     . LYS A 164 ? 0.6383 1.1571 0.8510 -0.0536 0.0932  0.0299  157 LYS A N     
1099 C  CA    . LYS A 164 ? 0.6485 1.2010 0.8877 -0.0358 0.0905  0.0230  157 LYS A CA    
1100 C  C     . LYS A 164 ? 0.6332 1.1587 0.8605 -0.0058 0.0886  0.0078  157 LYS A C     
1101 O  O     . LYS A 164 ? 0.6552 1.2140 0.8989 0.0153  0.0937  -0.0001 157 LYS A O     
1102 C  CB    . LYS A 164 ? 0.6434 1.1940 0.8989 -0.0496 0.0740  0.0291  157 LYS A CB    
1103 C  CG    . LYS A 164 ? 0.6576 1.2445 0.9426 -0.0339 0.0678  0.0243  157 LYS A CG    
1104 C  CD    . LYS A 164 ? 0.6597 1.2477 0.9591 -0.0526 0.0513  0.0319  157 LYS A CD    
1105 C  CE    . LYS A 164 ? 0.6738 1.2926 1.0004 -0.0373 0.0416  0.0277  157 LYS A CE    
1106 N  NZ    . LYS A 164 ? 0.7019 1.3771 1.0533 -0.0166 0.0540  0.0227  157 LYS A NZ    
1107 N  N     . TYR A 165 ? 0.6008 1.0675 0.8012 -0.0041 0.0808  0.0042  158 TYR A N     
1108 C  CA    . TYR A 165 ? 0.5892 1.0259 0.7793 0.0201  0.0756  -0.0078 158 TYR A CA    
1109 C  C     . TYR A 165 ? 0.5858 0.9956 0.7496 0.0309  0.0841  -0.0160 158 TYR A C     
1110 O  O     . TYR A 165 ? 0.5773 0.9537 0.7281 0.0474  0.0792  -0.0252 158 TYR A O     
1111 C  CB    . TYR A 165 ? 0.5616 0.9567 0.7437 0.0150  0.0596  -0.0059 158 TYR A CB    
1112 C  CG    . TYR A 165 ? 0.5720 0.9934 0.7791 0.0090  0.0492  -0.0006 158 TYR A CG    
1113 C  CD1   . TYR A 165 ? 0.5921 1.0403 0.8197 0.0284  0.0454  -0.0057 158 TYR A CD1   
1114 C  CD2   . TYR A 165 ? 0.5681 0.9887 0.7786 -0.0160 0.0423  0.0094  158 TYR A CD2   
1115 C  CE1   . TYR A 165 ? 0.6054 1.0818 0.8573 0.0226  0.0350  -0.0005 158 TYR A CE1   
1116 C  CE2   . TYR A 165 ? 0.5829 1.0288 0.8159 -0.0231 0.0317  0.0139  158 TYR A CE2   
1117 C  CZ    . TYR A 165 ? 0.6005 1.0763 0.8550 -0.0041 0.0281  0.0092  158 TYR A CZ    
1118 O  OH    . TYR A 165 ? 0.6171 1.1189 0.8940 -0.0118 0.0161  0.0140  158 TYR A OH    
1119 N  N     . ASP A 166 ? 0.5991 1.0255 0.7555 0.0219  0.0964  -0.0127 159 ASP A N     
1120 C  CA    . ASP A 166 ? 0.6062 1.0160 0.7391 0.0329  0.1049  -0.0212 159 ASP A CA    
1121 C  C     . ASP A 166 ? 0.5728 0.9243 0.6798 0.0282  0.0962  -0.0220 159 ASP A C     
1122 O  O     . ASP A 166 ? 0.5709 0.8947 0.6636 0.0441  0.0942  -0.0326 159 ASP A O     
1123 C  CB    . ASP A 166 ? 0.6324 1.0536 0.7690 0.0622  0.1089  -0.0363 159 ASP A CB    
1124 C  CG    . ASP A 166 ? 0.6545 1.0701 0.7686 0.0732  0.1196  -0.0461 159 ASP A CG    
1125 O  OD1   . ASP A 166 ? 0.6581 1.0802 0.7597 0.0580  0.1275  -0.0394 159 ASP A OD1   
1126 O  OD2   . ASP A 166 ? 0.6724 1.0740 0.7795 0.0968  0.1187  -0.0604 159 ASP A OD2   
1127 N  N     . ILE A 167 ? 0.5512 0.8852 0.6536 0.0067  0.0904  -0.0109 160 ILE A N     
1128 C  CA    . ILE A 167 ? 0.5228 0.8074 0.6028 0.0014  0.0833  -0.0107 160 ILE A CA    
1129 C  C     . ILE A 167 ? 0.5268 0.8073 0.5920 -0.0150 0.0884  -0.0023 160 ILE A C     
1130 O  O     . ILE A 167 ? 0.5388 0.8395 0.6123 -0.0322 0.0904  0.0087  160 ILE A O     
1131 C  CB    . ILE A 167 ? 0.4977 0.7581 0.5818 -0.0059 0.0704  -0.0065 160 ILE A CB    
1132 C  CG1   . ILE A 167 ? 0.4985 0.7621 0.5955 0.0098  0.0640  -0.0131 160 ILE A CG1   
1133 C  CG2   . ILE A 167 ? 0.4728 0.6875 0.5346 -0.0106 0.0652  -0.0065 160 ILE A CG2   
1134 C  CD1   . ILE A 167 ? 0.4844 0.7363 0.5879 0.0012  0.0521  -0.0079 160 ILE A CD1   
1135 N  N     . LYS A 168 ? 0.5197 0.7715 0.5625 -0.0110 0.0890  -0.0067 161 LYS A N     
1136 C  CA    . LYS A 168 ? 0.5244 0.7671 0.5513 -0.0259 0.0913  0.0018  161 LYS A CA    
1137 C  C     . LYS A 168 ? 0.5056 0.7238 0.5319 -0.0426 0.0816  0.0119  161 LYS A C     
1138 O  O     . LYS A 168 ? 0.4801 0.6707 0.5058 -0.0393 0.0726  0.0085  161 LYS A O     
1139 C  CB    . LYS A 168 ? 0.5247 0.7440 0.5286 -0.0167 0.0925  -0.0059 161 LYS A CB    
1140 C  CG    . LYS A 168 ? 0.5529 0.7928 0.5526 -0.0001 0.1018  -0.0172 161 LYS A CG    
1141 C  CD    . LYS A 168 ? 0.5561 0.7686 0.5321 0.0073  0.1003  -0.0257 161 LYS A CD    
1142 C  CE    . LYS A 168 ? 0.5647 0.7706 0.5221 -0.0060 0.1016  -0.0169 161 LYS A CE    
1143 N  NZ    . LYS A 168 ? 0.6066 0.8430 0.5539 -0.0039 0.1137  -0.0178 161 LYS A NZ    
1144 N  N     . PHE A 169 ? 0.5247 0.7541 0.5512 -0.0607 0.0836  0.0244  162 PHE A N     
1145 C  CA    . PHE A 169 ? 0.5198 0.7291 0.5472 -0.0774 0.0743  0.0341  162 PHE A CA    
1146 C  C     . PHE A 169 ? 0.5212 0.6985 0.5270 -0.0849 0.0709  0.0399  162 PHE A C     
1147 O  O     . PHE A 169 ? 0.5454 0.7303 0.5398 -0.0909 0.0768  0.0465  162 PHE A O     
1148 C  CB    . PHE A 169 ? 0.5469 0.7876 0.5917 -0.0941 0.0759  0.0449  162 PHE A CB    
1149 C  CG    . PHE A 169 ? 0.5542 0.7722 0.5977 -0.1135 0.0655  0.0551  162 PHE A CG    
1150 C  CD1   . PHE A 169 ? 0.5320 0.7185 0.5743 -0.1116 0.0538  0.0506  162 PHE A CD1   
1151 C  CD2   . PHE A 169 ? 0.5903 0.8183 0.6330 -0.1340 0.0671  0.0693  162 PHE A CD2   
1152 C  CE1   . PHE A 169 ? 0.5458 0.7092 0.5850 -0.1277 0.0437  0.0580  162 PHE A CE1   
1153 C  CE2   . PHE A 169 ? 0.6050 0.8080 0.6456 -0.1518 0.0560  0.0780  162 PHE A CE2   
1154 C  CZ    . PHE A 169 ? 0.5833 0.7535 0.6221 -0.1479 0.0441  0.0714  162 PHE A CZ    
1155 N  N     . LYS A 170 ? 0.4978 0.6394 0.4975 -0.0831 0.0611  0.0373  163 LYS A N     
1156 C  CA    . LYS A 170 ? 0.4957 0.6057 0.4767 -0.0846 0.0567  0.0399  163 LYS A CA    
1157 C  C     . LYS A 170 ? 0.4980 0.5818 0.4782 -0.0952 0.0465  0.0457  163 LYS A C     
1158 O  O     . LYS A 170 ? 0.4879 0.5695 0.4787 -0.0955 0.0415  0.0425  163 LYS A O     
1159 C  CB    . LYS A 170 ? 0.4691 0.5627 0.4427 -0.0684 0.0558  0.0286  163 LYS A CB    
1160 C  CG    . LYS A 170 ? 0.4624 0.5243 0.4216 -0.0681 0.0493  0.0298  163 LYS A CG    
1161 C  CD    . LYS A 170 ? 0.4415 0.4934 0.3958 -0.0544 0.0490  0.0195  163 LYS A CD    
1162 C  CE    . LYS A 170 ? 0.4304 0.4548 0.3774 -0.0529 0.0417  0.0195  163 LYS A CE    
1163 N  NZ    . LYS A 170 ? 0.4071 0.4238 0.3567 -0.0422 0.0403  0.0099  163 LYS A NZ    
1164 N  N     . LEU A 171 ? 0.5180 0.5819 0.4843 -0.1036 0.0430  0.0543  164 LEU A N     
1165 C  CA    . LEU A 171 ? 0.5315 0.5664 0.4938 -0.1129 0.0327  0.0597  164 LEU A CA    
1166 C  C     . LEU A 171 ? 0.5236 0.5270 0.4714 -0.1043 0.0273  0.0572  164 LEU A C     
1167 O  O     . LEU A 171 ? 0.5294 0.5326 0.4663 -0.1009 0.0301  0.0595  164 LEU A O     
1168 C  CB    . LEU A 171 ? 0.5759 0.6145 0.5358 -0.1325 0.0318  0.0744  164 LEU A CB    
1169 C  CG    . LEU A 171 ? 0.6016 0.6028 0.5531 -0.1422 0.0195  0.0804  164 LEU A CG    
1170 C  CD1   . LEU A 171 ? 0.5932 0.5860 0.5550 -0.1434 0.0122  0.0737  164 LEU A CD1   
1171 C  CD2   . LEU A 171 ? 0.6531 0.6549 0.5992 -0.1628 0.0184  0.0971  164 LEU A CD2   
1172 N  N     . ASN A 172 ? 0.5137 0.4922 0.4612 -0.1001 0.0194  0.0520  165 ASN A N     
1173 C  CA    . ASN A 172 ? 0.5102 0.4616 0.4470 -0.0912 0.0141  0.0493  165 ASN A CA    
1174 C  C     . ASN A 172 ? 0.5424 0.4634 0.4720 -0.0981 0.0041  0.0543  165 ASN A C     
1175 O  O     . ASN A 172 ? 0.5494 0.4639 0.4838 -0.1034 -0.0003 0.0522  165 ASN A O     
1176 C  CB    . ASN A 172 ? 0.4764 0.4225 0.4173 -0.0771 0.0139  0.0374  165 ASN A CB    
1177 C  CG    . ASN A 172 ? 0.4485 0.4143 0.3935 -0.0678 0.0212  0.0312  165 ASN A CG    
1178 O  OD1   . ASN A 172 ? 0.4540 0.4391 0.3990 -0.0706 0.0270  0.0340  165 ASN A OD1   
1179 N  ND2   . ASN A 172 ? 0.4240 0.3849 0.3716 -0.0574 0.0210  0.0228  165 ASN A ND2   
1180 N  N     . THR A 173 ? 0.5673 0.4695 0.4846 -0.0982 -0.0001 0.0611  166 THR A N     
1181 C  CA    . THR A 173 ? 0.6082 0.4768 0.5160 -0.1036 -0.0107 0.0665  166 THR A CA    
1182 C  C     . THR A 173 ? 0.6104 0.4558 0.5101 -0.0887 -0.0161 0.0625  166 THR A C     
1183 O  O     . THR A 173 ? 0.6056 0.4571 0.5010 -0.0825 -0.0142 0.0650  166 THR A O     
1184 C  CB    . THR A 173 ? 0.6536 0.5195 0.5534 -0.1205 -0.0125 0.0824  166 THR A CB    
1185 O  OG1   . THR A 173 ? 0.6556 0.5464 0.5661 -0.1348 -0.0076 0.0860  166 THR A OG1   
1186 C  CG2   . THR A 173 ? 0.7055 0.5306 0.5927 -0.1261 -0.0252 0.0894  166 THR A CG2   
1187 N  N     . VAL A 174 ? 0.6240 0.4433 0.5211 -0.0829 -0.0236 0.0563  167 VAL A N     
1188 C  CA    . VAL A 174 ? 0.6374 0.4341 0.5277 -0.0683 -0.0296 0.0528  167 VAL A CA    
1189 C  C     . VAL A 174 ? 0.6980 0.4600 0.5743 -0.0742 -0.0409 0.0629  167 VAL A C     
1190 O  O     . VAL A 174 ? 0.7322 0.4695 0.6036 -0.0810 -0.0483 0.0625  167 VAL A O     
1191 C  CB    . VAL A 174 ? 0.6240 0.4126 0.5176 -0.0552 -0.0304 0.0389  167 VAL A CB    
1192 C  CG1   . VAL A 174 ? 0.6428 0.4126 0.5315 -0.0387 -0.0357 0.0352  167 VAL A CG1   
1193 C  CG2   . VAL A 174 ? 0.5703 0.3897 0.4760 -0.0499 -0.0203 0.0305  167 VAL A CG2   
1194 N  N     . VAL A 175 ? 0.7139 0.4715 0.5833 -0.0694 -0.0435 0.0704  168 VAL A N     
1195 C  CA    . VAL A 175 ? 0.7758 0.4987 0.6303 -0.0726 -0.0552 0.0816  168 VAL A CA    
1196 C  C     . VAL A 175 ? 0.7989 0.4926 0.6499 -0.0536 -0.0641 0.0729  168 VAL A C     
1197 O  O     . VAL A 175 ? 0.7759 0.4810 0.6328 -0.0362 -0.0620 0.0659  168 VAL A O     
1198 C  CB    . VAL A 175 ? 0.7874 0.5208 0.6343 -0.0764 -0.0543 0.0948  168 VAL A CB    
1199 C  CG1   . VAL A 175 ? 0.8591 0.5551 0.6885 -0.0827 -0.0670 0.1095  168 VAL A CG1   
1200 C  CG2   . VAL A 175 ? 0.7630 0.5311 0.6139 -0.0913 -0.0431 0.1003  168 VAL A CG2   
1201 N  N     . ASN A 176 ? 0.8493 0.5055 0.6909 -0.0566 -0.0743 0.0726  169 ASN A N     
1202 C  CA    . ASN A 176 ? 0.8756 0.5038 0.7135 -0.0377 -0.0818 0.0609  169 ASN A CA    
1203 C  C     . ASN A 176 ? 0.9571 0.5345 0.7774 -0.0423 -0.0975 0.0686  169 ASN A C     
1204 O  O     . ASN A 176 ? 0.9885 0.5559 0.8008 -0.0619 -0.1016 0.0844  169 ASN A O     
1205 C  CB    . ASN A 176 ? 0.8445 0.4825 0.6899 -0.0333 -0.0761 0.0447  169 ASN A CB    
1206 C  CG    . ASN A 176 ? 0.8614 0.4889 0.7033 -0.0532 -0.0789 0.0462  169 ASN A CG    
1207 O  OD1   . ASN A 176 ? 0.9205 0.5085 0.7498 -0.0572 -0.0908 0.0460  169 ASN A OD1   
1208 N  ND2   . ASN A 176 ? 0.8152 0.4770 0.6681 -0.0659 -0.0693 0.0475  169 ASN A ND2   
1209 N  N     . LYS A 177 ? 0.9953 0.5412 0.8093 -0.0240 -0.1060 0.0577  170 LYS A N     
1210 C  CA    . LYS A 177 ? 1.0815 0.5723 0.8772 -0.0246 -0.1227 0.0627  170 LYS A CA    
1211 C  C     . LYS A 177 ? 1.1169 0.5861 0.9040 -0.0518 -0.1286 0.0703  170 LYS A C     
1212 O  O     . LYS A 177 ? 1.1824 0.6161 0.9554 -0.0644 -0.1405 0.0847  170 LYS A O     
1213 C  CB    . LYS A 177 ? 1.1144 0.5780 0.9053 -0.0004 -0.1288 0.0445  170 LYS A CB    
1214 C  CG    . LYS A 177 ? 1.1310 0.5911 0.9237 0.0274  -0.1321 0.0410  170 LYS A CG    
1215 C  CD    . LYS A 177 ? 1.2224 0.6283 0.9970 0.0330  -0.1504 0.0496  170 LYS A CD    
1216 C  CE    . LYS A 177 ? 1.2394 0.6418 1.0076 0.0157  -0.1554 0.0730  170 LYS A CE    
1217 N  NZ    . LYS A 177 ? 1.3330 0.6811 1.0829 0.0234  -0.1742 0.0823  170 LYS A NZ    
1218 N  N     . PHE A 178 ? 1.0793 0.5690 0.8748 -0.0613 -0.1214 0.0614  171 PHE A N     
1219 C  CA    . PHE A 178 ? 1.1161 0.5869 0.9058 -0.0860 -0.1284 0.0660  171 PHE A CA    
1220 C  C     . PHE A 178 ? 1.1061 0.6013 0.9013 -0.1136 -0.1236 0.0854  171 PHE A C     
1221 O  O     . PHE A 178 ? 1.1504 0.6277 0.9408 -0.1365 -0.1312 0.0931  171 PHE A O     
1222 C  CB    . PHE A 178 ? 1.0849 0.5695 0.8812 -0.0847 -0.1239 0.0488  171 PHE A CB    
1223 C  CG    . PHE A 178 ? 1.1042 0.5652 0.8924 -0.0593 -0.1279 0.0291  171 PHE A CG    
1224 C  CD1   . PHE A 178 ? 1.1790 0.5893 0.9503 -0.0462 -0.1418 0.0266  171 PHE A CD1   
1225 C  CD2   . PHE A 178 ? 1.0543 0.5430 0.8506 -0.0481 -0.1180 0.0131  171 PHE A CD2   
1226 C  CE1   . PHE A 178 ? 1.2023 0.5932 0.9658 -0.0211 -0.1445 0.0072  171 PHE A CE1   
1227 C  CE2   . PHE A 178 ? 1.0773 0.5473 0.8649 -0.0249 -0.1203 -0.0048 171 PHE A CE2   
1228 C  CZ    . PHE A 178 ? 1.1508 0.5734 0.9224 -0.0108 -0.1330 -0.0085 171 PHE A CZ    
1229 N  N     . ASN A 179 ? 1.0547 0.5909 0.8596 -0.1129 -0.1113 0.0932  172 ASN A N     
1230 C  CA    . ASN A 179 ? 1.0454 0.6103 0.8560 -0.1378 -0.1046 0.1091  172 ASN A CA    
1231 C  C     . ASN A 179 ? 1.0513 0.6265 0.8560 -0.1389 -0.1015 0.1250  172 ASN A C     
1232 O  O     . ASN A 179 ? 1.0390 0.6454 0.8480 -0.1560 -0.0929 0.1372  172 ASN A O     
1233 C  CB    . ASN A 179 ? 0.9712 0.5878 0.8013 -0.1406 -0.0896 0.1010  172 ASN A CB    
1234 C  CG    . ASN A 179 ? 0.9046 0.5543 0.7437 -0.1200 -0.0778 0.0926  172 ASN A CG    
1235 O  OD1   . ASN A 179 ? 0.9108 0.5475 0.7436 -0.1031 -0.0807 0.0913  172 ASN A OD1   
1236 N  ND2   . ASN A 179 ? 0.8454 0.5378 0.6997 -0.1218 -0.0652 0.0873  172 ASN A ND2   
1237 N  N     . HIS A 180 ? 1.0737 0.6250 0.8683 -0.1203 -0.1085 0.1250  173 HIS A N     
1238 C  CA    . HIS A 180 ? 1.0689 0.6367 0.8589 -0.1176 -0.1048 0.1372  173 HIS A CA    
1239 C  C     . HIS A 180 ? 1.1364 0.6855 0.9106 -0.1409 -0.1114 0.1608  173 HIS A C     
1240 O  O     . HIS A 180 ? 1.1351 0.7041 0.9038 -0.1447 -0.1064 0.1733  173 HIS A O     
1241 C  CB    . HIS A 180 ? 1.0673 0.6232 0.8551 -0.0895 -0.1100 0.1293  173 HIS A CB    
1242 C  CG    . HIS A 180 ? 1.1478 0.6488 0.9187 -0.0821 -0.1277 0.1346  173 HIS A CG    
1243 N  ND1   . HIS A 180 ? 1.1820 0.6453 0.9494 -0.0716 -0.1374 0.1221  173 HIS A ND1   
1244 C  CD2   . HIS A 180 ? 1.2060 0.6821 0.9609 -0.0822 -0.1381 0.1509  173 HIS A CD2   
1245 C  CE1   . HIS A 180 ? 1.2607 0.6759 1.0112 -0.0653 -0.1535 0.1304  173 HIS A CE1   
1246 N  NE2   . HIS A 180 ? 1.2755 0.6978 1.0185 -0.0717 -0.1545 0.1486  173 HIS A NE2   
1247 N  N     . LEU A 181 ? 1.1989 0.7106 0.9647 -0.1577 -0.1225 0.1672  174 LEU A N     
1248 C  CA    . LEU A 181 ? 1.2717 0.7630 1.0220 -0.1826 -0.1294 0.1913  174 LEU A CA    
1249 C  C     . LEU A 181 ? 1.2613 0.7871 1.0221 -0.2116 -0.1193 0.1998  174 LEU A C     
1250 O  O     . LEU A 181 ? 1.3135 0.8369 1.0650 -0.2357 -0.1206 0.2211  174 LEU A O     
1251 C  CB    . LEU A 181 ? 1.3604 0.7838 1.0936 -0.1837 -0.1502 0.1945  174 LEU A CB    
1252 C  CG    . LEU A 181 ? 1.3926 0.7787 1.1129 -0.1561 -0.1621 0.1910  174 LEU A CG    
1253 C  CD1   . LEU A 181 ? 1.4856 0.8017 1.1889 -0.1562 -0.1830 0.1915  174 LEU A CD1   
1254 C  CD2   . LEU A 181 ? 1.4116 0.8053 1.1200 -0.1561 -0.1619 0.2100  174 LEU A CD2   
1255 N  N     . GLU A 182 ? 1.1954 0.7570 0.9765 -0.2095 -0.1087 0.1840  175 GLU A N     
1256 C  CA    . GLU A 182 ? 1.1875 0.7831 0.9819 -0.2346 -0.1005 0.1900  175 GLU A CA    
1257 C  C     . GLU A 182 ? 1.1703 0.8131 0.9670 -0.2448 -0.0855 0.2040  175 GLU A C     
1258 O  O     . GLU A 182 ? 1.1323 0.7941 0.9265 -0.2274 -0.0779 0.2006  175 GLU A O     
1259 C  CB    . GLU A 182 ? 1.1198 0.7421 0.9343 -0.2244 -0.0935 0.1686  175 GLU A CB    
1260 C  CG    . GLU A 182 ? 1.1078 0.7686 0.9400 -0.2469 -0.0859 0.1720  175 GLU A CG    
1261 C  CD    . GLU A 182 ? 1.0555 0.7334 0.9045 -0.2377 -0.0832 0.1519  175 GLU A CD    
1262 O  OE1   . GLU A 182 ? 1.0458 0.6952 0.8894 -0.2184 -0.0901 0.1363  175 GLU A OE1   
1263 O  OE2   . GLU A 182 ? 1.0280 0.7490 0.8951 -0.2491 -0.0741 0.1521  175 GLU A OE2   
1264 N  N     . ASP A 183 ? 1.2011 0.8647 1.0031 -0.2732 -0.0813 0.2188  176 ASP A N     
1265 C  CA    . ASP A 183 ? 1.1864 0.9030 0.9934 -0.2842 -0.0647 0.2301  176 ASP A CA    
1266 C  C     . ASP A 183 ? 1.1369 0.9050 0.9705 -0.2906 -0.0521 0.2208  176 ASP A C     
1267 O  O     . ASP A 183 ? 1.1654 0.9346 1.0099 -0.3115 -0.0564 0.2251  176 ASP A O     
1268 C  CB    . ASP A 183 ? 1.2706 0.9770 1.0628 -0.3130 -0.0680 0.2576  176 ASP A CB    
1269 C  CG    . ASP A 183 ? 1.2618 1.0255 1.0568 -0.3230 -0.0494 0.2690  176 ASP A CG    
1270 O  OD1   . ASP A 183 ? 1.2380 1.0490 1.0546 -0.3345 -0.0375 0.2668  176 ASP A OD1   
1271 O  OD2   . ASP A 183 ? 1.2790 1.0415 1.0546 -0.3173 -0.0467 0.2787  176 ASP A OD2   
1272 N  N     . MET A 184 ? 1.0693 0.8820 0.9133 -0.2738 -0.0369 0.2094  177 MET A N     
1273 C  CA    . MET A 184 ? 1.0147 0.8709 0.8839 -0.2713 -0.0267 0.1960  177 MET A CA    
1274 C  C     . MET A 184 ? 1.0091 0.9229 0.8868 -0.2802 -0.0091 0.2042  177 MET A C     
1275 O  O     . MET A 184 ? 0.9636 0.9198 0.8615 -0.2744 0.0015  0.1933  177 MET A O     
1276 C  CB    . MET A 184 ? 0.9435 0.7999 0.8176 -0.2416 -0.0245 0.1736  177 MET A CB    
1277 C  CG    . MET A 184 ? 0.9500 0.7552 0.8158 -0.2301 -0.0396 0.1642  177 MET A CG    
1278 S  SD    . MET A 184 ? 0.8663 0.6826 0.7421 -0.1986 -0.0343 0.1389  177 MET A SD    
1279 C  CE    . MET A 184 ? 0.8921 0.6491 0.7523 -0.1841 -0.0505 0.1325  177 MET A CE    
1280 N  N     . ASN A 185 ? 1.0633 0.9778 0.9244 -0.2948 -0.0065 0.2241  178 ASN A N     
1281 C  CA    . ASN A 185 ? 1.0633 1.0303 0.9258 -0.2989 0.0112  0.2312  178 ASN A CA    
1282 C  C     . ASN A 185 ? 1.0656 1.0815 0.9540 -0.3157 0.0209  0.2336  178 ASN A C     
1283 O  O     . ASN A 185 ? 1.0303 1.0967 0.9322 -0.3065 0.0365  0.2253  178 ASN A O     
1284 C  CB    . ASN A 185 ? 1.1300 1.0839 0.9658 -0.3121 0.0107  0.2535  178 ASN A CB    
1285 C  CG    . ASN A 185 ? 1.1146 1.0483 0.9282 -0.2900 0.0087  0.2487  178 ASN A CG    
1286 O  OD1   . ASN A 185 ? 1.0720 1.0379 0.8864 -0.2731 0.0206  0.2374  178 ASN A OD1   
1287 N  ND2   . ASN A 185 ? 1.1556 1.0361 0.9489 -0.2903 -0.0071 0.2576  178 ASN A ND2   
1288 N  N     . ASP A 186 ? 1.1113 1.1129 1.0075 -0.3401 0.0111  0.2445  179 ASP A N     
1289 C  CA    . ASP A 186 ? 1.1247 1.1766 1.0466 -0.3596 0.0196  0.2502  179 ASP A CA    
1290 C  C     . ASP A 186 ? 1.0542 1.1355 1.0021 -0.3409 0.0239  0.2276  179 ASP A C     
1291 O  O     . ASP A 186 ? 1.0362 1.1753 1.0039 -0.3393 0.0387  0.2246  179 ASP A O     
1292 C  CB    . ASP A 186 ? 1.1971 1.2238 1.1203 -0.3923 0.0059  0.2679  179 ASP A CB    
1293 C  CG    . ASP A 186 ? 1.2763 1.2808 1.1744 -0.4137 0.0035  0.2938  179 ASP A CG    
1294 O  OD1   . ASP A 186 ? 1.2788 1.3017 1.1611 -0.4065 0.0157  0.3002  179 ASP A OD1   
1295 O  OD2   . ASP A 186 ? 1.3393 1.3046 1.2315 -0.4371 -0.0118 0.3071  179 ASP A OD2   
1296 N  N     . HIS A 187 ? 1.0179 1.0591 0.9640 -0.3250 0.0113  0.2115  180 HIS A N     
1297 C  CA    . HIS A 187 ? 0.9527 1.0134 0.9182 -0.3051 0.0138  0.1903  180 HIS A CA    
1298 C  C     . HIS A 187 ? 0.9012 0.9968 0.8680 -0.2810 0.0298  0.1792  180 HIS A C     
1299 O  O     . HIS A 187 ? 0.8730 1.0146 0.8612 -0.2745 0.0398  0.1710  180 HIS A O     
1300 C  CB    . HIS A 187 ? 0.9341 0.9414 0.8917 -0.2936 -0.0023 0.1773  180 HIS A CB    
1301 C  CG    . HIS A 187 ? 0.9790 0.9620 0.9419 -0.3151 -0.0176 0.1822  180 HIS A CG    
1302 N  ND1   . HIS A 187 ? 0.9820 0.9995 0.9701 -0.3283 -0.0179 0.1813  180 HIS A ND1   
1303 C  CD2   . HIS A 187 ? 1.0266 0.9536 0.9726 -0.3249 -0.0342 0.1872  180 HIS A CD2   
1304 C  CE1   . HIS A 187 ? 1.0311 1.0134 1.0164 -0.3474 -0.0346 0.1859  180 HIS A CE1   
1305 N  NE2   . HIS A 187 ? 1.0596 0.9849 1.0187 -0.3451 -0.0447 0.1889  180 HIS A NE2   
1306 N  N     . LEU A 188 ? 0.8945 0.9672 0.8381 -0.2677 0.0311  0.1787  181 LEU A N     
1307 C  CA    . LEU A 188 ? 0.8530 0.9506 0.7934 -0.2454 0.0438  0.1675  181 LEU A CA    
1308 C  C     . LEU A 188 ? 0.8732 1.0276 0.8219 -0.2526 0.0609  0.1746  181 LEU A C     
1309 O  O     . LEU A 188 ? 0.8390 1.0280 0.7975 -0.2358 0.0722  0.1619  181 LEU A O     
1310 C  CB    . LEU A 188 ? 0.8547 0.9157 0.7681 -0.2341 0.0394  0.1684  181 LEU A CB    
1311 C  CG    . LEU A 188 ? 0.8047 0.8332 0.7152 -0.2113 0.0312  0.1510  181 LEU A CG    
1312 C  CD1   . LEU A 188 ? 0.7494 0.8077 0.6711 -0.1909 0.0413  0.1336  181 LEU A CD1   
1313 C  CD2   . LEU A 188 ? 0.8030 0.8005 0.7217 -0.2155 0.0178  0.1469  181 LEU A CD2   
1314 N  N     . ASN A 189 ? 0.9349 1.0990 0.8792 -0.2780 0.0627  0.1954  182 ASN A N     
1315 C  CA    . ASN A 189 ? 0.9632 1.1854 0.9160 -0.2870 0.0800  0.2038  182 ASN A CA    
1316 C  C     . ASN A 189 ? 0.9481 1.2163 0.9354 -0.2897 0.0854  0.1974  182 ASN A C     
1317 O  O     . ASN A 189 ? 0.9493 1.2719 0.9490 -0.2843 0.1015  0.1948  182 ASN A O     
1318 C  CB    . ASN A 189 ? 1.0390 1.2587 0.9777 -0.3158 0.0802  0.2298  182 ASN A CB    
1319 C  CG    . ASN A 189 ? 1.0616 1.2484 0.9652 -0.3114 0.0782  0.2374  182 ASN A CG    
1320 O  OD1   . ASN A 189 ? 1.0267 1.2134 0.9181 -0.2878 0.0831  0.2243  182 ASN A OD1   
1321 N  ND2   . ASN A 189 ? 1.1255 1.2840 1.0125 -0.3347 0.0700  0.2593  182 ASN A ND2   
1322 N  N     . ALA A 190 ? 0.9410 1.1886 0.9433 -0.2983 0.0714  0.1954  183 ALA A N     
1323 C  CA    . ALA A 190 ? 0.9271 1.2146 0.9623 -0.3003 0.0730  0.1890  183 ALA A CA    
1324 C  C     . ALA A 190 ? 0.8609 1.1556 0.9053 -0.2694 0.0754  0.1658  183 ALA A C     
1325 O  O     . ALA A 190 ? 0.8492 1.1937 0.9169 -0.2615 0.0851  0.1591  183 ALA A O     
1326 C  CB    . ALA A 190 ? 0.9510 1.2098 0.9945 -0.3215 0.0554  0.1953  183 ALA A CB    
1327 N  N     . LEU A 191 ? 0.8227 1.0681 0.8493 -0.2522 0.0663  0.1543  184 LEU A N     
1328 C  CA    . LEU A 191 ? 0.7644 1.0079 0.7975 -0.2256 0.0661  0.1339  184 LEU A CA    
1329 C  C     . LEU A 191 ? 0.7441 1.0116 0.7707 -0.2043 0.0805  0.1247  184 LEU A C     
1330 O  O     . LEU A 191 ? 0.7167 1.0112 0.7587 -0.1875 0.0862  0.1118  184 LEU A O     
1331 C  CB    . LEU A 191 ? 0.7387 0.9233 0.7554 -0.2173 0.0517  0.1265  184 LEU A CB    
1332 C  CG    . LEU A 191 ? 0.7544 0.9111 0.7766 -0.2322 0.0359  0.1293  184 LEU A CG    
1333 C  CD1   . LEU A 191 ? 0.7464 0.8440 0.7470 -0.2257 0.0235  0.1251  184 LEU A CD1   
1334 C  CD2   . LEU A 191 ? 0.7295 0.9084 0.7753 -0.2265 0.0331  0.1186  184 LEU A CD2   
1335 N  N     . GLN A 192 ? 0.7613 1.0152 0.7632 -0.2042 0.0849  0.1307  185 GLN A N     
1336 C  CA    . GLN A 192 ? 0.7549 1.0312 0.7469 -0.1868 0.0982  0.1229  185 GLN A CA    
1337 C  C     . GLN A 192 ? 0.7017 0.9649 0.6956 -0.1606 0.0959  0.1024  185 GLN A C     
1338 O  O     . GLN A 192 ? 0.6901 0.9842 0.6936 -0.1445 0.1053  0.0908  185 GLN A O     
1339 C  CB    . GLN A 192 ? 0.7859 1.1231 0.7930 -0.1908 0.1143  0.1268  185 GLN A CB    
1340 C  CG    . GLN A 192 ? 0.8447 1.1983 0.8495 -0.2190 0.1178  0.1491  185 GLN A CG    
1341 C  CD    . GLN A 192 ? 0.8812 1.2889 0.8853 -0.2180 0.1373  0.1526  185 GLN A CD    
1342 O  OE1   . GLN A 192 ? 0.8766 1.3313 0.9028 -0.2074 0.1477  0.1437  185 GLN A OE1   
1343 N  NE2   . GLN A 192 ? 0.9213 1.3228 0.8988 -0.2274 0.1422  0.1653  185 GLN A NE2   
1344 N  N     . PRO A 193 ? 0.6728 0.8889 0.6563 -0.1549 0.0835  0.0974  186 PRO A N     
1345 C  CA    . PRO A 193 ? 0.6288 0.8302 0.6098 -0.1320 0.0818  0.0802  186 PRO A CA    
1346 C  C     . PRO A 193 ? 0.6364 0.8423 0.5982 -0.1209 0.0898  0.0760  186 PRO A C     
1347 O  O     . PRO A 193 ? 0.6681 0.8693 0.6124 -0.1308 0.0914  0.0871  186 PRO A O     
1348 C  CB    . PRO A 193 ? 0.6099 0.7635 0.5828 -0.1333 0.0677  0.0801  186 PRO A CB    
1349 C  CG    . PRO A 193 ? 0.6497 0.7865 0.6088 -0.1516 0.0636  0.0964  186 PRO A CG    
1350 C  CD    . PRO A 193 ? 0.6873 0.8621 0.6588 -0.1690 0.0711  0.1080  186 PRO A CD    
1351 N  N     . PHE A 194 ? 0.6125 0.8242 0.5756 -0.1010 0.0936  0.0603  187 PHE A N     
1352 C  CA    . PHE A 194 ? 0.6228 0.8358 0.5663 -0.0897 0.0995  0.0538  187 PHE A CA    
1353 C  C     . PHE A 194 ? 0.6099 0.7815 0.5343 -0.0882 0.0894  0.0540  187 PHE A C     
1354 O  O     . PHE A 194 ? 0.6268 0.7955 0.5315 -0.0839 0.0916  0.0526  187 PHE A O     
1355 C  CB    . PHE A 194 ? 0.6105 0.8401 0.5609 -0.0694 0.1054  0.0366  187 PHE A CB    
1356 C  CG    . PHE A 194 ? 0.5725 0.7699 0.5218 -0.0557 0.0964  0.0241  187 PHE A CG    
1357 C  CD1   . PHE A 194 ? 0.5413 0.7242 0.5062 -0.0557 0.0882  0.0227  187 PHE A CD1   
1358 C  CD2   . PHE A 194 ? 0.5726 0.7525 0.5032 -0.0454 0.0949  0.0153  187 PHE A CD2   
1359 C  CE1   . PHE A 194 ? 0.5112 0.6664 0.4743 -0.0449 0.0808  0.0130  187 PHE A CE1   
1360 C  CE2   . PHE A 194 ? 0.5422 0.6935 0.4725 -0.0358 0.0864  0.0058  187 PHE A CE2   
1361 C  CZ    . PHE A 194 ? 0.5117 0.6516 0.4584 -0.0357 0.0801  0.0051  187 PHE A CZ    
1362 N  N     . ARG A 195 ? 0.5851 0.7269 0.5152 -0.0918 0.0781  0.0560  188 ARG A N     
1363 C  CA    . ARG A 195 ? 0.5684 0.6742 0.4862 -0.0870 0.0684  0.0537  188 ARG A CA    
1364 C  C     . ARG A 195 ? 0.5637 0.6447 0.4869 -0.0968 0.0585  0.0614  188 ARG A C     
1365 O  O     . ARG A 195 ? 0.5473 0.6298 0.4864 -0.0981 0.0563  0.0587  188 ARG A O     
1366 C  CB    . ARG A 195 ? 0.5346 0.6334 0.4562 -0.0699 0.0671  0.0377  188 ARG A CB    
1367 C  CG    . ARG A 195 ? 0.5189 0.5878 0.4305 -0.0643 0.0582  0.0344  188 ARG A CG    
1368 C  CD    . ARG A 195 ? 0.4978 0.5645 0.4108 -0.0500 0.0584  0.0197  188 ARG A CD    
1369 N  NE    . ARG A 195 ? 0.4861 0.5303 0.3918 -0.0453 0.0506  0.0162  188 ARG A NE    
1370 C  CZ    . ARG A 195 ? 0.5042 0.5449 0.3942 -0.0438 0.0486  0.0159  188 ARG A CZ    
1371 N  NH1   . ARG A 195 ? 0.5368 0.5931 0.4133 -0.0465 0.0544  0.0191  188 ARG A NH1   
1372 N  NH2   . ARG A 195 ? 0.4928 0.5168 0.3805 -0.0394 0.0410  0.0120  188 ARG A NH2   
1373 N  N     . TRP A 196 ? 0.5838 0.6412 0.4924 -0.1032 0.0517  0.0709  189 TRP A N     
1374 C  CA    . TRP A 196 ? 0.5911 0.6205 0.5008 -0.1116 0.0415  0.0780  189 TRP A CA    
1375 C  C     . TRP A 196 ? 0.5820 0.5809 0.4812 -0.1021 0.0327  0.0751  189 TRP A C     
1376 O  O     . TRP A 196 ? 0.6077 0.5964 0.4912 -0.1036 0.0295  0.0826  189 TRP A O     
1377 C  CB    . TRP A 196 ? 0.6394 0.6688 0.5426 -0.1306 0.0407  0.0952  189 TRP A CB    
1378 C  CG    . TRP A 196 ? 0.6575 0.6521 0.5588 -0.1392 0.0285  0.1021  189 TRP A CG    
1379 C  CD1   . TRP A 196 ? 0.6355 0.6116 0.5465 -0.1348 0.0213  0.0940  189 TRP A CD1   
1380 C  CD2   . TRP A 196 ? 0.7087 0.6812 0.5960 -0.1536 0.0215  0.1183  189 TRP A CD2   
1381 N  NE1   . TRP A 196 ? 0.6690 0.6120 0.5726 -0.1437 0.0104  0.1020  189 TRP A NE1   
1382 C  CE2   . TRP A 196 ? 0.7150 0.6535 0.6045 -0.1556 0.0097  0.1174  189 TRP A CE2   
1383 C  CE3   . TRP A 196 ? 0.7551 0.7314 0.6263 -0.1648 0.0237  0.1337  189 TRP A CE3   
1384 C  CZ2   . TRP A 196 ? 0.7670 0.6727 0.6440 -0.1677 -0.0008 0.1307  189 TRP A CZ2   
1385 C  CZ3   . TRP A 196 ? 0.8056 0.7501 0.6645 -0.1781 0.0134  0.1487  189 TRP A CZ3   
1386 C  CH2   . TRP A 196 ? 0.8119 0.7202 0.6739 -0.1791 0.0008  0.1469  189 TRP A CH2   
1387 N  N     . LYS A 197 ? 0.5477 0.5344 0.4559 -0.0918 0.0286  0.0643  190 LYS A N     
1388 C  CA    . LYS A 197 ? 0.5391 0.5031 0.4411 -0.0819 0.0214  0.0608  190 LYS A CA    
1389 C  C     . LYS A 197 ? 0.5652 0.5000 0.4623 -0.0871 0.0116  0.0685  190 LYS A C     
1390 O  O     . LYS A 197 ? 0.5671 0.4922 0.4709 -0.0919 0.0085  0.0680  190 LYS A O     
1391 C  CB    . LYS A 197 ? 0.4987 0.4616 0.4115 -0.0696 0.0214  0.0474  190 LYS A CB    
1392 C  CG    . LYS A 197 ? 0.4744 0.4595 0.3935 -0.0631 0.0291  0.0380  190 LYS A CG    
1393 C  CD    . LYS A 197 ? 0.4786 0.4730 0.3883 -0.0577 0.0318  0.0348  190 LYS A CD    
1394 C  CE    . LYS A 197 ? 0.4703 0.4517 0.3763 -0.0498 0.0257  0.0307  190 LYS A CE    
1395 N  NZ    . LYS A 197 ? 0.4398 0.4192 0.3564 -0.0416 0.0254  0.0203  190 LYS A NZ    
1396 N  N     . CYS A 198 ? 0.5911 0.5101 0.4749 -0.0856 0.0055  0.0754  191 CYS A N     
1397 C  CA    . CYS A 198 ? 0.6222 0.5090 0.4995 -0.0869 -0.0052 0.0818  191 CYS A CA    
1398 C  C     . CYS A 198 ? 0.6089 0.4825 0.4871 -0.0706 -0.0112 0.0743  191 CYS A C     
1399 O  O     . CYS A 198 ? 0.6160 0.4924 0.4870 -0.0651 -0.0132 0.0766  191 CYS A O     
1400 C  CB    . CYS A 198 ? 0.6744 0.5521 0.5360 -0.0994 -0.0087 0.0984  191 CYS A CB    
1401 S  SG    . CYS A 198 ? 0.7021 0.5898 0.5664 -0.1217 -0.0042 0.1091  191 CYS A SG    
1402 N  N     . PHE A 199 ? 0.5910 0.4537 0.4786 -0.0628 -0.0135 0.0648  192 PHE A N     
1403 C  CA    . PHE A 199 ? 0.5796 0.4350 0.4712 -0.0472 -0.0175 0.0572  192 PHE A CA    
1404 C  C     . PHE A 199 ? 0.6214 0.4448 0.5055 -0.0422 -0.0284 0.0611  192 PHE A C     
1405 O  O     . PHE A 199 ? 0.6425 0.4454 0.5242 -0.0463 -0.0324 0.0612  192 PHE A O     
1406 C  CB    . PHE A 199 ? 0.5429 0.4056 0.4472 -0.0401 -0.0129 0.0444  192 PHE A CB    
1407 C  CG    . PHE A 199 ? 0.5066 0.3942 0.4191 -0.0442 -0.0036 0.0393  192 PHE A CG    
1408 C  CD1   . PHE A 199 ? 0.4873 0.3950 0.4014 -0.0421 0.0012  0.0373  192 PHE A CD1   
1409 C  CD2   . PHE A 199 ? 0.4969 0.3862 0.4147 -0.0493 -0.0009 0.0360  192 PHE A CD2   
1410 C  CE1   . PHE A 199 ? 0.4611 0.3880 0.3818 -0.0440 0.0088  0.0320  192 PHE A CE1   
1411 C  CE2   . PHE A 199 ? 0.4687 0.3801 0.3943 -0.0513 0.0065  0.0316  192 PHE A CE2   
1412 C  CZ    . PHE A 199 ? 0.4522 0.3813 0.3790 -0.0482 0.0115  0.0297  192 PHE A CZ    
1413 N  N     . GLN A 200 ? 0.6377 0.4558 0.5180 -0.0324 -0.0345 0.0637  193 GLN A N     
1414 C  CA    . GLN A 200 ? 0.6738 0.4639 0.5508 -0.0213 -0.0447 0.0636  193 GLN A CA    
1415 C  C     . GLN A 200 ? 0.6497 0.4421 0.5386 -0.0093 -0.0416 0.0494  193 GLN A C     
1416 O  O     . GLN A 200 ? 0.6101 0.4276 0.5108 -0.0030 -0.0349 0.0417  193 GLN A O     
1417 C  CB    . GLN A 200 ? 0.6928 0.4836 0.5668 -0.0109 -0.0516 0.0683  193 GLN A CB    
1418 C  CG    . GLN A 200 ? 0.7403 0.5010 0.6100 0.0024  -0.0635 0.0694  193 GLN A CG    
1419 C  CD    . GLN A 200 ? 0.7576 0.5240 0.6279 0.0147  -0.0710 0.0732  193 GLN A CD    
1420 O  OE1   . GLN A 200 ? 0.7372 0.5282 0.6089 0.0116  -0.0682 0.0756  193 GLN A OE1   
1421 N  NE2   . GLN A 200 ? 0.8003 0.5433 0.6693 0.0299  -0.0815 0.0730  193 GLN A NE2   
1422 N  N     . VAL A 201 ? 0.6775 0.4434 0.5620 -0.0072 -0.0464 0.0460  194 VAL A N     
1423 C  CA    . VAL A 201 ? 0.6594 0.4287 0.5521 0.0037  -0.0425 0.0322  194 VAL A CA    
1424 C  C     . VAL A 201 ? 0.6462 0.4329 0.5498 0.0211  -0.0410 0.0264  194 VAL A C     
1425 O  O     . VAL A 201 ? 0.6765 0.4546 0.5783 0.0308  -0.0487 0.0306  194 VAL A O     
1426 C  CB    . VAL A 201 ? 0.7038 0.4380 0.5867 0.0062  -0.0500 0.0280  194 VAL A CB    
1427 C  CG1   . VAL A 201 ? 0.7621 0.4649 0.6353 0.0165  -0.0621 0.0324  194 VAL A CG1   
1428 C  CG2   . VAL A 201 ? 0.6878 0.4279 0.5762 0.0169  -0.0447 0.0134  194 VAL A CG2   
1429 N  N     . LEU A 202 ? 0.6026 0.4162 0.5185 0.0238  -0.0313 0.0180  195 LEU A N     
1430 C  CA    . LEU A 202 ? 0.5853 0.4231 0.5146 0.0356  -0.0283 0.0138  195 LEU A CA    
1431 C  C     . LEU A 202 ? 0.5886 0.4293 0.5243 0.0491  -0.0244 0.0026  195 LEU A C     
1432 O  O     . LEU A 202 ? 0.5793 0.4161 0.5115 0.0456  -0.0195 -0.0033 195 LEU A O     
1433 C  CB    . LEU A 202 ? 0.5393 0.4059 0.4766 0.0260  -0.0205 0.0144  195 LEU A CB    
1434 C  CG    . LEU A 202 ? 0.5210 0.4147 0.4733 0.0335  -0.0176 0.0108  195 LEU A CG    
1435 C  CD1   . LEU A 202 ? 0.5422 0.4388 0.4954 0.0382  -0.0260 0.0171  195 LEU A CD1   
1436 C  CD2   . LEU A 202 ? 0.4808 0.3954 0.4388 0.0234  -0.0098 0.0091  195 LEU A CD2   
1437 N  N     . ILE A 203 ? 0.6080 0.4559 0.5521 0.0652  -0.0271 0.0000  196 ILE A N     
1438 C  CA    . ILE A 203 ? 0.6115 0.4725 0.5646 0.0795  -0.0211 -0.0105 196 ILE A CA    
1439 C  C     . ILE A 203 ? 0.5698 0.4691 0.5395 0.0761  -0.0116 -0.0119 196 ILE A C     
1440 O  O     . ILE A 203 ? 0.5590 0.4768 0.5389 0.0744  -0.0137 -0.0068 196 ILE A O     
1441 C  CB    . ILE A 203 ? 0.6571 0.5121 0.6142 0.0999  -0.0282 -0.0128 196 ILE A CB    
1442 C  CG1   . ILE A 203 ? 0.7074 0.5189 0.6464 0.1029  -0.0400 -0.0100 196 ILE A CG1   
1443 C  CG2   . ILE A 203 ? 0.6646 0.5376 0.6311 0.1155  -0.0200 -0.0244 196 ILE A CG2   
1444 C  CD1   . ILE A 203 ? 0.7222 0.5070 0.6463 0.0990  -0.0391 -0.0166 196 ILE A CD1   
1445 N  N     . VAL A 204 ? 0.5530 0.4628 0.5242 0.0750  -0.0020 -0.0186 197 VAL A N     
1446 C  CA    . VAL A 204 ? 0.5215 0.4644 0.5072 0.0709  0.0068  -0.0192 197 VAL A CA    
1447 C  C     . VAL A 204 ? 0.5397 0.4987 0.5328 0.0848  0.0138  -0.0271 197 VAL A C     
1448 O  O     . VAL A 204 ? 0.5525 0.4996 0.5344 0.0885  0.0177  -0.0336 197 VAL A O     
1449 C  CB    . VAL A 204 ? 0.4871 0.4306 0.4673 0.0550  0.0124  -0.0180 197 VAL A CB    
1450 C  CG1   . VAL A 204 ? 0.4649 0.4375 0.4578 0.0513  0.0211  -0.0187 197 VAL A CG1   
1451 C  CG2   . VAL A 204 ? 0.4712 0.4052 0.4459 0.0424  0.0073  -0.0110 197 VAL A CG2   
1452 N  N     . THR A 205 ? 0.5440 0.5320 0.5557 0.0922  0.0152  -0.0264 198 THR A N     
1453 C  CA    . THR A 205 ? 0.5634 0.5755 0.5857 0.1054  0.0236  -0.0329 198 THR A CA    
1454 C  C     . THR A 205 ? 0.5475 0.5677 0.5641 0.0975  0.0351  -0.0359 198 THR A C     
1455 O  O     . THR A 205 ? 0.5144 0.5425 0.5329 0.0812  0.0381  -0.0306 198 THR A O     
1456 C  CB    . THR A 205 ? 0.5645 0.6132 0.6116 0.1092  0.0234  -0.0294 198 THR A CB    
1457 O  OG1   . THR A 205 ? 0.5799 0.6163 0.6281 0.1150  0.0108  -0.0255 198 THR A OG1   
1458 C  CG2   . THR A 205 ? 0.5931 0.6712 0.6541 0.1255  0.0319  -0.0359 198 THR A CG2   
1459 N  N     . GLY A 206 ? 0.5767 0.5931 0.5844 0.1099  0.0408  -0.0446 199 GLY A N     
1460 C  CA    . GLY A 206 ? 0.5713 0.5955 0.5707 0.1045  0.0513  -0.0475 199 GLY A CA    
1461 C  C     . GLY A 206 ? 0.5624 0.5540 0.5392 0.0950  0.0483  -0.0488 199 GLY A C     
1462 O  O     . GLY A 206 ? 0.5633 0.5581 0.5301 0.0915  0.0554  -0.0513 199 GLY A O     
1463 N  N     . GLU A 207 ? 0.5570 0.5196 0.5260 0.0901  0.0375  -0.0463 200 GLU A N     
1464 C  CA    . GLU A 207 ? 0.5494 0.4847 0.5008 0.0795  0.0333  -0.0463 200 GLU A CA    
1465 C  C     . GLU A 207 ? 0.5884 0.4888 0.5240 0.0876  0.0243  -0.0523 200 GLU A C     
1466 O  O     . GLU A 207 ? 0.6069 0.4901 0.5262 0.0875  0.0238  -0.0587 200 GLU A O     
1467 C  CB    . GLU A 207 ? 0.5117 0.4451 0.4677 0.0632  0.0290  -0.0369 200 GLU A CB    
1468 C  CG    . GLU A 207 ? 0.4779 0.4349 0.4428 0.0523  0.0362  -0.0321 200 GLU A CG    
1469 C  CD    . GLU A 207 ? 0.4709 0.4234 0.4242 0.0451  0.0402  -0.0334 200 GLU A CD    
1470 O  OE1   . GLU A 207 ? 0.4921 0.4256 0.4304 0.0485  0.0377  -0.0390 200 GLU A OE1   
1471 O  OE2   . GLU A 207 ? 0.4478 0.4135 0.4061 0.0357  0.0443  -0.0286 200 GLU A OE2   
1472 N  N     . ASN A 208 ? 0.6057 0.4932 0.5447 0.0936  0.0158  -0.0499 201 ASN A N     
1473 C  CA    . ASN A 208 ? 0.6456 0.4941 0.5687 0.0973  0.0049  -0.0529 201 ASN A CA    
1474 C  C     . ASN A 208 ? 0.6863 0.5268 0.6135 0.1155  -0.0012 -0.0549 201 ASN A C     
1475 O  O     . ASN A 208 ? 0.7172 0.5250 0.6344 0.1160  -0.0125 -0.0527 201 ASN A O     
1476 C  CB    . ASN A 208 ? 0.6283 0.4579 0.5455 0.0789  -0.0025 -0.0438 201 ASN A CB    
1477 C  CG    . ASN A 208 ? 0.6064 0.4468 0.5354 0.0733  -0.0054 -0.0330 201 ASN A CG    
1478 O  OD1   . ASN A 208 ? 0.5982 0.4622 0.5413 0.0813  -0.0021 -0.0322 201 ASN A OD1   
1479 N  ND2   . ASN A 208 ? 0.6014 0.4264 0.5248 0.0596  -0.0117 -0.0248 201 ASN A ND2   
1480 N  N     . ASP A 209 ? 0.6923 0.5621 0.6339 0.1306  0.0057  -0.0591 202 ASP A N     
1481 C  CA    . ASP A 209 ? 0.7246 0.5955 0.6760 0.1478  -0.0003 -0.0589 202 ASP A CA    
1482 C  C     . ASP A 209 ? 0.7828 0.6462 0.7289 0.1727  0.0005  -0.0724 202 ASP A C     
1483 O  O     . ASP A 209 ? 0.8155 0.6817 0.7710 0.1904  -0.0045 -0.0734 202 ASP A O     
1484 C  CB    . ASP A 209 ? 0.6948 0.6097 0.6715 0.1481  0.0051  -0.0529 202 ASP A CB    
1485 C  CG    . ASP A 209 ? 0.6786 0.6323 0.6666 0.1496  0.0198  -0.0576 202 ASP A CG    
1486 O  OD1   . ASP A 209 ? 0.6727 0.6205 0.6475 0.1436  0.0265  -0.0623 202 ASP A OD1   
1487 O  OD2   . ASP A 209 ? 0.6736 0.6643 0.6836 0.1550  0.0241  -0.0553 202 ASP A OD2   
1488 N  N     . SER A 210 ? 0.8002 0.6559 0.7313 0.1760  0.0066  -0.0832 203 SER A N     
1489 C  CA    . SER A 210 ? 0.8637 0.7096 0.7865 0.2015  0.0072  -0.0979 203 SER A CA    
1490 C  C     . SER A 210 ? 0.8929 0.7082 0.7885 0.2001  0.0069  -0.1090 203 SER A C     
1491 O  O     . SER A 210 ? 0.8668 0.6648 0.7510 0.1793  0.0035  -0.1042 203 SER A O     
1492 C  CB    . SER A 210 ? 0.8646 0.7603 0.8070 0.2164  0.0212  -0.1025 203 SER A CB    
1493 O  OG    . SER A 210 ? 0.8413 0.7612 0.7802 0.2076  0.0350  -0.1051 203 SER A OG    
1494 N  N     . ASP A 211 ? 0.9518 0.7619 0.8370 0.2234  0.0101  -0.1248 204 ASP A N     
1495 C  CA    . ASP A 211 ? 0.9854 0.7702 0.8432 0.2236  0.0104  -0.1373 204 ASP A CA    
1496 C  C     . ASP A 211 ? 0.9631 0.7886 0.8218 0.2214  0.0278  -0.1408 204 ASP A C     
1497 O  O     . ASP A 211 ? 0.9906 0.8011 0.8257 0.2215  0.0294  -0.1511 204 ASP A O     
1498 C  CB    . ASP A 211 ? 1.0722 0.8199 0.9115 0.2493  0.0023  -0.1539 204 ASP A CB    
1499 C  CG    . ASP A 211 ? 1.1011 0.8034 0.9371 0.2496  -0.0163 -0.1485 204 ASP A CG    
1500 O  OD1   . ASP A 211 ? 1.0821 0.7550 0.9087 0.2262  -0.0265 -0.1393 204 ASP A OD1   
1501 O  OD2   . ASP A 211 ? 1.1443 0.8431 0.9880 0.2728  -0.0205 -0.1523 204 ASP A OD2   
1502 N  N     . LYS A 212 ? 0.9206 0.7963 0.8049 0.2192  0.0399  -0.1322 205 LYS A N     
1503 C  CA    . LYS A 212 ? 0.8970 0.8111 0.7830 0.2122  0.0559  -0.1314 205 LYS A CA    
1504 C  C     . LYS A 212 ? 0.8367 0.7485 0.7210 0.1835  0.0544  -0.1188 205 LYS A C     
1505 O  O     . LYS A 212 ? 0.8259 0.7526 0.7014 0.1751  0.0634  -0.1187 205 LYS A O     
1506 C  CB    . LYS A 212 ? 0.8834 0.8521 0.7983 0.2198  0.0688  -0.1266 205 LYS A CB    
1507 C  CG    . LYS A 212 ? 0.9456 0.9312 0.8649 0.2502  0.0751  -0.1400 205 LYS A CG    
1508 C  CD    . LYS A 212 ? 0.9765 0.9409 0.9046 0.2680  0.0620  -0.1427 205 LYS A CD    
1509 C  CE    . LYS A 212 ? 1.0394 1.0262 0.9760 0.3005  0.0686  -0.1558 205 LYS A CE    
1510 N  NZ    . LYS A 212 ? 1.0167 1.0694 0.9865 0.3018  0.0828  -0.1486 205 LYS A NZ    
1511 N  N     . THR A 213 ? 0.8028 0.6962 0.6944 0.1696  0.0431  -0.1084 206 THR A N     
1512 C  CA    . THR A 213 ? 0.7484 0.6413 0.6407 0.1446  0.0416  -0.0969 206 THR A CA    
1513 C  C     . THR A 213 ? 0.7649 0.6188 0.6325 0.1360  0.0322  -0.1014 206 THR A C     
1514 O  O     . THR A 213 ? 0.8188 0.6435 0.6685 0.1481  0.0260  -0.1131 206 THR A O     
1515 C  CB    . THR A 213 ? 0.7082 0.6065 0.6207 0.1349  0.0358  -0.0841 206 THR A CB    
1516 O  OG1   . THR A 213 ? 0.7415 0.6088 0.6498 0.1440  0.0236  -0.0862 206 THR A OG1   
1517 C  CG2   . THR A 213 ? 0.6866 0.6282 0.6240 0.1380  0.0449  -0.0785 206 THR A CG2   
1518 N  N     . LEU A 214 ? 0.7233 0.5771 0.5900 0.1154  0.0307  -0.0928 207 LEU A N     
1519 C  CA    . LEU A 214 ? 0.7382 0.5622 0.5843 0.1056  0.0222  -0.0964 207 LEU A CA    
1520 C  C     . LEU A 214 ? 0.7521 0.5408 0.5954 0.1000  0.0076  -0.0940 207 LEU A C     
1521 O  O     . LEU A 214 ? 0.7797 0.5384 0.6058 0.0933  -0.0020 -0.0983 207 LEU A O     
1522 C  CB    . LEU A 214 ? 0.6926 0.5335 0.5411 0.0876  0.0261  -0.0878 207 LEU A CB    
1523 C  CG    . LEU A 214 ? 0.6919 0.5604 0.5365 0.0908  0.0388  -0.0897 207 LEU A CG    
1524 C  CD1   . LEU A 214 ? 0.6448 0.5306 0.4967 0.0739  0.0419  -0.0782 207 LEU A CD1   
1525 C  CD2   . LEU A 214 ? 0.7438 0.5957 0.5611 0.0984  0.0376  -0.1026 207 LEU A CD2   
1526 N  N     . ARG A 215 ? 0.7370 0.5298 0.5966 0.1017  0.0055  -0.0863 208 ARG A N     
1527 C  CA    . ARG A 215 ? 0.7574 0.5180 0.6142 0.0978  -0.0076 -0.0821 208 ARG A CA    
1528 C  C     . ARG A 215 ? 0.7791 0.5400 0.6455 0.1146  -0.0092 -0.0821 208 ARG A C     
1529 O  O     . ARG A 215 ? 0.7612 0.5552 0.6430 0.1244  0.0002  -0.0818 208 ARG A O     
1530 C  CB    . ARG A 215 ? 0.7089 0.4763 0.5760 0.0765  -0.0099 -0.0679 208 ARG A CB    
1531 C  CG    . ARG A 215 ? 0.6854 0.4568 0.5472 0.0604  -0.0089 -0.0666 208 ARG A CG    
1532 C  CD    . ARG A 215 ? 0.7288 0.4654 0.5719 0.0543  -0.0202 -0.0720 208 ARG A CD    
1533 N  NE    . ARG A 215 ? 0.6994 0.4424 0.5452 0.0346  -0.0222 -0.0649 208 ARG A NE    
1534 C  CZ    . ARG A 215 ? 0.6806 0.4395 0.5241 0.0299  -0.0178 -0.0670 208 ARG A CZ    
1535 N  NH1   . ARG A 215 ? 0.6953 0.4607 0.5290 0.0416  -0.0117 -0.0765 208 ARG A NH1   
1536 N  NH2   . ARG A 215 ? 0.6521 0.4209 0.5023 0.0139  -0.0195 -0.0593 208 ARG A NH2   
1537 N  N     . ASN A 216 ? 0.8210 0.5447 0.6786 0.1167  -0.0223 -0.0812 209 ASN A N     
1538 C  CA    . ASN A 216 ? 0.8436 0.5620 0.7098 0.1300  -0.0276 -0.0778 209 ASN A CA    
1539 C  C     . ASN A 216 ? 0.8466 0.5386 0.7097 0.1143  -0.0398 -0.0647 209 ASN A C     
1540 O  O     . ASN A 216 ? 0.8915 0.5424 0.7374 0.1088  -0.0513 -0.0658 209 ASN A O     
1541 C  CB    . ASN A 216 ? 0.9147 0.6102 0.7699 0.1554  -0.0319 -0.0919 209 ASN A CB    
1542 C  CG    . ASN A 216 ? 0.9328 0.6370 0.8024 0.1738  -0.0343 -0.0892 209 ASN A CG    
1543 O  OD1   . ASN A 216 ? 0.9123 0.6181 0.7915 0.1651  -0.0398 -0.0757 209 ASN A OD1   
1544 N  ND2   . ASN A 216 ? 0.9719 0.6857 0.8436 0.1995  -0.0297 -0.1017 209 ASN A ND2   
1545 N  N     . ALA A 217 ? 0.8037 0.5193 0.6826 0.1062  -0.0375 -0.0520 210 ALA A N     
1546 C  CA    . ALA A 217 ? 0.8020 0.5002 0.6776 0.0892  -0.0463 -0.0384 210 ALA A CA    
1547 C  C     . ALA A 217 ? 0.8470 0.5239 0.7211 0.1004  -0.0572 -0.0328 210 ALA A C     
1548 O  O     . ALA A 217 ? 0.8567 0.5164 0.7254 0.0872  -0.0652 -0.0204 210 ALA A O     
1549 C  CB    . ALA A 217 ? 0.7372 0.4702 0.6267 0.0737  -0.0384 -0.0284 210 ALA A CB    
1550 N  N     . HIS A 218 ? 0.8778 0.5573 0.7562 0.1248  -0.0573 -0.0415 211 HIS A N     
1551 C  CA    . HIS A 218 ? 0.9208 0.5854 0.8007 0.1391  -0.0678 -0.0364 211 HIS A CA    
1552 C  C     . HIS A 218 ? 0.9853 0.5944 0.8441 0.1345  -0.0839 -0.0313 211 HIS A C     
1553 O  O     . HIS A 218 ? 1.0092 0.6038 0.8663 0.1336  -0.0939 -0.0189 211 HIS A O     
1554 C  CB    . HIS A 218 ? 0.9475 0.6277 0.8375 0.1682  -0.0644 -0.0485 211 HIS A CB    
1555 C  CG    . HIS A 218 ? 0.8964 0.6316 0.8111 0.1725  -0.0526 -0.0476 211 HIS A CG    
1556 N  ND1   . HIS A 218 ? 0.8737 0.6308 0.8029 0.1694  -0.0553 -0.0358 211 HIS A ND1   
1557 C  CD2   . HIS A 218 ? 0.8715 0.6432 0.7980 0.1796  -0.0389 -0.0570 211 HIS A CD2   
1558 C  CE1   . HIS A 218 ? 0.8359 0.6408 0.7863 0.1737  -0.0441 -0.0386 211 HIS A CE1   
1559 N  NE2   . HIS A 218 ? 0.8338 0.6487 0.7833 0.1795  -0.0335 -0.0508 211 HIS A NE2   
1560 N  N     . SER A 219 ? 1.0159 0.5936 0.8579 0.1293  -0.0873 -0.0394 212 SER A N     
1561 C  CA    . SER A 219 ? 1.0839 0.6061 0.9054 0.1224  -0.1036 -0.0346 212 SER A CA    
1562 C  C     . SER A 219 ? 1.0611 0.5791 0.8791 0.0915  -0.1063 -0.0177 212 SER A C     
1563 O  O     . SER A 219 ? 1.1166 0.5914 0.9188 0.0805  -0.1196 -0.0100 212 SER A O     
1564 C  CB    . SER A 219 ? 1.1368 0.6248 0.9406 0.1300  -0.1080 -0.0513 212 SER A CB    
1565 O  OG    . SER A 219 ? 1.0909 0.6019 0.8959 0.1181  -0.0973 -0.0586 212 SER A OG    
1566 N  N     . LEU A 220 ? 0.9849 0.5476 0.8177 0.0771  -0.0939 -0.0113 213 LEU A N     
1567 C  CA    . LEU A 220 ? 0.9643 0.5292 0.7953 0.0498  -0.0945 0.0036  213 LEU A CA    
1568 C  C     . LEU A 220 ? 0.9349 0.5243 0.7750 0.0452  -0.0921 0.0181  213 LEU A C     
1569 O  O     . LEU A 220 ? 0.9179 0.5145 0.7567 0.0237  -0.0908 0.0305  213 LEU A O     
1570 C  CB    . LEU A 220 ? 0.9084 0.5015 0.7461 0.0356  -0.0833 -0.0012 213 LEU A CB    
1571 C  CG    . LEU A 220 ? 0.9434 0.5083 0.7680 0.0302  -0.0887 -0.0110 213 LEU A CG    
1572 C  CD1   . LEU A 220 ? 0.9586 0.5209 0.7801 0.0537  -0.0859 -0.0296 213 LEU A CD1   
1573 C  CD2   . LEU A 220 ? 0.8990 0.4867 0.7290 0.0089  -0.0821 -0.0087 213 LEU A CD2   
1574 N  N     . THR A 221 ? 0.9293 0.5353 0.7790 0.0649  -0.0909 0.0158  214 THR A N     
1575 C  CA    . THR A 221 ? 0.9007 0.5337 0.7591 0.0621  -0.0888 0.0273  214 THR A CA    
1576 C  C     . THR A 221 ? 0.9582 0.5579 0.8018 0.0566  -0.1027 0.0430  214 THR A C     
1577 O  O     . THR A 221 ? 1.0244 0.5810 0.8547 0.0636  -0.1147 0.0424  214 THR A O     
1578 C  CB    . THR A 221 ? 0.8806 0.5441 0.7558 0.0839  -0.0843 0.0197  214 THR A CB    
1579 O  OG1   . THR A 221 ? 0.9377 0.5767 0.8097 0.1071  -0.0927 0.0119  214 THR A OG1   
1580 C  CG2   . THR A 221 ? 0.8198 0.5221 0.7101 0.0846  -0.0694 0.0085  214 THR A CG2   
1581 N  N     . ILE A 222 ? 0.9376 0.5560 0.7816 0.0438  -0.1011 0.0567  215 ILE A N     
1582 C  CA    . ILE A 222 ? 0.9912 0.5821 0.8190 0.0348  -0.1128 0.0743  215 ILE A CA    
1583 C  C     . ILE A 222 ? 0.9856 0.5979 0.8178 0.0438  -0.1151 0.0817  215 ILE A C     
1584 O  O     . ILE A 222 ? 0.9300 0.5833 0.7780 0.0488  -0.1056 0.0752  215 ILE A O     
1585 C  CB    . ILE A 222 ? 0.9841 0.5757 0.8031 0.0061  -0.1089 0.0864  215 ILE A CB    
1586 C  CG1   . ILE A 222 ? 0.9086 0.5502 0.7408 -0.0027 -0.0936 0.0844  215 ILE A CG1   
1587 C  CG2   . ILE A 222 ? 1.0108 0.5728 0.8225 -0.0048 -0.1118 0.0826  215 ILE A CG2   
1588 C  CD1   . ILE A 222 ? 0.9026 0.5522 0.7284 -0.0284 -0.0883 0.0957  215 ILE A CD1   
1589 N  N     . SER A 223 ? 1.0487 0.6312 0.8651 0.0437  -0.1288 0.0964  216 SER A N     
1590 C  CA    . SER A 223 ? 1.0571 0.6546 0.8731 0.0504  -0.1342 0.1060  216 SER A CA    
1591 C  C     . SER A 223 ? 1.0132 0.6443 0.8275 0.0306  -0.1244 0.1143  216 SER A C     
1592 O  O     . SER A 223 ? 0.9987 0.6309 0.8070 0.0099  -0.1170 0.1184  216 SER A O     
1593 C  CB    . SER A 223 ? 1.1442 0.6963 0.9399 0.0537  -0.1523 0.1213  216 SER A CB    
1594 O  OG    . SER A 223 ? 1.1718 0.7049 0.9478 0.0277  -0.1536 0.1381  216 SER A OG    
1595 N  N     . ASP A 224 ? 0.9997 0.6576 0.8189 0.0381  -0.1257 0.1167  217 ASP A N     
1596 C  CA    . ASP A 224 ? 0.9748 0.6602 0.7878 0.0227  -0.1195 0.1248  217 ASP A CA    
1597 C  C     . ASP A 224 ? 1.0245 0.6849 0.8129 0.0031  -0.1236 0.1436  217 ASP A C     
1598 O  O     . ASP A 224 ? 1.0010 0.6797 0.7840 -0.0156 -0.1131 0.1478  217 ASP A O     
1599 C  CB    . ASP A 224 ? 0.9760 0.6838 0.7935 0.0353  -0.1259 0.1261  217 ASP A CB    
1600 C  CG    . ASP A 224 ? 0.9260 0.6658 0.7699 0.0508  -0.1203 0.1091  217 ASP A CG    
1601 O  OD1   . ASP A 224 ? 0.8681 0.6395 0.7221 0.0427  -0.1079 0.1008  217 ASP A OD1   
1602 O  OD2   . ASP A 224 ? 0.9499 0.6826 0.8043 0.0710  -0.1286 0.1043  217 ASP A OD2   
1603 N  N     . ASP A 225 ? 1.0982 0.7170 0.8715 0.0078  -0.1390 0.1552  218 ASP A N     
1604 C  CA    . ASP A 225 ? 1.1565 0.7498 0.9047 -0.0116 -0.1445 0.1759  218 ASP A CA    
1605 C  C     . ASP A 225 ? 1.1541 0.7343 0.9005 -0.0317 -0.1372 0.1764  218 ASP A C     
1606 O  O     . ASP A 225 ? 1.1676 0.7527 0.9014 -0.0541 -0.1321 0.1898  218 ASP A O     
1607 C  CB    . ASP A 225 ? 1.2407 0.7930 0.9726 -0.0002 -0.1646 0.1893  218 ASP A CB    
1608 C  CG    . ASP A 225 ? 1.2462 0.8196 0.9761 0.0122  -0.1712 0.1939  218 ASP A CG    
1609 O  OD1   . ASP A 225 ? 1.1994 0.8029 0.9506 0.0298  -0.1684 0.1787  218 ASP A OD1   
1610 O  OD2   . ASP A 225 ? 1.2999 0.8611 1.0066 0.0029  -0.1792 0.2132  218 ASP A OD2   
1611 N  N     . GLU A 226 ? 1.1384 0.7057 0.8976 -0.0243 -0.1362 0.1617  219 GLU A N     
1612 C  CA    . GLU A 226 ? 1.1339 0.6925 0.8933 -0.0434 -0.1301 0.1607  219 GLU A CA    
1613 C  C     . GLU A 226 ? 1.0638 0.6705 0.8342 -0.0574 -0.1120 0.1564  219 GLU A C     
1614 O  O     . GLU A 226 ? 1.0737 0.6845 0.8378 -0.0802 -0.1066 0.1665  219 GLU A O     
1615 C  CB    . GLU A 226 ? 1.1372 0.6714 0.9053 -0.0304 -0.1340 0.1445  219 GLU A CB    
1616 C  CG    . GLU A 226 ? 1.2255 0.7024 0.9778 -0.0214 -0.1530 0.1506  219 GLU A CG    
1617 C  CD    . GLU A 226 ? 1.2357 0.6897 0.9951 -0.0003 -0.1579 0.1317  219 GLU A CD    
1618 O  OE1   . GLU A 226 ? 1.1801 0.6659 0.9578 0.0180  -0.1494 0.1151  219 GLU A OE1   
1619 O  OE2   . GLU A 226 ? 1.3049 0.7087 1.0505 -0.0022 -0.1705 0.1337  219 GLU A OE2   
1620 N  N     . PHE A 227 ? 0.9988 0.6421 0.7858 -0.0435 -0.1031 0.1420  220 PHE A N     
1621 C  CA    . PHE A 227 ? 0.9348 0.6207 0.7325 -0.0530 -0.0870 0.1357  220 PHE A CA    
1622 C  C     . PHE A 227 ? 0.9512 0.6534 0.7346 -0.0683 -0.0833 0.1509  220 PHE A C     
1623 O  O     . PHE A 227 ? 0.9396 0.6592 0.7227 -0.0856 -0.0733 0.1545  220 PHE A O     
1624 C  CB    . PHE A 227 ? 0.8722 0.5891 0.6885 -0.0361 -0.0802 0.1188  220 PHE A CB    
1625 C  CG    . PHE A 227 ? 0.8143 0.5704 0.6397 -0.0450 -0.0652 0.1125  220 PHE A CG    
1626 C  CD1   . PHE A 227 ? 0.7830 0.5468 0.6183 -0.0528 -0.0565 0.1049  220 PHE A CD1   
1627 C  CD2   . PHE A 227 ? 0.7972 0.5807 0.6198 -0.0453 -0.0607 0.1140  220 PHE A CD2   
1628 C  CE1   . PHE A 227 ? 0.7368 0.5344 0.5801 -0.0594 -0.0438 0.0995  220 PHE A CE1   
1629 C  CE2   . PHE A 227 ? 0.7528 0.5682 0.5819 -0.0522 -0.0477 0.1075  220 PHE A CE2   
1630 C  CZ    . PHE A 227 ? 0.7219 0.5444 0.5622 -0.0583 -0.0392 0.1003  220 PHE A CZ    
1631 N  N     . ASP A 228 ? 0.9873 0.6827 0.7573 -0.0618 -0.0922 0.1607  221 ASP A N     
1632 C  CA    . ASP A 228 ? 1.0112 0.7213 0.7634 -0.0748 -0.0893 0.1752  221 ASP A CA    
1633 C  C     . ASP A 228 ? 1.0635 0.7561 0.8003 -0.0980 -0.0893 0.1930  221 ASP A C     
1634 O  O     . ASP A 228 ? 1.0591 0.7785 0.7900 -0.1136 -0.0780 0.1994  221 ASP A O     
1635 C  CB    . ASP A 228 ? 1.0492 0.7506 0.7882 -0.0626 -0.1019 0.1831  221 ASP A CB    
1636 C  CG    . ASP A 228 ? 1.0001 0.7272 0.7551 -0.0435 -0.1012 0.1672  221 ASP A CG    
1637 O  OD1   . ASP A 228 ? 0.9374 0.6951 0.7081 -0.0437 -0.0884 0.1528  221 ASP A OD1   
1638 O  OD2   . ASP A 228 ? 1.0282 0.7437 0.7812 -0.0282 -0.1143 0.1693  221 ASP A OD2   
1639 N  N     . ARG A 229 ? 1.1170 0.7657 0.8473 -0.1006 -0.1016 0.2008  222 ARG A N     
1640 C  CA    . ARG A 229 ? 1.1767 0.8049 0.8921 -0.1249 -0.1037 0.2196  222 ARG A CA    
1641 C  C     . ARG A 229 ? 1.1400 0.7915 0.8702 -0.1417 -0.0902 0.2138  222 ARG A C     
1642 O  O     . ARG A 229 ? 1.1677 0.8304 0.8904 -0.1645 -0.0840 0.2282  222 ARG A O     
1643 C  CB    . ARG A 229 ? 1.2491 0.8193 0.9535 -0.1229 -0.1223 0.2279  222 ARG A CB    
1644 C  CG    . ARG A 229 ? 1.3110 0.8542 0.9951 -0.1124 -0.1375 0.2416  222 ARG A CG    
1645 C  CD    . ARG A 229 ? 1.3948 0.8763 1.0654 -0.1125 -0.1565 0.2517  222 ARG A CD    
1646 N  NE    . ARG A 229 ? 1.3792 0.8386 1.0650 -0.0916 -0.1628 0.2319  222 ARG A NE    
1647 C  CZ    . ARG A 229 ? 1.3745 0.8179 1.0690 -0.0982 -0.1618 0.2222  222 ARG A CZ    
1648 N  NH1   . ARG A 229 ? 1.3695 0.8245 1.0650 -0.1250 -0.1531 0.2285  222 ARG A NH1   
1649 N  NH2   . ARG A 229 ? 1.3776 0.7953 1.0800 -0.0774 -0.1696 0.2057  222 ARG A NH2   
1650 N  N     . PHE A 230 ? 1.0805 0.7419 0.8322 -0.1305 -0.0855 0.1933  223 PHE A N     
1651 C  CA    . PHE A 230 ? 1.0374 0.7282 0.8051 -0.1428 -0.0723 0.1859  223 PHE A CA    
1652 C  C     . PHE A 230 ? 1.0067 0.7456 0.7751 -0.1495 -0.0569 0.1881  223 PHE A C     
1653 O  O     . PHE A 230 ? 1.0182 0.7774 0.7870 -0.1689 -0.0482 0.1968  223 PHE A O     
1654 C  CB    . PHE A 230 ? 0.9792 0.6738 0.7670 -0.1266 -0.0702 0.1635  223 PHE A CB    
1655 C  CG    . PHE A 230 ? 0.9403 0.6611 0.7444 -0.1380 -0.0593 0.1560  223 PHE A CG    
1656 C  CD1   . PHE A 230 ? 0.8877 0.6546 0.7025 -0.1384 -0.0444 0.1500  223 PHE A CD1   
1657 C  CD2   . PHE A 230 ? 0.9638 0.6620 0.7715 -0.1485 -0.0652 0.1553  223 PHE A CD2   
1658 C  CE1   . PHE A 230 ? 0.8576 0.6496 0.6879 -0.1478 -0.0353 0.1441  223 PHE A CE1   
1659 C  CE2   . PHE A 230 ? 0.9324 0.6569 0.7556 -0.1594 -0.0566 0.1494  223 PHE A CE2   
1660 C  CZ    . PHE A 230 ? 0.8788 0.6509 0.7140 -0.1584 -0.0416 0.1442  223 PHE A CZ    
1661 N  N     . CYS A 231 ? 0.9672 0.7273 0.7374 -0.1327 -0.0529 0.1784  224 CYS A N     
1662 C  CA    . CYS A 231 ? 0.9404 0.7433 0.7100 -0.1361 -0.0389 0.1770  224 CYS A CA    
1663 C  C     . CYS A 231 ? 1.0006 0.8081 0.7480 -0.1534 -0.0371 0.1979  224 CYS A C     
1664 O  O     . CYS A 231 ? 0.9944 0.8371 0.7422 -0.1642 -0.0234 0.2000  224 CYS A O     
1665 C  CB    . CYS A 231 ? 0.8999 0.7170 0.6726 -0.1160 -0.0386 0.1636  224 CYS A CB    
1666 S  SG    . CYS A 231 ? 0.8297 0.6498 0.6293 -0.0993 -0.0369 0.1403  224 CYS A SG    
1667 N  N     . GLU A 232 ? 1.0618 0.8348 0.7895 -0.1548 -0.0508 0.2133  225 GLU A N     
1668 C  CA    . GLU A 232 ? 1.1316 0.9015 0.8347 -0.1724 -0.0515 0.2364  225 GLU A CA    
1669 C  C     . GLU A 232 ? 1.1627 0.9361 0.8686 -0.1981 -0.0455 0.2489  225 GLU A C     
1670 O  O     . GLU A 232 ? 1.1874 0.9896 0.8840 -0.2139 -0.0343 0.2606  225 GLU A O     
1671 C  CB    . GLU A 232 ? 1.1949 0.9193 0.8781 -0.1673 -0.0705 0.2502  225 GLU A CB    
1672 C  CG    . GLU A 232 ? 1.1784 0.9060 0.8563 -0.1450 -0.0768 0.2423  225 GLU A CG    
1673 C  CD    . GLU A 232 ? 1.2336 0.9167 0.8981 -0.1339 -0.0972 0.2519  225 GLU A CD    
1674 O  OE1   . GLU A 232 ? 1.2176 0.9048 0.8830 -0.1143 -0.1037 0.2439  225 GLU A OE1   
1675 O  OE2   . GLU A 232 ? 1.2972 0.9413 0.9506 -0.1450 -0.1074 0.2676  225 GLU A OE2   
1676 N  N     . ARG A 233 ? 1.1652 0.9107 0.8838 -0.2022 -0.0530 0.2460  226 ARG A N     
1677 C  CA    . ARG A 233 ? 1.1951 0.9415 0.9199 -0.2272 -0.0500 0.2563  226 ARG A CA    
1678 C  C     . ARG A 233 ? 1.1491 0.9526 0.8913 -0.2346 -0.0302 0.2492  226 ARG A C     
1679 O  O     . ARG A 233 ? 1.1837 1.0056 0.9272 -0.2579 -0.0233 0.2628  226 ARG A O     
1680 C  CB    . ARG A 233 ? 1.1947 0.9014 0.9310 -0.2239 -0.0627 0.2475  226 ARG A CB    
1681 C  CG    . ARG A 233 ? 1.2405 0.9346 0.9810 -0.2506 -0.0658 0.2588  226 ARG A CG    
1682 C  CD    . ARG A 233 ? 1.2524 0.8996 0.9983 -0.2456 -0.0811 0.2492  226 ARG A CD    
1683 N  NE    . ARG A 233 ? 1.2798 0.8793 1.0108 -0.2258 -0.0968 0.2473  226 ARG A NE    
1684 C  CZ    . ARG A 233 ? 1.2349 0.8247 0.9745 -0.1990 -0.1004 0.2267  226 ARG A CZ    
1685 N  NH1   . ARG A 233 ? 1.1610 0.7812 0.9220 -0.1897 -0.0903 0.2067  226 ARG A NH1   
1686 N  NH2   . ARG A 233 ? 1.2678 0.8186 0.9946 -0.1810 -0.1142 0.2268  226 ARG A NH2   
1687 N  N     . HIS A 234 ? 1.0758 0.9079 0.8317 -0.2146 -0.0214 0.2282  227 HIS A N     
1688 C  CA    . HIS A 234 ? 1.0297 0.9122 0.8037 -0.2162 -0.0042 0.2179  227 HIS A CA    
1689 C  C     . HIS A 234 ? 1.0179 0.9352 0.7808 -0.2075 0.0074  0.2150  227 HIS A C     
1690 O  O     . HIS A 234 ? 0.9694 0.9228 0.7462 -0.1986 0.0197  0.2000  227 HIS A O     
1691 C  CB    . HIS A 234 ? 0.9622 0.8459 0.7606 -0.2017 -0.0045 0.1958  227 HIS A CB    
1692 C  CG    . HIS A 234 ? 0.9806 0.8299 0.7864 -0.2100 -0.0163 0.1974  227 HIS A CG    
1693 N  ND1   . HIS A 234 ? 0.9953 0.7978 0.7928 -0.1995 -0.0316 0.1952  227 HIS A ND1   
1694 C  CD2   . HIS A 234 ? 0.9972 0.8490 0.8152 -0.2280 -0.0167 0.2016  227 HIS A CD2   
1695 C  CE1   . HIS A 234 ? 1.0215 0.7963 0.8237 -0.2099 -0.0408 0.1971  227 HIS A CE1   
1696 N  NE2   . HIS A 234 ? 1.0218 0.8255 0.8367 -0.2280 -0.0325 0.2009  227 HIS A NE2   
1697 N  N     . SER A 235 ? 1.0696 0.9760 0.8059 -0.2107 0.0034  0.2299  228 SER A N     
1698 C  CA    . SER A 235 ? 1.0648 0.9976 0.7861 -0.2005 0.0115  0.2259  228 SER A CA    
1699 C  C     . SER A 235 ? 1.0686 1.0524 0.7922 -0.2098 0.0311  0.2263  228 SER A C     
1700 O  O     . SER A 235 ? 1.0486 1.0600 0.7667 -0.1975 0.0402  0.2147  228 SER A O     
1701 C  CB    . SER A 235 ? 1.1247 1.0323 0.8156 -0.2018 0.0008  0.2423  228 SER A CB    
1702 O  OG    . SER A 235 ? 1.1954 1.0819 0.8738 -0.2241 -0.0044 0.2665  228 SER A OG    
1703 N  N     . SER A 236 ? 1.0946 1.0929 0.8283 -0.2305 0.0375  0.2379  229 SER A N     
1704 C  CA    . SER A 236 ? 1.1002 1.1519 0.8402 -0.2382 0.0569  0.2380  229 SER A CA    
1705 C  C     . SER A 236 ? 1.0319 1.1125 0.8019 -0.2252 0.0658  0.2154  229 SER A C     
1706 O  O     . SER A 236 ? 1.0344 1.1611 0.8137 -0.2286 0.0818  0.2130  229 SER A O     
1707 C  CB    . SER A 236 ? 1.1605 1.2216 0.9016 -0.2669 0.0605  0.2608  229 SER A CB    
1708 O  OG    . SER A 236 ? 1.1372 1.1908 0.9060 -0.2747 0.0557  0.2573  229 SER A OG    
1709 N  N     . GLN A 237 ? 0.9770 1.0314 0.7623 -0.2110 0.0557  0.1999  230 GLN A N     
1710 C  CA    . GLN A 237 ? 0.9152 0.9925 0.7259 -0.1975 0.0624  0.1791  230 GLN A CA    
1711 C  C     . GLN A 237 ? 0.8836 0.9712 0.6859 -0.1756 0.0669  0.1622  230 GLN A C     
1712 O  O     . GLN A 237 ? 0.8639 0.9221 0.6584 -0.1630 0.0562  0.1555  230 GLN A O     
1713 C  CB    . GLN A 237 ? 0.8777 0.9231 0.7062 -0.1936 0.0500  0.1712  230 GLN A CB    
1714 C  CG    . GLN A 237 ? 0.9147 0.9426 0.7492 -0.2153 0.0425  0.1864  230 GLN A CG    
1715 C  CD    . GLN A 237 ? 0.9316 1.0014 0.7831 -0.2321 0.0541  0.1927  230 GLN A CD    
1716 O  OE1   . GLN A 237 ? 0.9095 1.0227 0.7718 -0.2246 0.0681  0.1834  230 GLN A OE1   
1717 N  NE2   . GLN A 237 ? 0.9766 1.0340 0.8309 -0.2552 0.0478  0.2088  230 GLN A NE2   
1718 N  N     . THR A 238 ? 0.8845 1.0143 0.6886 -0.1713 0.0822  0.1551  231 THR A N     
1719 C  CA    . THR A 238 ? 0.8634 1.0022 0.6582 -0.1515 0.0862  0.1382  231 THR A CA    
1720 C  C     . THR A 238 ? 0.7992 0.9309 0.6160 -0.1350 0.0828  0.1178  231 THR A C     
1721 O  O     . THR A 238 ? 0.7779 0.9081 0.5891 -0.1188 0.0826  0.1029  231 THR A O     
1722 C  CB    . THR A 238 ? 0.8948 1.0789 0.6815 -0.1506 0.1036  0.1361  231 THR A CB    
1723 O  OG1   . THR A 238 ? 0.8716 1.0862 0.6860 -0.1489 0.1131  0.1280  231 THR A OG1   
1724 C  CG2   . THR A 238 ? 0.9634 1.1603 0.7294 -0.1694 0.1092  0.1582  231 THR A CG2   
1725 N  N     . CYS A 239 ? 0.7736 0.9008 0.6140 -0.1400 0.0798  0.1177  232 CYS A N     
1726 C  CA    . CYS A 239 ? 0.7178 0.8366 0.5769 -0.1256 0.0760  0.1005  232 CYS A CA    
1727 C  C     . CYS A 239 ? 0.6940 0.7708 0.5507 -0.1203 0.0612  0.0985  232 CYS A C     
1728 O  O     . CYS A 239 ? 0.6508 0.7191 0.5194 -0.1079 0.0579  0.0846  232 CYS A O     
1729 C  CB    . CYS A 239 ? 0.7029 0.8389 0.5878 -0.1316 0.0792  0.0997  232 CYS A CB    
1730 S  SG    . CYS A 239 ? 0.7275 0.8420 0.6182 -0.1539 0.0695  0.1175  232 CYS A SG    
1731 N  N     . LEU A 240 ? 0.7260 0.7778 0.5678 -0.1294 0.0525  0.1125  233 LEU A N     
1732 C  CA    . LEU A 240 ? 0.7130 0.7267 0.5530 -0.1237 0.0386  0.1116  233 LEU A CA    
1733 C  C     . LEU A 240 ? 0.6861 0.6938 0.5210 -0.1065 0.0353  0.0988  233 LEU A C     
1734 O  O     . LEU A 240 ? 0.7055 0.7214 0.5235 -0.1032 0.0372  0.0990  233 LEU A O     
1735 C  CB    . LEU A 240 ? 0.7650 0.7546 0.5875 -0.1359 0.0301  0.1302  233 LEU A CB    
1736 C  CG    . LEU A 240 ? 0.7640 0.7154 0.5812 -0.1273 0.0154  0.1302  233 LEU A CG    
1737 C  CD1   . LEU A 240 ? 0.7371 0.6689 0.5718 -0.1247 0.0093  0.1233  233 LEU A CD1   
1738 C  CD2   . LEU A 240 ? 0.8253 0.7538 0.6213 -0.1376 0.0069  0.1494  233 LEU A CD2   
1739 N  N     . VAL A 241 ? 0.6457 0.6385 0.4946 -0.0966 0.0296  0.0879  234 VAL A N     
1740 C  CA    . VAL A 241 ? 0.6214 0.6068 0.4695 -0.0824 0.0248  0.0769  234 VAL A CA    
1741 C  C     . VAL A 241 ? 0.6172 0.5733 0.4687 -0.0783 0.0130  0.0788  234 VAL A C     
1742 O  O     . VAL A 241 ? 0.5888 0.5368 0.4550 -0.0741 0.0114  0.0719  234 VAL A O     
1743 C  CB    . VAL A 241 ? 0.5790 0.5785 0.4417 -0.0728 0.0307  0.0608  234 VAL A CB    
1744 C  CG1   . VAL A 241 ? 0.5589 0.5489 0.4218 -0.0612 0.0245  0.0512  234 VAL A CG1   
1745 C  CG2   . VAL A 241 ? 0.5864 0.6143 0.4466 -0.0731 0.0421  0.0564  234 VAL A CG2   
1746 N  N     . PRO A 242 ? 0.6496 0.5892 0.4867 -0.0778 0.0041  0.0878  235 PRO A N     
1747 C  CA    . PRO A 242 ? 0.6536 0.5661 0.4941 -0.0717 -0.0071 0.0894  235 PRO A CA    
1748 C  C     . PRO A 242 ? 0.6213 0.5348 0.4720 -0.0571 -0.0107 0.0770  235 PRO A C     
1749 O  O     . PRO A 242 ? 0.6148 0.5425 0.4617 -0.0527 -0.0098 0.0720  235 PRO A O     
1750 C  CB    . PRO A 242 ? 0.7068 0.6039 0.5274 -0.0756 -0.0157 0.1044  235 PRO A CB    
1751 C  CG    . PRO A 242 ? 0.7185 0.6389 0.5250 -0.0785 -0.0094 0.1056  235 PRO A CG    
1752 C  CD    . PRO A 242 ? 0.6901 0.6366 0.5059 -0.0825 0.0043  0.0972  235 PRO A CD    
1753 N  N     . GLU A 243 ? 0.6081 0.5060 0.4707 -0.0505 -0.0154 0.0728  236 GLU A N     
1754 C  CA    . GLU A 243 ? 0.5821 0.4827 0.4566 -0.0377 -0.0183 0.0626  236 GLU A CA    
1755 C  C     . GLU A 243 ? 0.6033 0.4818 0.4797 -0.0290 -0.0283 0.0652  236 GLU A C     
1756 O  O     . GLU A 243 ? 0.5940 0.4622 0.4794 -0.0247 -0.0284 0.0600  236 GLU A O     
1757 C  CB    . GLU A 243 ? 0.5380 0.4502 0.4281 -0.0355 -0.0104 0.0505  236 GLU A CB    
1758 C  CG    . GLU A 243 ? 0.5213 0.4540 0.4102 -0.0405 -0.0016 0.0464  236 GLU A CG    
1759 C  CD    . GLU A 243 ? 0.4829 0.4260 0.3857 -0.0369 0.0044  0.0350  236 GLU A CD    
1760 O  OE1   . GLU A 243 ? 0.4667 0.4051 0.3796 -0.0302 0.0021  0.0298  236 GLU A OE1   
1761 O  OE2   . GLU A 243 ? 0.4742 0.4308 0.3766 -0.0401 0.0113  0.0316  236 GLU A OE2   
1762 N  N     . PRO A 244 ? 0.6355 0.5073 0.5032 -0.0241 -0.0377 0.0721  237 PRO A N     
1763 C  CA    . PRO A 244 ? 0.6584 0.5122 0.5299 -0.0119 -0.0478 0.0730  237 PRO A CA    
1764 C  C     . PRO A 244 ? 0.6231 0.4928 0.5142 -0.0001 -0.0454 0.0602  237 PRO A C     
1765 O  O     . PRO A 244 ? 0.5882 0.4803 0.4865 -0.0029 -0.0385 0.0532  237 PRO A O     
1766 C  CB    . PRO A 244 ? 0.7014 0.5496 0.5586 -0.0101 -0.0582 0.0841  237 PRO A CB    
1767 C  CG    . PRO A 244 ? 0.6907 0.5612 0.5389 -0.0194 -0.0523 0.0849  237 PRO A CG    
1768 C  CD    . PRO A 244 ? 0.6563 0.5381 0.5088 -0.0292 -0.0391 0.0791  237 PRO A CD    
1769 N  N     . ASN A 245 ? 0.6377 0.4959 0.5368 0.0127  -0.0513 0.0575  238 ASN A N     
1770 C  CA    . ASN A 245 ? 0.6095 0.4853 0.5279 0.0234  -0.0477 0.0462  238 ASN A CA    
1771 C  C     . ASN A 245 ? 0.5913 0.4947 0.5177 0.0235  -0.0477 0.0439  238 ASN A C     
1772 O  O     . ASN A 245 ? 0.5569 0.4799 0.4968 0.0230  -0.0407 0.0355  238 ASN A O     
1773 C  CB    . ASN A 245 ? 0.6387 0.5021 0.5637 0.0400  -0.0546 0.0441  238 ASN A CB    
1774 C  CG    . ASN A 245 ? 0.6547 0.4917 0.5746 0.0423  -0.0539 0.0411  238 ASN A CG    
1775 O  OD1   . ASN A 245 ? 0.6398 0.4696 0.5537 0.0306  -0.0479 0.0404  238 ASN A OD1   
1776 N  ND2   . ASN A 245 ? 0.6885 0.5120 0.6114 0.0585  -0.0604 0.0383  238 ASN A ND2   
1777 N  N     . ARG A 246 ? 0.6196 0.5235 0.5367 0.0235  -0.0567 0.0517  239 ARG A N     
1778 C  CA    . ARG A 246 ? 0.6116 0.5396 0.5350 0.0236  -0.0596 0.0493  239 ARG A CA    
1779 C  C     . ARG A 246 ? 0.5761 0.5192 0.4991 0.0122  -0.0502 0.0429  239 ARG A C     
1780 O  O     . ARG A 246 ? 0.5584 0.5211 0.4937 0.0123  -0.0496 0.0361  239 ARG A O     
1781 C  CB    . ARG A 246 ? 0.6553 0.5769 0.5629 0.0243  -0.0717 0.0599  239 ARG A CB    
1782 C  CG    . ARG A 246 ? 0.6554 0.5990 0.5627 0.0212  -0.0762 0.0581  239 ARG A CG    
1783 C  CD    . ARG A 246 ? 0.7050 0.6408 0.5943 0.0229  -0.0893 0.0694  239 ARG A CD    
1784 N  NE    . ARG A 246 ? 0.7094 0.6618 0.5893 0.0159  -0.0924 0.0676  239 ARG A NE    
1785 C  CZ    . ARG A 246 ? 0.7096 0.6615 0.5694 0.0044  -0.0863 0.0679  239 ARG A CZ    
1786 N  NH1   . ARG A 246 ? 0.7031 0.6420 0.5523 -0.0026 -0.0763 0.0712  239 ARG A NH1   
1787 N  NH2   . ARG A 246 ? 0.7221 0.6876 0.5720 0.0004  -0.0909 0.0647  239 ARG A NH2   
1788 N  N     . LEU A 247 ? 0.5712 0.5052 0.4803 0.0023  -0.0435 0.0451  240 LEU A N     
1789 C  CA    . LEU A 247 ? 0.5456 0.4919 0.4526 -0.0062 -0.0351 0.0390  240 LEU A CA    
1790 C  C     . LEU A 247 ? 0.5089 0.4574 0.4288 -0.0070 -0.0254 0.0311  240 LEU A C     
1791 O  O     . LEU A 247 ? 0.4873 0.4463 0.4100 -0.0112 -0.0196 0.0243  240 LEU A O     
1792 C  CB    . LEU A 247 ? 0.5654 0.5059 0.4516 -0.0151 -0.0328 0.0459  240 LEU A CB    
1793 C  CG    . LEU A 247 ? 0.6027 0.5451 0.4717 -0.0162 -0.0411 0.0526  240 LEU A CG    
1794 C  CD1   . LEU A 247 ? 0.6238 0.5645 0.4716 -0.0259 -0.0358 0.0593  240 LEU A CD1   
1795 C  CD2   . LEU A 247 ? 0.5960 0.5554 0.4690 -0.0145 -0.0445 0.0441  240 LEU A CD2   
1796 N  N     . MET A 248 ? 0.5068 0.4434 0.4322 -0.0031 -0.0240 0.0317  241 MET A N     
1797 C  CA    . MET A 248 ? 0.4771 0.4152 0.4112 -0.0045 -0.0154 0.0250  241 MET A CA    
1798 C  C     . MET A 248 ? 0.4601 0.4100 0.4112 0.0023  -0.0140 0.0181  241 MET A C     
1799 O  O     . MET A 248 ? 0.4356 0.3914 0.3932 0.0000  -0.0070 0.0124  241 MET A O     
1800 C  CB    . MET A 248 ? 0.4874 0.4067 0.4170 -0.0051 -0.0148 0.0280  241 MET A CB    
1801 C  CG    . MET A 248 ? 0.4610 0.3817 0.3966 -0.0077 -0.0069 0.0217  241 MET A CG    
1802 S  SD    . MET A 248 ? 0.4797 0.3776 0.4079 -0.0114 -0.0080 0.0250  241 MET A SD    
1803 C  CE    . MET A 248 ? 0.4465 0.3546 0.3809 -0.0166 0.0007  0.0182  241 MET A CE    
1804 N  N     . ALA A 249 ? 0.4771 0.4308 0.4356 0.0112  -0.0204 0.0192  242 ALA A N     
1805 C  CA    . ALA A 249 ? 0.4688 0.4347 0.4443 0.0190  -0.0180 0.0137  242 ALA A CA    
1806 C  C     . ALA A 249 ? 0.4434 0.4282 0.4293 0.0128  -0.0126 0.0086  242 ALA A C     
1807 O  O     . ALA A 249 ? 0.4290 0.4188 0.4230 0.0137  -0.0058 0.0046  242 ALA A O     
1808 C  CB    . ALA A 249 ? 0.4949 0.4675 0.4787 0.0300  -0.0262 0.0159  242 ALA A CB    
1809 N  N     . LYS A 250 ? 0.4449 0.4387 0.4295 0.0068  -0.0166 0.0091  243 LYS A N     
1810 C  CA    . LYS A 250 ? 0.4323 0.4421 0.4280 0.0012  -0.0145 0.0047  243 LYS A CA    
1811 C  C     . LYS A 250 ? 0.4264 0.4311 0.4103 -0.0082 -0.0138 0.0023  243 LYS A C     
1812 O  O     . LYS A 250 ? 0.4260 0.4393 0.4154 -0.0139 -0.0152 -0.0010 243 LYS A O     
1813 C  CB    . LYS A 250 ? 0.4490 0.4782 0.4585 0.0037  -0.0223 0.0055  243 LYS A CB    
1814 C  CG    . LYS A 250 ? 0.4636 0.5013 0.4858 0.0162  -0.0245 0.0075  243 LYS A CG    
1815 C  CD    . LYS A 250 ? 0.4574 0.5147 0.4994 0.0191  -0.0182 0.0046  243 LYS A CD    
1816 C  CE    . LYS A 250 ? 0.4366 0.4853 0.4748 0.0162  -0.0071 0.0016  243 LYS A CE    
1817 N  NZ    . LYS A 250 ? 0.4429 0.5047 0.4939 0.0257  -0.0009 -0.0003 243 LYS A NZ    
1818 N  N     . SER A 251 ? 0.4253 0.4163 0.3939 -0.0099 -0.0112 0.0037  244 SER A N     
1819 C  CA    . SER A 251 ? 0.4283 0.4165 0.3840 -0.0160 -0.0106 0.0011  244 SER A CA    
1820 C  C     . SER A 251 ? 0.4092 0.3928 0.3645 -0.0191 -0.0025 -0.0034 244 SER A C     
1821 O  O     . SER A 251 ? 0.4140 0.3951 0.3588 -0.0219 -0.0008 -0.0064 244 SER A O     
1822 C  CB    . SER A 251 ? 0.4465 0.4276 0.3861 -0.0160 -0.0127 0.0065  244 SER A CB    
1823 O  OG    . SER A 251 ? 0.4395 0.4110 0.3761 -0.0157 -0.0074 0.0100  244 SER A OG    
1824 N  N     . TYR A 252 ? 0.3923 0.3758 0.3582 -0.0176 0.0021  -0.0040 245 TYR A N     
1825 C  CA    . TYR A 252 ? 0.3777 0.3564 0.3432 -0.0197 0.0085  -0.0073 245 TYR A CA    
1826 C  C     . TYR A 252 ? 0.3728 0.3555 0.3484 -0.0223 0.0094  -0.0100 245 TYR A C     
1827 O  O     . TYR A 252 ? 0.3761 0.3681 0.3623 -0.0220 0.0074  -0.0086 245 TYR A O     
1828 C  CB    . TYR A 252 ? 0.3682 0.3409 0.3337 -0.0170 0.0127  -0.0047 245 TYR A CB    
1829 C  CG    . TYR A 252 ? 0.3756 0.3423 0.3309 -0.0178 0.0128  -0.0011 245 TYR A CG    
1830 C  CD1   . TYR A 252 ? 0.3925 0.3562 0.3431 -0.0163 0.0079  0.0038  245 TYR A CD1   
1831 C  CD2   . TYR A 252 ? 0.3707 0.3360 0.3215 -0.0205 0.0171  -0.0019 245 TYR A CD2   
1832 C  CE1   . TYR A 252 ? 0.4054 0.3627 0.3459 -0.0193 0.0078  0.0090  245 TYR A CE1   
1833 C  CE2   . TYR A 252 ? 0.3813 0.3445 0.3247 -0.0233 0.0177  0.0026  245 TYR A CE2   
1834 C  CZ    . TYR A 252 ? 0.3996 0.3580 0.3371 -0.0237 0.0131  0.0086  245 TYR A CZ    
1835 O  OH    . TYR A 252 ? 0.4163 0.3717 0.3454 -0.0286 0.0133  0.0150  245 TYR A OH    
1836 N  N     . LEU A 253 ? 0.3699 0.3462 0.3421 -0.0248 0.0120  -0.0134 246 LEU A N     
1837 C  CA    . LEU A 253 ? 0.3689 0.3441 0.3480 -0.0283 0.0135  -0.0142 246 LEU A CA    
1838 C  C     . LEU A 253 ? 0.3559 0.3272 0.3353 -0.0257 0.0193  -0.0124 246 LEU A C     
1839 O  O     . LEU A 253 ? 0.3516 0.3165 0.3243 -0.0237 0.0213  -0.0138 246 LEU A O     
1840 C  CB    . LEU A 253 ? 0.3831 0.3492 0.3555 -0.0315 0.0107  -0.0193 246 LEU A CB    
1841 C  CG    . LEU A 253 ? 0.4025 0.3713 0.3736 -0.0355 0.0034  -0.0221 246 LEU A CG    
1842 C  CD1   . LEU A 253 ? 0.4234 0.3790 0.3834 -0.0367 0.0002  -0.0294 246 LEU A CD1   
1843 C  CD2   . LEU A 253 ? 0.4084 0.3868 0.3933 -0.0416 0.0003  -0.0190 246 LEU A CD2   
1844 N  N     . ILE A 254 ? 0.3533 0.3309 0.3403 -0.0255 0.0220  -0.0096 247 ILE A N     
1845 C  CA    . ILE A 254 ? 0.3456 0.3205 0.3307 -0.0221 0.0267  -0.0083 247 ILE A CA    
1846 C  C     . ILE A 254 ? 0.3510 0.3275 0.3394 -0.0257 0.0298  -0.0062 247 ILE A C     
1847 O  O     . ILE A 254 ? 0.3584 0.3467 0.3554 -0.0278 0.0311  -0.0041 247 ILE A O     
1848 C  CB    . ILE A 254 ? 0.3456 0.3250 0.3325 -0.0164 0.0273  -0.0074 247 ILE A CB    
1849 C  CG1   . ILE A 254 ? 0.3464 0.3211 0.3278 -0.0146 0.0234  -0.0073 247 ILE A CG1   
1850 C  CG2   . ILE A 254 ? 0.3442 0.3189 0.3267 -0.0131 0.0312  -0.0075 247 ILE A CG2   
1851 C  CD1   . ILE A 254 ? 0.3547 0.3292 0.3367 -0.0089 0.0215  -0.0059 247 ILE A CD1   
1852 N  N     . LEU A 255 ? 0.3506 0.3170 0.3324 -0.0262 0.0310  -0.0060 248 LEU A N     
1853 C  CA    . LEU A 255 ? 0.3600 0.3254 0.3410 -0.0292 0.0340  -0.0024 248 LEU A CA    
1854 C  C     . LEU A 255 ? 0.3573 0.3239 0.3332 -0.0244 0.0379  -0.0018 248 LEU A C     
1855 O  O     . LEU A 255 ? 0.3498 0.3100 0.3200 -0.0206 0.0366  -0.0041 248 LEU A O     
1856 C  CB    . LEU A 255 ? 0.3684 0.3196 0.3437 -0.0314 0.0311  -0.0023 248 LEU A CB    
1857 C  CG    . LEU A 255 ? 0.3830 0.3280 0.3604 -0.0371 0.0265  -0.0033 248 LEU A CG    
1858 C  CD1   . LEU A 255 ? 0.3964 0.3240 0.3665 -0.0357 0.0233  -0.0045 248 LEU A CD1   
1859 C  CD2   . LEU A 255 ? 0.3982 0.3507 0.3829 -0.0458 0.0275  0.0018  248 LEU A CD2   
1860 N  N     . ASP A 256 ? 0.3685 0.3436 0.3455 -0.0256 0.0426  0.0011  249 ASP A N     
1861 C  CA    . ASP A 256 ? 0.3738 0.3486 0.3424 -0.0210 0.0462  0.0007  249 ASP A CA    
1862 C  C     . ASP A 256 ? 0.3836 0.3484 0.3422 -0.0236 0.0457  0.0042  249 ASP A C     
1863 O  O     . ASP A 256 ? 0.3858 0.3412 0.3441 -0.0275 0.0420  0.0065  249 ASP A O     
1864 C  CB    . ASP A 256 ? 0.3860 0.3769 0.3589 -0.0183 0.0523  0.0010  249 ASP A CB    
1865 C  CG    . ASP A 256 ? 0.4041 0.4059 0.3799 -0.0256 0.0573  0.0075  249 ASP A CG    
1866 O  OD1   . ASP A 256 ? 0.4088 0.4007 0.3820 -0.0332 0.0546  0.0120  249 ASP A OD1   
1867 O  OD2   . ASP A 256 ? 0.4173 0.4375 0.3986 -0.0236 0.0636  0.0081  249 ASP A OD2   
1868 N  N     . GLU A 257 ? 0.3952 0.3608 0.3439 -0.0205 0.0488  0.0043  250 GLU A N     
1869 C  CA    . GLU A 257 ? 0.4078 0.3641 0.3446 -0.0214 0.0471  0.0075  250 GLU A CA    
1870 C  C     . GLU A 257 ? 0.4282 0.3845 0.3634 -0.0288 0.0493  0.0158  250 GLU A C     
1871 O  O     . GLU A 257 ? 0.4432 0.3891 0.3684 -0.0301 0.0464  0.0202  250 GLU A O     
1872 C  CB    . GLU A 257 ? 0.4190 0.3756 0.3436 -0.0160 0.0487  0.0041  250 GLU A CB    
1873 C  CG    . GLU A 257 ? 0.4392 0.4087 0.3596 -0.0143 0.0570  0.0044  250 GLU A CG    
1874 C  CD    . GLU A 257 ? 0.4358 0.4153 0.3636 -0.0078 0.0605  -0.0018 250 GLU A CD    
1875 O  OE1   . GLU A 257 ? 0.4162 0.3949 0.3557 -0.0070 0.0571  -0.0042 250 GLU A OE1   
1876 O  OE2   . GLU A 257 ? 0.4575 0.4460 0.3785 -0.0026 0.0667  -0.0044 250 GLU A OE2   
1877 N  N     . TYR A 258 ? 0.4335 0.4020 0.3783 -0.0340 0.0537  0.0186  251 TYR A N     
1878 C  CA    . TYR A 258 ? 0.4573 0.4249 0.4023 -0.0442 0.0548  0.0277  251 TYR A CA    
1879 C  C     . TYR A 258 ? 0.4534 0.4123 0.4085 -0.0502 0.0487  0.0280  251 TYR A C     
1880 O  O     . TYR A 258 ? 0.4766 0.4338 0.4344 -0.0608 0.0483  0.0352  251 TYR A O     
1881 C  CB    . TYR A 258 ? 0.4737 0.4644 0.4242 -0.0481 0.0639  0.0315  251 TYR A CB    
1882 C  CG    . TYR A 258 ? 0.4890 0.4883 0.4263 -0.0422 0.0710  0.0311  251 TYR A CG    
1883 C  CD1   . TYR A 258 ? 0.5180 0.5115 0.4395 -0.0468 0.0727  0.0392  251 TYR A CD1   
1884 C  CD2   . TYR A 258 ? 0.4803 0.4908 0.4185 -0.0315 0.0749  0.0223  251 TYR A CD2   
1885 C  CE1   . TYR A 258 ? 0.5381 0.5398 0.4444 -0.0415 0.0791  0.0383  251 TYR A CE1   
1886 C  CE2   . TYR A 258 ? 0.5010 0.5166 0.4243 -0.0253 0.0806  0.0202  251 TYR A CE2   
1887 C  CZ    . TYR A 258 ? 0.5297 0.5425 0.4369 -0.0305 0.0832  0.0279  251 TYR A CZ    
1888 O  OH    . TYR A 258 ? 0.5554 0.5731 0.4447 -0.0244 0.0886  0.0254  251 TYR A OH    
1889 N  N     . MET A 259 ? 0.4294 0.3828 0.3888 -0.0444 0.0439  0.0203  252 MET A N     
1890 C  CA    . MET A 259 ? 0.4261 0.3723 0.3928 -0.0475 0.0381  0.0175  252 MET A CA    
1891 C  C     . MET A 259 ? 0.4331 0.3939 0.4122 -0.0555 0.0396  0.0194  252 MET A C     
1892 O  O     . MET A 259 ? 0.4494 0.4023 0.4320 -0.0638 0.0346  0.0210  252 MET A O     
1893 C  CB    . MET A 259 ? 0.4463 0.3699 0.4061 -0.0503 0.0317  0.0198  252 MET A CB    
1894 C  CG    . MET A 259 ? 0.4464 0.3590 0.3960 -0.0427 0.0297  0.0195  252 MET A CG    
1895 S  SD    . MET A 259 ? 0.4711 0.3571 0.4138 -0.0400 0.0208  0.0196  252 MET A SD    
1896 C  CE    . MET A 259 ? 0.4477 0.3362 0.3965 -0.0312 0.0184  0.0080  252 MET A CE    
1897 N  N     . ARG A 260 ? 0.4237 0.4054 0.4099 -0.0521 0.0453  0.0182  253 ARG A N     
1898 C  CA    . ARG A 260 ? 0.4243 0.4249 0.4255 -0.0554 0.0456  0.0178  253 ARG A CA    
1899 C  C     . ARG A 260 ? 0.4023 0.4040 0.4069 -0.0473 0.0418  0.0104  253 ARG A C     
1900 O  O     . ARG A 260 ? 0.3874 0.3855 0.3857 -0.0378 0.0431  0.0065  253 ARG A O     
1901 C  CB    . ARG A 260 ? 0.4330 0.4583 0.4404 -0.0535 0.0545  0.0206  253 ARG A CB    
1902 C  CG    . ARG A 260 ? 0.4585 0.4854 0.4592 -0.0610 0.0603  0.0291  253 ARG A CG    
1903 C  CD    . ARG A 260 ? 0.4719 0.5247 0.4755 -0.0572 0.0709  0.0309  253 ARG A CD    
1904 N  NE    . ARG A 260 ? 0.4598 0.5123 0.4548 -0.0424 0.0740  0.0232  253 ARG A NE    
1905 C  CZ    . ARG A 260 ? 0.4744 0.5469 0.4693 -0.0351 0.0829  0.0216  253 ARG A CZ    
1906 N  NH1   . ARG A 260 ? 0.4992 0.5984 0.5039 -0.0413 0.0910  0.0279  253 ARG A NH1   
1907 N  NH2   . ARG A 260 ? 0.4689 0.5354 0.4540 -0.0218 0.0837  0.0134  253 ARG A NH2   
1908 N  N     . PHE A 261 ? 0.4056 0.4139 0.4203 -0.0519 0.0369  0.0093  254 PHE A N     
1909 C  CA    . PHE A 261 ? 0.3920 0.4043 0.4098 -0.0452 0.0329  0.0041  254 PHE A CA    
1910 C  C     . PHE A 261 ? 0.3899 0.4225 0.4166 -0.0374 0.0373  0.0040  254 PHE A C     
1911 O  O     . PHE A 261 ? 0.4035 0.4566 0.4420 -0.0403 0.0414  0.0075  254 PHE A O     
1912 C  CB    . PHE A 261 ? 0.4025 0.4155 0.4263 -0.0525 0.0251  0.0028  254 PHE A CB    
1913 C  CG    . PHE A 261 ? 0.4074 0.3972 0.4197 -0.0556 0.0195  -0.0005 254 PHE A CG    
1914 C  CD1   . PHE A 261 ? 0.3936 0.3713 0.3948 -0.0476 0.0186  -0.0054 254 PHE A CD1   
1915 C  CD2   . PHE A 261 ? 0.4311 0.4102 0.4428 -0.0662 0.0158  0.0013  254 PHE A CD2   
1916 C  CE1   . PHE A 261 ? 0.4025 0.3622 0.3938 -0.0482 0.0144  -0.0097 254 PHE A CE1   
1917 C  CE2   . PHE A 261 ? 0.4418 0.3974 0.4417 -0.0662 0.0104  -0.0032 254 PHE A CE2   
1918 C  CZ    . PHE A 261 ? 0.4271 0.3745 0.4172 -0.0562 0.0102  -0.0094 254 PHE A CZ    
1919 N  N     . LEU A 262 ? 0.3774 0.4040 0.3984 -0.0273 0.0362  0.0001  255 LEU A N     
1920 C  CA    . LEU A 262 ? 0.3808 0.4194 0.4070 -0.0170 0.0386  -0.0013 255 LEU A CA    
1921 C  C     . LEU A 262 ? 0.3831 0.4282 0.4167 -0.0137 0.0316  -0.0023 255 LEU A C     
1922 O  O     . LEU A 262 ? 0.3766 0.4090 0.4030 -0.0151 0.0257  -0.0034 255 LEU A O     
1923 C  CB    . LEU A 262 ? 0.3743 0.3968 0.3869 -0.0089 0.0401  -0.0044 255 LEU A CB    
1924 C  CG    . LEU A 262 ? 0.3758 0.3915 0.3786 -0.0099 0.0457  -0.0041 255 LEU A CG    
1925 C  CD1   . LEU A 262 ? 0.3752 0.3766 0.3662 -0.0020 0.0453  -0.0080 255 LEU A CD1   
1926 C  CD2   . LEU A 262 ? 0.3923 0.4267 0.4013 -0.0105 0.0532  -0.0016 255 LEU A CD2   
1927 N  N     . ASP A 263 ? 0.3961 0.4622 0.4433 -0.0076 0.0327  -0.0019 256 ASP A N     
1928 C  CA    . ASP A 263 ? 0.4037 0.4787 0.4595 -0.0036 0.0250  -0.0019 256 ASP A CA    
1929 C  C     . ASP A 263 ? 0.4063 0.4674 0.4532 0.0088  0.0219  -0.0040 256 ASP A C     
1930 O  O     . ASP A 263 ? 0.4126 0.4719 0.4596 0.0113  0.0139  -0.0030 256 ASP A O     
1931 C  CB    . ASP A 263 ? 0.4210 0.5283 0.4987 -0.0030 0.0260  0.0000  256 ASP A CB    
1932 C  CG    . ASP A 263 ? 0.4296 0.5485 0.5181 -0.0085 0.0158  0.0016  256 ASP A CG    
1933 O  OD1   . ASP A 263 ? 0.4229 0.5234 0.4994 -0.0143 0.0088  0.0008  256 ASP A OD1   
1934 O  OD2   . ASP A 263 ? 0.4463 0.5944 0.5550 -0.0064 0.0149  0.0032  256 ASP A OD2   
1935 N  N     . ARG A 264 ? 0.4067 0.4563 0.4443 0.0156  0.0273  -0.0065 257 ARG A N     
1936 C  CA    . ARG A 264 ? 0.4156 0.4463 0.4426 0.0258  0.0234  -0.0083 257 ARG A CA    
1937 C  C     . ARG A 264 ? 0.4389 0.4811 0.4767 0.0378  0.0183  -0.0083 257 ARG A C     
1938 O  O     . ARG A 264 ? 0.4492 0.4765 0.4801 0.0416  0.0102  -0.0065 257 ARG A O     
1939 C  CB    . ARG A 264 ? 0.4051 0.4147 0.4185 0.0189  0.0178  -0.0062 257 ARG A CB    
1940 C  CG    . ARG A 264 ? 0.3854 0.3865 0.3906 0.0089  0.0219  -0.0066 257 ARG A CG    
1941 C  CD    . ARG A 264 ? 0.3849 0.3765 0.3823 0.0117  0.0273  -0.0092 257 ARG A CD    
1942 N  NE    . ARG A 264 ? 0.3934 0.3655 0.3798 0.0163  0.0236  -0.0101 257 ARG A NE    
1943 C  CZ    . ARG A 264 ? 0.4015 0.3611 0.3787 0.0186  0.0255  -0.0131 257 ARG A CZ    
1944 N  NH1   . ARG A 264 ? 0.4058 0.3726 0.3830 0.0200  0.0318  -0.0160 257 ARG A NH1   
1945 N  NH2   . ARG A 264 ? 0.4101 0.3501 0.3771 0.0185  0.0207  -0.0128 257 ARG A NH2   
1946 N  N     . ASN A 265 ? 0.4514 0.5203 0.5058 0.0438  0.0229  -0.0096 258 ASN A N     
1947 C  CA    . ASN A 265 ? 0.4776 0.5611 0.5449 0.0579  0.0183  -0.0103 258 ASN A CA    
1948 C  C     . ASN A 265 ? 0.4970 0.6068 0.5782 0.0688  0.0273  -0.0142 258 ASN A C     
1949 O  O     . ASN A 265 ? 0.5211 0.6510 0.6180 0.0815  0.0246  -0.0150 258 ASN A O     
1950 C  CB    . ASN A 265 ? 0.4781 0.5813 0.5602 0.0521  0.0105  -0.0057 258 ASN A CB    
1951 C  CG    . ASN A 265 ? 0.4656 0.5924 0.5605 0.0377  0.0157  -0.0038 258 ASN A CG    
1952 O  OD1   . ASN A 265 ? 0.4593 0.5899 0.5529 0.0338  0.0258  -0.0049 258 ASN A OD1   
1953 N  ND2   . ASN A 265 ? 0.4673 0.6081 0.5728 0.0292  0.0081  -0.0005 258 ASN A ND2   
1954 N  N     . GLY A 266 ? 0.4905 0.6033 0.5666 0.0645  0.0381  -0.0162 259 GLY A N     
1955 C  CA    . GLY A 266 ? 0.5128 0.6535 0.6000 0.0739  0.0485  -0.0196 259 GLY A CA    
1956 C  C     . GLY A 266 ? 0.5079 0.6839 0.6134 0.0606  0.0554  -0.0141 259 GLY A C     
1957 O  O     . GLY A 266 ? 0.5262 0.7278 0.6393 0.0647  0.0664  -0.0154 259 GLY A O     
1958 N  N     . GLN A 267 ? 0.4889 0.6660 0.6005 0.0444  0.0488  -0.0081 260 GLN A N     
1959 C  CA    . GLN A 267 ? 0.4877 0.6899 0.6132 0.0279  0.0533  -0.0022 260 GLN A CA    
1960 C  C     . GLN A 267 ? 0.4771 0.6639 0.5860 0.0172  0.0613  -0.0005 260 GLN A C     
1961 O  O     . GLN A 267 ? 0.4619 0.6159 0.5492 0.0183  0.0598  -0.0032 260 GLN A O     
1962 C  CB    . GLN A 267 ? 0.4763 0.6762 0.6081 0.0136  0.0421  0.0021  260 GLN A CB    
1963 C  CG    . GLN A 267 ? 0.4875 0.6995 0.6329 0.0222  0.0314  0.0016  260 GLN A CG    
1964 C  CD    . GLN A 267 ? 0.5128 0.7713 0.6880 0.0253  0.0337  0.0037  260 GLN A CD    
1965 O  OE1   . GLN A 267 ? 0.5323 0.8099 0.7164 0.0420  0.0402  0.0005  260 GLN A OE1   
1966 N  NE2   . GLN A 267 ? 0.5171 0.7947 0.7080 0.0095  0.0277  0.0086  260 GLN A NE2   
1967 N  N     . GLN A 268 ? 0.4884 0.6995 0.6079 0.0053  0.0689  0.0051  261 GLN A N     
1968 C  CA    . GLN A 268 ? 0.4858 0.6838 0.5898 -0.0052 0.0758  0.0086  261 GLN A CA    
1969 C  C     . GLN A 268 ? 0.4637 0.6299 0.5554 -0.0185 0.0669  0.0109  261 GLN A C     
1970 O  O     . GLN A 268 ? 0.4570 0.6210 0.5565 -0.0249 0.0574  0.0117  261 GLN A O     
1971 C  CB    . GLN A 268 ? 0.5105 0.7422 0.6284 -0.0165 0.0856  0.0162  261 GLN A CB    
1972 C  CG    . GLN A 268 ? 0.5355 0.7899 0.6520 -0.0042 0.0995  0.0137  261 GLN A CG    
1973 C  CD    . GLN A 268 ? 0.5346 0.7632 0.6232 -0.0036 0.1052  0.0126  261 GLN A CD    
1974 O  OE1   . GLN A 268 ? 0.5425 0.7690 0.6237 -0.0184 0.1094  0.0206  261 GLN A OE1   
1975 N  NE2   . GLN A 268 ? 0.5297 0.7372 0.6020 0.0129  0.1041  0.0032  261 GLN A NE2   
1976 N  N     . PRO A 269 ? 0.4561 0.5979 0.5278 -0.0221 0.0696  0.0115  262 PRO A N     
1977 C  CA    . PRO A 269 ? 0.4411 0.5547 0.5017 -0.0331 0.0623  0.0133  262 PRO A CA    
1978 C  C     . PRO A 269 ? 0.4555 0.5782 0.5273 -0.0506 0.0599  0.0205  262 PRO A C     
1979 O  O     . PRO A 269 ? 0.4776 0.6282 0.5632 -0.0568 0.0660  0.0260  262 PRO A O     
1980 C  CB    . PRO A 269 ? 0.4394 0.5333 0.4797 -0.0320 0.0670  0.0136  262 PRO A CB    
1981 C  CG    . PRO A 269 ? 0.4492 0.5539 0.4854 -0.0180 0.0749  0.0091  262 PRO A CG    
1982 C  CD    . PRO A 269 ? 0.4652 0.6040 0.5225 -0.0135 0.0787  0.0091  262 PRO A CD    
1983 N  N     . SER A 270 ? 0.4479 0.5467 0.5128 -0.0587 0.0510  0.0202  263 SER A N     
1984 C  CA    . SER A 270 ? 0.4680 0.5635 0.5368 -0.0762 0.0473  0.0265  263 SER A CA    
1985 C  C     . SER A 270 ? 0.4846 0.5737 0.5433 -0.0829 0.0544  0.0336  263 SER A C     
1986 O  O     . SER A 270 ? 0.4776 0.5614 0.5236 -0.0738 0.0610  0.0326  263 SER A O     
1987 C  CB    . SER A 270 ? 0.4619 0.5292 0.5216 -0.0801 0.0364  0.0224  263 SER A CB    
1988 O  OG    . SER A 270 ? 0.4533 0.4915 0.4937 -0.0768 0.0365  0.0210  263 SER A OG    
1989 N  N     . LYS A 271 ? 0.5117 0.5974 0.5737 -0.1001 0.0516  0.0413  264 LYS A N     
1990 C  CA    . LYS A 271 ? 0.5314 0.6000 0.5788 -0.1075 0.0548  0.0490  264 LYS A CA    
1991 C  C     . LYS A 271 ? 0.5172 0.5472 0.5455 -0.1015 0.0474  0.0438  264 LYS A C     
1992 O  O     . LYS A 271 ? 0.5015 0.5188 0.5300 -0.0976 0.0392  0.0360  264 LYS A O     
1993 C  CB    . LYS A 271 ? 0.5715 0.6428 0.6271 -0.1289 0.0519  0.0595  264 LYS A CB    
1994 C  CG    . LYS A 271 ? 0.5902 0.7052 0.6692 -0.1372 0.0587  0.0655  264 LYS A CG    
1995 C  CD    . LYS A 271 ? 0.5930 0.7372 0.6726 -0.1290 0.0737  0.0686  264 LYS A CD    
1996 C  CE    . LYS A 271 ? 0.6193 0.8107 0.7241 -0.1381 0.0812  0.0755  264 LYS A CE    
1997 N  NZ    . LYS A 271 ? 0.6420 0.8567 0.7419 -0.1370 0.0968  0.0825  264 LYS A NZ    
1998 N  N     . SER A 272 ? 0.5265 0.5400 0.5385 -0.1007 0.0502  0.0483  265 SER A N     
1999 C  CA    . SER A 272 ? 0.5171 0.4981 0.5131 -0.0939 0.0436  0.0439  265 SER A CA    
2000 C  C     . SER A 272 ? 0.5363 0.4927 0.5314 -0.1025 0.0327  0.0433  265 SER A C     
2001 O  O     . SER A 272 ? 0.5719 0.5246 0.5705 -0.1178 0.0299  0.0513  265 SER A O     
2002 C  CB    . SER A 272 ? 0.5305 0.5001 0.5101 -0.0919 0.0472  0.0500  265 SER A CB    
2003 O  OG    . SER A 272 ? 0.5233 0.4650 0.4908 -0.0844 0.0399  0.0455  265 SER A OG    
2004 N  N     . ILE A 273 ? 0.5183 0.4570 0.5077 -0.0929 0.0263  0.0337  266 ILE A N     
2005 C  CA    . ILE A 273 ? 0.5426 0.4524 0.5257 -0.0971 0.0160  0.0311  266 ILE A CA    
2006 C  C     . ILE A 273 ? 0.5805 0.4661 0.5518 -0.1035 0.0133  0.0402  266 ILE A C     
2007 O  O     . ILE A 273 ? 0.6172 0.4791 0.5851 -0.1123 0.0045  0.0415  266 ILE A O     
2008 C  CB    . ILE A 273 ? 0.5208 0.4183 0.4976 -0.0833 0.0118  0.0193  266 ILE A CB    
2009 C  CG1   . ILE A 273 ? 0.5085 0.3964 0.4744 -0.0712 0.0141  0.0186  266 ILE A CG1   
2010 C  CG2   . ILE A 273 ? 0.4902 0.4100 0.4765 -0.0785 0.0139  0.0127  266 ILE A CG2   
2011 C  CD1   . ILE A 273 ? 0.4904 0.3721 0.4526 -0.0587 0.0114  0.0081  266 ILE A CD1   
2012 N  N     . LEU A 274 ? 0.5777 0.4666 0.5412 -0.0994 0.0196  0.0465  267 LEU A N     
2013 C  CA    . LEU A 274 ? 0.6167 0.4821 0.5670 -0.1044 0.0163  0.0564  267 LEU A CA    
2014 C  C     . LEU A 274 ? 0.6570 0.5278 0.6108 -0.1240 0.0182  0.0698  267 LEU A C     
2015 O  O     . LEU A 274 ? 0.7011 0.5475 0.6436 -0.1320 0.0133  0.0797  267 LEU A O     
2016 C  CB    . LEU A 274 ? 0.6045 0.4741 0.5439 -0.0942 0.0218  0.0591  267 LEU A CB    
2017 C  CG    . LEU A 274 ? 0.5702 0.4366 0.5066 -0.0767 0.0200  0.0481  267 LEU A CG    
2018 C  CD1   . LEU A 274 ? 0.5618 0.4373 0.4889 -0.0698 0.0253  0.0513  267 LEU A CD1   
2019 C  CD2   . LEU A 274 ? 0.5888 0.4248 0.5182 -0.0702 0.0096  0.0440  267 LEU A CD2   
2020 N  N     . GLU A 275 ? 0.6454 0.5488 0.6152 -0.1312 0.0250  0.0707  268 GLU A N     
2021 C  CA    . GLU A 275 ? 0.6817 0.6012 0.6595 -0.1504 0.0291  0.0837  268 GLU A CA    
2022 C  C     . GLU A 275 ? 0.7022 0.6184 0.6934 -0.1645 0.0203  0.0822  268 GLU A C     
2023 O  O     . GLU A 275 ? 0.7514 0.6575 0.7429 -0.1836 0.0163  0.0935  268 GLU A O     
2024 C  CB    . GLU A 275 ? 0.6627 0.6248 0.6498 -0.1476 0.0434  0.0860  268 GLU A CB    
2025 C  CG    . GLU A 275 ? 0.6609 0.6223 0.6306 -0.1381 0.0508  0.0898  268 GLU A CG    
2026 C  CD    . GLU A 275 ? 0.6457 0.6446 0.6194 -0.1310 0.0647  0.0889  268 GLU A CD    
2027 O  OE1   . GLU A 275 ? 0.6361 0.6666 0.6292 -0.1327 0.0700  0.0862  268 GLU A OE1   
2028 O  OE2   . GLU A 275 ? 0.6470 0.6434 0.6040 -0.1226 0.0696  0.0902  268 GLU A OE2   
2029 N  N     . VAL A 276 ? 0.6707 0.5942 0.6717 -0.1568 0.0164  0.0692  269 VAL A N     
2030 C  CA    . VAL A 276 ? 0.6911 0.6190 0.7062 -0.1708 0.0084  0.0677  269 VAL A CA    
2031 C  C     . VAL A 276 ? 0.6911 0.5882 0.6982 -0.1645 -0.0042 0.0546  269 VAL A C     
2032 O  O     . VAL A 276 ? 0.7175 0.6083 0.7308 -0.1762 -0.0141 0.0518  269 VAL A O     
2033 C  CB    . VAL A 276 ? 0.6684 0.6432 0.7062 -0.1719 0.0153  0.0667  269 VAL A CB    
2034 C  CG1   . VAL A 276 ? 0.6788 0.6871 0.7253 -0.1785 0.0285  0.0790  269 VAL A CG1   
2035 C  CG2   . VAL A 276 ? 0.6161 0.6039 0.6559 -0.1513 0.0181  0.0539  269 VAL A CG2   
2036 N  N     . GLY A 277 ? 0.6686 0.5459 0.6611 -0.1468 -0.0046 0.0466  270 GLY A N     
2037 C  CA    . GLY A 277 ? 0.6695 0.5219 0.6535 -0.1382 -0.0143 0.0333  270 GLY A CA    
2038 C  C     . GLY A 277 ? 0.6240 0.5009 0.6157 -0.1266 -0.0113 0.0228  270 GLY A C     
2039 O  O     . GLY A 277 ? 0.6000 0.5108 0.6060 -0.1279 -0.0043 0.0258  270 GLY A O     
2040 N  N     . VAL A 278 ? 0.6195 0.4785 0.6011 -0.1155 -0.0171 0.0107  271 VAL A N     
2041 C  CA    . VAL A 278 ? 0.5807 0.4580 0.5649 -0.1034 -0.0143 0.0015  271 VAL A CA    
2042 C  C     . VAL A 278 ? 0.5845 0.4820 0.5813 -0.1126 -0.0186 0.0001  271 VAL A C     
2043 O  O     . VAL A 278 ? 0.5534 0.4795 0.5606 -0.1080 -0.0133 0.0004  271 VAL A O     
2044 C  CB    . VAL A 278 ? 0.5825 0.4379 0.5517 -0.0900 -0.0186 -0.0103 271 VAL A CB    
2045 C  CG1   . VAL A 278 ? 0.5506 0.4253 0.5214 -0.0807 -0.0162 -0.0179 271 VAL A CG1   
2046 C  CG2   . VAL A 278 ? 0.5758 0.4177 0.5359 -0.0788 -0.0144 -0.0090 271 VAL A CG2   
2047 N  N     . GLN A 279 ? 0.6279 0.5094 0.6236 -0.1255 -0.0294 -0.0015 272 GLN A N     
2048 C  CA    . GLN A 279 ? 0.6367 0.5367 0.6438 -0.1345 -0.0362 -0.0041 272 GLN A CA    
2049 C  C     . GLN A 279 ? 0.6210 0.5601 0.6505 -0.1418 -0.0293 0.0061  272 GLN A C     
2050 O  O     . GLN A 279 ? 0.6003 0.5656 0.6401 -0.1373 -0.0288 0.0037  272 GLN A O     
2051 C  CB    . GLN A 279 ? 0.6943 0.5679 0.6962 -0.1498 -0.0502 -0.0070 272 GLN A CB    
2052 C  CG    . GLN A 279 ? 0.7071 0.6008 0.7219 -0.1618 -0.0592 -0.0089 272 GLN A CG    
2053 C  CD    . GLN A 279 ? 0.7705 0.6373 0.7804 -0.1796 -0.0747 -0.0117 272 GLN A CD    
2054 O  OE1   . GLN A 279 ? 0.8034 0.6351 0.7928 -0.1750 -0.0837 -0.0234 272 GLN A OE1   
2055 N  NE2   . GLN A 279 ? 0.7929 0.6767 0.8216 -0.2004 -0.0780 -0.0013 272 GLN A NE2   
2056 N  N     . GLN A 280 ? 0.6360 0.5789 0.6720 -0.1524 -0.0242 0.0175  273 GLN A N     
2057 C  CA    . GLN A 280 ? 0.6297 0.6127 0.6876 -0.1595 -0.0168 0.0269  273 GLN A CA    
2058 C  C     . GLN A 280 ? 0.5819 0.5881 0.6426 -0.1414 -0.0046 0.0260  273 GLN A C     
2059 O  O     . GLN A 280 ? 0.5692 0.6098 0.6470 -0.1390 -0.0008 0.0274  273 GLN A O     
2060 C  CB    . GLN A 280 ? 0.6644 0.6453 0.7258 -0.1761 -0.0135 0.0401  273 GLN A CB    
2061 C  CG    . GLN A 280 ? 0.6604 0.6866 0.7436 -0.1817 -0.0029 0.0500  273 GLN A CG    
2062 C  CD    . GLN A 280 ? 0.6818 0.7379 0.7886 -0.1958 -0.0094 0.0518  273 GLN A CD    
2063 O  OE1   . GLN A 280 ? 0.7097 0.7490 0.8156 -0.2067 -0.0234 0.0475  273 GLN A OE1   
2064 N  NE2   . GLN A 280 ? 0.6708 0.7728 0.7989 -0.1940 0.0003  0.0570  273 GLN A NE2   
2065 N  N     . ALA A 281 ? 0.5603 0.5470 0.6043 -0.1283 0.0005  0.0234  274 ALA A N     
2066 C  CA    . ALA A 281 ? 0.5207 0.5236 0.5647 -0.1120 0.0101  0.0214  274 ALA A CA    
2067 C  C     . ALA A 281 ? 0.4981 0.5107 0.5449 -0.1016 0.0064  0.0130  274 ALA A C     
2068 O  O     . ALA A 281 ? 0.4826 0.5213 0.5409 -0.0951 0.0110  0.0138  274 ALA A O     
2069 C  CB    . ALA A 281 ? 0.5086 0.4882 0.5348 -0.1028 0.0141  0.0205  274 ALA A CB    
2070 N  N     . LEU A 282 ? 0.5035 0.4958 0.5398 -0.1005 -0.0024 0.0054  275 LEU A N     
2071 C  CA    . LEU A 282 ? 0.4873 0.4851 0.5214 -0.0910 -0.0062 -0.0016 275 LEU A CA    
2072 C  C     . LEU A 282 ? 0.4978 0.5221 0.5490 -0.0964 -0.0117 -0.0004 275 LEU A C     
2073 O  O     . LEU A 282 ? 0.4816 0.5205 0.5361 -0.0867 -0.0118 -0.0023 275 LEU A O     
2074 C  CB    . LEU A 282 ? 0.5005 0.4697 0.5166 -0.0896 -0.0136 -0.0101 275 LEU A CB    
2075 C  CG    . LEU A 282 ? 0.4896 0.4593 0.4968 -0.0798 -0.0168 -0.0174 275 LEU A CG    
2076 C  CD1   . LEU A 282 ? 0.4551 0.4332 0.4607 -0.0671 -0.0082 -0.0159 275 LEU A CD1   
2077 C  CD2   . LEU A 282 ? 0.5099 0.4528 0.4985 -0.0780 -0.0223 -0.0263 275 LEU A CD2   
2078 N  N     . GLN A 283 ? 0.5283 0.5596 0.5913 -0.1123 -0.0165 0.0038  276 GLN A N     
2079 C  CA    . GLN A 283 ? 0.5455 0.6051 0.6282 -0.1204 -0.0231 0.0058  276 GLN A CA    
2080 C  C     . GLN A 283 ? 0.5258 0.6211 0.6266 -0.1112 -0.0143 0.0106  276 GLN A C     
2081 O  O     . GLN A 283 ? 0.5289 0.6482 0.6434 -0.1082 -0.0193 0.0100  276 GLN A O     
2082 C  CB    . GLN A 283 ? 0.5866 0.6435 0.6776 -0.1418 -0.0291 0.0108  276 GLN A CB    
2083 C  CG    . GLN A 283 ? 0.6047 0.7021 0.7243 -0.1534 -0.0293 0.0188  276 GLN A CG    
2084 C  CD    . GLN A 283 ? 0.5952 0.7198 0.7290 -0.1520 -0.0145 0.0282  276 GLN A CD    
2085 O  OE1   . GLN A 283 ? 0.5995 0.7647 0.7572 -0.1527 -0.0113 0.0327  276 GLN A OE1   
2086 N  NE2   . GLN A 283 ? 0.5855 0.6900 0.7045 -0.1489 -0.0054 0.0309  276 GLN A NE2   
2087 N  N     . ALA A 284 ? 0.5087 0.6055 0.6074 -0.1046 -0.0018 0.0145  277 ALA A N     
2088 C  CA    . ALA A 284 ? 0.4985 0.6266 0.6122 -0.0955 0.0077  0.0181  277 ALA A CA    
2089 C  C     . ALA A 284 ? 0.4724 0.5989 0.5793 -0.0759 0.0093  0.0127  277 ALA A C     
2090 O  O     . ALA A 284 ? 0.4681 0.6166 0.5853 -0.0653 0.0162  0.0139  277 ALA A O     
2091 C  CB    . ALA A 284 ? 0.4997 0.6273 0.6101 -0.0979 0.0196  0.0239  277 ALA A CB    
2092 N  N     . VAL A 285 ? 0.4592 0.5589 0.5476 -0.0706 0.0038  0.0070  278 VAL A N     
2093 C  CA    . VAL A 285 ? 0.4408 0.5375 0.5222 -0.0546 0.0046  0.0038  278 VAL A CA    
2094 C  C     . VAL A 285 ? 0.4472 0.5395 0.5239 -0.0537 -0.0068 0.0003  278 VAL A C     
2095 O  O     . VAL A 285 ? 0.4614 0.5442 0.5332 -0.0638 -0.0145 -0.0018 278 VAL A O     
2096 C  CB    . VAL A 285 ? 0.4199 0.4916 0.4821 -0.0475 0.0110  0.0016  278 VAL A CB    
2097 C  CG1   . VAL A 285 ? 0.4167 0.4924 0.4802 -0.0468 0.0217  0.0048  278 VAL A CG1   
2098 C  CG2   . VAL A 285 ? 0.4188 0.4639 0.4642 -0.0530 0.0065  -0.0018 278 VAL A CG2   
2099 N  N     . PHE A 286 ? 0.4420 0.5390 0.5181 -0.0411 -0.0084 0.0000  279 PHE A N     
2100 C  CA    . PHE A 286 ? 0.4501 0.5405 0.5169 -0.0386 -0.0187 -0.0020 279 PHE A CA    
2101 C  C     . PHE A 286 ? 0.4357 0.4988 0.4791 -0.0340 -0.0162 -0.0046 279 PHE A C     
2102 O  O     . PHE A 286 ? 0.4204 0.4761 0.4593 -0.0264 -0.0088 -0.0036 279 PHE A O     
2103 C  CB    . PHE A 286 ? 0.4610 0.5715 0.5403 -0.0281 -0.0234 0.0005  279 PHE A CB    
2104 C  CG    . PHE A 286 ? 0.4733 0.5756 0.5401 -0.0245 -0.0342 0.0001  279 PHE A CG    
2105 C  CD1   . PHE A 286 ? 0.4925 0.5966 0.5562 -0.0341 -0.0449 -0.0018 279 PHE A CD1   
2106 C  CD2   . PHE A 286 ? 0.4713 0.5613 0.5263 -0.0126 -0.0343 0.0019  279 PHE A CD2   
2107 C  CE1   . PHE A 286 ? 0.5084 0.6049 0.5570 -0.0308 -0.0545 -0.0018 279 PHE A CE1   
2108 C  CE2   . PHE A 286 ? 0.4880 0.5700 0.5290 -0.0104 -0.0440 0.0034  279 PHE A CE2   
2109 C  CZ    . PHE A 286 ? 0.5061 0.5926 0.5435 -0.0190 -0.0538 0.0014  279 PHE A CZ    
2110 N  N     . TRP A 287 ? 0.4451 0.4949 0.4741 -0.0392 -0.0224 -0.0081 280 TRP A N     
2111 C  CA    . TRP A 287 ? 0.4383 0.4680 0.4462 -0.0356 -0.0206 -0.0104 280 TRP A CA    
2112 C  C     . TRP A 287 ? 0.4595 0.4895 0.4567 -0.0349 -0.0303 -0.0112 280 TRP A C     
2113 O  O     . TRP A 287 ? 0.4806 0.5123 0.4757 -0.0421 -0.0384 -0.0149 280 TRP A O     
2114 C  CB    . TRP A 287 ? 0.4346 0.4478 0.4328 -0.0411 -0.0166 -0.0150 280 TRP A CB    
2115 C  CG    . TRP A 287 ? 0.4326 0.4304 0.4111 -0.0374 -0.0143 -0.0182 280 TRP A CG    
2116 C  CD1   . TRP A 287 ? 0.4206 0.4154 0.3922 -0.0307 -0.0097 -0.0150 280 TRP A CD1   
2117 C  CD2   . TRP A 287 ? 0.4474 0.4320 0.4114 -0.0400 -0.0159 -0.0251 280 TRP A CD2   
2118 N  NE1   . TRP A 287 ? 0.4256 0.4106 0.3811 -0.0300 -0.0077 -0.0185 280 TRP A NE1   
2119 C  CE2   . TRP A 287 ? 0.4419 0.4210 0.3922 -0.0342 -0.0110 -0.0254 280 TRP A CE2   
2120 C  CE3   . TRP A 287 ? 0.4700 0.4461 0.4307 -0.0466 -0.0214 -0.0314 280 TRP A CE3   
2121 C  CZ2   . TRP A 287 ? 0.4566 0.4263 0.3915 -0.0330 -0.0099 -0.0322 280 TRP A CZ2   
2122 C  CZ3   . TRP A 287 ? 0.4865 0.4483 0.4298 -0.0444 -0.0215 -0.0391 280 TRP A CZ3   
2123 C  CH2   . TRP A 287 ? 0.4796 0.4401 0.4105 -0.0369 -0.0152 -0.0398 280 TRP A CH2   
2124 N  N     . ASP A 288 ? 0.4593 0.4869 0.4491 -0.0269 -0.0305 -0.0071 281 ASP A N     
2125 C  CA    . ASP A 288 ? 0.4837 0.5112 0.4606 -0.0255 -0.0397 -0.0056 281 ASP A CA    
2126 C  C     . ASP A 288 ? 0.4900 0.5027 0.4438 -0.0285 -0.0374 -0.0096 281 ASP A C     
2127 O  O     . ASP A 288 ? 0.4834 0.4870 0.4256 -0.0251 -0.0314 -0.0067 281 ASP A O     
2128 C  CB    . ASP A 288 ? 0.4880 0.5156 0.4646 -0.0162 -0.0413 0.0017  281 ASP A CB    
2129 C  CG    . ASP A 288 ? 0.5195 0.5492 0.4852 -0.0141 -0.0528 0.0057  281 ASP A CG    
2130 O  OD1   . ASP A 288 ? 0.5364 0.5651 0.4893 -0.0200 -0.0578 0.0021  281 ASP A OD1   
2131 O  OD2   . ASP A 288 ? 0.5312 0.5627 0.5010 -0.0058 -0.0573 0.0122  281 ASP A OD2   
2132 N  N     . GLU A 289 ? 0.5067 0.5176 0.4544 -0.0349 -0.0421 -0.0167 282 GLU A N     
2133 C  CA    . GLU A 289 ? 0.5194 0.5180 0.4454 -0.0360 -0.0397 -0.0230 282 GLU A CA    
2134 C  C     . GLU A 289 ? 0.5433 0.5419 0.4489 -0.0331 -0.0433 -0.0199 282 GLU A C     
2135 O  O     . GLU A 289 ? 0.5482 0.5404 0.4368 -0.0315 -0.0367 -0.0216 282 GLU A O     
2136 C  CB    . GLU A 289 ? 0.5395 0.5329 0.4636 -0.0428 -0.0454 -0.0325 282 GLU A CB    
2137 C  CG    . GLU A 289 ? 0.5503 0.5289 0.4558 -0.0414 -0.0404 -0.0412 282 GLU A CG    
2138 C  CD    . GLU A 289 ? 0.5654 0.5313 0.4722 -0.0469 -0.0436 -0.0503 282 GLU A CD    
2139 O  OE1   . GLU A 289 ? 0.5758 0.5288 0.4687 -0.0430 -0.0390 -0.0579 282 GLU A OE1   
2140 O  OE2   . GLU A 289 ? 0.5686 0.5377 0.4913 -0.0546 -0.0500 -0.0492 282 GLU A OE2   
2141 N  N     . GLU A 290 ? 0.5613 0.5687 0.4687 -0.0323 -0.0534 -0.0146 283 GLU A N     
2142 C  CA    . GLU A 290 ? 0.5888 0.5953 0.4756 -0.0298 -0.0577 -0.0092 283 GLU A CA    
2143 C  C     . GLU A 290 ? 0.5742 0.5747 0.4575 -0.0257 -0.0488 -0.0003 283 GLU A C     
2144 O  O     . GLU A 290 ? 0.5902 0.5860 0.4530 -0.0263 -0.0447 0.0020  283 GLU A O     
2145 C  CB    . GLU A 290 ? 0.6132 0.6300 0.5045 -0.0285 -0.0717 -0.0039 283 GLU A CB    
2146 C  CG    . GLU A 290 ? 0.6384 0.6617 0.5294 -0.0345 -0.0831 -0.0120 283 GLU A CG    
2147 C  CD    . GLU A 290 ? 0.6636 0.7014 0.5628 -0.0329 -0.0982 -0.0064 283 GLU A CD    
2148 O  OE1   . GLU A 290 ? 0.6566 0.6996 0.5672 -0.0256 -0.0990 0.0031  283 GLU A OE1   
2149 O  OE2   . GLU A 290 ? 0.6953 0.7381 0.5883 -0.0385 -0.1101 -0.0121 283 GLU A OE2   
2150 N  N     . ALA A 291 ? 0.5488 0.5499 0.4519 -0.0222 -0.0460 0.0042  284 ALA A N     
2151 C  CA    . ALA A 291 ? 0.5366 0.5290 0.4383 -0.0194 -0.0387 0.0112  284 ALA A CA    
2152 C  C     . ALA A 291 ? 0.5202 0.5074 0.4152 -0.0227 -0.0269 0.0072  284 ALA A C     
2153 O  O     . ALA A 291 ? 0.5279 0.5101 0.4111 -0.0239 -0.0222 0.0130  284 ALA A O     
2154 C  CB    . ALA A 291 ? 0.5182 0.5117 0.4410 -0.0139 -0.0385 0.0139  284 ALA A CB    
2155 N  N     . PHE A 292 ? 0.5023 0.4911 0.4051 -0.0244 -0.0227 -0.0017 285 PHE A N     
2156 C  CA    . PHE A 292 ? 0.4891 0.4745 0.3883 -0.0255 -0.0128 -0.0064 285 PHE A CA    
2157 C  C     . PHE A 292 ? 0.5149 0.5017 0.3925 -0.0265 -0.0101 -0.0079 285 PHE A C     
2158 O  O     . PHE A 292 ? 0.5133 0.5011 0.3855 -0.0270 -0.0021 -0.0047 285 PHE A O     
2159 C  CB    . PHE A 292 ? 0.4772 0.4615 0.3861 -0.0266 -0.0120 -0.0156 285 PHE A CB    
2160 C  CG    . PHE A 292 ? 0.4708 0.4509 0.3756 -0.0258 -0.0039 -0.0218 285 PHE A CG    
2161 C  CD1   . PHE A 292 ? 0.4465 0.4252 0.3601 -0.0244 0.0036  -0.0193 285 PHE A CD1   
2162 C  CD2   . PHE A 292 ? 0.4937 0.4707 0.3859 -0.0254 -0.0048 -0.0311 285 PHE A CD2   
2163 C  CE1   . PHE A 292 ? 0.4437 0.4206 0.3553 -0.0223 0.0099  -0.0249 285 PHE A CE1   
2164 C  CE2   . PHE A 292 ? 0.4920 0.4651 0.3823 -0.0222 0.0019  -0.0377 285 PHE A CE2   
2165 C  CZ    . PHE A 292 ? 0.4666 0.4409 0.3672 -0.0204 0.0093  -0.0340 285 PHE A CZ    
2166 N  N     . VAL A 293 ? 0.5438 0.5325 0.4084 -0.0273 -0.0171 -0.0124 286 VAL A N     
2167 C  CA    . VAL A 293 ? 0.5754 0.5669 0.4164 -0.0274 -0.0141 -0.0147 286 VAL A CA    
2168 C  C     . VAL A 293 ? 0.5916 0.5857 0.4210 -0.0291 -0.0128 -0.0018 286 VAL A C     
2169 O  O     . VAL A 293 ? 0.6039 0.6030 0.4214 -0.0304 -0.0041 0.0007  286 VAL A O     
2170 C  CB    . VAL A 293 ? 0.6094 0.6005 0.4361 -0.0279 -0.0233 -0.0235 286 VAL A CB    
2171 C  CG1   . VAL A 293 ? 0.6512 0.6466 0.4493 -0.0275 -0.0215 -0.0241 286 VAL A CG1   
2172 C  CG2   . VAL A 293 ? 0.6041 0.5886 0.4377 -0.0275 -0.0236 -0.0368 286 VAL A CG2   
2173 N  N     . GLU A 294 ? 0.5978 0.5891 0.4303 -0.0292 -0.0221 0.0067  287 GLU A N     
2174 C  CA    . GLU A 294 ? 0.6235 0.6124 0.4425 -0.0311 -0.0241 0.0201  287 GLU A CA    
2175 C  C     . GLU A 294 ? 0.6085 0.5938 0.4330 -0.0338 -0.0148 0.0279  287 GLU A C     
2176 O  O     . GLU A 294 ? 0.6356 0.6209 0.4446 -0.0383 -0.0122 0.0376  287 GLU A O     
2177 C  CB    . GLU A 294 ? 0.6327 0.6173 0.4582 -0.0281 -0.0372 0.0270  287 GLU A CB    
2178 C  CG    . GLU A 294 ? 0.6693 0.6470 0.4783 -0.0295 -0.0421 0.0421  287 GLU A CG    
2179 C  CD    . GLU A 294 ? 0.6956 0.6718 0.5037 -0.0249 -0.0577 0.0475  287 GLU A CD    
2180 O  OE1   . GLU A 294 ? 0.7085 0.6935 0.5125 -0.0243 -0.0651 0.0404  287 GLU A OE1   
2181 O  OE2   . GLU A 294 ? 0.7074 0.6730 0.5195 -0.0213 -0.0640 0.0586  287 GLU A OE2   
2182 N  N     . ARG A 295 ? 0.5705 0.5526 0.4160 -0.0321 -0.0107 0.0243  288 ARG A N     
2183 C  CA    . ARG A 295 ? 0.5600 0.5378 0.4108 -0.0354 -0.0039 0.0310  288 ARG A CA    
2184 C  C     . ARG A 295 ? 0.5570 0.5460 0.4041 -0.0385 0.0076  0.0268  288 ARG A C     
2185 O  O     . ARG A 295 ? 0.5541 0.5436 0.4048 -0.0432 0.0134  0.0328  288 ARG A O     
2186 C  CB    . ARG A 295 ? 0.5265 0.4966 0.3986 -0.0321 -0.0043 0.0289  288 ARG A CB    
2187 C  CG    . ARG A 295 ? 0.4942 0.4699 0.3800 -0.0295 0.0005  0.0172  288 ARG A CG    
2188 C  CD    . ARG A 295 ? 0.4680 0.4370 0.3708 -0.0271 0.0014  0.0170  288 ARG A CD    
2189 N  NE    . ARG A 295 ? 0.4412 0.4135 0.3570 -0.0248 0.0045  0.0081  288 ARG A NE    
2190 C  CZ    . ARG A 295 ? 0.4273 0.4027 0.3457 -0.0256 0.0112  0.0029  288 ARG A CZ    
2191 N  NH1   . ARG A 295 ? 0.4346 0.4143 0.3460 -0.0284 0.0167  0.0046  288 ARG A NH1   
2192 N  NH2   . ARG A 295 ? 0.4092 0.3843 0.3379 -0.0237 0.0123  -0.0033 288 ARG A NH2   
2193 N  N     . GLY A 296 ? 0.5617 0.5597 0.4023 -0.0356 0.0104  0.0161  289 GLY A N     
2194 C  CA    . GLY A 296 ? 0.5647 0.5752 0.4021 -0.0353 0.0213  0.0102  289 GLY A CA    
2195 C  C     . GLY A 296 ? 0.5319 0.5420 0.3869 -0.0307 0.0252  0.0000  289 GLY A C     
2196 O  O     . GLY A 296 ? 0.5274 0.5475 0.3871 -0.0300 0.0339  -0.0022 289 GLY A O     
2197 N  N     . GLY A 297 ? 0.5130 0.5132 0.3779 -0.0276 0.0184  -0.0058 290 GLY A N     
2198 C  CA    . GLY A 297 ? 0.4863 0.4832 0.3664 -0.0242 0.0208  -0.0134 290 GLY A CA    
2199 C  C     . GLY A 297 ? 0.4987 0.5001 0.3733 -0.0191 0.0260  -0.0246 290 GLY A C     
2200 O  O     . GLY A 297 ? 0.4816 0.4815 0.3677 -0.0160 0.0294  -0.0287 290 GLY A O     
2201 N  N     . ILE A 298 ? 0.5327 0.5377 0.3889 -0.0172 0.0254  -0.0303 291 ILE A N     
2202 C  CA    . ILE A 298 ? 0.5549 0.5644 0.4027 -0.0100 0.0310  -0.0421 291 ILE A CA    
2203 C  C     . ILE A 298 ? 0.5753 0.6047 0.4137 -0.0101 0.0411  -0.0376 291 ILE A C     
2204 O  O     . ILE A 298 ? 0.5953 0.6301 0.4200 -0.0152 0.0404  -0.0298 291 ILE A O     
2205 C  CB    . ILE A 298 ? 0.5879 0.5882 0.4191 -0.0072 0.0239  -0.0535 291 ILE A CB    
2206 C  CG1   . ILE A 298 ? 0.5738 0.5576 0.4150 -0.0105 0.0130  -0.0557 291 ILE A CG1   
2207 C  CG2   . ILE A 298 ? 0.6180 0.6193 0.4390 0.0025  0.0292  -0.0678 291 ILE A CG2   
2208 C  CD1   . ILE A 298 ? 0.5536 0.5276 0.4102 -0.0078 0.0139  -0.0601 291 ILE A CD1   
2209 N  N     . TYR A 299 ? 0.5724 0.6135 0.4194 -0.0048 0.0500  -0.0412 292 TYR A N     
2210 C  CA    . TYR A 299 ? 0.5924 0.6580 0.4355 -0.0053 0.0611  -0.0369 292 TYR A CA    
2211 C  C     . TYR A 299 ? 0.5997 0.6770 0.4508 0.0059  0.0687  -0.0477 292 TYR A C     
2212 O  O     . TYR A 299 ? 0.5894 0.6515 0.4475 0.0132  0.0641  -0.0572 292 TYR A O     
2213 C  CB    . TYR A 299 ? 0.5720 0.6430 0.4263 -0.0165 0.0622  -0.0206 292 TYR A CB    
2214 C  CG    . TYR A 299 ? 0.5337 0.6000 0.4113 -0.0180 0.0610  -0.0175 292 TYR A CG    
2215 C  CD1   . TYR A 299 ? 0.5038 0.5489 0.3901 -0.0194 0.0522  -0.0166 292 TYR A CD1   
2216 C  CD2   . TYR A 299 ? 0.5312 0.6167 0.4222 -0.0179 0.0687  -0.0156 292 TYR A CD2   
2217 C  CE1   . TYR A 299 ? 0.4745 0.5155 0.3785 -0.0205 0.0513  -0.0141 292 TYR A CE1   
2218 C  CE2   . TYR A 299 ? 0.5009 0.5818 0.4109 -0.0196 0.0663  -0.0129 292 TYR A CE2   
2219 C  CZ    . TYR A 299 ? 0.4732 0.5306 0.3881 -0.0209 0.0577  -0.0122 292 TYR A CZ    
2220 O  OH    . TYR A 299 ? 0.4486 0.5013 0.3787 -0.0227 0.0553  -0.0096 292 TYR A OH    
2221 N  N     . ASP A 300 ? 0.6219 0.7275 0.4724 0.0072  0.0801  -0.0455 293 ASP A N     
2222 C  CA    . ASP A 300 ? 0.6332 0.7553 0.4937 0.0196  0.0878  -0.0553 293 ASP A CA    
2223 C  C     . ASP A 300 ? 0.5958 0.7209 0.4828 0.0168  0.0870  -0.0488 293 ASP A C     
2224 O  O     . ASP A 300 ? 0.5920 0.7398 0.4905 0.0091  0.0931  -0.0382 293 ASP A O     
2225 C  CB    . ASP A 300 ? 0.6748 0.8319 0.5270 0.0226  0.1014  -0.0555 293 ASP A CB    
2226 C  CG    . ASP A 300 ? 0.7183 0.8745 0.5404 0.0247  0.1027  -0.0612 293 ASP A CG    
2227 O  OD1   . ASP A 300 ? 0.7318 0.8651 0.5406 0.0337  0.0956  -0.0753 293 ASP A OD1   
2228 O  OD2   . ASP A 300 ? 0.7428 0.9201 0.5536 0.0164  0.1101  -0.0512 293 ASP A OD2   
2229 N  N     . TRP A 301 ? 0.5734 0.6751 0.4688 0.0222  0.0790  -0.0549 294 TRP A N     
2230 C  CA    . TRP A 301 ? 0.5361 0.6327 0.4517 0.0172  0.0751  -0.0475 294 TRP A CA    
2231 C  C     . TRP A 301 ? 0.5389 0.6468 0.4703 0.0287  0.0778  -0.0537 294 TRP A C     
2232 O  O     . TRP A 301 ? 0.5132 0.6127 0.4589 0.0276  0.0728  -0.0504 294 TRP A O     
2233 C  CB    . TRP A 301 ? 0.5106 0.5755 0.4246 0.0131  0.0643  -0.0470 294 TRP A CB    
2234 C  CG    . TRP A 301 ? 0.5274 0.5715 0.4299 0.0213  0.0589  -0.0592 294 TRP A CG    
2235 C  CD1   . TRP A 301 ? 0.5548 0.5954 0.4536 0.0347  0.0597  -0.0721 294 TRP A CD1   
2236 C  CD2   . TRP A 301 ? 0.5205 0.5419 0.4152 0.0156  0.0501  -0.0592 294 TRP A CD2   
2237 N  NE1   . TRP A 301 ? 0.5666 0.5805 0.4546 0.0360  0.0512  -0.0798 294 TRP A NE1   
2238 C  CE2   . TRP A 301 ? 0.5450 0.5493 0.4313 0.0238  0.0455  -0.0719 294 TRP A CE2   
2239 C  CE3   . TRP A 301 ? 0.5000 0.5146 0.3949 0.0049  0.0451  -0.0498 294 TRP A CE3   
2240 C  CZ2   . TRP A 301 ? 0.5484 0.5313 0.4278 0.0191  0.0361  -0.0745 294 TRP A CZ2   
2241 C  CZ3   . TRP A 301 ? 0.5010 0.4974 0.3908 0.0023  0.0366  -0.0527 294 TRP A CZ3   
2242 C  CH2   . TRP A 301 ? 0.5239 0.5057 0.4069 0.0081  0.0321  -0.0644 294 TRP A CH2   
2243 N  N     . ASN A 302 ? 0.5745 0.7030 0.5028 0.0409  0.0856  -0.0628 295 ASN A N     
2244 C  CA    . ASN A 302 ? 0.5842 0.7325 0.5299 0.0529  0.0895  -0.0673 295 ASN A CA    
2245 C  C     . ASN A 302 ? 0.6182 0.8081 0.5653 0.0566  0.1027  -0.0679 295 ASN A C     
2246 O  O     . ASN A 302 ? 0.6462 0.8383 0.5729 0.0576  0.1075  -0.0723 295 ASN A O     
2247 C  CB    . ASN A 302 ? 0.6020 0.7282 0.5446 0.0704  0.0841  -0.0817 295 ASN A CB    
2248 C  CG    . ASN A 302 ? 0.6378 0.7481 0.5566 0.0784  0.0838  -0.0946 295 ASN A CG    
2249 O  OD1   . ASN A 302 ? 0.6670 0.7980 0.5739 0.0803  0.0925  -0.0977 295 ASN A OD1   
2250 N  ND2   . ASN A 302 ? 0.6402 0.7135 0.5505 0.0819  0.0735  -0.1016 295 ASN A ND2   
2251 N  N     . GLY B 24  ? 0.8455 0.6940 0.6540 0.1731  -0.0226 0.0980  17  GLY B N     
2252 C  CA    . GLY B 24  ? 0.8204 0.6948 0.6494 0.1849  -0.0305 0.0839  17  GLY B CA    
2253 C  C     . GLY B 24  ? 0.7650 0.6804 0.6118 0.1779  -0.0309 0.0721  17  GLY B C     
2254 O  O     . GLY B 24  ? 0.7592 0.7016 0.6167 0.1884  -0.0393 0.0637  17  GLY B O     
2255 N  N     . GLN B 25  ? 0.7274 0.6477 0.5787 0.1598  -0.0221 0.0708  18  GLN B N     
2256 C  CA    . GLN B 25  ? 0.6799 0.6328 0.5465 0.1521  -0.0221 0.0597  18  GLN B CA    
2257 C  C     . GLN B 25  ? 0.6413 0.6114 0.5334 0.1505  -0.0228 0.0467  18  GLN B C     
2258 O  O     . GLN B 25  ? 0.6398 0.5947 0.5376 0.1496  -0.0194 0.0460  18  GLN B O     
2259 C  CB    . GLN B 25  ? 0.6574 0.6073 0.5212 0.1353  -0.0124 0.0622  18  GLN B CB    
2260 C  CG    . GLN B 25  ? 0.6977 0.6364 0.5361 0.1361  -0.0099 0.0745  18  GLN B CG    
2261 C  CD    . GLN B 25  ? 0.6798 0.6191 0.5175 0.1207  0.0007  0.0765  18  GLN B CD    
2262 O  OE1   . GLN B 25  ? 0.6729 0.5977 0.5158 0.1099  0.0086  0.0800  18  GLN B OE1   
2263 N  NE2   . GLN B 25  ? 0.6776 0.6345 0.5083 0.1203  0.0007  0.0736  18  GLN B NE2   
2264 N  N     . VAL B 26  ? 0.6154 0.6165 0.5214 0.1495  -0.0272 0.0365  19  VAL B N     
2265 C  CA    . VAL B 26  ? 0.5818 0.6030 0.5115 0.1458  -0.0268 0.0249  19  VAL B CA    
2266 C  C     . VAL B 26  ? 0.5388 0.5636 0.4768 0.1280  -0.0196 0.0206  19  VAL B C     
2267 O  O     . VAL B 26  ? 0.5281 0.5650 0.4649 0.1224  -0.0210 0.0179  19  VAL B O     
2268 C  CB    . VAL B 26  ? 0.5862 0.6398 0.5281 0.1539  -0.0362 0.0166  19  VAL B CB    
2269 C  CG1   . VAL B 26  ? 0.5530 0.6306 0.5201 0.1463  -0.0341 0.0051  19  VAL B CG1   
2270 C  CG2   . VAL B 26  ? 0.6321 0.6842 0.5676 0.1740  -0.0445 0.0203  19  VAL B CG2   
2271 N  N     . PRO B 27  ? 0.5182 0.5323 0.4636 0.1202  -0.0129 0.0191  20  PRO B N     
2272 C  CA    . PRO B 27  ? 0.4829 0.4981 0.4344 0.1049  -0.0069 0.0161  20  PRO B CA    
2273 C  C     . PRO B 27  ? 0.4567 0.4964 0.4244 0.0990  -0.0086 0.0062  20  PRO B C     
2274 O  O     . PRO B 27  ? 0.4384 0.4817 0.4172 0.0934  -0.0053 0.0015  20  PRO B O     
2275 C  CB    . PRO B 27  ? 0.4806 0.4755 0.4325 0.1011  -0.0013 0.0181  20  PRO B CB    
2276 C  CG    . PRO B 27  ? 0.5001 0.4958 0.4559 0.1131  -0.0044 0.0153  20  PRO B CG    
2277 C  CD    . PRO B 27  ? 0.5325 0.5316 0.4793 0.1264  -0.0113 0.0197  20  PRO B CD    
2278 N  N     . VAL B 28  ? 0.4586 0.5139 0.4260 0.0989  -0.0136 0.0030  21  VAL B N     
2279 C  CA    . VAL B 28  ? 0.4452 0.5235 0.4282 0.0936  -0.0167 -0.0062 21  VAL B CA    
2280 C  C     . VAL B 28  ? 0.4167 0.4919 0.4063 0.0793  -0.0114 -0.0096 21  VAL B C     
2281 O  O     . VAL B 28  ? 0.4066 0.4946 0.4096 0.0731  -0.0109 -0.0152 21  VAL B O     
2282 C  CB    . VAL B 28  ? 0.4615 0.5560 0.4420 0.0968  -0.0251 -0.0099 21  VAL B CB    
2283 C  CG1   . VAL B 28  ? 0.4624 0.5456 0.4277 0.0928  -0.0240 -0.0077 21  VAL B CG1   
2284 C  CG2   . VAL B 28  ? 0.4536 0.5719 0.4524 0.0894  -0.0287 -0.0197 21  VAL B CG2   
2285 N  N     . SER B 29  ? 0.4089 0.4679 0.3885 0.0745  -0.0076 -0.0057 22  SER B N     
2286 C  CA    . SER B 29  ? 0.3878 0.4425 0.3715 0.0634  -0.0041 -0.0086 22  SER B CA    
2287 C  C     . SER B 29  ? 0.3800 0.4168 0.3578 0.0609  0.0018  -0.0028 22  SER B C     
2288 O  O     . SER B 29  ? 0.3905 0.4199 0.3582 0.0636  0.0033  0.0021  22  SER B O     
2289 C  CB    . SER B 29  ? 0.3916 0.4518 0.3724 0.0603  -0.0078 -0.0133 22  SER B CB    
2290 O  OG    . SER B 29  ? 0.3765 0.4296 0.3606 0.0511  -0.0051 -0.0159 22  SER B OG    
2291 N  N     . VAL B 30  ? 0.3658 0.3968 0.3497 0.0554  0.0053  -0.0032 23  VAL B N     
2292 C  CA    . VAL B 30  ? 0.3633 0.3793 0.3436 0.0533  0.0095  0.0013  23  VAL B CA    
2293 C  C     . VAL B 30  ? 0.3464 0.3594 0.3311 0.0448  0.0112  -0.0008 23  VAL B C     
2294 O  O     . VAL B 30  ? 0.3388 0.3564 0.3287 0.0407  0.0104  -0.0047 23  VAL B O     
2295 C  CB    . VAL B 30  ? 0.3715 0.3808 0.3523 0.0571  0.0106  0.0025  23  VAL B CB    
2296 C  CG1   . VAL B 30  ? 0.3725 0.3656 0.3505 0.0530  0.0138  0.0057  23  VAL B CG1   
2297 C  CG2   . VAL B 30  ? 0.3945 0.4044 0.3703 0.0679  0.0079  0.0051  23  VAL B CG2   
2298 N  N     . ASN B 31  ? 0.3457 0.3513 0.3279 0.0425  0.0135  0.0022  24  ASN B N     
2299 C  CA    . ASN B 31  ? 0.3348 0.3369 0.3210 0.0365  0.0143  0.0010  24  ASN B CA    
2300 C  C     . ASN B 31  ? 0.3365 0.3295 0.3235 0.0340  0.0157  0.0029  24  ASN B C     
2301 O  O     . ASN B 31  ? 0.3475 0.3341 0.3324 0.0343  0.0177  0.0070  24  ASN B O     
2302 C  CB    . ASN B 31  ? 0.3365 0.3406 0.3223 0.0362  0.0157  0.0018  24  ASN B CB    
2303 C  CG    . ASN B 31  ? 0.3362 0.3459 0.3211 0.0375  0.0130  -0.0031 24  ASN B CG    
2304 O  OD1   . ASN B 31  ? 0.3316 0.3391 0.3195 0.0349  0.0113  -0.0061 24  ASN B OD1   
2305 N  ND2   . ASN B 31  ? 0.3453 0.3605 0.3252 0.0415  0.0116  -0.0042 24  ASN B ND2   
2306 N  N     . TYR B 32  ? 0.3301 0.3214 0.3191 0.0305  0.0145  0.0000  25  TYR B N     
2307 C  CA    . TYR B 32  ? 0.3349 0.3175 0.3232 0.0278  0.0147  0.0001  25  TYR B CA    
2308 C  C     . TYR B 32  ? 0.3299 0.3121 0.3212 0.0231  0.0128  -0.0004 25  TYR B C     
2309 O  O     . TYR B 32  ? 0.3261 0.3090 0.3164 0.0214  0.0108  -0.0023 25  TYR B O     
2310 C  CB    . TYR B 32  ? 0.3389 0.3210 0.3246 0.0293  0.0150  -0.0029 25  TYR B CB    
2311 C  CG    . TYR B 32  ? 0.3493 0.3217 0.3311 0.0276  0.0147  -0.0049 25  TYR B CG    
2312 C  CD1   . TYR B 32  ? 0.3588 0.3212 0.3403 0.0250  0.0135  -0.0038 25  TYR B CD1   
2313 C  CD2   . TYR B 32  ? 0.3540 0.3283 0.3320 0.0278  0.0156  -0.0084 25  TYR B CD2   
2314 C  CE1   . TYR B 32  ? 0.3731 0.3258 0.3500 0.0231  0.0120  -0.0073 25  TYR B CE1   
2315 C  CE2   . TYR B 32  ? 0.3682 0.3337 0.3399 0.0270  0.0150  -0.0116 25  TYR B CE2   
2316 C  CZ    . TYR B 32  ? 0.3778 0.3317 0.3487 0.0248  0.0124  -0.0115 25  TYR B CZ    
2317 O  OH    . TYR B 32  ? 0.3966 0.3404 0.3605 0.0235  0.0104  -0.0160 25  TYR B OH    
2318 N  N     . HIS B 33  ? 0.3348 0.3161 0.3299 0.0210  0.0133  0.0017  26  HIS B N     
2319 C  CA    . HIS B 33  ? 0.3343 0.3184 0.3349 0.0176  0.0107  0.0007  26  HIS B CA    
2320 C  C     . HIS B 33  ? 0.3431 0.3195 0.3418 0.0139  0.0078  -0.0011 26  HIS B C     
2321 O  O     . HIS B 33  ? 0.3549 0.3277 0.3567 0.0101  0.0078  -0.0006 26  HIS B O     
2322 C  CB    . HIS B 33  ? 0.3392 0.3308 0.3472 0.0165  0.0135  0.0034  26  HIS B CB    
2323 C  CG    . HIS B 33  ? 0.3352 0.3346 0.3427 0.0211  0.0159  0.0038  26  HIS B CG    
2324 N  ND1   . HIS B 33  ? 0.3342 0.3425 0.3472 0.0234  0.0151  0.0016  26  HIS B ND1   
2325 C  CD2   . HIS B 33  ? 0.3354 0.3349 0.3365 0.0250  0.0181  0.0049  26  HIS B CD2   
2326 C  CE1   . HIS B 33  ? 0.3352 0.3474 0.3441 0.0280  0.0174  0.0009  26  HIS B CE1   
2327 N  NE2   . HIS B 33  ? 0.3357 0.3433 0.3374 0.0286  0.0189  0.0031  26  HIS B NE2   
2328 N  N     . PHE B 34  ? 0.3422 0.3153 0.3343 0.0146  0.0057  -0.0036 27  PHE B N     
2329 C  CA    . PHE B 34  ? 0.3554 0.3202 0.3411 0.0128  0.0039  -0.0065 27  PHE B CA    
2330 C  C     . PHE B 34  ? 0.3659 0.3299 0.3535 0.0087  -0.0017 -0.0084 27  PHE B C     
2331 O  O     . PHE B 34  ? 0.3823 0.3386 0.3644 0.0066  -0.0043 -0.0119 27  PHE B O     
2332 C  CB    . PHE B 34  ? 0.3560 0.3200 0.3328 0.0148  0.0052  -0.0081 27  PHE B CB    
2333 C  CG    . PHE B 34  ? 0.3554 0.3211 0.3283 0.0134  0.0025  -0.0072 27  PHE B CG    
2334 C  CD1   . PHE B 34  ? 0.3694 0.3306 0.3353 0.0116  -0.0020 -0.0085 27  PHE B CD1   
2335 C  CD2   . PHE B 34  ? 0.3464 0.3162 0.3213 0.0140  0.0037  -0.0051 27  PHE B CD2   
2336 C  CE1   . PHE B 34  ? 0.3761 0.3355 0.3353 0.0111  -0.0049 -0.0064 27  PHE B CE1   
2337 C  CE2   . PHE B 34  ? 0.3535 0.3200 0.3228 0.0125  0.0009  -0.0035 27  PHE B CE2   
2338 C  CZ    . PHE B 34  ? 0.3688 0.3296 0.3298 0.0114  -0.0031 -0.0034 27  PHE B CZ    
2339 N  N     A SER B 35  ? 0.3604 0.3331 0.3559 0.0085  -0.0045 -0.0071 28  SER B N     
2340 N  N     B SER B 35  ? 0.3604 0.3330 0.3554 0.0086  -0.0045 -0.0071 28  SER B N     
2341 C  CA    A SER B 35  ? 0.3716 0.3485 0.3722 0.0060  -0.0111 -0.0090 28  SER B CA    
2342 C  CA    B SER B 35  ? 0.3717 0.3488 0.3732 0.0056  -0.0107 -0.0090 28  SER B CA    
2343 C  C     A SER B 35  ? 0.3663 0.3569 0.3814 0.0068  -0.0109 -0.0074 28  SER B C     
2344 C  C     B SER B 35  ? 0.3660 0.3568 0.3820 0.0064  -0.0101 -0.0072 28  SER B C     
2345 O  O     A SER B 35  ? 0.3548 0.3487 0.3705 0.0112  -0.0074 -0.0055 28  SER B O     
2346 O  O     B SER B 35  ? 0.3544 0.3488 0.3716 0.0103  -0.0058 -0.0051 28  SER B O     
2347 C  CB    A SER B 35  ? 0.3793 0.3525 0.3693 0.0082  -0.0165 -0.0100 28  SER B CB    
2348 C  CB    B SER B 35  ? 0.3812 0.3557 0.3738 0.0072  -0.0172 -0.0105 28  SER B CB    
2349 O  OG    A SER B 35  ? 0.3707 0.3450 0.3589 0.0124  -0.0156 -0.0071 28  SER B OG    
2350 O  OG    B SER B 35  ? 0.3923 0.3754 0.3939 0.0062  -0.0245 -0.0122 28  SER B OG    
2351 N  N     . ARG B 36  ? 0.3781 0.3780 0.4051 0.0027  -0.0146 -0.0090 29  ARG B N     
2352 C  CA    . ARG B 36  ? 0.3779 0.3955 0.4210 0.0039  -0.0138 -0.0083 29  ARG B CA    
2353 C  C     . ARG B 36  ? 0.3859 0.4124 0.4334 0.0090  -0.0225 -0.0107 29  ARG B C     
2354 O  O     . ARG B 36  ? 0.3880 0.4308 0.4491 0.0129  -0.0222 -0.0111 29  ARG B O     
2355 C  CB    . ARG B 36  ? 0.3907 0.4163 0.4473 -0.0051 -0.0112 -0.0079 29  ARG B CB    
2356 C  CG    . ARG B 36  ? 0.3884 0.4073 0.4420 -0.0080 -0.0017 -0.0034 29  ARG B CG    
2357 C  CD    . ARG B 36  ? 0.4085 0.4329 0.4742 -0.0185 0.0018  -0.0012 29  ARG B CD    
2358 N  NE    . ARG B 36  ? 0.4122 0.4274 0.4714 -0.0200 0.0105  0.0048  29  ARG B NE    
2359 C  CZ    . ARG B 36  ? 0.4129 0.4399 0.4767 -0.0190 0.0184  0.0094  29  ARG B CZ    
2360 N  NH1   . ARG B 36  ? 0.4069 0.4559 0.4820 -0.0147 0.0193  0.0077  29  ARG B NH1   
2361 N  NH2   . ARG B 36  ? 0.4234 0.4397 0.4784 -0.0206 0.0253  0.0157  29  ARG B NH2   
2362 N  N     . LYS B 37  ? 0.3946 0.4109 0.4297 0.0106  -0.0299 -0.0122 30  LYS B N     
2363 C  CA    . LYS B 37  ? 0.4092 0.4319 0.4462 0.0167  -0.0396 -0.0135 30  LYS B CA    
2364 C  C     . LYS B 37  ? 0.4043 0.4253 0.4391 0.0262  -0.0384 -0.0113 30  LYS B C     
2365 O  O     . LYS B 37  ? 0.3932 0.4015 0.4168 0.0270  -0.0329 -0.0090 30  LYS B O     
2366 C  CB    . LYS B 37  ? 0.4259 0.4359 0.4458 0.0159  -0.0474 -0.0146 30  LYS B CB    
2367 C  CG    . LYS B 37  ? 0.4491 0.4653 0.4693 0.0222  -0.0595 -0.0157 30  LYS B CG    
2368 C  CD    . LYS B 37  ? 0.4730 0.4808 0.4774 0.0203  -0.0684 -0.0177 30  LYS B CD    
2369 C  CE    . LYS B 37  ? 0.4774 0.4638 0.4553 0.0220  -0.0658 -0.0137 30  LYS B CE    
2370 N  NZ    . LYS B 37  ? 0.5021 0.4809 0.4624 0.0191  -0.0718 -0.0166 30  LYS B NZ    
2371 N  N     . CYS B 38  ? 0.4166 0.4506 0.4627 0.0340  -0.0439 -0.0128 31  CYS B N     
2372 C  CA    . CYS B 38  ? 0.4214 0.4475 0.4614 0.0441  -0.0449 -0.0116 31  CYS B CA    
2373 C  C     . CYS B 38  ? 0.4483 0.4790 0.4914 0.0545  -0.0563 -0.0128 31  CYS B C     
2374 O  O     . CYS B 38  ? 0.4581 0.5095 0.5177 0.0551  -0.0614 -0.0159 31  CYS B O     
2375 C  CB    . CYS B 38  ? 0.4106 0.4489 0.4632 0.0471  -0.0365 -0.0132 31  CYS B CB    
2376 S  SG    . CYS B 38  ? 0.4204 0.4430 0.4622 0.0586  -0.0373 -0.0134 31  CYS B SG    
2377 N  N     . ASN B 39  ? 0.4626 0.4748 0.4916 0.0627  -0.0598 -0.0104 32  ASN B N     
2378 C  CA    . ASN B 39  ? 0.4954 0.5040 0.5214 0.0747  -0.0716 -0.0101 32  ASN B CA    
2379 C  C     . ASN B 39  ? 0.5060 0.5265 0.5471 0.0876  -0.0718 -0.0142 32  ASN B C     
2380 O  O     . ASN B 39  ? 0.5377 0.5541 0.5770 0.1006  -0.0819 -0.0144 32  ASN B O     
2381 C  CB    . ASN B 39  ? 0.5154 0.4922 0.5140 0.0755  -0.0756 -0.0039 32  ASN B CB    
2382 C  CG    . ASN B 39  ? 0.5103 0.4668 0.4984 0.0746  -0.0682 -0.0019 32  ASN B CG    
2383 O  OD1   . ASN B 39  ? 0.4822 0.4436 0.4756 0.0678  -0.0582 -0.0038 32  ASN B OD1   
2384 N  ND2   . ASN B 39  ? 0.5424 0.4742 0.5142 0.0808  -0.0739 0.0020  32  ASN B ND2   
2385 N  N     . LYS B 40  ? 0.4850 0.5202 0.5397 0.0856  -0.0612 -0.0176 33  LYS B N     
2386 C  CA    . LYS B 40  ? 0.4970 0.5429 0.5631 0.0983  -0.0591 -0.0226 33  LYS B CA    
2387 C  C     . LYS B 40  ? 0.4865 0.5687 0.5786 0.0963  -0.0520 -0.0269 33  LYS B C     
2388 O  O     . LYS B 40  ? 0.4724 0.5683 0.5733 0.0842  -0.0499 -0.0255 33  LYS B O     
2389 C  CB    . LYS B 40  ? 0.4906 0.5150 0.5425 0.0984  -0.0521 -0.0226 33  LYS B CB    
2390 C  CG    . LYS B 40  ? 0.5092 0.4978 0.5372 0.0999  -0.0580 -0.0185 33  LYS B CG    
2391 C  CD    . LYS B 40  ? 0.5503 0.5276 0.5733 0.1138  -0.0707 -0.0179 33  LYS B CD    
2392 C  CE    . LYS B 40  ? 0.5758 0.5139 0.5731 0.1134  -0.0754 -0.0123 33  LYS B CE    
2393 N  NZ    . LYS B 40  ? 0.5952 0.5159 0.5875 0.1212  -0.0738 -0.0165 33  LYS B NZ    
2394 N  N     . GLU B 41  ? 0.4992 0.5966 0.6031 0.1080  -0.0481 -0.0322 34  GLU B N     
2395 C  CA    . GLU B 41  ? 0.4988 0.6347 0.6289 0.1074  -0.0410 -0.0361 34  GLU B CA    
2396 C  C     . GLU B 41  ? 0.4978 0.6415 0.6295 0.1121  -0.0286 -0.0398 34  GLU B C     
2397 O  O     . GLU B 41  ? 0.5145 0.6883 0.6656 0.1207  -0.0243 -0.0451 34  GLU B O     
2398 C  CB    . GLU B 41  ? 0.5290 0.6883 0.6782 0.1207  -0.0513 -0.0406 34  GLU B CB    
2399 C  CG    . GLU B 41  ? 0.5370 0.6907 0.6833 0.1174  -0.0652 -0.0376 34  GLU B CG    
2400 C  CD    . GLU B 41  ? 0.5310 0.7148 0.6990 0.1042  -0.0654 -0.0381 34  GLU B CD    
2401 O  OE1   . GLU B 41  ? 0.5545 0.7682 0.7450 0.1113  -0.0730 -0.0425 34  GLU B OE1   
2402 O  OE2   . GLU B 41  ? 0.5072 0.6841 0.6698 0.0869  -0.0588 -0.0345 34  GLU B OE2   
2403 N  N     . CYS B 42  ? 0.4814 0.6011 0.5933 0.1067  -0.0225 -0.0376 35  CYS B N     
2404 C  CA    . CYS B 42  ? 0.4850 0.6098 0.5944 0.1117  -0.0120 -0.0416 35  CYS B CA    
2405 C  C     . CYS B 42  ? 0.4845 0.6460 0.6139 0.1070  -0.0006 -0.0420 35  CYS B C     
2406 O  O     . CYS B 42  ? 0.4673 0.6359 0.6015 0.0918  0.0038  -0.0362 35  CYS B O     
2407 C  CB    . CYS B 42  ? 0.4660 0.5641 0.5535 0.1032  -0.0081 -0.0384 35  CYS B CB    
2408 S  SG    . CYS B 42  ? 0.4696 0.5266 0.5351 0.1041  -0.0197 -0.0364 35  CYS B SG    
2409 N  N     . LEU B 43  ? 0.5089 0.6932 0.6495 0.1202  0.0045  -0.0489 36  LEU B N     
2410 C  CA    . LEU B 43  ? 0.5169 0.7413 0.6796 0.1162  0.0159  -0.0492 36  LEU B CA    
2411 C  C     . LEU B 43  ? 0.5032 0.7273 0.6564 0.1027  0.0293  -0.0434 36  LEU B C     
2412 O  O     . LEU B 43  ? 0.5061 0.7561 0.6745 0.0919  0.0384  -0.0394 36  LEU B O     
2413 C  CB    . LEU B 43  ? 0.5506 0.7993 0.7251 0.1355  0.0193  -0.0588 36  LEU B CB    
2414 C  CG    . LEU B 43  ? 0.5731 0.8312 0.7629 0.1508  0.0065  -0.0644 36  LEU B CG    
2415 C  CD1   . LEU B 43  ? 0.6096 0.8787 0.8022 0.1738  0.0089  -0.0752 36  LEU B CD1   
2416 C  CD2   . LEU B 43  ? 0.5750 0.8710 0.7951 0.1426  0.0057  -0.0624 36  LEU B CD2   
2417 N  N     . PHE B 44  ? 0.4917 0.6859 0.6197 0.1023  0.0298  -0.0424 37  PHE B N     
2418 C  CA    . PHE B 44  ? 0.4847 0.6775 0.6010 0.0926  0.0411  -0.0372 37  PHE B CA    
2419 C  C     . PHE B 44  ? 0.4572 0.6279 0.5636 0.0768  0.0382  -0.0284 37  PHE B C     
2420 O  O     . PHE B 44  ? 0.4533 0.6197 0.5488 0.0691  0.0460  -0.0231 37  PHE B O     
2421 C  CB    . PHE B 44  ? 0.4968 0.6756 0.5928 0.1039  0.0433  -0.0433 37  PHE B CB    
2422 C  CG    . PHE B 44  ? 0.4916 0.6372 0.5721 0.1102  0.0313  -0.0474 37  PHE B CG    
2423 C  CD1   . PHE B 44  ? 0.4660 0.5862 0.5362 0.0995  0.0245  -0.0414 37  PHE B CD1   
2424 C  CD2   . PHE B 44  ? 0.5172 0.6564 0.5942 0.1268  0.0264  -0.0572 37  PHE B CD2   
2425 C  CE1   . PHE B 44  ? 0.4659 0.5571 0.5228 0.1032  0.0146  -0.0442 37  PHE B CE1   
2426 C  CE2   . PHE B 44  ? 0.5191 0.6247 0.5812 0.1304  0.0155  -0.0599 37  PHE B CE2   
2427 C  CZ    . PHE B 44  ? 0.4934 0.5761 0.5459 0.1178  0.0101  -0.0529 37  PHE B CZ    
2428 N  N     . CYS B 45  ? 0.4434 0.6010 0.5526 0.0731  0.0272  -0.0271 38  CYS B N     
2429 C  CA    . CYS B 45  ? 0.4208 0.5540 0.5173 0.0618  0.0234  -0.0211 38  CYS B CA    
2430 C  C     . CYS B 45  ? 0.4178 0.5564 0.5146 0.0487  0.0328  -0.0139 38  CYS B C     
2431 O  O     . CYS B 45  ? 0.4281 0.5871 0.5420 0.0414  0.0368  -0.0117 38  CYS B O     
2432 C  CB    . CYS B 45  ? 0.4147 0.5416 0.5173 0.0585  0.0124  -0.0206 38  CYS B CB    
2433 S  SG    . CYS B 45  ? 0.3922 0.4896 0.4775 0.0471  0.0085  -0.0150 38  CYS B SG    
2434 N  N     . PHE B 46  ? 0.4080 0.5277 0.4863 0.0453  0.0356  -0.0101 39  PHE B N     
2435 C  CA    . PHE B 46  ? 0.4111 0.5300 0.4860 0.0344  0.0434  -0.0022 39  PHE B CA    
2436 C  C     . PHE B 46  ? 0.3972 0.4960 0.4670 0.0250  0.0380  0.0019  39  PHE B C     
2437 O  O     . PHE B 46  ? 0.4032 0.4949 0.4671 0.0172  0.0431  0.0085  39  PHE B O     
2438 C  CB    . PHE B 46  ? 0.4185 0.5326 0.4759 0.0380  0.0505  -0.0001 39  PHE B CB    
2439 C  CG    . PHE B 46  ? 0.4059 0.4997 0.4455 0.0442  0.0446  -0.0032 39  PHE B CG    
2440 C  CD1   . PHE B 46  ? 0.3870 0.4633 0.4238 0.0438  0.0351  -0.0053 39  PHE B CD1   
2441 C  CD2   . PHE B 46  ? 0.4178 0.5112 0.4427 0.0498  0.0491  -0.0040 39  PHE B CD2   
2442 C  CE1   . PHE B 46  ? 0.3798 0.4406 0.4025 0.0474  0.0308  -0.0079 39  PHE B CE1   
2443 C  CE2   . PHE B 46  ? 0.4104 0.4879 0.4210 0.0543  0.0432  -0.0077 39  PHE B CE2   
2444 C  CZ    . PHE B 46  ? 0.3909 0.4529 0.4019 0.0523  0.0343  -0.0095 39  PHE B CZ    
2445 N  N     . HIS B 47  ? 0.3850 0.4749 0.4567 0.0261  0.0282  -0.0015 40  HIS B N     
2446 C  CA    . HIS B 47  ? 0.3766 0.4497 0.4437 0.0182  0.0234  0.0008  40  HIS B CA    
2447 C  C     . HIS B 47  ? 0.3787 0.4570 0.4574 0.0164  0.0150  -0.0025 40  HIS B C     
2448 O  O     . HIS B 47  ? 0.3714 0.4390 0.4435 0.0209  0.0071  -0.0053 40  HIS B O     
2449 C  CB    . HIS B 47  ? 0.3627 0.4153 0.4116 0.0215  0.0215  0.0012  40  HIS B CB    
2450 C  CG    . HIS B 47  ? 0.3607 0.3984 0.4035 0.0144  0.0205  0.0045  40  HIS B CG    
2451 N  ND1   . HIS B 47  ? 0.3696 0.4016 0.4068 0.0105  0.0264  0.0099  40  HIS B ND1   
2452 C  CD2   . HIS B 47  ? 0.3578 0.3858 0.3995 0.0108  0.0146  0.0030  40  HIS B CD2   
2453 C  CE1   . HIS B 47  ? 0.3713 0.3885 0.4042 0.0058  0.0235  0.0107  40  HIS B CE1   
2454 N  NE2   . HIS B 47  ? 0.3636 0.3792 0.3991 0.0058  0.0167  0.0061  40  HIS B NE2   
2455 N  N     . THR B 48  ? 0.3934 0.4881 0.4886 0.0087  0.0166  -0.0017 41  THR B N     
2456 C  CA    . THR B 48  ? 0.4023 0.5115 0.5133 0.0083  0.0086  -0.0060 41  THR B CA    
2457 C  C     . THR B 48  ? 0.4039 0.4993 0.5114 0.0005  0.0001  -0.0069 41  THR B C     
2458 O  O     . THR B 48  ? 0.4021 0.4790 0.4984 -0.0062 0.0022  -0.0041 41  THR B O     
2459 C  CB    . THR B 48  ? 0.4218 0.5614 0.5559 0.0035  0.0146  -0.0059 41  THR B CB    
2460 O  OG1   . THR B 48  ? 0.4344 0.5720 0.5720 -0.0114 0.0205  -0.0008 41  THR B OG1   
2461 C  CG2   . THR B 48  ? 0.4256 0.5811 0.5621 0.0129  0.0235  -0.0063 41  THR B CG2   
2462 N  N     . ALA B 49  ? 0.4128 0.5183 0.5297 0.0027  -0.0098 -0.0114 42  ALA B N     
2463 C  CA    . ALA B 49  ? 0.4191 0.5127 0.5300 -0.0019 -0.0198 -0.0139 42  ALA B CA    
2464 C  C     . ALA B 49  ? 0.4387 0.5403 0.5634 -0.0162 -0.0209 -0.0150 42  ALA B C     
2465 O  O     . ALA B 49  ? 0.4558 0.5713 0.5931 -0.0188 -0.0303 -0.0196 42  ALA B O     
2466 C  CB    . ALA B 49  ? 0.4257 0.5251 0.5375 0.0077  -0.0311 -0.0177 42  ALA B CB    
2467 N  N     . THR B 50  ? 0.4406 0.5299 0.5606 -0.0253 -0.0124 -0.0109 43  THR B N     
2468 C  CA    . THR B 50  ? 0.4653 0.5568 0.5967 -0.0408 -0.0116 -0.0107 43  THR B CA    
2469 C  C     . THR B 50  ? 0.4764 0.5435 0.5942 -0.0464 -0.0195 -0.0145 43  THR B C     
2470 O  O     . THR B 50  ? 0.5033 0.5692 0.6297 -0.0597 -0.0220 -0.0164 43  THR B O     
2471 C  CB    . THR B 50  ? 0.4714 0.5596 0.6029 -0.0475 0.0016  -0.0032 43  THR B CB    
2472 O  OG1   . THR B 50  ? 0.4551 0.5181 0.5636 -0.0410 0.0060  0.0005  43  THR B OG1   
2473 C  CG2   . THR B 50  ? 0.4718 0.5890 0.6192 -0.0446 0.0103  -0.0004 43  THR B CG2   
2474 N  N     . THR B 51  ? 0.4604 0.5069 0.5562 -0.0373 -0.0225 -0.0156 44  THR B N     
2475 C  CA    . THR B 51  ? 0.4741 0.4997 0.5551 -0.0402 -0.0298 -0.0205 44  THR B CA    
2476 C  C     . THR B 51  ? 0.4604 0.4804 0.5253 -0.0287 -0.0357 -0.0228 44  THR B C     
2477 O  O     . THR B 51  ? 0.4406 0.4682 0.5052 -0.0195 -0.0333 -0.0197 44  THR B O     
2478 C  CB    . THR B 51  ? 0.4804 0.4793 0.5467 -0.0436 -0.0238 -0.0184 44  THR B CB    
2479 O  OG1   . THR B 51  ? 0.4555 0.4441 0.5056 -0.0324 -0.0187 -0.0154 44  THR B OG1   
2480 C  CG2   . THR B 51  ? 0.4961 0.4949 0.5731 -0.0539 -0.0157 -0.0129 44  THR B CG2   
2481 N  N     . SER B 52  ? 0.4771 0.4835 0.5284 -0.0298 -0.0434 -0.0283 45  SER B N     
2482 C  CA    . SER B 52  ? 0.4712 0.4681 0.5024 -0.0205 -0.0470 -0.0293 45  SER B CA    
2483 C  C     . SER B 52  ? 0.4743 0.4480 0.4851 -0.0197 -0.0427 -0.0307 45  SER B C     
2484 O  O     . SER B 52  ? 0.4776 0.4431 0.4704 -0.0141 -0.0449 -0.0323 45  SER B O     
2485 C  CB    . SER B 52  ? 0.4933 0.4981 0.5235 -0.0198 -0.0601 -0.0344 45  SER B CB    
2486 O  OG    . SER B 52  ? 0.5227 0.5188 0.5488 -0.0280 -0.0664 -0.0417 45  SER B OG    
2487 N  N     . HIS B 53  ? 0.4776 0.4409 0.4907 -0.0246 -0.0361 -0.0298 46  HIS B N     
2488 C  CA    . HIS B 53  ? 0.4845 0.4270 0.4802 -0.0217 -0.0321 -0.0318 46  HIS B CA    
2489 C  C     . HIS B 53  ? 0.4584 0.4007 0.4445 -0.0122 -0.0251 -0.0273 46  HIS B C     
2490 O  O     . HIS B 53  ? 0.4354 0.3867 0.4300 -0.0099 -0.0197 -0.0213 46  HIS B O     
2491 C  CB    . HIS B 53  ? 0.4980 0.4275 0.4980 -0.0274 -0.0270 -0.0303 46  HIS B CB    
2492 C  CG    . HIS B 53  ? 0.5081 0.4171 0.4912 -0.0215 -0.0233 -0.0328 46  HIS B CG    
2493 N  ND1   . HIS B 53  ? 0.5386 0.4312 0.5077 -0.0211 -0.0280 -0.0415 46  HIS B ND1   
2494 C  CD2   . HIS B 53  ? 0.4937 0.3980 0.4719 -0.0142 -0.0156 -0.0282 46  HIS B CD2   
2495 C  CE1   . HIS B 53  ? 0.5421 0.4215 0.4994 -0.0130 -0.0224 -0.0421 46  HIS B CE1   
2496 N  NE2   . HIS B 53  ? 0.5145 0.4016 0.4780 -0.0089 -0.0152 -0.0339 46  HIS B NE2   
2497 N  N     . VAL B 54  ? 0.4665 0.3991 0.4351 -0.0072 -0.0249 -0.0309 47  VAL B N     
2498 C  CA    . VAL B 54  ? 0.4489 0.3814 0.4097 -0.0001 -0.0175 -0.0277 47  VAL B CA    
2499 C  C     . VAL B 54  ? 0.4692 0.3878 0.4166 0.0034  -0.0146 -0.0332 47  VAL B C     
2500 O  O     . VAL B 54  ? 0.4965 0.4068 0.4330 0.0024  -0.0194 -0.0401 47  VAL B O     
2501 C  CB    . VAL B 54  ? 0.4399 0.3801 0.3936 0.0031  -0.0187 -0.0253 47  VAL B CB    
2502 C  CG1   . VAL B 54  ? 0.4254 0.3670 0.3740 0.0078  -0.0107 -0.0221 47  VAL B CG1   
2503 C  CG2   . VAL B 54  ? 0.4278 0.3795 0.3936 0.0018  -0.0230 -0.0213 47  VAL B CG2   
2504 N  N     . GLU B 55  ? 0.4594 0.3765 0.4071 0.0086  -0.0074 -0.0308 48  GLU B N     
2505 C  CA    . GLU B 55  ? 0.4807 0.3871 0.4171 0.0147  -0.0043 -0.0364 48  GLU B CA    
2506 C  C     . GLU B 55  ? 0.4906 0.4014 0.4127 0.0180  -0.0034 -0.0405 48  GLU B C     
2507 O  O     . GLU B 55  ? 0.4753 0.3978 0.3963 0.0172  -0.0022 -0.0363 48  GLU B O     
2508 C  CB    . GLU B 55  ? 0.4696 0.3776 0.4106 0.0214  0.0023  -0.0327 48  GLU B CB    
2509 C  CG    . GLU B 55  ? 0.4748 0.3725 0.4234 0.0197  0.0021  -0.0289 48  GLU B CG    
2510 C  CD    . GLU B 55  ? 0.5135 0.3884 0.4556 0.0191  -0.0007 -0.0344 48  GLU B CD    
2511 O  OE1   . GLU B 55  ? 0.5373 0.4023 0.4685 0.0272  0.0003  -0.0411 48  GLU B OE1   
2512 O  OE2   . GLU B 55  ? 0.5240 0.3909 0.4720 0.0104  -0.0039 -0.0324 48  GLU B OE2   
2513 N  N     . LYS B 56  ? 0.5224 0.4223 0.4315 0.0222  -0.0033 -0.0489 49  LYS B N     
2514 C  CA    . LYS B 56  ? 0.5370 0.4426 0.4311 0.0272  0.0008  -0.0528 49  LYS B CA    
2515 C  C     . LYS B 56  ? 0.5181 0.4382 0.4178 0.0324  0.0100  -0.0484 49  LYS B C     
2516 O  O     . LYS B 56  ? 0.5091 0.4289 0.4189 0.0368  0.0127  -0.0470 49  LYS B O     
2517 C  CB    . LYS B 56  ? 0.5789 0.4698 0.4587 0.0328  0.0002  -0.0641 49  LYS B CB    
2518 C  CG    . LYS B 56  ? 0.6077 0.4846 0.4788 0.0271  -0.0097 -0.0710 49  LYS B CG    
2519 C  CD    . LYS B 56  ? 0.6541 0.5123 0.5109 0.0331  -0.0109 -0.0835 49  LYS B CD    
2520 C  CE    . LYS B 56  ? 0.6864 0.5290 0.5369 0.0257  -0.0223 -0.0914 49  LYS B CE    
2521 N  NZ    . LYS B 56  ? 0.6900 0.5433 0.5303 0.0213  -0.0281 -0.0915 49  LYS B NZ    
2522 N  N     . PRO B 57  ? 0.5157 0.4490 0.4089 0.0315  0.0146  -0.0457 50  PRO B N     
2523 C  CA    . PRO B 57  ? 0.5044 0.4541 0.4039 0.0347  0.0234  -0.0427 50  PRO B CA    
2524 C  C     . PRO B 57  ? 0.5174 0.4688 0.4205 0.0449  0.0283  -0.0487 50  PRO B C     
2525 O  O     . PRO B 57  ? 0.4998 0.4613 0.4164 0.0478  0.0313  -0.0454 50  PRO B O     
2526 C  CB    . PRO B 57  ? 0.5220 0.4803 0.4071 0.0320  0.0281  -0.0418 50  PRO B CB    
2527 C  CG    . PRO B 57  ? 0.5270 0.4742 0.4023 0.0259  0.0193  -0.0396 50  PRO B CG    
2528 C  CD    . PRO B 57  ? 0.5316 0.4642 0.4097 0.0271  0.0112  -0.0454 50  PRO B CD    
2529 N  N     . GLU B 58  ? 0.5522 0.4928 0.4427 0.0514  0.0283  -0.0581 51  GLU B N     
2530 C  CA    . GLU B 58  ? 0.5704 0.5134 0.4636 0.0636  0.0332  -0.0643 51  GLU B CA    
2531 C  C     . GLU B 58  ? 0.5619 0.4917 0.4664 0.0671  0.0286  -0.0621 51  GLU B C     
2532 O  O     . GLU B 58  ? 0.5618 0.4998 0.4753 0.0762  0.0320  -0.0620 51  GLU B O     
2533 C  CB    . GLU B 58  ? 0.6162 0.5498 0.4911 0.0712  0.0347  -0.0761 51  GLU B CB    
2534 C  CG    . GLU B 58  ? 0.6308 0.5819 0.4934 0.0698  0.0423  -0.0775 51  GLU B CG    
2535 C  CD    . GLU B 58  ? 0.6192 0.5995 0.4934 0.0714  0.0529  -0.0733 51  GLU B CD    
2536 O  OE1   . GLU B 58  ? 0.6330 0.6236 0.5148 0.0833  0.0582  -0.0790 51  GLU B OE1   
2537 O  OE2   . GLU B 58  ? 0.5998 0.5926 0.4761 0.0606  0.0553  -0.0643 51  GLU B OE2   
2538 N  N     . ASN B 59  ? 0.5560 0.4679 0.4607 0.0593  0.0210  -0.0593 52  ASN B N     
2539 C  CA    . ASN B 59  ? 0.5517 0.4502 0.4653 0.0601  0.0174  -0.0551 52  ASN B CA    
2540 C  C     . ASN B 59  ? 0.5135 0.4286 0.4418 0.0575  0.0192  -0.0452 52  ASN B C     
2541 O  O     . ASN B 59  ? 0.5136 0.4290 0.4482 0.0645  0.0202  -0.0425 52  ASN B O     
2542 C  CB    . ASN B 59  ? 0.5646 0.4416 0.4745 0.0511  0.0099  -0.0560 52  ASN B CB    
2543 C  CG    . ASN B 59  ? 0.6124 0.4681 0.5077 0.0560  0.0072  -0.0675 52  ASN B CG    
2544 O  OD1   . ASN B 59  ? 0.6364 0.4913 0.5249 0.0682  0.0113  -0.0742 52  ASN B OD1   
2545 N  ND2   . ASN B 59  ? 0.6308 0.4695 0.5218 0.0470  0.0000  -0.0707 52  ASN B ND2   
2546 N  N     . ALA B 60  ? 0.4857 0.4139 0.4178 0.0485  0.0192  -0.0402 53  ALA B N     
2547 C  CA    . ALA B 60  ? 0.4545 0.3976 0.3987 0.0463  0.0207  -0.0327 53  ALA B CA    
2548 C  C     . ALA B 60  ? 0.4540 0.4151 0.4038 0.0543  0.0261  -0.0337 53  ALA B C     
2549 O  O     . ALA B 60  ? 0.4436 0.4112 0.4023 0.0578  0.0259  -0.0301 53  ALA B O     
2550 C  CB    . ALA B 60  ? 0.4338 0.3841 0.3790 0.0367  0.0191  -0.0286 53  ALA B CB    
2551 N  N     . LYS B 61  ? 0.4696 0.4408 0.4142 0.0573  0.0311  -0.0391 54  LYS B N     
2552 C  CA    . LYS B 61  ? 0.4758 0.4677 0.4281 0.0653  0.0367  -0.0416 54  LYS B CA    
2553 C  C     . LYS B 61  ? 0.4933 0.4790 0.4490 0.0788  0.0350  -0.0444 54  LYS B C     
2554 O  O     . LYS B 61  ? 0.4876 0.4891 0.4547 0.0844  0.0356  -0.0427 54  LYS B O     
2555 C  CB    . LYS B 61  ? 0.4972 0.5009 0.4418 0.0662  0.0436  -0.0473 54  LYS B CB    
2556 C  CG    . LYS B 61  ? 0.4862 0.5007 0.4282 0.0539  0.0468  -0.0426 54  LYS B CG    
2557 C  CD    . LYS B 61  ? 0.5155 0.5401 0.4465 0.0552  0.0547  -0.0475 54  LYS B CD    
2558 C  CE    . LYS B 61  ? 0.5163 0.5422 0.4371 0.0428  0.0567  -0.0419 54  LYS B CE    
2559 N  NZ    . LYS B 61  ? 0.5497 0.5908 0.4608 0.0446  0.0668  -0.0460 54  LYS B NZ    
2560 N  N     . ARG B 62  ? 0.5197 0.4811 0.4651 0.0840  0.0320  -0.0486 55  ARG B N     
2561 C  CA    . ARG B 62  ? 0.5432 0.4923 0.4893 0.0973  0.0295  -0.0500 55  ARG B CA    
2562 C  C     . ARG B 62  ? 0.5232 0.4700 0.4769 0.0948  0.0253  -0.0403 55  ARG B C     
2563 O  O     . ARG B 62  ? 0.5301 0.4860 0.4902 0.1051  0.0247  -0.0390 55  ARG B O     
2564 C  CB    . ARG B 62  ? 0.5789 0.4959 0.5111 0.1012  0.0260  -0.0556 55  ARG B CB    
2565 C  CG    . ARG B 62  ? 0.6134 0.5303 0.5354 0.1095  0.0297  -0.0674 55  ARG B CG    
2566 C  CD    . ARG B 62  ? 0.6535 0.5359 0.5601 0.1108  0.0249  -0.0744 55  ARG B CD    
2567 N  NE    . ARG B 62  ? 0.6772 0.5311 0.5833 0.1108  0.0186  -0.0691 55  ARG B NE    
2568 C  CZ    . ARG B 62  ? 0.6947 0.5252 0.5961 0.0983  0.0132  -0.0664 55  ARG B CZ    
2569 N  NH1   . ARG B 62  ? 0.6956 0.5300 0.5940 0.0857  0.0120  -0.0685 55  ARG B NH1   
2570 N  NH2   . ARG B 62  ? 0.7140 0.5181 0.6140 0.0981  0.0089  -0.0613 55  ARG B NH2   
2571 N  N     . GLY B 63  ? 0.5025 0.4395 0.4551 0.0821  0.0226  -0.0344 56  GLY B N     
2572 C  CA    . GLY B 63  ? 0.4865 0.4220 0.4442 0.0790  0.0198  -0.0255 56  GLY B CA    
2573 C  C     . GLY B 63  ? 0.4637 0.4257 0.4320 0.0805  0.0210  -0.0229 56  GLY B C     
2574 O  O     . GLY B 63  ? 0.4689 0.4330 0.4398 0.0874  0.0187  -0.0190 56  GLY B O     
2575 N  N     . LEU B 64  ? 0.4437 0.4250 0.4172 0.0737  0.0240  -0.0250 57  LEU B N     
2576 C  CA    . LEU B 64  ? 0.4258 0.4316 0.4101 0.0721  0.0247  -0.0234 57  LEU B CA    
2577 C  C     . LEU B 64  ? 0.4439 0.4667 0.4355 0.0848  0.0256  -0.0275 57  LEU B C     
2578 O  O     . LEU B 64  ? 0.4394 0.4766 0.4391 0.0878  0.0230  -0.0256 57  LEU B O     
2579 C  CB    . LEU B 64  ? 0.4105 0.4272 0.3963 0.0609  0.0281  -0.0243 57  LEU B CB    
2580 C  CG    . LEU B 64  ? 0.3944 0.3973 0.3748 0.0503  0.0258  -0.0204 57  LEU B CG    
2581 C  CD1   . LEU B 64  ? 0.3911 0.4000 0.3687 0.0417  0.0286  -0.0211 57  LEU B CD1   
2582 C  CD2   . LEU B 64  ? 0.3765 0.3815 0.3621 0.0472  0.0225  -0.0154 57  LEU B CD2   
2583 N  N     . THR B 65  ? 0.4683 0.4900 0.4566 0.0930  0.0289  -0.0338 58  THR B N     
2584 C  CA    . THR B 65  ? 0.4922 0.5295 0.4878 0.1081  0.0295  -0.0387 58  THR B CA    
2585 C  C     . THR B 65  ? 0.5084 0.5317 0.5015 0.1198  0.0228  -0.0347 58  THR B C     
2586 O  O     . THR B 65  ? 0.5158 0.5586 0.5187 0.1291  0.0203  -0.0351 58  THR B O     
2587 C  CB    . THR B 65  ? 0.5210 0.5559 0.5107 0.1162  0.0345  -0.0472 58  THR B CB    
2588 O  OG1   . THR B 65  ? 0.5117 0.5630 0.5024 0.1058  0.0415  -0.0499 58  THR B OG1   
2589 C  CG2   . THR B 65  ? 0.5513 0.6023 0.5493 0.1349  0.0349  -0.0531 58  THR B CG2   
2590 N  N     . LEU B 66  ? 0.5194 0.5096 0.4993 0.1194  0.0198  -0.0307 59  LEU B N     
2591 C  CA    . LEU B 66  ? 0.5412 0.5154 0.5158 0.1293  0.0141  -0.0248 59  LEU B CA    
2592 C  C     . LEU B 66  ? 0.5196 0.5079 0.4995 0.1251  0.0108  -0.0179 59  LEU B C     
2593 O  O     . LEU B 66  ? 0.5372 0.5311 0.5180 0.1366  0.0060  -0.0152 59  LEU B O     
2594 C  CB    . LEU B 66  ? 0.5600 0.4959 0.5199 0.1256  0.0125  -0.0208 59  LEU B CB    
2595 C  CG    . LEU B 66  ? 0.5886 0.5054 0.5404 0.1296  0.0141  -0.0288 59  LEU B CG    
2596 C  CD1   . LEU B 66  ? 0.6073 0.4874 0.5468 0.1218  0.0117  -0.0245 59  LEU B CD1   
2597 C  CD2   . LEU B 66  ? 0.6282 0.5465 0.5800 0.1504  0.0131  -0.0352 59  LEU B CD2   
2598 N  N     . LEU B 67  ? 0.4852 0.4798 0.4677 0.1094  0.0128  -0.0157 60  LEU B N     
2599 C  CA    . LEU B 67  ? 0.4672 0.4736 0.4531 0.1048  0.0099  -0.0107 60  LEU B CA    
2600 C  C     . LEU B 67  ? 0.4640 0.5028 0.4635 0.1093  0.0081  -0.0152 60  LEU B C     
2601 O  O     . LEU B 67  ? 0.4706 0.5185 0.4713 0.1148  0.0029  -0.0128 60  LEU B O     
2602 C  CB    . LEU B 67  ? 0.4364 0.4405 0.4221 0.0886  0.0123  -0.0089 60  LEU B CB    
2603 C  CG    . LEU B 67  ? 0.4380 0.4164 0.4137 0.0821  0.0130  -0.0034 60  LEU B CG    
2604 C  CD1   . LEU B 67  ? 0.4103 0.3920 0.3890 0.0686  0.0152  -0.0043 60  LEU B CD1   
2605 C  CD2   . LEU B 67  ? 0.4503 0.4193 0.4186 0.0848  0.0105  0.0045  60  LEU B CD2   
2606 N  N     . LYS B 68  ? 0.4592 0.5171 0.4690 0.1073  0.0124  -0.0220 61  LYS B N     
2607 C  CA    . LYS B 68  ? 0.4619 0.5536 0.4877 0.1105  0.0113  -0.0268 61  LYS B CA    
2608 C  C     . LYS B 68  ? 0.4933 0.5910 0.5212 0.1297  0.0057  -0.0276 61  LYS B C     
2609 O  O     . LYS B 68  ? 0.4982 0.6169 0.5347 0.1338  0.0000  -0.0280 61  LYS B O     
2610 C  CB    . LYS B 68  ? 0.4601 0.5702 0.4953 0.1054  0.0189  -0.0332 61  LYS B CB    
2611 C  CG    . LYS B 68  ? 0.4715 0.6204 0.5264 0.1093  0.0196  -0.0391 61  LYS B CG    
2612 C  CD    . LYS B 68  ? 0.4554 0.6242 0.5215 0.0963  0.0168  -0.0385 61  LYS B CD    
2613 C  CE    . LYS B 68  ? 0.4722 0.6809 0.5598 0.1008  0.0150  -0.0444 61  LYS B CE    
2614 N  NZ    . LYS B 68  ? 0.4602 0.6865 0.5590 0.0831  0.0146  -0.0452 61  LYS B NZ    
2615 N  N     . GLN B 69  ? 0.5191 0.5983 0.5389 0.1418  0.0068  -0.0287 62  GLN B N     
2616 C  CA    . GLN B 69  ? 0.5567 0.6383 0.5772 0.1625  0.0013  -0.0298 62  GLN B CA    
2617 C  C     . GLN B 69  ? 0.5678 0.6363 0.5780 0.1677  -0.0071 -0.0212 62  GLN B C     
2618 O  O     . GLN B 69  ? 0.5915 0.6758 0.6068 0.1818  -0.0141 -0.0216 62  GLN B O     
2619 C  CB    . GLN B 69  ? 0.5872 0.6439 0.5976 0.1738  0.0040  -0.0329 62  GLN B CB    
2620 C  CG    . GLN B 69  ? 0.6322 0.6944 0.6455 0.1980  -0.0012 -0.0362 62  GLN B CG    
2621 C  CD    . GLN B 69  ? 0.6334 0.7427 0.6700 0.2041  0.0009  -0.0454 62  GLN B CD    
2622 O  OE1   . GLN B 69  ? 0.6349 0.7721 0.6842 0.2087  -0.0049 -0.0452 62  GLN B OE1   
2623 N  NE2   . GLN B 69  ? 0.6349 0.7555 0.6773 0.2030  0.0098  -0.0538 62  GLN B NE2   
2624 N  N     . ALA B 70  ? 0.5536 0.5954 0.5495 0.1562  -0.0063 -0.0134 63  ALA B N     
2625 C  CA    . ALA B 70  ? 0.5673 0.5939 0.5497 0.1591  -0.0121 -0.0040 63  ALA B CA    
2626 C  C     . ALA B 70  ? 0.5483 0.6013 0.5377 0.1533  -0.0162 -0.0042 63  ALA B C     
2627 O  O     . ALA B 70  ? 0.5640 0.6112 0.5424 0.1576  -0.0217 0.0021  63  ALA B O     
2628 C  CB    . ALA B 70  ? 0.5622 0.5552 0.5293 0.1480  -0.0081 0.0032  63  ALA B CB    
2629 N  N     . GLY B 71  ? 0.5197 0.5997 0.5258 0.1429  -0.0134 -0.0116 64  GLY B N     
2630 C  CA    . GLY B 71  ? 0.5093 0.6160 0.5246 0.1379  -0.0183 -0.0144 64  GLY B CA    
2631 C  C     . GLY B 71  ? 0.4760 0.5800 0.4905 0.1191  -0.0146 -0.0143 64  GLY B C     
2632 O  O     . GLY B 71  ? 0.4715 0.5897 0.4888 0.1141  -0.0193 -0.0162 64  GLY B O     
2633 N  N     . MET B 72  ? 0.4564 0.5440 0.4680 0.1093  -0.0071 -0.0134 65  MET B N     
2634 C  CA    . MET B 72  ? 0.4287 0.5154 0.4414 0.0931  -0.0041 -0.0141 65  MET B CA    
2635 C  C     . MET B 72  ? 0.4204 0.5348 0.4499 0.0849  -0.0045 -0.0212 65  MET B C     
2636 O  O     . MET B 72  ? 0.4261 0.5585 0.4682 0.0863  -0.0018 -0.0258 65  MET B O     
2637 C  CB    . MET B 72  ? 0.4141 0.4796 0.4209 0.0855  0.0026  -0.0120 65  MET B CB    
2638 C  CG    . MET B 72  ? 0.3903 0.4531 0.3974 0.0711  0.0048  -0.0123 65  MET B CG    
2639 S  SD    . MET B 72  ? 0.3792 0.4189 0.3792 0.0644  0.0106  -0.0098 65  MET B SD    
2640 C  CE    . MET B 72  ? 0.3827 0.4331 0.3899 0.0636  0.0151  -0.0154 65  MET B CE    
2641 N  N     . LYS B 73  ? 0.4114 0.5296 0.4411 0.0756  -0.0074 -0.0224 66  LYS B N     
2642 C  CA    . LYS B 73  ? 0.4085 0.5475 0.4524 0.0644  -0.0082 -0.0286 66  LYS B CA    
2643 C  C     . LYS B 73  ? 0.3910 0.5159 0.4316 0.0495  -0.0039 -0.0280 66  LYS B C     
2644 O  O     . LYS B 73  ? 0.3910 0.5262 0.4415 0.0385  -0.0014 -0.0311 66  LYS B O     
2645 C  CB    . LYS B 73  ? 0.4225 0.5760 0.4685 0.0661  -0.0175 -0.0322 66  LYS B CB    
2646 C  CG    . LYS B 73  ? 0.4458 0.6215 0.4996 0.0800  -0.0239 -0.0344 66  LYS B CG    
2647 C  CD    . LYS B 73  ? 0.4638 0.6546 0.5181 0.0817  -0.0348 -0.0386 66  LYS B CD    
2648 C  CE    . LYS B 73  ? 0.4911 0.7055 0.5531 0.0973  -0.0427 -0.0407 66  LYS B CE    
2649 N  NZ    . LYS B 73  ? 0.5116 0.7415 0.5731 0.0980  -0.0546 -0.0456 66  LYS B NZ    
2650 N  N     . LYS B 74  ? 0.3811 0.4833 0.4077 0.0493  -0.0035 -0.0238 67  LYS B N     
2651 C  CA    . LYS B 74  ? 0.3684 0.4557 0.3908 0.0384  -0.0009 -0.0231 67  LYS B CA    
2652 C  C     . LYS B 74  ? 0.3570 0.4237 0.3696 0.0402  0.0036  -0.0177 67  LYS B C     
2653 O  O     . LYS B 74  ? 0.3592 0.4174 0.3643 0.0478  0.0033  -0.0140 67  LYS B O     
2654 C  CB    . LYS B 74  ? 0.3724 0.4556 0.3890 0.0364  -0.0060 -0.0252 67  LYS B CB    
2655 C  CG    . LYS B 74  ? 0.3656 0.4332 0.3783 0.0272  -0.0044 -0.0255 67  LYS B CG    
2656 C  CD    . LYS B 74  ? 0.3771 0.4420 0.3857 0.0247  -0.0099 -0.0305 67  LYS B CD    
2657 C  CE    . LYS B 74  ? 0.3755 0.4224 0.3798 0.0179  -0.0087 -0.0307 67  LYS B CE    
2658 N  NZ    . LYS B 74  ? 0.3652 0.3996 0.3608 0.0241  -0.0056 -0.0267 67  LYS B NZ    
2659 N  N     . ILE B 75  ? 0.3491 0.4079 0.3617 0.0322  0.0075  -0.0171 68  ILE B N     
2660 C  CA    . ILE B 75  ? 0.3406 0.3820 0.3457 0.0323  0.0104  -0.0133 68  ILE B CA    
2661 C  C     . ILE B 75  ? 0.3352 0.3665 0.3373 0.0247  0.0097  -0.0130 68  ILE B C     
2662 O  O     . ILE B 75  ? 0.3402 0.3743 0.3453 0.0174  0.0094  -0.0149 68  ILE B O     
2663 C  CB    . ILE B 75  ? 0.3432 0.3840 0.3486 0.0324  0.0148  -0.0132 68  ILE B CB    
2664 C  CG1   . ILE B 75  ? 0.3389 0.3623 0.3365 0.0319  0.0162  -0.0105 68  ILE B CG1   
2665 C  CG2   . ILE B 75  ? 0.3477 0.3971 0.3575 0.0240  0.0175  -0.0152 68  ILE B CG2   
2666 C  CD1   . ILE B 75  ? 0.3413 0.3551 0.3347 0.0383  0.0153  -0.0077 68  ILE B CD1   
2667 N  N     . ASN B 76  ? 0.3299 0.3502 0.3267 0.0267  0.0092  -0.0107 69  ASN B N     
2668 C  CA    . ASN B 76  ? 0.3283 0.3392 0.3228 0.0224  0.0080  -0.0108 69  ASN B CA    
2669 C  C     . ASN B 76  ? 0.3237 0.3258 0.3157 0.0220  0.0097  -0.0078 69  ASN B C     
2670 O  O     . ASN B 76  ? 0.3214 0.3217 0.3129 0.0255  0.0110  -0.0057 69  ASN B O     
2671 C  CB    . ASN B 76  ? 0.3308 0.3407 0.3229 0.0259  0.0060  -0.0121 69  ASN B CB    
2672 C  CG    . ASN B 76  ? 0.3356 0.3365 0.3260 0.0236  0.0038  -0.0140 69  ASN B CG    
2673 O  OD1   . ASN B 76  ? 0.3438 0.3396 0.3340 0.0181  0.0017  -0.0157 69  ASN B OD1   
2674 N  ND2   . ASN B 76  ? 0.3356 0.3346 0.3246 0.0281  0.0043  -0.0137 69  ASN B ND2   
2675 N  N     . PHE B 77  ? 0.3271 0.3229 0.3169 0.0170  0.0092  -0.0074 70  PHE B N     
2676 C  CA    . PHE B 77  ? 0.3269 0.3151 0.3135 0.0167  0.0089  -0.0055 70  PHE B CA    
2677 C  C     . PHE B 77  ? 0.3270 0.3103 0.3145 0.0181  0.0058  -0.0052 70  PHE B C     
2678 O  O     . PHE B 77  ? 0.3341 0.3129 0.3201 0.0173  0.0033  -0.0061 70  PHE B O     
2679 C  CB    . PHE B 77  ? 0.3365 0.3209 0.3176 0.0119  0.0097  -0.0047 70  PHE B CB    
2680 C  CG    . PHE B 77  ? 0.3394 0.3314 0.3206 0.0122  0.0140  -0.0059 70  PHE B CG    
2681 C  CD1   . PHE B 77  ? 0.3414 0.3307 0.3197 0.0154  0.0151  -0.0067 70  PHE B CD1   
2682 C  CD2   . PHE B 77  ? 0.3443 0.3468 0.3294 0.0096  0.0166  -0.0072 70  PHE B CD2   
2683 C  CE1   . PHE B 77  ? 0.3487 0.3443 0.3267 0.0181  0.0189  -0.0090 70  PHE B CE1   
2684 C  CE2   . PHE B 77  ? 0.3498 0.3628 0.3369 0.0120  0.0208  -0.0092 70  PHE B CE2   
2685 C  CZ    . PHE B 77  ? 0.3526 0.3613 0.3353 0.0170  0.0221  -0.0102 70  PHE B CZ    
2686 N  N     . ALA B 78  ? 0.3234 0.3080 0.3140 0.0205  0.0060  -0.0043 71  ALA B N     
2687 C  CA    . ALA B 78  ? 0.3253 0.3111 0.3199 0.0230  0.0041  -0.0046 71  ALA B CA    
2688 C  C     . ALA B 78  ? 0.3273 0.3137 0.3255 0.0216  0.0028  -0.0035 71  ALA B C     
2689 O  O     . ALA B 78  ? 0.3301 0.3118 0.3243 0.0188  0.0019  -0.0032 71  ALA B O     
2690 C  CB    . ALA B 78  ? 0.3238 0.3169 0.3212 0.0266  0.0069  -0.0051 71  ALA B CB    
2691 N  N     . GLY B 79  ? 0.3296 0.3234 0.3357 0.0235  0.0027  -0.0036 72  GLY B N     
2692 C  CA    . GLY B 79  ? 0.3353 0.3326 0.3478 0.0211  0.0003  -0.0035 72  GLY B CA    
2693 C  C     . GLY B 79  ? 0.3402 0.3510 0.3645 0.0237  0.0011  -0.0041 72  GLY B C     
2694 O  O     . GLY B 79  ? 0.3392 0.3562 0.3652 0.0259  0.0062  -0.0036 72  GLY B O     
2695 N  N     . GLY B 80  ? 0.3489 0.3658 0.3807 0.0243  -0.0040 -0.0057 73  GLY B N     
2696 C  CA    . GLY B 80  ? 0.3562 0.3652 0.3822 0.0248  -0.0118 -0.0065 73  GLY B CA    
2697 C  C     . GLY B 80  ? 0.3590 0.3554 0.3735 0.0294  -0.0143 -0.0062 73  GLY B C     
2698 O  O     . GLY B 80  ? 0.3529 0.3457 0.3636 0.0308  -0.0103 -0.0063 73  GLY B O     
2699 N  N     . GLU B 81  ? 0.3729 0.3611 0.3801 0.0307  -0.0214 -0.0056 74  GLU B N     
2700 C  CA    . GLU B 81  ? 0.3838 0.3564 0.3781 0.0330  -0.0239 -0.0038 74  GLU B CA    
2701 C  C     . GLU B 81  ? 0.3849 0.3467 0.3654 0.0265  -0.0222 -0.0012 74  GLU B C     
2702 O  O     . GLU B 81  ? 0.3954 0.3547 0.3693 0.0246  -0.0259 -0.0004 74  GLU B O     
2703 C  CB    . GLU B 81  ? 0.4076 0.3758 0.4001 0.0401  -0.0327 -0.0034 74  GLU B CB    
2704 C  CG    . GLU B 81  ? 0.4278 0.3744 0.4037 0.0408  -0.0356 0.0000  74  GLU B CG    
2705 C  CD    . GLU B 81  ? 0.4223 0.3611 0.3956 0.0387  -0.0300 -0.0005 74  GLU B CD    
2706 O  OE1   . GLU B 81  ? 0.4152 0.3618 0.3982 0.0434  -0.0278 -0.0047 74  GLU B OE1   
2707 O  OE2   . GLU B 81  ? 0.4283 0.3547 0.3900 0.0320  -0.0278 0.0025  74  GLU B OE2   
2708 N  N     . PRO B 82  ? 0.3767 0.3341 0.3528 0.0230  -0.0164 -0.0006 75  PRO B N     
2709 C  CA    . PRO B 82  ? 0.3790 0.3315 0.3448 0.0172  -0.0131 0.0011  75  PRO B CA    
2710 C  C     . PRO B 82  ? 0.4039 0.3444 0.3547 0.0156  -0.0169 0.0048  75  PRO B C     
2711 O  O     . PRO B 82  ? 0.4113 0.3509 0.3533 0.0126  -0.0158 0.0052  75  PRO B O     
2712 C  CB    . PRO B 82  ? 0.3707 0.3239 0.3377 0.0146  -0.0076 0.0007  75  PRO B CB    
2713 C  CG    . PRO B 82  ? 0.3567 0.3184 0.3351 0.0188  -0.0067 -0.0019 75  PRO B CG    
2714 C  CD    . PRO B 82  ? 0.3654 0.3269 0.3477 0.0243  -0.0122 -0.0025 75  PRO B CD    
2715 N  N     . PHE B 83  ? 0.4228 0.3523 0.3687 0.0184  -0.0220 0.0074  76  PHE B N     
2716 C  CA    . PHE B 83  ? 0.4539 0.3684 0.3820 0.0165  -0.0252 0.0128  76  PHE B CA    
2717 C  C     . PHE B 83  ? 0.4696 0.3844 0.3916 0.0207  -0.0329 0.0133  76  PHE B C     
2718 O  O     . PHE B 83  ? 0.5003 0.4024 0.4044 0.0200  -0.0364 0.0185  76  PHE B O     
2719 C  CB    . PHE B 83  ? 0.4756 0.3736 0.3988 0.0177  -0.0280 0.0159  76  PHE B CB    
2720 C  CG    . PHE B 83  ? 0.4739 0.3689 0.3961 0.0090  -0.0206 0.0168  76  PHE B CG    
2721 C  CD1   . PHE B 83  ? 0.4947 0.3826 0.4033 0.0003  -0.0163 0.0222  76  PHE B CD1   
2722 C  CD2   . PHE B 83  ? 0.4535 0.3561 0.3886 0.0089  -0.0175 0.0118  76  PHE B CD2   
2723 C  CE1   . PHE B 83  ? 0.4951 0.3851 0.4062 -0.0088 -0.0093 0.0225  76  PHE B CE1   
2724 C  CE2   . PHE B 83  ? 0.4542 0.3574 0.3902 0.0005  -0.0120 0.0116  76  PHE B CE2   
2725 C  CZ    . PHE B 83  ? 0.4751 0.3727 0.4005 -0.0088 -0.0080 0.0170  76  PHE B CZ    
2726 N  N     . LEU B 84  ? 0.4532 0.3825 0.3889 0.0240  -0.0356 0.0083  77  LEU B N     
2727 C  CA    . LEU B 84  ? 0.4680 0.4009 0.3991 0.0255  -0.0427 0.0070  77  LEU B CA    
2728 C  C     . LEU B 84  ? 0.4716 0.4029 0.3901 0.0194  -0.0381 0.0062  77  LEU B C     
2729 O  O     . LEU B 84  ? 0.4936 0.4235 0.4013 0.0201  -0.0444 0.0053  77  LEU B O     
2730 C  CB    . LEU B 84  ? 0.4541 0.4043 0.4055 0.0282  -0.0464 0.0016  77  LEU B CB    
2731 C  CG    . LEU B 84  ? 0.4618 0.4176 0.4249 0.0368  -0.0531 0.0012  77  LEU B CG    
2732 C  CD1   . LEU B 84  ? 0.4473 0.4250 0.4334 0.0371  -0.0534 -0.0040 77  LEU B CD1   
2733 C  CD2   . LEU B 84  ? 0.4981 0.4452 0.4481 0.0431  -0.0646 0.0043  77  LEU B CD2   
2734 N  N     . TYR B 85  ? 0.4544 0.3873 0.3741 0.0146  -0.0281 0.0056  78  TYR B N     
2735 C  CA    . TYR B 85  ? 0.4586 0.3924 0.3688 0.0109  -0.0226 0.0033  78  TYR B CA    
2736 C  C     . TYR B 85  ? 0.4633 0.3936 0.3652 0.0066  -0.0139 0.0072  78  TYR B C     
2737 O  O     . TYR B 85  ? 0.4479 0.3857 0.3562 0.0046  -0.0060 0.0047  78  TYR B O     
2738 C  CB    . TYR B 85  ? 0.4358 0.3788 0.3596 0.0103  -0.0187 -0.0026 78  TYR B CB    
2739 C  CG    . TYR B 85  ? 0.4343 0.3824 0.3686 0.0115  -0.0257 -0.0067 78  TYR B CG    
2740 C  CD1   . TYR B 85  ? 0.4214 0.3766 0.3720 0.0135  -0.0288 -0.0061 78  TYR B CD1   
2741 C  CD2   . TYR B 85  ? 0.4504 0.3971 0.3786 0.0100  -0.0291 -0.0119 78  TYR B CD2   
2742 C  CE1   . TYR B 85  ? 0.4232 0.3869 0.3861 0.0129  -0.0343 -0.0097 78  TYR B CE1   
2743 C  CE2   . TYR B 85  ? 0.4542 0.4062 0.3934 0.0088  -0.0361 -0.0159 78  TYR B CE2   
2744 C  CZ    . TYR B 85  ? 0.4398 0.4018 0.3977 0.0096  -0.0382 -0.0144 78  TYR B CZ    
2745 O  OH    . TYR B 85  ? 0.4456 0.4169 0.4176 0.0070  -0.0441 -0.0181 78  TYR B OH    
2746 N  N     . PRO B 86  ? 0.4901 0.4092 0.3772 0.0046  -0.0149 0.0139  79  PRO B N     
2747 C  CA    . PRO B 86  ? 0.4981 0.4153 0.3803 -0.0019 -0.0062 0.0181  79  PRO B CA    
2748 C  C     . PRO B 86  ? 0.5068 0.4326 0.3809 -0.0054 0.0028  0.0162  79  PRO B C     
2749 O  O     . PRO B 86  ? 0.5034 0.4369 0.3826 -0.0105 0.0115  0.0168  79  PRO B O     
2750 C  CB    . PRO B 86  ? 0.5337 0.4328 0.3999 -0.0033 -0.0109 0.0266  79  PRO B CB    
2751 C  CG    . PRO B 86  ? 0.5519 0.4457 0.4073 0.0032  -0.0211 0.0267  79  PRO B CG    
2752 C  CD    . PRO B 86  ? 0.5178 0.4252 0.3933 0.0084  -0.0248 0.0183  79  PRO B CD    
2753 N  N     . LYS B 87  ? 0.5204 0.4468 0.3831 -0.0022 0.0008  0.0126  80  LYS B N     
2754 C  CA    . LYS B 87  ? 0.5337 0.4684 0.3877 -0.0038 0.0101  0.0096  80  LYS B CA    
2755 C  C     . LYS B 87  ? 0.5031 0.4507 0.3761 -0.0010 0.0149  0.0021  80  LYS B C     
2756 O  O     . LYS B 87  ? 0.5030 0.4617 0.3801 -0.0031 0.0243  0.0013  80  LYS B O     
2757 C  CB    . LYS B 87  ? 0.5650 0.4947 0.3978 -0.0008 0.0064  0.0069  80  LYS B CB    
2758 C  CG    . LYS B 87  ? 0.5859 0.5243 0.4071 -0.0009 0.0168  0.0028  80  LYS B CG    
2759 C  CD    . LYS B 87  ? 0.6241 0.5566 0.4204 0.0022  0.0133  -0.0006 80  LYS B CD    
2760 C  CE    . LYS B 87  ? 0.6494 0.5920 0.4335 0.0031  0.0254  -0.0053 80  LYS B CE    
2761 N  NZ    . LYS B 87  ? 0.6713 0.6193 0.4468 -0.0041 0.0366  0.0041  80  LYS B NZ    
2762 N  N     . PHE B 88  ? 0.4821 0.4284 0.3663 0.0033  0.0081  -0.0026 81  PHE B N     
2763 C  CA    . PHE B 88  ? 0.4576 0.4118 0.3581 0.0064  0.0113  -0.0079 81  PHE B CA    
2764 C  C     . PHE B 88  ? 0.4380 0.4002 0.3521 0.0042  0.0161  -0.0048 81  PHE B C     
2765 O  O     . PHE B 88  ? 0.4332 0.4059 0.3540 0.0055  0.0226  -0.0075 81  PHE B O     
2766 C  CB    . PHE B 88  ? 0.4425 0.3926 0.3531 0.0089  0.0035  -0.0107 81  PHE B CB    
2767 C  CG    . PHE B 88  ? 0.4257 0.3795 0.3493 0.0119  0.0063  -0.0148 81  PHE B CG    
2768 C  CD1   . PHE B 88  ? 0.4396 0.3894 0.3588 0.0150  0.0071  -0.0212 81  PHE B CD1   
2769 C  CD2   . PHE B 88  ? 0.4016 0.3605 0.3398 0.0121  0.0076  -0.0122 81  PHE B CD2   
2770 C  CE1   . PHE B 88  ? 0.4308 0.3799 0.3600 0.0183  0.0089  -0.0236 81  PHE B CE1   
2771 C  CE2   . PHE B 88  ? 0.3918 0.3521 0.3392 0.0154  0.0095  -0.0143 81  PHE B CE2   
2772 C  CZ    . PHE B 88  ? 0.4072 0.3617 0.3500 0.0184  0.0101  -0.0194 81  PHE B CZ    
2773 N  N     . LEU B 89  ? 0.4305 0.3877 0.3487 0.0017  0.0118  0.0000  82  LEU B N     
2774 C  CA    . LEU B 89  ? 0.4146 0.3772 0.3453 -0.0004 0.0141  0.0016  82  LEU B CA    
2775 C  C     . LEU B 89  ? 0.4285 0.3994 0.3572 -0.0061 0.0221  0.0033  82  LEU B C     
2776 O  O     . LEU B 89  ? 0.4169 0.4008 0.3579 -0.0060 0.0262  0.0007  82  LEU B O     
2777 C  CB    . LEU B 89  ? 0.4147 0.3669 0.3460 -0.0011 0.0075  0.0054  82  LEU B CB    
2778 C  CG    . LEU B 89  ? 0.4052 0.3593 0.3466 -0.0034 0.0083  0.0060  82  LEU B CG    
2779 C  CD1   . LEU B 89  ? 0.3796 0.3447 0.3352 0.0008  0.0093  0.0015  82  LEU B CD1   
2780 C  CD2   . LEU B 89  ? 0.4144 0.3549 0.3530 -0.0023 0.0015  0.0088  82  LEU B CD2   
2781 N  N     . GLY B 90  ? 0.4570 0.4220 0.3704 -0.0112 0.0242  0.0078  83  GLY B N     
2782 C  CA    . GLY B 90  ? 0.4779 0.4522 0.3885 -0.0186 0.0333  0.0104  83  GLY B CA    
2783 C  C     . GLY B 90  ? 0.4761 0.4699 0.3927 -0.0149 0.0413  0.0042  83  GLY B C     
2784 O  O     . GLY B 90  ? 0.4764 0.4871 0.4050 -0.0187 0.0476  0.0033  83  GLY B O     
2785 N  N     . GLU B 91  ? 0.4782 0.4698 0.3871 -0.0072 0.0402  -0.0007 84  GLU B N     
2786 C  CA    . GLU B 91  ? 0.4824 0.4890 0.3952 -0.0011 0.0469  -0.0077 84  GLU B CA    
2787 C  C     . GLU B 91  ? 0.4556 0.4724 0.3889 0.0038  0.0459  -0.0115 84  GLU B C     
2788 O  O     . GLU B 91  ? 0.4605 0.4954 0.4028 0.0069  0.0523  -0.0152 84  GLU B O     
2789 C  CB    . GLU B 91  ? 0.4936 0.4902 0.3932 0.0063  0.0438  -0.0134 84  GLU B CB    
2790 C  CG    . GLU B 91  ? 0.5288 0.5197 0.4052 0.0035  0.0459  -0.0115 84  GLU B CG    
2791 C  CD    . GLU B 91  ? 0.5451 0.5273 0.4083 0.0110  0.0423  -0.0194 84  GLU B CD    
2792 O  OE1   . GLU B 91  ? 0.5464 0.5346 0.4150 0.0188  0.0456  -0.0278 84  GLU B OE1   
2793 O  OE2   . GLU B 91  ? 0.5608 0.5300 0.4081 0.0096  0.0357  -0.0177 84  GLU B OE2   
2794 N  N     . MET B 92  ? 0.4313 0.4376 0.3713 0.0061  0.0379  -0.0109 85  MET B N     
2795 C  CA    . MET B 92  ? 0.4115 0.4251 0.3667 0.0119  0.0366  -0.0138 85  MET B CA    
2796 C  C     . MET B 92  ? 0.4049 0.4323 0.3728 0.0066  0.0383  -0.0117 85  MET B C     
2797 O  O     . MET B 92  ? 0.4016 0.4443 0.3812 0.0112  0.0401  -0.0150 85  MET B O     
2798 C  CB    . MET B 92  ? 0.3933 0.3930 0.3504 0.0148  0.0290  -0.0131 85  MET B CB    
2799 C  CG    . MET B 92  ? 0.4018 0.3888 0.3501 0.0188  0.0261  -0.0162 85  MET B CG    
2800 S  SD    . MET B 92  ? 0.4221 0.4125 0.3675 0.0282  0.0309  -0.0237 85  MET B SD    
2801 C  CE    . MET B 92  ? 0.4514 0.4414 0.3789 0.0257  0.0348  -0.0261 85  MET B CE    
2802 N  N     . ILE B 93  ? 0.4081 0.4292 0.3732 -0.0025 0.0368  -0.0068 86  ILE B N     
2803 C  CA    . ILE B 93  ? 0.4096 0.4413 0.3855 -0.0098 0.0379  -0.0056 86  ILE B CA    
2804 C  C     . ILE B 93  ? 0.4281 0.4822 0.4102 -0.0132 0.0465  -0.0074 86  ILE B C     
2805 O  O     . ILE B 93  ? 0.4255 0.4987 0.4231 -0.0132 0.0475  -0.0105 86  ILE B O     
2806 C  CB    . ILE B 93  ? 0.4201 0.4355 0.3884 -0.0192 0.0348  0.0000  86  ILE B CB    
2807 C  CG1   . ILE B 93  ? 0.4016 0.4023 0.3704 -0.0146 0.0263  -0.0001 86  ILE B CG1   
2808 C  CG2   . ILE B 93  ? 0.4378 0.4616 0.4131 -0.0309 0.0379  0.0017  86  ILE B CG2   
2809 C  CD1   . ILE B 93  ? 0.4168 0.3971 0.3745 -0.0195 0.0221  0.0050  86  ILE B CD1   
2810 N  N     . ASP B 94  ? 0.4506 0.5041 0.4205 -0.0163 0.0528  -0.0054 87  ASP B N     
2811 C  CA    . ASP B 94  ? 0.4743 0.5513 0.4492 -0.0205 0.0631  -0.0065 87  ASP B CA    
2812 C  C     . ASP B 94  ? 0.4672 0.5644 0.4547 -0.0079 0.0652  -0.0145 87  ASP B C     
2813 O  O     . ASP B 94  ? 0.4728 0.5958 0.4775 -0.0091 0.0689  -0.0174 87  ASP B O     
2814 C  CB    . ASP B 94  ? 0.5045 0.5751 0.4594 -0.0250 0.0698  -0.0026 87  ASP B CB    
2815 C  CG    . ASP B 94  ? 0.5233 0.5750 0.4649 -0.0380 0.0686  0.0067  87  ASP B CG    
2816 O  OD1   . ASP B 94  ? 0.5167 0.5617 0.4664 -0.0453 0.0637  0.0097  87  ASP B OD1   
2817 O  OD2   . ASP B 94  ? 0.5490 0.5904 0.4699 -0.0397 0.0717  0.0109  87  ASP B OD2   
2818 N  N     . PHE B 95  ? 0.4584 0.5433 0.4381 0.0042  0.0617  -0.0183 88  PHE B N     
2819 C  CA    . PHE B 95  ? 0.4584 0.5561 0.4471 0.0178  0.0625  -0.0254 88  PHE B CA    
2820 C  C     . PHE B 95  ? 0.4409 0.5499 0.4479 0.0212  0.0572  -0.0266 88  PHE B C     
2821 O  O     . PHE B 95  ? 0.4497 0.5824 0.4707 0.0281  0.0598  -0.0312 88  PHE B O     
2822 C  CB    . PHE B 95  ? 0.4557 0.5308 0.4314 0.0278  0.0579  -0.0282 88  PHE B CB    
2823 C  CG    . PHE B 95  ? 0.4626 0.5419 0.4434 0.0430  0.0575  -0.0351 88  PHE B CG    
2824 C  CD1   . PHE B 95  ? 0.4906 0.5827 0.4691 0.0512  0.0649  -0.0418 88  PHE B CD1   
2825 C  CD2   . PHE B 95  ? 0.4470 0.5156 0.4331 0.0498  0.0500  -0.0347 88  PHE B CD2   
2826 C  CE1   . PHE B 95  ? 0.5034 0.5946 0.4847 0.0670  0.0635  -0.0485 88  PHE B CE1   
2827 C  CE2   . PHE B 95  ? 0.4608 0.5285 0.4491 0.0643  0.0489  -0.0399 88  PHE B CE2   
2828 C  CZ    . PHE B 95  ? 0.4895 0.5675 0.4756 0.0735  0.0552  -0.0471 88  PHE B CZ    
2829 N  N     . CYS B 96  ? 0.4196 0.5129 0.4262 0.0176  0.0494  -0.0228 89  CYS B N     
2830 C  CA    . CYS B 96  ? 0.4067 0.5078 0.4260 0.0220  0.0435  -0.0240 89  CYS B CA    
2831 C  C     . CYS B 96  ? 0.4158 0.5440 0.4518 0.0151  0.0455  -0.0256 89  CYS B C     
2832 O  O     . CYS B 96  ? 0.4171 0.5632 0.4661 0.0226  0.0427  -0.0293 89  CYS B O     
2833 C  CB    . CYS B 96  ? 0.3872 0.4682 0.4016 0.0189  0.0360  -0.0202 89  CYS B CB    
2834 S  SG    . CYS B 96  ? 0.3777 0.4341 0.3801 0.0284  0.0321  -0.0192 89  CYS B SG    
2835 N  N     . LYS B 97  ? 0.4253 0.5547 0.4604 0.0002  0.0492  -0.0223 90  LYS B N     
2836 C  CA    . LYS B 97  ? 0.4385 0.5922 0.4903 -0.0099 0.0508  -0.0236 90  LYS B CA    
2837 C  C     . LYS B 97  ? 0.4615 0.6464 0.5245 -0.0090 0.0606  -0.0271 90  LYS B C     
2838 O  O     . LYS B 97  ? 0.4689 0.6828 0.5516 -0.0071 0.0600  -0.0318 90  LYS B O     
2839 C  CB    . LYS B 97  ? 0.4474 0.5871 0.4939 -0.0273 0.0506  -0.0183 90  LYS B CB    
2840 C  CG    . LYS B 97  ? 0.4594 0.6170 0.5233 -0.0386 0.0479  -0.0206 90  LYS B CG    
2841 C  CD    . LYS B 97  ? 0.4417 0.5920 0.5087 -0.0328 0.0367  -0.0239 90  LYS B CD    
2842 C  CE    . LYS B 97  ? 0.4567 0.6248 0.5404 -0.0429 0.0320  -0.0281 90  LYS B CE    
2843 N  NZ    . LYS B 97  ? 0.4421 0.6087 0.5272 -0.0325 0.0215  -0.0326 90  LYS B NZ    
2844 N  N     . GLU B 98  ? 0.4754 0.6561 0.5258 -0.0088 0.0691  -0.0256 91  GLU B N     
2845 C  CA    . GLU B 98  ? 0.5030 0.7145 0.5622 -0.0089 0.0805  -0.0288 91  GLU B CA    
2846 C  C     . GLU B 98  ? 0.5055 0.7331 0.5718 0.0112  0.0811  -0.0369 91  GLU B C     
2847 O  O     . GLU B 98  ? 0.5227 0.7862 0.6089 0.0144  0.0859  -0.0421 91  GLU B O     
2848 C  CB    . GLU B 98  ? 0.5246 0.7254 0.5643 -0.0170 0.0899  -0.0239 91  GLU B CB    
2849 C  CG    . GLU B 98  ? 0.5367 0.7266 0.5713 -0.0377 0.0912  -0.0153 91  GLU B CG    
2850 C  CD    . GLU B 98  ? 0.5641 0.7406 0.5755 -0.0451 0.0997  -0.0088 91  GLU B CD    
2851 O  OE1   . GLU B 98  ? 0.5748 0.7301 0.5746 -0.0589 0.0982  -0.0004 91  GLU B OE1   
2852 O  OE2   . GLU B 98  ? 0.5800 0.7670 0.5837 -0.0363 0.1078  -0.0125 91  GLU B OE2   
2853 N  N     . THR B 99  ? 0.4944 0.6965 0.5452 0.0247  0.0767  -0.0383 92  THR B N     
2854 C  CA    . THR B 99  ? 0.5045 0.7150 0.5589 0.0446  0.0767  -0.0458 92  THR B CA    
2855 C  C     . THR B 99  ? 0.4897 0.7009 0.5556 0.0550  0.0660  -0.0472 92  THR B C     
2856 O  O     . THR B 99  ? 0.5036 0.7406 0.5856 0.0666  0.0656  -0.0527 92  THR B O     
2857 C  CB    . THR B 99  ? 0.5100 0.6917 0.5416 0.0531  0.0773  -0.0473 92  THR B CB    
2858 O  OG1   . THR B 99  ? 0.5305 0.7159 0.5505 0.0444  0.0874  -0.0464 92  THR B OG1   
2859 C  CG2   . THR B 99  ? 0.5271 0.7101 0.5595 0.0740  0.0765  -0.0554 92  THR B CG2   
2860 N  N     . LEU B 100 ? 0.4653 0.6488 0.5222 0.0523  0.0570  -0.0423 93  LEU B N     
2861 C  CA    . LEU B 100 ? 0.4573 0.6386 0.5201 0.0634  0.0475  -0.0428 93  LEU B CA    
2862 C  C     . LEU B 100 ? 0.4545 0.6611 0.5357 0.0568  0.0433  -0.0432 93  LEU B C     
2863 O  O     . LEU B 100 ? 0.4569 0.6709 0.5452 0.0677  0.0358  -0.0449 93  LEU B O     
2864 C  CB    . LEU B 100 ? 0.4373 0.5821 0.4833 0.0629  0.0409  -0.0375 93  LEU B CB    
2865 C  CG    . LEU B 100 ? 0.4435 0.5620 0.4724 0.0691  0.0427  -0.0380 93  LEU B CG    
2866 C  CD1   . LEU B 100 ? 0.4265 0.5148 0.4438 0.0676  0.0360  -0.0327 93  LEU B CD1   
2867 C  CD2   . LEU B 100 ? 0.4696 0.5919 0.4993 0.0870  0.0437  -0.0439 93  LEU B CD2   
2868 N  N     . GLN B 101 ? 0.4545 0.6727 0.5421 0.0390  0.0473  -0.0416 94  GLN B N     
2869 C  CA    . GLN B 101 ? 0.4572 0.6980 0.5625 0.0297  0.0429  -0.0430 94  GLN B CA    
2870 C  C     . GLN B 101 ? 0.4406 0.6646 0.5410 0.0323  0.0312  -0.0414 94  GLN B C     
2871 O  O     . GLN B 101 ? 0.4474 0.6914 0.5611 0.0358  0.0241  -0.0449 94  GLN B O     
2872 C  CB    . GLN B 101 ? 0.4795 0.7620 0.6077 0.0382  0.0446  -0.0498 94  GLN B CB    
2873 C  CG    . GLN B 101 ? 0.5008 0.8053 0.6354 0.0337  0.0580  -0.0518 94  GLN B CG    
2874 C  CD    . GLN B 101 ? 0.5251 0.8784 0.6882 0.0372  0.0600  -0.0587 94  GLN B CD    
2875 O  OE1   . GLN B 101 ? 0.5365 0.9056 0.7075 0.0572  0.0576  -0.0642 94  GLN B OE1   
2876 N  NE2   . GLN B 101 ? 0.5371 0.9143 0.7164 0.0175  0.0637  -0.0584 94  GLN B NE2   
2877 N  N     . LEU B 102 ? 0.4224 0.6121 0.5040 0.0292  0.0293  -0.0363 95  LEU B N     
2878 C  CA    . LEU B 102 ? 0.4096 0.5834 0.4846 0.0314  0.0201  -0.0346 95  LEU B CA    
2879 C  C     . LEU B 102 ? 0.4138 0.5966 0.4973 0.0176  0.0158  -0.0364 95  LEU B C     
2880 O  O     . LEU B 102 ? 0.4216 0.6081 0.5094 0.0029  0.0205  -0.0360 95  LEU B O     
2881 C  CB    . LEU B 102 ? 0.3925 0.5317 0.4481 0.0314  0.0204  -0.0293 95  LEU B CB    
2882 C  CG    . LEU B 102 ? 0.3926 0.5186 0.4388 0.0446  0.0222  -0.0281 95  LEU B CG    
2883 C  CD1   . LEU B 102 ? 0.3792 0.4754 0.4096 0.0418  0.0227  -0.0236 95  LEU B CD1   
2884 C  CD2   . LEU B 102 ? 0.3999 0.5292 0.4473 0.0588  0.0160  -0.0286 95  LEU B CD2   
2885 N  N     . GLU B 103 ? 0.4133 0.5963 0.4966 0.0222  0.0067  -0.0383 96  GLU B N     
2886 C  CA    . GLU B 103 ? 0.4224 0.6120 0.5122 0.0104  0.0007  -0.0419 96  GLU B CA    
2887 C  C     . GLU B 103 ? 0.4156 0.5770 0.4929 -0.0016 0.0019  -0.0388 96  GLU B C     
2888 O  O     . GLU B 103 ? 0.4295 0.5922 0.5123 -0.0163 0.0012  -0.0408 96  GLU B O     
2889 C  CB    . GLU B 103 ? 0.4274 0.6214 0.5153 0.0201  -0.0098 -0.0450 96  GLU B CB    
2890 C  CG    . GLU B 103 ? 0.4428 0.6675 0.5447 0.0320  -0.0139 -0.0488 96  GLU B CG    
2891 C  CD    . GLU B 103 ? 0.4551 0.6851 0.5531 0.0414  -0.0258 -0.0517 96  GLU B CD    
2892 O  OE1   . GLU B 103 ? 0.4558 0.6725 0.5444 0.0348  -0.0309 -0.0533 96  GLU B OE1   
2893 O  OE2   . GLU B 103 ? 0.4681 0.7150 0.5709 0.0564  -0.0301 -0.0525 96  GLU B OE2   
2894 N  N     . SER B 104 ? 0.3983 0.5335 0.4591 0.0047  0.0030  -0.0341 97  SER B N     
2895 C  CA    . SER B 104 ? 0.3942 0.5040 0.4435 -0.0029 0.0024  -0.0319 97  SER B CA    
2896 C  C     . SER B 104 ? 0.3785 0.4680 0.4155 0.0013  0.0075  -0.0261 97  SER B C     
2897 O  O     . SER B 104 ? 0.3673 0.4520 0.3986 0.0124  0.0074  -0.0243 97  SER B O     
2898 C  CB    . SER B 104 ? 0.3957 0.4976 0.4386 0.0008  -0.0054 -0.0351 97  SER B CB    
2899 O  OG    . SER B 104 ? 0.3949 0.4722 0.4270 -0.0041 -0.0058 -0.0338 97  SER B OG    
2900 N  N     . VAL B 105 ? 0.3829 0.4603 0.4155 -0.0083 0.0113  -0.0231 98  VAL B N     
2901 C  CA    . VAL B 105 ? 0.3730 0.4312 0.3936 -0.0058 0.0143  -0.0183 98  VAL B CA    
2902 C  C     . VAL B 105 ? 0.3762 0.4131 0.3885 -0.0104 0.0104  -0.0171 98  VAL B C     
2903 O  O     . VAL B 105 ? 0.3942 0.4262 0.4069 -0.0209 0.0099  -0.0171 98  VAL B O     
2904 C  CB    . VAL B 105 ? 0.3825 0.4449 0.4024 -0.0111 0.0215  -0.0158 98  VAL B CB    
2905 C  CG1   . VAL B 105 ? 0.3781 0.4204 0.3842 -0.0097 0.0230  -0.0114 98  VAL B CG1   
2906 C  CG2   . VAL B 105 ? 0.3835 0.4678 0.4120 -0.0041 0.0255  -0.0185 98  VAL B CG2   
2907 N  N     . SER B 106 ? 0.3631 0.3875 0.3683 -0.0026 0.0081  -0.0161 99  SER B N     
2908 C  CA    . SER B 106 ? 0.3685 0.3751 0.3670 -0.0037 0.0043  -0.0161 99  SER B CA    
2909 C  C     . SER B 106 ? 0.3598 0.3540 0.3513 0.0005  0.0052  -0.0120 99  SER B C     
2910 O  O     . SER B 106 ? 0.3479 0.3467 0.3395 0.0050  0.0079  -0.0103 99  SER B O     
2911 C  CB    . SER B 106 ? 0.3688 0.3771 0.3678 0.0014  -0.0002 -0.0208 99  SER B CB    
2912 O  OG    . SER B 106 ? 0.3544 0.3692 0.3526 0.0111  0.0006  -0.0200 99  SER B OG    
2913 N  N     . ILE B 107 ? 0.3700 0.3481 0.3556 -0.0003 0.0020  -0.0112 100 ILE B N     
2914 C  CA    . ILE B 107 ? 0.3667 0.3349 0.3471 0.0040  0.0010  -0.0082 100 ILE B CA    
2915 C  C     . ILE B 107 ? 0.3733 0.3332 0.3527 0.0092  -0.0032 -0.0111 100 ILE B C     
2916 O  O     . ILE B 107 ? 0.3904 0.3429 0.3681 0.0063  -0.0059 -0.0140 100 ILE B O     
2917 C  CB    . ILE B 107 ? 0.3830 0.3395 0.3553 -0.0014 0.0010  -0.0035 100 ILE B CB    
2918 C  CG1   . ILE B 107 ? 0.3875 0.3526 0.3595 -0.0085 0.0064  -0.0016 100 ILE B CG1   
2919 C  CG2   . ILE B 107 ? 0.3784 0.3301 0.3471 0.0043  -0.0010 -0.0013 100 ILE B CG2   
2920 C  CD1   . ILE B 107 ? 0.4141 0.3665 0.3756 -0.0162 0.0072  0.0035  100 ILE B CD1   
2921 N  N     . VAL B 108 ? 0.3631 0.3258 0.3444 0.0166  -0.0034 -0.0109 101 VAL B N     
2922 C  CA    . VAL B 108 ? 0.3727 0.3299 0.3538 0.0233  -0.0067 -0.0137 101 VAL B CA    
2923 C  C     . VAL B 108 ? 0.3785 0.3294 0.3585 0.0261  -0.0095 -0.0106 101 VAL B C     
2924 O  O     . VAL B 108 ? 0.3670 0.3243 0.3493 0.0255  -0.0082 -0.0077 101 VAL B O     
2925 C  CB    . VAL B 108 ? 0.3623 0.3329 0.3483 0.0297  -0.0039 -0.0165 101 VAL B CB    
2926 C  CG1   . VAL B 108 ? 0.3452 0.3264 0.3359 0.0299  0.0000  -0.0127 101 VAL B CG1   
2927 C  CG2   . VAL B 108 ? 0.3763 0.3446 0.3628 0.0378  -0.0060 -0.0205 101 VAL B CG2   
2928 N  N     . THR B 109 ? 0.4020 0.3384 0.3773 0.0296  -0.0146 -0.0116 102 THR B N     
2929 C  CA    . THR B 109 ? 0.4152 0.3435 0.3872 0.0328  -0.0193 -0.0082 102 THR B CA    
2930 C  C     . THR B 109 ? 0.4373 0.3582 0.4100 0.0432  -0.0245 -0.0119 102 THR B C     
2931 O  O     . THR B 109 ? 0.4525 0.3640 0.4220 0.0448  -0.0253 -0.0164 102 THR B O     
2932 C  CB    . THR B 109 ? 0.4343 0.3458 0.3943 0.0253  -0.0211 -0.0026 102 THR B CB    
2933 O  OG1   . THR B 109 ? 0.4533 0.3556 0.4072 0.0300  -0.0271 0.0011  102 THR B OG1   
2934 C  CG2   . THR B 109 ? 0.4595 0.3533 0.4125 0.0207  -0.0226 -0.0034 102 THR B CG2   
2935 N  N     . ASN B 110 ? 0.4437 0.3686 0.4202 0.0505  -0.0287 -0.0109 103 ASN B N     
2936 C  CA    . ASN B 110 ? 0.4722 0.3890 0.4488 0.0624  -0.0349 -0.0141 103 ASN B CA    
2937 C  C     . ASN B 110 ? 0.5094 0.3957 0.4702 0.0620  -0.0415 -0.0105 103 ASN B C     
2938 O  O     . ASN B 110 ? 0.5413 0.4141 0.4992 0.0726  -0.0474 -0.0134 103 ASN B O     
2939 C  CB    . ASN B 110 ? 0.4716 0.4060 0.4599 0.0711  -0.0380 -0.0147 103 ASN B CB    
2940 C  CG    . ASN B 110 ? 0.4767 0.4088 0.4608 0.0686  -0.0435 -0.0088 103 ASN B CG    
2941 O  OD1   . ASN B 110 ? 0.4979 0.4079 0.4665 0.0657  -0.0478 -0.0037 103 ASN B OD1   
2942 N  ND2   . ASN B 110 ? 0.4604 0.4148 0.4571 0.0680  -0.0431 -0.0093 103 ASN B ND2   
2943 N  N     . GLY B 111 ? 0.5113 0.3862 0.4614 0.0505  -0.0404 -0.0038 104 GLY B N     
2944 C  CA    . GLY B 111 ? 0.5504 0.3952 0.4842 0.0463  -0.0444 0.0008  104 GLY B CA    
2945 C  C     . GLY B 111 ? 0.5834 0.4122 0.5052 0.0515  -0.0523 0.0078  104 GLY B C     
2946 O  O     . GLY B 111 ? 0.6144 0.4198 0.5197 0.0440  -0.0536 0.0152  104 GLY B O     
2947 N  N     . SER B 112 ? 0.5779 0.4216 0.5078 0.0626  -0.0569 0.0063  105 SER B N     
2948 C  CA    . SER B 112 ? 0.6157 0.4450 0.5344 0.0709  -0.0669 0.0120  105 SER B CA    
2949 C  C     . SER B 112 ? 0.6264 0.4459 0.5278 0.0603  -0.0664 0.0216  105 SER B C     
2950 O  O     . SER B 112 ? 0.6725 0.4649 0.5545 0.0614  -0.0724 0.0293  105 SER B O     
2951 C  CB    . SER B 112 ? 0.6086 0.4611 0.5426 0.0841  -0.0724 0.0075  105 SER B CB    
2952 O  OG    . SER B 112 ? 0.5646 0.4473 0.5133 0.0779  -0.0663 0.0048  105 SER B OG    
2953 N  N     . LEU B 113 ? 0.5903 0.4296 0.4964 0.0504  -0.0591 0.0215  106 LEU B N     
2954 C  CA    . LEU B 113 ? 0.6035 0.4372 0.4928 0.0427  -0.0585 0.0290  106 LEU B CA    
2955 C  C     . LEU B 113 ? 0.6102 0.4319 0.4882 0.0280  -0.0496 0.0340  106 LEU B C     
2956 O  O     . LEU B 113 ? 0.6297 0.4449 0.4911 0.0213  -0.0477 0.0410  106 LEU B O     
2957 C  CB    . LEU B 113 ? 0.5697 0.4301 0.4691 0.0415  -0.0564 0.0251  106 LEU B CB    
2958 C  CG    . LEU B 113 ? 0.5664 0.4432 0.4788 0.0529  -0.0650 0.0205  106 LEU B CG    
2959 C  CD1   . LEU B 113 ? 0.5314 0.4334 0.4569 0.0481  -0.0611 0.0153  106 LEU B CD1   
2960 C  CD2   . LEU B 113 ? 0.6107 0.4749 0.5073 0.0607  -0.0769 0.0259  106 LEU B CD2   
2961 N  N     . VAL B 114 ? 0.5980 0.4186 0.4846 0.0228  -0.0442 0.0302  107 VAL B N     
2962 C  CA    . VAL B 114 ? 0.6037 0.4190 0.4845 0.0079  -0.0358 0.0337  107 VAL B CA    
2963 C  C     . VAL B 114 ? 0.6602 0.4451 0.5180 0.0019  -0.0381 0.0443  107 VAL B C     
2964 O  O     . VAL B 114 ? 0.6959 0.4562 0.5465 0.0081  -0.0457 0.0461  107 VAL B O     
2965 C  CB    . VAL B 114 ? 0.5907 0.4077 0.4844 0.0044  -0.0327 0.0269  107 VAL B CB    
2966 C  CG1   . VAL B 114 ? 0.6009 0.4158 0.4914 -0.0118 -0.0249 0.0301  107 VAL B CG1   
2967 C  CG2   . VAL B 114 ? 0.5424 0.3864 0.4559 0.0102  -0.0300 0.0176  107 VAL B CG2   
2968 N  N     . LYS B 115 ? 0.6733 0.4587 0.5196 -0.0104 -0.0306 0.0512  108 LYS B N     
2969 C  CA    . LYS B 115 ? 0.7328 0.4890 0.5559 -0.0186 -0.0309 0.0629  108 LYS B CA    
2970 C  C     . LYS B 115 ? 0.7422 0.4995 0.5674 -0.0371 -0.0201 0.0652  108 LYS B C     
2971 O  O     . LYS B 115 ? 0.7041 0.4895 0.5444 -0.0430 -0.0116 0.0595  108 LYS B O     
2972 C  CB    . LYS B 115 ? 0.7567 0.5106 0.5588 -0.0166 -0.0321 0.0711  108 LYS B CB    
2973 C  CG    . LYS B 115 ? 0.7651 0.5136 0.5618 0.0004  -0.0450 0.0707  108 LYS B CG    
2974 C  CD    . LYS B 115 ? 0.8057 0.5451 0.5756 0.0011  -0.0477 0.0804  108 LYS B CD    
2975 C  CE    . LYS B 115 ? 0.8122 0.5532 0.5795 0.0181  -0.0616 0.0786  108 LYS B CE    
2976 N  NZ    . LYS B 115 ? 0.8374 0.5809 0.5823 0.0182  -0.0631 0.0841  108 LYS B NZ    
2977 N  N     . GLU B 116 ? 0.7991 0.5253 0.6091 -0.0467 -0.0209 0.0739  109 GLU B N     
2978 C  CA    . GLU B 116 ? 0.8174 0.5440 0.6306 -0.0664 -0.0114 0.0765  109 GLU B CA    
2979 C  C     . GLU B 116 ? 0.8043 0.5590 0.6176 -0.0761 0.0011  0.0794  109 GLU B C     
2980 O  O     . GLU B 116 ? 0.7837 0.5618 0.6143 -0.0867 0.0097  0.0745  109 GLU B O     
2981 C  CB    . GLU B 116 ? 0.8928 0.5773 0.6849 -0.0765 -0.0141 0.0882  109 GLU B CB    
2982 C  CG    . GLU B 116 ? 0.9152 0.5979 0.7158 -0.0978 -0.0066 0.0885  109 GLU B CG    
2983 C  CD    . GLU B 116 ? 0.9959 0.6313 0.7758 -0.1085 -0.0104 0.0995  109 GLU B CD    
2984 O  OE1   . GLU B 116 ? 1.0331 0.6367 0.7913 -0.0969 -0.0195 0.1068  109 GLU B OE1   
2985 O  OE2   . GLU B 116 ? 1.0241 0.6551 0.8099 -0.1283 -0.0048 0.1007  109 GLU B OE2   
2986 N  N     . GLN B 117 ? 0.8191 0.5726 0.6132 -0.0711 0.0015  0.0864  110 GLN B N     
2987 C  CA    . GLN B 117 ? 0.8175 0.5944 0.6068 -0.0786 0.0135  0.0891  110 GLN B CA    
2988 C  C     . GLN B 117 ? 0.7534 0.5693 0.5688 -0.0751 0.0190  0.0761  110 GLN B C     
2989 O  O     . GLN B 117 ? 0.7509 0.5897 0.5722 -0.0845 0.0307  0.0754  110 GLN B O     
2990 C  CB    . GLN B 117 ? 0.8439 0.6118 0.6065 -0.0702 0.0101  0.0964  110 GLN B CB    
2991 C  CG    . GLN B 117 ? 0.8028 0.5794 0.5720 -0.0512 -0.0006 0.0875  110 GLN B CG    
2992 C  CD    . GLN B 117 ? 0.8380 0.5981 0.5814 -0.0410 -0.0099 0.0943  110 GLN B CD    
2993 O  OE1   . GLN B 117 ? 0.8910 0.6196 0.6142 -0.0404 -0.0166 0.1048  110 GLN B OE1   
2994 N  NE2   . GLN B 117 ? 0.8115 0.5914 0.5558 -0.0319 -0.0121 0.0877  110 GLN B NE2   
2995 N  N     . PHE B 118 ? 0.7063 0.5302 0.5370 -0.0612 0.0110  0.0661  111 PHE B N     
2996 C  CA    . PHE B 118 ? 0.6522 0.5084 0.5050 -0.0572 0.0155  0.0551  111 PHE B CA    
2997 C  C     . PHE B 118 ? 0.6419 0.5115 0.5143 -0.0677 0.0212  0.0508  111 PHE B C     
2998 O  O     . PHE B 118 ? 0.6211 0.5182 0.5069 -0.0709 0.0294  0.0459  111 PHE B O     
2999 C  CB    . PHE B 118 ? 0.6130 0.4719 0.4760 -0.0418 0.0060  0.0473  111 PHE B CB    
3000 C  CG    . PHE B 118 ? 0.5644 0.4513 0.4452 -0.0362 0.0095  0.0377  111 PHE B CG    
3001 C  CD1   . PHE B 118 ? 0.5355 0.4370 0.4365 -0.0375 0.0117  0.0309  111 PHE B CD1   
3002 C  CD2   . PHE B 118 ? 0.5524 0.4491 0.4285 -0.0293 0.0096  0.0354  111 PHE B CD2   
3003 C  CE1   . PHE B 118 ? 0.4975 0.4207 0.4123 -0.0313 0.0140  0.0235  111 PHE B CE1   
3004 C  CE2   . PHE B 118 ? 0.5154 0.4330 0.4062 -0.0245 0.0125  0.0272  111 PHE B CE2   
3005 C  CZ    . PHE B 118 ? 0.4882 0.4184 0.3981 -0.0251 0.0148  0.0219  111 PHE B CZ    
3006 N  N     . LEU B 119 ? 0.6595 0.5098 0.5344 -0.0721 0.0159  0.0514  112 LEU B N     
3007 C  CA    . LEU B 119 ? 0.6519 0.5141 0.5457 -0.0815 0.0186  0.0456  112 LEU B CA    
3008 C  C     . LEU B 119 ? 0.6884 0.5581 0.5812 -0.1003 0.0292  0.0519  112 LEU B C     
3009 O  O     . LEU B 119 ? 0.6749 0.5713 0.5867 -0.1075 0.0350  0.0463  112 LEU B O     
3010 C  CB    . LEU B 119 ? 0.6651 0.5022 0.5599 -0.0795 0.0087  0.0427  112 LEU B CB    
3011 C  CG    . LEU B 119 ? 0.6323 0.4666 0.5306 -0.0611 -0.0003 0.0360  112 LEU B CG    
3012 C  CD1   . LEU B 119 ? 0.6519 0.4632 0.5510 -0.0591 -0.0087 0.0316  112 LEU B CD1   
3013 C  CD2   . LEU B 119 ? 0.5773 0.4440 0.4934 -0.0532 0.0023  0.0271  112 LEU B CD2   
3014 N  N     . GLN B 120 ? 0.7375 0.5861 0.6078 -0.1077 0.0321  0.0638  113 GLN B N     
3015 C  CA    . GLN B 120 ? 0.7778 0.6354 0.6442 -0.1260 0.0444  0.0716  113 GLN B CA    
3016 C  C     . GLN B 120 ? 0.7525 0.6477 0.6258 -0.1229 0.0552  0.0680  113 GLN B C     
3017 O  O     . GLN B 120 ? 0.7597 0.6820 0.6473 -0.1347 0.0657  0.0666  113 GLN B O     
3018 C  CB    . GLN B 120 ? 0.8400 0.6623 0.6755 -0.1319 0.0441  0.0865  113 GLN B CB    
3019 C  CG    . GLN B 120 ? 0.8956 0.7208 0.7237 -0.1537 0.0573  0.0971  113 GLN B CG    
3020 C  CD    . GLN B 120 ? 0.9648 0.7467 0.7603 -0.1596 0.0547  0.1130  113 GLN B CD    
3021 O  OE1   . GLN B 120 ? 0.9676 0.7244 0.7443 -0.1444 0.0441  0.1159  113 GLN B OE1   
3022 N  NE2   . GLN B 120 ? 1.0255 0.7987 0.8143 -0.1819 0.0641  0.1237  113 GLN B NE2   
3023 N  N     . LYS B 121 ? 0.7284 0.6260 0.5915 -0.1072 0.0526  0.0660  114 LYS B N     
3024 C  CA    . LYS B 121 ? 0.7107 0.6398 0.5777 -0.1027 0.0622  0.0615  114 LYS B CA    
3025 C  C     . LYS B 121 ? 0.6608 0.6206 0.5568 -0.0965 0.0627  0.0488  114 LYS B C     
3026 O  O     . LYS B 121 ? 0.6603 0.6504 0.5677 -0.0997 0.0731  0.0452  114 LYS B O     
3027 C  CB    . LYS B 121 ? 0.7058 0.6256 0.5525 -0.0885 0.0578  0.0621  114 LYS B CB    
3028 C  CG    . LYS B 121 ? 0.6897 0.6365 0.5375 -0.0808 0.0654  0.0552  114 LYS B CG    
3029 C  CD    . LYS B 121 ? 0.7187 0.6533 0.5368 -0.0750 0.0649  0.0600  114 LYS B CD    
3030 C  CE    . LYS B 121 ? 0.6909 0.6384 0.5090 -0.0604 0.0630  0.0497  114 LYS B CE    
3031 N  NZ    . LYS B 121 ? 0.6715 0.6505 0.5083 -0.0588 0.0730  0.0405  114 LYS B NZ    
3032 N  N     . HIS B 122 ? 0.6227 0.5761 0.5296 -0.0864 0.0520  0.0420  115 HIS B N     
3033 C  CA    . HIS B 122 ? 0.5772 0.5558 0.5061 -0.0771 0.0511  0.0310  115 HIS B CA    
3034 C  C     . HIS B 122 ? 0.5672 0.5520 0.5161 -0.0825 0.0472  0.0260  115 HIS B C     
3035 O  O     . HIS B 122 ? 0.5350 0.5398 0.5008 -0.0749 0.0457  0.0178  115 HIS B O     
3036 C  CB    . HIS B 122 ? 0.5419 0.5121 0.4675 -0.0605 0.0426  0.0265  115 HIS B CB    
3037 C  CG    . HIS B 122 ? 0.5499 0.5164 0.4579 -0.0541 0.0445  0.0286  115 HIS B CG    
3038 N  ND1   . HIS B 122 ? 0.5479 0.5354 0.4572 -0.0506 0.0525  0.0244  115 HIS B ND1   
3039 C  CD2   . HIS B 122 ? 0.5660 0.5110 0.4539 -0.0504 0.0390  0.0336  115 HIS B CD2   
3040 C  CE1   . HIS B 122 ? 0.5614 0.5393 0.4512 -0.0453 0.0517  0.0261  115 HIS B CE1   
3041 N  NE2   . HIS B 122 ? 0.5735 0.5267 0.4501 -0.0458 0.0436  0.0322  115 HIS B NE2   
3042 N  N     . GLY B 123 ? 0.5994 0.5652 0.5449 -0.0952 0.0448  0.0308  116 GLY B N     
3043 C  CA    . GLY B 123 ? 0.5956 0.5607 0.5561 -0.0996 0.0384  0.0250  116 GLY B CA    
3044 C  C     . GLY B 123 ? 0.5847 0.5855 0.5695 -0.1044 0.0425  0.0175  116 GLY B C     
3045 O  O     . GLY B 123 ? 0.5636 0.5720 0.5616 -0.0995 0.0357  0.0094  116 GLY B O     
3046 N  N     . ARG B 124 ? 0.6015 0.6266 0.5921 -0.1127 0.0534  0.0198  117 ARG B N     
3047 C  CA    . ARG B 124 ? 0.5939 0.6575 0.6096 -0.1153 0.0571  0.0123  117 ARG B CA    
3048 C  C     . ARG B 124 ? 0.5481 0.6286 0.5730 -0.0956 0.0528  0.0037  117 ARG B C     
3049 O  O     . ARG B 124 ? 0.5386 0.6458 0.5839 -0.0940 0.0510  -0.0036 117 ARG B O     
3050 C  CB    . ARG B 124 ? 0.6216 0.7114 0.6414 -0.1249 0.0713  0.0162  117 ARG B CB    
3051 C  CG    . ARG B 124 ? 0.6093 0.7047 0.6163 -0.1114 0.0780  0.0174  117 ARG B CG    
3052 C  CD    . ARG B 124 ? 0.6449 0.7645 0.6521 -0.1208 0.0932  0.0213  117 ARG B CD    
3053 N  NE    . ARG B 124 ? 0.6356 0.7616 0.6304 -0.1060 0.0989  0.0197  117 ARG B NE    
3054 C  CZ    . ARG B 124 ? 0.6373 0.7356 0.6056 -0.0995 0.0971  0.0247  117 ARG B CZ    
3055 N  NH1   . ARG B 124 ? 0.6499 0.7127 0.6008 -0.1059 0.0903  0.0328  117 ARG B NH1   
3056 N  NH2   . ARG B 124 ? 0.6311 0.7369 0.5899 -0.0860 0.1012  0.0210  117 ARG B NH2   
3057 N  N     . ASN B 125 ? 0.5247 0.5893 0.5345 -0.0812 0.0508  0.0051  118 ASN B N     
3058 C  CA    . ASN B 125 ? 0.4886 0.5643 0.5040 -0.0638 0.0477  -0.0013 118 ASN B CA    
3059 C  C     . ASN B 125 ? 0.4641 0.5198 0.4756 -0.0549 0.0370  -0.0035 118 ASN B C     
3060 O  O     . ASN B 125 ? 0.4384 0.4998 0.4526 -0.0417 0.0345  -0.0073 118 ASN B O     
3061 C  CB    . ASN B 125 ? 0.4837 0.5603 0.4877 -0.0542 0.0535  0.0000  118 ASN B CB    
3062 C  CG    . ASN B 125 ? 0.5085 0.6111 0.5180 -0.0598 0.0652  0.0001  118 ASN B CG    
3063 O  OD1   . ASN B 125 ? 0.5145 0.6452 0.5438 -0.0636 0.0680  -0.0040 118 ASN B OD1   
3064 N  ND2   . ASN B 125 ? 0.5271 0.6227 0.5193 -0.0606 0.0721  0.0046  118 ASN B ND2   
3065 N  N     . ILE B 126 ? 0.4768 0.5091 0.4814 -0.0619 0.0315  -0.0010 119 ILE B N     
3066 C  CA    . ILE B 126 ? 0.4596 0.4750 0.4607 -0.0536 0.0224  -0.0039 119 ILE B CA    
3067 C  C     . ILE B 126 ? 0.4704 0.4903 0.4823 -0.0600 0.0171  -0.0095 119 ILE B C     
3068 O  O     . ILE B 126 ? 0.5018 0.5120 0.5132 -0.0738 0.0166  -0.0080 119 ILE B O     
3069 C  CB    . ILE B 126 ? 0.4718 0.4556 0.4555 -0.0537 0.0190  0.0016  119 ILE B CB    
3070 C  CG1   . ILE B 126 ? 0.4702 0.4495 0.4416 -0.0495 0.0233  0.0071  119 ILE B CG1   
3071 C  CG2   . ILE B 126 ? 0.4572 0.4272 0.4390 -0.0440 0.0107  -0.0021 119 ILE B CG2   
3072 C  CD1   . ILE B 126 ? 0.4918 0.4427 0.4459 -0.0507 0.0196  0.0136  119 ILE B CD1   
3073 N  N     . ASP B 127 ? 0.4493 0.4807 0.4687 -0.0502 0.0123  -0.0159 120 ASP B N     
3074 C  CA    . ASP B 127 ? 0.4609 0.4988 0.4893 -0.0545 0.0059  -0.0227 120 ASP B CA    
3075 C  C     . ASP B 127 ? 0.4680 0.4781 0.4848 -0.0521 -0.0010 -0.0245 120 ASP B C     
3076 O  O     . ASP B 127 ? 0.4955 0.4961 0.5132 -0.0614 -0.0058 -0.0283 120 ASP B O     
3077 C  CB    . ASP B 127 ? 0.4419 0.5060 0.4812 -0.0441 0.0040  -0.0281 120 ASP B CB    
3078 C  CG    . ASP B 127 ? 0.4443 0.5377 0.4974 -0.0464 0.0104  -0.0279 120 ASP B CG    
3079 O  OD1   . ASP B 127 ? 0.4687 0.5754 0.5331 -0.0601 0.0118  -0.0295 120 ASP B OD1   
3080 O  OD2   . ASP B 127 ? 0.4262 0.5286 0.4790 -0.0350 0.0143  -0.0265 120 ASP B OD2   
3081 N  N     . ILE B 128 ? 0.4462 0.4451 0.4536 -0.0392 -0.0017 -0.0227 121 ILE B N     
3082 C  CA    . ILE B 128 ? 0.4508 0.4291 0.4490 -0.0330 -0.0075 -0.0255 121 ILE B CA    
3083 C  C     . ILE B 128 ? 0.4430 0.4044 0.4309 -0.0268 -0.0059 -0.0195 121 ILE B C     
3084 O  O     . ILE B 128 ? 0.4202 0.3908 0.4086 -0.0211 -0.0018 -0.0159 121 ILE B O     
3085 C  CB    . ILE B 128 ? 0.4334 0.4242 0.4339 -0.0215 -0.0106 -0.0313 121 ILE B CB    
3086 C  CG1   . ILE B 128 ? 0.4448 0.4540 0.4548 -0.0262 -0.0143 -0.0380 121 ILE B CG1   
3087 C  CG2   . ILE B 128 ? 0.4385 0.4120 0.4294 -0.0131 -0.0147 -0.0345 121 ILE B CG2   
3088 C  CD1   . ILE B 128 ? 0.4281 0.4542 0.4394 -0.0143 -0.0159 -0.0408 121 ILE B CD1   
3089 N  N     . LEU B 129 ? 0.4657 0.4026 0.4446 -0.0271 -0.0102 -0.0194 122 LEU B N     
3090 C  CA    . LEU B 129 ? 0.4628 0.3847 0.4329 -0.0188 -0.0111 -0.0153 122 LEU B CA    
3091 C  C     . LEU B 129 ? 0.4691 0.3811 0.4364 -0.0086 -0.0165 -0.0215 122 LEU B C     
3092 O  O     . LEU B 129 ? 0.4989 0.3953 0.4623 -0.0114 -0.0213 -0.0263 122 LEU B O     
3093 C  CB    . LEU B 129 ? 0.4933 0.3943 0.4537 -0.0272 -0.0113 -0.0082 122 LEU B CB    
3094 C  CG    . LEU B 129 ? 0.4984 0.3832 0.4488 -0.0184 -0.0141 -0.0036 122 LEU B CG    
3095 C  CD1   . LEU B 129 ? 0.4655 0.3673 0.4189 -0.0115 -0.0107 -0.0013 122 LEU B CD1   
3096 C  CD2   . LEU B 129 ? 0.5367 0.3984 0.4740 -0.0265 -0.0149 0.0044  122 LEU B CD2   
3097 N  N     . ALA B 130 ? 0.4440 0.3669 0.4137 0.0027  -0.0152 -0.0222 123 ALA B N     
3098 C  CA    . ALA B 130 ? 0.4496 0.3685 0.4174 0.0138  -0.0182 -0.0278 123 ALA B CA    
3099 C  C     . ALA B 130 ? 0.4565 0.3640 0.4208 0.0214  -0.0202 -0.0246 123 ALA B C     
3100 O  O     . ALA B 130 ? 0.4395 0.3538 0.4059 0.0226  -0.0180 -0.0190 123 ALA B O     
3101 C  CB    . ALA B 130 ? 0.4242 0.3648 0.3975 0.0202  -0.0146 -0.0302 123 ALA B CB    
3102 N  N     . VAL B 131 ? 0.4861 0.3763 0.4451 0.0279  -0.0253 -0.0292 124 VAL B N     
3103 C  CA    . VAL B 131 ? 0.5001 0.3800 0.4565 0.0376  -0.0288 -0.0274 124 VAL B CA    
3104 C  C     . VAL B 131 ? 0.4995 0.3906 0.4608 0.0512  -0.0284 -0.0349 124 VAL B C     
3105 O  O     . VAL B 131 ? 0.5133 0.4023 0.4719 0.0540  -0.0290 -0.0429 124 VAL B O     
3106 C  CB    . VAL B 131 ? 0.5445 0.3924 0.4894 0.0355  -0.0353 -0.0256 124 VAL B CB    
3107 C  CG1   . VAL B 131 ? 0.5613 0.3999 0.5033 0.0472  -0.0402 -0.0228 124 VAL B CG1   
3108 C  CG2   . VAL B 131 ? 0.5525 0.3903 0.4916 0.0198  -0.0340 -0.0181 124 VAL B CG2   
3109 N  N     . SER B 132 ? 0.4850 0.3907 0.4537 0.0590  -0.0269 -0.0327 125 SER B N     
3110 C  CA    . SER B 132 ? 0.4851 0.4069 0.4607 0.0710  -0.0245 -0.0387 125 SER B CA    
3111 C  C     . SER B 132 ? 0.5211 0.4291 0.4946 0.0840  -0.0308 -0.0428 125 SER B C     
3112 O  O     . SER B 132 ? 0.5265 0.4311 0.5020 0.0869  -0.0349 -0.0379 125 SER B O     
3113 C  CB    . SER B 132 ? 0.4558 0.4024 0.4429 0.0710  -0.0194 -0.0343 125 SER B CB    
3114 O  OG    . SER B 132 ? 0.4286 0.3872 0.4170 0.0623  -0.0136 -0.0315 125 SER B OG    
3115 N  N     . CYS B 133 ? 0.5487 0.4490 0.5174 0.0924  -0.0321 -0.0522 126 CYS B N     
3116 C  CA    . CYS B 133 ? 0.5894 0.4754 0.5556 0.1075  -0.0381 -0.0578 126 CYS B CA    
3117 C  C     . CYS B 133 ? 0.6051 0.5024 0.5720 0.1192  -0.0345 -0.0695 126 CYS B C     
3118 O  O     . CYS B 133 ? 0.6152 0.5040 0.5729 0.1154  -0.0339 -0.0758 126 CYS B O     
3119 C  CB    . CYS B 133 ? 0.6285 0.4755 0.5801 0.1042  -0.0466 -0.0572 126 CYS B CB    
3120 S  SG    . CYS B 133 ? 0.6869 0.5098 0.6334 0.1246  -0.0563 -0.0620 126 CYS B SG    
3121 N  N     . ASP B 134 ? 0.6072 0.5273 0.5857 0.1325  -0.0314 -0.0724 127 ASP B N     
3122 C  CA    . ASP B 134 ? 0.6147 0.5564 0.5959 0.1421  -0.0241 -0.0816 127 ASP B CA    
3123 C  C     . ASP B 134 ? 0.6684 0.5915 0.6411 0.1592  -0.0292 -0.0942 127 ASP B C     
3124 O  O     . ASP B 134 ? 0.6850 0.6190 0.6540 0.1674  -0.0239 -0.1041 127 ASP B O     
3125 C  CB    . ASP B 134 ? 0.5951 0.5748 0.5949 0.1469  -0.0163 -0.0788 127 ASP B CB    
3126 C  CG    . ASP B 134 ? 0.5491 0.5437 0.5568 0.1308  -0.0121 -0.0671 127 ASP B CG    
3127 O  OD1   . ASP B 134 ? 0.5278 0.5200 0.5279 0.1189  -0.0086 -0.0640 127 ASP B OD1   
3128 O  OD2   . ASP B 134 ? 0.5391 0.5452 0.5595 0.1308  -0.0139 -0.0618 127 ASP B OD2   
3129 N  N     . SER B 135 ? 0.6997 0.5955 0.6684 0.1658  -0.0391 -0.0938 128 SER B N     
3130 C  CA    . SER B 135 ? 0.7581 0.6327 0.7183 0.1842  -0.0449 -0.1061 128 SER B CA    
3131 C  C     . SER B 135 ? 0.7961 0.6241 0.7424 0.1827  -0.0572 -0.1033 128 SER B C     
3132 O  O     . SER B 135 ? 0.7817 0.6004 0.7287 0.1735  -0.0613 -0.0911 128 SER B O     
3133 C  CB    . SER B 135 ? 0.7732 0.6746 0.7486 0.2045  -0.0427 -0.1110 128 SER B CB    
3134 O  OG    . SER B 135 ? 0.8349 0.7148 0.8018 0.2250  -0.0487 -0.1239 128 SER B OG    
3135 N  N     . PHE B 136 ? 0.8531 0.6497 0.7851 0.1931  -0.0632 -0.1149 129 PHE B N     
3136 C  CA    . PHE B 136 ? 0.9020 0.6504 0.8195 0.1934  -0.0751 -0.1121 129 PHE B CA    
3137 C  C     . PHE B 136 ? 0.9508 0.6904 0.8703 0.2188  -0.0821 -0.1168 129 PHE B C     
3138 O  O     . PHE B 136 ? 1.0052 0.7010 0.9106 0.2240  -0.0929 -0.1155 129 PHE B O     
3139 C  CB    . PHE B 136 ? 0.9379 0.6507 0.8374 0.1840  -0.0790 -0.1202 129 PHE B CB    
3140 C  CG    . PHE B 136 ? 0.8934 0.6136 0.7928 0.1582  -0.0746 -0.1130 129 PHE B CG    
3141 C  CD1   . PHE B 136 ? 0.8871 0.5870 0.7822 0.1402  -0.0780 -0.0996 129 PHE B CD1   
3142 C  CD2   . PHE B 136 ? 0.8610 0.6104 0.7643 0.1532  -0.0666 -0.1192 129 PHE B CD2   
3143 C  CE1   . PHE B 136 ? 0.8484 0.5590 0.7457 0.1180  -0.0734 -0.0938 129 PHE B CE1   
3144 C  CE2   . PHE B 136 ? 0.8227 0.5807 0.7271 0.1316  -0.0634 -0.1127 129 PHE B CE2   
3145 C  CZ    . PHE B 136 ? 0.8159 0.5557 0.7187 0.1144  -0.0667 -0.1006 129 PHE B CZ    
3146 N  N     . ASN B 137 ? 0.9337 0.7161 0.8713 0.2342  -0.0756 -0.1215 130 ASN B N     
3147 C  CA    . ASN B 137 ? 0.9684 0.7561 0.9150 0.2579  -0.0814 -0.1239 130 ASN B CA    
3148 C  C     . ASN B 137 ? 0.9249 0.7417 0.8887 0.2525  -0.0812 -0.1101 130 ASN B C     
3149 O  O     . ASN B 137 ? 0.8761 0.7384 0.8583 0.2473  -0.0712 -0.1085 130 ASN B O     
3150 C  CB    . ASN B 137 ? 0.9875 0.8068 0.9450 0.2797  -0.0744 -0.1396 130 ASN B CB    
3151 C  CG    . ASN B 137 ? 1.0429 0.8582 1.0064 0.3079  -0.0829 -0.1454 130 ASN B CG    
3152 O  OD1   . ASN B 137 ? 1.0271 0.8837 1.0133 0.3181  -0.0802 -0.1436 130 ASN B OD1   
3153 N  ND2   . ASN B 137 ? 1.1114 0.8762 1.0552 0.3202  -0.0940 -0.1520 130 ASN B ND2   
3154 N  N     . GLU B 138 ? 0.9524 0.7425 0.9097 0.2563  -0.0929 -0.1012 131 GLU B N     
3155 C  CA    . GLU B 138 ? 0.9169 0.7292 0.8862 0.2495  -0.0947 -0.0881 131 GLU B CA    
3156 C  C     . GLU B 138 ? 0.9041 0.7683 0.9009 0.2651  -0.0912 -0.0930 131 GLU B C     
3157 O  O     . GLU B 138 ? 0.8589 0.7561 0.8712 0.2548  -0.0878 -0.0854 131 GLU B O     
3158 C  CB    . GLU B 138 ? 0.9592 0.7283 0.9108 0.2510  -0.1085 -0.0775 131 GLU B CB    
3159 C  CG    . GLU B 138 ? 0.9640 0.6891 0.8916 0.2290  -0.1096 -0.0692 131 GLU B CG    
3160 C  CD    . GLU B 138 ? 0.8969 0.6419 0.8283 0.2026  -0.1007 -0.0596 131 GLU B CD    
3161 O  OE1   . GLU B 138 ? 0.8445 0.6353 0.7959 0.2001  -0.0924 -0.0610 131 GLU B OE1   
3162 O  OE2   . GLU B 138 ? 0.9013 0.6163 0.8161 0.1848  -0.1019 -0.0506 131 GLU B OE2   
3163 N  N     . ALA B 139 ? 0.9469 0.8201 0.9508 0.2895  -0.0918 -0.1064 132 ALA B N     
3164 C  CA    . ALA B 139 ? 0.9385 0.8663 0.9716 0.3037  -0.0870 -0.1118 132 ALA B CA    
3165 C  C     . ALA B 139 ? 0.8824 0.8544 0.9305 0.2888  -0.0701 -0.1133 132 ALA B C     
3166 O  O     . ALA B 139 ? 0.8555 0.8750 0.9288 0.2875  -0.0644 -0.1115 132 ALA B O     
3167 C  CB    . ALA B 139 ? 1.0019 0.9300 1.0387 0.3343  -0.0904 -0.1266 132 ALA B CB    
3168 N  N     . THR B 140 ? 0.8707 0.8269 0.9030 0.2776  -0.0624 -0.1169 133 THR B N     
3169 C  CA    . THR B 140 ? 0.8212 0.8124 0.8624 0.2620  -0.0473 -0.1160 133 THR B CA    
3170 C  C     . THR B 140 ? 0.7652 0.7631 0.8105 0.2381  -0.0465 -0.1010 133 THR B C     
3171 O  O     . THR B 140 ? 0.7286 0.7658 0.7918 0.2291  -0.0372 -0.0974 133 THR B O     
3172 C  CB    . THR B 140 ? 0.8265 0.7992 0.8482 0.2568  -0.0410 -0.1234 133 THR B CB    
3173 O  OG1   . THR B 140 ? 0.8845 0.8486 0.9001 0.2799  -0.0422 -0.1390 133 THR B OG1   
3174 C  CG2   . THR B 140 ? 0.7822 0.7910 0.8113 0.2428  -0.0260 -0.1214 133 THR B CG2   
3175 N  N     . ASN B 141 ? 0.7634 0.7223 0.7916 0.2275  -0.0557 -0.0926 134 ASN B N     
3176 C  CA    . ASN B 141 ? 0.7155 0.6786 0.7452 0.2061  -0.0547 -0.0797 134 ASN B CA    
3177 C  C     . ASN B 141 ? 0.7052 0.6989 0.7557 0.2092  -0.0580 -0.0748 134 ASN B C     
3178 O  O     . ASN B 141 ? 0.6634 0.6805 0.7243 0.1940  -0.0526 -0.0683 134 ASN B O     
3179 C  CB    . ASN B 141 ? 0.7223 0.6401 0.7295 0.1948  -0.0628 -0.0718 134 ASN B CB    
3180 C  CG    . ASN B 141 ? 0.7182 0.6144 0.7093 0.1837  -0.0581 -0.0750 134 ASN B CG    
3181 O  OD1   . ASN B 141 ? 0.6879 0.6069 0.6841 0.1766  -0.0477 -0.0780 134 ASN B OD1   
3182 N  ND2   . ASN B 141 ? 0.7548 0.6073 0.7264 0.1828  -0.0661 -0.0746 134 ASN B ND2   
3183 N  N     . ILE B 142 ? 0.7484 0.7400 0.8040 0.2292  -0.0682 -0.0783 135 ILE B N     
3184 C  CA    . ILE B 142 ? 0.7459 0.7691 0.8228 0.2339  -0.0734 -0.0752 135 ILE B CA    
3185 C  C     . ILE B 142 ? 0.7260 0.8033 0.8312 0.2344  -0.0613 -0.0809 135 ILE B C     
3186 O  O     . ILE B 142 ? 0.6971 0.8044 0.8197 0.2229  -0.0594 -0.0757 135 ILE B O     
3187 C  CB    . ILE B 142 ? 0.8033 0.8109 0.8781 0.2574  -0.0885 -0.0776 135 ILE B CB    
3188 C  CG1   . ILE B 142 ? 0.8214 0.7780 0.8684 0.2516  -0.1003 -0.0673 135 ILE B CG1   
3189 C  CG2   . ILE B 142 ? 0.8066 0.8593 0.9102 0.2665  -0.0930 -0.0785 135 ILE B CG2   
3190 C  CD1   . ILE B 142 ? 0.8900 0.8128 0.9239 0.2745  -0.1144 -0.0695 135 ILE B CD1   
3191 N  N     . LYS B 143 ? 0.7446 0.8335 0.8531 0.2462  -0.0527 -0.0915 136 LYS B N     
3192 C  CA    . LYS B 143 ? 0.7335 0.8742 0.8673 0.2466  -0.0395 -0.0963 136 LYS B CA    
3193 C  C     . LYS B 143 ? 0.6815 0.8340 0.8156 0.2207  -0.0279 -0.0883 136 LYS B C     
3194 O  O     . LYS B 143 ? 0.6645 0.8575 0.8214 0.2127  -0.0203 -0.0861 136 LYS B O     
3195 C  CB    . LYS B 143 ? 0.7690 0.9180 0.9019 0.2648  -0.0315 -0.1096 136 LYS B CB    
3196 C  CG    . LYS B 143 ? 0.7618 0.9650 0.9182 0.2637  -0.0150 -0.1138 136 LYS B CG    
3197 C  CD    . LYS B 143 ? 0.7590 1.0100 0.9499 0.2637  -0.0159 -0.1114 136 LYS B CD    
3198 C  CE    . LYS B 143 ? 0.7337 1.0302 0.9442 0.2471  0.0010  -0.1081 136 LYS B CE    
3199 N  NZ    . LYS B 143 ? 0.7133 1.0378 0.9488 0.2334  -0.0029 -0.1005 136 LYS B NZ    
3200 N  N     . ILE B 144 ? 0.6620 0.7789 0.7712 0.2083  -0.0267 -0.0842 137 ILE B N     
3201 C  CA    . ILE B 144 ? 0.6180 0.7413 0.7244 0.1861  -0.0168 -0.0768 137 ILE B CA    
3202 C  C     . ILE B 144 ? 0.5903 0.7195 0.7059 0.1718  -0.0220 -0.0670 137 ILE B C     
3203 O  O     . ILE B 144 ? 0.5630 0.7137 0.6888 0.1569  -0.0138 -0.0620 137 ILE B O     
3204 C  CB    . ILE B 144 ? 0.6086 0.6938 0.6877 0.1781  -0.0163 -0.0758 137 ILE B CB    
3205 C  CG1   . ILE B 144 ? 0.6320 0.7173 0.7019 0.1880  -0.0087 -0.0860 137 ILE B CG1   
3206 C  CG2   . ILE B 144 ? 0.5640 0.6482 0.6390 0.1558  -0.0112 -0.0659 137 ILE B CG2   
3207 C  CD1   . ILE B 144 ? 0.6399 0.6831 0.6836 0.1849  -0.0136 -0.0881 137 ILE B CD1   
3208 N  N     . GLY B 145 ? 0.6038 0.7118 0.7138 0.1768  -0.0359 -0.0644 138 GLY B N     
3209 C  CA    . GLY B 145 ? 0.5872 0.6989 0.7031 0.1662  -0.0431 -0.0567 138 GLY B CA    
3210 C  C     . GLY B 145 ? 0.5671 0.6417 0.6591 0.1521  -0.0469 -0.0485 138 GLY B C     
3211 O  O     . GLY B 145 ? 0.5516 0.6281 0.6450 0.1414  -0.0511 -0.0424 138 GLY B O     
3212 N  N     . ARG B 146 ? 0.5732 0.6154 0.6441 0.1527  -0.0462 -0.0492 139 ARG B N     
3213 C  CA    . ARG B 146 ? 0.5638 0.5712 0.6128 0.1411  -0.0501 -0.0421 139 ARG B CA    
3214 C  C     . ARG B 146 ? 0.6040 0.5788 0.6377 0.1514  -0.0625 -0.0407 139 ARG B C     
3215 O  O     . ARG B 146 ? 0.6052 0.5518 0.6208 0.1421  -0.0666 -0.0335 139 ARG B O     
3216 C  CB    . ARG B 146 ? 0.5507 0.5435 0.5868 0.1335  -0.0419 -0.0439 139 ARG B CB    
3217 C  CG    . ARG B 146 ? 0.5315 0.5007 0.5515 0.1173  -0.0423 -0.0364 139 ARG B CG    
3218 C  CD    . ARG B 146 ? 0.5245 0.4810 0.5335 0.1110  -0.0364 -0.0390 139 ARG B CD    
3219 N  NE    . ARG B 146 ? 0.5065 0.4876 0.5242 0.1105  -0.0263 -0.0434 139 ARG B NE    
3220 C  CZ    . ARG B 146 ? 0.4743 0.4669 0.4935 0.0982  -0.0191 -0.0394 139 ARG B CZ    
3221 N  NH1   . ARG B 146 ? 0.4534 0.4416 0.4708 0.0868  -0.0203 -0.0320 139 ARG B NH1   
3222 N  NH2   . ARG B 146 ? 0.4680 0.4754 0.4890 0.0985  -0.0108 -0.0428 139 ARG B NH2   
3223 N  N     . GLY B 147 ? 0.6420 0.6192 0.6816 0.1710  -0.0675 -0.0476 140 GLY B N     
3224 C  CA    . GLY B 147 ? 0.6910 0.6312 0.7134 0.1834  -0.0787 -0.0474 140 GLY B CA    
3225 C  C     . GLY B 147 ? 0.7129 0.6471 0.7328 0.1884  -0.0915 -0.0402 140 GLY B C     
3226 O  O     . GLY B 147 ? 0.7074 0.6749 0.7469 0.1937  -0.0942 -0.0414 140 GLY B O     
3227 N  N     . SER B 148 ? 0.7392 0.6316 0.7341 0.1849  -0.0988 -0.0325 141 SER B N     
3228 C  CA    . SER B 148 ? 0.7802 0.6541 0.7638 0.1937  -0.1128 -0.0254 141 SER B CA    
3229 C  C     . SER B 148 ? 0.8440 0.6767 0.8100 0.2097  -0.1216 -0.0266 141 SER B C     
3230 O  O     . SER B 148 ? 0.8900 0.6972 0.8404 0.2179  -0.1339 -0.0193 141 SER B O     
3231 C  CB    . SER B 148 ? 0.7663 0.6224 0.7314 0.1749  -0.1129 -0.0137 141 SER B CB    
3232 O  OG    . SER B 148 ? 0.7700 0.5924 0.7162 0.1631  -0.1074 -0.0110 141 SER B OG    
3233 N  N     . GLY B 149 ? 0.8514 0.6731 0.8163 0.2129  -0.1156 -0.0353 142 GLY B N     
3234 C  CA    . GLY B 149 ? 0.9155 0.6925 0.8617 0.2259  -0.1233 -0.0378 142 GLY B CA    
3235 C  C     . GLY B 149 ? 0.9322 0.6617 0.8511 0.2081  -0.1231 -0.0295 142 GLY B C     
3236 O  O     . GLY B 149 ? 0.9899 0.6768 0.8913 0.2154  -0.1293 -0.0310 142 GLY B O     
3237 N  N     . ASP B 150 ? 0.8868 0.6232 0.8023 0.1847  -0.1159 -0.0210 143 ASP B N     
3238 C  CA    . ASP B 150 ? 0.9023 0.6003 0.7950 0.1661  -0.1144 -0.0124 143 ASP B CA    
3239 C  C     . ASP B 150 ? 0.8490 0.5630 0.7485 0.1460  -0.1014 -0.0158 143 ASP B C     
3240 O  O     . ASP B 150 ? 0.8537 0.5453 0.7391 0.1280  -0.0985 -0.0091 143 ASP B O     
3241 C  CB    . ASP B 150 ? 0.9149 0.5991 0.7913 0.1573  -0.1192 0.0028  143 ASP B CB    
3242 C  CG    . ASP B 150 ? 0.9898 0.6376 0.8471 0.1734  -0.1337 0.0098  143 ASP B CG    
3243 O  OD1   . ASP B 150 ? 1.0473 0.6499 0.8863 0.1753  -0.1381 0.0110  143 ASP B OD1   
3244 O  OD2   . ASP B 150 ? 0.9947 0.6584 0.8549 0.1840  -0.1414 0.0141  143 ASP B OD2   
3245 N  N     . ASN B 151 ? 0.8058 0.5572 0.7259 0.1495  -0.0939 -0.0260 144 ASN B N     
3246 C  CA    . ASN B 151 ? 0.7570 0.5258 0.6832 0.1324  -0.0825 -0.0286 144 ASN B CA    
3247 C  C     . ASN B 151 ? 0.7847 0.5208 0.6968 0.1235  -0.0820 -0.0319 144 ASN B C     
3248 O  O     . ASN B 151 ? 0.7646 0.4978 0.6723 0.1042  -0.0768 -0.0273 144 ASN B O     
3249 C  CB    . ASN B 151 ? 0.7201 0.5297 0.6674 0.1400  -0.0751 -0.0386 144 ASN B CB    
3250 C  CG    . ASN B 151 ? 0.6896 0.5343 0.6533 0.1433  -0.0744 -0.0351 144 ASN B CG    
3251 O  OD1   . ASN B 151 ? 0.7154 0.5580 0.6799 0.1548  -0.0831 -0.0322 144 ASN B OD1   
3252 N  ND2   . ASN B 151 ? 0.6390 0.5146 0.6152 0.1327  -0.0649 -0.0350 144 ASN B ND2   
3253 N  N     . VAL B 152 ? 0.8359 0.5473 0.7412 0.1375  -0.0881 -0.0404 145 VAL B N     
3254 C  CA    . VAL B 152 ? 0.8670 0.5483 0.7603 0.1294  -0.0886 -0.0463 145 VAL B CA    
3255 C  C     . VAL B 152 ? 0.9030 0.5445 0.7775 0.1133  -0.0928 -0.0346 145 VAL B C     
3256 O  O     . VAL B 152 ? 0.8992 0.5321 0.7696 0.0943  -0.0889 -0.0340 145 VAL B O     
3257 C  CB    . VAL B 152 ? 0.9177 0.5816 0.8074 0.1495  -0.0941 -0.0603 145 VAL B CB    
3258 C  CG1   . VAL B 152 ? 0.9593 0.5862 0.8342 0.1393  -0.0966 -0.0666 145 VAL B CG1   
3259 C  CG2   . VAL B 152 ? 0.8846 0.5912 0.7923 0.1632  -0.0874 -0.0720 145 VAL B CG2   
3260 N  N     . GLN B 153 ? 0.9425 0.5605 0.8054 0.1207  -0.1008 -0.0248 146 GLN B N     
3261 C  CA    . GLN B 153 ? 0.9835 0.5632 0.8260 0.1053  -0.1039 -0.0115 146 GLN B CA    
3262 C  C     . GLN B 153 ? 0.9324 0.5353 0.7790 0.0825  -0.0942 -0.0024 146 GLN B C     
3263 O  O     . GLN B 153 ? 0.9472 0.5325 0.7851 0.0623  -0.0907 0.0025  146 GLN B O     
3264 C  CB    . GLN B 153 ? 1.0335 0.5892 0.8623 0.1205  -0.1145 -0.0019 146 GLN B CB    
3265 C  CG    . GLN B 153 ? 1.0855 0.5990 0.8894 0.1053  -0.1175 0.0140  146 GLN B CG    
3266 C  CD    . GLN B 153 ? 1.1484 0.6316 0.9343 0.1224  -0.1298 0.0234  146 GLN B CD    
3267 O  OE1   . GLN B 153 ? 1.1592 0.6505 0.9522 0.1473  -0.1376 0.0169  146 GLN B OE1   
3268 N  NE2   . GLN B 153 ? 1.1946 0.6436 0.9566 0.1091  -0.1315 0.0396  146 GLN B NE2   
3269 N  N     . LYS B 154 ? 0.8743 0.5186 0.7354 0.0856  -0.0895 -0.0012 147 LYS B N     
3270 C  CA    . LYS B 154 ? 0.8287 0.4953 0.6933 0.0670  -0.0806 0.0062  147 LYS B CA    
3271 C  C     . LYS B 154 ? 0.7961 0.4779 0.6710 0.0532  -0.0723 -0.0013 147 LYS B C     
3272 O  O     . LYS B 154 ? 0.7856 0.4697 0.6582 0.0347  -0.0663 0.0046  147 LYS B O     
3273 C  CB    . LYS B 154 ? 0.7821 0.4855 0.6588 0.0745  -0.0789 0.0079  147 LYS B CB    
3274 C  CG    . LYS B 154 ? 0.7455 0.4674 0.6222 0.0582  -0.0712 0.0158  147 LYS B CG    
3275 C  CD    . LYS B 154 ? 0.7855 0.4794 0.6404 0.0448  -0.0714 0.0290  147 LYS B CD    
3276 C  CE    . LYS B 154 ? 0.7518 0.4665 0.6073 0.0290  -0.0619 0.0347  147 LYS B CE    
3277 N  NZ    . LYS B 154 ? 0.7180 0.4600 0.5798 0.0363  -0.0623 0.0350  147 LYS B NZ    
3278 N  N     . LEU B 155 ? 0.7838 0.4776 0.6696 0.0629  -0.0720 -0.0144 148 LEU B N     
3279 C  CA    . LEU B 155 ? 0.7567 0.4660 0.6510 0.0519  -0.0657 -0.0222 148 LEU B CA    
3280 C  C     . LEU B 155 ? 0.7994 0.4775 0.6826 0.0353  -0.0674 -0.0211 148 LEU B C     
3281 O  O     . LEU B 155 ? 0.7790 0.4695 0.6668 0.0179  -0.0615 -0.0190 148 LEU B O     
3282 C  CB    . LEU B 155 ? 0.7479 0.4722 0.6514 0.0672  -0.0659 -0.0362 148 LEU B CB    
3283 C  CG    . LEU B 155 ? 0.7313 0.4684 0.6399 0.0590  -0.0616 -0.0457 148 LEU B CG    
3284 C  CD1   . LEU B 155 ? 0.6719 0.4445 0.5923 0.0480  -0.0529 -0.0413 148 LEU B CD1   
3285 C  CD2   . LEU B 155 ? 0.7369 0.4837 0.6493 0.0762  -0.0622 -0.0591 148 LEU B CD2   
3286 N  N     . TYR B 156 ? 0.8640 0.5010 0.7330 0.0404  -0.0758 -0.0226 149 TYR B N     
3287 C  CA    . TYR B 156 ? 0.9160 0.5180 0.7733 0.0231  -0.0782 -0.0208 149 TYR B CA    
3288 C  C     . TYR B 156 ? 0.9180 0.5170 0.7696 0.0032  -0.0732 -0.0053 149 TYR B C     
3289 O  O     . TYR B 156 ? 0.9269 0.5241 0.7801 -0.0171 -0.0693 -0.0042 149 TYR B O     
3290 C  CB    . TYR B 156 ? 0.9927 0.5459 0.8331 0.0347  -0.0889 -0.0233 149 TYR B CB    
3291 C  CG    . TYR B 156 ? 1.0114 0.5585 0.8542 0.0466  -0.0934 -0.0415 149 TYR B CG    
3292 C  CD1   . TYR B 156 ? 0.9848 0.5566 0.8368 0.0697  -0.0934 -0.0514 149 TYR B CD1   
3293 C  CD2   . TYR B 156 ? 1.0558 0.5764 0.8923 0.0338  -0.0967 -0.0495 149 TYR B CD2   
3294 C  CE1   . TYR B 156 ? 1.0047 0.5734 0.8572 0.0814  -0.0961 -0.0684 149 TYR B CE1   
3295 C  CE2   . TYR B 156 ? 1.0762 0.5918 0.9127 0.0451  -0.1010 -0.0675 149 TYR B CE2   
3296 C  CZ    . TYR B 156 ? 1.0515 0.5907 0.8948 0.0698  -0.1004 -0.0769 149 TYR B CZ    
3297 O  OH    . TYR B 156 ? 1.0736 0.6107 0.9153 0.0827  -0.1033 -0.0949 149 TYR B OH    
3298 N  N     . GLU B 157 ? 0.9136 0.5137 0.7584 0.0092  -0.0732 0.0063  150 GLU B N     
3299 C  CA    . GLU B 157 ? 0.9229 0.5192 0.7586 -0.0076 -0.0679 0.0212  150 GLU B CA    
3300 C  C     . GLU B 157 ? 0.8621 0.5009 0.7143 -0.0212 -0.0570 0.0200  150 GLU B C     
3301 O  O     . GLU B 157 ? 0.8741 0.5127 0.7246 -0.0412 -0.0508 0.0266  150 GLU B O     
3302 C  CB    . GLU B 157 ? 0.9300 0.5220 0.7542 0.0049  -0.0716 0.0317  150 GLU B CB    
3303 C  CG    . GLU B 157 ? 0.9596 0.5382 0.7666 -0.0101 -0.0676 0.0481  150 GLU B CG    
3304 C  CD    . GLU B 157 ? 0.9674 0.5447 0.7616 0.0029  -0.0722 0.0577  150 GLU B CD    
3305 O  OE1   . GLU B 157 ? 0.9304 0.5307 0.7359 0.0210  -0.0761 0.0510  150 GLU B OE1   
3306 O  OE2   . GLU B 157 ? 1.0140 0.5681 0.7867 -0.0057 -0.0719 0.0720  150 GLU B OE2   
3307 N  N     . ILE B 158 ? 0.8010 0.4765 0.6694 -0.0098 -0.0545 0.0122  151 ILE B N     
3308 C  CA    . ILE B 158 ? 0.7470 0.4607 0.6299 -0.0196 -0.0451 0.0113  151 ILE B CA    
3309 C  C     . ILE B 158 ? 0.7521 0.4695 0.6436 -0.0338 -0.0429 0.0041  151 ILE B C     
3310 O  O     . ILE B 158 ? 0.7394 0.4744 0.6374 -0.0491 -0.0358 0.0072  151 ILE B O     
3311 C  CB    . ILE B 158 ? 0.6880 0.4361 0.5850 -0.0051 -0.0432 0.0051  151 ILE B CB    
3312 C  CG1   . ILE B 158 ? 0.6825 0.4324 0.5736 0.0052  -0.0452 0.0123  151 ILE B CG1   
3313 C  CG2   . ILE B 158 ? 0.6414 0.4235 0.5525 -0.0145 -0.0347 0.0026  151 ILE B CG2   
3314 C  CD1   . ILE B 158 ? 0.6369 0.4156 0.5417 0.0195  -0.0450 0.0062  151 ILE B CD1   
3315 N  N     . GLY B 159 ? 0.7734 0.4759 0.6651 -0.0276 -0.0493 -0.0065 152 GLY B N     
3316 C  CA    . GLY B 159 ? 0.7870 0.4901 0.6853 -0.0404 -0.0497 -0.0151 152 GLY B CA    
3317 C  C     . GLY B 159 ? 0.8347 0.5171 0.7268 -0.0633 -0.0481 -0.0071 152 GLY B C     
3318 O  O     . GLY B 159 ? 0.8266 0.5289 0.7304 -0.0795 -0.0436 -0.0089 152 GLY B O     
3319 N  N     . SER B 160 ? 0.8896 0.5323 0.7634 -0.0647 -0.0520 0.0021  153 SER B N     
3320 C  CA    . SER B 160 ? 0.9426 0.5631 0.8082 -0.0877 -0.0493 0.0121  153 SER B CA    
3321 C  C     . SER B 160 ? 0.9119 0.5639 0.7837 -0.1000 -0.0377 0.0226  153 SER B C     
3322 O  O     . SER B 160 ? 0.9346 0.5910 0.8109 -0.1218 -0.0319 0.0266  153 SER B O     
3323 C  CB    . SER B 160 ? 1.0122 0.5813 0.8538 -0.0849 -0.0559 0.0215  153 SER B CB    
3324 O  OG    . SER B 160 ? 0.9958 0.5678 0.8275 -0.0711 -0.0550 0.0318  153 SER B OG    
3325 N  N     . TRP B 161 ? 0.8656 0.5394 0.7373 -0.0864 -0.0343 0.0268  154 TRP B N     
3326 C  CA    . TRP B 161 ? 0.8374 0.5417 0.7141 -0.0956 -0.0235 0.0344  154 TRP B CA    
3327 C  C     . TRP B 161 ? 0.7965 0.5412 0.6966 -0.1039 -0.0175 0.0255  154 TRP B C     
3328 O  O     . TRP B 161 ? 0.7994 0.5634 0.7058 -0.1195 -0.0085 0.0305  154 TRP B O     
3329 C  CB    . TRP B 161 ? 0.7984 0.5165 0.6705 -0.0781 -0.0229 0.0380  154 TRP B CB    
3330 C  CG    . TRP B 161 ? 0.8413 0.5260 0.6899 -0.0712 -0.0280 0.0490  154 TRP B CG    
3331 C  CD1   . TRP B 161 ? 0.9121 0.5567 0.7410 -0.0811 -0.0305 0.0592  154 TRP B CD1   
3332 C  CD2   . TRP B 161 ? 0.8217 0.5099 0.6634 -0.0529 -0.0321 0.0514  154 TRP B CD2   
3333 N  NE1   . TRP B 161 ? 0.9379 0.5606 0.7469 -0.0686 -0.0364 0.0681  154 TRP B NE1   
3334 C  CE2   . TRP B 161 ? 0.8826 0.5331 0.7000 -0.0512 -0.0378 0.0629  154 TRP B CE2   
3335 C  CE3   . TRP B 161 ? 0.7636 0.4824 0.6172 -0.0384 -0.0321 0.0451  154 TRP B CE3   
3336 C  CZ2   . TRP B 161 ? 0.8850 0.5310 0.6909 -0.0348 -0.0441 0.0675  154 TRP B CZ2   
3337 C  CZ3   . TRP B 161 ? 0.7659 0.4803 0.6096 -0.0242 -0.0378 0.0493  154 TRP B CZ3   
3338 C  CH2   . TRP B 161 ? 0.8247 0.5048 0.6454 -0.0219 -0.0441 0.0599  154 TRP B CH2   
3339 N  N     . CYS B 162 ? 0.7595 0.5196 0.6722 -0.0920 -0.0221 0.0127  155 CYS B N     
3340 C  CA    . CYS B 162 ? 0.7217 0.5200 0.6548 -0.0963 -0.0181 0.0045  155 CYS B CA    
3341 C  C     . CYS B 162 ? 0.7624 0.5582 0.7031 -0.1178 -0.0179 0.0020  155 CYS B C     
3342 O  O     . CYS B 162 ? 0.7505 0.5774 0.7064 -0.1292 -0.0114 0.0015  155 CYS B O     
3343 C  CB    . CYS B 162 ? 0.6849 0.4959 0.6258 -0.0797 -0.0235 -0.0076 155 CYS B CB    
3344 S  SG    . CYS B 162 ? 0.6312 0.4571 0.5705 -0.0577 -0.0219 -0.0058 155 CYS B SG    
3345 N  N     . GLN B 163 ? 0.8170 0.5743 0.7468 -0.1238 -0.0251 0.0009  156 GLN B N     
3346 C  CA    . GLN B 163 ? 0.8645 0.6152 0.8012 -0.1463 -0.0261 -0.0017 156 GLN B CA    
3347 C  C     . GLN B 163 ? 0.8887 0.6466 0.8257 -0.1664 -0.0153 0.0117  156 GLN B C     
3348 O  O     . GLN B 163 ? 0.8889 0.6768 0.8442 -0.1825 -0.0099 0.0095  156 GLN B O     
3349 C  CB    . GLN B 163 ? 0.9219 0.6243 0.8439 -0.1457 -0.0371 -0.0064 156 GLN B CB    
3350 C  CG    . GLN B 163 ? 0.9681 0.6634 0.8990 -0.1654 -0.0421 -0.0156 156 GLN B CG    
3351 C  CD    . GLN B 163 ? 1.0120 0.7062 0.9465 -0.1934 -0.0345 -0.0046 156 GLN B CD    
3352 O  OE1   . GLN B 163 ? 1.0351 0.7108 0.9550 -0.1978 -0.0284 0.0107  156 GLN B OE1   
3353 N  NE2   . GLN B 163 ? 1.0240 0.7421 0.9786 -0.2122 -0.0343 -0.0120 156 GLN B NE2   
3354 N  N     . LYS B 164 ? 0.9090 0.6431 0.8260 -0.1642 -0.0120 0.0254  157 LYS B N     
3355 C  CA    . LYS B 164 ? 0.9414 0.6769 0.8522 -0.1818 -0.0011 0.0398  157 LYS B CA    
3356 C  C     . LYS B 164 ? 0.8934 0.6805 0.8208 -0.1830 0.0104  0.0403  157 LYS B C     
3357 O  O     . LYS B 164 ? 0.9186 0.7235 0.8541 -0.2027 0.0203  0.0457  157 LYS B O     
3358 C  CB    . LYS B 164 ? 0.9668 0.6672 0.8495 -0.1724 -0.0022 0.0531  157 LYS B CB    
3359 C  CG    . LYS B 164 ? 1.0207 0.7085 0.8874 -0.1903 0.0074  0.0704  157 LYS B CG    
3360 C  CD    . LYS B 164 ? 1.0535 0.7005 0.8897 -0.1781 0.0023  0.0822  157 LYS B CD    
3361 C  CE    . LYS B 164 ? 1.1325 0.7485 0.9450 -0.1967 0.0083  0.1006  157 LYS B CE    
3362 N  NZ    . LYS B 164 ? 1.1640 0.7405 0.9460 -0.1807 0.0007  0.1112  157 LYS B NZ    
3363 N  N     . TYR B 165 ? 0.8290 0.6395 0.7610 -0.1616 0.0098  0.0347  158 TYR B N     
3364 C  CA    . TYR B 165 ? 0.7872 0.6404 0.7307 -0.1586 0.0200  0.0352  158 TYR B CA    
3365 C  C     . TYR B 165 ? 0.7430 0.6351 0.7123 -0.1542 0.0188  0.0219  158 TYR B C     
3366 O  O     . TYR B 165 ? 0.7025 0.6280 0.6814 -0.1458 0.0248  0.0200  158 TYR B O     
3367 C  CB    . TYR B 165 ? 0.7579 0.6054 0.6853 -0.1394 0.0199  0.0400  158 TYR B CB    
3368 C  CG    . TYR B 165 ? 0.8082 0.6212 0.7091 -0.1442 0.0212  0.0543  158 TYR B CG    
3369 C  CD1   . TYR B 165 ? 0.8446 0.6638 0.7385 -0.1603 0.0327  0.0650  158 TYR B CD1   
3370 C  CD2   . TYR B 165 ? 0.8276 0.6017 0.7099 -0.1332 0.0110  0.0572  158 TYR B CD2   
3371 C  CE1   . TYR B 165 ? 0.8992 0.6850 0.7658 -0.1656 0.0339  0.0794  158 TYR B CE1   
3372 C  CE2   . TYR B 165 ? 0.8809 0.6219 0.7373 -0.1369 0.0110  0.0711  158 TYR B CE2   
3373 C  CZ    . TYR B 165 ? 0.9188 0.6638 0.7660 -0.1540 0.0224  0.0827  158 TYR B CZ    
3374 O  OH    . TYR B 165 ? 0.9777 0.6895 0.7961 -0.1581 0.0229  0.0979  158 TYR B OH    
3375 N  N     . ASP B 166 ? 0.7559 0.6422 0.7348 -0.1593 0.0105  0.0126  159 ASP B N     
3376 C  CA    . ASP B 166 ? 0.7264 0.6486 0.7284 -0.1574 0.0081  0.0004  159 ASP B CA    
3377 C  C     . ASP B 166 ? 0.6651 0.6062 0.6695 -0.1338 0.0065  -0.0047 159 ASP B C     
3378 O  O     . ASP B 166 ? 0.6353 0.6130 0.6546 -0.1299 0.0113  -0.0076 159 ASP B O     
3379 C  CB    . ASP B 166 ? 0.7401 0.6990 0.7618 -0.1747 0.0175  0.0016  159 ASP B CB    
3380 C  CG    . ASP B 166 ? 0.7176 0.7147 0.7642 -0.1727 0.0134  -0.0109 159 ASP B CG    
3381 O  OD1   . ASP B 166 ? 0.7212 0.7073 0.7691 -0.1700 0.0021  -0.0205 159 ASP B OD1   
3382 O  OD2   . ASP B 166 ? 0.7004 0.7381 0.7638 -0.1728 0.0211  -0.0115 159 ASP B OD2   
3383 N  N     . ILE B 167 ? 0.6524 0.5684 0.6434 -0.1188 -0.0007 -0.0067 160 ILE B N     
3384 C  CA    . ILE B 167 ? 0.6025 0.5318 0.5950 -0.0982 -0.0032 -0.0119 160 ILE B CA    
3385 C  C     . ILE B 167 ? 0.6070 0.5233 0.5982 -0.0913 -0.0132 -0.0219 160 ILE B C     
3386 O  O     . ILE B 167 ? 0.6425 0.5263 0.6223 -0.0942 -0.0188 -0.0224 160 ILE B O     
3387 C  CB    . ILE B 167 ? 0.5859 0.5006 0.5633 -0.0862 -0.0009 -0.0042 160 ILE B CB    
3388 C  CG1   . ILE B 167 ? 0.5871 0.5132 0.5623 -0.0922 0.0088  0.0048  160 ILE B CG1   
3389 C  CG2   . ILE B 167 ? 0.5409 0.4668 0.5204 -0.0672 -0.0034 -0.0092 160 ILE B CG2   
3390 C  CD1   . ILE B 167 ? 0.5908 0.4951 0.5470 -0.0849 0.0092  0.0132  160 ILE B CD1   
3391 N  N     . LYS B 168 ? 0.5748 0.5137 0.5744 -0.0802 -0.0157 -0.0296 161 LYS B N     
3392 C  CA    . LYS B 168 ? 0.5779 0.5071 0.5732 -0.0708 -0.0241 -0.0392 161 LYS B CA    
3393 C  C     . LYS B 168 ? 0.5668 0.4750 0.5482 -0.0555 -0.0252 -0.0370 161 LYS B C     
3394 O  O     . LYS B 168 ? 0.5341 0.4515 0.5147 -0.0464 -0.0202 -0.0311 161 LYS B O     
3395 C  CB    . LYS B 168 ? 0.5520 0.5137 0.5588 -0.0641 -0.0254 -0.0462 161 LYS B CB    
3396 C  CG    . LYS B 168 ? 0.5653 0.5526 0.5890 -0.0782 -0.0250 -0.0489 161 LYS B CG    
3397 C  CD    . LYS B 168 ? 0.5385 0.5609 0.5738 -0.0691 -0.0257 -0.0532 161 LYS B CD    
3398 C  CE    . LYS B 168 ? 0.5425 0.5660 0.5732 -0.0597 -0.0347 -0.0631 161 LYS B CE    
3399 N  NZ    . LYS B 168 ? 0.5858 0.6025 0.6195 -0.0729 -0.0432 -0.0725 161 LYS B NZ    
3400 N  N     . PHE B 169 ? 0.5985 0.4790 0.5698 -0.0527 -0.0320 -0.0424 162 PHE B N     
3401 C  CA    . PHE B 169 ? 0.5995 0.4592 0.5590 -0.0385 -0.0340 -0.0413 162 PHE B CA    
3402 C  C     . PHE B 169 ? 0.5839 0.4534 0.5429 -0.0230 -0.0367 -0.0507 162 PHE B C     
3403 O  O     . PHE B 169 ? 0.6067 0.4729 0.5641 -0.0235 -0.0423 -0.0611 162 PHE B O     
3404 C  CB    . PHE B 169 ? 0.6538 0.4743 0.6014 -0.0444 -0.0394 -0.0407 162 PHE B CB    
3405 C  CG    . PHE B 169 ? 0.6665 0.4633 0.6022 -0.0285 -0.0432 -0.0408 162 PHE B CG    
3406 C  CD1   . PHE B 169 ? 0.6410 0.4425 0.5749 -0.0186 -0.0399 -0.0326 162 PHE B CD1   
3407 C  CD2   . PHE B 169 ? 0.7104 0.4795 0.6370 -0.0235 -0.0509 -0.0497 162 PHE B CD2   
3408 C  CE1   . PHE B 169 ? 0.6549 0.4392 0.5809 -0.0032 -0.0440 -0.0334 162 PHE B CE1   
3409 C  CE2   . PHE B 169 ? 0.7263 0.4758 0.6436 -0.0070 -0.0545 -0.0505 162 PHE B CE2   
3410 C  CZ    . PHE B 169 ? 0.6979 0.4566 0.6159 0.0031  -0.0511 -0.0421 162 PHE B CZ    
3411 N  N     . LYS B 170 ? 0.5505 0.4308 0.5096 -0.0098 -0.0328 -0.0471 163 LYS B N     
3412 C  CA    . LYS B 170 ? 0.5340 0.4277 0.4927 0.0042  -0.0326 -0.0533 163 LYS B CA    
3413 C  C     . LYS B 170 ? 0.5374 0.4192 0.4907 0.0173  -0.0326 -0.0523 163 LYS B C     
3414 O  O     . LYS B 170 ? 0.5323 0.4069 0.4852 0.0172  -0.0313 -0.0442 163 LYS B O     
3415 C  CB    . LYS B 170 ? 0.4931 0.4167 0.4603 0.0052  -0.0269 -0.0493 163 LYS B CB    
3416 C  CG    . LYS B 170 ? 0.4742 0.4133 0.4404 0.0183  -0.0242 -0.0516 163 LYS B CG    
3417 C  CD    . LYS B 170 ? 0.4438 0.4066 0.4166 0.0178  -0.0197 -0.0469 163 LYS B CD    
3418 C  CE    . LYS B 170 ? 0.4261 0.4010 0.3973 0.0288  -0.0153 -0.0448 163 LYS B CE    
3419 N  NZ    . LYS B 170 ? 0.4002 0.3902 0.3767 0.0282  -0.0107 -0.0377 163 LYS B NZ    
3420 N  N     . LEU B 171 ? 0.5515 0.4323 0.5002 0.0289  -0.0347 -0.0614 164 LEU B N     
3421 C  CA    . LEU B 171 ? 0.5552 0.4329 0.5020 0.0436  -0.0340 -0.0623 164 LEU B CA    
3422 C  C     . LEU B 171 ? 0.5285 0.4336 0.4795 0.0531  -0.0278 -0.0637 164 LEU B C     
3423 O  O     . LEU B 171 ? 0.5320 0.4476 0.4797 0.0547  -0.0273 -0.0701 164 LEU B O     
3424 C  CB    . LEU B 171 ? 0.6059 0.4566 0.5425 0.0497  -0.0410 -0.0724 164 LEU B CB    
3425 C  CG    . LEU B 171 ? 0.6214 0.4691 0.5562 0.0678  -0.0412 -0.0767 164 LEU B CG    
3426 C  CD1   . LEU B 171 ? 0.6166 0.4581 0.5550 0.0716  -0.0417 -0.0674 164 LEU B CD1   
3427 C  CD2   . LEU B 171 ? 0.6765 0.4973 0.5997 0.0748  -0.0482 -0.0891 164 LEU B CD2   
3428 N  N     . ASN B 172 ? 0.5087 0.4246 0.4661 0.0597  -0.0237 -0.0579 165 ASN B N     
3429 C  CA    . ASN B 172 ? 0.4901 0.4302 0.4523 0.0676  -0.0169 -0.0577 165 ASN B CA    
3430 C  C     . ASN B 172 ? 0.5106 0.4507 0.4742 0.0815  -0.0168 -0.0625 165 ASN B C     
3431 O  O     . ASN B 172 ? 0.5169 0.4475 0.4840 0.0844  -0.0201 -0.0595 165 ASN B O     
3432 C  CB    . ASN B 172 ? 0.4534 0.4093 0.4246 0.0622  -0.0118 -0.0474 165 ASN B CB    
3433 C  CG    . ASN B 172 ? 0.4330 0.3951 0.4043 0.0518  -0.0103 -0.0431 165 ASN B CG    
3434 O  OD1   . ASN B 172 ? 0.4442 0.4002 0.4109 0.0467  -0.0138 -0.0471 165 ASN B OD1   
3435 N  ND2   . ASN B 172 ? 0.4067 0.3818 0.3840 0.0491  -0.0056 -0.0358 165 ASN B ND2   
3436 N  N     . THR B 173 ? 0.5241 0.4765 0.4845 0.0909  -0.0129 -0.0698 166 THR B N     
3437 C  CA    . THR B 173 ? 0.5479 0.5063 0.5106 0.1059  -0.0111 -0.0763 166 THR B CA    
3438 C  C     . THR B 173 ? 0.5356 0.5248 0.5037 0.1102  -0.0008 -0.0747 166 THR B C     
3439 O  O     . THR B 173 ? 0.5331 0.5314 0.4935 0.1075  0.0033  -0.0753 166 THR B O     
3440 C  CB    . THR B 173 ? 0.5929 0.5322 0.5424 0.1143  -0.0164 -0.0895 166 THR B CB    
3441 O  OG1   . THR B 173 ? 0.6119 0.5195 0.5561 0.1089  -0.0259 -0.0900 166 THR B OG1   
3442 C  CG2   . THR B 173 ? 0.6223 0.5709 0.5733 0.1322  -0.0134 -0.0981 166 THR B CG2   
3443 N  N     . VAL B 174 ? 0.5310 0.5370 0.5124 0.1160  0.0032  -0.0718 167 VAL B N     
3444 C  CA    . VAL B 174 ? 0.5282 0.5643 0.5168 0.1195  0.0140  -0.0702 167 VAL B CA    
3445 C  C     . VAL B 174 ? 0.5676 0.6123 0.5541 0.1362  0.0170  -0.0818 167 VAL B C     
3446 O  O     . VAL B 174 ? 0.5851 0.6267 0.5795 0.1463  0.0128  -0.0862 167 VAL B O     
3447 C  CB    . VAL B 174 ? 0.5045 0.5574 0.5115 0.1146  0.0168  -0.0610 167 VAL B CB    
3448 C  CG1   . VAL B 174 ? 0.5090 0.5935 0.5255 0.1166  0.0286  -0.0592 167 VAL B CG1   
3449 C  CG2   . VAL B 174 ? 0.4703 0.5152 0.4777 0.0994  0.0147  -0.0508 167 VAL B CG2   
3450 N  N     . VAL B 175 ? 0.5853 0.6404 0.5602 0.1401  0.0239  -0.0867 168 VAL B N     
3451 C  CA    . VAL B 175 ? 0.6282 0.6920 0.5980 0.1568  0.0279  -0.0993 168 VAL B CA    
3452 C  C     . VAL B 175 ? 0.6288 0.7295 0.6147 0.1607  0.0403  -0.0954 168 VAL B C     
3453 O  O     . VAL B 175 ? 0.6141 0.7328 0.6005 0.1515  0.0496  -0.0865 168 VAL B O     
3454 C  CB    . VAL B 175 ? 0.6534 0.7116 0.6004 0.1593  0.0292  -0.1073 168 VAL B CB    
3455 C  CG1   . VAL B 175 ? 0.7048 0.7677 0.6436 0.1782  0.0321  -0.1228 168 VAL B CG1   
3456 C  CG2   . VAL B 175 ? 0.6481 0.6754 0.5825 0.1503  0.0175  -0.1090 168 VAL B CG2   
3457 N  N     . ASN B 176 ? 0.6498 0.7614 0.6498 0.1741  0.0402  -0.1018 169 ASN B N     
3458 C  CA    . ASN B 176 ? 0.6502 0.7998 0.6717 0.1763  0.0507  -0.0980 169 ASN B CA    
3459 C  C     . ASN B 176 ? 0.6962 0.8609 0.7232 0.1980  0.0535  -0.1118 169 ASN B C     
3460 O  O     . ASN B 176 ? 0.7263 0.8669 0.7390 0.2108  0.0461  -0.1236 169 ASN B O     
3461 C  CB    . ASN B 176 ? 0.6184 0.7713 0.6610 0.1672  0.0453  -0.0883 169 ASN B CB    
3462 C  CG    . ASN B 176 ? 0.6275 0.7570 0.6728 0.1766  0.0312  -0.0934 169 ASN B CG    
3463 O  OD1   . ASN B 176 ? 0.6546 0.7973 0.7129 0.1921  0.0297  -0.1005 169 ASN B OD1   
3464 N  ND2   . ASN B 176 ? 0.6097 0.7050 0.6428 0.1679  0.0209  -0.0896 169 ASN B ND2   
3465 N  N     . LYS B 177 ? 0.7042 0.9083 0.7534 0.2019  0.0635  -0.1105 170 LYS B N     
3466 C  CA    . LYS B 177 ? 0.7509 0.9764 0.8079 0.2239  0.0681  -0.1240 170 LYS B CA    
3467 C  C     . LYS B 177 ? 0.7728 0.9696 0.8285 0.2404  0.0527  -0.1341 170 LYS B C     
3468 O  O     . LYS B 177 ? 0.8189 1.0111 0.8655 0.2600  0.0525  -0.1486 170 LYS B O     
3469 C  CB    . LYS B 177 ? 0.7528 1.0276 0.8407 0.2233  0.0792  -0.1197 170 LYS B CB    
3470 C  CG    . LYS B 177 ? 0.8039 1.1107 0.9028 0.2461  0.0873  -0.1335 170 LYS B CG    
3471 C  CD    . LYS B 177 ? 0.8434 1.1494 0.9169 0.2570  0.0971  -0.1441 170 LYS B CD    
3472 C  CE    . LYS B 177 ? 0.8313 1.1464 0.8893 0.2394  0.1104  -0.1339 170 LYS B CE    
3473 N  NZ    . LYS B 177 ? 0.8775 1.1943 0.9092 0.2522  0.1194  -0.1454 170 LYS B NZ    
3474 N  N     . PHE B 178 ? 0.7460 0.9218 0.8089 0.2333  0.0397  -0.1267 171 PHE B N     
3475 C  CA    . PHE B 178 ? 0.7732 0.9224 0.8355 0.2491  0.0252  -0.1340 171 PHE B CA    
3476 C  C     . PHE B 178 ? 0.7920 0.8911 0.8254 0.2510  0.0152  -0.1405 171 PHE B C     
3477 O  O     . PHE B 178 ? 0.8305 0.9036 0.8586 0.2668  0.0044  -0.1488 171 PHE B O     
3478 C  CB    . PHE B 178 ? 0.7462 0.8931 0.8253 0.2418  0.0150  -0.1235 171 PHE B CB    
3479 C  CG    . PHE B 178 ? 0.7380 0.9332 0.8485 0.2418  0.0214  -0.1195 171 PHE B CG    
3480 C  CD1   . PHE B 178 ? 0.7763 1.0079 0.9043 0.2609  0.0283  -0.1298 171 PHE B CD1   
3481 C  CD2   . PHE B 178 ? 0.6962 0.9018 0.8197 0.2226  0.0204  -0.1065 171 PHE B CD2   
3482 C  CE1   . PHE B 178 ? 0.7719 1.0517 0.9317 0.2592  0.0343  -0.1265 171 PHE B CE1   
3483 C  CE2   . PHE B 178 ? 0.6933 0.9436 0.8469 0.2208  0.0254  -0.1038 171 PHE B CE2   
3484 C  CZ    . PHE B 178 ? 0.7306 1.0192 0.9034 0.2383  0.0325  -0.1135 171 PHE B CZ    
3485 N  N     . ASN B 179 ? 0.7727 0.8567 0.7871 0.2361  0.0178  -0.1376 172 ASN B N     
3486 C  CA    . ASN B 179 ? 0.7933 0.8310 0.7837 0.2359  0.0069  -0.1439 172 ASN B CA    
3487 C  C     . ASN B 179 ? 0.8127 0.8467 0.7814 0.2358  0.0125  -0.1530 172 ASN B C     
3488 O  O     . ASN B 179 ? 0.8311 0.8288 0.7804 0.2331  0.0034  -0.1590 172 ASN B O     
3489 C  CB    . ASN B 179 ? 0.7553 0.7658 0.7429 0.2166  -0.0023 -0.1312 172 ASN B CB    
3490 C  CG    . ASN B 179 ? 0.7061 0.7321 0.6940 0.1962  0.0051  -0.1200 172 ASN B CG    
3491 O  OD1   . ASN B 179 ? 0.7010 0.7570 0.6914 0.1960  0.0170  -0.1200 172 ASN B OD1   
3492 N  ND2   . ASN B 179 ? 0.6743 0.6804 0.6593 0.1797  -0.0012 -0.1100 172 ASN B ND2   
3493 N  N     . HIS B 180 ? 0.8150 0.8857 0.7858 0.2386  0.0268  -0.1546 173 HIS B N     
3494 C  CA    . HIS B 180 ? 0.8267 0.8955 0.7749 0.2347  0.0318  -0.1595 173 HIS B CA    
3495 C  C     . HIS B 180 ? 0.8879 0.9327 0.8153 0.2519  0.0262  -0.1791 173 HIS B C     
3496 O  O     . HIS B 180 ? 0.9032 0.9370 0.8086 0.2483  0.0256  -0.1851 173 HIS B O     
3497 C  CB    . HIS B 180 ? 0.8178 0.9297 0.7704 0.2317  0.0491  -0.1536 173 HIS B CB    
3498 C  CG    . HIS B 180 ? 0.8629 1.0053 0.8206 0.2517  0.0603  -0.1647 173 HIS B CG    
3499 N  ND1   . HIS B 180 ? 0.8661 1.0344 0.8506 0.2612  0.0639  -0.1642 173 HIS B ND1   
3500 C  CD2   . HIS B 180 ? 0.9103 1.0632 0.8499 0.2646  0.0686  -0.1773 173 HIS B CD2   
3501 C  CE1   . HIS B 180 ? 0.9133 1.1090 0.8979 0.2795  0.0749  -0.1762 173 HIS B CE1   
3502 N  NE2   . HIS B 180 ? 0.9413 1.1273 0.8975 0.2819  0.0784  -0.1842 173 HIS B NE2   
3503 N  N     . LEU B 181 ? 0.9268 0.9610 0.8601 0.2708  0.0207  -0.1894 174 LEU B N     
3504 C  CA    . LEU B 181 ? 0.9924 0.9988 0.9056 0.2885  0.0142  -0.2092 174 LEU B CA    
3505 C  C     . LEU B 181 ? 1.0077 0.9600 0.9107 0.2840  -0.0036 -0.2115 174 LEU B C     
3506 O  O     . LEU B 181 ? 1.0637 0.9847 0.9470 0.2942  -0.0111 -0.2275 174 LEU B O     
3507 C  CB    . LEU B 181 ? 1.0375 1.0655 0.9624 0.3151  0.0197  -0.2207 174 LEU B CB    
3508 C  CG    . LEU B 181 ? 1.0499 1.1283 0.9786 0.3240  0.0385  -0.2248 174 LEU B CG    
3509 C  CD1   . LEU B 181 ? 1.1006 1.1997 1.0428 0.3521  0.0428  -0.2380 174 LEU B CD1   
3510 C  CD2   . LEU B 181 ? 1.0781 1.1507 0.9767 0.3230  0.0428  -0.2348 174 LEU B CD2   
3511 N  N     . GLU B 182 ? 0.9642 0.9044 0.8792 0.2687  -0.0104 -0.1959 175 GLU B N     
3512 C  CA    . GLU B 182 ? 0.9830 0.8738 0.8901 0.2643  -0.0260 -0.1956 175 GLU B CA    
3513 C  C     . GLU B 182 ? 0.9966 0.8557 0.8816 0.2502  -0.0328 -0.2011 175 GLU B C     
3514 O  O     . GLU B 182 ? 0.9691 0.8459 0.8486 0.2377  -0.0270 -0.1988 175 GLU B O     
3515 C  CB    . GLU B 182 ? 0.9311 0.8230 0.8548 0.2495  -0.0292 -0.1764 175 GLU B CB    
3516 C  CG    . GLU B 182 ? 0.9511 0.7938 0.8665 0.2433  -0.0438 -0.1726 175 GLU B CG    
3517 C  CD    . GLU B 182 ? 0.9068 0.7527 0.8364 0.2313  -0.0463 -0.1543 175 GLU B CD    
3518 O  OE1   . GLU B 182 ? 0.8715 0.7560 0.8202 0.2338  -0.0389 -0.1473 175 GLU B OE1   
3519 O  OE2   . GLU B 182 ? 0.9099 0.7210 0.8311 0.2184  -0.0552 -0.1473 175 GLU B OE2   
3520 N  N     . ASP B 183 ? 1.0437 0.8546 0.9163 0.2519  -0.0461 -0.2079 176 ASP B N     
3521 C  CA    . ASP B 183 ? 1.0650 0.8418 0.9192 0.2370  -0.0549 -0.2137 176 ASP B CA    
3522 C  C     . ASP B 183 ? 1.0513 0.7956 0.9087 0.2190  -0.0645 -0.2002 176 ASP B C     
3523 O  O     . ASP B 183 ? 1.0853 0.8002 0.9424 0.2276  -0.0721 -0.1991 176 ASP B O     
3524 C  CB    . ASP B 183 ? 1.1474 0.8937 0.9811 0.2542  -0.0616 -0.2361 176 ASP B CB    
3525 C  CG    . ASP B 183 ? 1.1761 0.8925 0.9906 0.2388  -0.0705 -0.2454 176 ASP B CG    
3526 O  OD1   . ASP B 183 ? 1.1721 0.8580 0.9865 0.2196  -0.0796 -0.2372 176 ASP B OD1   
3527 O  OD2   . ASP B 183 ? 1.2063 0.9315 1.0059 0.2461  -0.0682 -0.2611 176 ASP B OD2   
3528 N  N     . MET B 184 ? 1.0034 0.7554 0.8638 0.1950  -0.0636 -0.1892 177 MET B N     
3529 C  CA    . MET B 184 ? 0.9803 0.7126 0.8461 0.1759  -0.0691 -0.1740 177 MET B CA    
3530 C  C     . MET B 184 ? 1.0096 0.7087 0.8627 0.1576  -0.0781 -0.1786 177 MET B C     
3531 O  O     . MET B 184 ? 0.9930 0.6783 0.8497 0.1382  -0.0815 -0.1665 177 MET B O     
3532 C  CB    . MET B 184 ? 0.9029 0.6734 0.7846 0.1621  -0.0601 -0.1576 177 MET B CB    
3533 C  CG    . MET B 184 ? 0.8721 0.6829 0.7674 0.1762  -0.0497 -0.1544 177 MET B CG    
3534 S  SD    . MET B 184 ? 0.7906 0.6369 0.7043 0.1599  -0.0413 -0.1343 177 MET B SD    
3535 C  CE    . MET B 184 ? 0.7776 0.6666 0.7056 0.1779  -0.0300 -0.1351 177 MET B CE    
3536 N  N     . ASN B 185 ? 1.0565 0.7449 0.8948 0.1633  -0.0818 -0.1967 178 ASN B N     
3537 C  CA    . ASN B 185 ? 1.0806 0.7481 0.9092 0.1445  -0.0898 -0.2029 178 ASN B CA    
3538 C  C     . ASN B 185 ? 1.1146 0.7362 0.9406 0.1299  -0.0995 -0.1966 178 ASN B C     
3539 O  O     . ASN B 185 ? 1.1012 0.7192 0.9308 0.1064  -0.1022 -0.1902 178 ASN B O     
3540 C  CB    . ASN B 185 ? 1.1371 0.7972 0.9478 0.1559  -0.0936 -0.2256 178 ASN B CB    
3541 C  CG    . ASN B 185 ? 1.1002 0.8063 0.9109 0.1589  -0.0847 -0.2285 178 ASN B CG    
3542 O  OD1   . ASN B 185 ? 1.0645 0.7885 0.8795 0.1413  -0.0845 -0.2224 178 ASN B OD1   
3543 N  ND2   . ASN B 185 ? 1.1123 0.8385 0.9179 0.1813  -0.0771 -0.2371 178 ASN B ND2   
3544 N  N     . ASP B 186 ? 1.1635 0.7504 0.9830 0.1440  -0.1047 -0.1982 179 ASP B N     
3545 C  CA    . ASP B 186 ? 1.2093 0.7466 1.0221 0.1314  -0.1142 -0.1917 179 ASP B CA    
3546 C  C     . ASP B 186 ? 1.1535 0.7034 0.9796 0.1127  -0.1097 -0.1690 179 ASP B C     
3547 O  O     . ASP B 186 ? 1.1613 0.6943 0.9868 0.0888  -0.1130 -0.1624 179 ASP B O     
3548 C  CB    . ASP B 186 ? 1.2752 0.7740 1.0772 0.1542  -0.1207 -0.1971 179 ASP B CB    
3549 C  CG    . ASP B 186 ? 1.3497 0.8235 1.1347 0.1710  -0.1272 -0.2212 179 ASP B CG    
3550 O  OD1   . ASP B 186 ? 1.3505 0.8376 1.1308 0.1642  -0.1269 -0.2342 179 ASP B OD1   
3551 O  OD2   . ASP B 186 ? 1.4112 0.8519 1.1865 0.1920  -0.1332 -0.2276 179 ASP B OD2   
3552 N  N     . HIS B 187 ? 1.0992 0.6813 0.9378 0.1232  -0.1018 -0.1578 180 HIS B N     
3553 C  CA    . HIS B 187 ? 1.0477 0.6435 0.8973 0.1075  -0.0974 -0.1377 180 HIS B CA    
3554 C  C     . HIS B 187 ? 0.9990 0.6227 0.8573 0.0850  -0.0923 -0.1340 180 HIS B C     
3555 O  O     . HIS B 187 ? 0.9925 0.6072 0.8531 0.0643  -0.0928 -0.1226 180 HIS B O     
3556 C  CB    . HIS B 187 ? 1.0036 0.6300 0.8650 0.1237  -0.0909 -0.1292 180 HIS B CB    
3557 C  CG    . HIS B 187 ? 1.0492 0.6492 0.9049 0.1431  -0.0971 -0.1281 180 HIS B CG    
3558 N  ND1   . HIS B 187 ? 1.0800 0.6444 0.9279 0.1368  -0.1037 -0.1156 180 HIS B ND1   
3559 C  CD2   . HIS B 187 ? 1.0693 0.6768 0.9268 0.1692  -0.0975 -0.1370 180 HIS B CD2   
3560 C  CE1   . HIS B 187 ? 1.1188 0.6679 0.9631 0.1596  -0.1091 -0.1172 180 HIS B CE1   
3561 N  NE2   . HIS B 187 ? 1.1117 0.6882 0.9633 0.1797  -0.1053 -0.1306 180 HIS B NE2   
3562 N  N     . LEU B 188 ? 0.9700 0.6276 0.8322 0.0895  -0.0875 -0.1433 181 LEU B N     
3563 C  CA    . LEU B 188 ? 0.9278 0.6135 0.7981 0.0715  -0.0838 -0.1405 181 LEU B CA    
3564 C  C     . LEU B 188 ? 0.9720 0.6306 0.8363 0.0516  -0.0922 -0.1461 181 LEU B C     
3565 O  O     . LEU B 188 ? 0.9468 0.6187 0.8202 0.0315  -0.0907 -0.1387 181 LEU B O     
3566 C  CB    . LEU B 188 ? 0.9022 0.6243 0.7734 0.0828  -0.0784 -0.1498 181 LEU B CB    
3567 C  CG    . LEU B 188 ? 0.8330 0.5972 0.7176 0.0866  -0.0674 -0.1380 181 LEU B CG    
3568 C  CD1   . LEU B 188 ? 0.7877 0.5685 0.6831 0.0666  -0.0647 -0.1256 181 LEU B CD1   
3569 C  CD2   . LEU B 188 ? 0.8245 0.5869 0.7144 0.0994  -0.0643 -0.1302 181 LEU B CD2   
3570 N  N     . ASN B 189 ? 1.0433 0.6639 0.8929 0.0567  -0.1013 -0.1601 182 ASN B N     
3571 C  CA    . ASN B 189 ? 1.0936 0.6858 0.9381 0.0359  -0.1101 -0.1661 182 ASN B CA    
3572 C  C     . ASN B 189 ? 1.1063 0.6731 0.9537 0.0168  -0.1109 -0.1501 182 ASN B C     
3573 O  O     . ASN B 189 ? 1.1202 0.6827 0.9723 -0.0071 -0.1135 -0.1483 182 ASN B O     
3574 C  CB    . ASN B 189 ? 1.1745 0.7275 1.0009 0.0459  -0.1203 -0.1858 182 ASN B CB    
3575 C  CG    . ASN B 189 ? 1.1739 0.7517 0.9953 0.0562  -0.1208 -0.2035 182 ASN B CG    
3576 O  OD1   . ASN B 189 ? 1.1196 0.7403 0.9507 0.0515  -0.1152 -0.2008 182 ASN B OD1   
3577 N  ND2   . ASN B 189 ? 1.2416 0.7901 1.0458 0.0700  -0.1282 -0.2222 182 ASN B ND2   
3578 N  N     . ALA B 190 ? 1.1061 0.6575 0.9503 0.0279  -0.1088 -0.1387 183 ALA B N     
3579 C  CA    . ALA B 190 ? 1.1264 0.6504 0.9684 0.0128  -0.1094 -0.1224 183 ALA B CA    
3580 C  C     . ALA B 190 ? 1.0570 0.6192 0.9146 -0.0013 -0.0997 -0.1059 183 ALA B C     
3581 O  O     . ALA B 190 ? 1.0690 0.6232 0.9292 -0.0244 -0.0987 -0.0966 183 ALA B O     
3582 C  CB    . ALA B 190 ? 1.1593 0.6525 0.9898 0.0327  -0.1126 -0.1177 183 ALA B CB    
3583 N  N     . LEU B 191 ? 0.9890 0.5929 0.8568 0.0120  -0.0920 -0.1029 184 LEU B N     
3584 C  CA    . LEU B 191 ? 0.9263 0.5642 0.8072 0.0020  -0.0831 -0.0884 184 LEU B CA    
3585 C  C     . LEU B 191 ? 0.9007 0.5672 0.7934 -0.0158 -0.0804 -0.0913 184 LEU B C     
3586 O  O     . LEU B 191 ? 0.8818 0.5604 0.7828 -0.0328 -0.0756 -0.0804 184 LEU B O     
3587 C  CB    . LEU B 191 ? 0.8695 0.5403 0.7574 0.0216  -0.0768 -0.0858 184 LEU B CB    
3588 C  CG    . LEU B 191 ? 0.8826 0.5364 0.7643 0.0376  -0.0783 -0.0791 184 LEU B CG    
3589 C  CD1   . LEU B 191 ? 0.8389 0.5263 0.7293 0.0578  -0.0734 -0.0822 184 LEU B CD1   
3590 C  CD2   . LEU B 191 ? 0.8751 0.5224 0.7560 0.0259  -0.0759 -0.0616 184 LEU B CD2   
3591 N  N     . GLN B 192 ? 0.9013 0.5815 0.7948 -0.0103 -0.0833 -0.1063 185 GLN B N     
3592 C  CA    . GLN B 192 ? 0.8843 0.5922 0.7882 -0.0243 -0.0832 -0.1112 185 GLN B CA    
3593 C  C     . GLN B 192 ? 0.8159 0.5655 0.7348 -0.0279 -0.0738 -0.0995 185 GLN B C     
3594 O  O     . GLN B 192 ? 0.8080 0.5714 0.7376 -0.0459 -0.0718 -0.0942 185 GLN B O     
3595 C  CB    . GLN B 192 ? 0.9365 0.6214 0.8411 -0.0485 -0.0891 -0.1127 185 GLN B CB    
3596 C  CG    . GLN B 192 ? 1.0115 0.6541 0.9011 -0.0472 -0.1000 -0.1271 185 GLN B CG    
3597 C  CD    . GLN B 192 ? 1.0578 0.6907 0.9522 -0.0727 -0.1066 -0.1331 185 GLN B CD    
3598 O  OE1   . GLN B 192 ? 1.0780 0.6985 0.9773 -0.0935 -0.1048 -0.1223 185 GLN B OE1   
3599 N  NE2   . GLN B 192 ? 1.0778 0.7184 0.9709 -0.0718 -0.1141 -0.1506 185 GLN B NE2   
3600 N  N     . PRO B 193 ? 0.7683 0.5401 0.6891 -0.0109 -0.0676 -0.0956 186 PRO B N     
3601 C  CA    . PRO B 193 ? 0.7090 0.5187 0.6424 -0.0129 -0.0596 -0.0869 186 PRO B CA    
3602 C  C     . PRO B 193 ? 0.7016 0.5370 0.6414 -0.0180 -0.0618 -0.0952 186 PRO B C     
3603 O  O     . PRO B 193 ? 0.7299 0.5598 0.6619 -0.0121 -0.0679 -0.1082 186 PRO B O     
3604 C  CB    . PRO B 193 ? 0.6767 0.4987 0.6082 0.0069  -0.0548 -0.0851 186 PRO B CB    
3605 C  CG    . PRO B 193 ? 0.7161 0.5198 0.6360 0.0201  -0.0602 -0.0981 186 PRO B CG    
3606 C  CD    . PRO B 193 ? 0.7735 0.5374 0.6854 0.0107  -0.0679 -0.1008 186 PRO B CD    
3607 N  N     . PHE B 194 ? 0.6679 0.5313 0.6208 -0.0271 -0.0573 -0.0883 187 PHE B N     
3608 C  CA    . PHE B 194 ? 0.6618 0.5526 0.6217 -0.0301 -0.0602 -0.0953 187 PHE B CA    
3609 C  C     . PHE B 194 ? 0.6341 0.5442 0.5888 -0.0120 -0.0579 -0.0978 187 PHE B C     
3610 O  O     . PHE B 194 ? 0.6437 0.5680 0.5956 -0.0085 -0.0625 -0.1066 187 PHE B O     
3611 C  CB    . PHE B 194 ? 0.6403 0.5563 0.6168 -0.0436 -0.0564 -0.0879 187 PHE B CB    
3612 C  CG    . PHE B 194 ? 0.5885 0.5319 0.5715 -0.0347 -0.0485 -0.0790 187 PHE B CG    
3613 C  CD1   . PHE B 194 ? 0.5627 0.5006 0.5448 -0.0314 -0.0409 -0.0678 187 PHE B CD1   
3614 C  CD2   . PHE B 194 ? 0.5714 0.5441 0.5602 -0.0297 -0.0496 -0.0818 187 PHE B CD2   
3615 C  CE1   . PHE B 194 ? 0.5212 0.4810 0.5085 -0.0240 -0.0343 -0.0607 187 PHE B CE1   
3616 C  CE2   . PHE B 194 ? 0.5310 0.5241 0.5244 -0.0214 -0.0428 -0.0736 187 PHE B CE2   
3617 C  CZ    . PHE B 194 ? 0.5063 0.4922 0.4992 -0.0192 -0.0351 -0.0634 187 PHE B CZ    
3618 N  N     . ARG B 195 ? 0.6051 0.5150 0.5573 -0.0008 -0.0508 -0.0898 188 ARG B N     
3619 C  CA    . ARG B 195 ? 0.5791 0.5071 0.5275 0.0140  -0.0462 -0.0890 188 ARG B CA    
3620 C  C     . ARG B 195 ? 0.5765 0.4914 0.5191 0.0259  -0.0422 -0.0866 188 ARG B C     
3621 O  O     . ARG B 195 ? 0.5659 0.4709 0.5124 0.0237  -0.0395 -0.0785 188 ARG B O     
3622 C  CB    . ARG B 195 ? 0.5381 0.4911 0.4976 0.0110  -0.0406 -0.0788 188 ARG B CB    
3623 C  CG    . ARG B 195 ? 0.5129 0.4850 0.4694 0.0233  -0.0355 -0.0753 188 ARG B CG    
3624 C  CD    . ARG B 195 ? 0.4860 0.4793 0.4525 0.0195  -0.0328 -0.0679 188 ARG B CD    
3625 N  NE    . ARG B 195 ? 0.4692 0.4773 0.4314 0.0301  -0.0286 -0.0634 188 ARG B NE    
3626 C  CZ    . ARG B 195 ? 0.4812 0.5025 0.4371 0.0355  -0.0319 -0.0670 188 ARG B CZ    
3627 N  NH1   . ARG B 195 ? 0.5095 0.5324 0.4634 0.0317  -0.0405 -0.0770 188 ARG B NH1   
3628 N  NH2   . ARG B 195 ? 0.4706 0.5018 0.4209 0.0443  -0.0274 -0.0607 188 ARG B NH2   
3629 N  N     . TRP B 196 ? 0.5888 0.5064 0.5222 0.0391  -0.0418 -0.0938 189 TRP B N     
3630 C  CA    . TRP B 196 ? 0.5926 0.5026 0.5223 0.0519  -0.0381 -0.0938 189 TRP B CA    
3631 C  C     . TRP B 196 ? 0.5715 0.5063 0.5001 0.0629  -0.0305 -0.0915 189 TRP B C     
3632 O  O     . TRP B 196 ? 0.5925 0.5340 0.5107 0.0709  -0.0306 -0.0999 189 TRP B O     
3633 C  CB    . TRP B 196 ? 0.6442 0.5293 0.5625 0.0580  -0.0448 -0.1070 189 TRP B CB    
3634 C  CG    . TRP B 196 ? 0.6538 0.5348 0.5694 0.0742  -0.0412 -0.1089 189 TRP B CG    
3635 C  CD1   . TRP B 196 ? 0.6289 0.5151 0.5533 0.0786  -0.0362 -0.0992 189 TRP B CD1   
3636 C  CD2   . TRP B 196 ? 0.6973 0.5684 0.6013 0.0886  -0.0434 -0.1225 189 TRP B CD2   
3637 N  NE1   . TRP B 196 ? 0.6507 0.5353 0.5723 0.0948  -0.0346 -0.1053 189 TRP B NE1   
3638 C  CE2   . TRP B 196 ? 0.6932 0.5681 0.6020 0.1018  -0.0384 -0.1196 189 TRP B CE2   
3639 C  CE3   . TRP B 196 ? 0.7415 0.6029 0.6316 0.0921  -0.0491 -0.1376 189 TRP B CE3   
3640 C  CZ2   . TRP B 196 ? 0.7319 0.6022 0.6332 0.1193  -0.0381 -0.1312 189 TRP B CZ2   
3641 C  CZ3   . TRP B 196 ? 0.7813 0.6347 0.6613 0.1093  -0.0489 -0.1496 189 TRP B CZ3   
3642 C  CH2   . TRP B 196 ? 0.7762 0.6348 0.6623 0.1232  -0.0431 -0.1463 189 TRP B CH2   
3643 N  N     . LYS B 197 ? 0.5340 0.4826 0.4717 0.0626  -0.0235 -0.0800 190 LYS B N     
3644 C  CA    . LYS B 197 ? 0.5194 0.4894 0.4562 0.0706  -0.0157 -0.0764 190 LYS B CA    
3645 C  C     . LYS B 197 ? 0.5367 0.5070 0.4718 0.0833  -0.0118 -0.0808 190 LYS B C     
3646 O  O     . LYS B 197 ? 0.5350 0.4963 0.4772 0.0852  -0.0124 -0.0788 190 LYS B O     
3647 C  CB    . LYS B 197 ? 0.4806 0.4629 0.4281 0.0661  -0.0097 -0.0634 190 LYS B CB    
3648 C  CG    . LYS B 197 ? 0.4601 0.4440 0.4129 0.0551  -0.0119 -0.0576 190 LYS B CG    
3649 C  CD    . LYS B 197 ? 0.4651 0.4593 0.4129 0.0533  -0.0144 -0.0597 190 LYS B CD    
3650 C  CE    . LYS B 197 ? 0.4568 0.4673 0.4004 0.0588  -0.0088 -0.0539 190 LYS B CE    
3651 N  NZ    . LYS B 197 ? 0.4289 0.4456 0.3805 0.0548  -0.0049 -0.0432 190 LYS B NZ    
3652 N  N     . CYS B 198 ? 0.5566 0.5386 0.4817 0.0924  -0.0080 -0.0867 191 CYS B N     
3653 C  CA    . CYS B 198 ? 0.5732 0.5639 0.4982 0.1052  -0.0016 -0.0904 191 CYS B CA    
3654 C  C     . CYS B 198 ? 0.5578 0.5742 0.4849 0.1067  0.0093  -0.0819 191 CYS B C     
3655 O  O     . CYS B 198 ? 0.5712 0.5979 0.4859 0.1089  0.0126  -0.0830 191 CYS B O     
3656 C  CB    . CYS B 198 ? 0.6205 0.6027 0.5305 0.1157  -0.0049 -0.1058 191 CYS B CB    
3657 S  SG    . CYS B 198 ? 0.6502 0.5967 0.5583 0.1148  -0.0173 -0.1156 191 CYS B SG    
3658 N  N     . PHE B 199 ? 0.5324 0.5579 0.4746 0.1042  0.0143  -0.0726 192 PHE B N     
3659 C  CA    . PHE B 199 ? 0.5210 0.5682 0.4670 0.1027  0.0247  -0.0633 192 PHE B CA    
3660 C  C     . PHE B 199 ? 0.5453 0.6106 0.4942 0.1136  0.0334  -0.0676 192 PHE B C     
3661 O  O     . PHE B 199 ? 0.5493 0.6153 0.5099 0.1193  0.0323  -0.0712 192 PHE B O     
3662 C  CB    . PHE B 199 ? 0.4869 0.5364 0.4493 0.0937  0.0257  -0.0523 192 PHE B CB    
3663 C  CG    . PHE B 199 ? 0.4628 0.4962 0.4265 0.0839  0.0181  -0.0483 192 PHE B CG    
3664 C  CD1   . PHE B 199 ? 0.4561 0.4883 0.4115 0.0785  0.0169  -0.0448 192 PHE B CD1   
3665 C  CD2   . PHE B 199 ? 0.4508 0.4725 0.4237 0.0808  0.0125  -0.0476 192 PHE B CD2   
3666 C  CE1   . PHE B 199 ? 0.4370 0.4585 0.3955 0.0702  0.0109  -0.0419 192 PHE B CE1   
3667 C  CE2   . PHE B 199 ? 0.4319 0.4418 0.4056 0.0714  0.0074  -0.0433 192 PHE B CE2   
3668 C  CZ    . PHE B 199 ? 0.4248 0.4358 0.3923 0.0662  0.0071  -0.0410 192 PHE B CZ    
3669 N  N     . GLN B 200 ? 0.5632 0.6449 0.5018 0.1162  0.0426  -0.0657 193 GLN B N     
3670 C  CA    . GLN B 200 ? 0.5817 0.6877 0.5274 0.1228  0.0543  -0.0656 193 GLN B CA    
3671 C  C     . GLN B 200 ? 0.5548 0.6730 0.5222 0.1139  0.0589  -0.0542 193 GLN B C     
3672 O  O     . GLN B 200 ? 0.5326 0.6482 0.5014 0.1024  0.0597  -0.0430 193 GLN B O     
3673 C  CB    . GLN B 200 ? 0.6095 0.7301 0.5376 0.1251  0.0643  -0.0633 193 GLN B CB    
3674 C  CG    . GLN B 200 ? 0.6387 0.7873 0.5726 0.1330  0.0780  -0.0652 193 GLN B CG    
3675 C  CD    . GLN B 200 ? 0.6719 0.8348 0.5856 0.1343  0.0894  -0.0611 193 GLN B CD    
3676 O  OE1   . GLN B 200 ? 0.6734 0.8254 0.5683 0.1296  0.0867  -0.0557 193 GLN B OE1   
3677 N  NE2   . GLN B 200 ? 0.7022 0.8919 0.6203 0.1408  0.1029  -0.0629 193 GLN B NE2   
3678 N  N     . VAL B 201 ? 0.5608 0.6933 0.5459 0.1198  0.0614  -0.0578 194 VAL B N     
3679 C  CA    . VAL B 201 ? 0.5377 0.6809 0.5444 0.1108  0.0630  -0.0488 194 VAL B CA    
3680 C  C     . VAL B 201 ? 0.5394 0.6982 0.5454 0.1002  0.0747  -0.0370 194 VAL B C     
3681 O  O     . VAL B 201 ? 0.5687 0.7435 0.5652 0.1038  0.0856  -0.0369 194 VAL B O     
3682 C  CB    . VAL B 201 ? 0.5500 0.7101 0.5768 0.1203  0.0631  -0.0554 194 VAL B CB    
3683 C  CG1   . VAL B 201 ? 0.5849 0.7758 0.6151 0.1289  0.0764  -0.0594 194 VAL B CG1   
3684 C  CG2   . VAL B 201 ? 0.5256 0.6916 0.5742 0.1111  0.0596  -0.0481 194 VAL B CG2   
3685 N  N     . LEU B 202 ? 0.5127 0.6633 0.5252 0.0869  0.0721  -0.0268 195 LEU B N     
3686 C  CA    . LEU B 202 ? 0.5175 0.6723 0.5250 0.0759  0.0807  -0.0146 195 LEU B CA    
3687 C  C     . LEU B 202 ? 0.5134 0.6836 0.5435 0.0651  0.0855  -0.0074 195 LEU B C     
3688 O  O     . LEU B 202 ? 0.4921 0.6587 0.5379 0.0621  0.0775  -0.0090 195 LEU B O     
3689 C  CB    . LEU B 202 ? 0.4984 0.6272 0.4907 0.0704  0.0731  -0.0096 195 LEU B CB    
3690 C  CG    . LEU B 202 ? 0.5058 0.6308 0.4900 0.0605  0.0791  0.0033  195 LEU B CG    
3691 C  CD1   . LEU B 202 ? 0.5406 0.6715 0.5031 0.0652  0.0874  0.0060  195 LEU B CD1   
3692 C  CD2   . LEU B 202 ? 0.4810 0.5821 0.4597 0.0555  0.0695  0.0070  195 LEU B CD2   
3693 N  N     . ILE B 203 ? 0.5395 0.7269 0.5697 0.0587  0.0985  0.0005  196 ILE B N     
3694 C  CA    . ILE B 203 ? 0.5449 0.7466 0.5949 0.0449  0.1046  0.0087  196 ILE B CA    
3695 C  C     . ILE B 203 ? 0.5388 0.7168 0.5784 0.0320  0.1031  0.0205  196 ILE B C     
3696 O  O     . ILE B 203 ? 0.5560 0.7230 0.5736 0.0315  0.1078  0.0274  196 ILE B O     
3697 C  CB    . ILE B 203 ? 0.5844 0.8189 0.6416 0.0433  0.1211  0.0116  196 ILE B CB    
3698 C  CG1   . ILE B 203 ? 0.5953 0.8557 0.6645 0.0584  0.1229  -0.0013 196 ILE B CG1   
3699 C  CG2   . ILE B 203 ? 0.5954 0.8428 0.6726 0.0254  0.1275  0.0214  196 ILE B CG2   
3700 C  CD1   . ILE B 203 ? 0.5734 0.8400 0.6678 0.0618  0.1121  -0.0091 196 ILE B CD1   
3701 N  N     . VAL B 204 ? 0.5182 0.6874 0.5723 0.0230  0.0955  0.0219  197 VAL B N     
3702 C  CA    . VAL B 204 ? 0.5161 0.6624 0.5636 0.0111  0.0933  0.0314  197 VAL B CA    
3703 C  C     . VAL B 204 ? 0.5349 0.6934 0.6021 -0.0045 0.0989  0.0376  197 VAL B C     
3704 O  O     . VAL B 204 ? 0.5247 0.6974 0.6146 -0.0071 0.0942  0.0318  197 VAL B O     
3705 C  CB    . VAL B 204 ? 0.4808 0.6039 0.5259 0.0138  0.0791  0.0265  197 VAL B CB    
3706 C  CG1   . VAL B 204 ? 0.4817 0.5820 0.5221 0.0030  0.0763  0.0342  197 VAL B CG1   
3707 C  CG2   . VAL B 204 ? 0.4667 0.5782 0.4941 0.0266  0.0736  0.0207  197 VAL B CG2   
3708 N  N     . THR B 205 ? 0.5657 0.7157 0.6231 -0.0154 0.1076  0.0497  198 THR B N     
3709 C  CA    . THR B 205 ? 0.5935 0.7521 0.6677 -0.0333 0.1140  0.0570  198 THR B CA    
3710 C  C     . THR B 205 ? 0.5738 0.7170 0.6604 -0.0411 0.1018  0.0536  198 THR B C     
3711 O  O     . THR B 205 ? 0.5555 0.6695 0.6276 -0.0376 0.0928  0.0532  198 THR B O     
3712 C  CB    . THR B 205 ? 0.6360 0.7796 0.6911 -0.0429 0.1246  0.0720  198 THR B CB    
3713 O  OG1   . THR B 205 ? 0.6370 0.7707 0.6646 -0.0292 0.1261  0.0735  198 THR B OG1   
3714 C  CG2   . THR B 205 ? 0.6805 0.8512 0.7483 -0.0559 0.1403  0.0796  198 THR B CG2   
3715 N  N     . GLY B 206 ? 0.5799 0.7452 0.6940 -0.0507 0.1012  0.0500  199 GLY B N     
3716 C  CA    . GLY B 206 ? 0.5690 0.7220 0.6946 -0.0590 0.0895  0.0460  199 GLY B CA    
3717 C  C     . GLY B 206 ? 0.5304 0.6868 0.6621 -0.0462 0.0764  0.0339  199 GLY B C     
3718 O  O     . GLY B 206 ? 0.5243 0.6755 0.6661 -0.0519 0.0664  0.0294  199 GLY B O     
3719 N  N     . GLU B 207 ? 0.5103 0.6743 0.6348 -0.0294 0.0761  0.0286  200 GLU B N     
3720 C  CA    . GLU B 207 ? 0.4802 0.6423 0.6066 -0.0172 0.0640  0.0187  200 GLU B CA    
3721 C  C     . GLU B 207 ? 0.4830 0.6776 0.6273 -0.0072 0.0648  0.0112  200 GLU B C     
3722 O  O     . GLU B 207 ? 0.4751 0.6782 0.6335 -0.0038 0.0550  0.0045  200 GLU B O     
3723 C  CB    . GLU B 207 ? 0.4578 0.5952 0.5592 -0.0056 0.0604  0.0178  200 GLU B CB    
3724 C  CG    . GLU B 207 ? 0.4495 0.5552 0.5352 -0.0109 0.0555  0.0218  200 GLU B CG    
3725 C  CD    . GLU B 207 ? 0.4309 0.5236 0.5186 -0.0111 0.0433  0.0164  200 GLU B CD    
3726 O  OE1   . GLU B 207 ? 0.4262 0.5335 0.5282 -0.0088 0.0374  0.0104  200 GLU B OE1   
3727 O  OE2   . GLU B 207 ? 0.4240 0.4919 0.4975 -0.0124 0.0395  0.0180  200 GLU B OE2   
3728 N  N     . ASN B 208 ? 0.4969 0.7075 0.6377 -0.0001 0.0756  0.0117  201 ASN B N     
3729 C  CA    . ASN B 208 ? 0.5017 0.7389 0.6551 0.0139  0.0762  0.0030  201 ASN B CA    
3730 C  C     . ASN B 208 ? 0.5339 0.8019 0.6946 0.0133  0.0923  0.0054  201 ASN B C     
3731 O  O     . ASN B 208 ? 0.5420 0.8253 0.7021 0.0281  0.0958  -0.0014 201 ASN B O     
3732 C  CB    . ASN B 208 ? 0.4826 0.7013 0.6179 0.0310  0.0689  -0.0038 201 ASN B CB    
3733 C  CG    . ASN B 208 ? 0.4856 0.6898 0.5956 0.0357  0.0757  -0.0012 201 ASN B CG    
3734 O  OD1   . ASN B 208 ? 0.5004 0.7041 0.6026 0.0266  0.0854  0.0072  201 ASN B OD1   
3735 N  ND2   . ASN B 208 ? 0.4764 0.6676 0.5727 0.0493  0.0700  -0.0082 201 ASN B ND2   
3736 N  N     . ASP B 209 ? 0.5573 0.8339 0.7246 -0.0038 0.1024  0.0148  202 ASP B N     
3737 C  CA    . ASP B 209 ? 0.5921 0.8915 0.7580 -0.0059 0.1199  0.0200  202 ASP B CA    
3738 C  C     . ASP B 209 ? 0.6212 0.9651 0.8210 -0.0145 0.1283  0.0192  202 ASP B C     
3739 O  O     . ASP B 209 ? 0.6553 1.0245 0.8571 -0.0166 0.1445  0.0231  202 ASP B O     
3740 C  CB    . ASP B 209 ? 0.6072 0.8812 0.7496 -0.0180 0.1273  0.0333  202 ASP B CB    
3741 C  CG    . ASP B 209 ? 0.6179 0.8793 0.7690 -0.0393 0.1260  0.0421  202 ASP B CG    
3742 O  OD1   . ASP B 209 ? 0.5957 0.8473 0.7581 -0.0425 0.1128  0.0372  202 ASP B OD1   
3743 O  OD2   . ASP B 209 ? 0.6522 0.9095 0.7949 -0.0522 0.1375  0.0540  202 ASP B OD2   
3744 N  N     . SER B 210 ? 0.6120 0.9672 0.8378 -0.0195 0.1175  0.0141  203 SER B N     
3745 C  CA    . SER B 210 ? 0.6410 1.0422 0.9030 -0.0283 0.1238  0.0123  203 SER B CA    
3746 C  C     . SER B 210 ? 0.6265 1.0425 0.9141 -0.0229 0.1075  0.0017  203 SER B C     
3747 O  O     . SER B 210 ? 0.5961 0.9886 0.8722 -0.0095 0.0927  -0.0045 203 SER B O     
3748 C  CB    . SER B 210 ? 0.6715 1.0731 0.9398 -0.0549 0.1334  0.0245  203 SER B CB    
3749 O  OG    . SER B 210 ? 0.6590 1.0369 0.9317 -0.0682 0.1198  0.0253  203 SER B OG    
3750 N  N     . ASP B 211 ? 0.6538 1.1121 0.9773 -0.0334 0.1107  0.0000  204 ASP B N     
3751 C  CA    . ASP B 211 ? 0.6495 1.1285 1.0007 -0.0296 0.0952  -0.0095 204 ASP B CA    
3752 C  C     . ASP B 211 ? 0.6474 1.1064 1.0026 -0.0511 0.0849  -0.0057 204 ASP B C     
3753 O  O     . ASP B 211 ? 0.6433 1.1103 1.0153 -0.0502 0.0692  -0.0130 204 ASP B O     
3754 C  CB    . ASP B 211 ? 0.6836 1.2242 1.0737 -0.0270 0.1033  -0.0154 204 ASP B CB    
3755 C  CG    . ASP B 211 ? 0.6958 1.2567 1.0799 -0.0076 0.1173  -0.0187 204 ASP B CG    
3756 O  OD1   . ASP B 211 ? 0.6769 1.2228 1.0457 0.0163  0.1091  -0.0266 204 ASP B OD1   
3757 O  OD2   . ASP B 211 ? 0.7285 1.3176 1.1209 -0.0172 0.1368  -0.0132 204 ASP B OD2   
3758 N  N     . LYS B 212 ? 0.6559 1.0879 0.9942 -0.0695 0.0934  0.0052  205 LYS B N     
3759 C  CA    . LYS B 212 ? 0.6533 1.0526 0.9849 -0.0867 0.0832  0.0085  205 LYS B CA    
3760 C  C     . LYS B 212 ? 0.6126 0.9683 0.9154 -0.0729 0.0683  0.0050  205 LYS B C     
3761 O  O     . LYS B 212 ? 0.6067 0.9455 0.9099 -0.0790 0.0543  0.0015  205 LYS B O     
3762 C  CB    . LYS B 212 ? 0.6798 1.0578 0.9981 -0.1076 0.0964  0.0217  205 LYS B CB    
3763 C  CG    . LYS B 212 ? 0.7286 1.1388 1.0773 -0.1323 0.1063  0.0264  205 LYS B CG    
3764 C  CD    . LYS B 212 ? 0.7541 1.2167 1.1252 -0.1295 0.1230  0.0268  205 LYS B CD    
3765 C  CE    . LYS B 212 ? 0.8049 1.3036 1.2110 -0.1562 0.1317  0.0307  205 LYS B CE    
3766 N  NZ    . LYS B 212 ? 0.8364 1.2988 1.2266 -0.1816 0.1384  0.0444  205 LYS B NZ    
3767 N  N     . THR B 213 ? 0.5887 0.9265 0.8661 -0.0550 0.0714  0.0054  206 THR B N     
3768 C  CA    . THR B 213 ? 0.5542 0.8507 0.8037 -0.0445 0.0597  0.0035  206 THR B CA    
3769 C  C     . THR B 213 ? 0.5371 0.8423 0.7937 -0.0275 0.0454  -0.0067 206 THR B C     
3770 O  O     . THR B 213 ? 0.5514 0.8938 0.8327 -0.0208 0.0449  -0.0126 206 THR B O     
3771 C  CB    . THR B 213 ? 0.5417 0.8146 0.7615 -0.0359 0.0687  0.0090  206 THR B CB    
3772 O  OG1   . THR B 213 ? 0.5504 0.8512 0.7758 -0.0231 0.0781  0.0061  206 THR B OG1   
3773 C  CG2   . THR B 213 ? 0.5601 0.8137 0.7661 -0.0514 0.0791  0.0204  206 THR B CG2   
3774 N  N     . LEU B 214 ? 0.5109 0.7818 0.7453 -0.0198 0.0339  -0.0086 207 LEU B N     
3775 C  CA    . LEU B 214 ? 0.5003 0.7723 0.7363 -0.0048 0.0196  -0.0163 207 LEU B CA    
3776 C  C     . LEU B 214 ? 0.4962 0.7759 0.7277 0.0154  0.0229  -0.0201 207 LEU B C     
3777 O  O     . LEU B 214 ? 0.4984 0.7848 0.7350 0.0300  0.0127  -0.0265 207 LEU B O     
3778 C  CB    . LEU B 214 ? 0.4795 0.7118 0.6909 -0.0048 0.0086  -0.0158 207 LEU B CB    
3779 C  CG    . LEU B 214 ? 0.4880 0.7092 0.7013 -0.0218 0.0025  -0.0149 207 LEU B CG    
3780 C  CD1   . LEU B 214 ? 0.4688 0.6505 0.6540 -0.0199 -0.0045 -0.0142 207 LEU B CD1   
3781 C  CD2   . LEU B 214 ? 0.5083 0.7565 0.7466 -0.0246 -0.0089 -0.0214 207 LEU B CD2   
3782 N  N     . ARG B 215 ? 0.4957 0.7726 0.7157 0.0167  0.0365  -0.0162 208 ARG B N     
3783 C  CA    . ARG B 215 ? 0.5005 0.7874 0.7169 0.0345  0.0416  -0.0208 208 ARG B CA    
3784 C  C     . ARG B 215 ? 0.5209 0.8308 0.7424 0.0301  0.0595  -0.0173 208 ARG B C     
3785 O  O     . ARG B 215 ? 0.5259 0.8305 0.7433 0.0138  0.0680  -0.0088 208 ARG B O     
3786 C  CB    . ARG B 215 ? 0.4792 0.7286 0.6648 0.0443  0.0380  -0.0210 208 ARG B CB    
3787 C  CG    . ARG B 215 ? 0.4629 0.6862 0.6383 0.0489  0.0224  -0.0232 208 ARG B CG    
3788 C  CD    . ARG B 215 ? 0.4773 0.7144 0.6647 0.0649  0.0130  -0.0308 208 ARG B CD    
3789 N  NE    . ARG B 215 ? 0.4667 0.6730 0.6370 0.0705  -0.0001 -0.0314 208 ARG B NE    
3790 C  CZ    . ARG B 215 ? 0.4608 0.6562 0.6294 0.0631  -0.0102 -0.0293 208 ARG B CZ    
3791 N  NH1   . ARG B 215 ? 0.4666 0.6813 0.6531 0.0510  -0.0110 -0.0284 208 ARG B NH1   
3792 N  NH2   . ARG B 215 ? 0.4540 0.6195 0.6026 0.0676  -0.0195 -0.0285 208 ARG B NH2   
3793 N  N     . ASN B 216 ? 0.5375 0.8711 0.7659 0.0459  0.0649  -0.0238 209 ASN B N     
3794 C  CA    . ASN B 216 ? 0.5605 0.9148 0.7876 0.0467  0.0824  -0.0219 209 ASN B CA    
3795 C  C     . ASN B 216 ? 0.5617 0.9050 0.7695 0.0678  0.0825  -0.0295 209 ASN B C     
3796 O  O     . ASN B 216 ? 0.5738 0.9325 0.7928 0.0849  0.0777  -0.0392 209 ASN B O     
3797 C  CB    . ASN B 216 ? 0.5926 0.9983 0.8539 0.0441  0.0913  -0.0244 209 ASN B CB    
3798 C  CG    . ASN B 216 ? 0.6225 1.0525 0.8825 0.0418  0.1117  -0.0208 209 ASN B CG    
3799 O  OD1   . ASN B 216 ? 0.6238 1.0371 0.8572 0.0507  0.1181  -0.0207 209 ASN B OD1   
3800 N  ND2   . ASN B 216 ? 0.6512 1.1220 0.9397 0.0293  0.1223  -0.0180 209 ASN B ND2   
3801 N  N     . ALA B 217 ? 0.5546 0.8716 0.7336 0.0673  0.0874  -0.0256 210 ALA B N     
3802 C  CA    . ALA B 217 ? 0.5551 0.8540 0.7129 0.0852  0.0843  -0.0334 210 ALA B CA    
3803 C  C     . ALA B 217 ? 0.5894 0.9135 0.7443 0.0952  0.0990  -0.0379 210 ALA B C     
3804 O  O     . ALA B 217 ? 0.5990 0.9110 0.7363 0.1106  0.0976  -0.0461 210 ALA B O     
3805 C  CB    . ALA B 217 ? 0.5315 0.7907 0.6609 0.0794  0.0800  -0.0281 210 ALA B CB    
3806 N  N     . HIS B 218 ? 0.6121 0.9704 0.7832 0.0852  0.1133  -0.0324 211 HIS B N     
3807 C  CA    . HIS B 218 ? 0.6480 1.0291 0.8114 0.0900  0.1306  -0.0330 211 HIS B CA    
3808 C  C     . HIS B 218 ? 0.6725 1.0690 0.8369 0.1144  0.1312  -0.0480 211 HIS B C     
3809 O  O     . HIS B 218 ? 0.6964 1.0925 0.8394 0.1233  0.1402  -0.0516 211 HIS B O     
3810 C  CB    . HIS B 218 ? 0.6735 1.0929 0.8595 0.0740  0.1459  -0.0245 211 HIS B CB    
3811 C  CG    . HIS B 218 ? 0.6715 1.0713 0.8412 0.0536  0.1521  -0.0094 211 HIS B CG    
3812 N  ND1   . HIS B 218 ? 0.6859 1.0696 0.8234 0.0556  0.1604  -0.0047 211 HIS B ND1   
3813 C  CD2   . HIS B 218 ? 0.6627 1.0545 0.8412 0.0327  0.1507  0.0014  211 HIS B CD2   
3814 C  CE1   . HIS B 218 ? 0.6870 1.0537 0.8146 0.0369  0.1641  0.0096  211 HIS B CE1   
3815 N  NE2   . HIS B 218 ? 0.6731 1.0428 0.8251 0.0226  0.1584  0.0133  211 HIS B NE2   
3816 N  N     . SER B 219 ? 0.6696 1.0754 0.8553 0.1261  0.1202  -0.0571 212 SER B N     
3817 C  CA    . SER B 219 ? 0.7000 1.1218 0.8904 0.1508  0.1201  -0.0719 212 SER B CA    
3818 C  C     . SER B 219 ? 0.6930 1.0706 0.8548 0.1655  0.1074  -0.0801 212 SER B C     
3819 O  O     . SER B 219 ? 0.7228 1.1032 0.8814 0.1871  0.1061  -0.0932 212 SER B O     
3820 C  CB    . SER B 219 ? 0.7076 1.1593 0.9334 0.1580  0.1133  -0.0774 212 SER B CB    
3821 O  OG    . SER B 219 ? 0.6788 1.0992 0.9040 0.1590  0.0933  -0.0774 212 SER B OG    
3822 N  N     . LEU B 220 ? 0.6578 0.9947 0.7998 0.1537  0.0981  -0.0727 213 LEU B N     
3823 C  CA    . LEU B 220 ? 0.6522 0.9471 0.7682 0.1634  0.0863  -0.0792 213 LEU B CA    
3824 C  C     . LEU B 220 ? 0.6561 0.9346 0.7421 0.1592  0.0932  -0.0773 213 LEU B C     
3825 O  O     . LEU B 220 ? 0.6588 0.9061 0.7227 0.1667  0.0849  -0.0840 213 LEU B O     
3826 C  CB    . LEU B 220 ? 0.6148 0.8779 0.7304 0.1545  0.0703  -0.0735 213 LEU B CB    
3827 C  CG    . LEU B 220 ? 0.6137 0.8867 0.7537 0.1598  0.0599  -0.0755 213 LEU B CG    
3828 C  CD1   . LEU B 220 ? 0.5963 0.8940 0.7592 0.1424  0.0634  -0.0657 213 LEU B CD1   
3829 C  CD2   . LEU B 220 ? 0.5982 0.8302 0.7255 0.1622  0.0428  -0.0760 213 LEU B CD2   
3830 N  N     . THR B 221 ? 0.6606 0.9586 0.7452 0.1468  0.1074  -0.0678 214 THR B N     
3831 C  CA    . THR B 221 ? 0.6685 0.9520 0.7235 0.1431  0.1132  -0.0645 214 THR B CA    
3832 C  C     . THR B 221 ? 0.7100 0.9970 0.7473 0.1623  0.1175  -0.0784 214 THR B C     
3833 O  O     . THR B 221 ? 0.7409 1.0560 0.7921 0.1758  0.1241  -0.0875 214 THR B O     
3834 C  CB    . THR B 221 ? 0.6755 0.9786 0.7310 0.1270  0.1282  -0.0503 214 THR B CB    
3835 O  OG1   . THR B 221 ? 0.7109 1.0570 0.7842 0.1316  0.1431  -0.0528 214 THR B OG1   
3836 C  CG2   . THR B 221 ? 0.6398 0.9328 0.7077 0.1075  0.1233  -0.0372 214 THR B CG2   
3837 N  N     . ILE B 222 ? 0.7137 0.9731 0.7208 0.1637  0.1131  -0.0810 215 ILE B N     
3838 C  CA    . ILE B 222 ? 0.7562 1.0133 0.7416 0.1809  0.1151  -0.0954 215 ILE B CA    
3839 C  C     . ILE B 222 ? 0.7770 1.0371 0.7353 0.1757  0.1252  -0.0895 215 ILE B C     
3840 O  O     . ILE B 222 ? 0.7569 1.0156 0.7127 0.1593  0.1287  -0.0740 215 ILE B O     
3841 C  CB    . ILE B 222 ? 0.7520 0.9708 0.7258 0.1895  0.0973  -0.1072 215 ILE B CB    
3842 C  CG1   . ILE B 222 ? 0.7158 0.9025 0.6763 0.1747  0.0864  -0.0989 215 ILE B CG1   
3843 C  CG2   . ILE B 222 ? 0.7453 0.9621 0.7426 0.1978  0.0886  -0.1128 215 ILE B CG2   
3844 C  CD1   . ILE B 222 ? 0.7220 0.8730 0.6674 0.1807  0.0712  -0.1104 215 ILE B CD1   
3845 N  N     . SER B 223 ? 0.8247 1.0901 0.7619 0.1910  0.1304  -0.1023 216 SER B N     
3846 C  CA    . SER B 223 ? 0.8555 1.1251 0.7630 0.1892  0.1397  -0.0984 216 SER B CA    
3847 C  C     . SER B 223 ? 0.8455 1.0783 0.7268 0.1868  0.1247  -0.1009 216 SER B C     
3848 O  O     . SER B 223 ? 0.8323 1.0393 0.7150 0.1916  0.1095  -0.1115 216 SER B O     
3849 C  CB    . SER B 223 ? 0.9160 1.2089 0.8104 0.2070  0.1519  -0.1117 216 SER B CB    
3850 O  OG    . SER B 223 ? 0.9357 1.2065 0.8189 0.2240  0.1395  -0.1318 216 SER B OG    
3851 N  N     . ASP B 224 ? 0.8596 1.0920 0.7166 0.1800  0.1297  -0.0915 217 ASP B N     
3852 C  CA    . ASP B 224 ? 0.8616 1.0663 0.6920 0.1795  0.1167  -0.0948 217 ASP B CA    
3853 C  C     . ASP B 224 ? 0.8933 1.0842 0.7105 0.1957  0.1073  -0.1173 217 ASP B C     
3854 O  O     . ASP B 224 ? 0.8757 1.0384 0.6909 0.1939  0.0907  -0.1241 217 ASP B O     
3855 C  CB    . ASP B 224 ? 0.8926 1.1041 0.6940 0.1758  0.1249  -0.0843 217 ASP B CB    
3856 C  CG    . ASP B 224 ? 0.8746 1.0962 0.6850 0.1600  0.1351  -0.0616 217 ASP B CG    
3857 O  OD1   . ASP B 224 ? 0.8252 1.0363 0.6584 0.1484  0.1286  -0.0531 217 ASP B OD1   
3858 O  OD2   . ASP B 224 ? 0.9153 1.1535 0.7076 0.1592  0.1495  -0.0526 217 ASP B OD2   
3859 N  N     . ASP B 225 ? 0.9441 1.1550 0.7530 0.2112  0.1183  -0.1292 218 ASP B N     
3860 C  CA    . ASP B 225 ? 0.9854 1.1820 0.7791 0.2283  0.1103  -0.1520 218 ASP B CA    
3861 C  C     . ASP B 225 ? 0.9622 1.1377 0.7786 0.2321  0.0971  -0.1615 218 ASP B C     
3862 O  O     . ASP B 225 ? 0.9741 1.1190 0.7787 0.2360  0.0819  -0.1747 218 ASP B O     
3863 C  CB    . ASP B 225 ? 1.0472 1.2726 0.8293 0.2455  0.1267  -0.1627 218 ASP B CB    
3864 C  CG    . ASP B 225 ? 1.0924 1.3286 0.8385 0.2467  0.1357  -0.1601 218 ASP B CG    
3865 O  OD1   . ASP B 225 ? 1.0705 1.3040 0.8085 0.2317  0.1357  -0.1425 218 ASP B OD1   
3866 O  OD2   . ASP B 225 ? 1.1537 1.4000 0.8785 0.2635  0.1423  -0.1758 218 ASP B OD2   
3867 N  N     . GLU B 226 ? 0.9365 1.1281 0.7841 0.2314  0.1027  -0.1553 219 GLU B N     
3868 C  CA    . GLU B 226 ? 0.9166 1.0881 0.7847 0.2349  0.0901  -0.1614 219 GLU B CA    
3869 C  C     . GLU B 226 ? 0.8744 1.0109 0.7413 0.2197  0.0734  -0.1554 219 GLU B C     
3870 O  O     . GLU B 226 ? 0.8836 0.9892 0.7465 0.2238  0.0593  -0.1664 219 GLU B O     
3871 C  CB    . GLU B 226 ? 0.8925 1.0904 0.7947 0.2339  0.0980  -0.1528 219 GLU B CB    
3872 C  CG    . GLU B 226 ? 0.9393 1.1673 0.8504 0.2539  0.1096  -0.1648 219 GLU B CG    
3873 C  CD    . GLU B 226 ? 0.9235 1.1922 0.8670 0.2501  0.1225  -0.1541 219 GLU B CD    
3874 O  OE1   . GLU B 226 ? 0.8800 1.1549 0.8359 0.2306  0.1247  -0.1364 219 GLU B OE1   
3875 O  OE2   . GLU B 226 ? 0.9586 1.2537 0.9158 0.2670  0.1301  -0.1643 219 GLU B OE2   
3876 N  N     . PHE B 227 ? 0.8329 0.9735 0.7030 0.2022  0.0752  -0.1379 220 PHE B N     
3877 C  CA    . PHE B 227 ? 0.7943 0.9067 0.6650 0.1882  0.0609  -0.1321 220 PHE B CA    
3878 C  C     . PHE B 227 ? 0.8233 0.9112 0.6685 0.1908  0.0493  -0.1448 220 PHE B C     
3879 O  O     . PHE B 227 ? 0.8177 0.8774 0.6648 0.1878  0.0354  -0.1511 220 PHE B O     
3880 C  CB    . PHE B 227 ? 0.7548 0.8770 0.6301 0.1718  0.0656  -0.1127 220 PHE B CB    
3881 C  CG    . PHE B 227 ? 0.7162 0.8137 0.5946 0.1587  0.0522  -0.1070 220 PHE B CG    
3882 C  CD1   . PHE B 227 ? 0.6842 0.7683 0.5829 0.1537  0.0447  -0.1048 220 PHE B CD1   
3883 C  CD2   . PHE B 227 ? 0.7182 0.8068 0.5783 0.1528  0.0466  -0.1052 220 PHE B CD2   
3884 C  CE1   . PHE B 227 ? 0.6541 0.7174 0.5547 0.1418  0.0337  -0.1002 220 PHE B CE1   
3885 C  CE2   . PHE B 227 ? 0.6865 0.7563 0.5515 0.1414  0.0349  -0.1011 220 PHE B CE2   
3886 C  CZ    . PHE B 227 ? 0.6543 0.7122 0.5397 0.1356  0.0295  -0.0984 220 PHE B CZ    
3887 N  N     . ASP B 228 ? 0.8597 0.9589 0.6805 0.1959  0.0551  -0.1487 221 ASP B N     
3888 C  CA    . ASP B 228 ? 0.8928 0.9727 0.6878 0.1980  0.0438  -0.1613 221 ASP B CA    
3889 C  C     . ASP B 228 ? 0.9313 0.9881 0.7221 0.2098  0.0343  -0.1820 221 ASP B C     
3890 O  O     . ASP B 228 ? 0.9380 0.9674 0.7223 0.2045  0.0193  -0.1901 221 ASP B O     
3891 C  CB    . ASP B 228 ? 0.9338 1.0322 0.7008 0.2039  0.0525  -0.1622 221 ASP B CB    
3892 C  CG    . ASP B 228 ? 0.9063 1.0178 0.6705 0.1916  0.0578  -0.1421 221 ASP B CG    
3893 O  OD1   . ASP B 228 ? 0.8592 0.9596 0.6378 0.1781  0.0498  -0.1314 221 ASP B OD1   
3894 O  OD2   . ASP B 228 ? 0.9365 1.0685 0.6833 0.1959  0.0703  -0.1369 221 ASP B OD2   
3895 N  N     . ARG B 229 ? 0.9604 1.0286 0.7557 0.2257  0.0430  -0.1905 222 ARG B N     
3896 C  CA    . ARG B 229 ? 1.0041 1.0474 0.7953 0.2397  0.0340  -0.2106 222 ARG B CA    
3897 C  C     . ARG B 229 ? 0.9733 0.9853 0.7820 0.2294  0.0198  -0.2071 222 ARG B C     
3898 O  O     . ARG B 229 ? 1.0048 0.9832 0.8022 0.2295  0.0059  -0.2201 222 ARG B O     
3899 C  CB    . ARG B 229 ? 1.0359 1.1007 0.8351 0.2592  0.0463  -0.2180 222 ARG B CB    
3900 C  CG    . ARG B 229 ? 1.0945 1.1804 0.8690 0.2743  0.0577  -0.2300 222 ARG B CG    
3901 C  CD    . ARG B 229 ? 1.1340 1.2400 0.9179 0.2958  0.0687  -0.2408 222 ARG B CD    
3902 N  NE    . ARG B 229 ? 1.1269 1.2741 0.9359 0.2932  0.0855  -0.2250 222 ARG B NE    
3903 C  CZ    . ARG B 229 ? 1.1134 1.2944 0.9173 0.2870  0.1016  -0.2132 222 ARG B CZ    
3904 N  NH1   . ARG B 229 ? 1.1121 1.2926 0.8839 0.2862  0.1038  -0.2160 222 ARG B NH1   
3905 N  NH2   . ARG B 229 ? 1.1079 1.3225 0.9379 0.2814  0.1151  -0.1985 222 ARG B NH2   
3906 N  N     . PHE B 230 ? 0.9184 0.9406 0.7525 0.2203  0.0234  -0.1903 223 PHE B N     
3907 C  CA    . PHE B 230 ? 0.8914 0.8859 0.7402 0.2109  0.0114  -0.1856 223 PHE B CA    
3908 C  C     . PHE B 230 ? 0.8851 0.8545 0.7228 0.1955  -0.0011 -0.1861 223 PHE B C     
3909 O  O     . PHE B 230 ? 0.9020 0.8383 0.7384 0.1923  -0.0135 -0.1928 223 PHE B O     
3910 C  CB    . PHE B 230 ? 0.8327 0.8446 0.7069 0.2008  0.0171  -0.1664 223 PHE B CB    
3911 C  CG    . PHE B 230 ? 0.8067 0.7910 0.6928 0.1903  0.0054  -0.1603 223 PHE B CG    
3912 C  CD1   . PHE B 230 ? 0.7750 0.7467 0.6597 0.1721  -0.0012 -0.1520 223 PHE B CD1   
3913 C  CD2   . PHE B 230 ? 0.8204 0.7913 0.7174 0.1997  0.0009  -0.1634 223 PHE B CD2   
3914 C  CE1   . PHE B 230 ? 0.7562 0.7042 0.6503 0.1620  -0.0104 -0.1460 223 PHE B CE1   
3915 C  CE2   . PHE B 230 ? 0.8031 0.7472 0.7074 0.1899  -0.0093 -0.1566 223 PHE B CE2   
3916 C  CZ    . PHE B 230 ? 0.7715 0.7044 0.6738 0.1705  -0.0143 -0.1480 223 PHE B CZ    
3917 N  N     . CYS B 231 ? 0.8612 0.8475 0.6928 0.1851  0.0021  -0.1774 224 CYS B N     
3918 C  CA    . CYS B 231 ? 0.8533 0.8238 0.6777 0.1705  -0.0092 -0.1770 224 CYS B CA    
3919 C  C     . CYS B 231 ? 0.9144 0.8633 0.7168 0.1765  -0.0196 -0.1976 224 CYS B C     
3920 O  O     . CYS B 231 ? 0.9243 0.8462 0.7265 0.1666  -0.0327 -0.2030 224 CYS B O     
3921 C  CB    . CYS B 231 ? 0.8228 0.8176 0.6443 0.1621  -0.0034 -0.1638 224 CYS B CB    
3922 S  SG    . CYS B 231 ? 0.7541 0.7663 0.6012 0.1512  0.0055  -0.1404 224 CYS B SG    
3923 N  N     . GLU B 232 ? 0.9598 0.9205 0.7431 0.1921  -0.0135 -0.2093 225 GLU B N     
3924 C  CA    . GLU B 232 ? 1.0249 0.9656 0.7844 0.1993  -0.0233 -0.2308 225 GLU B CA    
3925 C  C     . GLU B 232 ? 1.0543 0.9575 0.8186 0.2018  -0.0340 -0.2424 225 GLU B C     
3926 O  O     . GLU B 232 ? 1.0880 0.9628 0.8423 0.1948  -0.0480 -0.2541 225 GLU B O     
3927 C  CB    . GLU B 232 ? 1.0736 1.0337 0.8118 0.2186  -0.0129 -0.2421 225 GLU B CB    
3928 C  CG    . GLU B 232 ? 1.0632 1.0549 0.7885 0.2164  -0.0038 -0.2322 225 GLU B CG    
3929 C  CD    . GLU B 232 ? 1.0978 1.1172 0.8093 0.2338  0.0127  -0.2356 225 GLU B CD    
3930 O  OE1   . GLU B 232 ? 1.0798 1.1271 0.7874 0.2305  0.0242  -0.2209 225 GLU B OE1   
3931 O  OE2   . GLU B 232 ? 1.1474 1.1603 0.8513 0.2507  0.0146  -0.2528 225 GLU B OE2   
3932 N  N     . ARG B 233 ? 1.0452 0.9483 0.8248 0.2116  -0.0276 -0.2386 226 ARG B N     
3933 C  CA    . ARG B 233 ? 1.0783 0.9455 0.8616 0.2177  -0.0365 -0.2476 226 ARG B CA    
3934 C  C     . ARG B 233 ? 1.0595 0.8965 0.8511 0.1968  -0.0494 -0.2408 226 ARG B C     
3935 O  O     . ARG B 233 ? 1.1009 0.8996 0.8890 0.1980  -0.0598 -0.2497 226 ARG B O     
3936 C  CB    . ARG B 233 ? 1.0621 0.9430 0.8639 0.2310  -0.0269 -0.2405 226 ARG B CB    
3937 C  CG    . ARG B 233 ? 1.1085 0.9545 0.9114 0.2440  -0.0352 -0.2510 226 ARG B CG    
3938 C  CD    . ARG B 233 ? 1.0849 0.9476 0.9100 0.2546  -0.0279 -0.2411 226 ARG B CD    
3939 N  NE    . ARG B 233 ? 1.0796 0.9880 0.9086 0.2677  -0.0119 -0.2416 226 ARG B NE    
3940 C  CZ    . ARG B 233 ? 1.0255 0.9720 0.8738 0.2623  -0.0001 -0.2253 226 ARG B CZ    
3941 N  NH1   . ARG B 233 ? 0.9741 0.9187 0.8422 0.2492  -0.0030 -0.2086 226 ARG B NH1   
3942 N  NH2   . ARG B 233 ? 1.0291 1.0151 0.8761 0.2702  0.0146  -0.2261 226 ARG B NH2   
3943 N  N     . HIS B 234 ? 1.0022 0.8561 0.8043 0.1780  -0.0483 -0.2249 227 HIS B N     
3944 C  CA    . HIS B 234 ? 0.9790 0.8121 0.7919 0.1574  -0.0577 -0.2161 227 HIS B CA    
3945 C  C     . HIS B 234 ? 0.9753 0.8143 0.7820 0.1417  -0.0644 -0.2177 227 HIS B C     
3946 O  O     . HIS B 234 ? 0.9368 0.7780 0.7568 0.1237  -0.0673 -0.2057 227 HIS B O     
3947 C  CB    . HIS B 234 ? 0.9125 0.7620 0.7479 0.1499  -0.0503 -0.1948 227 HIS B CB    
3948 C  CG    . HIS B 234 ? 0.9191 0.7600 0.7629 0.1630  -0.0472 -0.1931 227 HIS B CG    
3949 N  ND1   . HIS B 234 ? 0.9086 0.7782 0.7578 0.1786  -0.0355 -0.1912 227 HIS B ND1   
3950 C  CD2   . HIS B 234 ? 0.9430 0.7511 0.7897 0.1642  -0.0545 -0.1937 227 HIS B CD2   
3951 C  CE1   . HIS B 234 ? 0.9231 0.7802 0.7804 0.1896  -0.0365 -0.1915 227 HIS B CE1   
3952 N  NE2   . HIS B 234 ? 0.9447 0.7629 0.7991 0.1817  -0.0483 -0.1926 227 HIS B NE2   
3953 N  N     . SER B 235 ? 1.0205 0.8626 0.8065 0.1493  -0.0676 -0.2336 228 SER B N     
3954 C  CA    . SER B 235 ? 1.0205 0.8760 0.7988 0.1384  -0.0737 -0.2357 228 SER B CA    
3955 C  C     . SER B 235 ? 1.0388 0.8686 0.8221 0.1190  -0.0885 -0.2407 228 SER B C     
3956 O  O     . SER B 235 ? 1.0271 0.8711 0.8127 0.1062  -0.0942 -0.2387 228 SER B O     
3957 C  CB    . SER B 235 ? 1.0721 0.9365 0.8243 0.1532  -0.0736 -0.2523 228 SER B CB    
3958 O  OG    . SER B 235 ? 1.1357 0.9713 0.8745 0.1663  -0.0778 -0.2711 228 SER B OG    
3959 N  N     . SER B 236 ? 1.0702 0.8630 0.8561 0.1163  -0.0948 -0.2461 229 SER B N     
3960 C  CA    . SER B 236 ? 1.0930 0.8603 0.8845 0.0954  -0.1077 -0.2494 229 SER B CA    
3961 C  C     . SER B 236 ? 1.0359 0.8088 0.8511 0.0778  -0.1044 -0.2288 229 SER B C     
3962 O  O     . SER B 236 ? 1.0523 0.8064 0.8750 0.0586  -0.1129 -0.2287 229 SER B O     
3963 C  CB    . SER B 236 ? 1.1647 0.8849 0.9447 0.0990  -0.1167 -0.2647 229 SER B CB    
3964 O  OG    . SER B 236 ? 1.1543 0.8563 0.9421 0.1061  -0.1112 -0.2551 229 SER B OG    
3965 N  N     . GLN B 237 ? 0.9746 0.7723 0.8012 0.0838  -0.0920 -0.2120 230 GLN B N     
3966 C  CA    . GLN B 237 ? 0.9208 0.7271 0.7678 0.0689  -0.0882 -0.1933 230 GLN B CA    
3967 C  C     . GLN B 237 ? 0.8816 0.7236 0.7355 0.0608  -0.0866 -0.1869 230 GLN B C     
3968 O  O     . GLN B 237 ? 0.8502 0.7200 0.7022 0.0712  -0.0784 -0.1812 230 GLN B O     
3969 C  CB    . GLN B 237 ? 0.8825 0.6934 0.7378 0.0792  -0.0774 -0.1800 230 GLN B CB    
3970 C  CG    . GLN B 237 ? 0.9249 0.7031 0.7732 0.0912  -0.0795 -0.1865 230 GLN B CG    
3971 C  CD    . GLN B 237 ? 0.9627 0.7011 0.8112 0.0769  -0.0893 -0.1874 230 GLN B CD    
3972 O  OE1   . GLN B 237 ? 0.9467 0.6857 0.8049 0.0567  -0.0919 -0.1795 230 GLN B OE1   
3973 N  NE2   . GLN B 237 ? 1.0186 0.7215 0.8560 0.0877  -0.0945 -0.1969 230 GLN B NE2   
3974 N  N     . THR B 238 ? 0.8898 0.7303 0.7519 0.0420  -0.0950 -0.1881 231 THR B N     
3975 C  CA    . THR B 238 ? 0.8639 0.7369 0.7332 0.0347  -0.0964 -0.1843 231 THR B CA    
3976 C  C     . THR B 238 ? 0.7988 0.6926 0.6857 0.0308  -0.0864 -0.1646 231 THR B C     
3977 O  O     . THR B 238 ? 0.7710 0.6929 0.6651 0.0278  -0.0856 -0.1587 231 THR B O     
3978 C  CB    . THR B 238 ? 0.8989 0.7660 0.7746 0.0154  -0.1090 -0.1931 231 THR B CB    
3979 O  OG1   . THR B 238 ? 0.8863 0.7399 0.7785 -0.0006 -0.1072 -0.1828 231 THR B OG1   
3980 C  CG2   . THR B 238 ? 0.9716 0.8106 0.8308 0.0157  -0.1207 -0.2138 231 THR B CG2   
3981 N  N     . CYS B 239 ? 0.7800 0.6584 0.6728 0.0316  -0.0798 -0.1550 232 CYS B N     
3982 C  CA    . CYS B 239 ? 0.7237 0.6185 0.6311 0.0286  -0.0706 -0.1376 232 CYS B CA    
3983 C  C     . CYS B 239 ? 0.6922 0.6029 0.5957 0.0450  -0.0605 -0.1310 232 CYS B C     
3984 O  O     . CYS B 239 ? 0.6471 0.5734 0.5611 0.0440  -0.0531 -0.1175 232 CYS B O     
3985 C  CB    . CYS B 239 ? 0.7245 0.5953 0.6395 0.0192  -0.0697 -0.1302 232 CYS B CB    
3986 S  SG    . CYS B 239 ? 0.7524 0.5920 0.6558 0.0341  -0.0687 -0.1338 232 CYS B SG    
3987 N  N     . LEU B 240 ? 0.7190 0.6281 0.6075 0.0596  -0.0601 -0.1408 233 LEU B N     
3988 C  CA    . LEU B 240 ? 0.6965 0.6210 0.5825 0.0738  -0.0494 -0.1347 233 LEU B CA    
3989 C  C     . LEU B 240 ? 0.6677 0.6214 0.5537 0.0745  -0.0446 -0.1267 233 LEU B C     
3990 O  O     . LEU B 240 ? 0.6885 0.6514 0.5643 0.0752  -0.0498 -0.1334 233 LEU B O     
3991 C  CB    . LEU B 240 ? 0.7411 0.6568 0.6108 0.0893  -0.0494 -0.1485 233 LEU B CB    
3992 C  CG    . LEU B 240 ? 0.7322 0.6713 0.5954 0.1037  -0.0384 -0.1455 233 LEU B CG    
3993 C  CD1   . LEU B 240 ? 0.6999 0.6441 0.5768 0.1076  -0.0292 -0.1343 233 LEU B CD1   
3994 C  CD2   . LEU B 240 ? 0.7859 0.7200 0.6297 0.1183  -0.0392 -0.1619 233 LEU B CD2   
3995 N  N     . VAL B 241 ? 0.6252 0.5918 0.5214 0.0753  -0.0354 -0.1124 234 VAL B N     
3996 C  CA    . VAL B 241 ? 0.6011 0.5907 0.4966 0.0772  -0.0294 -0.1027 234 VAL B CA    
3997 C  C     . VAL B 241 ? 0.5950 0.5940 0.4875 0.0880  -0.0182 -0.0975 234 VAL B C     
3998 O  O     . VAL B 241 ? 0.5679 0.5669 0.4728 0.0866  -0.0125 -0.0890 234 VAL B O     
3999 C  CB    . VAL B 241 ? 0.5608 0.5563 0.4723 0.0666  -0.0286 -0.0904 234 VAL B CB    
4000 C  CG1   . VAL B 241 ? 0.5428 0.5575 0.4520 0.0699  -0.0231 -0.0804 234 VAL B CG1   
4001 C  CG2   . VAL B 241 ? 0.5687 0.5589 0.4866 0.0548  -0.0381 -0.0952 234 VAL B CG2   
4002 N  N     . PRO B 242 ? 0.6236 0.6323 0.4998 0.0985  -0.0146 -0.1027 235 PRO B N     
4003 C  CA    . PRO B 242 ? 0.6234 0.6442 0.4984 0.1074  -0.0025 -0.0980 235 PRO B CA    
4004 C  C     . PRO B 242 ? 0.5982 0.6354 0.4758 0.1045  0.0056  -0.0825 235 PRO B C     
4005 O  O     . PRO B 242 ? 0.6027 0.6457 0.4706 0.1029  0.0031  -0.0789 235 PRO B O     
4006 C  CB    . PRO B 242 ? 0.6727 0.6971 0.5260 0.1192  -0.0019 -0.1106 235 PRO B CB    
4007 C  CG    . PRO B 242 ? 0.6883 0.7113 0.5293 0.1151  -0.0121 -0.1150 235 PRO B CG    
4008 C  CD    . PRO B 242 ? 0.6623 0.6725 0.5200 0.1021  -0.0215 -0.1136 235 PRO B CD    
4009 N  N     . GLU B 243 ? 0.5786 0.6229 0.4683 0.1046  0.0149  -0.0742 236 GLU B N     
4010 C  CA    . GLU B 243 ? 0.5626 0.6196 0.4549 0.1013  0.0237  -0.0600 236 GLU B CA    
4011 C  C     . GLU B 243 ? 0.5791 0.6513 0.4713 0.1077  0.0361  -0.0582 236 GLU B C     
4012 O  O     . GLU B 243 ? 0.5626 0.6399 0.4716 0.1058  0.0412  -0.0543 236 GLU B O     
4013 C  CB    . GLU B 243 ? 0.5218 0.5735 0.4326 0.0914  0.0224  -0.0504 236 GLU B CB    
4014 C  CG    . GLU B 243 ? 0.5091 0.5489 0.4221 0.0852  0.0116  -0.0532 236 GLU B CG    
4015 C  CD    . GLU B 243 ? 0.4757 0.5135 0.4011 0.0766  0.0112  -0.0429 236 GLU B CD    
4016 O  OE1   . GLU B 243 ? 0.4642 0.5077 0.3943 0.0750  0.0185  -0.0332 236 GLU B OE1   
4017 O  OE2   . GLU B 243 ? 0.4661 0.4968 0.3960 0.0712  0.0037  -0.0454 236 GLU B OE2   
4018 N  N     . PRO B 244 ? 0.6155 0.6979 0.4884 0.1149  0.0416  -0.0604 237 PRO B N     
4019 C  CA    . PRO B 244 ? 0.6333 0.7348 0.5057 0.1183  0.0562  -0.0548 237 PRO B CA    
4020 C  C     . PRO B 244 ? 0.6130 0.7201 0.4944 0.1082  0.0634  -0.0375 237 PRO B C     
4021 O  O     . PRO B 244 ? 0.5935 0.6897 0.4741 0.1012  0.0575  -0.0298 237 PRO B O     
4022 C  CB    . PRO B 244 ? 0.6810 0.7891 0.5255 0.1274  0.0591  -0.0603 237 PRO B CB    
4023 C  CG    . PRO B 244 ? 0.6801 0.7735 0.5117 0.1253  0.0455  -0.0630 237 PRO B CG    
4024 C  CD    . PRO B 244 ? 0.6456 0.7232 0.4961 0.1197  0.0343  -0.0686 237 PRO B CD    
4025 N  N     . ASN B 245 ? 0.6229 0.7477 0.5128 0.1073  0.0763  -0.0318 238 ASN B N     
4026 C  CA    . ASN B 245 ? 0.6108 0.7391 0.5097 0.0961  0.0833  -0.0159 238 ASN B CA    
4027 C  C     . ASN B 245 ? 0.6212 0.7384 0.5003 0.0925  0.0816  -0.0051 238 ASN B C     
4028 O  O     . ASN B 245 ? 0.5991 0.7053 0.4855 0.0838  0.0785  0.0044  238 ASN B O     
4029 C  CB    . ASN B 245 ? 0.6340 0.7861 0.5410 0.0948  0.0989  -0.0111 238 ASN B CB    
4030 C  CG    . ASN B 245 ? 0.6205 0.7858 0.5534 0.0973  0.0999  -0.0190 238 ASN B CG    
4031 O  OD1   . ASN B 245 ? 0.6417 0.8309 0.5842 0.0974  0.1123  -0.0172 238 ASN B OD1   
4032 N  ND2   . ASN B 245 ? 0.5915 0.7431 0.5353 0.0997  0.0876  -0.0275 238 ASN B ND2   
4033 N  N     . ARG B 246 ? 0.6598 0.7798 0.5126 0.1001  0.0832  -0.0069 239 ARG B N     
4034 C  CA    . ARG B 246 ? 0.6806 0.7921 0.5117 0.0991  0.0819  0.0040  239 ARG B CA    
4035 C  C     . ARG B 246 ? 0.6490 0.7426 0.4848 0.0962  0.0674  0.0044  239 ARG B C     
4036 O  O     . ARG B 246 ? 0.6511 0.7354 0.4820 0.0920  0.0668  0.0168  239 ARG B O     
4037 C  CB    . ARG B 246 ? 0.7284 0.8465 0.5300 0.1101  0.0830  -0.0023 239 ARG B CB    
4038 C  CG    . ARG B 246 ? 0.7594 0.8691 0.5336 0.1124  0.0792  0.0072  239 ARG B CG    
4039 C  CD    . ARG B 246 ? 0.8066 0.9231 0.5516 0.1242  0.0775  -0.0026 239 ARG B CD    
4040 N  NE    . ARG B 246 ? 0.8287 0.9354 0.5507 0.1281  0.0669  0.0021  239 ARG B NE    
4041 C  CZ    . ARG B 246 ? 0.8177 0.9177 0.5389 0.1318  0.0501  -0.0087 239 ARG B CZ    
4042 N  NH1   . ARG B 246 ? 0.7872 0.8858 0.5272 0.1312  0.0424  -0.0246 239 ARG B NH1   
4043 N  NH2   . ARG B 246 ? 0.8421 0.9368 0.5438 0.1361  0.0408  -0.0032 239 ARG B NH2   
4044 N  N     . LEU B 247 ? 0.6243 0.7132 0.4700 0.0985  0.0565  -0.0091 240 LEU B N     
4045 C  CA    . LEU B 247 ? 0.5988 0.6753 0.4498 0.0959  0.0436  -0.0105 240 LEU B CA    
4046 C  C     . LEU B 247 ? 0.5566 0.6263 0.4321 0.0870  0.0429  -0.0062 240 LEU B C     
4047 O  O     . LEU B 247 ? 0.5402 0.6015 0.4197 0.0835  0.0370  -0.0012 240 LEU B O     
4048 C  CB    . LEU B 247 ? 0.6012 0.6754 0.4496 0.1007  0.0326  -0.0267 240 LEU B CB    
4049 C  CG    . LEU B 247 ? 0.6450 0.7234 0.4670 0.1094  0.0289  -0.0327 240 LEU B CG    
4050 C  CD1   . LEU B 247 ? 0.6481 0.7215 0.4701 0.1113  0.0159  -0.0491 240 LEU B CD1   
4051 C  CD2   . LEU B 247 ? 0.6622 0.7398 0.4688 0.1106  0.0270  -0.0207 240 LEU B CD2   
4052 N  N     . MET B 248 ? 0.5423 0.6170 0.4339 0.0844  0.0484  -0.0087 241 MET B N     
4053 C  CA    . MET B 248 ? 0.5064 0.5749 0.4192 0.0766  0.0465  -0.0059 241 MET B CA    
4054 C  C     . MET B 248 ? 0.5054 0.5731 0.4230 0.0691  0.0537  0.0076  241 MET B C     
4055 O  O     . MET B 248 ? 0.4812 0.5396 0.4099 0.0631  0.0498  0.0109  241 MET B O     
4056 C  CB    . MET B 248 ? 0.4964 0.5700 0.4239 0.0779  0.0473  -0.0144 241 MET B CB    
4057 C  CG    . MET B 248 ? 0.4630 0.5288 0.4092 0.0711  0.0427  -0.0134 241 MET B CG    
4058 S  SD    . MET B 248 ? 0.4581 0.5269 0.4187 0.0752  0.0408  -0.0233 241 MET B SD    
4059 C  CE    . MET B 248 ? 0.4243 0.4777 0.3965 0.0671  0.0320  -0.0212 241 MET B CE    
4060 N  N     . ALA B 249 ? 0.5351 0.6115 0.4445 0.0685  0.0645  0.0154  242 ALA B N     
4061 C  CA    . ALA B 249 ? 0.5389 0.6142 0.4564 0.0589  0.0721  0.0274  242 ALA B CA    
4062 C  C     . ALA B 249 ? 0.5295 0.5857 0.4451 0.0545  0.0662  0.0351  242 ALA B C     
4063 O  O     . ALA B 249 ? 0.5123 0.5624 0.4429 0.0466  0.0658  0.0380  242 ALA B O     
4064 C  CB    . ALA B 249 ? 0.5812 0.6668 0.4861 0.0579  0.0849  0.0363  242 ALA B CB    
4065 N  N     . LYS B 250 ? 0.5459 0.5936 0.4426 0.0606  0.0615  0.0380  243 LYS B N     
4066 C  CA    . LYS B 250 ? 0.5527 0.5830 0.4439 0.0587  0.0581  0.0475  243 LYS B CA    
4067 C  C     . LYS B 250 ? 0.5388 0.5633 0.4266 0.0659  0.0459  0.0417  243 LYS B C     
4068 O  O     . LYS B 250 ? 0.5533 0.5653 0.4327 0.0684  0.0423  0.0488  243 LYS B O     
4069 C  CB    . LYS B 250 ? 0.6013 0.6262 0.4712 0.0590  0.0655  0.0610  243 LYS B CB    
4070 C  CG    . LYS B 250 ? 0.6244 0.6623 0.4950 0.0527  0.0792  0.0658  243 LYS B CG    
4071 C  CD    . LYS B 250 ? 0.6682 0.6956 0.5278 0.0449  0.0887  0.0826  243 LYS B CD    
4072 C  CE    . LYS B 250 ? 0.6587 0.6835 0.5403 0.0308  0.0939  0.0863  243 LYS B CE    
4073 N  NZ    . LYS B 250 ? 0.7034 0.7340 0.5809 0.0205  0.1084  0.0985  243 LYS B NZ    
4074 N  N     . SER B 251 ? 0.5141 0.5469 0.4099 0.0686  0.0397  0.0291  244 SER B N     
4075 C  CA    . SER B 251 ? 0.5072 0.5403 0.4006 0.0743  0.0288  0.0221  244 SER B CA    
4076 C  C     . SER B 251 ? 0.4724 0.5014 0.3842 0.0699  0.0235  0.0177  244 SER B C     
4077 O  O     . SER B 251 ? 0.4643 0.4965 0.3789 0.0724  0.0154  0.0112  244 SER B O     
4078 C  CB    . SER B 251 ? 0.5138 0.5573 0.4013 0.0789  0.0254  0.0111  244 SER B CB    
4079 O  OG    . SER B 251 ? 0.4902 0.5366 0.3923 0.0750  0.0259  0.0023  244 SER B OG    
4080 N  N     . TYR B 252 ? 0.4562 0.4792 0.3799 0.0629  0.0282  0.0212  245 TYR B N     
4081 C  CA    . TYR B 252 ? 0.4284 0.4469 0.3665 0.0589  0.0240  0.0176  245 TYR B CA    
4082 C  C     . TYR B 252 ? 0.4334 0.4393 0.3724 0.0571  0.0252  0.0252  245 TYR B C     
4083 O  O     . TYR B 252 ? 0.4547 0.4527 0.3873 0.0553  0.0305  0.0339  245 TYR B O     
4084 C  CB    . TYR B 252 ? 0.4064 0.4271 0.3580 0.0528  0.0260  0.0129  245 TYR B CB    
4085 C  CG    . TYR B 252 ? 0.4018 0.4300 0.3544 0.0548  0.0233  0.0037  245 TYR B CG    
4086 C  CD1   . TYR B 252 ? 0.4210 0.4565 0.3651 0.0591  0.0267  0.0018  245 TYR B CD1   
4087 C  CD2   . TYR B 252 ? 0.3844 0.4108 0.3449 0.0525  0.0176  -0.0032 245 TYR B CD2   
4088 C  CE1   . TYR B 252 ? 0.4228 0.4618 0.3666 0.0620  0.0235  -0.0079 245 TYR B CE1   
4089 C  CE2   . TYR B 252 ? 0.3874 0.4157 0.3475 0.0539  0.0144  -0.0115 245 TYR B CE2   
4090 C  CZ    . TYR B 252 ? 0.4069 0.4405 0.3585 0.0592  0.0168  -0.0144 245 TYR B CZ    
4091 O  OH    . TYR B 252 ? 0.4137 0.4456 0.3647 0.0611  0.0130  -0.0237 245 TYR B OH    
4092 N  N     . LEU B 253 ? 0.4187 0.4221 0.3648 0.0578  0.0202  0.0215  246 LEU B N     
4093 C  CA    . LEU B 253 ? 0.4222 0.4127 0.3708 0.0565  0.0207  0.0255  246 LEU B CA    
4094 C  C     . LEU B 253 ? 0.3987 0.3881 0.3597 0.0487  0.0218  0.0213  246 LEU B C     
4095 O  O     . LEU B 253 ? 0.3790 0.3753 0.3470 0.0478  0.0187  0.0144  246 LEU B O     
4096 C  CB    . LEU B 253 ? 0.4259 0.4176 0.3741 0.0641  0.0149  0.0230  246 LEU B CB    
4097 C  CG    . LEU B 253 ? 0.4563 0.4468 0.3911 0.0738  0.0121  0.0283  246 LEU B CG    
4098 C  CD1   . LEU B 253 ? 0.4588 0.4575 0.3976 0.0823  0.0052  0.0237  246 LEU B CD1   
4099 C  CD2   . LEU B 253 ? 0.4868 0.4577 0.4104 0.0740  0.0161  0.0391  246 LEU B CD2   
4100 N  N     . ILE B 254 ? 0.4059 0.3866 0.3688 0.0426  0.0258  0.0256  247 ILE B N     
4101 C  CA    . ILE B 254 ? 0.3888 0.3704 0.3626 0.0353  0.0261  0.0218  247 ILE B CA    
4102 C  C     . ILE B 254 ? 0.3987 0.3654 0.3735 0.0318  0.0256  0.0232  247 ILE B C     
4103 O  O     . ILE B 254 ? 0.4225 0.3781 0.3937 0.0286  0.0284  0.0294  247 ILE B O     
4104 C  CB    . ILE B 254 ? 0.3907 0.3809 0.3694 0.0305  0.0306  0.0234  247 ILE B CB    
4105 C  CG1   . ILE B 254 ? 0.3870 0.3899 0.3624 0.0356  0.0309  0.0204  247 ILE B CG1   
4106 C  CG2   . ILE B 254 ? 0.3776 0.3702 0.3684 0.0240  0.0293  0.0196  247 ILE B CG2   
4107 C  CD1   . ILE B 254 ? 0.3980 0.4118 0.3754 0.0339  0.0370  0.0222  247 ILE B CD1   
4108 N  N     . LEU B 255 ? 0.3846 0.3503 0.3635 0.0316  0.0222  0.0172  248 LEU B N     
4109 C  CA    . LEU B 255 ? 0.3942 0.3469 0.3739 0.0279  0.0211  0.0158  248 LEU B CA    
4110 C  C     . LEU B 255 ? 0.3846 0.3414 0.3726 0.0199  0.0201  0.0129  248 LEU B C     
4111 O  O     . LEU B 255 ? 0.3653 0.3330 0.3574 0.0199  0.0184  0.0093  248 LEU B O     
4112 C  CB    . LEU B 255 ? 0.3902 0.3414 0.3675 0.0335  0.0185  0.0104  248 LEU B CB    
4113 C  CG    . LEU B 255 ? 0.4067 0.3533 0.3775 0.0430  0.0181  0.0120  248 LEU B CG    
4114 C  CD1   . LEU B 255 ? 0.4013 0.3535 0.3736 0.0479  0.0167  0.0054  248 LEU B CD1   
4115 C  CD2   . LEU B 255 ? 0.4398 0.3652 0.4035 0.0438  0.0187  0.0170  248 LEU B CD2   
4116 N  N     . ASP B 256 ? 0.4029 0.3494 0.3927 0.0132  0.0200  0.0140  249 ASP B N     
4117 C  CA    . ASP B 256 ? 0.3994 0.3512 0.3981 0.0057  0.0175  0.0107  249 ASP B CA    
4118 C  C     . ASP B 256 ? 0.3997 0.3438 0.3944 0.0062  0.0127  0.0041  249 ASP B C     
4119 O  O     . ASP B 256 ? 0.3979 0.3371 0.3848 0.0128  0.0126  0.0018  249 ASP B O     
4120 C  CB    . ASP B 256 ? 0.4228 0.3714 0.4278 -0.0036 0.0198  0.0149  249 ASP B CB    
4121 C  CG    . ASP B 256 ? 0.4537 0.3801 0.4536 -0.0084 0.0182  0.0148  249 ASP B CG    
4122 O  OD1   . ASP B 256 ? 0.4576 0.3707 0.4478 -0.0021 0.0155  0.0110  249 ASP B OD1   
4123 O  OD2   . ASP B 256 ? 0.4782 0.4006 0.4842 -0.0188 0.0197  0.0182  249 ASP B OD2   
4124 N  N     . GLU B 257 ? 0.4047 0.3506 0.4050 -0.0002 0.0086  0.0006  250 GLU B N     
4125 C  CA    . GLU B 257 ? 0.4083 0.3491 0.4029 0.0000  0.0036  -0.0058 250 GLU B CA    
4126 C  C     . GLU B 257 ? 0.4347 0.3559 0.4201 0.0002  0.0027  -0.0092 250 GLU B C     
4127 O  O     . GLU B 257 ? 0.4414 0.3578 0.4185 0.0026  -0.0002 -0.0153 250 GLU B O     
4128 C  CB    . GLU B 257 ? 0.4102 0.3601 0.4128 -0.0059 -0.0020 -0.0086 250 GLU B CB    
4129 C  CG    . GLU B 257 ? 0.4323 0.3816 0.4453 -0.0158 -0.0041 -0.0088 250 GLU B CG    
4130 C  CD    . GLU B 257 ? 0.4312 0.3942 0.4586 -0.0207 0.0003  -0.0031 250 GLU B CD    
4131 O  OE1   . GLU B 257 ? 0.4164 0.3851 0.4431 -0.0155 0.0065  0.0018  250 GLU B OE1   
4132 O  OE2   . GLU B 257 ? 0.4473 0.4181 0.4872 -0.0296 -0.0023 -0.0043 250 GLU B OE2   
4133 N  N     . TYR B 258 ? 0.4546 0.3636 0.4402 -0.0019 0.0053  -0.0052 251 TYR B N     
4134 C  CA    . TYR B 258 ? 0.4868 0.3726 0.4625 0.0000  0.0045  -0.0078 251 TYR B CA    
4135 C  C     . TYR B 258 ? 0.4878 0.3680 0.4560 0.0111  0.0084  -0.0045 251 TYR B C     
4136 O  O     . TYR B 258 ? 0.5187 0.3782 0.4784 0.0154  0.0080  -0.0057 251 TYR B O     
4137 C  CB    . TYR B 258 ? 0.5182 0.3906 0.4986 -0.0112 0.0039  -0.0047 251 TYR B CB    
4138 C  CG    . TYR B 258 ? 0.5279 0.4048 0.5167 -0.0225 -0.0017 -0.0101 251 TYR B CG    
4139 C  CD1   . TYR B 258 ? 0.5526 0.4153 0.5339 -0.0241 -0.0081 -0.0195 251 TYR B CD1   
4140 C  CD2   . TYR B 258 ? 0.5147 0.4126 0.5193 -0.0306 -0.0013 -0.0066 251 TYR B CD2   
4141 C  CE1   . TYR B 258 ? 0.5644 0.4332 0.5534 -0.0343 -0.0150 -0.0251 251 TYR B CE1   
4142 C  CE2   . TYR B 258 ? 0.5253 0.4312 0.5397 -0.0400 -0.0077 -0.0120 251 TYR B CE2   
4143 C  CZ    . TYR B 258 ? 0.5501 0.4414 0.5567 -0.0422 -0.0151 -0.0211 251 TYR B CZ    
4144 O  OH    . TYR B 258 ? 0.5638 0.4643 0.5795 -0.0511 -0.0232 -0.0272 251 TYR B OH    
4145 N  N     . MET B 259 ? 0.4584 0.3564 0.4294 0.0166  0.0113  -0.0013 252 MET B N     
4146 C  CA    . MET B 259 ? 0.4574 0.3565 0.4240 0.0269  0.0139  0.0018  252 MET B CA    
4147 C  C     . MET B 259 ? 0.4862 0.3691 0.4482 0.0274  0.0155  0.0095  252 MET B C     
4148 O  O     . MET B 259 ? 0.5064 0.3784 0.4606 0.0371  0.0153  0.0108  252 MET B O     
4149 C  CB    . MET B 259 ? 0.4644 0.3612 0.4248 0.0366  0.0132  -0.0049 252 MET B CB    
4150 C  CG    . MET B 259 ? 0.4453 0.3554 0.4071 0.0347  0.0126  -0.0112 252 MET B CG    
4151 S  SD    . MET B 259 ? 0.4499 0.3679 0.4071 0.0454  0.0148  -0.0179 252 MET B SD    
4152 C  CE    . MET B 259 ? 0.4202 0.3624 0.3859 0.0477  0.0172  -0.0138 252 MET B CE    
4153 N  N     . ARG B 260 ? 0.4893 0.3733 0.4563 0.0174  0.0174  0.0152  253 ARG B N     
4154 C  CA    . ARG B 260 ? 0.5143 0.3886 0.4771 0.0155  0.0208  0.0251  253 ARG B CA    
4155 C  C     . ARG B 260 ? 0.4914 0.3868 0.4565 0.0181  0.0244  0.0300  253 ARG B C     
4156 O  O     . ARG B 260 ? 0.4618 0.3771 0.4359 0.0151  0.0248  0.0268  253 ARG B O     
4157 C  CB    . ARG B 260 ? 0.5369 0.4029 0.5055 0.0008  0.0220  0.0280  253 ARG B CB    
4158 C  CG    . ARG B 260 ? 0.5613 0.4076 0.5286 -0.0041 0.0172  0.0210  253 ARG B CG    
4159 C  CD    . ARG B 260 ? 0.5896 0.4285 0.5644 -0.0206 0.0177  0.0237  253 ARG B CD    
4160 N  NE    . ARG B 260 ? 0.5621 0.4286 0.5530 -0.0288 0.0180  0.0216  253 ARG B NE    
4161 C  CZ    . ARG B 260 ? 0.5792 0.4514 0.5826 -0.0435 0.0190  0.0235  253 ARG B CZ    
4162 N  NH1   . ARG B 260 ? 0.6262 0.4755 0.6272 -0.0542 0.0197  0.0275  253 ARG B NH1   
4163 N  NH2   . ARG B 260 ? 0.5536 0.4540 0.5724 -0.0475 0.0185  0.0206  253 ARG B NH2   
4164 N  N     . PHE B 261 ? 0.5103 0.3998 0.4654 0.0246  0.0263  0.0375  254 PHE B N     
4165 C  CA    . PHE B 261 ? 0.4977 0.4050 0.4518 0.0270  0.0295  0.0418  254 PHE B CA    
4166 C  C     . PHE B 261 ? 0.5088 0.4210 0.4674 0.0155  0.0355  0.0480  254 PHE B C     
4167 O  O     . PHE B 261 ? 0.5430 0.4386 0.4988 0.0077  0.0382  0.0544  254 PHE B O     
4168 C  CB    . PHE B 261 ? 0.5218 0.4210 0.4615 0.0381  0.0287  0.0481  254 PHE B CB    
4169 C  CG    . PHE B 261 ? 0.5070 0.4137 0.4461 0.0506  0.0234  0.0417  254 PHE B CG    
4170 C  CD1   . PHE B 261 ? 0.4721 0.4024 0.4184 0.0527  0.0220  0.0353  254 PHE B CD1   
4171 C  CD2   . PHE B 261 ? 0.5307 0.4212 0.4637 0.0596  0.0197  0.0409  254 PHE B CD2   
4172 C  CE1   . PHE B 261 ? 0.4621 0.4019 0.4105 0.0618  0.0177  0.0294  254 PHE B CE1   
4173 C  CE2   . PHE B 261 ? 0.5193 0.4218 0.4549 0.0709  0.0156  0.0344  254 PHE B CE2   
4174 C  CZ    . PHE B 261 ? 0.4847 0.4130 0.4288 0.0710  0.0148  0.0289  254 PHE B CZ    
4175 N  N     . LEU B 262 ? 0.4843 0.4196 0.4502 0.0145  0.0380  0.0458  255 LEU B N     
4176 C  CA    . LEU B 262 ? 0.4946 0.4410 0.4674 0.0050  0.0446  0.0503  255 LEU B CA    
4177 C  C     . LEU B 262 ? 0.5114 0.4645 0.4725 0.0096  0.0503  0.0576  255 LEU B C     
4178 O  O     . LEU B 262 ? 0.4976 0.4583 0.4517 0.0198  0.0479  0.0546  255 LEU B O     
4179 C  CB    . LEU B 262 ? 0.4627 0.4309 0.4513 0.0027  0.0434  0.0420  255 LEU B CB    
4180 C  CG    . LEU B 262 ? 0.4475 0.4124 0.4461 -0.0013 0.0372  0.0345  255 LEU B CG    
4181 C  CD1   . LEU B 262 ? 0.4210 0.4067 0.4321 -0.0007 0.0352  0.0277  255 LEU B CD1   
4182 C  CD2   . LEU B 262 ? 0.4755 0.4275 0.4786 -0.0128 0.0377  0.0372  255 LEU B CD2   
4183 N  N     . ASP B 263 ? 0.5444 0.4966 0.5037 0.0010  0.0583  0.0667  256 ASP B N     
4184 C  CA    . ASP B 263 ? 0.5693 0.5265 0.5138 0.0049  0.0647  0.0748  256 ASP B CA    
4185 C  C     . ASP B 263 ? 0.5520 0.5385 0.5047 0.0060  0.0697  0.0698  256 ASP B C     
4186 O  O     . ASP B 263 ? 0.5634 0.5580 0.5029 0.0132  0.0730  0.0719  256 ASP B O     
4187 C  CB    . ASP B 263 ? 0.6221 0.5620 0.5569 -0.0045 0.0719  0.0887  256 ASP B CB    
4188 C  CG    . ASP B 263 ? 0.6600 0.5885 0.5691 0.0034  0.0744  0.0996  256 ASP B CG    
4189 O  OD1   . ASP B 263 ? 0.6444 0.5788 0.5436 0.0172  0.0691  0.0953  256 ASP B OD1   
4190 O  OD2   . ASP B 263 ? 0.7099 0.6224 0.6083 -0.0047 0.0811  0.1127  256 ASP B OD2   
4191 N  N     . ARG B 264 ? 0.5293 0.5311 0.5026 0.0001  0.0695  0.0626  257 ARG B N     
4192 C  CA    . ARG B 264 ? 0.5158 0.5447 0.4992 0.0027  0.0733  0.0563  257 ARG B CA    
4193 C  C     . ARG B 264 ? 0.5523 0.5955 0.5327 -0.0020 0.0859  0.0644  257 ARG B C     
4194 O  O     . ARG B 264 ? 0.5524 0.6148 0.5309 0.0049  0.0902  0.0604  257 ARG B O     
4195 C  CB    . ARG B 264 ? 0.4916 0.5253 0.4670 0.0162  0.0677  0.0480  257 ARG B CB    
4196 C  CG    . ARG B 264 ? 0.4595 0.4818 0.4379 0.0199  0.0569  0.0407  257 ARG B CG    
4197 C  CD    . ARG B 264 ? 0.4391 0.4633 0.4354 0.0139  0.0527  0.0353  257 ARG B CD    
4198 N  NE    . ARG B 264 ? 0.4219 0.4633 0.4288 0.0178  0.0513  0.0271  257 ARG B NE    
4199 C  CZ    . ARG B 264 ? 0.4124 0.4622 0.4355 0.0138  0.0487  0.0229  257 ARG B CZ    
4200 N  NH1   . ARG B 264 ? 0.4218 0.4690 0.4543 0.0038  0.0491  0.0261  257 ARG B NH1   
4201 N  NH2   . ARG B 264 ? 0.3988 0.4589 0.4283 0.0202  0.0452  0.0153  257 ARG B NH2   
4202 N  N     . ASN B 265 ? 0.5879 0.6217 0.5675 -0.0143 0.0923  0.0753  258 ASN B N     
4203 C  CA    . ASN B 265 ? 0.6291 0.6769 0.6046 -0.0205 0.1060  0.0846  258 ASN B CA    
4204 C  C     . ASN B 265 ? 0.6621 0.7064 0.6502 -0.0394 0.1124  0.0933  258 ASN B C     
4205 O  O     . ASN B 265 ? 0.7097 0.7518 0.6876 -0.0477 0.1234  0.1059  258 ASN B O     
4206 C  CB    . ASN B 265 ? 0.6602 0.6949 0.6057 -0.0129 0.1094  0.0939  258 ASN B CB    
4207 C  CG    . ASN B 265 ? 0.6871 0.6868 0.6167 -0.0163 0.1056  0.1046  258 ASN B CG    
4208 O  OD1   . ASN B 265 ? 0.6965 0.6812 0.6363 -0.0281 0.1043  0.1078  258 ASN B OD1   
4209 N  ND2   . ASN B 265 ? 0.7045 0.6903 0.6084 -0.0051 0.1030  0.1098  258 ASN B ND2   
4210 N  N     . GLY B 266 ? 0.6419 0.6852 0.6510 -0.0470 0.1053  0.0866  259 GLY B N     
4211 C  CA    . GLY B 266 ? 0.6733 0.7159 0.6982 -0.0664 0.1095  0.0921  259 GLY B CA    
4212 C  C     . GLY B 266 ? 0.7045 0.7069 0.7156 -0.0746 0.1058  0.1006  259 GLY B C     
4213 O  O     . GLY B 266 ? 0.7253 0.7203 0.7502 -0.0904 0.1047  0.1015  259 GLY B O     
4214 N  N     . GLN B 267 ? 0.7127 0.6892 0.6970 -0.0636 0.1033  0.1063  260 GLN B N     
4215 C  CA    . GLN B 267 ? 0.7445 0.6802 0.7137 -0.0670 0.0984  0.1133  260 GLN B CA    
4216 C  C     . GLN B 267 ? 0.7129 0.6364 0.6930 -0.0654 0.0856  0.1012  260 GLN B C     
4217 O  O     . GLN B 267 ? 0.6653 0.6101 0.6602 -0.0598 0.0802  0.0888  260 GLN B O     
4218 C  CB    . GLN B 267 ? 0.7569 0.6730 0.6966 -0.0516 0.0968  0.1202  260 GLN B CB    
4219 C  CG    . GLN B 267 ? 0.7948 0.7202 0.7178 -0.0516 0.1088  0.1327  260 GLN B CG    
4220 C  CD    . GLN B 267 ? 0.8663 0.7614 0.7715 -0.0628 0.1154  0.1505  260 GLN B CD    
4221 O  OE1   . GLN B 267 ? 0.8979 0.7863 0.8153 -0.0819 0.1203  0.1555  260 GLN B OE1   
4222 N  NE2   . GLN B 267 ? 0.8979 0.7737 0.7734 -0.0515 0.1151  0.1606  260 GLN B NE2   
4223 N  N     . GLN B 268 ? 0.7448 0.6319 0.7148 -0.0694 0.0806  0.1048  261 GLN B N     
4224 C  CA    . GLN B 268 ? 0.7266 0.6003 0.7049 -0.0693 0.0696  0.0934  261 GLN B CA    
4225 C  C     . GLN B 268 ? 0.6862 0.5563 0.6544 -0.0492 0.0612  0.0852  261 GLN B C     
4226 O  O     . GLN B 268 ? 0.6899 0.5538 0.6406 -0.0367 0.0620  0.0905  261 GLN B O     
4227 C  CB    . GLN B 268 ? 0.7834 0.6179 0.7541 -0.0808 0.0676  0.0990  261 GLN B CB    
4228 C  CG    . GLN B 268 ? 0.8164 0.6578 0.8059 -0.1045 0.0726  0.1016  261 GLN B CG    
4229 C  CD    . GLN B 268 ? 0.7849 0.6443 0.7978 -0.1102 0.0646  0.0866  261 GLN B CD    
4230 O  OE1   . GLN B 268 ? 0.7855 0.6232 0.7958 -0.1082 0.0546  0.0777  261 GLN B OE1   
4231 N  NE2   . GLN B 268 ? 0.7618 0.6614 0.7971 -0.1163 0.0688  0.0833  261 GLN B NE2   
4232 N  N     . PRO B 269 ? 0.6497 0.5254 0.6285 -0.0457 0.0528  0.0720  262 PRO B N     
4233 C  CA    . PRO B 269 ? 0.6191 0.4905 0.5890 -0.0288 0.0458  0.0649  262 PRO B CA    
4234 C  C     . PRO B 269 ? 0.6555 0.4914 0.6075 -0.0222 0.0421  0.0684  262 PRO B C     
4235 O  O     . PRO B 269 ? 0.7015 0.5117 0.6497 -0.0320 0.0425  0.0732  262 PRO B O     
4236 C  CB    . PRO B 269 ? 0.5856 0.4683 0.5698 -0.0304 0.0391  0.0518  262 PRO B CB    
4237 C  CG    . PRO B 269 ? 0.5887 0.4906 0.5916 -0.0453 0.0423  0.0517  262 PRO B CG    
4238 C  CD    . PRO B 269 ? 0.6397 0.5276 0.6389 -0.0575 0.0496  0.0636  262 PRO B CD    
4239 N  N     . SER B 270 ? 0.6394 0.4738 0.5811 -0.0054 0.0382  0.0658  263 SER B N     
4240 C  CA    . SER B 270 ? 0.6718 0.4759 0.5993 0.0039  0.0333  0.0663  263 SER B CA    
4241 C  C     . SER B 270 ? 0.6789 0.4677 0.6121 -0.0010 0.0281  0.0563  263 SER B C     
4242 O  O     . SER B 270 ? 0.6518 0.4570 0.5993 -0.0097 0.0270  0.0484  263 SER B O     
4243 C  CB    . SER B 270 ? 0.6508 0.4638 0.5712 0.0225  0.0297  0.0633  263 SER B CB    
4244 O  OG    . SER B 270 ? 0.6065 0.4376 0.5379 0.0268  0.0258  0.0505  263 SER B OG    
4245 N  N     . LYS B 271 ? 0.7196 0.4762 0.6401 0.0058  0.0239  0.0557  264 LYS B N     
4246 C  CA    . LYS B 271 ? 0.7207 0.4667 0.6434 0.0076  0.0180  0.0429  264 LYS B CA    
4247 C  C     . LYS B 271 ? 0.6710 0.4432 0.5981 0.0211  0.0160  0.0336  264 LYS B C     
4248 O  O     . LYS B 271 ? 0.6509 0.4390 0.5760 0.0314  0.0174  0.0374  264 LYS B O     
4249 C  CB    . LYS B 271 ? 0.7815 0.4858 0.6884 0.0141  0.0141  0.0434  264 LYS B CB    
4250 C  CG    . LYS B 271 ? 0.8400 0.5141 0.7398 0.0004  0.0166  0.0554  264 LYS B CG    
4251 C  CD    . LYS B 271 ? 0.9034 0.5332 0.7929 -0.0021 0.0115  0.0515  264 LYS B CD    
4252 C  CE    . LYS B 271 ? 0.9703 0.5662 0.8497 -0.0151 0.0145  0.0661  264 LYS B CE    
4253 N  NZ    . LYS B 271 ? 0.9554 0.5751 0.8474 -0.0347 0.0225  0.0758  264 LYS B NZ    
4254 N  N     . SER B 272 ? 0.6590 0.4336 0.5904 0.0209  0.0123  0.0215  265 SER B N     
4255 C  CA    . SER B 272 ? 0.6180 0.4164 0.5535 0.0307  0.0113  0.0130  265 SER B CA    
4256 C  C     . SER B 272 ? 0.6289 0.4238 0.5561 0.0491  0.0105  0.0125  265 SER B C     
4257 O  O     . SER B 272 ? 0.6747 0.4417 0.5911 0.0565  0.0082  0.0126  265 SER B O     
4258 C  CB    . SER B 272 ? 0.6152 0.4131 0.5528 0.0269  0.0079  0.0011  265 SER B CB    
4259 O  OG    . SER B 272 ? 0.5803 0.4012 0.5205 0.0353  0.0082  -0.0056 265 SER B OG    
4260 N  N     . ILE B 273 ? 0.5908 0.4138 0.5236 0.0564  0.0117  0.0114  266 ILE B N     
4261 C  CA    . ILE B 273 ? 0.5977 0.4255 0.5271 0.0734  0.0104  0.0084  266 ILE B CA    
4262 C  C     . ILE B 273 ? 0.6207 0.4366 0.5460 0.0809  0.0086  -0.0024 266 ILE B C     
4263 O  O     . ILE B 273 ? 0.6479 0.4571 0.5681 0.0965  0.0070  -0.0046 266 ILE B O     
4264 C  CB    . ILE B 273 ? 0.5551 0.4174 0.4937 0.0775  0.0117  0.0072  266 ILE B CB    
4265 C  CG1   . ILE B 273 ? 0.5198 0.4021 0.4670 0.0710  0.0132  -0.0008 266 ILE B CG1   
4266 C  CG2   . ILE B 273 ? 0.5411 0.4127 0.4807 0.0726  0.0130  0.0167  266 ILE B CG2   
4267 C  CD1   . ILE B 273 ? 0.4867 0.3985 0.4424 0.0735  0.0143  -0.0018 266 ILE B CD1   
4268 N  N     . LEU B 274 ? 0.6122 0.4276 0.5395 0.0712  0.0086  -0.0097 267 LEU B N     
4269 C  CA    . LEU B 274 ? 0.6353 0.4411 0.5566 0.0774  0.0073  -0.0214 267 LEU B CA    
4270 C  C     . LEU B 274 ? 0.6952 0.4618 0.6042 0.0821  0.0038  -0.0226 267 LEU B C     
4271 O  O     . LEU B 274 ? 0.7262 0.4825 0.6280 0.0951  0.0028  -0.0319 267 LEU B O     
4272 C  CB    . LEU B 274 ? 0.6155 0.4299 0.5394 0.0651  0.0070  -0.0278 267 LEU B CB    
4273 C  CG    . LEU B 274 ? 0.5657 0.4136 0.4988 0.0613  0.0099  -0.0274 267 LEU B CG    
4274 C  CD1   . LEU B 274 ? 0.5547 0.4056 0.4882 0.0489  0.0079  -0.0313 267 LEU B CD1   
4275 C  CD2   . LEU B 274 ? 0.5589 0.4264 0.4928 0.0736  0.0133  -0.0329 267 LEU B CD2   
4276 N  N     . GLU B 275 ? 0.7150 0.4606 0.6215 0.0723  0.0027  -0.0130 268 GLU B N     
4277 C  CA    . GLU B 275 ? 0.7776 0.4811 0.6720 0.0723  -0.0007 -0.0121 268 GLU B CA    
4278 C  C     . GLU B 275 ? 0.8120 0.4983 0.6975 0.0860  -0.0014 -0.0027 268 GLU B C     
4279 O  O     . GLU B 275 ? 0.8702 0.5219 0.7431 0.0955  -0.0049 -0.0050 268 GLU B O     
4280 C  CB    . GLU B 275 ? 0.7847 0.4765 0.6826 0.0503  -0.0010 -0.0065 268 GLU B CB    
4281 C  CG    . GLU B 275 ? 0.8540 0.5002 0.7404 0.0447  -0.0044 -0.0044 268 GLU B CG    
4282 C  CD    . GLU B 275 ? 0.8606 0.5018 0.7547 0.0206  -0.0046 -0.0013 268 GLU B CD    
4283 O  OE1   . GLU B 275 ? 0.8480 0.4994 0.7488 0.0099  -0.0002 0.0114  268 GLU B OE1   
4284 O  OE2   . GLU B 275 ? 0.8788 0.5096 0.7730 0.0125  -0.0091 -0.0124 268 GLU B OE2   
4285 N  N     . VAL B 276 ? 0.7832 0.4906 0.6733 0.0876  0.0011  0.0078  269 VAL B N     
4286 C  CA    . VAL B 276 ? 0.8215 0.5111 0.7007 0.0992  -0.0005 0.0186  269 VAL B CA    
4287 C  C     . VAL B 276 ? 0.7936 0.5148 0.6779 0.1158  -0.0008 0.0187  269 VAL B C     
4288 O  O     . VAL B 276 ? 0.8257 0.5371 0.7011 0.1297  -0.0037 0.0260  269 VAL B O     
4289 C  CB    . VAL B 276 ? 0.8369 0.5125 0.7115 0.0840  0.0020  0.0338  269 VAL B CB    
4290 C  CG1   . VAL B 276 ? 0.8717 0.5171 0.7437 0.0659  0.0019  0.0337  269 VAL B CG1   
4291 C  CG2   . VAL B 276 ? 0.7781 0.4918 0.6646 0.0744  0.0067  0.0388  269 VAL B CG2   
4292 N  N     . GLY B 277 ? 0.7379 0.4972 0.6363 0.1143  0.0016  0.0111  270 GLY B N     
4293 C  CA    . GLY B 277 ? 0.7122 0.5038 0.6180 0.1265  0.0011  0.0107  270 GLY B CA    
4294 C  C     . GLY B 277 ? 0.6802 0.4910 0.5896 0.1180  0.0027  0.0205  270 GLY B C     
4295 O  O     . GLY B 277 ? 0.6875 0.4837 0.5912 0.1058  0.0046  0.0296  270 GLY B O     
4296 N  N     . VAL B 278 ? 0.6519 0.4952 0.5702 0.1256  0.0019  0.0179  271 VAL B N     
4297 C  CA    . VAL B 278 ? 0.6207 0.4854 0.5426 0.1186  0.0029  0.0239  271 VAL B CA    
4298 C  C     . VAL B 278 ? 0.6564 0.5047 0.5638 0.1233  0.0006  0.0366  271 VAL B C     
4299 O  O     . VAL B 278 ? 0.6502 0.4957 0.5532 0.1115  0.0039  0.0445  271 VAL B O     
4300 C  CB    . VAL B 278 ? 0.5881 0.4901 0.5237 0.1243  0.0017  0.0166  271 VAL B CB    
4301 C  CG1   . VAL B 278 ? 0.5691 0.4903 0.5056 0.1213  0.0004  0.0218  271 VAL B CG1   
4302 C  CG2   . VAL B 278 ? 0.5524 0.4694 0.4997 0.1148  0.0057  0.0071  271 VAL B CG2   
4303 N  N     . GLN B 279 ? 0.6998 0.5361 0.5983 0.1409  -0.0047 0.0390  272 GLN B N     
4304 C  CA    . GLN B 279 ? 0.7409 0.5610 0.6222 0.1473  -0.0077 0.0521  272 GLN B CA    
4305 C  C     . GLN B 279 ? 0.7700 0.5563 0.6376 0.1335  -0.0031 0.0634  272 GLN B C     
4306 O  O     . GLN B 279 ? 0.7750 0.5622 0.6338 0.1269  -0.0005 0.0738  272 GLN B O     
4307 C  CB    . GLN B 279 ? 0.7902 0.5994 0.6637 0.1704  -0.0154 0.0524  272 GLN B CB    
4308 C  CG    . GLN B 279 ? 0.8437 0.6305 0.6950 0.1783  -0.0194 0.0676  272 GLN B CG    
4309 C  CD    . GLN B 279 ? 0.9036 0.6715 0.7447 0.2022  -0.0279 0.0690  272 GLN B CD    
4310 O  OE1   . GLN B 279 ? 0.9080 0.6782 0.7590 0.2135  -0.0301 0.0579  272 GLN B OE1   
4311 N  NE2   . GLN B 279 ? 0.9551 0.7041 0.7750 0.2113  -0.0327 0.0828  272 GLN B NE2   
4312 N  N     . GLN B 280 ? 0.7938 0.5510 0.6593 0.1284  -0.0018 0.0612  273 GLN B N     
4313 C  CA    . GLN B 280 ? 0.8317 0.5549 0.6853 0.1144  0.0019  0.0718  273 GLN B CA    
4314 C  C     . GLN B 280 ? 0.7875 0.5304 0.6521 0.0932  0.0090  0.0726  273 GLN B C     
4315 O  O     . GLN B 280 ? 0.8065 0.5409 0.6633 0.0818  0.0139  0.0845  273 GLN B O     
4316 C  CB    . GLN B 280 ? 0.8713 0.5596 0.7212 0.1156  -0.0003 0.0661  273 GLN B CB    
4317 C  CG    . GLN B 280 ? 0.9160 0.5671 0.7562 0.0984  0.0028  0.0752  273 GLN B CG    
4318 C  CD    . GLN B 280 ? 0.9809 0.6009 0.7991 0.1021  0.0022  0.0927  273 GLN B CD    
4319 O  OE1   . GLN B 280 ? 1.0153 0.6248 0.8209 0.1227  -0.0037 0.0961  273 GLN B OE1   
4320 N  NE2   . GLN B 280 ? 1.0020 0.6082 0.8152 0.0822  0.0086  0.1043  273 GLN B NE2   
4321 N  N     . ALA B 281 ? 0.7312 0.5023 0.6137 0.0886  0.0100  0.0603  274 ALA B N     
4322 C  CA    . ALA B 281 ? 0.6923 0.4815 0.5862 0.0708  0.0155  0.0596  274 ALA B CA    
4323 C  C     . ALA B 281 ? 0.6761 0.4871 0.5678 0.0701  0.0185  0.0669  274 ALA B C     
4324 O  O     . ALA B 281 ? 0.6783 0.4908 0.5698 0.0572  0.0243  0.0738  274 ALA B O     
4325 C  CB    . ALA B 281 ? 0.6438 0.4552 0.5538 0.0684  0.0148  0.0458  274 ALA B CB    
4326 N  N     . LEU B 282 ? 0.6644 0.4931 0.5546 0.0842  0.0144  0.0647  275 LEU B N     
4327 C  CA    . LEU B 282 ? 0.6480 0.4998 0.5359 0.0852  0.0155  0.0682  275 LEU B CA    
4328 C  C     . LEU B 282 ? 0.6968 0.5309 0.5647 0.0853  0.0181  0.0831  275 LEU B C     
4329 O  O     . LEU B 282 ? 0.6914 0.5402 0.5549 0.0814  0.0219  0.0876  275 LEU B O     
4330 C  CB    . LEU B 282 ? 0.6314 0.5051 0.5233 0.0999  0.0088  0.0609  275 LEU B CB    
4331 C  CG    . LEU B 282 ? 0.6006 0.5040 0.4964 0.0988  0.0087  0.0580  275 LEU B CG    
4332 C  CD1   . LEU B 282 ? 0.5535 0.4731 0.4649 0.0857  0.0130  0.0503  275 LEU B CD1   
4333 C  CD2   . LEU B 282 ? 0.5953 0.5186 0.4953 0.1123  0.0010  0.0513  275 LEU B CD2   
4334 N  N     . GLN B 283 ? 0.7503 0.5509 0.6045 0.0897  0.0163  0.0911  276 GLN B N     
4335 C  CA    . GLN B 283 ? 0.8048 0.5865 0.6366 0.0913  0.0183  0.1069  276 GLN B CA    
4336 C  C     . GLN B 283 ? 0.8167 0.5898 0.6485 0.0708  0.0284  0.1150  276 GLN B C     
4337 O  O     . GLN B 283 ? 0.8571 0.6211 0.6720 0.0670  0.0335  0.1288  276 GLN B O     
4338 C  CB    . GLN B 283 ? 0.8625 0.6123 0.6780 0.1071  0.0110  0.1125  276 GLN B CB    
4339 C  CG    . GLN B 283 ? 0.9205 0.6265 0.7243 0.0985  0.0138  0.1223  276 GLN B CG    
4340 C  CD    . GLN B 283 ? 0.9846 0.6574 0.7693 0.1173  0.0057  0.1286  276 GLN B CD    
4341 O  OE1   . GLN B 283 ? 1.0154 0.6880 0.7830 0.1311  0.0014  0.1373  276 GLN B OE1   
4342 N  NE2   . GLN B 283 ? 1.0094 0.6533 0.7960 0.1190  0.0027  0.1234  276 GLN B NE2   
4343 N  N     . ALA B 284 ? 0.7812 0.5618 0.6327 0.0574  0.0314  0.1061  277 ALA B N     
4344 C  CA    . ALA B 284 ? 0.7887 0.5671 0.6465 0.0373  0.0401  0.1111  277 ALA B CA    
4345 C  C     . ALA B 284 ? 0.7483 0.5630 0.6165 0.0305  0.0465  0.1087  277 ALA B C     
4346 O  O     . ALA B 284 ? 0.7526 0.5734 0.6288 0.0148  0.0544  0.1122  277 ALA B O     
4347 C  CB    . ALA B 284 ? 0.7773 0.5457 0.6503 0.0282  0.0380  0.1017  277 ALA B CB    
4348 N  N     . VAL B 285 ? 0.7123 0.5519 0.5816 0.0422  0.0430  0.1020  278 VAL B N     
4349 C  CA    . VAL B 285 ? 0.6786 0.5496 0.5564 0.0377  0.0481  0.0981  278 VAL B CA    
4350 C  C     . VAL B 285 ? 0.6900 0.5716 0.5509 0.0498  0.0467  0.1017  278 VAL B C     
4351 O  O     . VAL B 285 ? 0.7081 0.5797 0.5567 0.0631  0.0394  0.1034  278 VAL B O     
4352 C  CB    . VAL B 285 ? 0.6192 0.5116 0.5185 0.0370  0.0444  0.0828  278 VAL B CB    
4353 C  CG1   . VAL B 285 ? 0.6115 0.4959 0.5259 0.0248  0.0453  0.0790  278 VAL B CG1   
4354 C  CG2   . VAL B 285 ? 0.5983 0.4941 0.4978 0.0508  0.0353  0.0745  278 VAL B CG2   
4355 N  N     . PHE B 286 ? 0.6822 0.5855 0.5431 0.0458  0.0534  0.1018  279 PHE B N     
4356 C  CA    . PHE B 286 ? 0.6879 0.6056 0.5341 0.0570  0.0512  0.1013  279 PHE B CA    
4357 C  C     . PHE B 286 ? 0.6350 0.5764 0.4963 0.0619  0.0451  0.0854  279 PHE B C     
4358 O  O     . PHE B 286 ? 0.6001 0.5547 0.4795 0.0541  0.0481  0.0776  279 PHE B O     
4359 C  CB    . PHE B 286 ? 0.7170 0.6446 0.5516 0.0512  0.0623  0.1094  279 PHE B CB    
4360 C  CG    . PHE B 286 ? 0.7301 0.6720 0.5462 0.0628  0.0602  0.1082  279 PHE B CG    
4361 C  CD1   . PHE B 286 ? 0.7590 0.6897 0.5552 0.0761  0.0514  0.1126  279 PHE B CD1   
4362 C  CD2   . PHE B 286 ? 0.7190 0.6853 0.5369 0.0615  0.0663  0.1019  279 PHE B CD2   
4363 C  CE1   . PHE B 286 ? 0.7756 0.7200 0.5537 0.0866  0.0480  0.1106  279 PHE B CE1   
4364 C  CE2   . PHE B 286 ? 0.7371 0.7149 0.5358 0.0722  0.0637  0.0995  279 PHE B CE2   
4365 C  CZ    . PHE B 286 ? 0.7652 0.7323 0.5438 0.0842  0.0543  0.1038  279 PHE B CZ    
4366 N  N     . TRP B 287 ? 0.6351 0.5817 0.4884 0.0746  0.0363  0.0813  280 TRP B N     
4367 C  CA    . TRP B 287 ? 0.5981 0.5663 0.4614 0.0787  0.0304  0.0677  280 TRP B CA    
4368 C  C     . TRP B 287 ? 0.6241 0.6022 0.4684 0.0882  0.0270  0.0680  280 TRP B C     
4369 O  O     . TRP B 287 ? 0.6543 0.6250 0.4845 0.0982  0.0206  0.0732  280 TRP B O     
4370 C  CB    . TRP B 287 ? 0.5725 0.5406 0.4492 0.0834  0.0215  0.0597  280 TRP B CB    
4371 C  CG    . TRP B 287 ? 0.5390 0.5279 0.4272 0.0851  0.0157  0.0464  280 TRP B CG    
4372 C  CD1   . TRP B 287 ? 0.5133 0.5153 0.4100 0.0792  0.0181  0.0383  280 TRP B CD1   
4373 C  CD2   . TRP B 287 ? 0.5332 0.5315 0.4262 0.0931  0.0060  0.0394  280 TRP B CD2   
4374 N  NE1   . TRP B 287 ? 0.4943 0.5093 0.3992 0.0817  0.0106  0.0276  280 TRP B NE1   
4375 C  CE2   . TRP B 287 ? 0.5052 0.5205 0.4091 0.0894  0.0035  0.0280  280 TRP B CE2   
4376 C  CE3   . TRP B 287 ? 0.5530 0.5475 0.4430 0.1034  -0.0007 0.0417  280 TRP B CE3   
4377 C  CZ2   . TRP B 287 ? 0.4966 0.5261 0.4093 0.0930  -0.0049 0.0192  280 TRP B CZ2   
4378 C  CZ3   . TRP B 287 ? 0.5413 0.5536 0.4421 0.1085  -0.0089 0.0322  280 TRP B CZ3   
4379 C  CH2   . TRP B 287 ? 0.5145 0.5447 0.4263 0.1024  -0.0109 0.0215  280 TRP B CH2   
4380 N  N     . ASP B 288 ? 0.6155 0.6102 0.4592 0.0863  0.0305  0.0615  281 ASP B N     
4381 C  CA    . ASP B 288 ? 0.6441 0.6488 0.4679 0.0949  0.0274  0.0600  281 ASP B CA    
4382 C  C     . ASP B 288 ? 0.6222 0.6394 0.4542 0.1009  0.0151  0.0465  281 ASP B C     
4383 O  O     . ASP B 288 ? 0.5950 0.6239 0.4388 0.0974  0.0142  0.0346  281 ASP B O     
4384 C  CB    . ASP B 288 ? 0.6522 0.6683 0.4706 0.0910  0.0373  0.0582  281 ASP B CB    
4385 C  CG    . ASP B 288 ? 0.6936 0.7177 0.4857 0.1000  0.0360  0.0580  281 ASP B CG    
4386 O  OD1   . ASP B 288 ? 0.7028 0.7294 0.4867 0.1089  0.0243  0.0534  281 ASP B OD1   
4387 O  OD2   . ASP B 288 ? 0.7198 0.7493 0.4999 0.0980  0.0470  0.0623  281 ASP B OD2   
4388 N  N     . GLU B 289 ? 0.6373 0.6518 0.4646 0.1097  0.0054  0.0483  282 GLU B N     
4389 C  CA    . GLU B 289 ? 0.6171 0.6462 0.4572 0.1132  -0.0059 0.0356  282 GLU B CA    
4390 C  C     . GLU B 289 ? 0.6352 0.6789 0.4630 0.1175  -0.0115 0.0268  282 GLU B C     
4391 O  O     . GLU B 289 ? 0.6155 0.6720 0.4564 0.1155  -0.0185 0.0140  282 GLU B O     
4392 C  CB    . GLU B 289 ? 0.6306 0.6561 0.4722 0.1223  -0.0144 0.0394  282 GLU B CB    
4393 C  CG    . GLU B 289 ? 0.6045 0.6474 0.4673 0.1230  -0.0238 0.0267  282 GLU B CG    
4394 C  CD    . GLU B 289 ? 0.6174 0.6616 0.4860 0.1331  -0.0315 0.0288  282 GLU B CD    
4395 O  OE1   . GLU B 289 ? 0.6011 0.6641 0.4880 0.1335  -0.0385 0.0185  282 GLU B OE1   
4396 O  OE2   . GLU B 289 ? 0.6462 0.6727 0.5021 0.1403  -0.0301 0.0403  282 GLU B OE2   
4397 N  N     . GLU B 290 ? 0.6771 0.7185 0.4788 0.1227  -0.0084 0.0334  283 GLU B N     
4398 C  CA    . GLU B 290 ? 0.6980 0.7524 0.4858 0.1267  -0.0129 0.0235  283 GLU B CA    
4399 C  C     . GLU B 290 ? 0.6699 0.7295 0.4695 0.1183  -0.0066 0.0125  283 GLU B C     
4400 O  O     . GLU B 290 ? 0.6663 0.7355 0.4695 0.1184  -0.0142 -0.0017 283 GLU B O     
4401 C  CB    . GLU B 290 ? 0.7542 0.8044 0.5085 0.1343  -0.0092 0.0339  283 GLU B CB    
4402 C  CG    . GLU B 290 ? 0.7935 0.8387 0.5314 0.1458  -0.0190 0.0432  283 GLU B CG    
4403 C  CD    . GLU B 290 ? 0.8563 0.8932 0.5574 0.1531  -0.0147 0.0568  283 GLU B CD    
4404 O  OE1   . GLU B 290 ? 0.8680 0.9018 0.5582 0.1473  -0.0005 0.0621  283 GLU B OE1   
4405 O  OE2   . GLU B 290 ? 0.8972 0.9325 0.5804 0.1649  -0.0255 0.0620  283 GLU B OE2   
4406 N  N     . ALA B 291 ? 0.6550 0.7079 0.4606 0.1113  0.0064  0.0187  284 ALA B N     
4407 C  CA    . ALA B 291 ? 0.6295 0.6871 0.4484 0.1052  0.0117  0.0087  284 ALA B CA    
4408 C  C     . ALA B 291 ? 0.5884 0.6471 0.4318 0.0997  0.0040  -0.0017 284 ALA B C     
4409 O  O     . ALA B 291 ? 0.5808 0.6436 0.4299 0.0981  0.0004  -0.0145 284 ALA B O     
4410 C  CB    . ALA B 291 ? 0.6219 0.6752 0.4466 0.0987  0.0256  0.0180  284 ALA B CB    
4411 N  N     . PHE B 292 ? 0.5671 0.6204 0.4237 0.0970  0.0017  0.0039  285 PHE B N     
4412 C  CA    . PHE B 292 ? 0.5327 0.5877 0.4112 0.0914  -0.0040 -0.0036 285 PHE B CA    
4413 C  C     . PHE B 292 ? 0.5430 0.6084 0.4211 0.0934  -0.0153 -0.0159 285 PHE B C     
4414 O  O     . PHE B 292 ? 0.5272 0.5936 0.4170 0.0873  -0.0179 -0.0258 285 PHE B O     
4415 C  CB    . PHE B 292 ? 0.5211 0.5708 0.4086 0.0914  -0.0050 0.0042  285 PHE B CB    
4416 C  CG    . PHE B 292 ? 0.4937 0.5485 0.4016 0.0869  -0.0107 -0.0026 285 PHE B CG    
4417 C  CD1   . PHE B 292 ? 0.4623 0.5131 0.3859 0.0781  -0.0067 -0.0056 285 PHE B CD1   
4418 C  CD2   . PHE B 292 ? 0.5040 0.5694 0.4151 0.0920  -0.0200 -0.0057 285 PHE B CD2   
4419 C  CE1   . PHE B 292 ? 0.4431 0.4990 0.3830 0.0734  -0.0107 -0.0110 285 PHE B CE1   
4420 C  CE2   . PHE B 292 ? 0.4830 0.5565 0.4138 0.0871  -0.0236 -0.0118 285 PHE B CE2   
4421 C  CZ    . PHE B 292 ? 0.4534 0.5216 0.3975 0.0773  -0.0184 -0.0141 285 PHE B CZ    
4422 N  N     . VAL B 293 ? 0.5742 0.6464 0.4386 0.1016  -0.0230 -0.0150 286 VAL B N     
4423 C  CA    . VAL B 293 ? 0.5896 0.6739 0.4542 0.1028  -0.0352 -0.0275 286 VAL B CA    
4424 C  C     . VAL B 293 ? 0.6068 0.6903 0.4601 0.1021  -0.0351 -0.0383 286 VAL B C     
4425 O  O     . VAL B 293 ? 0.6049 0.6912 0.4673 0.0967  -0.0420 -0.0511 286 VAL B O     
4426 C  CB    . VAL B 293 ? 0.6234 0.7166 0.4755 0.1134  -0.0446 -0.0237 286 VAL B CB    
4427 C  CG1   . VAL B 293 ? 0.6477 0.7559 0.4980 0.1147  -0.0584 -0.0376 286 VAL B CG1   
4428 C  CG2   . VAL B 293 ? 0.6060 0.7007 0.4744 0.1145  -0.0460 -0.0168 286 VAL B CG2   
4429 N  N     . GLU B 294 ? 0.6292 0.7086 0.4621 0.1077  -0.0272 -0.0333 287 GLU B N     
4430 C  CA    . GLU B 294 ? 0.6538 0.7336 0.4728 0.1100  -0.0265 -0.0440 287 GLU B CA    
4431 C  C     . GLU B 294 ? 0.6274 0.7004 0.4634 0.1025  -0.0232 -0.0528 287 GLU B C     
4432 O  O     . GLU B 294 ? 0.6456 0.7172 0.4772 0.1028  -0.0284 -0.0665 287 GLU B O     
4433 C  CB    . GLU B 294 ? 0.6839 0.7632 0.4792 0.1171  -0.0159 -0.0355 287 GLU B CB    
4434 C  CG    . GLU B 294 ? 0.7178 0.7998 0.4955 0.1222  -0.0150 -0.0478 287 GLU B CG    
4435 C  CD    . GLU B 294 ? 0.7632 0.8492 0.5111 0.1309  -0.0068 -0.0401 287 GLU B CD    
4436 O  OE1   . GLU B 294 ? 0.7882 0.8758 0.5200 0.1360  -0.0109 -0.0303 287 GLU B OE1   
4437 O  OE2   . GLU B 294 ? 0.7785 0.8667 0.5183 0.1334  0.0034  -0.0438 287 GLU B OE2   
4438 N  N     . ARG B 295 ? 0.5897 0.6568 0.4436 0.0963  -0.0155 -0.0453 288 ARG B N     
4439 C  CA    . ARG B 295 ? 0.5698 0.6292 0.4378 0.0906  -0.0131 -0.0524 288 ARG B CA    
4440 C  C     . ARG B 295 ? 0.5529 0.6089 0.4379 0.0822  -0.0223 -0.0595 288 ARG B C     
4441 O  O     . ARG B 295 ? 0.5424 0.5889 0.4372 0.0771  -0.0219 -0.0651 288 ARG B O     
4442 C  CB    . ARG B 295 ? 0.5420 0.5976 0.4212 0.0876  -0.0018 -0.0424 288 ARG B CB    
4443 C  CG    . ARG B 295 ? 0.5104 0.5638 0.4045 0.0815  -0.0015 -0.0326 288 ARG B CG    
4444 C  CD    . ARG B 295 ? 0.4858 0.5344 0.3922 0.0772  0.0071  -0.0263 288 ARG B CD    
4445 N  NE    . ARG B 295 ? 0.4624 0.5077 0.3795 0.0725  0.0081  -0.0172 288 ARG B NE    
4446 C  CZ    . ARG B 295 ? 0.4401 0.4822 0.3706 0.0670  0.0035  -0.0190 288 ARG B CZ    
4447 N  NH1   . ARG B 295 ? 0.4386 0.4804 0.3743 0.0639  -0.0029 -0.0284 288 ARG B NH1   
4448 N  NH2   . ARG B 295 ? 0.4238 0.4624 0.3619 0.0641  0.0061  -0.0113 288 ARG B NH2   
4449 N  N     . GLY B 296 ? 0.5544 0.6188 0.4429 0.0808  -0.0303 -0.0588 289 GLY B N     
4450 C  CA    . GLY B 296 ? 0.5463 0.6124 0.4510 0.0718  -0.0387 -0.0658 289 GLY B CA    
4451 C  C     . GLY B 296 ? 0.5098 0.5755 0.4335 0.0653  -0.0344 -0.0571 289 GLY B C     
4452 O  O     . GLY B 296 ? 0.4978 0.5600 0.4359 0.0558  -0.0363 -0.0608 289 GLY B O     
4453 N  N     . GLY B 297 ? 0.4982 0.5661 0.4200 0.0704  -0.0286 -0.0456 290 GLY B N     
4454 C  CA    . GLY B 297 ? 0.4687 0.5349 0.4051 0.0662  -0.0241 -0.0378 290 GLY B CA    
4455 C  C     . GLY B 297 ? 0.4652 0.5434 0.4163 0.0620  -0.0307 -0.0409 290 GLY B C     
4456 O  O     . GLY B 297 ? 0.4434 0.5205 0.4082 0.0562  -0.0273 -0.0381 290 GLY B O     
4457 N  N     . ILE B 298 ? 0.4901 0.5820 0.4380 0.0658  -0.0399 -0.0465 291 ILE B N     
4458 C  CA    . ILE B 298 ? 0.4931 0.6021 0.4576 0.0612  -0.0471 -0.0516 291 ILE B CA    
4459 C  C     . ILE B 298 ? 0.5067 0.6167 0.4768 0.0506  -0.0534 -0.0636 291 ILE B C     
4460 O  O     . ILE B 298 ? 0.5342 0.6448 0.4920 0.0534  -0.0602 -0.0711 291 ILE B O     
4461 C  CB    . ILE B 298 ? 0.5169 0.6434 0.4775 0.0720  -0.0552 -0.0509 291 ILE B CB    
4462 C  CG1   . ILE B 298 ? 0.5127 0.6343 0.4663 0.0830  -0.0501 -0.0386 291 ILE B CG1   
4463 C  CG2   . ILE B 298 ? 0.5226 0.6720 0.5047 0.0662  -0.0629 -0.0582 291 ILE B CG2   
4464 C  CD1   . ILE B 298 ? 0.4875 0.6089 0.4575 0.0803  -0.0440 -0.0338 291 ILE B CD1   
4465 N  N     . TYR B 299 ? 0.4931 0.6015 0.4796 0.0382  -0.0511 -0.0653 292 TYR B N     
4466 C  CA    . TYR B 299 ? 0.5119 0.6175 0.5043 0.0259  -0.0569 -0.0756 292 TYR B CA    
4467 C  C     . TYR B 299 ? 0.5058 0.6229 0.5202 0.0130  -0.0558 -0.0755 292 TYR B C     
4468 O  O     . TYR B 299 ? 0.4876 0.6169 0.5119 0.0157  -0.0509 -0.0688 292 TYR B O     
4469 C  CB    . TYR B 299 ? 0.5101 0.5894 0.4916 0.0237  -0.0525 -0.0765 292 TYR B CB    
4470 C  CG    . TYR B 299 ? 0.4810 0.5466 0.4672 0.0203  -0.0425 -0.0677 292 TYR B CG    
4471 C  CD1   . TYR B 299 ? 0.4583 0.5198 0.4382 0.0295  -0.0349 -0.0586 292 TYR B CD1   
4472 C  CD2   . TYR B 299 ? 0.4828 0.5370 0.4773 0.0076  -0.0413 -0.0687 292 TYR B CD2   
4473 C  CE1   . TYR B 299 ? 0.4363 0.4855 0.4193 0.0267  -0.0274 -0.0519 292 TYR B CE1   
4474 C  CE2   . TYR B 299 ? 0.4617 0.5026 0.4573 0.0058  -0.0335 -0.0608 292 TYR B CE2   
4475 C  CZ    . TYR B 299 ? 0.4373 0.4770 0.4278 0.0155  -0.0270 -0.0531 292 TYR B CZ    
4476 O  OH    . TYR B 299 ? 0.4202 0.4474 0.4115 0.0136  -0.0209 -0.0465 292 TYR B OH    
4477 N  N     . ASP B 300 ? 0.5262 0.6384 0.5473 -0.0011 -0.0599 -0.0832 293 ASP B N     
4478 C  CA    . ASP B 300 ? 0.5292 0.6521 0.5705 -0.0163 -0.0581 -0.0831 293 ASP B CA    
4479 C  C     . ASP B 300 ? 0.5073 0.6104 0.5472 -0.0210 -0.0472 -0.0742 293 ASP B C     
4480 O  O     . ASP B 300 ? 0.5188 0.5981 0.5529 -0.0296 -0.0466 -0.0753 293 ASP B O     
4481 C  CB    . ASP B 300 ? 0.5676 0.6896 0.6149 -0.0314 -0.0670 -0.0942 293 ASP B CB    
4482 C  CG    . ASP B 300 ? 0.5929 0.7394 0.6438 -0.0276 -0.0792 -0.1040 293 ASP B CG    
4483 O  OD1   . ASP B 300 ? 0.5808 0.7492 0.6338 -0.0145 -0.0800 -0.1007 293 ASP B OD1   
4484 O  OD2   . ASP B 300 ? 0.6288 0.7703 0.6787 -0.0370 -0.0885 -0.1151 293 ASP B OD2   
4485 N  N     . TRP B 301 ? 0.4805 0.5930 0.5248 -0.0145 -0.0397 -0.0658 294 TRP B N     
4486 C  CA    . TRP B 301 ? 0.4581 0.5518 0.4964 -0.0142 -0.0303 -0.0571 294 TRP B CA    
4487 C  C     . TRP B 301 ? 0.4586 0.5585 0.5093 -0.0264 -0.0237 -0.0532 294 TRP B C     
4488 O  O     . TRP B 301 ? 0.4418 0.5320 0.4885 -0.0254 -0.0160 -0.0459 294 TRP B O     
4489 C  CB    . TRP B 301 ? 0.4336 0.5276 0.4638 0.0015  -0.0265 -0.0509 294 TRP B CB    
4490 C  CG    . TRP B 301 ? 0.4311 0.5492 0.4691 0.0104  -0.0275 -0.0500 294 TRP B CG    
4491 C  CD1   . TRP B 301 ? 0.4366 0.5786 0.4916 0.0069  -0.0268 -0.0513 294 TRP B CD1   
4492 C  CD2   . TRP B 301 ? 0.4261 0.5451 0.4542 0.0257  -0.0286 -0.0466 294 TRP B CD2   
4493 N  NE1   . TRP B 301 ? 0.4354 0.5926 0.4920 0.0207  -0.0284 -0.0498 294 TRP B NE1   
4494 C  CE2   . TRP B 301 ? 0.4304 0.5718 0.4695 0.0320  -0.0297 -0.0462 294 TRP B CE2   
4495 C  CE3   . TRP B 301 ? 0.4232 0.5269 0.4343 0.0346  -0.0283 -0.0434 294 TRP B CE3   
4496 C  CZ2   . TRP B 301 ? 0.4339 0.5780 0.4655 0.0471  -0.0316 -0.0422 294 TRP B CZ2   
4497 C  CZ3   . TRP B 301 ? 0.4264 0.5340 0.4302 0.0475  -0.0289 -0.0387 294 TRP B CZ3   
4498 C  CH2   . TRP B 301 ? 0.4322 0.5573 0.4452 0.0538  -0.0309 -0.0377 294 TRP B CH2   
4499 N  N     . ASN B 302 ? 0.4829 0.5991 0.5482 -0.0395 -0.0267 -0.0582 295 ASN B N     
4500 C  CA    . ASN B 302 ? 0.4935 0.6118 0.5680 -0.0546 -0.0196 -0.0543 295 ASN B CA    
4501 C  C     . ASN B 302 ? 0.5311 0.6540 0.6162 -0.0722 -0.0255 -0.0612 295 ASN B C     
4502 O  O     . ASN B 302 ? 0.5453 0.6712 0.6302 -0.0705 -0.0355 -0.0698 295 ASN B O     
4503 C  CB    . ASN B 302 ? 0.4805 0.6265 0.5677 -0.0504 -0.0121 -0.0506 295 ASN B CB    
4504 C  CG    . ASN B 302 ? 0.4882 0.6692 0.5921 -0.0451 -0.0180 -0.0574 295 ASN B CG    
4505 O  OD1   . ASN B 302 ? 0.5118 0.7022 0.6237 -0.0531 -0.0263 -0.0649 295 ASN B OD1   
4506 N  ND2   . ASN B 302 ? 0.4726 0.6712 0.5805 -0.0306 -0.0152 -0.0555 295 ASN B ND2   
4507 N  N     . LYS B 303 ? 0.5519 0.6745 0.6447 -0.0898 -0.0194 -0.0575 296 LYS B N     
4508 C  CA    . LYS B 303 ? 0.5947 0.7146 0.6958 -0.1098 -0.0246 -0.0630 296 LYS B CA    
4509 C  C     . LYS B 303 ? 0.6096 0.7721 0.7356 -0.1153 -0.0291 -0.0710 296 LYS B C     
4510 O  O     . LYS B 303 ? 0.6434 0.8079 0.7767 -0.1274 -0.0382 -0.0797 296 LYS B O     
4511 C  CB    . LYS B 303 ? 0.6203 0.7221 0.7190 -0.1283 -0.0163 -0.0548 296 LYS B CB    
4512 C  CG    . LYS B 303 ? 0.6195 0.7501 0.7326 -0.1353 -0.0042 -0.0482 296 LYS B CG    
4513 C  CD    . LYS B 303 ? 0.6558 0.7679 0.7643 -0.1561 0.0039  -0.0394 296 LYS B CD    
4514 C  CE    . LYS B 303 ? 0.7052 0.7970 0.8150 -0.1763 -0.0034 -0.0435 296 LYS B CE    
4515 N  NZ    . LYS B 303 ? 0.7500 0.8305 0.8592 -0.1996 0.0056  -0.0341 296 LYS B NZ    
4516 N  N     . SER B 304 ? 0.5890 0.7854 0.7284 -0.1063 -0.0232 -0.0687 297 SER B N     
4517 C  CA    . SER B 304 ? 0.5993 0.8399 0.7624 -0.1048 -0.0288 -0.0766 297 SER B CA    
4518 C  C     . SER B 304 ? 0.6012 0.8415 0.7582 -0.0933 -0.0435 -0.0859 297 SER B C     
4519 O  O     . SER B 304 ? 0.6287 0.8942 0.8020 -0.1001 -0.0531 -0.0954 297 SER B O     
4520 C  CB    . SER B 304 ? 0.5762 0.8467 0.7496 -0.0907 -0.0208 -0.0728 297 SER B CB    
4521 O  OG    . SER B 304 ? 0.5905 0.8788 0.7785 -0.1047 -0.0087 -0.0683 297 SER B OG    
4522 N  N     . SER B 305 ? 0.5755 0.7890 0.7089 -0.0763 -0.0450 -0.0831 298 SER B N     
4523 C  CA    . SER B 305 ? 0.5799 0.7903 0.7023 -0.0642 -0.0572 -0.0905 298 SER B CA    
4524 C  C     . SER B 305 ? 0.6157 0.8065 0.7326 -0.0785 -0.0662 -0.0995 298 SER B C     
4525 O  O     . SER B 305 ? 0.6318 0.8270 0.7429 -0.0718 -0.0780 -0.1086 298 SER B O     
4526 C  CB    . SER B 305 ? 0.5485 0.7359 0.6477 -0.0450 -0.0542 -0.0843 298 SER B CB    
4527 O  OG    . SER B 305 ? 0.5212 0.7213 0.6240 -0.0331 -0.0462 -0.0764 298 SER B OG    
4528 N  N     . GLN C 25  ? 0.9661 1.1064 0.7863 0.0336  0.1489  0.1334  18  GLN C N     
4529 C  CA    . GLN C 25  ? 0.9259 1.0314 0.7305 0.0383  0.1280  0.1091  18  GLN C CA    
4530 C  C     . GLN C 25  ? 0.8899 1.0098 0.7172 0.0464  0.1285  0.0983  18  GLN C C     
4531 O  O     . GLN C 25  ? 0.8664 1.0197 0.7344 0.0386  0.1334  0.1079  18  GLN C O     
4532 C  CB    . GLN C 25  ? 0.8840 0.9710 0.7019 0.0186  0.1064  0.1065  18  GLN C CB    
4533 C  CG    . GLN C 25  ? 0.9258 0.9968 0.7228 0.0107  0.1050  0.1196  18  GLN C CG    
4534 C  CD    . GLN C 25  ? 0.8971 0.9466 0.7046 -0.0043 0.0849  0.1175  18  GLN C CD    
4535 O  OE1   . GLN C 25  ? 0.8768 0.9350 0.7141 -0.0207 0.0814  0.1247  18  GLN C OE1   
4536 N  NE2   . GLN C 25  ? 0.9053 0.9248 0.6859 0.0017  0.0708  0.1082  18  GLN C NE2   
4537 N  N     . VAL C 26  ? 0.8941 0.9872 0.6936 0.0615  0.1221  0.0795  19  VAL C N     
4538 C  CA    . VAL C 26  ? 0.8685 0.9671 0.6835 0.0700  0.1211  0.0690  19  VAL C CA    
4539 C  C     . VAL C 26  ? 0.8002 0.8905 0.6403 0.0533  0.0997  0.0597  19  VAL C C     
4540 O  O     . VAL C 26  ? 0.7896 0.8515 0.6128 0.0486  0.0838  0.0490  19  VAL C O     
4541 C  CB    . VAL C 26  ? 0.9182 0.9851 0.6874 0.0926  0.1230  0.0537  19  VAL C CB    
4542 C  CG1   . VAL C 26  ? 0.8986 0.9624 0.6795 0.1010  0.1193  0.0425  19  VAL C CG1   
4543 C  CG2   . VAL C 26  ? 0.9972 1.0706 0.7359 0.1127  0.1472  0.0625  19  VAL C CG2   
4544 N  N     . PRO C 27  ? 0.7591 0.8745 0.6389 0.0448  0.0986  0.0639  20  PRO C N     
4545 C  CA    . PRO C 27  ? 0.7041 0.8107 0.6028 0.0300  0.0807  0.0557  20  PRO C CA    
4546 C  C     . PRO C 27  ? 0.6891 0.7767 0.5794 0.0378  0.0721  0.0400  20  PRO C C     
4547 O  O     . PRO C 27  ? 0.6669 0.7662 0.5778 0.0377  0.0710  0.0391  20  PRO C O     
4548 C  CB    . PRO C 27  ? 0.6842 0.8240 0.6221 0.0183  0.0834  0.0683  20  PRO C CB    
4549 C  CG    . PRO C 27  ? 0.7177 0.8856 0.6626 0.0343  0.1011  0.0770  20  PRO C CG    
4550 C  CD    . PRO C 27  ? 0.7700 0.9254 0.6787 0.0489  0.1138  0.0778  20  PRO C CD    
4551 N  N     . VAL C 28  ? 0.7055 0.7627 0.5660 0.0423  0.0637  0.0287  21  VAL C N     
4552 C  CA    . VAL C 28  ? 0.7120 0.7469 0.5582 0.0496  0.0561  0.0154  21  VAL C CA    
4553 C  C     . VAL C 28  ? 0.6618 0.6965 0.5321 0.0364  0.0431  0.0104  21  VAL C C     
4554 O  O     . VAL C 28  ? 0.6625 0.6876 0.5318 0.0402  0.0398  0.0040  21  VAL C O     
4555 C  CB    . VAL C 28  ? 0.7563 0.7576 0.5623 0.0552  0.0477  0.0058  21  VAL C CB    
4556 C  CG1   . VAL C 28  ? 0.7391 0.7343 0.5470 0.0419  0.0338  0.0059  21  VAL C CG1   
4557 C  CG2   . VAL C 28  ? 0.7761 0.7497 0.5652 0.0602  0.0381  -0.0071 21  VAL C CG2   
4558 N  N     . SER C 29  ? 0.6295 0.6696 0.5156 0.0227  0.0359  0.0129  22  SER C N     
4559 C  CA    . SER C 29  ? 0.5915 0.6312 0.4963 0.0123  0.0260  0.0085  22  SER C CA    
4560 C  C     . SER C 29  ? 0.5655 0.6206 0.4914 0.0022  0.0273  0.0155  22  SER C C     
4561 O  O     . SER C 29  ? 0.5718 0.6242 0.4947 -0.0015 0.0260  0.0195  22  SER C O     
4562 C  CB    . SER C 29  ? 0.5933 0.6173 0.4910 0.0082  0.0136  0.0018  22  SER C CB    
4563 O  OG    . SER C 29  ? 0.5639 0.5919 0.4807 0.0004  0.0081  -0.0007 22  SER C OG    
4564 N  N     . VAL C 30  ? 0.5458 0.6128 0.4890 -0.0017 0.0285  0.0172  23  VAL C N     
4565 C  CA    . VAL C 30  ? 0.5346 0.6122 0.4931 -0.0121 0.0280  0.0236  23  VAL C CA    
4566 C  C     . VAL C 30  ? 0.5133 0.5855 0.4789 -0.0183 0.0213  0.0179  23  VAL C C     
4567 O  O     . VAL C 30  ? 0.5054 0.5762 0.4716 -0.0154 0.0200  0.0135  23  VAL C O     
4568 C  CB    . VAL C 30  ? 0.5447 0.6453 0.5168 -0.0121 0.0347  0.0337  23  VAL C CB    
4569 C  CG1   . VAL C 30  ? 0.5424 0.6510 0.5295 -0.0269 0.0297  0.0403  23  VAL C CG1   
4570 C  CG2   . VAL C 30  ? 0.5743 0.6831 0.5382 -0.0037 0.0454  0.0407  23  VAL C CG2   
4571 N  N     . ASN C 31  ? 0.5136 0.5796 0.4807 -0.0261 0.0177  0.0187  24  ASN C N     
4572 C  CA    . ASN C 31  ? 0.5064 0.5659 0.4752 -0.0310 0.0135  0.0142  24  ASN C CA    
4573 C  C     . ASN C 31  ? 0.5167 0.5818 0.4909 -0.0404 0.0105  0.0195  24  ASN C C     
4574 O  O     . ASN C 31  ? 0.5350 0.5986 0.5101 -0.0480 0.0086  0.0256  24  ASN C O     
4575 C  CB    . ASN C 31  ? 0.5135 0.5578 0.4759 -0.0302 0.0113  0.0102  24  ASN C CB    
4576 C  CG    . ASN C 31  ? 0.5042 0.5487 0.4679 -0.0231 0.0113  0.0052  24  ASN C CG    
4577 O  OD1   . ASN C 31  ? 0.4993 0.5443 0.4661 -0.0225 0.0120  0.0014  24  ASN C OD1   
4578 N  ND2   . ASN C 31  ? 0.5085 0.5535 0.4689 -0.0189 0.0102  0.0062  24  ASN C ND2   
4579 N  N     . TYR C 32  ? 0.5115 0.5818 0.4886 -0.0415 0.0082  0.0182  25  TYR C N     
4580 C  CA    . TYR C 32  ? 0.5279 0.6035 0.5093 -0.0516 0.0015  0.0233  25  TYR C CA    
4581 C  C     . TYR C 32  ? 0.5408 0.5960 0.5064 -0.0556 -0.0039 0.0159  25  TYR C C     
4582 O  O     . TYR C 32  ? 0.5332 0.5869 0.4938 -0.0508 -0.0023 0.0118  25  TYR C O     
4583 C  CB    . TYR C 32  ? 0.5235 0.6222 0.5190 -0.0476 0.0025  0.0297  25  TYR C CB    
4584 C  CG    . TYR C 32  ? 0.5433 0.6535 0.5475 -0.0579 -0.0072 0.0366  25  TYR C CG    
4585 C  CD1   . TYR C 32  ? 0.5689 0.6708 0.5703 -0.0731 -0.0165 0.0391  25  TYR C CD1   
4586 C  CD2   . TYR C 32  ? 0.5444 0.6698 0.5572 -0.0529 -0.0096 0.0406  25  TYR C CD2   
4587 C  CE1   . TYR C 32  ? 0.5959 0.7063 0.6037 -0.0852 -0.0295 0.0454  25  TYR C CE1   
4588 C  CE2   . TYR C 32  ? 0.5679 0.7051 0.5890 -0.0628 -0.0217 0.0477  25  TYR C CE2   
4589 C  CZ    . TYR C 32  ? 0.5939 0.7248 0.6131 -0.0801 -0.0325 0.0502  25  TYR C CZ    
4590 O  OH    . TYR C 32  ? 0.6269 0.7671 0.6526 -0.0933 -0.0486 0.0573  25  TYR C OH    
4591 N  N     . HIS C 33  ? 0.5676 0.6038 0.5222 -0.0631 -0.0090 0.0145  26  HIS C N     
4592 C  CA    . HIS C 33  ? 0.5965 0.6067 0.5287 -0.0649 -0.0134 0.0065  26  HIS C CA    
4593 C  C     . HIS C 33  ? 0.6270 0.6356 0.5544 -0.0780 -0.0261 0.0099  26  HIS C C     
4594 O  O     . HIS C 33  ? 0.6654 0.6578 0.5848 -0.0904 -0.0363 0.0117  26  HIS C O     
4595 C  CB    . HIS C 33  ? 0.6245 0.6076 0.5420 -0.0643 -0.0139 0.0025  26  HIS C CB    
4596 C  CG    . HIS C 33  ? 0.6024 0.5879 0.5248 -0.0510 -0.0041 0.0000  26  HIS C CG    
4597 N  ND1   . HIS C 33  ? 0.6128 0.5855 0.5241 -0.0394 0.0015  -0.0077 26  HIS C ND1   
4598 C  CD2   . HIS C 33  ? 0.5766 0.5778 0.5136 -0.0469 0.0001  0.0045  26  HIS C CD2   
4599 C  CE1   . HIS C 33  ? 0.5931 0.5756 0.5162 -0.0305 0.0069  -0.0066 26  HIS C CE1   
4600 N  NE2   . HIS C 33  ? 0.5718 0.5689 0.5076 -0.0353 0.0052  0.0000  26  HIS C NE2   
4601 N  N     . PHE C 34  ? 0.6162 0.6392 0.5473 -0.0758 -0.0270 0.0113  27  PHE C N     
4602 C  CA    . PHE C 34  ? 0.6367 0.6724 0.5744 -0.0865 -0.0399 0.0187  27  PHE C CA    
4603 C  C     . PHE C 34  ? 0.6919 0.6975 0.5997 -0.0971 -0.0538 0.0132  27  PHE C C     
4604 O  O     . PHE C 34  ? 0.7234 0.7352 0.6358 -0.1113 -0.0698 0.0201  27  PHE C O     
4605 C  CB    . PHE C 34  ? 0.6100 0.6695 0.5616 -0.0774 -0.0357 0.0231  27  PHE C CB    
4606 C  CG    . PHE C 34  ? 0.6120 0.6572 0.5429 -0.0698 -0.0319 0.0164  27  PHE C CG    
4607 C  CD1   . PHE C 34  ? 0.6500 0.6830 0.5601 -0.0754 -0.0426 0.0157  27  PHE C CD1   
4608 C  CD2   . PHE C 34  ? 0.5829 0.6279 0.5150 -0.0585 -0.0185 0.0125  27  PHE C CD2   
4609 C  CE1   . PHE C 34  ? 0.6581 0.6793 0.5477 -0.0684 -0.0370 0.0118  27  PHE C CE1   
4610 C  CE2   . PHE C 34  ? 0.5903 0.6258 0.5067 -0.0538 -0.0141 0.0096  27  PHE C CE2   
4611 C  CZ    . PHE C 34  ? 0.6275 0.6513 0.5221 -0.0582 -0.0219 0.0096  27  PHE C CZ    
4612 N  N     A SER C 35  ? 0.7115 0.6851 0.5887 -0.0898 -0.0482 0.0014  28  SER C N     
4613 N  N     B SER C 35  ? 0.7114 0.6852 0.5885 -0.0897 -0.0482 0.0014  28  SER C N     
4614 C  CA    A SER C 35  ? 0.7772 0.7130 0.6155 -0.0959 -0.0592 -0.0067 28  SER C CA    
4615 C  CA    B SER C 35  ? 0.7776 0.7134 0.6163 -0.0963 -0.0595 -0.0065 28  SER C CA    
4616 C  C     A SER C 35  ? 0.8015 0.7032 0.6150 -0.0861 -0.0501 -0.0176 28  SER C C     
4617 C  C     B SER C 35  ? 0.8016 0.7035 0.6167 -0.0873 -0.0510 -0.0170 28  SER C C     
4618 O  O     A SER C 35  ? 0.7611 0.6746 0.5896 -0.0732 -0.0348 -0.0183 28  SER C O     
4619 O  O     B SER C 35  ? 0.7613 0.6750 0.5932 -0.0759 -0.0368 -0.0170 28  SER C O     
4620 C  CB    A SER C 35  ? 0.7914 0.7254 0.6104 -0.0911 -0.0595 -0.0091 28  SER C CB    
4621 C  CB    B SER C 35  ? 0.7954 0.7265 0.6121 -0.0914 -0.0599 -0.0098 28  SER C CB    
4622 O  OG    A SER C 35  ? 0.7588 0.6992 0.5783 -0.0745 -0.0400 -0.0126 28  SER C OG    
4623 O  OG    B SER C 35  ? 0.8709 0.7603 0.6421 -0.0960 -0.0705 -0.0189 28  SER C OG    
4624 N  N     . ARG C 36  ? 0.8754 0.7333 0.6494 -0.0911 -0.0607 -0.0261 29  ARG C N     
4625 C  CA    . ARG C 36  ? 0.9145 0.7346 0.6603 -0.0784 -0.0523 -0.0369 29  ARG C CA    
4626 C  C     . ARG C 36  ? 0.9686 0.7588 0.6699 -0.0641 -0.0449 -0.0490 29  ARG C C     
4627 O  O     . ARG C 36  ? 1.0074 0.7685 0.6846 -0.0482 -0.0344 -0.0581 29  ARG C O     
4628 C  CB    . ARG C 36  ? 0.9714 0.7553 0.7023 -0.0926 -0.0683 -0.0376 29  ARG C CB    
4629 C  CG    . ARG C 36  ? 0.9291 0.7318 0.6947 -0.0952 -0.0643 -0.0283 29  ARG C CG    
4630 C  CD    . ARG C 36  ? 0.9946 0.7575 0.7436 -0.1106 -0.0799 -0.0270 29  ARG C CD    
4631 N  NE    . ARG C 36  ? 0.9554 0.7442 0.7407 -0.1183 -0.0778 -0.0135 29  ARG C NE    
4632 C  CZ    . ARG C 36  ? 0.9467 0.7271 0.7349 -0.1065 -0.0678 -0.0131 29  ARG C CZ    
4633 N  NH1   . ARG C 36  ? 0.9662 0.7198 0.7305 -0.0842 -0.0574 -0.0248 29  ARG C NH1   
4634 N  NH2   . ARG C 36  ? 0.9222 0.7240 0.7381 -0.1157 -0.0673 0.0003  29  ARG C NH2   
4635 N  N     . LYS C 37  ? 0.9771 0.7750 0.6665 -0.0672 -0.0484 -0.0481 30  LYS C N     
4636 C  CA    . LYS C 37  ? 1.0366 0.8068 0.6798 -0.0534 -0.0395 -0.0581 30  LYS C CA    
4637 C  C     . LYS C 37  ? 0.9919 0.7897 0.6535 -0.0325 -0.0124 -0.0568 30  LYS C C     
4638 O  O     . LYS C 37  ? 0.9148 0.7558 0.6207 -0.0340 -0.0062 -0.0469 30  LYS C O     
4639 C  CB    . LYS C 37  ? 1.0658 0.8349 0.6894 -0.0653 -0.0545 -0.0554 30  LYS C CB    
4640 C  CG    . LYS C 37  ? 1.1598 0.8852 0.7190 -0.0562 -0.0530 -0.0669 30  LYS C CG    
4641 C  CD    . LYS C 37  ? 1.2064 0.9221 0.7398 -0.0718 -0.0757 -0.0643 30  LYS C CD    
4642 C  CE    . LYS C 37  ? 1.1391 0.9040 0.7093 -0.0745 -0.0731 -0.0503 30  LYS C CE    
4643 N  NZ    . LYS C 37  ? 1.1943 0.9484 0.7362 -0.0869 -0.0956 -0.0471 30  LYS C NZ    
4644 N  N     . CYS C 38  ? 1.0477 0.8204 0.6757 -0.0130 0.0034  -0.0661 31  CYS C N     
4645 C  CA    . CYS C 38  ? 1.0198 0.8223 0.6656 0.0054  0.0291  -0.0626 31  CYS C CA    
4646 C  C     . CYS C 38  ? 1.1027 0.8800 0.6985 0.0221  0.0438  -0.0700 31  CYS C C     
4647 O  O     . CYS C 38  ? 1.1904 0.9171 0.7331 0.0260  0.0369  -0.0819 31  CYS C O     
4648 C  CB    . CYS C 38  ? 0.9880 0.8039 0.6651 0.0175  0.0397  -0.0618 31  CYS C CB    
4649 S  SG    . CYS C 38  ? 0.9676 0.8244 0.6708 0.0387  0.0692  -0.0556 31  CYS C SG    
4650 N  N     . ASN C 39  ? 1.0836 0.8943 0.6942 0.0320  0.0648  -0.0625 32  ASN C N     
4651 C  CA    . ASN C 39  ? 1.1651 0.9586 0.7305 0.0495  0.0837  -0.0667 32  ASN C CA    
4652 C  C     . ASN C 39  ? 1.2062 0.9948 0.7679 0.0763  0.1059  -0.0722 32  ASN C C     
4653 O  O     . ASN C 39  ? 1.2973 1.0587 0.8106 0.0957  0.1216  -0.0796 32  ASN C O     
4654 C  CB    . ASN C 39  ? 1.1444 0.9725 0.7213 0.0463  0.0961  -0.0540 32  ASN C CB    
4655 C  CG    . ASN C 39  ? 1.0560 0.9396 0.6988 0.0429  0.1061  -0.0400 32  ASN C CG    
4656 O  OD1   . ASN C 39  ? 0.9873 0.8864 0.6702 0.0333  0.0939  -0.0381 32  ASN C OD1   
4657 N  ND2   . ASN C 39  ? 1.0635 0.9761 0.7168 0.0492  0.1274  -0.0293 32  ASN C ND2   
4658 N  N     . LYS C 40  ? 1.1480 0.9616 0.7579 0.0794  0.1074  -0.0684 33  LYS C N     
4659 C  CA    . LYS C 40  ? 1.1759 1.0001 0.7970 0.1060  0.1296  -0.0689 33  LYS C CA    
4660 C  C     . LYS C 40  ? 1.2249 1.0017 0.8211 0.1163  0.1202  -0.0813 33  LYS C C     
4661 O  O     . LYS C 40  ? 1.2375 0.9743 0.8084 0.0996  0.0964  -0.0887 33  LYS C O     
4662 C  CB    . LYS C 40  ? 1.0883 0.9752 0.7804 0.1034  0.1373  -0.0540 33  LYS C CB    
4663 C  CG    . LYS C 40  ? 1.0561 0.9877 0.7731 0.0954  0.1493  -0.0403 33  LYS C CG    
4664 C  CD    . LYS C 40  ? 1.1395 1.0652 0.8182 0.1124  0.1731  -0.0403 33  LYS C CD    
4665 C  CE    . LYS C 40  ? 1.1168 1.0881 0.8223 0.1041  0.1871  -0.0236 33  LYS C CE    
4666 N  NZ    . LYS C 40  ? 1.1090 1.1330 0.8647 0.1168  0.2090  -0.0106 33  LYS C NZ    
4667 N  N     . GLU C 41  ? 1.2597 1.0424 0.8644 0.1441  0.1392  -0.0820 34  GLU C N     
4668 C  CA    . GLU C 41  ? 1.3273 1.0604 0.9029 0.1612  0.1349  -0.0935 34  GLU C CA    
4669 C  C     . GLU C 41  ? 1.2917 1.0603 0.9193 0.1772  0.1435  -0.0851 34  GLU C C     
4670 O  O     . GLU C 41  ? 1.3651 1.1129 0.9760 0.2072  0.1564  -0.0904 34  GLU C O     
4671 C  CB    . GLU C 41  ? 1.4566 1.1419 0.9650 0.1895  0.1520  -0.1067 34  GLU C CB    
4672 C  CG    . GLU C 41  ? 1.5204 1.1523 0.9620 0.1753  0.1379  -0.1184 34  GLU C CG    
4673 C  CD    . GLU C 41  ? 1.5900 1.1446 0.9801 0.1666  0.1113  -0.1335 34  GLU C CD    
4674 O  OE1   . GLU C 41  ? 1.7167 1.2069 1.0341 0.1847  0.1145  -0.1492 34  GLU C OE1   
4675 O  OE2   . GLU C 41  ? 1.5259 1.0829 0.9464 0.1415  0.0873  -0.1291 34  GLU C OE2   
4676 N  N     . CYS C 42  ? 1.1866 1.0063 0.8748 0.1584  0.1351  -0.0721 35  CYS C N     
4677 C  CA    . CYS C 42  ? 1.1523 1.0042 0.8886 0.1692  0.1373  -0.0635 35  CYS C CA    
4678 C  C     . CYS C 42  ? 1.2065 1.0031 0.9142 0.1792  0.1253  -0.0726 35  CYS C C     
4679 O  O     . CYS C 42  ? 1.2080 0.9623 0.8894 0.1590  0.1042  -0.0788 35  CYS C O     
4680 C  CB    . CYS C 42  ? 1.0438 0.9436 0.8353 0.1439  0.1244  -0.0511 35  CYS C CB    
4681 S  SG    . CYS C 42  ? 0.9887 0.9527 0.8195 0.1331  0.1376  -0.0379 35  CYS C SG    
4682 N  N     . LEU C 43  ? 1.2572 1.0560 0.9721 0.2107  0.1390  -0.0716 36  LEU C N     
4683 C  CA    . LEU C 43  ? 1.3332 1.0723 1.0136 0.2271  0.1313  -0.0804 36  LEU C CA    
4684 C  C     . LEU C 43  ? 1.2734 1.0112 0.9798 0.2063  0.1078  -0.0738 36  LEU C C     
4685 O  O     . LEU C 43  ? 1.3215 0.9998 0.9923 0.2017  0.0921  -0.0807 36  LEU C O     
4686 C  CB    . LEU C 43  ? 1.4023 1.1540 1.0905 0.2698  0.1546  -0.0785 36  LEU C CB    
4687 C  CG    . LEU C 43  ? 1.4955 1.2320 1.1421 0.2971  0.1804  -0.0873 36  LEU C CG    
4688 C  CD1   . LEU C 43  ? 1.5393 1.3189 1.2175 0.3376  0.2076  -0.0786 36  LEU C CD1   
4689 C  CD2   . LEU C 43  ? 1.6101 1.2514 1.1731 0.3060  0.1729  -0.1073 36  LEU C CD2   
4690 N  N     . PHE C 44  ? 1.1758 0.9766 0.9406 0.1921  0.1050  -0.0601 37  PHE C N     
4691 C  CA    . PHE C 44  ? 1.1251 0.9328 0.9169 0.1780  0.0871  -0.0519 37  PHE C CA    
4692 C  C     . PHE C 44  ? 1.0642 0.8657 0.8533 0.1416  0.0689  -0.0514 37  PHE C C     
4693 O  O     . PHE C 44  ? 1.0297 0.8332 0.8349 0.1289  0.0551  -0.0446 37  PHE C O     
4694 C  CB    . PHE C 44  ? 1.0670 0.9419 0.9190 0.1836  0.0918  -0.0378 37  PHE C CB    
4695 C  CG    . PHE C 44  ? 1.0057 0.9382 0.8917 0.1720  0.1010  -0.0314 37  PHE C CG    
4696 C  CD1   . PHE C 44  ? 0.9420 0.8818 0.8292 0.1420  0.0916  -0.0314 37  PHE C CD1   
4697 C  CD2   . PHE C 44  ? 1.0186 0.9992 0.9374 0.1915  0.1192  -0.0236 37  PHE C CD2   
4698 C  CE1   . PHE C 44  ? 0.8958 0.8822 0.8112 0.1319  0.0991  -0.0248 37  PHE C CE1   
4699 C  CE2   . PHE C 44  ? 0.9708 1.0018 0.9208 0.1782  0.1267  -0.0157 37  PHE C CE2   
4700 C  CZ    . PHE C 44  ? 0.9114 0.9412 0.8567 0.1484  0.1163  -0.0170 37  PHE C CZ    
4701 N  N     . CYS C 45  ? 1.0600 0.8541 0.8278 0.1270  0.0694  -0.0575 38  CYS C N     
4702 C  CA    . CYS C 45  ? 0.9943 0.8010 0.7715 0.0953  0.0558  -0.0542 38  CYS C CA    
4703 C  C     . CYS C 45  ? 0.9963 0.7720 0.7649 0.0779  0.0366  -0.0523 38  CYS C C     
4704 O  O     . CYS C 45  ? 1.0700 0.7903 0.7989 0.0789  0.0287  -0.0594 38  CYS C O     
4705 C  CB    . CYS C 45  ? 1.0159 0.8067 0.7616 0.0857  0.0565  -0.0617 38  CYS C CB    
4706 S  SG    . CYS C 45  ? 0.9416 0.7539 0.7031 0.0510  0.0409  -0.0559 38  CYS C SG    
4707 N  N     . PHE C 46  ? 0.9233 0.7334 0.7271 0.0621  0.0294  -0.0420 39  PHE C N     
4708 C  CA    . PHE C 46  ? 0.9225 0.7132 0.7242 0.0459  0.0145  -0.0365 39  PHE C CA    
4709 C  C     . PHE C 46  ? 0.8921 0.6879 0.6937 0.0183  0.0042  -0.0342 39  PHE C C     
4710 O  O     . PHE C 46  ? 0.8770 0.6734 0.6872 0.0019  -0.0054 -0.0262 39  PHE C O     
4711 C  CB    . PHE C 46  ? 0.8839 0.7033 0.7174 0.0513  0.0143  -0.0264 39  PHE C CB    
4712 C  CG    . PHE C 46  ? 0.8037 0.6750 0.6730 0.0416  0.0158  -0.0195 39  PHE C CG    
4713 C  CD1   . PHE C 46  ? 0.7625 0.6555 0.6389 0.0286  0.0177  -0.0209 39  PHE C CD1   
4714 C  CD2   . PHE C 46  ? 0.7787 0.6720 0.6707 0.0456  0.0133  -0.0114 39  PHE C CD2   
4715 C  CE1   . PHE C 46  ? 0.7013 0.6335 0.6054 0.0211  0.0181  -0.0153 39  PHE C CE1   
4716 C  CE2   . PHE C 46  ? 0.7193 0.6515 0.6368 0.0370  0.0128  -0.0066 39  PHE C CE2   
4717 C  CZ    . PHE C 46  ? 0.6820 0.6319 0.6050 0.0252  0.0156  -0.0089 39  PHE C CZ    
4718 N  N     . HIS C 47  ? 0.8868 0.6895 0.6803 0.0140  0.0070  -0.0396 40  HIS C N     
4719 C  CA    . HIS C 47  ? 0.8710 0.6773 0.6633 -0.0096 -0.0040 -0.0371 40  HIS C CA    
4720 C  C     . HIS C 47  ? 0.9277 0.7041 0.6827 -0.0088 -0.0056 -0.0476 40  HIS C C     
4721 O  O     . HIS C 47  ? 0.9095 0.7064 0.6661 -0.0026 0.0037  -0.0500 40  HIS C O     
4722 C  CB    . HIS C 47  ? 0.7886 0.6473 0.6188 -0.0166 -0.0003 -0.0289 40  HIS C CB    
4723 C  CG    . HIS C 47  ? 0.7689 0.6382 0.6097 -0.0385 -0.0117 -0.0212 40  HIS C CG    
4724 N  ND1   . HIS C 47  ? 0.7374 0.6256 0.6010 -0.0453 -0.0134 -0.0113 40  HIS C ND1   
4725 C  CD2   . HIS C 47  ? 0.7839 0.6494 0.6165 -0.0540 -0.0217 -0.0207 40  HIS C CD2   
4726 C  CE1   . HIS C 47  ? 0.7328 0.6319 0.6048 -0.0633 -0.0218 -0.0042 40  HIS C CE1   
4727 N  NE2   . HIS C 47  ? 0.7590 0.6461 0.6148 -0.0694 -0.0283 -0.0095 40  HIS C NE2   
4728 N  N     . THR C 48  ? 1.0058 0.7296 0.7236 -0.0156 -0.0184 -0.0533 41  THR C N     
4729 C  CA    . THR C 48  ? 1.0902 0.7677 0.7581 -0.0086 -0.0201 -0.0665 41  THR C CA    
4730 C  C     . THR C 48  ? 1.1064 0.7773 0.7597 -0.0327 -0.0371 -0.0666 41  THR C C     
4731 O  O     . THR C 48  ? 1.0676 0.7617 0.7484 -0.0554 -0.0498 -0.0559 41  THR C O     
4732 C  CB    . THR C 48  ? 1.1856 0.7986 0.8135 -0.0006 -0.0265 -0.0742 41  THR C CB    
4733 O  OG1   . THR C 48  ? 1.2068 0.7975 0.8339 -0.0273 -0.0478 -0.0675 41  THR C OG1   
4734 C  CG2   . THR C 48  ? 1.1801 0.7985 0.8220 0.0255  -0.0114 -0.0729 41  THR C CG2   
4735 N  N     . ALA C 49  ? 1.1744 0.8123 0.7821 -0.0264 -0.0377 -0.0782 42  ALA C N     
4736 C  CA    . ALA C 49  ? 1.1988 0.8303 0.7886 -0.0470 -0.0550 -0.0787 42  ALA C CA    
4737 C  C     . ALA C 49  ? 1.2850 0.8624 0.8421 -0.0690 -0.0818 -0.0817 42  ALA C C     
4738 O  O     . ALA C 49  ? 1.3855 0.9062 0.8846 -0.0673 -0.0912 -0.0948 42  ALA C O     
4739 C  CB    . ALA C 49  ? 1.2405 0.8598 0.7921 -0.0307 -0.0439 -0.0888 42  ALA C CB    
4740 N  N     . THR C 50  ? 1.2528 0.8470 0.8455 -0.0905 -0.0943 -0.0689 43  THR C N     
4741 C  CA    . THR C 50  ? 1.3331 0.8814 0.9043 -0.1159 -0.1204 -0.0675 43  THR C CA    
4742 C  C     . THR C 50  ? 1.3360 0.9054 0.9211 -0.1470 -0.1439 -0.0582 43  THR C C     
4743 O  O     . THR C 50  ? 1.4196 0.9487 0.9816 -0.1717 -0.1698 -0.0575 43  THR C O     
4744 C  CB    . THR C 50  ? 1.3119 0.8650 0.9131 -0.1232 -0.1204 -0.0558 43  THR C CB    
4745 O  OG1   . THR C 50  ? 1.2008 0.8272 0.8633 -0.1263 -0.1096 -0.0405 43  THR C OG1   
4746 C  CG2   . THR C 50  ? 1.3407 0.8582 0.9207 -0.0959 -0.1053 -0.0643 43  THR C CG2   
4747 N  N     . THR C 51  ? 1.2507 0.8831 0.8756 -0.1465 -0.1363 -0.0495 44  THR C N     
4748 C  CA    . THR C 51  ? 1.2578 0.9136 0.8951 -0.1703 -0.1574 -0.0408 44  THR C CA    
4749 C  C     . THR C 51  ? 1.2083 0.8989 0.8505 -0.1553 -0.1455 -0.0425 44  THR C C     
4750 O  O     . THR C 51  ? 1.1567 0.8621 0.8034 -0.1304 -0.1203 -0.0473 44  THR C O     
4751 C  CB    . THR C 51  ? 1.2065 0.9151 0.9044 -0.1925 -0.1651 -0.0196 44  THR C CB    
4752 O  OG1   . THR C 51  ? 1.1002 0.8714 0.8445 -0.1771 -0.1434 -0.0117 44  THR C OG1   
4753 C  CG2   . THR C 51  ? 1.2318 0.9200 0.9371 -0.2041 -0.1686 -0.0133 44  THR C CG2   
4754 N  N     . SER C 52  ? 1.2310 0.9344 0.8731 -0.1721 -0.1655 -0.0370 45  SER C N     
4755 C  CA    . SER C 52  ? 1.1896 0.9271 0.8390 -0.1615 -0.1580 -0.0349 45  SER C CA    
4756 C  C     . SER C 52  ? 1.1235 0.9263 0.8342 -0.1738 -0.1641 -0.0155 45  SER C C     
4757 O  O     . SER C 52  ? 1.0920 0.9244 0.8131 -0.1665 -0.1607 -0.0110 45  SER C O     
4758 C  CB    . SER C 52  ? 1.2817 0.9761 0.8713 -0.1641 -0.1740 -0.0455 45  SER C CB    
4759 O  OG    . SER C 52  ? 1.3600 1.0332 0.9371 -0.1932 -0.2087 -0.0418 45  SER C OG    
4760 N  N     . HIS C 53  ? 1.1074 0.9324 0.8578 -0.1901 -0.1710 -0.0030 46  HIS C N     
4761 C  CA    . HIS C 53  ? 1.0558 0.9445 0.8647 -0.1991 -0.1744 0.0162  46  HIS C CA    
4762 C  C     . HIS C 53  ? 0.9619 0.8927 0.8014 -0.1750 -0.1476 0.0189  46  HIS C C     
4763 O  O     . HIS C 53  ? 0.9223 0.8448 0.7583 -0.1583 -0.1261 0.0115  46  HIS C O     
4764 C  CB    . HIS C 53  ? 1.0621 0.9673 0.9065 -0.2193 -0.1818 0.0302  46  HIS C CB    
4765 C  CG    . HIS C 53  ? 1.0151 0.9898 0.9209 -0.2245 -0.1809 0.0510  46  HIS C CG    
4766 N  ND1   . HIS C 53  ? 1.0532 1.0574 0.9826 -0.2445 -0.2048 0.0654  46  HIS C ND1   
4767 C  CD2   . HIS C 53  ? 0.9400 0.9607 0.8871 -0.2098 -0.1584 0.0599  46  HIS C CD2   
4768 C  CE1   . HIS C 53  ? 1.0010 1.0698 0.9869 -0.2395 -0.1943 0.0830  46  HIS C CE1   
4769 N  NE2   . HIS C 53  ? 0.9339 1.0104 0.9278 -0.2180 -0.1658 0.0789  46  HIS C NE2   
4770 N  N     . VAL C 54  ? 0.9360 0.9102 0.8047 -0.1740 -0.1514 0.0302  47  VAL C N     
4771 C  CA    . VAL C 54  ? 0.8598 0.8746 0.7609 -0.1547 -0.1306 0.0357  47  VAL C CA    
4772 C  C     . VAL C 54  ? 0.8494 0.9176 0.7990 -0.1616 -0.1394 0.0548  47  VAL C C     
4773 O  O     . VAL C 54  ? 0.8944 0.9706 0.8447 -0.1739 -0.1612 0.0617  47  VAL C O     
4774 C  CB    . VAL C 54  ? 0.8500 0.8524 0.7240 -0.1376 -0.1220 0.0271  47  VAL C CB    
4775 C  CG1   . VAL C 54  ? 0.7857 0.8252 0.6912 -0.1205 -0.1053 0.0340  47  VAL C CG1   
4776 C  CG2   . VAL C 54  ? 0.8634 0.8214 0.6951 -0.1279 -0.1096 0.0105  47  VAL C CG2   
4777 N  N     . GLU C 55  ? 0.7970 0.9018 0.7854 -0.1522 -0.1223 0.0634  48  GLU C N     
4778 C  CA    . GLU C 55  ? 0.7897 0.9494 0.8265 -0.1532 -0.1249 0.0823  48  GLU C CA    
4779 C  C     . GLU C 55  ? 0.7971 0.9728 0.8363 -0.1444 -0.1334 0.0865  48  GLU C C     
4780 O  O     . GLU C 55  ? 0.7887 0.9372 0.7958 -0.1326 -0.1288 0.0751  48  GLU C O     
4781 C  CB    . GLU C 55  ? 0.7364 0.9242 0.8012 -0.1363 -0.1001 0.0870  48  GLU C CB    
4782 C  CG    . GLU C 55  ? 0.7431 0.9354 0.8219 -0.1488 -0.0959 0.0932  48  GLU C CG    
4783 C  CD    . GLU C 55  ? 0.7925 1.0151 0.9025 -0.1729 -0.1147 0.1116  48  GLU C CD    
4784 O  OE1   . GLU C 55  ? 0.7898 1.0657 0.9423 -0.1680 -0.1114 0.1285  48  GLU C OE1   
4785 O  OE2   . GLU C 55  ? 0.8412 1.0332 0.9319 -0.1959 -0.1338 0.1091  48  GLU C OE2   
4786 N  N     . LYS C 56  ? 0.8172 1.0399 0.8970 -0.1498 -0.1451 0.1049  49  LYS C N     
4787 C  CA    . LYS C 56  ? 0.8249 1.0696 0.9144 -0.1375 -0.1520 0.1122  49  LYS C CA    
4788 C  C     . LYS C 56  ? 0.7725 1.0307 0.8738 -0.1089 -0.1260 0.1112  49  LYS C C     
4789 O  O     . LYS C 56  ? 0.7425 1.0168 0.8640 -0.1024 -0.1079 0.1133  49  LYS C O     
4790 C  CB    . LYS C 56  ? 0.8647 1.1632 1.0016 -0.1485 -0.1711 0.1346  49  LYS C CB    
4791 C  CG    . LYS C 56  ? 0.9327 1.2215 1.0617 -0.1802 -0.2036 0.1388  49  LYS C CG    
4792 C  CD    . LYS C 56  ? 0.9470 1.2279 1.0821 -0.2032 -0.2054 0.1398  49  LYS C CD    
4793 C  CE    . LYS C 56  ? 1.0254 1.3126 1.1701 -0.2370 -0.2404 0.1513  49  LYS C CE    
4794 N  NZ    . LYS C 56  ? 1.0491 1.3122 1.1876 -0.2607 -0.2431 0.1497  49  LYS C NZ    
4795 N  N     . PRO C 57  ? 0.7692 1.0182 0.8553 -0.0920 -0.1245 0.1086  50  PRO C N     
4796 C  CA    . PRO C 57  ? 0.7317 0.9839 0.8229 -0.0662 -0.1023 0.1065  50  PRO C CA    
4797 C  C     . PRO C 57  ? 0.7235 1.0223 0.8598 -0.0547 -0.0904 0.1197  50  PRO C C     
4798 O  O     . PRO C 57  ? 0.6929 0.9877 0.8294 -0.0434 -0.0700 0.1143  50  PRO C O     
4799 C  CB    . PRO C 57  ? 0.7539 0.9984 0.8314 -0.0545 -0.1107 0.1094  50  PRO C CB    
4800 C  CG    . PRO C 57  ? 0.7898 1.0059 0.8331 -0.0737 -0.1309 0.1040  50  PRO C CG    
4801 C  CD    . PRO C 57  ? 0.8097 1.0381 0.8670 -0.0971 -0.1442 0.1072  50  PRO C CD    
4802 N  N     . GLU C 58  ? 0.7580 1.1027 0.9324 -0.0573 -0.1034 0.1381  51  GLU C N     
4803 C  CA    . GLU C 58  ? 0.7600 1.1546 0.9790 -0.0406 -0.0889 0.1530  51  GLU C CA    
4804 C  C     . GLU C 58  ? 0.7423 1.1460 0.9728 -0.0507 -0.0749 0.1532  51  GLU C C     
4805 O  O     . GLU C 58  ? 0.7300 1.1496 0.9728 -0.0319 -0.0526 0.1554  51  GLU C O     
4806 C  CB    . GLU C 58  ? 0.8065 1.2551 1.0696 -0.0415 -0.1064 0.1752  51  GLU C CB    
4807 C  CG    . GLU C 58  ? 0.8298 1.2697 1.0811 -0.0263 -0.1188 0.1770  51  GLU C CG    
4808 C  CD    . GLU C 58  ? 0.8132 1.2257 1.0420 0.0051  -0.0997 0.1680  51  GLU C CD    
4809 O  OE1   . GLU C 58  ? 0.8136 1.2505 1.0652 0.0295  -0.0798 0.1738  51  GLU C OE1   
4810 O  OE2   . GLU C 58  ? 0.8081 1.1727 0.9940 0.0052  -0.1046 0.1557  51  GLU C OE2   
4811 N  N     . ASN C 59  ? 0.7488 1.1359 0.9688 -0.0794 -0.0881 0.1499  52  ASN C N     
4812 C  CA    . ASN C 59  ? 0.7408 1.1307 0.9680 -0.0921 -0.0780 0.1513  52  ASN C CA    
4813 C  C     . ASN C 59  ? 0.6979 1.0463 0.8899 -0.0797 -0.0575 0.1330  52  ASN C C     
4814 O  O     . ASN C 59  ? 0.6879 1.0468 0.8887 -0.0751 -0.0402 0.1360  52  ASN C O     
4815 C  CB    . ASN C 59  ? 0.7731 1.1482 0.9940 -0.1263 -0.1010 0.1527  52  ASN C CB    
4816 C  CG    . ASN C 59  ? 0.8239 1.2474 1.0872 -0.1430 -0.1230 0.1743  52  ASN C CG    
4817 O  OD1   . ASN C 59  ? 0.8309 1.3051 1.1332 -0.1267 -0.1178 0.1897  52  ASN C OD1   
4818 N  ND2   . ASN C 59  ? 0.8668 1.2744 1.1224 -0.1746 -0.1484 0.1760  52  ASN C ND2   
4819 N  N     . ALA C 60  ? 0.6783 0.9810 0.8306 -0.0749 -0.0598 0.1154  53  ALA C N     
4820 C  CA    . ALA C 60  ? 0.6416 0.9111 0.7661 -0.0620 -0.0421 0.1000  53  ALA C CA    
4821 C  C     . ALA C 60  ? 0.6314 0.9166 0.7655 -0.0353 -0.0240 0.1022  53  ALA C C     
4822 O  O     . ALA C 60  ? 0.6169 0.8963 0.7449 -0.0261 -0.0077 0.0979  53  ALA C O     
4823 C  CB    . ALA C 60  ? 0.6320 0.8570 0.7179 -0.0639 -0.0487 0.0842  53  ALA C CB    
4824 N  N     . LYS C 61  ? 0.6479 0.9493 0.7934 -0.0213 -0.0275 0.1087  54  LYS C N     
4825 C  CA    . LYS C 61  ? 0.6516 0.9594 0.7999 0.0065  -0.0110 0.1094  54  LYS C CA    
4826 C  C     . LYS C 61  ? 0.6650 1.0115 0.8413 0.0136  0.0044  0.1212  54  LYS C C     
4827 O  O     . LYS C 61  ? 0.6650 1.0026 0.8291 0.0319  0.0226  0.1161  54  LYS C O     
4828 C  CB    . LYS C 61  ? 0.6782 0.9973 0.8356 0.0210  -0.0190 0.1168  54  LYS C CB    
4829 C  CG    . LYS C 61  ? 0.6728 0.9513 0.7979 0.0164  -0.0312 0.1066  54  LYS C CG    
4830 C  CD    . LYS C 61  ? 0.7065 0.9944 0.8388 0.0305  -0.0406 0.1160  54  LYS C CD    
4831 C  CE    . LYS C 61  ? 0.7080 0.9534 0.8043 0.0263  -0.0502 0.1074  54  LYS C CE    
4832 N  NZ    . LYS C 61  ? 0.7465 0.9943 0.8453 0.0444  -0.0568 0.1168  54  LYS C NZ    
4833 N  N     . ARG C 62  ? 0.6844 1.0732 0.8964 -0.0021 -0.0034 0.1379  55  ARG C N     
4834 C  CA    . ARG C 62  ? 0.7050 1.1379 0.9481 0.0032  0.0127  0.1532  55  ARG C CA    
4835 C  C     . ARG C 62  ? 0.6852 1.0913 0.9039 -0.0033 0.0252  0.1438  55  ARG C C     
4836 O  O     . ARG C 62  ? 0.6951 1.1075 0.9096 0.0153  0.0462  0.1447  55  ARG C O     
4837 C  CB    . ARG C 62  ? 0.7353 1.2202 1.0251 -0.0173 -0.0015 0.1751  55  ARG C CB    
4838 C  CG    . ARG C 62  ? 0.7621 1.2980 1.0892 -0.0188 0.0144  0.1950  55  ARG C CG    
4839 C  CD    . ARG C 62  ? 0.8010 1.3992 1.1728 0.0053  0.0264  0.2152  55  ARG C CD    
4840 N  NE    . ARG C 62  ? 0.8257 1.4637 1.2215 0.0076  0.0492  0.2310  55  ARG C NE    
4841 C  CZ    . ARG C 62  ? 0.8386 1.4782 1.2214 0.0383  0.0784  0.2289  55  ARG C CZ    
4842 N  NH1   . ARG C 62  ? 0.8347 1.4419 1.1860 0.0702  0.0870  0.2129  55  ARG C NH1   
4843 N  NH2   . ARG C 62  ? 0.8653 1.5380 1.2650 0.0367  0.0987  0.2439  55  ARG C NH2   
4844 N  N     . GLY C 63  ? 0.6646 1.0372 0.8628 -0.0275 0.0122  0.1343  56  GLY C N     
4845 C  CA    . GLY C 63  ? 0.6488 0.9928 0.8225 -0.0332 0.0211  0.1255  56  GLY C CA    
4846 C  C     . GLY C 63  ? 0.6295 0.9395 0.7693 -0.0112 0.0347  0.1092  56  GLY C C     
4847 O  O     . GLY C 63  ? 0.6333 0.9374 0.7610 -0.0051 0.0486  0.1080  56  GLY C O     
4848 N  N     . LEU C 64  ? 0.6151 0.8999 0.7369 -0.0016 0.0289  0.0972  57  LEU C N     
4849 C  CA    . LEU C 64  ? 0.6061 0.8575 0.6973 0.0160  0.0380  0.0828  57  LEU C CA    
4850 C  C     . LEU C 64  ? 0.6387 0.9075 0.7337 0.0420  0.0552  0.0883  57  LEU C C     
4851 O  O     . LEU C 64  ? 0.6481 0.8962 0.7185 0.0543  0.0665  0.0804  57  LEU C O     
4852 C  CB    . LEU C 64  ? 0.5926 0.8158 0.6674 0.0165  0.0268  0.0725  57  LEU C CB    
4853 C  CG    . LEU C 64  ? 0.5699 0.7724 0.6341 -0.0050 0.0134  0.0656  57  LEU C CG    
4854 C  CD1   . LEU C 64  ? 0.5692 0.7550 0.6225 -0.0049 0.0033  0.0612  57  LEU C CD1   
4855 C  CD2   . LEU C 64  ? 0.5503 0.7240 0.5921 -0.0089 0.0177  0.0540  57  LEU C CD2   
4856 N  N     . THR C 65  ? 0.6646 0.9731 0.7902 0.0514  0.0574  0.1028  58  THR C N     
4857 C  CA    . THR C 65  ? 0.7065 1.0368 0.8382 0.0795  0.0767  0.1100  58  THR C CA    
4858 C  C     . THR C 65  ? 0.7224 1.0683 0.8538 0.0794  0.0938  0.1163  58  THR C C     
4859 O  O     . THR C 65  ? 0.7538 1.0868 0.8609 0.1022  0.1110  0.1114  58  THR C O     
4860 C  CB    . THR C 65  ? 0.7332 1.1131 0.9070 0.0875  0.0746  0.1281  58  THR C CB    
4861 O  OG1   . THR C 65  ? 0.7200 1.0781 0.8867 0.0850  0.0569  0.1216  58  THR C OG1   
4862 C  CG2   . THR C 65  ? 0.7860 1.1914 0.9683 0.1220  0.0962  0.1365  58  THR C CG2   
4863 N  N     . LEU C 66  ? 0.7109 1.0818 0.8663 0.0537  0.0883  0.1280  59  LEU C N     
4864 C  CA    . LEU C 66  ? 0.7302 1.1160 0.8864 0.0496  0.1032  0.1372  59  LEU C CA    
4865 C  C     . LEU C 66  ? 0.7192 1.0537 0.8271 0.0534  0.1071  0.1192  59  LEU C C     
4866 O  O     . LEU C 66  ? 0.7516 1.0858 0.8419 0.0668  0.1249  0.1213  59  LEU C O     
4867 C  CB    . LEU C 66  ? 0.7238 1.1339 0.9099 0.0167  0.0914  0.1517  59  LEU C CB    
4868 C  CG    . LEU C 66  ? 0.7474 1.2162 0.9865 0.0088  0.0860  0.1737  59  LEU C CG    
4869 C  CD1   . LEU C 66  ? 0.7523 1.2343 1.0135 -0.0276 0.0714  0.1867  59  LEU C CD1   
4870 C  CD2   . LEU C 66  ? 0.7948 1.3155 1.0602 0.0340  0.1108  0.1914  59  LEU C CD2   
4871 N  N     . LEU C 67  ? 0.6797 0.9721 0.7658 0.0424  0.0903  0.1023  60  LEU C N     
4872 C  CA    . LEU C 67  ? 0.6688 0.9166 0.7154 0.0427  0.0896  0.0867  60  LEU C CA    
4873 C  C     . LEU C 67  ? 0.6969 0.9202 0.7122 0.0693  0.0990  0.0754  60  LEU C C     
4874 O  O     . LEU C 67  ? 0.7221 0.9273 0.7085 0.0777  0.1078  0.0709  60  LEU C O     
4875 C  CB    . LEU C 67  ? 0.6253 0.8436 0.6645 0.0239  0.0704  0.0749  60  LEU C CB    
4876 C  CG    . LEU C 67  ? 0.6122 0.8390 0.6679 -0.0014 0.0608  0.0826  60  LEU C CG    
4877 C  CD1   . LEU C 67  ? 0.5816 0.7835 0.6311 -0.0150 0.0438  0.0719  60  LEU C CD1   
4878 C  CD2   . LEU C 67  ? 0.6239 0.8405 0.6654 -0.0071 0.0665  0.0851  60  LEU C CD2   
4879 N  N     . LYS C 68  ? 0.7024 0.9213 0.7197 0.0827  0.0961  0.0711  61  LYS C N     
4880 C  CA    . LYS C 68  ? 0.7436 0.9338 0.7287 0.1085  0.1038  0.0607  61  LYS C CA    
4881 C  C     . LYS C 68  ? 0.8002 1.0110 0.7794 0.1303  0.1265  0.0695  61  LYS C C     
4882 O  O     . LYS C 68  ? 0.8404 1.0192 0.7785 0.1451  0.1342  0.0595  61  LYS C O     
4883 C  CB    . LYS C 68  ? 0.7510 0.9392 0.7451 0.1202  0.0982  0.0599  61  LYS C CB    
4884 C  CG    . LYS C 68  ? 0.8112 0.9700 0.7738 0.1508  0.1070  0.0516  61  LYS C CG    
4885 C  CD    . LYS C 68  ? 0.8179 0.9158 0.7365 0.1481  0.0958  0.0325  61  LYS C CD    
4886 C  CE    . LYS C 68  ? 0.8954 0.9559 0.7738 0.1779  0.1043  0.0232  61  LYS C CE    
4887 N  NZ    . LYS C 68  ? 0.9072 0.9093 0.7508 0.1716  0.0877  0.0073  61  LYS C NZ    
4888 N  N     . GLN C 69  ? 0.8095 1.0748 0.8293 0.1310  0.1369  0.0891  62  GLN C N     
4889 C  CA    . GLN C 69  ? 0.8701 1.1644 0.8901 0.1536  0.1624  0.1010  62  GLN C CA    
4890 C  C     . GLN C 69  ? 0.8825 1.1639 0.8754 0.1459  0.1704  0.1006  62  GLN C C     
4891 O  O     . GLN C 69  ? 0.9432 1.2172 0.9055 0.1689  0.1898  0.0999  62  GLN C O     
4892 C  CB    . GLN C 69  ? 0.8777 1.2412 0.9556 0.1513  0.1701  0.1257  62  GLN C CB    
4893 C  CG    . GLN C 69  ? 0.9499 1.3521 1.0347 0.1807  0.2000  0.1406  62  GLN C CG    
4894 C  CD    . GLN C 69  ? 1.0067 1.3803 1.0572 0.2207  0.2119  0.1283  62  GLN C CD    
4895 O  OE1   . GLN C 69  ? 1.0394 1.3606 1.0331 0.2350  0.2172  0.1110  62  GLN C OE1   
4896 N  NE2   . GLN C 69  ? 1.0281 1.4339 1.1111 0.2397  0.2150  0.1377  62  GLN C NE2   
4897 N  N     . ALA C 70  ? 0.8318 1.1057 0.8316 0.1150  0.1546  0.1001  63  ALA C N     
4898 C  CA    . ALA C 70  ? 0.8396 1.0994 0.8165 0.1041  0.1577  0.1012  63  ALA C CA    
4899 C  C     . ALA C 70  ? 0.8473 1.0487 0.7704 0.1107  0.1499  0.0799  63  ALA C C     
4900 O  O     . ALA C 70  ? 0.8631 1.0495 0.7617 0.1053  0.1517  0.0801  63  ALA C O     
4901 C  CB    . ALA C 70  ? 0.7930 1.0644 0.7980 0.0711  0.1429  0.1093  63  ALA C CB    
4902 N  N     . GLY C 71  ? 0.8417 1.0103 0.7470 0.1204  0.1396  0.0631  64  GLY C N     
4903 C  CA    . GLY C 71  ? 0.8591 0.9739 0.7161 0.1246  0.1296  0.0442  64  GLY C CA    
4904 C  C     . GLY C 71  ? 0.8008 0.8914 0.6625 0.1027  0.1055  0.0331  64  GLY C C     
4905 O  O     . GLY C 71  ? 0.8112 0.8640 0.6409 0.1004  0.0942  0.0204  64  GLY C O     
4906 N  N     . MET C 72  ? 0.7466 0.8592 0.6471 0.0869  0.0971  0.0384  65  MET C N     
4907 C  CA    . MET C 72  ? 0.7008 0.7924 0.6045 0.0701  0.0779  0.0285  65  MET C CA    
4908 C  C     . MET C 72  ? 0.7205 0.7782 0.6017 0.0803  0.0708  0.0153  65  MET C C     
4909 O  O     . MET C 72  ? 0.7511 0.8093 0.6300 0.0976  0.0779  0.0159  65  MET C O     
4910 C  CB    . MET C 72  ? 0.6538 0.7721 0.5960 0.0538  0.0717  0.0364  65  MET C CB    
4911 C  CG    . MET C 72  ? 0.6135 0.7126 0.5574 0.0384  0.0555  0.0273  65  MET C CG    
4912 S  SD    . MET C 72  ? 0.5763 0.6999 0.5540 0.0209  0.0485  0.0354  65  MET C SD    
4913 C  CE    . MET C 72  ? 0.5885 0.7244 0.5781 0.0332  0.0498  0.0387  65  MET C CE    
4914 N  N     . LYS C 73  ? 0.7115 0.7391 0.5759 0.0700  0.0565  0.0046  66  LYS C N     
4915 C  CA    . LYS C 73  ? 0.7316 0.7245 0.5770 0.0722  0.0457  -0.0064 66  LYS C CA    
4916 C  C     . LYS C 73  ? 0.6836 0.6767 0.5500 0.0526  0.0321  -0.0078 66  LYS C C     
4917 O  O     . LYS C 73  ? 0.6948 0.6693 0.5568 0.0527  0.0256  -0.0118 66  LYS C O     
4918 C  CB    . LYS C 73  ? 0.7820 0.7384 0.5864 0.0764  0.0394  -0.0167 66  LYS C CB    
4919 C  CG    . LYS C 73  ? 0.8453 0.7944 0.6179 0.0984  0.0542  -0.0168 66  LYS C CG    
4920 C  CD    . LYS C 73  ? 0.9064 0.8119 0.6306 0.1016  0.0443  -0.0286 66  LYS C CD    
4921 C  CE    . LYS C 73  ? 0.9926 0.8752 0.6720 0.1287  0.0583  -0.0331 66  LYS C CE    
4922 N  NZ    . LYS C 73  ? 1.0623 0.8947 0.6878 0.1297  0.0442  -0.0464 66  LYS C NZ    
4923 N  N     . LYS C 74  ? 0.6405 0.6510 0.5260 0.0374  0.0286  -0.0042 67  LYS C N     
4924 C  CA    . LYS C 74  ? 0.6018 0.6158 0.5062 0.0217  0.0194  -0.0047 67  LYS C CA    
4925 C  C     . LYS C 74  ? 0.5649 0.6062 0.4944 0.0146  0.0237  0.0029  67  LYS C C     
4926 O  O     . LYS C 74  ? 0.5609 0.6158 0.4951 0.0135  0.0285  0.0081  67  LYS C O     
4927 C  CB    . LYS C 74  ? 0.5981 0.6026 0.4986 0.0118  0.0095  -0.0090 67  LYS C CB    
4928 C  CG    . LYS C 74  ? 0.5688 0.5794 0.4888 -0.0012 0.0030  -0.0086 67  LYS C CG    
4929 C  CD    . LYS C 74  ? 0.5839 0.5831 0.5006 -0.0086 -0.0087 -0.0123 67  LYS C CD    
4930 C  CE    . LYS C 74  ? 0.5631 0.5744 0.5023 -0.0200 -0.0122 -0.0098 67  LYS C CE    
4931 N  NZ    . LYS C 74  ? 0.5320 0.5633 0.4876 -0.0206 -0.0060 -0.0062 67  LYS C NZ    
4932 N  N     . ILE C 75  ? 0.5458 0.5916 0.4884 0.0084  0.0205  0.0041  68  ILE C N     
4933 C  CA    . ILE C 75  ? 0.5204 0.5835 0.4800 -0.0006 0.0205  0.0091  68  ILE C CA    
4934 C  C     . ILE C 75  ? 0.5060 0.5607 0.4673 -0.0098 0.0149  0.0051  68  ILE C C     
4935 O  O     . ILE C 75  ? 0.5140 0.5574 0.4709 -0.0101 0.0120  0.0027  68  ILE C O     
4936 C  CB    . ILE C 75  ? 0.5244 0.6033 0.4953 0.0025  0.0225  0.0160  68  ILE C CB    
4937 C  CG1   . ILE C 75  ? 0.5108 0.6044 0.4953 -0.0088 0.0192  0.0211  68  ILE C CG1   
4938 C  CG2   . ILE C 75  ? 0.5348 0.6017 0.5006 0.0067  0.0193  0.0143  68  ILE C CG2   
4939 C  CD1   . ILE C 75  ? 0.5124 0.6173 0.5034 -0.0140 0.0216  0.0262  68  ILE C CD1   
4940 N  N     . ASN C 76  ? 0.4931 0.5524 0.4596 -0.0163 0.0145  0.0052  69  ASN C N     
4941 C  CA    . ASN C 76  ? 0.4857 0.5421 0.4549 -0.0222 0.0129  0.0029  69  ASN C CA    
4942 C  C     . ASN C 76  ? 0.4852 0.5454 0.4553 -0.0268 0.0129  0.0051  69  ASN C C     
4943 O  O     . ASN C 76  ? 0.4885 0.5504 0.4592 -0.0296 0.0121  0.0069  69  ASN C O     
4944 C  CB    . ASN C 76  ? 0.4847 0.5392 0.4555 -0.0226 0.0120  0.0005  69  ASN C CB    
4945 C  CG    . ASN C 76  ? 0.4850 0.5412 0.4613 -0.0249 0.0132  -0.0007 69  ASN C CG    
4946 O  OD1   . ASN C 76  ? 0.4883 0.5455 0.4676 -0.0274 0.0131  0.0000  69  ASN C OD1   
4947 N  ND2   . ASN C 76  ? 0.4891 0.5449 0.4662 -0.0233 0.0152  -0.0016 69  ASN C ND2   
4948 N  N     . PHE C 77  ? 0.4894 0.5476 0.4567 -0.0289 0.0124  0.0053  70  PHE C N     
4949 C  CA    . PHE C 77  ? 0.4999 0.5568 0.4615 -0.0337 0.0099  0.0064  70  PHE C CA    
4950 C  C     . PHE C 77  ? 0.5096 0.5571 0.4626 -0.0348 0.0128  0.0017  70  PHE C C     
4951 O  O     . PHE C 77  ? 0.5108 0.5581 0.4641 -0.0325 0.0179  0.0003  70  PHE C O     
4952 C  CB    . PHE C 77  ? 0.5099 0.5669 0.4673 -0.0341 0.0076  0.0097  70  PHE C CB    
4953 C  CG    . PHE C 77  ? 0.5114 0.5785 0.4771 -0.0301 0.0044  0.0154  70  PHE C CG    
4954 C  CD1   . PHE C 77  ? 0.5192 0.5987 0.4921 -0.0334 -0.0008 0.0205  70  PHE C CD1   
4955 C  CD2   . PHE C 77  ? 0.5125 0.5767 0.4796 -0.0226 0.0066  0.0161  70  PHE C CD2   
4956 C  CE1   . PHE C 77  ? 0.5249 0.6207 0.5108 -0.0270 -0.0017 0.0277  70  PHE C CE1   
4957 C  CE2   . PHE C 77  ? 0.5224 0.5955 0.4961 -0.0141 0.0060  0.0211  70  PHE C CE2   
4958 C  CZ    . PHE C 77  ? 0.5270 0.6191 0.5122 -0.0154 0.0028  0.0275  70  PHE C CZ    
4959 N  N     . ALA C 78  ? 0.5233 0.5629 0.4695 -0.0380 0.0096  0.0002  71  ALA C N     
4960 C  CA    . ALA C 78  ? 0.5439 0.5690 0.4779 -0.0352 0.0127  -0.0050 71  ALA C CA    
4961 C  C     . ALA C 78  ? 0.5787 0.5859 0.4935 -0.0417 0.0056  -0.0070 71  ALA C C     
4962 O  O     . ALA C 78  ? 0.5839 0.5954 0.4980 -0.0490 -0.0019 -0.0033 71  ALA C O     
4963 C  CB    . ALA C 78  ? 0.5357 0.5612 0.4780 -0.0306 0.0147  -0.0056 71  ALA C CB    
4964 N  N     . GLY C 79  ? 0.6097 0.5957 0.5081 -0.0382 0.0069  -0.0128 72  GLY C N     
4965 C  CA    . GLY C 79  ? 0.6587 0.6172 0.5313 -0.0446 -0.0018 -0.0167 72  GLY C CA    
4966 C  C     . GLY C 79  ? 0.6971 0.6280 0.5510 -0.0353 0.0022  -0.0239 72  GLY C C     
4967 O  O     . GLY C 79  ? 0.6820 0.6170 0.5494 -0.0299 0.0056  -0.0222 72  GLY C O     
4968 N  N     . GLY C 80  ? 0.7536 0.6550 0.5736 -0.0306 0.0027  -0.0320 73  GLY C N     
4969 C  CA    . GLY C 80  ? 0.7770 0.6738 0.5763 -0.0336 0.0010  -0.0341 73  GLY C CA    
4970 C  C     . GLY C 80  ? 0.7432 0.6686 0.5574 -0.0253 0.0151  -0.0305 73  GLY C C     
4971 O  O     . GLY C 80  ? 0.6982 0.6488 0.5421 -0.0204 0.0229  -0.0262 73  GLY C O     
4972 N  N     . GLU C 81  ? 0.7730 0.6921 0.5641 -0.0252 0.0166  -0.0317 74  GLU C N     
4973 C  CA    . GLU C 81  ? 0.7543 0.6963 0.5555 -0.0196 0.0298  -0.0264 74  GLU C CA    
4974 C  C     . GLU C 81  ? 0.7260 0.6837 0.5391 -0.0310 0.0202  -0.0186 74  GLU C C     
4975 O  O     . GLU C 81  ? 0.7588 0.7029 0.5488 -0.0376 0.0095  -0.0187 74  GLU C O     
4976 C  CB    . GLU C 81  ? 0.8162 0.7410 0.5810 -0.0092 0.0418  -0.0308 74  GLU C CB    
4977 C  CG    . GLU C 81  ? 0.8029 0.7528 0.5794 -0.0069 0.0552  -0.0221 74  GLU C CG    
4978 C  CD    . GLU C 81  ? 0.7444 0.7287 0.5670 -0.0068 0.0621  -0.0145 74  GLU C CD    
4979 O  OE1   . GLU C 81  ? 0.7344 0.7253 0.5738 0.0012  0.0674  -0.0170 74  GLU C OE1   
4980 O  OE2   . GLU C 81  ? 0.7185 0.7196 0.5570 -0.0142 0.0612  -0.0062 74  GLU C OE2   
4981 N  N     . PRO C 82  ? 0.6723 0.6565 0.5194 -0.0328 0.0219  -0.0116 75  PRO C N     
4982 C  CA    . PRO C 82  ? 0.6530 0.6485 0.5105 -0.0404 0.0122  -0.0045 75  PRO C CA    
4983 C  C     . PRO C 82  ? 0.6846 0.6745 0.5209 -0.0411 0.0127  -0.0006 75  PRO C C     
4984 O  O     . PRO C 82  ? 0.6938 0.6833 0.5257 -0.0468 0.0003  0.0037  75  PRO C O     
4985 C  CB    . PRO C 82  ? 0.6052 0.6215 0.4945 -0.0385 0.0169  -0.0002 75  PRO C CB    
4986 C  CG    . PRO C 82  ? 0.5949 0.6106 0.4927 -0.0344 0.0211  -0.0052 75  PRO C CG    
4987 C  CD    . PRO C 82  ? 0.6354 0.6368 0.5107 -0.0277 0.0300  -0.0104 75  PRO C CD    
4988 N  N     . PHE C 83  ? 0.7081 0.6948 0.5311 -0.0349 0.0272  -0.0009 76  PHE C N     
4989 C  CA    . PHE C 83  ? 0.7390 0.7227 0.5434 -0.0358 0.0306  0.0057  76  PHE C CA    
4990 C  C     . PHE C 83  ? 0.8017 0.7596 0.5617 -0.0360 0.0242  0.0012  76  PHE C C     
4991 O  O     . PHE C 83  ? 0.8395 0.7902 0.5756 -0.0366 0.0254  0.0067  76  PHE C O     
4992 C  CB    . PHE C 83  ? 0.7415 0.7383 0.5552 -0.0311 0.0497  0.0108  76  PHE C CB    
4993 C  CG    . PHE C 83  ? 0.6984 0.7140 0.5469 -0.0361 0.0493  0.0187  76  PHE C CG    
4994 C  CD1   . PHE C 83  ? 0.7060 0.7197 0.5525 -0.0416 0.0451  0.0280  76  PHE C CD1   
4995 C  CD2   . PHE C 83  ? 0.6589 0.6886 0.5376 -0.0352 0.0506  0.0163  76  PHE C CD2   
4996 C  CE1   . PHE C 83  ? 0.6801 0.7020 0.5519 -0.0461 0.0430  0.0340  76  PHE C CE1   
4997 C  CE2   . PHE C 83  ? 0.6327 0.6727 0.5360 -0.0404 0.0478  0.0222  76  PHE C CE2   
4998 C  CZ    . PHE C 83  ? 0.6444 0.6784 0.5433 -0.0459 0.0436  0.0302  76  PHE C CZ    
4999 N  N     . LEU C 84  ? 0.8212 0.7614 0.5667 -0.0372 0.0149  -0.0081 77  LEU C N     
5000 C  CA    . LEU C 84  ? 0.8843 0.7969 0.5883 -0.0422 0.0000  -0.0121 77  LEU C CA    
5001 C  C     . LEU C 84  ? 0.8729 0.7962 0.5890 -0.0533 -0.0206 -0.0036 77  LEU C C     
5002 O  O     . LEU C 84  ? 0.9278 0.8340 0.6113 -0.0581 -0.0340 -0.0028 77  LEU C O     
5003 C  CB    . LEU C 84  ? 0.9152 0.8022 0.6017 -0.0433 -0.0075 -0.0236 77  LEU C CB    
5004 C  CG    . LEU C 84  ? 0.9575 0.8236 0.6169 -0.0284 0.0109  -0.0333 77  LEU C CG    
5005 C  CD1   . LEU C 84  ? 0.9793 0.8197 0.6298 -0.0292 0.0023  -0.0434 77  LEU C CD1   
5006 C  CD2   . LEU C 84  ? 1.0404 0.8795 0.6447 -0.0216 0.0166  -0.0369 77  LEU C CD2   
5007 N  N     . TYR C 85  ? 0.8106 0.7612 0.5711 -0.0560 -0.0235 0.0026  78  TYR C N     
5008 C  CA    . TYR C 85  ? 0.8011 0.7676 0.5793 -0.0623 -0.0402 0.0121  78  TYR C CA    
5009 C  C     . TYR C 85  ? 0.7644 0.7499 0.5666 -0.0563 -0.0323 0.0214  78  TYR C C     
5010 O  O     . TYR C 85  ? 0.7222 0.7281 0.5588 -0.0550 -0.0341 0.0255  78  TYR C O     
5011 C  CB    . TYR C 85  ? 0.7724 0.7536 0.5808 -0.0689 -0.0503 0.0122  78  TYR C CB    
5012 C  CG    . TYR C 85  ? 0.8110 0.7701 0.5995 -0.0776 -0.0603 0.0040  78  TYR C CG    
5013 C  CD1   . TYR C 85  ? 0.8084 0.7514 0.5890 -0.0731 -0.0485 -0.0056 78  TYR C CD1   
5014 C  CD2   . TYR C 85  ? 0.8591 0.8111 0.6355 -0.0906 -0.0834 0.0066  78  TYR C CD2   
5015 C  CE1   . TYR C 85  ? 0.8552 0.7698 0.6126 -0.0803 -0.0585 -0.0134 78  TYR C CE1   
5016 C  CE2   . TYR C 85  ? 0.9071 0.8315 0.6608 -0.1010 -0.0951 -0.0011 78  TYR C CE2   
5017 C  CZ    . TYR C 85  ? 0.9067 0.8094 0.6489 -0.0953 -0.0822 -0.0116 78  TYR C CZ    
5018 O  OH    . TYR C 85  ? 0.9623 0.8308 0.6790 -0.1046 -0.0941 -0.0195 78  TYR C OH    
5019 N  N     . PRO C 86  ? 0.7880 0.7651 0.5709 -0.0526 -0.0239 0.0258  79  PRO C N     
5020 C  CA    . PRO C 86  ? 0.7644 0.7522 0.5670 -0.0488 -0.0188 0.0351  79  PRO C CA    
5021 C  C     . PRO C 86  ? 0.7603 0.7595 0.5804 -0.0475 -0.0341 0.0437  79  PRO C C     
5022 O  O     . PRO C 86  ? 0.7346 0.7419 0.5769 -0.0422 -0.0306 0.0483  79  PRO C O     
5023 C  CB    . PRO C 86  ? 0.8081 0.7812 0.5806 -0.0480 -0.0088 0.0402  79  PRO C CB    
5024 C  CG    . PRO C 86  ? 0.8645 0.8186 0.5955 -0.0497 -0.0135 0.0345  79  PRO C CG    
5025 C  CD    . PRO C 86  ? 0.8455 0.8000 0.5848 -0.0513 -0.0170 0.0227  79  PRO C CD    
5026 N  N     . LYS C 87  ? 0.7925 0.7925 0.6029 -0.0515 -0.0520 0.0464  80  LYS C N     
5027 C  CA    . LYS C 87  ? 0.7943 0.8116 0.6263 -0.0478 -0.0660 0.0569  80  LYS C CA    
5028 C  C     . LYS C 87  ? 0.7501 0.7928 0.6218 -0.0462 -0.0661 0.0559  80  LYS C C     
5029 O  O     . LYS C 87  ? 0.7298 0.7852 0.6251 -0.0363 -0.0623 0.0612  80  LYS C O     
5030 C  CB    . LYS C 87  ? 0.8506 0.8652 0.6630 -0.0532 -0.0875 0.0632  80  LYS C CB    
5031 C  CG    . LYS C 87  ? 0.8581 0.8963 0.6978 -0.0466 -0.1019 0.0766  80  LYS C CG    
5032 C  CD    . LYS C 87  ? 0.9186 0.9575 0.7422 -0.0520 -0.1262 0.0850  80  LYS C CD    
5033 C  CE    . LYS C 87  ? 0.9271 0.9957 0.7849 -0.0421 -0.1391 0.1002  80  LYS C CE    
5034 N  NZ    . LYS C 87  ? 0.9220 0.9823 0.7821 -0.0255 -0.1277 0.1066  80  LYS C NZ    
5035 N  N     . PHE C 88  ? 0.7436 0.7896 0.6183 -0.0552 -0.0694 0.0491  81  PHE C N     
5036 C  CA    . PHE C 88  ? 0.7055 0.7732 0.6139 -0.0552 -0.0662 0.0486  81  PHE C CA    
5037 C  C     . PHE C 88  ? 0.6622 0.7297 0.5827 -0.0454 -0.0478 0.0446  81  PHE C C     
5038 O  O     . PHE C 88  ? 0.6429 0.7279 0.5884 -0.0369 -0.0445 0.0492  81  PHE C O     
5039 C  CB    . PHE C 88  ? 0.7129 0.7724 0.6134 -0.0675 -0.0703 0.0410  81  PHE C CB    
5040 C  CG    . PHE C 88  ? 0.6860 0.7681 0.6193 -0.0706 -0.0694 0.0435  81  PHE C CG    
5041 C  CD1   . PHE C 88  ? 0.7035 0.8121 0.6616 -0.0782 -0.0839 0.0543  81  PHE C CD1   
5042 C  CD2   . PHE C 88  ? 0.6486 0.7276 0.5887 -0.0661 -0.0539 0.0370  81  PHE C CD2   
5043 C  CE1   . PHE C 88  ? 0.6846 0.8161 0.6729 -0.0816 -0.0803 0.0589  81  PHE C CE1   
5044 C  CE2   . PHE C 88  ? 0.6309 0.7282 0.5962 -0.0688 -0.0519 0.0403  81  PHE C CE2   
5045 C  CZ    . PHE C 88  ? 0.6496 0.7729 0.6384 -0.0769 -0.0639 0.0516  81  PHE C CZ    
5046 N  N     . LEU C 89  ? 0.6553 0.7030 0.5570 -0.0462 -0.0363 0.0364  82  LEU C N     
5047 C  CA    . LEU C 89  ? 0.6212 0.6682 0.5340 -0.0403 -0.0223 0.0326  82  LEU C CA    
5048 C  C     . LEU C 89  ? 0.6227 0.6696 0.5425 -0.0315 -0.0209 0.0390  82  LEU C C     
5049 O  O     . LEU C 89  ? 0.6034 0.6569 0.5399 -0.0244 -0.0168 0.0386  82  LEU C O     
5050 C  CB    . LEU C 89  ? 0.6242 0.6558 0.5191 -0.0430 -0.0117 0.0258  82  LEU C CB    
5051 C  CG    . LEU C 89  ? 0.5967 0.6296 0.5045 -0.0397 -0.0002 0.0233  82  LEU C CG    
5052 C  CD1   . LEU C 89  ? 0.5665 0.6088 0.4919 -0.0386 0.0008  0.0184  82  LEU C CD1   
5053 C  CD2   . LEU C 89  ? 0.6094 0.6349 0.5048 -0.0415 0.0106  0.0209  82  LEU C CD2   
5054 N  N     . GLY C 90  ? 0.6546 0.6897 0.5575 -0.0309 -0.0244 0.0451  83  GLY C N     
5055 C  CA    . GLY C 90  ? 0.6704 0.6981 0.5749 -0.0223 -0.0254 0.0522  83  GLY C CA    
5056 C  C     . GLY C 90  ? 0.6699 0.7146 0.5959 -0.0106 -0.0313 0.0571  83  GLY C C     
5057 O  O     . GLY C 90  ? 0.6697 0.7086 0.6025 -0.0001 -0.0267 0.0571  83  GLY C O     
5058 N  N     . GLU C 91  ? 0.6774 0.7431 0.6137 -0.0123 -0.0416 0.0617  84  GLU C N     
5059 C  CA    . GLU C 91  ? 0.6817 0.7732 0.6448 -0.0009 -0.0457 0.0691  84  GLU C CA    
5060 C  C     . GLU C 91  ? 0.6502 0.7538 0.6318 0.0039  -0.0342 0.0637  84  GLU C C     
5061 O  O     . GLU C 91  ? 0.6587 0.7728 0.6547 0.0198  -0.0296 0.0677  84  GLU C O     
5062 C  CB    . GLU C 91  ? 0.6974 0.8142 0.6727 -0.0093 -0.0603 0.0760  84  GLU C CB    
5063 C  CG    . GLU C 91  ? 0.7426 0.8594 0.7091 -0.0075 -0.0760 0.0865  84  GLU C CG    
5064 C  CD    . GLU C 91  ? 0.7629 0.9137 0.7528 -0.0143 -0.0928 0.0960  84  GLU C CD    
5065 O  OE1   . GLU C 91  ? 0.7583 0.9432 0.7845 -0.0047 -0.0909 0.1041  84  GLU C OE1   
5066 O  OE2   . GLU C 91  ? 0.7885 0.9317 0.7600 -0.0297 -0.1075 0.0954  84  GLU C OE2   
5067 N  N     . MET C 92  ? 0.6219 0.7245 0.6016 -0.0079 -0.0297 0.0555  85  MET C N     
5068 C  CA    . MET C 92  ? 0.5980 0.7118 0.5923 -0.0046 -0.0203 0.0519  85  MET C CA    
5069 C  C     . MET C 92  ? 0.5927 0.6851 0.5765 0.0051  -0.0103 0.0453  85  MET C C     
5070 O  O     . MET C 92  ? 0.5944 0.6928 0.5859 0.0166  -0.0033 0.0450  85  MET C O     
5071 C  CB    . MET C 92  ? 0.5778 0.6919 0.5706 -0.0191 -0.0199 0.0459  85  MET C CB    
5072 C  CG    . MET C 92  ? 0.5931 0.7244 0.5953 -0.0311 -0.0317 0.0520  85  MET C CG    
5073 S  SD    . MET C 92  ? 0.6081 0.7827 0.6474 -0.0249 -0.0348 0.0671  85  MET C SD    
5074 C  CE    . MET C 92  ? 0.6438 0.8246 0.6831 -0.0207 -0.0496 0.0765  85  MET C CE    
5075 N  N     A ILE C 93  ? 0.5948 0.6616 0.5598 0.0001  -0.0099 0.0407  86  ILE C N     
5076 N  N     B ILE C 93  ? 0.5944 0.6617 0.5593 -0.0004 -0.0102 0.0408  86  ILE C N     
5077 C  CA    A ILE C 93  ? 0.5972 0.6423 0.5528 0.0047  -0.0041 0.0350  86  ILE C CA    
5078 C  CA    B ILE C 93  ? 0.5978 0.6423 0.5524 0.0034  -0.0047 0.0354  86  ILE C CA    
5079 C  C     A ILE C 93  ? 0.6336 0.6654 0.5839 0.0202  -0.0053 0.0391  86  ILE C C     
5080 C  C     B ILE C 93  ? 0.6318 0.6662 0.5835 0.0200  -0.0054 0.0393  86  ILE C C     
5081 O  O     A ILE C 93  ? 0.6472 0.6638 0.5908 0.0295  -0.0013 0.0342  86  ILE C O     
5082 O  O     B ILE C 93  ? 0.6415 0.6659 0.5895 0.0299  -0.0006 0.0347  86  ILE C O     
5083 C  CB    A ILE C 93  ? 0.5938 0.6210 0.5367 -0.0075 -0.0031 0.0315  86  ILE C CB    
5084 C  CB    B ILE C 93  ? 0.6013 0.6273 0.5415 -0.0080 -0.0048 0.0339  86  ILE C CB    
5085 C  CG1   A ILE C 93  ? 0.6186 0.6370 0.5495 -0.0116 -0.0075 0.0383  86  ILE C CG1   
5086 C  CG1   B ILE C 93  ? 0.5734 0.6058 0.5162 -0.0186 -0.0002 0.0275  86  ILE C CG1   
5087 C  CG2   A ILE C 93  ? 0.5647 0.6021 0.5120 -0.0172 0.0004  0.0258  86  ILE C CG2   
5088 C  CG2   B ILE C 93  ? 0.6258 0.6255 0.5554 -0.0057 -0.0045 0.0333  86  ILE C CG2   
5089 C  CD1   A ILE C 93  ? 0.6207 0.6291 0.5415 -0.0237 -0.0031 0.0374  86  ILE C CD1   
5090 C  CD1   B ILE C 93  ? 0.5823 0.6069 0.5144 -0.0280 0.0022  0.0285  86  ILE C CD1   
5091 N  N     . ASP C 94  ? 0.6583 0.6910 0.6072 0.0238  -0.0120 0.0476  87  ASP C N     
5092 C  CA    . ASP C 94  ? 0.7013 0.7199 0.6449 0.0417  -0.0138 0.0527  87  ASP C CA    
5093 C  C     . ASP C 94  ? 0.7071 0.7489 0.6679 0.0599  -0.0080 0.0543  87  ASP C C     
5094 O  O     . ASP C 94  ? 0.7397 0.7627 0.6905 0.0772  -0.0030 0.0514  87  ASP C O     
5095 C  CB    . ASP C 94  ? 0.7304 0.7470 0.6692 0.0422  -0.0235 0.0634  87  ASP C CB    
5096 C  CG    . ASP C 94  ? 0.7416 0.7314 0.6583 0.0274  -0.0263 0.0643  87  ASP C CG    
5097 O  OD1   . ASP C 94  ? 0.7360 0.7051 0.6429 0.0191  -0.0212 0.0580  87  ASP C OD1   
5098 O  OD2   . ASP C 94  ? 0.7628 0.7538 0.6720 0.0241  -0.0341 0.0729  87  ASP C OD2   
5099 N  N     . PHE C 95  ? 0.6835 0.7643 0.6682 0.0555  -0.0083 0.0591  88  PHE C N     
5100 C  CA    . PHE C 95  ? 0.6920 0.8038 0.6985 0.0706  -0.0010 0.0642  88  PHE C CA    
5101 C  C     . PHE C 95  ? 0.6832 0.7841 0.6802 0.0749  0.0110  0.0544  88  PHE C C     
5102 O  O     . PHE C 95  ? 0.7137 0.8172 0.7104 0.0956  0.0206  0.0551  88  PHE C O     
5103 C  CB    . PHE C 95  ? 0.6739 0.8289 0.7091 0.0584  -0.0067 0.0734  88  PHE C CB    
5104 C  CG    . PHE C 95  ? 0.6839 0.8801 0.7486 0.0696  0.0016  0.0825  88  PHE C CG    
5105 C  CD1   . PHE C 95  ? 0.7232 0.9456 0.8086 0.0906  0.0026  0.0949  88  PHE C CD1   
5106 C  CD2   . PHE C 95  ? 0.6600 0.8710 0.7330 0.0600  0.0094  0.0804  88  PHE C CD2   
5107 C  CE1   . PHE C 95  ? 0.7381 1.0050 0.8546 0.1017  0.0132  0.1057  88  PHE C CE1   
5108 C  CE2   . PHE C 95  ? 0.6756 0.9272 0.7764 0.0691  0.0192  0.0914  88  PHE C CE2   
5109 C  CZ    . PHE C 95  ? 0.7145 0.9964 0.8384 0.0900  0.0221  0.1043  88  PHE C CZ    
5110 N  N     . CYS C 96  ? 0.6488 0.7369 0.6358 0.0569  0.0108  0.0455  89  CYS C N     
5111 C  CA    . CYS C 96  ? 0.6443 0.7218 0.6205 0.0594  0.0194  0.0369  89  CYS C CA    
5112 C  C     . CYS C 96  ? 0.6843 0.7222 0.6331 0.0730  0.0210  0.0292  89  CYS C C     
5113 O  O     . CYS C 96  ? 0.7142 0.7461 0.6524 0.0895  0.0296  0.0259  89  CYS C O     
5114 C  CB    . CYS C 96  ? 0.6053 0.6780 0.5783 0.0390  0.0168  0.0304  89  CYS C CB    
5115 S  SG    . CYS C 96  ? 0.5775 0.6883 0.5751 0.0275  0.0178  0.0372  89  CYS C SG    
5116 N  N     . LYS C 97  ? 0.6934 0.7014 0.6276 0.0652  0.0126  0.0266  90  LYS C N     
5117 C  CA    . LYS C 97  ? 0.7399 0.7034 0.6456 0.0729  0.0105  0.0193  90  LYS C CA    
5118 C  C     . LYS C 97  ? 0.7975 0.7494 0.6946 0.0995  0.0138  0.0229  90  LYS C C     
5119 O  O     . LYS C 97  ? 0.8444 0.7701 0.7186 0.1162  0.0185  0.0157  90  LYS C O     
5120 C  CB    . LYS C 97  ? 0.7390 0.6771 0.6353 0.0540  0.0009  0.0186  90  LYS C CB    
5121 C  CG    . LYS C 97  ? 0.7814 0.6741 0.6508 0.0506  -0.0047 0.0104  90  LYS C CG    
5122 C  CD    . LYS C 97  ? 0.7660 0.6598 0.6315 0.0442  -0.0037 0.0014  90  LYS C CD    
5123 C  CE    . LYS C 97  ? 0.8280 0.6756 0.6609 0.0492  -0.0098 -0.0081 90  LYS C CE    
5124 N  NZ    . LYS C 97  ? 0.8185 0.6708 0.6454 0.0470  -0.0089 -0.0159 90  LYS C NZ    
5125 N  N     . GLU C 98  ? 0.8028 0.7721 0.7155 0.1055  0.0108  0.0339  91  GLU C N     
5126 C  CA    . GLU C 98  ? 0.8669 0.8186 0.7696 0.1318  0.0117  0.0382  91  GLU C CA    
5127 C  C     . GLU C 98  ? 0.8861 0.8721 0.8056 0.1577  0.0246  0.0431  91  GLU C C     
5128 O  O     . GLU C 98  ? 0.9487 0.9100 0.8478 0.1841  0.0318  0.0393  91  GLU C O     
5129 C  CB    . GLU C 98  ? 0.8755 0.8316 0.7872 0.1300  0.0017  0.0500  91  GLU C CB    
5130 C  CG    . GLU C 98  ? 0.8858 0.8006 0.7750 0.1117  -0.0086 0.0485  91  GLU C CG    
5131 C  CD    . GLU C 98  ? 0.8934 0.8145 0.7883 0.1070  -0.0181 0.0612  91  GLU C CD    
5132 O  OE1   . GLU C 98  ? 0.9128 0.8001 0.7880 0.0936  -0.0248 0.0627  91  GLU C OE1   
5133 O  OE2   . GLU C 98  ? 0.8852 0.8456 0.8039 0.1154  -0.0194 0.0707  91  GLU C OE2   
5134 N  N     . THR C 99  ? 0.8415 0.8832 0.7974 0.1503  0.0274  0.0524  92  THR C N     
5135 C  CA    . THR C 99  ? 0.8595 0.9461 0.8415 0.1711  0.0398  0.0620  92  THR C CA    
5136 C  C     . THR C 99  ? 0.8564 0.9484 0.8308 0.1745  0.0545  0.0552  92  THR C C     
5137 O  O     . THR C 99  ? 0.9068 1.0039 0.8761 0.2021  0.0694  0.0564  92  THR C O     
5138 C  CB    . THR C 99  ? 0.8235 0.9670 0.8488 0.1576  0.0334  0.0770  92  THR C CB    
5139 O  OG1   . THR C 99  ? 0.8397 0.9773 0.8678 0.1582  0.0194  0.0844  92  THR C OG1   
5140 C  CG2   . THR C 99  ? 0.8439 1.0420 0.9037 0.1750  0.0462  0.0903  92  THR C CG2   
5141 N  N     . LEU C 100 ? 0.8033 0.8961 0.7767 0.1483  0.0512  0.0492  93  LEU C N     
5142 C  CA    . LEU C 100 ? 0.8000 0.8988 0.7659 0.1488  0.0632  0.0446  93  LEU C CA    
5143 C  C     . LEU C 100 ? 0.8319 0.8743 0.7518 0.1537  0.0629  0.0282  93  LEU C C     
5144 O  O     . LEU C 100 ? 0.8500 0.8885 0.7533 0.1604  0.0730  0.0233  93  LEU C O     
5145 C  CB    . LEU C 100 ? 0.7370 0.8617 0.7235 0.1197  0.0582  0.0474  93  LEU C CB    
5146 C  CG    . LEU C 100 ? 0.7167 0.8956 0.7460 0.1113  0.0569  0.0635  93  LEU C CG    
5147 C  CD1   . LEU C 100 ? 0.6689 0.8594 0.7082 0.0833  0.0512  0.0636  93  LEU C CD1   
5148 C  CD2   . LEU C 100 ? 0.7561 0.9754 0.8066 0.1331  0.0734  0.0762  93  LEU C CD2   
5149 N  N     . GLN C 101 ? 0.8441 0.8427 0.7424 0.1480  0.0501  0.0207  94  GLN C N     
5150 C  CA    . GLN C 101 ? 0.8853 0.8274 0.7406 0.1491  0.0453  0.0061  94  GLN C CA    
5151 C  C     . GLN C 101 ? 0.8563 0.7996 0.7040 0.1332  0.0454  -0.0007 94  GLN C C     
5152 O  O     . GLN C 101 ? 0.9034 0.8168 0.7173 0.1433  0.0483  -0.0104 94  GLN C O     
5153 C  CB    . GLN C 101 ? 0.9729 0.8849 0.7970 0.1828  0.0548  0.0015  94  GLN C CB    
5154 C  CG    . GLN C 101 ? 1.0088 0.9217 0.8424 0.2028  0.0552  0.0101  94  GLN C CG    
5155 C  CD    . GLN C 101 ? 1.1079 0.9823 0.9053 0.2393  0.0645  0.0042  94  GLN C CD    
5156 O  OE1   . GLN C 101 ? 1.1399 1.0457 0.9514 0.2680  0.0806  0.0124  94  GLN C OE1   
5157 N  NE2   . GLN C 101 ? 1.1656 0.9707 0.9155 0.2388  0.0540  -0.0096 94  GLN C NE2   
5158 N  N     . LEU C 102 ? 0.7867 0.7607 0.6624 0.1092  0.0409  0.0038  95  LEU C N     
5159 C  CA    . LEU C 102 ? 0.7573 0.7312 0.6286 0.0926  0.0381  -0.0014 95  LEU C CA    
5160 C  C     . LEU C 102 ? 0.7816 0.7099 0.6245 0.0829  0.0251  -0.0126 95  LEU C C     
5161 O  O     . LEU C 102 ? 0.7978 0.7018 0.6349 0.0785  0.0161  -0.0138 95  LEU C O     
5162 C  CB    . LEU C 102 ? 0.6898 0.6966 0.5934 0.0707  0.0340  0.0051  95  LEU C CB    
5163 C  CG    . LEU C 102 ? 0.6661 0.7179 0.5985 0.0718  0.0427  0.0164  95  LEU C CG    
5164 C  CD1   . LEU C 102 ? 0.6141 0.6830 0.5661 0.0491  0.0360  0.0191  95  LEU C CD1   
5165 C  CD2   . LEU C 102 ? 0.6895 0.7528 0.6150 0.0835  0.0555  0.0182  95  LEU C CD2   
5166 N  N     . GLU C 103 ? 0.7870 0.7056 0.6140 0.0773  0.0226  -0.0191 96  GLU C N     
5167 C  CA    . GLU C 103 ? 0.8200 0.6979 0.6214 0.0669  0.0077  -0.0287 96  GLU C CA    
5168 C  C     . GLU C 103 ? 0.7712 0.6606 0.5984 0.0420  -0.0030 -0.0251 96  GLU C C     
5169 O  O     . GLU C 103 ? 0.7985 0.6597 0.6164 0.0320  -0.0148 -0.0277 96  GLU C O     
5170 C  CB    . GLU C 103 ? 0.8489 0.7136 0.6241 0.0689  0.0059  -0.0357 96  GLU C CB    
5171 C  CG    . GLU C 103 ? 0.9168 0.7623 0.6561 0.0955  0.0176  -0.0404 96  GLU C CG    
5172 C  CD    . GLU C 103 ? 0.9627 0.7853 0.6650 0.0977  0.0137  -0.0484 96  GLU C CD    
5173 O  OE1   . GLU C 103 ? 0.9480 0.7641 0.6517 0.0773  -0.0027 -0.0512 96  GLU C OE1   
5174 O  OE2   . GLU C 103 ? 1.0204 0.8322 0.6913 0.1210  0.0272  -0.0512 96  GLU C OE2   
5175 N  N     . SER C 104 ? 0.7085 0.6374 0.5662 0.0328  0.0019  -0.0186 97  SER C N     
5176 C  CA    . SER C 104 ? 0.6683 0.6107 0.5483 0.0129  -0.0047 -0.0155 97  SER C CA    
5177 C  C     . SER C 104 ? 0.6180 0.5939 0.5252 0.0092  0.0025  -0.0079 97  SER C C     
5178 O  O     . SER C 104 ? 0.5962 0.5945 0.5127 0.0134  0.0099  -0.0049 97  SER C O     
5179 C  CB    . SER C 104 ? 0.6620 0.6071 0.5421 0.0037  -0.0112 -0.0186 97  SER C CB    
5180 O  OG    . SER C 104 ? 0.6275 0.5908 0.5321 -0.0114 -0.0145 -0.0144 97  SER C OG    
5181 N  N     . VAL C 105 ? 0.6085 0.5848 0.5254 -0.0001 -0.0004 -0.0042 98  VAL C N     
5182 C  CA    . VAL C 105 ? 0.5743 0.5744 0.5091 -0.0049 0.0038  0.0016  98  VAL C CA    
5183 C  C     . VAL C 105 ? 0.5589 0.5643 0.5035 -0.0192 0.0016  0.0026  98  VAL C C     
5184 O  O     . VAL C 105 ? 0.5785 0.5711 0.5207 -0.0266 -0.0026 0.0041  98  VAL C O     
5185 C  CB    . VAL C 105 ? 0.5890 0.5862 0.5222 0.0012  0.0044  0.0069  98  VAL C CB    
5186 C  CG1   . VAL C 105 ? 0.5639 0.5815 0.5097 -0.0054 0.0057  0.0124  98  VAL C CG1   
5187 C  CG2   . VAL C 105 ? 0.6107 0.6084 0.5387 0.0188  0.0085  0.0076  98  VAL C CG2   
5188 N  N     . SER C 106 ? 0.5312 0.5549 0.4866 -0.0225 0.0051  0.0025  99  SER C N     
5189 C  CA    . SER C 106 ? 0.5229 0.5550 0.4885 -0.0313 0.0058  0.0036  99  SER C CA    
5190 C  C     . SER C 106 ? 0.5083 0.5519 0.4767 -0.0317 0.0114  0.0053  99  SER C C     
5191 O  O     . SER C 106 ? 0.5014 0.5483 0.4671 -0.0279 0.0119  0.0055  99  SER C O     
5192 C  CB    . SER C 106 ? 0.5195 0.5566 0.4914 -0.0326 0.0029  0.0008  99  SER C CB    
5193 O  OG    . SER C 106 ? 0.5061 0.5484 0.4760 -0.0265 0.0050  -0.0011 99  SER C OG    
5194 N  N     . ILE C 107 ? 0.5121 0.5616 0.4851 -0.0366 0.0155  0.0073  100 ILE C N     
5195 C  CA    . ILE C 107 ? 0.5122 0.5660 0.4802 -0.0357 0.0209  0.0071  100 ILE C CA    
5196 C  C     . ILE C 107 ? 0.5153 0.5786 0.4919 -0.0345 0.0267  0.0061  100 ILE C C     
5197 O  O     . ILE C 107 ? 0.5215 0.5934 0.5111 -0.0377 0.0276  0.0095  100 ILE C O     
5198 C  CB    . ILE C 107 ? 0.5307 0.5799 0.4884 -0.0386 0.0230  0.0116  100 ILE C CB    
5199 C  CG1   . ILE C 107 ? 0.5349 0.5756 0.4873 -0.0375 0.0165  0.0144  100 ILE C CG1   
5200 C  CG2   . ILE C 107 ? 0.5443 0.5915 0.4878 -0.0374 0.0269  0.0101  100 ILE C CG2   
5201 C  CD1   . ILE C 107 ? 0.5600 0.5929 0.5030 -0.0410 0.0172  0.0208  100 ILE C CD1   
5202 N  N     . VAL C 108 ? 0.5183 0.5795 0.4883 -0.0297 0.0298  0.0024  101 VAL C N     
5203 C  CA    . VAL C 108 ? 0.5323 0.6006 0.5075 -0.0240 0.0374  0.0017  101 VAL C CA    
5204 C  C     . VAL C 108 ? 0.5611 0.6207 0.5164 -0.0204 0.0454  0.0000  101 VAL C C     
5205 O  O     . VAL C 108 ? 0.5697 0.6130 0.5058 -0.0211 0.0410  -0.0039 101 VAL C O     
5206 C  CB    . VAL C 108 ? 0.5272 0.5933 0.5064 -0.0181 0.0342  -0.0016 101 VAL C CB    
5207 C  CG1   . VAL C 108 ? 0.5283 0.5772 0.4909 -0.0190 0.0295  -0.0054 101 VAL C CG1   
5208 C  CG2   . VAL C 108 ? 0.5493 0.6230 0.5351 -0.0081 0.0424  -0.0016 101 VAL C CG2   
5209 N  N     . THR C 109 ? 0.5839 0.6551 0.5432 -0.0168 0.0569  0.0038  102 THR C N     
5210 C  CA    . THR C 109 ? 0.6230 0.6847 0.5577 -0.0118 0.0669  0.0027  102 THR C CA    
5211 C  C     . THR C 109 ? 0.6550 0.7309 0.5963 0.0005  0.0828  0.0045  102 THR C C     
5212 O  O     . THR C 109 ? 0.6452 0.7475 0.6177 0.0004  0.0862  0.0113  102 THR C O     
5213 C  CB    . THR C 109 ? 0.6324 0.6961 0.5606 -0.0201 0.0688  0.0099  102 THR C CB    
5214 O  OG1   . THR C 109 ? 0.6796 0.7326 0.5784 -0.0141 0.0793  0.0089  102 THR C OG1   
5215 C  CG2   . THR C 109 ? 0.6271 0.7138 0.5827 -0.0267 0.0731  0.0202  102 THR C CG2   
5216 N  N     . ASN C 110 ? 0.7019 0.7609 0.6125 0.0108  0.0925  -0.0005 103 ASN C N     
5217 C  CA    . ASN C 110 ? 0.7473 0.8210 0.6588 0.0255  0.1126  0.0027  103 ASN C CA    
5218 C  C     . ASN C 110 ? 0.7608 0.8588 0.6826 0.0191  0.1246  0.0154  103 ASN C C     
5219 O  O     . ASN C 110 ? 0.7906 0.9162 0.7298 0.0281  0.1423  0.0235  103 ASN C O     
5220 C  CB    . ASN C 110 ? 0.8083 0.8491 0.6749 0.0407  0.1200  -0.0078 103 ASN C CB    
5221 C  CG    . ASN C 110 ? 0.8365 0.8488 0.6606 0.0335  0.1153  -0.0117 103 ASN C CG    
5222 O  OD1   . ASN C 110 ? 0.8411 0.8650 0.6638 0.0263  0.1206  -0.0032 103 ASN C OD1   
5223 N  ND2   . ASN C 110 ? 0.8636 0.8371 0.6520 0.0346  0.1040  -0.0233 103 ASN C ND2   
5224 N  N     . GLY C 111 ? 0.7464 0.8354 0.6585 0.0042  0.1160  0.0188  104 GLY C N     
5225 C  CA    . GLY C 111 ? 0.7553 0.8655 0.6824 -0.0059 0.1234  0.0331  104 GLY C CA    
5226 C  C     . GLY C 111 ? 0.8163 0.9191 0.7092 -0.0006 0.1399  0.0373  104 GLY C C     
5227 O  O     . GLY C 111 ? 0.8328 0.9465 0.7297 -0.0107 0.1457  0.0504  104 GLY C O     
5228 N  N     . SER C 112 ? 0.8583 0.9380 0.7132 0.0148  0.1467  0.0264  105 SER C N     
5229 C  CA    . SER C 112 ? 0.9308 1.0011 0.7465 0.0237  0.1647  0.0292  105 SER C CA    
5230 C  C     . SER C 112 ? 0.9409 0.9878 0.7250 0.0106  0.1534  0.0318  105 SER C C     
5231 O  O     . SER C 112 ? 0.9898 1.0399 0.7549 0.0101  0.1672  0.0422  105 SER C O     
5232 C  CB    . SER C 112 ? 0.9869 1.0301 0.7625 0.0448  0.1731  0.0149  105 SER C CB    
5233 O  OG    . SER C 112 ? 0.9778 0.9809 0.7237 0.0406  0.1509  0.0005  105 SER C OG    
5234 N  N     . LEU C 113 ? 0.8991 0.9254 0.6796 0.0008  0.1289  0.0243  106 LEU C N     
5235 C  CA    . LEU C 113 ? 0.9136 0.9165 0.6635 -0.0084 0.1147  0.0255  106 LEU C CA    
5236 C  C     . LEU C 113 ? 0.8660 0.8808 0.6460 -0.0235 0.1025  0.0360  106 LEU C C     
5237 O  O     . LEU C 113 ? 0.8710 0.8691 0.6332 -0.0300 0.0879  0.0377  106 LEU C O     
5238 C  CB    . LEU C 113 ? 0.9141 0.8871 0.6389 -0.0078 0.0952  0.0111  106 LEU C CB    
5239 C  CG    . LEU C 113 ? 0.9791 0.9248 0.6607 0.0060  0.1021  -0.0015 106 LEU C CG    
5240 C  CD1   . LEU C 113 ? 0.9754 0.8933 0.6423 0.0014  0.0793  -0.0140 106 LEU C CD1   
5241 C  CD2   . LEU C 113 ? 1.0622 0.9885 0.6915 0.0112  0.1122  0.0009  106 LEU C CD2   
5242 N  N     A VAL C 114 ? 0.8289 0.8700 0.6521 -0.0286 0.1070  0.0432  107 VAL C N     
5243 N  N     B VAL C 114 ? 0.8290 0.8704 0.6523 -0.0283 0.1073  0.0429  107 VAL C N     
5244 C  CA    A VAL C 114 ? 0.8002 0.8440 0.6443 -0.0419 0.0954  0.0521  107 VAL C CA    
5245 C  CA    B VAL C 114 ? 0.8015 0.8485 0.6484 -0.0417 0.0976  0.0529  107 VAL C CA    
5246 C  C     A VAL C 114 ? 0.8472 0.8940 0.6823 -0.0490 0.1063  0.0684  107 VAL C C     
5247 C  C     B VAL C 114 ? 0.8532 0.8978 0.6826 -0.0479 0.1071  0.0679  107 VAL C C     
5248 O  O     A VAL C 114 ? 0.8804 0.9466 0.7210 -0.0469 0.1261  0.0764  107 VAL C O     
5249 O  O     B VAL C 114 ? 0.8977 0.9545 0.7186 -0.0431 0.1272  0.0740  107 VAL C O     
5250 C  CB    A VAL C 114 ? 0.7499 0.8121 0.6376 -0.0466 0.0901  0.0516  107 VAL C CB    
5251 C  CB    B VAL C 114 ? 0.7638 0.8358 0.6563 -0.0463 0.0986  0.0556  107 VAL C CB    
5252 C  CG1   A VAL C 114 ? 0.7638 0.8557 0.6792 -0.0477 0.1062  0.0605  107 VAL C CG1   
5253 C  CG1   B VAL C 114 ? 0.7482 0.8174 0.6589 -0.0603 0.0867  0.0641  107 VAL C CG1   
5254 C  CG2   A VAL C 114 ? 0.7294 0.7821 0.6278 -0.0574 0.0749  0.0565  107 VAL C CG2   
5255 C  CG2   B VAL C 114 ? 0.7224 0.7957 0.6276 -0.0389 0.0912  0.0423  107 VAL C CG2   
5256 N  N     . LYS C 115 ? 0.8540 0.8827 0.6770 -0.0568 0.0936  0.0746  108 LYS C N     
5257 C  CA    . LYS C 115 ? 0.9044 0.9278 0.7135 -0.0651 0.1002  0.0915  108 LYS C CA    
5258 C  C     . LYS C 115 ? 0.8885 0.9056 0.7203 -0.0777 0.0875  0.1000  108 LYS C C     
5259 O  O     . LYS C 115 ? 0.8473 0.8551 0.6902 -0.0763 0.0709  0.0915  108 LYS C O     
5260 C  CB    . LYS C 115 ? 0.9488 0.9460 0.7106 -0.0611 0.0941  0.0922  108 LYS C CB    
5261 C  CG    . LYS C 115 ? 0.9889 0.9799 0.7132 -0.0493 0.1043  0.0835  108 LYS C CG    
5262 C  CD    . LYS C 115 ? 1.0508 1.0149 0.7241 -0.0481 0.0978  0.0878  108 LYS C CD    
5263 C  CE    . LYS C 115 ? 1.0983 1.0458 0.7261 -0.0367 0.1015  0.0754  108 LYS C CE    
5264 N  NZ    . LYS C 115 ? 1.1668 1.0863 0.7418 -0.0370 0.0919  0.0801  108 LYS C NZ    
5265 N  N     . GLU C 116 ? 0.9322 0.9511 0.7665 -0.0896 0.0957  0.1177  109 GLU C N     
5266 C  CA    . GLU C 116 ? 0.9329 0.9399 0.7858 -0.1032 0.0837  0.1263  109 GLU C CA    
5267 C  C     . GLU C 116 ? 0.9294 0.9034 0.7621 -0.0983 0.0639  0.1223  109 GLU C C     
5268 O  O     . GLU C 116 ? 0.9062 0.8677 0.7539 -0.0998 0.0498  0.1177  109 GLU C O     
5269 C  CB    . GLU C 116 ? 0.9942 1.0064 0.8497 -0.1192 0.0959  0.1485  109 GLU C CB    
5270 C  CG    . GLU C 116 ? 1.0057 1.0021 0.8812 -0.1365 0.0821  0.1572  109 GLU C CG    
5271 C  CD    . GLU C 116 ? 1.0690 1.0724 0.9557 -0.1579 0.0915  0.1811  109 GLU C CD    
5272 O  OE1   . GLU C 116 ? 1.1031 1.1331 0.9876 -0.1587 0.1136  0.1930  109 GLU C OE1   
5273 O  OE2   . GLU C 116 ? 1.0900 1.0722 0.9876 -0.1738 0.0771  0.1879  109 GLU C OE2   
5274 N  N     . GLN C 117 ? 0.9599 0.9201 0.7570 -0.0908 0.0630  0.1243  110 GLN C N     
5275 C  CA    . GLN C 117 ? 0.9669 0.9012 0.7466 -0.0846 0.0446  0.1238  110 GLN C CA    
5276 C  C     . GLN C 117 ? 0.9059 0.8449 0.7051 -0.0749 0.0318  0.1074  110 GLN C C     
5277 O  O     . GLN C 117 ? 0.9038 0.8265 0.7059 -0.0703 0.0178  0.1074  110 GLN C O     
5278 C  CB    . GLN C 117 ? 1.0123 0.9361 0.7511 -0.0784 0.0441  0.1279  110 GLN C CB    
5279 C  CG    . GLN C 117 ? 0.9990 0.9368 0.7250 -0.0704 0.0502  0.1148  110 GLN C CG    
5280 C  CD    . GLN C 117 ? 1.0566 0.9777 0.7359 -0.0656 0.0456  0.1182  110 GLN C CD    
5281 O  OE1   . GLN C 117 ? 1.1193 1.0273 0.7710 -0.0696 0.0518  0.1331  110 GLN C OE1   
5282 N  NE2   . GLN C 117 ? 1.0433 0.9629 0.7116 -0.0584 0.0329  0.1055  110 GLN C NE2   
5283 N  N     . PHE C 118 ? 0.8641 0.8245 0.6752 -0.0706 0.0375  0.0945  111 PHE C N     
5284 C  CA    . PHE C 118 ? 0.8120 0.7781 0.6412 -0.0631 0.0270  0.0813  111 PHE C CA    
5285 C  C     . PHE C 118 ? 0.7907 0.7539 0.6453 -0.0667 0.0233  0.0802  111 PHE C C     
5286 O  O     . PHE C 118 ? 0.7761 0.7305 0.6361 -0.0595 0.0122  0.0758  111 PHE C O     
5287 C  CB    . PHE C 118 ? 0.7819 0.7657 0.6147 -0.0587 0.0329  0.0690  111 PHE C CB    
5288 C  CG    . PHE C 118 ? 0.7368 0.7263 0.5853 -0.0523 0.0221  0.0581  111 PHE C CG    
5289 C  CD1   . PHE C 118 ? 0.6987 0.6958 0.5735 -0.0523 0.0217  0.0527  111 PHE C CD1   
5290 C  CD2   . PHE C 118 ? 0.7407 0.7281 0.5770 -0.0475 0.0111  0.0550  111 PHE C CD2   
5291 C  CE1   . PHE C 118 ? 0.6646 0.6678 0.5514 -0.0461 0.0142  0.0445  111 PHE C CE1   
5292 C  CE2   . PHE C 118 ? 0.7049 0.7021 0.5590 -0.0434 0.0028  0.0478  111 PHE C CE2   
5293 C  CZ    . PHE C 118 ? 0.6669 0.6720 0.5454 -0.0420 0.0058  0.0429  111 PHE C CZ    
5294 N  N     . LEU C 119 ? 0.7989 0.7687 0.6676 -0.0777 0.0318  0.0853  112 LEU C N     
5295 C  CA    . LEU C 119 ? 0.7876 0.7517 0.6769 -0.0833 0.0252  0.0830  112 LEU C CA    
5296 C  C     . LEU C 119 ? 0.8309 0.7610 0.7081 -0.0865 0.0142  0.0909  112 LEU C C     
5297 O  O     . LEU C 119 ? 0.8271 0.7398 0.7075 -0.0822 0.0037  0.0843  112 LEU C O     
5298 C  CB    . LEU C 119 ? 0.7885 0.7752 0.7001 -0.0954 0.0354  0.0874  112 LEU C CB    
5299 C  CG    . LEU C 119 ? 0.7547 0.7714 0.6768 -0.0883 0.0467  0.0794  112 LEU C CG    
5300 C  CD1   . LEU C 119 ? 0.7630 0.8067 0.7122 -0.0980 0.0568  0.0863  112 LEU C CD1   
5301 C  CD2   . LEU C 119 ? 0.7057 0.7238 0.6341 -0.0776 0.0385  0.0641  112 LEU C CD2   
5302 N  N     . GLN C 120 ? 0.8801 0.7965 0.7378 -0.0915 0.0166  0.1047  113 GLN C N     
5303 C  CA    . GLN C 120 ? 0.9322 0.8110 0.7730 -0.0926 0.0058  0.1138  113 GLN C CA    
5304 C  C     . GLN C 120 ? 0.9219 0.7871 0.7530 -0.0727 -0.0055 0.1060  113 GLN C C     
5305 O  O     . GLN C 120 ? 0.9433 0.7807 0.7711 -0.0670 -0.0154 0.1037  113 GLN C O     
5306 C  CB    . GLN C 120 ? 0.9885 0.8591 0.8084 -0.1013 0.0123  0.1316  113 GLN C CB    
5307 C  CG    . GLN C 120 ? 1.0545 0.8817 0.8532 -0.1030 0.0011  0.1438  113 GLN C CG    
5308 C  CD    . GLN C 120 ? 1.1168 0.9376 0.8993 -0.1183 0.0099  0.1644  113 GLN C CD    
5309 O  OE1   . GLN C 120 ? 1.1178 0.9607 0.8899 -0.1176 0.0224  0.1688  113 GLN C OE1   
5310 N  NE2   . GLN C 120 ? 1.1774 0.9658 0.9554 -0.1332 0.0040  0.1775  113 GLN C NE2   
5311 N  N     . LYS C 121 ? 0.8979 0.7822 0.7238 -0.0621 -0.0043 0.1025  114 LYS C N     
5312 C  CA    . LYS C 121 ? 0.8941 0.7747 0.7165 -0.0444 -0.0150 0.0991  114 LYS C CA    
5313 C  C     . LYS C 121 ? 0.8511 0.7407 0.6938 -0.0348 -0.0172 0.0855  114 LYS C C     
5314 O  O     . LYS C 121 ? 0.8664 0.7431 0.7082 -0.0200 -0.0246 0.0845  114 LYS C O     
5315 C  CB    . LYS C 121 ? 0.8874 0.7875 0.7001 -0.0402 -0.0158 0.0999  114 LYS C CB    
5316 C  CG    . LYS C 121 ? 0.8841 0.7913 0.7003 -0.0242 -0.0282 0.0987  114 LYS C CG    
5317 C  CD    . LYS C 121 ? 0.9213 0.8291 0.7157 -0.0228 -0.0361 0.1078  114 LYS C CD    
5318 C  CE    . LYS C 121 ? 0.9028 0.8357 0.7073 -0.0152 -0.0467 0.1038  114 LYS C CE    
5319 N  NZ    . LYS C 121 ? 0.8792 0.8250 0.7119 -0.0013 -0.0515 0.1005  114 LYS C NZ    
5320 N  N     . HIS C 122 ? 0.8051 0.7162 0.6645 -0.0415 -0.0099 0.0760  115 HIS C N     
5321 C  CA    . HIS C 122 ? 0.7641 0.6883 0.6397 -0.0320 -0.0109 0.0640  115 HIS C CA    
5322 C  C     . HIS C 122 ? 0.7569 0.6730 0.6412 -0.0383 -0.0099 0.0572  115 HIS C C     
5323 O  O     . HIS C 122 ? 0.7357 0.6558 0.6273 -0.0295 -0.0111 0.0480  115 HIS C O     
5324 C  CB    . HIS C 122 ? 0.7200 0.6755 0.6052 -0.0320 -0.0066 0.0581  115 HIS C CB    
5325 C  CG    . HIS C 122 ? 0.7311 0.6943 0.6082 -0.0260 -0.0123 0.0628  115 HIS C CG    
5326 N  ND1   . HIS C 122 ? 0.7316 0.7028 0.6163 -0.0130 -0.0201 0.0637  115 HIS C ND1   
5327 C  CD2   . HIS C 122 ? 0.7476 0.7138 0.6093 -0.0319 -0.0118 0.0672  115 HIS C CD2   
5328 C  CE1   . HIS C 122 ? 0.7489 0.7279 0.6250 -0.0132 -0.0271 0.0696  115 HIS C CE1   
5329 N  NE2   . HIS C 122 ? 0.7602 0.7331 0.6188 -0.0245 -0.0225 0.0707  115 HIS C NE2   
5330 N  N     . GLY C 123 ? 0.7816 0.6870 0.6647 -0.0541 -0.0084 0.0631  116 GLY C N     
5331 C  CA    . GLY C 123 ? 0.7881 0.6843 0.6793 -0.0639 -0.0116 0.0590  116 GLY C CA    
5332 C  C     . GLY C 123 ? 0.8060 0.6752 0.6878 -0.0529 -0.0207 0.0498  116 GLY C C     
5333 O  O     . GLY C 123 ? 0.7900 0.6636 0.6791 -0.0548 -0.0225 0.0411  116 GLY C O     
5334 N  N     . ARG C 124 ? 0.8465 0.6864 0.7096 -0.0395 -0.0260 0.0516  117 ARG C N     
5335 C  CA    . ARG C 124 ? 0.8774 0.6877 0.7258 -0.0251 -0.0322 0.0423  117 ARG C CA    
5336 C  C     . ARG C 124 ? 0.8287 0.6674 0.6884 -0.0110 -0.0263 0.0318  117 ARG C C     
5337 O  O     . ARG C 124 ? 0.8470 0.6687 0.6958 -0.0022 -0.0286 0.0223  117 ARG C O     
5338 C  CB    . ARG C 124 ? 0.9342 0.7112 0.7615 -0.0080 -0.0368 0.0471  117 ARG C CB    
5339 C  CG    . ARG C 124 ? 0.9092 0.7145 0.7454 0.0098  -0.0319 0.0515  117 ARG C CG    
5340 C  CD    . ARG C 124 ? 0.9731 0.7471 0.7908 0.0244  -0.0379 0.0604  117 ARG C CD    
5341 N  NE    . ARG C 124 ? 0.9575 0.7613 0.7871 0.0442  -0.0358 0.0648  117 ARG C NE    
5342 C  CZ    . ARG C 124 ? 0.9173 0.7586 0.7619 0.0377  -0.0345 0.0711  117 ARG C CZ    
5343 N  NH1   . ARG C 124 ? 0.8950 0.7446 0.7399 0.0155  -0.0326 0.0742  117 ARG C NH1   
5344 N  NH2   . ARG C 124 ? 0.9090 0.7789 0.7673 0.0539  -0.0356 0.0753  117 ARG C NH2   
5345 N  N     . ASN C 125 ? 0.7759 0.6546 0.6536 -0.0094 -0.0190 0.0340  118 ASN C N     
5346 C  CA    . ASN C 125 ? 0.7377 0.6430 0.6266 0.0027  -0.0136 0.0274  118 ASN C CA    
5347 C  C     . ASN C 125 ? 0.6893 0.6203 0.5936 -0.0095 -0.0097 0.0227  118 ASN C C     
5348 O  O     . ASN C 125 ? 0.6581 0.6114 0.5720 -0.0027 -0.0053 0.0189  118 ASN C O     
5349 C  CB    . ASN C 125 ? 0.7238 0.6536 0.6221 0.0137  -0.0114 0.0336  118 ASN C CB    
5350 C  CG    . ASN C 125 ? 0.7739 0.6839 0.6609 0.0323  -0.0148 0.0385  118 ASN C CG    
5351 O  OD1   . ASN C 125 ? 0.8105 0.6964 0.6844 0.0463  -0.0146 0.0332  118 ASN C OD1   
5352 N  ND2   . ASN C 125 ? 0.7831 0.7015 0.6725 0.0343  -0.0182 0.0484  118 ASN C ND2   
5353 N  N     . ILE C 126 ? 0.6878 0.6180 0.5962 -0.0270 -0.0106 0.0251  119 ILE C N     
5354 C  CA    . ILE C 126 ? 0.6503 0.6050 0.5746 -0.0362 -0.0068 0.0219  119 ILE C CA    
5355 C  C     . ILE C 126 ? 0.6698 0.6101 0.5932 -0.0442 -0.0136 0.0177  119 ILE C C     
5356 O  O     . ILE C 126 ? 0.6968 0.6278 0.6225 -0.0587 -0.0179 0.0232  119 ILE C O     
5357 C  CB    . ILE C 126 ? 0.6404 0.6122 0.5734 -0.0477 -0.0009 0.0290  119 ILE C CB    
5358 C  CG1   . ILE C 126 ? 0.6376 0.6161 0.5639 -0.0424 0.0023  0.0336  119 ILE C CG1   
5359 C  CG2   . ILE C 126 ? 0.6085 0.6052 0.5578 -0.0523 0.0042  0.0255  119 ILE C CG2   
5360 C  CD1   . ILE C 126 ? 0.6462 0.6336 0.5711 -0.0519 0.0090  0.0405  119 ILE C CD1   
5361 N  N     . ASP C 127 ? 0.6595 0.6011 0.5806 -0.0368 -0.0150 0.0095  120 ASP C N     
5362 C  CA    . ASP C 127 ? 0.6866 0.6121 0.6026 -0.0445 -0.0247 0.0050  120 ASP C CA    
5363 C  C     . ASP C 127 ? 0.6659 0.6177 0.6061 -0.0598 -0.0248 0.0095  120 ASP C C     
5364 O  O     . ASP C 127 ? 0.6985 0.6415 0.6431 -0.0747 -0.0338 0.0132  120 ASP C O     
5365 C  CB    . ASP C 127 ? 0.6946 0.6097 0.5945 -0.0308 -0.0261 -0.0043 120 ASP C CB    
5366 C  CG    . ASP C 127 ? 0.7297 0.6192 0.6064 -0.0132 -0.0242 -0.0072 120 ASP C CG    
5367 O  OD1   . ASP C 127 ? 0.7830 0.6365 0.6414 -0.0149 -0.0321 -0.0072 120 ASP C OD1   
5368 O  OD2   . ASP C 127 ? 0.7103 0.6158 0.5880 0.0024  -0.0148 -0.0082 120 ASP C OD2   
5369 N  N     . ILE C 128 ? 0.6204 0.6036 0.5765 -0.0561 -0.0151 0.0101  121 ILE C N     
5370 C  CA    . ILE C 128 ? 0.6045 0.6145 0.5833 -0.0642 -0.0127 0.0136  121 ILE C CA    
5371 C  C     . ILE C 128 ? 0.5782 0.6105 0.5661 -0.0612 0.0004  0.0175  121 ILE C C     
5372 O  O     . ILE C 128 ? 0.5574 0.5905 0.5367 -0.0516 0.0053  0.0139  121 ILE C O     
5373 C  CB    . ILE C 128 ? 0.5907 0.6081 0.5721 -0.0588 -0.0167 0.0073  121 ILE C CB    
5374 C  CG1   . ILE C 128 ? 0.6271 0.6190 0.5922 -0.0608 -0.0307 0.0020  121 ILE C CG1   
5375 C  CG2   . ILE C 128 ? 0.5778 0.6249 0.5846 -0.0631 -0.0136 0.0118  121 ILE C CG2   
5376 C  CD1   . ILE C 128 ? 0.6199 0.6125 0.5765 -0.0516 -0.0333 -0.0043 121 ILE C CD1   
5377 N  N     . LEU C 129 ? 0.5856 0.6374 0.5909 -0.0692 0.0058  0.0248  122 LEU C N     
5378 C  CA    . LEU C 129 ? 0.5744 0.6444 0.5832 -0.0643 0.0194  0.0273  122 LEU C CA    
5379 C  C     . LEU C 129 ? 0.5708 0.6672 0.6021 -0.0626 0.0239  0.0289  122 LEU C C     
5380 O  O     . LEU C 129 ? 0.5898 0.7011 0.6423 -0.0721 0.0206  0.0360  122 LEU C O     
5381 C  CB    . LEU C 129 ? 0.6013 0.6695 0.6055 -0.0715 0.0259  0.0368  122 LEU C CB    
5382 C  CG    . LEU C 129 ? 0.6065 0.6883 0.6056 -0.0660 0.0410  0.0396  122 LEU C CG    
5383 C  CD1   . LEU C 129 ? 0.5876 0.6602 0.5673 -0.0544 0.0421  0.0304  122 LEU C CD1   
5384 C  CD2   . LEU C 129 ? 0.6409 0.7165 0.6294 -0.0735 0.0465  0.0502  122 LEU C CD2   
5385 N  N     . ALA C 130 ? 0.5522 0.6529 0.5792 -0.0507 0.0293  0.0226  123 ALA C N     
5386 C  CA    . ALA C 130 ? 0.5539 0.6756 0.5986 -0.0441 0.0340  0.0234  123 ALA C CA    
5387 C  C     . ALA C 130 ? 0.5698 0.7000 0.6094 -0.0359 0.0502  0.0251  123 ALA C C     
5388 O  O     . ALA C 130 ? 0.5687 0.6820 0.5841 -0.0299 0.0542  0.0192  123 ALA C O     
5389 C  CB    . ALA C 130 ? 0.5359 0.6497 0.5750 -0.0355 0.0279  0.0157  123 ALA C CB    
5390 N  N     . VAL C 131 ? 0.5924 0.7499 0.6548 -0.0349 0.0594  0.0335  124 VAL C N     
5391 C  CA    . VAL C 131 ? 0.6193 0.7849 0.6741 -0.0230 0.0776  0.0348  124 VAL C CA    
5392 C  C     . VAL C 131 ? 0.6277 0.8088 0.6978 -0.0078 0.0819  0.0331  124 VAL C C     
5393 O  O     . VAL C 131 ? 0.6253 0.8302 0.7271 -0.0105 0.0750  0.0392  124 VAL C O     
5394 C  CB    . VAL C 131 ? 0.6513 0.8388 0.7187 -0.0306 0.0899  0.0483  124 VAL C CB    
5395 C  CG1   . VAL C 131 ? 0.6880 0.8753 0.7340 -0.0166 0.1104  0.0480  124 VAL C CG1   
5396 C  CG2   . VAL C 131 ? 0.6470 0.8179 0.7051 -0.0481 0.0807  0.0523  124 VAL C CG2   
5397 N  N     . SER C 132 ? 0.6428 0.8051 0.6868 0.0074  0.0900  0.0245  125 SER C N     
5398 C  CA    . SER C 132 ? 0.6627 0.8292 0.7118 0.0259  0.0953  0.0215  125 SER C CA    
5399 C  C     . SER C 132 ? 0.7113 0.9042 0.7713 0.0409  0.1171  0.0287  125 SER C C     
5400 O  O     . SER C 132 ? 0.7486 0.9232 0.7764 0.0522  0.1311  0.0235  125 SER C O     
5401 C  CB    . SER C 132 ? 0.6686 0.7954 0.6804 0.0341  0.0921  0.0087  125 SER C CB    
5402 O  OG    . SER C 132 ? 0.6291 0.7384 0.6364 0.0228  0.0742  0.0043  125 SER C OG    
5403 N  N     . CYS C 133 ? 0.7182 0.9529 0.8221 0.0428  0.1190  0.0403  126 CYS C N     
5404 C  CA    . CYS C 133 ? 0.7682 1.0389 0.8931 0.0597  0.1409  0.0502  126 CYS C CA    
5405 C  C     . CYS C 133 ? 0.7786 1.0742 0.9369 0.0751  0.1371  0.0541  126 CYS C C     
5406 O  O     . CYS C 133 ? 0.7555 1.0766 0.9506 0.0621  0.1209  0.0622  126 CYS C O     
5407 C  CB    . CYS C 133 ? 0.7756 1.0846 0.9308 0.0423  0.1475  0.0669  126 CYS C CB    
5408 S  SG    . CYS C 133 ? 0.8452 1.2083 1.0305 0.0615  0.1794  0.0836  126 CYS C SG    
5409 N  N     . ASP C 134 ? 0.8216 1.1056 0.9634 0.1034  0.1505  0.0480  127 ASP C N     
5410 C  CA    . ASP C 134 ? 0.8368 1.1344 1.0025 0.1215  0.1452  0.0502  127 ASP C CA    
5411 C  C     . ASP C 134 ? 0.8813 1.2415 1.0980 0.1373  0.1617  0.0677  127 ASP C C     
5412 O  O     . ASP C 134 ? 0.8910 1.2762 1.1415 0.1483  0.1534  0.0744  127 ASP C O     
5413 C  CB    . ASP C 134 ? 0.8703 1.1176 0.9913 0.1453  0.1486  0.0352  127 ASP C CB    
5414 C  CG    . ASP C 134 ? 0.8447 1.0333 0.9138 0.1316  0.1374  0.0197  127 ASP C CG    
5415 O  OD1   . ASP C 134 ? 0.7928 0.9682 0.8629 0.1121  0.1159  0.0173  127 ASP C OD1   
5416 O  OD2   . ASP C 134 ? 0.8842 1.0412 0.9119 0.1413  0.1501  0.0106  127 ASP C OD2   
5417 N  N     . SER C 135 ? 0.9151 1.3024 1.1380 0.1399  0.1856  0.0764  128 SER C N     
5418 C  CA    . SER C 135 ? 0.9621 1.4175 1.2392 0.1534  0.2041  0.0963  128 SER C CA    
5419 C  C     . SER C 135 ? 0.9632 1.4558 1.2631 0.1299  0.2143  0.1121  128 SER C C     
5420 O  O     . SER C 135 ? 0.9339 1.3941 1.2014 0.1080  0.2091  0.1060  128 SER C O     
5421 C  CB    . SER C 135 ? 1.0384 1.4909 1.2970 0.1953  0.2328  0.0928  128 SER C CB    
5422 N  N     . PHE C 136 ? 1.0020 1.5653 1.3615 0.1341  0.2279  0.1345  129 PHE C N     
5423 C  CA    . PHE C 136 ? 1.0270 1.6313 1.4096 0.1174  0.2453  0.1533  129 PHE C CA    
5424 C  C     . PHE C 136 ? 1.1085 1.7496 1.4979 0.1520  0.2853  0.1632  129 PHE C C     
5425 O  O     . PHE C 136 ? 1.1471 1.8431 1.5729 0.1444  0.3049  0.1854  129 PHE C O     
5426 C  CB    . PHE C 136 ? 1.0080 1.6654 1.4575 0.0848  0.2243  0.1742  129 PHE C CB    
5427 C  CG    . PHE C 136 ? 0.9424 1.5547 1.3718 0.0513  0.1894  0.1633  129 PHE C CG    
5428 C  CD1   . PHE C 136 ? 0.9244 1.5054 1.3230 0.0263  0.1874  0.1612  129 PHE C CD1   
5429 C  CD2   . PHE C 136 ? 0.9052 1.5004 1.3392 0.0487  0.1600  0.1539  129 PHE C CD2   
5430 C  CE1   . PHE C 136 ? 0.8722 1.4090 1.2489 0.0007  0.1576  0.1502  129 PHE C CE1   
5431 C  CE2   . PHE C 136 ? 0.8541 1.4049 1.2635 0.0221  0.1313  0.1429  129 PHE C CE2   
5432 C  CZ    . PHE C 136 ? 0.8384 1.3610 1.2204 -0.0007 0.1307  0.1408  129 PHE C CZ    
5433 N  N     . ASN C 137 ? 1.1415 1.7489 1.4930 0.1899  0.2970  0.1468  130 ASN C N     
5434 C  CA    . ASN C 137 ? 1.2303 1.8519 1.5667 0.2294  0.3362  0.1494  130 ASN C CA    
5435 C  C     . ASN C 137 ? 1.2511 1.7888 1.4959 0.2441  0.3440  0.1231  130 ASN C C     
5436 O  O     . ASN C 137 ? 1.2335 1.7115 1.4378 0.2533  0.3267  0.1018  130 ASN C O     
5437 C  CB    . ASN C 137 ? 1.2777 1.9361 1.6527 0.2670  0.3447  0.1552  130 ASN C CB    
5438 C  CG    . ASN C 137 ? 1.3801 2.0769 1.7590 0.3064  0.3896  0.1662  130 ASN C CG    
5439 O  OD1   . ASN C 137 ? 1.4431 2.0983 1.7723 0.3465  0.4075  0.1502  130 ASN C OD1   
5440 N  ND2   . ASN C 137 ? 1.4058 2.1801 1.8412 0.2949  0.4086  0.1939  130 ASN C ND2   
5441 N  N     . GLU C 138 ? 1.2997 1.8348 1.5121 0.2464  0.3705  0.1265  131 GLU C N     
5442 C  CA    . GLU C 138 ? 1.3236 1.7809 1.4480 0.2527  0.3743  0.1039  131 GLU C CA    
5443 C  C     . GLU C 138 ? 1.4021 1.8181 1.4795 0.2982  0.3898  0.0862  131 GLU C C     
5444 O  O     . GLU C 138 ? 1.4121 1.7508 1.4187 0.3023  0.3792  0.0624  131 GLU C O     
5445 C  CB    . GLU C 138 ? 1.3625 1.8324 1.4671 0.2419  0.3976  0.1154  131 GLU C CB    
5446 C  CG    . GLU C 138 ? 1.2984 1.8074 1.4511 0.1975  0.3824  0.1350  131 GLU C CG    
5447 C  CD    . GLU C 138 ? 1.2003 1.6690 1.3470 0.1625  0.3411  0.1234  131 GLU C CD    
5448 O  OE1   . GLU C 138 ? 1.1691 1.5854 1.2829 0.1694  0.3212  0.1014  131 GLU C OE1   
5449 O  OE2   . GLU C 138 ? 1.1620 1.6506 1.3358 0.1283  0.3293  0.1372  131 GLU C OE2   
5450 N  N     . ALA C 139 ? 1.4641 1.9312 1.5820 0.3324  0.4136  0.0985  132 ALA C N     
5451 C  CA    . ALA C 139 ? 1.5462 1.9733 1.6235 0.3789  0.4270  0.0826  132 ALA C CA    
5452 C  C     . ALA C 139 ? 1.4947 1.8623 1.5524 0.3736  0.3909  0.0630  132 ALA C C     
5453 O  O     . ALA C 139 ? 1.5469 1.8387 1.5348 0.3943  0.3896  0.0404  132 ALA C O     
5454 C  CB    . ALA C 139 ? 1.6127 2.1150 1.7508 0.4150  0.4554  0.1027  132 ALA C CB    
5455 N  N     . THR C 140 ? 1.4020 1.8032 1.5195 0.3451  0.3619  0.0729  133 THR C N     
5456 C  CA    . THR C 140 ? 1.3497 1.7050 1.4571 0.3368  0.3280  0.0590  133 THR C CA    
5457 C  C     . THR C 140 ? 1.3071 1.5872 1.3495 0.3099  0.3074  0.0387  133 THR C C     
5458 O  O     . THR C 140 ? 1.3348 1.5449 1.3219 0.3215  0.2976  0.0191  133 THR C O     
5459 C  CB    . THR C 140 ? 1.2712 1.6844 1.4558 0.3123  0.3038  0.0761  133 THR C CB    
5460 O  OG1   . THR C 140 ? 1.3209 1.8105 1.5691 0.3368  0.3238  0.0974  133 THR C OG1   
5461 C  CG2   . THR C 140 ? 1.2272 1.5994 1.4041 0.3068  0.2713  0.0649  133 THR C CG2   
5462 N  N     . ASN C 141 ? 1.2458 1.5417 1.2975 0.2736  0.2997  0.0451  134 ASN C N     
5463 C  CA    . ASN C 141 ? 1.2019 1.4390 1.2025 0.2463  0.2797  0.0298  134 ASN C CA    
5464 C  C     . ASN C 141 ? 1.2826 1.4510 1.2022 0.2673  0.2911  0.0102  134 ASN C C     
5465 O  O     . ASN C 141 ? 1.2705 1.3761 1.1439 0.2574  0.2701  -0.0068 134 ASN C O     
5466 C  CB    . ASN C 141 ? 1.1523 1.4201 1.1723 0.2129  0.2779  0.0421  134 ASN C CB    
5467 C  CG    . ASN C 141 ? 1.0772 1.3970 1.1666 0.1873  0.2595  0.0579  134 ASN C CG    
5468 O  OD1   . ASN C 141 ? 1.0477 1.3712 1.1628 0.1893  0.2420  0.0567  134 ASN C OD1   
5469 N  ND2   . ASN C 141 ? 1.0546 1.4105 1.1707 0.1626  0.2621  0.0730  134 ASN C ND2   
5470 N  N     . ILE C 142 ? 1.3745 1.5555 1.2767 0.2970  0.3246  0.0136  135 ILE C N     
5471 C  CA    . ILE C 142 ? 1.4753 1.5890 1.2953 0.3227  0.3380  -0.0053 135 ILE C CA    
5472 C  C     . ILE C 142 ? 1.5093 1.5664 1.3010 0.3431  0.3241  -0.0222 135 ILE C C     
5473 O  O     . ILE C 142 ? 1.5187 1.5026 1.2524 0.3331  0.3032  -0.0411 135 ILE C O     
5474 C  CB    . ILE C 142 ? 1.5757 1.7230 1.3896 0.3557  0.3806  0.0041  135 ILE C CB    
5475 C  CG1   . ILE C 142 ? 1.5620 1.7373 1.3746 0.3321  0.3919  0.0164  135 ILE C CG1   
5476 C  CG2   . ILE C 142 ? 1.7039 1.7811 1.4360 0.3954  0.3968  -0.0165 135 ILE C CG2   
5477 C  CD1   . ILE C 142 ? 1.6385 1.8730 1.4715 0.3561  0.4340  0.0351  135 ILE C CD1   
5478 N  N     . LYS C 143 ? 1.5296 1.6229 1.3663 0.3700  0.3336  -0.0134 136 LYS C N     
5479 C  CA    . LYS C 143 ? 1.5725 1.6128 1.3840 0.3924  0.3219  -0.0269 136 LYS C CA    
5480 C  C     . LYS C 143 ? 1.4878 1.4876 1.2933 0.3569  0.2822  -0.0353 136 LYS C C     
5481 O  O     . LYS C 143 ? 1.5328 1.4577 1.2835 0.3624  0.2681  -0.0526 136 LYS C O     
5482 C  CB    . LYS C 143 ? 1.6008 1.6976 1.4720 0.4256  0.3368  -0.0119 136 LYS C CB    
5483 C  CG    . LYS C 143 ? 1.6521 1.6967 1.5019 0.4520  0.3250  -0.0228 136 LYS C CG    
5484 C  CD    . LYS C 143 ? 1.7583 1.7009 1.5110 0.4718  0.3267  -0.0482 136 LYS C CD    
5485 C  CE    . LYS C 143 ? 1.7669 1.6402 1.4920 0.4703  0.2976  -0.0604 136 LYS C CE    
5486 N  NZ    . LYS C 143 ? 1.7752 1.5627 1.4270 0.4436  0.2753  -0.0805 136 LYS C NZ    
5487 N  N     . ILE C 144 ? 1.3748 1.4209 1.2333 0.3204  0.2645  -0.0230 137 ILE C N     
5488 C  CA    . ILE C 144 ? 1.2984 1.3121 1.1527 0.2884  0.2305  -0.0293 137 ILE C CA    
5489 C  C     . ILE C 144 ? 1.3127 1.2608 1.0998 0.2703  0.2195  -0.0458 137 ILE C C     
5490 O  O     . ILE C 144 ? 1.3072 1.2024 1.0654 0.2584  0.1965  -0.0565 137 ILE C O     
5491 C  CB    . ILE C 144 ? 1.1872 1.2605 1.1061 0.2559  0.2153  -0.0137 137 ILE C CB    
5492 C  CG1   . ILE C 144 ? 1.1730 1.3035 1.1571 0.2686  0.2158  0.0018  137 ILE C CG1   
5493 C  CG2   . ILE C 144 ? 1.1194 1.1554 1.0226 0.2237  0.1851  -0.0214 137 ILE C CG2   
5494 C  CD1   . ILE C 144 ? 1.0820 1.2695 1.1259 0.2374  0.2010  0.0170  137 ILE C CD1   
5495 N  N     . GLY C 145 ? 1.3338 1.2882 1.0985 0.2665  0.2347  -0.0459 138 GLY C N     
5496 C  CA    . GLY C 145 ? 1.3550 1.2527 1.0571 0.2494  0.2235  -0.0597 138 GLY C CA    
5497 C  C     . GLY C 145 ? 1.2640 1.1884 0.9876 0.2117  0.2097  -0.0519 138 GLY C C     
5498 O  O     . GLY C 145 ? 1.2748 1.1598 0.9537 0.1951  0.1978  -0.0608 138 GLY C O     
5499 N  N     . ARG C 146 ? 1.1830 1.1721 0.9736 0.1986  0.2098  -0.0352 139 ARG C N     
5500 C  CA    . ARG C 146 ? 1.1114 1.1273 0.9227 0.1677  0.2011  -0.0264 139 ARG C CA    
5501 C  C     . ARG C 146 ? 1.1527 1.1944 0.9568 0.1731  0.2260  -0.0176 139 ARG C C     
5502 O  O     . ARG C 146 ? 1.1372 1.1722 0.9233 0.1535  0.2210  -0.0161 139 ARG C O     
5503 C  CB    . ARG C 146 ? 1.0233 1.0898 0.9021 0.1510  0.1896  -0.0129 139 ARG C CB    
5504 C  CG    . ARG C 146 ? 0.9487 1.0212 0.8388 0.1181  0.1713  -0.0090 139 ARG C CG    
5505 C  CD    . ARG C 146 ? 0.8768 0.9910 0.8246 0.1026  0.1591  0.0023  139 ARG C CD    
5506 N  NE    . ARG C 146 ? 0.8508 0.9534 0.8099 0.1044  0.1427  -0.0022 139 ARG C NE    
5507 C  CZ    . ARG C 146 ? 0.8129 0.8856 0.7576 0.0894  0.1222  -0.0093 139 ARG C CZ    
5508 N  NH1   . ARG C 146 ? 0.7956 0.8471 0.7156 0.0725  0.1143  -0.0136 139 ARG C NH1   
5509 N  NH2   . ARG C 146 ? 0.7966 0.8631 0.7532 0.0917  0.1100  -0.0106 139 ARG C NH2   
5510 N  N     . GLY C 147 ? 1.2124 1.2839 1.0300 0.2012  0.2535  -0.0108 140 GLY C N     
5511 C  CA    . GLY C 147 ? 1.2376 1.3588 1.0756 0.2041  0.2796  0.0057  140 GLY C CA    
5512 C  C     . GLY C 147 ? 1.3274 1.4146 1.0982 0.2167  0.2990  -0.0009 140 GLY C C     
5513 O  O     . GLY C 147 ? 1.4106 1.4491 1.1257 0.2425  0.3068  -0.0166 140 GLY C O     
5514 N  N     . SER C 148 ? 1.3168 1.4257 1.0895 0.1978  0.3052  0.0113  141 SER C N     
5515 C  CA    . SER C 148 ? 1.4082 1.5018 1.1267 0.2102  0.3295  0.0118  141 SER C CA    
5516 C  C     . SER C 148 ? 1.4216 1.5862 1.1876 0.2101  0.3580  0.0377  141 SER C C     
5517 O  O     . SER C 148 ? 1.4699 1.6347 1.2056 0.2064  0.3738  0.0458  141 SER C O     
5518 C  CB    . SER C 148 ? 1.3996 1.4460 1.0664 0.1867  0.3091  0.0037  141 SER C CB    
5519 O  OG    . SER C 148 ? 1.3286 1.4110 1.0358 0.1560  0.3002  0.0208  141 SER C OG    
5520 N  N     . GLY C 149 ? 1.3803 1.6057 1.2223 0.2113  0.3619  0.0522  142 GLY C N     
5521 C  CA    . GLY C 149 ? 1.4028 1.7028 1.2996 0.2122  0.3889  0.0790  142 GLY C CA    
5522 C  C     . GLY C 149 ? 1.3278 1.6651 1.2751 0.1714  0.3733  0.0981  142 GLY C C     
5523 O  O     . GLY C 149 ? 1.3292 1.7337 1.3399 0.1651  0.3864  0.1218  142 GLY C O     
5524 N  N     . ASP C 150 ? 1.2702 1.5639 1.1903 0.1442  0.3448  0.0887  143 ASP C N     
5525 C  CA    . ASP C 150 ? 1.2232 1.5370 1.1720 0.1087  0.3325  0.1052  143 ASP C CA    
5526 C  C     . ASP C 150 ? 1.1252 1.4398 1.1159 0.0847  0.2978  0.1019  143 ASP C C     
5527 O  O     . ASP C 150 ? 1.0852 1.4031 1.0925 0.0556  0.2821  0.1112  143 ASP C O     
5528 C  CB    . ASP C 150 ? 1.2445 1.5101 1.1297 0.0972  0.3279  0.1001  143 ASP C CB    
5529 C  CG    . ASP C 150 ? 1.3477 1.6154 1.1903 0.1139  0.3620  0.1087  143 ASP C CG    
5530 O  OD1   . ASP C 150 ? 1.3829 1.7062 1.2645 0.1119  0.3866  0.1329  143 ASP C OD1   
5531 O  OD2   . ASP C 150 ? 1.3982 1.6117 1.1677 0.1273  0.3630  0.0920  143 ASP C OD2   
5532 N  N     . ASN C 151 ? 1.0959 1.4037 1.0992 0.0983  0.2863  0.0887  144 ASN C N     
5533 C  CA    . ASN C 151 ? 1.0125 1.3131 1.0436 0.0793  0.2542  0.0829  144 ASN C CA    
5534 C  C     . ASN C 151 ? 0.9815 1.3295 1.0725 0.0529  0.2465  0.1036  144 ASN C C     
5535 O  O     . ASN C 151 ? 0.9321 1.2624 1.0246 0.0275  0.2235  0.1027  144 ASN C O     
5536 C  CB    . ASN C 151 ? 1.0010 1.2987 1.0445 0.0993  0.2477  0.0717  144 ASN C CB    
5537 C  CG    . ASN C 151 ? 1.0458 1.2917 1.0289 0.1247  0.2540  0.0517  144 ASN C CG    
5538 O  OD1   . ASN C 151 ? 1.1226 1.3653 1.0757 0.1466  0.2798  0.0515  144 ASN C OD1   
5539 N  ND2   . ASN C 151 ? 1.0076 1.2107 0.9701 0.1216  0.2306  0.0352  144 ASN C ND2   
5540 N  N     . VAL C 152 ? 1.0194 1.4271 1.1593 0.0593  0.2657  0.1226  145 VAL C N     
5541 C  CA    . VAL C 152 ? 0.9968 1.4515 1.2003 0.0337  0.2537  0.1421  145 VAL C CA    
5542 C  C     . VAL C 152 ? 1.0071 1.4595 1.2051 0.0052  0.2536  0.1562  145 VAL C C     
5543 O  O     . VAL C 152 ? 0.9681 1.4127 1.1833 -0.0228 0.2286  0.1596  145 VAL C O     
5544 C  CB    . VAL C 152 ? 1.0383 1.5633 1.3026 0.0476  0.2715  0.1605  145 VAL C CB    
5545 C  CG1   . VAL C 152 ? 1.0307 1.6068 1.3611 0.0161  0.2583  0.1840  145 VAL C CG1   
5546 C  CG2   . VAL C 152 ? 1.0259 1.5485 1.2975 0.0741  0.2655  0.1471  145 VAL C CG2   
5547 N  N     . GLN C 153 ? 1.0667 1.5197 1.2349 0.0134  0.2808  0.1638  146 GLN C N     
5548 C  CA    . GLN C 153 ? 1.0843 1.5283 1.2399 -0.0123 0.2808  0.1777  146 GLN C CA    
5549 C  C     . GLN C 153 ? 1.0273 1.4102 1.1452 -0.0281 0.2505  0.1609  146 GLN C C     
5550 O  O     . GLN C 153 ? 1.0107 1.3867 1.1418 -0.0560 0.2329  0.1700  146 GLN C O     
5551 C  CB    . GLN C 153 ? 1.1627 1.6073 1.2786 0.0026  0.3146  0.1857  146 GLN C CB    
5552 N  N     . LYS C 154 ? 1.0033 1.3419 1.0757 -0.0099 0.2436  0.1369  147 LYS C N     
5553 C  CA    . LYS C 154 ? 0.9541 1.2405 0.9932 -0.0213 0.2171  0.1217  147 LYS C CA    
5554 C  C     . LYS C 154 ? 0.8922 1.1811 0.9686 -0.0381 0.1895  0.1191  147 LYS C C     
5555 O  O     . LYS C 154 ? 0.8687 1.1332 0.9386 -0.0574 0.1705  0.1194  147 LYS C O     
5556 C  CB    . LYS C 154 ? 0.9516 1.1959 0.9393 0.0000  0.2158  0.0990  147 LYS C CB    
5557 C  CG    . LYS C 154 ? 0.9235 1.1186 0.8707 -0.0100 0.1945  0.0876  147 LYS C CG    
5558 C  CD    . LYS C 154 ? 0.9544 1.1398 0.8823 -0.0255 0.1965  0.1011  147 LYS C CD    
5559 C  CE    . LYS C 154 ? 0.9208 1.0659 0.8235 -0.0366 0.1717  0.0929  147 LYS C CE    
5560 N  NZ    . LYS C 154 ? 0.9283 1.0382 0.7836 -0.0227 0.1665  0.0756  147 LYS C NZ    
5561 N  N     . LEU C 155 ? 0.8759 1.1941 0.9902 -0.0298 0.1876  0.1178  148 LEU C N     
5562 C  CA    . LEU C 155 ? 0.8270 1.1450 0.9705 -0.0440 0.1611  0.1144  148 LEU C CA    
5563 C  C     . LEU C 155 ? 0.8379 1.1700 1.0107 -0.0735 0.1502  0.1318  148 LEU C C     
5564 O  O     . LEU C 155 ? 0.8103 1.1103 0.9727 -0.0893 0.1274  0.1260  148 LEU C O     
5565 C  CB    . LEU C 155 ? 0.8215 1.1707 0.9984 -0.0278 0.1625  0.1124  148 LEU C CB    
5566 C  CG    . LEU C 155 ? 0.7815 1.1328 0.9868 -0.0401 0.1353  0.1095  148 LEU C CG    
5567 C  CD1   . LEU C 155 ? 0.7334 1.0325 0.9005 -0.0408 0.1157  0.0898  148 LEU C CD1   
5568 C  CD2   . LEU C 155 ? 0.7892 1.1775 1.0308 -0.0235 0.1380  0.1119  148 LEU C CD2   
5569 N  N     . TYR C 156 ? 0.8875 1.2653 1.0944 -0.0810 0.1672  0.1539  149 TYR C N     
5570 C  CA    . TYR C 156 ? 0.9113 1.3040 1.1497 -0.1123 0.1560  0.1732  149 TYR C CA    
5571 C  C     . TYR C 156 ? 0.9161 1.2595 1.1128 -0.1274 0.1479  0.1722  149 TYR C C     
5572 O  O     . TYR C 156 ? 0.9125 1.2325 1.1125 -0.1499 0.1248  0.1740  149 TYR C O     
5573 C  CB    . TYR C 156 ? 0.9715 1.4273 1.2563 -0.1180 0.1786  0.2003  149 TYR C CB    
5574 C  CG    . TYR C 156 ? 0.9742 1.4862 1.3202 -0.1159 0.1749  0.2088  149 TYR C CG    
5575 C  CD1   . TYR C 156 ? 0.9692 1.5062 1.3235 -0.0838 0.1903  0.2013  149 TYR C CD1   
5576 C  CD2   . TYR C 156 ? 0.9895 1.5264 1.3834 -0.1461 0.1533  0.2246  149 TYR C CD2   
5577 C  CE1   . TYR C 156 ? 0.9765 1.5661 1.3880 -0.0799 0.1856  0.2105  149 TYR C CE1   
5578 C  CE2   . TYR C 156 ? 0.9969 1.5872 1.4483 -0.1452 0.1463  0.2337  149 TYR C CE2   
5579 C  CZ    . TYR C 156 ? 0.9888 1.6081 1.4509 -0.1110 0.1631  0.2273  149 TYR C CZ    
5580 O  OH    . TYR C 156 ? 1.0008 1.6745 1.5214 -0.1085 0.1551  0.2378  149 TYR C OH    
5581 N  N     . GLU C 157 ? 0.9319 1.2558 1.0854 -0.1131 0.1661  0.1685  150 GLU C N     
5582 C  CA    . GLU C 157 ? 0.9433 1.2219 1.0544 -0.1230 0.1599  0.1685  150 GLU C CA    
5583 C  C     . GLU C 157 ? 0.8919 1.1249 0.9848 -0.1266 0.1310  0.1504  150 GLU C C     
5584 O  O     . GLU C 157 ? 0.9022 1.1075 0.9891 -0.1452 0.1144  0.1552  150 GLU C O     
5585 C  CB    . GLU C 157 ? 0.9677 1.2317 1.0313 -0.1027 0.1810  0.1635  150 GLU C CB    
5586 C  CG    . GLU C 157 ? 1.0062 1.2382 1.0324 -0.1141 0.1812  0.1730  150 GLU C CG    
5587 C  CD    . GLU C 157 ? 1.0377 1.2487 1.0093 -0.0953 0.1971  0.1669  150 GLU C CD    
5588 O  OE1   . GLU C 157 ? 1.0178 1.2228 0.9713 -0.0736 0.2006  0.1488  150 GLU C OE1   
5589 O  OE2   . GLU C 157 ? 1.0907 1.2888 1.0356 -0.1031 0.2051  0.1810  150 GLU C OE2   
5590 N  N     . ILE C 158 ? 0.8441 1.0691 0.9281 -0.1078 0.1260  0.1305  151 ILE C N     
5591 C  CA    . ILE C 158 ? 0.7986 0.9855 0.8647 -0.1073 0.1030  0.1138  151 ILE C CA    
5592 C  C     . ILE C 158 ? 0.7945 0.9812 0.8889 -0.1260 0.0823  0.1174  151 ILE C C     
5593 O  O     . ILE C 158 ? 0.7964 0.9473 0.8744 -0.1362 0.0655  0.1148  151 ILE C O     
5594 C  CB    . ILE C 158 ? 0.7578 0.9407 0.8119 -0.0855 0.1036  0.0950  151 ILE C CB    
5595 C  CG1   . ILE C 158 ? 0.7768 0.9489 0.7939 -0.0697 0.1199  0.0904  151 ILE C CG1   
5596 C  CG2   . ILE C 158 ? 0.7146 0.8661 0.7566 -0.0856 0.0818  0.0806  151 ILE C CG2   
5597 C  CD1   . ILE C 158 ? 0.7573 0.9271 0.7641 -0.0497 0.1233  0.0751  151 ILE C CD1   
5598 N  N     . GLY C 159 ? 0.7989 1.0249 0.9347 -0.1298 0.0833  0.1240  152 GLY C N     
5599 C  CA    . GLY C 159 ? 0.8119 1.0419 0.9764 -0.1508 0.0626  0.1302  152 GLY C CA    
5600 C  C     . GLY C 159 ? 0.8557 1.0581 1.0103 -0.1746 0.0528  0.1418  152 GLY C C     
5601 O  O     . GLY C 159 ? 0.8577 1.0210 0.9968 -0.1838 0.0308  0.1343  152 GLY C O     
5602 N  N     . SER C 160 ? 0.8988 1.1185 1.0582 -0.1829 0.0703  0.1603  153 SER C N     
5603 C  CA    . SER C 160 ? 0.9522 1.1467 1.1036 -0.2071 0.0626  0.1752  153 SER C CA    
5604 C  C     . SER C 160 ? 0.9429 1.0773 1.0438 -0.2002 0.0527  0.1626  153 SER C C     
5605 O  O     . SER C 160 ? 0.9742 1.0689 1.0630 -0.2160 0.0333  0.1642  153 SER C O     
5606 C  CB    . SER C 160 ? 1.0021 1.2296 1.1659 -0.2145 0.0870  0.1985  153 SER C CB    
5607 O  OG    . SER C 160 ? 0.9877 1.2113 1.1175 -0.1906 0.1083  0.1917  153 SER C OG    
5608 N  N     . TRP C 161 ? 0.9085 1.0363 0.9802 -0.1763 0.0654  0.1509  154 TRP C N     
5609 C  CA    . TRP C 161 ? 0.8961 0.9762 0.9255 -0.1662 0.0563  0.1392  154 TRP C CA    
5610 C  C     . TRP C 161 ? 0.8708 0.9212 0.8962 -0.1649 0.0332  0.1236  154 TRP C C     
5611 O  O     . TRP C 161 ? 0.8942 0.9016 0.8959 -0.1682 0.0196  0.1220  154 TRP C O     
5612 C  CB    . TRP C 161 ? 0.8641 0.9481 0.8688 -0.1425 0.0703  0.1284  154 TRP C CB    
5613 C  CG    . TRP C 161 ? 0.9043 1.0019 0.8947 -0.1407 0.0918  0.1416  154 TRP C CG    
5614 C  CD1   . TRP C 161 ? 0.9651 1.0654 0.9567 -0.1574 0.0999  0.1631  154 TRP C CD1   
5615 C  CD2   . TRP C 161 ? 0.8980 1.0042 0.8654 -0.1212 0.1081  0.1346  154 TRP C CD2   
5616 N  NE1   . TRP C 161 ? 0.9959 1.1083 0.9662 -0.1481 0.1219  0.1702  154 TRP C NE1   
5617 C  CE2   . TRP C 161 ? 0.9581 1.0721 0.9111 -0.1254 0.1266  0.1519  154 TRP C CE2   
5618 C  CE3   . TRP C 161 ? 0.8570 0.9616 0.8114 -0.1016 0.1083  0.1160  154 TRP C CE3   
5619 C  CZ2   . TRP C 161 ? 0.9806 1.0982 0.9027 -0.1089 0.1448  0.1491  154 TRP C CZ2   
5620 C  CZ3   . TRP C 161 ? 0.8798 0.9863 0.8057 -0.0874 0.1242  0.1132  154 TRP C CZ3   
5621 C  CH2   . TRP C 161 ? 0.9421 1.0540 0.8500 -0.0899 0.1423  0.1286  154 TRP C CH2   
5622 N  N     . CYS C 162 ? 0.8312 0.9026 0.8769 -0.1584 0.0293  0.1127  155 CYS C N     
5623 C  CA    . CYS C 162 ? 0.8111 0.8557 0.8483 -0.1543 0.0101  0.0974  155 CYS C CA    
5624 C  C     . CYS C 162 ? 0.8645 0.8785 0.9008 -0.1751 -0.0097 0.1027  155 CYS C C     
5625 O  O     . CYS C 162 ? 0.8721 0.8450 0.8840 -0.1704 -0.0250 0.0910  155 CYS C O     
5626 C  CB    . CYS C 162 ? 0.7716 0.8461 0.8316 -0.1464 0.0094  0.0885  155 CYS C CB    
5627 S  SG    . CYS C 162 ? 0.7134 0.8014 0.7612 -0.1196 0.0246  0.0753  155 CYS C SG    
5628 N  N     . GLN C 163 ? 0.9080 0.9433 0.9716 -0.1978 -0.0091 0.1207  156 GLN C N     
5629 C  CA    . GLN C 163 ? 0.9740 0.9810 1.0395 -0.2237 -0.0294 0.1293  156 GLN C CA    
5630 C  C     . GLN C 163 ? 1.0192 0.9760 1.0488 -0.2269 -0.0321 0.1341  156 GLN C C     
5631 O  O     . GLN C 163 ? 1.0582 0.9614 1.0603 -0.2300 -0.0511 0.1270  156 GLN C O     
5632 C  CB    . GLN C 163 ? 1.0083 1.0631 1.1201 -0.2478 -0.0253 0.1509  156 GLN C CB    
5633 C  CG    . GLN C 163 ? 1.0653 1.1071 1.1936 -0.2758 -0.0523 0.1563  156 GLN C CG    
5634 C  CD    . GLN C 163 ? 1.1410 1.1214 1.2395 -0.2956 -0.0693 0.1620  156 GLN C CD    
5635 O  OE1   . GLN C 163 ? 1.1838 1.1625 1.2833 -0.3097 -0.0602 0.1809  156 GLN C OE1   
5636 N  NE2   . GLN C 163 ? 1.1673 1.0930 1.2352 -0.2960 -0.0941 0.1460  156 GLN C NE2   
5637 N  N     . LYS C 164 ? 1.0209 0.9937 1.0477 -0.2239 -0.0124 0.1464  157 LYS C N     
5638 C  CA    . LYS C 164 ? 1.0666 0.9981 1.0607 -0.2257 -0.0124 0.1547  157 LYS C CA    
5639 C  C     . LYS C 164 ? 1.0473 0.9338 1.0029 -0.2022 -0.0212 0.1364  157 LYS C C     
5640 O  O     . LYS C 164 ? 1.1015 0.9374 1.0290 -0.2049 -0.0325 0.1395  157 LYS C O     
5641 C  CB    . LYS C 164 ? 1.0647 1.0297 1.0613 -0.2222 0.0124  0.1689  157 LYS C CB    
5642 C  CG    . LYS C 164 ? 1.1196 1.0483 1.0833 -0.2255 0.0145  0.1820  157 LYS C CG    
5643 C  CD    . LYS C 164 ? 1.1220 1.0826 1.0816 -0.2196 0.0394  0.1941  157 LYS C CD    
5644 C  CE    . LYS C 164 ? 1.1963 1.1269 1.1291 -0.2308 0.0420  0.2144  157 LYS C CE    
5645 N  NZ    . LYS C 164 ? 1.2090 1.1724 1.1344 -0.2254 0.0680  0.2269  157 LYS C NZ    
5646 N  N     . TYR C 165 ? 0.9775 0.8822 0.9327 -0.1788 -0.0159 0.1190  158 TYR C N     
5647 C  CA    . TYR C 165 ? 0.9595 0.8332 0.8847 -0.1556 -0.0207 0.1051  158 TYR C CA    
5648 C  C     . TYR C 165 ? 0.9375 0.7983 0.8601 -0.1455 -0.0328 0.0868  158 TYR C C     
5649 O  O     . TYR C 165 ? 0.9132 0.7622 0.8186 -0.1238 -0.0329 0.0753  158 TYR C O     
5650 C  CB    . TYR C 165 ? 0.9097 0.8106 0.8307 -0.1371 -0.0051 0.1021  158 TYR C CB    
5651 C  CG    . TYR C 165 ? 0.9431 0.8489 0.8551 -0.1437 0.0064  0.1190  158 TYR C CG    
5652 C  CD1   . TYR C 165 ? 0.9977 0.8642 0.8828 -0.1446 0.0001  0.1284  158 TYR C CD1   
5653 C  CD2   . TYR C 165 ? 0.9315 0.8784 0.8594 -0.1482 0.0240  0.1267  158 TYR C CD2   
5654 C  CE1   . TYR C 165 ? 1.0371 0.9053 0.9098 -0.1513 0.0102  0.1454  158 TYR C CE1   
5655 C  CE2   . TYR C 165 ? 0.9725 0.9221 0.8867 -0.1533 0.0363  0.1427  158 TYR C CE2   
5656 C  CZ    . TYR C 165 ? 1.0245 0.9349 0.9107 -0.1559 0.0290  0.1524  158 TYR C CZ    
5657 O  OH    . TYR C 165 ? 1.0718 0.9830 0.9405 -0.1611 0.0409  0.1694  158 TYR C OH    
5658 N  N     . ASP C 166 ? 0.9537 0.8169 0.8922 -0.1612 -0.0435 0.0856  159 ASP C N     
5659 C  CA    . ASP C 166 ? 0.9544 0.7950 0.8811 -0.1534 -0.0575 0.0693  159 ASP C CA    
5660 C  C     . ASP C 166 ? 0.8800 0.7506 0.8120 -0.1309 -0.0472 0.0563  159 ASP C C     
5661 O  O     . ASP C 166 ? 0.8692 0.7209 0.7798 -0.1106 -0.0475 0.0450  159 ASP C O     
5662 C  CB    . ASP C 166 ? 1.0165 0.7937 0.9040 -0.1462 -0.0703 0.0637  159 ASP C CB    
5663 C  CG    . ASP C 166 ? 1.0366 0.7829 0.9031 -0.1368 -0.0838 0.0467  159 ASP C CG    
5664 O  OD1   . ASP C 166 ? 1.0350 0.7955 0.9163 -0.1498 -0.0926 0.0437  159 ASP C OD1   
5665 O  OD2   . ASP C 166 ? 1.0618 0.7698 0.8959 -0.1157 -0.0856 0.0372  159 ASP C OD2   
5666 N  N     . ILE C 167 ? 0.8356 0.7541 0.7975 -0.1346 -0.0374 0.0594  160 ILE C N     
5667 C  CA    . ILE C 167 ? 0.7737 0.7193 0.7424 -0.1173 -0.0292 0.0487  160 ILE C CA    
5668 C  C     . ILE C 167 ? 0.7623 0.7363 0.7574 -0.1258 -0.0336 0.0482  160 ILE C C     
5669 O  O     . ILE C 167 ? 0.7720 0.7751 0.7943 -0.1399 -0.0296 0.0602  160 ILE C O     
5670 C  CB    . ILE C 167 ? 0.7363 0.7092 0.7099 -0.1081 -0.0115 0.0528  160 ILE C CB    
5671 C  CG1   . ILE C 167 ? 0.7501 0.6990 0.6991 -0.0994 -0.0094 0.0546  160 ILE C CG1   
5672 C  CG2   . ILE C 167 ? 0.6825 0.6803 0.6637 -0.0939 -0.0049 0.0429  160 ILE C CG2   
5673 C  CD1   . ILE C 167 ? 0.7323 0.7028 0.6810 -0.0949 0.0045  0.0603  160 ILE C CD1   
5674 N  N     . LYS C 168 ? 0.7460 0.7147 0.7340 -0.1161 -0.0408 0.0360  161 LYS C N     
5675 C  CA    . LYS C 168 ? 0.7383 0.7337 0.7499 -0.1222 -0.0467 0.0361  161 LYS C CA    
5676 C  C     . LYS C 168 ? 0.6944 0.7353 0.7324 -0.1158 -0.0293 0.0414  161 LYS C C     
5677 O  O     . LYS C 168 ? 0.6573 0.7024 0.6857 -0.1002 -0.0169 0.0362  161 LYS C O     
5678 C  CB    . LYS C 168 ? 0.7363 0.7133 0.7284 -0.1115 -0.0571 0.0226  161 LYS C CB    
5679 C  CG    . LYS C 168 ? 0.7962 0.7228 0.7556 -0.1156 -0.0742 0.0159  161 LYS C CG    
5680 C  CD    . LYS C 168 ? 0.8012 0.7053 0.7313 -0.0996 -0.0791 0.0020  161 LYS C CD    
5681 C  CE    . LYS C 168 ? 0.8041 0.7231 0.7431 -0.1040 -0.0904 -0.0003 161 LYS C CE    
5682 N  NZ    . LYS C 168 ? 0.8674 0.7713 0.8089 -0.1265 -0.1132 0.0032  161 LYS C NZ    
5683 N  N     . PHE C 169 ? 0.7070 0.7816 0.7783 -0.1276 -0.0290 0.0522  162 PHE C N     
5684 C  CA    . PHE C 169 ? 0.6814 0.7972 0.7761 -0.1193 -0.0107 0.0581  162 PHE C CA    
5685 C  C     . PHE C 169 ? 0.6623 0.8009 0.7741 -0.1104 -0.0143 0.0537  162 PHE C C     
5686 O  O     . PHE C 169 ? 0.6864 0.8374 0.8189 -0.1213 -0.0289 0.0583  162 PHE C O     
5687 C  CB    . PHE C 169 ? 0.7162 0.8609 0.8399 -0.1351 -0.0037 0.0760  162 PHE C CB    
5688 C  CG    . PHE C 169 ? 0.7069 0.8970 0.8564 -0.1250 0.0166  0.0836  162 PHE C CG    
5689 C  CD1   . PHE C 169 ? 0.6825 0.8710 0.8126 -0.1064 0.0349  0.0775  162 PHE C CD1   
5690 C  CD2   . PHE C 169 ? 0.7332 0.9673 0.9261 -0.1341 0.0173  0.0978  162 PHE C CD2   
5691 C  CE1   . PHE C 169 ? 0.6883 0.9116 0.8350 -0.0945 0.0546  0.0832  162 PHE C CE1   
5692 C  CE2   . PHE C 169 ? 0.7347 1.0109 0.9503 -0.1208 0.0390  0.1053  162 PHE C CE2   
5693 C  CZ    . PHE C 169 ? 0.7143 0.9818 0.9036 -0.0999 0.0581  0.0970  162 PHE C CZ    
5694 N  N     . LYS C 170 ? 0.6260 0.7685 0.7282 -0.0914 -0.0024 0.0459  163 LYS C N     
5695 C  CA    . LYS C 170 ? 0.6105 0.7692 0.7235 -0.0797 -0.0040 0.0420  163 LYS C CA    
5696 C  C     . LYS C 170 ? 0.6050 0.7921 0.7329 -0.0669 0.0151  0.0462  163 LYS C C     
5697 O  O     . LYS C 170 ? 0.6035 0.7864 0.7186 -0.0631 0.0297  0.0467  163 LYS C O     
5698 C  CB    . LYS C 170 ? 0.5853 0.7144 0.6675 -0.0688 -0.0084 0.0288  163 LYS C CB    
5699 C  CG    . LYS C 170 ? 0.5671 0.7044 0.6502 -0.0537 -0.0048 0.0243  163 LYS C CG    
5700 C  CD    . LYS C 170 ? 0.5510 0.6601 0.6051 -0.0475 -0.0095 0.0146  163 LYS C CD    
5701 C  CE    . LYS C 170 ? 0.5356 0.6451 0.5840 -0.0340 -0.0036 0.0109  163 LYS C CE    
5702 N  NZ    . LYS C 170 ? 0.5231 0.6094 0.5457 -0.0306 -0.0048 0.0046  163 LYS C NZ    
5703 N  N     . LEU C 171 ? 0.6108 0.8246 0.7630 -0.0589 0.0145  0.0494  164 LEU C N     
5704 C  CA    . LEU C 171 ? 0.6166 0.8537 0.7800 -0.0415 0.0330  0.0521  164 LEU C CA    
5705 C  C     . LEU C 171 ? 0.6044 0.8320 0.7585 -0.0246 0.0297  0.0436  164 LEU C C     
5706 O  O     . LEU C 171 ? 0.6029 0.8291 0.7629 -0.0273 0.0130  0.0428  164 LEU C O     
5707 C  CB    . LEU C 171 ? 0.6503 0.9355 0.8590 -0.0456 0.0378  0.0683  164 LEU C CB    
5708 C  CG    . LEU C 171 ? 0.6703 0.9862 0.8968 -0.0234 0.0573  0.0729  164 LEU C CG    
5709 C  CD1   . LEU C 171 ? 0.6822 0.9907 0.8859 -0.0135 0.0816  0.0714  164 LEU C CD1   
5710 C  CD2   . LEU C 171 ? 0.7052 1.0767 0.9862 -0.0281 0.0571  0.0912  164 LEU C CD2   
5711 N  N     . ASN C 172 ? 0.6059 0.8247 0.7431 -0.0077 0.0451  0.0383  165 ASN C N     
5712 C  CA    . ASN C 172 ? 0.6026 0.8033 0.7240 0.0077  0.0435  0.0302  165 ASN C CA    
5713 C  C     . ASN C 172 ? 0.6365 0.8550 0.7694 0.0283  0.0589  0.0334  165 ASN C C     
5714 O  O     . ASN C 172 ? 0.6557 0.8708 0.7751 0.0364  0.0760  0.0319  165 ASN C O     
5715 C  CB    . ASN C 172 ? 0.5869 0.7486 0.6685 0.0097  0.0458  0.0190  165 ASN C CB    
5716 C  CG    . ASN C 172 ? 0.5588 0.6990 0.6255 -0.0015 0.0311  0.0142  165 ASN C CG    
5717 O  OD1   . ASN C 172 ? 0.5528 0.7002 0.6306 -0.0126 0.0204  0.0175  165 ASN C OD1   
5718 N  ND2   . ASN C 172 ? 0.5498 0.6631 0.5900 0.0010  0.0310  0.0070  165 ASN C ND2   
5719 N  N     . THR C 173 ? 0.6507 0.8860 0.8055 0.0384  0.0520  0.0378  166 THR C N     
5720 C  CA    . THR C 173 ? 0.6910 0.9453 0.8606 0.0623  0.0654  0.0419  166 THR C CA    
5721 C  C     . THR C 173 ? 0.7006 0.9209 0.8454 0.0780  0.0600  0.0336  166 THR C C     
5722 O  O     . THR C 173 ? 0.6866 0.8993 0.8324 0.0725  0.0422  0.0339  166 THR C O     
5723 C  CB    . THR C 173 ? 0.7111 1.0181 0.9330 0.0629  0.0605  0.0573  166 THR C CB    
5724 O  OG1   . THR C 173 ? 0.7073 1.0443 0.9542 0.0429  0.0618  0.0671  166 THR C OG1   
5725 C  CG2   . THR C 173 ? 0.7598 1.0923 1.0013 0.0916  0.0770  0.0633  166 THR C CG2   
5726 N  N     . VAL C 174 ? 0.7351 0.9329 0.8553 0.0978  0.0750  0.0271  167 VAL C N     
5727 C  CA    . VAL C 174 ? 0.7633 0.9311 0.8650 0.1155  0.0705  0.0222  167 VAL C CA    
5728 C  C     . VAL C 174 ? 0.8127 1.0127 0.9456 0.1418  0.0788  0.0314  167 VAL C C     
5729 O  O     . VAL C 174 ? 0.8514 1.0676 0.9896 0.1587  0.0994  0.0332  167 VAL C O     
5730 C  CB    . VAL C 174 ? 0.7866 0.9024 0.8387 0.1216  0.0781  0.0092  167 VAL C CB    
5731 C  CG1   . VAL C 174 ? 0.8280 0.9070 0.8588 0.1388  0.0728  0.0051  167 VAL C CG1   
5732 C  CG2   . VAL C 174 ? 0.7422 0.8338 0.7699 0.0967  0.0696  0.0026  167 VAL C CG2   
5733 N  N     . VAL C 175 ? 0.8175 1.0271 0.9696 0.1466  0.0630  0.0379  168 VAL C N     
5734 C  CA    . VAL C 175 ? 0.8652 1.1104 1.0532 0.1717  0.0667  0.0490  168 VAL C CA    
5735 C  C     . VAL C 175 ? 0.9218 1.1224 1.0760 0.2006  0.0738  0.0416  168 VAL C C     
5736 O  O     . VAL C 175 ? 0.9187 1.0733 1.0408 0.1963  0.0603  0.0353  168 VAL C O     
5737 C  CB    . VAL C 175 ? 0.8521 1.1280 1.0752 0.1623  0.0429  0.0605  168 VAL C CB    
5738 C  CG1   . VAL C 175 ? 0.9021 1.2290 1.1739 0.1862  0.0454  0.0756  168 VAL C CG1   
5739 C  CG2   . VAL C 175 ? 0.8029 1.1026 1.0438 0.1297  0.0309  0.0640  168 VAL C CG2   
5740 N  N     . ASN C 176 ? 0.9810 1.1951 1.1421 0.2300  0.0956  0.0433  169 ASN C N     
5741 C  CA    . ASN C 176 ? 1.0492 1.2107 1.1671 0.2587  0.1067  0.0329  169 ASN C CA    
5742 C  C     . ASN C 176 ? 1.1239 1.3186 1.2710 0.2984  0.1230  0.0423  169 ASN C C     
5743 O  O     . ASN C 176 ? 1.1191 1.3842 1.3246 0.3016  0.1266  0.0583  169 ASN C O     
5744 C  CB    . ASN C 176 ? 1.0585 1.1804 1.1288 0.2539  0.1219  0.0183  169 ASN C CB    
5745 C  CG    . ASN C 176 ? 1.0608 1.2297 1.1535 0.2557  0.1442  0.0236  169 ASN C CG    
5746 O  OD1   . ASN C 176 ? 1.1256 1.3152 1.2280 0.2862  0.1662  0.0276  169 ASN C OD1   
5747 N  ND2   . ASN C 176 ? 0.9980 1.1821 1.0963 0.2243  0.1402  0.0243  169 ASN C ND2   
5748 N  N     . LYS C 177 ? 1.2015 1.3439 1.3071 0.3292  0.1328  0.0327  170 LYS C N     
5749 C  CA    . LYS C 177 ? 1.2871 1.4519 1.4125 0.3734  0.1506  0.0399  170 LYS C CA    
5750 C  C     . LYS C 177 ? 1.2989 1.5280 1.4601 0.3827  0.1780  0.0484  170 LYS C C     
5751 O  O     . LYS C 177 ? 1.3335 1.6263 1.5492 0.4059  0.1882  0.0649  170 LYS C O     
5752 C  CB    . LYS C 177 ? 1.3784 1.4613 1.4385 0.4032  0.1581  0.0243  170 LYS C CB    
5753 C  CG    . LYS C 177 ? 1.4853 1.5777 1.5544 0.4557  0.1786  0.0290  170 LYS C CG    
5754 C  CD    . LYS C 177 ? 1.4915 1.6491 1.6286 0.4733  0.1703  0.0503  170 LYS C CD    
5755 C  CE    . LYS C 177 ? 1.4402 1.5846 1.5849 0.4493  0.1355  0.0558  170 LYS C CE    
5756 N  NZ    . LYS C 177 ? 1.4780 1.6669 1.6733 0.4751  0.1261  0.0743  170 LYS C NZ    
5757 N  N     . PHE C 178 ? 1.2732 1.4889 1.4060 0.3633  0.1893  0.0391  171 PHE C N     
5758 C  CA    . PHE C 178 ? 1.3061 1.5674 1.4561 0.3762  0.2198  0.0454  171 PHE C CA    
5759 C  C     . PHE C 178 ? 1.2447 1.5921 1.4662 0.3507  0.2174  0.0658  171 PHE C C     
5760 O  O     . PHE C 178 ? 1.2793 1.6823 1.5328 0.3630  0.2429  0.0781  171 PHE C O     
5761 C  CB    . PHE C 178 ? 1.3224 1.5276 1.4053 0.3694  0.2326  0.0275  171 PHE C CB    
5762 C  CG    . PHE C 178 ? 1.4083 1.5289 1.4193 0.3972  0.2370  0.0081  171 PHE C CG    
5763 C  CD1   . PHE C 178 ? 1.5134 1.6303 1.5187 0.4455  0.2580  0.0086  171 PHE C CD1   
5764 C  CD2   . PHE C 178 ? 1.3933 1.4373 1.3426 0.3753  0.2196  -0.0098 171 PHE C CD2   
5765 C  CE1   . PHE C 178 ? 1.6057 1.6357 1.5389 0.4711  0.2603  -0.0102 171 PHE C CE1   
5766 C  CE2   . PHE C 178 ? 1.4833 1.4451 1.3650 0.3974  0.2205  -0.0271 171 PHE C CE2   
5767 C  CZ    . PHE C 178 ? 1.5915 1.5422 1.4621 0.4452  0.2403  -0.0282 171 PHE C CZ    
5768 N  N     . ASN C 179 ? 1.1636 1.5214 1.4084 0.3151  0.1878  0.0701  172 ASN C N     
5769 C  CA    . ASN C 179 ? 1.1149 1.5427 1.4184 0.2870  0.1828  0.0874  172 ASN C CA    
5770 C  C     . ASN C 179 ? 1.0824 1.5447 1.4345 0.2732  0.1531  0.1000  172 ASN C C     
5771 O  O     . ASN C 179 ? 1.0420 1.5511 1.4367 0.2437  0.1412  0.1125  172 ASN C O     
5772 C  CB    . ASN C 179 ? 1.0518 1.4573 1.3283 0.2492  0.1781  0.0795  172 ASN C CB    
5773 C  CG    . ASN C 179 ? 0.9910 1.3413 1.2320 0.2243  0.1497  0.0662  172 ASN C CG    
5774 O  OD1   . ASN C 179 ? 1.0022 1.3174 1.2248 0.2361  0.1367  0.0598  172 ASN C OD1   
5775 N  ND2   . ASN C 179 ? 0.9330 1.2756 1.1643 0.1908  0.1410  0.0632  172 ASN C ND2   
5776 N  N     . HIS C 180 ? 1.1097 1.5476 1.4538 0.2944  0.1403  0.0977  173 HIS C N     
5777 C  CA    . HIS C 180 ? 1.0807 1.5366 1.4555 0.2791  0.1083  0.1068  173 HIS C CA    
5778 C  C     . HIS C 180 ? 1.1075 1.6515 1.5615 0.2847  0.1057  0.1312  173 HIS C C     
5779 O  O     . HIS C 180 ? 1.0839 1.6518 1.5683 0.2646  0.0769  0.1407  173 HIS C O     
5780 C  CB    . HIS C 180 ? 1.1053 1.5056 1.4446 0.2972  0.0933  0.0987  173 HIS C CB    
5781 C  CG    . HIS C 180 ? 1.1915 1.5945 1.5369 0.3441  0.1085  0.1030  173 HIS C CG    
5782 N  ND1   . HIS C 180 ? 1.2497 1.6282 1.5645 0.3740  0.1389  0.0939  173 HIS C ND1   
5783 C  CD2   . HIS C 180 ? 1.2377 1.6614 1.6128 0.3681  0.0968  0.1153  173 HIS C CD2   
5784 C  CE1   . HIS C 180 ? 1.3303 1.7135 1.6560 0.4164  0.1465  0.1000  173 HIS C CE1   
5785 N  NE2   . HIS C 180 ? 1.3221 1.7342 1.6864 0.4135  0.1209  0.1136  173 HIS C NE2   
5786 N  N     . LEU C 181 ? 1.1645 1.7569 1.6512 0.3122  0.1350  0.1420  174 LEU C N     
5787 C  CA    . LEU C 181 ? 1.1943 1.8805 1.7642 0.3155  0.1347  0.1684  174 LEU C CA    
5788 C  C     . LEU C 181 ? 1.1644 1.9008 1.7689 0.2816  0.1419  0.1797  174 LEU C C     
5789 O  O     . LEU C 181 ? 1.1819 1.9971 1.8587 0.2721  0.1355  0.2033  174 LEU C O     
5790 C  CB    . LEU C 181 ? 1.2848 2.0036 1.8774 0.3676  0.1645  0.1775  174 LEU C CB    
5791 C  CG    . LEU C 181 ? 1.3344 2.0250 1.9159 0.4041  0.1535  0.1752  174 LEU C CG    
5792 C  CD1   . LEU C 181 ? 1.4323 2.1703 2.0495 0.4568  0.1837  0.1885  174 LEU C CD1   
5793 C  CD2   . LEU C 181 ? 1.3077 2.0212 1.9256 0.3839  0.1123  0.1870  174 LEU C CD2   
5794 N  N     . GLU C 182 ? 1.1254 1.8175 1.6808 0.2620  0.1532  0.1649  175 GLU C N     
5795 C  CA    . GLU C 182 ? 1.1140 1.8500 1.6975 0.2360  0.1659  0.1768  175 GLU C CA    
5796 C  C     . GLU C 182 ? 1.0728 1.8418 1.6992 0.1923  0.1322  0.1894  175 GLU C C     
5797 O  O     . GLU C 182 ? 1.0380 1.7736 1.6484 0.1779  0.1000  0.1813  175 GLU C O     
5798 C  CB    . GLU C 182 ? 1.0862 1.7618 1.6029 0.2257  0.1820  0.1580  175 GLU C CB    
5799 N  N     . ASP C 183 ? 1.0878 1.9211 1.7668 0.1718  0.1400  0.2102  176 ASP C N     
5800 C  CA    . ASP C 183 ? 1.0613 1.9193 1.7750 0.1262  0.1092  0.2219  176 ASP C CA    
5801 C  C     . ASP C 183 ? 1.0277 1.8546 1.7077 0.0955  0.1169  0.2155  176 ASP C C     
5802 O  O     . ASP C 183 ? 1.0552 1.9078 1.7427 0.1007  0.1483  0.2244  176 ASP C O     
5803 C  CB    . ASP C 183 ? 1.1161 2.0736 1.9218 0.1228  0.1074  0.2540  176 ASP C CB    
5804 C  CG    . ASP C 183 ? 1.1069 2.0897 1.9522 0.0765  0.0676  0.2672  176 ASP C CG    
5805 O  OD1   . ASP C 183 ? 1.0585 1.9779 1.8554 0.0477  0.0433  0.2502  176 ASP C OD1   
5806 O  OD2   . ASP C 183 ? 1.1560 2.2219 2.0803 0.0701  0.0605  0.2948  176 ASP C OD2   
5807 N  N     . MET C 184 ? 0.9754 1.7466 1.6165 0.0654  0.0890  0.2009  177 MET C N     
5808 C  CA    . MET C 184 ? 0.9441 1.6760 1.5463 0.0394  0.0936  0.1928  177 MET C CA    
5809 C  C     . MET C 184 ? 0.9416 1.6890 1.5727 -0.0048 0.0650  0.2047  177 MET C C     
5810 O  O     . MET C 184 ? 0.9160 1.6214 1.5118 -0.0292 0.0601  0.1967  177 MET C O     
5811 C  CB    . MET C 184 ? 0.8920 1.5387 1.4180 0.0432  0.0869  0.1645  177 MET C CB    
5812 C  CG    . MET C 184 ? 0.9002 1.5165 1.3860 0.0812  0.1122  0.1502  177 MET C CG    
5813 S  SD    . MET C 184 ? 0.8433 1.3660 1.2470 0.0771  0.1015  0.1211  177 MET C SD    
5814 C  CE    . MET C 184 ? 0.8730 1.3682 1.2474 0.1208  0.1164  0.1090  177 MET C CE    
5815 N  N     . ASN C 185 ? 0.9775 1.7843 1.6726 -0.0152 0.0455  0.2248  178 ASN C N     
5816 C  CA    . ASN C 185 ? 0.9827 1.7886 1.6946 -0.0570 0.0082  0.2315  178 ASN C CA    
5817 C  C     . ASN C 185 ? 1.0018 1.8214 1.7282 -0.0901 0.0153  0.2455  178 ASN C C     
5818 O  O     . ASN C 185 ? 0.9900 1.7623 1.6864 -0.1230 -0.0082 0.2380  178 ASN C O     
5819 C  CB    . ASN C 185 ? 1.0245 1.8880 1.7987 -0.0610 -0.0190 0.2493  178 ASN C CB    
5820 C  CG    . ASN C 185 ? 1.0050 1.8259 1.7466 -0.0517 -0.0484 0.2326  178 ASN C CG    
5821 O  OD1   . ASN C 185 ? 0.9787 1.7369 1.6704 -0.0716 -0.0720 0.2157  178 ASN C OD1   
5822 N  ND2   . ASN C 185 ? 1.0257 1.8803 1.7948 -0.0208 -0.0473 0.2384  178 ASN C ND2   
5823 N  N     . ASP C 186 ? 1.0395 1.9210 1.8092 -0.0809 0.0479  0.2664  179 ASP C N     
5824 C  CA    . ASP C 186 ? 1.0652 1.9612 1.8478 -0.1107 0.0589  0.2825  179 ASP C CA    
5825 C  C     . ASP C 186 ? 1.0213 1.8369 1.7255 -0.1127 0.0687  0.2599  179 ASP C C     
5826 O  O     . ASP C 186 ? 1.0177 1.7947 1.7003 -0.1460 0.0501  0.2579  179 ASP C O     
5827 C  CB    . ASP C 186 ? 1.1189 2.0970 1.9579 -0.0955 0.0970  0.3094  179 ASP C CB    
5828 C  CG    . ASP C 186 ? 1.1780 2.2502 2.1106 -0.1074 0.0858  0.3414  179 ASP C CG    
5829 O  OD1   . ASP C 186 ? 1.1867 2.2607 2.1435 -0.1398 0.0440  0.3465  179 ASP C OD1   
5830 O  OD2   . ASP C 186 ? 1.2223 2.3664 2.2029 -0.0834 0.1191  0.3616  179 ASP C OD2   
5831 N  N     . HIS C 187 ? 0.9942 1.7814 1.6540 -0.0764 0.0958  0.2425  180 HIS C N     
5832 C  CA    . HIS C 187 ? 0.9585 1.6765 1.5474 -0.0749 0.1066  0.2228  180 HIS C CA    
5833 C  C     . HIS C 187 ? 0.9148 1.5650 1.4605 -0.0965 0.0727  0.2038  180 HIS C C     
5834 O  O     . HIS C 187 ? 0.9050 1.5137 1.4154 -0.1147 0.0713  0.1989  180 HIS C O     
5835 C  CB    . HIS C 187 ? 0.9468 1.6450 1.4966 -0.0329 0.1353  0.2068  180 HIS C CB    
5836 C  CG    . HIS C 187 ? 1.0002 1.7477 1.5714 -0.0140 0.1747  0.2233  180 HIS C CG    
5837 N  ND1   . HIS C 187 ? 1.0194 1.7564 1.5654 -0.0227 0.1965  0.2286  180 HIS C ND1   
5838 C  CD2   . HIS C 187 ? 1.0458 1.8518 1.6577 0.0148  0.1971  0.2361  180 HIS C CD2   
5839 C  CE1   . HIS C 187 ? 1.0766 1.8647 1.6458 -0.0003 0.2322  0.2441  180 HIS C CE1   
5840 N  NE2   . HIS C 187 ? 1.0936 1.9248 1.7039 0.0237  0.2339  0.2487  180 HIS C NE2   
5841 N  N     . LEU C 188 ? 0.8969 1.5370 1.4452 -0.0933 0.0462  0.1945  181 LEU C N     
5842 C  CA    . LEU C 188 ? 0.8678 1.4477 1.3763 -0.1117 0.0148  0.1777  181 LEU C CA    
5843 C  C     . LEU C 188 ? 0.9038 1.4862 1.4329 -0.1525 -0.0102 0.1907  181 LEU C C     
5844 O  O     . LEU C 188 ? 0.8924 1.4175 1.3783 -0.1693 -0.0243 0.1788  181 LEU C O     
5845 C  CB    . LEU C 188 ? 0.8516 1.4227 1.3559 -0.0959 -0.0046 0.1667  181 LEU C CB    
5846 C  CG    . LEU C 188 ? 0.8037 1.3198 1.2497 -0.0706 0.0030  0.1425  181 LEU C CG    
5847 C  CD1   . LEU C 188 ? 0.7738 1.2244 1.1660 -0.0867 -0.0108 0.1258  181 LEU C CD1   
5848 C  CD2   . LEU C 188 ? 0.7978 1.3181 1.2305 -0.0439 0.0388  0.1398  181 LEU C CD2   
5849 N  N     . ASN C 189 ? 0.9545 1.6022 1.5494 -0.1682 -0.0168 0.2155  182 ASN C N     
5850 C  CA    . ASN C 189 ? 1.0020 1.6521 1.6196 -0.2103 -0.0458 0.2293  182 ASN C CA    
5851 C  C     . ASN C 189 ? 1.0181 1.6457 1.6178 -0.2315 -0.0329 0.2360  182 ASN C C     
5852 O  O     . ASN C 189 ? 1.0456 1.6333 1.6281 -0.2631 -0.0582 0.2355  182 ASN C O     
5853 C  CB    . ASN C 189 ? 1.0584 1.7908 1.7572 -0.2236 -0.0565 0.2572  182 ASN C CB    
5854 C  CG    . ASN C 189 ? 1.0625 1.8033 1.7751 -0.2179 -0.0875 0.2522  182 ASN C CG    
5855 O  OD1   . ASN C 189 ? 1.0324 1.7112 1.6912 -0.2122 -0.1065 0.2286  182 ASN C OD1   
5856 N  ND2   . ASN C 189 ? 1.1062 1.9258 1.8919 -0.2195 -0.0930 0.2760  182 ASN C ND2   
5857 N  N     . ALA C 190 ? 1.0102 1.6595 1.6101 -0.2132 0.0056  0.2422  183 ALA C N     
5858 C  CA    . ALA C 190 ? 1.0254 1.6495 1.6005 -0.2285 0.0206  0.2479  183 ALA C CA    
5859 C  C     . ALA C 190 ? 0.9791 1.5180 1.4779 -0.2218 0.0150  0.2207  183 ALA C C     
5860 O  O     . ALA C 190 ? 0.9986 1.4920 1.4718 -0.2469 -0.0012 0.2197  183 ALA C O     
5861 C  CB    . ALA C 190 ? 1.0390 1.7109 1.6318 -0.2079 0.0633  0.2620  183 ALA C CB    
5862 N  N     . LEU C 191 ? 0.9251 1.4434 1.3893 -0.1877 0.0282  0.1997  184 LEU C N     
5863 C  CA    . LEU C 191 ? 0.8819 1.3321 1.2800 -0.1767 0.0300  0.1769  184 LEU C CA    
5864 C  C     . LEU C 191 ? 0.8724 1.2676 1.2404 -0.1915 -0.0036 0.1619  184 LEU C C     
5865 O  O     . LEU C 191 ? 0.8646 1.2063 1.1883 -0.1965 -0.0074 0.1517  184 LEU C O     
5866 C  CB    . LEU C 191 ? 0.8379 1.2856 1.2142 -0.1396 0.0489  0.1608  184 LEU C CB    
5867 C  CG    . LEU C 191 ? 0.8530 1.3323 1.2339 -0.1191 0.0852  0.1689  184 LEU C CG    
5868 C  CD1   . LEU C 191 ? 0.8282 1.3094 1.1971 -0.0839 0.0979  0.1549  184 LEU C CD1   
5869 C  CD2   . LEU C 191 ? 0.8535 1.2941 1.1890 -0.1223 0.0985  0.1655  184 LEU C CD2   
5870 N  N     . GLN C 192 ? 0.8800 1.2886 1.2705 -0.1962 -0.0272 0.1608  185 GLN C N     
5871 C  CA    . GLN C 192 ? 0.8853 1.2445 1.2465 -0.2085 -0.0597 0.1469  185 GLN C CA    
5872 C  C     . GLN C 192 ? 0.8389 1.1369 1.1381 -0.1900 -0.0567 0.1228  185 GLN C C     
5873 O  O     . GLN C 192 ? 0.8537 1.0994 1.1161 -0.2016 -0.0706 0.1143  185 GLN C O     
5874 C  CB    . GLN C 192 ? 0.9474 1.2873 1.3128 -0.2451 -0.0820 0.1579  185 GLN C CB    
5875 C  CG    . GLN C 192 ? 1.0033 1.4008 1.4320 -0.2695 -0.0965 0.1814  185 GLN C CG    
5876 C  CD    . GLN C 192 ? 1.0694 1.4284 1.4885 -0.3051 -0.1335 0.1835  185 GLN C CD    
5877 O  OE1   . GLN C 192 ? 1.0996 1.4138 1.4903 -0.3225 -0.1367 0.1840  185 GLN C OE1   
5878 N  NE2   . GLN C 192 ? 1.0998 1.4703 1.5372 -0.3153 -0.1634 0.1839  185 GLN C NE2   
5879 N  N     . PRO C 193 ? 0.7890 1.0906 1.0750 -0.1608 -0.0403 0.1112  186 PRO C N     
5880 C  CA    . PRO C 193 ? 0.7512 1.0019 0.9865 -0.1458 -0.0435 0.0900  186 PRO C CA    
5881 C  C     . PRO C 193 ? 0.7687 0.9892 0.9861 -0.1533 -0.0722 0.0806  186 PRO C C     
5882 O  O     . PRO C 193 ? 0.7941 1.0400 1.0393 -0.1603 -0.0886 0.0871  186 PRO C O     
5883 C  CB    . PRO C 193 ? 0.7119 0.9816 0.9488 -0.1180 -0.0256 0.0842  186 PRO C CB    
5884 C  CG    . PRO C 193 ? 0.7358 1.0646 1.0253 -0.1171 -0.0207 0.1005  186 PRO C CG    
5885 C  CD    . PRO C 193 ? 0.7756 1.1273 1.0927 -0.1404 -0.0182 0.1184  186 PRO C CD    
5886 N  N     . PHE C 194 ? 0.7632 0.9301 0.9334 -0.1511 -0.0784 0.0661  187 PHE C N     
5887 C  CA    . PHE C 194 ? 0.7869 0.9183 0.9288 -0.1537 -0.1020 0.0549  187 PHE C CA    
5888 C  C     . PHE C 194 ? 0.7534 0.8922 0.8882 -0.1323 -0.0995 0.0465  187 PHE C C     
5889 O  O     . PHE C 194 ? 0.7784 0.9023 0.8990 -0.1333 -0.1190 0.0410  187 PHE C O     
5890 C  CB    . PHE C 194 ? 0.8001 0.8735 0.8932 -0.1535 -0.1055 0.0429  187 PHE C CB    
5891 C  CG    . PHE C 194 ? 0.7529 0.8080 0.8146 -0.1290 -0.0905 0.0297  187 PHE C CG    
5892 C  CD1   . PHE C 194 ? 0.7078 0.7758 0.7728 -0.1171 -0.0673 0.0309  187 PHE C CD1   
5893 C  CD2   . PHE C 194 ? 0.7605 0.7875 0.7896 -0.1186 -0.1000 0.0173  187 PHE C CD2   
5894 C  CE1   . PHE C 194 ? 0.6707 0.7252 0.7113 -0.0980 -0.0562 0.0207  187 PHE C CE1   
5895 C  CE2   . PHE C 194 ? 0.7224 0.7381 0.7277 -0.0982 -0.0855 0.0082  187 PHE C CE2   
5896 C  CZ    . PHE C 194 ? 0.6767 0.7077 0.6906 -0.0892 -0.0646 0.0105  187 PHE C CZ    
5897 N  N     . ARG C 195 ? 0.7054 0.8631 0.8462 -0.1136 -0.0764 0.0457  188 ARG C N     
5898 C  CA    . ARG C 195 ? 0.6781 0.8375 0.8094 -0.0938 -0.0726 0.0387  188 ARG C CA    
5899 C  C     . ARG C 195 ? 0.6529 0.8490 0.8115 -0.0799 -0.0521 0.0451  188 ARG C C     
5900 O  O     . ARG C 195 ? 0.6357 0.8328 0.7917 -0.0769 -0.0340 0.0457  188 ARG C O     
5901 C  CB    . ARG C 195 ? 0.6529 0.7730 0.7407 -0.0825 -0.0657 0.0254  188 ARG C CB    
5902 C  CG    . ARG C 195 ? 0.6327 0.7494 0.7069 -0.0653 -0.0627 0.0195  188 ARG C CG    
5903 C  CD    . ARG C 195 ? 0.6221 0.7032 0.6571 -0.0589 -0.0589 0.0092  188 ARG C CD    
5904 N  NE    . ARG C 195 ? 0.6105 0.6858 0.6301 -0.0456 -0.0562 0.0055  188 ARG C NE    
5905 C  CZ    . ARG C 195 ? 0.6371 0.7045 0.6444 -0.0437 -0.0699 0.0043  188 ARG C CZ    
5906 N  NH1   . ARG C 195 ? 0.6783 0.7415 0.6860 -0.0548 -0.0893 0.0053  188 ARG C NH1   
5907 N  NH2   . ARG C 195 ? 0.6293 0.6914 0.6225 -0.0321 -0.0653 0.0031  188 ARG C NH2   
5908 N  N     . TRP C 196 ? 0.6598 0.8828 0.8411 -0.0704 -0.0555 0.0499  189 TRP C N     
5909 C  CA    . TRP C 196 ? 0.6495 0.9034 0.8535 -0.0533 -0.0357 0.0552  189 TRP C CA    
5910 C  C     . TRP C 196 ? 0.6373 0.8783 0.8243 -0.0334 -0.0349 0.0481  189 TRP C C     
5911 O  O     . TRP C 196 ? 0.6568 0.9062 0.8534 -0.0310 -0.0506 0.0512  189 TRP C O     
5912 C  CB    . TRP C 196 ? 0.6833 0.9894 0.9396 -0.0586 -0.0382 0.0719  189 TRP C CB    
5913 C  CG    . TRP C 196 ? 0.6867 1.0260 0.9665 -0.0358 -0.0177 0.0778  189 TRP C CG    
5914 C  CD1   . TRP C 196 ? 0.6691 0.9936 0.9264 -0.0182 0.0051  0.0705  189 TRP C CD1   
5915 C  CD2   . TRP C 196 ? 0.7189 1.1086 1.0459 -0.0262 -0.0182 0.0918  189 TRP C CD2   
5916 N  NE1   . TRP C 196 ? 0.6915 1.0471 0.9727 0.0030  0.0198  0.0771  189 TRP C NE1   
5917 C  CE2   . TRP C 196 ? 0.7205 1.1195 1.0473 0.0000  0.0073  0.0909  189 TRP C CE2   
5918 C  CE3   . TRP C 196 ? 0.7533 1.1814 1.1228 -0.0369 -0.0388 0.1054  189 TRP C CE3   
5919 C  CZ2   . TRP C 196 ? 0.7552 1.2003 1.1224 0.0193  0.0156  0.1030  189 TRP C CZ2   
5920 C  CZ3   . TRP C 196 ? 0.7829 1.2626 1.1981 -0.0197 -0.0321 0.1190  189 TRP C CZ3   
5921 C  CH2   . TRP C 196 ? 0.7835 1.2716 1.1974 0.0098  -0.0039 0.1177  189 TRP C CH2   
5922 N  N     . LYS C 197 ? 0.6125 0.8320 0.7738 -0.0203 -0.0183 0.0398  190 LYS C N     
5923 C  CA    . LYS C 197 ? 0.6078 0.8091 0.7498 -0.0042 -0.0176 0.0341  190 LYS C CA    
5924 C  C     . LYS C 197 ? 0.6273 0.8511 0.7900 0.0148  -0.0057 0.0394  190 LYS C C     
5925 O  O     . LYS C 197 ? 0.6302 0.8619 0.7963 0.0216  0.0123  0.0398  190 LYS C O     
5926 C  CB    . LYS C 197 ? 0.5824 0.7482 0.6874 -0.0014 -0.0081 0.0238  190 LYS C CB    
5927 C  CG    . LYS C 197 ? 0.5663 0.7089 0.6485 -0.0148 -0.0152 0.0182  190 LYS C CG    
5928 C  CD    . LYS C 197 ? 0.5793 0.7100 0.6501 -0.0194 -0.0328 0.0170  190 LYS C CD    
5929 C  CE    . LYS C 197 ? 0.5796 0.6914 0.6283 -0.0093 -0.0337 0.0140  190 LYS C CE    
5930 N  NZ    . LYS C 197 ? 0.5601 0.6485 0.5820 -0.0094 -0.0252 0.0081  190 LYS C NZ    
5931 N  N     . CYS C 198 ? 0.6487 0.8801 0.8215 0.0254  -0.0161 0.0434  191 CYS C N     
5932 C  CA    . CYS C 198 ? 0.6759 0.9213 0.8628 0.0487  -0.0053 0.0475  191 CYS C CA    
5933 C  C     . CYS C 198 ? 0.6823 0.8899 0.8371 0.0616  -0.0081 0.0411  191 CYS C C     
5934 O  O     . CYS C 198 ? 0.6926 0.8938 0.8433 0.0610  -0.0251 0.0437  191 CYS C O     
5935 C  CB    . CYS C 198 ? 0.7086 1.0006 0.9418 0.0532  -0.0150 0.0614  191 CYS C CB    
5936 S  SG    . CYS C 198 ? 0.7152 1.0584 0.9941 0.0372  -0.0094 0.0735  191 CYS C SG    
5937 N  N     . PHE C 199 ? 0.6844 0.8649 0.8138 0.0720  0.0074  0.0336  192 PHE C N     
5938 C  CA    . PHE C 199 ? 0.6956 0.8347 0.7916 0.0797  0.0046  0.0281  192 PHE C CA    
5939 C  C     . PHE C 199 ? 0.7450 0.8848 0.8482 0.1056  0.0101  0.0318  192 PHE C C     
5940 O  O     . PHE C 199 ? 0.7672 0.9179 0.8785 0.1195  0.0264  0.0311  192 PHE C O     
5941 C  CB    . PHE C 199 ? 0.6825 0.7857 0.7437 0.0743  0.0146  0.0180  192 PHE C CB    
5942 C  CG    . PHE C 199 ? 0.6399 0.7444 0.6954 0.0535  0.0141  0.0144  192 PHE C CG    
5943 C  CD1   . PHE C 199 ? 0.6165 0.7135 0.6632 0.0395  0.0019  0.0143  192 PHE C CD1   
5944 C  CD2   . PHE C 199 ? 0.6316 0.7428 0.6874 0.0501  0.0265  0.0115  192 PHE C CD2   
5945 C  CE1   . PHE C 199 ? 0.5861 0.6830 0.6272 0.0242  0.0020  0.0112  192 PHE C CE1   
5946 C  CE2   . PHE C 199 ? 0.5988 0.7091 0.6487 0.0329  0.0250  0.0092  192 PHE C CE2   
5947 C  CZ    . PHE C 199 ? 0.5763 0.6795 0.6201 0.0209  0.0128  0.0089  192 PHE C CZ    
5948 N  N     . GLN C 200 ? 0.7689 0.8959 0.8667 0.1134  -0.0029 0.0361  193 GLN C N     
5949 C  CA    . GLN C 200 ? 0.8233 0.9315 0.9133 0.1392  0.0020  0.0373  193 GLN C CA    
5950 C  C     . GLN C 200 ? 0.8322 0.8930 0.8817 0.1395  0.0136  0.0259  193 GLN C C     
5951 O  O     . GLN C 200 ? 0.8104 0.8409 0.8325 0.1222  0.0075  0.0215  193 GLN C O     
5952 C  CB    . GLN C 200 ? 0.8512 0.9424 0.9324 0.1451  -0.0152 0.0440  193 GLN C CB    
5953 C  CG    . GLN C 200 ? 0.9168 0.9777 0.9832 0.1728  -0.0105 0.0449  193 GLN C CG    
5954 C  CD    . GLN C 200 ? 0.9529 0.9990 1.0126 0.1804  -0.0282 0.0542  193 GLN C CD    
5955 O  OE1   . GLN C 200 ? 0.9300 0.9781 0.9848 0.1630  -0.0435 0.0583  193 GLN C OE1   
5956 N  NE2   . GLN C 200 ? 1.0188 1.0457 1.0736 0.2083  -0.0259 0.0577  193 GLN C NE2   
5957 N  N     . VAL C 201 ? 0.8706 0.9267 0.9164 0.1589  0.0303  0.0217  194 VAL C N     
5958 C  CA    . VAL C 201 ? 0.8953 0.9012 0.8979 0.1596  0.0385  0.0100  194 VAL C CA    
5959 C  C     . VAL C 201 ? 0.9166 0.8727 0.8871 0.1545  0.0250  0.0093  194 VAL C C     
5960 O  O     . VAL C 201 ? 0.9436 0.8967 0.9202 0.1656  0.0154  0.0171  194 VAL C O     
5961 C  CB    . VAL C 201 ? 0.9599 0.9591 0.9555 0.1886  0.0569  0.0058  194 VAL C CB    
5962 C  CG1   . VAL C 201 ? 1.0253 1.0164 1.0260 0.2186  0.0556  0.0114  194 VAL C CG1   
5963 C  CG2   . VAL C 201 ? 0.9902 0.9361 0.9364 0.1856  0.0635  -0.0079 194 VAL C CG2   
5964 N  N     . LEU C 202 ? 0.9077 0.8271 0.8457 0.1361  0.0231  0.0018  195 LEU C N     
5965 C  CA    . LEU C 202 ? 0.9170 0.7992 0.8310 0.1225  0.0100  0.0045  195 LEU C CA    
5966 C  C     . LEU C 202 ? 0.9716 0.7952 0.8435 0.1200  0.0099  -0.0032 195 LEU C C     
5967 O  O     . LEU C 202 ? 0.9656 0.7807 0.8236 0.1106  0.0152  -0.0118 195 LEU C O     
5968 C  CB    . LEU C 202 ? 0.8486 0.7520 0.7712 0.0950  0.0040  0.0071  195 LEU C CB    
5969 C  CG    . LEU C 202 ? 0.8556 0.7296 0.7569 0.0783  -0.0061 0.0122  195 LEU C CG    
5970 C  CD1   . LEU C 202 ? 0.8740 0.7498 0.7800 0.0859  -0.0156 0.0228  195 LEU C CD1   
5971 C  CD2   . LEU C 202 ? 0.7985 0.6911 0.7044 0.0544  -0.0067 0.0125  195 LEU C CD2   
5972 N  N     . ILE C 203 ? 1.0294 0.8096 0.8787 0.1251  0.0011  0.0007  196 ILE C N     
5973 C  CA    . ILE C 203 ? 1.0879 0.8069 0.8956 0.1157  -0.0040 -0.0047 196 ILE C CA    
5974 C  C     . ILE C 203 ? 1.0482 0.7680 0.8543 0.0825  -0.0134 0.0015  196 ILE C C     
5975 O  O     . ILE C 203 ? 1.0204 0.7587 0.8406 0.0749  -0.0189 0.0125  196 ILE C O     
5976 C  CB    . ILE C 203 ? 1.1820 0.8465 0.9622 0.1349  -0.0097 -0.0024 196 ILE C CB    
5977 C  CG1   . ILE C 203 ? 1.2285 0.8980 1.0150 0.1735  0.0012  -0.0063 196 ILE C CG1   
5978 C  CG2   . ILE C 203 ? 1.2524 0.8479 0.9865 0.1208  -0.0177 -0.0085 196 ILE C CG2   
5979 C  CD1   . ILE C 203 ? 1.2584 0.9176 1.0279 0.1864  0.0153  -0.0208 196 ILE C CD1   
5980 N  N     . VAL C 204 ? 1.0550 0.7545 0.8425 0.0643  -0.0151 -0.0052 197 VAL C N     
5981 C  CA    . VAL C 204 ? 1.0347 0.7325 0.8204 0.0334  -0.0236 0.0013  197 VAL C CA    
5982 C  C     . VAL C 204 ? 1.1203 0.7543 0.8670 0.0231  -0.0336 -0.0021 197 VAL C C     
5983 O  O     . VAL C 204 ? 1.1526 0.7641 0.8782 0.0264  -0.0325 -0.0147 197 VAL C O     
5984 C  CB    . VAL C 204 ? 0.9634 0.7039 0.7688 0.0189  -0.0188 -0.0021 197 VAL C CB    
5985 C  CG1   . VAL C 204 ? 0.9509 0.6935 0.7576 -0.0107 -0.0268 0.0056  197 VAL C CG1   
5986 C  CG2   . VAL C 204 ? 0.8903 0.6865 0.7299 0.0277  -0.0107 0.0003  197 VAL C CG2   
5987 N  N     . THR C 205 ? 1.1635 0.7671 0.8984 0.0102  -0.0439 0.0093  198 THR C N     
5988 C  CA    . THR C 205 ? 1.2536 0.7932 0.9520 -0.0055 -0.0571 0.0088  198 THR C CA    
5989 C  C     . THR C 205 ? 1.2429 0.7870 0.9383 -0.0292 -0.0622 0.0028  198 THR C C     
5990 O  O     . THR C 205 ? 1.1674 0.7643 0.8939 -0.0453 -0.0592 0.0089  198 THR C O     
5991 C  CB    . THR C 205 ? 1.2877 0.8083 0.9830 -0.0244 -0.0667 0.0270  198 THR C CB    
5992 O  OG1   . THR C 205 ? 1.2045 0.7864 0.9357 -0.0312 -0.0596 0.0392  198 THR C OG1   
5993 C  CG2   . THR C 205 ? 1.3680 0.8373 1.0378 -0.0041 -0.0706 0.0301  198 THR C CG2   
5994 N  N     . GLY C 206 ? 1.3271 0.8131 0.9821 -0.0290 -0.0705 -0.0095 199 GLY C N     
5995 C  CA    . GLY C 206 ? 1.3415 0.8196 0.9849 -0.0526 -0.0806 -0.0152 199 GLY C CA    
5996 C  C     . GLY C 206 ? 1.2856 0.8011 0.9377 -0.0400 -0.0691 -0.0278 199 GLY C C     
5997 O  O     . GLY C 206 ? 1.2954 0.8081 0.9377 -0.0573 -0.0775 -0.0327 199 GLY C O     
5998 N  N     . GLU C 207 ? 1.2327 0.7837 0.9039 -0.0115 -0.0512 -0.0313 200 GLU C N     
5999 C  CA    . GLU C 207 ? 1.1852 0.7719 0.8656 -0.0001 -0.0389 -0.0407 200 GLU C CA    
6000 C  C     . GLU C 207 ? 1.2426 0.8013 0.8958 0.0338  -0.0266 -0.0539 200 GLU C C     
6001 O  O     . GLU C 207 ? 1.2872 0.8225 0.9090 0.0390  -0.0247 -0.0665 200 GLU C O     
6002 C  CB    . GLU C 207 ? 1.0744 0.7346 0.8054 -0.0008 -0.0285 -0.0313 200 GLU C CB    
6003 C  CG    . GLU C 207 ? 1.0231 0.7148 0.7785 -0.0304 -0.0369 -0.0200 200 GLU C CG    
6004 C  CD    . GLU C 207 ? 1.0026 0.7113 0.7590 -0.0449 -0.0404 -0.0239 200 GLU C CD    
6005 O  OE1   . GLU C 207 ? 1.0273 0.7218 0.7619 -0.0334 -0.0362 -0.0359 200 GLU C OE1   
6006 O  OE2   . GLU C 207 ? 0.9670 0.7043 0.7458 -0.0666 -0.0467 -0.0138 200 GLU C OE2   
6007 N  N     . ASN C 208 ? 1.2491 0.8107 0.9130 0.0582  -0.0183 -0.0504 201 ASN C N     
6008 C  CA    . ASN C 208 ? 1.2956 0.8471 0.9459 0.0947  -0.0027 -0.0598 201 ASN C CA    
6009 C  C     . ASN C 208 ? 1.3673 0.8790 1.0034 0.1178  -0.0040 -0.0576 201 ASN C C     
6010 O  O     . ASN C 208 ? 1.3767 0.9075 1.0260 0.1502  0.0105  -0.0580 201 ASN C O     
6011 C  CB    . ASN C 208 ? 1.2100 0.8356 0.9063 0.1080  0.0146  -0.0558 201 ASN C CB    
6012 C  CG    . ASN C 208 ? 1.1381 0.8111 0.8806 0.1054  0.0132  -0.0415 201 ASN C CG    
6013 O  OD1   . ASN C 208 ? 1.1520 0.8043 0.8920 0.0971  0.0015  -0.0337 201 ASN C OD1   
6014 N  ND2   . ASN C 208 ? 1.0693 0.8035 0.8516 0.1118  0.0240  -0.0372 201 ASN C ND2   
6015 N  N     . ASP C 209 ? 1.4258 0.8826 1.0355 0.1015  -0.0214 -0.0540 202 ASP C N     
6016 C  CA    . ASP C 209 ? 1.4755 0.9033 1.0808 0.1167  -0.0257 -0.0460 202 ASP C CA    
6017 C  C     . ASP C 209 ? 1.6167 0.9536 1.1623 0.1334  -0.0319 -0.0566 202 ASP C C     
6018 O  O     . ASP C 209 ? 1.6743 0.9772 1.2101 0.1482  -0.0366 -0.0501 202 ASP C O     
6019 C  CB    . ASP C 209 ? 1.4366 0.8746 1.0612 0.0864  -0.0397 -0.0289 202 ASP C CB    
6020 C  CG    . ASP C 209 ? 1.4824 0.8743 1.0792 0.0503  -0.0578 -0.0272 202 ASP C CG    
6021 O  OD1   . ASP C 209 ? 1.4413 0.8556 1.0446 0.0280  -0.0601 -0.0308 202 ASP C OD1   
6022 O  OD2   . ASP C 209 ? 1.5624 0.8979 1.1332 0.0434  -0.0706 -0.0206 202 ASP C OD2   
6023 N  N     . SER C 210 ? 1.6824 0.9743 1.1835 0.1314  -0.0337 -0.0727 203 SER C N     
6024 C  CA    . SER C 210 ? 1.8316 1.0281 1.2672 0.1484  -0.0404 -0.0854 203 SER C CA    
6025 C  C     . SER C 210 ? 1.8890 1.0562 1.2805 0.1566  -0.0345 -0.1054 203 SER C C     
6026 O  O     . SER C 210 ? 1.8083 1.0351 1.2253 0.1527  -0.0230 -0.1074 203 SER C O     
6027 C  CB    . SER C 210 ? 1.8989 1.0303 1.3062 0.1163  -0.0663 -0.0785 203 SER C CB    
6028 O  OG    . SER C 210 ? 1.8831 1.0119 1.2836 0.0742  -0.0821 -0.0794 203 SER C OG    
6029 N  N     . ASP C 211 ? 2.0378 1.1087 1.3587 0.1683  -0.0432 -0.1201 204 ASP C N     
6030 C  CA    . ASP C 211 ? 2.1188 1.1457 1.3831 0.1749  -0.0411 -0.1406 204 ASP C CA    
6031 C  C     . ASP C 211 ? 2.1363 1.1309 1.3757 0.1258  -0.0689 -0.1427 204 ASP C C     
6032 O  O     . ASP C 211 ? 2.2043 1.1610 1.3942 0.1239  -0.0728 -0.1589 204 ASP C O     
6033 C  CB    . ASP C 211 ? 2.2859 1.2201 1.4795 0.2158  -0.0360 -0.1573 204 ASP C CB    
6034 C  CG    . ASP C 211 ? 2.2813 1.2506 1.5017 0.2678  -0.0079 -0.1540 204 ASP C CG    
6035 O  OD1   . ASP C 211 ? 2.1944 1.2456 1.4580 0.2847  0.0163  -0.1515 204 ASP C OD1   
6036 O  OD2   . ASP C 211 ? 2.3691 1.2847 1.5689 0.2905  -0.0116 -0.1525 204 ASP C OD2   
6037 N  N     . LYS C 212 ? 2.0850 1.0942 1.3573 0.0867  -0.0885 -0.1254 205 LYS C N     
6038 C  CA    . LYS C 212 ? 2.0772 1.0821 1.3470 0.0377  -0.1133 -0.1217 205 LYS C CA    
6039 C  C     . LYS C 212 ? 1.9414 1.0392 1.2615 0.0259  -0.1028 -0.1172 205 LYS C C     
6040 O  O     . LYS C 212 ? 1.9581 1.0490 1.2582 0.0047  -0.1148 -0.1240 205 LYS C O     
6041 C  CB    . LYS C 212 ? 2.0741 1.0697 1.3660 0.0023  -0.1340 -0.1020 205 LYS C CB    
6042 C  CG    . LYS C 212 ? 2.2370 1.1218 1.4657 -0.0061 -0.1572 -0.1064 205 LYS C CG    
6043 C  CD    . LYS C 212 ? 2.3267 1.1535 1.5198 0.0396  -0.1452 -0.1144 205 LYS C CD    
6044 C  CE    . LYS C 212 ? 2.5081 1.2118 1.6271 0.0320  -0.1699 -0.1219 205 LYS C CE    
6045 N  NZ    . LYS C 212 ? 2.5176 1.2076 1.6546 -0.0133 -0.1939 -0.0999 205 LYS C NZ    
6046 N  N     . THR C 213 ? 1.8162 0.9971 1.1984 0.0402  -0.0819 -0.1059 206 THR C N     
6047 C  CA    . THR C 213 ? 1.6900 0.9563 1.1210 0.0301  -0.0719 -0.1003 206 THR C CA    
6048 C  C     . THR C 213 ? 1.7062 0.9779 1.1132 0.0561  -0.0543 -0.1158 206 THR C C     
6049 O  O     . THR C 213 ? 1.8095 1.0257 1.1662 0.0861  -0.0462 -0.1304 206 THR C O     
6050 C  CB    . THR C 213 ? 1.5674 0.9113 1.0658 0.0354  -0.0580 -0.0837 206 THR C CB    
6051 O  OG1   . THR C 213 ? 1.5895 0.9298 1.0870 0.0753  -0.0402 -0.0870 206 THR C OG1   
6052 C  CG2   . THR C 213 ? 1.5449 0.8926 1.0677 0.0063  -0.0736 -0.0664 206 THR C CG2   
6053 N  N     . LEU C 214 ? 1.6111 0.9484 1.0521 0.0451  -0.0477 -0.1118 207 LEU C N     
6054 C  CA    . LEU C 214 ? 1.6227 0.9707 1.0431 0.0649  -0.0312 -0.1233 207 LEU C CA    
6055 C  C     . LEU C 214 ? 1.5956 0.9806 1.0393 0.1048  -0.0014 -0.1227 207 LEU C C     
6056 O  O     . LEU C 214 ? 1.6478 1.0232 1.0615 0.1311  0.0162  -0.1335 207 LEU C O     
6057 C  CB    . LEU C 214 ? 1.5329 0.9382 0.9845 0.0394  -0.0352 -0.1165 207 LEU C CB    
6058 C  CG    . LEU C 214 ? 1.5758 0.9484 1.0011 0.0032  -0.0641 -0.1178 207 LEU C CG    
6059 C  CD1   . LEU C 214 ? 1.4825 0.9193 0.9458 -0.0166 -0.0661 -0.1088 207 LEU C CD1   
6060 C  CD2   . LEU C 214 ? 1.7186 1.0094 1.0630 0.0108  -0.0730 -0.1370 207 LEU C CD2   
6061 N  N     . ARG C 215 ? 1.5226 0.9501 1.0186 0.1089  0.0035  -0.1093 208 ARG C N     
6062 C  CA    . ARG C 215 ? 1.5034 0.9676 1.0278 0.1443  0.0270  -0.1058 208 ARG C CA    
6063 C  C     . ARG C 215 ? 1.5441 0.9783 1.0696 0.1579  0.0218  -0.1011 208 ARG C C     
6064 O  O     . ARG C 215 ? 1.5553 0.9575 1.0739 0.1341  0.0012  -0.0962 208 ARG C O     
6065 C  CB    . ARG C 215 ? 1.3710 0.9255 0.9632 0.1365  0.0369  -0.0921 208 ARG C CB    
6066 C  CG    . ARG C 215 ? 1.3324 0.9213 0.9275 0.1287  0.0456  -0.0946 208 ARG C CG    
6067 C  CD    . ARG C 215 ? 1.4070 0.9835 0.9698 0.1604  0.0676  -0.1048 208 ARG C CD    
6068 N  NE    . ARG C 215 ? 1.3735 0.9858 0.9400 0.1544  0.0782  -0.1044 208 ARG C NE    
6069 C  CZ    . ARG C 215 ? 1.3929 0.9806 0.9246 0.1341  0.0666  -0.1109 208 ARG C CZ    
6070 N  NH1   . ARG C 215 ? 1.4350 0.9691 0.9331 0.1128  0.0417  -0.1169 208 ARG C NH1   
6071 N  NH2   . ARG C 215 ? 1.3725 0.9915 0.9053 0.1332  0.0785  -0.1094 208 ARG C NH2   
6072 N  N     . ASN C 216 ? 1.5706 1.0185 1.1068 0.1966  0.0410  -0.1007 209 ASN C N     
6073 C  CA    . ASN C 216 ? 1.5960 1.0330 1.1455 0.2152  0.0391  -0.0929 209 ASN C CA    
6074 C  C     . ASN C 216 ? 1.5339 1.0484 1.1413 0.2405  0.0587  -0.0823 209 ASN C C     
6075 O  O     . ASN C 216 ? 1.5873 1.1082 1.1891 0.2761  0.0793  -0.0871 209 ASN C O     
6076 C  CB    . ASN C 216 ? 1.7453 1.0950 1.2325 0.2440  0.0389  -0.1054 209 ASN C CB    
6077 C  CG    . ASN C 216 ? 1.7782 1.1164 1.2791 0.2667  0.0370  -0.0959 209 ASN C CG    
6078 O  OD1   . ASN C 216 ? 1.6890 1.0888 1.2467 0.2622  0.0366  -0.0801 209 ASN C OD1   
6079 N  ND2   . ASN C 216 ? 1.9136 1.1698 1.3597 0.2916  0.0345  -0.1055 209 ASN C ND2   
6080 N  N     . ALA C 217 ? 1.4302 1.0037 1.0926 0.2228  0.0524  -0.0672 210 ALA C N     
6081 C  CA    . ALA C 217 ? 1.3635 1.0165 1.0833 0.2373  0.0671  -0.0569 210 ALA C CA    
6082 C  C     . ALA C 217 ? 1.4027 1.0626 1.1428 0.2684  0.0695  -0.0481 210 ALA C C     
6083 O  O     . ALA C 217 ? 1.3466 1.0729 1.1404 0.2749  0.0740  -0.0358 210 ALA C O     
6084 C  CB    . ALA C 217 ? 1.2455 0.9532 1.0078 0.2036  0.0579  -0.0469 210 ALA C CB    
6085 N  N     . HIS C 218 ? 1.5076 1.0966 1.2037 0.2878  0.0648  -0.0541 211 HIS C N     
6086 C  CA    . HIS C 218 ? 1.5448 1.1279 1.2548 0.3097  0.0589  -0.0436 211 HIS C CA    
6087 C  C     . HIS C 218 ? 1.5825 1.2074 1.3222 0.3542  0.0792  -0.0393 211 HIS C C     
6088 O  O     . HIS C 218 ? 1.5740 1.2321 1.3517 0.3685  0.0747  -0.0254 211 HIS C O     
6089 C  CB    . HIS C 218 ? 1.6512 1.1387 1.3024 0.3132  0.0447  -0.0497 211 HIS C CB    
6090 C  CG    . HIS C 218 ? 1.6124 1.0776 1.2576 0.2729  0.0217  -0.0426 211 HIS C CG    
6091 N  ND1   . HIS C 218 ? 1.5293 1.0451 1.2192 0.2573  0.0127  -0.0263 211 HIS C ND1   
6092 C  CD2   . HIS C 218 ? 1.6516 1.0523 1.2526 0.2452  0.0062  -0.0480 211 HIS C CD2   
6093 C  CE1   . HIS C 218 ? 1.5196 1.0035 1.1920 0.2235  -0.0044 -0.0217 211 HIS C CE1   
6094 N  NE2   . HIS C 218 ? 1.5921 1.0083 1.2140 0.2146  -0.0091 -0.0337 211 HIS C NE2   
6095 N  N     . SER C 219 ? 1.6316 1.2556 1.3536 0.3766  0.1013  -0.0500 212 SER C N     
6096 C  CA    . SER C 219 ? 1.6712 1.3438 1.4257 0.4194  0.1248  -0.0441 212 SER C CA    
6097 C  C     . SER C 219 ? 1.5646 1.3395 1.3905 0.4064  0.1331  -0.0303 212 SER C C     
6098 O  O     . SER C 219 ? 1.5858 1.4177 1.4529 0.4365  0.1514  -0.0208 212 SER C O     
6099 C  CB    . SER C 219 ? 1.7779 1.4075 1.4808 0.4501  0.1474  -0.0601 212 SER C CB    
6100 O  OG    . SER C 219 ? 1.7296 1.3746 1.4219 0.4253  0.1551  -0.0677 212 SER C OG    
6101 N  N     . LEU C 220 ? 1.4601 1.2564 1.2995 0.3621  0.1197  -0.0288 213 LEU C N     
6102 C  CA    . LEU C 220 ? 1.3634 1.2441 1.2614 0.3436  0.1241  -0.0175 213 LEU C CA    
6103 C  C     . LEU C 220 ? 1.2902 1.2106 1.2344 0.3246  0.1032  -0.0029 213 LEU C C     
6104 O  O     . LEU C 220 ? 1.2293 1.2207 1.2266 0.3150  0.1051  0.0084  213 LEU C O     
6105 C  CB    . LEU C 220 ? 1.3059 1.1803 1.1836 0.3094  0.1237  -0.0263 213 LEU C CB    
6106 C  CG    . LEU C 220 ? 1.3683 1.2164 1.2037 0.3233  0.1446  -0.0393 213 LEU C CG    
6107 C  CD1   . LEU C 220 ? 1.4253 1.1832 1.1885 0.3144  0.1331  -0.0564 213 LEU C CD1   
6108 C  CD2   . LEU C 220 ? 1.2988 1.1988 1.1577 0.3014  0.1539  -0.0358 213 LEU C CD2   
6109 N  N     . THR C 221 ? 1.3028 1.1741 1.2226 0.3168  0.0830  -0.0031 214 THR C N     
6110 C  CA    . THR C 221 ? 1.2503 1.1464 1.2005 0.3004  0.0621  0.0097  214 THR C CA    
6111 C  C     . THR C 221 ? 1.2614 1.2202 1.2669 0.3247  0.0640  0.0250  214 THR C C     
6112 O  O     . THR C 221 ? 1.3246 1.2980 1.3410 0.3594  0.0815  0.0263  214 THR C O     
6113 C  CB    . THR C 221 ? 1.2909 1.1195 1.2013 0.2961  0.0440  0.0091  214 THR C CB    
6114 O  OG1   . THR C 221 ? 1.3990 1.1700 1.2712 0.3285  0.0515  0.0021  214 THR C OG1   
6115 C  CG2   . THR C 221 ? 1.2508 1.0405 1.1274 0.2586  0.0334  0.0021  214 THR C CG2   
6116 N  N     . ILE C 222 ? 1.2078 1.2024 1.2463 0.3069  0.0450  0.0371  215 ILE C N     
6117 C  CA    . ILE C 222 ? 1.2137 1.2729 1.3088 0.3227  0.0405  0.0535  215 ILE C CA    
6118 C  C     . ILE C 222 ? 1.2074 1.2579 1.3037 0.3131  0.0138  0.0633  215 ILE C C     
6119 O  O     . ILE C 222 ? 1.1731 1.1860 1.2371 0.2864  0.0012  0.0588  215 ILE C O     
6120 C  CB    . ILE C 222 ? 1.1505 1.2845 1.2959 0.3054  0.0465  0.0595  215 ILE C CB    
6121 C  CG1   . ILE C 222 ? 1.0642 1.1977 1.2021 0.2623  0.0331  0.0556  215 ILE C CG1   
6122 C  CG2   . ILE C 222 ? 1.1746 1.3238 1.3222 0.3212  0.0753  0.0538  215 ILE C CG2   
6123 C  CD1   . ILE C 222 ? 1.0144 1.2174 1.2035 0.2442  0.0309  0.0649  215 ILE C CD1   
6124 N  N     . SER C 223 ? 1.2479 1.3358 1.3822 0.3366  0.0059  0.0781  216 SER C N     
6125 C  CA    . SER C 223 ? 1.2520 1.3388 1.3903 0.3302  -0.0205 0.0898  216 SER C CA    
6126 C  C     . SER C 223 ? 1.1720 1.2958 1.3295 0.2923  -0.0362 0.0929  216 SER C C     
6127 O  O     . SER C 223 ? 1.1201 1.2830 1.3018 0.2757  -0.0272 0.0896  216 SER C O     
6128 C  CB    . SER C 223 ? 1.3168 1.4431 1.4968 0.3645  -0.0259 0.1058  216 SER C CB    
6129 O  OG    . SER C 223 ? 1.2853 1.4955 1.5287 0.3596  -0.0250 0.1159  216 SER C OG    
6130 N  N     . ASP C 224 ? 1.1748 1.2831 1.3187 0.2811  -0.0599 0.0999  217 ASP C N     
6131 C  CA    . ASP C 224 ? 1.1234 1.2615 1.2803 0.2509  -0.0787 0.1040  217 ASP C CA    
6132 C  C     . ASP C 224 ? 1.1287 1.3424 1.3489 0.2560  -0.0873 0.1170  217 ASP C C     
6133 O  O     . ASP C 224 ? 1.0830 1.3314 1.3237 0.2298  -0.0957 0.1174  217 ASP C O     
6134 C  CB    . ASP C 224 ? 1.1466 1.2449 1.2669 0.2436  -0.1002 0.1094  217 ASP C CB    
6135 C  CG    . ASP C 224 ? 1.1550 1.1819 1.2183 0.2388  -0.0919 0.1007  217 ASP C CG    
6136 O  OD1   . ASP C 224 ? 1.1031 1.1132 1.1424 0.2115  -0.0884 0.0921  217 ASP C OD1   
6137 O  OD2   . ASP C 224 ? 1.2194 1.2081 1.2639 0.2626  -0.0891 0.1034  217 ASP C OD2   
6138 N  N     . ASP C 225 ? 1.1925 1.4308 1.4439 0.2899  -0.0858 0.1284  218 ASP C N     
6139 C  CA    . ASP C 225 ? 1.2103 1.5273 1.5295 0.2978  -0.0936 0.1443  218 ASP C CA    
6140 C  C     . ASP C 225 ? 1.1765 1.5393 1.5314 0.2927  -0.0697 0.1412  218 ASP C C     
6141 O  O     . ASP C 225 ? 1.1492 1.5678 1.5469 0.2713  -0.0786 0.1489  218 ASP C O     
6142 C  CB    . ASP C 225 ? 1.2952 1.6274 1.6393 0.3399  -0.0960 0.1586  218 ASP C CB    
6143 C  CG    . ASP C 225 ? 1.3431 1.6169 1.6427 0.3509  -0.1146 0.1614  218 ASP C CG    
6144 O  OD1   . ASP C 225 ? 1.3396 1.5413 1.5800 0.3481  -0.1054 0.1484  218 ASP C OD1   
6145 O  OD2   . ASP C 225 ? 1.3899 1.6909 1.7147 0.3617  -0.1388 0.1781  218 ASP C OD2   
6146 N  N     . GLU C 226 ? 1.1882 1.5241 1.5222 0.3122  -0.0402 0.1306  219 GLU C N     
6147 C  CA    . GLU C 226 ? 1.1677 1.5390 1.5255 0.3112  -0.0138 0.1274  219 GLU C CA    
6148 C  C     . GLU C 226 ? 1.0887 1.4639 1.4401 0.2685  -0.0176 0.1199  219 GLU C C     
6149 O  O     . GLU C 226 ? 1.0696 1.5003 1.4636 0.2563  -0.0107 0.1268  219 GLU C O     
6150 C  CB    . GLU C 226 ? 1.2005 1.5203 1.5151 0.3365  0.0145  0.1131  219 GLU C CB    
6151 C  CG    . GLU C 226 ? 1.2918 1.6195 1.6216 0.3850  0.0267  0.1210  219 GLU C CG    
6152 C  CD    . GLU C 226 ? 1.3474 1.5950 1.6143 0.4109  0.0430  0.1053  219 GLU C CD    
6153 O  OE1   . GLU C 226 ? 1.3142 1.4974 1.5252 0.3881  0.0396  0.0899  219 GLU C OE1   
6154 O  OE2   . GLU C 226 ? 1.4314 1.6810 1.7054 0.4542  0.0585  0.1092  219 GLU C OE2   
6155 N  N     . PHE C 227 ? 1.0497 1.3652 1.3474 0.2469  -0.0271 0.1068  220 PHE C N     
6156 C  CA    . PHE C 227 ? 0.9819 1.2939 1.2677 0.2099  -0.0310 0.0990  220 PHE C CA    
6157 C  C     . PHE C 227 ? 0.9702 1.3328 1.2976 0.1884  -0.0546 0.1112  220 PHE C C     
6158 O  O     . PHE C 227 ? 0.9378 1.3303 1.2868 0.1664  -0.0519 0.1119  220 PHE C O     
6159 C  CB    . PHE C 227 ? 0.9549 1.1994 1.1803 0.1948  -0.0382 0.0861  220 PHE C CB    
6160 C  CG    . PHE C 227 ? 0.8917 1.1289 1.1017 0.1611  -0.0409 0.0776  220 PHE C CG    
6161 C  CD1   . PHE C 227 ? 0.8599 1.0960 1.0645 0.1531  -0.0210 0.0690  220 PHE C CD1   
6162 C  CD2   . PHE C 227 ? 0.8731 1.1035 1.0717 0.1393  -0.0632 0.0787  220 PHE C CD2   
6163 C  CE1   . PHE C 227 ? 0.8084 1.0369 0.9993 0.1249  -0.0239 0.0622  220 PHE C CE1   
6164 C  CE2   . PHE C 227 ? 0.8250 1.0460 1.0075 0.1124  -0.0645 0.0706  220 PHE C CE2   
6165 C  CZ    . PHE C 227 ? 0.7915 1.0124 0.9722 0.1056  -0.0450 0.0628  220 PHE C CZ    
6166 N  N     . ASP C 228 ? 1.0065 1.3757 1.3430 0.1950  -0.0789 0.1214  221 ASP C N     
6167 C  CA    . ASP C 228 ? 1.0077 1.4111 1.3707 0.1724  -0.1082 0.1313  221 ASP C CA    
6168 C  C     . ASP C 228 ? 1.0251 1.5067 1.4597 0.1713  -0.1070 0.1470  221 ASP C C     
6169 O  O     . ASP C 228 ? 1.0073 1.5144 1.4616 0.1415  -0.1209 0.1502  221 ASP C O     
6170 C  CB    . ASP C 228 ? 1.0522 1.4384 1.4004 0.1813  -0.1352 0.1386  221 ASP C CB    
6171 C  CG    . ASP C 228 ? 1.0349 1.3520 1.3153 0.1695  -0.1429 0.1265  221 ASP C CG    
6172 O  OD1   . ASP C 228 ? 0.9840 1.2729 1.2336 0.1491  -0.1328 0.1130  221 ASP C OD1   
6173 O  OD2   . ASP C 228 ? 1.0778 1.3710 1.3370 0.1819  -0.1585 0.1322  221 ASP C OD2   
6174 N  N     . ARG C 229 ? 1.0677 1.5867 1.5407 0.2037  -0.0902 0.1575  222 ARG C N     
6175 C  CA    . ARG C 229 ? 1.0919 1.6930 1.6387 0.2051  -0.0854 0.1757  222 ARG C CA    
6176 C  C     . ARG C 229 ? 1.0471 1.6606 1.5994 0.1804  -0.0670 0.1706  222 ARG C C     
6177 O  O     . ARG C 229 ? 1.0505 1.7195 1.6521 0.1583  -0.0754 0.1839  222 ARG C O     
6178 C  CB    . ARG C 229 ? 1.1486 1.7815 1.7273 0.2499  -0.0618 0.1856  222 ARG C CB    
6179 C  CG    . ARG C 229 ? 1.2116 1.8642 1.8151 0.2757  -0.0828 0.2004  222 ARG C CG    
6180 C  CD    . ARG C 229 ? 1.2755 1.9646 1.9150 0.3229  -0.0565 0.2110  222 ARG C CD    
6181 N  NE    . ARG C 229 ? 1.3338 1.9959 1.9584 0.3567  -0.0682 0.2148  222 ARG C NE    
6182 C  CZ    . ARG C 229 ? 1.3381 1.9154 1.8924 0.3702  -0.0647 0.1985  222 ARG C CZ    
6183 N  NH1   . ARG C 229 ? 1.2879 1.8037 1.7839 0.3547  -0.0482 0.1772  222 ARG C NH1   
6184 N  NH2   . ARG C 229 ? 1.3994 1.9542 1.9432 0.3990  -0.0783 0.2052  222 ARG C NH2   
6185 N  N     . PHE C 230 ? 1.0122 1.5723 1.5128 0.1838  -0.0429 0.1523  223 PHE C N     
6186 C  CA    . PHE C 230 ? 0.9708 1.5312 1.4654 0.1615  -0.0260 0.1460  223 PHE C CA    
6187 C  C     . PHE C 230 ? 0.9368 1.4923 1.4276 0.1202  -0.0529 0.1449  223 PHE C C     
6188 O  O     . PHE C 230 ? 0.9307 1.5225 1.4533 0.0976  -0.0520 0.1529  223 PHE C O     
6189 C  CB    . PHE C 230 ? 0.9456 1.4427 1.3793 0.1718  -0.0021 0.1260  223 PHE C CB    
6190 C  CG    . PHE C 230 ? 0.9068 1.3991 1.3284 0.1507  0.0144  0.1193  223 PHE C CG    
6191 C  CD1   . PHE C 230 ? 0.8564 1.3136 1.2459 0.1190  0.0007  0.1090  223 PHE C CD1   
6192 C  CD2   . PHE C 230 ? 0.9287 1.4525 1.3703 0.1640  0.0441  0.1244  223 PHE C CD2   
6193 C  CE1   . PHE C 230 ? 0.8267 1.2782 1.2050 0.1012  0.0146  0.1040  223 PHE C CE1   
6194 C  CE2   . PHE C 230 ? 0.8994 1.4169 1.3269 0.1446  0.0583  0.1196  223 PHE C CE2   
6195 C  CZ    . PHE C 230 ? 0.8477 1.3289 1.2446 0.1130  0.0425  0.1097  223 PHE C CZ    
6196 N  N     . CYS C 231 ? 0.9249 1.4336 1.3748 0.1112  -0.0766 0.1358  224 CYS C N     
6197 C  CA    . CYS C 231 ? 0.8986 1.3852 1.3270 0.0761  -0.0988 0.1298  224 CYS C CA    
6198 C  C     . CYS C 231 ? 0.9372 1.4730 1.4135 0.0575  -0.1290 0.1463  224 CYS C C     
6199 O  O     . CYS C 231 ? 0.9301 1.4662 1.4077 0.0262  -0.1427 0.1459  224 CYS C O     
6200 C  CB    . CYS C 231 ? 0.8800 1.2991 1.2438 0.0748  -0.1094 0.1145  224 CYS C CB    
6201 S  SG    . CYS C 231 ? 0.8372 1.1989 1.1466 0.0871  -0.0785 0.0962  224 CYS C SG    
6202 N  N     . GLU C 232 ? 0.9852 1.5612 1.5007 0.0769  -0.1402 0.1614  225 GLU C N     
6203 C  CA    . GLU C 232 ? 1.0333 1.6670 1.6047 0.0620  -0.1697 0.1808  225 GLU C CA    
6204 C  C     . GLU C 232 ? 1.0441 1.7474 1.6821 0.0533  -0.1546 0.1972  225 GLU C C     
6205 O  O     . GLU C 232 ? 1.0699 1.8098 1.7455 0.0235  -0.1779 0.2098  225 GLU C O     
6206 C  CB    . GLU C 232 ? 1.0856 1.7457 1.6825 0.0902  -0.1836 0.1939  225 GLU C CB    
6207 C  CG    . GLU C 232 ? 1.0885 1.6840 1.6227 0.1005  -0.1987 0.1821  225 GLU C CG    
6208 C  CD    . GLU C 232 ? 1.1395 1.7491 1.6893 0.1360  -0.2042 0.1935  225 GLU C CD    
6209 O  OE1   . GLU C 232 ? 1.1378 1.6887 1.6327 0.1519  -0.2022 0.1831  225 GLU C OE1   
6210 O  OE2   . GLU C 232 ? 1.1870 1.8668 1.8049 0.1471  -0.2119 0.2144  225 GLU C OE2   
6211 N  N     . ARG C 233 ? 1.0343 1.7541 1.6845 0.0795  -0.1161 0.1978  226 ARG C N     
6212 C  CA    . ARG C 233 ? 1.0467 1.8293 1.7526 0.0758  -0.0932 0.2131  226 ARG C CA    
6213 C  C     . ARG C 233 ? 1.0168 1.7851 1.7110 0.0354  -0.0957 0.2089  226 ARG C C     
6214 O  O     . ARG C 233 ? 1.0365 1.8597 1.7812 0.0206  -0.0864 0.2258  226 ARG C O     
6215 C  CB    . ARG C 233 ? 1.0421 1.8191 1.7355 0.1131  -0.0497 0.2072  226 ARG C CB    
6216 C  CG    . ARG C 233 ? 1.0532 1.8817 1.7863 0.1112  -0.0185 0.2195  226 ARG C CG    
6217 C  CD    . ARG C 233 ? 1.0702 1.8934 1.7883 0.1538  0.0224  0.2142  226 ARG C CD    
6218 N  NE    . ARG C 233 ? 1.1070 1.9258 1.8247 0.1929  0.0205  0.2142  226 ARG C NE    
6219 C  CZ    . ARG C 233 ? 1.1021 1.8542 1.7592 0.2199  0.0319  0.1949  226 ARG C CZ    
6220 N  NH1   . ARG C 233 ? 1.0623 1.7525 1.6578 0.2137  0.0481  0.1744  226 ARG C NH1   
6221 N  NH2   . ARG C 233 ? 1.1449 1.8927 1.8042 0.2532  0.0264  0.1974  226 ARG C NH2   
6222 N  N     . HIS C 234 ? 0.9748 1.6686 1.6013 0.0196  -0.1063 0.1875  227 HIS C N     
6223 C  CA    . HIS C 234 ? 0.9444 1.6089 1.5453 -0.0105 -0.1031 0.1793  227 HIS C CA    
6224 C  C     . HIS C 234 ? 0.9512 1.5786 1.5245 -0.0423 -0.1417 0.1726  227 HIS C C     
6225 O  O     . HIS C 234 ? 0.9224 1.4977 1.4486 -0.0598 -0.1421 0.1579  227 HIS C O     
6226 C  CB    . HIS C 234 ? 0.8933 1.5007 1.4349 0.0044  -0.0742 0.1587  227 HIS C CB    
6227 C  CG    . HIS C 234 ? 0.8969 1.5305 1.4544 0.0316  -0.0361 0.1628  227 HIS C CG    
6228 N  ND1   . HIS C 234 ? 0.9035 1.5253 1.4458 0.0688  -0.0193 0.1568  227 HIS C ND1   
6229 C  CD2   . HIS C 234 ? 0.9057 1.5742 1.4896 0.0275  -0.0116 0.1728  227 HIS C CD2   
6230 C  CE1   . HIS C 234 ? 0.9183 1.5640 1.4737 0.0877  0.0142  0.1611  227 HIS C CE1   
6231 N  NE2   . HIS C 234 ? 0.9187 1.5953 1.5000 0.0633  0.0203  0.1714  227 HIS C NE2   
6232 N  N     . SER C 235 ? 0.9984 1.6534 1.6008 -0.0490 -0.1745 0.1842  228 SER C N     
6233 C  CA    . SER C 235 ? 1.0169 1.6254 1.5783 -0.0702 -0.2121 0.1745  228 SER C CA    
6234 C  C     . SER C 235 ? 1.0324 1.6229 1.5857 -0.1104 -0.2291 0.1732  228 SER C C     
6235 O  O     . SER C 235 ? 1.0353 1.5635 1.5304 -0.1244 -0.2481 0.1570  228 SER C O     
6236 C  CB    . SER C 235 ? 1.0741 1.7170 1.6673 -0.0669 -0.2448 0.1883  228 SER C CB    
6237 O  OG    . SER C 235 ? 1.1229 1.8409 1.7932 -0.0845 -0.2579 0.2130  228 SER C OG    
6238 N  N     . SER C 236 ? 1.0521 1.6955 1.6621 -0.1284 -0.2225 0.1912  229 SER C N     
6239 C  CA    . SER C 236 ? 1.0823 1.7106 1.6903 -0.1690 -0.2417 0.1937  229 SER C CA    
6240 C  C     . SER C 236 ? 1.0353 1.5975 1.5820 -0.1725 -0.2216 0.1738  229 SER C C     
6241 O  O     . SER C 236 ? 1.0601 1.5843 1.5819 -0.2019 -0.2388 0.1690  229 SER C O     
6242 C  CB    . SER C 236 ? 1.1226 1.8295 1.8116 -0.1878 -0.2390 0.2218  229 SER C CB    
6243 O  OG    . SER C 236 ? 1.0863 1.8298 1.8012 -0.1651 -0.1941 0.2286  229 SER C OG    
6244 N  N     . GLN C 237 ? 0.9749 1.5216 1.4964 -0.1419 -0.1867 0.1624  230 GLN C N     
6245 C  CA    . GLN C 237 ? 0.9294 1.4216 1.3986 -0.1413 -0.1658 0.1455  230 GLN C CA    
6246 C  C     . GLN C 237 ? 0.9201 1.3396 1.3195 -0.1415 -0.1831 0.1236  230 GLN C C     
6247 O  O     . GLN C 237 ? 0.8867 1.2823 1.2538 -0.1167 -0.1732 0.1116  230 GLN C O     
6248 C  CB    . GLN C 237 ? 0.8809 1.3857 1.3504 -0.1098 -0.1258 0.1426  230 GLN C CB    
6249 C  CG    . GLN C 237 ? 0.9001 1.4768 1.4341 -0.1049 -0.1044 0.1642  230 GLN C CG    
6250 C  CD    . GLN C 237 ? 0.9282 1.5230 1.4878 -0.1373 -0.1062 0.1779  230 GLN C CD    
6251 O  OE1   . GLN C 237 ? 0.9234 1.4680 1.4438 -0.1585 -0.1154 0.1681  230 GLN C OE1   
6252 N  NE2   . GLN C 237 ? 0.9645 1.6321 1.5908 -0.1408 -0.0964 0.2022  230 GLN C NE2   
6253 N  N     . THR C 238 ? 0.9575 1.3404 1.3326 -0.1696 -0.2075 0.1192  231 THR C N     
6254 C  CA    . THR C 238 ? 0.9673 1.2809 1.2747 -0.1708 -0.2249 0.0994  231 THR C CA    
6255 C  C     . THR C 238 ? 0.9079 1.1766 1.1653 -0.1518 -0.1971 0.0819  231 THR C C     
6256 O  O     . THR C 238 ? 0.9088 1.1275 1.1122 -0.1446 -0.2039 0.0663  231 THR C O     
6257 C  CB    . THR C 238 ? 1.0326 1.3105 1.3205 -0.2039 -0.2548 0.0977  231 THR C CB    
6258 O  OG1   . THR C 238 ? 1.0189 1.2897 1.3106 -0.2157 -0.2371 0.1000  231 THR C OG1   
6259 C  CG2   . THR C 238 ? 1.1050 1.4206 1.4379 -0.2291 -0.2894 0.1148  231 THR C CG2   
6260 N  N     . CYS C 239 ? 0.8639 1.1511 1.1386 -0.1443 -0.1666 0.0854  232 CYS C N     
6261 C  CA    . CYS C 239 ? 0.8120 1.0624 1.0451 -0.1281 -0.1422 0.0710  232 CYS C CA    
6262 C  C     . CYS C 239 ? 0.7691 1.0274 0.9969 -0.0990 -0.1236 0.0664  232 CYS C C     
6263 O  O     . CYS C 239 ? 0.7312 0.9588 0.9240 -0.0864 -0.1071 0.0548  232 CYS C O     
6264 C  CB    . CYS C 239 ? 0.7946 1.0564 1.0427 -0.1345 -0.1205 0.0770  232 CYS C CB    
6265 S  SG    . CYS C 239 ? 0.7814 1.1134 1.0890 -0.1216 -0.0953 0.0943  232 CYS C SG    
6266 N  N     . LEU C 240 ? 0.7807 1.0801 1.0446 -0.0885 -0.1264 0.0766  233 LEU C N     
6267 C  CA    . LEU C 240 ? 0.7522 1.0578 1.0136 -0.0608 -0.1085 0.0741  233 LEU C CA    
6268 C  C     . LEU C 240 ? 0.7439 1.0035 0.9554 -0.0512 -0.1162 0.0609  233 LEU C C     
6269 O  O     . LEU C 240 ? 0.7762 1.0166 0.9683 -0.0606 -0.1405 0.0584  233 LEU C O     
6270 C  CB    . LEU C 240 ? 0.7805 1.1405 1.0937 -0.0507 -0.1121 0.0897  233 LEU C CB    
6271 C  CG    . LEU C 240 ? 0.7770 1.1343 1.0823 -0.0230 -0.1069 0.0877  233 LEU C CG    
6272 C  CD1   . LEU C 240 ? 0.7497 1.1080 1.0526 -0.0012 -0.0748 0.0845  233 LEU C CD1   
6273 C  CD2   . LEU C 240 ? 0.8222 1.2258 1.1729 -0.0172 -0.1242 0.1033  233 LEU C CD2   
6274 N  N     . VAL C 241 ? 0.7077 0.9488 0.8965 -0.0333 -0.0950 0.0533  234 VAL C N     
6275 C  CA    . VAL C 241 ? 0.6991 0.9016 0.8446 -0.0233 -0.0963 0.0437  234 VAL C CA    
6276 C  C     . VAL C 241 ? 0.6902 0.8983 0.8402 -0.0009 -0.0818 0.0455  234 VAL C C     
6277 O  O     . VAL C 241 ? 0.6640 0.8652 0.8079 0.0067  -0.0611 0.0413  234 VAL C O     
6278 C  CB    . VAL C 241 ? 0.6701 0.8356 0.7776 -0.0283 -0.0857 0.0321  234 VAL C CB    
6279 C  CG1   . VAL C 241 ? 0.6640 0.7971 0.7325 -0.0178 -0.0832 0.0252  234 VAL C CG1   
6280 C  CG2   . VAL C 241 ? 0.6887 0.8391 0.7847 -0.0473 -0.0991 0.0289  234 VAL C CG2   
6281 N  N     . PRO C 242 ? 0.7192 0.9332 0.8739 0.0106  -0.0933 0.0512  235 PRO C N     
6282 C  CA    . PRO C 242 ? 0.7230 0.9354 0.8786 0.0331  -0.0807 0.0531  235 PRO C CA    
6283 C  C     . PRO C 242 ? 0.7144 0.8818 0.8244 0.0391  -0.0760 0.0455  235 PRO C C     
6284 O  O     . PRO C 242 ? 0.7202 0.8646 0.8012 0.0307  -0.0877 0.0425  235 PRO C O     
6285 C  CB    . PRO C 242 ? 0.7678 1.0071 0.9501 0.0410  -0.0999 0.0649  235 PRO C CB    
6286 C  CG    . PRO C 242 ? 0.7854 1.0091 0.9462 0.0236  -0.1247 0.0632  235 PRO C CG    
6287 C  CD    . PRO C 242 ? 0.7596 0.9770 0.9145 0.0031  -0.1210 0.0561  235 PRO C CD    
6288 N  N     . GLU C 243 ? 0.7094 0.8636 0.8121 0.0533  -0.0589 0.0431  236 GLU C N     
6289 C  CA    . GLU C 243 ? 0.7081 0.8216 0.7720 0.0562  -0.0546 0.0384  236 GLU C CA    
6290 C  C     . GLU C 243 ? 0.7414 0.8418 0.8024 0.0764  -0.0495 0.0418  236 GLU C C     
6291 O  O     . GLU C 243 ? 0.7403 0.8229 0.7908 0.0828  -0.0348 0.0368  236 GLU C O     
6292 C  CB    . GLU C 243 ? 0.6712 0.7669 0.7164 0.0460  -0.0403 0.0294  236 GLU C CB    
6293 C  CG    . GLU C 243 ? 0.6463 0.7476 0.6893 0.0290  -0.0446 0.0258  236 GLU C CG    
6294 C  CD    . GLU C 243 ? 0.6161 0.6986 0.6382 0.0206  -0.0333 0.0187  236 GLU C CD    
6295 O  OE1   . GLU C 243 ? 0.5981 0.6871 0.6235 0.0104  -0.0328 0.0156  236 GLU C OE1   
6296 O  OE2   . GLU C 243 ? 0.6175 0.6784 0.6202 0.0237  -0.0271 0.0175  236 GLU C OE2   
6297 N  N     . PRO C 244 ? 0.7809 0.8802 0.8424 0.0867  -0.0635 0.0500  237 PRO C N     
6298 C  CA    . PRO C 244 ? 0.8218 0.8950 0.8695 0.1055  -0.0605 0.0533  237 PRO C CA    
6299 C  C     . PRO C 244 ? 0.8183 0.8455 0.8251 0.0980  -0.0539 0.0483  237 PRO C C     
6300 O  O     . PRO C 244 ? 0.7890 0.8077 0.7781 0.0802  -0.0541 0.0449  237 PRO C O     
6301 C  CB    . PRO C 244 ? 0.8633 0.9443 0.9158 0.1129  -0.0811 0.0643  237 PRO C CB    
6302 C  CG    . PRO C 244 ? 0.8426 0.9333 0.8890 0.0922  -0.0947 0.0632  237 PRO C CG    
6303 C  CD    . PRO C 244 ? 0.7974 0.9138 0.8666 0.0802  -0.0847 0.0564  237 PRO C CD    
6304 N  N     . ASN C 245 ? 0.8570 0.8538 0.8491 0.1121  -0.0483 0.0489  238 ASN C N     
6305 C  CA    . ASN C 245 ? 0.8657 0.8185 0.8225 0.1033  -0.0433 0.0461  238 ASN C CA    
6306 C  C     . ASN C 245 ? 0.8622 0.8040 0.7974 0.0880  -0.0523 0.0520  238 ASN C C     
6307 O  O     . ASN C 245 ? 0.8399 0.7692 0.7584 0.0714  -0.0464 0.0494  238 ASN C O     
6308 C  CB    . ASN C 245 ? 0.9287 0.8445 0.8701 0.1223  -0.0410 0.0476  238 ASN C CB    
6309 C  CG    . ASN C 245 ? 0.9425 0.8666 0.8990 0.1405  -0.0287 0.0405  238 ASN C CG    
6310 O  OD1   . ASN C 245 ? 1.0026 0.9073 0.9545 0.1639  -0.0274 0.0424  238 ASN C OD1   
6311 N  ND2   . ASN C 245 ? 0.8960 0.8477 0.8685 0.1324  -0.0185 0.0330  238 ASN C ND2   
6312 N  N     . ARG C 246 ? 0.8891 0.8386 0.8250 0.0943  -0.0664 0.0608  239 ARG C N     
6313 C  CA    . ARG C 246 ? 0.9015 0.8382 0.8108 0.0834  -0.0744 0.0672  239 ARG C CA    
6314 C  C     . ARG C 246 ? 0.8533 0.8041 0.7583 0.0650  -0.0692 0.0607  239 ARG C C     
6315 O  O     . ARG C 246 ? 0.8576 0.7919 0.7368 0.0543  -0.0652 0.0636  239 ARG C O     
6316 C  CB    . ARG C 246 ? 0.9397 0.8886 0.8532 0.0939  -0.0929 0.0760  239 ARG C CB    
6317 C  CG    . ARG C 246 ? 0.9612 0.8986 0.8427 0.0843  -0.1023 0.0818  239 ARG C CG    
6318 C  CD    . ARG C 246 ? 1.0066 0.9552 0.8905 0.0941  -0.1242 0.0902  239 ARG C CD    
6319 N  NE    . ARG C 246 ? 1.0200 0.9636 0.8732 0.0826  -0.1328 0.0907  239 ARG C NE    
6320 C  CZ    . ARG C 246 ? 1.0038 0.9696 0.8648 0.0743  -0.1422 0.0839  239 ARG C CZ    
6321 N  NH1   . ARG C 246 ? 0.9740 0.9735 0.8776 0.0749  -0.1458 0.0792  239 ARG C NH1   
6322 N  NH2   . ARG C 246 ? 1.0268 0.9791 0.8508 0.0658  -0.1479 0.0825  239 ARG C NH2   
6323 N  N     . LEU C 247 ? 0.8144 0.7958 0.7450 0.0622  -0.0687 0.0532  240 LEU C N     
6324 C  CA    . LEU C 247 ? 0.7786 0.7715 0.7054 0.0479  -0.0663 0.0469  240 LEU C CA    
6325 C  C     . LEU C 247 ? 0.7381 0.7287 0.6672 0.0394  -0.0501 0.0398  240 LEU C C     
6326 O  O     . LEU C 247 ? 0.7187 0.7088 0.6360 0.0291  -0.0451 0.0368  240 LEU C O     
6327 C  CB    . LEU C 247 ? 0.7674 0.7908 0.7201 0.0470  -0.0764 0.0440  240 LEU C CB    
6328 C  CG    . LEU C 247 ? 0.8085 0.8362 0.7547 0.0488  -0.0972 0.0498  240 LEU C CG    
6329 C  CD1   . LEU C 247 ? 0.7985 0.8547 0.7704 0.0413  -0.1078 0.0466  240 LEU C CD1   
6330 C  CD2   . LEU C 247 ? 0.8337 0.8351 0.7361 0.0433  -0.1001 0.0508  240 LEU C CD2   
6331 N  N     . MET C 248 ? 0.7341 0.7217 0.6758 0.0452  -0.0423 0.0373  241 MET C N     
6332 C  CA    . MET C 248 ? 0.7006 0.6887 0.6456 0.0372  -0.0301 0.0300  241 MET C CA    
6333 C  C     . MET C 248 ? 0.7151 0.6750 0.6384 0.0301  -0.0247 0.0324  241 MET C C     
6334 O  O     . MET C 248 ? 0.6908 0.6520 0.6114 0.0184  -0.0180 0.0296  241 MET C O     
6335 C  CB    . MET C 248 ? 0.6980 0.6968 0.6633 0.0470  -0.0242 0.0253  241 MET C CB    
6336 C  CG    . MET C 248 ? 0.6659 0.6678 0.6329 0.0382  -0.0136 0.0178  241 MET C CG    
6337 S  SD    . MET C 248 ? 0.6794 0.6872 0.6594 0.0517  -0.0033 0.0128  241 MET C SD    
6338 C  CE    . MET C 248 ? 0.6386 0.6558 0.6190 0.0374  0.0050  0.0061  241 MET C CE    
6339 N  N     . ALA C 249 ? 0.7610 0.6956 0.6700 0.0364  -0.0290 0.0392  242 ALA C N     
6340 C  CA    . ALA C 249 ? 0.7892 0.6921 0.6802 0.0293  -0.0258 0.0420  242 ALA C CA    
6341 C  C     . ALA C 249 ? 0.7716 0.6787 0.6553 0.0110  -0.0211 0.0459  242 ALA C C     
6342 O  O     . ALA C 249 ? 0.7684 0.6678 0.6509 0.0000  -0.0170 0.0442  242 ALA C O     
6343 C  CB    . ALA C 249 ? 0.8497 0.7219 0.7239 0.0381  -0.0329 0.0508  242 ALA C CB    
6344 N  N     . LYS C 250 ? 0.7669 0.6871 0.6451 0.0087  -0.0218 0.0516  243 LYS C N     
6345 C  CA    . LYS C 250 ? 0.7669 0.6910 0.6365 -0.0047 -0.0149 0.0586  243 LYS C CA    
6346 C  C     . LYS C 250 ? 0.7378 0.6874 0.6091 -0.0044 -0.0107 0.0555  243 LYS C C     
6347 O  O     . LYS C 250 ? 0.7530 0.7065 0.6125 -0.0095 -0.0042 0.0634  243 LYS C O     
6348 C  CB    . LYS C 250 ? 0.8224 0.7239 0.6703 -0.0075 -0.0169 0.0731  243 LYS C CB    
6349 C  CG    . LYS C 250 ? 0.8677 0.7378 0.7065 0.0012  -0.0261 0.0761  243 LYS C CG    
6350 C  CD    . LYS C 250 ? 0.9277 0.7656 0.7467 -0.0084 -0.0271 0.0905  243 LYS C CD    
6351 C  CE    . LYS C 250 ? 0.9358 0.7578 0.7587 -0.0234 -0.0253 0.0894  243 LYS C CE    
6352 N  NZ    . LYS C 250 ? 1.0094 0.7881 0.8116 -0.0309 -0.0313 0.1016  243 LYS C NZ    
6353 N  N     . SER C 251 ? 0.7039 0.6694 0.5886 0.0012  -0.0134 0.0448  244 SER C N     
6354 C  CA    . SER C 251 ? 0.6901 0.6703 0.5712 0.0031  -0.0133 0.0402  244 SER C CA    
6355 C  C     . SER C 251 ? 0.6517 0.6474 0.5460 -0.0019 -0.0055 0.0335  244 SER C C     
6356 O  O     . SER C 251 ? 0.6415 0.6451 0.5341 0.0003  -0.0064 0.0275  244 SER C O     
6357 C  CB    . SER C 251 ? 0.6924 0.6771 0.5790 0.0108  -0.0258 0.0350  244 SER C CB    
6358 O  OG    . SER C 251 ? 0.6645 0.6600 0.5766 0.0121  -0.0265 0.0288  244 SER C OG    
6359 N  N     . TYR C 252 ? 0.6380 0.6342 0.5436 -0.0088 -0.0002 0.0345  245 TYR C N     
6360 C  CA    . TYR C 252 ? 0.6063 0.6164 0.5249 -0.0134 0.0050  0.0295  245 TYR C CA    
6361 C  C     . TYR C 252 ? 0.6145 0.6302 0.5345 -0.0225 0.0123  0.0380  245 TYR C C     
6362 O  O     . TYR C 252 ? 0.6428 0.6483 0.5573 -0.0287 0.0122  0.0471  245 TYR C O     
6363 C  CB    . TYR C 252 ? 0.5873 0.5963 0.5192 -0.0144 0.0031  0.0226  245 TYR C CB    
6364 C  CG    . TYR C 252 ? 0.5761 0.5903 0.5167 -0.0070 -0.0013 0.0158  245 TYR C CG    
6365 C  CD1   . TYR C 252 ? 0.5963 0.6048 0.5368 0.0006  -0.0075 0.0172  245 TYR C CD1   
6366 C  CD2   . TYR C 252 ? 0.5511 0.5779 0.5023 -0.0082 0.0002  0.0102  245 TYR C CD2   
6367 C  CE1   . TYR C 252 ? 0.5905 0.6114 0.5459 0.0063  -0.0115 0.0138  245 TYR C CE1   
6368 C  CE2   . TYR C 252 ? 0.5465 0.5820 0.5097 -0.0044 -0.0032 0.0068  245 TYR C CE2   
6369 C  CZ    . TYR C 252 ? 0.5657 0.6011 0.5334 0.0026  -0.0089 0.0090  245 TYR C CZ    
6370 O  OH    . TYR C 252 ? 0.5651 0.6167 0.5513 0.0054  -0.0123 0.0083  245 TYR C OH    
6371 N  N     . LEU C 253 ? 0.5950 0.6278 0.5239 -0.0233 0.0177  0.0364  246 LEU C N     
6372 C  CA    . LEU C 253 ? 0.5989 0.6462 0.5388 -0.0321 0.0232  0.0447  246 LEU C CA    
6373 C  C     . LEU C 253 ? 0.5783 0.6267 0.5309 -0.0385 0.0184  0.0391  246 LEU C C     
6374 O  O     . LEU C 253 ? 0.5543 0.6078 0.5105 -0.0327 0.0182  0.0310  246 LEU C O     
6375 C  CB    . LEU C 253 ? 0.6006 0.6666 0.5400 -0.0241 0.0326  0.0469  246 LEU C CB    
6376 C  CG    . LEU C 253 ? 0.6346 0.6984 0.5546 -0.0169 0.0396  0.0532  246 LEU C CG    
6377 C  CD1   . LEU C 253 ? 0.6446 0.7203 0.5577 -0.0041 0.0495  0.0516  246 LEU C CD1   
6378 C  CD2   . LEU C 253 ? 0.6657 0.7355 0.5887 -0.0270 0.0449  0.0693  246 LEU C CD2   
6379 N  N     . ILE C 254 ? 0.5965 0.6354 0.5514 -0.0506 0.0133  0.0434  247 ILE C N     
6380 C  CA    . ILE C 254 ? 0.5923 0.6218 0.5489 -0.0561 0.0066  0.0366  247 ILE C CA    
6381 C  C     . ILE C 254 ? 0.6102 0.6501 0.5777 -0.0715 0.0025  0.0453  247 ILE C C     
6382 O  O     . ILE C 254 ? 0.6441 0.6767 0.6109 -0.0835 -0.0006 0.0550  247 ILE C O     
6383 C  CB    . ILE C 254 ? 0.6159 0.6137 0.5572 -0.0550 0.0009  0.0313  247 ILE C CB    
6384 C  CG1   . ILE C 254 ? 0.6034 0.5973 0.5401 -0.0400 0.0033  0.0251  247 ILE C CG1   
6385 C  CG2   . ILE C 254 ? 0.6275 0.6097 0.5622 -0.0594 -0.0048 0.0237  247 ILE C CG2   
6386 C  CD1   . ILE C 254 ? 0.6368 0.6041 0.5608 -0.0356 -0.0006 0.0251  247 ILE C CD1   
6387 N  N     . LEU C 255 ? 0.5935 0.6490 0.5710 -0.0722 0.0010  0.0430  248 LEU C N     
6388 C  CA    . LEU C 255 ? 0.6133 0.6818 0.6037 -0.0871 -0.0063 0.0513  248 LEU C CA    
6389 C  C     . LEU C 255 ? 0.6321 0.6741 0.6069 -0.0943 -0.0182 0.0424  248 LEU C C     
6390 O  O     . LEU C 255 ? 0.6145 0.6460 0.5777 -0.0839 -0.0164 0.0309  248 LEU C O     
6391 C  CB    . LEU C 255 ? 0.5924 0.6949 0.6020 -0.0808 -0.0017 0.0554  248 LEU C CB    
6392 C  CG    . LEU C 255 ? 0.5885 0.7181 0.6109 -0.0716 0.0113  0.0648  248 LEU C CG    
6393 C  CD1   . LEU C 255 ? 0.5718 0.7245 0.6055 -0.0585 0.0166  0.0644  248 LEU C CD1   
6394 C  CD2   . LEU C 255 ? 0.6224 0.7717 0.6620 -0.0858 0.0119  0.0823  248 LEU C CD2   
6395 N  N     . ASP C 256 ? 0.6740 0.7082 0.6492 -0.1130 -0.0304 0.0490  249 ASP C N     
6396 C  CA    . ASP C 256 ? 0.7073 0.7108 0.6605 -0.1204 -0.0435 0.0399  249 ASP C CA    
6397 C  C     . ASP C 256 ? 0.7062 0.7326 0.6714 -0.1265 -0.0517 0.0430  249 ASP C C     
6398 O  O     . ASP C 256 ? 0.6740 0.7392 0.6647 -0.1206 -0.0451 0.0506  249 ASP C O     
6399 C  CB    . ASP C 256 ? 0.7694 0.7375 0.7061 -0.1376 -0.0560 0.0426  249 ASP C CB    
6400 C  CG    . ASP C 256 ? 0.8026 0.7911 0.7621 -0.1616 -0.0669 0.0601  249 ASP C CG    
6401 O  OD1   . ASP C 256 ? 0.7746 0.8115 0.7670 -0.1621 -0.0621 0.0716  249 ASP C OD1   
6402 O  OD2   . ASP C 256 ? 0.8626 0.8185 0.8075 -0.1792 -0.0799 0.0631  249 ASP C OD2   
6403 N  N     . GLU C 257 ? 0.7521 0.7501 0.6945 -0.1375 -0.0672 0.0370  250 GLU C N     
6404 C  CA    . GLU C 257 ? 0.7600 0.7717 0.7050 -0.1420 -0.0777 0.0380  250 GLU C CA    
6405 C  C     . GLU C 257 ? 0.7762 0.8260 0.7561 -0.1596 -0.0888 0.0562  250 GLU C C     
6406 O  O     . GLU C 257 ? 0.7779 0.8502 0.7692 -0.1610 -0.0968 0.0605  250 GLU C O     
6407 C  CB    . GLU C 257 ? 0.8141 0.7795 0.7166 -0.1465 -0.0906 0.0249  250 GLU C CB    
6408 C  CG    . GLU C 257 ? 0.8874 0.8161 0.7706 -0.1675 -0.1087 0.0255  250 GLU C CG    
6409 C  CD    . GLU C 257 ? 0.9160 0.7974 0.7695 -0.1616 -0.1036 0.0156  250 GLU C CD    
6410 O  OE1   . GLU C 257 ? 0.9921 0.8293 0.8165 -0.1765 -0.1204 0.0120  250 GLU C OE1   
6411 O  OE2   . GLU C 257 ? 0.8703 0.7571 0.7291 -0.1426 -0.0846 0.0121  250 GLU C OE2   
6412 N  N     . TYR C 258 ? 0.7915 0.8518 0.7905 -0.1722 -0.0885 0.0686  251 TYR C N     
6413 C  CA    . TYR C 258 ? 0.8054 0.9135 0.8464 -0.1870 -0.0940 0.0896  251 TYR C CA    
6414 C  C     . TYR C 258 ? 0.7595 0.9108 0.8312 -0.1710 -0.0711 0.0998  251 TYR C C     
6415 O  O     . TYR C 258 ? 0.7715 0.9681 0.8808 -0.1786 -0.0692 0.1190  251 TYR C O     
6416 C  CB    . TYR C 258 ? 0.8716 0.9643 0.9141 -0.2164 -0.1109 0.1003  251 TYR C CB    
6417 C  CG    . TYR C 258 ? 0.9367 0.9816 0.9441 -0.2343 -0.1369 0.0904  251 TYR C CG    
6418 C  CD1   . TYR C 258 ? 0.9776 1.0399 0.9975 -0.2526 -0.1599 0.0984  251 TYR C CD1   
6419 C  CD2   . TYR C 258 ? 0.9648 0.9455 0.9234 -0.2306 -0.1388 0.0726  251 TYR C CD2   
6420 C  CE1   . TYR C 258 ? 1.0486 1.0607 1.0283 -0.2688 -0.1853 0.0879  251 TYR C CE1   
6421 C  CE2   . TYR C 258 ? 1.0362 0.9664 0.9542 -0.2435 -0.1611 0.0615  251 TYR C CE2   
6422 C  CZ    . TYR C 258 ? 1.0800 1.0235 1.0059 -0.2636 -0.1851 0.0686  251 TYR C CZ    
6423 O  OH    . TYR C 258 ? 1.1614 1.0475 1.0384 -0.2758 -0.2082 0.0558  251 TYR C OH    
6424 N  N     . MET C 259 ? 0.7145 0.8517 0.7690 -0.1485 -0.0540 0.0872  252 MET C N     
6425 C  CA    . MET C 259 ? 0.6791 0.8443 0.7492 -0.1304 -0.0333 0.0921  252 MET C CA    
6426 C  C     . MET C 259 ? 0.7020 0.8720 0.7800 -0.1398 -0.0266 0.1047  252 MET C C     
6427 O  O     . MET C 259 ? 0.6992 0.9049 0.7988 -0.1329 -0.0122 0.1175  252 MET C O     
6428 C  CB    . MET C 259 ? 0.6667 0.8789 0.7671 -0.1201 -0.0281 0.1018  252 MET C CB    
6429 C  CG    . MET C 259 ? 0.6508 0.8562 0.7417 -0.1110 -0.0351 0.0916  252 MET C CG    
6430 S  SD    . MET C 259 ? 0.6335 0.8812 0.7498 -0.0879 -0.0237 0.0988  252 MET C SD    
6431 C  CE    . MET C 259 ? 0.5962 0.8205 0.6879 -0.0639 -0.0041 0.0845  252 MET C CE    
6432 N  N     . ARG C 260 ? 0.7312 0.8602 0.7863 -0.1531 -0.0359 0.1004  253 ARG C N     
6433 C  CA    . ARG C 260 ? 0.7573 0.8763 0.8091 -0.1607 -0.0306 0.1099  253 ARG C CA    
6434 C  C     . ARG C 260 ? 0.7302 0.8196 0.7542 -0.1409 -0.0196 0.0964  253 ARG C C     
6435 O  O     . ARG C 260 ? 0.7158 0.7744 0.7170 -0.1321 -0.0240 0.0794  253 ARG C O     
6436 C  CB    . ARG C 260 ? 0.8189 0.9040 0.8594 -0.1875 -0.0502 0.1138  253 ARG C CB    
6437 C  CG    . ARG C 260 ? 0.8559 0.9683 0.9238 -0.2113 -0.0665 0.1277  253 ARG C CG    
6438 C  CD    . ARG C 260 ? 0.9284 0.9959 0.9768 -0.2392 -0.0896 0.1288  253 ARG C CD    
6439 N  NE    . ARG C 260 ? 0.9383 0.9471 0.9415 -0.2318 -0.0996 0.1054  253 ARG C NE    
6440 C  CZ    . ARG C 260 ? 1.0053 0.9556 0.9746 -0.2465 -0.1158 0.0994  253 ARG C CZ    
6441 N  NH1   . ARG C 260 ? 1.0695 1.0111 1.0466 -0.2742 -0.1277 0.1160  253 ARG C NH1   
6442 N  NH2   . ARG C 260 ? 1.0167 0.9162 0.9433 -0.2335 -0.1199 0.0776  253 ARG C NH2   
6443 N  N     . PHE C 261 ? 0.7309 0.8310 0.7568 -0.1345 -0.0059 0.1052  254 PHE C N     
6444 C  CA    . PHE C 261 ? 0.7149 0.7889 0.7157 -0.1177 0.0012  0.0949  254 PHE C CA    
6445 C  C     . PHE C 261 ? 0.7520 0.7785 0.7291 -0.1266 -0.0099 0.0911  254 PHE C C     
6446 O  O     . PHE C 261 ? 0.8012 0.8183 0.7803 -0.1464 -0.0168 0.1041  254 PHE C O     
6447 C  CB    . PHE C 261 ? 0.7201 0.8152 0.7238 -0.1094 0.0171  0.1065  254 PHE C CB    
6448 C  CG    . PHE C 261 ? 0.6878 0.8143 0.7002 -0.0905 0.0302  0.1036  254 PHE C CG    
6449 C  CD1   . PHE C 261 ? 0.6508 0.7643 0.6488 -0.0730 0.0307  0.0862  254 PHE C CD1   
6450 C  CD2   . PHE C 261 ? 0.7027 0.8706 0.7374 -0.0898 0.0422  0.1190  254 PHE C CD2   
6451 C  CE1   . PHE C 261 ? 0.6327 0.7665 0.6340 -0.0565 0.0406  0.0829  254 PHE C CE1   
6452 C  CE2   . PHE C 261 ? 0.6841 0.8742 0.7221 -0.0694 0.0541  0.1149  254 PHE C CE2   
6453 C  CZ    . PHE C 261 ? 0.6511 0.8202 0.6699 -0.0533 0.0524  0.0963  254 PHE C CZ    
6454 N  N     . LEU C 262 ? 0.7360 0.7328 0.6917 -0.1122 -0.0119 0.0745  255 LEU C N     
6455 C  CA    . LEU C 262 ? 0.7772 0.7268 0.7081 -0.1140 -0.0205 0.0697  255 LEU C CA    
6456 C  C     . LEU C 262 ? 0.7835 0.7219 0.7025 -0.1020 -0.0140 0.0730  255 LEU C C     
6457 O  O     . LEU C 262 ? 0.7453 0.7042 0.6682 -0.0865 -0.0049 0.0698  255 LEU C O     
6458 C  CB    . LEU C 262 ? 0.7666 0.6940 0.6827 -0.1031 -0.0250 0.0513  255 LEU C CB    
6459 C  CG    . LEU C 262 ? 0.7688 0.7002 0.6879 -0.1131 -0.0332 0.0464  255 LEU C CG    
6460 C  CD1   . LEU C 262 ? 0.7702 0.6755 0.6678 -0.0996 -0.0344 0.0290  255 LEU C CD1   
6461 C  CD2   . LEU C 262 ? 0.8287 0.7436 0.7454 -0.1385 -0.0476 0.0560  255 LEU C CD2   
6462 N  N     . ASP C 263 ? 0.8398 0.7407 0.7409 -0.1091 -0.0210 0.0789  256 ASP C N     
6463 C  CA    . ASP C 263 ? 0.8597 0.7445 0.7463 -0.0987 -0.0178 0.0841  256 ASP C CA    
6464 C  C     . ASP C 263 ? 0.8697 0.7198 0.7374 -0.0804 -0.0229 0.0701  256 ASP C C     
6465 O  O     . ASP C 263 ? 0.8797 0.7200 0.7376 -0.0665 -0.0218 0.0718  256 ASP C O     
6466 C  CB    . ASP C 263 ? 0.9243 0.7910 0.8041 -0.1182 -0.0215 0.1032  256 ASP C CB    
6467 C  CG    . ASP C 263 ? 0.9360 0.8156 0.8120 -0.1143 -0.0118 0.1181  256 ASP C CG    
6468 O  OD1   . ASP C 263 ? 0.8920 0.8010 0.7726 -0.0984 -0.0017 0.1142  256 ASP C OD1   
6469 O  OD2   . ASP C 263 ? 0.9981 0.8547 0.8629 -0.1280 -0.0149 0.1342  256 ASP C OD2   
6470 N  N     . ARG C 264 ? 0.8733 0.7061 0.7353 -0.0787 -0.0282 0.0569  257 ARG C N     
6471 C  CA    . ARG C 264 ? 0.8816 0.6909 0.7301 -0.0577 -0.0289 0.0432  257 ARG C CA    
6472 C  C     . ARG C 264 ? 0.9477 0.7125 0.7735 -0.0509 -0.0347 0.0479  257 ARG C C     
6473 O  O     . ARG C 264 ? 0.9455 0.7078 0.7693 -0.0284 -0.0321 0.0430  257 ARG C O     
6474 C  CB    . ARG C 264 ? 0.8192 0.6657 0.6848 -0.0398 -0.0201 0.0371  257 ARG C CB    
6475 C  CG    . ARG C 264 ? 0.7614 0.6481 0.6471 -0.0462 -0.0146 0.0349  257 ARG C CG    
6476 C  CD    . ARG C 264 ? 0.7607 0.6423 0.6443 -0.0517 -0.0169 0.0257  257 ARG C CD    
6477 N  NE    . ARG C 264 ? 0.7579 0.6320 0.6358 -0.0341 -0.0137 0.0132  257 ARG C NE    
6478 C  CZ    . ARG C 264 ? 0.7866 0.6382 0.6484 -0.0325 -0.0155 0.0037  257 ARG C CZ    
6479 N  NH1   . ARG C 264 ? 0.8305 0.6548 0.6755 -0.0485 -0.0249 0.0041  257 ARG C NH1   
6480 N  NH2   . ARG C 264 ? 0.7817 0.6362 0.6422 -0.0148 -0.0083 -0.0054 257 ARG C NH2   
6481 N  N     . PRO C 269 ? 1.0493 0.9193 0.9731 -0.2203 -0.0711 0.1228  262 PRO C N     
6482 C  CA    . PRO C 269 ? 0.9742 0.9068 0.9297 -0.2083 -0.0574 0.1227  262 PRO C CA    
6483 C  C     . PRO C 269 ? 0.9805 0.9676 0.9740 -0.2240 -0.0495 0.1478  262 PRO C C     
6484 O  O     . PRO C 269 ? 1.0438 1.0261 1.0460 -0.2518 -0.0596 0.1656  262 PRO C O     
6485 C  CB    . PRO C 269 ? 0.9654 0.8969 0.9208 -0.2116 -0.0702 0.1095  262 PRO C CB    
6486 C  CG    . PRO C 269 ? 1.0223 0.8841 0.9354 -0.2138 -0.0856 0.0947  262 PRO C CG    
6487 C  CD    . PRO C 269 ? 1.0906 0.9198 0.9929 -0.2303 -0.0910 0.1091  262 PRO C CD    
6488 N  N     . SER C 270 ? 0.9226 0.9605 0.9379 -0.2059 -0.0313 0.1496  263 SER C N     
6489 C  CA    . SER C 270 ? 0.9291 1.0254 0.9820 -0.2143 -0.0198 0.1724  263 SER C CA    
6490 C  C     . SER C 270 ? 0.9396 1.0655 1.0231 -0.2325 -0.0337 0.1783  263 SER C C     
6491 O  O     . SER C 270 ? 0.9371 1.0353 1.0065 -0.2356 -0.0509 0.1625  263 SER C O     
6492 C  CB    . SER C 270 ? 0.8778 1.0103 0.9369 -0.1862 0.0032  0.1701  263 SER C CB    
6493 O  OG    . SER C 270 ? 0.8270 0.9803 0.8963 -0.1710 0.0037  0.1566  263 SER C OG    
6494 N  N     . LYS C 271 ? 0.9579 1.1415 1.0829 -0.2437 -0.0262 0.2022  264 LYS C N     
6495 C  CA    . LYS C 271 ? 0.9572 1.1840 1.1185 -0.2531 -0.0361 0.2088  264 LYS C CA    
6496 C  C     . LYS C 271 ? 0.8883 1.1335 1.0488 -0.2210 -0.0250 0.1918  264 LYS C C     
6497 O  O     . LYS C 271 ? 0.8500 1.0929 0.9945 -0.1947 -0.0054 0.1831  264 LYS C O     
6498 C  CB    . LYS C 271 ? 0.9980 1.2902 1.2100 -0.2703 -0.0284 0.2412  264 LYS C CB    
6499 C  CG    . LYS C 271 ? 1.0701 1.3478 1.2835 -0.3009 -0.0332 0.2625  264 LYS C CG    
6500 C  CD    . LYS C 271 ? 1.1313 1.4612 1.3973 -0.3347 -0.0439 0.2930  264 LYS C CD    
6501 C  CE    . LYS C 271 ? 1.2102 1.5238 1.4771 -0.3674 -0.0482 0.3164  264 LYS C CE    
6502 N  NZ    . LYS C 271 ? 1.2438 1.4674 1.4582 -0.3817 -0.0711 0.2992  264 LYS C NZ    
6503 N  N     . SER C 272 ? 0.8817 1.1431 1.0580 -0.2250 -0.0396 0.1883  265 SER C N     
6504 C  CA    . SER C 272 ? 0.8273 1.1021 1.0026 -0.1980 -0.0328 0.1739  265 SER C CA    
6505 C  C     . SER C 272 ? 0.8066 1.1332 1.0070 -0.1747 -0.0067 0.1847  265 SER C C     
6506 O  O     . SER C 272 ? 0.8396 1.2127 1.0743 -0.1823 0.0028  0.2083  265 SER C O     
6507 C  CB    . SER C 272 ? 0.8403 1.1258 1.0297 -0.2100 -0.0549 0.1734  265 SER C CB    
6508 O  OG    . SER C 272 ? 0.7987 1.1098 0.9971 -0.1850 -0.0469 0.1670  265 SER C OG    
6509 N  N     . ILE C 273 ? 0.7596 1.0775 0.9414 -0.1455 0.0053  0.1679  266 ILE C N     
6510 C  CA    . ILE C 273 ? 0.7511 1.1097 0.9492 -0.1203 0.0285  0.1751  266 ILE C CA    
6511 C  C     . ILE C 273 ? 0.7694 1.1854 1.0135 -0.1209 0.0257  0.1918  266 ILE C C     
6512 O  O     . ILE C 273 ? 0.7858 1.2476 1.0546 -0.1049 0.0455  0.2062  266 ILE C O     
6513 C  CB    . ILE C 273 ? 0.7078 1.0364 0.8720 -0.0916 0.0381  0.1527  266 ILE C CB    
6514 C  CG1   . ILE C 273 ? 0.6779 0.9859 0.8321 -0.0883 0.0228  0.1364  266 ILE C CG1   
6515 C  CG2   . ILE C 273 ? 0.7000 0.9841 0.8270 -0.0909 0.0419  0.1418  266 ILE C CG2   
6516 C  CD1   . ILE C 273 ? 0.6451 0.9312 0.7733 -0.0623 0.0324  0.1189  266 ILE C CD1   
6517 N  N     . LEU C 274 ? 0.7733 1.1851 1.0261 -0.1377 0.0013  0.1897  267 LEU C N     
6518 C  CA    . LEU C 274 ? 0.7944 1.2582 1.0907 -0.1403 -0.0076 0.2053  267 LEU C CA    
6519 C  C     . LEU C 274 ? 0.8488 1.3616 1.1916 -0.1672 -0.0126 0.2342  267 LEU C C     
6520 O  O     . LEU C 274 ? 0.8744 1.4432 1.2631 -0.1696 -0.0181 0.2525  267 LEU C O     
6521 C  CB    . LEU C 274 ? 0.7893 1.2238 1.0703 -0.1517 -0.0352 0.1923  267 LEU C CB    
6522 C  CG    . LEU C 274 ? 0.7433 1.1349 0.9840 -0.1290 -0.0328 0.1671  267 LEU C CG    
6523 C  CD1   . LEU C 274 ? 0.7519 1.1104 0.9716 -0.1442 -0.0593 0.1561  267 LEU C CD1   
6524 C  CD2   . LEU C 274 ? 0.7277 1.1503 0.9832 -0.0977 -0.0173 0.1691  267 LEU C CD2   
6525 N  N     . GLU C 275 ? 0.8721 1.3626 1.2035 -0.1891 -0.0131 0.2394  268 GLU C N     
6526 C  CA    . GLU C 275 ? 0.9320 1.4614 1.3043 -0.2206 -0.0202 0.2678  268 GLU C CA    
6527 C  C     . GLU C 275 ? 0.9503 1.5156 1.3388 -0.2112 0.0108  0.2866  268 GLU C C     
6528 O  O     . GLU C 275 ? 0.9971 1.6251 1.4366 -0.2244 0.0160  0.3161  268 GLU C O     
6529 C  CB    . GLU C 275 ? 0.9620 1.4323 1.3052 -0.2552 -0.0467 0.2610  268 GLU C CB    
6530 C  CG    . GLU C 275 ? 1.0352 1.5345 1.4176 -0.2963 -0.0663 0.2881  268 GLU C CG    
6531 C  CD    . GLU C 275 ? 1.0757 1.5037 1.4198 -0.3284 -0.0967 0.2770  268 GLU C CD    
6532 O  OE1   . GLU C 275 ? 1.1182 1.5226 1.4534 -0.3495 -0.0966 0.2870  268 GLU C OE1   
6533 O  OE2   . GLU C 275 ? 1.0717 1.4640 1.3907 -0.3308 -0.1198 0.2582  268 GLU C OE2   
6534 N  N     . VAL C 276 ? 0.9203 1.4477 1.2657 -0.1889 0.0310  0.2710  269 VAL C N     
6535 C  CA    . VAL C 276 ? 0.9479 1.4960 1.2954 -0.1822 0.0586  0.2873  269 VAL C CA    
6536 C  C     . VAL C 276 ? 0.9214 1.4764 1.2492 -0.1392 0.0878  0.2767  269 VAL C C     
6537 O  O     . VAL C 276 ? 0.9549 1.5401 1.2889 -0.1280 0.1141  0.2927  269 VAL C O     
6538 C  CB    . VAL C 276 ? 0.9639 1.4549 1.2731 -0.2019 0.0531  0.2835  269 VAL C CB    
6539 C  CG1   . VAL C 276 ? 1.0150 1.4989 1.3428 -0.2459 0.0270  0.2989  269 VAL C CG1   
6540 C  CG2   . VAL C 276 ? 0.9131 1.3323 1.1656 -0.1867 0.0461  0.2505  269 VAL C CG2   
6541 N  N     . GLY C 277 ? 0.8708 1.3932 1.1702 -0.1159 0.0836  0.2501  270 GLY C N     
6542 C  CA    . GLY C 277 ? 0.8534 1.3636 1.1217 -0.0787 0.1065  0.2361  270 GLY C CA    
6543 C  C     . GLY C 277 ? 0.8244 1.2662 1.0365 -0.0756 0.1033  0.2129  270 GLY C C     
6544 O  O     . GLY C 277 ? 0.8263 1.2360 1.0257 -0.0999 0.0890  0.2120  270 GLY C O     
6545 N  N     . VAL C 278 ? 0.8051 1.2242 0.9839 -0.0454 0.1152  0.1949  271 VAL C N     
6546 C  CA    . VAL C 278 ? 0.7770 1.1362 0.9072 -0.0407 0.1095  0.1726  271 VAL C CA    
6547 C  C     . VAL C 278 ? 0.8116 1.1592 0.9195 -0.0440 0.1216  0.1812  271 VAL C C     
6548 O  O     . VAL C 278 ? 0.8015 1.1070 0.8832 -0.0552 0.1105  0.1728  271 VAL C O     
6549 C  CB    . VAL C 278 ? 0.7569 1.0968 0.8610 -0.0107 0.1155  0.1527  271 VAL C CB    
6550 C  CG1   . VAL C 278 ? 0.7409 1.0274 0.7977 -0.0046 0.1119  0.1333  271 VAL C CG1   
6551 C  CG2   . VAL C 278 ? 0.7245 1.0669 0.8450 -0.0097 0.1010  0.1440  271 VAL C CG2   
6552 N  N     . GLN C 279 ? 0.8589 1.2449 0.9765 -0.0322 0.1455  0.1992  272 GLN C N     
6553 C  CA    . GLN C 279 ? 0.9020 1.2784 0.9933 -0.0315 0.1603  0.2088  272 GLN C CA    
6554 C  C     . GLN C 279 ? 0.9180 1.2889 1.0225 -0.0659 0.1479  0.2243  272 GLN C C     
6555 O  O     . GLN C 279 ? 0.9304 1.2627 1.0020 -0.0722 0.1446  0.2219  272 GLN C O     
6556 C  CB    . GLN C 279 ? 0.9599 1.3839 1.0609 -0.0113 0.1912  0.2274  272 GLN C CB    
6557 C  CG    . GLN C 279 ? 1.0129 1.4215 1.0758 -0.0066 0.2085  0.2359  272 GLN C CG    
6558 C  CD    . GLN C 279 ? 1.0832 1.5417 1.1551 0.0117  0.2421  0.2580  272 GLN C CD    
6559 O  OE1   . GLN C 279 ? 1.0959 1.6093 1.2114 0.0196  0.2538  0.2711  272 GLN C OE1   
6560 N  NE2   . GLN C 279 ? 1.1364 1.5772 1.1660 0.0198  0.2586  0.2636  272 GLN C NE2   
6561 N  N     . GLN C 280 ? 0.9264 1.3351 1.0784 -0.0882 0.1399  0.2413  273 GLN C N     
6562 C  CA    . GLN C 280 ? 0.9577 1.3615 1.1241 -0.1237 0.1270  0.2587  273 GLN C CA    
6563 C  C     . GLN C 280 ? 0.9243 1.2650 1.0632 -0.1374 0.0998  0.2377  273 GLN C C     
6564 O  O     . GLN C 280 ? 0.9502 1.2543 1.0669 -0.1525 0.0932  0.2412  273 GLN C O     
6565 C  CB    . GLN C 280 ? 0.9836 1.4464 1.2095 -0.1446 0.1229  0.2824  273 GLN C CB    
6566 C  CG    . GLN C 280 ? 1.0334 1.4939 1.2770 -0.1851 0.1090  0.3044  273 GLN C CG    
6567 C  CD    . GLN C 280 ? 1.0874 1.5454 1.3134 -0.1885 0.1285  0.3231  273 GLN C CD    
6568 O  OE1   . GLN C 280 ? 1.1140 1.6122 1.3446 -0.1682 0.1579  0.3364  273 GLN C OE1   
6569 N  NE2   . GLN C 280 ? 1.1115 1.5180 1.3124 -0.2122 0.1128  0.3240  273 GLN C NE2   
6570 N  N     . ALA C 281 ? 0.8736 1.2013 1.0126 -0.1303 0.0854  0.2168  274 ALA C N     
6571 C  CA    . ALA C 281 ? 0.8459 1.1182 0.9594 -0.1391 0.0626  0.1964  274 ALA C CA    
6572 C  C     . ALA C 281 ? 0.8340 1.0611 0.9026 -0.1232 0.0670  0.1815  274 ALA C C     
6573 O  O     . ALA C 281 ? 0.8437 1.0274 0.8912 -0.1345 0.0537  0.1762  274 ALA C O     
6574 C  CB    . ALA C 281 ? 0.8000 1.0731 0.9208 -0.1310 0.0513  0.1791  274 ALA C CB    
6575 N  N     . LEU C 282 ? 0.8226 1.0591 0.8761 -0.0968 0.0845  0.1757  275 LEU C N     
6576 C  CA    . LEU C 282 ? 0.8104 1.0062 0.8225 -0.0808 0.0847  0.1597  275 LEU C CA    
6577 C  C     . LEU C 282 ? 0.8589 1.0365 0.8498 -0.0884 0.0891  0.1731  275 LEU C C     
6578 O  O     . LEU C 282 ? 0.8574 0.9931 0.8210 -0.0880 0.0785  0.1636  275 LEU C O     
6579 C  CB    . LEU C 282 ? 0.7970 1.0036 0.7957 -0.0525 0.0988  0.1492  275 LEU C CB    
6580 C  CG    . LEU C 282 ? 0.7710 0.9375 0.7345 -0.0374 0.0913  0.1270  275 LEU C CG    
6581 C  CD1   . LEU C 282 ? 0.7230 0.8694 0.6933 -0.0438 0.0725  0.1108  275 LEU C CD1   
6582 C  CD2   . LEU C 282 ? 0.7765 0.9492 0.7231 -0.0122 0.1039  0.1184  275 LEU C CD2   
6583 N  N     . GLN C 283 ? 0.9081 1.1183 0.9137 -0.0964 0.1043  0.1973  276 GLN C N     
6584 C  CA    . GLN C 283 ? 0.9622 1.1539 0.9445 -0.1037 0.1096  0.2123  276 GLN C CA    
6585 C  C     . GLN C 283 ? 0.9799 1.1365 0.9630 -0.1305 0.0891  0.2169  276 GLN C C     
6586 O  O     . GLN C 283 ? 1.0256 1.1544 0.9849 -0.1372 0.0885  0.2272  276 GLN C O     
6587 C  CB    . GLN C 283 ? 1.0176 1.2562 1.0148 -0.1042 0.1344  0.2390  276 GLN C CB    
6588 C  CG    . GLN C 283 ? 1.0527 1.3229 1.0930 -0.1354 0.1318  0.2648  276 GLN C CG    
6589 C  CD    . GLN C 283 ? 1.1052 1.4346 1.1694 -0.1331 0.1594  0.2923  276 GLN C CD    
6590 O  OE1   . GLN C 283 ? 1.1255 1.4653 1.1654 -0.1070 0.1823  0.2924  276 GLN C OE1   
6591 N  NE2   . GLN C 283 ? 1.1358 1.5046 1.2472 -0.1605 0.1570  0.3165  276 GLN C NE2   
6592 N  N     . ALA C 284 ? 0.9529 1.1053 0.9578 -0.1446 0.0714  0.2089  277 ALA C N     
6593 C  CA    . ALA C 284 ? 0.9817 1.0939 0.9818 -0.1686 0.0508  0.2108  277 ALA C CA    
6594 C  C     . ALA C 284 ? 0.9569 1.0146 0.9236 -0.1562 0.0368  0.1872  277 ALA C C     
6595 O  O     . ALA C 284 ? 0.9859 1.0032 0.9425 -0.1709 0.0201  0.1855  277 ALA C O     
6596 C  CB    . ALA C 284 ? 0.9820 1.1124 1.0159 -0.1905 0.0374  0.2144  277 ALA C CB    
6597 N  N     . VAL C 285 ? 0.9113 0.9677 0.8618 -0.1295 0.0429  0.1697  278 VAL C N     
6598 C  CA    . VAL C 285 ? 0.8886 0.9034 0.8145 -0.1163 0.0311  0.1495  278 VAL C CA    
6599 C  C     . VAL C 285 ? 0.8884 0.8966 0.7883 -0.0953 0.0389  0.1461  278 VAL C C     
6600 O  O     . VAL C 285 ? 0.8898 0.9254 0.7881 -0.0858 0.0538  0.1515  278 VAL C O     
6601 C  CB    . VAL C 285 ? 0.8306 0.8498 0.7671 -0.1078 0.0244  0.1286  278 VAL C CB    
6602 C  CG1   . VAL C 285 ? 0.8409 0.8517 0.7914 -0.1274 0.0112  0.1281  278 VAL C CG1   
6603 C  CG2   . VAL C 285 ? 0.7904 0.8497 0.7406 -0.0939 0.0371  0.1245  278 VAL C CG2   
6604 N  N     . PHE C 286 ? 0.8917 0.8625 0.7702 -0.0867 0.0277  0.1361  279 PHE C N     
6605 C  CA    . PHE C 286 ? 0.8937 0.8555 0.7479 -0.0677 0.0291  0.1310  279 PHE C CA    
6606 C  C     . PHE C 286 ? 0.8357 0.8067 0.6957 -0.0520 0.0257  0.1100  279 PHE C C     
6607 O  O     . PHE C 286 ? 0.8060 0.7695 0.6783 -0.0529 0.0173  0.0982  279 PHE C O     
6608 C  CB    . PHE C 286 ? 0.9379 0.8579 0.7700 -0.0668 0.0175  0.1350  279 PHE C CB    
6609 C  CG    . PHE C 286 ? 0.9497 0.8601 0.7568 -0.0485 0.0150  0.1320  279 PHE C CG    
6610 C  CD1   . PHE C 286 ? 0.9864 0.9051 0.7724 -0.0452 0.0251  0.1441  279 PHE C CD1   
6611 C  CD2   . PHE C 286 ? 0.9305 0.8258 0.7353 -0.0344 0.0024  0.1177  279 PHE C CD2   
6612 C  CE1   . PHE C 286 ? 1.0060 0.9129 0.7645 -0.0293 0.0195  0.1407  279 PHE C CE1   
6613 C  CE2   . PHE C 286 ? 0.9466 0.8362 0.7314 -0.0195 -0.0033 0.1161  279 PHE C CE2   
6614 C  CZ    . PHE C 286 ? 0.9853 0.8782 0.7449 -0.0177 0.0036  0.1269  279 PHE C CZ    
6615 N  N     . TRP C 287 ? 0.8295 0.8144 0.6777 -0.0386 0.0326  0.1063  280 TRP C N     
6616 C  CA    . TRP C 287 ? 0.7900 0.7782 0.6382 -0.0251 0.0274  0.0886  280 TRP C CA    
6617 C  C     . TRP C 287 ? 0.8197 0.7945 0.6385 -0.0125 0.0230  0.0872  280 TRP C C     
6618 O  O     . TRP C 287 ? 0.8555 0.8344 0.6526 -0.0079 0.0326  0.0943  280 TRP C O     
6619 C  CB    . TRP C 287 ? 0.7614 0.7773 0.6229 -0.0225 0.0379  0.0839  280 TRP C CB    
6620 C  CG    . TRP C 287 ? 0.7287 0.7449 0.5891 -0.0114 0.0322  0.0670  280 TRP C CG    
6621 C  CD1   . TRP C 287 ? 0.6991 0.7063 0.5683 -0.0100 0.0201  0.0554  280 TRP C CD1   
6622 C  CD2   . TRP C 287 ? 0.7318 0.7567 0.5812 -0.0005 0.0390  0.0610  280 TRP C CD2   
6623 N  NE1   . TRP C 287 ? 0.6821 0.6933 0.5491 -0.0024 0.0178  0.0442  280 TRP C NE1   
6624 C  CE2   . TRP C 287 ? 0.7042 0.7218 0.5560 0.0038  0.0280  0.0463  280 TRP C CE2   
6625 C  CE3   . TRP C 287 ? 0.7641 0.8007 0.6000 0.0070  0.0541  0.0672  280 TRP C CE3   
6626 C  CZ2   . TRP C 287 ? 0.7101 0.7259 0.5490 0.0132  0.0289  0.0370  280 TRP C CZ2   
6627 C  CZ3   . TRP C 287 ? 0.7714 0.8050 0.5918 0.0202  0.0565  0.0564  280 TRP C CZ3   
6628 C  CH2   . TRP C 287 ? 0.7464 0.7666 0.5666 0.0222  0.0427  0.0412  280 TRP C CH2   
6629 N  N     . ASP C 288 ? 0.8115 0.7716 0.6291 -0.0062 0.0083  0.0785  281 ASP C N     
6630 C  CA    . ASP C 288 ? 0.8442 0.7918 0.6364 0.0041  -0.0011 0.0775  281 ASP C CA    
6631 C  C     . ASP C 288 ? 0.8263 0.7832 0.6146 0.0113  -0.0042 0.0639  281 ASP C C     
6632 O  O     . ASP C 288 ? 0.7933 0.7552 0.5998 0.0127  -0.0141 0.0530  281 ASP C O     
6633 C  CB    . ASP C 288 ? 0.8558 0.7864 0.6520 0.0077  -0.0160 0.0783  281 ASP C CB    
6634 C  CG    . ASP C 288 ? 0.9003 0.8185 0.6714 0.0174  -0.0291 0.0809  281 ASP C CG    
6635 O  OD1   . ASP C 288 ? 0.9205 0.8403 0.6683 0.0210  -0.0287 0.0787  281 ASP C OD1   
6636 O  OD2   . ASP C 288 ? 0.9211 0.8262 0.6944 0.0223  -0.0404 0.0851  281 ASP C OD2   
6637 N  N     . GLU C 289 ? 0.8579 0.8150 0.6198 0.0160  0.0046  0.0654  282 GLU C N     
6638 C  CA    . GLU C 289 ? 0.8558 0.8137 0.6067 0.0228  0.0028  0.0525  282 GLU C CA    
6639 C  C     . GLU C 289 ? 0.8850 0.8260 0.6158 0.0275  -0.0178 0.0453  282 GLU C C     
6640 O  O     . GLU C 289 ? 0.8772 0.8164 0.6082 0.0286  -0.0266 0.0333  282 GLU C O     
6641 C  CB    . GLU C 289 ? 0.8939 0.8542 0.6188 0.0296  0.0210  0.0565  282 GLU C CB    
6642 C  CG    . GLU C 289 ? 0.8826 0.8456 0.6059 0.0364  0.0242  0.0432  282 GLU C CG    
6643 C  CD    . GLU C 289 ? 0.9177 0.8876 0.6225 0.0474  0.0457  0.0462  282 GLU C CD    
6644 O  OE1   . GLU C 289 ? 0.9162 0.8827 0.6169 0.0552  0.0472  0.0347  282 GLU C OE1   
6645 O  OE2   . GLU C 289 ? 0.9535 0.9317 0.6474 0.0491  0.0612  0.0607  282 GLU C OE2   
6646 N  N     . GLU C 290 ? 0.9270 0.8545 0.6391 0.0295  -0.0273 0.0539  283 GLU C N     
6647 C  CA    . GLU C 290 ? 0.9558 0.8721 0.6563 0.0325  -0.0508 0.0493  283 GLU C CA    
6648 C  C     . GLU C 290 ? 0.9054 0.8377 0.6506 0.0285  -0.0629 0.0444  283 GLU C C     
6649 O  O     . GLU C 290 ? 0.9027 0.8392 0.6560 0.0268  -0.0777 0.0357  283 GLU C O     
6650 C  CB    . GLU C 290 ? 1.0154 0.9149 0.6879 0.0367  -0.0590 0.0619  283 GLU C CB    
6651 C  CG    . GLU C 290 ? 1.0826 0.9647 0.7031 0.0422  -0.0485 0.0676  283 GLU C CG    
6652 C  CD    . GLU C 290 ? 1.1479 1.0116 0.7368 0.0455  -0.0537 0.0830  283 GLU C CD    
6653 O  OE1   . GLU C 290 ? 1.1379 1.0016 0.7486 0.0434  -0.0613 0.0921  283 GLU C OE1   
6654 O  OE2   . GLU C 290 ? 1.2173 1.0635 0.7557 0.0517  -0.0496 0.0863  283 GLU C OE2   
6655 N  N     . ALA C 291 ? 0.8713 0.8121 0.6448 0.0263  -0.0553 0.0501  284 ALA C N     
6656 C  CA    . ALA C 291 ? 0.8301 0.7863 0.6433 0.0255  -0.0617 0.0458  284 ALA C CA    
6657 C  C     . ALA C 291 ? 0.7858 0.7569 0.6182 0.0202  -0.0576 0.0345  284 ALA C C     
6658 O  O     . ALA C 291 ? 0.7702 0.7545 0.6259 0.0188  -0.0677 0.0295  284 ALA C O     
6659 C  CB    . ALA C 291 ? 0.8155 0.7691 0.6444 0.0253  -0.0526 0.0522  284 ALA C CB    
6660 N  N     . PHE C 292 ? 0.7701 0.7408 0.5942 0.0172  -0.0422 0.0320  285 PHE C N     
6661 C  CA    . PHE C 292 ? 0.7333 0.7146 0.5732 0.0132  -0.0378 0.0227  285 PHE C CA    
6662 C  C     . PHE C 292 ? 0.7569 0.7321 0.5850 0.0128  -0.0522 0.0148  285 PHE C C     
6663 O  O     . PHE C 292 ? 0.7357 0.7205 0.5857 0.0077  -0.0589 0.0093  285 PHE C O     
6664 C  CB    . PHE C 292 ? 0.7263 0.7086 0.5569 0.0130  -0.0199 0.0240  285 PHE C CB    
6665 C  CG    . PHE C 292 ? 0.7072 0.6940 0.5421 0.0126  -0.0154 0.0153  285 PHE C CG    
6666 C  CD1   . PHE C 292 ? 0.6614 0.6614 0.5261 0.0072  -0.0133 0.0118  285 PHE C CD1   
6667 C  CD2   . PHE C 292 ? 0.7436 0.7179 0.5487 0.0191  -0.0124 0.0110  285 PHE C CD2   
6668 C  CE1   . PHE C 292 ? 0.6497 0.6510 0.5167 0.0072  -0.0098 0.0054  285 PHE C CE1   
6669 C  CE2   . PHE C 292 ? 0.7339 0.7078 0.5411 0.0207  -0.0084 0.0034  285 PHE C CE2   
6670 C  CZ    . PHE C 292 ? 0.6853 0.6733 0.5247 0.0141  -0.0075 0.0014  285 PHE C CZ    
6671 N  N     . VAL C 293 ? 0.8114 0.7677 0.6012 0.0172  -0.0584 0.0147  286 VAL C N     
6672 C  CA    . VAL C 293 ? 0.8507 0.7932 0.6216 0.0152  -0.0761 0.0067  286 VAL C CA    
6673 C  C     . VAL C 293 ? 0.8557 0.8097 0.6507 0.0098  -0.0982 0.0090  286 VAL C C     
6674 O  O     . VAL C 293 ? 0.8565 0.8151 0.6662 0.0017  -0.1113 0.0038  286 VAL C O     
6675 C  CB    . VAL C 293 ? 0.9207 0.8354 0.6365 0.0230  -0.0765 0.0055  286 VAL C CB    
6676 C  CG1   . VAL C 293 ? 0.9800 0.8736 0.6697 0.0197  -0.1019 -0.0019 286 VAL C CG1   
6677 C  CG2   . VAL C 293 ? 0.9233 0.8313 0.6197 0.0302  -0.0542 0.0021  286 VAL C CG2   
6678 N  N     . GLU C 294 ? 0.8651 0.8248 0.6659 0.0144  -0.1027 0.0185  287 GLU C N     
6679 C  CA    . GLU C 294 ? 0.8793 0.8539 0.7043 0.0131  -0.1234 0.0234  287 GLU C CA    
6680 C  C     . GLU C 294 ? 0.8301 0.8342 0.7060 0.0077  -0.1216 0.0224  287 GLU C C     
6681 O  O     . GLU C 294 ? 0.8456 0.8655 0.7435 0.0014  -0.1396 0.0234  287 GLU C O     
6682 C  CB    . GLU C 294 ? 0.9004 0.8728 0.7213 0.0226  -0.1250 0.0347  287 GLU C CB    
6683 C  CG    . GLU C 294 ? 0.9226 0.9136 0.7707 0.0250  -0.1466 0.0415  287 GLU C CG    
6684 C  CD    . GLU C 294 ? 0.9756 0.9533 0.8015 0.0347  -0.1572 0.0523  287 GLU C CD    
6685 O  OE1   . GLU C 294 ? 1.0211 0.9714 0.7981 0.0352  -0.1592 0.0525  287 GLU C OE1   
6686 O  OE2   . GLU C 294 ? 0.9801 0.9735 0.8349 0.0433  -0.1636 0.0612  287 GLU C OE2   
6687 N  N     . ARG C 295 ? 0.7779 0.7901 0.6717 0.0090  -0.1005 0.0212  288 ARG C N     
6688 C  CA    . ARG C 295 ? 0.7397 0.7785 0.6769 0.0065  -0.0962 0.0215  288 ARG C CA    
6689 C  C     . ARG C 295 ? 0.7262 0.7687 0.6707 -0.0049 -0.0973 0.0146  288 ARG C C     
6690 O  O     . ARG C 295 ? 0.6999 0.7647 0.6780 -0.0086 -0.0928 0.0158  288 ARG C O     
6691 C  CB    . ARG C 295 ? 0.7023 0.7427 0.6494 0.0124  -0.0759 0.0226  288 ARG C CB    
6692 C  CG    . ARG C 295 ? 0.6757 0.7036 0.6062 0.0081  -0.0602 0.0170  288 ARG C CG    
6693 C  CD    . ARG C 295 ? 0.6436 0.6760 0.5893 0.0101  -0.0451 0.0175  288 ARG C CD    
6694 N  NE    . ARG C 295 ? 0.6253 0.6487 0.5574 0.0060  -0.0325 0.0152  288 ARG C NE    
6695 C  CZ    . ARG C 295 ? 0.6017 0.6299 0.5379 0.0007  -0.0269 0.0100  288 ARG C CZ    
6696 N  NH1   . ARG C 295 ? 0.5940 0.6323 0.5446 -0.0030 -0.0320 0.0064  288 ARG C NH1   
6697 N  NH2   . ARG C 295 ? 0.5906 0.6146 0.5181 -0.0011 -0.0162 0.0103  288 ARG C NH2   
6698 N  N     . GLY C 296 ? 0.7508 0.7688 0.6606 -0.0088 -0.1013 0.0080  289 GLY C N     
6699 C  CA    . GLY C 296 ? 0.7525 0.7626 0.6591 -0.0184 -0.1036 0.0009  289 GLY C CA    
6700 C  C     . GLY C 296 ? 0.7142 0.7190 0.6169 -0.0161 -0.0826 -0.0033 289 GLY C C     
6701 O  O     . GLY C 296 ? 0.7008 0.7085 0.6165 -0.0234 -0.0811 -0.0060 289 GLY C O     
6702 N  N     . GLY C 297 ? 0.7075 0.7027 0.5896 -0.0071 -0.0685 -0.0030 290 GLY C N     
6703 C  CA    . GLY C 297 ? 0.6754 0.6710 0.5578 -0.0045 -0.0498 -0.0047 290 GLY C CA    
6704 C  C     . GLY C 297 ? 0.6978 0.6739 0.5561 -0.0032 -0.0479 -0.0119 290 GLY C C     
6705 O  O     . GLY C 297 ? 0.6722 0.6525 0.5391 -0.0026 -0.0365 -0.0131 290 GLY C O     
6706 N  N     . ILE C 298 ? 0.7544 0.7060 0.5787 -0.0011 -0.0597 -0.0168 291 ILE C N     
6707 C  CA    . ILE C 298 ? 0.7931 0.7177 0.5900 0.0008  -0.0620 -0.0255 291 ILE C CA    
6708 C  C     . ILE C 298 ? 0.8149 0.7313 0.6203 -0.0133 -0.0831 -0.0289 291 ILE C C     
6709 O  O     . ILE C 298 ? 0.8436 0.7594 0.6481 -0.0201 -0.1016 -0.0275 291 ILE C O     
6710 C  CB    . ILE C 298 ? 0.8583 0.7540 0.6039 0.0132  -0.0608 -0.0300 291 ILE C CB    
6711 C  CG1   . ILE C 298 ? 0.8443 0.7537 0.5852 0.0250  -0.0393 -0.0229 291 ILE C CG1   
6712 C  CG2   . ILE C 298 ? 0.9100 0.7713 0.6225 0.0187  -0.0625 -0.0405 291 ILE C CG2   
6713 C  CD1   . ILE C 298 ? 0.8159 0.7374 0.5690 0.0323  -0.0188 -0.0214 291 ILE C CD1   
6714 N  N     . TYR C 299 ? 0.8083 0.7184 0.6223 -0.0185 -0.0816 -0.0318 292 TYR C N     
6715 C  CA    . TYR C 299 ? 0.8327 0.7364 0.6585 -0.0354 -0.1008 -0.0323 292 TYR C CA    
6716 C  C     . TYR C 299 ? 0.8496 0.7293 0.6648 -0.0370 -0.0979 -0.0370 292 TYR C C     
6717 O  O     . TYR C 299 ? 0.8459 0.7145 0.6431 -0.0222 -0.0820 -0.0404 292 TYR C O     
6718 C  CB    . TYR C 299 ? 0.7855 0.7305 0.6626 -0.0467 -0.1023 -0.0223 292 TYR C CB    
6719 C  CG    . TYR C 299 ? 0.7220 0.6936 0.6309 -0.0450 -0.0826 -0.0171 292 TYR C CG    
6720 C  CD1   . TYR C 299 ? 0.6775 0.6662 0.5935 -0.0336 -0.0655 -0.0147 292 TYR C CD1   
6721 C  CD2   . TYR C 299 ? 0.7154 0.6930 0.6451 -0.0563 -0.0826 -0.0138 292 TYR C CD2   
6722 C  CE1   . TYR C 299 ? 0.6313 0.6395 0.5710 -0.0332 -0.0508 -0.0109 292 TYR C CE1   
6723 C  CE2   . TYR C 299 ? 0.6674 0.6665 0.6203 -0.0545 -0.0657 -0.0092 292 TYR C CE2   
6724 C  CZ    . TYR C 299 ? 0.6262 0.6397 0.5828 -0.0427 -0.0506 -0.0086 292 TYR C CZ    
6725 O  OH    . TYR C 299 ? 0.5899 0.6200 0.5641 -0.0418 -0.0368 -0.0050 292 TYR C OH    
6726 N  N     . ASP C 300 ? 0.8775 0.7487 0.7035 -0.0549 -0.1146 -0.0357 293 ASP C N     
6727 C  CA    . ASP C 300 ? 0.9108 0.7504 0.7218 -0.0586 -0.1164 -0.0394 293 ASP C CA    
6728 C  C     . ASP C 300 ? 0.8466 0.7161 0.6939 -0.0595 -0.0987 -0.0312 293 ASP C C     
6729 O  O     . ASP C 300 ? 0.8253 0.7199 0.7086 -0.0752 -0.1015 -0.0222 293 ASP C O     
6730 C  CB    . ASP C 300 ? 0.9822 0.7942 0.7846 -0.0801 -0.1439 -0.0404 293 ASP C CB    
6731 C  CG    . ASP C 300 ? 1.0720 0.8329 0.8184 -0.0765 -0.1624 -0.0526 293 ASP C CG    
6732 O  OD1   . ASP C 300 ? 1.0875 0.8268 0.7943 -0.0536 -0.1497 -0.0614 293 ASP C OD1   
6733 O  OD2   . ASP C 300 ? 1.1332 0.8765 0.8748 -0.0969 -0.1896 -0.0526 293 ASP C OD2   
6734 N  N     . TRP C 301 ? 0.8200 0.6896 0.6573 -0.0415 -0.0798 -0.0334 294 TRP C N     
6735 C  CA    . TRP C 301 ? 0.7541 0.6576 0.6229 -0.0390 -0.0625 -0.0261 294 TRP C CA    
6736 C  C     . TRP C 301 ? 0.7658 0.6512 0.6272 -0.0356 -0.0568 -0.0256 294 TRP C C     
6737 O  O     . TRP C 301 ? 0.7242 0.6297 0.6014 -0.0301 -0.0432 -0.0208 294 TRP C O     
6738 C  CB    . TRP C 301 ? 0.7157 0.6404 0.5859 -0.0247 -0.0486 -0.0259 294 TRP C CB    
6739 C  CG    . TRP C 301 ? 0.7468 0.6509 0.5830 -0.0067 -0.0415 -0.0318 294 TRP C CG    
6740 C  CD1   . TRP C 301 ? 0.7956 0.6673 0.6018 0.0044  -0.0400 -0.0376 294 TRP C CD1   
6741 C  CD2   . TRP C 301 ? 0.7362 0.6533 0.5656 0.0039  -0.0323 -0.0308 294 TRP C CD2   
6742 N  NE1   . TRP C 301 ? 0.8136 0.6826 0.5977 0.0231  -0.0280 -0.0399 294 TRP C NE1   
6743 C  CE2   . TRP C 301 ? 0.7781 0.6751 0.5759 0.0214  -0.0234 -0.0352 294 TRP C CE2   
6744 C  CE3   . TRP C 301 ? 0.7026 0.6449 0.5488 0.0009  -0.0302 -0.0257 294 TRP C CE3   
6745 C  CZ2   . TRP C 301 ? 0.7851 0.6913 0.5702 0.0342  -0.0113 -0.0330 294 TRP C CZ2   
6746 C  CZ3   . TRP C 301 ? 0.7104 0.6563 0.5417 0.0119  -0.0207 -0.0239 294 TRP C CZ3   
6747 C  CH2   . TRP C 301 ? 0.7493 0.6801 0.5521 0.0275  -0.0104 -0.0267 294 TRP C CH2   
6748 N  N     . ASN C 302 ? 0.8314 0.6752 0.6667 -0.0399 -0.0697 -0.0302 295 ASN C N     
6749 C  CA    . ASN C 302 ? 0.8514 0.6757 0.6835 -0.0418 -0.0686 -0.0270 295 ASN C CA    
6750 C  C     . ASN C 302 ? 0.9223 0.7087 0.7396 -0.0603 -0.0896 -0.0281 295 ASN C C     
6751 O  O     . ASN C 302 ? 0.9552 0.7318 0.7638 -0.0699 -0.1052 -0.0321 295 ASN C O     
6752 C  CB    . ASN C 302 ? 0.8657 0.6724 0.6743 -0.0176 -0.0563 -0.0312 295 ASN C CB    
6753 C  CG    . ASN C 302 ? 0.9281 0.6980 0.6936 -0.0007 -0.0590 -0.0428 295 ASN C CG    
6754 O  OD1   . ASN C 302 ? 0.9992 0.7255 0.7344 -0.0075 -0.0758 -0.0498 295 ASN C OD1   
6755 N  ND2   . ASN C 302 ? 0.9104 0.6967 0.6712 0.0207  -0.0427 -0.0441 295 ASN C ND2   
6756 N  N     . LYS C 303 ? 0.9520 0.7162 0.7664 -0.0672 -0.0921 -0.0231 296 LYS C N     
6757 C  CA    . LYS C 303 ? 1.0271 0.7533 0.8290 -0.0890 -0.1136 -0.0219 296 LYS C CA    
6758 C  C     . LYS C 303 ? 1.1168 0.7802 0.8643 -0.0793 -0.1278 -0.0365 296 LYS C C     
6759 O  O     . LYS C 303 ? 1.1872 0.8173 0.9187 -0.0986 -0.1510 -0.0390 296 LYS C O     
6760 C  CB    . LYS C 303 ? 1.0422 0.7585 0.8531 -0.0997 -0.1119 -0.0108 296 LYS C CB    
6761 C  CG    . LYS C 303 ? 1.0734 0.7518 0.8530 -0.0780 -0.1044 -0.0146 296 LYS C CG    
6762 C  CD    . LYS C 303 ? 1.1071 0.7661 0.8892 -0.0910 -0.1072 -0.0026 296 LYS C CD    
6763 C  CE    . LYS C 303 ? 1.1665 0.8056 0.9535 -0.1243 -0.1275 0.0047  296 LYS C CE    
6764 N  NZ    . LYS C 303 ? 1.2248 0.8281 1.0015 -0.1354 -0.1321 0.0157  296 LYS C NZ    
6765 N  N     . SER C 304 ? 1.1224 0.7696 0.8406 -0.0493 -0.1140 -0.0457 297 SER C N     
6766 C  CA    . SER C 304 ? 1.2121 0.8010 0.8734 -0.0334 -0.1223 -0.0607 297 SER C CA    
6767 C  C     . SER C 304 ? 1.2180 0.8143 0.8688 -0.0367 -0.1314 -0.0677 297 SER C C     
6768 O  O     . SER C 304 ? 1.3073 0.8501 0.9045 -0.0273 -0.1422 -0.0810 297 SER C O     
6769 C  CB    . SER C 304 ? 1.2167 0.7971 0.8563 0.0017  -0.1013 -0.0657 297 SER C CB    
6770 O  OG    . SER C 304 ? 1.2277 0.7941 0.8712 0.0063  -0.0967 -0.0592 297 SER C OG    
6771 N  N1    . CTP D .   ? 0.3757 0.3200 0.3365 -0.0084 0.0158  -0.0005 401 CTP A N1    
6772 C  C2    . CTP D .   ? 0.3802 0.3249 0.3456 -0.0015 0.0167  -0.0033 401 CTP A C2    
6773 N  N3    . CTP D .   ? 0.3907 0.3413 0.3620 0.0046  0.0142  -0.0030 401 CTP A N3    
6774 C  C4    . CTP D .   ? 0.3969 0.3506 0.3681 0.0035  0.0094  0.0004  401 CTP A C4    
6775 C  C5    . CTP D .   ? 0.3950 0.3454 0.3581 -0.0037 0.0081  0.0034  401 CTP A C5    
6776 C  C6    . CTP D .   ? 0.3840 0.3310 0.3428 -0.0092 0.0121  0.0026  401 CTP A C6    
6777 O  O2    . CTP D .   ? 0.3765 0.3187 0.3407 -0.0010 0.0200  -0.0062 401 CTP A O2    
6778 N  N4    . CTP D .   ? 0.4099 0.3710 0.3883 0.0104  0.0058  0.0009  401 CTP A N4    
6779 C  "C1'" . CTP D .   ? 0.3671 0.3093 0.3246 -0.0138 0.0186  -0.0010 401 CTP A "C1'" 
6780 C  "C2'" . CTP D .   ? 0.3540 0.3061 0.3132 -0.0173 0.0215  -0.0024 401 CTP A "C2'" 
6781 O  "O2'" . CTP D .   ? 0.3436 0.3001 0.3080 -0.0159 0.0241  -0.0057 401 CTP A "O2'" 
6782 C  "C3'" . CTP D .   ? 0.3550 0.3061 0.3110 -0.0218 0.0227  -0.0011 401 CTP A "C3'" 
6783 C  "C4'" . CTP D .   ? 0.3733 0.3146 0.3239 -0.0241 0.0189  0.0036  401 CTP A "C4'" 
6784 O  "O4'" . CTP D .   ? 0.3808 0.3155 0.3317 -0.0181 0.0159  0.0032  401 CTP A "O4'" 
6785 O  "O3'" . CTP D .   ? 0.3480 0.2982 0.3062 -0.0215 0.0242  -0.0034 401 CTP A "O3'" 
6786 C  "C5'" . CTP D .   ? 0.3861 0.3308 0.3314 -0.0294 0.0184  0.0089  401 CTP A "C5'" 
6787 O  "O5'" . CTP D .   ? 0.3826 0.3372 0.3297 -0.0342 0.0221  0.0089  401 CTP A "O5'" 
6788 P  PA    . CTP D .   ? 0.3880 0.3575 0.3322 -0.0366 0.0261  0.0099  401 CTP A PA    
6789 O  O1A   . CTP D .   ? 0.4047 0.3707 0.3400 -0.0375 0.0235  0.0144  401 CTP A O1A   
6790 O  O2A   . CTP D .   ? 0.3907 0.3721 0.3395 -0.0411 0.0297  0.0109  401 CTP A O2A   
6791 O  O3A   . CTP D .   ? 0.3716 0.3464 0.3195 -0.0299 0.0284  0.0019  401 CTP A O3A   
6792 P  PB    . CTP D .   ? 0.3750 0.3607 0.3207 -0.0268 0.0321  -0.0033 401 CTP A PB    
6793 O  O1B   . CTP D .   ? 0.3686 0.3478 0.3148 -0.0227 0.0295  -0.0085 401 CTP A O1B   
6794 O  O2B   . CTP D .   ? 0.3740 0.3705 0.3255 -0.0259 0.0362  -0.0053 401 CTP A O2B   
6795 O  O3B   . CTP D .   ? 0.3961 0.3867 0.3313 -0.0306 0.0323  0.0014  401 CTP A O3B   
6796 P  PG    . CTP D .   ? 0.4159 0.4196 0.3417 -0.0293 0.0366  -0.0016 401 CTP A PG    
6797 O  O1G   . CTP D .   ? 0.4318 0.4305 0.3463 -0.0314 0.0323  0.0025  401 CTP A O1G   
6798 O  O2G   . CTP D .   ? 0.4272 0.4460 0.3549 -0.0339 0.0424  0.0031  401 CTP A O2G   
6799 O  O3G   . CTP D .   ? 0.4122 0.4164 0.3396 -0.0220 0.0376  -0.0118 401 CTP A O3G   
6800 FE FE1   . SF4 E .   ? 0.5497 0.3684 0.4495 -0.0381 -0.0208 -0.0185 402 SF4 A FE1   
6801 FE FE2   . SF4 E .   ? 0.5141 0.3605 0.4139 -0.0292 -0.0122 -0.0271 402 SF4 A FE2   
6802 FE FE3   . SF4 E .   ? 0.4698 0.3411 0.3924 -0.0371 -0.0051 -0.0122 402 SF4 A FE3   
6803 FE FE4   . SF4 E .   ? 0.5033 0.3469 0.4086 -0.0147 -0.0046 -0.0245 402 SF4 A FE4   
6804 S  S1    . SF4 E .   ? 0.4593 0.3343 0.3743 -0.0197 0.0022  -0.0223 402 SF4 A S1    
6805 S  S2    . SF4 E .   ? 0.5015 0.3456 0.4156 -0.0305 -0.0090 -0.0113 402 SF4 A S2    
6806 S  S3    . SF4 E .   ? 0.5647 0.3745 0.4487 -0.0175 -0.0172 -0.0344 402 SF4 A S3    
6807 S  S4    . SF4 E .   ? 0.5202 0.3699 0.4320 -0.0495 -0.0192 -0.0158 402 SF4 A S4    
6808 N  N     . SAM F .   ? 0.4286 0.3346 0.3656 -0.0392 0.0012  -0.0100 403 SAM A N     
6809 C  CA    . SAM F .   ? 0.4121 0.3347 0.3599 -0.0432 0.0051  -0.0044 403 SAM A CA    
6810 C  C     . SAM F .   ? 0.4313 0.3461 0.3778 -0.0512 0.0021  0.0009  403 SAM A C     
6811 O  O     . SAM F .   ? 0.4254 0.3550 0.3788 -0.0560 0.0053  0.0060  403 SAM A O     
6812 O  OXT   . SAM F .   ? 0.4552 0.3484 0.3924 -0.0511 -0.0030 -0.0004 403 SAM A OXT   
6813 C  CB    . SAM F .   ? 0.3884 0.3189 0.3391 -0.0355 0.0119  -0.0048 403 SAM A CB    
6814 C  CG    . SAM F .   ? 0.3892 0.3091 0.3345 -0.0284 0.0133  -0.0072 403 SAM A CG    
6815 S  SD    . SAM F .   ? 0.4108 0.3146 0.3507 -0.0286 0.0095  -0.0047 403 SAM A SD    
6816 C  CE    . SAM F .   ? 0.4118 0.3109 0.3489 -0.0164 0.0120  -0.0102 403 SAM A CE    
6817 C  "C5'" . SAM F .   ? 0.3923 0.3117 0.3389 -0.0296 0.0140  0.0000  403 SAM A "C5'" 
6818 C  "C4'" . SAM F .   ? 0.4111 0.3241 0.3540 -0.0349 0.0108  0.0063  403 SAM A "C4'" 
6819 O  "O4'" . SAM F .   ? 0.4257 0.3247 0.3639 -0.0284 0.0074  0.0060  403 SAM A "O4'" 
6820 C  "C3'" . SAM F .   ? 0.4350 0.3394 0.3748 -0.0450 0.0061  0.0103  403 SAM A "C3'" 
6821 O  "O3'" . SAM F .   ? 0.4434 0.3570 0.3840 -0.0539 0.0072  0.0180  403 SAM A "O3'" 
6822 C  "C2'" . SAM F .   ? 0.4631 0.3419 0.3941 -0.0414 -0.0005 0.0091  403 SAM A "C2'" 
6823 O  "O2'" . SAM F .   ? 0.4972 0.3604 0.4223 -0.0517 -0.0071 0.0151  403 SAM A "O2'" 
6824 C  "C1'" . SAM F .   ? 0.4580 0.3378 0.3887 -0.0330 0.0009  0.0101  403 SAM A "C1'" 
6825 N  N9    . SAM F .   ? 0.4778 0.3402 0.4037 -0.0229 -0.0032 0.0065  403 SAM A N9    
6826 C  C8    . SAM F .   ? 0.4875 0.3397 0.4102 -0.0161 -0.0043 -0.0012 403 SAM A C8    
6827 N  N7    . SAM F .   ? 0.5104 0.3492 0.4292 -0.0054 -0.0075 -0.0040 403 SAM A N7    
6828 C  C5    . SAM F .   ? 0.5155 0.3548 0.4356 -0.0057 -0.0099 0.0031  403 SAM A C5    
6829 C  C6    . SAM F .   ? 0.5393 0.3689 0.4578 0.0043  -0.0147 0.0044  403 SAM A C6    
6830 N  N6    . SAM F .   ? 0.5622 0.3810 0.4791 0.0179  -0.0168 -0.0025 403 SAM A N6    
6831 N  N1    . SAM F .   ? 0.5409 0.3750 0.4598 0.0012  -0.0169 0.0128  403 SAM A N1    
6832 C  C2    . SAM F .   ? 0.5214 0.3686 0.4409 -0.0110 -0.0135 0.0185  403 SAM A C2    
6833 N  N3    . SAM F .   ? 0.4983 0.3570 0.4207 -0.0200 -0.0080 0.0171  403 SAM A N3    
6834 C  C4    . SAM F .   ? 0.4964 0.3496 0.4194 -0.0170 -0.0071 0.0097  403 SAM A C4    
6835 FE FE1   . SF4 G .   ? 0.4067 0.4430 0.4581 0.0616  -0.0236 -0.0170 401 SF4 B FE1   
6836 FE FE2   . SF4 G .   ? 0.4277 0.4736 0.4839 0.0801  -0.0169 -0.0259 401 SF4 B FE2   
6837 FE FE3   . SF4 G .   ? 0.3920 0.4572 0.4572 0.0576  -0.0042 -0.0183 401 SF4 B FE3   
6838 FE FE4   . SF4 G .   ? 0.3915 0.4074 0.4233 0.0594  -0.0129 -0.0177 401 SF4 B FE4   
6839 S  S1    . SF4 G .   ? 0.4014 0.4474 0.4484 0.0688  -0.0029 -0.0235 401 SF4 B S1    
6840 S  S2    . SF4 G .   ? 0.3753 0.4096 0.4207 0.0466  -0.0106 -0.0130 401 SF4 B S2    
6841 S  S3    . SF4 G .   ? 0.4268 0.4347 0.4597 0.0730  -0.0265 -0.0199 401 SF4 B S3    
6842 S  S4    . SF4 G .   ? 0.4210 0.4985 0.5015 0.0709  -0.0178 -0.0230 401 SF4 B S4    
6843 N  N     . SAM H .   ? 0.3792 0.3683 0.3914 0.0469  -0.0156 -0.0116 402 SAM B N     
6844 C  CA    . SAM H .   ? 0.3767 0.3553 0.3797 0.0449  -0.0127 -0.0125 402 SAM B CA    
6845 C  C     . SAM H .   ? 0.3921 0.3691 0.3952 0.0532  -0.0132 -0.0177 402 SAM B C     
6846 O  O     . SAM H .   ? 0.4004 0.3898 0.4128 0.0612  -0.0133 -0.0205 402 SAM B O     
6847 O  OXT   . SAM H .   ? 0.3982 0.3633 0.3928 0.0513  -0.0134 -0.0195 402 SAM B OXT   
6848 C  CB    . SAM H .   ? 0.3574 0.3442 0.3616 0.0392  -0.0059 -0.0113 402 SAM B CB    
6849 C  CG    . SAM H .   ? 0.3504 0.3537 0.3647 0.0395  -0.0013 -0.0107 402 SAM B CG    
6850 S  SD    . SAM H .   ? 0.3605 0.3765 0.3796 0.0476  0.0030  -0.0148 402 SAM B SD    
6851 C  CE    . SAM H .   ? 0.3567 0.3915 0.3873 0.0434  0.0098  -0.0111 402 SAM B CE    
6852 C  "C5'" . SAM H .   ? 0.3560 0.3671 0.3638 0.0461  0.0068  -0.0154 402 SAM B "C5'" 
6853 C  "C4'" . SAM H .   ? 0.3720 0.3847 0.3756 0.0536  0.0074  -0.0214 402 SAM B "C4'" 
6854 O  "O4'" . SAM H .   ? 0.3788 0.4087 0.3876 0.0577  0.0140  -0.0214 402 SAM B "O4'" 
6855 C  "C3'" . SAM H .   ? 0.3893 0.3921 0.3923 0.0599  0.0015  -0.0265 402 SAM B "C3'" 
6856 O  "O3'" . SAM H .   ? 0.4044 0.3952 0.3975 0.0621  -0.0012 -0.0322 402 SAM B "O3'" 
6857 C  "C2'" . SAM H .   ? 0.4003 0.4197 0.4131 0.0680  0.0046  -0.0289 402 SAM B "C2'" 
6858 O  "O2'" . SAM H .   ? 0.4249 0.4386 0.4360 0.0785  0.0008  -0.0360 402 SAM B "O2'" 
6859 C  "C1'" . SAM H .   ? 0.3979 0.4314 0.4091 0.0671  0.0130  -0.0278 402 SAM B "C1'" 
6860 N  N9    . SAM H .   ? 0.4051 0.4602 0.4270 0.0699  0.0198  -0.0269 402 SAM B N9    
6861 C  C8    . SAM H .   ? 0.4022 0.4690 0.4391 0.0679  0.0196  -0.0244 402 SAM B C8    
6862 N  N7    . SAM H .   ? 0.4126 0.5017 0.4593 0.0688  0.0276  -0.0236 402 SAM B N7    
6863 C  C5    . SAM H .   ? 0.4246 0.5155 0.4596 0.0731  0.0335  -0.0258 402 SAM B C5    
6864 C  C6    . SAM H .   ? 0.4440 0.5548 0.4795 0.0761  0.0439  -0.0259 402 SAM B C6    
6865 N  N6    . SAM H .   ? 0.4531 0.5875 0.5045 0.0734  0.0511  -0.0229 402 SAM B N6    
6866 N  N1    . SAM H .   ? 0.4559 0.5622 0.4741 0.0800  0.0471  -0.0280 402 SAM B N1    
6867 C  C2    . SAM H .   ? 0.4485 0.5334 0.4533 0.0808  0.0394  -0.0311 402 SAM B C2    
6868 N  N3    . SAM H .   ? 0.4304 0.4971 0.4358 0.0770  0.0303  -0.0311 402 SAM B N3    
6869 C  C4    . SAM H .   ? 0.4194 0.4893 0.4390 0.0737  0.0280  -0.0281 402 SAM B C4    
6870 N  N1    . CTP I .   ? 0.3794 0.4163 0.3669 0.0435  0.0327  0.0029  403 CTP B N1    
6871 C  C2    . CTP I .   ? 0.3852 0.4275 0.3813 0.0382  0.0380  0.0081  403 CTP B C2    
6872 N  N3    . CTP I .   ? 0.4069 0.4567 0.3988 0.0374  0.0460  0.0138  403 CTP B N3    
6873 C  C4    . CTP I .   ? 0.4227 0.4738 0.3999 0.0431  0.0482  0.0145  403 CTP B C4    
6874 C  C5    . CTP I .   ? 0.4162 0.4625 0.3845 0.0495  0.0415  0.0080  403 CTP B C5    
6875 C  C6    . CTP I .   ? 0.3947 0.4344 0.3697 0.0488  0.0343  0.0025  403 CTP B C6    
6876 O  O2    . CTP I .   ? 0.3744 0.4152 0.3814 0.0337  0.0352  0.0074  403 CTP B O2    
6877 N  N4    . CTP I .   ? 0.4491 0.5066 0.4195 0.0419  0.0568  0.0214  403 CTP B N4    
6878 C  "C1'" . CTP I .   ? 0.3623 0.3912 0.3535 0.0429  0.0253  -0.0022 403 CTP B "C1'" 
6879 C  "C2'" . CTP I .   ? 0.3552 0.3759 0.3403 0.0421  0.0211  -0.0022 403 CTP B "C2'" 
6880 O  "O2'" . CTP I .   ? 0.3508 0.3660 0.3379 0.0380  0.0222  0.0031  403 CTP B "O2'" 
6881 C  "C3'" . CTP I .   ? 0.3476 0.3634 0.3354 0.0415  0.0155  -0.0083 403 CTP B "C3'" 
6882 C  "C4'" . CTP I .   ? 0.3594 0.3795 0.3475 0.0466  0.0160  -0.0132 403 CTP B "C4'" 
6883 O  "O4'" . CTP I .   ? 0.3680 0.3986 0.3575 0.0482  0.0228  -0.0094 403 CTP B "O4'" 
6884 O  "O3'" . CTP I .   ? 0.3372 0.3473 0.3311 0.0371  0.0135  -0.0073 403 CTP B "O3'" 
6885 C  "C5'" . CTP I .   ? 0.3720 0.3905 0.3520 0.0505  0.0129  -0.0196 403 CTP B "C5'" 
6886 O  "O5'" . CTP I .   ? 0.3681 0.3759 0.3492 0.0466  0.0070  -0.0227 403 CTP B "O5'" 
6887 P  PA    . CTP I .   ? 0.3757 0.3804 0.3516 0.0442  0.0021  -0.0273 403 CTP B PA    
6888 O  O1A   . CTP I .   ? 0.3941 0.4043 0.3615 0.0500  0.0018  -0.0323 403 CTP B O1A   
6889 O  O2A   . CTP I .   ? 0.3766 0.3694 0.3553 0.0383  -0.0020 -0.0288 403 CTP B O2A   
6890 O  O3A   . CTP I .   ? 0.3619 0.3731 0.3397 0.0413  0.0040  -0.0212 403 CTP B O3A   
6891 P  PB    . CTP I .   ? 0.3631 0.3787 0.3416 0.0380  0.0003  -0.0228 403 CTP B PB    
6892 O  O1B   . CTP I .   ? 0.3583 0.3804 0.3359 0.0413  0.0031  -0.0170 403 CTP B O1B   
6893 O  O2B   . CTP I .   ? 0.3609 0.3709 0.3446 0.0306  -0.0020 -0.0244 403 CTP B O2B   
6894 O  O3B   . CTP I .   ? 0.3839 0.4023 0.3555 0.0411  -0.0039 -0.0302 403 CTP B O3B   
6895 P  PG    . CTP I .   ? 0.3990 0.4252 0.3699 0.0393  -0.0105 -0.0363 403 CTP B PG    
6896 O  O1G   . CTP I .   ? 0.4083 0.4250 0.3824 0.0322  -0.0143 -0.0420 403 CTP B O1G   
6897 O  O2G   . CTP I .   ? 0.3885 0.4247 0.3666 0.0376  -0.0103 -0.0320 403 CTP B O2G   
6898 O  O3G   . CTP I .   ? 0.4190 0.4501 0.3780 0.0472  -0.0121 -0.0399 403 CTP B O3G   
6899 N  N     . SAM J .   ? 0.7157 0.6889 0.5736 0.0096  0.0553  -0.0265 401 SAM C N     
6900 C  CA    . SAM J .   ? 0.6608 0.6683 0.5575 0.0051  0.0559  -0.0182 401 SAM C CA    
6901 C  C     . SAM J .   ? 0.6669 0.6950 0.5853 0.0182  0.0676  -0.0151 401 SAM C C     
6902 O  O     . SAM J .   ? 0.7043 0.7185 0.6109 0.0319  0.0729  -0.0198 401 SAM C O     
6903 O  OXT   . SAM J .   ? 0.6394 0.6958 0.5861 0.0140  0.0693  -0.0077 401 SAM C OXT   
6904 C  CB    . SAM J .   ? 0.6230 0.6307 0.5334 -0.0039 0.0425  -0.0170 401 SAM C CB    
6905 C  CG    . SAM J .   ? 0.6463 0.6279 0.5409 -0.0032 0.0352  -0.0218 401 SAM C CG    
6906 S  SD    . SAM J .   ? 0.6605 0.6420 0.5655 0.0123  0.0407  -0.0224 401 SAM C SD    
6907 C  CE    . SAM J .   ? 0.7027 0.6424 0.5809 0.0108  0.0306  -0.0273 401 SAM C CE    
6908 C  "C5'" . SAM J .   ? 0.6054 0.6135 0.5433 0.0056  0.0337  -0.0149 401 SAM C "C5'" 
6909 C  "C4'" . SAM J .   ? 0.6055 0.6334 0.5653 0.0169  0.0382  -0.0115 401 SAM C "C4'" 
6910 O  "O4'" . SAM J .   ? 0.6353 0.6454 0.5877 0.0275  0.0362  -0.0128 401 SAM C "O4'" 
6911 C  "C3'" . SAM J .   ? 0.6245 0.6704 0.5932 0.0265  0.0512  -0.0102 401 SAM C "C3'" 
6912 O  "O3'" . SAM J .   ? 0.6076 0.6869 0.6077 0.0258  0.0524  -0.0029 401 SAM C "O3'" 
6913 C  "C2'" . SAM J .   ? 0.6720 0.7049 0.6319 0.0455  0.0579  -0.0131 401 SAM C "C2'" 
6914 O  "O2'" . SAM J .   ? 0.6880 0.7513 0.6709 0.0578  0.0700  -0.0078 401 SAM C "O2'" 
6915 C  "C1'" . SAM J .   ? 0.6630 0.6853 0.6260 0.0444  0.0457  -0.0118 401 SAM C "C1'" 
6916 N  N9    . SAM J .   ? 0.7131 0.7047 0.6557 0.0586  0.0466  -0.0159 401 SAM C N9    
6917 C  C8    . SAM J .   ? 0.7615 0.7178 0.6701 0.0642  0.0509  -0.0241 401 SAM C C8    
6918 N  N7    . SAM J .   ? 0.8127 0.7392 0.7046 0.0784  0.0500  -0.0269 401 SAM C N7    
6919 C  C5    . SAM J .   ? 0.7928 0.7399 0.7118 0.0827  0.0450  -0.0190 401 SAM C C5    
6920 C  C6    . SAM J .   ? 0.8305 0.7613 0.7477 0.0976  0.0409  -0.0163 401 SAM C C6    
6921 N  N6    . SAM J .   ? 0.8991 0.7847 0.7843 0.1112  0.0422  -0.0224 401 SAM C N6    
6922 N  N1    . SAM J .   ? 0.8031 0.7615 0.7488 0.0977  0.0339  -0.0073 401 SAM C N1    
6923 C  C2    . SAM J .   ? 0.7461 0.7425 0.7178 0.0837  0.0312  -0.0028 401 SAM C C2    
6924 N  N3    . SAM J .   ? 0.7092 0.7207 0.6845 0.0696  0.0351  -0.0050 401 SAM C N3    
6925 C  C4    . SAM J .   ? 0.7328 0.7198 0.6821 0.0701  0.0423  -0.0126 401 SAM C C4    
6926 N  N1    . CTP K .   ? 0.6148 0.5896 0.5501 -0.0044 0.0040  0.0049  402 CTP C N1    
6927 C  C2    . CTP K .   ? 0.6521 0.5982 0.5703 -0.0092 0.0012  0.0051  402 CTP C C2    
6928 N  N3    . CTP K .   ? 0.6852 0.6113 0.5934 -0.0085 -0.0032 0.0110  402 CTP C N3    
6929 C  C4    . CTP K .   ? 0.6811 0.6163 0.5946 -0.0020 -0.0047 0.0165  402 CTP C C4    
6930 C  C5    . CTP K .   ? 0.6450 0.6094 0.5744 0.0028  -0.0033 0.0152  402 CTP C C5    
6931 C  C6    . CTP K .   ? 0.6135 0.5959 0.5538 0.0007  0.0008  0.0094  402 CTP C C6    
6932 O  O2    . CTP K .   ? 0.6616 0.5980 0.5714 -0.0151 0.0012  0.0006  402 CTP C O2    
6933 N  N4    . CTP K .   ? 0.7206 0.6330 0.6211 -0.0013 -0.0093 0.0234  402 CTP C N4    
6934 C  "C1'" . CTP K .   ? 0.5858 0.5793 0.5309 -0.0059 0.0085  0.0002  402 CTP C "C1'" 
6935 C  "C2'" . CTP K .   ? 0.5534 0.5657 0.5065 -0.0134 0.0082  0.0027  402 CTP C "C2'" 
6936 O  "O2'" . CTP K .   ? 0.5541 0.5634 0.5023 -0.0236 0.0075  0.0055  402 CTP C "O2'" 
6937 C  "C3'" . CTP K .   ? 0.5354 0.5629 0.4993 -0.0108 0.0116  -0.0010 402 CTP C "C3'" 
6938 C  "C4'" . CTP K .   ? 0.5541 0.5818 0.5235 0.0000  0.0137  -0.0024 402 CTP C "C4'" 
6939 O  "O4'" . CTP K .   ? 0.5824 0.5900 0.5404 0.0045  0.0109  -0.0011 402 CTP C "O4'" 
6940 O  "O3'" . CTP K .   ? 0.5340 0.5593 0.4928 -0.0155 0.0146  -0.0036 402 CTP C "O3'" 
6941 C  "C5'" . CTP K .   ? 0.5467 0.5945 0.5342 0.0037  0.0112  0.0000  402 CTP C "C5'" 
6942 O  "O5'" . CTP K .   ? 0.5292 0.5908 0.5253 -0.0023 0.0137  -0.0005 402 CTP C "O5'" 
6943 P  PA    . CTP K .   ? 0.5185 0.5919 0.5243 -0.0085 0.0068  0.0013  402 CTP C PA    
6944 O  O1A   . CTP K .   ? 0.5331 0.6135 0.5483 -0.0042 -0.0011 0.0042  402 CTP C O1A   
6945 O  O2A   . CTP K .   ? 0.5122 0.5944 0.5251 -0.0144 0.0112  0.0017  402 CTP C O2A   
6946 O  O3A   . CTP K .   ? 0.5095 0.5691 0.4978 -0.0127 0.0040  0.0000  402 CTP C O3A   
6947 P  PB    . CTP K .   ? 0.5078 0.5644 0.4893 -0.0169 -0.0004 -0.0009 402 CTP C PB    
6948 O  O1B   . CTP K .   ? 0.5109 0.5588 0.4774 -0.0146 0.0012  0.0000  402 CTP C O1B   
6949 O  O2B   . CTP K .   ? 0.5013 0.5602 0.4867 -0.0217 0.0018  -0.0016 402 CTP C O2B   
6950 O  O3B   . CTP K .   ? 0.5251 0.5858 0.5129 -0.0170 -0.0105 0.0000  402 CTP C O3B   
6951 P  PG    . CTP K .   ? 0.5476 0.6006 0.5273 -0.0214 -0.0223 -0.0018 402 CTP C PG    
6952 O  O1G   . CTP K .   ? 0.5511 0.6149 0.5494 -0.0295 -0.0256 0.0001  402 CTP C O1G   
6953 O  O2G   . CTP K .   ? 0.5524 0.5889 0.5100 -0.0193 -0.0194 -0.0052 402 CTP C O2G   
6954 O  O3G   . CTP K .   ? 0.5680 0.6207 0.5444 -0.0176 -0.0315 0.0000  402 CTP C O3G   
6955 FE FE1   . SF4 L .   ? 0.7798 0.7410 0.6319 0.0413  0.0729  -0.0325 403 SF4 C FE1   
6956 FE FE2   . SF4 L .   ? 0.9090 0.8434 0.7243 0.0869  0.1019  -0.0421 403 SF4 C FE2   
6957 FE FE3   . SF4 L .   ? 0.9108 0.7987 0.6727 0.0517  0.0759  -0.0502 403 SF4 C FE3   
6958 FE FE4   . SF4 L .   ? 0.8974 0.7722 0.6854 0.0598  0.0650  -0.0504 403 SF4 C FE4   
6959 S  S1    . SF4 L .   ? 0.9996 0.8442 0.7351 0.0827  0.0841  -0.0609 403 SF4 C S1    
6960 S  S2    . SF4 L .   ? 0.8090 0.7206 0.6224 0.0283  0.0532  -0.0412 403 SF4 C S2    
6961 S  S3    . SF4 L .   ? 0.8193 0.7712 0.6812 0.0684  0.0785  -0.0347 403 SF4 C S3    
6962 S  S4    . SF4 L .   ? 0.8671 0.8250 0.6822 0.0620  0.1011  -0.0352 403 SF4 C S4    
# 
