data_9DN3
# 
_entry.id   9DN3 
# 
_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   9DN3         pdb_00009dn3 10.2210/pdb9dn3/pdb 
WWPDB D_1000288437 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-19 ? 
2 'Structure model' 1 1 2025-03-19 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.journal_volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DN3 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-16 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              robin.stanley@nih.gov 
_pdbx_contact_author.name_first         Robin 
_pdbx_contact_author.name_last          Stanley 
_pdbx_contact_author.name_mi            E 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2106-3102 
# 
_audit_author.name               'Wang, H.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-2701-7155 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            301 
_citation.language                  ? 
_citation.page_first                108274 
_citation.page_last                 108274 
_citation.title                     
'Biochemical and biophysical characterization of inositol-tetrakisphosphate 1-kinase inhibitors.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2025.108274 
_citation.pdbx_database_id_PubMed   39922495 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ng, M.Y.'       1  ? 
primary 'Wang, H.'       2  ? 
primary 'Zhang, H.'      3  ? 
primary 'Prucker, I.'    4  ? 
primary 'Perera, L.'     5  ? 
primary 'Goncharova, E.' 6  ? 
primary 'Wamiru, A.'     7  ? 
primary 'Jessen, H.J.'   8  ? 
primary 'Stanley, R.E.'  9  ? 
primary 'Shears, S.B.'   10 ? 
primary 'Luo, J.'        11 ? 
primary 
;O'Keefe, B.R.
;
12 ? 
primary 'Wilson, B.A.P.' 13 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Inositol-tetrakisphosphate 1-kinase' 37304.441 1  2.7.1.134,2.7.1.159 ? ? ? 
2 non-polymer syn 'SULFATE ION'                         96.063    1  ?                   ? ? ? 
3 non-polymer nat 9-cyclopentyl-9H-purin-6-amine        203.244   1  ?                   ? ? ? 
4 water       nat water                                 18.015    62 ?                   ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Inositol 1,3,4-trisphosphate 5/6-kinase,Inositol-triphosphate 5/6-kinase,Ins(1,4)P(3) 5/6-kinase' 
# 
_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       
;GSGTMQTFLKGKRVGYWLSEKKIKKLNFQAFAELCRKRGMEVVQLNLSRPIEEQGPLDVIIHKLTDVILEADQNDSQSLE
LVHRFQEYIDAHPETIVLDPLPAIRTLLDRSKSYELIRKIEAYMEDDRICSPPFMELTSLCGDDTMRLLEKNGLTFPFIC
KTRVAHGTNSHEMAIVFNQEGLNAIQPPCVVQNFINHNAVLYKVFVVGESYTVVQRPSLKNFSAGTSDRESIFFNSHNVS
KPESSSVLTELDKIEGVFERPSDEVIRELSRALRQALGVSLFGIDIIINNQTGQHAVIDINAFPGYEGVSEFFTDLLNHI
ATVLQGQSTAM
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSGTMQTFLKGKRVGYWLSEKKIKKLNFQAFAELCRKRGMEVVQLNLSRPIEEQGPLDVIIHKLTDVILEADQNDSQSLE
LVHRFQEYIDAHPETIVLDPLPAIRTLLDRSKSYELIRKIEAYMEDDRICSPPFMELTSLCGDDTMRLLEKNGLTFPFIC
KTRVAHGTNSHEMAIVFNQEGLNAIQPPCVVQNFINHNAVLYKVFVVGESYTVVQRPSLKNFSAGTSDRESIFFNSHNVS
KPESSSVLTELDKIEGVFERPSDEVIRELSRALRQALGVSLFGIDIIINNQTGQHAVIDINAFPGYEGVSEFFTDLLNHI
ATVLQGQSTAM
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                  SO4   
3 9-cyclopentyl-9H-purin-6-amine A1A7Y 
4 water                          HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   GLY n 
1 4   THR n 
1 5   MET n 
1 6   GLN n 
1 7   THR n 
1 8   PHE n 
1 9   LEU n 
1 10  LYS n 
1 11  GLY n 
1 12  LYS n 
1 13  ARG n 
1 14  VAL n 
1 15  GLY n 
1 16  TYR n 
1 17  TRP n 
1 18  LEU n 
1 19  SER n 
1 20  GLU n 
1 21  LYS n 
1 22  LYS n 
1 23  ILE n 
1 24  LYS n 
1 25  LYS n 
1 26  LEU n 
1 27  ASN n 
1 28  PHE n 
1 29  GLN n 
1 30  ALA n 
1 31  PHE n 
1 32  ALA n 
1 33  GLU n 
1 34  LEU n 
1 35  CYS n 
1 36  ARG n 
1 37  LYS n 
1 38  ARG n 
1 39  GLY n 
1 40  MET n 
1 41  GLU n 
1 42  VAL n 
1 43  VAL n 
1 44  GLN n 
1 45  LEU n 
1 46  ASN n 
1 47  LEU n 
1 48  SER n 
1 49  ARG n 
1 50  PRO n 
1 51  ILE n 
1 52  GLU n 
1 53  GLU n 
1 54  GLN n 
1 55  GLY n 
1 56  PRO n 
1 57  LEU n 
1 58  ASP n 
1 59  VAL n 
1 60  ILE n 
1 61  ILE n 
1 62  HIS n 
1 63  LYS n 
1 64  LEU n 
1 65  THR n 
1 66  ASP n 
1 67  VAL n 
1 68  ILE n 
1 69  LEU n 
1 70  GLU n 
1 71  ALA n 
1 72  ASP n 
1 73  GLN n 
1 74  ASN n 
1 75  ASP n 
1 76  SER n 
1 77  GLN n 
1 78  SER n 
1 79  LEU n 
1 80  GLU n 
1 81  LEU n 
1 82  VAL n 
1 83  HIS n 
1 84  ARG n 
1 85  PHE n 
1 86  GLN n 
1 87  GLU n 
1 88  TYR n 
1 89  ILE n 
1 90  ASP n 
1 91  ALA n 
1 92  HIS n 
1 93  PRO n 
1 94  GLU n 
1 95  THR n 
1 96  ILE n 
1 97  VAL n 
1 98  LEU n 
1 99  ASP n 
1 100 PRO n 
1 101 LEU n 
1 102 PRO n 
1 103 ALA n 
1 104 ILE n 
1 105 ARG n 
1 106 THR n 
1 107 LEU n 
1 108 LEU n 
1 109 ASP n 
1 110 ARG n 
1 111 SER n 
1 112 LYS n 
1 113 SER n 
1 114 TYR n 
1 115 GLU n 
1 116 LEU n 
1 117 ILE n 
1 118 ARG n 
1 119 LYS n 
1 120 ILE n 
1 121 GLU n 
1 122 ALA n 
1 123 TYR n 
1 124 MET n 
1 125 GLU n 
1 126 ASP n 
1 127 ASP n 
1 128 ARG n 
1 129 ILE n 
1 130 CYS n 
1 131 SER n 
1 132 PRO n 
1 133 PRO n 
1 134 PHE n 
1 135 MET n 
1 136 GLU n 
1 137 LEU n 
1 138 THR n 
1 139 SER n 
1 140 LEU n 
1 141 CYS n 
1 142 GLY n 
1 143 ASP n 
1 144 ASP n 
1 145 THR n 
1 146 MET n 
1 147 ARG n 
1 148 LEU n 
1 149 LEU n 
1 150 GLU n 
1 151 LYS n 
1 152 ASN n 
1 153 GLY n 
1 154 LEU n 
1 155 THR n 
1 156 PHE n 
1 157 PRO n 
1 158 PHE n 
1 159 ILE n 
1 160 CYS n 
1 161 LYS n 
1 162 THR n 
1 163 ARG n 
1 164 VAL n 
1 165 ALA n 
1 166 HIS n 
1 167 GLY n 
1 168 THR n 
1 169 ASN n 
1 170 SER n 
1 171 HIS n 
1 172 GLU n 
1 173 MET n 
1 174 ALA n 
1 175 ILE n 
1 176 VAL n 
1 177 PHE n 
1 178 ASN n 
1 179 GLN n 
1 180 GLU n 
1 181 GLY n 
1 182 LEU n 
1 183 ASN n 
1 184 ALA n 
1 185 ILE n 
1 186 GLN n 
1 187 PRO n 
1 188 PRO n 
1 189 CYS n 
1 190 VAL n 
1 191 VAL n 
1 192 GLN n 
1 193 ASN n 
1 194 PHE n 
1 195 ILE n 
1 196 ASN n 
1 197 HIS n 
1 198 ASN n 
1 199 ALA n 
1 200 VAL n 
1 201 LEU n 
1 202 TYR n 
1 203 LYS n 
1 204 VAL n 
1 205 PHE n 
1 206 VAL n 
1 207 VAL n 
1 208 GLY n 
1 209 GLU n 
1 210 SER n 
1 211 TYR n 
1 212 THR n 
1 213 VAL n 
1 214 VAL n 
1 215 GLN n 
1 216 ARG n 
1 217 PRO n 
1 218 SER n 
1 219 LEU n 
1 220 LYS n 
1 221 ASN n 
1 222 PHE n 
1 223 SER n 
1 224 ALA n 
1 225 GLY n 
1 226 THR n 
1 227 SER n 
1 228 ASP n 
1 229 ARG n 
1 230 GLU n 
1 231 SER n 
1 232 ILE n 
1 233 PHE n 
1 234 PHE n 
1 235 ASN n 
1 236 SER n 
1 237 HIS n 
1 238 ASN n 
1 239 VAL n 
1 240 SER n 
1 241 LYS n 
1 242 PRO n 
1 243 GLU n 
1 244 SER n 
1 245 SER n 
1 246 SER n 
1 247 VAL n 
1 248 LEU n 
1 249 THR n 
1 250 GLU n 
1 251 LEU n 
1 252 ASP n 
1 253 LYS n 
1 254 ILE n 
1 255 GLU n 
1 256 GLY n 
1 257 VAL n 
1 258 PHE n 
1 259 GLU n 
1 260 ARG n 
1 261 PRO n 
1 262 SER n 
1 263 ASP n 
1 264 GLU n 
1 265 VAL n 
1 266 ILE n 
1 267 ARG n 
1 268 GLU n 
1 269 LEU n 
1 270 SER n 
1 271 ARG n 
1 272 ALA n 
1 273 LEU n 
1 274 ARG n 
1 275 GLN n 
1 276 ALA n 
1 277 LEU n 
1 278 GLY n 
1 279 VAL n 
1 280 SER n 
1 281 LEU n 
1 282 PHE n 
1 283 GLY n 
1 284 ILE n 
1 285 ASP n 
1 286 ILE n 
1 287 ILE n 
1 288 ILE n 
1 289 ASN n 
1 290 ASN n 
1 291 GLN n 
1 292 THR n 
1 293 GLY n 
1 294 GLN n 
1 295 HIS n 
1 296 ALA n 
1 297 VAL n 
1 298 ILE n 
1 299 ASP n 
1 300 ILE n 
1 301 ASN n 
1 302 ALA n 
1 303 PHE n 
1 304 PRO n 
1 305 GLY n 
1 306 TYR n 
1 307 GLU n 
1 308 GLY n 
1 309 VAL n 
1 310 SER n 
1 311 GLU n 
1 312 PHE n 
1 313 PHE n 
1 314 THR n 
1 315 ASP n 
1 316 LEU n 
1 317 LEU n 
1 318 ASN n 
1 319 HIS n 
1 320 ILE n 
1 321 ALA n 
1 322 THR n 
1 323 VAL n 
1 324 LEU n 
1 325 GLN n 
1 326 GLY n 
1 327 GLN n 
1 328 SER n 
1 329 THR n 
1 330 ALA n 
1 331 MET n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   331 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ITPK1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A7Y non-polymer         . 9-cyclopentyl-9H-purin-6-amine ? 'C10 H13 N5'     203.244 
ALA   'L-peptide linking' y ALANINE                        ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                       ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                     ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                       ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                      ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                        ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                      ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                          ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                     ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                        ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                         ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                     ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                  ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                        ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                         ? 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                  ? 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                      ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                     ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                       ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                         ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -3  ?   ?   ?   A . n 
A 1 2   SER 2   -2  ?   ?   ?   A . n 
A 1 3   GLY 3   -1  ?   ?   ?   A . n 
A 1 4   THR 4   0   ?   ?   ?   A . n 
A 1 5   MET 5   1   ?   ?   ?   A . n 
A 1 6   GLN 6   2   ?   ?   ?   A . n 
A 1 7   THR 7   3   ?   ?   ?   A . n 
A 1 8   PHE 8   4   ?   ?   ?   A . n 
A 1 9   LEU 9   5   5   LEU LEU A . n 
A 1 10  LYS 10  6   6   LYS LYS A . n 
A 1 11  GLY 11  7   7   GLY GLY A . n 
A 1 12  LYS 12  8   8   LYS LYS A . n 
A 1 13  ARG 13  9   9   ARG ARG A . n 
A 1 14  VAL 14  10  10  VAL VAL A . n 
A 1 15  GLY 15  11  11  GLY GLY A . n 
A 1 16  TYR 16  12  12  TYR TYR A . n 
A 1 17  TRP 17  13  13  TRP TRP A . n 
A 1 18  LEU 18  14  14  LEU LEU A . n 
A 1 19  SER 19  15  15  SER SER A . n 
A 1 20  GLU 20  16  16  GLU GLU A . n 
A 1 21  LYS 21  17  17  LYS LYS A . n 
A 1 22  LYS 22  18  18  LYS LYS A . n 
A 1 23  ILE 23  19  19  ILE ILE A . n 
A 1 24  LYS 24  20  20  LYS LYS A . n 
A 1 25  LYS 25  21  21  LYS LYS A . n 
A 1 26  LEU 26  22  22  LEU LEU A . n 
A 1 27  ASN 27  23  23  ASN ASN A . n 
A 1 28  PHE 28  24  24  PHE PHE A . n 
A 1 29  GLN 29  25  25  GLN GLN A . n 
A 1 30  ALA 30  26  26  ALA ALA A . n 
A 1 31  PHE 31  27  27  PHE PHE A . n 
A 1 32  ALA 32  28  28  ALA ALA A . n 
A 1 33  GLU 33  29  29  GLU GLU A . n 
A 1 34  LEU 34  30  30  LEU LEU A . n 
A 1 35  CYS 35  31  31  CYS CYS A . n 
A 1 36  ARG 36  32  32  ARG ARG A . n 
A 1 37  LYS 37  33  33  LYS LYS A . n 
A 1 38  ARG 38  34  34  ARG ARG A . n 
A 1 39  GLY 39  35  35  GLY GLY A . n 
A 1 40  MET 40  36  36  MET MET A . n 
A 1 41  GLU 41  37  37  GLU GLU A . n 
A 1 42  VAL 42  38  38  VAL VAL A . n 
A 1 43  VAL 43  39  39  VAL VAL A . n 
A 1 44  GLN 44  40  40  GLN GLN A . n 
A 1 45  LEU 45  41  41  LEU LEU A . n 
A 1 46  ASN 46  42  42  ASN ASN A . n 
A 1 47  LEU 47  43  43  LEU LEU A . n 
A 1 48  SER 48  44  44  SER SER A . n 
A 1 49  ARG 49  45  45  ARG ARG A . n 
A 1 50  PRO 50  46  46  PRO PRO A . n 
A 1 51  ILE 51  47  47  ILE ILE A . n 
A 1 52  GLU 52  48  48  GLU GLU A . n 
A 1 53  GLU 53  49  49  GLU GLU A . n 
A 1 54  GLN 54  50  50  GLN GLN A . n 
A 1 55  GLY 55  51  51  GLY GLY A . n 
A 1 56  PRO 56  52  52  PRO PRO A . n 
A 1 57  LEU 57  53  53  LEU LEU A . n 
A 1 58  ASP 58  54  54  ASP ASP A . n 
A 1 59  VAL 59  55  55  VAL VAL A . n 
A 1 60  ILE 60  56  56  ILE ILE A . n 
A 1 61  ILE 61  57  57  ILE ILE A . n 
A 1 62  HIS 62  58  58  HIS HIS A . n 
A 1 63  LYS 63  59  59  LYS LYS A . n 
A 1 64  LEU 64  60  60  LEU LEU A . n 
A 1 65  THR 65  61  61  THR THR A . n 
A 1 66  ASP 66  62  62  ASP ASP A . n 
A 1 67  VAL 67  63  63  VAL VAL A . n 
A 1 68  ILE 68  64  64  ILE ILE A . n 
A 1 69  LEU 69  65  65  LEU LEU A . n 
A 1 70  GLU 70  66  66  GLU GLU A . n 
A 1 71  ALA 71  67  67  ALA ALA A . n 
A 1 72  ASP 72  68  68  ASP ASP A . n 
A 1 73  GLN 73  69  69  GLN GLN A . n 
A 1 74  ASN 74  70  70  ASN ASN A . n 
A 1 75  ASP 75  71  71  ASP ASP A . n 
A 1 76  SER 76  72  72  SER SER A . n 
A 1 77  GLN 77  73  73  GLN GLN A . n 
A 1 78  SER 78  74  74  SER SER A . n 
A 1 79  LEU 79  75  75  LEU LEU A . n 
A 1 80  GLU 80  76  76  GLU GLU A . n 
A 1 81  LEU 81  77  77  LEU LEU A . n 
A 1 82  VAL 82  78  78  VAL VAL A . n 
A 1 83  HIS 83  79  79  HIS HIS A . n 
A 1 84  ARG 84  80  80  ARG ARG A . n 
A 1 85  PHE 85  81  81  PHE PHE A . n 
A 1 86  GLN 86  82  82  GLN GLN A . n 
A 1 87  GLU 87  83  83  GLU GLU A . n 
A 1 88  TYR 88  84  84  TYR TYR A . n 
A 1 89  ILE 89  85  85  ILE ILE A . n 
A 1 90  ASP 90  86  86  ASP ASP A . n 
A 1 91  ALA 91  87  87  ALA ALA A . n 
A 1 92  HIS 92  88  88  HIS HIS A . n 
A 1 93  PRO 93  89  89  PRO PRO A . n 
A 1 94  GLU 94  90  90  GLU GLU A . n 
A 1 95  THR 95  91  91  THR THR A . n 
A 1 96  ILE 96  92  92  ILE ILE A . n 
A 1 97  VAL 97  93  93  VAL VAL A . n 
A 1 98  LEU 98  94  94  LEU LEU A . n 
A 1 99  ASP 99  95  95  ASP ASP A . n 
A 1 100 PRO 100 96  96  PRO PRO A . n 
A 1 101 LEU 101 97  97  LEU LEU A . n 
A 1 102 PRO 102 98  98  PRO PRO A . n 
A 1 103 ALA 103 99  99  ALA ALA A . n 
A 1 104 ILE 104 100 100 ILE ILE A . n 
A 1 105 ARG 105 101 101 ARG ARG A . n 
A 1 106 THR 106 102 102 THR THR A . n 
A 1 107 LEU 107 103 103 LEU LEU A . n 
A 1 108 LEU 108 104 104 LEU LEU A . n 
A 1 109 ASP 109 105 105 ASP ASP A . n 
A 1 110 ARG 110 106 106 ARG ARG A . n 
A 1 111 SER 111 107 107 SER SER A . n 
A 1 112 LYS 112 108 108 LYS LYS A . n 
A 1 113 SER 113 109 109 SER SER A . n 
A 1 114 TYR 114 110 110 TYR TYR A . n 
A 1 115 GLU 115 111 111 GLU GLU A . n 
A 1 116 LEU 116 112 112 LEU LEU A . n 
A 1 117 ILE 117 113 113 ILE ILE A . n 
A 1 118 ARG 118 114 114 ARG ARG A . n 
A 1 119 LYS 119 115 115 LYS LYS A . n 
A 1 120 ILE 120 116 116 ILE ILE A . n 
A 1 121 GLU 121 117 117 GLU GLU A . n 
A 1 122 ALA 122 118 118 ALA ALA A . n 
A 1 123 TYR 123 119 119 TYR TYR A . n 
A 1 124 MET 124 120 120 MET MET A . n 
A 1 125 GLU 125 121 121 GLU GLU A . n 
A 1 126 ASP 126 122 122 ASP ASP A . n 
A 1 127 ASP 127 123 123 ASP ASP A . n 
A 1 128 ARG 128 124 124 ARG ARG A . n 
A 1 129 ILE 129 125 125 ILE ILE A . n 
A 1 130 CYS 130 126 126 CYS CYS A . n 
A 1 131 SER 131 127 127 SER SER A . n 
A 1 132 PRO 132 128 128 PRO PRO A . n 
A 1 133 PRO 133 129 129 PRO PRO A . n 
A 1 134 PHE 134 130 130 PHE PHE A . n 
A 1 135 MET 135 131 131 MET MET A . n 
A 1 136 GLU 136 132 132 GLU GLU A . n 
A 1 137 LEU 137 133 133 LEU LEU A . n 
A 1 138 THR 138 134 134 THR THR A . n 
A 1 139 SER 139 135 135 SER SER A . n 
A 1 140 LEU 140 136 136 LEU LEU A . n 
A 1 141 CYS 141 137 137 CYS CYS A . n 
A 1 142 GLY 142 138 138 GLY GLY A . n 
A 1 143 ASP 143 139 139 ASP ASP A . n 
A 1 144 ASP 144 140 140 ASP ASP A . n 
A 1 145 THR 145 141 141 THR THR A . n 
A 1 146 MET 146 142 142 MET MET A . n 
A 1 147 ARG 147 143 143 ARG ARG A . n 
A 1 148 LEU 148 144 144 LEU LEU A . n 
A 1 149 LEU 149 145 145 LEU LEU A . n 
A 1 150 GLU 150 146 146 GLU GLU A . n 
A 1 151 LYS 151 147 147 LYS LYS A . n 
A 1 152 ASN 152 148 148 ASN ASN A . n 
A 1 153 GLY 153 149 149 GLY GLY A . n 
A 1 154 LEU 154 150 150 LEU LEU A . n 
A 1 155 THR 155 151 151 THR THR A . n 
A 1 156 PHE 156 152 152 PHE PHE A . n 
A 1 157 PRO 157 153 153 PRO PRO A . n 
A 1 158 PHE 158 154 154 PHE PHE A . n 
A 1 159 ILE 159 155 155 ILE ILE A . n 
A 1 160 CYS 160 156 156 CYS CYS A . n 
A 1 161 LYS 161 157 157 LYS LYS A . n 
A 1 162 THR 162 158 158 THR THR A . n 
A 1 163 ARG 163 159 159 ARG ARG A . n 
A 1 164 VAL 164 160 160 VAL VAL A . n 
A 1 165 ALA 165 161 161 ALA ALA A . n 
A 1 166 HIS 166 162 162 HIS HIS A . n 
A 1 167 GLY 167 163 163 GLY GLY A . n 
A 1 168 THR 168 164 164 THR THR A . n 
A 1 169 ASN 169 165 165 ASN ASN A . n 
A 1 170 SER 170 166 166 SER SER A . n 
A 1 171 HIS 171 167 167 HIS HIS A . n 
A 1 172 GLU 172 168 168 GLU GLU A . n 
A 1 173 MET 173 169 169 MET MET A . n 
A 1 174 ALA 174 170 170 ALA ALA A . n 
A 1 175 ILE 175 171 171 ILE ILE A . n 
A 1 176 VAL 176 172 172 VAL VAL A . n 
A 1 177 PHE 177 173 173 PHE PHE A . n 
A 1 178 ASN 178 174 174 ASN ASN A . n 
A 1 179 GLN 179 175 175 GLN GLN A . n 
A 1 180 GLU 180 176 176 GLU GLU A . n 
A 1 181 GLY 181 177 177 GLY GLY A . n 
A 1 182 LEU 182 178 178 LEU LEU A . n 
A 1 183 ASN 183 179 179 ASN ASN A . n 
A 1 184 ALA 184 180 180 ALA ALA A . n 
A 1 185 ILE 185 181 181 ILE ILE A . n 
A 1 186 GLN 186 182 182 GLN GLN A . n 
A 1 187 PRO 187 183 183 PRO PRO A . n 
A 1 188 PRO 188 184 184 PRO PRO A . n 
A 1 189 CYS 189 185 185 CYS CYS A . n 
A 1 190 VAL 190 186 186 VAL VAL A . n 
A 1 191 VAL 191 187 187 VAL VAL A . n 
A 1 192 GLN 192 188 188 GLN GLN A . n 
A 1 193 ASN 193 189 189 ASN ASN A . n 
A 1 194 PHE 194 190 190 PHE PHE A . n 
A 1 195 ILE 195 191 191 ILE ILE A . n 
A 1 196 ASN 196 192 192 ASN ASN A . n 
A 1 197 HIS 197 193 193 HIS HIS A . n 
A 1 198 ASN 198 194 194 ASN ASN A . n 
A 1 199 ALA 199 195 195 ALA ALA A . n 
A 1 200 VAL 200 196 196 VAL VAL A . n 
A 1 201 LEU 201 197 197 LEU LEU A . n 
A 1 202 TYR 202 198 198 TYR TYR A . n 
A 1 203 LYS 203 199 199 LYS LYS A . n 
A 1 204 VAL 204 200 200 VAL VAL A . n 
A 1 205 PHE 205 201 201 PHE PHE A . n 
A 1 206 VAL 206 202 202 VAL VAL A . n 
A 1 207 VAL 207 203 203 VAL VAL A . n 
A 1 208 GLY 208 204 204 GLY GLY A . n 
A 1 209 GLU 209 205 205 GLU GLU A . n 
A 1 210 SER 210 206 206 SER SER A . n 
A 1 211 TYR 211 207 207 TYR TYR A . n 
A 1 212 THR 212 208 208 THR THR A . n 
A 1 213 VAL 213 209 209 VAL VAL A . n 
A 1 214 VAL 214 210 210 VAL VAL A . n 
A 1 215 GLN 215 211 211 GLN GLN A . n 
A 1 216 ARG 216 212 212 ARG ARG A . n 
A 1 217 PRO 217 213 213 PRO PRO A . n 
A 1 218 SER 218 214 214 SER SER A . n 
A 1 219 LEU 219 215 215 LEU LEU A . n 
A 1 220 LYS 220 216 216 LYS LYS A . n 
A 1 221 ASN 221 217 217 ASN ASN A . n 
A 1 222 PHE 222 218 218 PHE PHE A . n 
A 1 223 SER 223 219 219 SER SER A . n 
A 1 224 ALA 224 220 220 ALA ALA A . n 
A 1 225 GLY 225 221 221 GLY GLY A . n 
A 1 226 THR 226 222 222 THR THR A . n 
A 1 227 SER 227 223 223 SER SER A . n 
A 1 228 ASP 228 224 224 ASP ASP A . n 
A 1 229 ARG 229 225 225 ARG ARG A . n 
A 1 230 GLU 230 226 226 GLU GLU A . n 
A 1 231 SER 231 227 227 SER SER A . n 
A 1 232 ILE 232 228 228 ILE ILE A . n 
A 1 233 PHE 233 229 229 PHE PHE A . n 
A 1 234 PHE 234 230 230 PHE PHE A . n 
A 1 235 ASN 235 231 231 ASN ASN A . n 
A 1 236 SER 236 232 232 SER SER A . n 
A 1 237 HIS 237 233 233 HIS HIS A . n 
A 1 238 ASN 238 234 234 ASN ASN A . n 
A 1 239 VAL 239 235 235 VAL VAL A . n 
A 1 240 SER 240 236 236 SER SER A . n 
A 1 241 LYS 241 237 237 LYS LYS A . n 
A 1 242 PRO 242 238 238 PRO PRO A . n 
A 1 243 GLU 243 239 239 GLU GLU A . n 
A 1 244 SER 244 240 240 SER SER A . n 
A 1 245 SER 245 241 241 SER SER A . n 
A 1 246 SER 246 242 242 SER SER A . n 
A 1 247 VAL 247 243 243 VAL VAL A . n 
A 1 248 LEU 248 244 244 LEU LEU A . n 
A 1 249 THR 249 245 245 THR THR A . n 
A 1 250 GLU 250 246 246 GLU GLU A . n 
A 1 251 LEU 251 247 247 LEU LEU A . n 
A 1 252 ASP 252 248 248 ASP ASP A . n 
A 1 253 LYS 253 249 249 LYS LYS A . n 
A 1 254 ILE 254 250 250 ILE ILE A . n 
A 1 255 GLU 255 251 251 GLU GLU A . n 
A 1 256 GLY 256 252 252 GLY GLY A . n 
A 1 257 VAL 257 253 253 VAL VAL A . n 
A 1 258 PHE 258 254 254 PHE PHE A . n 
A 1 259 GLU 259 255 255 GLU GLU A . n 
A 1 260 ARG 260 256 256 ARG ARG A . n 
A 1 261 PRO 261 257 257 PRO PRO A . n 
A 1 262 SER 262 258 258 SER SER A . n 
A 1 263 ASP 263 259 259 ASP ASP A . n 
A 1 264 GLU 264 260 260 GLU GLU A . n 
A 1 265 VAL 265 261 261 VAL VAL A . n 
A 1 266 ILE 266 262 262 ILE ILE A . n 
A 1 267 ARG 267 263 263 ARG ARG A . n 
A 1 268 GLU 268 264 264 GLU GLU A . n 
A 1 269 LEU 269 265 265 LEU LEU A . n 
A 1 270 SER 270 266 266 SER SER A . n 
A 1 271 ARG 271 267 267 ARG ARG A . n 
A 1 272 ALA 272 268 268 ALA ALA A . n 
A 1 273 LEU 273 269 269 LEU LEU A . n 
A 1 274 ARG 274 270 270 ARG ARG A . n 
A 1 275 GLN 275 271 271 GLN GLN A . n 
A 1 276 ALA 276 272 272 ALA ALA A . n 
A 1 277 LEU 277 273 273 LEU LEU A . n 
A 1 278 GLY 278 274 274 GLY GLY A . n 
A 1 279 VAL 279 275 275 VAL VAL A . n 
A 1 280 SER 280 276 276 SER SER A . n 
A 1 281 LEU 281 277 277 LEU LEU A . n 
A 1 282 PHE 282 278 278 PHE PHE A . n 
A 1 283 GLY 283 279 279 GLY GLY A . n 
A 1 284 ILE 284 280 280 ILE ILE A . n 
A 1 285 ASP 285 281 281 ASP ASP A . n 
A 1 286 ILE 286 282 282 ILE ILE A . n 
A 1 287 ILE 287 283 283 ILE ILE A . n 
A 1 288 ILE 288 284 284 ILE ILE A . n 
A 1 289 ASN 289 285 285 ASN ASN A . n 
A 1 290 ASN 290 286 286 ASN ASN A . n 
A 1 291 GLN 291 287 287 GLN GLN A . n 
A 1 292 THR 292 288 288 THR THR A . n 
A 1 293 GLY 293 289 289 GLY GLY A . n 
A 1 294 GLN 294 290 290 GLN GLN A . n 
A 1 295 HIS 295 291 291 HIS HIS A . n 
A 1 296 ALA 296 292 292 ALA ALA A . n 
A 1 297 VAL 297 293 293 VAL VAL A . n 
A 1 298 ILE 298 294 294 ILE ILE A . n 
A 1 299 ASP 299 295 295 ASP ASP A . n 
A 1 300 ILE 300 296 296 ILE ILE A . n 
A 1 301 ASN 301 297 297 ASN ASN A . n 
A 1 302 ALA 302 298 298 ALA ALA A . n 
A 1 303 PHE 303 299 299 PHE PHE A . n 
A 1 304 PRO 304 300 300 PRO PRO A . n 
A 1 305 GLY 305 301 301 GLY GLY A . n 
A 1 306 TYR 306 302 302 TYR TYR A . n 
A 1 307 GLU 307 303 303 GLU GLU A . n 
A 1 308 GLY 308 304 304 GLY GLY A . n 
A 1 309 VAL 309 305 305 VAL VAL A . n 
A 1 310 SER 310 306 306 SER SER A . n 
A 1 311 GLU 311 307 307 GLU GLU A . n 
A 1 312 PHE 312 308 308 PHE PHE A . n 
A 1 313 PHE 313 309 309 PHE PHE A . n 
A 1 314 THR 314 310 310 THR THR A . n 
A 1 315 ASP 315 311 311 ASP ASP A . n 
A 1 316 LEU 316 312 312 LEU LEU A . n 
A 1 317 LEU 317 313 313 LEU LEU A . n 
A 1 318 ASN 318 314 314 ASN ASN A . n 
A 1 319 HIS 319 315 315 HIS HIS A . n 
A 1 320 ILE 320 316 316 ILE ILE A . n 
A 1 321 ALA 321 317 317 ALA ALA A . n 
A 1 322 THR 322 318 318 THR THR A . n 
A 1 323 VAL 323 319 319 VAL VAL A . n 
A 1 324 LEU 324 320 320 LEU LEU A . n 
A 1 325 GLN 325 321 321 GLN GLN A . n 
A 1 326 GLY 326 322 322 GLY GLY A . n 
A 1 327 GLN 327 323 ?   ?   ?   A . n 
A 1 328 SER 328 324 ?   ?   ?   A . n 
A 1 329 THR 329 325 ?   ?   ?   A . n 
A 1 330 ALA 330 326 ?   ?   ?   A . n 
A 1 331 MET 331 327 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A7Y 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A7Y 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 SO4   1  401 1   SO4   SO4 A . 
C 3 A1A7Y 1  402 501 A1A7Y 9CP A . 
D 4 HOH   1  501 57  HOH   HOH A . 
D 4 HOH   2  502 8   HOH   HOH A . 
D 4 HOH   3  503 40  HOH   HOH A . 
D 4 HOH   4  504 58  HOH   HOH A . 
D 4 HOH   5  505 38  HOH   HOH A . 
D 4 HOH   6  506 36  HOH   HOH A . 
D 4 HOH   7  507 28  HOH   HOH A . 
D 4 HOH   8  508 26  HOH   HOH A . 
D 4 HOH   9  509 30  HOH   HOH A . 
D 4 HOH   10 510 44  HOH   HOH A . 
D 4 HOH   11 511 7   HOH   HOH A . 
D 4 HOH   12 512 13  HOH   HOH A . 
D 4 HOH   13 513 41  HOH   HOH A . 
D 4 HOH   14 514 49  HOH   HOH A . 
D 4 HOH   15 515 14  HOH   HOH A . 
D 4 HOH   16 516 4   HOH   HOH A . 
D 4 HOH   17 517 10  HOH   HOH A . 
D 4 HOH   18 518 15  HOH   HOH A . 
D 4 HOH   19 519 37  HOH   HOH A . 
D 4 HOH   20 520 19  HOH   HOH A . 
D 4 HOH   21 521 17  HOH   HOH A . 
D 4 HOH   22 522 11  HOH   HOH A . 
D 4 HOH   23 523 52  HOH   HOH A . 
D 4 HOH   24 524 5   HOH   HOH A . 
D 4 HOH   25 525 60  HOH   HOH A . 
D 4 HOH   26 526 1   HOH   HOH A . 
D 4 HOH   27 527 29  HOH   HOH A . 
D 4 HOH   28 528 9   HOH   HOH A . 
D 4 HOH   29 529 18  HOH   HOH A . 
D 4 HOH   30 530 12  HOH   HOH A . 
D 4 HOH   31 531 31  HOH   HOH A . 
D 4 HOH   32 532 43  HOH   HOH A . 
D 4 HOH   33 533 32  HOH   HOH A . 
D 4 HOH   34 534 61  HOH   HOH A . 
D 4 HOH   35 535 62  HOH   HOH A . 
D 4 HOH   36 536 6   HOH   HOH A . 
D 4 HOH   37 537 34  HOH   HOH A . 
D 4 HOH   38 538 42  HOH   HOH A . 
D 4 HOH   39 539 20  HOH   HOH A . 
D 4 HOH   40 540 56  HOH   HOH A . 
D 4 HOH   41 541 16  HOH   HOH A . 
D 4 HOH   42 542 33  HOH   HOH A . 
D 4 HOH   43 543 23  HOH   HOH A . 
D 4 HOH   44 544 53  HOH   HOH A . 
D 4 HOH   45 545 27  HOH   HOH A . 
D 4 HOH   46 546 35  HOH   HOH A . 
D 4 HOH   47 547 3   HOH   HOH A . 
D 4 HOH   48 548 50  HOH   HOH A . 
D 4 HOH   49 549 47  HOH   HOH A . 
D 4 HOH   50 550 45  HOH   HOH A . 
D 4 HOH   51 551 21  HOH   HOH A . 
D 4 HOH   52 552 46  HOH   HOH A . 
D 4 HOH   53 553 22  HOH   HOH A . 
D 4 HOH   54 554 51  HOH   HOH A . 
D 4 HOH   55 555 54  HOH   HOH A . 
D 4 HOH   56 556 48  HOH   HOH A . 
D 4 HOH   57 557 2   HOH   HOH A . 
D 4 HOH   58 558 63  HOH   HOH A . 
D 4 HOH   59 559 25  HOH   HOH A . 
D 4 HOH   60 560 24  HOH   HOH A . 
D 4 HOH   61 561 59  HOH   HOH A . 
D 4 HOH   62 562 55  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '1.18.2_3874: ???' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DN3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     39.592 
_cell.length_a_esd                 ? 
_cell.length_b                     60.244 
_cell.length_b_esd                 ? 
_cell.length_c                     115.467 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DN3 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9DN3 
_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             2.12 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.01 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Hanging drops comprised 2 ul of 14 mg/mL protein solution and 2 ul of well buffer (21% (w/v) PEG 8000, 0.17 mM (NH4)2SO4, 85 mM Tris-HCl, pH 8.0, and 10% Glycerol) that was present in the reservoir. Crystal complexes with inhibitors were formed in a soaking buffer (25% (w/v) PEG 8000, 0.17 mM (NH4)2SO4, 85 mM Tris-HCl, pH 8.0, 20% Glycerol)
;
_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 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-05 
_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   0.920072 
_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-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.920072 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DN3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.95 
_reflns.d_resolution_low                               50 
_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                                     19525 
_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                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.088 
_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                                0.108 
_reflns.pdbx_Rpim_I_all                                0.034 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.951 
_reflns.pdbx_CC_star                                   0.998 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.102 
_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                                    1.95 
_reflns_shell.d_res_low                                     1.98 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.43 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             962 
_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                               10.7 
_reflns_shell.pdbx_chi_squared                              0.530 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.816 
_reflns_shell.pdbx_Rpim_I_all                               0.245 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.826 
_reflns_shell.pdbx_CC_star                                  0.998 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.777 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DN3 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.25 
_refine.ls_d_res_low                             33.09 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     13706 
_refine.ls_number_reflns_R_free                  917 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 6.69 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2229 
_refine.ls_R_factor_R_free                       0.2709 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2194 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 28.10 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.33 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.25 
_refine_hist.d_res_low                        33.09 
_refine_hist.number_atoms_solvent             62 
_refine_hist.number_atoms_total               2611 
_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        2529 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_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' ? 0.004  ? 2598 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.721  ? 3518 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 22.276 ? 357  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.050  ? 399  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 457  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.25 2.37  . . 128 1777 100.00 . . . . 0.2734 . . . . . . . . . . . 0.3591 
'X-RAY DIFFRACTION' 2.37 2.52  . . 129 1797 100.00 . . . . 0.2674 . . . . . . . . . . . 0.3687 
'X-RAY DIFFRACTION' 2.52 2.71  . . 128 1792 100.00 . . . . 0.2619 . . . . . . . . . . . 0.3409 
'X-RAY DIFFRACTION' 2.71 2.98  . . 130 1813 100.00 . . . . 0.2490 . . . . . . . . . . . 0.2974 
'X-RAY DIFFRACTION' 2.98 3.42  . . 130 1824 100.00 . . . . 0.2304 . . . . . . . . . . . 0.2917 
'X-RAY DIFFRACTION' 3.42 4.30  . . 133 1845 100.00 . . . . 0.1965 . . . . . . . . . . . 0.2821 
'X-RAY DIFFRACTION' 4.30 33.09 . . 139 1941 100.00 . . . . 0.2018 . . . . . . . . . . . 0.2141 
# 
_struct.entry_id                     9DN3 
_struct.title                        
'Crystal Structure of Human Inositol 1,3,4-Trisphosphate 5/6-kinase (ITPK1) in Complex with an Inhibitor 9-cylcopentyladenine' 
_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        9DN3 
_struct_keywords.text            
;inhibitor development, inositol phosphate kinase, inhibitor complex, cancer therapy, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR complex
;
_struct_keywords.pdbx_keywords   'TRANSFERASE/TRANSFERASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ITPK1_HUMAN 
_struct_ref.pdbx_db_accession          Q13572 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MQTFLKGKRVGYWLSEKKIKKLNFQAFAELCRKRGMEVVQLNLSRPIEEQGPLDVIIHKLTDVILEADQNDSQSLELVHR
FQEYIDAHPETIVLDPLPAIRTLLDRSKSYELIRKIEAYMEDDRICSPPFMELTSLCGDDTMRLLEKNGLTFPFICKTRV
AHGTNSHEMAIVFNQEGLNAIQPPCVVQNFINHNAVLYKVFVVGESYTVVQRPSLKNFSAGTSDRESIFFNSHNVSKPES
SSVLTELDKIEGVFERPSDEVIRELSRALRQALGVSLFGIDIIINNQTGQHAVIDINAFPGYEGVSEFFTDLLNHIATVL
QGQSTAM
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9DN3 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 5 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 331 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q13572 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  327 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       327 
# 
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 9DN3 GLY A 1 ? UNP Q13572 ? ? 'expression tag' -3 1 
1 9DN3 SER A 2 ? UNP Q13572 ? ? 'expression tag' -2 2 
1 9DN3 GLY A 3 ? UNP Q13572 ? ? 'expression tag' -1 3 
1 9DN3 THR A 4 ? UNP Q13572 ? ? 'expression tag' 0  4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_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 SER A 19  ? ASN A 27  ? SER A 15  ASN A 23  1 ? 9  
HELX_P HELX_P2  AA2 ASN A 27  ? ARG A 38  ? ASN A 23  ARG A 34  1 ? 12 
HELX_P HELX_P3  AA3 PRO A 50  ? GLY A 55  ? PRO A 46  GLY A 51  5 ? 6  
HELX_P HELX_P4  AA4 LEU A 64  ? GLN A 73  ? LEU A 60  GLN A 69  1 ? 10 
HELX_P HELX_P5  AA5 ASP A 75  ? HIS A 92  ? ASP A 71  HIS A 88  1 ? 18 
HELX_P HELX_P6  AA6 PRO A 100 ? LEU A 108 ? PRO A 96  LEU A 104 1 ? 9  
HELX_P HELX_P7  AA7 ASP A 109 ? GLU A 125 ? ASP A 105 GLU A 121 1 ? 17 
HELX_P HELX_P8  AA8 CYS A 141 ? ASP A 143 ? CYS A 137 ASP A 139 5 ? 3  
HELX_P HELX_P9  AA9 ASP A 144 ? LYS A 151 ? ASP A 140 LYS A 147 1 ? 8  
HELX_P HELX_P10 AB1 ASN A 178 ? ILE A 185 ? ASN A 174 ILE A 181 5 ? 8  
HELX_P HELX_P11 AB2 SER A 236 ? LYS A 241 ? SER A 232 LYS A 237 1 ? 6  
HELX_P HELX_P12 AB3 SER A 262 ? GLY A 278 ? SER A 258 GLY A 274 1 ? 17 
HELX_P HELX_P13 AB4 GLU A 311 ? GLN A 325 ? GLU A 307 GLN A 321 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
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 55  A . ? GLY 51  A PRO 56  A ? PRO 52  A 1 -2.07 
2 LEU 98  A . ? LEU 94  A ASP 99  A ? ASP 95  A 1 2.41  
3 PHE 156 A . ? PHE 152 A PRO 157 A ? PRO 153 A 1 -2.55 
4 PRO 187 A . ? PRO 183 A PRO 188 A ? PRO 184 A 1 -4.38 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
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      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 41  ? GLN A 44  ? GLU A 37  GLN A 40  
AA1 2 ARG A 13  ? TRP A 17  ? ARG A 9   TRP A 13  
AA1 3 VAL A 59  ? HIS A 62  ? VAL A 55  HIS A 58  
AA1 4 ILE A 96  ? LEU A 98  ? ILE A 92  LEU A 94  
AA2 1 ILE A 129 ? CYS A 130 ? ILE A 125 CYS A 126 
AA2 2 HIS A 295 ? ALA A 302 ? HIS A 291 ALA A 298 
AA2 3 LEU A 281 ? ILE A 288 ? LEU A 277 ILE A 284 
AA2 4 VAL A 200 ? VAL A 207 ? VAL A 196 VAL A 203 
AA2 5 SER A 210 ? PRO A 217 ? SER A 206 PRO A 213 
AA3 1 PHE A 134 ? LEU A 137 ? PHE A 130 LEU A 133 
AA3 2 CYS A 189 ? ASN A 193 ? CYS A 185 ASN A 189 
AA3 3 PHE A 158 ? LYS A 161 ? PHE A 154 LYS A 157 
AA3 4 GLU A 172 ? VAL A 176 ? GLU A 168 VAL A 172 
AA3 5 ILE A 232 ? ASN A 235 ? ILE A 228 ASN A 231 
# 
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 GLU A 41  ? O GLU A 37  N VAL A 14  ? N VAL A 10  
AA1 2 3 N GLY A 15  ? N GLY A 11  O VAL A 59  ? O VAL A 55  
AA1 3 4 N ILE A 60  ? N ILE A 56  O LEU A 98  ? O LEU A 94  
AA2 1 2 N CYS A 130 ? N CYS A 126 O HIS A 295 ? O HIS A 291 
AA2 2 3 O ALA A 296 ? O ALA A 292 N ILE A 287 ? N ILE A 283 
AA2 3 4 O ILE A 284 ? O ILE A 280 N VAL A 204 ? N VAL A 200 
AA2 4 5 N PHE A 205 ? N PHE A 201 O THR A 212 ? O THR A 208 
AA3 1 2 N LEU A 137 ? N LEU A 133 O CYS A 189 ? O CYS A 185 
AA3 2 3 O GLN A 192 ? O GLN A 188 N ILE A 159 ? N ILE A 155 
AA3 3 4 N CYS A 160 ? N CYS A 156 O ALA A 174 ? O ALA A 170 
AA3 4 5 N MET A 173 ? N MET A 169 O PHE A 234 ? O PHE A 230 
# 
_pdbx_entry_details.entry_id                   9DN3 
_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 16  ? ? -56.05  3.52    
2 1 LEU A 43  ? ? -77.01  22.26   
3 1 ALA A 161 ? ? -92.06  52.73   
4 1 HIS A 193 ? ? -144.67 21.65   
5 1 ASN A 285 ? ? -56.83  106.08  
6 1 PHE A 299 ? ? 38.18   76.81   
7 1 PRO A 300 ? ? -77.37  -166.58 
8 1 GLU A 307 ? ? 73.27   34.48   
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         7.0230 
_pdbx_refine_tls.origin_y         -3.5159 
_pdbx_refine_tls.origin_z         -7.6426 
_pdbx_refine_tls.T[1][1]          0.2460 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0185 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0135 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2225 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0171 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2978 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.9366 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.2013 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.2102 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.2406 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.9243 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.8335 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0111 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0292 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0553 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0933 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0468 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0522 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0223 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0763 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0339 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -3  ? A GLY 1   
2  1 Y 1 A SER -2  ? A SER 2   
3  1 Y 1 A GLY -1  ? A GLY 3   
4  1 Y 1 A THR 0   ? A THR 4   
5  1 Y 1 A MET 1   ? A MET 5   
6  1 Y 1 A GLN 2   ? A GLN 6   
7  1 Y 1 A THR 3   ? A THR 7   
8  1 Y 1 A PHE 4   ? A PHE 8   
9  1 Y 1 A GLN 323 ? A GLN 327 
10 1 Y 1 A SER 324 ? A SER 328 
11 1 Y 1 A THR 325 ? A THR 329 
12 1 Y 1 A ALA 326 ? A ALA 330 
13 1 Y 1 A MET 327 ? A MET 331 
# 
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 
A1A7Y C1   C Y N 1   
A1A7Y C2   C Y N 2   
A1A7Y C3   C Y N 3   
A1A7Y C7   C N N 4   
A1A7Y N2   N Y N 5   
A1A7Y C4   C Y N 6   
A1A7Y N1   N Y N 7   
A1A7Y C5   C Y N 8   
A1A7Y C6   C N N 9   
A1A7Y C10  C N N 10  
A1A7Y C8   C N N 11  
A1A7Y C9   C N N 12  
A1A7Y N3   N Y N 13  
A1A7Y N4   N Y N 14  
A1A7Y N5   N N N 15  
A1A7Y H1   H N N 16  
A1A7Y H2   H N N 17  
A1A7Y H3   H N N 18  
A1A7Y H4   H N N 19  
A1A7Y H5   H N N 20  
A1A7Y H6   H N N 21  
A1A7Y H7   H N N 22  
A1A7Y H8   H N N 23  
A1A7Y H9   H N N 24  
A1A7Y H10  H N N 25  
A1A7Y H11  H N N 26  
A1A7Y H12  H N N 27  
A1A7Y H13  H N N 28  
ALA   N    N N N 29  
ALA   CA   C N S 30  
ALA   C    C N N 31  
ALA   O    O N N 32  
ALA   CB   C N N 33  
ALA   OXT  O N N 34  
ALA   H    H N N 35  
ALA   H2   H N N 36  
ALA   HA   H N N 37  
ALA   HB1  H N N 38  
ALA   HB2  H N N 39  
ALA   HB3  H N N 40  
ALA   HXT  H N N 41  
ARG   N    N N N 42  
ARG   CA   C N S 43  
ARG   C    C N N 44  
ARG   O    O N N 45  
ARG   CB   C N N 46  
ARG   CG   C N N 47  
ARG   CD   C N N 48  
ARG   NE   N N N 49  
ARG   CZ   C N N 50  
ARG   NH1  N N N 51  
ARG   NH2  N N N 52  
ARG   OXT  O N N 53  
ARG   H    H N N 54  
ARG   H2   H N N 55  
ARG   HA   H N N 56  
ARG   HB2  H N N 57  
ARG   HB3  H N N 58  
ARG   HG2  H N N 59  
ARG   HG3  H N N 60  
ARG   HD2  H N N 61  
ARG   HD3  H N N 62  
ARG   HE   H N N 63  
ARG   HH11 H N N 64  
ARG   HH12 H N N 65  
ARG   HH21 H N N 66  
ARG   HH22 H N N 67  
ARG   HXT  H N N 68  
ASN   N    N N N 69  
ASN   CA   C N S 70  
ASN   C    C N N 71  
ASN   O    O N N 72  
ASN   CB   C N N 73  
ASN   CG   C N N 74  
ASN   OD1  O N N 75  
ASN   ND2  N N N 76  
ASN   OXT  O N N 77  
ASN   H    H N N 78  
ASN   H2   H N N 79  
ASN   HA   H N N 80  
ASN   HB2  H N N 81  
ASN   HB3  H N N 82  
ASN   HD21 H N N 83  
ASN   HD22 H N N 84  
ASN   HXT  H N N 85  
ASP   N    N N N 86  
ASP   CA   C N S 87  
ASP   C    C N N 88  
ASP   O    O N N 89  
ASP   CB   C N N 90  
ASP   CG   C N N 91  
ASP   OD1  O N N 92  
ASP   OD2  O N N 93  
ASP   OXT  O N N 94  
ASP   H    H N N 95  
ASP   H2   H N N 96  
ASP   HA   H N N 97  
ASP   HB2  H N N 98  
ASP   HB3  H N N 99  
ASP   HD2  H N N 100 
ASP   HXT  H N N 101 
CYS   N    N N N 102 
CYS   CA   C N R 103 
CYS   C    C N N 104 
CYS   O    O N N 105 
CYS   CB   C N N 106 
CYS   SG   S N N 107 
CYS   OXT  O N N 108 
CYS   H    H N N 109 
CYS   H2   H N N 110 
CYS   HA   H N N 111 
CYS   HB2  H N N 112 
CYS   HB3  H N N 113 
CYS   HG   H N N 114 
CYS   HXT  H N N 115 
GLN   N    N N N 116 
GLN   CA   C N S 117 
GLN   C    C N N 118 
GLN   O    O N N 119 
GLN   CB   C N N 120 
GLN   CG   C N N 121 
GLN   CD   C N N 122 
GLN   OE1  O N N 123 
GLN   NE2  N N N 124 
GLN   OXT  O N N 125 
GLN   H    H N N 126 
GLN   H2   H N N 127 
GLN   HA   H N N 128 
GLN   HB2  H N N 129 
GLN   HB3  H N N 130 
GLN   HG2  H N N 131 
GLN   HG3  H N N 132 
GLN   HE21 H N N 133 
GLN   HE22 H N N 134 
GLN   HXT  H N N 135 
GLU   N    N N N 136 
GLU   CA   C N S 137 
GLU   C    C N N 138 
GLU   O    O N N 139 
GLU   CB   C N N 140 
GLU   CG   C N N 141 
GLU   CD   C N N 142 
GLU   OE1  O N N 143 
GLU   OE2  O N N 144 
GLU   OXT  O N N 145 
GLU   H    H N N 146 
GLU   H2   H N N 147 
GLU   HA   H N N 148 
GLU   HB2  H N N 149 
GLU   HB3  H N N 150 
GLU   HG2  H N N 151 
GLU   HG3  H N N 152 
GLU   HE2  H N N 153 
GLU   HXT  H N N 154 
GLY   N    N N N 155 
GLY   CA   C N N 156 
GLY   C    C N N 157 
GLY   O    O N N 158 
GLY   OXT  O N N 159 
GLY   H    H N N 160 
GLY   H2   H N N 161 
GLY   HA2  H N N 162 
GLY   HA3  H N N 163 
GLY   HXT  H N N 164 
HIS   N    N N N 165 
HIS   CA   C N S 166 
HIS   C    C N N 167 
HIS   O    O N N 168 
HIS   CB   C N N 169 
HIS   CG   C Y N 170 
HIS   ND1  N Y N 171 
HIS   CD2  C Y N 172 
HIS   CE1  C Y N 173 
HIS   NE2  N Y N 174 
HIS   OXT  O N N 175 
HIS   H    H N N 176 
HIS   H2   H N N 177 
HIS   HA   H N N 178 
HIS   HB2  H N N 179 
HIS   HB3  H N N 180 
HIS   HD1  H N N 181 
HIS   HD2  H N N 182 
HIS   HE1  H N N 183 
HIS   HE2  H N N 184 
HIS   HXT  H N N 185 
HOH   O    O N N 186 
HOH   H1   H N N 187 
HOH   H2   H N N 188 
ILE   N    N N N 189 
ILE   CA   C N S 190 
ILE   C    C N N 191 
ILE   O    O N N 192 
ILE   CB   C N S 193 
ILE   CG1  C N N 194 
ILE   CG2  C N N 195 
ILE   CD1  C N N 196 
ILE   OXT  O N N 197 
ILE   H    H N N 198 
ILE   H2   H N N 199 
ILE   HA   H N N 200 
ILE   HB   H N N 201 
ILE   HG12 H N N 202 
ILE   HG13 H N N 203 
ILE   HG21 H N N 204 
ILE   HG22 H N N 205 
ILE   HG23 H N N 206 
ILE   HD11 H N N 207 
ILE   HD12 H N N 208 
ILE   HD13 H N N 209 
ILE   HXT  H N N 210 
LEU   N    N N N 211 
LEU   CA   C N S 212 
LEU   C    C N N 213 
LEU   O    O N N 214 
LEU   CB   C N N 215 
LEU   CG   C N N 216 
LEU   CD1  C N N 217 
LEU   CD2  C N N 218 
LEU   OXT  O N N 219 
LEU   H    H N N 220 
LEU   H2   H N N 221 
LEU   HA   H N N 222 
LEU   HB2  H N N 223 
LEU   HB3  H N N 224 
LEU   HG   H N N 225 
LEU   HD11 H N N 226 
LEU   HD12 H N N 227 
LEU   HD13 H N N 228 
LEU   HD21 H N N 229 
LEU   HD22 H N N 230 
LEU   HD23 H N N 231 
LEU   HXT  H N N 232 
LYS   N    N N N 233 
LYS   CA   C N S 234 
LYS   C    C N N 235 
LYS   O    O N N 236 
LYS   CB   C N N 237 
LYS   CG   C N N 238 
LYS   CD   C N N 239 
LYS   CE   C N N 240 
LYS   NZ   N N N 241 
LYS   OXT  O N N 242 
LYS   H    H N N 243 
LYS   H2   H N N 244 
LYS   HA   H N N 245 
LYS   HB2  H N N 246 
LYS   HB3  H N N 247 
LYS   HG2  H N N 248 
LYS   HG3  H N N 249 
LYS   HD2  H N N 250 
LYS   HD3  H N N 251 
LYS   HE2  H N N 252 
LYS   HE3  H N N 253 
LYS   HZ1  H N N 254 
LYS   HZ2  H N N 255 
LYS   HZ3  H N N 256 
LYS   HXT  H N N 257 
MET   N    N N N 258 
MET   CA   C N S 259 
MET   C    C N N 260 
MET   O    O N N 261 
MET   CB   C N N 262 
MET   CG   C N N 263 
MET   SD   S N N 264 
MET   CE   C N N 265 
MET   OXT  O N N 266 
MET   H    H N N 267 
MET   H2   H N N 268 
MET   HA   H N N 269 
MET   HB2  H N N 270 
MET   HB3  H N N 271 
MET   HG2  H N N 272 
MET   HG3  H N N 273 
MET   HE1  H N N 274 
MET   HE2  H N N 275 
MET   HE3  H N N 276 
MET   HXT  H N N 277 
PHE   N    N N N 278 
PHE   CA   C N S 279 
PHE   C    C N N 280 
PHE   O    O N N 281 
PHE   CB   C N N 282 
PHE   CG   C Y N 283 
PHE   CD1  C Y N 284 
PHE   CD2  C Y N 285 
PHE   CE1  C Y N 286 
PHE   CE2  C Y N 287 
PHE   CZ   C Y N 288 
PHE   OXT  O N N 289 
PHE   H    H N N 290 
PHE   H2   H N N 291 
PHE   HA   H N N 292 
PHE   HB2  H N N 293 
PHE   HB3  H N N 294 
PHE   HD1  H N N 295 
PHE   HD2  H N N 296 
PHE   HE1  H N N 297 
PHE   HE2  H N N 298 
PHE   HZ   H N N 299 
PHE   HXT  H N N 300 
PRO   N    N N N 301 
PRO   CA   C N S 302 
PRO   C    C N N 303 
PRO   O    O N N 304 
PRO   CB   C N N 305 
PRO   CG   C N N 306 
PRO   CD   C N N 307 
PRO   OXT  O N N 308 
PRO   H    H N N 309 
PRO   HA   H N N 310 
PRO   HB2  H N N 311 
PRO   HB3  H N N 312 
PRO   HG2  H N N 313 
PRO   HG3  H N N 314 
PRO   HD2  H N N 315 
PRO   HD3  H N N 316 
PRO   HXT  H N N 317 
SER   N    N N N 318 
SER   CA   C N S 319 
SER   C    C N N 320 
SER   O    O N N 321 
SER   CB   C N N 322 
SER   OG   O N N 323 
SER   OXT  O N N 324 
SER   H    H N N 325 
SER   H2   H N N 326 
SER   HA   H N N 327 
SER   HB2  H N N 328 
SER   HB3  H N N 329 
SER   HG   H N N 330 
SER   HXT  H N N 331 
SO4   S    S N N 332 
SO4   O1   O N N 333 
SO4   O2   O N N 334 
SO4   O3   O N N 335 
SO4   O4   O N N 336 
THR   N    N N N 337 
THR   CA   C N S 338 
THR   C    C N N 339 
THR   O    O N N 340 
THR   CB   C N R 341 
THR   OG1  O N N 342 
THR   CG2  C N N 343 
THR   OXT  O N N 344 
THR   H    H N N 345 
THR   H2   H N N 346 
THR   HA   H N N 347 
THR   HB   H N N 348 
THR   HG1  H N N 349 
THR   HG21 H N N 350 
THR   HG22 H N N 351 
THR   HG23 H N N 352 
THR   HXT  H N N 353 
TRP   N    N N N 354 
TRP   CA   C N S 355 
TRP   C    C N N 356 
TRP   O    O N N 357 
TRP   CB   C N N 358 
TRP   CG   C Y N 359 
TRP   CD1  C Y N 360 
TRP   CD2  C Y N 361 
TRP   NE1  N Y N 362 
TRP   CE2  C Y N 363 
TRP   CE3  C Y N 364 
TRP   CZ2  C Y N 365 
TRP   CZ3  C Y N 366 
TRP   CH2  C Y N 367 
TRP   OXT  O N N 368 
TRP   H    H N N 369 
TRP   H2   H N N 370 
TRP   HA   H N N 371 
TRP   HB2  H N N 372 
TRP   HB3  H N N 373 
TRP   HD1  H N N 374 
TRP   HE1  H N N 375 
TRP   HE3  H N N 376 
TRP   HZ2  H N N 377 
TRP   HZ3  H N N 378 
TRP   HH2  H N N 379 
TRP   HXT  H N N 380 
TYR   N    N N N 381 
TYR   CA   C N S 382 
TYR   C    C N N 383 
TYR   O    O N N 384 
TYR   CB   C N N 385 
TYR   CG   C Y N 386 
TYR   CD1  C Y N 387 
TYR   CD2  C Y N 388 
TYR   CE1  C Y N 389 
TYR   CE2  C Y N 390 
TYR   CZ   C Y N 391 
TYR   OH   O N N 392 
TYR   OXT  O N N 393 
TYR   H    H N N 394 
TYR   H2   H N N 395 
TYR   HA   H N N 396 
TYR   HB2  H N N 397 
TYR   HB3  H N N 398 
TYR   HD1  H N N 399 
TYR   HD2  H N N 400 
TYR   HE1  H N N 401 
TYR   HE2  H N N 402 
TYR   HH   H N N 403 
TYR   HXT  H N N 404 
VAL   N    N N N 405 
VAL   CA   C N S 406 
VAL   C    C N N 407 
VAL   O    O N N 408 
VAL   CB   C N N 409 
VAL   CG1  C N N 410 
VAL   CG2  C N N 411 
VAL   OXT  O N N 412 
VAL   H    H N N 413 
VAL   H2   H N N 414 
VAL   HA   H N N 415 
VAL   HB   H N N 416 
VAL   HG11 H N N 417 
VAL   HG12 H N N 418 
VAL   HG13 H N N 419 
VAL   HG21 H N N 420 
VAL   HG22 H N N 421 
VAL   HG23 H N N 422 
VAL   HXT  H N N 423 
# 
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 
A1A7Y N1  C1   doub Y N 1   
A1A7Y N1  C4   sing Y N 2   
A1A7Y N5  C4   sing N N 3   
A1A7Y C1  N2   sing Y N 4   
A1A7Y C4  C3   doub Y N 5   
A1A7Y N2  C2   doub Y N 6   
A1A7Y C3  C2   sing Y N 7   
A1A7Y C3  N4   sing Y N 8   
A1A7Y C2  N3   sing Y N 9   
A1A7Y N4  C5   doub Y N 10  
A1A7Y N3  C5   sing Y N 11  
A1A7Y N3  C6   sing N N 12  
A1A7Y C7  C6   sing N N 13  
A1A7Y C7  C8   sing N N 14  
A1A7Y C10 C6   sing N N 15  
A1A7Y C10 C9   sing N N 16  
A1A7Y C9  C8   sing N N 17  
A1A7Y C1  H1   sing N N 18  
A1A7Y C7  H2   sing N N 19  
A1A7Y C7  H3   sing N N 20  
A1A7Y C5  H4   sing N N 21  
A1A7Y C6  H5   sing N N 22  
A1A7Y C10 H6   sing N N 23  
A1A7Y C10 H7   sing N N 24  
A1A7Y C8  H8   sing N N 25  
A1A7Y C8  H9   sing N N 26  
A1A7Y C9  H10  sing N N 27  
A1A7Y C9  H11  sing N N 28  
A1A7Y N5  H12  sing N N 29  
A1A7Y N5  H13  sing N N 30  
ALA   N   CA   sing N N 31  
ALA   N   H    sing N N 32  
ALA   N   H2   sing N N 33  
ALA   CA  C    sing N N 34  
ALA   CA  CB   sing N N 35  
ALA   CA  HA   sing N N 36  
ALA   C   O    doub N N 37  
ALA   C   OXT  sing N N 38  
ALA   CB  HB1  sing N N 39  
ALA   CB  HB2  sing N N 40  
ALA   CB  HB3  sing N N 41  
ALA   OXT HXT  sing N N 42  
ARG   N   CA   sing N N 43  
ARG   N   H    sing N N 44  
ARG   N   H2   sing N N 45  
ARG   CA  C    sing N N 46  
ARG   CA  CB   sing N N 47  
ARG   CA  HA   sing N N 48  
ARG   C   O    doub N N 49  
ARG   C   OXT  sing N N 50  
ARG   CB  CG   sing N N 51  
ARG   CB  HB2  sing N N 52  
ARG   CB  HB3  sing N N 53  
ARG   CG  CD   sing N N 54  
ARG   CG  HG2  sing N N 55  
ARG   CG  HG3  sing N N 56  
ARG   CD  NE   sing N N 57  
ARG   CD  HD2  sing N N 58  
ARG   CD  HD3  sing N N 59  
ARG   NE  CZ   sing N N 60  
ARG   NE  HE   sing N N 61  
ARG   CZ  NH1  sing N N 62  
ARG   CZ  NH2  doub N N 63  
ARG   NH1 HH11 sing N N 64  
ARG   NH1 HH12 sing N N 65  
ARG   NH2 HH21 sing N N 66  
ARG   NH2 HH22 sing N N 67  
ARG   OXT HXT  sing N N 68  
ASN   N   CA   sing N N 69  
ASN   N   H    sing N N 70  
ASN   N   H2   sing N N 71  
ASN   CA  C    sing N N 72  
ASN   CA  CB   sing N N 73  
ASN   CA  HA   sing N N 74  
ASN   C   O    doub N N 75  
ASN   C   OXT  sing N N 76  
ASN   CB  CG   sing N N 77  
ASN   CB  HB2  sing N N 78  
ASN   CB  HB3  sing N N 79  
ASN   CG  OD1  doub N N 80  
ASN   CG  ND2  sing N N 81  
ASN   ND2 HD21 sing N N 82  
ASN   ND2 HD22 sing N N 83  
ASN   OXT HXT  sing N N 84  
ASP   N   CA   sing N N 85  
ASP   N   H    sing N N 86  
ASP   N   H2   sing N N 87  
ASP   CA  C    sing N N 88  
ASP   CA  CB   sing N N 89  
ASP   CA  HA   sing N N 90  
ASP   C   O    doub N N 91  
ASP   C   OXT  sing N N 92  
ASP   CB  CG   sing N N 93  
ASP   CB  HB2  sing N N 94  
ASP   CB  HB3  sing N N 95  
ASP   CG  OD1  doub N N 96  
ASP   CG  OD2  sing N N 97  
ASP   OD2 HD2  sing N N 98  
ASP   OXT HXT  sing N N 99  
CYS   N   CA   sing N N 100 
CYS   N   H    sing N N 101 
CYS   N   H2   sing N N 102 
CYS   CA  C    sing N N 103 
CYS   CA  CB   sing N N 104 
CYS   CA  HA   sing N N 105 
CYS   C   O    doub N N 106 
CYS   C   OXT  sing N N 107 
CYS   CB  SG   sing N N 108 
CYS   CB  HB2  sing N N 109 
CYS   CB  HB3  sing N N 110 
CYS   SG  HG   sing N N 111 
CYS   OXT HXT  sing N N 112 
GLN   N   CA   sing N N 113 
GLN   N   H    sing N N 114 
GLN   N   H2   sing N N 115 
GLN   CA  C    sing N N 116 
GLN   CA  CB   sing N N 117 
GLN   CA  HA   sing N N 118 
GLN   C   O    doub N N 119 
GLN   C   OXT  sing N N 120 
GLN   CB  CG   sing N N 121 
GLN   CB  HB2  sing N N 122 
GLN   CB  HB3  sing N N 123 
GLN   CG  CD   sing N N 124 
GLN   CG  HG2  sing N N 125 
GLN   CG  HG3  sing N N 126 
GLN   CD  OE1  doub N N 127 
GLN   CD  NE2  sing N N 128 
GLN   NE2 HE21 sing N N 129 
GLN   NE2 HE22 sing N N 130 
GLN   OXT HXT  sing N N 131 
GLU   N   CA   sing N N 132 
GLU   N   H    sing N N 133 
GLU   N   H2   sing N N 134 
GLU   CA  C    sing N N 135 
GLU   CA  CB   sing N N 136 
GLU   CA  HA   sing N N 137 
GLU   C   O    doub N N 138 
GLU   C   OXT  sing N N 139 
GLU   CB  CG   sing N N 140 
GLU   CB  HB2  sing N N 141 
GLU   CB  HB3  sing N N 142 
GLU   CG  CD   sing N N 143 
GLU   CG  HG2  sing N N 144 
GLU   CG  HG3  sing N N 145 
GLU   CD  OE1  doub N N 146 
GLU   CD  OE2  sing N N 147 
GLU   OE2 HE2  sing N N 148 
GLU   OXT HXT  sing N N 149 
GLY   N   CA   sing N N 150 
GLY   N   H    sing N N 151 
GLY   N   H2   sing N N 152 
GLY   CA  C    sing N N 153 
GLY   CA  HA2  sing N N 154 
GLY   CA  HA3  sing N N 155 
GLY   C   O    doub N N 156 
GLY   C   OXT  sing N N 157 
GLY   OXT HXT  sing N N 158 
HIS   N   CA   sing N N 159 
HIS   N   H    sing N N 160 
HIS   N   H2   sing N N 161 
HIS   CA  C    sing N N 162 
HIS   CA  CB   sing N N 163 
HIS   CA  HA   sing N N 164 
HIS   C   O    doub N N 165 
HIS   C   OXT  sing N N 166 
HIS   CB  CG   sing N N 167 
HIS   CB  HB2  sing N N 168 
HIS   CB  HB3  sing N N 169 
HIS   CG  ND1  sing Y N 170 
HIS   CG  CD2  doub Y N 171 
HIS   ND1 CE1  doub Y N 172 
HIS   ND1 HD1  sing N N 173 
HIS   CD2 NE2  sing Y N 174 
HIS   CD2 HD2  sing N N 175 
HIS   CE1 NE2  sing Y N 176 
HIS   CE1 HE1  sing N N 177 
HIS   NE2 HE2  sing N N 178 
HIS   OXT HXT  sing N N 179 
HOH   O   H1   sing N N 180 
HOH   O   H2   sing N N 181 
ILE   N   CA   sing N N 182 
ILE   N   H    sing N N 183 
ILE   N   H2   sing N N 184 
ILE   CA  C    sing N N 185 
ILE   CA  CB   sing N N 186 
ILE   CA  HA   sing N N 187 
ILE   C   O    doub N N 188 
ILE   C   OXT  sing N N 189 
ILE   CB  CG1  sing N N 190 
ILE   CB  CG2  sing N N 191 
ILE   CB  HB   sing N N 192 
ILE   CG1 CD1  sing N N 193 
ILE   CG1 HG12 sing N N 194 
ILE   CG1 HG13 sing N N 195 
ILE   CG2 HG21 sing N N 196 
ILE   CG2 HG22 sing N N 197 
ILE   CG2 HG23 sing N N 198 
ILE   CD1 HD11 sing N N 199 
ILE   CD1 HD12 sing N N 200 
ILE   CD1 HD13 sing N N 201 
ILE   OXT HXT  sing N N 202 
LEU   N   CA   sing N N 203 
LEU   N   H    sing N N 204 
LEU   N   H2   sing N N 205 
LEU   CA  C    sing N N 206 
LEU   CA  CB   sing N N 207 
LEU   CA  HA   sing N N 208 
LEU   C   O    doub N N 209 
LEU   C   OXT  sing N N 210 
LEU   CB  CG   sing N N 211 
LEU   CB  HB2  sing N N 212 
LEU   CB  HB3  sing N N 213 
LEU   CG  CD1  sing N N 214 
LEU   CG  CD2  sing N N 215 
LEU   CG  HG   sing N N 216 
LEU   CD1 HD11 sing N N 217 
LEU   CD1 HD12 sing N N 218 
LEU   CD1 HD13 sing N N 219 
LEU   CD2 HD21 sing N N 220 
LEU   CD2 HD22 sing N N 221 
LEU   CD2 HD23 sing N N 222 
LEU   OXT HXT  sing N N 223 
LYS   N   CA   sing N N 224 
LYS   N   H    sing N N 225 
LYS   N   H2   sing N N 226 
LYS   CA  C    sing N N 227 
LYS   CA  CB   sing N N 228 
LYS   CA  HA   sing N N 229 
LYS   C   O    doub N N 230 
LYS   C   OXT  sing N N 231 
LYS   CB  CG   sing N N 232 
LYS   CB  HB2  sing N N 233 
LYS   CB  HB3  sing N N 234 
LYS   CG  CD   sing N N 235 
LYS   CG  HG2  sing N N 236 
LYS   CG  HG3  sing N N 237 
LYS   CD  CE   sing N N 238 
LYS   CD  HD2  sing N N 239 
LYS   CD  HD3  sing N N 240 
LYS   CE  NZ   sing N N 241 
LYS   CE  HE2  sing N N 242 
LYS   CE  HE3  sing N N 243 
LYS   NZ  HZ1  sing N N 244 
LYS   NZ  HZ2  sing N N 245 
LYS   NZ  HZ3  sing N N 246 
LYS   OXT HXT  sing N N 247 
MET   N   CA   sing N N 248 
MET   N   H    sing N N 249 
MET   N   H2   sing N N 250 
MET   CA  C    sing N N 251 
MET   CA  CB   sing N N 252 
MET   CA  HA   sing N N 253 
MET   C   O    doub N N 254 
MET   C   OXT  sing N N 255 
MET   CB  CG   sing N N 256 
MET   CB  HB2  sing N N 257 
MET   CB  HB3  sing N N 258 
MET   CG  SD   sing N N 259 
MET   CG  HG2  sing N N 260 
MET   CG  HG3  sing N N 261 
MET   SD  CE   sing N N 262 
MET   CE  HE1  sing N N 263 
MET   CE  HE2  sing N N 264 
MET   CE  HE3  sing N N 265 
MET   OXT HXT  sing N N 266 
PHE   N   CA   sing N N 267 
PHE   N   H    sing N N 268 
PHE   N   H2   sing N N 269 
PHE   CA  C    sing N N 270 
PHE   CA  CB   sing N N 271 
PHE   CA  HA   sing N N 272 
PHE   C   O    doub N N 273 
PHE   C   OXT  sing N N 274 
PHE   CB  CG   sing N N 275 
PHE   CB  HB2  sing N N 276 
PHE   CB  HB3  sing N N 277 
PHE   CG  CD1  doub Y N 278 
PHE   CG  CD2  sing Y N 279 
PHE   CD1 CE1  sing Y N 280 
PHE   CD1 HD1  sing N N 281 
PHE   CD2 CE2  doub Y N 282 
PHE   CD2 HD2  sing N N 283 
PHE   CE1 CZ   doub Y N 284 
PHE   CE1 HE1  sing N N 285 
PHE   CE2 CZ   sing Y N 286 
PHE   CE2 HE2  sing N N 287 
PHE   CZ  HZ   sing N N 288 
PHE   OXT HXT  sing N N 289 
PRO   N   CA   sing N N 290 
PRO   N   CD   sing N N 291 
PRO   N   H    sing N N 292 
PRO   CA  C    sing N N 293 
PRO   CA  CB   sing N N 294 
PRO   CA  HA   sing N N 295 
PRO   C   O    doub N N 296 
PRO   C   OXT  sing N N 297 
PRO   CB  CG   sing N N 298 
PRO   CB  HB2  sing N N 299 
PRO   CB  HB3  sing N N 300 
PRO   CG  CD   sing N N 301 
PRO   CG  HG2  sing N N 302 
PRO   CG  HG3  sing N N 303 
PRO   CD  HD2  sing N N 304 
PRO   CD  HD3  sing N N 305 
PRO   OXT HXT  sing N N 306 
SER   N   CA   sing N N 307 
SER   N   H    sing N N 308 
SER   N   H2   sing N N 309 
SER   CA  C    sing N N 310 
SER   CA  CB   sing N N 311 
SER   CA  HA   sing N N 312 
SER   C   O    doub N N 313 
SER   C   OXT  sing N N 314 
SER   CB  OG   sing N N 315 
SER   CB  HB2  sing N N 316 
SER   CB  HB3  sing N N 317 
SER   OG  HG   sing N N 318 
SER   OXT HXT  sing N N 319 
SO4   S   O1   doub N N 320 
SO4   S   O2   doub N N 321 
SO4   S   O3   sing N N 322 
SO4   S   O4   sing N N 323 
THR   N   CA   sing N N 324 
THR   N   H    sing N N 325 
THR   N   H2   sing N N 326 
THR   CA  C    sing N N 327 
THR   CA  CB   sing N N 328 
THR   CA  HA   sing N N 329 
THR   C   O    doub N N 330 
THR   C   OXT  sing N N 331 
THR   CB  OG1  sing N N 332 
THR   CB  CG2  sing N N 333 
THR   CB  HB   sing N N 334 
THR   OG1 HG1  sing N N 335 
THR   CG2 HG21 sing N N 336 
THR   CG2 HG22 sing N N 337 
THR   CG2 HG23 sing N N 338 
THR   OXT HXT  sing N N 339 
TRP   N   CA   sing N N 340 
TRP   N   H    sing N N 341 
TRP   N   H2   sing N N 342 
TRP   CA  C    sing N N 343 
TRP   CA  CB   sing N N 344 
TRP   CA  HA   sing N N 345 
TRP   C   O    doub N N 346 
TRP   C   OXT  sing N N 347 
TRP   CB  CG   sing N N 348 
TRP   CB  HB2  sing N N 349 
TRP   CB  HB3  sing N N 350 
TRP   CG  CD1  doub Y N 351 
TRP   CG  CD2  sing Y N 352 
TRP   CD1 NE1  sing Y N 353 
TRP   CD1 HD1  sing N N 354 
TRP   CD2 CE2  doub Y N 355 
TRP   CD2 CE3  sing Y N 356 
TRP   NE1 CE2  sing Y N 357 
TRP   NE1 HE1  sing N N 358 
TRP   CE2 CZ2  sing Y N 359 
TRP   CE3 CZ3  doub Y N 360 
TRP   CE3 HE3  sing N N 361 
TRP   CZ2 CH2  doub Y N 362 
TRP   CZ2 HZ2  sing N N 363 
TRP   CZ3 CH2  sing Y N 364 
TRP   CZ3 HZ3  sing N N 365 
TRP   CH2 HH2  sing N N 366 
TRP   OXT HXT  sing N N 367 
TYR   N   CA   sing N N 368 
TYR   N   H    sing N N 369 
TYR   N   H2   sing N N 370 
TYR   CA  C    sing N N 371 
TYR   CA  CB   sing N N 372 
TYR   CA  HA   sing N N 373 
TYR   C   O    doub N N 374 
TYR   C   OXT  sing N N 375 
TYR   CB  CG   sing N N 376 
TYR   CB  HB2  sing N N 377 
TYR   CB  HB3  sing N N 378 
TYR   CG  CD1  doub Y N 379 
TYR   CG  CD2  sing Y N 380 
TYR   CD1 CE1  sing Y N 381 
TYR   CD1 HD1  sing N N 382 
TYR   CD2 CE2  doub Y N 383 
TYR   CD2 HD2  sing N N 384 
TYR   CE1 CZ   doub Y N 385 
TYR   CE1 HE1  sing N N 386 
TYR   CE2 CZ   sing Y N 387 
TYR   CE2 HE2  sing N N 388 
TYR   CZ  OH   sing N N 389 
TYR   OH  HH   sing N N 390 
TYR   OXT HXT  sing N N 391 
VAL   N   CA   sing N N 392 
VAL   N   H    sing N N 393 
VAL   N   H2   sing N N 394 
VAL   CA  C    sing N N 395 
VAL   CA  CB   sing N N 396 
VAL   CA  HA   sing N N 397 
VAL   C   O    doub N N 398 
VAL   C   OXT  sing N N 399 
VAL   CB  CG1  sing N N 400 
VAL   CB  CG2  sing N N 401 
VAL   CB  HB   sing N N 402 
VAL   CG1 HG11 sing N N 403 
VAL   CG1 HG12 sing N N 404 
VAL   CG1 HG13 sing N N 405 
VAL   CG2 HG21 sing N N 406 
VAL   CG2 HG22 sing N N 407 
VAL   CG2 HG23 sing N N 408 
VAL   OXT HXT  sing N N 409 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of Environmental Health Sciences (NIH/NIEHS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           1ZIAES103340 
_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   2q7d 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DN3 
_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]   0.025258 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016599 
_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]   0.008660 
_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 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LEU   A 1 9   ? 21.131  15.045  13.762  1.00 66.61  ? 5   LEU   A N   1 
ATOM   2    C CA  . LEU   A 1 9   ? 20.404  13.807  13.508  1.00 65.63  ? 5   LEU   A CA  1 
ATOM   3    C C   . LEU   A 1 9   ? 20.162  13.060  14.816  1.00 77.91  ? 5   LEU   A C   1 
ATOM   4    O O   . LEU   A 1 9   ? 19.269  12.217  14.910  1.00 68.47  ? 5   LEU   A O   1 
ATOM   5    C CB  . LEU   A 1 9   ? 21.171  12.929  12.520  1.00 67.88  ? 5   LEU   A CB  1 
ATOM   6    C CG  . LEU   A 1 9   ? 20.361  11.836  11.826  1.00 69.66  ? 5   LEU   A CG  1 
ATOM   7    C CD1 . LEU   A 1 9   ? 19.208  12.445  11.041  1.00 54.71  ? 5   LEU   A CD1 1 
ATOM   8    C CD2 . LEU   A 1 9   ? 21.255  11.011  10.915  1.00 74.94  ? 5   LEU   A CD2 1 
ATOM   9    N N   . LYS   A 1 10  ? 20.972  13.379  15.821  1.00 79.79  ? 6   LYS   A N   1 
ATOM   10   C CA  . LYS   A 1 10  ? 20.765  12.835  17.155  1.00 91.76  ? 6   LYS   A CA  1 
ATOM   11   C C   . LYS   A 1 10  ? 19.491  13.409  17.760  1.00 88.36  ? 6   LYS   A C   1 
ATOM   12   O O   . LYS   A 1 10  ? 19.227  14.611  17.669  1.00 81.75  ? 6   LYS   A O   1 
ATOM   13   C CB  . LYS   A 1 10  ? 21.966  13.153  18.045  1.00 81.71  ? 6   LYS   A CB  1 
ATOM   14   C CG  . LYS   A 1 10  ? 21.963  12.473  19.402  1.00 80.29  ? 6   LYS   A CG  1 
ATOM   15   C CD  . LYS   A 1 10  ? 23.132  12.962  20.243  1.00 74.90  ? 6   LYS   A CD  1 
ATOM   16   C CE  . LYS   A 1 10  ? 24.458  12.480  19.673  1.00 86.05  ? 6   LYS   A CE  1 
ATOM   17   N NZ  . LYS   A 1 10  ? 25.623  12.981  20.455  1.00 89.77  ? 6   LYS   A NZ  1 
ATOM   18   N N   . GLY   A 1 11  ? 18.693  12.540  18.377  1.00 81.05  ? 7   GLY   A N   1 
ATOM   19   C CA  . GLY   A 1 11  ? 17.418  12.928  18.929  1.00 65.53  ? 7   GLY   A CA  1 
ATOM   20   C C   . GLY   A 1 11  ? 16.244  12.779  17.985  1.00 70.13  ? 7   GLY   A C   1 
ATOM   21   O O   . GLY   A 1 11  ? 15.097  12.750  18.446  1.00 65.24  ? 7   GLY   A O   1 
ATOM   22   N N   . LYS   A 1 12  ? 16.493  12.693  16.679  1.00 57.81  ? 8   LYS   A N   1 
ATOM   23   C CA  . LYS   A 1 12  ? 15.416  12.450  15.730  1.00 59.87  ? 8   LYS   A CA  1 
ATOM   24   C C   . LYS   A 1 12  ? 14.788  11.088  15.994  1.00 56.35  ? 8   LYS   A C   1 
ATOM   25   O O   . LYS   A 1 12  ? 15.479  10.114  16.307  1.00 48.95  ? 8   LYS   A O   1 
ATOM   26   C CB  . LYS   A 1 12  ? 15.938  12.531  14.296  1.00 56.40  ? 8   LYS   A CB  1 
ATOM   27   C CG  . LYS   A 1 12  ? 16.556  13.874  13.943  1.00 56.55  ? 8   LYS   A CG  1 
ATOM   28   C CD  . LYS   A 1 12  ? 15.483  14.900  13.614  1.00 54.95  ? 8   LYS   A CD  1 
ATOM   29   C CE  . LYS   A 1 12  ? 16.090  16.182  13.069  1.00 46.71  ? 8   LYS   A CE  1 
ATOM   30   N NZ  . LYS   A 1 12  ? 15.463  17.390  13.674  1.00 69.02  ? 8   LYS   A NZ  1 
ATOM   31   N N   . ARG   A 1 13  ? 13.465  11.025  15.869  1.00 48.64  ? 9   ARG   A N   1 
ATOM   32   C CA  . ARG   A 1 13  ? 12.688  9.876   16.313  1.00 57.00  ? 9   ARG   A CA  1 
ATOM   33   C C   . ARG   A 1 13  ? 11.927  9.296   15.131  1.00 50.72  ? 9   ARG   A C   1 
ATOM   34   O O   . ARG   A 1 13  ? 11.130  9.995   14.497  1.00 57.88  ? 9   ARG   A O   1 
ATOM   35   C CB  . ARG   A 1 13  ? 11.735  10.281  17.438  1.00 51.35  ? 9   ARG   A CB  1 
ATOM   36   C CG  . ARG   A 1 13  ? 10.993  9.139   18.092  1.00 60.04  ? 9   ARG   A CG  1 
ATOM   37   C CD  . ARG   A 1 13  ? 10.401  9.600   19.412  1.00 64.15  ? 9   ARG   A CD  1 
ATOM   38   N NE  . ARG   A 1 13  ? 9.393   8.674   19.915  1.00 69.00  ? 9   ARG   A NE  1 
ATOM   39   C CZ  . ARG   A 1 13  ? 9.668   7.599   20.642  1.00 78.54  ? 9   ARG   A CZ  1 
ATOM   40   N NH1 . ARG   A 1 13  ? 8.687   6.809   21.057  1.00 85.29  ? 9   ARG   A NH1 1 
ATOM   41   N NH2 . ARG   A 1 13  ? 10.924  7.317   20.961  1.00 78.94  ? 9   ARG   A NH2 1 
ATOM   42   N N   . VAL   A 1 14  ? 12.174  8.022   14.843  1.00 45.23  ? 10  VAL   A N   1 
ATOM   43   C CA  . VAL   A 1 14  ? 11.575  7.331   13.709  1.00 49.62  ? 10  VAL   A CA  1 
ATOM   44   C C   . VAL   A 1 14  ? 10.816  6.106   14.202  1.00 53.34  ? 10  VAL   A C   1 
ATOM   45   O O   . VAL   A 1 14  ? 11.298  5.363   15.064  1.00 51.79  ? 10  VAL   A O   1 
ATOM   46   C CB  . VAL   A 1 14  ? 12.644  6.944   12.665  1.00 59.14  ? 10  VAL   A CB  1 
ATOM   47   C CG1 . VAL   A 1 14  ? 13.215  8.191   12.020  1.00 56.05  ? 10  VAL   A CG1 1 
ATOM   48   C CG2 . VAL   A 1 14  ? 13.774  6.186   13.337  1.00 51.94  ? 10  VAL   A CG2 1 
ATOM   49   N N   . GLY   A 1 15  ? 9.615   5.914   13.662  1.00 41.52  ? 11  GLY   A N   1 
ATOM   50   C CA  . GLY   A 1 15  ? 8.820   4.739   13.945  1.00 43.08  ? 11  GLY   A CA  1 
ATOM   51   C C   . GLY   A 1 15  ? 8.578   3.928   12.692  1.00 48.21  ? 11  GLY   A C   1 
ATOM   52   O O   . GLY   A 1 15  ? 8.656   4.464   11.582  1.00 49.93  ? 11  GLY   A O   1 
ATOM   53   N N   . TYR   A 1 16  ? 8.289   2.637   12.842  1.00 47.72  ? 12  TYR   A N   1 
ATOM   54   C CA  . TYR   A 1 16  ? 8.102   1.785   11.678  1.00 48.03  ? 12  TYR   A CA  1 
ATOM   55   C C   . TYR   A 1 16  ? 7.096   0.687   11.982  1.00 49.48  ? 12  TYR   A C   1 
ATOM   56   O O   . TYR   A 1 16  ? 7.099   0.111   13.074  1.00 47.78  ? 12  TYR   A O   1 
ATOM   57   C CB  . TYR   A 1 16  ? 9.431   1.169   11.216  1.00 40.93  ? 12  TYR   A CB  1 
ATOM   58   C CG  . TYR   A 1 16  ? 10.064  0.209   12.201  1.00 56.35  ? 12  TYR   A CG  1 
ATOM   59   C CD1 . TYR   A 1 16  ? 10.839  0.676   13.255  1.00 48.01  ? 12  TYR   A CD1 1 
ATOM   60   C CD2 . TYR   A 1 16  ? 9.899   -1.165  12.069  1.00 52.15  ? 12  TYR   A CD2 1 
ATOM   61   C CE1 . TYR   A 1 16  ? 11.423  -0.195  14.155  1.00 47.72  ? 12  TYR   A CE1 1 
ATOM   62   C CE2 . TYR   A 1 16  ? 10.480  -2.045  12.965  1.00 55.75  ? 12  TYR   A CE2 1 
ATOM   63   C CZ  . TYR   A 1 16  ? 11.241  -1.553  14.006  1.00 54.88  ? 12  TYR   A CZ  1 
ATOM   64   O OH  . TYR   A 1 16  ? 11.822  -2.422  14.901  1.00 45.86  ? 12  TYR   A OH  1 
ATOM   65   N N   . TRP   A 1 17  ? 6.230   0.417   11.009  1.00 56.17  ? 13  TRP   A N   1 
ATOM   66   C CA  . TRP   A 1 17  ? 5.414   -0.791  10.981  1.00 59.29  ? 13  TRP   A CA  1 
ATOM   67   C C   . TRP   A 1 17  ? 5.836   -1.583  9.754   1.00 50.71  ? 13  TRP   A C   1 
ATOM   68   O O   . TRP   A 1 17  ? 5.616   -1.144  8.620   1.00 45.59  ? 13  TRP   A O   1 
ATOM   69   C CB  . TRP   A 1 17  ? 3.918   -0.479  10.938  1.00 64.11  ? 13  TRP   A CB  1 
ATOM   70   C CG  . TRP   A 1 17  ? 3.048   -1.693  11.183  1.00 80.67  ? 13  TRP   A CG  1 
ATOM   71   C CD1 . TRP   A 1 17  ? 2.355   -1.982  12.322  1.00 80.87  ? 13  TRP   A CD1 1 
ATOM   72   C CD2 . TRP   A 1 17  ? 2.783   -2.774  10.272  1.00 90.30  ? 13  TRP   A CD2 1 
ATOM   73   N NE1 . TRP   A 1 17  ? 1.678   -3.168  12.180  1.00 93.42  ? 13  TRP   A NE1 1 
ATOM   74   C CE2 . TRP   A 1 17  ? 1.925   -3.674  10.931  1.00 90.76  ? 13  TRP   A CE2 1 
ATOM   75   C CE3 . TRP   A 1 17  ? 3.186   -3.064  8.963   1.00 78.13  ? 13  TRP   A CE3 1 
ATOM   76   C CZ2 . TRP   A 1 17  ? 1.464   -4.842  10.329  1.00 89.74  ? 13  TRP   A CZ2 1 
ATOM   77   C CZ3 . TRP   A 1 17  ? 2.731   -4.228  8.370   1.00 71.85  ? 13  TRP   A CZ3 1 
ATOM   78   C CH2 . TRP   A 1 17  ? 1.879   -5.102  9.052   1.00 76.03  ? 13  TRP   A CH2 1 
ATOM   79   N N   . LEU   A 1 18  ? 6.443   -2.741  9.978   1.00 53.80  ? 14  LEU   A N   1 
ATOM   80   C CA  . LEU   A 1 18  ? 6.777   -3.661  8.908   1.00 51.29  ? 14  LEU   A CA  1 
ATOM   81   C C   . LEU   A 1 18  ? 6.379   -5.066  9.324   1.00 54.28  ? 14  LEU   A C   1 
ATOM   82   O O   . LEU   A 1 18  ? 6.292   -5.387  10.512  1.00 42.25  ? 14  LEU   A O   1 
ATOM   83   C CB  . LEU   A 1 18  ? 8.271   -3.617  8.561   1.00 46.42  ? 14  LEU   A CB  1 
ATOM   84   C CG  . LEU   A 1 18  ? 8.818   -2.305  8.002   1.00 50.11  ? 14  LEU   A CG  1 
ATOM   85   C CD1 . LEU   A 1 18  ? 10.312  -2.193  8.260   1.00 44.53  ? 14  LEU   A CD1 1 
ATOM   86   C CD2 . LEU   A 1 18  ? 8.513   -2.215  6.521   1.00 43.37  ? 14  LEU   A CD2 1 
ATOM   87   N N   . SER   A 1 19  ? 6.115   -5.898  8.325   1.00 46.34  ? 15  SER   A N   1 
ATOM   88   C CA  . SER   A 1 19  ? 5.910   -7.312  8.573   1.00 56.82  ? 15  SER   A CA  1 
ATOM   89   C C   . SER   A 1 19  ? 7.250   -7.954  8.905   1.00 51.48  ? 15  SER   A C   1 
ATOM   90   O O   . SER   A 1 19  ? 8.262   -7.675  8.251   1.00 48.85  ? 15  SER   A O   1 
ATOM   91   C CB  . SER   A 1 19  ? 5.269   -7.972  7.352   1.00 45.92  ? 15  SER   A CB  1 
ATOM   92   O OG  . SER   A 1 19  ? 6.246   -8.362  6.405   1.00 55.08  ? 15  SER   A OG  1 
ATOM   93   N N   . GLU   A 1 20  ? 7.259   -8.805  9.942   1.00 54.52  ? 16  GLU   A N   1 
ATOM   94   C CA  . GLU   A 1 20  ? 8.470   -9.513  10.367  1.00 66.01  ? 16  GLU   A CA  1 
ATOM   95   C C   . GLU   A 1 20  ? 9.085   -10.318 9.241   1.00 54.29  ? 16  GLU   A C   1 
ATOM   96   O O   . GLU   A 1 20  ? 10.075  -11.031 9.456   1.00 58.78  ? 16  GLU   A O   1 
ATOM   97   C CB  . GLU   A 1 20  ? 8.146   -10.423 11.567  1.00 81.02  ? 16  GLU   A CB  1 
ATOM   98   C CG  . GLU   A 1 20  ? 6.885   -11.283 11.382  1.00 79.49  ? 16  GLU   A CG  1 
ATOM   99   C CD  . GLU   A 1 20  ? 5.594   -10.513 11.687  1.00 101.92 ? 16  GLU   A CD  1 
ATOM   100  O OE1 . GLU   A 1 20  ? 5.561   -9.280  11.476  1.00 94.94  ? 16  GLU   A OE1 1 
ATOM   101  O OE2 . GLU   A 1 20  ? 4.604   -11.139 12.115  1.00 111.95 ? 16  GLU   A OE2 1 
ATOM   102  N N   . LYS   A 1 21  ? 8.505   -10.211 8.062   1.00 62.25  ? 17  LYS   A N   1 
ATOM   103  C CA  . LYS   A 1 21  ? 8.872   -10.974 6.896   1.00 46.23  ? 17  LYS   A CA  1 
ATOM   104  C C   . LYS   A 1 21  ? 9.606   -10.050 5.928   1.00 53.62  ? 17  LYS   A C   1 
ATOM   105  O O   . LYS   A 1 21  ? 10.617  -10.435 5.327   1.00 51.10  ? 17  LYS   A O   1 
ATOM   106  C CB  . LYS   A 1 21  ? 7.597   -11.559 6.260   1.00 55.34  ? 17  LYS   A CB  1 
ATOM   107  C CG  . LYS   A 1 21  ? 6.816   -12.790 6.861   1.00 74.42  ? 17  LYS   A CG  1 
ATOM   108  C CD  . LYS   A 1 21  ? 6.027   -12.362 8.119   1.00 83.00  ? 17  LYS   A CD  1 
ATOM   109  C CE  . LYS   A 1 21  ? 5.005   -11.253 7.818   1.00 79.03  ? 17  LYS   A CE  1 
ATOM   110  N NZ  . LYS   A 1 21  ? 4.144   -10.819 8.975   1.00 89.40  ? 17  LYS   A NZ  1 
ATOM   111  N N   . LYS   A 1 22  ? 9.081   -8.827  5.791   1.00 51.92  ? 18  LYS   A N   1 
ATOM   112  C CA  . LYS   A 1 22  ? 9.865   -7.678  5.352   1.00 52.13  ? 18  LYS   A CA  1 
ATOM   113  C C   . LYS   A 1 22  ? 11.032  -7.410  6.305   1.00 35.69  ? 18  LYS   A C   1 
ATOM   114  O O   . LYS   A 1 22  ? 12.180  -7.236  5.875   1.00 50.16  ? 18  LYS   A O   1 
ATOM   115  C CB  . LYS   A 1 22  ? 8.942   -6.462  5.273   1.00 50.70  ? 18  LYS   A CB  1 
ATOM   116  C CG  . LYS   A 1 22  ? 9.399   -5.448  4.304   1.00 54.55  ? 18  LYS   A CG  1 
ATOM   117  C CD  . LYS   A 1 22  ? 9.368   -6.078  2.939   1.00 44.78  ? 18  LYS   A CD  1 
ATOM   118  C CE  . LYS   A 1 22  ? 9.931   -5.128  1.925   1.00 53.18  ? 18  LYS   A CE  1 
ATOM   119  N NZ  . LYS   A 1 22  ? 9.734   -5.666  0.559   1.00 56.19  ? 18  LYS   A NZ  1 
ATOM   120  N N   . ILE   A 1 23  ? 10.755  -7.400  7.614   1.00 34.42  ? 19  ILE   A N   1 
ATOM   121  C CA  . ILE   A 1 23  ? 11.783  -7.057  8.599   1.00 48.37  ? 19  ILE   A CA  1 
ATOM   122  C C   . ILE   A 1 23  ? 12.973  -7.997  8.481   1.00 41.03  ? 19  ILE   A C   1 
ATOM   123  O O   . ILE   A 1 23  ? 14.121  -7.558  8.351   1.00 38.49  ? 19  ILE   A O   1 
ATOM   124  C CB  . ILE   A 1 23  ? 11.208  -7.083  10.028  1.00 45.47  ? 19  ILE   A CB  1 
ATOM   125  C CG1 . ILE   A 1 23  ? 10.295  -5.884  10.277  1.00 50.62  ? 19  ILE   A CG1 1 
ATOM   126  C CG2 . ILE   A 1 23  ? 12.344  -7.097  11.060  1.00 42.84  ? 19  ILE   A CG2 1 
ATOM   127  C CD1 . ILE   A 1 23  ? 9.436   -6.022  11.518  1.00 54.43  ? 19  ILE   A CD1 1 
ATOM   128  N N   . LYS   A 1 24  ? 12.715  -9.306  8.528   1.00 49.41  ? 20  LYS   A N   1 
ATOM   129  C CA  . LYS   A 1 24  ? 13.797  -10.286 8.520   1.00 54.07  ? 20  LYS   A CA  1 
ATOM   130  C C   . LYS   A 1 24  ? 14.595  -10.229 7.227   1.00 49.39  ? 20  LYS   A C   1 
ATOM   131  O O   . LYS   A 1 24  ? 15.828  -10.315 7.237   1.00 57.84  ? 20  LYS   A O   1 
ATOM   132  C CB  . LYS   A 1 24  ? 13.222  -11.685 8.717   1.00 65.29  ? 20  LYS   A CB  1 
ATOM   133  C CG  . LYS   A 1 24  ? 14.236  -12.800 8.579   1.00 82.53  ? 20  LYS   A CG  1 
ATOM   134  C CD  . LYS   A 1 24  ? 13.557  -14.121 8.838   1.00 84.06  ? 20  LYS   A CD  1 
ATOM   135  C CE  . LYS   A 1 24  ? 12.531  -14.399 7.755   1.00 83.07  ? 20  LYS   A CE  1 
ATOM   136  N NZ  . LYS   A 1 24  ? 11.878  -15.714 7.938   1.00 85.99  ? 20  LYS   A NZ  1 
ATOM   137  N N   . LYS   A 1 25  ? 13.904  -10.089 6.102   1.00 54.37  ? 21  LYS   A N   1 
ATOM   138  C CA  . LYS   A 1 25  ? 14.559  -10.141 4.802   1.00 57.28  ? 21  LYS   A CA  1 
ATOM   139  C C   . LYS   A 1 25  ? 15.360  -8.880  4.525   1.00 43.90  ? 21  LYS   A C   1 
ATOM   140  O O   . LYS   A 1 25  ? 16.415  -8.929  3.882   1.00 48.83  ? 21  LYS   A O   1 
ATOM   141  C CB  . LYS   A 1 25  ? 13.499  -10.349 3.734   1.00 55.73  ? 21  LYS   A CB  1 
ATOM   142  C CG  . LYS   A 1 25  ? 14.016  -10.531 2.320   1.00 74.34  ? 21  LYS   A CG  1 
ATOM   143  C CD  . LYS   A 1 25  ? 12.770  -10.785 1.537   1.00 80.30  ? 21  LYS   A CD  1 
ATOM   144  C CE  . LYS   A 1 25  ? 12.980  -11.013 0.061   1.00 79.00  ? 21  LYS   A CE  1 
ATOM   145  N NZ  . LYS   A 1 25  ? 11.642  -11.125 -0.564  1.00 78.54  ? 21  LYS   A NZ  1 
ATOM   146  N N   . LEU   A 1 26  ? 14.844  -7.735  4.953   1.00 49.00  ? 22  LEU   A N   1 
ATOM   147  C CA  . LEU   A 1 26  ? 15.633  -6.518  4.955   1.00 43.10  ? 22  LEU   A CA  1 
ATOM   148  C C   . LEU   A 1 26  ? 16.672  -6.515  6.064   1.00 42.94  ? 22  LEU   A C   1 
ATOM   149  O O   . LEU   A 1 26  ? 17.519  -5.614  6.089   1.00 37.66  ? 22  LEU   A O   1 
ATOM   150  C CB  . LEU   A 1 26  ? 14.729  -5.287  5.109   1.00 49.43  ? 22  LEU   A CB  1 
ATOM   151  C CG  . LEU   A 1 26  ? 13.687  -4.998  4.030   1.00 53.42  ? 22  LEU   A CG  1 
ATOM   152  C CD1 . LEU   A 1 26  ? 12.655  -4.021  4.563   1.00 44.93  ? 22  LEU   A CD1 1 
ATOM   153  C CD2 . LEU   A 1 26  ? 14.352  -4.448  2.783   1.00 62.30  ? 22  LEU   A CD2 1 
ATOM   154  N N   . ASN   A 1 27  ? 16.633  -7.503  6.960   1.00 40.22  ? 23  ASN   A N   1 
ATOM   155  C CA  . ASN   A 1 27  ? 17.413  -7.487  8.196   1.00 43.92  ? 23  ASN   A CA  1 
ATOM   156  C C   . ASN   A 1 27  ? 17.205  -6.160  8.923   1.00 41.68  ? 23  ASN   A C   1 
ATOM   157  O O   . ASN   A 1 27  ? 18.148  -5.509  9.379   1.00 45.19  ? 23  ASN   A O   1 
ATOM   158  C CB  . ASN   A 1 27  ? 18.895  -7.751  7.922   1.00 37.68  ? 23  ASN   A CB  1 
ATOM   159  C CG  . ASN   A 1 27  ? 19.633  -8.249  9.147   1.00 55.91  ? 23  ASN   A CG  1 
ATOM   160  O OD1 . ASN   A 1 27  ? 19.021  -8.717  10.107  1.00 65.89  ? 23  ASN   A OD1 1 
ATOM   161  N ND2 . ASN   A 1 27  ? 20.957  -8.152  9.120   1.00 54.28  ? 23  ASN   A ND2 1 
ATOM   162  N N   . PHE   A 1 28  ? 15.934  -5.760  9.019   1.00 40.45  ? 24  PHE   A N   1 
ATOM   163  C CA  . PHE   A 1 28  ? 15.603  -4.413  9.470   1.00 42.34  ? 24  PHE   A CA  1 
ATOM   164  C C   . PHE   A 1 28  ? 15.960  -4.192  10.933  1.00 39.46  ? 24  PHE   A C   1 
ATOM   165  O O   . PHE   A 1 28  ? 16.276  -3.063  11.324  1.00 43.05  ? 24  PHE   A O   1 
ATOM   166  C CB  . PHE   A 1 28  ? 14.118  -4.133  9.244   1.00 38.56  ? 24  PHE   A CB  1 
ATOM   167  C CG  . PHE   A 1 28  ? 13.780  -2.673  9.219   1.00 43.69  ? 24  PHE   A CG  1 
ATOM   168  C CD1 . PHE   A 1 28  ? 13.930  -1.934  8.056   1.00 44.42  ? 24  PHE   A CD1 1 
ATOM   169  C CD2 . PHE   A 1 28  ? 13.323  -2.034  10.359  1.00 36.43  ? 24  PHE   A CD2 1 
ATOM   170  C CE1 . PHE   A 1 28  ? 13.625  -0.588  8.030   1.00 45.52  ? 24  PHE   A CE1 1 
ATOM   171  C CE2 . PHE   A 1 28  ? 13.015  -0.688  10.340  1.00 47.37  ? 24  PHE   A CE2 1 
ATOM   172  C CZ  . PHE   A 1 28  ? 13.167  0.037   9.173   1.00 40.51  ? 24  PHE   A CZ  1 
ATOM   173  N N   . GLN   A 1 29  ? 15.908  -5.242  11.755  1.00 39.50  ? 25  GLN   A N   1 
ATOM   174  C CA  . GLN   A 1 29  ? 16.275  -5.086  13.158  1.00 42.05  ? 25  GLN   A CA  1 
ATOM   175  C C   . GLN   A 1 29  ? 17.739  -4.696  13.308  1.00 39.98  ? 25  GLN   A C   1 
ATOM   176  O O   . GLN   A 1 29  ? 18.095  -3.965  14.239  1.00 38.78  ? 25  GLN   A O   1 
ATOM   177  C CB  . GLN   A 1 29  ? 15.976  -6.373  13.926  1.00 39.24  ? 25  GLN   A CB  1 
ATOM   178  C CG  . GLN   A 1 29  ? 14.494  -6.658  14.108  1.00 41.92  ? 25  GLN   A CG  1 
ATOM   179  C CD  . GLN   A 1 29  ? 13.757  -5.517  14.783  1.00 47.38  ? 25  GLN   A CD  1 
ATOM   180  O OE1 . GLN   A 1 29  ? 14.251  -4.923  15.742  1.00 60.90  ? 25  GLN   A OE1 1 
ATOM   181  N NE2 . GLN   A 1 29  ? 12.567  -5.205  14.284  1.00 59.92  ? 25  GLN   A NE2 1 
ATOM   182  N N   . ALA   A 1 30  ? 18.599  -5.164  12.401  1.00 41.91  ? 26  ALA   A N   1 
ATOM   183  C CA  . ALA   A 1 30  ? 19.991  -4.729  12.411  1.00 37.94  ? 26  ALA   A CA  1 
ATOM   184  C C   . ALA   A 1 30  ? 20.116  -3.280  11.959  1.00 44.33  ? 26  ALA   A C   1 
ATOM   185  O O   . ALA   A 1 30  ? 20.967  -2.537  12.462  1.00 37.21  ? 26  ALA   A O   1 
ATOM   186  C CB  . ALA   A 1 30  ? 20.836  -5.644  11.525  1.00 39.80  ? 26  ALA   A CB  1 
ATOM   187  N N   . PHE   A 1 31  ? 19.275  -2.860  11.010  1.00 35.66  ? 27  PHE   A N   1 
ATOM   188  C CA  . PHE   A 1 31  ? 19.303  -1.472  10.561  1.00 45.04  ? 27  PHE   A CA  1 
ATOM   189  C C   . PHE   A 1 31  ? 18.795  -0.523  11.639  1.00 36.00  ? 27  PHE   A C   1 
ATOM   190  O O   . PHE   A 1 31  ? 19.277  0.611   11.740  1.00 43.15  ? 27  PHE   A O   1 
ATOM   191  C CB  . PHE   A 1 31  ? 18.478  -1.311  9.284   1.00 36.93  ? 27  PHE   A CB  1 
ATOM   192  C CG  . PHE   A 1 31  ? 18.356  0.112   8.818   1.00 34.54  ? 27  PHE   A CG  1 
ATOM   193  C CD1 . PHE   A 1 31  ? 19.394  0.721   8.132   1.00 49.56  ? 27  PHE   A CD1 1 
ATOM   194  C CD2 . PHE   A 1 31  ? 17.205  0.843   9.068   1.00 36.32  ? 27  PHE   A CD2 1 
ATOM   195  C CE1 . PHE   A 1 31  ? 19.287  2.031   7.703   1.00 38.92  ? 27  PHE   A CE1 1 
ATOM   196  C CE2 . PHE   A 1 31  ? 17.093  2.153   8.643   1.00 28.89  ? 27  PHE   A CE2 1 
ATOM   197  C CZ  . PHE   A 1 31  ? 18.136  2.748   7.960   1.00 42.86  ? 27  PHE   A CZ  1 
ATOM   198  N N   . ALA   A 1 32  ? 17.821  -0.958  12.442  1.00 38.34  ? 28  ALA   A N   1 
ATOM   199  C CA  . ALA   A 1 32  ? 17.346  -0.122  13.539  1.00 39.85  ? 28  ALA   A CA  1 
ATOM   200  C C   . ALA   A 1 32  ? 18.444  0.100   14.570  1.00 35.37  ? 28  ALA   A C   1 
ATOM   201  O O   . ALA   A 1 32  ? 18.635  1.222   15.053  1.00 37.58  ? 28  ALA   A O   1 
ATOM   202  C CB  . ALA   A 1 32  ? 16.116  -0.754  14.189  1.00 42.47  ? 28  ALA   A CB  1 
ATOM   203  N N   . GLU   A 1 33  ? 19.178  -0.960  14.919  1.00 45.21  ? 29  GLU   A N   1 
ATOM   204  C CA  . GLU   A 1 33  ? 20.325  -0.806  15.807  1.00 56.58  ? 29  GLU   A CA  1 
ATOM   205  C C   . GLU   A 1 33  ? 21.399  0.068   15.175  1.00 53.26  ? 29  GLU   A C   1 
ATOM   206  O O   . GLU   A 1 33  ? 22.096  0.805   15.882  1.00 49.98  ? 29  GLU   A O   1 
ATOM   207  C CB  . GLU   A 1 33  ? 20.896  -2.177  16.170  1.00 37.94  ? 29  GLU   A CB  1 
ATOM   208  C CG  . GLU   A 1 33  ? 21.700  -2.199  17.459  1.00 56.71  ? 29  GLU   A CG  1 
ATOM   209  C CD  . GLU   A 1 33  ? 21.045  -1.401  18.570  1.00 70.45  ? 29  GLU   A CD  1 
ATOM   210  O OE1 . GLU   A 1 33  ? 21.557  -0.311  18.901  1.00 80.08  ? 29  GLU   A OE1 1 
ATOM   211  O OE2 . GLU   A 1 33  ? 20.020  -1.863  19.113  1.00 58.40  ? 29  GLU   A OE2 1 
ATOM   212  N N   . LEU   A 1 34  ? 21.550  -0.008  13.850  1.00 43.34  ? 30  LEU   A N   1 
ATOM   213  C CA  . LEU   A 1 34  ? 22.457  0.894   13.148  1.00 48.07  ? 30  LEU   A CA  1 
ATOM   214  C C   . LEU   A 1 34  ? 22.087  2.348   13.399  1.00 47.43  ? 30  LEU   A C   1 
ATOM   215  O O   . LEU   A 1 34  ? 22.959  3.183   13.668  1.00 55.13  ? 30  LEU   A O   1 
ATOM   216  C CB  . LEU   A 1 34  ? 22.433  0.591   11.650  1.00 57.86  ? 30  LEU   A CB  1 
ATOM   217  C CG  . LEU   A 1 34  ? 23.505  1.222   10.760  1.00 64.77  ? 30  LEU   A CG  1 
ATOM   218  C CD1 . LEU   A 1 34  ? 24.872  0.610   11.044  1.00 64.02  ? 30  LEU   A CD1 1 
ATOM   219  C CD2 . LEU   A 1 34  ? 23.134  1.099   9.288   1.00 67.47  ? 30  LEU   A CD2 1 
ATOM   220  N N   . CYS   A 1 35  ? 20.793  2.666   13.323  1.00 51.63  ? 31  CYS   A N   1 
ATOM   221  C CA  . CYS   A 1 35  ? 20.352  4.046   13.478  1.00 47.51  ? 31  CYS   A CA  1 
ATOM   222  C C   . CYS   A 1 35  ? 20.451  4.518   14.923  1.00 46.79  ? 31  CYS   A C   1 
ATOM   223  O O   . CYS   A 1 35  ? 20.720  5.699   15.168  1.00 49.37  ? 31  CYS   A O   1 
ATOM   224  C CB  . CYS   A 1 35  ? 18.916  4.198   12.975  1.00 42.82  ? 31  CYS   A CB  1 
ATOM   225  S SG  . CYS   A 1 35  ? 18.717  3.956   11.202  1.00 52.57  ? 31  CYS   A SG  1 
ATOM   226  N N   . ARG   A 1 36  ? 20.232  3.621   15.887  1.00 47.46  ? 32  ARG   A N   1 
ATOM   227  C CA  . ARG   A 1 36  ? 20.289  4.019   17.290  1.00 54.02  ? 32  ARG   A CA  1 
ATOM   228  C C   . ARG   A 1 36  ? 21.695  4.444   17.690  1.00 51.84  ? 32  ARG   A C   1 
ATOM   229  O O   . ARG   A 1 36  ? 21.863  5.275   18.593  1.00 58.13  ? 32  ARG   A O   1 
ATOM   230  C CB  . ARG   A 1 36  ? 19.797  2.875   18.179  1.00 49.06  ? 32  ARG   A CB  1 
ATOM   231  C CG  . ARG   A 1 36  ? 18.323  2.545   17.988  1.00 51.06  ? 32  ARG   A CG  1 
ATOM   232  C CD  . ARG   A 1 36  ? 17.828  1.557   19.037  1.00 46.09  ? 32  ARG   A CD  1 
ATOM   233  N NE  . ARG   A 1 36  ? 16.430  1.186   18.825  1.00 51.40  ? 32  ARG   A NE  1 
ATOM   234  C CZ  . ARG   A 1 36  ? 16.038  0.083   18.195  1.00 52.55  ? 32  ARG   A CZ  1 
ATOM   235  N NH1 . ARG   A 1 36  ? 16.937  -0.765  17.713  1.00 45.24  ? 32  ARG   A NH1 1 
ATOM   236  N NH2 . ARG   A 1 36  ? 14.745  -0.175  18.045  1.00 49.23  ? 32  ARG   A NH2 1 
ATOM   237  N N   . LYS   A 1 37  ? 22.718  3.898   17.024  1.00 55.87  ? 33  LYS   A N   1 
ATOM   238  C CA  . LYS   A 1 37  ? 24.079  4.325   17.316  1.00 64.66  ? 33  LYS   A CA  1 
ATOM   239  C C   . LYS   A 1 37  ? 24.351  5.700   16.731  1.00 58.56  ? 33  LYS   A C   1 
ATOM   240  O O   . LYS   A 1 37  ? 25.207  6.431   17.238  1.00 68.41  ? 33  LYS   A O   1 
ATOM   241  C CB  . LYS   A 1 37  ? 25.084  3.317   16.766  1.00 65.07  ? 33  LYS   A CB  1 
ATOM   242  C CG  . LYS   A 1 37  ? 24.927  1.936   17.366  1.00 68.65  ? 33  LYS   A CG  1 
ATOM   243  C CD  . LYS   A 1 37  ? 25.988  0.991   16.900  1.00 74.22  ? 33  LYS   A CD  1 
ATOM   244  C CE  . LYS   A 1 37  ? 25.682  -0.415  17.372  1.00 76.38  ? 33  LYS   A CE  1 
ATOM   245  N NZ  . LYS   A 1 37  ? 25.715  -0.593  18.826  1.00 92.25  ? 33  LYS   A NZ  1 
ATOM   246  N N   . ARG   A 1 38  ? 23.650  6.055   15.654  1.00 56.50  ? 34  ARG   A N   1 
ATOM   247  C CA  . ARG   A 1 38  ? 23.765  7.382   15.064  1.00 58.33  ? 34  ARG   A CA  1 
ATOM   248  C C   . ARG   A 1 38  ? 23.145  8.468   15.932  1.00 59.37  ? 34  ARG   A C   1 
ATOM   249  O O   . ARG   A 1 38  ? 23.284  9.653   15.605  1.00 69.53  ? 34  ARG   A O   1 
ATOM   250  C CB  . ARG   A 1 38  ? 23.106  7.410   13.680  1.00 59.66  ? 34  ARG   A CB  1 
ATOM   251  C CG  . ARG   A 1 38  ? 23.497  6.265   12.759  1.00 64.64  ? 34  ARG   A CG  1 
ATOM   252  C CD  . ARG   A 1 38  ? 24.792  6.570   12.026  1.00 69.80  ? 34  ARG   A CD  1 
ATOM   253  N NE  . ARG   A 1 38  ? 25.944  6.228   12.851  1.00 79.81  ? 34  ARG   A NE  1 
ATOM   254  C CZ  . ARG   A 1 38  ? 26.420  4.994   12.988  1.00 84.31  ? 34  ARG   A CZ  1 
ATOM   255  N NH1 . ARG   A 1 38  ? 25.850  3.985   12.343  1.00 81.57  ? 34  ARG   A NH1 1 
ATOM   256  N NH2 . ARG   A 1 38  ? 27.465  4.768   13.768  1.00 85.93  ? 34  ARG   A NH2 1 
ATOM   257  N N   . GLY   A 1 39  ? 22.464  8.100   17.014  1.00 47.92  ? 35  GLY   A N   1 
ATOM   258  C CA  . GLY   A 1 39  ? 21.804  9.052   17.883  1.00 69.08  ? 35  GLY   A CA  1 
ATOM   259  C C   . GLY   A 1 39  ? 20.295  9.069   17.775  1.00 67.13  ? 35  GLY   A C   1 
ATOM   260  O O   . GLY   A 1 39  ? 19.655  9.882   18.453  1.00 66.72  ? 35  GLY   A O   1 
ATOM   261  N N   . MET   A 1 40  ? 19.705  8.204   16.956  1.00 58.06  ? 36  MET   A N   1 
ATOM   262  C CA  . MET   A 1 40  ? 18.265  8.178   16.759  1.00 58.22  ? 36  MET   A CA  1 
ATOM   263  C C   . MET   A 1 40  ? 17.575  7.306   17.802  1.00 62.55  ? 36  MET   A C   1 
ATOM   264  O O   . MET   A 1 40  ? 18.186  6.449   18.445  1.00 70.67  ? 36  MET   A O   1 
ATOM   265  C CB  . MET   A 1 40  ? 17.908  7.647   15.371  1.00 51.62  ? 36  MET   A CB  1 
ATOM   266  C CG  . MET   A 1 40  ? 18.526  8.364   14.191  1.00 54.41  ? 36  MET   A CG  1 
ATOM   267  S SD  . MET   A 1 40  ? 17.697  7.793   12.692  1.00 66.99  ? 36  MET   A SD  1 
ATOM   268  C CE  . MET   A 1 40  ? 18.339  8.917   11.463  1.00 61.93  ? 36  MET   A CE  1 
ATOM   269  N N   . GLU   A 1 41  ? 16.273  7.535   17.949  1.00 54.30  ? 37  GLU   A N   1 
ATOM   270  C CA  . GLU   A 1 41  ? 15.370  6.613   18.622  1.00 62.84  ? 37  GLU   A CA  1 
ATOM   271  C C   . GLU   A 1 41  ? 14.515  5.945   17.554  1.00 57.17  ? 37  GLU   A C   1 
ATOM   272  O O   . GLU   A 1 41  ? 13.792  6.626   16.819  1.00 57.60  ? 37  GLU   A O   1 
ATOM   273  C CB  . GLU   A 1 41  ? 14.491  7.331   19.645  1.00 62.36  ? 37  GLU   A CB  1 
ATOM   274  C CG  . GLU   A 1 41  ? 15.232  7.857   20.861  1.00 74.06  ? 37  GLU   A CG  1 
ATOM   275  C CD  . GLU   A 1 41  ? 14.303  8.515   21.863  1.00 88.63  ? 37  GLU   A CD  1 
ATOM   276  O OE1 . GLU   A 1 41  ? 14.477  9.720   22.138  1.00 98.08  ? 37  GLU   A OE1 1 
ATOM   277  O OE2 . GLU   A 1 41  ? 13.396  7.825   22.375  1.00 91.59  ? 37  GLU   A OE2 1 
ATOM   278  N N   . VAL   A 1 42  ? 14.611  4.623   17.459  1.00 54.26  ? 38  VAL   A N   1 
ATOM   279  C CA  . VAL   A 1 42  ? 13.850  3.840   16.492  1.00 55.62  ? 38  VAL   A CA  1 
ATOM   280  C C   . VAL   A 1 42  ? 12.856  2.991   17.268  1.00 52.20  ? 38  VAL   A C   1 
ATOM   281  O O   . VAL   A 1 42  ? 13.252  2.110   18.041  1.00 54.42  ? 38  VAL   A O   1 
ATOM   282  C CB  . VAL   A 1 42  ? 14.765  2.966   15.622  1.00 48.97  ? 38  VAL   A CB  1 
ATOM   283  C CG1 . VAL   A 1 42  ? 13.958  2.281   14.530  1.00 40.24  ? 38  VAL   A CG1 1 
ATOM   284  C CG2 . VAL   A 1 42  ? 15.887  3.801   15.026  1.00 42.82  ? 38  VAL   A CG2 1 
ATOM   285  N N   . VAL   A 1 43  ? 11.568  3.253   17.068  1.00 53.19  ? 39  VAL   A N   1 
ATOM   286  C CA  . VAL   A 1 43  ? 10.505  2.583   17.807  1.00 54.41  ? 39  VAL   A CA  1 
ATOM   287  C C   . VAL   A 1 43  ? 9.720   1.695   16.853  1.00 50.13  ? 39  VAL   A C   1 
ATOM   288  O O   . VAL   A 1 43  ? 9.402   2.099   15.727  1.00 43.85  ? 39  VAL   A O   1 
ATOM   289  C CB  . VAL   A 1 43  ? 9.590   3.594   18.523  1.00 61.41  ? 39  VAL   A CB  1 
ATOM   290  C CG1 . VAL   A 1 43  ? 10.412  4.459   19.454  1.00 63.25  ? 39  VAL   A CG1 1 
ATOM   291  C CG2 . VAL   A 1 43  ? 8.841   4.470   17.527  1.00 55.36  ? 39  VAL   A CG2 1 
ATOM   292  N N   . GLN   A 1 44  ? 9.436   0.473   17.295  1.00 57.89  ? 40  GLN   A N   1 
ATOM   293  C CA  . GLN   A 1 44  ? 8.553   -0.427  16.564  1.00 55.26  ? 40  GLN   A CA  1 
ATOM   294  C C   . GLN   A 1 44  ? 7.121   -0.103  16.964  1.00 59.72  ? 40  GLN   A C   1 
ATOM   295  O O   . GLN   A 1 44  ? 6.723   -0.326  18.112  1.00 69.40  ? 40  GLN   A O   1 
ATOM   296  C CB  . GLN   A 1 44  ? 8.900   -1.883  16.862  1.00 72.16  ? 40  GLN   A CB  1 
ATOM   297  C CG  . GLN   A 1 44  ? 8.434   -2.861  15.796  1.00 68.07  ? 40  GLN   A CG  1 
ATOM   298  C CD  . GLN   A 1 44  ? 9.273   -4.123  15.756  1.00 69.46  ? 40  GLN   A CD  1 
ATOM   299  O OE1 . GLN   A 1 44  ? 10.408  -4.143  16.234  1.00 63.16  ? 40  GLN   A OE1 1 
ATOM   300  N NE2 . GLN   A 1 44  ? 8.718   -5.185  15.185  1.00 73.16  ? 40  GLN   A NE2 1 
ATOM   301  N N   . LEU   A 1 45  ? 6.352   0.437   16.024  1.00 68.49  ? 41  LEU   A N   1 
ATOM   302  C CA  . LEU   A 1 45  ? 5.014   0.916   16.334  1.00 68.47  ? 41  LEU   A CA  1 
ATOM   303  C C   . LEU   A 1 45  ? 4.096   -0.233  16.728  1.00 74.62  ? 41  LEU   A C   1 
ATOM   304  O O   . LEU   A 1 45  ? 4.150   -1.323  16.152  1.00 64.88  ? 41  LEU   A O   1 
ATOM   305  C CB  . LEU   A 1 45  ? 4.425   1.659   15.136  1.00 59.73  ? 41  LEU   A CB  1 
ATOM   306  C CG  . LEU   A 1 45  ? 5.031   3.022   14.797  1.00 52.10  ? 41  LEU   A CG  1 
ATOM   307  C CD1 . LEU   A 1 45  ? 4.411   3.574   13.524  1.00 41.47  ? 41  LEU   A CD1 1 
ATOM   308  C CD2 . LEU   A 1 45  ? 4.852   3.994   15.952  1.00 48.30  ? 41  LEU   A CD2 1 
ATOM   309  N N   . ASN   A 1 46  ? 3.255   0.017   17.728  1.00 75.56  ? 42  ASN   A N   1 
ATOM   310  C CA  . ASN   A 1 46  ? 2.157   -0.875  18.078  1.00 86.74  ? 42  ASN   A CA  1 
ATOM   311  C C   . ASN   A 1 46  ? 0.871   -0.261  17.541  1.00 94.78  ? 42  ASN   A C   1 
ATOM   312  O O   . ASN   A 1 46  ? 0.373   0.729   18.087  1.00 92.40  ? 42  ASN   A O   1 
ATOM   313  C CB  . ASN   A 1 46  ? 2.069   -1.093  19.588  1.00 86.23  ? 42  ASN   A CB  1 
ATOM   314  C CG  . ASN   A 1 46  ? 3.205   -1.941  20.127  1.00 84.35  ? 42  ASN   A CG  1 
ATOM   315  O OD1 . ASN   A 1 46  ? 4.005   -1.482  20.943  1.00 87.70  ? 42  ASN   A OD1 1 
ATOM   316  N ND2 . ASN   A 1 46  ? 3.279   -3.188  19.675  1.00 70.16  ? 42  ASN   A ND2 1 
ATOM   317  N N   . LEU   A 1 47  ? 0.342   -0.839  16.461  1.00 94.13  ? 43  LEU   A N   1 
ATOM   318  C CA  . LEU   A 1 47  ? -0.968  -0.459  15.944  1.00 107.54 ? 43  LEU   A CA  1 
ATOM   319  C C   . LEU   A 1 47  ? -2.118  -1.034  16.754  1.00 97.89  ? 43  LEU   A C   1 
ATOM   320  O O   . LEU   A 1 47  ? -3.233  -1.147  16.233  1.00 101.66 ? 43  LEU   A O   1 
ATOM   321  C CB  . LEU   A 1 47  ? -1.101  -0.853  14.468  1.00 100.89 ? 43  LEU   A CB  1 
ATOM   322  C CG  . LEU   A 1 47  ? -0.660  0.183   13.431  1.00 102.36 ? 43  LEU   A CG  1 
ATOM   323  C CD1 . LEU   A 1 47  ? -1.599  1.375   13.488  1.00 96.32  ? 43  LEU   A CD1 1 
ATOM   324  C CD2 . LEU   A 1 47  ? 0.770   0.649   13.652  1.00 90.59  ? 43  LEU   A CD2 1 
ATOM   325  N N   . SER   A 1 48  ? -1.880  -1.393  18.013  1.00 89.12  ? 44  SER   A N   1 
ATOM   326  C CA  . SER   A 1 48  ? -2.960  -1.618  18.964  1.00 84.59  ? 44  SER   A CA  1 
ATOM   327  C C   . SER   A 1 48  ? -3.265  -0.350  19.751  1.00 87.65  ? 44  SER   A C   1 
ATOM   328  O O   . SER   A 1 48  ? -4.427  -0.070  20.064  1.00 83.42  ? 44  SER   A O   1 
ATOM   329  C CB  . SER   A 1 48  ? -2.594  -2.752  19.922  1.00 74.22  ? 44  SER   A CB  1 
ATOM   330  O OG  . SER   A 1 48  ? -1.587  -2.341  20.828  1.00 89.16  ? 44  SER   A OG  1 
ATOM   331  N N   . ARG   A 1 49  ? -2.223  0.418   20.073  1.00 88.94  ? 45  ARG   A N   1 
ATOM   332  C CA  . ARG   A 1 49  ? -2.285  1.721   20.708  1.00 86.47  ? 45  ARG   A CA  1 
ATOM   333  C C   . ARG   A 1 49  ? -2.664  2.789   19.686  1.00 78.17  ? 45  ARG   A C   1 
ATOM   334  O O   . ARG   A 1 49  ? -2.448  2.611   18.486  1.00 82.20  ? 45  ARG   A O   1 
ATOM   335  C CB  . ARG   A 1 49  ? -0.930  2.067   21.336  1.00 90.71  ? 45  ARG   A CB  1 
ATOM   336  C CG  . ARG   A 1 49  ? -0.568  1.249   22.565  1.00 97.57  ? 45  ARG   A CG  1 
ATOM   337  C CD  . ARG   A 1 49  ? 0.766   1.665   23.213  1.00 96.84  ? 45  ARG   A CD  1 
ATOM   338  N NE  . ARG   A 1 49  ? 1.957   1.149   22.536  1.00 105.20 ? 45  ARG   A NE  1 
ATOM   339  C CZ  . ARG   A 1 49  ? 3.202   1.523   22.827  1.00 104.44 ? 45  ARG   A CZ  1 
ATOM   340  N NH1 . ARG   A 1 49  ? 3.421   2.416   23.783  1.00 109.45 ? 45  ARG   A NH1 1 
ATOM   341  N NH2 . ARG   A 1 49  ? 4.232   0.999   22.173  1.00 91.14  ? 45  ARG   A NH2 1 
ATOM   342  N N   . PRO   A 1 50  ? -3.232  3.907   20.130  1.00 73.40  ? 46  PRO   A N   1 
ATOM   343  C CA  . PRO   A 1 50  ? -3.270  5.082   19.253  1.00 80.57  ? 46  PRO   A CA  1 
ATOM   344  C C   . PRO   A 1 50  ? -1.854  5.596   19.050  1.00 75.71  ? 46  PRO   A C   1 
ATOM   345  O O   . PRO   A 1 50  ? -1.029  5.560   19.964  1.00 71.73  ? 46  PRO   A O   1 
ATOM   346  C CB  . PRO   A 1 50  ? -4.151  6.090   20.006  1.00 73.59  ? 46  PRO   A CB  1 
ATOM   347  C CG  . PRO   A 1 50  ? -4.390  5.528   21.360  1.00 74.48  ? 46  PRO   A CG  1 
ATOM   348  C CD  . PRO   A 1 50  ? -3.810  4.157   21.460  1.00 76.02  ? 46  PRO   A CD  1 
ATOM   349  N N   . ILE   A 1 51  ? -1.564  6.054   17.830  1.00 66.17  ? 47  ILE   A N   1 
ATOM   350  C CA  . ILE   A 1 51  ? -0.176  6.326   17.484  1.00 66.68  ? 47  ILE   A CA  1 
ATOM   351  C C   . ILE   A 1 51  ? 0.317   7.600   18.168  1.00 67.75  ? 47  ILE   A C   1 
ATOM   352  O O   . ILE   A 1 51  ? 1.530   7.783   18.337  1.00 68.72  ? 47  ILE   A O   1 
ATOM   353  C CB  . ILE   A 1 51  ? -0.025  6.412   15.959  1.00 57.99  ? 47  ILE   A CB  1 
ATOM   354  C CG1 . ILE   A 1 51  ? -0.548  5.127   15.312  1.00 65.23  ? 47  ILE   A CG1 1 
ATOM   355  C CG2 . ILE   A 1 51  ? 1.447   6.507   15.581  1.00 60.72  ? 47  ILE   A CG2 1 
ATOM   356  C CD1 . ILE   A 1 51  ? -0.716  5.230   13.809  1.00 68.76  ? 47  ILE   A CD1 1 
ATOM   357  N N   . GLU   A 1 52  ? -0.600  8.483   18.587  1.00 72.78  ? 48  GLU   A N   1 
ATOM   358  C CA  . GLU   A 1 52  ? -0.206  9.663   19.354  1.00 78.25  ? 48  GLU   A CA  1 
ATOM   359  C C   . GLU   A 1 52  ? 0.426   9.282   20.687  1.00 71.98  ? 48  GLU   A C   1 
ATOM   360  O O   . GLU   A 1 52  ? 1.239   10.039  21.228  1.00 78.29  ? 48  GLU   A O   1 
ATOM   361  C CB  . GLU   A 1 52  ? -1.416  10.568  19.586  1.00 92.45  ? 48  GLU   A CB  1 
ATOM   362  C CG  . GLU   A 1 52  ? -1.741  11.494  18.422  1.00 92.18  ? 48  GLU   A CG  1 
ATOM   363  C CD  . GLU   A 1 52  ? -2.960  12.361  18.674  1.00 102.91 ? 48  GLU   A CD  1 
ATOM   364  O OE1 . GLU   A 1 52  ? -3.671  12.121  19.673  1.00 112.07 ? 48  GLU   A OE1 1 
ATOM   365  O OE2 . GLU   A 1 52  ? -3.209  13.281  17.866  1.00 90.96  ? 48  GLU   A OE2 1 
ATOM   366  N N   . GLU   A 1 53  ? 0.062   8.118   21.233  1.00 69.44  ? 49  GLU   A N   1 
ATOM   367  C CA  . GLU   A 1 53  ? 0.681   7.637   22.462  1.00 55.66  ? 49  GLU   A CA  1 
ATOM   368  C C   . GLU   A 1 53  ? 2.136   7.240   22.257  1.00 66.10  ? 49  GLU   A C   1 
ATOM   369  O O   . GLU   A 1 53  ? 2.869   7.086   23.240  1.00 65.07  ? 49  GLU   A O   1 
ATOM   370  C CB  . GLU   A 1 53  ? -0.102  6.446   23.015  1.00 60.41  ? 49  GLU   A CB  1 
ATOM   371  C CG  . GLU   A 1 53  ? -1.464  6.798   23.583  1.00 67.36  ? 49  GLU   A CG  1 
ATOM   372  C CD  . GLU   A 1 53  ? -2.100  5.635   24.319  1.00 82.86  ? 49  GLU   A CD  1 
ATOM   373  O OE1 . GLU   A 1 53  ? -1.385  4.653   24.609  1.00 85.18  ? 49  GLU   A OE1 1 
ATOM   374  O OE2 . GLU   A 1 53  ? -3.313  5.702   24.607  1.00 78.82  ? 49  GLU   A OE2 1 
ATOM   375  N N   . GLN   A 1 54  ? 2.566   7.066   21.009  1.00 68.58  ? 50  GLN   A N   1 
ATOM   376  C CA  . GLN   A 1 54  ? 3.934   6.688   20.692  1.00 62.99  ? 50  GLN   A CA  1 
ATOM   377  C C   . GLN   A 1 54  ? 4.731   7.828   20.078  1.00 64.44  ? 50  GLN   A C   1 
ATOM   378  O O   . GLN   A 1 54  ? 5.881   7.618   19.678  1.00 67.64  ? 50  GLN   A O   1 
ATOM   379  C CB  . GLN   A 1 54  ? 3.934   5.481   19.749  1.00 55.17  ? 50  GLN   A CB  1 
ATOM   380  C CG  . GLN   A 1 54  ? 2.969   4.385   20.171  1.00 70.32  ? 50  GLN   A CG  1 
ATOM   381  C CD  . GLN   A 1 54  ? 2.902   3.244   19.177  1.00 75.20  ? 50  GLN   A CD  1 
ATOM   382  O OE1 . GLN   A 1 54  ? 3.883   2.531   18.968  1.00 81.72  ? 50  GLN   A OE1 1 
ATOM   383  N NE2 . GLN   A 1 54  ? 1.741   3.065   18.559  1.00 78.12  ? 50  GLN   A NE2 1 
ATOM   384  N N   . GLY   A 1 55  ? 4.155   9.026   19.994  1.00 69.96  ? 51  GLY   A N   1 
ATOM   385  C CA  . GLY   A 1 55  ? 4.841   10.156  19.421  1.00 66.34  ? 51  GLY   A CA  1 
ATOM   386  C C   . GLY   A 1 55  ? 5.794   10.807  20.400  1.00 69.97  ? 51  GLY   A C   1 
ATOM   387  O O   . GLY   A 1 55  ? 5.965   10.370  21.546  1.00 74.31  ? 51  GLY   A O   1 
ATOM   388  N N   . PRO   A 1 56  ? 6.450   11.886  19.942  1.00 71.60  ? 52  PRO   A N   1 
ATOM   389  C CA  . PRO   A 1 56  ? 6.325   12.414  18.580  1.00 65.63  ? 52  PRO   A CA  1 
ATOM   390  C C   . PRO   A 1 56  ? 7.124   11.589  17.580  1.00 65.39  ? 52  PRO   A C   1 
ATOM   391  O O   . PRO   A 1 56  ? 7.962   10.790  17.986  1.00 63.02  ? 52  PRO   A O   1 
ATOM   392  C CB  . PRO   A 1 56  ? 6.894   13.827  18.703  1.00 56.23  ? 52  PRO   A CB  1 
ATOM   393  C CG  . PRO   A 1 56  ? 7.911   13.710  19.782  1.00 65.74  ? 52  PRO   A CG  1 
ATOM   394  C CD  . PRO   A 1 56  ? 7.383   12.685  20.757  1.00 73.66  ? 52  PRO   A CD  1 
ATOM   395  N N   . LEU   A 1 57  ? 6.860   11.766  16.290  1.00 51.72  ? 53  LEU   A N   1 
ATOM   396  C CA  . LEU   A 1 57  ? 7.555   11.019  15.254  1.00 52.16  ? 53  LEU   A CA  1 
ATOM   397  C C   . LEU   A 1 57  ? 8.007   11.978  14.167  1.00 55.48  ? 53  LEU   A C   1 
ATOM   398  O O   . LEU   A 1 57  ? 7.198   12.745  13.634  1.00 56.21  ? 53  LEU   A O   1 
ATOM   399  C CB  . LEU   A 1 57  ? 6.662   9.921   14.665  1.00 50.58  ? 53  LEU   A CB  1 
ATOM   400  C CG  . LEU   A 1 57  ? 6.478   8.688   15.553  1.00 50.29  ? 53  LEU   A CG  1 
ATOM   401  C CD1 . LEU   A 1 57  ? 5.378   7.788   15.015  1.00 51.91  ? 53  LEU   A CD1 1 
ATOM   402  C CD2 . LEU   A 1 57  ? 7.786   7.923   15.689  1.00 51.63  ? 53  LEU   A CD2 1 
ATOM   403  N N   . ASP   A 1 58  ? 9.300   11.942  13.852  1.00 43.46  ? 54  ASP   A N   1 
ATOM   404  C CA  . ASP   A 1 58  ? 9.837   12.741  12.762  1.00 45.77  ? 54  ASP   A CA  1 
ATOM   405  C C   . ASP   A 1 58  ? 9.709   12.043  11.416  1.00 42.55  ? 54  ASP   A C   1 
ATOM   406  O O   . ASP   A 1 58  ? 9.517   12.714  10.395  1.00 41.00  ? 54  ASP   A O   1 
ATOM   407  C CB  . ASP   A 1 58  ? 11.306  13.082  13.031  1.00 38.65  ? 54  ASP   A CB  1 
ATOM   408  C CG  . ASP   A 1 58  ? 11.497  13.857  14.322  1.00 57.33  ? 54  ASP   A CG  1 
ATOM   409  O OD1 . ASP   A 1 58  ? 10.986  14.993  14.415  1.00 63.05  ? 54  ASP   A OD1 1 
ATOM   410  O OD2 . ASP   A 1 58  ? 12.156  13.331  15.243  1.00 53.70  ? 54  ASP   A OD2 1 
ATOM   411  N N   . VAL   A 1 59  ? 9.803   10.715  11.393  1.00 42.48  ? 55  VAL   A N   1 
ATOM   412  C CA  . VAL   A 1 59  ? 9.699   9.929   10.168  1.00 49.70  ? 55  VAL   A CA  1 
ATOM   413  C C   . VAL   A 1 59  ? 8.964   8.633   10.486  1.00 47.73  ? 55  VAL   A C   1 
ATOM   414  O O   . VAL   A 1 59  ? 9.200   8.013   11.529  1.00 47.07  ? 55  VAL   A O   1 
ATOM   415  C CB  . VAL   A 1 59  ? 11.089  9.636   9.557   1.00 43.48  ? 55  VAL   A CB  1 
ATOM   416  C CG1 . VAL   A 1 59  ? 11.011  8.512   8.532   1.00 47.67  ? 55  VAL   A CG1 1 
ATOM   417  C CG2 . VAL   A 1 59  ? 11.679  10.887  8.924   1.00 53.03  ? 55  VAL   A CG2 1 
ATOM   418  N N   . ILE   A 1 60  ? 8.065   8.231   9.591   1.00 47.76  ? 56  ILE   A N   1 
ATOM   419  C CA  . ILE   A 1 60  ? 7.374   6.949   9.674   1.00 39.89  ? 56  ILE   A CA  1 
ATOM   420  C C   . ILE   A 1 60  ? 7.651   6.187   8.386   1.00 51.73  ? 56  ILE   A C   1 
ATOM   421  O O   . ILE   A 1 60  ? 7.272   6.639   7.298   1.00 50.67  ? 56  ILE   A O   1 
ATOM   422  C CB  . ILE   A 1 60  ? 5.862   7.122   9.889   1.00 42.47  ? 56  ILE   A CB  1 
ATOM   423  C CG1 . ILE   A 1 60  ? 5.586   7.814   11.226  1.00 54.17  ? 56  ILE   A CG1 1 
ATOM   424  C CG2 . ILE   A 1 60  ? 5.159   5.773   9.824   1.00 37.91  ? 56  ILE   A CG2 1 
ATOM   425  C CD1 . ILE   A 1 60  ? 4.123   7.827   11.614  1.00 61.40  ? 56  ILE   A CD1 1 
ATOM   426  N N   . ILE   A 1 61  ? 8.316   5.041   8.505   1.00 47.30  ? 57  ILE   A N   1 
ATOM   427  C CA  . ILE   A 1 61  ? 8.607   4.166   7.375   1.00 45.32  ? 57  ILE   A CA  1 
ATOM   428  C C   . ILE   A 1 61  ? 7.792   2.891   7.546   1.00 50.89  ? 57  ILE   A C   1 
ATOM   429  O O   . ILE   A 1 61  ? 7.789   2.288   8.626   1.00 45.76  ? 57  ILE   A O   1 
ATOM   430  C CB  . ILE   A 1 61  ? 10.114  3.867   7.263   1.00 43.32  ? 57  ILE   A CB  1 
ATOM   431  C CG1 . ILE   A 1 61  ? 10.382  2.835   6.165   1.00 49.84  ? 57  ILE   A CG1 1 
ATOM   432  C CG2 . ILE   A 1 61  ? 10.688  3.419   8.602   1.00 50.13  ? 57  ILE   A CG2 1 
ATOM   433  C CD1 . ILE   A 1 61  ? 11.847  2.691   5.812   1.00 54.51  ? 57  ILE   A CD1 1 
ATOM   434  N N   . HIS   A 1 62  ? 7.089   2.487   6.492   1.00 45.79  ? 58  HIS   A N   1 
ATOM   435  C CA  . HIS   A 1 62  ? 6.114   1.415   6.626   1.00 52.84  ? 58  HIS   A CA  1 
ATOM   436  C C   . HIS   A 1 62  ? 5.903   0.736   5.282   1.00 49.63  ? 58  HIS   A C   1 
ATOM   437  O O   . HIS   A 1 62  ? 6.327   1.228   4.233   1.00 46.00  ? 58  HIS   A O   1 
ATOM   438  C CB  . HIS   A 1 62  ? 4.781   1.949   7.160   1.00 44.69  ? 58  HIS   A CB  1 
ATOM   439  C CG  . HIS   A 1 62  ? 3.992   2.711   6.140   1.00 54.52  ? 58  HIS   A CG  1 
ATOM   440  N ND1 . HIS   A 1 62  ? 3.126   2.100   5.258   1.00 44.67  ? 58  HIS   A ND1 1 
ATOM   441  C CD2 . HIS   A 1 62  ? 3.949   4.034   5.853   1.00 50.37  ? 58  HIS   A CD2 1 
ATOM   442  C CE1 . HIS   A 1 62  ? 2.579   3.014   4.477   1.00 55.48  ? 58  HIS   A CE1 1 
ATOM   443  N NE2 . HIS   A 1 62  ? 3.061   4.196   4.817   1.00 50.76  ? 58  HIS   A NE2 1 
ATOM   444  N N   . LYS   A 1 63  ? 5.227   -0.418  5.336   1.00 47.95  ? 59  LYS   A N   1 
ATOM   445  C CA  . LYS   A 1 63  ? 4.651   -1.083  4.168   1.00 55.19  ? 59  LYS   A CA  1 
ATOM   446  C C   . LYS   A 1 63  ? 3.387   -1.795  4.660   1.00 48.68  ? 59  LYS   A C   1 
ATOM   447  O O   . LYS   A 1 63  ? 3.385   -2.986  4.983   1.00 42.90  ? 59  LYS   A O   1 
ATOM   448  C CB  . LYS   A 1 63  ? 5.618   -2.053  3.491   1.00 52.37  ? 59  LYS   A CB  1 
ATOM   449  C CG  . LYS   A 1 63  ? 5.216   -2.386  2.063   1.00 37.94  ? 59  LYS   A CG  1 
ATOM   450  C CD  . LYS   A 1 63  ? 6.166   -3.372  1.411   1.00 48.67  ? 59  LYS   A CD  1 
ATOM   451  C CE  . LYS   A 1 63  ? 5.508   -4.041  0.215   1.00 43.21  ? 59  LYS   A CE  1 
ATOM   452  N NZ  . LYS   A 1 63  ? 6.426   -4.990  -0.472  1.00 63.39  ? 59  LYS   A NZ  1 
ATOM   453  N N   . LEU   A 1 64  ? 2.294   -1.035  4.728   1.00 55.40  ? 60  LEU   A N   1 
ATOM   454  C CA  . LEU   A 1 64  ? 1.015   -1.526  5.219   1.00 58.90  ? 60  LEU   A CA  1 
ATOM   455  C C   . LEU   A 1 64  ? 0.117   -2.048  4.104   1.00 55.51  ? 60  LEU   A C   1 
ATOM   456  O O   . LEU   A 1 64  ? -1.107  -2.071  4.272   1.00 52.57  ? 60  LEU   A O   1 
ATOM   457  C CB  . LEU   A 1 64  ? 0.292   -0.420  5.991   1.00 51.95  ? 60  LEU   A CB  1 
ATOM   458  C CG  . LEU   A 1 64  ? 0.786   -0.116  7.406   1.00 55.39  ? 60  LEU   A CG  1 
ATOM   459  C CD1 . LEU   A 1 64  ? 0.506   1.335   7.766   1.00 59.78  ? 60  LEU   A CD1 1 
ATOM   460  C CD2 . LEU   A 1 64  ? 0.139   -1.054  8.411   1.00 69.71  ? 60  LEU   A CD2 1 
ATOM   461  N N   . THR   A 1 65  ? 0.698   -2.475  2.979   1.00 58.92  ? 61  THR   A N   1 
ATOM   462  C CA  . THR   A 1 65  ? -0.106  -2.878  1.828   1.00 68.50  ? 61  THR   A CA  1 
ATOM   463  C C   . THR   A 1 65  ? -1.036  -4.040  2.157   1.00 58.67  ? 61  THR   A C   1 
ATOM   464  O O   . THR   A 1 65  ? -2.118  -4.152  1.569   1.00 61.44  ? 61  THR   A O   1 
ATOM   465  C CB  . THR   A 1 65  ? 0.805   -3.241  0.651   1.00 53.25  ? 61  THR   A CB  1 
ATOM   466  O OG1 . THR   A 1 65  ? 0.008   -3.642  -0.470  1.00 63.86  ? 61  THR   A OG1 1 
ATOM   467  C CG2 . THR   A 1 65  ? 1.757   -4.370  1.027   1.00 54.77  ? 61  THR   A CG2 1 
ATOM   468  N N   . ASP   A 1 66  ? -0.647  -4.904  3.096   1.00 55.84  ? 62  ASP   A N   1 
ATOM   469  C CA  . ASP   A 1 66  ? -1.467  -6.058  3.442   1.00 50.79  ? 62  ASP   A CA  1 
ATOM   470  C C   . ASP   A 1 66  ? -2.569  -5.723  4.442   1.00 58.38  ? 62  ASP   A C   1 
ATOM   471  O O   . ASP   A 1 66  ? -3.573  -6.441  4.496   1.00 50.87  ? 62  ASP   A O   1 
ATOM   472  C CB  . ASP   A 1 66  ? -0.575  -7.186  3.967   1.00 64.92  ? 62  ASP   A CB  1 
ATOM   473  C CG  . ASP   A 1 66  ? 0.511   -6.686  4.897   1.00 80.82  ? 62  ASP   A CG  1 
ATOM   474  O OD1 . ASP   A 1 66  ? 0.239   -5.764  5.694   1.00 74.35  ? 62  ASP   A OD1 1 
ATOM   475  O OD2 . ASP   A 1 66  ? 1.639   -7.220  4.833   1.00 78.02  ? 62  ASP   A OD2 1 
ATOM   476  N N   . VAL   A 1 67  ? -2.404  -4.662  5.235   1.00 50.29  ? 63  VAL   A N   1 
ATOM   477  C CA  . VAL   A 1 67  ? -3.541  -4.072  5.935   1.00 47.41  ? 63  VAL   A CA  1 
ATOM   478  C C   . VAL   A 1 67  ? -4.429  -3.300  4.970   1.00 52.68  ? 63  VAL   A C   1 
ATOM   479  O O   . VAL   A 1 67  ? -5.660  -3.347  5.070   1.00 44.63  ? 63  VAL   A O   1 
ATOM   480  C CB  . VAL   A 1 67  ? -3.057  -3.183  7.096   1.00 43.62  ? 63  VAL   A CB  1 
ATOM   481  C CG1 . VAL   A 1 67  ? -4.210  -2.364  7.651   1.00 49.26  ? 63  VAL   A CG1 1 
ATOM   482  C CG2 . VAL   A 1 67  ? -2.486  -4.046  8.208   1.00 59.95  ? 63  VAL   A CG2 1 
ATOM   483  N N   . ILE   A 1 68  ? -3.822  -2.591  4.016   1.00 46.32  ? 64  ILE   A N   1 
ATOM   484  C CA  . ILE   A 1 68  ? -4.600  -1.816  3.052   1.00 50.70  ? 64  ILE   A CA  1 
ATOM   485  C C   . ILE   A 1 68  ? -5.533  -2.726  2.262   1.00 46.12  ? 64  ILE   A C   1 
ATOM   486  O O   . ILE   A 1 68  ? -6.691  -2.376  1.999   1.00 42.16  ? 64  ILE   A O   1 
ATOM   487  C CB  . ILE   A 1 68  ? -3.662  -1.019  2.125   1.00 55.84  ? 64  ILE   A CB  1 
ATOM   488  C CG1 . ILE   A 1 68  ? -2.953  0.087   2.911   1.00 54.87  ? 64  ILE   A CG1 1 
ATOM   489  C CG2 . ILE   A 1 68  ? -4.432  -0.434  0.960   1.00 52.49  ? 64  ILE   A CG2 1 
ATOM   490  C CD1 . ILE   A 1 68  ? -3.885  1.161   3.418   1.00 62.14  ? 64  ILE   A CD1 1 
ATOM   491  N N   . LEU   A 1 69  ? -5.050  -3.914  1.889   1.00 50.78  ? 65  LEU   A N   1 
ATOM   492  C CA  . LEU   A 1 69  ? -5.878  -4.853  1.137   1.00 56.83  ? 65  LEU   A CA  1 
ATOM   493  C C   . LEU   A 1 69  ? -7.093  -5.293  1.944   1.00 47.61  ? 65  LEU   A C   1 
ATOM   494  O O   . LEU   A 1 69  ? -8.214  -5.328  1.423   1.00 48.62  ? 65  LEU   A O   1 
ATOM   495  C CB  . LEU   A 1 69  ? -5.047  -6.069  0.725   1.00 49.84  ? 65  LEU   A CB  1 
ATOM   496  C CG  . LEU   A 1 69  ? -4.203  -5.942  -0.542  1.00 63.99  ? 65  LEU   A CG  1 
ATOM   497  C CD1 . LEU   A 1 69  ? -3.163  -7.050  -0.605  1.00 53.92  ? 65  LEU   A CD1 1 
ATOM   498  C CD2 . LEU   A 1 69  ? -5.093  -5.970  -1.773  1.00 52.52  ? 65  LEU   A CD2 1 
ATOM   499  N N   . GLU   A 1 70  ? -6.889  -5.638  3.217   1.00 47.76  ? 66  GLU   A N   1 
ATOM   500  C CA  . GLU   A 1 70  ? -7.995  -6.105  4.047   1.00 42.44  ? 66  GLU   A CA  1 
ATOM   501  C C   . GLU   A 1 70  ? -9.006  -4.995  4.297   1.00 48.95  ? 66  GLU   A C   1 
ATOM   502  O O   . GLU   A 1 70  ? -10.218 -5.240  4.307   1.00 41.65  ? 66  GLU   A O   1 
ATOM   503  C CB  . GLU   A 1 70  ? -7.460  -6.643  5.372   1.00 51.88  ? 66  GLU   A CB  1 
ATOM   504  C CG  . GLU   A 1 70  ? -6.968  -8.073  5.319   1.00 55.60  ? 66  GLU   A CG  1 
ATOM   505  C CD  . GLU   A 1 70  ? -5.902  -8.350  6.360   1.00 61.90  ? 66  GLU   A CD  1 
ATOM   506  O OE1 . GLU   A 1 70  ? -5.405  -9.493  6.413   1.00 62.38  ? 66  GLU   A OE1 1 
ATOM   507  O OE2 . GLU   A 1 70  ? -5.560  -7.423  7.126   1.00 60.11  ? 66  GLU   A OE2 1 
ATOM   508  N N   . ALA   A 1 71  ? -8.524  -3.768  4.507   1.00 48.73  ? 67  ALA   A N   1 
ATOM   509  C CA  . ALA   A 1 71  ? -9.420  -2.644  4.756   1.00 50.21  ? 67  ALA   A CA  1 
ATOM   510  C C   . ALA   A 1 71  ? -10.338 -2.384  3.569   1.00 52.65  ? 67  ALA   A C   1 
ATOM   511  O O   . ALA   A 1 71  ? -11.499 -2.000  3.754   1.00 52.59  ? 67  ALA   A O   1 
ATOM   512  C CB  . ALA   A 1 71  ? -8.603  -1.396  5.084   1.00 51.12  ? 67  ALA   A CB  1 
ATOM   513  N N   . ASP   A 1 72  ? -9.840  -2.586  2.347   1.00 52.83  ? 68  ASP   A N   1 
ATOM   514  C CA  . ASP   A 1 72  ? -10.675 -2.399  1.167   1.00 52.77  ? 68  ASP   A CA  1 
ATOM   515  C C   . ASP   A 1 72  ? -11.729 -3.491  1.045   1.00 58.10  ? 68  ASP   A C   1 
ATOM   516  O O   . ASP   A 1 72  ? -12.787 -3.265  0.449   1.00 62.30  ? 68  ASP   A O   1 
ATOM   517  C CB  . ASP   A 1 72  ? -9.805  -2.358  -0.089  1.00 60.14  ? 68  ASP   A CB  1 
ATOM   518  C CG  . ASP   A 1 72  ? -8.952  -1.106  -0.168  1.00 69.01  ? 68  ASP   A CG  1 
ATOM   519  O OD1 . ASP   A 1 72  ? -9.174  -0.182  0.642   1.00 76.55  ? 68  ASP   A OD1 1 
ATOM   520  O OD2 . ASP   A 1 72  ? -8.057  -1.048  -1.037  1.00 80.01  ? 68  ASP   A OD2 1 
ATOM   521  N N   . GLN   A 1 73  ? -11.461 -4.677  1.597   1.00 60.87  ? 69  GLN   A N   1 
ATOM   522  C CA  . GLN   A 1 73  ? -12.420 -5.776  1.594   1.00 54.10  ? 69  GLN   A CA  1 
ATOM   523  C C   . GLN   A 1 73  ? -13.288 -5.797  2.848   1.00 55.43  ? 69  GLN   A C   1 
ATOM   524  O O   . GLN   A 1 73  ? -13.781 -6.865  3.240   1.00 55.40  ? 69  GLN   A O   1 
ATOM   525  C CB  . GLN   A 1 73  ? -11.694 -7.110  1.418   1.00 53.90  ? 69  GLN   A CB  1 
ATOM   526  C CG  . GLN   A 1 73  ? -11.219 -7.372  -0.006  1.00 53.18  ? 69  GLN   A CG  1 
ATOM   527  C CD  . GLN   A 1 73  ? -12.308 -7.144  -1.040  1.00 70.98  ? 69  GLN   A CD  1 
ATOM   528  O OE1 . GLN   A 1 73  ? -13.378 -7.751  -0.977  1.00 75.49  ? 69  GLN   A OE1 1 
ATOM   529  N NE2 . GLN   A 1 73  ? -12.038 -6.268  -2.002  1.00 56.66  ? 69  GLN   A NE2 1 
ATOM   530  N N   . ASN   A 1 74  ? -13.470 -4.642  3.494   1.00 52.33  ? 70  ASN   A N   1 
ATOM   531  C CA  . ASN   A 1 74  ? -14.414 -4.470  4.600   1.00 60.77  ? 70  ASN   A CA  1 
ATOM   532  C C   . ASN   A 1 74  ? -14.028 -5.302  5.823   1.00 59.40  ? 70  ASN   A C   1 
ATOM   533  O O   . ASN   A 1 74  ? -14.884 -5.899  6.477   1.00 66.79  ? 70  ASN   A O   1 
ATOM   534  C CB  . ASN   A 1 74  ? -15.846 -4.787  4.162   1.00 62.63  ? 70  ASN   A CB  1 
ATOM   535  C CG  . ASN   A 1 74  ? -16.223 -4.099  2.866   1.00 69.00  ? 70  ASN   A CG  1 
ATOM   536  O OD1 . ASN   A 1 74  ? -16.041 -2.891  2.716   1.00 64.87  ? 70  ASN   A OD1 1 
ATOM   537  N ND2 . ASN   A 1 74  ? -16.749 -4.868  1.919   1.00 67.72  ? 70  ASN   A ND2 1 
ATOM   538  N N   . ASP   A 1 75  ? -12.737 -5.337  6.143   1.00 56.02  ? 71  ASP   A N   1 
ATOM   539  C CA  . ASP   A 1 75  ? -12.270 -5.942  7.383   1.00 56.63  ? 71  ASP   A CA  1 
ATOM   540  C C   . ASP   A 1 75  ? -12.312 -4.885  8.480   1.00 57.27  ? 71  ASP   A C   1 
ATOM   541  O O   . ASP   A 1 75  ? -11.664 -3.839  8.364   1.00 57.96  ? 71  ASP   A O   1 
ATOM   542  C CB  . ASP   A 1 75  ? -10.860 -6.509  7.225   1.00 65.50  ? 71  ASP   A CB  1 
ATOM   543  C CG  . ASP   A 1 75  ? -10.401 -7.282  8.449   1.00 62.80  ? 71  ASP   A CG  1 
ATOM   544  O OD1 . ASP   A 1 75  ? -9.984  -6.644  9.438   1.00 63.90  ? 71  ASP   A OD1 1 
ATOM   545  O OD2 . ASP   A 1 75  ? -10.460 -8.530  8.423   1.00 60.56  ? 71  ASP   A OD2 1 
ATOM   546  N N   . SER   A 1 76  ? -13.081 -5.158  9.538   1.00 62.41  ? 72  SER   A N   1 
ATOM   547  C CA  . SER   A 1 76  ? -13.269 -4.171  10.598  1.00 54.21  ? 72  SER   A CA  1 
ATOM   548  C C   . SER   A 1 76  ? -11.953 -3.828  11.281  1.00 52.22  ? 72  SER   A C   1 
ATOM   549  O O   . SER   A 1 76  ? -11.695 -2.661  11.600  1.00 54.59  ? 72  SER   A O   1 
ATOM   550  C CB  . SER   A 1 76  ? -14.280 -4.686  11.622  1.00 49.43  ? 72  SER   A CB  1 
ATOM   551  O OG  . SER   A 1 76  ? -15.467 -5.131  10.990  1.00 55.31  ? 72  SER   A OG  1 
ATOM   552  N N   . GLN   A 1 77  ? -11.109 -4.833  11.518  1.00 56.61  ? 73  GLN   A N   1 
ATOM   553  C CA  . GLN   A 1 77  ? -9.836  -4.584  12.184  1.00 54.10  ? 73  GLN   A CA  1 
ATOM   554  C C   . GLN   A 1 77  ? -8.927  -3.715  11.326  1.00 54.73  ? 73  GLN   A C   1 
ATOM   555  O O   . GLN   A 1 77  ? -8.251  -2.818  11.842  1.00 54.51  ? 73  GLN   A O   1 
ATOM   556  C CB  . GLN   A 1 77  ? -9.158  -5.911  12.521  1.00 56.05  ? 73  GLN   A CB  1 
ATOM   557  C CG  . GLN   A 1 77  ? -9.984  -6.802  13.434  1.00 53.70  ? 73  GLN   A CG  1 
ATOM   558  C CD  . GLN   A 1 77  ? -10.337 -6.117  14.737  1.00 61.18  ? 73  GLN   A CD  1 
ATOM   559  O OE1 . GLN   A 1 77  ? -11.509 -5.940  15.065  1.00 57.78  ? 73  GLN   A OE1 1 
ATOM   560  N NE2 . GLN   A 1 77  ? -9.320  -5.722  15.488  1.00 59.98  ? 73  GLN   A NE2 1 
ATOM   561  N N   . SER   A 1 78  ? -8.915  -3.947  10.012  1.00 55.65  ? 74  SER   A N   1 
ATOM   562  C CA  . SER   A 1 78  ? -7.966  -3.248  9.153   1.00 55.82  ? 74  SER   A CA  1 
ATOM   563  C C   . SER   A 1 78  ? -8.412  -1.828  8.816   1.00 44.85  ? 74  SER   A C   1 
ATOM   564  O O   . SER   A 1 78  ? -7.570  -0.927  8.747   1.00 41.45  ? 74  SER   A O   1 
ATOM   565  C CB  . SER   A 1 78  ? -7.699  -4.064  7.885   1.00 52.39  ? 74  SER   A CB  1 
ATOM   566  O OG  . SER   A 1 78  ? -6.999  -5.250  8.204   1.00 58.53  ? 74  SER   A OG  1 
ATOM   567  N N   . LEU   A 1 79  ? -9.709  -1.586  8.591   1.00 45.57  ? 75  LEU   A N   1 
ATOM   568  C CA  . LEU   A 1 79  ? -10.145 -0.194  8.453   1.00 57.95  ? 75  LEU   A CA  1 
ATOM   569  C C   . LEU   A 1 79  ? -9.889  0.611   9.713   1.00 54.12  ? 75  LEU   A C   1 
ATOM   570  O O   . LEU   A 1 79  ? -9.603  1.811   9.636   1.00 52.83  ? 75  LEU   A O   1 
ATOM   571  C CB  . LEU   A 1 79  ? -11.620 -0.070  8.052   1.00 55.79  ? 75  LEU   A CB  1 
ATOM   572  C CG  . LEU   A 1 79  ? -12.024 -0.354  6.619   1.00 60.04  ? 75  LEU   A CG  1 
ATOM   573  C CD1 . LEU   A 1 79  ? -13.529 -0.272  6.467   1.00 59.19  ? 75  LEU   A CD1 1 
ATOM   574  C CD2 . LEU   A 1 79  ? -11.346 0.696   5.750   1.00 65.22  ? 75  LEU   A CD2 1 
ATOM   575  N N   . GLU   A 1 80  ? -9.993  -0.016  10.880  1.00 51.71  ? 76  GLU   A N   1 
ATOM   576  C CA  . GLU   A 1 80  ? -9.656  0.719   12.089  1.00 56.27  ? 76  GLU   A CA  1 
ATOM   577  C C   . GLU   A 1 80  ? -8.187  1.118   12.085  1.00 62.57  ? 76  GLU   A C   1 
ATOM   578  O O   . GLU   A 1 80  ? -7.848  2.256   12.426  1.00 61.11  ? 76  GLU   A O   1 
ATOM   579  C CB  . GLU   A 1 80  ? -10.003 -0.097  13.335  1.00 55.47  ? 76  GLU   A CB  1 
ATOM   580  C CG  . GLU   A 1 80  ? -10.144 0.755   14.594  1.00 76.73  ? 76  GLU   A CG  1 
ATOM   581  C CD  . GLU   A 1 80  ? -11.164 1.879   14.441  1.00 92.46  ? 76  GLU   A CD  1 
ATOM   582  O OE1 . GLU   A 1 80  ? -12.136 1.724   13.670  1.00 87.41  ? 76  GLU   A OE1 1 
ATOM   583  O OE2 . GLU   A 1 80  ? -10.988 2.929   15.094  1.00 94.41  ? 76  GLU   A OE2 1 
ATOM   584  N N   . LEU   A 1 81  ? -7.306  0.213   11.652  1.00 56.48  ? 77  LEU   A N   1 
ATOM   585  C CA  . LEU   A 1 81  ? -5.880  0.525   11.609  1.00 58.28  ? 77  LEU   A CA  1 
ATOM   586  C C   . LEU   A 1 81  ? -5.581  1.633   10.604  1.00 51.11  ? 77  LEU   A C   1 
ATOM   587  O O   . LEU   A 1 81  ? -4.796  2.545   10.890  1.00 44.48  ? 77  LEU   A O   1 
ATOM   588  C CB  . LEU   A 1 81  ? -5.081  -0.732  11.266  1.00 55.37  ? 77  LEU   A CB  1 
ATOM   589  C CG  . LEU   A 1 81  ? -5.207  -1.906  12.237  1.00 62.03  ? 77  LEU   A CG  1 
ATOM   590  C CD1 . LEU   A 1 81  ? -4.182  -2.984  11.913  1.00 49.07  ? 77  LEU   A CD1 1 
ATOM   591  C CD2 . LEU   A 1 81  ? -5.073  -1.439  13.674  1.00 71.44  ? 77  LEU   A CD2 1 
ATOM   592  N N   . VAL   A 1 82  ? -6.195  1.569   9.420   1.00 52.86  ? 78  VAL   A N   1 
ATOM   593  C CA  . VAL   A 1 82  ? -5.939  2.576   8.394   1.00 51.37  ? 78  VAL   A CA  1 
ATOM   594  C C   . VAL   A 1 82  ? -6.456  3.938   8.840   1.00 51.04  ? 78  VAL   A C   1 
ATOM   595  O O   . VAL   A 1 82  ? -5.831  4.973   8.572   1.00 37.68  ? 78  VAL   A O   1 
ATOM   596  C CB  . VAL   A 1 82  ? -6.561  2.138   7.055   1.00 55.91  ? 78  VAL   A CB  1 
ATOM   597  C CG1 . VAL   A 1 82  ? -6.567  3.288   6.054   1.00 50.07  ? 78  VAL   A CG1 1 
ATOM   598  C CG2 . VAL   A 1 82  ? -5.816  0.938   6.494   1.00 51.62  ? 78  VAL   A CG2 1 
ATOM   599  N N   . HIS   A 1 83  ? -7.596  3.960   9.535   1.00 52.45  ? 79  HIS   A N   1 
ATOM   600  C CA  . HIS   A 1 83  ? -8.150  5.218   10.027  1.00 57.29  ? 79  HIS   A CA  1 
ATOM   601  C C   . HIS   A 1 83  ? -7.174  5.927   10.957  1.00 63.34  ? 79  HIS   A C   1 
ATOM   602  O O   . HIS   A 1 83  ? -6.904  7.124   10.800  1.00 70.67  ? 79  HIS   A O   1 
ATOM   603  C CB  . HIS   A 1 83  ? -9.469  4.962   10.752  1.00 60.73  ? 79  HIS   A CB  1 
ATOM   604  C CG  . HIS   A 1 83  ? -9.892  6.091   11.638  1.00 72.06  ? 79  HIS   A CG  1 
ATOM   605  N ND1 . HIS   A 1 83  ? -9.706  6.074   13.004  1.00 83.40  ? 79  HIS   A ND1 1 
ATOM   606  C CD2 . HIS   A 1 83  ? -10.500 7.268   11.357  1.00 70.49  ? 79  HIS   A CD2 1 
ATOM   607  C CE1 . HIS   A 1 83  ? -10.174 7.194   13.525  1.00 83.56  ? 79  HIS   A CE1 1 
ATOM   608  N NE2 . HIS   A 1 83  ? -10.663 7.935   12.547  1.00 81.72  ? 79  HIS   A NE2 1 
ATOM   609  N N   . ARG   A 1 84  ? -6.637  5.201   11.939  1.00 61.42  ? 80  ARG   A N   1 
ATOM   610  C CA  . ARG   A 1 84  ? -5.810  5.831   12.962  1.00 65.31  ? 80  ARG   A CA  1 
ATOM   611  C C   . ARG   A 1 84  ? -4.497  6.352   12.392  1.00 52.43  ? 80  ARG   A C   1 
ATOM   612  O O   . ARG   A 1 84  ? -3.983  7.372   12.865  1.00 56.55  ? 80  ARG   A O   1 
ATOM   613  C CB  . ARG   A 1 84  ? -5.567  4.845   14.105  1.00 57.55  ? 80  ARG   A CB  1 
ATOM   614  C CG  . ARG   A 1 84  ? -6.856  4.181   14.565  1.00 75.42  ? 80  ARG   A CG  1 
ATOM   615  C CD  . ARG   A 1 84  ? -6.730  3.441   15.883  1.00 88.41  ? 80  ARG   A CD  1 
ATOM   616  N NE  . ARG   A 1 84  ? -5.515  2.643   15.977  1.00 88.67  ? 80  ARG   A NE  1 
ATOM   617  C CZ  . ARG   A 1 84  ? -5.369  1.617   16.807  1.00 97.69  ? 80  ARG   A CZ  1 
ATOM   618  N NH1 . ARG   A 1 84  ? -4.231  0.948   16.836  1.00 100.70 ? 80  ARG   A NH1 1 
ATOM   619  N NH2 . ARG   A 1 84  ? -6.367  1.254   17.601  1.00 93.48  ? 80  ARG   A NH2 1 
ATOM   620  N N   . PHE   A 1 85  ? -3.947  5.686   11.375  1.00 52.40  ? 81  PHE   A N   1 
ATOM   621  C CA  . PHE   A 1 85  ? -2.739  6.203   10.741  1.00 58.00  ? 81  PHE   A CA  1 
ATOM   622  C C   . PHE   A 1 85  ? -3.047  7.431   9.893   1.00 57.07  ? 81  PHE   A C   1 
ATOM   623  O O   . PHE   A 1 85  ? -2.262  8.386   9.867   1.00 54.54  ? 81  PHE   A O   1 
ATOM   624  C CB  . PHE   A 1 85  ? -2.075  5.120   9.892   1.00 56.12  ? 81  PHE   A CB  1 
ATOM   625  C CG  . PHE   A 1 85  ? -0.723  5.510   9.366   1.00 67.24  ? 81  PHE   A CG  1 
ATOM   626  C CD1 . PHE   A 1 85  ? 0.167   6.211   10.163  1.00 78.00  ? 81  PHE   A CD1 1 
ATOM   627  C CD2 . PHE   A 1 85  ? -0.340  5.179   8.077   1.00 62.87  ? 81  PHE   A CD2 1 
ATOM   628  C CE1 . PHE   A 1 85  ? 1.412   6.574   9.685   1.00 80.04  ? 81  PHE   A CE1 1 
ATOM   629  C CE2 . PHE   A 1 85  ? 0.906   5.539   7.596   1.00 63.32  ? 81  PHE   A CE2 1 
ATOM   630  C CZ  . PHE   A 1 85  ? 1.781   6.237   8.400   1.00 72.40  ? 81  PHE   A CZ  1 
ATOM   631  N N   . GLN   A 1 86  ? -4.188  7.429   9.199   1.00 61.21  ? 82  GLN   A N   1 
ATOM   632  C CA  . GLN   A 1 86  ? -4.534  8.562   8.347   1.00 61.65  ? 82  GLN   A CA  1 
ATOM   633  C C   . GLN   A 1 86  ? -4.875  9.796   9.173   1.00 57.06  ? 82  GLN   A C   1 
ATOM   634  O O   . GLN   A 1 86  ? -4.483  10.914  8.818   1.00 64.15  ? 82  GLN   A O   1 
ATOM   635  C CB  . GLN   A 1 86  ? -5.697  8.192   7.426   1.00 63.25  ? 82  GLN   A CB  1 
ATOM   636  C CG  . GLN   A 1 86  ? -5.924  9.172   6.281   1.00 71.54  ? 82  GLN   A CG  1 
ATOM   637  C CD  . GLN   A 1 86  ? -4.628  9.683   5.677   1.00 71.53  ? 82  GLN   A CD  1 
ATOM   638  O OE1 . GLN   A 1 86  ? -3.946  8.967   4.945   1.00 72.78  ? 82  GLN   A OE1 1 
ATOM   639  N NE2 . GLN   A 1 86  ? -4.287  10.932  5.978   1.00 66.68  ? 82  GLN   A NE2 1 
ATOM   640  N N   . GLU   A 1 87  ? -5.604  9.619   10.275  1.00 48.12  ? 83  GLU   A N   1 
ATOM   641  C CA  . GLU   A 1 87  ? -5.938  10.755  11.125  1.00 57.59  ? 83  GLU   A CA  1 
ATOM   642  C C   . GLU   A 1 87  ? -4.759  11.216  11.969  1.00 58.85  ? 83  GLU   A C   1 
ATOM   643  O O   . GLU   A 1 87  ? -4.767  12.354  12.451  1.00 58.59  ? 83  GLU   A O   1 
ATOM   644  C CB  . GLU   A 1 87  ? -7.127  10.415  12.028  1.00 58.99  ? 83  GLU   A CB  1 
ATOM   645  C CG  . GLU   A 1 87  ? -8.383  9.970   11.279  1.00 77.93  ? 83  GLU   A CG  1 
ATOM   646  C CD  . GLU   A 1 87  ? -8.935  11.016  10.317  1.00 82.98  ? 83  GLU   A CD  1 
ATOM   647  O OE1 . GLU   A 1 87  ? -8.524  12.195  10.385  1.00 83.57  ? 83  GLU   A OE1 1 
ATOM   648  O OE2 . GLU   A 1 87  ? -9.792  10.652  9.484   1.00 77.65  ? 83  GLU   A OE2 1 
ATOM   649  N N   . TYR   A 1 88  ? -3.750  10.364  12.163  1.00 47.91  ? 84  TYR   A N   1 
ATOM   650  C CA  . TYR   A 1 88  ? -2.508  10.831  12.769  1.00 57.25  ? 84  TYR   A CA  1 
ATOM   651  C C   . TYR   A 1 88  ? -1.702  11.661  11.779  1.00 54.91  ? 84  TYR   A C   1 
ATOM   652  O O   . TYR   A 1 88  ? -1.033  12.626  12.167  1.00 49.89  ? 84  TYR   A O   1 
ATOM   653  C CB  . TYR   A 1 88  ? -1.682  9.648   13.273  1.00 50.96  ? 84  TYR   A CB  1 
ATOM   654  C CG  . TYR   A 1 88  ? -0.434  10.057  14.026  1.00 41.50  ? 84  TYR   A CG  1 
ATOM   655  C CD1 . TYR   A 1 88  ? -0.473  10.296  15.392  1.00 59.00  ? 84  TYR   A CD1 1 
ATOM   656  C CD2 . TYR   A 1 88  ? 0.781   10.210  13.370  1.00 46.82  ? 84  TYR   A CD2 1 
ATOM   657  C CE1 . TYR   A 1 88  ? 0.663   10.674  16.084  1.00 64.98  ? 84  TYR   A CE1 1 
ATOM   658  C CE2 . TYR   A 1 88  ? 1.922   10.588  14.055  1.00 47.25  ? 84  TYR   A CE2 1 
ATOM   659  C CZ  . TYR   A 1 88  ? 1.856   10.818  15.412  1.00 60.09  ? 84  TYR   A CZ  1 
ATOM   660  O OH  . TYR   A 1 88  ? 2.986   11.194  16.102  1.00 72.61  ? 84  TYR   A OH  1 
ATOM   661  N N   . ILE   A 1 89  ? -1.754  11.300  10.495  1.00 53.70  ? 85  ILE   A N   1 
ATOM   662  C CA  . ILE   A 1 89  ? -1.021  12.050  9.481   1.00 56.38  ? 85  ILE   A CA  1 
ATOM   663  C C   . ILE   A 1 89  ? -1.637  13.431  9.287   1.00 55.44  ? 85  ILE   A C   1 
ATOM   664  O O   . ILE   A 1 89  ? -0.920  14.428  9.136   1.00 59.61  ? 85  ILE   A O   1 
ATOM   665  C CB  . ILE   A 1 89  ? -0.968  11.254  8.163   1.00 48.62  ? 85  ILE   A CB  1 
ATOM   666  C CG1 . ILE   A 1 89  ? -0.055  10.036  8.314   1.00 59.20  ? 85  ILE   A CG1 1 
ATOM   667  C CG2 . ILE   A 1 89  ? -0.486  12.130  7.018   1.00 64.17  ? 85  ILE   A CG2 1 
ATOM   668  C CD1 . ILE   A 1 89  ? -0.030  9.138   7.096   1.00 61.80  ? 85  ILE   A CD1 1 
ATOM   669  N N   . ASP   A 1 90  ? -2.971  13.518  9.295   1.00 53.39  ? 86  ASP   A N   1 
ATOM   670  C CA  . ASP   A 1 90  ? -3.622  14.818  9.153   1.00 62.26  ? 86  ASP   A CA  1 
ATOM   671  C C   . ASP   A 1 90  ? -3.312  15.725  10.337  1.00 56.85  ? 86  ASP   A C   1 
ATOM   672  O O   . ASP   A 1 90  ? -3.164  16.942  10.176  1.00 62.23  ? 86  ASP   A O   1 
ATOM   673  C CB  . ASP   A 1 90  ? -5.133  14.646  8.996   1.00 66.10  ? 86  ASP   A CB  1 
ATOM   674  C CG  . ASP   A 1 90  ? -5.510  13.936  7.711   1.00 78.42  ? 86  ASP   A CG  1 
ATOM   675  O OD1 . ASP   A 1 90  ? -4.607  13.385  7.046   1.00 84.24  ? 86  ASP   A OD1 1 
ATOM   676  O OD2 . ASP   A 1 90  ? -6.708  13.941  7.360   1.00 83.83  ? 86  ASP   A OD2 1 
ATOM   677  N N   . ALA   A 1 91  ? -3.213  15.153  11.537  1.00 54.40  ? 87  ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 91  ? -2.862  15.932  12.716  1.00 56.94  ? 87  ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 91  ? -1.370  16.218  12.813  1.00 56.74  ? 87  ALA   A C   1 
ATOM   680  O O   . ALA   A 1 91  ? -0.962  16.992  13.684  1.00 52.35  ? 87  ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 91  ? -3.331  15.213  13.983  1.00 59.30  ? 87  ALA   A CB  1 
ATOM   682  N N   . HIS   A 1 92  ? -0.553  15.618  11.949  1.00 48.60  ? 88  HIS   A N   1 
ATOM   683  C CA  . HIS   A 1 92  ? 0.898   15.815  11.965  1.00 51.04  ? 88  HIS   A CA  1 
ATOM   684  C C   . HIS   A 1 92  ? 1.418   15.864  10.537  1.00 50.86  ? 88  HIS   A C   1 
ATOM   685  O O   . HIS   A 1 92  ? 1.949   14.876  10.015  1.00 62.09  ? 88  HIS   A O   1 
ATOM   686  C CB  . HIS   A 1 92  ? 1.596   14.708  12.760  1.00 44.75  ? 88  HIS   A CB  1 
ATOM   687  C CG  . HIS   A 1 92  ? 1.176   14.634  14.194  1.00 50.58  ? 88  HIS   A CG  1 
ATOM   688  N ND1 . HIS   A 1 92  ? 0.007   14.024  14.598  1.00 56.59  ? 88  HIS   A ND1 1 
ATOM   689  C CD2 . HIS   A 1 92  ? 1.769   15.093  15.322  1.00 61.23  ? 88  HIS   A CD2 1 
ATOM   690  C CE1 . HIS   A 1 92  ? -0.102  14.111  15.911  1.00 64.74  ? 88  HIS   A CE1 1 
ATOM   691  N NE2 . HIS   A 1 92  ? 0.954   14.755  16.375  1.00 56.59  ? 88  HIS   A NE2 1 
ATOM   692  N N   . PRO   A 1 93  ? 1.284   17.012  9.865   1.00 53.43  ? 89  PRO   A N   1 
ATOM   693  C CA  . PRO   A 1 93  ? 1.880   17.154  8.529   1.00 58.39  ? 89  PRO   A CA  1 
ATOM   694  C C   . PRO   A 1 93  ? 3.385   17.357  8.555   1.00 56.20  ? 89  PRO   A C   1 
ATOM   695  O O   . PRO   A 1 93  ? 4.009   17.372  7.485   1.00 54.65  ? 89  PRO   A O   1 
ATOM   696  C CB  . PRO   A 1 93  ? 1.166   18.384  7.950   1.00 55.88  ? 89  PRO   A CB  1 
ATOM   697  C CG  . PRO   A 1 93  ? 0.654   19.144  9.125   1.00 71.43  ? 89  PRO   A CG  1 
ATOM   698  C CD  . PRO   A 1 93  ? 0.629   18.247  10.330  1.00 63.48  ? 89  PRO   A CD  1 
ATOM   699  N N   . GLU   A 1 94  ? 3.984   17.517  9.737   1.00 61.12  ? 90  GLU   A N   1 
ATOM   700  C CA  . GLU   A 1 94  ? 5.434   17.619  9.840   1.00 64.86  ? 90  GLU   A CA  1 
ATOM   701  C C   . GLU   A 1 94  ? 6.102   16.252  9.789   1.00 56.45  ? 90  GLU   A C   1 
ATOM   702  O O   . GLU   A 1 94  ? 7.243   16.140  9.325   1.00 61.30  ? 90  GLU   A O   1 
ATOM   703  C CB  . GLU   A 1 94  ? 5.817   18.346  11.132  1.00 71.06  ? 90  GLU   A CB  1 
ATOM   704  C CG  . GLU   A 1 94  ? 7.298   18.663  11.260  1.00 85.68  ? 90  GLU   A CG  1 
ATOM   705  C CD  . GLU   A 1 94  ? 7.651   20.032  10.714  1.00 89.32  ? 90  GLU   A CD  1 
ATOM   706  O OE1 . GLU   A 1 94  ? 8.826   20.439  10.839  1.00 89.71  ? 90  GLU   A OE1 1 
ATOM   707  O OE2 . GLU   A 1 94  ? 6.755   20.701  10.158  1.00 93.78  ? 90  GLU   A OE2 1 
ATOM   708  N N   . THR   A 1 95  ? 5.414   15.210  10.251  1.00 66.48  ? 91  THR   A N   1 
ATOM   709  C CA  . THR   A 1 95  ? 5.966   13.864  10.209  1.00 58.57  ? 91  THR   A CA  1 
ATOM   710  C C   . THR   A 1 95  ? 6.100   13.393  8.766   1.00 50.14  ? 91  THR   A C   1 
ATOM   711  O O   . THR   A 1 95  ? 5.138   13.441  7.993   1.00 49.72  ? 91  THR   A O   1 
ATOM   712  C CB  . THR   A 1 95  ? 5.079   12.901  10.998  1.00 50.33  ? 91  THR   A CB  1 
ATOM   713  O OG1 . THR   A 1 95  ? 4.906   13.391  12.334  1.00 45.91  ? 91  THR   A OG1 1 
ATOM   714  C CG2 . THR   A 1 95  ? 5.706   11.515  11.045  1.00 48.64  ? 91  THR   A CG2 1 
ATOM   715  N N   . ILE   A 1 96  ? 7.297   12.943  8.404   1.00 44.08  ? 92  ILE   A N   1 
ATOM   716  C CA  . ILE   A 1 96  ? 7.556   12.449  7.056   1.00 52.93  ? 92  ILE   A CA  1 
ATOM   717  C C   . ILE   A 1 96  ? 7.059   11.014  6.950   1.00 49.78  ? 92  ILE   A C   1 
ATOM   718  O O   . ILE   A 1 96  ? 7.336   10.181  7.822   1.00 51.24  ? 92  ILE   A O   1 
ATOM   719  C CB  . ILE   A 1 96  ? 9.052   12.547  6.718   1.00 57.95  ? 92  ILE   A CB  1 
ATOM   720  C CG1 . ILE   A 1 96  ? 9.557   13.973  6.944   1.00 50.21  ? 92  ILE   A CG1 1 
ATOM   721  C CG2 . ILE   A 1 96  ? 9.305   12.106  5.283   1.00 47.25  ? 92  ILE   A CG2 1 
ATOM   722  C CD1 . ILE   A 1 96  ? 8.945   14.993  6.008   1.00 57.73  ? 92  ILE   A CD1 1 
ATOM   723  N N   . VAL   A 1 97  ? 6.323   10.721  5.882   1.00 37.95  ? 93  VAL   A N   1 
ATOM   724  C CA  . VAL   A 1 97  ? 5.740   9.404   5.656   1.00 48.29  ? 93  VAL   A CA  1 
ATOM   725  C C   . VAL   A 1 97  ? 6.436   8.773   4.459   1.00 41.54  ? 93  VAL   A C   1 
ATOM   726  O O   . VAL   A 1 97  ? 6.414   9.327   3.353   1.00 49.89  ? 93  VAL   A O   1 
ATOM   727  C CB  . VAL   A 1 97  ? 4.223   9.486   5.430   1.00 53.89  ? 93  VAL   A CB  1 
ATOM   728  C CG1 . VAL   A 1 97  ? 3.636   8.091   5.262   1.00 49.96  ? 93  VAL   A CG1 1 
ATOM   729  C CG2 . VAL   A 1 97  ? 3.554   10.218  6.584   1.00 47.54  ? 93  VAL   A CG2 1 
ATOM   730  N N   . LEU   A 1 98  ? 7.056   7.617   4.681   1.00 42.14  ? 94  LEU   A N   1 
ATOM   731  C CA  . LEU   A 1 98  ? 7.699   6.835   3.627   1.00 52.43  ? 94  LEU   A CA  1 
ATOM   732  C C   . LEU   A 1 98  ? 7.052   5.454   3.626   1.00 36.65  ? 94  LEU   A C   1 
ATOM   733  O O   . LEU   A 1 98  ? 7.428   4.589   4.422   1.00 41.15  ? 94  LEU   A O   1 
ATOM   734  C CB  . LEU   A 1 98  ? 9.208   6.742   3.845   1.00 46.84  ? 94  LEU   A CB  1 
ATOM   735  C CG  . LEU   A 1 98  ? 9.968   8.041   4.118   1.00 54.93  ? 94  LEU   A CG  1 
ATOM   736  C CD1 . LEU   A 1 98  ? 11.347  7.741   4.689   1.00 45.20  ? 94  LEU   A CD1 1 
ATOM   737  C CD2 . LEU   A 1 98  ? 10.079  8.877   2.853   1.00 48.12  ? 94  LEU   A CD2 1 
ATOM   738  N N   . ASP   A 1 99  ? 6.086   5.240   2.737   1.00 46.51  ? 95  ASP   A N   1 
ATOM   739  C CA  . ASP   A 1 99  ? 5.671   6.236   1.755   1.00 51.83  ? 95  ASP   A CA  1 
ATOM   740  C C   . ASP   A 1 99  ? 4.187   6.568   1.939   1.00 48.32  ? 95  ASP   A C   1 
ATOM   741  O O   . ASP   A 1 99  ? 3.493   5.874   2.682   1.00 42.06  ? 95  ASP   A O   1 
ATOM   742  C CB  . ASP   A 1 99  ? 5.950   5.719   0.340   1.00 52.80  ? 95  ASP   A CB  1 
ATOM   743  C CG  . ASP   A 1 99  ? 7.425   5.752   -0.011  1.00 55.12  ? 95  ASP   A CG  1 
ATOM   744  O OD1 . ASP   A 1 99  ? 8.066   6.803   0.207   1.00 59.65  ? 95  ASP   A OD1 1 
ATOM   745  O OD2 . ASP   A 1 99  ? 7.946   4.727   -0.499  1.00 53.01  ? 95  ASP   A OD2 1 
ATOM   746  N N   . PRO   A 1 100 ? 3.709   7.637   1.292   1.00 49.27  ? 96  PRO   A N   1 
ATOM   747  C CA  . PRO   A 1 100 ? 2.277   7.957   1.359   1.00 47.01  ? 96  PRO   A CA  1 
ATOM   748  C C   . PRO   A 1 100 ? 1.403   6.775   0.957   1.00 58.80  ? 96  PRO   A C   1 
ATOM   749  O O   . PRO   A 1 100 ? 1.813   5.898   0.194   1.00 62.65  ? 96  PRO   A O   1 
ATOM   750  C CB  . PRO   A 1 100 ? 2.134   9.123   0.377   1.00 57.15  ? 96  PRO   A CB  1 
ATOM   751  C CG  . PRO   A 1 100 ? 3.448   9.812   0.452   1.00 61.63  ? 96  PRO   A CG  1 
ATOM   752  C CD  . PRO   A 1 100 ? 4.482   8.736   0.683   1.00 53.38  ? 96  PRO   A CD  1 
ATOM   753  N N   . LEU   A 1 101 ? 0.178   6.770   1.481   1.00 57.88  ? 97  LEU   A N   1 
ATOM   754  C CA  . LEU   A 1 101 ? -0.746  5.648   1.342   1.00 63.83  ? 97  LEU   A CA  1 
ATOM   755  C C   . LEU   A 1 101 ? -1.387  5.564   -0.043  1.00 58.15  ? 97  LEU   A C   1 
ATOM   756  O O   . LEU   A 1 101 ? -1.543  4.452   -0.563  1.00 58.34  ? 97  LEU   A O   1 
ATOM   757  C CB  . LEU   A 1 101 ? -1.834  5.713   2.419   1.00 57.37  ? 97  LEU   A CB  1 
ATOM   758  C CG  . LEU   A 1 101 ? -1.505  5.067   3.767   1.00 62.76  ? 97  LEU   A CG  1 
ATOM   759  C CD1 . LEU   A 1 101 ? -1.201  3.588   3.591   1.00 66.49  ? 97  LEU   A CD1 1 
ATOM   760  C CD2 . LEU   A 1 101 ? -0.350  5.774   4.449   1.00 65.99  ? 97  LEU   A CD2 1 
ATOM   761  N N   . PRO   A 1 102 ? -1.800  6.679   -0.666  1.00 66.50  ? 98  PRO   A N   1 
ATOM   762  C CA  . PRO   A 1 102 ? -2.281  6.581   -2.056  1.00 58.38  ? 98  PRO   A CA  1 
ATOM   763  C C   . PRO   A 1 102 ? -1.297  5.902   -2.992  1.00 54.66  ? 98  PRO   A C   1 
ATOM   764  O O   . PRO   A 1 102 ? -1.719  5.248   -3.955  1.00 57.90  ? 98  PRO   A O   1 
ATOM   765  C CB  . PRO   A 1 102 ? -2.514  8.046   -2.442  1.00 62.41  ? 98  PRO   A CB  1 
ATOM   766  C CG  . PRO   A 1 102 ? -2.886  8.695   -1.170  1.00 54.31  ? 98  PRO   A CG  1 
ATOM   767  C CD  . PRO   A 1 102 ? -2.061  8.020   -0.106  1.00 58.05  ? 98  PRO   A CD  1 
ATOM   768  N N   . ALA   A 1 103 ? 0.007   6.033   -2.737  1.00 56.26  ? 99  ALA   A N   1 
ATOM   769  C CA  . ALA   A 1 103 ? 0.990   5.302   -3.528  1.00 53.04  ? 99  ALA   A CA  1 
ATOM   770  C C   . ALA   A 1 103 ? 0.956   3.810   -3.222  1.00 51.76  ? 99  ALA   A C   1 
ATOM   771  O O   . ALA   A 1 103 ? 1.208   2.991   -4.112  1.00 53.25  ? 99  ALA   A O   1 
ATOM   772  C CB  . ALA   A 1 103 ? 2.389   5.864   -3.281  1.00 57.59  ? 99  ALA   A CB  1 
ATOM   773  N N   . ILE   A 1 104 ? 0.650   3.440   -1.975  1.00 61.70  ? 100 ILE   A N   1 
ATOM   774  C CA  . ILE   A 1 104 ? 0.529   2.027   -1.621  1.00 60.68  ? 100 ILE   A CA  1 
ATOM   775  C C   . ILE   A 1 104 ? -0.604  1.379   -2.406  1.00 47.25  ? 100 ILE   A C   1 
ATOM   776  O O   . ILE   A 1 104 ? -0.435  0.315   -3.014  1.00 47.88  ? 100 ILE   A O   1 
ATOM   777  C CB  . ILE   A 1 104 ? 0.321   1.868   -0.103  1.00 63.67  ? 100 ILE   A CB  1 
ATOM   778  C CG1 . ILE   A 1 104 ? 1.628   2.119   0.654   1.00 65.00  ? 100 ILE   A CG1 1 
ATOM   779  C CG2 . ILE   A 1 104 ? -0.242  0.491   0.222   1.00 64.86  ? 100 ILE   A CG2 1 
ATOM   780  C CD1 . ILE   A 1 104 ? 2.635   0.997   0.521   1.00 64.69  ? 100 ILE   A CD1 1 
ATOM   781  N N   . ARG   A 1 105 ? -1.778  2.018   -2.409  1.00 52.19  ? 101 ARG   A N   1 
ATOM   782  C CA  . ARG   A 1 105 ? -2.936  1.450   -3.092  1.00 49.30  ? 101 ARG   A CA  1 
ATOM   783  C C   . ARG   A 1 105 ? -2.691  1.296   -4.586  1.00 51.32  ? 101 ARG   A C   1 
ATOM   784  O O   . ARG   A 1 105 ? -3.172  0.335   -5.198  1.00 62.10  ? 101 ARG   A O   1 
ATOM   785  C CB  . ARG   A 1 105 ? -4.167  2.321   -2.847  1.00 52.79  ? 101 ARG   A CB  1 
ATOM   786  C CG  . ARG   A 1 105 ? -4.910  1.991   -1.567  1.00 71.45  ? 101 ARG   A CG  1 
ATOM   787  C CD  . ARG   A 1 105 ? -6.390  2.327   -1.673  1.00 66.59  ? 101 ARG   A CD  1 
ATOM   788  N NE  . ARG   A 1 105 ? -7.086  2.171   -0.398  1.00 74.54  ? 101 ARG   A NE  1 
ATOM   789  C CZ  . ARG   A 1 105 ? -6.946  2.986   0.644   1.00 71.86  ? 101 ARG   A CZ  1 
ATOM   790  N NH1 . ARG   A 1 105 ? -7.624  2.756   1.760   1.00 73.30  ? 101 ARG   A NH1 1 
ATOM   791  N NH2 . ARG   A 1 105 ? -6.138  4.035   0.571   1.00 54.42  ? 101 ARG   A NH2 1 
ATOM   792  N N   . THR   A 1 106 ? -1.946  2.223   -5.188  1.00 41.73  ? 102 THR   A N   1 
ATOM   793  C CA  . THR   A 1 106 ? -1.684  2.147   -6.621  1.00 59.71  ? 102 THR   A CA  1 
ATOM   794  C C   . THR   A 1 106 ? -0.787  0.961   -6.955  1.00 48.85  ? 102 THR   A C   1 
ATOM   795  O O   . THR   A 1 106 ? -1.053  0.216   -7.906  1.00 55.80  ? 102 THR   A O   1 
ATOM   796  C CB  . THR   A 1 106 ? -1.050  3.452   -7.109  1.00 48.48  ? 102 THR   A CB  1 
ATOM   797  O OG1 . THR   A 1 106 ? -1.975  4.533   -6.928  1.00 58.80  ? 102 THR   A OG1 1 
ATOM   798  C CG2 . THR   A 1 106 ? -0.680  3.350   -8.581  1.00 49.01  ? 102 THR   A CG2 1 
ATOM   799  N N   . LEU   A 1 107 ? 0.274   0.760   -6.173  1.00 39.23  ? 103 LEU   A N   1 
ATOM   800  C CA  . LEU   A 1 107 ? 1.284   -0.236  -6.503  1.00 47.65  ? 103 LEU   A CA  1 
ATOM   801  C C   . LEU   A 1 107 ? 0.887   -1.657  -6.123  1.00 47.69  ? 103 LEU   A C   1 
ATOM   802  O O   . LEU   A 1 107 ? 1.533   -2.603  -6.589  1.00 62.72  ? 103 LEU   A O   1 
ATOM   803  C CB  . LEU   A 1 107 ? 2.613   0.131   -5.837  1.00 42.85  ? 103 LEU   A CB  1 
ATOM   804  C CG  . LEU   A 1 107 ? 3.188   1.486   -6.261  1.00 42.29  ? 103 LEU   A CG  1 
ATOM   805  C CD1 . LEU   A 1 107 ? 4.637   1.631   -5.824  1.00 37.35  ? 103 LEU   A CD1 1 
ATOM   806  C CD2 . LEU   A 1 107 ? 3.059   1.679   -7.766  1.00 32.93  ? 103 LEU   A CD2 1 
ATOM   807  N N   . LEU   A 1 108 ? -0.147  -1.841  -5.301  1.00 45.99  ? 104 LEU   A N   1 
ATOM   808  C CA  . LEU   A 1 108 ? -0.616  -3.187  -4.998  1.00 54.24  ? 104 LEU   A CA  1 
ATOM   809  C C   . LEU   A 1 108 ? -1.561  -3.735  -6.059  1.00 45.66  ? 104 LEU   A C   1 
ATOM   810  O O   . LEU   A 1 108 ? -1.908  -4.919  -6.003  1.00 49.79  ? 104 LEU   A O   1 
ATOM   811  C CB  . LEU   A 1 108 ? -1.302  -3.222  -3.625  1.00 46.05  ? 104 LEU   A CB  1 
ATOM   812  C CG  . LEU   A 1 108 ? -2.574  -2.405  -3.376  1.00 60.76  ? 104 LEU   A CG  1 
ATOM   813  C CD1 . LEU   A 1 108 ? -3.836  -3.174  -3.753  1.00 52.94  ? 104 LEU   A CD1 1 
ATOM   814  C CD2 . LEU   A 1 108 ? -2.634  -1.979  -1.918  1.00 59.76  ? 104 LEU   A CD2 1 
ATOM   815  N N   . ASP   A 1 109 ? -1.986  -2.909  -7.013  1.00 47.94  ? 105 ASP   A N   1 
ATOM   816  C CA  . ASP   A 1 109 ? -2.909  -3.311  -8.069  1.00 47.90  ? 105 ASP   A CA  1 
ATOM   817  C C   . ASP   A 1 109 ? -2.163  -3.256  -9.396  1.00 48.15  ? 105 ASP   A C   1 
ATOM   818  O O   . ASP   A 1 109 ? -1.775  -2.174  -9.851  1.00 47.78  ? 105 ASP   A O   1 
ATOM   819  C CB  . ASP   A 1 109 ? -4.139  -2.406  -8.084  1.00 56.46  ? 105 ASP   A CB  1 
ATOM   820  C CG  . ASP   A 1 109 ? -5.322  -3.040  -8.788  1.00 74.41  ? 105 ASP   A CG  1 
ATOM   821  O OD1 . ASP   A 1 109 ? -6.095  -3.761  -8.122  1.00 82.54  ? 105 ASP   A OD1 1 
ATOM   822  O OD2 . ASP   A 1 109 ? -5.484  -2.810  -10.005 1.00 63.15  ? 105 ASP   A OD2 1 
ATOM   823  N N   . ARG   A 1 110 ? -1.963  -4.424  -10.015 1.00 42.54  ? 106 ARG   A N   1 
ATOM   824  C CA  . ARG   A 1 110 ? -1.193  -4.483  -11.255 1.00 44.32  ? 106 ARG   A CA  1 
ATOM   825  C C   . ARG   A 1 110 ? -1.865  -3.690  -12.368 1.00 39.33  ? 106 ARG   A C   1 
ATOM   826  O O   . ARG   A 1 110 ? -1.187  -3.047  -13.177 1.00 36.44  ? 106 ARG   A O   1 
ATOM   827  C CB  . ARG   A 1 110 ? -0.991  -5.935  -11.685 1.00 45.69  ? 106 ARG   A CB  1 
ATOM   828  C CG  . ARG   A 1 110 ? 0.171   -6.625  -11.000 1.00 48.88  ? 106 ARG   A CG  1 
ATOM   829  C CD  . ARG   A 1 110 ? 0.722   -7.756  -11.851 1.00 36.21  ? 106 ARG   A CD  1 
ATOM   830  N NE  . ARG   A 1 110 ? 1.072   -8.913  -11.034 1.00 39.07  ? 106 ARG   A NE  1 
ATOM   831  C CZ  . ARG   A 1 110 ? 2.268   -9.105  -10.487 1.00 41.85  ? 106 ARG   A CZ  1 
ATOM   832  N NH1 . ARG   A 1 110 ? 3.233   -8.215  -10.674 1.00 45.54  ? 106 ARG   A NH1 1 
ATOM   833  N NH2 . ARG   A 1 110 ? 2.499   -10.185 -9.754  1.00 51.26  ? 106 ARG   A NH2 1 
ATOM   834  N N   . SER   A 1 111 ? -3.198  -3.729  -12.429 1.00 38.71  ? 107 SER   A N   1 
ATOM   835  C CA  . SER   A 1 111 ? -3.915  -2.971  -13.450 1.00 46.72  ? 107 SER   A CA  1 
ATOM   836  C C   . SER   A 1 111 ? -3.669  -1.476  -13.295 1.00 48.87  ? 107 SER   A C   1 
ATOM   837  O O   . SER   A 1 111 ? -3.384  -0.776  -14.274 1.00 48.23  ? 107 SER   A O   1 
ATOM   838  C CB  . SER   A 1 111 ? -5.411  -3.283  -13.381 1.00 53.37  ? 107 SER   A CB  1 
ATOM   839  O OG  . SER   A 1 111 ? -6.175  -2.240  -13.962 1.00 75.63  ? 107 SER   A OG  1 
ATOM   840  N N   . LYS   A 1 112 ? -3.768  -0.969  -12.064 1.00 38.71  ? 108 LYS   A N   1 
ATOM   841  C CA  . LYS   A 1 112 ? -3.532  0.452   -11.830 1.00 41.56  ? 108 LYS   A CA  1 
ATOM   842  C C   . LYS   A 1 112 ? -2.072  0.816   -12.067 1.00 40.71  ? 108 LYS   A C   1 
ATOM   843  O O   . LYS   A 1 112 ? -1.775  1.877   -12.630 1.00 31.07  ? 108 LYS   A O   1 
ATOM   844  C CB  . LYS   A 1 112 ? -3.956  0.827   -10.409 1.00 45.81  ? 108 LYS   A CB  1 
ATOM   845  C CG  . LYS   A 1 112 ? -5.443  0.659   -10.138 1.00 60.83  ? 108 LYS   A CG  1 
ATOM   846  C CD  . LYS   A 1 112 ? -5.754  0.792   -8.654  1.00 64.84  ? 108 LYS   A CD  1 
ATOM   847  C CE  . LYS   A 1 112 ? -7.233  0.573   -8.375  1.00 65.13  ? 108 LYS   A CE  1 
ATOM   848  N NZ  . LYS   A 1 112 ? -7.622  -0.859  -8.512  1.00 71.42  ? 108 LYS   A NZ  1 
ATOM   849  N N   . SER   A 1 113 ? -1.147  -0.052  -11.650 1.00 37.14  ? 109 SER   A N   1 
ATOM   850  C CA  . SER   A 1 113 ? 0.272   0.230   -11.840 1.00 35.56  ? 109 SER   A CA  1 
ATOM   851  C C   . SER   A 1 113 ? 0.645   0.234   -13.317 1.00 42.06  ? 109 SER   A C   1 
ATOM   852  O O   . SER   A 1 113 ? 1.427   1.081   -13.762 1.00 40.22  ? 109 SER   A O   1 
ATOM   853  C CB  . SER   A 1 113 ? 1.117   -0.791  -11.079 1.00 29.74  ? 109 SER   A CB  1 
ATOM   854  O OG  . SER   A 1 113 ? 1.067   -0.554  -9.685  1.00 53.05  ? 109 SER   A OG  1 
ATOM   855  N N   . TYR   A 1 114 ? 0.096   -0.706  -14.091 1.00 35.35  ? 110 TYR   A N   1 
ATOM   856  C CA  . TYR   A 1 114 ? 0.403   -0.757  -15.517 1.00 41.52  ? 110 TYR   A CA  1 
ATOM   857  C C   . TYR   A 1 114 ? -0.168  0.453   -16.245 1.00 43.32  ? 110 TYR   A C   1 
ATOM   858  O O   . TYR   A 1 114 ? 0.453   0.972   -17.181 1.00 34.48  ? 110 TYR   A O   1 
ATOM   859  C CB  . TYR   A 1 114 ? -0.136  -2.051  -16.126 1.00 40.39  ? 110 TYR   A CB  1 
ATOM   860  C CG  . TYR   A 1 114 ? 0.640   -3.294  -15.750 1.00 33.89  ? 110 TYR   A CG  1 
ATOM   861  C CD1 . TYR   A 1 114 ? 1.776   -3.219  -14.955 1.00 32.81  ? 110 TYR   A CD1 1 
ATOM   862  C CD2 . TYR   A 1 114 ? 0.234   -4.546  -16.194 1.00 37.34  ? 110 TYR   A CD2 1 
ATOM   863  C CE1 . TYR   A 1 114 ? 2.484   -4.355  -14.611 1.00 30.37  ? 110 TYR   A CE1 1 
ATOM   864  C CE2 . TYR   A 1 114 ? 0.936   -5.687  -15.857 1.00 35.63  ? 110 TYR   A CE2 1 
ATOM   865  C CZ  . TYR   A 1 114 ? 2.059   -5.586  -15.066 1.00 30.70  ? 110 TYR   A CZ  1 
ATOM   866  O OH  . TYR   A 1 114 ? 2.759   -6.721  -14.729 1.00 32.29  ? 110 TYR   A OH  1 
ATOM   867  N N   . GLU   A 1 115 ? -1.350  0.915   -15.833 1.00 32.83  ? 111 GLU   A N   1 
ATOM   868  C CA  . GLU   A 1 115 ? -1.924  2.112   -16.437 1.00 43.15  ? 111 GLU   A CA  1 
ATOM   869  C C   . GLU   A 1 115 ? -1.134  3.355   -16.052 1.00 38.73  ? 111 GLU   A C   1 
ATOM   870  O O   . GLU   A 1 115 ? -0.954  4.261   -16.874 1.00 43.44  ? 111 GLU   A O   1 
ATOM   871  C CB  . GLU   A 1 115 ? -3.389  2.257   -16.028 1.00 50.72  ? 111 GLU   A CB  1 
ATOM   872  C CG  . GLU   A 1 115 ? -4.162  3.274   -16.848 1.00 54.39  ? 111 GLU   A CG  1 
ATOM   873  C CD  . GLU   A 1 115 ? -4.410  2.805   -18.267 1.00 71.13  ? 111 GLU   A CD  1 
ATOM   874  O OE1 . GLU   A 1 115 ? -5.222  1.874   -18.453 1.00 83.55  ? 111 GLU   A OE1 1 
ATOM   875  O OE2 . GLU   A 1 115 ? -3.792  3.366   -19.196 1.00 77.33  ? 111 GLU   A OE2 1 
ATOM   876  N N   . LEU   A 1 116 ? -0.658  3.418   -14.804 1.00 36.73  ? 112 LEU   A N   1 
ATOM   877  C CA  . LEU   A 1 116 ? 0.158   4.550   -14.378 1.00 44.37  ? 112 LEU   A CA  1 
ATOM   878  C C   . LEU   A 1 116 ? 1.419   4.643   -15.229 1.00 43.09  ? 112 LEU   A C   1 
ATOM   879  O O   . LEU   A 1 116 ? 1.821   5.734   -15.649 1.00 40.10  ? 112 LEU   A O   1 
ATOM   880  C CB  . LEU   A 1 116 ? 0.559   4.397   -12.910 1.00 48.63  ? 112 LEU   A CB  1 
ATOM   881  C CG  . LEU   A 1 116 ? 1.212   5.627   -12.262 1.00 52.68  ? 112 LEU   A CG  1 
ATOM   882  C CD1 . LEU   A 1 116 ? 0.165   6.734   -12.019 1.00 59.39  ? 112 LEU   A CD1 1 
ATOM   883  C CD2 . LEU   A 1 116 ? 2.062   5.329   -11.018 1.00 62.37  ? 112 LEU   A CD2 1 
ATOM   884  N N   . ILE   A 1 117 ? 2.053   3.493   -15.492 1.00 33.96  ? 113 ILE   A N   1 
ATOM   885  C CA  . ILE   A 1 117 ? 3.279   3.447   -16.283 1.00 39.33  ? 113 ILE   A CA  1 
ATOM   886  C C   . ILE   A 1 117 ? 3.026   3.996   -17.679 1.00 41.04  ? 113 ILE   A C   1 
ATOM   887  O O   . ILE   A 1 117 ? 3.798   4.811   -18.196 1.00 40.41  ? 113 ILE   A O   1 
ATOM   888  C CB  . ILE   A 1 117 ? 3.812   2.005   -16.348 1.00 43.09  ? 113 ILE   A CB  1 
ATOM   889  C CG1 . ILE   A 1 117 ? 4.355   1.541   -15.004 1.00 38.53  ? 113 ILE   A CG1 1 
ATOM   890  C CG2 . ILE   A 1 117 ? 4.901   1.887   -17.398 1.00 47.64  ? 113 ILE   A CG2 1 
ATOM   891  C CD1 . ILE   A 1 117 ? 4.370   0.032   -14.888 1.00 49.97  ? 113 ILE   A CD1 1 
ATOM   892  N N   . ARG   A 1 118 ? 1.946   3.537   -18.319 1.00 46.79  ? 114 ARG   A N   1 
ATOM   893  C CA  . ARG   A 1 118 ? 1.648   3.967   -19.681 1.00 51.82  ? 114 ARG   A CA  1 
ATOM   894  C C   . ARG   A 1 118 ? 1.403   5.467   -19.754 1.00 45.37  ? 114 ARG   A C   1 
ATOM   895  O O   . ARG   A 1 118 ? 1.727   6.098   -20.766 1.00 47.24  ? 114 ARG   A O   1 
ATOM   896  C CB  . ARG   A 1 118 ? 0.442   3.197   -20.216 1.00 52.04  ? 114 ARG   A CB  1 
ATOM   897  C CG  . ARG   A 1 118 ? 0.239   3.331   -21.713 1.00 66.39  ? 114 ARG   A CG  1 
ATOM   898  C CD  . ARG   A 1 118 ? -0.830  2.369   -22.215 1.00 66.66  ? 114 ARG   A CD  1 
ATOM   899  N NE  . ARG   A 1 118 ? -2.187  2.747   -21.813 1.00 61.11  ? 114 ARG   A NE  1 
ATOM   900  C CZ  . ARG   A 1 118 ? -2.781  3.907   -22.087 1.00 64.07  ? 114 ARG   A CZ  1 
ATOM   901  N NH1 . ARG   A 1 118 ? -2.166  4.842   -22.801 1.00 75.30  ? 114 ARG   A NH1 1 
ATOM   902  N NH2 . ARG   A 1 118 ? -4.017  4.126   -21.659 1.00 67.67  ? 114 ARG   A NH2 1 
ATOM   903  N N   . LYS   A 1 119 ? 0.846   6.057   -18.694 1.00 46.05  ? 115 LYS   A N   1 
ATOM   904  C CA  . LYS   A 1 119 ? 0.625   7.499   -18.689 1.00 52.01  ? 115 LYS   A CA  1 
ATOM   905  C C   . LYS   A 1 119 ? 1.929   8.262   -18.484 1.00 48.51  ? 115 LYS   A C   1 
ATOM   906  O O   . LYS   A 1 119 ? 2.130   9.323   -19.086 1.00 47.24  ? 115 LYS   A O   1 
ATOM   907  C CB  . LYS   A 1 119 ? -0.403  7.871   -17.620 1.00 50.18  ? 115 LYS   A CB  1 
ATOM   908  C CG  . LYS   A 1 119 ? -1.810  7.325   -17.868 1.00 57.38  ? 115 LYS   A CG  1 
ATOM   909  C CD  . LYS   A 1 119 ? -2.503  8.024   -19.035 1.00 64.06  ? 115 LYS   A CD  1 
ATOM   910  C CE  . LYS   A 1 119 ? -2.511  7.158   -20.289 1.00 71.31  ? 115 LYS   A CE  1 
ATOM   911  N NZ  . LYS   A 1 119 ? -3.119  7.862   -21.452 1.00 81.44  ? 115 LYS   A NZ  1 
ATOM   912  N N   . ILE   A 1 120 ? 2.826   7.743   -17.642 1.00 42.68  ? 116 ILE   A N   1 
ATOM   913  C CA  . ILE   A 1 120 ? 4.128   8.385   -17.474 1.00 47.32  ? 116 ILE   A CA  1 
ATOM   914  C C   . ILE   A 1 120 ? 4.957   8.319   -18.756 1.00 51.32  ? 116 ILE   A C   1 
ATOM   915  O O   . ILE   A 1 120 ? 5.746   9.229   -19.037 1.00 59.50  ? 116 ILE   A O   1 
ATOM   916  C CB  . ILE   A 1 120 ? 4.877   7.789   -16.259 1.00 44.32  ? 116 ILE   A CB  1 
ATOM   917  C CG1 . ILE   A 1 120 ? 4.189   8.190   -14.951 1.00 43.32  ? 116 ILE   A CG1 1 
ATOM   918  C CG2 . ILE   A 1 120 ? 6.343   8.166   -16.265 1.00 55.09  ? 116 ILE   A CG2 1 
ATOM   919  C CD1 . ILE   A 1 120 ? 4.723   7.478   -13.719 1.00 52.42  ? 116 ILE   A CD1 1 
ATOM   920  N N   . GLU   A 1 121 ? 4.769   7.279   -19.547 1.00 47.32  ? 117 GLU   A N   1 
ATOM   921  C CA  . GLU   A 1 121 ? 5.498   7.169   -20.834 1.00 56.18  ? 117 GLU   A CA  1 
ATOM   922  C C   . GLU   A 1 121 ? 5.021   8.257   -21.795 1.00 45.92  ? 117 GLU   A C   1 
ATOM   923  O O   . GLU   A 1 121 ? 5.872   8.820   -22.481 1.00 49.22  ? 117 GLU   A O   1 
ATOM   924  C CB  . GLU   A 1 121 ? 5.314   5.770   -21.403 1.00 48.38  ? 117 GLU   A CB  1 
ATOM   925  C CG  . GLU   A 1 121 ? 5.872   4.699   -20.498 1.00 60.49  ? 117 GLU   A CG  1 
ATOM   926  C CD  . GLU   A 1 121 ? 5.652   3.286   -20.999 1.00 67.72  ? 117 GLU   A CD  1 
ATOM   927  O OE1 . GLU   A 1 121 ? 6.374   2.390   -20.540 1.00 72.77  ? 117 GLU   A OE1 1 
ATOM   928  O OE2 . GLU   A 1 121 ? 4.760   3.090   -21.844 1.00 67.94  ? 117 GLU   A OE2 1 
ATOM   929  N N   . ALA   A 1 122 ? 3.716   8.514   -21.850 1.00 53.28  ? 118 ALA   A N   1 
ATOM   930  C CA  . ALA   A 1 122 ? 3.188   9.614   -22.650 1.00 54.15  ? 118 ALA   A CA  1 
ATOM   931  C C   . ALA   A 1 122 ? 3.645   10.961  -22.110 1.00 56.45  ? 118 ALA   A C   1 
ATOM   932  O O   . ALA   A 1 122 ? 3.730   11.939  -22.862 1.00 73.93  ? 118 ALA   A O   1 
ATOM   933  C CB  . ALA   A 1 122 ? 1.663   9.545   -22.690 1.00 53.59  ? 118 ALA   A CB  1 
ATOM   934  N N   . TYR   A 1 123 ? 3.939   11.030  -20.810 1.00 63.96  ? 119 TYR   A N   1 
ATOM   935  C CA  . TYR   A 1 123 ? 4.456   12.259  -20.218 1.00 67.26  ? 119 TYR   A CA  1 
ATOM   936  C C   . TYR   A 1 123 ? 5.857   12.568  -20.733 1.00 65.69  ? 119 TYR   A C   1 
ATOM   937  O O   . TYR   A 1 123 ? 6.137   13.691  -21.169 1.00 63.16  ? 119 TYR   A O   1 
ATOM   938  C CB  . TYR   A 1 123 ? 4.447   12.134  -18.692 1.00 75.43  ? 119 TYR   A CB  1 
ATOM   939  C CG  . TYR   A 1 123 ? 5.129   13.260  -17.945 1.00 82.46  ? 119 TYR   A CG  1 
ATOM   940  C CD1 . TYR   A 1 123 ? 4.416   14.378  -17.537 1.00 89.38  ? 119 TYR   A CD1 1 
ATOM   941  C CD2 . TYR   A 1 123 ? 6.479   13.193  -17.623 1.00 77.95  ? 119 TYR   A CD2 1 
ATOM   942  C CE1 . TYR   A 1 123 ? 5.029   15.406  -16.846 1.00 89.82  ? 119 TYR   A CE1 1 
ATOM   943  C CE2 . TYR   A 1 123 ? 7.102   14.217  -16.934 1.00 93.26  ? 119 TYR   A CE2 1 
ATOM   944  C CZ  . TYR   A 1 123 ? 6.371   15.321  -16.547 1.00 96.71  ? 119 TYR   A CZ  1 
ATOM   945  O OH  . TYR   A 1 123 ? 6.984   16.343  -15.859 1.00 102.51 ? 119 TYR   A OH  1 
ATOM   946  N N   . MET   A 1 124 ? 6.752   11.576  -20.697 1.00 66.49  ? 120 MET   A N   1 
ATOM   947  C CA  . MET   A 1 124 ? 8.135   11.816  -21.093 1.00 69.74  ? 120 MET   A CA  1 
ATOM   948  C C   . MET   A 1 124 ? 8.268   12.017  -22.597 1.00 60.81  ? 120 MET   A C   1 
ATOM   949  O O   . MET   A 1 124 ? 9.121   12.797  -23.039 1.00 64.77  ? 120 MET   A O   1 
ATOM   950  C CB  . MET   A 1 124 ? 9.023   10.657  -20.638 1.00 55.05  ? 120 MET   A CB  1 
ATOM   951  C CG  . MET   A 1 124 ? 8.967   10.374  -19.147 1.00 66.23  ? 120 MET   A CG  1 
ATOM   952  S SD  . MET   A 1 124 ? 9.934   8.919   -18.699 1.00 65.62  ? 120 MET   A SD  1 
ATOM   953  C CE  . MET   A 1 124 ? 8.695   7.633   -18.807 1.00 59.69  ? 120 MET   A CE  1 
ATOM   954  N N   . GLU   A 1 125 ? 7.444   11.328  -23.390 1.00 55.67  ? 121 GLU   A N   1 
ATOM   955  C CA  . GLU   A 1 125 ? 7.489   11.413  -24.852 1.00 65.05  ? 121 GLU   A CA  1 
ATOM   956  C C   . GLU   A 1 125 ? 8.882   11.087  -25.386 1.00 67.99  ? 121 GLU   A C   1 
ATOM   957  O O   . GLU   A 1 125 ? 9.353   11.682  -26.357 1.00 69.51  ? 121 GLU   A O   1 
ATOM   958  C CB  . GLU   A 1 125 ? 7.024   12.785  -25.346 1.00 59.79  ? 121 GLU   A CB  1 
ATOM   959  C CG  . GLU   A 1 125 ? 5.516   12.927  -25.430 1.00 61.60  ? 121 GLU   A CG  1 
ATOM   960  C CD  . GLU   A 1 125 ? 5.069   14.373  -25.405 1.00 75.75  ? 121 GLU   A CD  1 
ATOM   961  O OE1 . GLU   A 1 125 ? 5.937   15.261  -25.273 1.00 82.80  ? 121 GLU   A OE1 1 
ATOM   962  O OE2 . GLU   A 1 125 ? 3.850   14.621  -25.516 1.00 77.55  ? 121 GLU   A OE2 1 
ATOM   963  N N   . ASP   A 1 126 ? 9.546   10.136  -24.740 1.00 62.76  ? 122 ASP   A N   1 
ATOM   964  C CA  . ASP   A 1 126 ? 10.858  9.661   -25.157 1.00 64.59  ? 122 ASP   A CA  1 
ATOM   965  C C   . ASP   A 1 126 ? 10.682  8.298   -25.817 1.00 55.23  ? 122 ASP   A C   1 
ATOM   966  O O   . ASP   A 1 126 ? 10.144  7.368   -25.205 1.00 42.99  ? 122 ASP   A O   1 
ATOM   967  C CB  . ASP   A 1 126 ? 11.807  9.592   -23.958 1.00 66.54  ? 122 ASP   A CB  1 
ATOM   968  C CG  . ASP   A 1 126 ? 13.231  9.191   -24.335 1.00 66.45  ? 122 ASP   A CG  1 
ATOM   969  O OD1 . ASP   A 1 126 ? 13.450  8.606   -25.417 1.00 58.35  ? 122 ASP   A OD1 1 
ATOM   970  O OD2 . ASP   A 1 126 ? 14.143  9.455   -23.524 1.00 68.10  ? 122 ASP   A OD2 1 
ATOM   971  N N   . ASP   A 1 127 ? 11.145  8.188   -27.064 1.00 55.81  ? 123 ASP   A N   1 
ATOM   972  C CA  . ASP   A 1 127 ? 10.984  6.979   -27.863 1.00 59.90  ? 123 ASP   A CA  1 
ATOM   973  C C   . ASP   A 1 127 ? 11.727  5.778   -27.289 1.00 55.10  ? 123 ASP   A C   1 
ATOM   974  O O   . ASP   A 1 127 ? 11.588  4.672   -27.824 1.00 53.39  ? 123 ASP   A O   1 
ATOM   975  C CB  . ASP   A 1 127 ? 11.459  7.260   -29.293 1.00 63.97  ? 123 ASP   A CB  1 
ATOM   976  C CG  . ASP   A 1 127 ? 10.998  6.215   -30.285 1.00 76.22  ? 123 ASP   A CG  1 
ATOM   977  O OD1 . ASP   A 1 127 ? 9.772   6.015   -30.416 1.00 82.95  ? 123 ASP   A OD1 1 
ATOM   978  O OD2 . ASP   A 1 127 ? 11.864  5.601   -30.941 1.00 83.62  ? 123 ASP   A OD2 1 
ATOM   979  N N   . ARG   A 1 128 ? 12.501  5.960   -26.223 1.00 52.21  ? 124 ARG   A N   1 
ATOM   980  C CA  . ARG   A 1 128 ? 13.263  4.870   -25.634 1.00 51.36  ? 124 ARG   A CA  1 
ATOM   981  C C   . ARG   A 1 128 ? 12.472  4.057   -24.616 1.00 42.86  ? 124 ARG   A C   1 
ATOM   982  O O   . ARG   A 1 128 ? 12.952  3.002   -24.190 1.00 37.29  ? 124 ARG   A O   1 
ATOM   983  C CB  . ARG   A 1 128 ? 14.535  5.411   -24.969 1.00 51.63  ? 124 ARG   A CB  1 
ATOM   984  C CG  . ARG   A 1 128 ? 15.536  6.018   -25.942 1.00 47.38  ? 124 ARG   A CG  1 
ATOM   985  C CD  . ARG   A 1 128 ? 16.713  6.638   -25.208 1.00 49.62  ? 124 ARG   A CD  1 
ATOM   986  N NE  . ARG   A 1 128 ? 16.343  7.872   -24.520 1.00 54.59  ? 124 ARG   A NE  1 
ATOM   987  C CZ  . ARG   A 1 128 ? 17.196  8.639   -23.851 1.00 51.10  ? 124 ARG   A CZ  1 
ATOM   988  N NH1 . ARG   A 1 128 ? 18.477  8.304   -23.778 1.00 51.11  ? 124 ARG   A NH1 1 
ATOM   989  N NH2 . ARG   A 1 128 ? 16.770  9.745   -23.254 1.00 43.92  ? 124 ARG   A NH2 1 
ATOM   990  N N   . ILE   A 1 129 ? 11.280  4.502   -24.215 1.00 46.42  ? 125 ILE   A N   1 
ATOM   991  C CA  . ILE   A 1 129 ? 10.492  3.799   -23.210 1.00 39.16  ? 125 ILE   A CA  1 
ATOM   992  C C   . ILE   A 1 129 ? 9.277   3.211   -23.911 1.00 47.35  ? 125 ILE   A C   1 
ATOM   993  O O   . ILE   A 1 129 ? 8.699   3.843   -24.803 1.00 50.33  ? 125 ILE   A O   1 
ATOM   994  C CB  . ILE   A 1 129 ? 10.024  4.709   -22.056 1.00 51.74  ? 125 ILE   A CB  1 
ATOM   995  C CG1 . ILE   A 1 129 ? 11.173  5.501   -21.455 1.00 55.62  ? 125 ILE   A CG1 1 
ATOM   996  C CG2 . ILE   A 1 129 ? 9.501   3.856   -20.915 1.00 48.91  ? 125 ILE   A CG2 1 
ATOM   997  C CD1 . ILE   A 1 129 ? 11.323  6.850   -22.090 1.00 58.17  ? 125 ILE   A CD1 1 
ATOM   998  N N   . CYS   A 1 130 ? 8.875   2.013   -23.495 1.00 48.53  ? 126 CYS   A N   1 
ATOM   999  C CA  . CYS   A 1 130 ? 7.648   1.423   -24.004 1.00 52.66  ? 126 CYS   A CA  1 
ATOM   1000 C C   . CYS   A 1 130 ? 7.041   0.538   -22.927 1.00 50.56  ? 126 CYS   A C   1 
ATOM   1001 O O   . CYS   A 1 130 ? 7.729   0.074   -22.014 1.00 55.12  ? 126 CYS   A O   1 
ATOM   1002 C CB  . CYS   A 1 130 ? 7.893   0.613   -25.282 1.00 51.37  ? 126 CYS   A CB  1 
ATOM   1003 S SG  . CYS   A 1 130 ? 8.747   -0.957  -25.015 1.00 61.92  ? 126 CYS   A SG  1 
ATOM   1004 N N   . SER   A 1 131 ? 5.735   0.321   -23.039 1.00 61.58  ? 127 SER   A N   1 
ATOM   1005 C CA  . SER   A 1 131 ? 5.030   -0.633  -22.209 1.00 55.29  ? 127 SER   A CA  1 
ATOM   1006 C C   . SER   A 1 131 ? 4.413   -1.715  -23.081 1.00 51.70  ? 127 SER   A C   1 
ATOM   1007 O O   . SER   A 1 131 ? 3.784   -1.397  -24.100 1.00 63.82  ? 127 SER   A O   1 
ATOM   1008 C CB  . SER   A 1 131 ? 3.929   0.038   -21.375 1.00 57.91  ? 127 SER   A CB  1 
ATOM   1009 O OG  . SER   A 1 131 ? 4.478   0.806   -20.325 1.00 68.88  ? 127 SER   A OG  1 
ATOM   1010 N N   . PRO   A 1 132 ? 4.575   -2.986  -22.733 1.00 43.73  ? 128 PRO   A N   1 
ATOM   1011 C CA  . PRO   A 1 132 ? 3.839   -4.039  -23.425 1.00 40.22  ? 128 PRO   A CA  1 
ATOM   1012 C C   . PRO   A 1 132 ? 2.347   -3.854  -23.227 1.00 38.35  ? 128 PRO   A C   1 
ATOM   1013 O O   . PRO   A 1 132 ? 1.906   -3.438  -22.144 1.00 32.29  ? 128 PRO   A O   1 
ATOM   1014 C CB  . PRO   A 1 132 ? 4.338   -5.328  -22.752 1.00 37.95  ? 128 PRO   A CB  1 
ATOM   1015 C CG  . PRO   A 1 132 ? 4.925   -4.884  -21.448 1.00 50.18  ? 128 PRO   A CG  1 
ATOM   1016 C CD  . PRO   A 1 132 ? 5.474   -3.518  -21.696 1.00 44.60  ? 128 PRO   A CD  1 
ATOM   1017 N N   . PRO   A 1 133 ? 1.541   -4.117  -24.255 1.00 38.45  ? 129 PRO   A N   1 
ATOM   1018 C CA  . PRO   A 1 133 ? 0.086   -4.035  -24.086 1.00 36.94  ? 129 PRO   A CA  1 
ATOM   1019 C C   . PRO   A 1 133 ? -0.391  -4.962  -22.979 1.00 39.31  ? 129 PRO   A C   1 
ATOM   1020 O O   . PRO   A 1 133 ? 0.210   -6.004  -22.705 1.00 36.97  ? 129 PRO   A O   1 
ATOM   1021 C CB  . PRO   A 1 133 ? -0.456  -4.465  -25.453 1.00 32.48  ? 129 PRO   A CB  1 
ATOM   1022 C CG  . PRO   A 1 133 ? 0.645   -4.160  -26.409 1.00 40.88  ? 129 PRO   A CG  1 
ATOM   1023 C CD  . PRO   A 1 133 ? 1.929   -4.363  -25.654 1.00 39.88  ? 129 PRO   A CD  1 
ATOM   1024 N N   . PHE   A 1 134 ? -1.483  -4.564  -22.334 1.00 33.10  ? 130 PHE   A N   1 
ATOM   1025 C CA  . PHE   A 1 134 ? -2.011  -5.302  -21.198 1.00 33.17  ? 130 PHE   A CA  1 
ATOM   1026 C C   . PHE   A 1 134 ? -3.513  -5.077  -21.115 1.00 35.21  ? 130 PHE   A C   1 
ATOM   1027 O O   . PHE   A 1 134 ? -4.071  -4.203  -21.783 1.00 41.63  ? 130 PHE   A O   1 
ATOM   1028 C CB  . PHE   A 1 134 ? -1.334  -4.874  -19.892 1.00 37.15  ? 130 PHE   A CB  1 
ATOM   1029 C CG  . PHE   A 1 134 ? -1.771  -3.521  -19.402 1.00 42.78  ? 130 PHE   A CG  1 
ATOM   1030 C CD1 . PHE   A 1 134 ? -1.232  -2.367  -19.946 1.00 39.73  ? 130 PHE   A CD1 1 
ATOM   1031 C CD2 . PHE   A 1 134 ? -2.728  -3.403  -18.405 1.00 39.57  ? 130 PHE   A CD2 1 
ATOM   1032 C CE1 . PHE   A 1 134 ? -1.634  -1.121  -19.503 1.00 43.31  ? 130 PHE   A CE1 1 
ATOM   1033 C CE2 . PHE   A 1 134 ? -3.136  -2.160  -17.959 1.00 36.33  ? 130 PHE   A CE2 1 
ATOM   1034 C CZ  . PHE   A 1 134 ? -2.587  -1.017  -18.508 1.00 39.01  ? 130 PHE   A CZ  1 
ATOM   1035 N N   . MET   A 1 135 ? -4.159  -5.881  -20.274 1.00 36.24  ? 131 MET   A N   1 
ATOM   1036 C CA  . MET   A 1 135 ? -5.576  -5.741  -19.964 1.00 49.73  ? 131 MET   A CA  1 
ATOM   1037 C C   . MET   A 1 135 ? -5.902  -6.662  -18.799 1.00 48.35  ? 131 MET   A C   1 
ATOM   1038 O O   . MET   A 1 135 ? -5.217  -7.665  -18.578 1.00 38.24  ? 131 MET   A O   1 
ATOM   1039 C CB  . MET   A 1 135 ? -6.465  -6.071  -21.173 1.00 45.23  ? 131 MET   A CB  1 
ATOM   1040 C CG  . MET   A 1 135 ? -6.665  -7.556  -21.426 1.00 52.05  ? 131 MET   A CG  1 
ATOM   1041 S SD  . MET   A 1 135 ? -7.904  -7.891  -22.695 1.00 58.80  ? 131 MET   A SD  1 
ATOM   1042 C CE  . MET   A 1 135 ? -9.393  -7.340  -21.866 1.00 49.22  ? 131 MET   A CE  1 
ATOM   1043 N N   . GLU   A 1 136 ? -6.941  -6.303  -18.051 1.00 60.01  ? 132 GLU   A N   1 
ATOM   1044 C CA  . GLU   A 1 136 ? -7.428  -7.141  -16.965 1.00 62.50  ? 132 GLU   A CA  1 
ATOM   1045 C C   . GLU   A 1 136 ? -8.481  -8.098  -17.505 1.00 61.65  ? 132 GLU   A C   1 
ATOM   1046 O O   . GLU   A 1 136 ? -9.410  -7.681  -18.204 1.00 57.74  ? 132 GLU   A O   1 
ATOM   1047 C CB  . GLU   A 1 136 ? -8.007  -6.293  -15.832 1.00 67.46  ? 132 GLU   A CB  1 
ATOM   1048 C CG  . GLU   A 1 136 ? -8.570  -7.115  -14.682 1.00 73.96  ? 132 GLU   A CG  1 
ATOM   1049 C CD  . GLU   A 1 136 ? -8.386  -6.444  -13.335 1.00 84.74  ? 132 GLU   A CD  1 
ATOM   1050 O OE1 . GLU   A 1 136 ? -8.708  -5.244  -13.217 1.00 86.93  ? 132 GLU   A OE1 1 
ATOM   1051 O OE2 . GLU   A 1 136 ? -7.921  -7.119  -12.394 1.00 78.02  ? 132 GLU   A OE2 1 
ATOM   1052 N N   . LEU   A 1 137 ? -8.328  -9.379  -17.185 1.00 62.04  ? 133 LEU   A N   1 
ATOM   1053 C CA  . LEU   A 1 137 ? -9.212  -10.435 -17.669 1.00 66.90  ? 133 LEU   A CA  1 
ATOM   1054 C C   . LEU   A 1 137 ? -9.955  -11.010 -16.465 1.00 65.98  ? 133 LEU   A C   1 
ATOM   1055 O O   . LEU   A 1 137 ? -9.465  -11.913 -15.786 1.00 66.55  ? 133 LEU   A O   1 
ATOM   1056 C CB  . LEU   A 1 137 ? -8.418  -11.507 -18.412 1.00 62.20  ? 133 LEU   A CB  1 
ATOM   1057 C CG  . LEU   A 1 137 ? -9.200  -12.484 -19.291 1.00 69.85  ? 133 LEU   A CG  1 
ATOM   1058 C CD1 . LEU   A 1 137 ? -9.840  -11.760 -20.465 1.00 71.89  ? 133 LEU   A CD1 1 
ATOM   1059 C CD2 . LEU   A 1 137 ? -8.284  -13.594 -19.780 1.00 65.46  ? 133 LEU   A CD2 1 
ATOM   1060 N N   . THR   A 1 138 ? -11.148 -10.472 -16.204 1.00 72.61  ? 134 THR   A N   1 
ATOM   1061 C CA  . THR   A 1 138 ? -11.950 -10.953 -15.086 1.00 67.89  ? 134 THR   A CA  1 
ATOM   1062 C C   . THR   A 1 138 ? -12.539 -12.333 -15.346 1.00 62.17  ? 134 THR   A C   1 
ATOM   1063 O O   . THR   A 1 138 ? -12.915 -13.020 -14.390 1.00 59.24  ? 134 THR   A O   1 
ATOM   1064 C CB  . THR   A 1 138 ? -13.077 -9.966  -14.778 1.00 60.02  ? 134 THR   A CB  1 
ATOM   1065 O OG1 . THR   A 1 138 ? -13.840 -9.729  -15.966 1.00 78.08  ? 134 THR   A OG1 1 
ATOM   1066 C CG2 . THR   A 1 138 ? -12.509 -8.647  -14.274 1.00 62.76  ? 134 THR   A CG2 1 
ATOM   1067 N N   . SER   A 1 139 ? -12.625 -12.753 -16.606 1.00 58.45  ? 135 SER   A N   1 
ATOM   1068 C CA  . SER   A 1 139 ? -13.202 -14.046 -16.947 1.00 65.37  ? 135 SER   A CA  1 
ATOM   1069 C C   . SER   A 1 139 ? -12.857 -14.386 -18.389 1.00 69.06  ? 135 SER   A C   1 
ATOM   1070 O O   . SER   A 1 139 ? -12.680 -13.494 -19.224 1.00 77.02  ? 135 SER   A O   1 
ATOM   1071 C CB  . SER   A 1 139 ? -14.725 -14.049 -16.759 1.00 63.45  ? 135 SER   A CB  1 
ATOM   1072 O OG  . SER   A 1 139 ? -15.316 -15.158 -17.416 1.00 67.00  ? 135 SER   A OG  1 
ATOM   1073 N N   . LEU   A 1 140 ? -12.759 -15.683 -18.665 1.00 70.75  ? 136 LEU   A N   1 
ATOM   1074 C CA  . LEU   A 1 140 ? -12.673 -16.159 -20.036 1.00 71.72  ? 136 LEU   A CA  1 
ATOM   1075 C C   . LEU   A 1 140 ? -14.061 -16.165 -20.664 1.00 75.10  ? 136 LEU   A C   1 
ATOM   1076 O O   . LEU   A 1 140 ? -15.075 -16.312 -19.976 1.00 80.41  ? 136 LEU   A O   1 
ATOM   1077 C CB  . LEU   A 1 140 ? -12.064 -17.560 -20.089 1.00 80.20  ? 136 LEU   A CB  1 
ATOM   1078 C CG  . LEU   A 1 140 ? -10.581 -17.637 -20.457 1.00 74.93  ? 136 LEU   A CG  1 
ATOM   1079 C CD1 . LEU   A 1 140 ? -9.745  -16.932 -19.410 1.00 74.64  ? 136 LEU   A CD1 1 
ATOM   1080 C CD2 . LEU   A 1 140 ? -10.134 -19.081 -20.618 1.00 80.41  ? 136 LEU   A CD2 1 
ATOM   1081 N N   . CYS   A 1 141 ? -14.102 -16.001 -21.986 1.00 74.75  ? 137 CYS   A N   1 
ATOM   1082 C CA  . CYS   A 1 141 ? -15.363 -15.841 -22.706 1.00 78.28  ? 137 CYS   A CA  1 
ATOM   1083 C C   . CYS   A 1 141 ? -15.390 -16.744 -23.943 1.00 73.03  ? 137 CYS   A C   1 
ATOM   1084 O O   . CYS   A 1 141 ? -15.518 -16.289 -25.079 1.00 70.22  ? 137 CYS   A O   1 
ATOM   1085 C CB  . CYS   A 1 141 ? -15.587 -14.375 -23.071 1.00 75.98  ? 137 CYS   A CB  1 
ATOM   1086 S SG  . CYS   A 1 141 ? -14.158 -13.567 -23.817 1.00 80.61  ? 137 CYS   A SG  1 
ATOM   1087 N N   . GLY   A 1 142 ? -15.269 -18.047 -23.709 1.00 63.42  ? 138 GLY   A N   1 
ATOM   1088 C CA  . GLY   A 1 142 ? -15.578 -19.034 -24.725 1.00 59.36  ? 138 GLY   A CA  1 
ATOM   1089 C C   . GLY   A 1 142 ? -14.454 -19.328 -25.697 1.00 66.81  ? 138 GLY   A C   1 
ATOM   1090 O O   . GLY   A 1 142 ? -13.282 -18.993 -25.498 1.00 63.36  ? 138 GLY   A O   1 
ATOM   1091 N N   . ASP   A 1 143 ? -14.849 -19.984 -26.792 1.00 59.34  ? 139 ASP   A N   1 
ATOM   1092 C CA  . ASP   A 1 143 ? -13.929 -20.396 -27.846 1.00 68.01  ? 139 ASP   A CA  1 
ATOM   1093 C C   . ASP   A 1 143 ? -13.312 -19.221 -28.590 1.00 74.92  ? 139 ASP   A C   1 
ATOM   1094 O O   . ASP   A 1 143 ? -12.440 -19.437 -29.439 1.00 66.27  ? 139 ASP   A O   1 
ATOM   1095 C CB  . ASP   A 1 143 ? -14.657 -21.295 -28.848 1.00 68.40  ? 139 ASP   A CB  1 
ATOM   1096 C CG  . ASP   A 1 143 ? -15.364 -22.458 -28.183 1.00 69.80  ? 139 ASP   A CG  1 
ATOM   1097 O OD1 . ASP   A 1 143 ? -14.843 -22.976 -27.174 1.00 71.64  ? 139 ASP   A OD1 1 
ATOM   1098 O OD2 . ASP   A 1 143 ? -16.446 -22.851 -28.670 1.00 65.91  ? 139 ASP   A OD2 1 
ATOM   1099 N N   . ASP   A 1 144 ? -13.737 -17.996 -28.293 1.00 77.67  ? 140 ASP   A N   1 
ATOM   1100 C CA  . ASP   A 1 144 ? -13.375 -16.815 -29.062 1.00 75.75  ? 140 ASP   A CA  1 
ATOM   1101 C C   . ASP   A 1 144 ? -12.637 -15.797 -28.201 1.00 67.74  ? 140 ASP   A C   1 
ATOM   1102 O O   . ASP   A 1 144 ? -12.720 -14.591 -28.441 1.00 68.30  ? 140 ASP   A O   1 
ATOM   1103 C CB  . ASP   A 1 144 ? -14.629 -16.200 -29.677 1.00 73.22  ? 140 ASP   A CB  1 
ATOM   1104 C CG  . ASP   A 1 144 ? -14.391 -15.652 -31.057 1.00 95.97  ? 140 ASP   A CG  1 
ATOM   1105 O OD1 . ASP   A 1 144 ? -13.264 -15.798 -31.576 1.00 104.28 ? 140 ASP   A OD1 1 
ATOM   1106 O OD2 . ASP   A 1 144 ? -15.345 -15.091 -31.634 1.00 92.19  ? 140 ASP   A OD2 1 
ATOM   1107 N N   . THR   A 1 145 ? -11.900 -16.282 -27.199 1.00 60.35  ? 141 THR   A N   1 
ATOM   1108 C CA  . THR   A 1 145 ? -11.333 -15.395 -26.188 1.00 69.00  ? 141 THR   A CA  1 
ATOM   1109 C C   . THR   A 1 145 ? -10.310 -14.437 -26.787 1.00 64.11  ? 141 THR   A C   1 
ATOM   1110 O O   . THR   A 1 145 ? -10.230 -13.272 -26.380 1.00 56.01  ? 141 THR   A O   1 
ATOM   1111 C CB  . THR   A 1 145 ? -10.704 -16.227 -25.068 1.00 71.07  ? 141 THR   A CB  1 
ATOM   1112 O OG1 . THR   A 1 145 ? -11.702 -17.073 -24.483 1.00 72.18  ? 141 THR   A OG1 1 
ATOM   1113 C CG2 . THR   A 1 145 ? -10.126 -15.331 -23.986 1.00 58.08  ? 141 THR   A CG2 1 
ATOM   1114 N N   . MET   A 1 146 ? -9.534  -14.900 -27.772 1.00 51.88  ? 142 MET   A N   1 
ATOM   1115 C CA  . MET   A 1 146 ? -8.428  -14.092 -28.276 1.00 64.67  ? 142 MET   A CA  1 
ATOM   1116 C C   . MET   A 1 146 ? -8.906  -12.806 -28.939 1.00 63.84  ? 142 MET   A C   1 
ATOM   1117 O O   . MET   A 1 146 ? -8.214  -11.784 -28.864 1.00 60.08  ? 142 MET   A O   1 
ATOM   1118 C CB  . MET   A 1 146 ? -7.575  -14.906 -29.249 1.00 70.27  ? 142 MET   A CB  1 
ATOM   1119 C CG  . MET   A 1 146 ? -6.610  -15.853 -28.557 1.00 55.58  ? 142 MET   A CG  1 
ATOM   1120 S SD  . MET   A 1 146 ? -5.640  -15.021 -27.282 1.00 59.64  ? 142 MET   A SD  1 
ATOM   1121 C CE  . MET   A 1 146 ? -4.711  -13.844 -28.262 1.00 64.61  ? 142 MET   A CE  1 
ATOM   1122 N N   . ARG   A 1 147 ? -10.077 -12.824 -29.584 1.00 58.28  ? 143 ARG   A N   1 
ATOM   1123 C CA  . ARG   A 1 147 ? -10.565 -11.602 -30.219 1.00 65.70  ? 143 ARG   A CA  1 
ATOM   1124 C C   . ARG   A 1 147 ? -10.829 -10.507 -29.193 1.00 64.10  ? 143 ARG   A C   1 
ATOM   1125 O O   . ARG   A 1 147 ? -10.705 -9.318  -29.508 1.00 66.59  ? 143 ARG   A O   1 
ATOM   1126 C CB  . ARG   A 1 147 ? -11.826 -11.879 -31.040 1.00 64.76  ? 143 ARG   A CB  1 
ATOM   1127 C CG  . ARG   A 1 147 ? -12.295 -10.660 -31.831 1.00 72.95  ? 143 ARG   A CG  1 
ATOM   1128 C CD  . ARG   A 1 147 ? -12.887 -11.016 -33.184 1.00 83.11  ? 143 ARG   A CD  1 
ATOM   1129 N NE  . ARG   A 1 147 ? -14.286 -11.411 -33.074 1.00 84.51  ? 143 ARG   A NE  1 
ATOM   1130 C CZ  . ARG   A 1 147 ? -14.702 -12.671 -33.078 1.00 88.52  ? 143 ARG   A CZ  1 
ATOM   1131 N NH1 . ARG   A 1 147 ? -15.994 -12.949 -32.966 1.00 68.80  ? 143 ARG   A NH1 1 
ATOM   1132 N NH2 . ARG   A 1 147 ? -13.822 -13.654 -33.205 1.00 86.22  ? 143 ARG   A NH2 1 
ATOM   1133 N N   . LEU   A 1 148 ? -11.184 -10.881 -27.962 1.00 52.30  ? 144 LEU   A N   1 
ATOM   1134 C CA  . LEU   A 1 148 ? -11.259 -9.889  -26.895 1.00 48.60  ? 144 LEU   A CA  1 
ATOM   1135 C C   . LEU   A 1 148 ? -9.873  -9.378  -26.525 1.00 51.51  ? 144 LEU   A C   1 
ATOM   1136 O O   . LEU   A 1 148 ? -9.697  -8.187  -26.242 1.00 49.82  ? 144 LEU   A O   1 
ATOM   1137 C CB  . LEU   A 1 148 ? -11.959 -10.478 -25.673 1.00 53.83  ? 144 LEU   A CB  1 
ATOM   1138 C CG  . LEU   A 1 148 ? -12.054 -9.533  -24.476 1.00 61.65  ? 144 LEU   A CG  1 
ATOM   1139 C CD1 . LEU   A 1 148 ? -12.892 -8.315  -24.829 1.00 71.62  ? 144 LEU   A CD1 1 
ATOM   1140 C CD2 . LEU   A 1 148 ? -12.626 -10.260 -23.270 1.00 58.61  ? 144 LEU   A CD2 1 
ATOM   1141 N N   . LEU   A 1 149 ? -8.875  -10.263 -26.527 1.00 49.92  ? 145 LEU   A N   1 
ATOM   1142 C CA  . LEU   A 1 149 ? -7.505  -9.848  -26.251 1.00 52.32  ? 145 LEU   A CA  1 
ATOM   1143 C C   . LEU   A 1 149 ? -6.884  -9.106  -27.427 1.00 53.43  ? 145 LEU   A C   1 
ATOM   1144 O O   . LEU   A 1 149 ? -6.055  -8.213  -27.220 1.00 58.75  ? 145 LEU   A O   1 
ATOM   1145 C CB  . LEU   A 1 149 ? -6.648  -11.063 -25.890 1.00 54.17  ? 145 LEU   A CB  1 
ATOM   1146 C CG  . LEU   A 1 149 ? -6.751  -11.585 -24.455 1.00 46.62  ? 145 LEU   A CG  1 
ATOM   1147 C CD1 . LEU   A 1 149 ? -7.951  -12.497 -24.293 1.00 65.43  ? 145 LEU   A CD1 1 
ATOM   1148 C CD2 . LEU   A 1 149 ? -5.476  -12.309 -24.058 1.00 41.33  ? 145 LEU   A CD2 1 
ATOM   1149 N N   . GLU   A 1 150 ? -7.269  -9.456  -28.657 1.00 56.23  ? 146 GLU   A N   1 
ATOM   1150 C CA  . GLU   A 1 150 ? -6.708  -8.785  -29.826 1.00 60.27  ? 146 GLU   A CA  1 
ATOM   1151 C C   . GLU   A 1 150 ? -7.105  -7.316  -29.879 1.00 66.58  ? 146 GLU   A C   1 
ATOM   1152 O O   . GLU   A 1 150 ? -6.352  -6.491  -30.411 1.00 66.75  ? 146 GLU   A O   1 
ATOM   1153 C CB  . GLU   A 1 150 ? -7.148  -9.498  -31.107 1.00 77.82  ? 146 GLU   A CB  1 
ATOM   1154 C CG  . GLU   A 1 150 ? -6.519  -10.869 -31.312 1.00 92.69  ? 146 GLU   A CG  1 
ATOM   1155 C CD  . GLU   A 1 150 ? -6.262  -11.184 -32.773 1.00 109.28 ? 146 GLU   A CD  1 
ATOM   1156 O OE1 . GLU   A 1 150 ? -5.452  -12.093 -33.053 1.00 106.32 ? 146 GLU   A OE1 1 
ATOM   1157 O OE2 . GLU   A 1 150 ? -6.870  -10.525 -33.642 1.00 120.73 ? 146 GLU   A OE2 1 
ATOM   1158 N N   . LYS   A 1 151 ? -8.273  -6.966  -29.337 1.00 60.18  ? 147 LYS   A N   1 
ATOM   1159 C CA  . LYS   A 1 151 ? -8.716  -5.578  -29.361 1.00 62.53  ? 147 LYS   A CA  1 
ATOM   1160 C C   . LYS   A 1 151 ? -8.018  -4.711  -28.324 1.00 48.95  ? 147 LYS   A C   1 
ATOM   1161 O O   . LYS   A 1 151 ? -8.147  -3.484  -28.380 1.00 55.50  ? 147 LYS   A O   1 
ATOM   1162 C CB  . LYS   A 1 151 ? -10.235 -5.499  -29.174 1.00 66.14  ? 147 LYS   A CB  1 
ATOM   1163 C CG  . LYS   A 1 151 ? -11.048 -6.217  -30.258 1.00 68.54  ? 147 LYS   A CG  1 
ATOM   1164 C CD  . LYS   A 1 151 ? -10.976 -5.502  -31.609 1.00 78.44  ? 147 LYS   A CD  1 
ATOM   1165 C CE  . LYS   A 1 151 ? -9.902  -6.098  -32.518 1.00 76.41  ? 147 LYS   A CE  1 
ATOM   1166 N NZ  . LYS   A 1 151 ? -9.871  -5.456  -33.860 1.00 81.91  ? 147 LYS   A NZ  1 
ATOM   1167 N N   . ASN   A 1 152 ? -7.285  -5.308  -27.390 1.00 59.40  ? 148 ASN   A N   1 
ATOM   1168 C CA  . ASN   A 1 152 ? -6.427  -4.567  -26.479 1.00 48.60  ? 148 ASN   A CA  1 
ATOM   1169 C C   . ASN   A 1 152 ? -4.962  -4.635  -26.888 1.00 48.47  ? 148 ASN   A C   1 
ATOM   1170 O O   . ASN   A 1 152 ? -4.092  -4.200  -26.126 1.00 54.74  ? 148 ASN   A O   1 
ATOM   1171 C CB  . ASN   A 1 152 ? -6.609  -5.076  -25.048 1.00 59.35  ? 148 ASN   A CB  1 
ATOM   1172 C CG  . ASN   A 1 152 ? -8.002  -4.806  -24.510 1.00 64.56  ? 148 ASN   A CG  1 
ATOM   1173 O OD1 . ASN   A 1 152 ? -8.922  -5.600  -24.709 1.00 60.41  ? 148 ASN   A OD1 1 
ATOM   1174 N ND2 . ASN   A 1 152 ? -8.164  -3.679  -23.826 1.00 57.13  ? 148 ASN   A ND2 1 
ATOM   1175 N N   . GLY   A 1 153 ? -4.674  -5.169  -28.072 1.00 52.07  ? 149 GLY   A N   1 
ATOM   1176 C CA  . GLY   A 1 153 ? -3.325  -5.223  -28.594 1.00 50.96  ? 149 GLY   A CA  1 
ATOM   1177 C C   . GLY   A 1 153 ? -2.496  -6.403  -28.146 1.00 48.34  ? 149 GLY   A C   1 
ATOM   1178 O O   . GLY   A 1 153 ? -1.274  -6.384  -28.335 1.00 41.00  ? 149 GLY   A O   1 
ATOM   1179 N N   . LEU   A 1 154 ? -3.112  -7.431  -27.570 1.00 46.51  ? 150 LEU   A N   1 
ATOM   1180 C CA  . LEU   A 1 154 ? -2.373  -8.568  -27.041 1.00 50.76  ? 150 LEU   A CA  1 
ATOM   1181 C C   . LEU   A 1 154 ? -2.262  -9.677  -28.079 1.00 50.34  ? 150 LEU   A C   1 
ATOM   1182 O O   . LEU   A 1 154 ? -3.225  -9.984  -28.788 1.00 39.56  ? 150 LEU   A O   1 
ATOM   1183 C CB  . LEU   A 1 154 ? -3.038  -9.105  -25.774 1.00 47.19  ? 150 LEU   A CB  1 
ATOM   1184 C CG  . LEU   A 1 154 ? -2.756  -8.316  -24.493 1.00 53.05  ? 150 LEU   A CG  1 
ATOM   1185 C CD1 . LEU   A 1 154 ? -3.691  -7.123  -24.354 1.00 40.03  ? 150 LEU   A CD1 1 
ATOM   1186 C CD2 . LEU   A 1 154 ? -2.845  -9.222  -23.282 1.00 46.79  ? 150 LEU   A CD2 1 
ATOM   1187 N N   . THR   A 1 155 ? -1.074  -10.272 -28.164 1.00 45.71  ? 151 THR   A N   1 
ATOM   1188 C CA  . THR   A 1 155 ? -0.793  -11.375 -29.072 1.00 48.04  ? 151 THR   A CA  1 
ATOM   1189 C C   . THR   A 1 155 ? -0.050  -12.472 -28.321 1.00 40.78  ? 151 THR   A C   1 
ATOM   1190 O O   . THR   A 1 155 ? 0.454   -12.269 -27.213 1.00 39.28  ? 151 THR   A O   1 
ATOM   1191 C CB  . THR   A 1 155 ? 0.043   -10.923 -30.281 1.00 51.83  ? 151 THR   A CB  1 
ATOM   1192 O OG1 . THR   A 1 155 ? 1.374   -10.607 -29.853 1.00 49.43  ? 151 THR   A OG1 1 
ATOM   1193 C CG2 . THR   A 1 155 ? -0.575  -9.704  -30.953 1.00 44.83  ? 151 THR   A CG2 1 
ATOM   1194 N N   . PHE   A 1 156 ? 0.012   -13.646 -28.941 1.00 34.47  ? 152 PHE   A N   1 
ATOM   1195 C CA  . PHE   A 1 156 ? 0.837   -14.719 -28.408 1.00 35.81  ? 152 PHE   A CA  1 
ATOM   1196 C C   . PHE   A 1 156 ? 2.311   -14.416 -28.671 1.00 45.53  ? 152 PHE   A C   1 
ATOM   1197 O O   . PHE   A 1 156 ? 2.667   -13.969 -29.766 1.00 52.46  ? 152 PHE   A O   1 
ATOM   1198 C CB  . PHE   A 1 156 ? 0.466   -16.058 -29.047 1.00 45.60  ? 152 PHE   A CB  1 
ATOM   1199 C CG  . PHE   A 1 156 ? -0.893  -16.568 -28.659 1.00 47.44  ? 152 PHE   A CG  1 
ATOM   1200 C CD1 . PHE   A 1 156 ? -1.177  -16.902 -27.344 1.00 41.40  ? 152 PHE   A CD1 1 
ATOM   1201 C CD2 . PHE   A 1 156 ? -1.884  -16.726 -29.614 1.00 45.42  ? 152 PHE   A CD2 1 
ATOM   1202 C CE1 . PHE   A 1 156 ? -2.426  -17.378 -26.990 1.00 41.41  ? 152 PHE   A CE1 1 
ATOM   1203 C CE2 . PHE   A 1 156 ? -3.134  -17.200 -29.265 1.00 46.82  ? 152 PHE   A CE2 1 
ATOM   1204 C CZ  . PHE   A 1 156 ? -3.405  -17.526 -27.952 1.00 43.15  ? 152 PHE   A CZ  1 
ATOM   1205 N N   . PRO   A 1 157 ? 3.195   -14.644 -27.689 1.00 37.48  ? 153 PRO   A N   1 
ATOM   1206 C CA  . PRO   A 1 157 ? 2.848   -15.118 -26.347 1.00 35.48  ? 153 PRO   A CA  1 
ATOM   1207 C C   . PRO   A 1 157 ? 2.582   -13.979 -25.368 1.00 40.61  ? 153 PRO   A C   1 
ATOM   1208 O O   . PRO   A 1 157 ? 3.085   -12.872 -25.563 1.00 32.63  ? 153 PRO   A O   1 
ATOM   1209 C CB  . PRO   A 1 157 ? 4.089   -15.905 -25.934 1.00 38.83  ? 153 PRO   A CB  1 
ATOM   1210 C CG  . PRO   A 1 157 ? 5.211   -15.189 -26.616 1.00 40.40  ? 153 PRO   A CG  1 
ATOM   1211 C CD  . PRO   A 1 157 ? 4.654   -14.599 -27.893 1.00 38.45  ? 153 PRO   A CD  1 
ATOM   1212 N N   . PHE   A 1 158 ? 1.795   -14.249 -24.328 1.00 31.23  ? 154 PHE   A N   1 
ATOM   1213 C CA  . PHE   A 1 158 ? 1.550   -13.288 -23.264 1.00 30.87  ? 154 PHE   A CA  1 
ATOM   1214 C C   . PHE   A 1 158 ? 1.698   -13.983 -21.917 1.00 35.63  ? 154 PHE   A C   1 
ATOM   1215 O O   . PHE   A 1 158 ? 1.724   -15.213 -21.824 1.00 29.63  ? 154 PHE   A O   1 
ATOM   1216 C CB  . PHE   A 1 158 ? 0.165   -12.631 -23.395 1.00 29.30  ? 154 PHE   A CB  1 
ATOM   1217 C CG  . PHE   A 1 158 ? -0.977  -13.606 -23.473 1.00 35.90  ? 154 PHE   A CG  1 
ATOM   1218 C CD1 . PHE   A 1 158 ? -1.500  -14.182 -22.326 1.00 37.05  ? 154 PHE   A CD1 1 
ATOM   1219 C CD2 . PHE   A 1 158 ? -1.543  -13.930 -24.695 1.00 32.16  ? 154 PHE   A CD2 1 
ATOM   1220 C CE1 . PHE   A 1 158 ? -2.554  -15.072 -22.398 1.00 42.19  ? 154 PHE   A CE1 1 
ATOM   1221 C CE2 . PHE   A 1 158 ? -2.597  -14.819 -24.772 1.00 37.51  ? 154 PHE   A CE2 1 
ATOM   1222 C CZ  . PHE   A 1 158 ? -3.103  -15.391 -23.622 1.00 39.80  ? 154 PHE   A CZ  1 
ATOM   1223 N N   . ILE   A 1 159 ? 1.796   -13.177 -20.863 1.00 27.28  ? 155 ILE   A N   1 
ATOM   1224 C CA  . ILE   A 1 159 ? 2.022   -13.665 -19.507 1.00 28.16  ? 155 ILE   A CA  1 
ATOM   1225 C C   . ILE   A 1 159 ? 0.793   -13.356 -18.665 1.00 40.68  ? 155 ILE   A C   1 
ATOM   1226 O O   . ILE   A 1 159 ? 0.271   -12.235 -18.701 1.00 34.02  ? 155 ILE   A O   1 
ATOM   1227 C CB  . ILE   A 1 159 ? 3.285   -13.041 -18.889 1.00 30.78  ? 155 ILE   A CB  1 
ATOM   1228 C CG1 . ILE   A 1 159 ? 4.537   -13.591 -19.571 1.00 34.57  ? 155 ILE   A CG1 1 
ATOM   1229 C CG2 . ILE   A 1 159 ? 3.344   -13.306 -17.392 1.00 30.73  ? 155 ILE   A CG2 1 
ATOM   1230 C CD1 . ILE   A 1 159 ? 5.811   -12.924 -19.119 1.00 38.32  ? 155 ILE   A CD1 1 
ATOM   1231 N N   . CYS   A 1 160 ? 0.332   -14.351 -17.912 1.00 34.15  ? 156 CYS   A N   1 
ATOM   1232 C CA  . CYS   A 1 160 ? -0.773  -14.189 -16.977 1.00 40.10  ? 156 CYS   A CA  1 
ATOM   1233 C C   . CYS   A 1 160 ? -0.207  -13.985 -15.578 1.00 40.39  ? 156 CYS   A C   1 
ATOM   1234 O O   . CYS   A 1 160 ? 0.573   -14.812 -15.094 1.00 39.22  ? 156 CYS   A O   1 
ATOM   1235 C CB  . CYS   A 1 160 ? -1.696  -15.406 -17.004 1.00 49.01  ? 156 CYS   A CB  1 
ATOM   1236 S SG  . CYS   A 1 160 ? -2.916  -15.446 -15.671 1.00 56.68  ? 156 CYS   A SG  1 
ATOM   1237 N N   . LYS   A 1 161 ? -0.596  -12.889 -14.935 1.00 32.00  ? 157 LYS   A N   1 
ATOM   1238 C CA  . LYS   A 1 161 ? -0.158  -12.583 -13.583 1.00 35.14  ? 157 LYS   A CA  1 
ATOM   1239 C C   . LYS   A 1 161 ? -1.370  -12.293 -12.713 1.00 38.02  ? 157 LYS   A C   1 
ATOM   1240 O O   . LYS   A 1 161 ? -2.463  -12.006 -13.207 1.00 31.70  ? 157 LYS   A O   1 
ATOM   1241 C CB  . LYS   A 1 161 ? 0.796   -11.380 -13.549 1.00 30.10  ? 157 LYS   A CB  1 
ATOM   1242 C CG  . LYS   A 1 161 ? 1.707   -11.265 -14.756 1.00 43.87  ? 157 LYS   A CG  1 
ATOM   1243 C CD  . LYS   A 1 161 ? 2.508   -9.977  -14.710 1.00 36.86  ? 157 LYS   A CD  1 
ATOM   1244 C CE  . LYS   A 1 161 ? 3.799   -10.099 -15.499 1.00 36.56  ? 157 LYS   A CE  1 
ATOM   1245 N NZ  . LYS   A 1 161 ? 4.553   -8.817  -15.513 1.00 39.37  ? 157 LYS   A NZ  1 
ATOM   1246 N N   . THR   A 1 162 ? -1.163  -12.376 -11.402 1.00 30.11  ? 158 THR   A N   1 
ATOM   1247 C CA  . THR   A 1 162 ? -2.188  -11.930 -10.473 1.00 29.71  ? 158 THR   A CA  1 
ATOM   1248 C C   . THR   A 1 162 ? -2.406  -10.429 -10.627 1.00 44.99  ? 158 THR   A C   1 
ATOM   1249 O O   . THR   A 1 162 ? -1.501  -9.679  -10.998 1.00 42.31  ? 158 THR   A O   1 
ATOM   1250 C CB  . THR   A 1 162 ? -1.801  -12.264 -9.032  1.00 35.13  ? 158 THR   A CB  1 
ATOM   1251 O OG1 . THR   A 1 162 ? -0.589  -11.581 -8.688  1.00 45.12  ? 158 THR   A OG1 1 
ATOM   1252 C CG2 . THR   A 1 162 ? -1.605  -13.764 -8.864  1.00 40.20  ? 158 THR   A CG2 1 
ATOM   1253 N N   . ARG   A 1 163 ? -3.630  -10.000 -10.352 1.00 40.74  ? 159 ARG   A N   1 
ATOM   1254 C CA  . ARG   A 1 163 ? -4.049  -8.611  -10.491 1.00 56.91  ? 159 ARG   A CA  1 
ATOM   1255 C C   . ARG   A 1 163 ? -3.797  -7.801  -9.226  1.00 45.53  ? 159 ARG   A C   1 
ATOM   1256 O O   . ARG   A 1 163 ? -3.931  -6.573  -9.254  1.00 55.72  ? 159 ARG   A O   1 
ATOM   1257 C CB  . ARG   A 1 163 ? -5.539  -8.560  -10.847 1.00 55.38  ? 159 ARG   A CB  1 
ATOM   1258 C CG  . ARG   A 1 163 ? -6.414  -8.753  -9.630  1.00 53.58  ? 159 ARG   A CG  1 
ATOM   1259 C CD  . ARG   A 1 163 ? -6.316  -10.180 -9.169  1.00 72.32  ? 159 ARG   A CD  1 
ATOM   1260 N NE  . ARG   A 1 163 ? -7.218  -10.530 -8.091  1.00 89.02  ? 159 ARG   A NE  1 
ATOM   1261 C CZ  . ARG   A 1 163 ? -7.039  -11.607 -7.339  1.00 86.70  ? 159 ARG   A CZ  1 
ATOM   1262 N NH1 . ARG   A 1 163 ? -5.971  -12.371 -7.539  1.00 47.11  ? 159 ARG   A NH1 1 
ATOM   1263 N NH2 . ARG   A 1 163 ? -7.888  -11.894 -6.364  1.00 79.60  ? 159 ARG   A NH2 1 
ATOM   1264 N N   . VAL   A 1 164 ? -3.470  -8.463  -8.118  1.00 40.29  ? 160 VAL   A N   1 
ATOM   1265 C CA  . VAL   A 1 164 ? -2.984  -7.818  -6.902  1.00 46.49  ? 160 VAL   A CA  1 
ATOM   1266 C C   . VAL   A 1 164 ? -1.535  -8.245  -6.721  1.00 34.62  ? 160 VAL   A C   1 
ATOM   1267 O O   . VAL   A 1 164 ? -1.247  -9.439  -6.570  1.00 38.86  ? 160 VAL   A O   1 
ATOM   1268 C CB  . VAL   A 1 164 ? -3.830  -8.190  -5.674  1.00 43.28  ? 160 VAL   A CB  1 
ATOM   1269 C CG1 . VAL   A 1 164 ? -3.119  -7.769  -4.394  1.00 44.43  ? 160 VAL   A CG1 1 
ATOM   1270 C CG2 . VAL   A 1 164 ? -5.205  -7.546  -5.758  1.00 55.66  ? 160 VAL   A CG2 1 
ATOM   1271 N N   . ALA   A 1 165 ? -0.624  -7.277  -6.743  1.00 43.22  ? 161 ALA   A N   1 
ATOM   1272 C CA  . ALA   A 1 165 ? 0.811   -7.563  -6.761  1.00 43.08  ? 161 ALA   A CA  1 
ATOM   1273 C C   . ALA   A 1 165 ? 1.407   -7.613  -5.358  1.00 49.35  ? 161 ALA   A C   1 
ATOM   1274 O O   . ALA   A 1 165 ? 2.397   -6.946  -5.060  1.00 47.85  ? 161 ALA   A O   1 
ATOM   1275 C CB  . ALA   A 1 165 ? 1.530   -6.533  -7.623  1.00 51.26  ? 161 ALA   A CB  1 
ATOM   1276 N N   . HIS   A 1 166 ? 0.807   -8.418  -4.484  1.00 54.09  ? 162 HIS   A N   1 
ATOM   1277 C CA  . HIS   A 1 166 ? 1.331   -8.607  -3.139  1.00 50.79  ? 162 HIS   A CA  1 
ATOM   1278 C C   . HIS   A 1 166 ? 0.711   -9.863  -2.545  1.00 54.57  ? 162 HIS   A C   1 
ATOM   1279 O O   . HIS   A 1 166 ? -0.389  -10.269 -2.929  1.00 53.36  ? 162 HIS   A O   1 
ATOM   1280 C CB  . HIS   A 1 166 ? 1.047   -7.395  -2.242  1.00 60.36  ? 162 HIS   A CB  1 
ATOM   1281 C CG  . HIS   A 1 166 ? 1.497   -7.575  -0.825  1.00 61.63  ? 162 HIS   A CG  1 
ATOM   1282 N ND1 . HIS   A 1 166 ? 2.823   -7.531  -0.454  1.00 66.80  ? 162 HIS   A ND1 1 
ATOM   1283 C CD2 . HIS   A 1 166 ? 0.796   -7.807  0.311   1.00 66.67  ? 162 HIS   A CD2 1 
ATOM   1284 C CE1 . HIS   A 1 166 ? 2.921   -7.725  0.849   1.00 73.41  ? 162 HIS   A CE1 1 
ATOM   1285 N NE2 . HIS   A 1 166 ? 1.705   -7.895  1.337   1.00 72.14  ? 162 HIS   A NE2 1 
ATOM   1286 N N   . GLY   A 1 167 ? 1.434   -10.475 -1.611  1.00 57.24  ? 163 GLY   A N   1 
ATOM   1287 C CA  . GLY   A 1 167 ? 0.932   -11.635 -0.907  1.00 53.92  ? 163 GLY   A CA  1 
ATOM   1288 C C   . GLY   A 1 167 ? 1.363   -12.943 -1.534  1.00 47.72  ? 163 GLY   A C   1 
ATOM   1289 O O   . GLY   A 1 167 ? 2.145   -13.004 -2.488  1.00 58.20  ? 163 GLY   A O   1 
ATOM   1290 N N   . THR   A 1 168 ? 0.824   -14.021 -0.971  1.00 53.98  ? 164 THR   A N   1 
ATOM   1291 C CA  . THR   A 1 168 ? 1.157   -15.362 -1.429  1.00 56.62  ? 164 THR   A CA  1 
ATOM   1292 C C   . THR   A 1 168 ? 0.649   -15.584 -2.850  1.00 61.85  ? 164 THR   A C   1 
ATOM   1293 O O   . THR   A 1 168 ? -0.463  -15.178 -3.200  1.00 56.65  ? 164 THR   A O   1 
ATOM   1294 C CB  . THR   A 1 168 ? 0.560   -16.402 -0.477  1.00 61.92  ? 164 THR   A CB  1 
ATOM   1295 O OG1 . THR   A 1 168 ? 1.320   -16.429 0.738   1.00 67.09  ? 164 THR   A OG1 1 
ATOM   1296 C CG2 . THR   A 1 168 ? 0.572   -17.791 -1.099  1.00 69.87  ? 164 THR   A CG2 1 
ATOM   1297 N N   . ASN   A 1 169 ? 1.489   -16.213 -3.674  1.00 56.73  ? 165 ASN   A N   1 
ATOM   1298 C CA  . ASN   A 1 169 ? 1.210   -16.579 -5.061  1.00 66.25  ? 165 ASN   A CA  1 
ATOM   1299 C C   . ASN   A 1 169 ? 1.082   -15.374 -5.983  1.00 41.94  ? 165 ASN   A C   1 
ATOM   1300 O O   . ASN   A 1 169 ? 0.668   -15.531 -7.139  1.00 44.39  ? 165 ASN   A O   1 
ATOM   1301 C CB  . ASN   A 1 169 ? -0.049  -17.447 -5.184  1.00 53.80  ? 165 ASN   A CB  1 
ATOM   1302 C CG  . ASN   A 1 169 ? 0.114   -18.804 -4.531  1.00 61.83  ? 165 ASN   A CG  1 
ATOM   1303 O OD1 . ASN   A 1 169 ? 1.130   -19.476 -4.712  1.00 58.63  ? 165 ASN   A OD1 1 
ATOM   1304 N ND2 . ASN   A 1 169 ? -0.892  -19.219 -3.770  1.00 68.56  ? 165 ASN   A ND2 1 
ATOM   1305 N N   . SER   A 1 170 ? 1.428   -14.173 -5.515  1.00 40.96  ? 166 SER   A N   1 
ATOM   1306 C CA  . SER   A 1 170 ? 1.405   -13.007 -6.389  1.00 42.03  ? 166 SER   A CA  1 
ATOM   1307 C C   . SER   A 1 170 ? 2.542   -13.029 -7.402  1.00 45.04  ? 166 SER   A C   1 
ATOM   1308 O O   . SER   A 1 170 ? 2.488   -12.294 -8.393  1.00 38.11  ? 166 SER   A O   1 
ATOM   1309 C CB  . SER   A 1 170 ? 1.463   -11.722 -5.560  1.00 42.51  ? 166 SER   A CB  1 
ATOM   1310 O OG  . SER   A 1 170 ? 2.726   -11.567 -4.938  1.00 37.05  ? 166 SER   A OG  1 
ATOM   1311 N N   . HIS   A 1 171 ? 3.564   -13.854 -7.178  1.00 38.45  ? 167 HIS   A N   1 
ATOM   1312 C CA  . HIS   A 1 171 ? 4.664   -14.019 -8.116  1.00 40.59  ? 167 HIS   A CA  1 
ATOM   1313 C C   . HIS   A 1 171 ? 4.484   -15.224 -9.028  1.00 33.46  ? 167 HIS   A C   1 
ATOM   1314 O O   . HIS   A 1 171 ? 5.302   -15.428 -9.931  1.00 36.39  ? 167 HIS   A O   1 
ATOM   1315 C CB  . HIS   A 1 171 ? 5.991   -14.142 -7.359  1.00 47.27  ? 167 HIS   A CB  1 
ATOM   1316 C CG  . HIS   A 1 171 ? 6.374   -12.907 -6.604  1.00 47.77  ? 167 HIS   A CG  1 
ATOM   1317 N ND1 . HIS   A 1 171 ? 6.242   -11.641 -7.131  1.00 50.23  ? 167 HIS   A ND1 1 
ATOM   1318 C CD2 . HIS   A 1 171 ? 6.886   -12.746 -5.361  1.00 46.81  ? 167 HIS   A CD2 1 
ATOM   1319 C CE1 . HIS   A 1 171 ? 6.657   -10.752 -6.246  1.00 46.87  ? 167 HIS   A CE1 1 
ATOM   1320 N NE2 . HIS   A 1 171 ? 7.052   -11.397 -5.163  1.00 61.21  ? 167 HIS   A NE2 1 
ATOM   1321 N N   . GLU   A 1 172 ? 3.446   -16.028 -8.813  1.00 40.47  ? 168 GLU   A N   1 
ATOM   1322 C CA  . GLU   A 1 172 ? 3.172   -17.173 -9.671  1.00 40.25  ? 168 GLU   A CA  1 
ATOM   1323 C C   . GLU   A 1 172 ? 2.517   -16.690 -10.958 1.00 40.04  ? 168 GLU   A C   1 
ATOM   1324 O O   . GLU   A 1 172 ? 1.453   -16.062 -10.922 1.00 42.46  ? 168 GLU   A O   1 
ATOM   1325 C CB  . GLU   A 1 172 ? 2.278   -18.181 -8.952  1.00 54.45  ? 168 GLU   A CB  1 
ATOM   1326 C CG  . GLU   A 1 172 ? 2.942   -18.876 -7.774  1.00 49.60  ? 168 GLU   A CG  1 
ATOM   1327 C CD  . GLU   A 1 172 ? 4.046   -19.826 -8.199  1.00 53.99  ? 168 GLU   A CD  1 
ATOM   1328 O OE1 . GLU   A 1 172 ? 4.920   -20.134 -7.361  1.00 61.31  ? 168 GLU   A OE1 1 
ATOM   1329 O OE2 . GLU   A 1 172 ? 4.040   -20.267 -9.368  1.00 50.85  ? 168 GLU   A OE2 1 
ATOM   1330 N N   . MET   A 1 173 ? 3.152   -16.975 -12.091 1.00 36.72  ? 169 MET   A N   1 
ATOM   1331 C CA  . MET   A 1 173 ? 2.680   -16.525 -13.390 1.00 31.59  ? 169 MET   A CA  1 
ATOM   1332 C C   . MET   A 1 173 ? 2.664   -17.690 -14.370 1.00 37.05  ? 169 MET   A C   1 
ATOM   1333 O O   . MET   A 1 173 ? 3.130   -18.794 -14.073 1.00 32.77  ? 169 MET   A O   1 
ATOM   1334 C CB  . MET   A 1 173 ? 3.548   -15.384 -13.940 1.00 29.37  ? 169 MET   A CB  1 
ATOM   1335 C CG  . MET   A 1 173 ? 3.842   -14.284 -12.934 1.00 31.69  ? 169 MET   A CG  1 
ATOM   1336 S SD  . MET   A 1 173 ? 4.936   -13.013 -13.591 1.00 40.94  ? 169 MET   A SD  1 
ATOM   1337 C CE  . MET   A 1 173 ? 4.891   -11.814 -12.261 1.00 39.56  ? 169 MET   A CE  1 
ATOM   1338 N N   . ALA   A 1 174 ? 2.117   -17.426 -15.554 1.00 31.14  ? 170 ALA   A N   1 
ATOM   1339 C CA  . ALA   A 1 174 ? 2.054   -18.413 -16.620 1.00 35.71  ? 170 ALA   A CA  1 
ATOM   1340 C C   . ALA   A 1 174 ? 2.154   -17.697 -17.957 1.00 36.74  ? 170 ALA   A C   1 
ATOM   1341 O O   . ALA   A 1 174 ? 1.524   -16.655 -18.159 1.00 41.39  ? 170 ALA   A O   1 
ATOM   1342 C CB  . ALA   A 1 174 ? 0.762   -19.235 -16.553 1.00 35.56  ? 170 ALA   A CB  1 
ATOM   1343 N N   . ILE   A 1 175 ? 2.949   -18.257 -18.864 1.00 29.51  ? 171 ILE   A N   1 
ATOM   1344 C CA  . ILE   A 1 175 ? 3.127   -17.716 -20.207 1.00 31.53  ? 171 ILE   A CA  1 
ATOM   1345 C C   . ILE   A 1 175 ? 2.397   -18.625 -21.186 1.00 26.44  ? 171 ILE   A C   1 
ATOM   1346 O O   . ILE   A 1 175 ? 2.633   -19.840 -21.213 1.00 31.58  ? 171 ILE   A O   1 
ATOM   1347 C CB  . ILE   A 1 175 ? 4.617   -17.569 -20.567 1.00 30.55  ? 171 ILE   A CB  1 
ATOM   1348 C CG1 . ILE   A 1 175 ? 4.787   -17.269 -22.058 1.00 36.78  ? 171 ILE   A CG1 1 
ATOM   1349 C CG2 . ILE   A 1 175 ? 5.404   -18.806 -20.155 1.00 42.55  ? 171 ILE   A CG2 1 
ATOM   1350 C CD1 . ILE   A 1 175 ? 6.179   -16.802 -22.429 1.00 45.68  ? 171 ILE   A CD1 1 
ATOM   1351 N N   . VAL   A 1 176 ? 1.501   -18.039 -21.977 1.00 29.37  ? 172 VAL   A N   1 
ATOM   1352 C CA  . VAL   A 1 176 ? 0.636   -18.773 -22.895 1.00 28.55  ? 172 VAL   A CA  1 
ATOM   1353 C C   . VAL   A 1 176 ? 1.130   -18.535 -24.315 1.00 39.64  ? 172 VAL   A C   1 
ATOM   1354 O O   . VAL   A 1 176 ? 1.383   -17.389 -24.705 1.00 27.46  ? 172 VAL   A O   1 
ATOM   1355 C CB  . VAL   A 1 176 ? -0.833  -18.343 -22.743 1.00 37.19  ? 172 VAL   A CB  1 
ATOM   1356 C CG1 . VAL   A 1 176 ? -1.729  -19.169 -23.653 1.00 33.24  ? 172 VAL   A CG1 1 
ATOM   1357 C CG2 . VAL   A 1 176 ? -1.270  -18.467 -21.291 1.00 32.92  ? 172 VAL   A CG2 1 
ATOM   1358 N N   . PHE   A 1 177 ? 1.254   -19.616 -25.091 1.00 29.55  ? 173 PHE   A N   1 
ATOM   1359 C CA  . PHE   A 1 177 ? 1.863   -19.545 -26.412 1.00 39.63  ? 173 PHE   A CA  1 
ATOM   1360 C C   . PHE   A 1 177 ? 0.893   -19.739 -27.569 1.00 38.45  ? 173 PHE   A C   1 
ATOM   1361 O O   . PHE   A 1 177 ? 1.221   -19.342 -28.691 1.00 34.00  ? 173 PHE   A O   1 
ATOM   1362 C CB  . PHE   A 1 177 ? 2.980   -20.592 -26.542 1.00 38.84  ? 173 PHE   A CB  1 
ATOM   1363 C CG  . PHE   A 1 177 ? 4.084   -20.433 -25.537 1.00 39.94  ? 173 PHE   A CG  1 
ATOM   1364 C CD1 . PHE   A 1 177 ? 5.172   -19.620 -25.807 1.00 33.71  ? 173 PHE   A CD1 1 
ATOM   1365 C CD2 . PHE   A 1 177 ? 4.039   -21.106 -24.328 1.00 41.65  ? 173 PHE   A CD2 1 
ATOM   1366 C CE1 . PHE   A 1 177 ? 6.191   -19.475 -24.885 1.00 40.76  ? 173 PHE   A CE1 1 
ATOM   1367 C CE2 . PHE   A 1 177 ? 5.055   -20.965 -23.402 1.00 42.31  ? 173 PHE   A CE2 1 
ATOM   1368 C CZ  . PHE   A 1 177 ? 6.133   -20.149 -23.681 1.00 43.43  ? 173 PHE   A CZ  1 
ATOM   1369 N N   . ASN   A 1 178 ? -0.274  -20.335 -27.341 1.00 35.82  ? 174 ASN   A N   1 
ATOM   1370 C CA  . ASN   A 1 178 ? -1.163  -20.674 -28.445 1.00 46.37  ? 174 ASN   A CA  1 
ATOM   1371 C C   . ASN   A 1 178 ? -2.597  -20.747 -27.935 1.00 49.60  ? 174 ASN   A C   1 
ATOM   1372 O O   . ASN   A 1 178 ? -2.868  -20.576 -26.743 1.00 47.45  ? 174 ASN   A O   1 
ATOM   1373 C CB  . ASN   A 1 178 ? -0.741  -21.991 -29.101 1.00 36.23  ? 174 ASN   A CB  1 
ATOM   1374 C CG  . ASN   A 1 178 ? -0.450  -23.078 -28.088 1.00 41.36  ? 174 ASN   A CG  1 
ATOM   1375 O OD1 . ASN   A 1 178 ? -1.346  -23.539 -27.381 1.00 42.35  ? 174 ASN   A OD1 1 
ATOM   1376 N ND2 . ASN   A 1 178 ? 0.809   -23.492 -28.009 1.00 43.04  ? 174 ASN   A ND2 1 
ATOM   1377 N N   . GLN   A 1 179 ? -3.519  -21.007 -28.867 1.00 43.94  ? 175 GLN   A N   1 
ATOM   1378 C CA  . GLN   A 1 179 ? -4.932  -21.127 -28.525 1.00 51.08  ? 175 GLN   A CA  1 
ATOM   1379 C C   . GLN   A 1 179 ? -5.189  -22.309 -27.600 1.00 44.96  ? 175 GLN   A C   1 
ATOM   1380 O O   . GLN   A 1 179 ? -6.081  -22.246 -26.746 1.00 54.70  ? 175 GLN   A O   1 
ATOM   1381 C CB  . GLN   A 1 179 ? -5.761  -21.258 -29.805 1.00 53.54  ? 175 GLN   A CB  1 
ATOM   1382 C CG  . GLN   A 1 179 ? -7.255  -21.440 -29.589 1.00 63.23  ? 175 GLN   A CG  1 
ATOM   1383 C CD  . GLN   A 1 179 ? -7.873  -20.312 -28.790 1.00 61.44  ? 175 GLN   A CD  1 
ATOM   1384 O OE1 . GLN   A 1 179 ? -8.403  -20.527 -27.700 1.00 67.33  ? 175 GLN   A OE1 1 
ATOM   1385 N NE2 . GLN   A 1 179 ? -7.806  -19.099 -29.327 1.00 65.93  ? 175 GLN   A NE2 1 
ATOM   1386 N N   . GLU   A 1 180 ? -4.418  -23.389 -27.749 1.00 39.54  ? 176 GLU   A N   1 
ATOM   1387 C CA  . GLU   A 1 180 ? -4.613  -24.566 -26.907 1.00 44.83  ? 176 GLU   A CA  1 
ATOM   1388 C C   . GLU   A 1 180 ? -4.297  -24.279 -25.445 1.00 57.43  ? 176 GLU   A C   1 
ATOM   1389 O O   . GLU   A 1 180 ? -4.835  -24.946 -24.554 1.00 59.52  ? 176 GLU   A O   1 
ATOM   1390 C CB  . GLU   A 1 180 ? -3.745  -25.722 -27.407 1.00 48.59  ? 176 GLU   A CB  1 
ATOM   1391 C CG  . GLU   A 1 180 ? -4.370  -26.558 -28.511 1.00 53.92  ? 176 GLU   A CG  1 
ATOM   1392 C CD  . GLU   A 1 180 ? -3.982  -26.081 -29.898 1.00 80.50  ? 176 GLU   A CD  1 
ATOM   1393 O OE1 . GLU   A 1 180 ? -3.812  -24.857 -30.083 1.00 77.19  ? 176 GLU   A OE1 1 
ATOM   1394 O OE2 . GLU   A 1 180 ? -3.841  -26.931 -30.802 1.00 88.09  ? 176 GLU   A OE2 1 
ATOM   1395 N N   . GLY   A 1 181 ? -3.437  -23.301 -25.177 1.00 48.54  ? 177 GLY   A N   1 
ATOM   1396 C CA  . GLY   A 1 181 ? -2.962  -23.029 -23.838 1.00 54.50  ? 177 GLY   A CA  1 
ATOM   1397 C C   . GLY   A 1 181 ? -3.748  -22.012 -23.042 1.00 53.03  ? 177 GLY   A C   1 
ATOM   1398 O O   . GLY   A 1 181 ? -3.275  -21.583 -21.984 1.00 56.04  ? 177 GLY   A O   1 
ATOM   1399 N N   . LEU   A 1 182 ? -4.933  -21.609 -23.507 1.00 46.39  ? 178 LEU   A N   1 
ATOM   1400 C CA  . LEU   A 1 182 ? -5.722  -20.635 -22.762 1.00 49.04  ? 178 LEU   A CA  1 
ATOM   1401 C C   . LEU   A 1 182 ? -6.297  -21.214 -21.476 1.00 51.66  ? 178 LEU   A C   1 
ATOM   1402 O O   . LEU   A 1 182 ? -6.674  -20.449 -20.582 1.00 44.10  ? 178 LEU   A O   1 
ATOM   1403 C CB  . LEU   A 1 182 ? -6.851  -20.082 -23.633 1.00 43.55  ? 178 LEU   A CB  1 
ATOM   1404 C CG  . LEU   A 1 182 ? -6.570  -18.767 -24.366 1.00 52.74  ? 178 LEU   A CG  1 
ATOM   1405 C CD1 . LEU   A 1 182 ? -6.383  -17.627 -23.373 1.00 54.24  ? 178 LEU   A CD1 1 
ATOM   1406 C CD2 . LEU   A 1 182 ? -5.363  -18.889 -25.281 1.00 53.42  ? 178 LEU   A CD2 1 
ATOM   1407 N N   . ASN   A 1 183 ? -6.371  -22.543 -21.360 1.00 49.42  ? 179 ASN   A N   1 
ATOM   1408 C CA  . ASN   A 1 183 ? -6.844  -23.155 -20.123 1.00 57.86  ? 179 ASN   A CA  1 
ATOM   1409 C C   . ASN   A 1 183 ? -5.895  -22.905 -18.959 1.00 61.92  ? 179 ASN   A C   1 
ATOM   1410 O O   . ASN   A 1 183 ? -6.291  -23.083 -17.802 1.00 57.97  ? 179 ASN   A O   1 
ATOM   1411 C CB  . ASN   A 1 183 ? -7.045  -24.659 -20.320 1.00 56.45  ? 179 ASN   A CB  1 
ATOM   1412 C CG  . ASN   A 1 183 ? -5.750  -25.386 -20.627 1.00 70.91  ? 179 ASN   A CG  1 
ATOM   1413 O OD1 . ASN   A 1 183 ? -4.851  -24.836 -21.263 1.00 68.12  ? 179 ASN   A OD1 1 
ATOM   1414 N ND2 . ASN   A 1 183 ? -5.650  -26.631 -20.177 1.00 71.67  ? 179 ASN   A ND2 1 
ATOM   1415 N N   . ALA   A 1 184 ? -4.654  -22.497 -19.238 1.00 60.46  ? 180 ALA   A N   1 
ATOM   1416 C CA  . ALA   A 1 184 ? -3.723  -22.140 -18.176 1.00 54.64  ? 180 ALA   A CA  1 
ATOM   1417 C C   . ALA   A 1 184 ? -4.122  -20.854 -17.467 1.00 56.50  ? 180 ALA   A C   1 
ATOM   1418 O O   . ALA   A 1 184 ? -3.713  -20.642 -16.320 1.00 51.30  ? 180 ALA   A O   1 
ATOM   1419 C CB  . ALA   A 1 184 ? -2.310  -22.005 -18.743 1.00 60.66  ? 180 ALA   A CB  1 
ATOM   1420 N N   . ILE   A 1 185 ? -4.903  -19.993 -18.123 1.00 54.53  ? 181 ILE   A N   1 
ATOM   1421 C CA  . ILE   A 1 185 ? -5.367  -18.768 -17.485 1.00 55.54  ? 181 ILE   A CA  1 
ATOM   1422 C C   . ILE   A 1 185 ? -6.286  -19.124 -16.327 1.00 44.74  ? 181 ILE   A C   1 
ATOM   1423 O O   . ILE   A 1 185 ? -7.167  -19.983 -16.453 1.00 45.37  ? 181 ILE   A O   1 
ATOM   1424 C CB  . ILE   A 1 185 ? -6.087  -17.871 -18.504 1.00 47.74  ? 181 ILE   A CB  1 
ATOM   1425 C CG1 . ILE   A 1 185 ? -5.176  -17.544 -19.689 1.00 47.33  ? 181 ILE   A CG1 1 
ATOM   1426 C CG2 . ILE   A 1 185 ? -6.550  -16.585 -17.840 1.00 53.58  ? 181 ILE   A CG2 1 
ATOM   1427 C CD1 . ILE   A 1 185 ? -3.922  -16.805 -19.312 1.00 58.96  ? 181 ILE   A CD1 1 
ATOM   1428 N N   . GLN   A 1 186 ? -6.082  -18.470 -15.186 1.00 51.91  ? 182 GLN   A N   1 
ATOM   1429 C CA  . GLN   A 1 186 ? -6.959  -18.623 -14.026 1.00 65.26  ? 182 GLN   A CA  1 
ATOM   1430 C C   . GLN   A 1 186 ? -7.453  -17.247 -13.595 1.00 54.94  ? 182 GLN   A C   1 
ATOM   1431 O O   . GLN   A 1 186 ? -6.738  -16.513 -12.890 1.00 53.18  ? 182 GLN   A O   1 
ATOM   1432 C CB  . GLN   A 1 186 ? -6.254  -19.363 -12.891 1.00 62.05  ? 182 GLN   A CB  1 
ATOM   1433 C CG  . GLN   A 1 186 ? -4.838  -18.901 -12.580 1.00 68.87  ? 182 GLN   A CG  1 
ATOM   1434 C CD  . GLN   A 1 186 ? -4.005  -19.990 -11.925 1.00 60.08  ? 182 GLN   A CD  1 
ATOM   1435 O OE1 . GLN   A 1 186 ? -4.455  -21.126 -11.774 1.00 53.63  ? 182 GLN   A OE1 1 
ATOM   1436 N NE2 . GLN   A 1 186 ? -2.788  -19.643 -11.525 1.00 70.70  ? 182 GLN   A NE2 1 
ATOM   1437 N N   . PRO   A 1 187 ? -8.653  -16.856 -14.015 1.00 62.37  ? 183 PRO   A N   1 
ATOM   1438 C CA  . PRO   A 1 187 ? -9.142  -15.494 -13.754 1.00 54.26  ? 183 PRO   A CA  1 
ATOM   1439 C C   . PRO   A 1 187 ? -9.687  -15.361 -12.343 1.00 56.24  ? 183 PRO   A C   1 
ATOM   1440 O O   . PRO   A 1 187 ? -9.956  -16.372 -11.678 1.00 57.19  ? 183 PRO   A O   1 
ATOM   1441 C CB  . PRO   A 1 187 ? -10.260 -15.321 -14.797 1.00 63.00  ? 183 PRO   A CB  1 
ATOM   1442 C CG  . PRO   A 1 187 ? -10.004 -16.379 -15.827 1.00 66.64  ? 183 PRO   A CG  1 
ATOM   1443 C CD  . PRO   A 1 187 ? -9.444  -17.530 -15.056 1.00 53.63  ? 183 PRO   A CD  1 
ATOM   1444 N N   . PRO   A 1 188 ? -9.873  -14.124 -11.842 1.00 61.90  ? 184 PRO   A N   1 
ATOM   1445 C CA  . PRO   A 1 188 ? -9.519  -12.851 -12.487 1.00 61.97  ? 184 PRO   A CA  1 
ATOM   1446 C C   . PRO   A 1 188 ? -8.021  -12.581 -12.425 1.00 53.46  ? 184 PRO   A C   1 
ATOM   1447 O O   . PRO   A 1 188 ? -7.397  -12.823 -11.393 1.00 56.39  ? 184 PRO   A O   1 
ATOM   1448 C CB  . PRO   A 1 188 ? -10.298 -11.814 -11.674 1.00 56.11  ? 184 PRO   A CB  1 
ATOM   1449 C CG  . PRO   A 1 188 ? -10.455 -12.433 -10.337 1.00 64.00  ? 184 PRO   A CG  1 
ATOM   1450 C CD  . PRO   A 1 188 ? -10.578 -13.913 -10.566 1.00 56.75  ? 184 PRO   A CD  1 
ATOM   1451 N N   . CYS   A 1 189 ? -7.453  -12.083 -13.520 1.00 52.00  ? 185 CYS   A N   1 
ATOM   1452 C CA  . CYS   A 1 189 ? -6.009  -11.949 -13.629 1.00 47.64  ? 185 CYS   A CA  1 
ATOM   1453 C C   . CYS   A 1 189 ? -5.677  -10.762 -14.522 1.00 45.88  ? 185 CYS   A C   1 
ATOM   1454 O O   . CYS   A 1 189 ? -6.561  -10.087 -15.055 1.00 46.76  ? 185 CYS   A O   1 
ATOM   1455 C CB  . CYS   A 1 189 ? -5.387  -13.235 -14.178 1.00 58.62  ? 185 CYS   A CB  1 
ATOM   1456 S SG  . CYS   A 1 189 ? -5.873  -13.594 -15.881 1.00 50.22  ? 185 CYS   A SG  1 
ATOM   1457 N N   . VAL   A 1 190 ? -4.379  -10.518 -14.680 1.00 41.40  ? 186 VAL   A N   1 
ATOM   1458 C CA  . VAL   A 1 190 ? -3.854  -9.496  -15.576 1.00 42.12  ? 186 VAL   A CA  1 
ATOM   1459 C C   . VAL   A 1 190 ? -2.978  -10.189 -16.609 1.00 37.97  ? 186 VAL   A C   1 
ATOM   1460 O O   . VAL   A 1 190 ? -2.078  -10.956 -16.251 1.00 47.16  ? 186 VAL   A O   1 
ATOM   1461 C CB  . VAL   A 1 190 ? -3.057  -8.422  -14.813 1.00 51.25  ? 186 VAL   A CB  1 
ATOM   1462 C CG1 . VAL   A 1 190 ? -2.157  -7.647  -15.765 1.00 36.87  ? 186 VAL   A CG1 1 
ATOM   1463 C CG2 . VAL   A 1 190 ? -4.000  -7.481  -14.080 1.00 48.85  ? 186 VAL   A CG2 1 
ATOM   1464 N N   . VAL   A 1 191 ? -3.249  -9.929  -17.884 1.00 37.54  ? 187 VAL   A N   1 
ATOM   1465 C CA  . VAL   A 1 191 ? -2.470  -10.489 -18.979 1.00 33.80  ? 187 VAL   A CA  1 
ATOM   1466 C C   . VAL   A 1 191 ? -1.635  -9.380  -19.603 1.00 36.84  ? 187 VAL   A C   1 
ATOM   1467 O O   . VAL   A 1 191 ? -2.052  -8.217  -19.666 1.00 37.51  ? 187 VAL   A O   1 
ATOM   1468 C CB  . VAL   A 1 191 ? -3.369  -11.174 -20.029 1.00 31.24  ? 187 VAL   A CB  1 
ATOM   1469 C CG1 . VAL   A 1 191 ? -3.857  -12.514 -19.505 1.00 37.63  ? 187 VAL   A CG1 1 
ATOM   1470 C CG2 . VAL   A 1 191 ? -4.551  -10.290 -20.366 1.00 34.18  ? 187 VAL   A CG2 1 
ATOM   1471 N N   . GLN   A 1 192 ? -0.441  -9.749  -20.062 1.00 37.00  ? 188 GLN   A N   1 
ATOM   1472 C CA  . GLN   A 1 192 ? 0.530   -8.786  -20.560 1.00 36.91  ? 188 GLN   A CA  1 
ATOM   1473 C C   . GLN   A 1 192 ? 1.373   -9.445  -21.641 1.00 36.05  ? 188 GLN   A C   1 
ATOM   1474 O O   . GLN   A 1 192 ? 1.797   -10.593 -21.490 1.00 29.50  ? 188 GLN   A O   1 
ATOM   1475 C CB  . GLN   A 1 192 ? 1.423   -8.275  -19.424 1.00 31.86  ? 188 GLN   A CB  1 
ATOM   1476 C CG  . GLN   A 1 192 ? 2.290   -7.081  -19.778 1.00 26.60  ? 188 GLN   A CG  1 
ATOM   1477 C CD  . GLN   A 1 192 ? 3.360   -6.821  -18.733 1.00 40.37  ? 188 GLN   A CD  1 
ATOM   1478 O OE1 . GLN   A 1 192 ? 4.016   -7.748  -18.258 1.00 33.84  ? 188 GLN   A OE1 1 
ATOM   1479 N NE2 . GLN   A 1 192 ? 3.536   -5.557  -18.365 1.00 32.30  ? 188 GLN   A NE2 1 
ATOM   1480 N N   . ASN   A 1 193 ? 1.615   -8.708  -22.725 1.00 31.15  ? 189 ASN   A N   1 
ATOM   1481 C CA  . ASN   A 1 193 ? 2.402   -9.235  -23.834 1.00 38.34  ? 189 ASN   A CA  1 
ATOM   1482 C C   . ASN   A 1 193 ? 3.807   -9.600  -23.374 1.00 36.13  ? 189 ASN   A C   1 
ATOM   1483 O O   . ASN   A 1 193 ? 4.478   -8.814  -22.698 1.00 30.33  ? 189 ASN   A O   1 
ATOM   1484 C CB  . ASN   A 1 193 ? 2.471   -8.210  -24.966 1.00 37.70  ? 189 ASN   A CB  1 
ATOM   1485 C CG  . ASN   A 1 193 ? 1.405   -8.431  -26.017 1.00 44.06  ? 189 ASN   A CG  1 
ATOM   1486 O OD1 . ASN   A 1 193 ? 0.552   -9.305  -25.875 1.00 37.23  ? 189 ASN   A OD1 1 
ATOM   1487 N ND2 . ASN   A 1 193 ? 1.449   -7.638  -27.082 1.00 43.54  ? 189 ASN   A ND2 1 
ATOM   1488 N N   . PHE   A 1 194 ? 4.250   -10.801 -23.741 1.00 37.04  ? 190 PHE   A N   1 
ATOM   1489 C CA  . PHE   A 1 194 ? 5.603   -11.238 -23.429 1.00 34.76  ? 190 PHE   A CA  1 
ATOM   1490 C C   . PHE   A 1 194 ? 6.582   -10.618 -24.417 1.00 34.91  ? 190 PHE   A C   1 
ATOM   1491 O O   . PHE   A 1 194 ? 6.384   -10.698 -25.634 1.00 34.78  ? 190 PHE   A O   1 
ATOM   1492 C CB  . PHE   A 1 194 ? 5.702   -12.763 -23.470 1.00 35.44  ? 190 PHE   A CB  1 
ATOM   1493 C CG  . PHE   A 1 194 ? 7.103   -13.284 -23.306 1.00 39.75  ? 190 PHE   A CG  1 
ATOM   1494 C CD1 . PHE   A 1 194 ? 7.664   -13.411 -22.046 1.00 35.08  ? 190 PHE   A CD1 1 
ATOM   1495 C CD2 . PHE   A 1 194 ? 7.859   -13.648 -24.409 1.00 38.09  ? 190 PHE   A CD2 1 
ATOM   1496 C CE1 . PHE   A 1 194 ? 8.953   -13.888 -21.889 1.00 35.39  ? 190 PHE   A CE1 1 
ATOM   1497 C CE2 . PHE   A 1 194 ? 9.148   -14.125 -24.257 1.00 43.58  ? 190 PHE   A CE2 1 
ATOM   1498 C CZ  . PHE   A 1 194 ? 9.695   -14.245 -22.995 1.00 31.66  ? 190 PHE   A CZ  1 
ATOM   1499 N N   . ILE   A 1 195 ? 7.638   -10.005 -23.894 1.00 34.00  ? 191 ILE   A N   1 
ATOM   1500 C CA  . ILE   A 1 195 ? 8.636   -9.315  -24.703 1.00 36.17  ? 191 ILE   A CA  1 
ATOM   1501 C C   . ILE   A 1 195 ? 9.929   -10.117 -24.654 1.00 34.98  ? 191 ILE   A C   1 
ATOM   1502 O O   . ILE   A 1 195 ? 10.464  -10.381 -23.570 1.00 35.86  ? 191 ILE   A O   1 
ATOM   1503 C CB  . ILE   A 1 195 ? 8.866   -7.877  -24.214 1.00 31.34  ? 191 ILE   A CB  1 
ATOM   1504 C CG1 . ILE   A 1 195 ? 7.555   -7.089  -24.227 1.00 35.29  ? 191 ILE   A CG1 1 
ATOM   1505 C CG2 . ILE   A 1 195 ? 9.919   -7.187  -25.069 1.00 38.25  ? 191 ILE   A CG2 1 
ATOM   1506 C CD1 . ILE   A 1 195 ? 6.974   -6.892  -25.609 1.00 40.86  ? 191 ILE   A CD1 1 
ATOM   1507 N N   . ASN   A 1 196 ? 10.426  -10.509 -25.826 1.00 34.14  ? 192 ASN   A N   1 
ATOM   1508 C CA  . ASN   A 1 196 ? 11.750  -11.110 -25.907 1.00 37.43  ? 192 ASN   A CA  1 
ATOM   1509 C C   . ASN   A 1 196 ? 12.800  -10.089 -25.489 1.00 35.85  ? 192 ASN   A C   1 
ATOM   1510 O O   . ASN   A 1 196 ? 12.815  -8.959  -25.985 1.00 32.19  ? 192 ASN   A O   1 
ATOM   1511 C CB  . ASN   A 1 196 ? 12.027  -11.606 -27.326 1.00 34.59  ? 192 ASN   A CB  1 
ATOM   1512 C CG  . ASN   A 1 196 ? 11.314  -12.907 -27.642 1.00 37.95  ? 192 ASN   A CG  1 
ATOM   1513 O OD1 . ASN   A 1 196 ? 11.055  -13.719 -26.754 1.00 36.85  ? 192 ASN   A OD1 1 
ATOM   1514 N ND2 . ASN   A 1 196 ? 10.996  -13.113 -28.915 1.00 34.69  ? 192 ASN   A ND2 1 
ATOM   1515 N N   . HIS   A 1 197 ? 13.679  -10.486 -24.565 1.00 33.85  ? 193 HIS   A N   1 
ATOM   1516 C CA  . HIS   A 1 197 ? 14.653  -9.547  -24.023 1.00 37.16  ? 193 HIS   A CA  1 
ATOM   1517 C C   . HIS   A 1 197 ? 15.997  -10.202 -23.721 1.00 33.48  ? 193 HIS   A C   1 
ATOM   1518 O O   . HIS   A 1 197 ? 16.762  -9.672  -22.906 1.00 33.79  ? 193 HIS   A O   1 
ATOM   1519 C CB  . HIS   A 1 197 ? 14.107  -8.883  -22.755 1.00 28.57  ? 193 HIS   A CB  1 
ATOM   1520 C CG  . HIS   A 1 197 ? 13.664  -9.855  -21.708 1.00 28.43  ? 193 HIS   A CG  1 
ATOM   1521 N ND1 . HIS   A 1 197 ? 12.503  -10.590 -21.816 1.00 29.42  ? 193 HIS   A ND1 1 
ATOM   1522 C CD2 . HIS   A 1 197 ? 14.229  -10.216 -20.531 1.00 30.26  ? 193 HIS   A CD2 1 
ATOM   1523 C CE1 . HIS   A 1 197 ? 12.372  -11.361 -20.751 1.00 33.50  ? 193 HIS   A CE1 1 
ATOM   1524 N NE2 . HIS   A 1 197 ? 13.405  -11.152 -19.956 1.00 35.80  ? 193 HIS   A NE2 1 
ATOM   1525 N N   . ASN   A 1 198 ? 16.296  -11.341 -24.350 1.00 25.24  ? 194 ASN   A N   1 
ATOM   1526 C CA  . ASN   A 1 198 ? 17.581  -12.029 -24.205 1.00 29.49  ? 194 ASN   A CA  1 
ATOM   1527 C C   . ASN   A 1 198 ? 17.864  -12.433 -22.758 1.00 33.91  ? 194 ASN   A C   1 
ATOM   1528 O O   . ASN   A 1 198 ? 19.023  -12.519 -22.344 1.00 34.40  ? 194 ASN   A O   1 
ATOM   1529 C CB  . ASN   A 1 198 ? 18.729  -11.184 -24.766 1.00 26.70  ? 194 ASN   A CB  1 
ATOM   1530 C CG  . ASN   A 1 198 ? 18.683  -11.075 -26.279 1.00 32.29  ? 194 ASN   A CG  1 
ATOM   1531 O OD1 . ASN   A 1 198 ? 18.583  -12.081 -26.981 1.00 30.74  ? 194 ASN   A OD1 1 
ATOM   1532 N ND2 . ASN   A 1 198 ? 18.748  -9.851  -26.789 1.00 38.38  ? 194 ASN   A ND2 1 
ATOM   1533 N N   . ALA   A 1 199 ? 16.801  -12.672 -21.985 1.00 27.42  ? 195 ALA   A N   1 
ATOM   1534 C CA  . ALA   A 1 199 ? 16.893  -13.301 -20.664 1.00 32.45  ? 195 ALA   A CA  1 
ATOM   1535 C C   . ALA   A 1 199 ? 17.751  -12.493 -19.692 1.00 31.77  ? 195 ALA   A C   1 
ATOM   1536 O O   . ALA   A 1 199 ? 18.483  -13.051 -18.873 1.00 35.62  ? 195 ALA   A O   1 
ATOM   1537 C CB  . ALA   A 1 199 ? 17.411  -14.737 -20.775 1.00 30.42  ? 195 ALA   A CB  1 
ATOM   1538 N N   . VAL   A 1 200 ? 17.658  -11.168 -19.771 1.00 30.66  ? 196 VAL   A N   1 
ATOM   1539 C CA  . VAL   A 1 200 ? 18.352  -10.280 -18.845 1.00 38.94  ? 196 VAL   A CA  1 
ATOM   1540 C C   . VAL   A 1 200 ? 17.336  -9.296  -18.282 1.00 43.46  ? 196 VAL   A C   1 
ATOM   1541 O O   . VAL   A 1 200 ? 16.701  -8.553  -19.039 1.00 31.96  ? 196 VAL   A O   1 
ATOM   1542 C CB  . VAL   A 1 200 ? 19.517  -9.531  -19.515 1.00 39.33  ? 196 VAL   A CB  1 
ATOM   1543 C CG1 . VAL   A 1 200 ? 20.171  -8.585  -18.523 1.00 39.30  ? 196 VAL   A CG1 1 
ATOM   1544 C CG2 . VAL   A 1 200 ? 20.541  -10.516 -20.061 1.00 43.76  ? 196 VAL   A CG2 1 
ATOM   1545 N N   . LEU   A 1 201 ? 17.180  -9.296  -16.961 1.00 30.76  ? 197 LEU   A N   1 
ATOM   1546 C CA  . LEU   A 1 201 ? 16.279  -8.387  -16.268 1.00 28.47  ? 197 LEU   A CA  1 
ATOM   1547 C C   . LEU   A 1 201 ? 17.098  -7.389  -15.463 1.00 35.60  ? 197 LEU   A C   1 
ATOM   1548 O O   . LEU   A 1 201 ? 17.978  -7.781  -14.690 1.00 36.08  ? 197 LEU   A O   1 
ATOM   1549 C CB  . LEU   A 1 201 ? 15.322  -9.151  -15.351 1.00 35.33  ? 197 LEU   A CB  1 
ATOM   1550 C CG  . LEU   A 1 201 ? 14.545  -8.314  -14.330 1.00 39.09  ? 197 LEU   A CG  1 
ATOM   1551 C CD1 . LEU   A 1 201 ? 13.480  -7.473  -15.017 1.00 39.89  ? 197 LEU   A CD1 1 
ATOM   1552 C CD2 . LEU   A 1 201 ? 13.921  -9.202  -13.266 1.00 39.68  ? 197 LEU   A CD2 1 
ATOM   1553 N N   . TYR   A 1 202 ? 16.809  -6.103  -15.648 1.00 30.78  ? 198 TYR   A N   1 
ATOM   1554 C CA  . TYR   A 1 202 ? 17.491  -5.029  -14.932 1.00 30.61  ? 198 TYR   A CA  1 
ATOM   1555 C C   . TYR   A 1 202 ? 16.553  -4.520  -13.842 1.00 38.31  ? 198 TYR   A C   1 
ATOM   1556 O O   . TYR   A 1 202 ? 15.593  -3.797  -14.120 1.00 35.59  ? 198 TYR   A O   1 
ATOM   1557 C CB  . TYR   A 1 202 ? 17.902  -3.912  -15.886 1.00 30.37  ? 198 TYR   A CB  1 
ATOM   1558 C CG  . TYR   A 1 202 ? 18.799  -4.369  -17.017 1.00 35.61  ? 198 TYR   A CG  1 
ATOM   1559 C CD1 . TYR   A 1 202 ? 20.166  -4.528  -16.825 1.00 29.76  ? 198 TYR   A CD1 1 
ATOM   1560 C CD2 . TYR   A 1 202 ? 18.279  -4.638  -18.276 1.00 28.58  ? 198 TYR   A CD2 1 
ATOM   1561 C CE1 . TYR   A 1 202 ? 20.989  -4.946  -17.855 1.00 38.26  ? 198 TYR   A CE1 1 
ATOM   1562 C CE2 . TYR   A 1 202 ? 19.095  -5.055  -19.312 1.00 36.53  ? 198 TYR   A CE2 1 
ATOM   1563 C CZ  . TYR   A 1 202 ? 20.449  -5.206  -19.097 1.00 37.20  ? 198 TYR   A CZ  1 
ATOM   1564 O OH  . TYR   A 1 202 ? 21.263  -5.621  -20.126 1.00 48.55  ? 198 TYR   A OH  1 
ATOM   1565 N N   . LYS   A 1 203 ? 16.832  -4.903  -12.600 1.00 34.39  ? 199 LYS   A N   1 
ATOM   1566 C CA  . LYS   A 1 203 ? 16.037  -4.471  -11.458 1.00 38.94  ? 199 LYS   A CA  1 
ATOM   1567 C C   . LYS   A 1 203 ? 16.619  -3.175  -10.906 1.00 41.40  ? 199 LYS   A C   1 
ATOM   1568 O O   . LYS   A 1 203 ? 17.755  -3.156  -10.419 1.00 38.29  ? 199 LYS   A O   1 
ATOM   1569 C CB  . LYS   A 1 203 ? 16.004  -5.554  -10.380 1.00 44.78  ? 199 LYS   A CB  1 
ATOM   1570 C CG  . LYS   A 1 203 ? 15.110  -6.736  -10.720 1.00 54.47  ? 199 LYS   A CG  1 
ATOM   1571 C CD  . LYS   A 1 203 ? 15.190  -7.822  -9.659  1.00 47.34  ? 199 LYS   A CD  1 
ATOM   1572 C CE  . LYS   A 1 203 ? 14.369  -7.459  -8.432  1.00 55.51  ? 199 LYS   A CE  1 
ATOM   1573 N NZ  . LYS   A 1 203 ? 12.920  -7.331  -8.750  1.00 44.07  ? 199 LYS   A NZ  1 
ATOM   1574 N N   . VAL   A 1 204 ? 15.844  -2.099  -10.986 1.00 36.68  ? 200 VAL   A N   1 
ATOM   1575 C CA  . VAL   A 1 204 ? 16.263  -0.782  -10.520 1.00 35.59  ? 200 VAL   A CA  1 
ATOM   1576 C C   . VAL   A 1 204 ? 15.673  -0.572  -9.132  1.00 40.32  ? 200 VAL   A C   1 
ATOM   1577 O O   . VAL   A 1 204 ? 14.453  -0.463  -8.976  1.00 38.95  ? 200 VAL   A O   1 
ATOM   1578 C CB  . VAL   A 1 204 ? 15.823  0.325   -11.486 1.00 40.38  ? 200 VAL   A CB  1 
ATOM   1579 C CG1 . VAL   A 1 204 ? 16.132  1.696   -10.901 1.00 36.84  ? 200 VAL   A CG1 1 
ATOM   1580 C CG2 . VAL   A 1 204 ? 16.498  0.149   -12.838 1.00 34.60  ? 200 VAL   A CG2 1 
ATOM   1581 N N   . PHE   A 1 205 ? 16.537  -0.512  -8.121  1.00 31.07  ? 201 PHE   A N   1 
ATOM   1582 C CA  . PHE   A 1 205 ? 16.124  -0.296  -6.739  1.00 33.59  ? 201 PHE   A CA  1 
ATOM   1583 C C   . PHE   A 1 205 ? 16.338  1.170   -6.382  1.00 39.54  ? 201 PHE   A C   1 
ATOM   1584 O O   . PHE   A 1 205 ? 17.468  1.665   -6.435  1.00 33.48  ? 201 PHE   A O   1 
ATOM   1585 C CB  . PHE   A 1 205 ? 16.910  -1.200  -5.790  1.00 31.57  ? 201 PHE   A CB  1 
ATOM   1586 C CG  . PHE   A 1 205 ? 16.496  -2.644  -5.843  1.00 36.73  ? 201 PHE   A CG  1 
ATOM   1587 C CD1 . PHE   A 1 205 ? 15.390  -3.089  -5.139  1.00 38.64  ? 201 PHE   A CD1 1 
ATOM   1588 C CD2 . PHE   A 1 205 ? 17.216  -3.557  -6.595  1.00 34.09  ? 201 PHE   A CD2 1 
ATOM   1589 C CE1 . PHE   A 1 205 ? 15.010  -4.417  -5.182  1.00 41.12  ? 201 PHE   A CE1 1 
ATOM   1590 C CE2 . PHE   A 1 205 ? 16.841  -4.887  -6.641  1.00 38.06  ? 201 PHE   A CE2 1 
ATOM   1591 C CZ  . PHE   A 1 205 ? 15.736  -5.317  -5.934  1.00 41.83  ? 201 PHE   A CZ  1 
ATOM   1592 N N   . VAL   A 1 206 ? 15.259  1.856   -6.011  1.00 39.26  ? 202 VAL   A N   1 
ATOM   1593 C CA  . VAL   A 1 206 ? 15.284  3.288   -5.736  1.00 38.02  ? 202 VAL   A CA  1 
ATOM   1594 C C   . VAL   A 1 206 ? 15.108  3.509   -4.240  1.00 36.15  ? 202 VAL   A C   1 
ATOM   1595 O O   . VAL   A 1 206 ? 14.175  2.972   -3.631  1.00 41.57  ? 202 VAL   A O   1 
ATOM   1596 C CB  . VAL   A 1 206 ? 14.197  4.033   -6.529  1.00 38.87  ? 202 VAL   A CB  1 
ATOM   1597 C CG1 . VAL   A 1 206 ? 14.270  5.528   -6.254  1.00 40.61  ? 202 VAL   A CG1 1 
ATOM   1598 C CG2 . VAL   A 1 206 ? 14.335  3.750   -8.018  1.00 34.22  ? 202 VAL   A CG2 1 
ATOM   1599 N N   . VAL   A 1 207 ? 16.007  4.296   -3.652  1.00 35.78  ? 203 VAL   A N   1 
ATOM   1600 C CA  . VAL   A 1 207 ? 15.902  4.730   -2.258  1.00 42.18  ? 203 VAL   A CA  1 
ATOM   1601 C C   . VAL   A 1 207 ? 16.081  6.246   -2.276  1.00 45.24  ? 203 VAL   A C   1 
ATOM   1602 O O   . VAL   A 1 207 ? 17.205  6.757   -2.211  1.00 43.38  ? 203 VAL   A O   1 
ATOM   1603 C CB  . VAL   A 1 207 ? 16.932  4.058   -1.343  1.00 42.99  ? 203 VAL   A CB  1 
ATOM   1604 C CG1 . VAL   A 1 207 ? 16.802  4.583   0.081   1.00 41.91  ? 203 VAL   A CG1 1 
ATOM   1605 C CG2 . VAL   A 1 207 ? 16.765  2.551   -1.370  1.00 37.28  ? 203 VAL   A CG2 1 
ATOM   1606 N N   . GLY   A 1 208 ? 14.974  6.975   -2.375  1.00 45.44  ? 204 GLY   A N   1 
ATOM   1607 C CA  . GLY   A 1 208 ? 15.037  8.418   -2.489  1.00 41.72  ? 204 GLY   A CA  1 
ATOM   1608 C C   . GLY   A 1 208 ? 15.630  8.864   -3.810  1.00 55.19  ? 204 GLY   A C   1 
ATOM   1609 O O   . GLY   A 1 208 ? 15.082  8.569   -4.876  1.00 45.09  ? 204 GLY   A O   1 
ATOM   1610 N N   . GLU   A 1 209 ? 16.758  9.572   -3.753  1.00 49.72  ? 205 GLU   A N   1 
ATOM   1611 C CA  . GLU   A 1 209 ? 17.419  10.046  -4.963  1.00 58.28  ? 205 GLU   A CA  1 
ATOM   1612 C C   . GLU   A 1 209 ? 18.404  9.027   -5.523  1.00 61.54  ? 205 GLU   A C   1 
ATOM   1613 O O   . GLU   A 1 209 ? 18.526  8.893   -6.745  1.00 70.95  ? 205 GLU   A O   1 
ATOM   1614 C CB  . GLU   A 1 209 ? 18.138  11.369  -4.684  1.00 76.85  ? 205 GLU   A CB  1 
ATOM   1615 C CG  . GLU   A 1 209 ? 17.198  12.547  -4.484  1.00 79.50  ? 205 GLU   A CG  1 
ATOM   1616 C CD  . GLU   A 1 209 ? 17.935  13.842  -4.210  1.00 109.40 ? 205 GLU   A CD  1 
ATOM   1617 O OE1 . GLU   A 1 209 ? 19.174  13.801  -4.057  1.00 116.10 ? 205 GLU   A OE1 1 
ATOM   1618 O OE2 . GLU   A 1 209 ? 17.276  14.901  -4.150  1.00 108.00 ? 205 GLU   A OE2 1 
ATOM   1619 N N   . SER   A 1 210 ? 19.107  8.304   -4.656  1.00 54.52  ? 206 SER   A N   1 
ATOM   1620 C CA  . SER   A 1 210 ? 20.037  7.285   -5.118  1.00 51.85  ? 206 SER   A CA  1 
ATOM   1621 C C   . SER   A 1 210 ? 19.282  6.050   -5.596  1.00 50.77  ? 206 SER   A C   1 
ATOM   1622 O O   . SER   A 1 210 ? 18.226  5.691   -5.067  1.00 48.42  ? 206 SER   A O   1 
ATOM   1623 C CB  . SER   A 1 210 ? 21.012  6.904   -4.004  1.00 56.44  ? 206 SER   A CB  1 
ATOM   1624 O OG  . SER   A 1 210 ? 20.337  6.274   -2.930  1.00 58.09  ? 206 SER   A OG  1 
ATOM   1625 N N   . TYR   A 1 211 ? 19.837  5.396   -6.614  1.00 45.69  ? 207 TYR   A N   1 
ATOM   1626 C CA  . TYR   A 1 211 ? 19.236  4.205   -7.190  1.00 38.67  ? 207 TYR   A CA  1 
ATOM   1627 C C   . TYR   A 1 211 ? 20.331  3.215   -7.554  1.00 41.79  ? 207 TYR   A C   1 
ATOM   1628 O O   . TYR   A 1 211 ? 21.478  3.597   -7.801  1.00 39.36  ? 207 TYR   A O   1 
ATOM   1629 C CB  . TYR   A 1 211 ? 18.394  4.536   -8.431  1.00 43.53  ? 207 TYR   A CB  1 
ATOM   1630 C CG  . TYR   A 1 211 ? 19.204  5.061   -9.592  1.00 40.95  ? 207 TYR   A CG  1 
ATOM   1631 C CD1 . TYR   A 1 211 ? 19.637  6.380   -9.622  1.00 53.26  ? 207 TYR   A CD1 1 
ATOM   1632 C CD2 . TYR   A 1 211 ? 19.542  4.237   -10.657 1.00 44.51  ? 207 TYR   A CD2 1 
ATOM   1633 C CE1 . TYR   A 1 211 ? 20.382  6.864   -10.679 1.00 61.42  ? 207 TYR   A CE1 1 
ATOM   1634 C CE2 . TYR   A 1 211 ? 20.286  4.711   -11.720 1.00 46.86  ? 207 TYR   A CE2 1 
ATOM   1635 C CZ  . TYR   A 1 211 ? 20.702  6.025   -11.725 1.00 55.74  ? 207 TYR   A CZ  1 
ATOM   1636 O OH  . TYR   A 1 211 ? 21.444  6.503   -12.779 1.00 61.27  ? 207 TYR   A OH  1 
ATOM   1637 N N   . THR   A 1 212 ? 19.964  1.936   -7.588  1.00 39.73  ? 208 THR   A N   1 
ATOM   1638 C CA  . THR   A 1 212 ? 20.891  0.860   -7.912  1.00 47.72  ? 208 THR   A CA  1 
ATOM   1639 C C   . THR   A 1 212 ? 20.269  -0.034  -8.973  1.00 42.26  ? 208 THR   A C   1 
ATOM   1640 O O   . THR   A 1 212 ? 19.134  -0.496  -8.812  1.00 43.78  ? 208 THR   A O   1 
ATOM   1641 C CB  . THR   A 1 212 ? 21.246  0.034   -6.670  1.00 53.04  ? 208 THR   A CB  1 
ATOM   1642 O OG1 . THR   A 1 212 ? 21.519  0.913   -5.571  1.00 56.24  ? 208 THR   A OG1 1 
ATOM   1643 C CG2 . THR   A 1 212 ? 22.469  -0.831  -6.938  1.00 53.05  ? 208 THR   A CG2 1 
ATOM   1644 N N   . VAL   A 1 213 ? 21.010  -0.274  -10.050 1.00 36.74  ? 209 VAL   A N   1 
ATOM   1645 C CA  . VAL   A 1 213 ? 20.576  -1.148  -11.133 1.00 37.55  ? 209 VAL   A CA  1 
ATOM   1646 C C   . VAL   A 1 213 ? 21.245  -2.501  -10.941 1.00 47.53  ? 209 VAL   A C   1 
ATOM   1647 O O   . VAL   A 1 213 ? 22.478  -2.604  -10.971 1.00 44.86  ? 209 VAL   A O   1 
ATOM   1648 C CB  . VAL   A 1 213 ? 20.916  -0.552  -12.508 1.00 42.79  ? 209 VAL   A CB  1 
ATOM   1649 C CG1 . VAL   A 1 213 ? 20.277  -1.377  -13.616 1.00 37.11  ? 209 VAL   A CG1 1 
ATOM   1650 C CG2 . VAL   A 1 213 ? 20.462  0.897   -12.584 1.00 29.99  ? 209 VAL   A CG2 1 
ATOM   1651 N N   . VAL   A 1 214 ? 20.437  -3.538  -10.739 1.00 41.27  ? 210 VAL   A N   1 
ATOM   1652 C CA  . VAL   A 1 214 ? 20.924  -4.892  -10.501 1.00 44.85  ? 210 VAL   A CA  1 
ATOM   1653 C C   . VAL   A 1 214 ? 20.499  -5.769  -11.671 1.00 44.51  ? 210 VAL   A C   1 
ATOM   1654 O O   . VAL   A 1 214 ? 19.312  -5.827  -12.015 1.00 45.39  ? 210 VAL   A O   1 
ATOM   1655 C CB  . VAL   A 1 214 ? 20.399  -5.455  -9.169  1.00 54.09  ? 210 VAL   A CB  1 
ATOM   1656 C CG1 . VAL   A 1 214 ? 20.766  -6.923  -9.032  1.00 47.96  ? 210 VAL   A CG1 1 
ATOM   1657 C CG2 . VAL   A 1 214 ? 20.952  -4.651  -8.000  1.00 41.73  ? 210 VAL   A CG2 1 
ATOM   1658 N N   . GLN   A 1 215 ? 21.468  -6.448  -12.278 1.00 41.28  ? 211 GLN   A N   1 
ATOM   1659 C CA  . GLN   A 1 215 ? 21.218  -7.320  -13.417 1.00 48.81  ? 211 GLN   A CA  1 
ATOM   1660 C C   . GLN   A 1 215 ? 20.914  -8.729  -12.921 1.00 43.57  ? 211 GLN   A C   1 
ATOM   1661 O O   . GLN   A 1 215 ? 21.694  -9.305  -12.156 1.00 53.75  ? 211 GLN   A O   1 
ATOM   1662 C CB  . GLN   A 1 215 ? 22.424  -7.321  -14.356 1.00 43.69  ? 211 GLN   A CB  1 
ATOM   1663 C CG  . GLN   A 1 215 ? 22.386  -8.369  -15.448 1.00 47.64  ? 211 GLN   A CG  1 
ATOM   1664 C CD  . GLN   A 1 215 ? 23.364  -8.063  -16.565 1.00 61.58  ? 211 GLN   A CD  1 
ATOM   1665 O OE1 . GLN   A 1 215 ? 23.986  -7.000  -16.586 1.00 58.63  ? 211 GLN   A OE1 1 
ATOM   1666 N NE2 . GLN   A 1 215 ? 23.513  -8.998  -17.496 1.00 62.84  ? 211 GLN   A NE2 1 
ATOM   1667 N N   . ARG   A 1 216 ? 19.787  -9.276  -13.356 1.00 46.28  ? 212 ARG   A N   1 
ATOM   1668 C CA  . ARG   A 1 216 ? 19.258  -10.531 -12.853 1.00 38.85  ? 212 ARG   A CA  1 
ATOM   1669 C C   . ARG   A 1 216 ? 18.921  -11.465 -14.011 1.00 40.33  ? 212 ARG   A C   1 
ATOM   1670 O O   . ARG   A 1 216 ? 18.723  -11.014 -15.141 1.00 38.63  ? 212 ARG   A O   1 
ATOM   1671 C CB  . ARG   A 1 216 ? 18.000  -10.288 -12.006 1.00 39.60  ? 212 ARG   A CB  1 
ATOM   1672 C CG  . ARG   A 1 216 ? 18.244  -9.468  -10.751 1.00 40.82  ? 212 ARG   A CG  1 
ATOM   1673 C CD  . ARG   A 1 216 ? 18.941  -10.295 -9.693  1.00 51.18  ? 212 ARG   A CD  1 
ATOM   1674 N NE  . ARG   A 1 216 ? 18.927  -9.654  -8.382  1.00 62.55  ? 212 ARG   A NE  1 
ATOM   1675 C CZ  . ARG   A 1 216 ? 17.906  -9.708  -7.532  1.00 58.83  ? 212 ARG   A CZ  1 
ATOM   1676 N NH1 . ARG   A 1 216 ? 16.807  -10.376 -7.853  1.00 53.76  ? 212 ARG   A NH1 1 
ATOM   1677 N NH2 . ARG   A 1 216 ? 17.985  -9.094  -6.360  1.00 61.38  ? 212 ARG   A NH2 1 
ATOM   1678 N N   . PRO   A 1 217 ? 18.859  -12.770 -13.752 1.00 39.39  ? 213 PRO   A N   1 
ATOM   1679 C CA  . PRO   A 1 217 ? 18.378  -13.698 -14.784 1.00 38.24  ? 213 PRO   A CA  1 
ATOM   1680 C C   . PRO   A 1 217 ? 16.894  -13.501 -15.051 1.00 35.25  ? 213 PRO   A C   1 
ATOM   1681 O O   . PRO   A 1 217 ? 16.147  -12.977 -14.222 1.00 32.41  ? 213 PRO   A O   1 
ATOM   1682 C CB  . PRO   A 1 217 ? 18.654  -15.083 -14.183 1.00 41.10  ? 213 PRO   A CB  1 
ATOM   1683 C CG  . PRO   A 1 217 ? 19.622  -14.847 -13.064 1.00 48.30  ? 213 PRO   A CG  1 
ATOM   1684 C CD  . PRO   A 1 217 ? 19.326  -13.477 -12.550 1.00 39.72  ? 213 PRO   A CD  1 
ATOM   1685 N N   . SER   A 1 218 ? 16.468  -13.938 -16.235 1.00 32.83  ? 214 SER   A N   1 
ATOM   1686 C CA  . SER   A 1 218 ? 15.093  -13.742 -16.671 1.00 26.70  ? 214 SER   A CA  1 
ATOM   1687 C C   . SER   A 1 218 ? 14.718  -14.835 -17.666 1.00 39.09  ? 214 SER   A C   1 
ATOM   1688 O O   . SER   A 1 218 ? 15.503  -15.745 -17.948 1.00 42.31  ? 214 SER   A O   1 
ATOM   1689 C CB  . SER   A 1 218 ? 14.907  -12.348 -17.275 1.00 32.31  ? 214 SER   A CB  1 
ATOM   1690 O OG  . SER   A 1 218 ? 13.549  -12.110 -17.598 1.00 37.21  ? 214 SER   A OG  1 
ATOM   1691 N N   . LEU   A 1 219 ? 13.502  -14.734 -18.199 1.00 32.93  ? 215 LEU   A N   1 
ATOM   1692 C CA  . LEU   A 1 219 ? 13.002  -15.731 -19.138 1.00 38.73  ? 215 LEU   A CA  1 
ATOM   1693 C C   . LEU   A 1 219 ? 13.730  -15.633 -20.472 1.00 29.92  ? 215 LEU   A C   1 
ATOM   1694 O O   . LEU   A 1 219 ? 13.991  -14.538 -20.978 1.00 29.99  ? 215 LEU   A O   1 
ATOM   1695 C CB  . LEU   A 1 219 ? 11.500  -15.554 -19.359 1.00 31.52  ? 215 LEU   A CB  1 
ATOM   1696 C CG  . LEU   A 1 219 ? 10.564  -15.729 -18.163 1.00 33.72  ? 215 LEU   A CG  1 
ATOM   1697 C CD1 . LEU   A 1 219 ? 9.139   -15.369 -18.554 1.00 42.49  ? 215 LEU   A CD1 1 
ATOM   1698 C CD2 . LEU   A 1 219 ? 10.630  -17.149 -17.632 1.00 38.38  ? 215 LEU   A CD2 1 
ATOM   1699 N N   . LYS   A 1 220 ? 14.038  -16.790 -21.052 1.00 29.54  ? 216 LYS   A N   1 
ATOM   1700 C CA  . LYS   A 1 220 ? 14.733  -16.841 -22.328 1.00 36.37  ? 216 LYS   A CA  1 
ATOM   1701 C C   . LYS   A 1 220 ? 13.805  -16.394 -23.457 1.00 37.43  ? 216 LYS   A C   1 
ATOM   1702 O O   . LYS   A 1 220 ? 12.627  -16.084 -23.255 1.00 28.95  ? 216 LYS   A O   1 
ATOM   1703 C CB  . LYS   A 1 220 ? 15.265  -18.249 -22.586 1.00 29.69  ? 216 LYS   A CB  1 
ATOM   1704 C CG  . LYS   A 1 220 ? 14.179  -19.299 -22.751 1.00 39.67  ? 216 LYS   A CG  1 
ATOM   1705 C CD  . LYS   A 1 220 ? 14.775  -20.688 -22.904 1.00 57.51  ? 216 LYS   A CD  1 
ATOM   1706 C CE  . LYS   A 1 220 ? 13.701  -21.724 -23.185 1.00 64.86  ? 216 LYS   A CE  1 
ATOM   1707 N NZ  . LYS   A 1 220 ? 14.271  -23.096 -23.289 1.00 76.25  ? 216 LYS   A NZ  1 
ATOM   1708 N N   . ASN   A 1 221 ? 14.350  -16.367 -24.669 1.00 36.71  ? 217 ASN   A N   1 
ATOM   1709 C CA  . ASN   A 1 221 ? 13.586  -15.948 -25.833 1.00 34.23  ? 217 ASN   A CA  1 
ATOM   1710 C C   . ASN   A 1 221 ? 12.718  -17.087 -26.353 1.00 36.98  ? 217 ASN   A C   1 
ATOM   1711 O O   . ASN   A 1 221 ? 13.093  -18.262 -26.299 1.00 34.51  ? 217 ASN   A O   1 
ATOM   1712 C CB  . ASN   A 1 221 ? 14.518  -15.468 -26.947 1.00 42.40  ? 217 ASN   A CB  1 
ATOM   1713 C CG  . ASN   A 1 221 ? 15.301  -14.229 -26.561 1.00 42.85  ? 217 ASN   A CG  1 
ATOM   1714 O OD1 . ASN   A 1 221 ? 14.842  -13.413 -25.762 1.00 32.87  ? 217 ASN   A OD1 1 
ATOM   1715 N ND2 . ASN   A 1 221 ? 16.488  -14.079 -27.136 1.00 35.95  ? 217 ASN   A ND2 1 
ATOM   1716 N N   . PHE   A 1 222 ? 11.544  -16.722 -26.860 1.00 40.09  ? 218 PHE   A N   1 
ATOM   1717 C CA  . PHE   A 1 222 ? 10.658  -17.649 -27.544 1.00 42.45  ? 218 PHE   A CA  1 
ATOM   1718 C C   . PHE   A 1 222 ? 10.285  -17.062 -28.897 1.00 40.84  ? 218 PHE   A C   1 
ATOM   1719 O O   . PHE   A 1 222 ? 10.460  -15.866 -29.147 1.00 45.16  ? 218 PHE   A O   1 
ATOM   1720 C CB  . PHE   A 1 222 ? 9.392   -17.943 -26.726 1.00 46.31  ? 218 PHE   A CB  1 
ATOM   1721 C CG  . PHE   A 1 222 ? 9.668   -18.513 -25.364 1.00 34.78  ? 218 PHE   A CG  1 
ATOM   1722 C CD1 . PHE   A 1 222 ? 9.960   -19.857 -25.208 1.00 33.61  ? 218 PHE   A CD1 1 
ATOM   1723 C CD2 . PHE   A 1 222 ? 9.629   -17.705 -24.240 1.00 40.86  ? 218 PHE   A CD2 1 
ATOM   1724 C CE1 . PHE   A 1 222 ? 10.213  -20.385 -23.956 1.00 40.50  ? 218 PHE   A CE1 1 
ATOM   1725 C CE2 . PHE   A 1 222 ? 9.881   -18.227 -22.985 1.00 31.03  ? 218 PHE   A CE2 1 
ATOM   1726 C CZ  . PHE   A 1 222 ? 10.173  -19.569 -22.843 1.00 33.35  ? 218 PHE   A CZ  1 
ATOM   1727 N N   . SER   A 1 223 ? 9.772   -17.921 -29.773 1.00 46.55  ? 219 SER   A N   1 
ATOM   1728 C CA  . SER   A 1 223 ? 9.368   -17.477 -31.100 1.00 52.90  ? 219 SER   A CA  1 
ATOM   1729 C C   . SER   A 1 223 ? 8.247   -16.452 -31.001 1.00 61.21  ? 219 SER   A C   1 
ATOM   1730 O O   . SER   A 1 223 ? 7.278   -16.641 -30.259 1.00 61.23  ? 219 SER   A O   1 
ATOM   1731 C CB  . SER   A 1 223 ? 8.919   -18.671 -31.942 1.00 55.57  ? 219 SER   A CB  1 
ATOM   1732 O OG  . SER   A 1 223 ? 8.505   -18.257 -33.233 1.00 73.78  ? 219 SER   A OG  1 
ATOM   1733 N N   . ALA   A 1 224 ? 8.389   -15.356 -31.741 1.00 62.04  ? 220 ALA   A N   1 
ATOM   1734 C CA  . ALA   A 1 224 ? 7.324   -14.368 -31.817 1.00 69.95  ? 220 ALA   A CA  1 
ATOM   1735 C C   . ALA   A 1 224 ? 6.127   -14.946 -32.561 1.00 65.19  ? 220 ALA   A C   1 
ATOM   1736 O O   . ALA   A 1 224 ? 6.269   -15.746 -33.489 1.00 68.31  ? 220 ALA   A O   1 
ATOM   1737 C CB  . ALA   A 1 224 ? 7.816   -13.097 -32.509 1.00 50.49  ? 220 ALA   A CB  1 
ATOM   1738 N N   . GLY   A 1 225 ? 4.935   -14.537 -32.140 1.00 67.71  ? 221 GLY   A N   1 
ATOM   1739 C CA  . GLY   A 1 225 ? 3.720   -15.097 -32.696 1.00 71.53  ? 221 GLY   A CA  1 
ATOM   1740 C C   . GLY   A 1 225 ? 3.302   -16.365 -31.982 1.00 76.10  ? 221 GLY   A C   1 
ATOM   1741 O O   . GLY   A 1 225 ? 3.639   -16.561 -30.811 1.00 73.99  ? 221 GLY   A O   1 
ATOM   1742 N N   . THR   A 1 226 ? 2.578   -17.239 -32.675 1.00 77.45  ? 222 THR   A N   1 
ATOM   1743 C CA  . THR   A 1 226 ? 2.074   -18.466 -32.075 1.00 75.11  ? 222 THR   A CA  1 
ATOM   1744 C C   . THR   A 1 226 ? 3.101   -19.584 -32.200 1.00 74.32  ? 222 THR   A C   1 
ATOM   1745 O O   . THR   A 1 226 ? 3.713   -19.770 -33.256 1.00 76.59  ? 222 THR   A O   1 
ATOM   1746 C CB  . THR   A 1 226 ? 0.761   -18.891 -32.734 1.00 70.11  ? 222 THR   A CB  1 
ATOM   1747 O OG1 . THR   A 1 226 ? -0.171  -17.803 -32.692 1.00 68.29  ? 222 THR   A OG1 1 
ATOM   1748 C CG2 . THR   A 1 226 ? 0.164   -20.084 -32.005 1.00 51.20  ? 222 THR   A CG2 1 
ATOM   1749 N N   . SER   A 1 227 ? 3.285   -20.325 -31.111 1.00 75.96  ? 223 SER   A N   1 
ATOM   1750 C CA  . SER   A 1 227 ? 4.151   -21.492 -31.083 1.00 71.28  ? 223 SER   A CA  1 
ATOM   1751 C C   . SER   A 1 227 ? 3.339   -22.720 -30.692 1.00 57.79  ? 223 SER   A C   1 
ATOM   1752 O O   . SER   A 1 227 ? 2.247   -22.616 -30.128 1.00 62.99  ? 223 SER   A O   1 
ATOM   1753 C CB  . SER   A 1 227 ? 5.316   -21.305 -30.101 1.00 60.20  ? 223 SER   A CB  1 
ATOM   1754 O OG  . SER   A 1 227 ? 6.243   -20.347 -30.580 1.00 72.84  ? 223 SER   A OG  1 
ATOM   1755 N N   . ASP   A 1 228 ? 3.888   -23.895 -31.003 1.00 65.17  ? 224 ASP   A N   1 
ATOM   1756 C CA  . ASP   A 1 228 ? 3.293   -25.167 -30.611 1.00 58.16  ? 224 ASP   A CA  1 
ATOM   1757 C C   . ASP   A 1 228 ? 3.704   -25.590 -29.205 1.00 60.04  ? 224 ASP   A C   1 
ATOM   1758 O O   . ASP   A 1 228 ? 3.698   -26.788 -28.890 1.00 76.87  ? 224 ASP   A O   1 
ATOM   1759 C CB  . ASP   A 1 228 ? 3.662   -26.250 -31.626 1.00 62.45  ? 224 ASP   A CB  1 
ATOM   1760 C CG  . ASP   A 1 228 ? 2.646   -27.374 -31.675 1.00 62.57  ? 224 ASP   A CG  1 
ATOM   1761 O OD1 . ASP   A 1 228 ? 1.519   -27.138 -32.158 1.00 79.05  ? 224 ASP   A OD1 1 
ATOM   1762 O OD2 . ASP   A 1 228 ? 2.977   -28.494 -31.232 1.00 80.06  ? 224 ASP   A OD2 1 
ATOM   1763 N N   . ARG   A 1 229 ? 4.052   -24.633 -28.350 1.00 54.91  ? 225 ARG   A N   1 
ATOM   1764 C CA  . ARG   A 1 229 ? 4.612   -24.919 -27.038 1.00 54.37  ? 225 ARG   A CA  1 
ATOM   1765 C C   . ARG   A 1 229 ? 3.524   -24.930 -25.972 1.00 56.75  ? 225 ARG   A C   1 
ATOM   1766 O O   . ARG   A 1 229 ? 2.587   -24.128 -26.011 1.00 53.81  ? 225 ARG   A O   1 
ATOM   1767 C CB  . ARG   A 1 229 ? 5.679   -23.880 -26.686 1.00 45.36  ? 225 ARG   A CB  1 
ATOM   1768 C CG  . ARG   A 1 229 ? 6.441   -24.163 -25.405 1.00 55.81  ? 225 ARG   A CG  1 
ATOM   1769 C CD  . ARG   A 1 229 ? 7.491   -23.094 -25.155 1.00 52.11  ? 225 ARG   A CD  1 
ATOM   1770 N NE  . ARG   A 1 229 ? 8.649   -23.255 -26.028 1.00 52.41  ? 225 ARG   A NE  1 
ATOM   1771 C CZ  . ARG   A 1 229 ? 9.725   -23.968 -25.716 1.00 70.35  ? 225 ARG   A CZ  1 
ATOM   1772 N NH1 . ARG   A 1 229 ? 10.734  -24.061 -26.571 1.00 77.77  ? 225 ARG   A NH1 1 
ATOM   1773 N NH2 . ARG   A 1 229 ? 9.794   -24.589 -24.546 1.00 76.22  ? 225 ARG   A NH2 1 
ATOM   1774 N N   . GLU   A 1 230 ? 3.658   -25.848 -25.018 1.00 48.00  ? 226 GLU   A N   1 
ATOM   1775 C CA  . GLU   A 1 230 ? 2.725   -25.917 -23.904 1.00 55.51  ? 226 GLU   A CA  1 
ATOM   1776 C C   . GLU   A 1 230 ? 2.925   -24.731 -22.967 1.00 46.71  ? 226 GLU   A C   1 
ATOM   1777 O O   . GLU   A 1 230 ? 4.019   -24.171 -22.860 1.00 43.97  ? 226 GLU   A O   1 
ATOM   1778 C CB  . GLU   A 1 230 ? 2.907   -27.226 -23.136 1.00 65.86  ? 226 GLU   A CB  1 
ATOM   1779 C CG  . GLU   A 1 230 ? 2.855   -28.473 -24.006 1.00 72.38  ? 226 GLU   A CG  1 
ATOM   1780 C CD  . GLU   A 1 230 ? 4.234   -28.998 -24.358 1.00 87.11  ? 226 GLU   A CD  1 
ATOM   1781 O OE1 . GLU   A 1 230 ? 5.177   -28.183 -24.456 1.00 72.95  ? 226 GLU   A OE1 1 
ATOM   1782 O OE2 . GLU   A 1 230 ? 4.376   -30.226 -24.537 1.00 94.04  ? 226 GLU   A OE2 1 
ATOM   1783 N N   . SER   A 1 231 ? 1.847   -24.348 -22.285 1.00 37.48  ? 227 SER   A N   1 
ATOM   1784 C CA  . SER   A 1 231 ? 1.915   -23.240 -21.342 1.00 38.60  ? 227 SER   A CA  1 
ATOM   1785 C C   . SER   A 1 231 ? 2.869   -23.572 -20.201 1.00 49.69  ? 227 SER   A C   1 
ATOM   1786 O O   . SER   A 1 231 ? 2.941   -24.715 -19.742 1.00 37.83  ? 227 SER   A O   1 
ATOM   1787 C CB  . SER   A 1 231 ? 0.524   -22.923 -20.795 1.00 39.88  ? 227 SER   A CB  1 
ATOM   1788 O OG  . SER   A 1 231 ? -0.247  -22.209 -21.746 1.00 32.63  ? 227 SER   A OG  1 
ATOM   1789 N N   . ILE   A 1 232 ? 3.603   -22.562 -19.744 1.00 34.13  ? 228 ILE   A N   1 
ATOM   1790 C CA  . ILE   A 1 232 ? 4.659   -22.735 -18.753 1.00 37.03  ? 228 ILE   A CA  1 
ATOM   1791 C C   . ILE   A 1 232 ? 4.290   -21.939 -17.510 1.00 36.11  ? 228 ILE   A C   1 
ATOM   1792 O O   . ILE   A 1 232 ? 4.078   -20.722 -17.585 1.00 31.90  ? 228 ILE   A O   1 
ATOM   1793 C CB  . ILE   A 1 232 ? 6.027   -22.294 -19.298 1.00 45.26  ? 228 ILE   A CB  1 
ATOM   1794 C CG1 . ILE   A 1 232 ? 6.530   -23.287 -20.348 1.00 37.93  ? 228 ILE   A CG1 1 
ATOM   1795 C CG2 . ILE   A 1 232 ? 7.029   -22.153 -18.166 1.00 44.68  ? 228 ILE   A CG2 1 
ATOM   1796 C CD1 . ILE   A 1 232 ? 7.618   -22.731 -21.240 1.00 35.33  ? 228 ILE   A CD1 1 
ATOM   1797 N N   . PHE   A 1 233 ? 4.222   -22.622 -16.371 1.00 37.28  ? 229 PHE   A N   1 
ATOM   1798 C CA  . PHE   A 1 233 ? 3.976   -21.993 -15.082 1.00 38.75  ? 229 PHE   A CA  1 
ATOM   1799 C C   . PHE   A 1 233 ? 5.297   -21.790 -14.352 1.00 36.10  ? 229 PHE   A C   1 
ATOM   1800 O O   . PHE   A 1 233 ? 6.134   -22.695 -14.305 1.00 39.72  ? 229 PHE   A O   1 
ATOM   1801 C CB  . PHE   A 1 233 ? 3.037   -22.844 -14.226 1.00 42.42  ? 229 PHE   A CB  1 
ATOM   1802 C CG  . PHE   A 1 233 ? 1.629   -22.890 -14.737 1.00 37.15  ? 229 PHE   A CG  1 
ATOM   1803 C CD1 . PHE   A 1 233 ? 1.264   -23.799 -15.716 1.00 40.47  ? 229 PHE   A CD1 1 
ATOM   1804 C CD2 . PHE   A 1 233 ? 0.670   -22.026 -14.239 1.00 43.64  ? 229 PHE   A CD2 1 
ATOM   1805 C CE1 . PHE   A 1 233 ? -0.031  -23.843 -16.189 1.00 44.50  ? 229 PHE   A CE1 1 
ATOM   1806 C CE2 . PHE   A 1 233 ? -0.626  -22.065 -14.708 1.00 44.68  ? 229 PHE   A CE2 1 
ATOM   1807 C CZ  . PHE   A 1 233 ? -0.976  -22.975 -15.684 1.00 50.42  ? 229 PHE   A CZ  1 
ATOM   1808 N N   . PHE   A 1 234 ? 5.476   -20.604 -13.778 1.00 32.42  ? 230 PHE   A N   1 
ATOM   1809 C CA  . PHE   A 1 234 ? 6.730   -20.269 -13.120 1.00 33.56  ? 230 PHE   A CA  1 
ATOM   1810 C C   . PHE   A 1 234 ? 6.471   -19.255 -12.016 1.00 40.64  ? 230 PHE   A C   1 
ATOM   1811 O O   . PHE   A 1 234 ? 5.373   -18.710 -11.882 1.00 32.95  ? 230 PHE   A O   1 
ATOM   1812 C CB  . PHE   A 1 234 ? 7.756   -19.726 -14.122 1.00 38.41  ? 230 PHE   A CB  1 
ATOM   1813 C CG  . PHE   A 1 234 ? 7.397   -18.381 -14.690 1.00 32.42  ? 230 PHE   A CG  1 
ATOM   1814 C CD1 . PHE   A 1 234 ? 6.488   -18.272 -15.730 1.00 34.93  ? 230 PHE   A CD1 1 
ATOM   1815 C CD2 . PHE   A 1 234 ? 7.971   -17.225 -14.185 1.00 33.36  ? 230 PHE   A CD2 1 
ATOM   1816 C CE1 . PHE   A 1 234 ? 6.157   -17.036 -16.254 1.00 35.47  ? 230 PHE   A CE1 1 
ATOM   1817 C CE2 . PHE   A 1 234 ? 7.643   -15.986 -14.705 1.00 36.84  ? 230 PHE   A CE2 1 
ATOM   1818 C CZ  . PHE   A 1 234 ? 6.735   -15.892 -15.741 1.00 34.39  ? 230 PHE   A CZ  1 
ATOM   1819 N N   . ASN   A 1 235 ? 7.511   -19.010 -11.223 1.00 38.66  ? 231 ASN   A N   1 
ATOM   1820 C CA  . ASN   A 1 235 ? 7.494   -18.018 -10.155 1.00 34.97  ? 231 ASN   A CA  1 
ATOM   1821 C C   . ASN   A 1 235 ? 8.491   -16.923 -10.510 1.00 34.39  ? 231 ASN   A C   1 
ATOM   1822 O O   . ASN   A 1 235 ? 9.696   -17.184 -10.594 1.00 34.09  ? 231 ASN   A O   1 
ATOM   1823 C CB  . ASN   A 1 235 ? 7.839   -18.659 -8.810  1.00 38.69  ? 231 ASN   A CB  1 
ATOM   1824 C CG  . ASN   A 1 235 ? 7.682   -17.699 -7.646  1.00 44.34  ? 231 ASN   A CG  1 
ATOM   1825 O OD1 . ASN   A 1 235 ? 8.401   -16.706 -7.541  1.00 35.48  ? 231 ASN   A OD1 1 
ATOM   1826 N ND2 . ASN   A 1 235 ? 6.738   -17.996 -6.761  1.00 45.04  ? 231 ASN   A ND2 1 
ATOM   1827 N N   . SER   A 1 236 ? 7.987   -15.702 -10.711 1.00 33.80  ? 232 SER   A N   1 
ATOM   1828 C CA  . SER   A 1 236 ? 8.842   -14.613 -11.176 1.00 35.85  ? 232 SER   A CA  1 
ATOM   1829 C C   . SER   A 1 236 ? 9.948   -14.303 -10.176 1.00 36.26  ? 232 SER   A C   1 
ATOM   1830 O O   . SER   A 1 236 ? 11.067  -13.952 -10.569 1.00 40.73  ? 232 SER   A O   1 
ATOM   1831 C CB  . SER   A 1 236 ? 8.001   -13.365 -11.446 1.00 39.71  ? 232 SER   A CB  1 
ATOM   1832 O OG  . SER   A 1 236 ? 7.279   -12.978 -10.291 1.00 37.82  ? 232 SER   A OG  1 
ATOM   1833 N N   . HIS   A 1 237 ? 9.656   -14.419 -8.879  1.00 36.78  ? 233 HIS   A N   1 
ATOM   1834 C CA  . HIS   A 1 237 ? 10.690  -14.189 -7.876  1.00 38.71  ? 233 HIS   A CA  1 
ATOM   1835 C C   . HIS   A 1 237 ? 11.757  -15.275 -7.928  1.00 40.28  ? 233 HIS   A C   1 
ATOM   1836 O O   . HIS   A 1 237 ? 12.954  -14.982 -7.828  1.00 44.20  ? 233 HIS   A O   1 
ATOM   1837 C CB  . HIS   A 1 237 ? 10.069  -14.115 -6.482  1.00 40.03  ? 233 HIS   A CB  1 
ATOM   1838 C CG  . HIS   A 1 237 ? 11.052  -13.783 -5.403  1.00 42.34  ? 233 HIS   A CG  1 
ATOM   1839 N ND1 . HIS   A 1 237 ? 11.764  -14.747 -4.723  1.00 61.97  ? 233 HIS   A ND1 1 
ATOM   1840 C CD2 . HIS   A 1 237 ? 11.442  -12.594 -4.887  1.00 53.95  ? 233 HIS   A CD2 1 
ATOM   1841 C CE1 . HIS   A 1 237 ? 12.550  -14.166 -3.834  1.00 60.24  ? 233 HIS   A CE1 1 
ATOM   1842 N NE2 . HIS   A 1 237 ? 12.374  -12.860 -3.913  1.00 55.88  ? 233 HIS   A NE2 1 
ATOM   1843 N N   . ASN   A 1 238 ? 11.343  -16.533 -8.086  1.00 29.53  ? 234 ASN   A N   1 
ATOM   1844 C CA  . ASN   A 1 238 ? 12.311  -17.622 -8.157  1.00 41.03  ? 234 ASN   A CA  1 
ATOM   1845 C C   . ASN   A 1 238 ? 13.139  -17.542 -9.433  1.00 47.03  ? 234 ASN   A C   1 
ATOM   1846 O O   . ASN   A 1 238 ? 14.342  -17.817 -9.411  1.00 38.85  ? 234 ASN   A O   1 
ATOM   1847 C CB  . ASN   A 1 238 ? 11.596  -18.970 -8.064  1.00 42.31  ? 234 ASN   A CB  1 
ATOM   1848 C CG  . ASN   A 1 238 ? 11.014  -19.226 -6.688  1.00 51.37  ? 234 ASN   A CG  1 
ATOM   1849 O OD1 . ASN   A 1 238 ? 11.317  -18.513 -5.731  1.00 47.84  ? 234 ASN   A OD1 1 
ATOM   1850 N ND2 . ASN   A 1 238 ? 10.175  -20.250 -6.580  1.00 43.92  ? 234 ASN   A ND2 1 
ATOM   1851 N N   . VAL   A 1 239 ? 12.517  -17.152 -10.548 1.00 44.89  ? 235 VAL   A N   1 
ATOM   1852 C CA  . VAL   A 1 239 ? 13.223  -17.110 -11.826 1.00 49.28  ? 235 VAL   A CA  1 
ATOM   1853 C C   . VAL   A 1 239 ? 14.273  -16.003 -11.832 1.00 48.48  ? 235 VAL   A C   1 
ATOM   1854 O O   . VAL   A 1 239 ? 15.363  -16.166 -12.393 1.00 40.27  ? 235 VAL   A O   1 
ATOM   1855 C CB  . VAL   A 1 239 ? 12.214  -16.943 -12.980 1.00 41.88  ? 235 VAL   A CB  1 
ATOM   1856 C CG1 . VAL   A 1 239 ? 12.928  -16.619 -14.284 1.00 45.92  ? 235 VAL   A CG1 1 
ATOM   1857 C CG2 . VAL   A 1 239 ? 11.371  -18.200 -13.136 1.00 47.56  ? 235 VAL   A CG2 1 
ATOM   1858 N N   . SER   A 1 240 ? 13.972  -14.866 -11.204 1.00 44.69  ? 236 SER   A N   1 
ATOM   1859 C CA  . SER   A 1 240 ? 14.826  -13.685 -11.276 1.00 43.45  ? 236 SER   A CA  1 
ATOM   1860 C C   . SER   A 1 240 ? 15.573  -13.410 -9.975  1.00 52.71  ? 236 SER   A C   1 
ATOM   1861 O O   . SER   A 1 240 ? 16.154  -12.333 -9.816  1.00 56.45  ? 236 SER   A O   1 
ATOM   1862 C CB  . SER   A 1 240 ? 14.001  -12.461 -11.670 1.00 31.28  ? 236 SER   A CB  1 
ATOM   1863 O OG  . SER   A 1 240 ? 13.206  -12.021 -10.583 1.00 61.62  ? 236 SER   A OG  1 
ATOM   1864 N N   . LYS   A 1 241 ? 15.566  -14.361 -9.044  1.00 52.57  ? 237 LYS   A N   1 
ATOM   1865 C CA  . LYS   A 1 241 ? 16.298  -14.262 -7.787  1.00 62.12  ? 237 LYS   A CA  1 
ATOM   1866 C C   . LYS   A 1 241 ? 17.765  -14.027 -8.167  1.00 82.89  ? 237 LYS   A C   1 
ATOM   1867 O O   . LYS   A 1 241 ? 18.143  -14.334 -9.297  1.00 74.51  ? 237 LYS   A O   1 
ATOM   1868 C CB  . LYS   A 1 241 ? 16.028  -15.545 -6.988  1.00 56.72  ? 237 LYS   A CB  1 
ATOM   1869 C CG  . LYS   A 1 241 ? 16.279  -15.521 -5.501  1.00 72.93  ? 237 LYS   A CG  1 
ATOM   1870 C CD  . LYS   A 1 241 ? 15.356  -16.435 -4.743  1.00 70.71  ? 237 LYS   A CD  1 
ATOM   1871 C CE  . LYS   A 1 241 ? 15.441  -17.854 -5.256  1.00 61.61  ? 237 LYS   A CE  1 
ATOM   1872 N NZ  . LYS   A 1 241 ? 14.865  -18.803 -4.267  1.00 64.16  ? 237 LYS   A NZ  1 
ATOM   1873 N N   . PRO   A 1 242 ? 18.653  -13.448 -7.261  1.00 74.32  ? 238 PRO   A N   1 
ATOM   1874 C CA  . PRO   A 1 242 ? 19.960  -13.002 -7.781  1.00 73.91  ? 238 PRO   A CA  1 
ATOM   1875 C C   . PRO   A 1 242 ? 20.640  -14.084 -8.609  1.00 88.52  ? 238 PRO   A C   1 
ATOM   1876 O O   . PRO   A 1 242 ? 21.470  -13.772 -9.473  1.00 97.11  ? 238 PRO   A O   1 
ATOM   1877 C CB  . PRO   A 1 242 ? 20.777  -12.646 -6.527  1.00 68.06  ? 238 PRO   A CB  1 
ATOM   1878 C CG  . PRO   A 1 242 ? 20.025  -13.095 -5.387  1.00 81.32  ? 238 PRO   A CG  1 
ATOM   1879 C CD  . PRO   A 1 242 ? 18.725  -13.671 -5.806  1.00 77.22  ? 238 PRO   A CD  1 
ATOM   1880 N N   . GLU   A 1 243 ? 20.260  -15.346 -8.376  1.00 77.95  ? 239 GLU   A N   1 
ATOM   1881 C CA  . GLU   A 1 243 ? 20.601  -16.441 -9.276  1.00 90.81  ? 239 GLU   A CA  1 
ATOM   1882 C C   . GLU   A 1 243 ? 19.561  -17.553 -9.188  1.00 101.43 ? 239 GLU   A C   1 
ATOM   1883 O O   . GLU   A 1 243 ? 19.457  -18.236 -8.161  1.00 102.52 ? 239 GLU   A O   1 
ATOM   1884 C CB  . GLU   A 1 243 ? 21.989  -16.976 -8.980  1.00 96.68  ? 239 GLU   A CB  1 
ATOM   1885 C CG  . GLU   A 1 243 ? 23.110  -16.211 -9.692  1.00 113.49 ? 239 GLU   A CG  1 
ATOM   1886 C CD  . GLU   A 1 243 ? 22.944  -16.268 -11.213 1.00 123.92 ? 239 GLU   A CD  1 
ATOM   1887 O OE1 . GLU   A 1 243 ? 22.359  -17.250 -11.706 1.00 126.12 ? 239 GLU   A OE1 1 
ATOM   1888 O OE2 . GLU   A 1 243 ? 23.366  -15.322 -11.899 1.00 119.55 ? 239 GLU   A OE2 1 
ATOM   1889 N N   . SER   A 1 244 ? 18.788  -17.715 -10.265 1.00 96.48  ? 240 SER   A N   1 
ATOM   1890 C CA  . SER   A 1 244 ? 18.087  -18.952 -10.587 1.00 94.53  ? 240 SER   A CA  1 
ATOM   1891 C C   . SER   A 1 244 ? 18.852  -19.708 -11.661 1.00 98.93  ? 240 SER   A C   1 
ATOM   1892 O O   . SER   A 1 244 ? 19.522  -19.108 -12.501 1.00 103.63 ? 240 SER   A O   1 
ATOM   1893 C CB  . SER   A 1 244 ? 16.663  -18.680 -11.088 1.00 75.97  ? 240 SER   A CB  1 
ATOM   1894 O OG  . SER   A 1 244 ? 15.997  -19.879 -11.496 1.00 83.59  ? 240 SER   A OG  1 
ATOM   1895 N N   . SER   A 1 245 ? 18.750  -21.031 -11.629 1.00 101.72 ? 241 SER   A N   1 
ATOM   1896 C CA  . SER   A 1 245 ? 19.163  -21.879 -12.745 1.00 98.82  ? 241 SER   A CA  1 
ATOM   1897 C C   . SER   A 1 245 ? 17.935  -22.688 -13.145 1.00 92.13  ? 241 SER   A C   1 
ATOM   1898 O O   . SER   A 1 245 ? 17.584  -23.669 -12.481 1.00 77.70  ? 241 SER   A O   1 
ATOM   1899 C CB  . SER   A 1 245 ? 20.342  -22.777 -12.383 1.00 109.65 ? 241 SER   A CB  1 
ATOM   1900 O OG  . SER   A 1 245 ? 21.541  -22.029 -12.272 1.00 107.69 ? 241 SER   A OG  1 
ATOM   1901 N N   . SER   A 1 246 ? 17.271  -22.259 -14.214 1.00 89.83  ? 242 SER   A N   1 
ATOM   1902 C CA  . SER   A 1 246 ? 16.019  -22.855 -14.647 1.00 75.27  ? 242 SER   A CA  1 
ATOM   1903 C C   . SER   A 1 246 ? 16.086  -23.163 -16.135 1.00 71.61  ? 242 SER   A C   1 
ATOM   1904 O O   . SER   A 1 246 ? 16.899  -22.602 -16.873 1.00 73.98  ? 242 SER   A O   1 
ATOM   1905 C CB  . SER   A 1 246 ? 14.830  -21.926 -14.361 1.00 81.16  ? 242 SER   A CB  1 
ATOM   1906 O OG  . SER   A 1 246 ? 14.777  -21.563 -12.992 1.00 84.22  ? 242 SER   A OG  1 
ATOM   1907 N N   . VAL   A 1 247 ? 15.207  -24.070 -16.569 1.00 66.21  ? 243 VAL   A N   1 
ATOM   1908 C CA  . VAL   A 1 247 ? 15.035  -24.328 -17.993 1.00 66.80  ? 243 VAL   A CA  1 
ATOM   1909 C C   . VAL   A 1 247 ? 14.550  -23.076 -18.713 1.00 67.71  ? 243 VAL   A C   1 
ATOM   1910 O O   . VAL   A 1 247 ? 14.701  -22.960 -19.935 1.00 79.39  ? 243 VAL   A O   1 
ATOM   1911 C CB  . VAL   A 1 247 ? 14.069  -25.519 -18.194 1.00 77.90  ? 243 VAL   A CB  1 
ATOM   1912 C CG1 . VAL   A 1 247 ? 12.696  -25.191 -17.644 1.00 76.40  ? 243 VAL   A CG1 1 
ATOM   1913 C CG2 . VAL   A 1 247 ? 13.979  -25.921 -19.662 1.00 81.60  ? 243 VAL   A CG2 1 
ATOM   1914 N N   . LEU   A 1 248 ? 13.988  -22.118 -17.976 1.00 63.07  ? 244 LEU   A N   1 
ATOM   1915 C CA  . LEU   A 1 248 ? 13.524  -20.861 -18.545 1.00 52.65  ? 244 LEU   A CA  1 
ATOM   1916 C C   . LEU   A 1 248 ? 14.595  -19.779 -18.559 1.00 48.68  ? 244 LEU   A C   1 
ATOM   1917 O O   . LEU   A 1 248 ? 14.465  -18.808 -19.312 1.00 48.58  ? 244 LEU   A O   1 
ATOM   1918 C CB  . LEU   A 1 248 ? 12.310  -20.354 -17.764 1.00 49.92  ? 244 LEU   A CB  1 
ATOM   1919 C CG  . LEU   A 1 248 ? 11.201  -21.374 -17.504 1.00 54.48  ? 244 LEU   A CG  1 
ATOM   1920 C CD1 . LEU   A 1 248 ? 10.054  -20.725 -16.750 1.00 39.54  ? 244 LEU   A CD1 1 
ATOM   1921 C CD2 . LEU   A 1 248 ? 10.714  -21.983 -18.808 1.00 54.93  ? 244 LEU   A CD2 1 
ATOM   1922 N N   . THR   A 1 249 ? 15.640  -19.919 -17.745 1.00 55.39  ? 245 THR   A N   1 
ATOM   1923 C CA  . THR   A 1 249 ? 16.691  -18.913 -17.651 1.00 52.66  ? 245 THR   A CA  1 
ATOM   1924 C C   . THR   A 1 249 ? 17.795  -19.122 -18.681 1.00 51.50  ? 245 THR   A C   1 
ATOM   1925 O O   . THR   A 1 249 ? 18.365  -18.142 -19.179 1.00 41.45  ? 245 THR   A O   1 
ATOM   1926 C CB  . THR   A 1 249 ? 17.277  -18.913 -16.231 1.00 58.55  ? 245 THR   A CB  1 
ATOM   1927 O OG1 . THR   A 1 249 ? 16.352  -18.284 -15.335 1.00 65.28  ? 245 THR   A OG1 1 
ATOM   1928 C CG2 . THR   A 1 249 ? 18.605  -18.171 -16.170 1.00 59.34  ? 245 THR   A CG2 1 
ATOM   1929 N N   . GLU   A 1 250 ? 18.090  -20.374 -19.032 1.00 40.75  ? 246 GLU   A N   1 
ATOM   1930 C CA  . GLU   A 1 250 ? 19.129  -20.683 -20.008 1.00 50.72  ? 246 GLU   A CA  1 
ATOM   1931 C C   . GLU   A 1 250 ? 18.786  -20.117 -21.381 1.00 46.85  ? 246 GLU   A C   1 
ATOM   1932 O O   . GLU   A 1 250 ? 17.917  -20.648 -22.080 1.00 48.22  ? 246 GLU   A O   1 
ATOM   1933 C CB  . GLU   A 1 250 ? 19.335  -22.196 -20.099 1.00 47.58  ? 246 GLU   A CB  1 
ATOM   1934 C CG  . GLU   A 1 250 ? 20.479  -22.722 -19.249 1.00 57.74  ? 246 GLU   A CG  1 
ATOM   1935 C CD  . GLU   A 1 250 ? 20.747  -24.196 -19.484 1.00 78.77  ? 246 GLU   A CD  1 
ATOM   1936 O OE1 . GLU   A 1 250 ? 19.785  -24.937 -19.777 1.00 73.03  ? 246 GLU   A OE1 1 
ATOM   1937 O OE2 . GLU   A 1 250 ? 21.919  -24.614 -19.371 1.00 70.87  ? 246 GLU   A OE2 1 
ATOM   1938 N N   . LEU   A 1 251 ? 19.463  -19.043 -21.775 1.00 39.76  ? 247 LEU   A N   1 
ATOM   1939 C CA  . LEU   A 1 251 ? 19.224  -18.443 -23.080 1.00 44.68  ? 247 LEU   A CA  1 
ATOM   1940 C C   . LEU   A 1 251 ? 19.832  -19.303 -24.181 1.00 44.11  ? 247 LEU   A C   1 
ATOM   1941 O O   . LEU   A 1 251 ? 20.951  -19.807 -24.052 1.00 48.00  ? 247 LEU   A O   1 
ATOM   1942 C CB  . LEU   A 1 251 ? 19.807  -17.031 -23.130 1.00 41.48  ? 247 LEU   A CB  1 
ATOM   1943 C CG  . LEU   A 1 251 ? 19.491  -16.186 -24.367 1.00 42.45  ? 247 LEU   A CG  1 
ATOM   1944 C CD1 . LEU   A 1 251 ? 18.041  -15.730 -24.357 1.00 30.59  ? 247 LEU   A CD1 1 
ATOM   1945 C CD2 . LEU   A 1 251 ? 20.430  -14.992 -24.455 1.00 37.59  ? 247 LEU   A CD2 1 
ATOM   1946 N N   . ASP   A 1 252 ? 19.082  -19.475 -25.271 1.00 49.22  ? 248 ASP   A N   1 
ATOM   1947 C CA  . ASP   A 1 252 ? 19.592  -20.239 -26.405 1.00 53.18  ? 248 ASP   A CA  1 
ATOM   1948 C C   . ASP   A 1 252 ? 20.690  -19.470 -27.129 1.00 44.26  ? 248 ASP   A C   1 
ATOM   1949 O O   . ASP   A 1 252 ? 21.790  -19.991 -27.346 1.00 52.82  ? 248 ASP   A O   1 
ATOM   1950 C CB  . ASP   A 1 252 ? 18.451  -20.580 -27.365 1.00 53.32  ? 248 ASP   A CB  1 
ATOM   1951 C CG  . ASP   A 1 252 ? 17.445  -21.537 -26.759 1.00 71.38  ? 248 ASP   A CG  1 
ATOM   1952 O OD1 . ASP   A 1 252 ? 17.850  -22.643 -26.343 1.00 74.80  ? 248 ASP   A OD1 1 
ATOM   1953 O OD2 . ASP   A 1 252 ? 16.248  -21.184 -26.699 1.00 70.41  ? 248 ASP   A OD2 1 
ATOM   1954 N N   . LYS   A 1 253 ? 20.407  -18.226 -27.506 1.00 45.71  ? 249 LYS   A N   1 
ATOM   1955 C CA  . LYS   A 1 253 ? 21.357  -17.390 -28.224 1.00 52.54  ? 249 LYS   A CA  1 
ATOM   1956 C C   . LYS   A 1 253 ? 20.883  -15.948 -28.139 1.00 44.76  ? 249 LYS   A C   1 
ATOM   1957 O O   . LYS   A 1 253 ? 19.711  -15.677 -27.864 1.00 39.11  ? 249 LYS   A O   1 
ATOM   1958 C CB  . LYS   A 1 253 ? 21.496  -17.828 -29.687 1.00 49.83  ? 249 LYS   A CB  1 
ATOM   1959 C CG  . LYS   A 1 253 ? 20.175  -17.873 -30.441 1.00 54.47  ? 249 LYS   A CG  1 
ATOM   1960 C CD  . LYS   A 1 253 ? 20.343  -18.461 -31.833 1.00 56.84  ? 249 LYS   A CD  1 
ATOM   1961 C CE  . LYS   A 1 253 ? 21.056  -17.492 -32.762 1.00 67.76  ? 249 LYS   A CE  1 
ATOM   1962 N NZ  . LYS   A 1 253 ? 20.222  -16.298 -33.073 1.00 69.67  ? 249 LYS   A NZ  1 
ATOM   1963 N N   . ILE   A 1 254 ? 21.813  -15.021 -28.367 1.00 52.14  ? 250 ILE   A N   1 
ATOM   1964 C CA  . ILE   A 1 254 ? 21.447  -13.612 -28.445 1.00 47.24  ? 250 ILE   A CA  1 
ATOM   1965 C C   . ILE   A 1 254 ? 20.676  -13.375 -29.734 1.00 46.89  ? 250 ILE   A C   1 
ATOM   1966 O O   . ILE   A 1 254 ? 21.098  -13.803 -30.817 1.00 56.40  ? 250 ILE   A O   1 
ATOM   1967 C CB  . ILE   A 1 254 ? 22.694  -12.719 -28.373 1.00 57.78  ? 250 ILE   A CB  1 
ATOM   1968 C CG1 . ILE   A 1 254 ? 23.424  -12.914 -27.045 1.00 55.65  ? 250 ILE   A CG1 1 
ATOM   1969 C CG2 . ILE   A 1 254 ? 22.310  -11.257 -28.551 1.00 48.04  ? 250 ILE   A CG2 1 
ATOM   1970 C CD1 . ILE   A 1 254 ? 24.822  -12.344 -27.049 1.00 59.91  ? 250 ILE   A CD1 1 
ATOM   1971 N N   . GLU   A 1 255 ? 19.537  -12.697 -29.626 1.00 42.46  ? 251 GLU   A N   1 
ATOM   1972 C CA  . GLU   A 1 255 ? 18.690  -12.442 -30.782 1.00 47.81  ? 251 GLU   A CA  1 
ATOM   1973 C C   . GLU   A 1 255 ? 18.219  -10.998 -30.753 1.00 52.03  ? 251 GLU   A C   1 
ATOM   1974 O O   . GLU   A 1 255 ? 17.724  -10.524 -29.727 1.00 50.54  ? 251 GLU   A O   1 
ATOM   1975 C CB  . GLU   A 1 255 ? 17.493  -13.400 -30.808 1.00 50.24  ? 251 GLU   A CB  1 
ATOM   1976 C CG  . GLU   A 1 255 ? 17.866  -14.825 -31.194 1.00 62.02  ? 251 GLU   A CG  1 
ATOM   1977 C CD  . GLU   A 1 255 ? 17.060  -15.871 -30.447 1.00 82.70  ? 251 GLU   A CD  1 
ATOM   1978 O OE1 . GLU   A 1 255 ? 17.359  -16.123 -29.261 1.00 76.99  ? 251 GLU   A OE1 1 
ATOM   1979 O OE2 . GLU   A 1 255 ? 16.131  -16.448 -31.050 1.00 101.45 ? 251 GLU   A OE2 1 
ATOM   1980 N N   . GLY   A 1 256 ? 18.385  -10.304 -31.878 1.00 45.36  ? 252 GLY   A N   1 
ATOM   1981 C CA  . GLY   A 1 256 ? 17.939  -8.929  -31.974 1.00 41.52  ? 252 GLY   A CA  1 
ATOM   1982 C C   . GLY   A 1 256 ? 18.838  -7.970  -31.211 1.00 42.36  ? 252 GLY   A C   1 
ATOM   1983 O O   . GLY   A 1 256 ? 20.033  -8.210  -31.012 1.00 47.56  ? 252 GLY   A O   1 
ATOM   1984 N N   . VAL   A 1 257 ? 18.243  -6.859  -30.775 1.00 40.30  ? 253 VAL   A N   1 
ATOM   1985 C CA  . VAL   A 1 257 ? 18.992  -5.836  -30.057 1.00 46.49  ? 253 VAL   A CA  1 
ATOM   1986 C C   . VAL   A 1 257 ? 19.352  -6.341  -28.668 1.00 48.74  ? 253 VAL   A C   1 
ATOM   1987 O O   . VAL   A 1 257 ? 18.520  -6.922  -27.958 1.00 45.65  ? 253 VAL   A O   1 
ATOM   1988 C CB  . VAL   A 1 257 ? 18.181  -4.531  -29.981 1.00 53.20  ? 253 VAL   A CB  1 
ATOM   1989 C CG1 . VAL   A 1 257 ? 18.985  -3.441  -29.287 1.00 48.40  ? 253 VAL   A CG1 1 
ATOM   1990 C CG2 . VAL   A 1 257 ? 17.762  -4.087  -31.373 1.00 55.40  ? 253 VAL   A CG2 1 
ATOM   1991 N N   . PHE   A 1 258 ? 20.610  -6.123  -28.270 1.00 45.10  ? 254 PHE   A N   1 
ATOM   1992 C CA  . PHE   A 1 258 ? 21.104  -6.526  -26.954 1.00 60.12  ? 254 PHE   A CA  1 
ATOM   1993 C C   . PHE   A 1 258 ? 22.017  -5.407  -26.453 1.00 48.79  ? 254 PHE   A C   1 
ATOM   1994 O O   . PHE   A 1 258 ? 23.246  -5.500  -26.499 1.00 63.54  ? 254 PHE   A O   1 
ATOM   1995 C CB  . PHE   A 1 258 ? 21.823  -7.873  -27.011 1.00 52.30  ? 254 PHE   A CB  1 
ATOM   1996 C CG  . PHE   A 1 258 ? 22.095  -8.474  -25.662 1.00 68.15  ? 254 PHE   A CG  1 
ATOM   1997 C CD1 . PHE   A 1 258 ? 21.132  -8.445  -24.667 1.00 61.72  ? 254 PHE   A CD1 1 
ATOM   1998 C CD2 . PHE   A 1 258 ? 23.307  -9.086  -25.395 1.00 67.35  ? 254 PHE   A CD2 1 
ATOM   1999 C CE1 . PHE   A 1 258 ? 21.380  -9.002  -23.426 1.00 63.67  ? 254 PHE   A CE1 1 
ATOM   2000 C CE2 . PHE   A 1 258 ? 23.559  -9.648  -24.157 1.00 60.16  ? 254 PHE   A CE2 1 
ATOM   2001 C CZ  . PHE   A 1 258 ? 22.595  -9.605  -23.172 1.00 57.59  ? 254 PHE   A CZ  1 
ATOM   2002 N N   . GLU   A 1 259 ? 21.401  -4.330  -25.980 1.00 50.99  ? 255 GLU   A N   1 
ATOM   2003 C CA  . GLU   A 1 259 ? 22.120  -3.190  -25.440 1.00 55.76  ? 255 GLU   A CA  1 
ATOM   2004 C C   . GLU   A 1 259 ? 21.824  -3.055  -23.954 1.00 56.23  ? 255 GLU   A C   1 
ATOM   2005 O O   . GLU   A 1 259 ? 20.884  -3.649  -23.418 1.00 58.04  ? 255 GLU   A O   1 
ATOM   2006 C CB  . GLU   A 1 259 ? 21.752  -1.897  -26.177 1.00 40.86  ? 255 GLU   A CB  1 
ATOM   2007 C CG  . GLU   A 1 259 ? 22.256  -1.844  -27.607 1.00 54.74  ? 255 GLU   A CG  1 
ATOM   2008 C CD  . GLU   A 1 259 ? 23.757  -1.641  -27.688 1.00 75.03  ? 255 GLU   A CD  1 
ATOM   2009 O OE1 . GLU   A 1 259 ? 24.324  -1.001  -26.777 1.00 81.68  ? 255 GLU   A OE1 1 
ATOM   2010 O OE2 . GLU   A 1 259 ? 24.370  -2.126  -28.662 1.00 84.85  ? 255 GLU   A OE2 1 
ATOM   2011 N N   . ARG   A 1 260 ? 22.606  -2.298  -23.328 1.00 56.63  ? 256 ARG   A N   1 
ATOM   2012 C CA  . ARG   A 1 260 ? 22.477  -2.094  -21.900 1.00 55.23  ? 256 ARG   A CA  1 
ATOM   2013 C C   . ARG   A 1 260 ? 21.645  -0.845  -21.632 1.00 43.86  ? 256 ARG   A C   1 
ATOM   2014 O O   . ARG   A 1 260 ? 21.661  0.096   -22.429 1.00 57.67  ? 256 ARG   A O   1 
ATOM   2015 C CB  . ARG   A 1 260 ? 23.859  -1.964  -21.274 1.00 69.09  ? 256 ARG   A CB  1 
ATOM   2016 C CG  . ARG   A 1 260 ? 24.749  -3.130  -21.681 1.00 75.82  ? 256 ARG   A CG  1 
ATOM   2017 C CD  . ARG   A 1 260 ? 24.334  -4.415  -20.993 1.00 87.39  ? 256 ARG   A CD  1 
ATOM   2018 N NE  . ARG   A 1 260 ? 24.883  -5.591  -21.663 1.00 116.03 ? 256 ARG   A NE  1 
ATOM   2019 C CZ  . ARG   A 1 260 ? 24.709  -6.839  -21.241 1.00 103.76 ? 256 ARG   A CZ  1 
ATOM   2020 N NH1 . ARG   A 1 260 ? 24.021  -7.076  -20.132 1.00 75.07  ? 256 ARG   A NH1 1 
ATOM   2021 N NH2 . ARG   A 1 260 ? 25.227  -7.850  -21.921 1.00 93.00  ? 256 ARG   A NH2 1 
ATOM   2022 N N   . PRO   A 1 261 ? 20.890  -0.823  -20.534 1.00 47.70  ? 257 PRO   A N   1 
ATOM   2023 C CA  . PRO   A 1 261 ? 19.912  0.254   -20.338 1.00 47.26  ? 257 PRO   A CA  1 
ATOM   2024 C C   . PRO   A 1 261 ? 20.570  1.623   -20.288 1.00 53.53  ? 257 PRO   A C   1 
ATOM   2025 O O   . PRO   A 1 261 ? 21.697  1.784   -19.814 1.00 50.42  ? 257 PRO   A O   1 
ATOM   2026 C CB  . PRO   A 1 261 ? 19.256  -0.099  -18.997 1.00 52.24  ? 257 PRO   A CB  1 
ATOM   2027 C CG  . PRO   A 1 261 ? 20.242  -0.981  -18.308 1.00 48.20  ? 257 PRO   A CG  1 
ATOM   2028 C CD  . PRO   A 1 261 ? 20.920  -1.755  -19.394 1.00 52.20  ? 257 PRO   A CD  1 
ATOM   2029 N N   . SER   A 1 262 ? 19.851  2.614   -20.807 1.00 60.16  ? 258 SER   A N   1 
ATOM   2030 C CA  . SER   A 1 262 ? 20.305  3.995   -20.761 1.00 57.17  ? 258 SER   A CA  1 
ATOM   2031 C C   . SER   A 1 262 ? 20.151  4.538   -19.347 1.00 51.55  ? 258 SER   A C   1 
ATOM   2032 O O   . SER   A 1 262 ? 19.068  4.461   -18.758 1.00 52.42  ? 258 SER   A O   1 
ATOM   2033 C CB  . SER   A 1 262 ? 19.514  4.851   -21.749 1.00 42.98  ? 258 SER   A CB  1 
ATOM   2034 O OG  . SER   A 1 262 ? 19.635  6.229   -21.440 1.00 49.31  ? 258 SER   A OG  1 
ATOM   2035 N N   . ASP   A 1 263 ? 21.240  5.082   -18.802 1.00 56.37  ? 259 ASP   A N   1 
ATOM   2036 C CA  . ASP   A 1 263 ? 21.183  5.649   -17.461 1.00 51.77  ? 259 ASP   A CA  1 
ATOM   2037 C C   . ASP   A 1 263 ? 20.288  6.880   -17.410 1.00 57.49  ? 259 ASP   A C   1 
ATOM   2038 O O   . ASP   A 1 263 ? 19.684  7.163   -16.368 1.00 42.75  ? 259 ASP   A O   1 
ATOM   2039 C CB  . ASP   A 1 263 ? 22.592  5.992   -16.978 1.00 57.10  ? 259 ASP   A CB  1 
ATOM   2040 C CG  . ASP   A 1 263 ? 22.616  6.450   -15.537 1.00 68.42  ? 259 ASP   A CG  1 
ATOM   2041 O OD1 . ASP   A 1 263 ? 22.571  5.584   -14.637 1.00 71.93  ? 259 ASP   A OD1 1 
ATOM   2042 O OD2 . ASP   A 1 263 ? 22.677  7.675   -15.302 1.00 84.11  ? 259 ASP   A OD2 1 
ATOM   2043 N N   . GLU   A 1 264 ? 20.186  7.619   -18.517 1.00 54.06  ? 260 GLU   A N   1 
ATOM   2044 C CA  . GLU   A 1 264 ? 19.311  8.785   -18.551 1.00 49.97  ? 260 GLU   A CA  1 
ATOM   2045 C C   . GLU   A 1 264 ? 17.844  8.378   -18.481 1.00 57.44  ? 260 GLU   A C   1 
ATOM   2046 O O   . GLU   A 1 264 ? 17.038  9.049   -17.827 1.00 45.71  ? 260 GLU   A O   1 
ATOM   2047 C CB  . GLU   A 1 264 ? 19.578  9.606   -19.812 1.00 45.94  ? 260 GLU   A CB  1 
ATOM   2048 C CG  . GLU   A 1 264 ? 18.928  10.979  -19.806 1.00 66.55  ? 260 GLU   A CG  1 
ATOM   2049 C CD  . GLU   A 1 264 ? 18.597  11.472  -21.201 1.00 78.08  ? 260 GLU   A CD  1 
ATOM   2050 O OE1 . GLU   A 1 264 ? 17.603  12.215  -21.349 1.00 82.42  ? 260 GLU   A OE1 1 
ATOM   2051 O OE2 . GLU   A 1 264 ? 19.327  11.115  -22.149 1.00 68.45  ? 260 GLU   A OE2 1 
ATOM   2052 N N   . VAL   A 1 265 ? 17.481  7.281   -19.151 1.00 44.95  ? 261 VAL   A N   1 
ATOM   2053 C CA  . VAL   A 1 265 ? 16.094  6.825   -19.136 1.00 46.89  ? 261 VAL   A CA  1 
ATOM   2054 C C   . VAL   A 1 265 ? 15.689  6.393   -17.732 1.00 47.22  ? 261 VAL   A C   1 
ATOM   2055 O O   . VAL   A 1 265 ? 14.586  6.704   -17.267 1.00 31.45  ? 261 VAL   A O   1 
ATOM   2056 C CB  . VAL   A 1 265 ? 15.899  5.691   -20.159 1.00 39.96  ? 261 VAL   A CB  1 
ATOM   2057 C CG1 . VAL   A 1 265 ? 14.556  5.005   -19.954 1.00 31.08  ? 261 VAL   A CG1 1 
ATOM   2058 C CG2 . VAL   A 1 265 ? 16.015  6.230   -21.575 1.00 49.10  ? 261 VAL   A CG2 1 
ATOM   2059 N N   . ILE   A 1 266 ? 16.576  5.683   -17.032 1.00 46.97  ? 262 ILE   A N   1 
ATOM   2060 C CA  . ILE   A 1 266 ? 16.262  5.210   -15.686 1.00 44.14  ? 262 ILE   A CA  1 
ATOM   2061 C C   . ILE   A 1 266 ? 16.074  6.386   -14.735 1.00 47.11  ? 262 ILE   A C   1 
ATOM   2062 O O   . ILE   A 1 266 ? 15.156  6.394   -13.905 1.00 45.87  ? 262 ILE   A O   1 
ATOM   2063 C CB  . ILE   A 1 266 ? 17.360  4.248   -15.193 1.00 38.29  ? 262 ILE   A CB  1 
ATOM   2064 C CG1 . ILE   A 1 266 ? 17.255  2.905   -15.918 1.00 45.31  ? 262 ILE   A CG1 1 
ATOM   2065 C CG2 . ILE   A 1 266 ? 17.273  4.054   -13.686 1.00 43.10  ? 262 ILE   A CG2 1 
ATOM   2066 C CD1 . ILE   A 1 266 ? 18.560  2.141   -15.981 1.00 40.92  ? 262 ILE   A CD1 1 
ATOM   2067 N N   . ARG   A 1 267 ? 16.933  7.402   -14.846 1.00 44.36  ? 263 ARG   A N   1 
ATOM   2068 C CA  . ARG   A 1 267 ? 16.844  8.551   -13.951 1.00 50.91  ? 263 ARG   A CA  1 
ATOM   2069 C C   . ARG   A 1 267 ? 15.570  9.350   -14.202 1.00 45.91  ? 263 ARG   A C   1 
ATOM   2070 O O   . ARG   A 1 267 ? 14.846  9.695   -13.261 1.00 42.43  ? 263 ARG   A O   1 
ATOM   2071 C CB  . ARG   A 1 267 ? 18.079  9.437   -14.113 1.00 46.39  ? 263 ARG   A CB  1 
ATOM   2072 C CG  . ARG   A 1 267 ? 19.341  8.846   -13.508 1.00 52.76  ? 263 ARG   A CG  1 
ATOM   2073 C CD  . ARG   A 1 267 ? 20.511  9.813   -13.594 1.00 46.49  ? 263 ARG   A CD  1 
ATOM   2074 N NE  . ARG   A 1 267 ? 21.009  9.955   -14.959 1.00 53.17  ? 263 ARG   A NE  1 
ATOM   2075 C CZ  . ARG   A 1 267 ? 20.875  11.055  -15.692 1.00 61.04  ? 263 ARG   A CZ  1 
ATOM   2076 N NH1 . ARG   A 1 267 ? 20.255  12.115  -15.192 1.00 67.12  ? 263 ARG   A NH1 1 
ATOM   2077 N NH2 . ARG   A 1 267 ? 21.361  11.098  -16.925 1.00 58.79  ? 263 ARG   A NH2 1 
ATOM   2078 N N   . GLU   A 1 268 ? 15.280  9.654   -15.470 1.00 43.48  ? 264 GLU   A N   1 
ATOM   2079 C CA  . GLU   A 1 268 ? 14.076  10.412  -15.791 1.00 56.17  ? 264 GLU   A CA  1 
ATOM   2080 C C   . GLU   A 1 268 ? 12.814  9.626   -15.461 1.00 49.02  ? 264 GLU   A C   1 
ATOM   2081 O O   . GLU   A 1 268 ? 11.787  10.220  -15.112 1.00 51.05  ? 264 GLU   A O   1 
ATOM   2082 C CB  . GLU   A 1 268 ? 14.085  10.812  -17.266 1.00 58.96  ? 264 GLU   A CB  1 
ATOM   2083 C CG  . GLU   A 1 268 ? 13.350  12.109  -17.567 1.00 87.85  ? 264 GLU   A CG  1 
ATOM   2084 C CD  . GLU   A 1 268 ? 13.406  12.482  -19.037 1.00 93.56  ? 264 GLU   A CD  1 
ATOM   2085 O OE1 . GLU   A 1 268 ? 12.390  12.984  -19.564 1.00 76.65  ? 264 GLU   A OE1 1 
ATOM   2086 O OE2 . GLU   A 1 268 ? 14.465  12.274  -19.665 1.00 89.43  ? 264 GLU   A OE2 1 
ATOM   2087 N N   . LEU   A 1 269 ? 12.869  8.296   -15.564 1.00 50.10  ? 265 LEU   A N   1 
ATOM   2088 C CA  . LEU   A 1 269 ? 11.715  7.478   -15.209 1.00 45.77  ? 265 LEU   A CA  1 
ATOM   2089 C C   . LEU   A 1 269 ? 11.532  7.415   -13.698 1.00 55.39  ? 265 LEU   A C   1 
ATOM   2090 O O   . LEU   A 1 269 ? 10.399  7.394   -13.203 1.00 37.45  ? 265 LEU   A O   1 
ATOM   2091 C CB  . LEU   A 1 269 ? 11.872  6.075   -15.796 1.00 51.67  ? 265 LEU   A CB  1 
ATOM   2092 C CG  . LEU   A 1 269 ? 10.626  5.208   -15.978 1.00 60.42  ? 265 LEU   A CG  1 
ATOM   2093 C CD1 . LEU   A 1 269 ? 10.827  4.259   -17.147 1.00 57.25  ? 265 LEU   A CD1 1 
ATOM   2094 C CD2 . LEU   A 1 269 ? 10.308  4.428   -14.713 1.00 55.01  ? 265 LEU   A CD2 1 
ATOM   2095 N N   . SER   A 1 270 ? 12.637  7.383   -12.948 1.00 46.74  ? 266 SER   A N   1 
ATOM   2096 C CA  . SER   A 1 270 ? 12.541  7.356   -11.493 1.00 49.47  ? 266 SER   A CA  1 
ATOM   2097 C C   . SER   A 1 270 ? 11.961  8.657   -10.953 1.00 48.88  ? 266 SER   A C   1 
ATOM   2098 O O   . SER   A 1 270 ? 11.152  8.640   -10.018 1.00 40.95  ? 266 SER   A O   1 
ATOM   2099 C CB  . SER   A 1 270 ? 13.916  7.085   -10.882 1.00 47.42  ? 266 SER   A CB  1 
ATOM   2100 O OG  . SER   A 1 270 ? 13.890  7.248   -9.474  1.00 62.50  ? 266 SER   A OG  1 
ATOM   2101 N N   . ARG   A 1 271 ? 12.360  9.793   -11.530 1.00 39.15  ? 267 ARG   A N   1 
ATOM   2102 C CA  . ARG   A 1 271 ? 11.816  11.076  -11.095 1.00 45.06  ? 267 ARG   A CA  1 
ATOM   2103 C C   . ARG   A 1 271 ? 10.319  11.159  -11.362 1.00 51.41  ? 267 ARG   A C   1 
ATOM   2104 O O   . ARG   A 1 271 ? 9.555   11.644  -10.518 1.00 48.44  ? 267 ARG   A O   1 
ATOM   2105 C CB  . ARG   A 1 271 ? 12.546  12.222  -11.796 1.00 49.46  ? 267 ARG   A CB  1 
ATOM   2106 C CG  . ARG   A 1 271 ? 11.848  13.569  -11.673 1.00 54.55  ? 267 ARG   A CG  1 
ATOM   2107 C CD  . ARG   A 1 271 ? 12.573  14.649  -12.460 1.00 63.42  ? 267 ARG   A CD  1 
ATOM   2108 N NE  . ARG   A 1 271 ? 12.403  14.485  -13.901 1.00 73.13  ? 267 ARG   A NE  1 
ATOM   2109 C CZ  . ARG   A 1 271 ? 11.659  15.281  -14.662 1.00 93.17  ? 267 ARG   A CZ  1 
ATOM   2110 N NH1 . ARG   A 1 271 ? 11.008  16.302  -14.120 1.00 88.19  ? 267 ARG   A NH1 1 
ATOM   2111 N NH2 . ARG   A 1 271 ? 11.563  15.057  -15.965 1.00 96.44  ? 267 ARG   A NH2 1 
ATOM   2112 N N   . ALA   A 1 272 ? 9.880   10.681  -12.528 1.00 45.80  ? 268 ALA   A N   1 
ATOM   2113 C CA  . ALA   A 1 272 ? 8.466   10.757  -12.875 1.00 55.05  ? 268 ALA   A CA  1 
ATOM   2114 C C   . ALA   A 1 272 ? 7.612   9.874   -11.974 1.00 44.71  ? 268 ALA   A C   1 
ATOM   2115 O O   . ALA   A 1 272 ? 6.424   10.155  -11.782 1.00 43.43  ? 268 ALA   A O   1 
ATOM   2116 C CB  . ALA   A 1 272 ? 8.267   10.377  -14.340 1.00 38.46  ? 268 ALA   A CB  1 
ATOM   2117 N N   . LEU   A 1 273 ? 8.191   8.810   -11.413 1.00 39.47  ? 269 LEU   A N   1 
ATOM   2118 C CA  . LEU   A 1 273 ? 7.441   7.968   -10.486 1.00 42.28  ? 269 LEU   A CA  1 
ATOM   2119 C C   . LEU   A 1 273 ? 7.375   8.591   -9.097  1.00 50.38  ? 269 LEU   A C   1 
ATOM   2120 O O   . LEU   A 1 273 ? 6.353   8.476   -8.411  1.00 43.36  ? 269 LEU   A O   1 
ATOM   2121 C CB  . LEU   A 1 273 ? 8.062   6.573   -10.418 1.00 40.95  ? 269 LEU   A CB  1 
ATOM   2122 C CG  . LEU   A 1 273 ? 7.522   5.552   -11.421 1.00 53.53  ? 269 LEU   A CG  1 
ATOM   2123 C CD1 . LEU   A 1 273 ? 8.444   4.348   -11.514 1.00 49.26  ? 269 LEU   A CD1 1 
ATOM   2124 C CD2 . LEU   A 1 273 ? 6.111   5.122   -11.047 1.00 36.31  ? 269 LEU   A CD2 1 
ATOM   2125 N N   . ARG   A 1 274 ? 8.453   9.251   -8.665  1.00 41.43  ? 270 ARG   A N   1 
ATOM   2126 C CA  . ARG   A 1 274 ? 8.435   9.921   -7.370  1.00 51.63  ? 270 ARG   A CA  1 
ATOM   2127 C C   . ARG   A 1 274 ? 7.534   11.149  -7.386  1.00 50.76  ? 270 ARG   A C   1 
ATOM   2128 O O   . ARG   A 1 274 ? 6.914   11.475  -6.368  1.00 55.76  ? 270 ARG   A O   1 
ATOM   2129 C CB  . ARG   A 1 274 ? 9.855   10.308  -6.955  1.00 47.42  ? 270 ARG   A CB  1 
ATOM   2130 C CG  . ARG   A 1 274 ? 10.834  9.143   -6.925  1.00 46.58  ? 270 ARG   A CG  1 
ATOM   2131 C CD  . ARG   A 1 274 ? 12.131  9.520   -6.227  1.00 57.17  ? 270 ARG   A CD  1 
ATOM   2132 N NE  . ARG   A 1 274 ? 13.018  10.289  -7.097  1.00 64.20  ? 270 ARG   A NE  1 
ATOM   2133 C CZ  . ARG   A 1 274 ? 13.159  11.609  -7.040  1.00 57.63  ? 270 ARG   A CZ  1 
ATOM   2134 N NH1 . ARG   A 1 274 ? 12.472  12.313  -6.152  1.00 63.31  ? 270 ARG   A NH1 1 
ATOM   2135 N NH2 . ARG   A 1 274 ? 13.988  12.226  -7.872  1.00 68.60  ? 270 ARG   A NH2 1 
ATOM   2136 N N   . GLN   A 1 275 ? 7.448   11.840  -8.525  1.00 48.55  ? 271 GLN   A N   1 
ATOM   2137 C CA  . GLN   A 1 275 ? 6.576   13.007  -8.614  1.00 48.54  ? 271 GLN   A CA  1 
ATOM   2138 C C   . GLN   A 1 275 ? 5.110   12.599  -8.684  1.00 48.07  ? 271 GLN   A C   1 
ATOM   2139 O O   . GLN   A 1 275 ? 4.243   13.273  -8.115  1.00 61.72  ? 271 GLN   A O   1 
ATOM   2140 C CB  . GLN   A 1 275 ? 6.950   13.852  -9.831  1.00 43.18  ? 271 GLN   A CB  1 
ATOM   2141 C CG  . GLN   A 1 275 ? 8.032   14.885  -9.574  1.00 57.50  ? 271 GLN   A CG  1 
ATOM   2142 C CD  . GLN   A 1 275 ? 8.462   15.599  -10.840 1.00 69.63  ? 271 GLN   A CD  1 
ATOM   2143 O OE1 . GLN   A 1 275 ? 7.731   15.624  -11.830 1.00 57.91  ? 271 GLN   A OE1 1 
ATOM   2144 N NE2 . GLN   A 1 275 ? 9.654   16.183  -10.815 1.00 82.01  ? 271 GLN   A NE2 1 
ATOM   2145 N N   . ALA   A 1 276 ? 4.813   11.496  -9.373  1.00 52.16  ? 272 ALA   A N   1 
ATOM   2146 C CA  . ALA   A 1 276 ? 3.425   11.100  -9.586  1.00 54.98  ? 272 ALA   A CA  1 
ATOM   2147 C C   . ALA   A 1 276 ? 2.808   10.449  -8.355  1.00 52.73  ? 272 ALA   A C   1 
ATOM   2148 O O   . ALA   A 1 276 ? 1.587   10.520  -8.173  1.00 58.13  ? 272 ALA   A O   1 
ATOM   2149 C CB  . ALA   A 1 276 ? 3.327   10.149  -10.780 1.00 51.39  ? 272 ALA   A CB  1 
ATOM   2150 N N   . LEU   A 1 277 ? 3.618   9.818   -7.506  1.00 46.31  ? 273 LEU   A N   1 
ATOM   2151 C CA  . LEU   A 1 277 ? 3.104   9.082   -6.361  1.00 53.10  ? 273 LEU   A CA  1 
ATOM   2152 C C   . LEU   A 1 277 ? 3.611   9.579   -5.017  1.00 45.61  ? 273 LEU   A C   1 
ATOM   2153 O O   . LEU   A 1 277 ? 3.064   9.171   -3.986  1.00 61.17  ? 273 LEU   A O   1 
ATOM   2154 C CB  . LEU   A 1 277 ? 3.450   7.590   -6.486  1.00 57.03  ? 273 LEU   A CB  1 
ATOM   2155 C CG  . LEU   A 1 277 ? 2.694   6.776   -7.535  1.00 51.15  ? 273 LEU   A CG  1 
ATOM   2156 C CD1 . LEU   A 1 277 ? 3.259   5.368   -7.608  1.00 38.19  ? 273 LEU   A CD1 1 
ATOM   2157 C CD2 . LEU   A 1 277 ? 1.208   6.745   -7.218  1.00 40.20  ? 273 LEU   A CD2 1 
ATOM   2158 N N   . GLY   A 1 278 ? 4.628   10.436  -4.988  1.00 52.40  ? 274 GLY   A N   1 
ATOM   2159 C CA  . GLY   A 1 278 ? 5.279   10.735  -3.730  1.00 44.33  ? 274 GLY   A CA  1 
ATOM   2160 C C   . GLY   A 1 278 ? 6.047   9.575   -3.145  1.00 53.97  ? 274 GLY   A C   1 
ATOM   2161 O O   . GLY   A 1 278 ? 6.482   9.652   -1.992  1.00 49.65  ? 274 GLY   A O   1 
ATOM   2162 N N   . VAL   A 1 279 ? 6.222   8.500   -3.908  1.00 52.98  ? 275 VAL   A N   1 
ATOM   2163 C CA  . VAL   A 1 279 ? 6.923   7.314   -3.436  1.00 46.10  ? 275 VAL   A CA  1 
ATOM   2164 C C   . VAL   A 1 279 ? 8.425   7.552   -3.511  1.00 44.90  ? 275 VAL   A C   1 
ATOM   2165 O O   . VAL   A 1 279 ? 8.926   8.262   -4.389  1.00 50.16  ? 275 VAL   A O   1 
ATOM   2166 C CB  . VAL   A 1 279 ? 6.493   6.077   -4.255  1.00 46.04  ? 275 VAL   A CB  1 
ATOM   2167 C CG1 . VAL   A 1 279 ? 6.995   6.175   -5.692  1.00 42.89  ? 275 VAL   A CG1 1 
ATOM   2168 C CG2 . VAL   A 1 279 ? 6.975   4.794   -3.597  1.00 52.98  ? 275 VAL   A CG2 1 
ATOM   2169 N N   . SER   A 1 280 ? 9.151   6.969   -2.559  1.00 50.95  ? 276 SER   A N   1 
ATOM   2170 C CA  . SER   A 1 280 ? 10.602  7.068   -2.529  1.00 42.42  ? 276 SER   A CA  1 
ATOM   2171 C C   . SER   A 1 280 ? 11.298  5.743   -2.262  1.00 47.59  ? 276 SER   A C   1 
ATOM   2172 O O   . SER   A 1 280 ? 12.523  5.674   -2.413  1.00 40.84  ? 276 SER   A O   1 
ATOM   2173 C CB  . SER   A 1 280 ? 11.050  8.092   -1.474  1.00 46.54  ? 276 SER   A CB  1 
ATOM   2174 O OG  . SER   A 1 280 ? 10.776  7.632   -0.164  1.00 46.92  ? 276 SER   A OG  1 
ATOM   2175 N N   . LEU   A 1 281 ? 10.570  4.699   -1.878  1.00 46.20  ? 277 LEU   A N   1 
ATOM   2176 C CA  . LEU   A 1 281 ? 11.140  3.372   -1.665  1.00 44.54  ? 277 LEU   A CA  1 
ATOM   2177 C C   . LEU   A 1 281 ? 10.409  2.441   -2.627  1.00 51.00  ? 277 LEU   A C   1 
ATOM   2178 O O   . LEU   A 1 281 ? 9.277   2.029   -2.353  1.00 45.24  ? 277 LEU   A O   1 
ATOM   2179 C CB  . LEU   A 1 281 ? 10.970  2.907   -0.219  1.00 45.91  ? 277 LEU   A CB  1 
ATOM   2180 C CG  . LEU   A 1 281 ? 11.882  3.464   0.883   1.00 45.89  ? 277 LEU   A CG  1 
ATOM   2181 C CD1 . LEU   A 1 281 ? 13.361  3.199   0.605   1.00 49.41  ? 277 LEU   A CD1 1 
ATOM   2182 C CD2 . LEU   A 1 281 ? 11.607  4.932   1.187   1.00 63.42  ? 277 LEU   A CD2 1 
ATOM   2183 N N   . PHE   A 1 282 ? 11.033  2.118   -3.757  1.00 40.01  ? 278 PHE   A N   1 
ATOM   2184 C CA  . PHE   A 1 282 ? 10.362  1.294   -4.755  1.00 47.37  ? 278 PHE   A CA  1 
ATOM   2185 C C   . PHE   A 1 282 ? 11.392  0.690   -5.698  1.00 42.00  ? 278 PHE   A C   1 
ATOM   2186 O O   . PHE   A 1 282 ? 12.565  1.070   -5.704  1.00 38.21  ? 278 PHE   A O   1 
ATOM   2187 C CB  . PHE   A 1 282 ? 9.314   2.100   -5.534  1.00 44.25  ? 278 PHE   A CB  1 
ATOM   2188 C CG  . PHE   A 1 282 ? 9.890   3.211   -6.364  1.00 35.25  ? 278 PHE   A CG  1 
ATOM   2189 C CD1 . PHE   A 1 282 ? 10.199  4.434   -5.791  1.00 43.38  ? 278 PHE   A CD1 1 
ATOM   2190 C CD2 . PHE   A 1 282 ? 10.112  3.037   -7.720  1.00 35.92  ? 278 PHE   A CD2 1 
ATOM   2191 C CE1 . PHE   A 1 282 ? 10.724  5.459   -6.553  1.00 43.83  ? 278 PHE   A CE1 1 
ATOM   2192 C CE2 . PHE   A 1 282 ? 10.637  4.058   -8.488  1.00 39.24  ? 278 PHE   A CE2 1 
ATOM   2193 C CZ  . PHE   A 1 282 ? 10.944  5.271   -7.903  1.00 48.10  ? 278 PHE   A CZ  1 
ATOM   2194 N N   . GLY   A 1 283 ? 10.927  -0.263  -6.497  1.00 40.62  ? 279 GLY   A N   1 
ATOM   2195 C CA  . GLY   A 1 283 ? 11.770  -0.914  -7.480  1.00 49.80  ? 279 GLY   A CA  1 
ATOM   2196 C C   . GLY   A 1 283 ? 11.078  -1.005  -8.819  1.00 43.54  ? 279 GLY   A C   1 
ATOM   2197 O O   . GLY   A 1 283 ? 9.857   -1.147  -8.908  1.00 42.13  ? 279 GLY   A O   1 
ATOM   2198 N N   . ILE   A 1 284 ? 11.880  -0.921  -9.879  1.00 44.14  ? 280 ILE   A N   1 
ATOM   2199 C CA  . ILE   A 1 284 ? 11.392  -0.953  -11.254 1.00 36.93  ? 280 ILE   A CA  1 
ATOM   2200 C C   . ILE   A 1 284 ? 12.048  -2.127  -11.966 1.00 36.06  ? 280 ILE   A C   1 
ATOM   2201 O O   . ILE   A 1 284 ? 13.281  -2.218  -12.017 1.00 37.11  ? 280 ILE   A O   1 
ATOM   2202 C CB  . ILE   A 1 284 ? 11.681  0.361   -11.997 1.00 41.11  ? 280 ILE   A CB  1 
ATOM   2203 C CG1 . ILE   A 1 284 ? 11.487  1.561   -11.068 1.00 48.79  ? 280 ILE   A CG1 1 
ATOM   2204 C CG2 . ILE   A 1 284 ? 10.794  0.483   -13.228 1.00 42.15  ? 280 ILE   A CG2 1 
ATOM   2205 C CD1 . ILE   A 1 284 ? 11.831  2.887   -11.708 1.00 50.48  ? 280 ILE   A CD1 1 
ATOM   2206 N N   . ASP   A 1 285 ? 11.229  -3.018  -12.518 1.00 34.22  ? 281 ASP   A N   1 
ATOM   2207 C CA  . ASP   A 1 285 ? 11.717  -4.131  -13.321 1.00 39.81  ? 281 ASP   A CA  1 
ATOM   2208 C C   . ASP   A 1 285 ? 11.715  -3.716  -14.788 1.00 34.97  ? 281 ASP   A C   1 
ATOM   2209 O O   . ASP   A 1 285 ? 10.659  -3.399  -15.346 1.00 44.95  ? 281 ASP   A O   1 
ATOM   2210 C CB  . ASP   A 1 285 ? 10.857  -5.376  -13.106 1.00 36.22  ? 281 ASP   A CB  1 
ATOM   2211 C CG  . ASP   A 1 285 ? 11.005  -5.951  -11.710 1.00 60.40  ? 281 ASP   A CG  1 
ATOM   2212 O OD1 . ASP   A 1 285 ? 12.025  -5.660  -11.051 1.00 52.61  ? 281 ASP   A OD1 1 
ATOM   2213 O OD2 . ASP   A 1 285 ? 10.102  -6.695  -11.272 1.00 64.28  ? 281 ASP   A OD2 1 
ATOM   2214 N N   . ILE   A 1 286 ? 12.893  -3.716  -15.408 1.00 32.36  ? 282 ILE   A N   1 
ATOM   2215 C CA  . ILE   A 1 286 ? 13.071  -3.205  -16.761 1.00 34.51  ? 282 ILE   A CA  1 
ATOM   2216 C C   . ILE   A 1 286 ? 13.733  -4.280  -17.611 1.00 31.65  ? 282 ILE   A C   1 
ATOM   2217 O O   . ILE   A 1 286 ? 14.719  -4.893  -17.188 1.00 35.87  ? 282 ILE   A O   1 
ATOM   2218 C CB  . ILE   A 1 286 ? 13.911  -1.912  -16.772 1.00 30.27  ? 282 ILE   A CB  1 
ATOM   2219 C CG1 . ILE   A 1 286 ? 13.089  -0.737  -16.238 1.00 37.46  ? 282 ILE   A CG1 1 
ATOM   2220 C CG2 . ILE   A 1 286 ? 14.426  -1.609  -18.172 1.00 39.55  ? 282 ILE   A CG2 1 
ATOM   2221 C CD1 . ILE   A 1 286 ? 13.870  0.554   -16.129 1.00 29.34  ? 282 ILE   A CD1 1 
ATOM   2222 N N   . ILE   A 1 287 ? 13.185  -4.511  -18.803 1.00 28.08  ? 283 ILE   A N   1 
ATOM   2223 C CA  . ILE   A 1 287 ? 13.778  -5.399  -19.791 1.00 37.53  ? 283 ILE   A CA  1 
ATOM   2224 C C   . ILE   A 1 287 ? 13.983  -4.609  -21.077 1.00 34.21  ? 283 ILE   A C   1 
ATOM   2225 O O   . ILE   A 1 287 ? 13.328  -3.594  -21.323 1.00 36.61  ? 283 ILE   A O   1 
ATOM   2226 C CB  . ILE   A 1 287 ? 12.917  -6.652  -20.051 1.00 33.98  ? 283 ILE   A CB  1 
ATOM   2227 C CG1 . ILE   A 1 287 ? 11.510  -6.249  -20.498 1.00 25.51  ? 283 ILE   A CG1 1 
ATOM   2228 C CG2 . ILE   A 1 287 ? 12.856  -7.524  -18.807 1.00 32.91  ? 283 ILE   A CG2 1 
ATOM   2229 C CD1 . ILE   A 1 287 ? 10.660  -7.413  -20.954 1.00 26.63  ? 283 ILE   A CD1 1 
ATOM   2230 N N   . ILE   A 1 288 ? 14.908  -5.088  -21.902 1.00 30.98  ? 284 ILE   A N   1 
ATOM   2231 C CA  . ILE   A 1 288 ? 15.256  -4.429  -23.155 1.00 27.95  ? 284 ILE   A CA  1 
ATOM   2232 C C   . ILE   A 1 288 ? 14.615  -5.208  -24.294 1.00 32.96  ? 284 ILE   A C   1 
ATOM   2233 O O   . ILE   A 1 288 ? 15.002  -6.347  -24.579 1.00 30.91  ? 284 ILE   A O   1 
ATOM   2234 C CB  . ILE   A 1 288 ? 16.775  -4.319  -23.338 1.00 46.90  ? 284 ILE   A CB  1 
ATOM   2235 C CG1 . ILE   A 1 288 ? 17.386  -3.482  -22.213 1.00 40.59  ? 284 ILE   A CG1 1 
ATOM   2236 C CG2 . ILE   A 1 288 ? 17.102  -3.707  -24.693 1.00 33.25  ? 284 ILE   A CG2 1 
ATOM   2237 C CD1 . ILE   A 1 288 ? 16.908  -2.047  -22.193 1.00 35.68  ? 284 ILE   A CD1 1 
ATOM   2238 N N   . ASN   A 1 289 ? 13.630  -4.590  -24.943 1.00 33.07  ? 285 ASN   A N   1 
ATOM   2239 C CA  . ASN   A 1 289 ? 12.985  -5.149  -26.123 1.00 32.26  ? 285 ASN   A CA  1 
ATOM   2240 C C   . ASN   A 1 289 ? 14.016  -5.434  -27.209 1.00 38.86  ? 285 ASN   A C   1 
ATOM   2241 O O   . ASN   A 1 289 ? 14.511  -4.506  -27.853 1.00 28.11  ? 285 ASN   A O   1 
ATOM   2242 C CB  . ASN   A 1 289 ? 11.912  -4.181  -26.633 1.00 34.13  ? 285 ASN   A CB  1 
ATOM   2243 C CG  . ASN   A 1 289 ? 10.897  -4.848  -27.537 1.00 45.50  ? 285 ASN   A CG  1 
ATOM   2244 O OD1 . ASN   A 1 289 ? 11.245  -5.669  -28.381 1.00 43.09  ? 285 ASN   A OD1 1 
ATOM   2245 N ND2 . ASN   A 1 289 ? 9.629   -4.492  -27.367 1.00 37.86  ? 285 ASN   A ND2 1 
ATOM   2246 N N   . ASN   A 1 290 ? 14.344  -6.714  -27.429 1.00 28.85  ? 286 ASN   A N   1 
ATOM   2247 C CA  . ASN   A 1 290 ? 15.339  -7.124  -28.430 1.00 40.90  ? 286 ASN   A CA  1 
ATOM   2248 C C   . ASN   A 1 290 ? 14.862  -6.930  -29.864 1.00 48.74  ? 286 ASN   A C   1 
ATOM   2249 O O   . ASN   A 1 290 ? 15.523  -7.337  -30.826 1.00 45.28  ? 286 ASN   A O   1 
ATOM   2250 C CB  . ASN   A 1 290 ? 15.726  -8.589  -28.212 1.00 34.22  ? 286 ASN   A CB  1 
ATOM   2251 C CG  . ASN   A 1 290 ? 14.666  -9.564  -28.714 1.00 39.63  ? 286 ASN   A CG  1 
ATOM   2252 O OD1 . ASN   A 1 290 ? 13.501  -9.205  -28.901 1.00 36.44  ? 286 ASN   A OD1 1 
ATOM   2253 N ND2 . ASN   A 1 290 ? 15.072  -10.808 -28.937 1.00 40.65  ? 286 ASN   A ND2 1 
ATOM   2254 N N   . GLN   A 1 291 ? 13.697  -6.300  -29.970 1.00 44.26  ? 287 GLN   A N   1 
ATOM   2255 C CA  . GLN   A 1 291 ? 12.915  -6.253  -31.193 1.00 53.36  ? 287 GLN   A CA  1 
ATOM   2256 C C   . GLN   A 1 291 ? 12.544  -4.824  -31.575 1.00 61.72  ? 287 GLN   A C   1 
ATOM   2257 O O   . GLN   A 1 291 ? 12.100  -4.598  -32.706 1.00 73.98  ? 287 GLN   A O   1 
ATOM   2258 C CB  . GLN   A 1 291 ? 11.671  -7.149  -31.013 1.00 61.72  ? 287 GLN   A CB  1 
ATOM   2259 C CG  . GLN   A 1 291 ? 10.511  -7.092  -32.002 1.00 85.79  ? 287 GLN   A CG  1 
ATOM   2260 C CD  . GLN   A 1 291 ? 10.920  -7.217  -33.453 1.00 92.18  ? 287 GLN   A CD  1 
ATOM   2261 O OE1 . GLN   A 1 291 ? 10.578  -6.364  -34.272 1.00 98.24  ? 287 GLN   A OE1 1 
ATOM   2262 N NE2 . GLN   A 1 291 ? 11.653  -8.274  -33.781 1.00 82.66  ? 287 GLN   A NE2 1 
ATOM   2263 N N   . THR   A 1 292 ? 12.728  -3.856  -30.671 1.00 60.81  ? 288 THR   A N   1 
ATOM   2264 C CA  . THR   A 1 292 ? 12.864  -2.444  -31.022 1.00 55.72  ? 288 THR   A CA  1 
ATOM   2265 C C   . THR   A 1 292 ? 14.019  -1.751  -30.312 1.00 43.84  ? 288 THR   A C   1 
ATOM   2266 O O   . THR   A 1 292 ? 14.422  -0.667  -30.752 1.00 50.46  ? 288 THR   A O   1 
ATOM   2267 C CB  . THR   A 1 292 ? 11.579  -1.657  -30.712 1.00 50.45  ? 288 THR   A CB  1 
ATOM   2268 O OG1 . THR   A 1 292 ? 11.313  -1.699  -29.304 1.00 41.84  ? 288 THR   A OG1 1 
ATOM   2269 C CG2 . THR   A 1 292 ? 10.386  -2.211  -31.482 1.00 55.44  ? 288 THR   A CG2 1 
ATOM   2270 N N   . GLY   A 1 293 ? 14.563  -2.327  -29.240 1.00 52.52  ? 289 GLY   A N   1 
ATOM   2271 C CA  . GLY   A 1 293 ? 15.605  -1.695  -28.458 1.00 31.33  ? 289 GLY   A CA  1 
ATOM   2272 C C   . GLY   A 1 293 ? 15.117  -0.865  -27.291 1.00 43.23  ? 289 GLY   A C   1 
ATOM   2273 O O   . GLY   A 1 293 ? 15.946  -0.322  -26.549 1.00 41.90  ? 289 GLY   A O   1 
ATOM   2274 N N   . GLN   A 1 294 ? 13.806  -0.763  -27.093 1.00 31.82  ? 290 GLN   A N   1 
ATOM   2275 C CA  . GLN   A 1 294 ? 13.242  0.165   -26.127 1.00 31.80  ? 290 GLN   A CA  1 
ATOM   2276 C C   . GLN   A 1 294 ? 13.260  -0.418  -24.716 1.00 35.72  ? 290 GLN   A C   1 
ATOM   2277 O O   . GLN   A 1 294 ? 13.326  -1.633  -24.512 1.00 26.78  ? 290 GLN   A O   1 
ATOM   2278 C CB  . GLN   A 1 294 ? 11.809  0.530   -26.513 1.00 37.29  ? 290 GLN   A CB  1 
ATOM   2279 C CG  . GLN   A 1 294 ? 11.700  1.383   -27.764 1.00 42.09  ? 290 GLN   A CG  1 
ATOM   2280 C CD  . GLN   A 1 294 ? 10.302  1.378   -28.350 1.00 48.60  ? 290 GLN   A CD  1 
ATOM   2281 O OE1 . GLN   A 1 294 ? 9.683   0.325   -28.502 1.00 50.35  ? 290 GLN   A OE1 1 
ATOM   2282 N NE2 . GLN   A 1 294 ? 9.794   2.560   -28.679 1.00 42.29  ? 290 GLN   A NE2 1 
ATOM   2283 N N   . HIS   A 1 295 ? 13.196  0.480   -23.735 1.00 30.34  ? 291 HIS   A N   1 
ATOM   2284 C CA  . HIS   A 1 295 ? 13.071  0.092   -22.336 1.00 37.87  ? 291 HIS   A CA  1 
ATOM   2285 C C   . HIS   A 1 295 ? 11.625  -0.290  -22.050 1.00 36.47  ? 291 HIS   A C   1 
ATOM   2286 O O   . HIS   A 1 295 ? 10.710  0.507   -22.283 1.00 44.46  ? 291 HIS   A O   1 
ATOM   2287 C CB  . HIS   A 1 295 ? 13.507  1.234   -21.421 1.00 37.11  ? 291 HIS   A CB  1 
ATOM   2288 C CG  . HIS   A 1 295 ? 14.976  1.512   -21.455 1.00 34.23  ? 291 HIS   A CG  1 
ATOM   2289 N ND1 . HIS   A 1 295 ? 15.641  1.865   -22.609 1.00 38.57  ? 291 HIS   A ND1 1 
ATOM   2290 C CD2 . HIS   A 1 295 ? 15.908  1.496   -20.473 1.00 33.88  ? 291 HIS   A CD2 1 
ATOM   2291 C CE1 . HIS   A 1 295 ? 16.920  2.050   -22.338 1.00 29.57  ? 291 HIS   A CE1 1 
ATOM   2292 N NE2 . HIS   A 1 295 ? 17.108  1.833   -21.049 1.00 43.30  ? 291 HIS   A NE2 1 
ATOM   2293 N N   . ALA   A 1 296 ? 11.417  -1.500  -21.541 1.00 40.03  ? 292 ALA   A N   1 
ATOM   2294 C CA  . ALA   A 1 296 ? 10.084  -2.008  -21.237 1.00 43.89  ? 292 ALA   A CA  1 
ATOM   2295 C C   . ALA   A 1 296 ? 9.961   -2.189  -19.729 1.00 41.75  ? 292 ALA   A C   1 
ATOM   2296 O O   . ALA   A 1 296 ? 10.613  -3.063  -19.147 1.00 39.31  ? 292 ALA   A O   1 
ATOM   2297 C CB  . ALA   A 1 296 ? 9.817   -3.319  -21.973 1.00 29.09  ? 292 ALA   A CB  1 
ATOM   2298 N N   . VAL   A 1 297 ? 9.133   -1.360  -19.101 1.00 33.52  ? 293 VAL   A N   1 
ATOM   2299 C CA  . VAL   A 1 297 ? 8.821   -1.517  -17.684 1.00 36.29  ? 293 VAL   A CA  1 
ATOM   2300 C C   . VAL   A 1 297 ? 7.700   -2.539  -17.556 1.00 41.62  ? 293 VAL   A C   1 
ATOM   2301 O O   . VAL   A 1 297 ? 6.589   -2.324  -18.054 1.00 48.41  ? 293 VAL   A O   1 
ATOM   2302 C CB  . VAL   A 1 297 ? 8.426   -0.178  -17.048 1.00 45.39  ? 293 VAL   A CB  1 
ATOM   2303 C CG1 . VAL   A 1 297 ? 8.013   -0.385  -15.601 1.00 37.61  ? 293 VAL   A CG1 1 
ATOM   2304 C CG2 . VAL   A 1 297 ? 9.576   0.810   -17.142 1.00 43.02  ? 293 VAL   A CG2 1 
ATOM   2305 N N   . ILE   A 1 298 ? 7.987   -3.654  -16.891 1.00 36.95  ? 294 ILE   A N   1 
ATOM   2306 C CA  . ILE   A 1 298 ? 7.045   -4.761  -16.813 1.00 37.58  ? 294 ILE   A CA  1 
ATOM   2307 C C   . ILE   A 1 298 ? 6.367   -4.877  -15.453 1.00 49.36  ? 294 ILE   A C   1 
ATOM   2308 O O   . ILE   A 1 298 ? 5.290   -5.489  -15.373 1.00 41.44  ? 294 ILE   A O   1 
ATOM   2309 C CB  . ILE   A 1 298 ? 7.726   -6.095  -17.184 1.00 46.44  ? 294 ILE   A CB  1 
ATOM   2310 C CG1 . ILE   A 1 298 ? 9.067   -6.229  -16.460 1.00 28.28  ? 294 ILE   A CG1 1 
ATOM   2311 C CG2 . ILE   A 1 298 ? 7.913   -6.192  -18.692 1.00 36.28  ? 294 ILE   A CG2 1 
ATOM   2312 C CD1 . ILE   A 1 298 ? 9.665   -7.615  -16.533 1.00 32.90  ? 294 ILE   A CD1 1 
ATOM   2313 N N   . ASP   A 1 299 ? 6.945   -4.315  -14.392 1.00 47.95  ? 295 ASP   A N   1 
ATOM   2314 C CA  . ASP   A 1 299 ? 6.348   -4.377  -13.064 1.00 44.22  ? 295 ASP   A CA  1 
ATOM   2315 C C   . ASP   A 1 299 ? 6.924   -3.263  -12.201 1.00 46.49  ? 295 ASP   A C   1 
ATOM   2316 O O   . ASP   A 1 299 ? 8.067   -2.841  -12.392 1.00 46.13  ? 295 ASP   A O   1 
ATOM   2317 C CB  . ASP   A 1 299 ? 6.590   -5.737  -12.394 1.00 38.21  ? 295 ASP   A CB  1 
ATOM   2318 C CG  . ASP   A 1 299 ? 5.577   -6.788  -12.814 1.00 55.31  ? 295 ASP   A CG  1 
ATOM   2319 O OD1 . ASP   A 1 299 ? 4.364   -6.489  -12.791 1.00 35.86  ? 295 ASP   A OD1 1 
ATOM   2320 O OD2 . ASP   A 1 299 ? 5.994   -7.911  -13.170 1.00 49.98  ? 295 ASP   A OD2 1 
ATOM   2321 N N   . ILE   A 1 300 ? 6.116   -2.793  -11.252 1.00 44.94  ? 296 ILE   A N   1 
ATOM   2322 C CA  . ILE   A 1 300 ? 6.548   -1.852  -10.224 1.00 34.05  ? 296 ILE   A CA  1 
ATOM   2323 C C   . ILE   A 1 300 ? 6.376   -2.522  -8.869  1.00 48.54  ? 296 ILE   A C   1 
ATOM   2324 O O   . ILE   A 1 300 ? 5.422   -3.278  -8.657  1.00 49.79  ? 296 ILE   A O   1 
ATOM   2325 C CB  . ILE   A 1 300 ? 5.763   -0.524  -10.276 1.00 38.64  ? 296 ILE   A CB  1 
ATOM   2326 C CG1 . ILE   A 1 300 ? 5.675   -0.010  -11.708 1.00 41.63  ? 296 ILE   A CG1 1 
ATOM   2327 C CG2 . ILE   A 1 300 ? 6.420   0.525   -9.389  1.00 43.10  ? 296 ILE   A CG2 1 
ATOM   2328 C CD1 . ILE   A 1 300 ? 6.962   0.598   -12.221 1.00 50.19  ? 296 ILE   A CD1 1 
ATOM   2329 N N   . ASN   A 1 301 ? 7.300   -2.240  -7.953  1.00 46.32  ? 297 ASN   A N   1 
ATOM   2330 C CA  . ASN   A 1 301 ? 7.315   -2.862  -6.635  1.00 52.08  ? 297 ASN   A CA  1 
ATOM   2331 C C   . ASN   A 1 301 ? 7.417   -1.774  -5.579  1.00 52.86  ? 297 ASN   A C   1 
ATOM   2332 O O   . ASN   A 1 301 ? 8.346   -0.962  -5.612  1.00 47.15  ? 297 ASN   A O   1 
ATOM   2333 C CB  . ASN   A 1 301 ? 8.483   -3.844  -6.509  1.00 54.49  ? 297 ASN   A CB  1 
ATOM   2334 C CG  . ASN   A 1 301 ? 8.663   -4.694  -7.751  1.00 65.10  ? 297 ASN   A CG  1 
ATOM   2335 O OD1 . ASN   A 1 301 ? 7.817   -5.528  -8.075  1.00 62.30  ? 297 ASN   A OD1 1 
ATOM   2336 N ND2 . ASN   A 1 301 ? 9.766   -4.480  -8.461  1.00 60.09  ? 297 ASN   A ND2 1 
ATOM   2337 N N   . ALA   A 1 302 ? 6.468   -1.759  -4.647  1.00 49.88  ? 298 ALA   A N   1 
ATOM   2338 C CA  . ALA   A 1 302 ? 6.507   -0.815  -3.539  1.00 52.11  ? 298 ALA   A CA  1 
ATOM   2339 C C   . ALA   A 1 302 ? 7.411   -1.349  -2.436  1.00 41.97  ? 298 ALA   A C   1 
ATOM   2340 O O   . ALA   A 1 302 ? 7.211   -2.467  -1.953  1.00 50.64  ? 298 ALA   A O   1 
ATOM   2341 C CB  . ALA   A 1 302 ? 5.101   -0.566  -2.994  1.00 48.40  ? 298 ALA   A CB  1 
ATOM   2342 N N   . PHE   A 1 303 ? 8.406   -0.539  -2.042  1.00 46.45  ? 299 PHE   A N   1 
ATOM   2343 C CA  . PHE   A 1 303 ? 9.393   -0.829  -1.003  1.00 46.11  ? 299 PHE   A CA  1 
ATOM   2344 C C   . PHE   A 1 303 ? 9.802   -2.296  -1.063  1.00 50.68  ? 299 PHE   A C   1 
ATOM   2345 O O   . PHE   A 1 303 ? 9.337   -3.105  -0.252  1.00 44.86  ? 299 PHE   A O   1 
ATOM   2346 C CB  . PHE   A 1 303 ? 8.837   -0.455  0.374   1.00 45.85  ? 299 PHE   A CB  1 
ATOM   2347 C CG  . PHE   A 1 303 ? 9.830   -0.600  1.499   1.00 51.52  ? 299 PHE   A CG  1 
ATOM   2348 C CD1 . PHE   A 1 303 ? 11.184  -0.399  1.283   1.00 61.91  ? 299 PHE   A CD1 1 
ATOM   2349 C CD2 . PHE   A 1 303 ? 9.400   -0.884  2.784   1.00 59.27  ? 299 PHE   A CD2 1 
ATOM   2350 C CE1 . PHE   A 1 303 ? 12.092  -0.519  2.319   1.00 62.70  ? 299 PHE   A CE1 1 
ATOM   2351 C CE2 . PHE   A 1 303 ? 10.303  -0.999  3.824   1.00 57.32  ? 299 PHE   A CE2 1 
ATOM   2352 C CZ  . PHE   A 1 303 ? 11.650  -0.815  3.591   1.00 55.32  ? 299 PHE   A CZ  1 
ATOM   2353 N N   . PRO   A 1 304 ? 10.648  -2.679  -2.021  1.00 46.29  ? 300 PRO   A N   1 
ATOM   2354 C CA  . PRO   A 1 304 ? 10.946  -4.104  -2.222  1.00 40.70  ? 300 PRO   A CA  1 
ATOM   2355 C C   . PRO   A 1 304 ? 11.916  -4.670  -1.199  1.00 48.78  ? 300 PRO   A C   1 
ATOM   2356 O O   . PRO   A 1 304 ? 12.185  -4.050  -0.166  1.00 51.40  ? 300 PRO   A O   1 
ATOM   2357 C CB  . PRO   A 1 304 ? 11.548  -4.132  -3.631  1.00 44.90  ? 300 PRO   A CB  1 
ATOM   2358 C CG  . PRO   A 1 304 ? 12.171  -2.787  -3.783  1.00 46.99  ? 300 PRO   A CG  1 
ATOM   2359 C CD  . PRO   A 1 304 ? 11.274  -1.831  -3.050  1.00 42.33  ? 300 PRO   A CD  1 
ATOM   2360 N N   . GLY   A 1 305 ? 12.441  -5.866  -1.481  1.00 51.56  ? 301 GLY   A N   1 
ATOM   2361 C CA  . GLY   A 1 305 ? 13.351  -6.516  -0.557  1.00 56.18  ? 301 GLY   A CA  1 
ATOM   2362 C C   . GLY   A 1 305 ? 14.776  -6.017  -0.617  1.00 47.22  ? 301 GLY   A C   1 
ATOM   2363 O O   . GLY   A 1 305 ? 15.525  -6.214  0.345   1.00 56.86  ? 301 GLY   A O   1 
ATOM   2364 N N   . TYR   A 1 306 ? 15.164  -5.373  -1.721  1.00 47.13  ? 302 TYR   A N   1 
ATOM   2365 C CA  . TYR   A 1 306 ? 16.533  -4.890  -1.915  1.00 53.72  ? 302 TYR   A CA  1 
ATOM   2366 C C   . TYR   A 1 306 ? 17.544  -6.003  -1.653  1.00 66.69  ? 302 TYR   A C   1 
ATOM   2367 O O   . TYR   A 1 306 ? 18.582  -5.794  -1.022  1.00 66.51  ? 302 TYR   A O   1 
ATOM   2368 C CB  . TYR   A 1 306 ? 16.820  -3.672  -1.033  1.00 50.13  ? 302 TYR   A CB  1 
ATOM   2369 C CG  . TYR   A 1 306 ? 15.914  -2.489  -1.296  1.00 48.18  ? 302 TYR   A CG  1 
ATOM   2370 C CD1 . TYR   A 1 306 ? 16.244  -1.535  -2.250  1.00 36.73  ? 302 TYR   A CD1 1 
ATOM   2371 C CD2 . TYR   A 1 306 ? 14.735  -2.320  -0.583  1.00 45.90  ? 302 TYR   A CD2 1 
ATOM   2372 C CE1 . TYR   A 1 306 ? 15.420  -0.453  -2.494  1.00 40.76  ? 302 TYR   A CE1 1 
ATOM   2373 C CE2 . TYR   A 1 306 ? 13.905  -1.239  -0.818  1.00 41.79  ? 302 TYR   A CE2 1 
ATOM   2374 C CZ  . TYR   A 1 306 ? 14.253  -0.308  -1.774  1.00 42.81  ? 302 TYR   A CZ  1 
ATOM   2375 O OH  . TYR   A 1 306 ? 13.431  0.770   -2.013  1.00 35.67  ? 302 TYR   A OH  1 
ATOM   2376 N N   . GLU   A 1 307 ? 17.226  -7.203  -2.142  1.00 73.64  ? 303 GLU   A N   1 
ATOM   2377 C CA  . GLU   A 1 307 ? 17.995  -8.404  -1.840  1.00 77.58  ? 303 GLU   A CA  1 
ATOM   2378 C C   . GLU   A 1 307 ? 19.452  -8.267  -2.264  1.00 81.24  ? 303 GLU   A C   1 
ATOM   2379 O O   . GLU   A 1 307 ? 19.757  -8.210  -3.460  1.00 78.71  ? 303 GLU   A O   1 
ATOM   2380 C CB  . GLU   A 1 307 ? 17.367  -9.623  -2.519  1.00 80.75  ? 303 GLU   A CB  1 
ATOM   2381 C CG  . GLU   A 1 307 ? 18.260  -10.852 -2.526  1.00 88.88  ? 303 GLU   A CG  1 
ATOM   2382 C CD  . GLU   A 1 307 ? 17.510  -12.116 -2.885  1.00 88.85  ? 303 GLU   A CD  1 
ATOM   2383 O OE1 . GLU   A 1 307 ? 16.320  -12.020 -3.251  1.00 72.72  ? 303 GLU   A OE1 1 
ATOM   2384 O OE2 . GLU   A 1 307 ? 18.107  -13.209 -2.788  1.00 89.16  ? 303 GLU   A OE2 1 
ATOM   2385 N N   . GLY   A 1 308 ? 20.354  -8.202  -1.288  1.00 73.83  ? 304 GLY   A N   1 
ATOM   2386 C CA  . GLY   A 1 308 ? 21.776  -8.159  -1.565  1.00 69.98  ? 304 GLY   A CA  1 
ATOM   2387 C C   . GLY   A 1 308 ? 22.245  -6.921  -2.303  1.00 70.00  ? 304 GLY   A C   1 
ATOM   2388 O O   . GLY   A 1 308 ? 23.393  -6.871  -2.754  1.00 74.80  ? 304 GLY   A O   1 
ATOM   2389 N N   . VAL   A 1 309 ? 21.365  -5.924  -2.447  1.00 71.64  ? 305 VAL   A N   1 
ATOM   2390 C CA  . VAL   A 1 309 ? 21.763  -4.654  -3.044  1.00 64.73  ? 305 VAL   A CA  1 
ATOM   2391 C C   . VAL   A 1 309 ? 22.953  -4.073  -2.299  1.00 54.52  ? 305 VAL   A C   1 
ATOM   2392 O O   . VAL   A 1 309 ? 22.961  -3.988  -1.065  1.00 57.15  ? 305 VAL   A O   1 
ATOM   2393 C CB  . VAL   A 1 309 ? 20.583  -3.672  -3.069  1.00 55.38  ? 305 VAL   A CB  1 
ATOM   2394 C CG1 . VAL   A 1 309 ? 21.068  -2.280  -3.437  1.00 52.41  ? 305 VAL   A CG1 1 
ATOM   2395 C CG2 . VAL   A 1 309 ? 19.572  -4.122  -4.105  1.00 59.43  ? 305 VAL   A CG2 1 
ATOM   2396 N N   . SER   A 1 310 ? 23.969  -3.675  -3.058  1.00 64.52  ? 306 SER   A N   1 
ATOM   2397 C CA  . SER   A 1 310 ? 25.186  -3.118  -2.487  1.00 53.63  ? 306 SER   A CA  1 
ATOM   2398 C C   . SER   A 1 310 ? 24.894  -1.770  -1.838  1.00 56.54  ? 306 SER   A C   1 
ATOM   2399 O O   . SER   A 1 310 ? 24.370  -0.860  -2.491  1.00 59.85  ? 306 SER   A O   1 
ATOM   2400 C CB  . SER   A 1 310 ? 26.247  -2.976  -3.575  1.00 47.52  ? 306 SER   A CB  1 
ATOM   2401 O OG  . SER   A 1 310 ? 27.518  -2.677  -3.024  1.00 60.07  ? 306 SER   A OG  1 
ATOM   2402 N N   . GLU   A 1 311 ? 25.205  -1.663  -0.543  1.00 50.91  ? 307 GLU   A N   1 
ATOM   2403 C CA  . GLU   A 1 311 ? 25.229  -0.401  0.193   1.00 56.69  ? 307 GLU   A CA  1 
ATOM   2404 C C   . GLU   A 1 311 ? 23.823  0.126   0.470   1.00 54.85  ? 307 GLU   A C   1 
ATOM   2405 O O   . GLU   A 1 311 ? 23.604  1.341   0.503   1.00 52.50  ? 307 GLU   A O   1 
ATOM   2406 C CB  . GLU   A 1 311 ? 26.056  0.633   -0.578  1.00 57.65  ? 307 GLU   A CB  1 
ATOM   2407 C CG  . GLU   A 1 311 ? 26.807  1.629   0.276   1.00 72.70  ? 307 GLU   A CG  1 
ATOM   2408 C CD  . GLU   A 1 311 ? 27.814  2.422   -0.532  1.00 78.95  ? 307 GLU   A CD  1 
ATOM   2409 O OE1 . GLU   A 1 311 ? 28.831  2.858   0.044   1.00 72.35  ? 307 GLU   A OE1 1 
ATOM   2410 O OE2 . GLU   A 1 311 ? 27.586  2.606   -1.748  1.00 83.92  ? 307 GLU   A OE2 1 
ATOM   2411 N N   . PHE   A 1 312 ? 22.870  -0.782  0.701   1.00 50.21  ? 308 PHE   A N   1 
ATOM   2412 C CA  . PHE   A 1 312 ? 21.478  -0.375  0.879   1.00 52.25  ? 308 PHE   A CA  1 
ATOM   2413 C C   . PHE   A 1 312 ? 21.255  0.297   2.229   1.00 47.44  ? 308 PHE   A C   1 
ATOM   2414 O O   . PHE   A 1 312 ? 20.547  1.308   2.313   1.00 46.01  ? 308 PHE   A O   1 
ATOM   2415 C CB  . PHE   A 1 312 ? 20.556  -1.585  0.720   1.00 50.00  ? 308 PHE   A CB  1 
ATOM   2416 C CG  . PHE   A 1 312 ? 19.184  -1.386  1.300   1.00 47.31  ? 308 PHE   A CG  1 
ATOM   2417 C CD1 . PHE   A 1 312 ? 18.293  -0.495  0.724   1.00 48.78  ? 308 PHE   A CD1 1 
ATOM   2418 C CD2 . PHE   A 1 312 ? 18.782  -2.098  2.418   1.00 50.97  ? 308 PHE   A CD2 1 
ATOM   2419 C CE1 . PHE   A 1 312 ? 17.029  -0.314  1.255   1.00 49.26  ? 308 PHE   A CE1 1 
ATOM   2420 C CE2 . PHE   A 1 312 ? 17.519  -1.921  2.955   1.00 52.52  ? 308 PHE   A CE2 1 
ATOM   2421 C CZ  . PHE   A 1 312 ? 16.642  -1.029  2.372   1.00 44.06  ? 308 PHE   A CZ  1 
ATOM   2422 N N   . PHE   A 1 313 ? 21.840  -0.252  3.298   1.00 45.90  ? 309 PHE   A N   1 
ATOM   2423 C CA  . PHE   A 1 313 ? 21.683  0.352   4.619   1.00 52.51  ? 309 PHE   A CA  1 
ATOM   2424 C C   . PHE   A 1 313 ? 22.240  1.770   4.645   1.00 49.72  ? 309 PHE   A C   1 
ATOM   2425 O O   . PHE   A 1 313 ? 21.669  2.658   5.290   1.00 43.55  ? 309 PHE   A O   1 
ATOM   2426 C CB  . PHE   A 1 313 ? 22.371  -0.510  5.679   1.00 46.26  ? 309 PHE   A CB  1 
ATOM   2427 C CG  . PHE   A 1 313 ? 21.581  -1.724  6.089   1.00 45.03  ? 309 PHE   A CG  1 
ATOM   2428 C CD1 . PHE   A 1 313 ? 20.324  -1.967  5.559   1.00 43.07  ? 309 PHE   A CD1 1 
ATOM   2429 C CD2 . PHE   A 1 313 ? 22.100  -2.623  7.006   1.00 42.66  ? 309 PHE   A CD2 1 
ATOM   2430 C CE1 . PHE   A 1 313 ? 19.601  -3.084  5.936   1.00 41.62  ? 309 PHE   A CE1 1 
ATOM   2431 C CE2 . PHE   A 1 313 ? 21.383  -3.741  7.388   1.00 47.01  ? 309 PHE   A CE2 1 
ATOM   2432 C CZ  . PHE   A 1 313 ? 20.132  -3.972  6.852   1.00 43.33  ? 309 PHE   A CZ  1 
ATOM   2433 N N   . THR   A 1 314 ? 23.353  2.000   3.946   1.00 46.36  ? 310 THR   A N   1 
ATOM   2434 C CA  . THR   A 1 314 ? 23.938  3.336   3.901   1.00 45.44  ? 310 THR   A CA  1 
ATOM   2435 C C   . THR   A 1 314 ? 23.052  4.301   3.125   1.00 53.65  ? 310 THR   A C   1 
ATOM   2436 O O   . THR   A 1 314 ? 22.838  5.440   3.555   1.00 44.31  ? 310 THR   A O   1 
ATOM   2437 C CB  . THR   A 1 314 ? 25.333  3.277   3.282   1.00 48.06  ? 310 THR   A CB  1 
ATOM   2438 O OG1 . THR   A 1 314 ? 26.106  2.268   3.943   1.00 66.69  ? 310 THR   A OG1 1 
ATOM   2439 C CG2 . THR   A 1 314 ? 26.035  4.618   3.418   1.00 60.82  ? 310 THR   A CG2 1 
ATOM   2440 N N   . ASP   A 1 315 ? 22.528  3.865   1.978   1.00 46.80  ? 311 ASP   A N   1 
ATOM   2441 C CA  . ASP   A 1 315 ? 21.628  4.719   1.215   1.00 45.87  ? 311 ASP   A CA  1 
ATOM   2442 C C   . ASP   A 1 315 ? 20.324  4.963   1.964   1.00 45.95  ? 311 ASP   A C   1 
ATOM   2443 O O   . ASP   A 1 315 ? 19.659  5.978   1.732   1.00 40.95  ? 311 ASP   A O   1 
ATOM   2444 C CB  . ASP   A 1 315 ? 21.355  4.101   -0.156  1.00 49.04  ? 311 ASP   A CB  1 
ATOM   2445 C CG  . ASP   A 1 315 ? 22.582  4.106   -1.052  1.00 51.53  ? 311 ASP   A CG  1 
ATOM   2446 O OD1 . ASP   A 1 315 ? 23.431  5.009   -0.895  1.00 58.55  ? 311 ASP   A OD1 1 
ATOM   2447 O OD2 . ASP   A 1 315 ? 22.700  3.208   -1.913  1.00 60.57  ? 311 ASP   A OD2 1 
ATOM   2448 N N   . LEU   A 1 316 ? 19.948  4.061   2.875   1.00 43.81  ? 312 LEU   A N   1 
ATOM   2449 C CA  . LEU   A 1 316 ? 18.694  4.240   3.601   1.00 48.01  ? 312 LEU   A CA  1 
ATOM   2450 C C   . LEU   A 1 316 ? 18.824  5.300   4.691   1.00 46.20  ? 312 LEU   A C   1 
ATOM   2451 O O   . LEU   A 1 316 ? 17.920  6.127   4.856   1.00 47.18  ? 312 LEU   A O   1 
ATOM   2452 C CB  . LEU   A 1 316 ? 18.210  2.905   4.175   1.00 56.64  ? 312 LEU   A CB  1 
ATOM   2453 C CG  . LEU   A 1 316 ? 16.769  2.892   4.708   1.00 48.63  ? 312 LEU   A CG  1 
ATOM   2454 C CD1 . LEU   A 1 316 ? 15.790  3.445   3.679   1.00 52.29  ? 312 LEU   A CD1 1 
ATOM   2455 C CD2 . LEU   A 1 316 ? 16.356  1.488   5.132   1.00 41.54  ? 312 LEU   A CD2 1 
ATOM   2456 N N   . LEU   A 1 317 ? 19.928  5.300   5.451   1.00 47.00  ? 313 LEU   A N   1 
ATOM   2457 C CA  . LEU   A 1 317 ? 20.197  6.442   6.329   1.00 45.70  ? 313 LEU   A CA  1 
ATOM   2458 C C   . LEU   A 1 317 ? 20.240  7.752   5.563   1.00 45.43  ? 313 LEU   A C   1 
ATOM   2459 O O   . LEU   A 1 317 ? 19.551  8.714   5.925   1.00 52.21  ? 313 LEU   A O   1 
ATOM   2460 C CB  . LEU   A 1 317 ? 21.493  6.279   7.126   1.00 52.91  ? 313 LEU   A CB  1 
ATOM   2461 C CG  . LEU   A 1 317 ? 21.564  5.417   8.366   1.00 64.61  ? 313 LEU   A CG  1 
ATOM   2462 C CD1 . LEU   A 1 317 ? 22.995  5.321   8.848   1.00 66.07  ? 313 LEU   A CD1 1 
ATOM   2463 C CD2 . LEU   A 1 317 ? 20.734  6.147   9.405   1.00 54.24  ? 313 LEU   A CD2 1 
ATOM   2464 N N   . ASN   A 1 318 ? 21.065  7.819   4.520   1.00 44.58  ? 314 ASN   A N   1 
ATOM   2465 C CA  . ASN   A 1 318 ? 21.210  9.078   3.802   1.00 51.82  ? 314 ASN   A CA  1 
ATOM   2466 C C   . ASN   A 1 318 ? 19.870  9.581   3.284   1.00 43.95  ? 314 ASN   A C   1 
ATOM   2467 O O   . ASN   A 1 318 ? 19.649  10.796  3.210   1.00 51.54  ? 314 ASN   A O   1 
ATOM   2468 C CB  . ASN   A 1 318 ? 22.219  8.925   2.662   1.00 46.94  ? 314 ASN   A CB  1 
ATOM   2469 C CG  . ASN   A 1 318 ? 23.603  8.549   3.164   1.00 60.90  ? 314 ASN   A CG  1 
ATOM   2470 O OD1 . ASN   A 1 318 ? 23.992  8.922   4.275   1.00 60.40  ? 314 ASN   A OD1 1 
ATOM   2471 N ND2 . ASN   A 1 318 ? 24.354  7.822   2.351   1.00 68.28  ? 314 ASN   A ND2 1 
ATOM   2472 N N   . HIS   A 1 319 ? 18.952  8.668   2.965   1.00 50.39  ? 315 HIS   A N   1 
ATOM   2473 C CA  . HIS   A 1 319 ? 17.605  9.078   2.588   1.00 49.86  ? 315 HIS   A CA  1 
ATOM   2474 C C   . HIS   A 1 319 ? 16.832  9.615   3.787   1.00 53.28  ? 315 HIS   A C   1 
ATOM   2475 O O   . HIS   A 1 319 ? 16.160  10.648  3.685   1.00 42.71  ? 315 HIS   A O   1 
ATOM   2476 C CB  . HIS   A 1 319 ? 16.859  7.905   1.953   1.00 42.68  ? 315 HIS   A CB  1 
ATOM   2477 C CG  . HIS   A 1 319 ? 15.467  8.243   1.524   1.00 52.50  ? 315 HIS   A CG  1 
ATOM   2478 N ND1 . HIS   A 1 319 ? 15.138  9.461   0.970   1.00 48.23  ? 315 HIS   A ND1 1 
ATOM   2479 C CD2 . HIS   A 1 319 ? 14.320  7.526   1.567   1.00 42.88  ? 315 HIS   A CD2 1 
ATOM   2480 C CE1 . HIS   A 1 319 ? 13.847  9.479   0.690   1.00 46.02  ? 315 HIS   A CE1 1 
ATOM   2481 N NE2 . HIS   A 1 319 ? 13.328  8.317   1.043   1.00 51.40  ? 315 HIS   A NE2 1 
ATOM   2482 N N   . ILE   A 1 320 ? 16.911  8.928   4.931   1.00 43.57  ? 316 ILE   A N   1 
ATOM   2483 C CA  . ILE   A 1 320 ? 16.214  9.393   6.128   1.00 48.27  ? 316 ILE   A CA  1 
ATOM   2484 C C   . ILE   A 1 320 ? 16.786  10.727  6.591   1.00 55.48  ? 316 ILE   A C   1 
ATOM   2485 O O   . ILE   A 1 320 ? 16.047  11.626  7.011   1.00 51.85  ? 316 ILE   A O   1 
ATOM   2486 C CB  . ILE   A 1 320 ? 16.285  8.327   7.239   1.00 46.96  ? 316 ILE   A CB  1 
ATOM   2487 C CG1 . ILE   A 1 320 ? 15.516  7.072   6.823   1.00 40.32  ? 316 ILE   A CG1 1 
ATOM   2488 C CG2 . ILE   A 1 320 ? 15.737  8.874   8.551   1.00 43.32  ? 316 ILE   A CG2 1 
ATOM   2489 C CD1 . ILE   A 1 320 ? 15.746  5.887   7.734   1.00 48.82  ? 316 ILE   A CD1 1 
ATOM   2490 N N   . ALA   A 1 321 ? 18.109  10.882  6.514   1.00 53.51  ? 317 ALA   A N   1 
ATOM   2491 C CA  . ALA   A 1 321 ? 18.720  12.159  6.864   1.00 52.08  ? 317 ALA   A CA  1 
ATOM   2492 C C   . ALA   A 1 321 ? 18.368  13.245  5.856   1.00 52.97  ? 317 ALA   A C   1 
ATOM   2493 O O   . ALA   A 1 321 ? 18.264  14.420  6.226   1.00 63.54  ? 317 ALA   A O   1 
ATOM   2494 C CB  . ALA   A 1 321 ? 20.237  12.005  6.972   1.00 43.81  ? 317 ALA   A CB  1 
ATOM   2495 N N   . THR   A 1 322 ? 18.173  12.875  4.588   1.00 61.25  ? 318 THR   A N   1 
ATOM   2496 C CA  . THR   A 1 322 ? 17.853  13.865  3.564   1.00 60.29  ? 318 THR   A CA  1 
ATOM   2497 C C   . THR   A 1 322 ? 16.469  14.463  3.786   1.00 65.06  ? 318 THR   A C   1 
ATOM   2498 O O   . THR   A 1 322 ? 16.303  15.689  3.782   1.00 72.83  ? 318 THR   A O   1 
ATOM   2499 C CB  . THR   A 1 322 ? 17.946  13.233  2.174   1.00 65.42  ? 318 THR   A CB  1 
ATOM   2500 O OG1 . THR   A 1 322 ? 19.316  12.943  1.869   1.00 67.32  ? 318 THR   A OG1 1 
ATOM   2501 C CG2 . THR   A 1 322 ? 17.385  14.174  1.117   1.00 70.80  ? 318 THR   A CG2 1 
ATOM   2502 N N   . VAL   A 1 323 ? 15.459  13.611  3.984   1.00 62.72  ? 319 VAL   A N   1 
ATOM   2503 C CA  . VAL   A 1 323 ? 14.099  14.103  4.171   1.00 64.51  ? 319 VAL   A CA  1 
ATOM   2504 C C   . VAL   A 1 323 ? 13.958  14.901  5.460   1.00 65.51  ? 319 VAL   A C   1 
ATOM   2505 O O   . VAL   A 1 323 ? 13.062  15.746  5.565   1.00 68.30  ? 319 VAL   A O   1 
ATOM   2506 C CB  . VAL   A 1 323 ? 13.091  12.938  4.143   1.00 60.77  ? 319 VAL   A CB  1 
ATOM   2507 C CG1 . VAL   A 1 323 ? 13.097  12.264  2.780   1.00 55.66  ? 319 VAL   A CG1 1 
ATOM   2508 C CG2 . VAL   A 1 323 ? 13.399  11.934  5.243   1.00 47.34  ? 319 VAL   A CG2 1 
ATOM   2509 N N   . LEU   A 1 324 ? 14.824  14.661  6.446   1.00 64.54  ? 320 LEU   A N   1 
ATOM   2510 C CA  . LEU   A 1 324 ? 14.784  15.427  7.683   1.00 63.91  ? 320 LEU   A CA  1 
ATOM   2511 C C   . LEU   A 1 324 ? 15.445  16.793  7.548   1.00 78.19  ? 320 LEU   A C   1 
ATOM   2512 O O   . LEU   A 1 324 ? 15.234  17.655  8.407   1.00 85.08  ? 320 LEU   A O   1 
ATOM   2513 C CB  . LEU   A 1 324 ? 15.450  14.638  8.812   1.00 68.70  ? 320 LEU   A CB  1 
ATOM   2514 C CG  . LEU   A 1 324 ? 14.649  13.449  9.347   1.00 60.21  ? 320 LEU   A CG  1 
ATOM   2515 C CD1 . LEU   A 1 324 ? 15.530  12.530  10.180  1.00 42.86  ? 320 LEU   A CD1 1 
ATOM   2516 C CD2 . LEU   A 1 324 ? 13.454  13.932  10.155  1.00 64.00  ? 320 LEU   A CD2 1 
ATOM   2517 N N   . GLN   A 1 325 ? 16.233  17.008  6.496   1.00 82.22  ? 321 GLN   A N   1 
ATOM   2518 C CA  . GLN   A 1 325 ? 16.862  18.299  6.251   1.00 80.81  ? 321 GLN   A CA  1 
ATOM   2519 C C   . GLN   A 1 325 ? 15.938  19.286  5.551   1.00 81.69  ? 321 GLN   A C   1 
ATOM   2520 O O   . GLN   A 1 325 ? 16.370  20.403  5.246   1.00 96.12  ? 321 GLN   A O   1 
ATOM   2521 C CB  . GLN   A 1 325 ? 18.138  18.116  5.423   1.00 76.34  ? 321 GLN   A CB  1 
ATOM   2522 C CG  . GLN   A 1 325 ? 19.292  17.484  6.186   1.00 66.53  ? 321 GLN   A CG  1 
ATOM   2523 C CD  . GLN   A 1 325 ? 20.528  17.301  5.327   1.00 67.23  ? 321 GLN   A CD  1 
ATOM   2524 O OE1 . GLN   A 1 325 ? 20.441  17.233  4.101   1.00 68.91  ? 321 GLN   A OE1 1 
ATOM   2525 N NE2 . GLN   A 1 325 ? 21.688  17.218  5.968   1.00 57.51  ? 321 GLN   A NE2 1 
ATOM   2526 N N   . GLY   A 1 326 ? 14.691  18.909  5.290   1.00 77.02  ? 322 GLY   A N   1 
ATOM   2527 C CA  . GLY   A 1 326 ? 13.745  19.795  4.638   1.00 77.90  ? 322 GLY   A CA  1 
ATOM   2528 C C   . GLY   A 1 326 ? 12.648  20.278  5.566   1.00 83.23  ? 322 GLY   A C   1 
ATOM   2529 O O   . GLY   A 1 326 ? 12.504  19.783  6.684   1.00 87.55  ? 322 GLY   A O   1 
HETATM 2530 S S   . SO4   B 2 .   ? 4.926   -15.980 -4.086  1.00 51.22  ? 401 SO4   A S   1 
HETATM 2531 O O1  . SO4   B 2 .   ? 4.401   -16.257 -5.420  1.00 55.71  ? 401 SO4   A O1  1 
HETATM 2532 O O2  . SO4   B 2 .   ? 4.840   -14.547 -3.817  1.00 59.45  ? 401 SO4   A O2  1 
HETATM 2533 O O3  . SO4   B 2 .   ? 4.142   -16.711 -3.093  1.00 62.76  ? 401 SO4   A O3  1 
HETATM 2534 O O4  . SO4   B 2 .   ? 6.321   -16.405 -4.016  1.00 67.23  ? 401 SO4   A O4  1 
HETATM 2535 C C1  . A1A7Y C 3 .   ? 9.137   -10.765 -20.460 1.00 32.54  ? 402 A1A7Y A C1  1 
HETATM 2536 C C2  . A1A7Y C 3 .   ? 8.499   -10.623 -18.373 1.00 38.76  ? 402 A1A7Y A C2  1 
HETATM 2537 C C3  . A1A7Y C 3 .   ? 7.384   -9.883  -18.699 1.00 36.96  ? 402 A1A7Y A C3  1 
HETATM 2538 C C7  . A1A7Y C 3 .   ? 10.865  -11.164 -16.221 1.00 44.88  ? 402 A1A7Y A C7  1 
HETATM 2539 N N2  . A1A7Y C 3 .   ? 9.425   -11.099 -19.207 1.00 34.81  ? 402 A1A7Y A N2  1 
HETATM 2540 C C4  . A1A7Y C 3 .   ? 7.182   -9.599  -20.056 1.00 36.53  ? 402 A1A7Y A C4  1 
HETATM 2541 N N1  . A1A7Y C 3 .   ? 8.101   -10.064 -20.932 1.00 33.77  ? 402 A1A7Y A N1  1 
HETATM 2542 C C5  . A1A7Y C 3 .   ? 7.324   -10.108 -16.580 1.00 38.83  ? 402 A1A7Y A C5  1 
HETATM 2543 C C6  . A1A7Y C 3 .   ? 9.379   -11.455 -16.080 1.00 46.99  ? 402 A1A7Y A C6  1 
HETATM 2544 C C10 . A1A7Y C 3 .   ? 9.366   -12.978 -16.132 1.00 37.81  ? 402 A1A7Y A C10 1 
HETATM 2545 C C8  . A1A7Y C 3 .   ? 11.393  -12.102 -15.148 1.00 43.92  ? 402 A1A7Y A C8  1 
HETATM 2546 C C9  . A1A7Y C 3 .   ? 10.600  -13.353 -15.317 1.00 47.82  ? 402 A1A7Y A C9  1 
HETATM 2547 N N3  . A1A7Y C 3 .   ? 8.467   -10.772 -16.993 1.00 43.34  ? 402 A1A7Y A N3  1 
HETATM 2548 N N4  . A1A7Y C 3 .   ? 6.663   -9.569  -17.579 1.00 43.11  ? 402 A1A7Y A N4  1 
HETATM 2549 N N5  . A1A7Y C 3 .   ? 6.150   -8.896  -20.510 1.00 31.45  ? 402 A1A7Y A N5  1 
HETATM 2550 O O   . HOH   D 4 .   ? 7.329   -9.759  -13.381 1.00 52.21  ? 501 HOH   A O   1 
HETATM 2551 O O   . HOH   D 4 .   ? -4.848  -5.412  -11.021 1.00 56.34  ? 502 HOH   A O   1 
HETATM 2552 O O   . HOH   D 4 .   ? 7.055   2.547   -0.605  1.00 45.87  ? 503 HOH   A O   1 
HETATM 2553 O O   . HOH   D 4 .   ? 5.189   -8.758  -9.435  1.00 53.02  ? 504 HOH   A O   1 
HETATM 2554 O O   . HOH   D 4 .   ? 4.905   -4.758  5.510   1.00 46.75  ? 505 HOH   A O   1 
HETATM 2555 O O   . HOH   D 4 .   ? 5.779   18.019  -14.599 1.00 77.09  ? 506 HOH   A O   1 
HETATM 2556 O O   . HOH   D 4 .   ? 13.435  -2.333  16.799  1.00 48.97  ? 507 HOH   A O   1 
HETATM 2557 O O   . HOH   D 4 .   ? 16.546  -7.291  -21.234 1.00 32.90  ? 508 HOH   A O   1 
HETATM 2558 O O   . HOH   D 4 .   ? 5.926   2.333   1.977   1.00 48.66  ? 509 HOH   A O   1 
HETATM 2559 O O   . HOH   D 4 .   ? 17.665  -22.524 -9.867  1.00 86.94  ? 510 HOH   A O   1 
HETATM 2560 O O   . HOH   D 4 .   ? 4.491   13.263  15.955  1.00 61.05  ? 511 HOH   A O   1 
HETATM 2561 O O   . HOH   D 4 .   ? 18.946  -15.398 -17.926 1.00 40.60  ? 512 HOH   A O   1 
HETATM 2562 O O   . HOH   D 4 .   ? 10.226  13.917  -25.396 1.00 67.57  ? 513 HOH   A O   1 
HETATM 2563 O O   . HOH   D 4 .   ? 1.911   -0.325  -18.877 1.00 43.15  ? 514 HOH   A O   1 
HETATM 2564 O O   . HOH   D 4 .   ? 2.095   -3.504  -19.553 1.00 41.71  ? 515 HOH   A O   1 
HETATM 2565 O O   . HOH   D 4 .   ? 1.358   -13.053 -10.623 1.00 30.31  ? 516 HOH   A O   1 
HETATM 2566 O O   . HOH   D 4 .   ? 2.707   -20.492 -11.604 1.00 43.97  ? 517 HOH   A O   1 
HETATM 2567 O O   . HOH   D 4 .   ? -9.654  -17.365 -28.672 1.00 60.28  ? 518 HOH   A O   1 
HETATM 2568 O O   . HOH   D 4 .   ? 5.494   -18.191 -29.127 1.00 54.69  ? 519 HOH   A O   1 
HETATM 2569 O O   . HOH   D 4 .   ? 16.843  -3.128  16.579  1.00 48.38  ? 520 HOH   A O   1 
HETATM 2570 O O   . HOH   D 4 .   ? 16.087  -18.713 -25.819 1.00 38.08  ? 521 HOH   A O   1 
HETATM 2571 O O   . HOH   D 4 .   ? 2.473   13.631  7.754   1.00 40.87  ? 522 HOH   A O   1 
HETATM 2572 O O   . HOH   D 4 .   ? 5.681   12.837  4.357   1.00 49.52  ? 523 HOH   A O   1 
HETATM 2573 O O   . HOH   D 4 .   ? 17.454  -7.458  -25.541 1.00 40.08  ? 524 HOH   A O   1 
HETATM 2574 O O   . HOH   D 4 .   ? 3.805   -9.926  -6.812  1.00 52.32  ? 525 HOH   A O   1 
HETATM 2575 O O   . HOH   D 4 .   ? 14.067  -12.907 -23.148 1.00 30.42  ? 526 HOH   A O   1 
HETATM 2576 O O   . HOH   D 4 .   ? -0.737  -25.401 -25.495 1.00 39.68  ? 527 HOH   A O   1 
HETATM 2577 O O   . HOH   D 4 .   ? 0.520   -22.380 -24.370 1.00 41.15  ? 528 HOH   A O   1 
HETATM 2578 O O   . HOH   D 4 .   ? -3.328  -8.894  3.243   1.00 63.11  ? 529 HOH   A O   1 
HETATM 2579 O O   . HOH   D 4 .   ? 9.482   -20.950 -11.158 1.00 40.75  ? 530 HOH   A O   1 
HETATM 2580 O O   . HOH   D 4 .   ? -0.614  -25.635 -22.533 1.00 44.76  ? 531 HOH   A O   1 
HETATM 2581 O O   . HOH   D 4 .   ? -14.208 -11.150 -19.131 1.00 66.83  ? 532 HOH   A O   1 
HETATM 2582 O O   . HOH   D 4 .   ? 16.231  10.928  -11.154 1.00 45.89  ? 533 HOH   A O   1 
HETATM 2583 O O   . HOH   D 4 .   ? 4.176   -7.047  3.624   1.00 61.56  ? 534 HOH   A O   1 
HETATM 2584 O O   . HOH   D 4 .   ? 11.965  -5.050  -6.787  1.00 59.39  ? 535 HOH   A O   1 
HETATM 2585 O O   . HOH   D 4 .   ? 19.854  7.815   -0.408  1.00 50.84  ? 536 HOH   A O   1 
HETATM 2586 O O   . HOH   D 4 .   ? 21.766  -7.302  -5.263  1.00 61.62  ? 537 HOH   A O   1 
HETATM 2587 O O   . HOH   D 4 .   ? -0.500  8.835   3.343   1.00 67.00  ? 538 HOH   A O   1 
HETATM 2588 O O   . HOH   D 4 .   ? 7.359   -11.635 -28.167 1.00 37.02  ? 539 HOH   A O   1 
HETATM 2589 O O   . HOH   D 4 .   ? -3.254  -20.132 -31.602 1.00 48.64  ? 540 HOH   A O   1 
HETATM 2590 O O   . HOH   D 4 .   ? 3.514   -10.895 -27.627 1.00 45.53  ? 541 HOH   A O   1 
HETATM 2591 O O   . HOH   D 4 .   ? 19.852  16.419  11.530  1.00 56.30  ? 542 HOH   A O   1 
HETATM 2592 O O   . HOH   D 4 .   ? -0.889  -13.798 -31.748 1.00 58.02  ? 543 HOH   A O   1 
HETATM 2593 O O   . HOH   D 4 .   ? 13.259  -25.519 -26.085 1.00 59.51  ? 544 HOH   A O   1 
HETATM 2594 O O   . HOH   D 4 .   ? 19.736  -6.418  -22.537 1.00 48.97  ? 545 HOH   A O   1 
HETATM 2595 O O   . HOH   D 4 .   ? 6.973   19.422  -16.003 1.00 72.70  ? 546 HOH   A O   1 
HETATM 2596 O O   . HOH   D 4 .   ? 9.129   -9.772  -28.531 1.00 44.32  ? 547 HOH   A O   1 
HETATM 2597 O O   . HOH   D 4 .   ? 15.142  3.742   20.415  1.00 58.82  ? 548 HOH   A O   1 
HETATM 2598 O O   . HOH   D 4 .   ? 18.618  14.757  -6.999  1.00 64.84  ? 549 HOH   A O   1 
HETATM 2599 O O   . HOH   D 4 .   ? 7.227   -5.088  -3.754  1.00 50.39  ? 550 HOH   A O   1 
HETATM 2600 O O   . HOH   D 4 .   ? 4.229   -6.025  -27.267 1.00 47.79  ? 551 HOH   A O   1 
HETATM 2601 O O   . HOH   D 4 .   ? 16.319  -20.750 -8.353  1.00 79.92  ? 552 HOH   A O   1 
HETATM 2602 O O   . HOH   D 4 .   ? 6.883   -22.169 -10.356 1.00 48.55  ? 553 HOH   A O   1 
HETATM 2603 O O   . HOH   D 4 .   ? 23.013  6.901   -21.022 1.00 54.99  ? 554 HOH   A O   1 
HETATM 2604 O O   . HOH   D 4 .   ? 8.385   -12.165 -0.602  1.00 60.36  ? 555 HOH   A O   1 
HETATM 2605 O O   . HOH   D 4 .   ? 24.466  5.018   -19.954 1.00 55.53  ? 556 HOH   A O   1 
HETATM 2606 O O   . HOH   D 4 .   ? 11.508  -7.018  -5.631  1.00 46.84  ? 557 HOH   A O   1 
HETATM 2607 O O   . HOH   D 4 .   ? 24.762  -6.744  -11.230 1.00 51.58  ? 558 HOH   A O   1 
HETATM 2608 O O   . HOH   D 4 .   ? -2.397  -17.490 -14.219 1.00 45.37  ? 559 HOH   A O   1 
HETATM 2609 O O   . HOH   D 4 .   ? 10.616  -21.568 -29.401 1.00 45.50  ? 560 HOH   A O   1 
HETATM 2610 O O   . HOH   D 4 .   ? 14.021  -7.930  -4.362  1.00 54.76  ? 561 HOH   A O   1 
HETATM 2611 O O   . HOH   D 4 .   ? 15.538  -18.669 5.645   1.00 89.41  ? 562 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . LEU   A 9   ? 0.9216 0.8153 0.7941 -0.1275 -0.0630 -0.1268 5   LEU   A N   
2    C CA  . LEU   A 9   ? 0.9026 0.8068 0.7843 -0.1093 -0.0619 -0.1156 5   LEU   A CA  
3    C C   . LEU   A 9   ? 1.0574 0.9727 0.9300 -0.0992 -0.0665 -0.1169 5   LEU   A C   
4    O O   . LEU   A 9   ? 0.9385 0.8528 0.8103 -0.0851 -0.0639 -0.1092 5   LEU   A O   
5    C CB  . LEU   A 9   ? 0.9144 0.8471 0.8176 -0.1096 -0.0645 -0.1089 5   LEU   A CB  
6    C CG  . LEU   A 9   ? 0.9328 0.8683 0.8456 -0.0936 -0.0613 -0.0966 5   LEU   A CG  
7    C CD1 . LEU   A 9   ? 0.7553 0.6599 0.6636 -0.0899 -0.0525 -0.0920 5   LEU   A CD1 
8    C CD2 . LEU   A 9   ? 0.9832 0.9478 0.9164 -0.0943 -0.0646 -0.0922 5   LEU   A CD2 
9    N N   . LYS   A 10  ? 1.0805 1.0061 0.9449 -0.1077 -0.0734 -0.1268 6   LYS   A N   
10   C CA  . LYS   A 10  ? 1.2349 1.1665 1.0850 -0.0998 -0.0781 -0.1289 6   LYS   A CA  
11   C C   . LYS   A 10  ? 1.2079 1.1099 1.0394 -0.0944 -0.0702 -0.1316 6   LYS   A C   
12   O O   . LYS   A 10  ? 1.1350 1.0126 0.9586 -0.1015 -0.0655 -0.1387 6   LYS   A O   
13   C CB  . LYS   A 10  ? 1.1031 1.0531 0.9483 -0.1110 -0.0881 -0.1402 6   LYS   A CB  
14   C CG  . LYS   A 10  ? 1.0871 1.0469 0.9165 -0.1029 -0.0953 -0.1418 6   LYS   A CG  
15   C CD  . LYS   A 10  ? 1.0149 0.9921 0.8390 -0.1148 -0.1056 -0.1546 6   LYS   A CD  
16   C CE  . LYS   A 10  ? 1.1363 1.1503 0.9828 -0.1189 -0.1149 -0.1555 6   LYS   A CE  
17   N NZ  . LYS   A 10  ? 1.1770 1.2129 1.0210 -0.1315 -0.1254 -0.1696 6   LYS   A NZ  
18   N N   . GLY   A 11  ? 1.1176 1.0210 0.9409 -0.0819 -0.0686 -0.1263 7   GLY   A N   
19   C CA  . GLY   A 11  ? 0.9334 0.8151 0.7415 -0.0755 -0.0601 -0.1291 7   GLY   A CA  
20   C C   . GLY   A 11  ? 0.9923 0.8625 0.8099 -0.0659 -0.0506 -0.1216 7   GLY   A C   
21   O O   . GLY   A 11  ? 0.9366 0.7974 0.7449 -0.0579 -0.0434 -0.1228 7   GLY   A O   
22   N N   . LYS   A 12  ? 0.8293 0.7019 0.6651 -0.0668 -0.0502 -0.1148 8   LYS   A N   
23   C CA  . LYS   A 12  ? 0.8550 0.7196 0.7004 -0.0571 -0.0426 -0.1072 8   LYS   A CA  
24   C C   . LYS   A 12  ? 0.8053 0.6839 0.6517 -0.0473 -0.0408 -0.0989 8   LYS   A C   
25   O O   . LYS   A 12  ? 0.7057 0.6016 0.5525 -0.0475 -0.0473 -0.0942 8   LYS   A O   
26   C CB  . LYS   A 12  ? 0.8047 0.6708 0.6674 -0.0611 -0.0435 -0.1011 8   LYS   A CB  
27   C CG  . LYS   A 12  ? 0.8138 0.6623 0.6725 -0.0735 -0.0443 -0.1083 8   LYS   A CG  
28   C CD  . LYS   A 12  ? 0.8071 0.6238 0.6572 -0.0682 -0.0376 -0.1114 8   LYS   A CD  
29   C CE  . LYS   A 12  ? 0.7130 0.5057 0.5562 -0.0811 -0.0384 -0.1164 8   LYS   A CE  
30   N NZ  . LYS   A 12  ? 1.0131 0.7732 0.8362 -0.0794 -0.0358 -0.1268 8   LYS   A NZ  
31   N N   . ARG   A 13  ? 0.7105 0.5811 0.5564 -0.0386 -0.0323 -0.0976 9   ARG   A N   
32   C CA  . ARG   A 13  ? 0.8145 0.6949 0.6564 -0.0319 -0.0284 -0.0921 9   ARG   A CA  
33   C C   . ARG   A 13  ? 0.7284 0.6119 0.5867 -0.0252 -0.0234 -0.0835 9   ARG   A C   
34   O O   . ARG   A 13  ? 0.8201 0.6940 0.6852 -0.0206 -0.0179 -0.0862 9   ARG   A O   
35   C CB  . ARG   A 13  ? 0.7509 0.6243 0.5759 -0.0295 -0.0216 -0.1009 9   ARG   A CB  
36   C CG  . ARG   A 13  ? 0.8609 0.7437 0.6766 -0.0265 -0.0167 -0.0963 9   ARG   A CG  
37   C CD  . ARG   A 13  ? 0.9212 0.7996 0.7166 -0.0273 -0.0113 -0.1068 9   ARG   A CD  
38   N NE  . ARG   A 13  ? 0.9830 0.8691 0.7697 -0.0256 -0.0030 -0.1038 9   ARG   A NE  
39   C CZ  . ARG   A 13  ? 1.1079 0.9982 0.8780 -0.0295 -0.0054 -0.0972 9   ARG   A CZ  
40   N NH1 . ARG   A 13  ? 1.1953 1.0900 0.9555 -0.0302 0.0036  -0.0947 9   ARG   A NH1 
41   N NH2 . ARG   A 13  ? 1.1158 1.0058 0.8779 -0.0328 -0.0172 -0.0935 9   ARG   A NH2 
42   N N   . VAL   A 14  ? 0.6531 0.5490 0.5164 -0.0239 -0.0260 -0.0736 10  VAL   A N   
43   C CA  . VAL   A 14  ? 0.7022 0.6024 0.5806 -0.0187 -0.0223 -0.0652 10  VAL   A CA  
44   C C   . VAL   A 14  ? 0.7501 0.6562 0.6204 -0.0161 -0.0180 -0.0600 10  VAL   A C   
45   O O   . VAL   A 14  ? 0.7346 0.6430 0.5903 -0.0184 -0.0223 -0.0574 10  VAL   A O   
46   C CB  . VAL   A 14  ? 0.8155 0.7231 0.7083 -0.0205 -0.0292 -0.0585 10  VAL   A CB  
47   C CG1 . VAL   A 14  ? 0.7766 0.6765 0.6765 -0.0254 -0.0310 -0.0633 10  VAL   A CG1 
48   C CG2 . VAL   A 14  ? 0.7234 0.6412 0.6088 -0.0230 -0.0382 -0.0564 10  VAL   A CG2 
49   N N   . GLY   A 15  ? 0.5972 0.5049 0.4756 -0.0119 -0.0097 -0.0588 11  GLY   A N   
50   C CA  . GLY   A 15  ? 0.6172 0.5304 0.4893 -0.0120 -0.0042 -0.0538 11  GLY   A CA  
51   C C   . GLY   A 15  ? 0.6752 0.5934 0.5630 -0.0094 -0.0037 -0.0452 11  GLY   A C   
52   O O   . GLY   A 15  ? 0.6913 0.6097 0.5961 -0.0061 -0.0049 -0.0449 11  GLY   A O   
53   N N   . TYR   A 16  ? 0.6710 0.5910 0.5510 -0.0115 -0.0018 -0.0383 12  TYR   A N   
54   C CA  . TYR   A 16  ? 0.6695 0.5929 0.5627 -0.0097 -0.0017 -0.0306 12  TYR   A CA  
55   C C   . TYR   A 16  ? 0.6908 0.6152 0.5741 -0.0139 0.0059  -0.0273 12  TYR   A C   
56   O O   . TYR   A 16  ? 0.6787 0.5969 0.5397 -0.0189 0.0069  -0.0259 12  TYR   A O   
57   C CB  . TYR   A 16  ? 0.5797 0.5010 0.4746 -0.0083 -0.0122 -0.0233 12  TYR   A CB  
58   C CG  . TYR   A 16  ? 0.7846 0.6991 0.6575 -0.0099 -0.0180 -0.0188 12  TYR   A CG  
59   C CD1 . TYR   A 16  ? 0.6841 0.5965 0.5434 -0.0110 -0.0239 -0.0229 12  TYR   A CD1 
60   C CD2 . TYR   A 16  ? 0.7366 0.6447 0.6001 -0.0101 -0.0183 -0.0106 12  TYR   A CD2 
61   C CE1 . TYR   A 16  ? 0.6904 0.5955 0.5274 -0.0109 -0.0306 -0.0186 12  TYR   A CE1 
62   C CE2 . TYR   A 16  ? 0.7939 0.6910 0.6333 -0.0101 -0.0248 -0.0059 12  TYR   A CE2 
63   C CZ  . TYR   A 16  ? 0.7876 0.6838 0.6139 -0.0098 -0.0313 -0.0097 12  TYR   A CZ  
64   O OH  . TYR   A 16  ? 0.6860 0.5702 0.4861 -0.0083 -0.0392 -0.0048 12  TYR   A OH  
65   N N   . TRP   A 17  ? 0.7678 0.6998 0.6665 -0.0128 0.0113  -0.0262 13  TRP   A N   
66   C CA  . TRP   A 17  ? 0.8092 0.7423 0.7012 -0.0187 0.0176  -0.0219 13  TRP   A CA  
67   C C   . TRP   A 17  ? 0.6978 0.6286 0.6006 -0.0162 0.0124  -0.0138 13  TRP   A C   
68   O O   . TRP   A 17  ? 0.6231 0.5621 0.5469 -0.0115 0.0123  -0.0150 13  TRP   A O   
69   C CB  . TRP   A 17  ? 0.8621 0.8105 0.7634 -0.0206 0.0292  -0.0298 13  TRP   A CB  
70   C CG  . TRP   A 17  ? 1.0748 1.0252 0.9650 -0.0308 0.0375  -0.0270 13  TRP   A CG  
71   C CD1 . TRP   A 17  ? 1.0830 1.0351 0.9545 -0.0403 0.0465  -0.0307 13  TRP   A CD1 
72   C CD2 . TRP   A 17  ? 1.1954 1.1451 1.0905 -0.0344 0.0380  -0.0204 13  TRP   A CD2 
73   N NE1 . TRP   A 17  ? 1.2447 1.1964 1.1085 -0.0508 0.0530  -0.0265 13  TRP   A NE1 
74   C CE2 . TRP   A 17  ? 1.2069 1.1565 1.0851 -0.0471 0.0476  -0.0203 13  TRP   A CE2 
75   C CE3 . TRP   A 17  ? 1.0364 0.9850 0.9474 -0.0290 0.0317  -0.0150 13  TRP   A CE3 
76   C CZ2 . TRP   A 17  ? 1.1956 1.1424 1.0718 -0.0550 0.0507  -0.0151 13  TRP   A CZ2 
77   C CZ3 . TRP   A 17  ? 0.9579 0.9046 0.8675 -0.0353 0.0345  -0.0101 13  TRP   A CZ3 
78   C CH2 . TRP   A 17  ? 1.0171 0.9621 0.9095 -0.0484 0.0437  -0.0102 13  TRP   A CH2 
79   N N   . LEU   A 18  ? 0.7466 0.6646 0.6332 -0.0186 0.0077  -0.0058 14  LEU   A N   
80   C CA  . LEU   A 18  ? 0.7137 0.6278 0.6071 -0.0164 0.0034  0.0013  14  LEU   A CA  
81   C C   . LEU   A 18  ? 0.7639 0.6636 0.6349 -0.0237 0.0063  0.0074  14  LEU   A C   
82   O O   . LEU   A 18  ? 0.6235 0.5122 0.4697 -0.0293 0.0081  0.0083  14  LEU   A O   
83   C CB  . LEU   A 18  ? 0.6520 0.5625 0.5492 -0.0088 -0.0085 0.0046  14  LEU   A CB  
84   C CG  . LEU   A 18  ? 0.6883 0.6100 0.6056 -0.0041 -0.0116 -0.0005 14  LEU   A CG  
85   C CD1 . LEU   A 18  ? 0.6189 0.5396 0.5333 -0.0002 -0.0223 0.0003  14  LEU   A CD1 
86   C CD2 . LEU   A 18  ? 0.5932 0.5226 0.5319 -0.0015 -0.0100 0.0005  14  LEU   A CD2 
87   N N   . SER   A 19  ? 0.6617 0.5594 0.5395 -0.0244 0.0069  0.0115  15  SER   A N   
88   C CA  . SER   A 19  ? 0.8088 0.6869 0.6631 -0.0312 0.0080  0.0182  15  SER   A CA  
89   C C   . SER   A 19  ? 0.7538 0.6120 0.5902 -0.0237 -0.0044 0.0248  15  SER   A C   
90   O O   . SER   A 19  ? 0.7135 0.5776 0.5650 -0.0133 -0.0133 0.0250  15  SER   A O   
91   C CB  . SER   A 19  ? 0.6654 0.5469 0.5326 -0.0341 0.0117  0.0195  15  SER   A CB  
92   O OG  . SER   A 19  ? 0.7806 0.6565 0.6558 -0.0246 0.0021  0.0237  15  SER   A OG  
93   N N   . GLU   A 20  ? 0.8112 0.6462 0.6141 -0.0290 -0.0050 0.0299  16  GLU   A N   
94   C CA  . GLU   A 20  ? 0.9710 0.7846 0.7524 -0.0202 -0.0181 0.0361  16  GLU   A CA  
95   C C   . GLU   A 20  ? 0.8222 0.6290 0.6117 -0.0113 -0.0257 0.0401  16  GLU   A C   
96   O O   . GLU   A 20  ? 0.8905 0.6796 0.6633 -0.0016 -0.0373 0.0446  16  GLU   A O   
97   C CB  . GLU   A 20  ? 1.1851 0.9693 0.9241 -0.0288 -0.0164 0.0420  16  GLU   A CB  
98   C CG  . GLU   A 20  ? 1.1740 0.9459 0.9002 -0.0443 -0.0042 0.0446  16  GLU   A CG  
99   C CD  . GLU   A 20  ? 1.4468 1.2416 1.1841 -0.0577 0.0113  0.0369  16  GLU   A CD  
100  O OE1 . GLU   A 20  ? 1.3395 1.1624 1.1055 -0.0525 0.0128  0.0292  16  GLU   A OE1 
101  O OE2 . GLU   A 20  ? 1.5839 1.3686 1.3011 -0.0736 0.0220  0.0380  16  GLU   A OE2 
102  N N   . LYS   A 21  ? 0.9101 0.7309 0.7241 -0.0136 -0.0196 0.0377  17  LYS   A N   
103  C CA  . LYS   A 21  ? 0.7061 0.5218 0.5285 -0.0072 -0.0243 0.0403  17  LYS   A CA  
104  C C   . LYS   A 21  ? 0.7799 0.6217 0.6357 0.0026  -0.0287 0.0356  17  LYS   A C   
105  O O   . LYS   A 21  ? 0.7464 0.5875 0.6077 0.0134  -0.0378 0.0365  17  LYS   A O   
106  C CB  . LYS   A 21  ? 0.8221 0.6348 0.6457 -0.0192 -0.0136 0.0406  17  LYS   A CB  
107  C CG  . LYS   A 21  ? 1.0852 0.8680 0.8744 -0.0324 -0.0081 0.0459  17  LYS   A CG  
108  C CD  . LYS   A 21  ? 1.1984 0.9829 0.9722 -0.0450 0.0011  0.0441  17  LYS   A CD  
109  C CE  . LYS   A 21  ? 1.1266 0.9462 0.9302 -0.0512 0.0122  0.0353  17  LYS   A CE  
110  N NZ  . LYS   A 21  ? 1.2597 1.0857 1.0513 -0.0632 0.0226  0.0314  17  LYS   A NZ  
111  N N   . LYS   A 22  ? 0.7441 0.6081 0.6206 -0.0013 -0.0220 0.0300  18  LYS   A N   
112  C CA  . LYS   A 22  ? 0.7323 0.6166 0.6321 0.0056  -0.0262 0.0255  18  LYS   A CA  
113  C C   . LYS   A 22  ? 0.5279 0.4106 0.4177 0.0115  -0.0355 0.0248  18  LYS   A C   
114  O O   . LYS   A 22  ? 0.7041 0.5964 0.6053 0.0197  -0.0437 0.0233  18  LYS   A O   
115  C CB  . LYS   A 22  ? 0.7035 0.6039 0.6190 0.0000  -0.0174 0.0199  18  LYS   A CB  
116  C CG  . LYS   A 22  ? 0.7386 0.6553 0.6786 0.0047  -0.0193 0.0164  18  LYS   A CG  
117  C CD  . LYS   A 22  ? 0.6104 0.5292 0.5620 0.0071  -0.0197 0.0189  18  LYS   A CD  
118  C CE  . LYS   A 22  ? 0.7050 0.6380 0.6776 0.0109  -0.0218 0.0163  18  LYS   A CE  
119  N NZ  . LYS   A 22  ? 0.7386 0.6745 0.7218 0.0124  -0.0209 0.0182  18  LYS   A NZ  
120  N N   . ILE   A 23  ? 0.5225 0.3948 0.3904 0.0070  -0.0342 0.0253  19  ILE   A N   
121  C CA  . ILE   A 23  ? 0.7027 0.5749 0.5602 0.0120  -0.0432 0.0238  19  ILE   A CA  
122  C C   . ILE   A 23  ? 0.6150 0.4793 0.4645 0.0234  -0.0561 0.0272  19  ILE   A C   
123  O O   . ILE   A 23  ? 0.5735 0.4532 0.4358 0.0312  -0.0647 0.0233  19  ILE   A O   
124  C CB  . ILE   A 23  ? 0.6796 0.5385 0.5098 0.0048  -0.0395 0.0245  19  ILE   A CB  
125  C CG1 . ILE   A 23  ? 0.7364 0.6092 0.5777 -0.0032 -0.0288 0.0179  19  ILE   A CG1 
126  C CG2 . ILE   A 23  ? 0.6537 0.5075 0.4665 0.0115  -0.0515 0.0246  19  ILE   A CG2 
127  C CD1 . ILE   A 23  ? 0.7968 0.6586 0.6125 -0.0124 -0.0214 0.0179  19  ILE   A CD1 
128  N N   . LYS   A 24  ? 0.7366 0.5765 0.5641 0.0246  -0.0575 0.0338  20  LYS   A N   
129  C CA  . LYS   A 24  ? 0.8038 0.6316 0.6191 0.0380  -0.0708 0.0368  20  LYS   A CA  
130  C C   . LYS   A 24  ? 0.7283 0.5761 0.5723 0.0473  -0.0753 0.0331  20  LYS   A C   
131  O O   . LYS   A 24  ? 0.8303 0.6881 0.6791 0.0595  -0.0869 0.0301  20  LYS   A O   
132  C CB  . LYS   A 24  ? 0.9683 0.7606 0.7519 0.0360  -0.0702 0.0447  20  LYS   A CB  
133  C CG  . LYS   A 24  ? 1.1974 0.9720 0.9665 0.0520  -0.0843 0.0478  20  LYS   A CG  
134  C CD  . LYS   A 24  ? 1.2427 0.9757 0.9754 0.0475  -0.0827 0.0560  20  LYS   A CD  
135  C CE  . LYS   A 24  ? 1.2260 0.9586 0.9716 0.0367  -0.0706 0.0564  20  LYS   A CE  
136  N NZ  . LYS   A 24  ? 1.2889 0.9799 0.9986 0.0300  -0.0684 0.0637  20  LYS   A NZ  
137  N N   . LYS   A 25  ? 0.7823 0.6379 0.6455 0.0415  -0.0662 0.0325  21  LYS   A N   
138  C CA  . LYS   A 25  ? 0.8057 0.6778 0.6930 0.0489  -0.0690 0.0294  21  LYS   A CA  
139  C C   . LYS   A 25  ? 0.6172 0.5202 0.5305 0.0498  -0.0705 0.0225  21  LYS   A C   
140  O O   . LYS   A 25  ? 0.6692 0.5887 0.5975 0.0583  -0.0769 0.0186  21  LYS   A O   
141  C CB  . LYS   A 25  ? 0.7837 0.6535 0.6804 0.0414  -0.0588 0.0310  21  LYS   A CB  
142  C CG  . LYS   A 25  ? 1.0079 0.8912 0.9257 0.0478  -0.0604 0.0284  21  LYS   A CG  
143  C CD  . LYS   A 25  ? 1.0844 0.9615 1.0052 0.0388  -0.0506 0.0305  21  LYS   A CD  
144  C CE  . LYS   A 25  ? 1.0585 0.9460 0.9973 0.0426  -0.0500 0.0285  21  LYS   A CE  
145  N NZ  . LYS   A 25  ? 1.0531 0.9367 0.9944 0.0325  -0.0406 0.0299  21  LYS   A NZ  
146  N N   . LEU   A 26  ? 0.6774 0.5884 0.5961 0.0402  -0.0639 0.0202  22  LEU   A N   
147  C CA  . LEU   A 26  ? 0.5890 0.5231 0.5254 0.0392  -0.0659 0.0138  22  LEU   A CA  
148  C C   . LEU   A 26  ? 0.5895 0.5271 0.5151 0.0450  -0.0767 0.0111  22  LEU   A C   
149  O O   . LEU   A 26  ? 0.5108 0.4694 0.4507 0.0440  -0.0799 0.0047  22  LEU   A O   
150  C CB  . LEU   A 26  ? 0.6662 0.6032 0.6086 0.0283  -0.0562 0.0117  22  LEU   A CB  
151  C CG  . LEU   A 26  ? 0.7121 0.6499 0.6675 0.0231  -0.0465 0.0128  22  LEU   A CG  
152  C CD1 . LEU   A 26  ? 0.6059 0.5416 0.5596 0.0156  -0.0385 0.0106  22  LEU   A CD1 
153  C CD2 . LEU   A 26  ? 0.8117 0.7663 0.7892 0.0240  -0.0470 0.0100  22  LEU   A CD2 
154  N N   . ASN   A 27  ? 0.5707 0.4876 0.4700 0.0505  -0.0825 0.0156  23  ASN   A N   
155  C CA  . ASN   A 27  ? 0.6230 0.5393 0.5063 0.0557  -0.0930 0.0138  23  ASN   A CA  
156  C C   . ASN   A 27  ? 0.5904 0.5165 0.4768 0.0454  -0.0883 0.0091  23  ASN   A C   
157  O O   . ASN   A 27  ? 0.6270 0.5706 0.5195 0.0469  -0.0954 0.0027  23  ASN   A O   
158  C CB  . ASN   A 27  ? 0.5335 0.4698 0.4285 0.0689  -0.1060 0.0086  23  ASN   A CB  
159  C CG  . ASN   A 27  ? 0.7745 0.7035 0.6465 0.0791  -0.1198 0.0085  23  ASN   A CG  
160  O OD1 . ASN   A 27  ? 0.9201 0.8215 0.7617 0.0776  -0.1201 0.0148  23  ASN   A OD1 
161  N ND2 . ASN   A 27  ? 0.7407 0.6955 0.6262 0.0893  -0.1315 0.0010  23  ASN   A ND2 
162  N N   . PHE   A 28  ? 0.5797 0.4953 0.4620 0.0349  -0.0762 0.0111  24  PHE   A N   
163  C CA  . PHE   A 28  ? 0.5986 0.5230 0.4871 0.0258  -0.0701 0.0056  24  PHE   A CA  
164  C C   . PHE   A 28  ? 0.5706 0.4905 0.4381 0.0254  -0.0761 0.0033  24  PHE   A C   
165  O O   . PHE   A 28  ? 0.6098 0.5416 0.4842 0.0207  -0.0761 -0.0036 24  PHE   A O   
166  C CB  . PHE   A 28  ? 0.5534 0.4692 0.4423 0.0173  -0.0566 0.0072  24  PHE   A CB  
167  C CG  . PHE   A 28  ? 0.6106 0.5366 0.5129 0.0106  -0.0501 0.0006  24  PHE   A CG  
168  C CD1 . PHE   A 28  ? 0.6079 0.5459 0.5339 0.0097  -0.0477 -0.0021 24  PHE   A CD1 
169  C CD2 . PHE   A 28  ? 0.5247 0.4459 0.4134 0.0056  -0.0467 -0.0032 24  PHE   A CD2 
170  C CE1 . PHE   A 28  ? 0.6179 0.5595 0.5522 0.0044  -0.0426 -0.0078 24  PHE   A CE1 
171  C CE2 . PHE   A 28  ? 0.6580 0.5851 0.5569 0.0010  -0.0414 -0.0100 24  PHE   A CE2 
172  C CZ  . PHE   A 28  ? 0.5609 0.4965 0.4819 0.0006  -0.0398 -0.0120 24  PHE   A CZ  
173  N N   . GLN   A 29  ? 0.5869 0.4875 0.4264 0.0297  -0.0813 0.0090  25  GLN   A N   
174  C CA  . GLN   A 29  ? 0.6287 0.5239 0.4450 0.0299  -0.0879 0.0072  25  GLN   A CA  
175  C C   . GLN   A 29  ? 0.5918 0.5084 0.4189 0.0373  -0.1014 0.0006  25  GLN   A C   
176  O O   . GLN   A 29  ? 0.5767 0.4998 0.3969 0.0340  -0.1050 -0.0050 25  GLN   A O   
177  C CB  . GLN   A 29  ? 0.6148 0.4811 0.3951 0.0335  -0.0917 0.0159  25  GLN   A CB  
178  C CG  . GLN   A 29  ? 0.6603 0.5073 0.4251 0.0221  -0.0773 0.0207  25  GLN   A CG  
179  C CD  . GLN   A 29  ? 0.7267 0.5812 0.4922 0.0111  -0.0671 0.0146  25  GLN   A CD  
180  O OE1 . GLN   A 29  ? 0.8999 0.7585 0.6555 0.0110  -0.0723 0.0101  25  GLN   A OE1 
181  N NE2 . GLN   A 29  ? 0.8809 0.7380 0.6579 0.0025  -0.0529 0.0136  25  GLN   A NE2 
182  N N   . ALA   A 30  ? 0.6060 0.5359 0.4506 0.0466  -0.1086 0.0000  26  ALA   A N   
183  C CA  . ALA   A 30  ? 0.5411 0.4988 0.4016 0.0522  -0.1201 -0.0084 26  ALA   A CA  
184  C C   . ALA   A 30  ? 0.6062 0.5859 0.4924 0.0403  -0.1129 -0.0167 26  ALA   A C   
185  O O   . ALA   A 30  ? 0.5079 0.5062 0.3996 0.0377  -0.1193 -0.0250 26  ALA   A O   
186  C CB  . ALA   A 30  ? 0.5569 0.5253 0.4300 0.0658  -0.1287 -0.0081 26  ALA   A CB  
187  N N   . PHE   A 31  ? 0.4927 0.4689 0.3931 0.0327  -0.1001 -0.0148 27  PHE   A N   
188  C CA  . PHE   A 31  ? 0.6006 0.5903 0.5204 0.0214  -0.0932 -0.0216 27  PHE   A CA  
189  C C   . PHE   A 31  ? 0.4938 0.4743 0.3997 0.0129  -0.0893 -0.0254 27  PHE   A C   
190  O O   . PHE   A 31  ? 0.5775 0.5695 0.4924 0.0050  -0.0893 -0.0334 27  PHE   A O   
191  C CB  . PHE   A 31  ? 0.4944 0.4795 0.4292 0.0175  -0.0819 -0.0179 27  PHE   A CB  
192  C CG  . PHE   A 31  ? 0.4576 0.4484 0.4065 0.0066  -0.0746 -0.0234 27  PHE   A CG  
193  C CD1 . PHE   A 31  ? 0.6348 0.6459 0.6022 0.0022  -0.0771 -0.0293 27  PHE   A CD1 
194  C CD2 . PHE   A 31  ? 0.4876 0.4626 0.4297 0.0006  -0.0653 -0.0233 27  PHE   A CD2 
195  C CE1 . PHE   A 31  ? 0.4976 0.5080 0.4732 -0.0091 -0.0706 -0.0336 27  PHE   A CE1 
196  C CE2 . PHE   A 31  ? 0.3904 0.3654 0.3419 -0.0077 -0.0598 -0.0282 27  PHE   A CE2 
197  C CZ  . PHE   A 31  ? 0.5573 0.5474 0.5238 -0.0131 -0.0625 -0.0327 27  PHE   A CZ  
198  N N   . ALA   A 32  ? 0.5380 0.4976 0.4211 0.0132  -0.0853 -0.0204 28  ALA   A N   
199  C CA  . ALA   A 32  ? 0.5646 0.5166 0.4329 0.0061  -0.0816 -0.0251 28  ALA   A CA  
200  C C   . ALA   A 32  ? 0.5079 0.4699 0.3663 0.0072  -0.0936 -0.0312 28  ALA   A C   
201  O O   . ALA   A 32  ? 0.5338 0.5010 0.3932 -0.0006 -0.0927 -0.0395 28  ALA   A O   
202  C CB  . ALA   A 32  ? 0.6127 0.5431 0.4577 0.0055  -0.0743 -0.0190 28  ALA   A CB  
203  N N   . GLU   A 33  ? 0.6355 0.5993 0.4831 0.0173  -0.1056 -0.0277 29  GLU   A N   
204  C CA  . GLU   A 33  ? 0.7772 0.7550 0.6178 0.0204  -0.1193 -0.0343 29  GLU   A CA  
205  C C   . GLU   A 33  ? 0.7156 0.7231 0.5848 0.0159  -0.1229 -0.0441 29  GLU   A C   
206  O O   . GLU   A 33  ? 0.6700 0.6910 0.5380 0.0109  -0.1291 -0.0532 29  GLU   A O   
207  C CB  . GLU   A 33  ? 0.5484 0.5213 0.3720 0.0351  -0.1327 -0.0284 29  GLU   A CB  
208  C CG  . GLU   A 33  ? 0.7911 0.7689 0.5946 0.0398  -0.1470 -0.0329 29  GLU   A CG  
209  C CD  . GLU   A 33  ? 0.9762 0.9414 0.7592 0.0287  -0.1408 -0.0358 29  GLU   A CD  
210  O OE1 . GLU   A 33  ? 1.0892 1.0718 0.8817 0.0210  -0.1425 -0.0463 29  GLU   A OE1 
211  O OE2 . GLU   A 33  ? 0.8413 0.7795 0.5982 0.0270  -0.1338 -0.0283 29  GLU   A OE2 
212  N N   . LEU   A 34  ? 0.5782 0.5964 0.4719 0.0163  -0.1189 -0.0430 30  LEU   A N   
213  C CA  . LEU   A 34  ? 0.6206 0.6653 0.5404 0.0084  -0.1193 -0.0522 30  LEU   A CA  
214  C C   . LEU   A 34  ? 0.6145 0.6533 0.5344 -0.0070 -0.1109 -0.0585 30  LEU   A C   
215  O O   . LEU   A 34  ? 0.7038 0.7602 0.6306 -0.0155 -0.1153 -0.0685 30  LEU   A O   
216  C CB  . LEU   A 34  ? 0.7350 0.7866 0.6769 0.0099  -0.1135 -0.0486 30  LEU   A CB  
217  C CG  . LEU   A 34  ? 0.8035 0.8853 0.7721 0.0027  -0.1143 -0.0571 30  LEU   A CG  
218  C CD1 . LEU   A 34  ? 0.7813 0.8939 0.7575 0.0121  -0.1290 -0.0639 30  LEU   A CD1 
219  C CD2 . LEU   A 34  ? 0.8327 0.9130 0.8177 0.0014  -0.1050 -0.0523 30  LEU   A CD2 
220  N N   . CYS   A 35  ? 0.6787 0.6928 0.5903 -0.0106 -0.0991 -0.0537 31  CYS   A N   
221  C CA  . CYS   A 35  ? 0.6300 0.6345 0.5406 -0.0228 -0.0911 -0.0598 31  CYS   A CA  
222  C C   . CYS   A 35  ? 0.6292 0.6292 0.5196 -0.0262 -0.0954 -0.0664 31  CYS   A C   
223  O O   . CYS   A 35  ? 0.6613 0.6619 0.5526 -0.0370 -0.0941 -0.0754 31  CYS   A O   
224  C CB  . CYS   A 35  ? 0.5787 0.5609 0.4873 -0.0227 -0.0783 -0.0539 31  CYS   A CB  
225  S SG  . CYS   A 35  ? 0.6935 0.6789 0.6251 -0.0212 -0.0722 -0.0476 31  CYS   A SG  
226  N N   . ARG   A 36  ? 0.6468 0.6401 0.5165 -0.0179 -0.1005 -0.0622 32  ARG   A N   
227  C CA  . ARG   A 36  ? 0.7389 0.7272 0.5864 -0.0210 -0.1046 -0.0682 32  ARG   A CA  
228  C C   . ARG   A 36  ? 0.7014 0.7136 0.5547 -0.0247 -0.1170 -0.0781 32  ARG   A C   
229  O O   . ARG   A 36  ? 0.7852 0.7963 0.6270 -0.0324 -0.1187 -0.0869 32  ARG   A O   
230  C CB  . ARG   A 36  ? 0.6896 0.6639 0.5105 -0.0119 -0.1077 -0.0603 32  ARG   A CB  
231  C CG  . ARG   A 36  ? 0.7250 0.6774 0.5377 -0.0116 -0.0942 -0.0526 32  ARG   A CG  
232  C CD  . ARG   A 36  ? 0.6782 0.6142 0.4590 -0.0070 -0.0958 -0.0460 32  ARG   A CD  
233  N NE  . ARG   A 36  ? 0.7531 0.6723 0.5276 -0.0086 -0.0822 -0.0396 32  ARG   A NE  
234  C CZ  . ARG   A 36  ? 0.7701 0.6817 0.5449 -0.0037 -0.0802 -0.0297 32  ARG   A CZ  
235  N NH1 . ARG   A 36  ? 0.6739 0.5910 0.4540 0.0050  -0.0913 -0.0249 32  ARG   A NH1 
236  N NH2 . ARG   A 36  ? 0.7337 0.6332 0.5036 -0.0073 -0.0673 -0.0257 32  ARG   A NH2 
237  N N   . LYS   A 37  ? 0.7384 0.7744 0.6100 -0.0196 -0.1256 -0.0782 33  LYS   A N   
238  C CA  . LYS   A 37  ? 0.8367 0.9019 0.7181 -0.0241 -0.1371 -0.0895 33  LYS   A CA  
239  C C   . LYS   A 37  ? 0.7516 0.8235 0.6500 -0.0415 -0.1298 -0.0987 33  LYS   A C   
240  O O   . LYS   A 37  ? 0.8701 0.9588 0.7702 -0.0513 -0.1359 -0.1102 33  LYS   A O   
241  C CB  . LYS   A 37  ? 0.8277 0.9197 0.7249 -0.0123 -0.1482 -0.0884 33  LYS   A CB  
242  C CG  . LYS   A 37  ? 0.8835 0.9647 0.7600 0.0058  -0.1575 -0.0795 33  LYS   A CG  
243  C CD  . LYS   A 37  ? 0.9406 1.0479 0.8315 0.0198  -0.1703 -0.0804 33  LYS   A CD  
244  C CE  . LYS   A 37  ? 0.9831 1.0697 0.8493 0.0382  -0.1784 -0.0696 33  LYS   A CE  
245  N NZ  . LYS   A 37  ? 1.1987 1.2734 1.0329 0.0426  -0.1885 -0.0696 33  LYS   A NZ  
246  N N   . ARG   A 38  ? 0.7266 0.7844 0.6358 -0.0460 -0.1172 -0.0938 34  ARG   A N   
247  C CA  . ARG   A 38  ? 0.7473 0.8022 0.6667 -0.0626 -0.1095 -0.1008 34  ARG   A CA  
248  C C   . ARG   A 38  ? 0.7750 0.8058 0.6751 -0.0713 -0.1045 -0.1067 34  ARG   A C   
249  O O   . ARG   A 38  ? 0.9051 0.9285 0.8084 -0.0857 -0.0994 -0.1135 34  ARG   A O   
250  C CB  . ARG   A 38  ? 0.7639 0.8067 0.6962 -0.0628 -0.0984 -0.0929 34  ARG   A CB  
251  C CG  . ARG   A 38  ? 0.8150 0.8768 0.7642 -0.0526 -0.1015 -0.0863 34  ARG   A CG  
252  C CD  . ARG   A 38  ? 0.8627 0.9558 0.8338 -0.0621 -0.1048 -0.0940 34  ARG   A CD  
253  N NE  . ARG   A 38  ? 0.9785 1.1021 0.9519 -0.0595 -0.1183 -0.1026 34  ARG   A NE  
254  C CZ  . ARG   A 38  ? 1.0279 1.1704 1.0051 -0.0432 -0.1286 -0.1001 34  ARG   A CZ  
255  N NH1 . ARG   A 38  ? 0.9961 1.1285 0.9748 -0.0298 -0.1260 -0.0894 34  ARG   A NH1 
256  N NH2 . ARG   A 38  ? 1.0386 1.2091 1.0172 -0.0397 -0.1421 -0.1089 34  ARG   A NH2 
257  N N   . GLY   A 39  ? 0.6418 0.6586 0.5203 -0.0635 -0.1056 -0.1044 35  GLY   A N   
258  C CA  . GLY   A 39  ? 0.9237 0.9181 0.7829 -0.0698 -0.1004 -0.1107 35  GLY   A CA  
259  C C   . GLY   A 39  ? 0.9113 0.8782 0.7612 -0.0639 -0.0883 -0.1042 35  GLY   A C   
260  O O   . GLY   A 39  ? 0.9174 0.8658 0.7520 -0.0675 -0.0830 -0.1103 35  GLY   A O   
261  N N   . MET   A 40  ? 0.7939 0.7591 0.6529 -0.0547 -0.0839 -0.0932 36  MET   A N   
262  C CA  . MET   A 40  ? 0.8047 0.7490 0.6584 -0.0494 -0.0725 -0.0880 36  MET   A CA  
263  C C   . MET   A 40  ? 0.8682 0.8070 0.7012 -0.0419 -0.0721 -0.0839 36  MET   A C   
264  O O   . MET   A 40  ? 0.9711 0.9196 0.7944 -0.0380 -0.0813 -0.0813 36  MET   A O   
265  C CB  . MET   A 40  ? 0.7144 0.6600 0.5867 -0.0444 -0.0677 -0.0786 36  MET   A CB  
266  C CG  . MET   A 40  ? 0.7422 0.6921 0.6333 -0.0520 -0.0670 -0.0806 36  MET   A CG  
267  S SD  . MET   A 40  ? 0.8978 0.8430 0.8046 -0.0448 -0.0593 -0.0696 36  MET   A SD  
268  C CE  . MET   A 40  ? 0.8296 0.7729 0.7506 -0.0563 -0.0573 -0.0729 36  MET   A CE  
269  N N   . GLU   A 41  ? 0.7717 0.6945 0.5971 -0.0398 -0.0612 -0.0836 37  GLU   A N   
270  C CA  . GLU   A 41  ? 0.8873 0.8044 0.6959 -0.0343 -0.0568 -0.0780 37  GLU   A CA  
271  C C   . GLU   A 41  ? 0.8116 0.7269 0.6338 -0.0289 -0.0493 -0.0689 37  GLU   A C   
272  O O   . GLU   A 41  ? 0.8147 0.7244 0.6493 -0.0287 -0.0412 -0.0710 37  GLU   A O   
273  C CB  . GLU   A 41  ? 0.8913 0.7966 0.6816 -0.0367 -0.0490 -0.0865 37  GLU   A CB  
274  C CG  . GLU   A 41  ? 1.0454 0.9513 0.8174 -0.0421 -0.0563 -0.0955 37  GLU   A CG  
275  C CD  . GLU   A 41  ? 1.2401 1.1344 0.9930 -0.0438 -0.0477 -0.1044 37  GLU   A CD  
276  O OE1 . GLU   A 41  ? 1.3626 1.2504 1.1136 -0.0486 -0.0474 -0.1158 37  GLU   A OE1 
277  O OE2 . GLU   A 41  ? 1.2833 1.1746 1.0222 -0.0411 -0.0407 -0.1007 37  GLU   A OE2 
278  N N   . VAL   A 42  ? 0.7749 0.6935 0.5934 -0.0242 -0.0528 -0.0592 38  VAL   A N   
279  C CA  . VAL   A 42  ? 0.7889 0.7060 0.6183 -0.0200 -0.0465 -0.0506 38  VAL   A CA  
280  C C   . VAL   A 42  ? 0.7557 0.6639 0.5638 -0.0197 -0.0401 -0.0463 38  VAL   A C   
281  O O   . VAL   A 42  ? 0.7921 0.6961 0.5796 -0.0187 -0.0464 -0.0417 38  VAL   A O   
282  C CB  . VAL   A 42  ? 0.6976 0.6236 0.5396 -0.0155 -0.0551 -0.0431 38  VAL   A CB  
283  C CG1 . VAL   A 42  ? 0.5837 0.5073 0.4378 -0.0121 -0.0482 -0.0355 38  VAL   A CG1 
284  C CG2 . VAL   A 42  ? 0.6095 0.5477 0.4698 -0.0183 -0.0614 -0.0487 38  VAL   A CG2 
285  N N   . VAL   A 43  ? 0.7679 0.6733 0.5798 -0.0208 -0.0278 -0.0483 39  VAL   A N   
286  C CA  . VAL   A 43  ? 0.7915 0.6915 0.5843 -0.0235 -0.0190 -0.0464 39  VAL   A CA  
287  C C   . VAL   A 43  ? 0.7333 0.6345 0.5370 -0.0224 -0.0127 -0.0388 39  VAL   A C   
288  O O   . VAL   A 43  ? 0.6436 0.5510 0.4713 -0.0195 -0.0097 -0.0396 39  VAL   A O   
289  C CB  . VAL   A 43  ? 0.8819 0.7823 0.6691 -0.0263 -0.0090 -0.0577 39  VAL   A CB  
290  C CG1 . VAL   A 43  ? 0.9102 0.8078 0.6853 -0.0282 -0.0157 -0.0657 39  VAL   A CG1 
291  C CG2 . VAL   A 43  ? 0.7952 0.7008 0.6074 -0.0226 -0.0019 -0.0632 39  VAL   A CG2 
292  N N   . GLN   A 44  ? 0.8409 0.7341 0.6246 -0.0254 -0.0114 -0.0312 40  GLN   A N   
293  C CA  . GLN   A 44  ? 0.8059 0.6986 0.5951 -0.0272 -0.0040 -0.0250 40  GLN   A CA  
294  C C   . GLN   A 44  ? 0.8609 0.7603 0.6481 -0.0332 0.0109  -0.0320 40  GLN   A C   
295  O O   . GLN   A 44  ? 0.9935 0.8878 0.7555 -0.0399 0.0161  -0.0338 40  GLN   A O   
296  C CB  . GLN   A 44  ? 1.0330 0.9101 0.7985 -0.0287 -0.0092 -0.0140 40  GLN   A CB  
297  C CG  . GLN   A 44  ? 0.9788 0.8535 0.7539 -0.0290 -0.0061 -0.0066 40  GLN   A CG  
298  C CD  . GLN   A 44  ? 1.0080 0.8652 0.7658 -0.0252 -0.0168 0.0039  40  GLN   A CD  
299  O OE1 . GLN   A 44  ? 0.9332 0.7857 0.6809 -0.0190 -0.0291 0.0051  40  GLN   A OE1 
300  N NE2 . GLN   A 44  ? 1.0594 0.9071 0.8134 -0.0284 -0.0127 0.0106  40  GLN   A NE2 
301  N N   . LEU   A 45  ? 0.9591 0.8711 0.7722 -0.0304 0.0174  -0.0367 41  LEU   A N   
302  C CA  . LEU   A 45  ? 0.9537 0.8778 0.7701 -0.0333 0.0307  -0.0461 41  LEU   A CA  
303  C C   . LEU   A 45  ? 1.0368 0.9613 0.8372 -0.0436 0.0405  -0.0425 41  LEU   A C   
304  O O   . LEU   A 45  ? 0.9162 0.8341 0.7148 -0.0466 0.0389  -0.0329 41  LEU   A O   
305  C CB  . LEU   A 45  ? 0.8284 0.7654 0.6758 -0.0259 0.0333  -0.0513 41  LEU   A CB  
306  C CG  . LEU   A 45  ? 0.7281 0.6628 0.5887 -0.0175 0.0269  -0.0573 41  LEU   A CG  
307  C CD1 . LEU   A 45  ? 0.5819 0.5250 0.4687 -0.0098 0.0286  -0.0600 41  LEU   A CD1 
308  C CD2 . LEU   A 45  ? 0.6844 0.6182 0.5326 -0.0176 0.0303  -0.0687 41  LEU   A CD2 
309  N N   . ASN   A 46  ? 1.0507 0.9823 0.8379 -0.0501 0.0513  -0.0509 42  ASN   A N   
310  C CA  . ASN   A 46  ? 1.1946 1.1319 0.9693 -0.0624 0.0641  -0.0506 42  ASN   A CA  
311  C C   . ASN   A 46  ? 1.2782 1.2430 1.0801 -0.0601 0.0753  -0.0625 42  ASN   A C   
312  O O   . ASN   A 46  ? 1.2422 1.2203 1.0484 -0.0566 0.0812  -0.0753 42  ASN   A O   
313  C CB  . ASN   A 46  ? 1.2028 1.1316 0.9421 -0.0727 0.0696  -0.0523 42  ASN   A CB  
314  C CG  . ASN   A 46  ? 1.1987 1.0993 0.9069 -0.0751 0.0582  -0.0394 42  ASN   A CG  
315  O OD1 . ASN   A 46  ? 1.2494 1.1408 0.9418 -0.0718 0.0507  -0.0407 42  ASN   A OD1 
316  N ND2 . ASN   A 46  ? 1.0270 0.9132 0.7256 -0.0801 0.0562  -0.0276 42  ASN   A ND2 
317  N N   . LEU   A 47  ? 1.2608 1.2345 1.0811 -0.0610 0.0775  -0.0591 43  LEU   A N   
318  C CA  . LEU   A 47  ? 1.4126 1.4155 1.2578 -0.0596 0.0878  -0.0704 43  LEU   A CA  
319  C C   . LEU   A 47  ? 1.2896 1.3083 1.1215 -0.0750 0.1037  -0.0768 43  LEU   A C   
320  O O   . LEU   A 47  ? 1.3221 1.3671 1.1736 -0.0777 0.1127  -0.0842 43  LEU   A O   
321  C CB  . LEU   A 47  ? 1.3185 1.3268 1.1881 -0.0552 0.0837  -0.0650 43  LEU   A CB  
322  C CG  . LEU   A 47  ? 1.3281 1.3377 1.2236 -0.0381 0.0737  -0.0668 43  LEU   A CG  
323  C CD1 . LEU   A 47  ? 1.2381 1.2702 1.1514 -0.0286 0.0795  -0.0825 43  LEU   A CD1 
324  C CD2 . LEU   A 47  ? 1.1902 1.1763 1.0754 -0.0321 0.0616  -0.0607 43  LEU   A CD2 
325  N N   . SER   A 48  ? 1.1943 1.1989 0.9928 -0.0859 0.1075  -0.0746 44  SER   A N   
326  C CA  . SER   A 48  ? 1.1360 1.1579 0.9204 -0.1005 0.1241  -0.0838 44  SER   A CA  
327  C C   . SER   A 48  ? 1.1678 1.2061 0.9563 -0.0926 0.1288  -0.0996 44  SER   A C   
328  O O   . SER   A 48  ? 1.1011 1.1696 0.8988 -0.0966 0.1428  -0.1140 44  SER   A O   
329  C CB  . SER   A 48  ? 1.0283 1.0229 0.7690 -0.1181 0.1263  -0.0725 44  SER   A CB  
330  O OG  . SER   A 48  ? 1.2326 1.2054 0.9498 -0.1131 0.1177  -0.0694 44  SER   A OG  
331  N N   . ARG   A 49  ? 1.1926 1.2121 0.9745 -0.0815 0.1174  -0.0981 45  ARG   A N   
332  C CA  . ARG   A 49  ? 1.1575 1.1853 0.9427 -0.0715 0.1186  -0.1123 45  ARG   A CA  
333  C C   . ARG   A 49  ? 1.0343 1.0790 0.8568 -0.0535 0.1153  -0.1221 45  ARG   A C   
334  O O   . ARG   A 49  ? 1.0795 1.1216 0.9220 -0.0472 0.1077  -0.1147 45  ARG   A O   
335  C CB  . ARG   A 49  ? 1.2280 1.2270 0.9915 -0.0679 0.1060  -0.1061 45  ARG   A CB  
336  C CG  . ARG   A 49  ? 1.3345 1.3160 1.0566 -0.0827 0.1082  -0.0990 45  ARG   A CG  
337  C CD  . ARG   A 49  ? 1.3400 1.2973 1.0422 -0.0778 0.0945  -0.0948 45  ARG   A CD  
338  N NE  . ARG   A 49  ? 1.4523 1.3891 1.1556 -0.0732 0.0786  -0.0799 45  ARG   A NE  
339  C CZ  . ARG   A 49  ? 1.4512 1.3718 1.1454 -0.0673 0.0647  -0.0766 45  ARG   A CZ  
340  N NH1 . ARG   A 49  ? 1.5189 1.4389 1.2007 -0.0659 0.0644  -0.0865 45  ARG   A NH1 
341  N NH2 . ARG   A 49  ? 1.2861 1.1931 0.9837 -0.0629 0.0511  -0.0645 45  ARG   A NH2 
342  N N   . PRO   A 50  ? 0.9661 1.0263 0.7965 -0.0442 0.1206  -0.1390 46  PRO   A N   
343  C CA  . PRO   A 50  ? 1.0466 1.1100 0.9046 -0.0243 0.1132  -0.1465 46  PRO   A CA  
344  C C   . PRO   A 50  ? 0.9982 1.0292 0.8492 -0.0178 0.0977  -0.1373 46  PRO   A C   
345  O O   . PRO   A 50  ? 0.9622 0.9751 0.7882 -0.0243 0.0944  -0.1338 46  PRO   A O   
346  C CB  . PRO   A 50  ? 0.9506 1.0340 0.8115 -0.0164 0.1227  -0.1673 46  PRO   A CB  
347  C CG  . PRO   A 50  ? 0.9693 1.0583 0.8024 -0.0331 0.1345  -0.1703 46  PRO   A CG  
348  C CD  . PRO   A 50  ? 1.0014 1.0738 0.8132 -0.0511 0.1330  -0.1519 46  PRO   A CD  
349  N N   . ILE   A 51  ? 0.8723 0.8970 0.7450 -0.0059 0.0882  -0.1337 47  ILE   A N   
350  C CA  . ILE   A 51  ? 0.8897 0.8866 0.7571 -0.0036 0.0743  -0.1233 47  ILE   A CA  
351  C C   . ILE   A 51  ? 0.9115 0.8937 0.7689 0.0030  0.0703  -0.1330 47  ILE   A C   
352  O O   . ILE   A 51  ? 0.9348 0.8959 0.7805 0.0003  0.0605  -0.1266 47  ILE   A O   
353  C CB  . ILE   A 51  ? 0.7727 0.7668 0.6638 0.0051  0.0664  -0.1164 47  ILE   A CB  
354  C CG1 . ILE   A 51  ? 0.8565 0.8653 0.7565 -0.0022 0.0707  -0.1079 47  ILE   A CG1 
355  C CG2 . ILE   A 51  ? 0.8173 0.7867 0.7030 0.0042  0.0535  -0.1051 47  ILE   A CG2 
356  C CD1 . ILE   A 51  ? 0.8919 0.9041 0.8165 0.0070  0.0652  -0.1041 47  ILE   A CD1 
357  N N   . GLU   A 52  ? 0.9701 0.9638 0.8314 0.0116  0.0775  -0.1495 48  GLU   A N   
358  C CA  . GLU   A 52  ? 1.0490 1.0271 0.8972 0.0170  0.0748  -0.1603 48  GLU   A CA  
359  C C   . GLU   A 52  ? 0.9817 0.9523 0.8010 0.0038  0.0761  -0.1588 48  GLU   A C   
360  O O   . GLU   A 52  ? 1.0726 1.0242 0.8780 0.0043  0.0696  -0.1623 48  GLU   A O   
361  C CB  . GLU   A 52  ? 1.2204 1.2145 1.0779 0.0301  0.0832  -0.1796 48  GLU   A CB  
362  C CG  . GLU   A 52  ? 1.2118 1.2001 1.0906 0.0482  0.0769  -0.1840 48  GLU   A CG  
363  C CD  . GLU   A 52  ? 1.3391 1.3442 1.2267 0.0641  0.0840  -0.2042 48  GLU   A CD  
364  O OE1 . GLU   A 52  ? 1.4495 1.4777 1.3309 0.0596  0.0959  -0.2153 48  GLU   A OE1 
365  O OE2 . GLU   A 52  ? 1.1871 1.1820 1.0868 0.0815  0.0776  -0.2095 48  GLU   A OE2 
366  N N   . GLU   A 53  ? 0.9488 0.9329 0.7568 -0.0087 0.0842  -0.1537 49  GLU   A N   
367  C CA  . GLU   A 53  ? 0.7879 0.7622 0.5647 -0.0213 0.0843  -0.1501 49  GLU   A CA  
368  C C   . GLU   A 53  ? 0.9306 0.8826 0.6982 -0.0254 0.0698  -0.1350 49  GLU   A C   
369  O O   . GLU   A 53  ? 0.9300 0.8705 0.6719 -0.0325 0.0658  -0.1330 49  GLU   A O   
370  C CB  . GLU   A 53  ? 0.8471 0.8373 0.6108 -0.0347 0.0967  -0.1471 49  GLU   A CB  
371  C CG  . GLU   A 53  ? 0.9253 0.9419 0.6922 -0.0342 0.1128  -0.1645 49  GLU   A CG  
372  C CD  . GLU   A 53  ? 1.1241 1.1533 0.8710 -0.0519 0.1258  -0.1616 49  GLU   A CD  
373  O OE1 . GLU   A 53  ? 1.1676 1.1781 0.8909 -0.0638 0.1211  -0.1463 49  GLU   A OE1 
374  O OE2 . GLU   A 53  ? 1.0613 1.1187 0.8149 -0.0541 0.1407  -0.1750 49  GLU   A OE2 
375  N N   . GLN   A 54  ? 0.9567 0.9043 0.7446 -0.0207 0.0617  -0.1253 50  GLN   A N   
376  C CA  . GLN   A 54  ? 0.8928 0.8242 0.6764 -0.0234 0.0482  -0.1124 50  GLN   A CA  
377  C C   . GLN   A 54  ? 0.9110 0.8303 0.7073 -0.0159 0.0383  -0.1155 50  GLN   A C   
378  O O   . GLN   A 54  ? 0.9542 0.8642 0.7516 -0.0179 0.0274  -0.1064 50  GLN   A O   
379  C CB  . GLN   A 54  ? 0.7890 0.7240 0.5832 -0.0260 0.0467  -0.0983 50  GLN   A CB  
380  C CG  . GLN   A 54  ? 0.9810 0.9267 0.7642 -0.0349 0.0581  -0.0959 50  GLN   A CG  
381  C CD  . GLN   A 54  ? 1.0389 0.9859 0.8324 -0.0375 0.0568  -0.0832 50  GLN   A CD  
382  O OE1 . GLN   A 54  ? 1.1286 1.0619 0.9144 -0.0393 0.0470  -0.0712 50  GLN   A OE1 
383  N NE2 . GLN   A 54  ? 1.0641 1.0289 0.8753 -0.0371 0.0665  -0.0869 50  GLN   A NE2 
384  N N   . GLY   A 55  ? 0.9783 0.8968 0.7830 -0.0074 0.0420  -0.1284 51  GLY   A N   
385  C CA  . GLY   A 55  ? 0.9354 0.8374 0.7479 -0.0018 0.0335  -0.1315 51  GLY   A CA  
386  C C   . GLY   A 55  ? 0.9928 0.8807 0.7852 -0.0072 0.0275  -0.1373 51  GLY   A C   
387  O O   . GLY   A 55  ? 1.0535 0.9445 0.8253 -0.0143 0.0289  -0.1384 51  GLY   A O   
388  N N   . PRO   A 56  ? 1.0178 0.8884 0.8144 -0.0049 0.0203  -0.1410 52  PRO   A N   
389  C CA  . PRO   A 56  ? 0.9383 0.8008 0.7546 0.0026  0.0178  -0.1385 52  PRO   A CA  
390  C C   . PRO   A 56  ? 0.9298 0.7962 0.7588 -0.0021 0.0110  -0.1232 52  PRO   A C   
391  O O   . PRO   A 56  ? 0.9002 0.7724 0.7220 -0.0103 0.0062  -0.1161 52  PRO   A O   
392  C CB  . PRO   A 56  ? 0.8302 0.6684 0.6379 0.0028  0.0127  -0.1480 52  PRO   A CB  
393  C CG  . PRO   A 56  ? 0.9570 0.7942 0.7465 -0.0088 0.0077  -0.1494 52  PRO   A CG  
394  C CD  . PRO   A 56  ? 1.0545 0.9105 0.8338 -0.0108 0.0140  -0.1483 52  PRO   A CD  
395  N N   . LEU   A 57  ? 0.7517 0.6151 0.5984 0.0041  0.0102  -0.1188 53  LEU   A N   
396  C CA  . LEU   A 57  ? 0.7516 0.6193 0.6110 0.0005  0.0047  -0.1054 53  LEU   A CA  
397  C C   . LEU   A 57  ? 0.7969 0.6471 0.6641 0.0021  -0.0004 -0.1048 53  LEU   A C   
398  O O   . LEU   A 57  ? 0.8080 0.6480 0.6796 0.0116  0.0023  -0.1097 53  LEU   A O   
399  C CB  . LEU   A 57  ? 0.7215 0.6066 0.5939 0.0047  0.0101  -0.0981 53  LEU   A CB  
400  C CG  . LEU   A 57  ? 0.7163 0.6158 0.5786 -0.0011 0.0140  -0.0943 53  LEU   A CG  
401  C CD1 . LEU   A 57  ? 0.7279 0.6428 0.6017 0.0018  0.0213  -0.0902 53  LEU   A CD1 
402  C CD2 . LEU   A 57  ? 0.7358 0.6343 0.5915 -0.0089 0.0053  -0.0848 53  LEU   A CD2 
403  N N   . ASP   A 58  ? 0.6457 0.4923 0.5133 -0.0071 -0.0078 -0.0992 54  ASP   A N   
404  C CA  . ASP   A 58  ? 0.6785 0.5088 0.5516 -0.0091 -0.0119 -0.0972 54  ASP   A CA  
405  C C   . ASP   A 58  ? 0.6293 0.4680 0.5195 -0.0060 -0.0121 -0.0862 54  ASP   A C   
406  O O   . ASP   A 58  ? 0.6132 0.4370 0.5075 -0.0025 -0.0126 -0.0849 54  ASP   A O   
407  C CB  . ASP   A 58  ? 0.5919 0.4182 0.4585 -0.0226 -0.0188 -0.0982 54  ASP   A CB  
408  C CG  . ASP   A 58  ? 0.8379 0.6542 0.6863 -0.0268 -0.0194 -0.1100 54  ASP   A CG  
409  O OD1 . ASP   A 58  ? 0.9209 0.7146 0.7600 -0.0230 -0.0171 -0.1187 54  ASP   A OD1 
410  O OD2 . ASP   A 58  ? 0.7896 0.6194 0.6315 -0.0331 -0.0228 -0.1108 54  ASP   A OD2 
411  N N   . VAL   A 59  ? 0.6189 0.4784 0.5167 -0.0069 -0.0120 -0.0782 55  VAL   A N   
412  C CA  . VAL   A 59  ? 0.7022 0.5707 0.6154 -0.0043 -0.0122 -0.0682 55  VAL   A CA  
413  C C   . VAL   A 59  ? 0.6703 0.5565 0.5866 -0.0008 -0.0080 -0.0640 55  VAL   A C   
414  O O   . VAL   A 59  ? 0.6630 0.5563 0.5692 -0.0046 -0.0082 -0.0643 55  VAL   A O   
415  C CB  . VAL   A 59  ? 0.6200 0.4930 0.5389 -0.0130 -0.0187 -0.0618 55  VAL   A CB  
416  C CG1 . VAL   A 59  ? 0.6640 0.5503 0.5970 -0.0102 -0.0186 -0.0518 55  VAL   A CG1 
417  C CG2 . VAL   A 59  ? 0.7479 0.6025 0.6647 -0.0185 -0.0211 -0.0647 55  VAL   A CG2 
418  N N   . ILE   A 60  ? 0.6648 0.5568 0.5931 0.0056  -0.0043 -0.0602 56  ILE   A N   
419  C CA  . ILE   A 60  ? 0.5587 0.4665 0.4906 0.0066  0.0000  -0.0555 56  ILE   A CA  
420  C C   . ILE   A 60  ? 0.7025 0.6155 0.6477 0.0068  -0.0027 -0.0459 56  ILE   A C   
421  O O   . ILE   A 60  ? 0.6865 0.5964 0.6422 0.0118  -0.0027 -0.0450 56  ILE   A O   
422  C CB  . ILE   A 60  ? 0.5881 0.5028 0.5227 0.0135  0.0082  -0.0625 56  ILE   A CB  
423  C CG1 . ILE   A 60  ? 0.7421 0.6533 0.6626 0.0134  0.0117  -0.0732 56  ILE   A CG1 
424  C CG2 . ILE   A 60  ? 0.5235 0.4545 0.4622 0.0115  0.0133  -0.0575 56  ILE   A CG2 
425  C CD1 . ILE   A 60  ? 0.8284 0.7528 0.7516 0.0193  0.0209  -0.0816 56  ILE   A CD1 
426  N N   . ILE   A 61  ? 0.6449 0.5644 0.5879 0.0023  -0.0056 -0.0389 57  ILE   A N   
427  C CA  . ILE   A 61  ? 0.6143 0.5393 0.5683 0.0027  -0.0080 -0.0304 57  ILE   A CA  
428  C C   . ILE   A 61  ? 0.6830 0.6155 0.6349 0.0026  -0.0034 -0.0266 57  ILE   A C   
429  O O   . ILE   A 61  ? 0.6230 0.5550 0.5605 -0.0010 -0.0022 -0.0265 57  ILE   A O   
430  C CB  . ILE   A 61  ? 0.5889 0.5147 0.5424 -0.0012 -0.0159 -0.0264 57  ILE   A CB  
431  C CG1 . ILE   A 61  ? 0.6658 0.5983 0.6296 0.0003  -0.0178 -0.0186 57  ILE   A CG1 
432  C CG2 . ILE   A 61  ? 0.6801 0.6065 0.6182 -0.0042 -0.0192 -0.0275 57  ILE   A CG2 
433  C CD1 . ILE   A 61  ? 0.7220 0.6595 0.6898 -0.0020 -0.0252 -0.0166 57  ILE   A CD1 
434  N N   . HIS   A 62  ? 0.6126 0.5506 0.5766 0.0053  -0.0007 -0.0236 58  HIS   A N   
435  C CA  . HIS   A 62  ? 0.7001 0.6454 0.6623 0.0033  0.0053  -0.0219 58  HIS   A CA  
436  C C   . HIS   A 62  ? 0.6535 0.6036 0.6286 0.0049  0.0046  -0.0163 58  HIS   A C   
437  O O   . HIS   A 62  ? 0.6043 0.5531 0.5902 0.0086  0.0006  -0.0147 58  HIS   A O   
438  C CB  . HIS   A 62  ? 0.5940 0.5472 0.5569 0.0047  0.0134  -0.0305 58  HIS   A CB  
439  C CG  . HIS   A 62  ? 0.7108 0.6702 0.6904 0.0125  0.0146  -0.0346 58  HIS   A CG  
440  N ND1 . HIS   A 62  ? 0.5782 0.5495 0.5697 0.0137  0.0174  -0.0332 58  HIS   A ND1 
441  C CD2 . HIS   A 62  ? 0.6588 0.6121 0.6430 0.0199  0.0123  -0.0399 58  HIS   A CD2 
442  C CE1 . HIS   A 62  ? 0.7101 0.6843 0.7135 0.0227  0.0163  -0.0376 58  HIS   A CE1 
443  N NE2 . HIS   A 62  ? 0.6563 0.6177 0.6544 0.0269  0.0131  -0.0413 58  HIS   A NE2 
444  N N   . LYS   A 63  ? 0.6319 0.5862 0.6036 0.0007  0.0090  -0.0137 59  LYS   A N   
445  C CA  . LYS   A 63  ? 0.7174 0.6785 0.7008 0.0012  0.0104  -0.0108 59  LYS   A CA  
446  C C   . LYS   A 63  ? 0.6335 0.6033 0.6127 -0.0053 0.0191  -0.0138 59  LYS   A C   
447  O O   . LYS   A 63  ? 0.5666 0.5302 0.5332 -0.0127 0.0209  -0.0091 59  LYS   A O   
448  C CB  . LYS   A 63  ? 0.6847 0.6385 0.6666 0.0006  0.0045  -0.0027 59  LYS   A CB  
449  C CG  . LYS   A 63  ? 0.4950 0.4552 0.4912 0.0027  0.0044  -0.0007 59  LYS   A CG  
450  C CD  . LYS   A 63  ? 0.6340 0.5871 0.6281 0.0029  -0.0009 0.0060  59  LYS   A CD  
451  C CE  . LYS   A 63  ? 0.5599 0.5185 0.5633 0.0024  0.0008  0.0075  59  LYS   A CE  
452  N NZ  . LYS   A 63  ? 0.8185 0.7700 0.8198 0.0038  -0.0043 0.0128  59  LYS   A NZ  
453  N N   . LEU   A 64  ? 0.7107 0.6948 0.6995 -0.0026 0.0247  -0.0223 60  LEU   A N   
454  C CA  . LEU   A 64  ? 0.7504 0.7493 0.7383 -0.0094 0.0343  -0.0279 60  LEU   A CA  
455  C C   . LEU   A 64  ? 0.6972 0.7113 0.7007 -0.0101 0.0365  -0.0289 60  LEU   A C   
456  O O   . LEU   A 64  ? 0.6506 0.6852 0.6614 -0.0131 0.0442  -0.0370 60  LEU   A O   
457  C CB  . LEU   A 64  ? 0.6574 0.6681 0.6483 -0.0050 0.0393  -0.0391 60  LEU   A CB  
458  C CG  . LEU   A 64  ? 0.7108 0.7110 0.6827 -0.0084 0.0408  -0.0408 60  LEU   A CG  
459  C CD1 . LEU   A 64  ? 0.7628 0.7677 0.7406 0.0012  0.0412  -0.0511 60  LEU   A CD1 
460  C CD2 . LEU   A 64  ? 0.8957 0.9009 0.8520 -0.0215 0.0503  -0.0420 60  LEU   A CD2 
461  N N   . THR   A 65  ? 0.7410 0.7478 0.7499 -0.0078 0.0302  -0.0217 61  THR   A N   
462  C CA  . THR   A 65  ? 0.8526 0.8736 0.8763 -0.0076 0.0310  -0.0231 61  THR   A CA  
463  C C   . THR   A 65  ? 0.7266 0.7572 0.7453 -0.0210 0.0395  -0.0250 61  THR   A C   
464  O O   . THR   A 65  ? 0.7497 0.8018 0.7827 -0.0223 0.0431  -0.0312 61  THR   A O   
465  C CB  . THR   A 65  ? 0.6625 0.6716 0.6891 -0.0042 0.0232  -0.0148 61  THR   A CB  
466  O OG1 . THR   A 65  ? 0.7879 0.8108 0.8276 -0.0043 0.0237  -0.0165 61  THR   A OG1 
467  C CG2 . THR   A 65  ? 0.6940 0.6838 0.7031 -0.0111 0.0214  -0.0066 61  THR   A CG2 
468  N N   . ASP   A 66  ? 0.7033 0.7179 0.7004 -0.0316 0.0424  -0.0202 62  ASP   A N   
469  C CA  . ASP   A 66  ? 0.6418 0.6595 0.6286 -0.0472 0.0510  -0.0211 62  ASP   A CA  
470  C C   . ASP   A 66  ? 0.7311 0.7693 0.7177 -0.0544 0.0619  -0.0313 62  ASP   A C   
471  O O   . ASP   A 66  ? 0.6315 0.6836 0.6177 -0.0678 0.0707  -0.0357 62  ASP   A O   
472  C CB  . ASP   A 66  ? 0.8402 0.8269 0.7996 -0.0550 0.0487  -0.0109 62  ASP   A CB  
473  C CG  . ASP   A 66  ? 1.0520 1.0217 0.9972 -0.0488 0.0435  -0.0070 62  ASP   A CG  
474  O OD1 . ASP   A 66  ? 0.9661 0.9462 0.9128 -0.0467 0.0470  -0.0133 62  ASP   A OD1 
475  O OD2 . ASP   A 66  ? 1.0282 0.9754 0.9607 -0.0455 0.0355  0.0014  62  ASP   A OD2 
476  N N   . VAL   A 67  ? 0.6278 0.6690 0.6141 -0.0469 0.0620  -0.0358 63  VAL   A N   
477  C CA  . VAL   A 67  ? 0.5800 0.6477 0.5735 -0.0490 0.0717  -0.0486 63  VAL   A CA  
478  C C   . VAL   A 67  ? 0.6271 0.7241 0.6502 -0.0376 0.0706  -0.0583 63  VAL   A C   
479  O O   . VAL   A 67  ? 0.5112 0.6386 0.5461 -0.0424 0.0791  -0.0694 63  VAL   A O   
480  C CB  . VAL   A 67  ? 0.5386 0.5980 0.5206 -0.0439 0.0717  -0.0511 63  VAL   A CB  
481  C CG1 . VAL   A 67  ? 0.5961 0.6854 0.5900 -0.0414 0.0805  -0.0663 63  VAL   A CG1 
482  C CG2 . VAL   A 67  ? 0.7637 0.7996 0.7144 -0.0572 0.0745  -0.0436 63  VAL   A CG2 
483  N N   . ILE   A 68  ? 0.5455 0.6345 0.5801 -0.0224 0.0599  -0.0548 64  ILE   A N   
484  C CA  . ILE   A 68  ? 0.5852 0.6971 0.6442 -0.0093 0.0568  -0.0629 64  ILE   A CA  
485  C C   . ILE   A 68  ? 0.5157 0.6497 0.5869 -0.0175 0.0603  -0.0658 64  ILE   A C   
486  O O   . ILE   A 68  ? 0.4485 0.6148 0.5385 -0.0131 0.0633  -0.0777 64  ILE   A O   
487  C CB  . ILE   A 68  ? 0.6555 0.7480 0.7183 0.0055  0.0447  -0.0562 64  ILE   A CB  
488  C CG1 . ILE   A 68  ? 0.6518 0.7277 0.7054 0.0136  0.0420  -0.0569 64  ILE   A CG1 
489  C CG2 . ILE   A 68  ? 0.5999 0.7110 0.6835 0.0183  0.0400  -0.0620 64  ILE   A CG2 
490  C CD1 . ILE   A 68  ? 0.7348 0.8290 0.7974 0.0237  0.0453  -0.0706 64  ILE   A CD1 
491  N N   . LEU   A 69  ? 0.5839 0.7014 0.6442 -0.0293 0.0596  -0.0559 65  LEU   A N   
492  C CA  . LEU   A 69  ? 0.6517 0.7868 0.7209 -0.0393 0.0629  -0.0586 65  LEU   A CA  
493  C C   . LEU   A 69  ? 0.5253 0.6878 0.5957 -0.0545 0.0759  -0.0695 65  LEU   A C   
494  O O   . LEU   A 69  ? 0.5202 0.7168 0.6103 -0.0559 0.0791  -0.0800 65  LEU   A O   
495  C CB  . LEU   A 69  ? 0.5782 0.6847 0.6309 -0.0493 0.0600  -0.0462 65  LEU   A CB  
496  C CG  . LEU   A 69  ? 0.7603 0.8522 0.8188 -0.0376 0.0486  -0.0384 65  LEU   A CG  
497  C CD1 . LEU   A 69  ? 0.6502 0.7102 0.6884 -0.0452 0.0459  -0.0267 65  LEU   A CD1 
498  C CD2 . LEU   A 69  ? 0.5998 0.7167 0.6790 -0.0347 0.0466  -0.0444 65  LEU   A CD2 
499  N N   . GLU   A 70  ? 0.5388 0.6883 0.5875 -0.0666 0.0837  -0.0676 66  GLU   A N   
500  C CA  . GLU   A 70  ? 0.4642 0.6382 0.5102 -0.0842 0.0977  -0.0776 66  GLU   A CA  
501  C C   . GLU   A 70  ? 0.5252 0.7400 0.5947 -0.0735 0.1019  -0.0942 66  GLU   A C   
502  O O   . GLU   A 70  ? 0.4154 0.6680 0.4991 -0.0828 0.1110  -0.1069 66  GLU   A O   
503  C CB  . GLU   A 70  ? 0.6038 0.7503 0.6172 -0.0983 0.1041  -0.0708 66  GLU   A CB  
504  C CG  . GLU   A 70  ? 0.6704 0.7842 0.6577 -0.1153 0.1046  -0.0585 66  GLU   A CG  
505  C CD  . GLU   A 70  ? 0.7746 0.8488 0.7285 -0.1182 0.1027  -0.0473 66  GLU   A CD  
506  O OE1 . GLU   A 70  ? 0.7999 0.8420 0.7284 -0.1296 0.1016  -0.0367 66  GLU   A OE1 
507  O OE2 . GLU   A 70  ? 0.7523 0.8269 0.7045 -0.1085 0.1017  -0.0496 66  GLU   A OE2 
508  N N   . ALA   A 71  ? 0.5231 0.7314 0.5968 -0.0538 0.0953  -0.0953 67  ALA   A N   
509  C CA  . ALA   A 71  ? 0.5237 0.7662 0.6176 -0.0402 0.0978  -0.1116 67  ALA   A CA  
510  C C   . ALA   A 71  ? 0.5336 0.8099 0.6571 -0.0292 0.0932  -0.1209 67  ALA   A C   
511  O O   . ALA   A 71  ? 0.5126 0.8306 0.6552 -0.0258 0.0992  -0.1376 67  ALA   A O   
512  C CB  . ALA   A 71  ? 0.5443 0.7648 0.6333 -0.0210 0.0898  -0.1095 67  ALA   A CB  
513  N N   . ASP   A 72  ? 0.5398 0.8003 0.6673 -0.0232 0.0824  -0.1113 68  ASP   A N   
514  C CA  . ASP   A 72  ? 0.5205 0.8111 0.6734 -0.0129 0.0767  -0.1192 68  ASP   A CA  
515  C C   . ASP   A 72  ? 0.5737 0.8981 0.7359 -0.0330 0.0864  -0.1273 68  ASP   A C   
516  O O   . ASP   A 72  ? 0.6049 0.9701 0.7920 -0.0263 0.0853  -0.1405 68  ASP   A O   
517  C CB  . ASP   A 72  ? 0.6237 0.8864 0.7749 -0.0029 0.0633  -0.1062 68  ASP   A CB  
518  C CG  . ASP   A 72  ? 0.7466 0.9826 0.8929 0.0178  0.0533  -0.1011 68  ASP   A CG  
519  O OD1 . ASP   A 72  ? 0.8398 1.0816 0.9870 0.0273  0.0555  -0.1093 68  ASP   A OD1 
520  O OD2 . ASP   A 72  ? 0.8970 1.1058 1.0373 0.0235  0.0438  -0.0894 68  ASP   A OD2 
521  N N   . GLN   A 73  ? 0.6212 0.9288 0.7627 -0.0577 0.0953  -0.1200 69  GLN   A N   
522  C CA  . GLN   A 73  ? 0.5253 0.8599 0.6704 -0.0813 0.1062  -0.1273 69  GLN   A CA  
523  C C   . GLN   A 73  ? 0.5326 0.8967 0.6768 -0.0954 0.1219  -0.1405 69  GLN   A C   
524  O O   . GLN   A 73  ? 0.5332 0.9048 0.6669 -0.1223 0.1339  -0.1425 69  GLN   A O   
525  C CB  . GLN   A 73  ? 0.5441 0.8400 0.6637 -0.1010 0.1070  -0.1122 69  GLN   A CB  
526  C CG  . GLN   A 73  ? 0.5379 0.8192 0.6636 -0.0926 0.0945  -0.1039 69  GLN   A CG  
527  C CD  . GLN   A 73  ? 0.7382 1.0642 0.8946 -0.0861 0.0912  -0.1169 69  GLN   A CD  
528  O OE1 . GLN   A 73  ? 0.7806 1.1409 0.9466 -0.1033 0.1004  -0.1284 69  GLN   A OE1 
529  N NE2 . GLN   A 73  ? 0.5521 0.8780 0.7229 -0.0619 0.0778  -0.1154 69  GLN   A NE2 
530  N N   . ASN   A 74  ? 0.4854 0.8645 0.6383 -0.0788 0.1224  -0.1497 70  ASN   A N   
531  C CA  . ASN   A 74  ? 0.5786 0.9945 0.7359 -0.0882 0.1371  -0.1659 70  ASN   A CA  
532  C C   . ASN   A 74  ? 0.5814 0.9709 0.7046 -0.1142 0.1498  -0.1581 70  ASN   A C   
533  O O   . ASN   A 74  ? 0.6669 1.0836 0.7874 -0.1369 0.1652  -0.1679 70  ASN   A O   
534  C CB  . ASN   A 74  ? 0.5729 1.0482 0.7586 -0.0968 0.1442  -0.1842 70  ASN   A CB  
535  C CG  . ASN   A 74  ? 0.6354 1.1345 0.8519 -0.0714 0.1299  -0.1907 70  ASN   A CG  
536  O OD1 . ASN   A 74  ? 0.5803 1.0776 0.8068 -0.0431 0.1198  -0.1936 70  ASN   A OD1 
537  N ND2 . ASN   A 74  ? 0.6083 1.1274 0.8375 -0.0818 0.1285  -0.1929 70  ASN   A ND2 
538  N N   . ASP   A 75  ? 0.5651 0.9021 0.6613 -0.1111 0.1433  -0.1408 71  ASP   A N   
539  C CA  . ASP   A 75  ? 0.5943 0.9023 0.6552 -0.1305 0.1528  -0.1331 71  ASP   A CA  
540  C C   . ASP   A 75  ? 0.5998 0.9172 0.6590 -0.1200 0.1570  -0.1419 71  ASP   A C   
541  O O   . ASP   A 75  ? 0.6112 0.9149 0.6760 -0.0962 0.1461  -0.1398 71  ASP   A O   
542  C CB  . ASP   A 75  ? 0.7352 0.9852 0.7683 -0.1309 0.1427  -0.1116 71  ASP   A CB  
543  C CG  . ASP   A 75  ? 0.7252 0.9426 0.7185 -0.1513 0.1509  -0.1027 71  ASP   A CG  
544  O OD1 . ASP   A 75  ? 0.7467 0.9540 0.7271 -0.1452 0.1519  -0.1028 71  ASP   A OD1 
545  O OD2 . ASP   A 75  ? 0.7094 0.9093 0.6823 -0.1733 0.1560  -0.0957 71  ASP   A OD2 
546  N N   . SER   A 76  ? 0.6601 1.0006 0.7105 -0.1388 0.1735  -0.1524 72  SER   A N   
547  C CA  . SER   A 76  ? 0.5516 0.9067 0.6015 -0.1297 0.1793  -0.1637 72  SER   A CA  
548  C C   . SER   A 76  ? 0.5527 0.8578 0.5737 -0.1221 0.1718  -0.1496 72  SER   A C   
549  O O   . SER   A 76  ? 0.5804 0.8859 0.6079 -0.1017 0.1667  -0.1552 72  SER   A O   
550  C CB  . SER   A 76  ? 0.4832 0.8703 0.5245 -0.1554 0.1999  -0.1764 72  SER   A CB  
551  O OG  . SER   A 76  ? 0.5332 0.9680 0.6005 -0.1662 0.2073  -0.1896 72  SER   A OG  
552  N N   . GLN   A 77  ? 0.6337 0.8952 0.6220 -0.1380 0.1704  -0.1319 73  GLN   A N   
553  C CA  . GLN   A 77  ? 0.6260 0.8427 0.5869 -0.1314 0.1625  -0.1190 73  GLN   A CA  
554  C C   . GLN   A 77  ? 0.6344 0.8340 0.6110 -0.1049 0.1448  -0.1129 73  GLN   A C   
555  O O   . GLN   A 77  ? 0.6387 0.8233 0.6091 -0.0912 0.1391  -0.1125 73  GLN   A O   
556  C CB  . GLN   A 77  ? 0.6774 0.8518 0.6004 -0.1520 0.1631  -0.1019 73  GLN   A CB  
557  C CG  . GLN   A 77  ? 0.6524 0.8357 0.5521 -0.1813 0.1810  -0.1061 73  GLN   A CG  
558  C CD  . GLN   A 77  ? 0.7449 0.9445 0.6349 -0.1835 0.1918  -0.1173 73  GLN   A CD  
559  O OE1 . GLN   A 77  ? 0.6827 0.9261 0.5866 -0.1928 0.2063  -0.1341 73  GLN   A OE1 
560  N NE2 . GLN   A 77  ? 0.7486 0.9151 0.6152 -0.1750 0.1847  -0.1091 73  GLN   A NE2 
561  N N   . SER   A 78  ? 0.6389 0.8407 0.6348 -0.0984 0.1365  -0.1088 74  SER   A N   
562  C CA  . SER   A 78  ? 0.6446 0.8258 0.6507 -0.0766 0.1204  -0.1010 74  SER   A CA  
563  C C   . SER   A 78  ? 0.4884 0.6942 0.5216 -0.0537 0.1161  -0.1141 74  SER   A C   
564  O O   . SER   A 78  ? 0.4529 0.6373 0.4846 -0.0374 0.1060  -0.1102 74  SER   A O   
565  C CB  . SER   A 78  ? 0.6027 0.7731 0.6150 -0.0788 0.1130  -0.0909 74  SER   A CB  
566  O OG  . SER   A 78  ? 0.7015 0.8381 0.6845 -0.0950 0.1134  -0.0770 74  SER   A OG  
567  N N   . LEU   A 79  ? 0.4748 0.7244 0.5321 -0.0515 0.1229  -0.1301 75  LEU   A N   
568  C CA  . LEU   A 79  ? 0.6177 0.8877 0.6964 -0.0276 0.1186  -0.1436 75  LEU   A CA  
569  C C   . LEU   A 79  ? 0.5768 0.8385 0.6410 -0.0232 0.1226  -0.1495 75  LEU   A C   
570  O O   . LEU   A 79  ? 0.5614 0.8145 0.6314 -0.0022 0.1145  -0.1536 75  LEU   A O   
571  C CB  . LEU   A 79  ? 0.5627 0.8859 0.6711 -0.0240 0.1247  -0.1619 75  LEU   A CB  
572  C CG  . LEU   A 79  ? 0.6038 0.9425 0.7348 -0.0183 0.1170  -0.1612 75  LEU   A CG  
573  C CD1 . LEU   A 79  ? 0.5642 0.9613 0.7235 -0.0167 0.1244  -0.1817 75  LEU   A CD1 
574  C CD2 . LEU   A 79  ? 0.6754 0.9901 0.8127 0.0079  0.1003  -0.1555 75  LEU   A CD2 
575  N N   . GLU   A 80  ? 0.5532 0.8153 0.5962 -0.0431 0.1351  -0.1502 76  GLU   A N   
576  C CA  . GLU   A 80  ? 0.6202 0.8715 0.6464 -0.0395 0.1383  -0.1549 76  GLU   A CA  
577  C C   . GLU   A 80  ? 0.7215 0.9257 0.7302 -0.0309 0.1250  -0.1403 76  GLU   A C   
578  O O   . GLU   A 80  ? 0.7063 0.9013 0.7144 -0.0155 0.1201  -0.1457 76  GLU   A O   
579  C CB  . GLU   A 80  ? 0.6158 0.8736 0.6184 -0.0642 0.1541  -0.1571 76  GLU   A CB  
580  C CG  . GLU   A 80  ? 0.8863 1.1507 0.8784 -0.0600 0.1611  -0.1694 76  GLU   A CG  
581  C CD  . GLU   A 80  ? 1.0619 1.3669 1.0841 -0.0401 0.1635  -0.1911 76  GLU   A CD  
582  O OE1 . GLU   A 80  ? 0.9764 1.3184 1.0262 -0.0376 0.1660  -0.2003 76  GLU   A OE1 
583  O OE2 . GLU   A 80  ? 1.0898 1.3896 1.1078 -0.0262 0.1622  -0.1997 76  GLU   A OE2 
584  N N   . LEU   A 81  ? 0.6585 0.8337 0.6538 -0.0403 0.1188  -0.1227 77  LEU   A N   
585  C CA  . LEU   A 81  ? 0.6993 0.8348 0.6802 -0.0332 0.1062  -0.1097 77  LEU   A CA  
586  C C   . LEU   A 81  ? 0.6033 0.7343 0.6043 -0.0113 0.0941  -0.1110 77  LEU   A C   
587  O O   . LEU   A 81  ? 0.5287 0.6389 0.5225 -0.0012 0.0872  -0.1102 77  LEU   A O   
588  C CB  . LEU   A 81  ? 0.6763 0.7861 0.6413 -0.0460 0.1020  -0.0924 77  LEU   A CB  
589  C CG  . LEU   A 81  ? 0.7722 0.8750 0.7096 -0.0683 0.1120  -0.0879 77  LEU   A CG  
590  C CD1 . LEU   A 81  ? 0.6257 0.6945 0.5442 -0.0755 0.1041  -0.0703 77  LEU   A CD1 
591  C CD2 . LEU   A 81  ? 0.9002 0.9981 0.8162 -0.0714 0.1175  -0.0931 77  LEU   A CD2 
592  N N   . VAL   A 82  ? 0.6117 0.7606 0.6361 -0.0045 0.0913  -0.1130 78  VAL   A N   
593  C CA  . VAL   A 82  ? 0.5903 0.7315 0.6301 0.0156  0.0795  -0.1131 78  VAL   A CA  
594  C C   . VAL   A 82  ? 0.5806 0.7316 0.6272 0.0325  0.0799  -0.1282 78  VAL   A C   
595  O O   . VAL   A 82  ? 0.4197 0.5478 0.4643 0.0467  0.0704  -0.1269 78  VAL   A O   
596  C CB  . VAL   A 82  ? 0.6345 0.7940 0.6956 0.0187  0.0764  -0.1123 78  VAL   A CB  
597  C CG1 . VAL   A 82  ? 0.5572 0.7123 0.6330 0.0409  0.0652  -0.1150 78  VAL   A CG1 
598  C CG2 . VAL   A 82  ? 0.5895 0.7304 0.6416 0.0052  0.0734  -0.0964 78  VAL   A CG2 
599  N N   . HIS   A 83  ? 0.5848 0.7694 0.6386 0.0306  0.0912  -0.1435 79  HIS   A N   
600  C CA  . HIS   A 83  ? 0.6403 0.8360 0.7003 0.0479  0.0921  -0.1600 79  HIS   A CA  
601  C C   . HIS   A 83  ? 0.7354 0.8984 0.7727 0.0493  0.0896  -0.1577 79  HIS   A C   
602  O O   . HIS   A 83  ? 0.8341 0.9797 0.8715 0.0668  0.0815  -0.1620 79  HIS   A O   
603  C CB  . HIS   A 83  ? 0.6656 0.9063 0.7357 0.0422  0.1067  -0.1773 79  HIS   A CB  
604  C CG  . HIS   A 83  ? 0.8062 1.0561 0.8757 0.0560  0.1104  -0.1945 79  HIS   A CG  
605  N ND1 . HIS   A 83  ? 0.9580 1.2038 1.0068 0.0447  0.1200  -0.1985 79  HIS   A ND1 
606  C CD2 . HIS   A 83  ? 0.7772 1.0387 0.8625 0.0809  0.1054  -0.2093 79  HIS   A CD2 
607  C CE1 . HIS   A 83  ? 0.9555 1.2111 1.0084 0.0617  0.1214  -0.2156 79  HIS   A CE1 
608  N NE2 . HIS   A 83  ? 0.9218 1.1863 0.9967 0.0844  0.1125  -0.2225 79  HIS   A NE2 
609  N N   . ARG   A 84  ? 0.7218 0.8745 0.7373 0.0306  0.0960  -0.1511 80  ARG   A N   
610  C CA  . ARG   A 84  ? 0.7870 0.9140 0.7804 0.0306  0.0945  -0.1512 80  ARG   A CA  
611  C C   . ARG   A 84  ? 0.6390 0.7278 0.6254 0.0371  0.0804  -0.1390 80  ARG   A C   
612  O O   . ARG   A 84  ? 0.7009 0.7703 0.6774 0.0450  0.0761  -0.1434 80  ARG   A O   
613  C CB  . ARG   A 84  ? 0.6973 0.8223 0.6670 0.0090  0.1037  -0.1463 80  ARG   A CB  
614  C CG  . ARG   A 84  ? 0.9091 1.0721 0.8843 -0.0021 0.1191  -0.1569 80  ARG   A CG  
615  C CD  . ARG   A 84  ? 1.0845 1.2434 1.0311 -0.0226 0.1296  -0.1548 80  ARG   A CD  
616  N NE  . ARG   A 84  ? 1.1075 1.2309 1.0304 -0.0338 0.1224  -0.1357 80  ARG   A NE  
617  C CZ  . ARG   A 84  ? 1.2336 1.3484 1.1297 -0.0535 0.1293  -0.1286 80  ARG   A CZ  
618  N NH1 . ARG   A 84  ? 1.2897 1.3714 1.1651 -0.0598 0.1206  -0.1119 80  ARG   A NH1 
619  N NH2 . ARG   A 84  ? 1.1746 1.3137 1.0635 -0.0668 0.1449  -0.1386 80  ARG   A NH2 
620  N N   . PHE   A 85  ? 0.6404 0.7190 0.6317 0.0333  0.0735  -0.1248 81  PHE   A N   
621  C CA  . PHE   A 85  ? 0.7233 0.7702 0.7103 0.0388  0.0610  -0.1145 81  PHE   A CA  
622  C C   . PHE   A 85  ? 0.7088 0.7507 0.7090 0.0582  0.0540  -0.1211 81  PHE   A C   
623  O O   . PHE   A 85  ? 0.6888 0.7035 0.6800 0.0645  0.0465  -0.1200 81  PHE   A O   
624  C CB  . PHE   A 85  ? 0.7017 0.7408 0.6899 0.0296  0.0563  -0.0986 81  PHE   A CB  
625  C CG  . PHE   A 85  ? 0.8542 0.8643 0.8365 0.0318  0.0450  -0.0883 81  PHE   A CG  
626  C CD1 . PHE   A 85  ? 1.0023 0.9924 0.9688 0.0310  0.0416  -0.0893 81  PHE   A CD1 
627  C CD2 . PHE   A 85  ? 0.7973 0.8019 0.7896 0.0334  0.0383  -0.0785 81  PHE   A CD2 
628  C CE1 . PHE   A 85  ? 1.0373 1.0045 0.9995 0.0309  0.0321  -0.0811 81  PHE   A CE1 
629  C CE2 . PHE   A 85  ? 0.8124 0.7937 0.7997 0.0338  0.0293  -0.0702 81  PHE   A CE2 
630  C CZ  . PHE   A 85  ? 0.9381 0.9017 0.9110 0.0321  0.0263  -0.0717 81  PHE   A CZ  
631  N N   . GLN   A 86  ? 0.7462 0.8132 0.7662 0.0676  0.0558  -0.1282 82  GLN   A N   
632  C CA  . GLN   A 86  ? 0.7506 0.8108 0.7808 0.0881  0.0477  -0.1341 82  GLN   A CA  
633  C C   . GLN   A 86  ? 0.6964 0.7513 0.7202 0.1013  0.0489  -0.1491 82  GLN   A C   
634  O O   . GLN   A 86  ? 0.7979 0.8245 0.8152 0.1142  0.0401  -0.1499 82  GLN   A O   
635  C CB  . GLN   A 86  ? 0.7528 0.8445 0.8060 0.0958  0.0484  -0.1389 82  GLN   A CB  
636  C CG  . GLN   A 86  ? 0.8588 0.9391 0.9202 0.1169  0.0372  -0.1406 82  GLN   A CG  
637  C CD  . GLN   A 86  ? 0.8782 0.9149 0.9246 0.1166  0.0269  -0.1270 82  GLN   A CD  
638  O OE1 . GLN   A 86  ? 0.8969 0.9255 0.9429 0.1064  0.0238  -0.1131 82  GLN   A OE1 
639  N NE2 . GLN   A 86  ? 0.8306 0.8391 0.8638 0.1273  0.0220  -0.1317 82  GLN   A NE2 
640  N N   . GLU   A 87  ? 0.5748 0.6551 0.5985 0.0977  0.0599  -0.1616 83  GLU   A N   
641  C CA  . GLU   A 87  ? 0.6983 0.7748 0.7152 0.1104  0.0618  -0.1774 83  GLU   A CA  
642  C C   . GLU   A 87  ? 0.7341 0.7758 0.7262 0.1026  0.0595  -0.1731 83  GLU   A C   
643  O O   . GLU   A 87  ? 0.7391 0.7648 0.7222 0.1144  0.0575  -0.1839 83  GLU   A O   
644  C CB  . GLU   A 87  ? 0.6991 0.8178 0.7245 0.1084  0.0755  -0.1936 83  GLU   A CB  
645  C CG  . GLU   A 87  ? 0.9160 1.0765 0.9683 0.1150  0.0787  -0.2010 83  GLU   A CG  
646  C CD  . GLU   A 87  ? 0.9757 1.1346 1.0426 0.1424  0.0681  -0.2092 83  GLU   A CD  
647  O OE1 . GLU   A 87  ? 0.9981 1.1243 1.0530 0.1574  0.0602  -0.2123 83  GLU   A OE1 
648  O OE2 . GLU   A 87  ? 0.8908 1.0799 0.9797 0.1488  0.0672  -0.2126 83  GLU   A OE2 
649  N N   . TYR   A 88  ? 0.6034 0.6331 0.5837 0.0838  0.0592  -0.1583 84  TYR   A N   
650  C CA  . TYR   A 88  ? 0.7398 0.7368 0.6987 0.0772  0.0542  -0.1534 84  TYR   A CA  
651  C C   . TYR   A 88  ? 0.7217 0.6858 0.6790 0.0849  0.0420  -0.1463 84  TYR   A C   
652  O O   . TYR   A 88  ? 0.6724 0.6087 0.6146 0.0869  0.0373  -0.1494 84  TYR   A O   
653  C CB  . TYR   A 88  ? 0.6643 0.6606 0.6114 0.0568  0.0564  -0.1407 84  TYR   A CB  
654  C CG  . TYR   A 88  ? 0.5607 0.5298 0.4864 0.0496  0.0514  -0.1374 84  TYR   A CG  
655  C CD1 . TYR   A 88  ? 0.7877 0.7578 0.6964 0.0452  0.0571  -0.1467 84  TYR   A CD1 
656  C CD2 . TYR   A 88  ? 0.6372 0.5819 0.5597 0.0465  0.0410  -0.1259 84  TYR   A CD2 
657  C CE1 . TYR   A 88  ? 0.8774 0.8246 0.7668 0.0384  0.0517  -0.1446 84  TYR   A CE1 
658  C CE2 . TYR   A 88  ? 0.6554 0.5796 0.5602 0.0391  0.0361  -0.1244 84  TYR   A CE2 
659  C CZ  . TYR   A 88  ? 0.8232 0.7485 0.7115 0.0353  0.0410  -0.1337 84  TYR   A CZ  
660  O OH  . TYR   A 88  ? 0.9938 0.9005 0.8646 0.0278  0.0355  -0.1330 84  TYR   A OH  
661  N N   . ILE   A 89  ? 0.7011 0.6671 0.6721 0.0878  0.0369  -0.1370 85  ILE   A N   
662  C CA  . ILE   A 89  ? 0.7466 0.6813 0.7143 0.0935  0.0261  -0.1296 85  ILE   A CA  
663  C C   . ILE   A 89  ? 0.7406 0.6597 0.7063 0.1136  0.0220  -0.1417 85  ILE   A C   
664  O O   . ILE   A 89  ? 0.8104 0.6936 0.7611 0.1161  0.0151  -0.1406 85  ILE   A O   
665  C CB  . ILE   A 89  ? 0.6412 0.5835 0.6228 0.0913  0.0224  -0.1170 85  ILE   A CB  
666  C CG1 . ILE   A 89  ? 0.7747 0.7212 0.7532 0.0725  0.0239  -0.1042 85  ILE   A CG1 
667  C CG2 . ILE   A 89  ? 0.8493 0.7615 0.8273 0.0994  0.0123  -0.1114 85  ILE   A CG2 
668  C CD1 . ILE   A 89  ? 0.8004 0.7558 0.7918 0.0696  0.0213  -0.0930 85  ILE   A CD1 
669  N N   . ASP   A 90  ? 0.7013 0.6466 0.6808 0.1282  0.0260  -0.1540 86  ASP   A N   
670  C CA  . ASP   A 90  ? 0.8193 0.7501 0.7962 0.1507  0.0212  -0.1670 86  ASP   A CA  
671  C C   . ASP   A 90  ? 0.7641 0.6742 0.7218 0.1517  0.0232  -0.1778 86  ASP   A C   
672  O O   . ASP   A 90  ? 0.8484 0.7237 0.7925 0.1644  0.0160  -0.1828 86  ASP   A O   
673  C CB  . ASP   A 90  ? 0.8474 0.8181 0.8459 0.1667  0.0253  -0.1800 86  ASP   A CB  
674  C CG  . ASP   A 90  ? 0.9915 0.9798 1.0083 0.1685  0.0215  -0.1711 86  ASP   A CG  
675  O OD1 . ASP   A 90  ? 1.0715 1.0448 1.0845 0.1550  0.0177  -0.1544 86  ASP   A OD1 
676  O OD2 . ASP   A 90  ? 1.0438 1.0624 1.0788 0.1838  0.0219  -0.1818 86  ASP   A OD2 
677  N N   . ALA   A 91  ? 0.7281 0.6568 0.6819 0.1381  0.0326  -0.1816 87  ALA   A N   
678  C CA  . ALA   A 91  ? 0.7730 0.6833 0.7072 0.1370  0.0348  -0.1918 87  ALA   A CA  
679  C C   . ALA   A 91  ? 0.7895 0.6624 0.7038 0.1223  0.0284  -0.1809 87  ALA   A C   
680  O O   . ALA   A 91  ? 0.7469 0.5990 0.6430 0.1209  0.0283  -0.1891 87  ALA   A O   
681  C CB  . ALA   A 91  ? 0.7914 0.7357 0.7261 0.1273  0.0474  -0.2001 87  ALA   A CB  
682  N N   . HIS   A 92  ? 0.6876 0.5536 0.6054 0.1110  0.0233  -0.1639 88  HIS   A N   
683  C CA  . HIS   A 92  ? 0.7334 0.5703 0.6357 0.0960  0.0174  -0.1541 88  HIS   A CA  
684  C C   . HIS   A 92  ? 0.7354 0.5548 0.6422 0.0955  0.0093  -0.1409 88  HIS   A C   
685  O O   . HIS   A 92  ? 0.8706 0.7025 0.7861 0.0842  0.0088  -0.1280 88  HIS   A O   
686  C CB  . HIS   A 92  ? 0.6486 0.5034 0.5483 0.0768  0.0216  -0.1472 88  HIS   A CB  
687  C CG  . HIS   A 92  ? 0.7204 0.5900 0.6112 0.0747  0.0297  -0.1589 88  HIS   A CG  
688  N ND1 . HIS   A 92  ? 0.7821 0.6847 0.6832 0.0791  0.0392  -0.1660 88  HIS   A ND1 
689  C CD2 . HIS   A 92  ? 0.8660 0.7228 0.7377 0.0676  0.0301  -0.1654 88  HIS   A CD2 
690  C CE1 . HIS   A 92  ? 0.8878 0.7964 0.7754 0.0747  0.0456  -0.1759 88  HIS   A CE1 
691  N NE2 . HIS   A 92  ? 0.8000 0.6807 0.6695 0.0684  0.0398  -0.1757 88  HIS   A NE2 
692  N N   . PRO   A 93  ? 0.7810 0.5692 0.6799 0.1081  0.0028  -0.1440 89  PRO   A N   
693  C CA  . PRO   A 93  ? 0.8513 0.6179 0.7492 0.1054  -0.0046 -0.1311 89  PRO   A CA  
694  C C   . PRO   A 93  ? 0.8363 0.5790 0.7199 0.0859  -0.0081 -0.1230 89  PRO   A C   
695  O O   . PRO   A 93  ? 0.8218 0.5501 0.7044 0.0800  -0.0128 -0.1120 89  PRO   A O   
696  C CB  . PRO   A 93  ? 0.8323 0.5696 0.7212 0.1262  -0.0105 -0.1384 89  PRO   A CB  
697  C CG  . PRO   A 93  ? 1.0344 0.7661 0.9134 0.1359  -0.0074 -0.1554 89  PRO   A CG  
698  C CD  . PRO   A 93  ? 0.9190 0.6869 0.8060 0.1249  0.0018  -0.1596 89  PRO   A CD  
699  N N   . GLU   A 94  ? 0.9033 0.6434 0.7757 0.0754  -0.0057 -0.1290 90  GLU   A N   
700  C CA  . GLU   A 94  ? 0.9592 0.6843 0.8208 0.0557  -0.0090 -0.1228 90  GLU   A CA  
701  C C   . GLU   A 94  ? 0.8378 0.5938 0.7133 0.0423  -0.0076 -0.1118 90  GLU   A C   
702  O O   . GLU   A 94  ? 0.9017 0.6515 0.7757 0.0285  -0.0113 -0.1036 90  GLU   A O   
703  C CB  . GLU   A 94  ? 1.0485 0.7593 0.8921 0.0502  -0.0081 -0.1345 90  GLU   A CB  
704  C CG  . GLU   A 94  ? 1.2434 0.9374 1.0748 0.0300  -0.0123 -0.1309 90  GLU   A CG  
705  C CD  . GLU   A 94  ? 1.3113 0.9592 1.1233 0.0286  -0.0171 -0.1335 90  GLU   A CD  
706  O OE1 . GLU   A 94  ? 1.3251 0.9577 1.1256 0.0106  -0.0199 -0.1327 90  GLU   A OE1 
707  O OE2 . GLU   A 94  ? 1.3766 1.0030 1.1838 0.0454  -0.0184 -0.1365 90  GLU   A OE2 
708  N N   . THR   A 95  ? 0.9499 0.7383 0.8377 0.0458  -0.0021 -0.1120 91  THR   A N   
709  C CA  . THR   A 95  ? 0.8379 0.6516 0.7360 0.0349  -0.0013 -0.1016 91  THR   A CA  
710  C C   . THR   A 95  ? 0.7260 0.5422 0.6370 0.0353  -0.0043 -0.0900 91  THR   A C   
711  O O   . THR   A 95  ? 0.7169 0.5356 0.6368 0.0473  -0.0035 -0.0898 91  THR   A O   
712  C CB  . THR   A 95  ? 0.7219 0.5645 0.6261 0.0380  0.0058  -0.1047 91  THR   A CB  
713  O OG1 . THR   A 95  ? 0.6713 0.5113 0.5617 0.0379  0.0092  -0.1163 91  THR   A OG1 
714  C CG2 . THR   A 95  ? 0.6922 0.5542 0.6016 0.0269  0.0057  -0.0939 91  THR   A CG2 
715  N N   . ILE   A 96  ? 0.6483 0.4659 0.5607 0.0226  -0.0079 -0.0812 92  ILE   A N   
716  C CA  . ILE   A 96  ? 0.7555 0.5766 0.6791 0.0214  -0.0103 -0.0704 92  ILE   A CA  
717  C C   . ILE   A 96  ? 0.7012 0.5510 0.6391 0.0234  -0.0071 -0.0647 92  ILE   A C   
718  O O   . ILE   A 96  ? 0.7150 0.5801 0.6517 0.0176  -0.0055 -0.0642 92  ILE   A O   
719  C CB  . ILE   A 96  ? 0.8224 0.6367 0.7427 0.0068  -0.0148 -0.0651 92  ILE   A CB  
720  C CG1 . ILE   A 96  ? 0.7401 0.5243 0.6434 0.0016  -0.0173 -0.0717 92  ILE   A CG1 
721  C CG2 . ILE   A 96  ? 0.6823 0.4999 0.6130 0.0056  -0.0165 -0.0550 92  ILE   A CG2 
722  C CD1 . ILE   A 96  ? 0.8473 0.6029 0.7435 0.0101  -0.0185 -0.0720 92  ILE   A CD1 
723  N N   . VAL   A 97  ? 0.5459 0.4011 0.4950 0.0312  -0.0066 -0.0605 93  VAL   A N   
724  C CA  . VAL   A 97  ? 0.6643 0.5443 0.6262 0.0325  -0.0032 -0.0557 93  VAL   A CA  
725  C C   . VAL   A 97  ? 0.5753 0.4578 0.5451 0.0277  -0.0067 -0.0451 93  VAL   A C   
726  O O   . VAL   A 97  ? 0.6845 0.5551 0.6561 0.0313  -0.0096 -0.0422 93  VAL   A O   
727  C CB  . VAL   A 97  ? 0.7291 0.6191 0.6993 0.0453  0.0006  -0.0614 93  VAL   A CB  
728  C CG1 . VAL   A 97  ? 0.6668 0.5825 0.6489 0.0433  0.0048  -0.0573 93  VAL   A CG1 
729  C CG2 . VAL   A 97  ? 0.6518 0.5402 0.6144 0.0511  0.0044  -0.0738 93  VAL   A CG2 
730  N N   . LEU   A 98  ? 0.5774 0.4737 0.5501 0.0202  -0.0067 -0.0395 94  LEU   A N   
731  C CA  . LEU   A 98  ? 0.7030 0.6052 0.6839 0.0165  -0.0094 -0.0305 94  LEU   A CA  
732  C C   . LEU   A 98  ? 0.4949 0.4148 0.4827 0.0177  -0.0061 -0.0271 94  LEU   A C   
733  O O   . LEU   A 98  ? 0.5514 0.4779 0.5343 0.0129  -0.0058 -0.0255 94  LEU   A O   
734  C CB  . LEU   A 98  ? 0.6338 0.5350 0.6108 0.0069  -0.0137 -0.0280 94  LEU   A CB  
735  C CG  . LEU   A 98  ? 0.7448 0.6297 0.7125 0.0015  -0.0163 -0.0328 94  LEU   A CG  
736  C CD1 . LEU   A 98  ? 0.6198 0.5124 0.5851 -0.0080 -0.0202 -0.0328 94  LEU   A CD1 
737  C CD2 . LEU   A 98  ? 0.6635 0.5332 0.6316 0.0012  -0.0176 -0.0303 94  LEU   A CD2 
738  N N   . ASP   A 99  ? 0.6146 0.5405 0.6119 0.0236  -0.0042 -0.0260 95  ASP   A N   
739  C CA  . ASP   A 99  ? 0.6842 0.6002 0.6847 0.0308  -0.0063 -0.0271 95  ASP   A CA  
740  C C   . ASP   A 99  ? 0.6358 0.5592 0.6408 0.0410  -0.0029 -0.0347 95  ASP   A C   
741  O O   . ASP   A 99  ? 0.5503 0.4899 0.5579 0.0400  0.0024  -0.0382 95  ASP   A O   
742  C CB  . ASP   A 99  ? 0.6932 0.6115 0.7014 0.0302  -0.0089 -0.0193 95  ASP   A CB  
743  C CG  . ASP   A 99  ? 0.7262 0.6373 0.7309 0.0216  -0.0125 -0.0142 95  ASP   A CG  
744  O OD1 . ASP   A 99  ? 0.7914 0.6874 0.7876 0.0184  -0.0144 -0.0164 95  ASP   A OD1 
745  O OD2 . ASP   A 99  ? 0.6942 0.6155 0.7046 0.0179  -0.0131 -0.0088 95  ASP   A OD2 
746  N N   . PRO   A 100 ? 0.6521 0.5634 0.6565 0.0507  -0.0058 -0.0377 96  PRO   A N   
747  C CA  . PRO   A 100 ? 0.6178 0.5398 0.6288 0.0632  -0.0038 -0.0461 96  PRO   A CA  
748  C C   . PRO   A 100 ? 0.7531 0.7024 0.7788 0.0632  -0.0003 -0.0453 96  PRO   A C   
749  O O   . PRO   A 100 ? 0.7989 0.7524 0.8289 0.0570  -0.0015 -0.0371 96  PRO   A O   
750  C CB  . PRO   A 100 ? 0.7549 0.6555 0.7612 0.0740  -0.0103 -0.0461 96  PRO   A CB  
751  C CG  . PRO   A 100 ? 0.8255 0.6991 0.8169 0.0654  -0.0133 -0.0418 96  PRO   A CG  
752  C CD  . PRO   A 100 ? 0.7163 0.6012 0.7106 0.0506  -0.0112 -0.0350 96  PRO   A CD  
753  N N   . LEU   A 101 ? 0.7326 0.7011 0.7656 0.0698  0.0043  -0.0551 97  LEU   A N   
754  C CA  . LEU   A 101 ? 0.7939 0.7913 0.8401 0.0668  0.0094  -0.0567 97  LEU   A CA  
755  C C   . LEU   A 101 ? 0.7149 0.7213 0.7733 0.0750  0.0048  -0.0553 97  LEU   A C   
756  O O   . LEU   A 101 ? 0.7101 0.7308 0.7759 0.0677  0.0066  -0.0509 97  LEU   A O   
757  C CB  . LEU   A 101 ? 0.7035 0.7224 0.7539 0.0693  0.0170  -0.0693 97  LEU   A CB  
758  C CG  . LEU   A 101 ? 0.7743 0.7960 0.8143 0.0558  0.0245  -0.0696 97  LEU   A CG  
759  C CD1 . LEU   A 101 ? 0.8198 0.8474 0.8590 0.0416  0.0272  -0.0604 97  LEU   A CD1 
760  C CD2 . LEU   A 101 ? 0.8294 0.8248 0.8530 0.0538  0.0213  -0.0671 97  LEU   A CD2 
761  N N   . PRO   A 102 ? 0.8235 0.8209 0.8825 0.0904  -0.0015 -0.0592 98  PRO   A N   
762  C CA  . PRO   A 102 ? 0.7158 0.7189 0.7833 0.0981  -0.0075 -0.0565 98  PRO   A CA  
763  C C   . PRO   A 102 ? 0.6738 0.6655 0.7375 0.0878  -0.0102 -0.0435 98  PRO   A C   
764  O O   . PRO   A 102 ? 0.7073 0.7127 0.7801 0.0882  -0.0120 -0.0411 98  PRO   A O   
765  C CB  . PRO   A 102 ? 0.7765 0.7586 0.8364 0.1158  -0.0154 -0.0604 98  PRO   A CB  
766  C CG  . PRO   A 102 ? 0.6741 0.6579 0.7314 0.1210  -0.0112 -0.0715 98  PRO   A CG  
767  C CD  . PRO   A 102 ? 0.7234 0.7070 0.7751 0.1031  -0.0036 -0.0680 98  PRO   A CD  
768  N N   . ALA   A 103 ? 0.7058 0.6749 0.7569 0.0787  -0.0105 -0.0362 99  ALA   A N   
769  C CA  . ALA   A 103 ? 0.6679 0.6307 0.7168 0.0687  -0.0121 -0.0255 99  ALA   A CA  
770  C C   . ALA   A 103 ? 0.6427 0.6251 0.6988 0.0579  -0.0066 -0.0237 99  ALA   A C   
771  O O   . ALA   A 103 ? 0.6592 0.6453 0.7189 0.0535  -0.0078 -0.0177 99  ALA   A O   
772  C CB  . ALA   A 103 ? 0.7382 0.6764 0.7735 0.0617  -0.0137 -0.0203 99  ALA   A CB  
773  N N   . ILE   A 104 ? 0.7652 0.7578 0.8211 0.0532  -0.0005 -0.0288 100 ILE   A N   
774  C CA  . ILE   A 104 ? 0.7470 0.7534 0.8052 0.0423  0.0049  -0.0270 100 ILE   A CA  
775  C C   . ILE   A 104 ? 0.5654 0.5933 0.6365 0.0437  0.0062  -0.0299 100 ILE   A C   
776  O O   . ILE   A 104 ? 0.5719 0.6027 0.6446 0.0366  0.0064  -0.0247 100 ILE   A O   
777  C CB  . ILE   A 104 ? 0.7854 0.7965 0.8372 0.0367  0.0115  -0.0322 100 ILE   A CB  
778  C CG1 . ILE   A 104 ? 0.8136 0.8049 0.8514 0.0322  0.0096  -0.0277 100 ILE   A CG1 
779  C CG2 . ILE   A 104 ? 0.7952 0.8213 0.8479 0.0260  0.0181  -0.0322 100 ILE   A CG2 
780  C CD1 . ILE   A 104 ? 0.8137 0.7983 0.8457 0.0233  0.0081  -0.0188 100 ILE   A CD1 
781  N N   . ARG   A 105 ? 0.6195 0.6635 0.7002 0.0533  0.0067  -0.0394 101 ARG   A N   
782  C CA  . ARG   A 105 ? 0.5694 0.6393 0.6644 0.0545  0.0077  -0.0444 101 ARG   A CA  
783  C C   . ARG   A 105 ? 0.5958 0.6603 0.6937 0.0580  0.0005  -0.0378 101 ARG   A C   
784  O O   . ARG   A 105 ? 0.7247 0.8048 0.8302 0.0523  0.0017  -0.0379 101 ARG   A O   
785  C CB  . ARG   A 105 ? 0.6031 0.6933 0.7092 0.0675  0.0080  -0.0573 101 ARG   A CB  
786  C CG  . ARG   A 105 ? 0.8311 0.9430 0.9405 0.0606  0.0181  -0.0670 101 ARG   A CG  
787  C CD  . ARG   A 105 ? 0.7520 0.8987 0.8796 0.0707  0.0194  -0.0814 101 ARG   A CD  
788  N NE  . ARG   A 105 ? 0.8444 1.0131 0.9746 0.0642  0.0301  -0.0923 101 ARG   A NE  
789  C CZ  . ARG   A 105 ? 0.8156 0.9765 0.9383 0.0693  0.0328  -0.0975 101 ARG   A CZ  
790  N NH1 . ARG   A 105 ? 0.8257 1.0092 0.9503 0.0620  0.0435  -0.1078 101 ARG   A NH1 
791  N NH2 . ARG   A 105 ? 0.6086 0.7387 0.7205 0.0806  0.0252  -0.0930 101 ARG   A NH2 
792  N N   . THR   A 106 ? 0.4846 0.5262 0.5747 0.0660  -0.0065 -0.0324 102 THR   A N   
793  C CA  . THR   A 106 ? 0.7146 0.7496 0.8045 0.0688  -0.0130 -0.0260 102 THR   A CA  
794  C C   . THR   A 106 ? 0.5799 0.6099 0.6662 0.0557  -0.0110 -0.0177 102 THR   A C   
795  O O   . THR   A 106 ? 0.6632 0.7024 0.7547 0.0535  -0.0124 -0.0160 102 THR   A O   
796  C CB  . THR   A 106 ? 0.5851 0.5934 0.6634 0.0780  -0.0199 -0.0218 102 THR   A CB  
797  O OG1 . THR   A 106 ? 0.7144 0.7250 0.7947 0.0931  -0.0234 -0.0301 102 THR   A OG1 
798  C CG2 . THR   A 106 ? 0.5960 0.5956 0.6705 0.0788  -0.0258 -0.0144 102 THR   A CG2 
799  N N   . LEU   A 107 ? 0.4658 0.4818 0.5430 0.0478  -0.0082 -0.0133 103 LEU   A N   
800  C CA  . LEU   A 107 ? 0.5764 0.5851 0.6490 0.0386  -0.0078 -0.0058 103 LEU   A CA  
801  C C   . LEU   A 107 ? 0.5725 0.5926 0.6470 0.0291  -0.0027 -0.0068 103 LEU   A C   
802  O O   . LEU   A 107 ? 0.7658 0.7803 0.8369 0.0235  -0.0032 -0.0017 103 LEU   A O   
803  C CB  . LEU   A 107 ? 0.5249 0.5160 0.5872 0.0352  -0.0082 -0.0017 103 LEU   A CB  
804  C CG  . LEU   A 107 ? 0.5250 0.5002 0.5817 0.0407  -0.0127 0.0001  103 LEU   A CG  
805  C CD1 . LEU   A 107 ? 0.4694 0.4317 0.5179 0.0343  -0.0131 0.0040  103 LEU   A CD1 
806  C CD2 . LEU   A 107 ? 0.4067 0.3798 0.4647 0.0450  -0.0171 0.0034  103 LEU   A CD2 
807  N N   . LEU   A 108 ? 0.5446 0.5794 0.6232 0.0268  0.0026  -0.0137 104 LEU   A N   
808  C CA  . LEU   A 108 ? 0.6467 0.6900 0.7243 0.0154  0.0082  -0.0147 104 LEU   A CA  
809  C C   . LEU   A 108 ? 0.5285 0.5894 0.6170 0.0144  0.0077  -0.0180 104 LEU   A C   
810  O O   . LEU   A 108 ? 0.5802 0.6453 0.6665 0.0032  0.0119  -0.0185 104 LEU   A O   
811  C CB  . LEU   A 108 ? 0.5406 0.5933 0.6159 0.0099  0.0156  -0.0209 104 LEU   A CB  
812  C CG  . LEU   A 108 ? 0.7148 0.7911 0.8027 0.0163  0.0182  -0.0318 104 LEU   A CG  
813  C CD1 . LEU   A 108 ? 0.6030 0.7059 0.7024 0.0098  0.0226  -0.0388 104 LEU   A CD1 
814  C CD2 . LEU   A 108 ? 0.7046 0.7803 0.7855 0.0144  0.0239  -0.0362 104 LEU   A CD2 
815  N N   . ASP   A 109 ? 0.5514 0.6206 0.6495 0.0253  0.0021  -0.0204 105 ASP   A N   
816  C CA  . ASP   A 109 ? 0.5409 0.6291 0.6498 0.0260  0.0000  -0.0245 105 ASP   A CA  
817  C C   . ASP   A 109 ? 0.5498 0.6246 0.6551 0.0306  -0.0070 -0.0173 105 ASP   A C   
818  O O   . ASP   A 109 ? 0.5494 0.6139 0.6522 0.0412  -0.0127 -0.0146 105 ASP   A O   
819  C CB  . ASP   A 109 ? 0.6370 0.7488 0.7594 0.0368  -0.0017 -0.0345 105 ASP   A CB  
820  C CG  . ASP   A 109 ? 0.8502 0.9908 0.9862 0.0341  -0.0017 -0.0420 105 ASP   A CG  
821  O OD1 . ASP   A 109 ? 0.9447 1.1051 1.0863 0.0228  0.0061  -0.0490 105 ASP   A OD1 
822  O OD2 . ASP   A 109 ? 0.7052 0.8491 0.8452 0.0422  -0.0094 -0.0413 105 ASP   A OD2 
823  N N   . ARG   A 110 ? 0.4799 0.5533 0.5829 0.0220  -0.0063 -0.0146 106 ARG   A N   
824  C CA  . ARG   A 110 ? 0.5079 0.5695 0.6064 0.0250  -0.0118 -0.0084 106 ARG   A CA  
825  C C   . ARG   A 110 ? 0.4391 0.5112 0.5440 0.0357  -0.0186 -0.0108 106 ARG   A C   
826  O O   . ARG   A 110 ? 0.4094 0.4677 0.5076 0.0420  -0.0238 -0.0053 106 ARG   A O   
827  C CB  . ARG   A 110 ? 0.5275 0.5865 0.6222 0.0145  -0.0097 -0.0069 106 ARG   A CB  
828  C CG  . ARG   A 110 ? 0.5785 0.6173 0.6614 0.0085  -0.0067 -0.0013 106 ARG   A CG  
829  C CD  . ARG   A 110 ? 0.4231 0.4529 0.5000 0.0041  -0.0078 0.0014  106 ARG   A CD  
830  N NE  . ARG   A 110 ? 0.4674 0.4836 0.5334 -0.0045 -0.0039 0.0027  106 ARG   A NE  
831  C CZ  . ARG   A 110 ? 0.5116 0.5105 0.5680 -0.0028 -0.0046 0.0075  106 ARG   A CZ  
832  N NH1 . ARG   A 110 ? 0.5587 0.5547 0.6169 0.0050  -0.0079 0.0107  106 ARG   A NH1 
833  N NH2 . ARG   A 110 ? 0.6400 0.6240 0.6838 -0.0092 -0.0023 0.0088  106 ARG   A NH2 
834  N N   . SER   A 111 ? 0.4190 0.5159 0.5359 0.0376  -0.0189 -0.0194 107 SER   A N   
835  C CA  . SER   A 111 ? 0.5148 0.6229 0.6373 0.0501  -0.0271 -0.0226 107 SER   A CA  
836  C C   . SER   A 111 ? 0.5486 0.6425 0.6656 0.0643  -0.0321 -0.0204 107 SER   A C   
837  O O   . SER   A 111 ? 0.5477 0.6285 0.6565 0.0731  -0.0395 -0.0157 107 SER   A O   
838  C CB  . SER   A 111 ? 0.5820 0.7247 0.7210 0.0500  -0.0264 -0.0343 107 SER   A CB  
839  O OG  . SER   A 111 ? 0.8579 1.0127 1.0031 0.0668  -0.0352 -0.0391 107 SER   A OG  
840  N N   . LYS   A 112 ? 0.4195 0.5133 0.5382 0.0658  -0.0279 -0.0238 108 LYS   A N   
841  C CA  . LYS   A 112 ? 0.4636 0.5404 0.5750 0.0786  -0.0323 -0.0226 108 LYS   A CA  
842  C C   . LYS   A 112 ? 0.4691 0.5138 0.5640 0.0752  -0.0333 -0.0118 108 LYS   A C   
843  O O   . LYS   A 112 ? 0.3570 0.3825 0.4410 0.0842  -0.0395 -0.0079 108 LYS   A O   
844  C CB  . LYS   A 112 ? 0.5130 0.5979 0.6297 0.0799  -0.0269 -0.0299 108 LYS   A CB  
845  C CG  . LYS   A 112 ? 0.6855 0.8061 0.8198 0.0841  -0.0254 -0.0427 108 LYS   A CG  
846  C CD  . LYS   A 112 ? 0.7317 0.8618 0.8700 0.0811  -0.0173 -0.0499 108 LYS   A CD  
847  C CE  . LYS   A 112 ? 0.7155 0.8863 0.8728 0.0833  -0.0143 -0.0642 108 LYS   A CE  
848  N NZ  . LYS   A 112 ? 0.7859 0.9773 0.9505 0.0656  -0.0080 -0.0659 108 LYS   A NZ  
849  N N   . SER   A 113 ? 0.4271 0.4654 0.5187 0.0622  -0.0273 -0.0072 109 SER   A N   
850  C CA  . SER   A 113 ? 0.4194 0.4335 0.4983 0.0581  -0.0276 0.0013  109 SER   A CA  
851  C C   . SER   A 113 ? 0.5064 0.5130 0.5787 0.0592  -0.0325 0.0068  109 SER   A C   
852  O O   . SER   A 113 ? 0.4938 0.4804 0.5538 0.0608  -0.0352 0.0123  109 SER   A O   
853  C CB  . SER   A 113 ? 0.3465 0.3590 0.4246 0.0462  -0.0214 0.0036  109 SER   A CB  
854  O OG  . SER   A 113 ? 0.6417 0.6540 0.7200 0.0449  -0.0174 0.0004  109 SER   A OG  
855  N N   . TYR   A 114 ? 0.4141 0.4361 0.4929 0.0572  -0.0333 0.0051  110 TYR   A N   
856  C CA  . TYR   A 114 ? 0.4967 0.5128 0.5681 0.0580  -0.0377 0.0097  110 TYR   A CA  
857  C C   . TYR   A 114 ? 0.5243 0.5331 0.5885 0.0706  -0.0458 0.0102  110 TYR   A C   
858  O O   . TYR   A 114 ? 0.4231 0.4142 0.4729 0.0715  -0.0493 0.0166  110 TYR   A O   
859  C CB  . TYR   A 114 ? 0.4737 0.5080 0.5531 0.0528  -0.0370 0.0064  110 TYR   A CB  
860  C CG  . TYR   A 114 ? 0.3916 0.4245 0.4714 0.0412  -0.0307 0.0078  110 TYR   A CG  
861  C CD1 . TYR   A 114 ? 0.3842 0.4034 0.4589 0.0371  -0.0268 0.0116  110 TYR   A CD1 
862  C CD2 . TYR   A 114 ? 0.4302 0.4743 0.5143 0.0348  -0.0293 0.0047  110 TYR   A CD2 
863  C CE1 . TYR   A 114 ? 0.3545 0.3712 0.4282 0.0292  -0.0227 0.0125  110 TYR   A CE1 
864  C CE2 . TYR   A 114 ? 0.4114 0.4494 0.4928 0.0260  -0.0245 0.0058  110 TYR   A CE2 
865  C CZ  . TYR   A 114 ? 0.3553 0.3796 0.4314 0.0243  -0.0217 0.0098  110 TYR   A CZ  
866  O OH  . TYR   A 114 ? 0.3792 0.3965 0.4513 0.0182  -0.0185 0.0106  110 TYR   A OH  
867  N N   . GLU   A 115 ? 0.3842 0.4060 0.4570 0.0809  -0.0491 0.0032  111 GLU   A N   
868  C CA  . GLU   A 115 ? 0.5210 0.5332 0.5853 0.0961  -0.0583 0.0031  111 GLU   A CA  
869  C C   . GLU   A 115 ? 0.4812 0.4617 0.5287 0.0990  -0.0591 0.0084  111 GLU   A C   
870  O O   . GLU   A 115 ? 0.5546 0.5119 0.5841 0.1058  -0.0658 0.0137  111 GLU   A O   
871  C CB  . GLU   A 115 ? 0.6030 0.6413 0.6830 0.1078  -0.0617 -0.0079 111 GLU   A CB  
872  C CG  . GLU   A 115 ? 0.6534 0.6870 0.7262 0.1266  -0.0737 -0.0095 111 GLU   A CG  
873  C CD  . GLU   A 115 ? 0.8644 0.9047 0.9336 0.1275  -0.0802 -0.0071 111 GLU   A CD  
874  O OE1 . GLU   A 115 ? 1.0051 1.0779 1.0916 0.1247  -0.0798 -0.0145 111 GLU   A OE1 
875  O OE2 . GLU   A 115 ? 0.9592 0.9719 1.0070 0.1297  -0.0854 0.0019  111 GLU   A OE2 
876  N N   . LEU   A 116 ? 0.4559 0.4331 0.5067 0.0931  -0.0524 0.0070  112 LEU   A N   
877  C CA  . LEU   A 116 ? 0.5679 0.5153 0.6028 0.0933  -0.0525 0.0112  112 LEU   A CA  
878  C C   . LEU   A 116 ? 0.5642 0.4903 0.5828 0.0832  -0.0518 0.0207  112 LEU   A C   
879  O O   . LEU   A 116 ? 0.5424 0.4400 0.5412 0.0856  -0.0556 0.0256  112 LEU   A O   
880  C CB  . LEU   A 116 ? 0.6183 0.5692 0.6601 0.0863  -0.0450 0.0078  112 LEU   A CB  
881  C CG  . LEU   A 116 ? 0.6839 0.6069 0.7110 0.0870  -0.0452 0.0093  112 LEU   A CG  
882  C CD1 . LEU   A 116 ? 0.7724 0.6880 0.7960 0.1044  -0.0513 0.0031  112 LEU   A CD1 
883  C CD2 . LEU   A 116 ? 0.8051 0.7291 0.8355 0.0756  -0.0378 0.0085  112 LEU   A CD2 
884  N N   . ILE   A 117 ? 0.4419 0.3810 0.4674 0.0715  -0.0466 0.0229  113 ILE   A N   
885  C CA  . ILE   A 117 ? 0.5185 0.4442 0.5317 0.0612  -0.0446 0.0301  113 ILE   A CA  
886  C C   . ILE   A 117 ? 0.5501 0.4620 0.5471 0.0664  -0.0512 0.0348  113 ILE   A C   
887  O O   . ILE   A 117 ? 0.5570 0.4442 0.5343 0.0618  -0.0517 0.0409  113 ILE   A O   
888  C CB  . ILE   A 117 ? 0.5556 0.5007 0.5808 0.0514  -0.0390 0.0295  113 ILE   A CB  
889  C CG1 . ILE   A 117 ? 0.4925 0.4442 0.5272 0.0452  -0.0332 0.0268  113 ILE   A CG1 
890  C CG2 . ILE   A 117 ? 0.6195 0.5568 0.6338 0.0429  -0.0374 0.0350  113 ILE   A CG2 
891  C CD1 . ILE   A 117 ? 0.6272 0.5976 0.6738 0.0403  -0.0296 0.0244  113 ILE   A CD1 
892  N N   . ARG   A 118 ? 0.6154 0.5432 0.6193 0.0750  -0.0564 0.0318  114 ARG   A N   
893  C CA  . ARG   A 118 ? 0.6884 0.6045 0.6759 0.0810  -0.0638 0.0362  114 ARG   A CA  
894  C C   . ARG   A 118 ? 0.6239 0.5095 0.5906 0.0917  -0.0710 0.0392  114 ARG   A C   
895  O O   . ARG   A 118 ? 0.6638 0.5248 0.6064 0.0915  -0.0752 0.0464  114 ARG   A O   
896  C CB  . ARG   A 118 ? 0.6778 0.6205 0.6788 0.0891  -0.0689 0.0305  114 ARG   A CB  
897  C CG  . ARG   A 118 ? 0.8676 0.8027 0.8524 0.0932  -0.0763 0.0349  114 ARG   A CG  
898  C CD  . ARG   A 118 ? 0.8553 0.8214 0.8561 0.0977  -0.0802 0.0281  114 ARG   A CD  
899  N NE  . ARG   A 118 ? 0.7758 0.7577 0.7884 0.1133  -0.0876 0.0201  114 ARG   A NE  
900  C CZ  . ARG   A 118 ? 0.8227 0.7894 0.8222 0.1299  -0.0980 0.0207  114 ARG   A CZ  
901  N NH1 . ARG   A 118 ? 0.9867 0.9172 0.9571 0.1319  -0.1024 0.0303  114 ARG   A NH1 
902  N NH2 . ARG   A 118 ? 0.8563 0.8441 0.8708 0.1446  -0.1041 0.0112  114 ARG   A NH2 
903  N N   . LYS   A 119 ? 0.6307 0.5151 0.6038 0.1008  -0.0724 0.0339  115 LYS   A N   
904  C CA  . LYS   A 119 ? 0.7244 0.5758 0.6759 0.1123  -0.0796 0.0360  115 LYS   A CA  
905  C C   . LYS   A 119 ? 0.6982 0.5161 0.6289 0.0991  -0.0746 0.0429  115 LYS   A C   
906  O O   . LYS   A 119 ? 0.7037 0.4852 0.6058 0.1016  -0.0799 0.0492  115 LYS   A O   
907  C CB  . LYS   A 119 ? 0.6928 0.5555 0.6585 0.1271  -0.0825 0.0263  115 LYS   A CB  
908  C CG  . LYS   A 119 ? 0.7661 0.6628 0.7512 0.1413  -0.0885 0.0178  115 LYS   A CG  
909  C CD  . LYS   A 119 ? 0.8616 0.7434 0.8289 0.1582  -0.1019 0.0201  115 LYS   A CD  
910  C CE  . LYS   A 119 ? 0.9489 0.8446 0.9161 0.1526  -0.1039 0.0240  115 LYS   A CE  
911  N NZ  . LYS   A 119 ? 1.0899 0.9684 1.0360 0.1689  -0.1178 0.0271  115 LYS   A NZ  
912  N N   . ILE   A 120 ? 0.6165 0.4455 0.5596 0.0845  -0.0648 0.0417  116 ILE   A N   
913  C CA  . ILE   A 120 ? 0.6895 0.4929 0.6155 0.0698  -0.0595 0.0469  116 ILE   A CA  
914  C C   . ILE   A 120 ? 0.7498 0.5418 0.6582 0.0579  -0.0579 0.0550  116 ILE   A C   
915  O O   . ILE   A 120 ? 0.8720 0.6330 0.7559 0.0484  -0.0567 0.0606  116 ILE   A O   
916  C CB  . ILE   A 120 ? 0.6390 0.4613 0.5838 0.0585  -0.0507 0.0427  116 ILE   A CB  
917  C CG1 . ILE   A 120 ? 0.6227 0.4469 0.5766 0.0683  -0.0517 0.0354  116 ILE   A CG1 
918  C CG2 . ILE   A 120 ? 0.7848 0.5915 0.7169 0.0406  -0.0446 0.0470  116 ILE   A CG2 
919  C CD1 . ILE   A 120 ? 0.7249 0.5699 0.6970 0.0594  -0.0442 0.0309  116 ILE   A CD1 
920  N N   . GLU   A 121 ? 0.6879 0.5035 0.6065 0.0571  -0.0575 0.0553  117 GLU   A N   
921  C CA  . GLU   A 121 ? 0.8094 0.6151 0.7101 0.0465  -0.0558 0.0621  117 GLU   A CA  
922  C C   . GLU   A 121 ? 0.7016 0.4726 0.5708 0.0546  -0.0646 0.0687  117 GLU   A C   
923  O O   . GLU   A 121 ? 0.7612 0.5054 0.6036 0.0429  -0.0624 0.0758  117 GLU   A O   
924  C CB  . GLU   A 121 ? 0.6941 0.5320 0.6121 0.0452  -0.0538 0.0599  117 GLU   A CB  
925  C CG  . GLU   A 121 ? 0.8301 0.6956 0.7726 0.0361  -0.0453 0.0549  117 GLU   A CG  
926  C CD  . GLU   A 121 ? 0.9058 0.8005 0.8669 0.0395  -0.0454 0.0506  117 GLU   A CD  
927  O OE1 . GLU   A 121 ? 0.9570 0.8716 0.9364 0.0343  -0.0397 0.0464  117 GLU   A OE1 
928  O OE2 . GLU   A 121 ? 0.9097 0.8060 0.8659 0.0476  -0.0517 0.0512  117 GLU   A OE2 
929  N N   . ALA   A 122 ? 0.7941 0.5654 0.6650 0.0744  -0.0749 0.0660  118 ALA   A N   
930  C CA  . ALA   A 122 ? 0.8280 0.5627 0.6668 0.0859  -0.0856 0.0718  118 ALA   A CA  
931  C C   . ALA   A 122 ? 0.8797 0.5716 0.6936 0.0835  -0.0859 0.0752  118 ALA   A C   
932  O O   . ALA   A 122 ? 1.1271 0.7772 0.9046 0.0845  -0.0916 0.0831  118 ALA   A O   
933  C CB  . ALA   A 122 ? 0.8121 0.5619 0.6623 0.1099  -0.0972 0.0657  118 ALA   A CB  
934  N N   . TYR   A 123 ? 0.9668 0.6661 0.7973 0.0797  -0.0800 0.0696  119 TYR   A N   
935  C CA  . TYR   A 123 ? 1.0294 0.6890 0.8372 0.0749  -0.0792 0.0717  119 TYR   A CA  
936  C C   . TYR   A 123 ? 1.0243 0.6622 0.8094 0.0501  -0.0709 0.0793  119 TYR   A C   
937  O O   . TYR   A 123 ? 1.0202 0.6115 0.7684 0.0459  -0.0738 0.0861  119 TYR   A O   
938  C CB  . TYR   A 123 ? 1.1184 0.7963 0.9513 0.0758  -0.0745 0.0627  119 TYR   A CB  
939  C CG  . TYR   A 123 ? 1.2259 0.8679 1.0392 0.0674  -0.0719 0.0632  119 TYR   A CG  
940  C CD1 . TYR   A 123 ? 1.3303 0.9394 1.1263 0.0836  -0.0802 0.0610  119 TYR   A CD1 
941  C CD2 . TYR   A 123 ? 1.1688 0.8114 0.9817 0.0437  -0.0616 0.0647  119 TYR   A CD2 
942  C CE1 . TYR   A 123 ? 1.3542 0.9280 1.1306 0.0752  -0.0779 0.0608  119 TYR   A CE1 
943  C CE2 . TYR   A 123 ? 1.3791 0.9902 1.1742 0.0342  -0.0593 0.0642  119 TYR   A CE2 
944  C CZ  . TYR   A 123 ? 1.4412 1.0162 1.2171 0.0495  -0.0673 0.0625  119 TYR   A CZ  
945  O OH  . TYR   A 123 ? 1.5326 1.0735 1.2889 0.0395  -0.0650 0.0614  119 TYR   A OH  
946  N N   . MET   A 124 ? 1.0165 0.6874 0.8223 0.0334  -0.0606 0.0778  120 MET   A N   
947  C CA  . MET   A 124 ? 1.0672 0.7261 0.8565 0.0089  -0.0514 0.0825  120 MET   A CA  
948  C C   . MET   A 124 ? 0.9708 0.6093 0.7304 0.0033  -0.0530 0.0914  120 MET   A C   
949  O O   . MET   A 124 ? 1.0412 0.6487 0.7709 -0.0143 -0.0485 0.0973  120 MET   A O   
950  C CB  . MET   A 124 ? 0.8557 0.5590 0.6770 -0.0042 -0.0410 0.0770  120 MET   A CB  
951  C CG  . MET   A 124 ? 0.9814 0.7050 0.8298 -0.0001 -0.0392 0.0688  120 MET   A CG  
952  S SD  . MET   A 124 ? 0.9459 0.7189 0.8285 -0.0115 -0.0296 0.0628  120 MET   A SD  
953  C CE  . MET   A 124 ? 0.8521 0.6563 0.7598 0.0070  -0.0345 0.0594  120 MET   A CE  
954  N N   . GLU   A 125 ? 0.8980 0.5533 0.6641 0.0166  -0.0591 0.0920  121 GLU   A N   
955  C CA  . GLU   A 125 ? 1.0315 0.6704 0.7696 0.0127  -0.0614 0.1000  121 GLU   A CA  
956  C C   . GLU   A 125 ? 1.0675 0.7154 0.8004 -0.0134 -0.0484 0.1021  121 GLU   A C   
957  O O   . GLU   A 125 ? 1.1083 0.7269 0.8060 -0.0258 -0.0466 0.1100  121 GLU   A O   
958  C CB  . GLU   A 125 ? 0.9985 0.5810 0.6923 0.0204  -0.0713 0.1082  121 GLU   A CB  
959  C CG  . GLU   A 125 ? 1.0224 0.6010 0.7172 0.0498  -0.0866 0.1066  121 GLU   A CG  
960  C CD  . GLU   A 125 ? 1.2333 0.7552 0.8897 0.0613  -0.0971 0.1118  121 GLU   A CD  
961  O OE1 . GLU   A 125 ? 1.3449 0.8281 0.9731 0.0445  -0.0917 0.1170  121 GLU   A OE1 
962  O OE2 . GLU   A 125 ? 1.2587 0.7748 0.9129 0.0873  -0.1110 0.1100  121 GLU   A OE2 
963  N N   . ASP   A 126 ? 0.9761 0.6652 0.7434 -0.0218 -0.0393 0.0947  122 ASP   A N   
964  C CA  . ASP   A 126 ? 0.9919 0.7002 0.7621 -0.0438 -0.0270 0.0936  122 ASP   A CA  
965  C C   . ASP   A 126 ? 0.8537 0.6000 0.6450 -0.0388 -0.0259 0.0901  122 ASP   A C   
966  O O   . ASP   A 126 ? 0.6783 0.4542 0.5010 -0.0264 -0.0283 0.0836  122 ASP   A O   
967  C CB  . ASP   A 126 ? 1.0033 0.7297 0.7953 -0.0555 -0.0187 0.0869  122 ASP   A CB  
968  C CG  . ASP   A 126 ? 0.9931 0.7424 0.7895 -0.0780 -0.0062 0.0840  122 ASP   A CG  
969  O OD1 . ASP   A 126 ? 0.8873 0.6499 0.6797 -0.0825 -0.0029 0.0852  122 ASP   A OD1 
970  O OD2 . ASP   A 126 ? 1.0087 0.7653 0.8136 -0.0911 0.0002  0.0796  122 ASP   A OD2 
971  N N   . ASP   A 127 ? 0.8684 0.6120 0.6402 -0.0497 -0.0218 0.0941  123 ASP   A N   
972  C CA  . ASP   A 127 ? 0.9053 0.6796 0.6910 -0.0457 -0.0210 0.0909  123 ASP   A CA  
973  C C   . ASP   A 127 ? 0.8176 0.6361 0.6400 -0.0502 -0.0125 0.0811  123 ASP   A C   
974  O O   . ASP   A 127 ? 0.7827 0.6270 0.6190 -0.0457 -0.0119 0.0770  123 ASP   A O   
975  C CB  . ASP   A 127 ? 0.9730 0.7320 0.7257 -0.0590 -0.0170 0.0971  123 ASP   A CB  
976  C CG  . ASP   A 127 ? 1.1189 0.8998 0.8772 -0.0515 -0.0194 0.0951  123 ASP   A CG  
977  O OD1 . ASP   A 127 ? 1.2041 0.9826 0.9650 -0.0328 -0.0309 0.0958  123 ASP   A OD1 
978  O OD2 . ASP   A 127 ? 1.2052 1.0069 0.9653 -0.0644 -0.0098 0.0918  123 ASP   A OD2 
979  N N   . ARG   A 128 ? 0.7735 0.5999 0.6103 -0.0581 -0.0069 0.0770  124 ARG   A N   
980  C CA  . ARG   A 128 ? 0.7388 0.6047 0.6079 -0.0609 -0.0002 0.0677  124 ARG   A CA  
981  C C   . ARG   A 128 ? 0.6160 0.4989 0.5137 -0.0439 -0.0061 0.0628  124 ARG   A C   
982  O O   . ARG   A 128 ? 0.5273 0.4400 0.4495 -0.0431 -0.0024 0.0556  124 ARG   A O   
983  C CB  . ARG   A 128 ? 0.7401 0.6101 0.6115 -0.0778 0.0081  0.0647  124 ARG   A CB  
984  C CG  . ARG   A 128 ? 0.6970 0.5591 0.5441 -0.0992 0.0171  0.0672  124 ARG   A CG  
985  C CD  . ARG   A 128 ? 0.7229 0.5897 0.5727 -0.1172 0.0249  0.0632  124 ARG   A CD  
986  N NE  . ARG   A 128 ? 0.8043 0.6334 0.6363 -0.1186 0.0203  0.0685  124 ARG   A NE  
987  C CZ  . ARG   A 128 ? 0.7631 0.5869 0.5915 -0.1348 0.0256  0.0661  124 ARG   A CZ  
988  N NH1 . ARG   A 128 ? 0.7468 0.6045 0.5904 -0.1510 0.0354  0.0580  124 ARG   A NH1 
989  N NH2 . ARG   A 128 ? 0.6910 0.4767 0.5010 -0.1344 0.0207  0.0707  124 ARG   A NH2 
990  N N   . ILE   A 129 ? 0.6682 0.5331 0.5624 -0.0304 -0.0149 0.0658  125 ILE   A N   
991  C CA  . ILE   A 129 ? 0.5625 0.4435 0.4820 -0.0166 -0.0193 0.0608  125 ILE   A CA  
992  C C   . ILE   A 129 ? 0.6643 0.5498 0.5850 -0.0036 -0.0263 0.0611  125 ILE   A C   
993  O O   . ILE   A 129 ? 0.7159 0.5816 0.6149 0.0001  -0.0319 0.0666  125 ILE   A O   
994  C CB  . ILE   A 129 ? 0.7279 0.5912 0.6467 -0.0109 -0.0233 0.0614  125 ILE   A CB  
995  C CG1 . ILE   A 129 ? 0.7824 0.6360 0.6948 -0.0252 -0.0173 0.0614  125 ILE   A CG1 
996  C CG2 . ILE   A 129 ? 0.6757 0.5608 0.6218 -0.0013 -0.0247 0.0551  125 ILE   A CG2 
997  C CD1 . ILE   A 129 ? 0.8381 0.6548 0.7173 -0.0331 -0.0181 0.0685  125 ILE   A CD1 
998  N N   . CYS   A 130 ? 0.6630 0.5734 0.6075 0.0031  -0.0267 0.0552  126 CYS   A N   
999  C CA  . CYS   A 130 ? 0.7115 0.6293 0.6601 0.0143  -0.0333 0.0538  126 CYS   A CA  
1000 C C   . CYS   A 130 ? 0.6703 0.6071 0.6439 0.0209  -0.0339 0.0475  126 CYS   A C   
1001 O O   . CYS   A 130 ? 0.7204 0.6668 0.7072 0.0165  -0.0287 0.0443  126 CYS   A O   
1002 C CB  . CYS   A 130 ? 0.6931 0.6216 0.6370 0.0103  -0.0315 0.0531  126 CYS   A CB  
1003 S SG  . CYS   A 130 ? 0.8101 0.7666 0.7760 0.0052  -0.0238 0.0454  126 CYS   A SG  
1004 N N   . SER   A 131 ? 0.8063 0.7486 0.7849 0.0312  -0.0405 0.0455  127 SER   A N   
1005 C CA  . SER   A 131 ? 0.7132 0.6746 0.7130 0.0353  -0.0404 0.0391  127 SER   A CA  
1006 C C   . SER   A 131 ? 0.6611 0.6378 0.6656 0.0365  -0.0425 0.0355  127 SER   A C   
1007 O O   . SER   A 131 ? 0.8189 0.7928 0.8129 0.0413  -0.0486 0.0371  127 SER   A O   
1008 C CB  . SER   A 131 ? 0.7452 0.7048 0.7504 0.0451  -0.0454 0.0372  127 SER   A CB  
1009 O OG  . SER   A 131 ? 0.8884 0.8362 0.8925 0.0433  -0.0426 0.0386  127 SER   A OG  
1010 N N   . PRO   A 132 ? 0.5510 0.5419 0.5687 0.0325  -0.0383 0.0307  128 PRO   A N   
1011 C CA  . PRO   A 132 ? 0.5005 0.5049 0.5229 0.0330  -0.0405 0.0260  128 PRO   A CA  
1012 C C   . PRO   A 132 ? 0.4710 0.4850 0.5010 0.0402  -0.0467 0.0225  128 PRO   A C   
1013 O O   . PRO   A 132 ? 0.3910 0.4065 0.4293 0.0435  -0.0466 0.0212  128 PRO   A O   
1014 C CB  . PRO   A 132 ? 0.4657 0.4771 0.4990 0.0274  -0.0346 0.0217  128 PRO   A CB  
1015 C CG  . PRO   A 132 ? 0.6210 0.6265 0.6589 0.0267  -0.0312 0.0235  128 PRO   A CG  
1016 C CD  . PRO   A 132 ? 0.5583 0.5514 0.5850 0.0273  -0.0320 0.0291  128 PRO   A CD  
1017 N N   . PRO   A 133 ? 0.4703 0.4930 0.4976 0.0432  -0.0523 0.0201  129 PRO   A N   
1018 C CA  . PRO   A 133 ? 0.4424 0.4810 0.4801 0.0501  -0.0585 0.0145  129 PRO   A CA  
1019 C C   . PRO   A 133 ? 0.4616 0.5151 0.5171 0.0447  -0.0535 0.0079  129 PRO   A C   
1020 O O   . PRO   A 133 ? 0.4317 0.4836 0.4894 0.0358  -0.0472 0.0067  129 PRO   A O   
1021 C CB  . PRO   A 133 ? 0.3849 0.4324 0.4166 0.0512  -0.0645 0.0121  129 PRO   A CB  
1022 C CG  . PRO   A 133 ? 0.5038 0.5334 0.5160 0.0484  -0.0633 0.0191  129 PRO   A CG  
1023 C CD  . PRO   A 133 ? 0.4941 0.5136 0.5077 0.0408  -0.0538 0.0219  129 PRO   A CD  
1024 N N   . PHE   A 134 ? 0.3747 0.4417 0.4414 0.0505  -0.0564 0.0031  130 PHE   A N   
1025 C CA  . PHE   A 134 ? 0.3659 0.4468 0.4475 0.0442  -0.0508 -0.0032 130 PHE   A CA  
1026 C C   . PHE   A 134 ? 0.3789 0.4853 0.4738 0.0501  -0.0558 -0.0117 130 PHE   A C   
1027 O O   . PHE   A 134 ? 0.4595 0.5704 0.5520 0.0622  -0.0646 -0.0122 130 PHE   A O   
1028 C CB  . PHE   A 134 ? 0.4205 0.4887 0.5025 0.0432  -0.0451 0.0002  130 PHE   A CB  
1029 C CG  . PHE   A 134 ? 0.4917 0.5587 0.5749 0.0544  -0.0490 0.0004  130 PHE   A CG  
1030 C CD1 . PHE   A 134 ? 0.4642 0.5120 0.5334 0.0623  -0.0538 0.0070  130 PHE   A CD1 
1031 C CD2 . PHE   A 134 ? 0.4412 0.5248 0.5376 0.0567  -0.0475 -0.0066 130 PHE   A CD2 
1032 C CE1 . PHE   A 134 ? 0.5121 0.5539 0.5795 0.0734  -0.0580 0.0069  130 PHE   A CE1 
1033 C CE2 . PHE   A 134 ? 0.4005 0.4824 0.4975 0.0687  -0.0514 -0.0077 130 PHE   A CE2 
1034 C CZ  . PHE   A 134 ? 0.4470 0.5062 0.5289 0.0777  -0.0571 -0.0009 130 PHE   A CZ  
1035 N N   . MET   A 135 ? 0.3819 0.5053 0.4899 0.0416  -0.0502 -0.0189 131 MET   A N   
1036 C CA  . MET   A 135 ? 0.5372 0.6908 0.6613 0.0449  -0.0527 -0.0292 131 MET   A CA  
1037 C C   . MET   A 135 ? 0.5133 0.6771 0.6466 0.0308  -0.0428 -0.0347 131 MET   A C   
1038 O O   . MET   A 135 ? 0.3928 0.5414 0.5186 0.0182  -0.0364 -0.0315 131 MET   A O   
1039 C CB  . MET   A 135 ? 0.4715 0.6467 0.6001 0.0467  -0.0603 -0.0356 131 MET   A CB  
1040 C CG  . MET   A 135 ? 0.5541 0.7383 0.6853 0.0297  -0.0554 -0.0407 131 MET   A CG  
1041 S SD  . MET   A 135 ? 0.6260 0.8424 0.7656 0.0309  -0.0647 -0.0512 131 MET   A SD  
1042 C CE  . MET   A 135 ? 0.4832 0.7402 0.6467 0.0368  -0.0662 -0.0639 131 MET   A CE  
1043 N N   . GLU   A 136 ? 0.6480 0.8364 0.7958 0.0333  -0.0417 -0.0433 132 GLU   A N   
1044 C CA  . GLU   A 136 ? 0.6727 0.8740 0.8281 0.0183  -0.0318 -0.0496 132 GLU   A CA  
1045 C C   . GLU   A 136 ? 0.6490 0.8786 0.8146 0.0071  -0.0316 -0.0600 132 GLU   A C   
1046 O O   . GLU   A 136 ? 0.5863 0.8438 0.7639 0.0158  -0.0393 -0.0678 132 GLU   A O   
1047 C CB  . GLU   A 136 ? 0.7270 0.9431 0.8929 0.0249  -0.0292 -0.0550 132 GLU   A CB  
1048 C CG  . GLU   A 136 ? 0.8024 1.0333 0.9745 0.0080  -0.0179 -0.0620 132 GLU   A CG  
1049 C CD  . GLU   A 136 ? 0.9410 1.1662 1.1124 0.0112  -0.0123 -0.0614 132 GLU   A CD  
1050 O OE1 . GLU   A 136 ? 0.9631 1.1977 1.1420 0.0279  -0.0173 -0.0646 132 GLU   A OE1 
1051 O OE2 . GLU   A 136 ? 0.8644 1.0741 1.0261 -0.0024 -0.0034 -0.0579 132 GLU   A OE2 
1052 N N   . LEU   A 137 ? 0.6589 0.8802 0.8182 -0.0121 -0.0235 -0.0603 133 LEU   A N   
1053 C CA  . LEU   A 137 ? 0.7114 0.9540 0.8767 -0.0271 -0.0219 -0.0699 133 LEU   A CA  
1054 C C   . LEU   A 137 ? 0.6923 0.9507 0.8639 -0.0441 -0.0110 -0.0777 133 LEU   A C   
1055 O O   . LEU   A 137 ? 0.7125 0.9466 0.8697 -0.0594 -0.0025 -0.0734 133 LEU   A O   
1056 C CB  . LEU   A 137 ? 0.6666 0.8816 0.8152 -0.0365 -0.0217 -0.0642 133 LEU   A CB  
1057 C CG  . LEU   A 137 ? 0.7565 0.9891 0.9082 -0.0493 -0.0230 -0.0734 133 LEU   A CG  
1058 C CD1 . LEU   A 137 ? 0.7694 1.0292 0.9327 -0.0354 -0.0346 -0.0786 133 LEU   A CD1 
1059 C CD2 . LEU   A 137 ? 0.7191 0.9174 0.8509 -0.0587 -0.0211 -0.0676 133 LEU   A CD2 
1060 N N   . THR   A 138 ? 0.7558 1.0553 0.9478 -0.0410 -0.0114 -0.0895 134 THR   A N   
1061 C CA  . THR   A 138 ? 0.6867 1.0071 0.8858 -0.0583 0.0000  -0.0986 134 THR   A CA  
1062 C C   . THR   A 138 ? 0.6120 0.9413 0.8087 -0.0835 0.0059  -0.1059 134 THR   A C   
1063 O O   . THR   A 138 ? 0.5754 0.9073 0.7683 -0.1039 0.0176  -0.1100 134 THR   A O   
1064 C CB  . THR   A 138 ? 0.5634 0.9300 0.7871 -0.0467 -0.0020 -0.1114 134 THR   A CB  
1065 O OG1 . THR   A 138 ? 0.7765 1.1748 1.0155 -0.0371 -0.0129 -0.1200 134 THR   A OG1 
1066 C CG2 . THR   A 138 ? 0.6033 0.9557 0.8256 -0.0245 -0.0059 -0.1047 134 THR   A CG2 
1067 N N   . SER   A 139 ? 0.5639 0.8962 0.7607 -0.0838 -0.0015 -0.1077 135 SER   A N   
1068 C CA  . SER   A 139 ? 0.6501 0.9899 0.8438 -0.1081 0.0032  -0.1156 135 SER   A CA  
1069 C C   . SER   A 139 ? 0.7026 1.0314 0.8898 -0.1033 -0.0066 -0.1132 135 SER   A C   
1070 O O   . SER   A 139 ? 0.7993 1.1345 0.9927 -0.0816 -0.0179 -0.1106 135 SER   A O   
1071 C CB  . SER   A 139 ? 0.5987 0.9951 0.8169 -0.1187 0.0065  -0.1337 135 SER   A CB  
1072 O OG  . SER   A 139 ? 0.6402 1.0481 0.8575 -0.1400 0.0080  -0.1426 135 SER   A OG  
1073 N N   . LEU   A 140 ? 0.7354 1.0451 0.9077 -0.1240 -0.0020 -0.1142 136 LEU   A N   
1074 C CA  . LEU   A 140 ? 0.7505 1.0567 0.9179 -0.1237 -0.0101 -0.1158 136 LEU   A CA  
1075 C C   . LEU   A 140 ? 0.7683 1.1274 0.9579 -0.1297 -0.0144 -0.1324 136 LEU   A C   
1076 O O   . LEU   A 140 ? 0.8194 1.2123 1.0235 -0.1440 -0.0074 -0.1439 136 LEU   A O   
1077 C CB  . LEU   A 140 ? 0.8805 1.1445 1.0222 -0.1430 -0.0039 -0.1119 136 LEU   A CB  
1078 C CG  . LEU   A 140 ? 0.8367 1.0529 0.9573 -0.1300 -0.0074 -0.0978 136 LEU   A CG  
1079 C CD1 . LEU   A 140 ? 0.8411 1.0372 0.9576 -0.1179 -0.0042 -0.0865 136 LEU   A CD1 
1080 C CD2 . LEU   A 140 ? 0.9270 1.1050 1.0231 -0.1476 -0.0028 -0.0969 136 LEU   A CD2 
1081 N N   . CYS   A 141 ? 0.7600 1.1282 0.9520 -0.1189 -0.0261 -0.1343 137 CYS   A N   
1082 C CA  . CYS   A 141 ? 0.7797 1.2008 0.9937 -0.1192 -0.0336 -0.1500 137 CYS   A CA  
1083 C C   . CYS   A 141 ? 0.7185 1.1340 0.9224 -0.1294 -0.0388 -0.1542 137 CYS   A C   
1084 O O   . CYS   A 141 ? 0.6767 1.1068 0.8846 -0.1143 -0.0515 -0.1560 137 CYS   A O   
1085 C CB  . CYS   A 141 ? 0.7367 1.1835 0.9668 -0.0891 -0.0461 -0.1496 137 CYS   A CB  
1086 S SG  . CYS   A 141 ? 0.8177 1.2181 1.0270 -0.0632 -0.0555 -0.1307 137 CYS   A SG  
1087 N N   . GLY   A 142 ? 0.6100 1.0015 0.7980 -0.1555 -0.0290 -0.1559 138 GLY   A N   
1088 C CA  . GLY   A 142 ? 0.5607 0.9535 0.7414 -0.1710 -0.0319 -0.1643 138 GLY   A CA  
1089 C C   . GLY   A 142 ? 0.6771 1.0268 0.8345 -0.1616 -0.0376 -0.1541 138 GLY   A C   
1090 O O   . GLY   A 142 ? 0.6509 0.9622 0.7941 -0.1471 -0.0370 -0.1395 138 GLY   A O   
1091 N N   . ASP   A 143 ? 0.5805 0.9397 0.7344 -0.1708 -0.0432 -0.1634 139 ASP   A N   
1092 C CA  . ASP   A 143 ? 0.7094 1.0330 0.8414 -0.1647 -0.0483 -0.1572 139 ASP   A CA  
1093 C C   . ASP   A 143 ? 0.7966 1.1204 0.9296 -0.1349 -0.0594 -0.1476 139 ASP   A C   
1094 O O   . ASP   A 143 ? 0.7029 0.9977 0.8174 -0.1280 -0.0629 -0.1415 139 ASP   A O   
1095 C CB  . ASP   A 143 ? 0.7095 1.0497 0.8395 -0.1820 -0.0522 -0.1716 139 ASP   A CB  
1096 C CG  . ASP   A 143 ? 0.7280 1.0688 0.8554 -0.2147 -0.0411 -0.1824 139 ASP   A CG  
1097 O OD1 . ASP   A 143 ? 0.7688 1.0722 0.8812 -0.2252 -0.0299 -0.1752 139 ASP   A OD1 
1098 O OD2 . ASP   A 143 ? 0.6622 1.0408 0.8013 -0.2306 -0.0439 -0.1982 139 ASP   A OD2 
1099 N N   . ASP   A 144 ? 0.8149 1.1691 0.9672 -0.1176 -0.0648 -0.1465 140 ASP   A N   
1100 C CA  . ASP   A 144 ? 0.7894 1.1469 0.9416 -0.0906 -0.0767 -0.1390 140 ASP   A CA  
1101 C C   . ASP   A 144 ? 0.6942 1.0333 0.8464 -0.0738 -0.0739 -0.1257 140 ASP   A C   
1102 O O   . ASP   A 144 ? 0.6948 1.0467 0.8534 -0.0524 -0.0829 -0.1218 140 ASP   A O   
1103 C CB  . ASP   A 144 ? 0.7329 1.1434 0.9058 -0.0823 -0.0890 -0.1512 140 ASP   A CB  
1104 C CG  . ASP   A 144 ? 1.0250 1.4340 1.1873 -0.0642 -0.1031 -0.1477 140 ASP   A CG  
1105 O OD1 . ASP   A 144 ? 1.1513 1.5202 1.2908 -0.0604 -0.1020 -0.1367 140 ASP   A OD1 
1106 O OD2 . ASP   A 144 ? 0.9591 1.4084 1.1352 -0.0538 -0.1154 -0.1566 140 ASP   A OD2 
1107 N N   . THR   A 145 ? 0.6145 0.9212 0.7573 -0.0831 -0.0620 -0.1186 141 THR   A N   
1108 C CA  . THR   A 145 ? 0.7276 1.0214 0.8728 -0.0708 -0.0582 -0.1082 141 THR   A CA  
1109 C C   . THR   A 145 ? 0.6768 0.9485 0.8106 -0.0490 -0.0649 -0.0955 141 THR   A C   
1110 O O   . THR   A 145 ? 0.5707 0.8464 0.7109 -0.0329 -0.0679 -0.0900 141 THR   A O   
1111 C CB  . THR   A 145 ? 0.7684 1.0297 0.9023 -0.0858 -0.0451 -0.1034 141 THR   A CB  
1112 O OG1 . THR   A 145 ? 0.7735 1.0540 0.9152 -0.1083 -0.0380 -0.1149 141 THR   A OG1 
1113 C CG2 . THR   A 145 ? 0.6071 0.8565 0.7432 -0.0740 -0.0414 -0.0935 141 THR   A CG2 
1114 N N   . MET   A 146 ? 0.5357 0.7837 0.6516 -0.0489 -0.0671 -0.0915 142 MET   A N   
1115 C CA  . MET   A 146 ? 0.7101 0.9343 0.8126 -0.0321 -0.0708 -0.0793 142 MET   A CA  
1116 C C   . MET   A 146 ? 0.6914 0.9356 0.7988 -0.0135 -0.0829 -0.0781 142 MET   A C   
1117 O O   . MET   A 146 ? 0.6514 0.8795 0.7520 0.0008  -0.0848 -0.0676 142 MET   A O   
1118 C CB  . MET   A 146 ? 0.7958 0.9953 0.8788 -0.0367 -0.0701 -0.0774 142 MET   A CB  
1119 C CG  . MET   A 146 ? 0.6244 0.7909 0.6966 -0.0467 -0.0594 -0.0737 142 MET   A CG  
1120 S SD  . MET   A 146 ? 0.6820 0.8289 0.7553 -0.0369 -0.0534 -0.0613 142 MET   A SD  
1121 C CE  . MET   A 146 ? 0.7511 0.8893 0.8143 -0.0187 -0.0598 -0.0515 142 MET   A CE  
1122 N N   . ARG   A 147 ? 0.6061 0.8845 0.7239 -0.0132 -0.0917 -0.0890 143 ARG   A N   
1123 C CA  . ARG   A 147 ? 0.6937 0.9891 0.8136 0.0069  -0.1050 -0.0880 143 ARG   A CA  
1124 C C   . ARG   A 147 ? 0.6666 0.9697 0.7993 0.0197  -0.1052 -0.0853 143 ARG   A C   
1125 O O   . ARG   A 147 ? 0.7024 0.9993 0.8285 0.0390  -0.1140 -0.0786 143 ARG   A O   
1126 C CB  . ARG   A 147 ? 0.6650 0.9999 0.7956 0.0054  -0.1153 -0.1019 143 ARG   A CB  
1127 C CG  . ARG   A 147 ? 0.7649 1.1138 0.8932 0.0286  -0.1314 -0.1006 143 ARG   A CG  
1128 C CD  . ARG   A 147 ? 0.8888 1.2572 1.0118 0.0286  -0.1431 -0.1086 143 ARG   A CD  
1129 N NE  . ARG   A 147 ? 0.8816 1.2997 1.0296 0.0226  -0.1477 -0.1261 143 ARG   A NE  
1130 C CZ  . ARG   A 147 ? 0.9246 1.3584 1.0804 -0.0004 -0.1413 -0.1376 143 ARG   A CZ  
1131 N NH1 . ARG   A 147 ? 0.6506 1.1333 0.8303 -0.0068 -0.1452 -0.1544 143 ARG   A NH1 
1132 N NH2 . ARG   A 147 ? 0.9120 1.3126 1.0513 -0.0169 -0.1311 -0.1331 143 ARG   A NH2 
1133 N N   . LEU   A 148 ? 0.5082 0.8224 0.6567 0.0090  -0.0956 -0.0905 144 LEU   A N   
1134 C CA  . LEU   A 148 ? 0.4574 0.7737 0.6155 0.0203  -0.0938 -0.0874 144 LEU   A CA  
1135 C C   . LEU   A 148 ? 0.5143 0.7878 0.6552 0.0259  -0.0888 -0.0720 144 LEU   A C   
1136 O O   . LEU   A 148 ? 0.4960 0.7617 0.6351 0.0421  -0.0928 -0.0660 144 LEU   A O   
1137 C CB  . LEU   A 148 ? 0.5099 0.8486 0.6868 0.0053  -0.0836 -0.0970 144 LEU   A CB  
1138 C CG  . LEU   A 148 ? 0.6044 0.9466 0.7914 0.0154  -0.0803 -0.0953 144 LEU   A CG  
1139 C CD1 . LEU   A 148 ? 0.7179 1.0873 0.9161 0.0383  -0.0935 -0.1006 144 LEU   A CD1 
1140 C CD2 . LEU   A 148 ? 0.5551 0.9156 0.7563 -0.0032 -0.0680 -0.1041 144 LEU   A CD2 
1141 N N   . LEU   A 149 ? 0.5079 0.7533 0.6354 0.0130  -0.0803 -0.0663 145 LEU   A N   
1142 C CA  . LEU   A 149 ? 0.5556 0.7645 0.6680 0.0176  -0.0757 -0.0532 145 LEU   A CA  
1143 C C   . LEU   A 149 ? 0.5807 0.7736 0.6757 0.0299  -0.0838 -0.0451 145 LEU   A C   
1144 O O   . LEU   A 149 ? 0.6587 0.8295 0.7440 0.0386  -0.0833 -0.0352 145 LEU   A O   
1145 C CB  . LEU   A 149 ? 0.5892 0.7757 0.6934 0.0018  -0.0650 -0.0511 145 LEU   A CB  
1146 C CG  . LEU   A 149 ? 0.4913 0.6765 0.6037 -0.0092 -0.0550 -0.0532 145 LEU   A CG  
1147 C CD1 . LEU   A 149 ? 0.7169 0.9280 0.8410 -0.0241 -0.0528 -0.0657 145 LEU   A CD1 
1148 C CD2 . LEU   A 149 ? 0.4402 0.5917 0.5385 -0.0161 -0.0470 -0.0461 145 LEU   A CD2 
1149 N N   . GLU   A 150 ? 0.6147 0.8177 0.7040 0.0296  -0.0910 -0.0494 146 GLU   A N   
1150 C CA  . GLU   A 150 ? 0.6780 0.8648 0.7472 0.0399  -0.0984 -0.0417 146 GLU   A CA  
1151 C C   . GLU   A 150 ? 0.7582 0.9464 0.8250 0.0586  -0.1085 -0.0374 146 GLU   A C   
1152 O O   . GLU   A 150 ? 0.7754 0.9387 0.8222 0.0667  -0.1115 -0.0271 146 GLU   A O   
1153 C CB  . GLU   A 150 ? 0.8982 1.0975 0.9611 0.0355  -0.1047 -0.0483 146 GLU   A CB  
1154 C CG  . GLU   A 150 ? 1.0922 1.2802 1.1495 0.0190  -0.0957 -0.0510 146 GLU   A CG  
1155 C CD  . GLU   A 150 ? 1.3100 1.4929 1.3492 0.0186  -0.1009 -0.0515 146 GLU   A CD  
1156 O OE1 . GLU   A 150 ? 1.2814 1.4477 1.3107 0.0089  -0.0937 -0.0516 146 GLU   A OE1 
1157 O OE2 . GLU   A 150 ? 1.4528 1.6479 1.4864 0.0287  -0.1126 -0.0521 146 GLU   A OE2 
1158 N N   . LYS   A 151 ? 0.6615 0.8777 0.7473 0.0656  -0.1136 -0.0457 147 LYS   A N   
1159 C CA  . LYS   A 151 ? 0.6922 0.9087 0.7752 0.0860  -0.1243 -0.0430 147 LYS   A CA  
1160 C C   . LYS   A 151 ? 0.5293 0.7215 0.6092 0.0911  -0.1184 -0.0345 147 LYS   A C   
1161 O O   . LYS   A 151 ? 0.6187 0.8001 0.6899 0.1080  -0.1268 -0.0300 147 LYS   A O   
1162 C CB  . LYS   A 151 ? 0.7158 0.9752 0.8219 0.0937  -0.1326 -0.0570 147 LYS   A CB  
1163 C CG  . LYS   A 151 ? 0.7357 1.0232 0.8453 0.0903  -0.1409 -0.0669 147 LYS   A CG  
1164 C CD  . LYS   A 151 ? 0.8735 1.1476 0.9594 0.1055  -0.1555 -0.0607 147 LYS   A CD  
1165 C CE  . LYS   A 151 ? 0.8651 1.1108 0.9272 0.0938  -0.1508 -0.0523 147 LYS   A CE  
1166 N NZ  . LYS   A 151 ? 0.9476 1.1806 0.9839 0.1065  -0.1643 -0.0465 147 LYS   A NZ  
1167 N N   . ASN   A 152 ? 0.6634 0.8451 0.7484 0.0774  -0.1050 -0.0323 148 ASN   A N   
1168 C CA  . ASN   A 152 ? 0.5370 0.6933 0.6165 0.0800  -0.0989 -0.0237 148 ASN   A CA  
1169 C C   . ASN   A 152 ? 0.5530 0.6765 0.6121 0.0732  -0.0932 -0.0126 148 ASN   A C   
1170 O O   . ASN   A 152 ? 0.6405 0.7439 0.6955 0.0718  -0.0867 -0.0060 148 ASN   A O   
1171 C CB  . ASN   A 152 ? 0.6628 0.8309 0.7614 0.0709  -0.0886 -0.0291 148 ASN   A CB  
1172 C CG  . ASN   A 152 ? 0.7106 0.9126 0.8299 0.0783  -0.0929 -0.0405 148 ASN   A CG  
1173 O OD1 . ASN   A 152 ? 0.6430 0.8757 0.7765 0.0716  -0.0938 -0.0512 148 ASN   A OD1 
1174 N ND2 . ASN   A 152 ? 0.6171 0.8152 0.7385 0.0917  -0.0955 -0.0395 148 ASN   A ND2 
1175 N N   . GLY   A 153 ? 0.6038 0.7239 0.6506 0.0687  -0.0953 -0.0114 149 GLY   A N   
1176 C CA  . GLY   A 153 ? 0.6049 0.6988 0.6327 0.0626  -0.0900 -0.0026 149 GLY   A CA  
1177 C C   . GLY   A 153 ? 0.5710 0.6614 0.6042 0.0483  -0.0784 -0.0040 149 GLY   A C   
1178 O O   . GLY   A 153 ? 0.4886 0.5597 0.5095 0.0442  -0.0727 0.0024  149 GLY   A O   
1179 N N   . LEU   A 154 ? 0.5366 0.6444 0.5862 0.0406  -0.0748 -0.0125 150 LEU   A N   
1180 C CA  . LEU   A 154 ? 0.5922 0.6922 0.6443 0.0286  -0.0648 -0.0137 150 LEU   A CA  
1181 C C   . LEU   A 154 ? 0.5888 0.6901 0.6337 0.0211  -0.0647 -0.0183 150 LEU   A C   
1182 O O   . LEU   A 154 ? 0.4457 0.5642 0.4930 0.0204  -0.0708 -0.0250 150 LEU   A O   
1183 C CB  . LEU   A 154 ? 0.5375 0.6493 0.6064 0.0225  -0.0601 -0.0196 150 LEU   A CB  
1184 C CG  . LEU   A 154 ? 0.6122 0.7170 0.6865 0.0266  -0.0564 -0.0151 150 LEU   A CG  
1185 C CD1 . LEU   A 154 ? 0.4406 0.5588 0.5217 0.0386  -0.0636 -0.0164 150 LEU   A CD1 
1186 C CD2 . LEU   A 154 ? 0.5296 0.6356 0.6127 0.0161  -0.0483 -0.0189 150 LEU   A CD2 
1187 N N   . THR   A 155 ? 0.5387 0.6229 0.5750 0.0160  -0.0579 -0.0156 151 THR   A N   
1188 C CA  . THR   A 155 ? 0.5718 0.6535 0.5998 0.0095  -0.0565 -0.0205 151 THR   A CA  
1189 C C   . THR   A 155 ? 0.4839 0.5524 0.5132 0.0024  -0.0482 -0.0224 151 THR   A C   
1190 O O   . THR   A 155 ? 0.4660 0.5262 0.5002 0.0033  -0.0437 -0.0184 151 THR   A O   
1191 C CB  . THR   A 155 ? 0.6285 0.7014 0.6394 0.0134  -0.0580 -0.0158 151 THR   A CB  
1192 O OG1 . THR   A 155 ? 0.6046 0.6624 0.6113 0.0143  -0.0512 -0.0096 151 THR   A OG1 
1193 C CG2 . THR   A 155 ? 0.5401 0.6188 0.5444 0.0220  -0.0670 -0.0117 151 THR   A CG2 
1194 N N   . PHE   A 156 ? 0.4072 0.4721 0.4302 -0.0040 -0.0469 -0.0289 152 PHE   A N   
1195 C CA  . PHE   A 156 ? 0.4313 0.4788 0.4506 -0.0082 -0.0403 -0.0309 152 PHE   A CA  
1196 C C   . PHE   A 156 ? 0.5605 0.5971 0.5722 -0.0018 -0.0368 -0.0261 152 PHE   A C   
1197 O O   . PHE   A 156 ? 0.6498 0.6902 0.6533 0.0013  -0.0385 -0.0250 152 PHE   A O   
1198 C CB  . PHE   A 156 ? 0.5589 0.6026 0.5712 -0.0164 -0.0404 -0.0401 152 PHE   A CB  
1199 C CG  . PHE   A 156 ? 0.5763 0.6303 0.5961 -0.0264 -0.0420 -0.0464 152 PHE   A CG  
1200 C CD1 . PHE   A 156 ? 0.4998 0.5478 0.5255 -0.0324 -0.0378 -0.0461 152 PHE   A CD1 
1201 C CD2 . PHE   A 156 ? 0.5448 0.6160 0.5649 -0.0309 -0.0475 -0.0534 152 PHE   A CD2 
1202 C CE1 . PHE   A 156 ? 0.4937 0.5536 0.5260 -0.0441 -0.0379 -0.0528 152 PHE   A CE1 
1203 C CE2 . PHE   A 156 ? 0.5550 0.6402 0.5837 -0.0417 -0.0485 -0.0607 152 PHE   A CE2 
1204 C CZ  . PHE   A 156 ? 0.5082 0.5881 0.5431 -0.0491 -0.0430 -0.0606 152 PHE   A CZ  
1205 N N   . PRO   A 157 ? 0.4620 0.4865 0.4758 -0.0001 -0.0320 -0.0237 153 PRO   A N   
1206 C CA  . PRO   A 157 ? 0.4370 0.4541 0.4568 -0.0038 -0.0299 -0.0238 153 PRO   A CA  
1207 C C   . PRO   A 157 ? 0.4964 0.5203 0.5263 -0.0011 -0.0302 -0.0175 153 PRO   A C   
1208 O O   . PRO   A 157 ? 0.3939 0.4217 0.4243 0.0048  -0.0310 -0.0120 153 PRO   A O   
1209 C CB  . PRO   A 157 ? 0.4873 0.4869 0.5011 -0.0006 -0.0260 -0.0246 153 PRO   A CB  
1210 C CG  . PRO   A 157 ? 0.5059 0.5110 0.5180 0.0064  -0.0250 -0.0219 153 PRO   A CG  
1211 C CD  . PRO   A 157 ? 0.4782 0.4960 0.4868 0.0052  -0.0282 -0.0221 153 PRO   A CD  
1212 N N   . PHE   A 158 ? 0.3756 0.3997 0.4114 -0.0063 -0.0291 -0.0187 154 PHE   A N   
1213 C CA  . PHE   A 158 ? 0.3662 0.3957 0.4110 -0.0039 -0.0286 -0.0140 154 PHE   A CA  
1214 C C   . PHE   A 158 ? 0.4312 0.4474 0.4749 -0.0086 -0.0242 -0.0138 154 PHE   A C   
1215 O O   . PHE   A 158 ? 0.3625 0.3653 0.3981 -0.0147 -0.0223 -0.0175 154 PHE   A O   
1216 C CB  . PHE   A 158 ? 0.3363 0.3863 0.3907 -0.0046 -0.0325 -0.0165 154 PHE   A CB  
1217 C CG  . PHE   A 158 ? 0.4160 0.4749 0.4730 -0.0150 -0.0324 -0.0246 154 PHE   A CG  
1218 C CD1 . PHE   A 158 ? 0.4302 0.4873 0.4904 -0.0239 -0.0278 -0.0272 154 PHE   A CD1 
1219 C CD2 . PHE   A 158 ? 0.3657 0.4353 0.4209 -0.0171 -0.0367 -0.0301 154 PHE   A CD2 
1220 C CE1 . PHE   A 158 ? 0.4919 0.5576 0.5536 -0.0364 -0.0267 -0.0352 154 PHE   A CE1 
1221 C CE2 . PHE   A 158 ? 0.4292 0.5088 0.4873 -0.0285 -0.0366 -0.0386 154 PHE   A CE2 
1222 C CZ  . PHE   A 158 ? 0.4576 0.5353 0.5191 -0.0389 -0.0312 -0.0414 154 PHE   A CZ  
1223 N N   . ILE   A 159 ? 0.3233 0.3407 0.3726 -0.0056 -0.0229 -0.0094 155 ILE   A N   
1224 C CA  . ILE   A 159 ? 0.3399 0.3440 0.3861 -0.0091 -0.0192 -0.0080 155 ILE   A CA  
1225 C C   . ILE   A 159 ? 0.4917 0.5080 0.5458 -0.0151 -0.0174 -0.0099 155 ILE   A C   
1226 O O   . ILE   A 159 ? 0.3984 0.4315 0.4627 -0.0104 -0.0194 -0.0095 155 ILE   A O   
1227 C CB  . ILE   A 159 ? 0.3760 0.3720 0.4213 -0.0011 -0.0187 -0.0022 155 ILE   A CB  
1228 C CG1 . ILE   A 159 ? 0.4298 0.4159 0.4680 0.0038  -0.0193 -0.0024 155 ILE   A CG1 
1229 C CG2 . ILE   A 159 ? 0.3801 0.3652 0.4223 -0.0039 -0.0159 -0.0003 155 ILE   A CG2 
1230 C CD1 . ILE   A 159 ? 0.4773 0.4617 0.5170 0.0110  -0.0190 0.0016  155 ILE   A CD1 
1231 N N   . CYS   A 160 ? 0.4142 0.4213 0.4622 -0.0255 -0.0136 -0.0126 156 CYS   A N   
1232 C CA  . CYS   A 160 ? 0.4834 0.5027 0.5376 -0.0335 -0.0100 -0.0154 156 CYS   A CA  
1233 C C   . CYS   A 160 ? 0.4934 0.4991 0.5423 -0.0323 -0.0068 -0.0103 156 CYS   A C   
1234 O O   . CYS   A 160 ? 0.4916 0.4726 0.5260 -0.0338 -0.0056 -0.0073 156 CYS   A O   
1235 C CB  . CYS   A 160 ? 0.5987 0.6163 0.6471 -0.0492 -0.0066 -0.0218 156 CYS   A CB  
1236 S SG  . CYS   A 160 ? 0.6903 0.7206 0.7427 -0.0631 0.0005  -0.0260 156 CYS   A SG  
1237 N N   . LYS   A 161 ? 0.3784 0.3995 0.4379 -0.0285 -0.0060 -0.0099 157 LYS   A N   
1238 C CA  . LYS   A 161 ? 0.4230 0.4341 0.4778 -0.0276 -0.0031 -0.0059 157 LYS   A CA  
1239 C C   . LYS   A 161 ? 0.4514 0.4799 0.5133 -0.0351 0.0018  -0.0108 157 LYS   A C   
1240 O O   . LYS   A 161 ? 0.3588 0.4120 0.4336 -0.0370 0.0015  -0.0172 157 LYS   A O   
1241 C CB  . LYS   A 161 ? 0.3579 0.3686 0.4171 -0.0146 -0.0066 -0.0009 157 LYS   A CB  
1242 C CG  . LYS   A 161 ? 0.5339 0.5406 0.5925 -0.0070 -0.0112 0.0016  157 LYS   A CG  
1243 C CD  . LYS   A 161 ? 0.4434 0.4513 0.5058 0.0025  -0.0135 0.0058  157 LYS   A CD  
1244 C CE  . LYS   A 161 ? 0.4440 0.4435 0.5018 0.0073  -0.0158 0.0087  157 LYS   A CE  
1245 N NZ  . LYS   A 161 ? 0.4781 0.4792 0.5385 0.0134  -0.0173 0.0123  157 LYS   A NZ  
1246 N N   . THR   A 162 ? 0.3578 0.3750 0.4111 -0.0389 0.0060  -0.0083 158 THR   A N   
1247 C CA  . THR   A 162 ? 0.3444 0.3797 0.4046 -0.0447 0.0114  -0.0132 158 THR   A CA  
1248 C C   . THR   A 162 ? 0.5253 0.5817 0.6023 -0.0315 0.0080  -0.0151 158 THR   A C   
1249 O O   . THR   A 162 ? 0.4938 0.5422 0.5715 -0.0196 0.0028  -0.0100 158 THR   A O   
1250 C CB  . THR   A 162 ? 0.4248 0.4410 0.4690 -0.0508 0.0163  -0.0095 158 THR   A CB  
1251 O OG1 . THR   A 162 ? 0.5569 0.5597 0.5978 -0.0385 0.0120  -0.0030 158 THR   A OG1 
1252 C CG2 . THR   A 162 ? 0.5051 0.4944 0.5279 -0.0632 0.0188  -0.0071 158 THR   A CG2 
1253 N N   . ARG   A 163 ? 0.4583 0.5415 0.5481 -0.0340 0.0111  -0.0231 159 ARG   A N   
1254 C CA  . ARG   A 163 ? 0.6514 0.7545 0.7563 -0.0204 0.0073  -0.0266 159 ARG   A CA  
1255 C C   . ARG   A 163 ? 0.5095 0.6083 0.6121 -0.0163 0.0103  -0.0256 159 ARG   A C   
1256 O O   . ARG   A 163 ? 0.6329 0.7403 0.7440 -0.0034 0.0066  -0.0275 159 ARG   A O   
1257 C CB  . ARG   A 163 ? 0.6148 0.7531 0.7365 -0.0230 0.0082  -0.0378 159 ARG   A CB  
1258 C CG  . ARG   A 163 ? 0.5853 0.7403 0.7101 -0.0340 0.0174  -0.0453 159 ARG   A CG  
1259 C CD  . ARG   A 163 ? 0.8333 0.9721 0.9423 -0.0541 0.0248  -0.0433 159 ARG   A CD  
1260 N NE  . ARG   A 163 ? 1.0397 1.1941 1.1486 -0.0690 0.0350  -0.0506 159 ARG   A NE  
1261 C CZ  . ARG   A 163 ? 1.0242 1.1571 1.1129 -0.0866 0.0424  -0.0472 159 ARG   A CZ  
1262 N NH1 . ARG   A 163 ? 0.5419 0.6374 0.6108 -0.0880 0.0394  -0.0371 159 ARG   A NH1 
1263 N NH2 . ARG   A 163 ? 0.9301 1.0775 1.0168 -0.1021 0.0528  -0.0540 159 ARG   A NH2 
1264 N N   . VAL   A 164 ? 0.4526 0.5365 0.5417 -0.0267 0.0166  -0.0230 160 VAL   A N   
1265 C CA  . VAL   A 164 ? 0.5364 0.6108 0.6190 -0.0235 0.0189  -0.0208 160 VAL   A CA  
1266 C C   . VAL   A 164 ? 0.4021 0.4454 0.4681 -0.0228 0.0160  -0.0109 160 VAL   A C   
1267 O O   . VAL   A 164 ? 0.4659 0.4928 0.5180 -0.0325 0.0180  -0.0076 160 VAL   A O   
1268 C CB  . VAL   A 164 ? 0.4936 0.5783 0.5725 -0.0361 0.0284  -0.0266 160 VAL   A CB  
1269 C CG1 . VAL   A 164 ? 0.5179 0.5861 0.5841 -0.0345 0.0304  -0.0227 160 VAL   A CG1 
1270 C CG2 . VAL   A 164 ? 0.6315 0.7529 0.7303 -0.0337 0.0309  -0.0384 160 VAL   A CG2 
1271 N N   . ALA   A 165 ? 0.5135 0.5485 0.5802 -0.0114 0.0110  -0.0069 161 ALA   A N   
1272 C CA  . ALA   A 165 ? 0.5231 0.5352 0.5785 -0.0088 0.0070  0.0008  161 ALA   A CA  
1273 C C   . ALA   A 165 ? 0.6117 0.6098 0.6537 -0.0114 0.0092  0.0034  161 ALA   A C   
1274 O O   . ALA   A 165 ? 0.5961 0.5861 0.6359 -0.0049 0.0055  0.0065  161 ALA   A O   
1275 C CB  . ALA   A 165 ? 0.6245 0.6361 0.6869 0.0023  0.0009  0.0033  161 ALA   A CB  
1276 N N   . HIS   A 166 ? 0.6760 0.6713 0.7078 -0.0222 0.0151  0.0019  162 HIS   A N   
1277 C CA  . HIS   A 166 ? 0.6451 0.6247 0.6599 -0.0255 0.0168  0.0049  162 HIS   A CA  
1278 C C   . HIS   A 166 ? 0.7017 0.6717 0.7000 -0.0399 0.0230  0.0050  162 HIS   A C   
1279 O O   . HIS   A 166 ? 0.6799 0.6634 0.6841 -0.0488 0.0282  0.0000  162 HIS   A O   
1280 C CB  . HIS   A 166 ? 0.7609 0.7517 0.7807 -0.0220 0.0193  0.0007  162 HIS   A CB  
1281 C CG  . HIS   A 166 ? 0.7881 0.7643 0.7893 -0.0262 0.0213  0.0031  162 HIS   A CG  
1282 N ND1 . HIS   A 166 ? 0.8628 0.8216 0.8537 -0.0205 0.0150  0.0087  162 HIS   A ND1 
1283 C CD2 . HIS   A 166 ? 0.8552 0.8327 0.8452 -0.0358 0.0287  0.0002  162 HIS   A CD2 
1284 C CE1 . HIS   A 166 ? 0.9557 0.9043 0.9291 -0.0255 0.0174  0.0096  162 HIS   A CE1 
1285 N NE2 . HIS   A 166 ? 0.9371 0.8955 0.9085 -0.0353 0.0262  0.0049  162 HIS   A NE2 
1286 N N   . GLY   A 167 ? 0.7510 0.6967 0.7270 -0.0426 0.0221  0.0104  163 GLY   A N   
1287 C CA  . GLY   A 167 ? 0.7220 0.6513 0.6756 -0.0572 0.0279  0.0118  163 GLY   A CA  
1288 C C   . GLY   A 167 ? 0.6564 0.5611 0.5955 -0.0597 0.0242  0.0166  163 GLY   A C   
1289 O O   . GLY   A 167 ? 0.7878 0.6892 0.7345 -0.0492 0.0170  0.0186  163 GLY   A O   
1290 N N   . THR   A 168 ? 0.7498 0.6356 0.6656 -0.0748 0.0298  0.0179  164 THR   A N   
1291 C CA  . THR   A 168 ? 0.7999 0.6556 0.6959 -0.0785 0.0266  0.0223  164 THR   A CA  
1292 C C   . THR   A 168 ? 0.8549 0.7256 0.7694 -0.0800 0.0268  0.0176  164 THR   A C   
1293 O O   . THR   A 168 ? 0.7733 0.6731 0.7061 -0.0878 0.0330  0.0106  164 THR   A O   
1294 C CB  . THR   A 168 ? 0.8865 0.7161 0.7502 -0.0973 0.0337  0.0246  164 THR   A CB  
1295 O OG1 . THR   A 168 ? 0.9679 0.7737 0.8074 -0.0931 0.0304  0.0309  164 THR   A OG1 
1296 C CG2 . THR   A 168 ? 1.0040 0.8030 0.8478 -0.1045 0.0322  0.0271  164 THR   A CG2 
1297 N N   . ASN   A 169 ? 0.7977 0.6502 0.7076 -0.0712 0.0192  0.0207  165 ASN   A N   
1298 C CA  . ASN   A 169 ? 0.9114 0.7720 0.8337 -0.0715 0.0180  0.0170  165 ASN   A CA  
1299 C C   . ASN   A 169 ? 0.5806 0.4774 0.5355 -0.0616 0.0161  0.0126  165 ASN   A C   
1300 O O   . ASN   A 169 ? 0.6036 0.5125 0.5705 -0.0627 0.0156  0.0087  165 ASN   A O   
1301 C CB  . ASN   A 169 ? 0.7572 0.6160 0.6710 -0.0922 0.0260  0.0126  165 ASN   A CB  
1302 C CG  . ASN   A 169 ? 0.8862 0.7006 0.7625 -0.1031 0.0271  0.0176  165 ASN   A CG  
1303 O OD1 . ASN   A 169 ? 0.8616 0.6449 0.7211 -0.0929 0.0194  0.0225  165 ASN   A OD1 
1304 N ND2 . ASN   A 169 ? 0.9775 0.7882 0.8391 -0.1239 0.0367  0.0158  165 ASN   A ND2 
1305 N N   . SER   A 170 ? 0.5589 0.4712 0.5262 -0.0522 0.0147  0.0132  166 SER   A N   
1306 C CA  . SER   A 170 ? 0.5548 0.4944 0.5479 -0.0420 0.0120  0.0102  166 SER   A CA  
1307 C C   . SER   A 170 ? 0.5937 0.5270 0.5907 -0.0299 0.0046  0.0130  166 SER   A C   
1308 O O   . SER   A 170 ? 0.4941 0.4457 0.5084 -0.0236 0.0024  0.0109  166 SER   A O   
1309 C CB  . SER   A 170 ? 0.5534 0.5065 0.5551 -0.0363 0.0128  0.0097  166 SER   A CB  
1310 O OG  . SER   A 170 ? 0.4931 0.4298 0.4850 -0.0282 0.0081  0.0150  166 SER   A OG  
1311 N N   . HIS   A 171 ? 0.5241 0.4324 0.5045 -0.0260 0.0005  0.0172  167 HIS   A N   
1312 C CA  . HIS   A 171 ? 0.5514 0.4556 0.5350 -0.0148 -0.0058 0.0182  167 HIS   A CA  
1313 C C   . HIS   A 171 ? 0.4682 0.3594 0.4437 -0.0184 -0.0063 0.0165  167 HIS   A C   
1314 O O   . HIS   A 171 ? 0.5047 0.3946 0.4834 -0.0095 -0.0108 0.0159  167 HIS   A O   
1315 C CB  . HIS   A 171 ? 0.6449 0.5336 0.6176 -0.0052 -0.0112 0.0220  167 HIS   A CB  
1316 C CG  . HIS   A 171 ? 0.6439 0.5459 0.6253 -0.0009 -0.0117 0.0230  167 HIS   A CG  
1317 N ND1 . HIS   A 171 ? 0.6609 0.5858 0.6620 0.0016  -0.0108 0.0210  167 HIS   A ND1 
1318 C CD2 . HIS   A 171 ? 0.6382 0.5313 0.6091 0.0012  -0.0135 0.0255  167 HIS   A CD2 
1319 C CE1 . HIS   A 171 ? 0.6163 0.5454 0.6190 0.0044  -0.0116 0.0219  167 HIS   A CE1 
1320 N NE2 . HIS   A 171 ? 0.8094 0.7212 0.7949 0.0041  -0.0132 0.0244  167 HIS   A NE2 
1321 N N   . GLU   A 172 ? 0.5638 0.4457 0.5282 -0.0322 -0.0015 0.0148  168 GLU   A N   
1322 C CA  . GLU   A 172 ? 0.5688 0.4367 0.5239 -0.0378 -0.0016 0.0123  168 GLU   A CA  
1323 C C   . GLU   A 172 ? 0.5498 0.4454 0.5261 -0.0388 -0.0009 0.0071  168 GLU   A C   
1324 O O   . GLU   A 172 ? 0.5682 0.4874 0.5578 -0.0459 0.0032  0.0038  168 GLU   A O   
1325 C CB  . GLU   A 172 ? 0.7627 0.6098 0.6964 -0.0550 0.0040  0.0121  168 GLU   A CB  
1326 C CG  . GLU   A 172 ? 0.7225 0.5339 0.6280 -0.0540 0.0021  0.0180  168 GLU   A CG  
1327 C CD  . GLU   A 172 ? 0.7937 0.5750 0.6827 -0.0423 -0.0056 0.0198  168 GLU   A CD  
1328 O OE1 . GLU   A 172 ? 0.9004 0.6577 0.7712 -0.0337 -0.0106 0.0246  168 GLU   A OE1 
1329 O OE2 . GLU   A 172 ? 0.7520 0.5342 0.6459 -0.0409 -0.0071 0.0158  168 GLU   A OE2 
1330 N N   . MET   A 173 ? 0.5076 0.4011 0.4863 -0.0309 -0.0052 0.0058  169 MET   A N   
1331 C CA  . MET   A 173 ? 0.4292 0.3463 0.4248 -0.0303 -0.0059 0.0016  169 MET   A CA  
1332 C C   . MET   A 173 ? 0.5064 0.4093 0.4919 -0.0336 -0.0072 -0.0022 169 MET   A C   
1333 O O   . MET   A 173 ? 0.4688 0.3419 0.4344 -0.0343 -0.0081 -0.0014 169 MET   A O   
1334 C CB  . MET   A 173 ? 0.3908 0.3243 0.4010 -0.0166 -0.0096 0.0035  169 MET   A CB  
1335 C CG  . MET   A 173 ? 0.4155 0.3567 0.4321 -0.0121 -0.0092 0.0073  169 MET   A CG  
1336 S SD  . MET   A 173 ? 0.5234 0.4790 0.5530 0.0005  -0.0129 0.0094  169 MET   A SD  
1337 C CE  . MET   A 173 ? 0.5022 0.4640 0.5367 0.0016  -0.0115 0.0123  169 MET   A CE  
1338 N N   . ALA   A 174 ? 0.4208 0.3438 0.4185 -0.0349 -0.0078 -0.0066 170 ALA   A N   
1339 C CA  . ALA   A 174 ? 0.4845 0.3978 0.4744 -0.0380 -0.0092 -0.0114 170 ALA   A CA  
1340 C C   . ALA   A 174 ? 0.4850 0.4216 0.4895 -0.0306 -0.0123 -0.0136 170 ALA   A C   
1341 O O   . ALA   A 174 ? 0.5302 0.4923 0.5500 -0.0302 -0.0126 -0.0137 170 ALA   A O   
1342 C CB  . ALA   A 174 ? 0.4860 0.3963 0.4690 -0.0561 -0.0053 -0.0165 170 ALA   A CB  
1343 N N   . ILE   A 175 ? 0.3990 0.3254 0.3968 -0.0243 -0.0149 -0.0156 171 ILE   A N   
1344 C CA  . ILE   A 175 ? 0.4155 0.3602 0.4223 -0.0184 -0.0174 -0.0177 171 ILE   A CA  
1345 C C   . ILE   A 175 ? 0.3538 0.2963 0.3543 -0.0269 -0.0179 -0.0248 171 ILE   A C   
1346 O O   . ILE   A 175 ? 0.4324 0.3503 0.4173 -0.0300 -0.0175 -0.0282 171 ILE   A O   
1347 C CB  . ILE   A 175 ? 0.4051 0.3452 0.4104 -0.0052 -0.0191 -0.0161 171 ILE   A CB  
1348 C CG1 . ILE   A 175 ? 0.4779 0.4326 0.4869 -0.0019 -0.0206 -0.0192 171 ILE   A CG1 
1349 C CG2 . ILE   A 175 ? 0.5718 0.4836 0.5612 -0.0016 -0.0196 -0.0178 171 ILE   A CG2 
1350 C CD1 . ILE   A 175 ? 0.5884 0.5476 0.5996 0.0091  -0.0207 -0.0178 171 ILE   A CD1 
1351 N N   . VAL   A 176 ? 0.3792 0.3461 0.3905 -0.0304 -0.0194 -0.0276 172 VAL   A N   
1352 C CA  . VAL   A 176 ? 0.3688 0.3396 0.3764 -0.0399 -0.0205 -0.0352 172 VAL   A CA  
1353 C C   . VAL   A 176 ? 0.5066 0.4857 0.5140 -0.0321 -0.0239 -0.0371 172 VAL   A C   
1354 O O   . VAL   A 176 ? 0.3438 0.3396 0.3600 -0.0237 -0.0260 -0.0330 172 VAL   A O   
1355 C CB  . VAL   A 176 ? 0.4656 0.4616 0.4857 -0.0497 -0.0205 -0.0386 172 VAL   A CB  
1356 C CG1 . VAL   A 176 ? 0.4147 0.4166 0.4315 -0.0612 -0.0218 -0.0477 172 VAL   A CG1 
1357 C CG2 . VAL   A 176 ? 0.4134 0.4037 0.4337 -0.0579 -0.0157 -0.0367 172 VAL   A CG2 
1358 N N   . PHE   A 177 ? 0.3874 0.3529 0.3825 -0.0355 -0.0243 -0.0435 173 PHE   A N   
1359 C CA  . PHE   A 177 ? 0.5146 0.4849 0.5063 -0.0283 -0.0266 -0.0461 173 PHE   A CA  
1360 C C   . PHE   A 177 ? 0.4950 0.4799 0.4861 -0.0357 -0.0299 -0.0531 173 PHE   A C   
1361 O O   . PHE   A 177 ? 0.4357 0.4308 0.4253 -0.0297 -0.0323 -0.0540 173 PHE   A O   
1362 C CB  . PHE   A 177 ? 0.5182 0.4623 0.4953 -0.0229 -0.0251 -0.0493 173 PHE   A CB  
1363 C CG  . PHE   A 177 ? 0.5361 0.4681 0.5133 -0.0131 -0.0234 -0.0436 173 PHE   A CG  
1364 C CD1 . PHE   A 177 ? 0.4512 0.3947 0.4348 -0.0016 -0.0231 -0.0402 173 PHE   A CD1 
1365 C CD2 . PHE   A 177 ? 0.5680 0.4772 0.5375 -0.0164 -0.0221 -0.0419 173 PHE   A CD2 
1366 C CE1 . PHE   A 177 ? 0.5425 0.4786 0.5277 0.0070  -0.0221 -0.0363 173 PHE   A CE1 
1367 C CE2 . PHE   A 177 ? 0.5799 0.4789 0.5489 -0.0066 -0.0218 -0.0370 173 PHE   A CE2 
1368 C CZ  . PHE   A 177 ? 0.5859 0.5001 0.5641 0.0055  -0.0221 -0.0347 173 PHE   A CZ  
1369 N N   . ASN   A 178 ? 0.4608 0.4479 0.4523 -0.0492 -0.0299 -0.0586 174 ASN   A N   
1370 C CA  . ASN   A 178 ? 0.5902 0.5912 0.5804 -0.0571 -0.0335 -0.0671 174 ASN   A CA  
1371 C C   . ASN   A 178 ? 0.6221 0.6404 0.6221 -0.0712 -0.0336 -0.0716 174 ASN   A C   
1372 O O   . ASN   A 178 ? 0.5931 0.6107 0.5992 -0.0750 -0.0300 -0.0681 174 ASN   A O   
1373 C CB  . ASN   A 178 ? 0.4761 0.4524 0.4479 -0.0611 -0.0326 -0.0746 174 ASN   A CB  
1374 C CG  . ASN   A 178 ? 0.5568 0.4990 0.5157 -0.0671 -0.0281 -0.0750 174 ASN   A CG  
1375 O OD1 . ASN   A 178 ? 0.5710 0.5093 0.5289 -0.0816 -0.0259 -0.0773 174 ASN   A OD1 
1376 N ND2 . ASN   A 178 ? 0.5901 0.5076 0.5377 -0.0560 -0.0268 -0.0732 174 ASN   A ND2 
1377 N N   . GLN   A 179 ? 0.5439 0.5801 0.5453 -0.0792 -0.0376 -0.0803 175 GLN   A N   
1378 C CA  . GLN   A 179 ? 0.6230 0.6822 0.6356 -0.0938 -0.0379 -0.0873 175 GLN   A CA  
1379 C C   . GLN   A 179 ? 0.5569 0.5922 0.5592 -0.1115 -0.0308 -0.0910 175 GLN   A C   
1380 O O   . GLN   A 179 ? 0.6722 0.7220 0.6842 -0.1228 -0.0275 -0.0931 175 GLN   A O   
1381 C CB  . GLN   A 179 ? 0.6455 0.7285 0.6603 -0.0987 -0.0445 -0.0971 175 GLN   A CB  
1382 C CG  . GLN   A 179 ? 0.7538 0.8668 0.7820 -0.1146 -0.0454 -0.1071 175 GLN   A CG  
1383 C CD  . GLN   A 179 ? 0.7139 0.8568 0.7636 -0.1086 -0.0462 -0.1038 175 GLN   A CD  
1384 O OE1 . GLN   A 179 ? 0.7852 0.9317 0.8415 -0.1201 -0.0400 -0.1056 175 GLN   A OE1 
1385 N NE2 . GLN   A 179 ? 0.7614 0.9238 0.8200 -0.0907 -0.0537 -0.0991 175 GLN   A NE2 
1386 N N   . GLU   A 180 ? 0.5080 0.5056 0.4888 -0.1139 -0.0284 -0.0920 176 GLU   A N   
1387 C CA  . GLU   A 180 ? 0.5906 0.5573 0.5553 -0.1306 -0.0223 -0.0947 176 GLU   A CA  
1388 C C   . GLU   A 180 ? 0.7542 0.7083 0.7196 -0.1286 -0.0173 -0.0855 176 GLU   A C   
1389 O O   . GLU   A 180 ? 0.7885 0.7279 0.7449 -0.1455 -0.0118 -0.0871 176 GLU   A O   
1390 C CB  . GLU   A 180 ? 0.6607 0.5855 0.6000 -0.1292 -0.0222 -0.0975 176 GLU   A CB  
1391 C CG  . GLU   A 180 ? 0.7311 0.6563 0.6613 -0.1422 -0.0245 -0.1097 176 GLU   A CG  
1392 C CD  . GLU   A 180 ? 1.0600 1.0037 0.9951 -0.1284 -0.0306 -0.1122 176 GLU   A CD  
1393 O OE1 . GLU   A 180 ? 1.0028 0.9750 0.9551 -0.1143 -0.0337 -0.1059 176 GLU   A OE1 
1394 O OE2 . GLU   A 180 ? 1.1667 1.0943 1.0861 -0.1319 -0.0322 -0.1204 176 GLU   A OE2 
1395 N N   . GLY   A 181 ? 0.6370 0.5960 0.6112 -0.1097 -0.0188 -0.0762 177 GLY   A N   
1396 C CA  . GLY   A 181 ? 0.7177 0.6625 0.6906 -0.1057 -0.0149 -0.0675 177 GLY   A CA  
1397 C C   . GLY   A 181 ? 0.6819 0.6580 0.6748 -0.1079 -0.0131 -0.0651 177 GLY   A C   
1398 O O   . GLY   A 181 ? 0.7227 0.6905 0.7161 -0.1021 -0.0105 -0.0575 177 GLY   A O   
1399 N N   . LEU   A 182 ? 0.5802 0.5929 0.5895 -0.1153 -0.0148 -0.0722 178 LEU   A N   
1400 C CA  . LEU   A 182 ? 0.5964 0.6412 0.6257 -0.1155 -0.0135 -0.0717 178 LEU   A CA  
1401 C C   . LEU   A 182 ? 0.6345 0.6705 0.6579 -0.1335 -0.0051 -0.0731 178 LEU   A C   
1402 O O   . LEU   A 182 ? 0.5282 0.5829 0.5645 -0.1321 -0.0023 -0.0711 178 LEU   A O   
1403 C CB  . LEU   A 182 ? 0.5059 0.5944 0.5545 -0.1166 -0.0188 -0.0804 178 LEU   A CB  
1404 C CG  . LEU   A 182 ? 0.6111 0.7204 0.6725 -0.0953 -0.0268 -0.0761 178 LEU   A CG  
1405 C CD1 . LEU   A 182 ? 0.6239 0.7406 0.6963 -0.0840 -0.0255 -0.0687 178 LEU   A CD1 
1406 C CD2 . LEU   A 182 ? 0.6324 0.7176 0.6797 -0.0838 -0.0303 -0.0708 178 LEU   A CD2 
1407 N N   . ASN   A 183 ? 0.6231 0.6292 0.6254 -0.1508 -0.0009 -0.0766 179 ASN   A N   
1408 C CA  . ASN   A 183 ? 0.7389 0.7300 0.7296 -0.1698 0.0077  -0.0768 179 ASN   A CA  
1409 C C   . ASN   A 183 ? 0.8029 0.7667 0.7831 -0.1596 0.0102  -0.0652 179 ASN   A C   
1410 O O   . ASN   A 183 ? 0.7573 0.7148 0.7307 -0.1725 0.0172  -0.0639 179 ASN   A O   
1411 C CB  . ASN   A 183 ? 0.7411 0.6981 0.7057 -0.1905 0.0111  -0.0823 179 ASN   A CB  
1412 C CG  . ASN   A 183 ? 0.9491 0.8567 0.8885 -0.1791 0.0076  -0.0765 179 ASN   A CG  
1413 O OD1 . ASN   A 183 ? 0.9106 0.8208 0.8569 -0.1572 0.0014  -0.0724 179 ASN   A OD1 
1414 N ND2 . ASN   A 183 ? 0.9841 0.8461 0.8930 -0.1939 0.0116  -0.0766 179 ASN   A ND2 
1415 N N   . ALA   A 184 ? 0.7899 0.7391 0.7683 -0.1378 0.0048  -0.0575 180 ALA   A N   
1416 C CA  . ALA   A 184 ? 0.7252 0.6543 0.6966 -0.1266 0.0058  -0.0474 180 ALA   A CA  
1417 C C   . ALA   A 184 ? 0.7304 0.6927 0.7236 -0.1213 0.0074  -0.0451 180 ALA   A C   
1418 O O   . ALA   A 184 ? 0.6712 0.6201 0.6579 -0.1189 0.0103  -0.0386 180 ALA   A O   
1419 C CB  . ALA   A 184 ? 0.8088 0.7204 0.7757 -0.1054 -0.0004 -0.0418 180 ALA   A CB  
1420 N N   . ILE   A 185 ? 0.6836 0.6876 0.7008 -0.1183 0.0047  -0.0506 181 ILE   A N   
1421 C CA  . ILE   A 185 ? 0.6793 0.7143 0.7165 -0.1121 0.0057  -0.0499 181 ILE   A CA  
1422 C C   . ILE   A 185 ? 0.5415 0.5821 0.5764 -0.1310 0.0145  -0.0538 181 ILE   A C   
1423 O O   . ILE   A 185 ? 0.5494 0.5944 0.5799 -0.1509 0.0187  -0.0618 181 ILE   A O   
1424 C CB  . ILE   A 185 ? 0.5591 0.6351 0.6197 -0.1041 -0.0003 -0.0560 181 ILE   A CB  
1425 C CG1 . ILE   A 185 ? 0.5569 0.6253 0.6159 -0.0876 -0.0082 -0.0518 181 ILE   A CG1 
1426 C CG2 . ILE   A 185 ? 0.6171 0.7220 0.6967 -0.0953 -0.0002 -0.0559 181 ILE   A CG2 
1427 C CD1 . ILE   A 185 ? 0.7111 0.7625 0.7668 -0.0711 -0.0097 -0.0414 181 ILE   A CD1 
1428 N N   . GLN   A 186 ? 0.6316 0.6723 0.6683 -0.1262 0.0178  -0.0488 182 GLN   A N   
1429 C CA  . GLN   A 186 ? 0.7978 0.8484 0.8335 -0.1432 0.0270  -0.0527 182 GLN   A CA  
1430 C C   . GLN   A 186 ? 0.6461 0.7350 0.7064 -0.1323 0.0269  -0.0553 182 GLN   A C   
1431 O O   . GLN   A 186 ? 0.6274 0.7066 0.6865 -0.1195 0.0261  -0.0479 182 GLN   A O   
1432 C CB  . GLN   A 186 ? 0.7813 0.7880 0.7883 -0.1504 0.0321  -0.0444 182 GLN   A CB  
1433 C CG  . GLN   A 186 ? 0.8787 0.8599 0.8781 -0.1300 0.0267  -0.0333 182 GLN   A CG  
1434 C CD  . GLN   A 186 ? 0.7950 0.7260 0.7616 -0.1349 0.0279  -0.0260 182 GLN   A CD  
1435 O OE1 . GLN   A 186 ? 0.7273 0.6367 0.6736 -0.1538 0.0326  -0.0284 182 GLN   A OE1 
1436 N NE2 . GLN   A 186 ? 0.9382 0.8496 0.8983 -0.1180 0.0232  -0.0175 182 GLN   A NE2 
1437 N N   . PRO   A 187 ? 0.7181 0.8508 0.8008 -0.1361 0.0269  -0.0664 183 PRO   A N   
1438 C CA  . PRO   A 187 ? 0.5953 0.7646 0.7019 -0.1219 0.0249  -0.0701 183 PRO   A CA  
1439 C C   . PRO   A 187 ? 0.6167 0.7966 0.7238 -0.1325 0.0350  -0.0734 183 PRO   A C   
1440 O O   . PRO   A 187 ? 0.6387 0.8046 0.7295 -0.1547 0.0441  -0.0746 183 PRO   A O   
1441 C CB  . PRO   A 187 ? 0.6843 0.8965 0.8129 -0.1222 0.0202  -0.0824 183 PRO   A CB  
1442 C CG  . PRO   A 187 ? 0.7411 0.9340 0.8569 -0.1309 0.0172  -0.0820 183 PRO   A CG  
1443 C CD  . PRO   A 187 ? 0.5998 0.7500 0.6881 -0.1478 0.0252  -0.0760 183 PRO   A CD  
1444 N N   . PRO   A 188 ? 0.6753 0.8780 0.7986 -0.1177 0.0339  -0.0750 184 PRO   A N   
1445 C CA  . PRO   A 188 ? 0.6681 0.8807 0.8058 -0.0918 0.0234  -0.0724 184 PRO   A CA  
1446 C C   . PRO   A 188 ? 0.5793 0.7511 0.7008 -0.0789 0.0191  -0.0582 184 PRO   A C   
1447 O O   . PRO   A 188 ? 0.6299 0.7766 0.7359 -0.0837 0.0245  -0.0518 184 PRO   A O   
1448 C CB  . PRO   A 188 ? 0.5768 0.8228 0.7324 -0.0849 0.0263  -0.0802 184 PRO   A CB  
1449 C CG  . PRO   A 188 ? 0.6834 0.9213 0.8268 -0.1040 0.0388  -0.0809 184 PRO   A CG  
1450 C CD  . PRO   A 188 ? 0.6023 0.8241 0.7298 -0.1275 0.0440  -0.0811 184 PRO   A CD  
1451 N N   . CYS   A 189 ? 0.5616 0.7282 0.6859 -0.0633 0.0095  -0.0539 185 CYS   A N   
1452 C CA  . CYS   A 189 ? 0.5230 0.6544 0.6328 -0.0534 0.0059  -0.0419 185 CYS   A CA  
1453 C C   . CYS   A 189 ? 0.4957 0.6334 0.6142 -0.0338 -0.0034 -0.0392 185 CYS   A C   
1454 O O   . CYS   A 189 ? 0.4923 0.6581 0.6260 -0.0264 -0.0080 -0.0459 185 CYS   A O   
1455 C CB  . CYS   A 189 ? 0.6766 0.7812 0.7696 -0.0628 0.0061  -0.0383 185 CYS   A CB  
1456 S SG  . CYS   A 189 ? 0.5628 0.6826 0.6627 -0.0627 -0.0006 -0.0440 185 CYS   A SG  
1457 N N   . VAL   A 190 ? 0.4515 0.5623 0.5590 -0.0254 -0.0063 -0.0295 186 VAL   A N   
1458 C CA  . VAL   A 190 ? 0.4605 0.5695 0.5702 -0.0098 -0.0141 -0.0252 186 VAL   A CA  
1459 C C   . VAL   A 190 ? 0.4176 0.5087 0.5164 -0.0108 -0.0168 -0.0207 186 VAL   A C   
1460 O O   . VAL   A 190 ? 0.5454 0.6141 0.6324 -0.0160 -0.0135 -0.0163 186 VAL   A O   
1461 C CB  . VAL   A 190 ? 0.5816 0.6775 0.6883 -0.0001 -0.0143 -0.0190 186 VAL   A CB  
1462 C CG1 . VAL   A 190 ? 0.4053 0.4888 0.5068 0.0112  -0.0207 -0.0124 186 VAL   A CG1 
1463 C CG2 . VAL   A 190 ? 0.5405 0.6566 0.6590 0.0054  -0.0137 -0.0248 186 VAL   A CG2 
1464 N N   . VAL   A 191 ? 0.4078 0.5089 0.5097 -0.0051 -0.0232 -0.0223 187 VAL   A N   
1465 C CA  . VAL   A 191 ? 0.3684 0.4556 0.4602 -0.0053 -0.0257 -0.0191 187 VAL   A CA  
1466 C C   . VAL   A 191 ? 0.4112 0.4901 0.4987 0.0072  -0.0305 -0.0123 187 VAL   A C   
1467 O O   . VAL   A 191 ? 0.4150 0.5027 0.5075 0.0166  -0.0348 -0.0118 187 VAL   A O   
1468 C CB  . VAL   A 191 ? 0.3296 0.4327 0.4245 -0.0109 -0.0287 -0.0264 187 VAL   A CB  
1469 C CG1 . VAL   A 191 ? 0.4116 0.5135 0.5045 -0.0272 -0.0226 -0.0321 187 VAL   A CG1 
1470 C CG2 . VAL   A 191 ? 0.3529 0.4846 0.4613 -0.0037 -0.0346 -0.0321 187 VAL   A CG2 
1471 N N   . GLN   A 192 ? 0.4227 0.4837 0.4996 0.0071  -0.0297 -0.0076 188 GLN   A N   
1472 C CA  . GLN   A 192 ? 0.4268 0.4781 0.4974 0.0153  -0.0321 -0.0010 188 GLN   A CA  
1473 C C   . GLN   A 192 ? 0.4218 0.4649 0.4830 0.0136  -0.0321 -0.0001 188 GLN   A C   
1474 O O   . GLN   A 192 ? 0.3425 0.3779 0.4003 0.0081  -0.0287 -0.0023 188 GLN   A O   
1475 C CB  . GLN   A 192 ? 0.3672 0.4065 0.4368 0.0169  -0.0285 0.0038  188 GLN   A CB  
1476 C CG  . GLN   A 192 ? 0.3055 0.3362 0.3691 0.0232  -0.0304 0.0098  188 GLN   A CG  
1477 C CD  . GLN   A 192 ? 0.4839 0.5038 0.5462 0.0226  -0.0266 0.0133  188 GLN   A CD  
1478 O OE1 . GLN   A 192 ? 0.4033 0.4180 0.4645 0.0188  -0.0233 0.0126  188 GLN   A OE1 
1479 N NE2 . GLN   A 192 ? 0.3837 0.3989 0.4447 0.0267  -0.0278 0.0166  188 GLN   A NE2 
1480 N N   . ASN   A 193 ? 0.3618 0.4050 0.4168 0.0188  -0.0360 0.0028  189 ASN   A N   
1481 C CA  . ASN   A 193 ? 0.4578 0.4957 0.5032 0.0172  -0.0355 0.0029  189 ASN   A CA  
1482 C C   . ASN   A 193 ? 0.4347 0.4611 0.4771 0.0159  -0.0301 0.0049  189 ASN   A C   
1483 O O   . ASN   A 193 ? 0.3626 0.3840 0.4058 0.0180  -0.0284 0.0093  189 ASN   A O   
1484 C CB  . ASN   A 193 ? 0.4529 0.4907 0.4889 0.0221  -0.0401 0.0069  189 ASN   A CB  
1485 C CG  . ASN   A 193 ? 0.5303 0.5794 0.5644 0.0230  -0.0462 0.0027  189 ASN   A CG  
1486 O OD1 . ASN   A 193 ? 0.4375 0.4973 0.4795 0.0190  -0.0468 -0.0039 189 ASN   A OD1 
1487 N ND2 . ASN   A 193 ? 0.5287 0.5751 0.5506 0.0275  -0.0510 0.0065  189 ASN   A ND2 
1488 N N   . PHE   A 194 ? 0.4486 0.4713 0.4874 0.0129  -0.0279 0.0008  190 PHE   A N   
1489 C CA  . PHE   A 194 ? 0.4232 0.4378 0.4596 0.0141  -0.0240 0.0010  190 PHE   A CA  
1490 C C   . PHE   A 194 ? 0.4262 0.4437 0.4566 0.0159  -0.0228 0.0029  190 PHE   A C   
1491 O O   . PHE   A 194 ? 0.4255 0.4467 0.4491 0.0151  -0.0242 0.0013  190 PHE   A O   
1492 C CB  . PHE   A 194 ? 0.4357 0.4425 0.4683 0.0121  -0.0228 -0.0050 190 PHE   A CB  
1493 C CG  . PHE   A 194 ? 0.4934 0.4936 0.5233 0.0164  -0.0202 -0.0064 190 PHE   A CG  
1494 C CD1 . PHE   A 194 ? 0.4359 0.4286 0.4683 0.0189  -0.0192 -0.0048 190 PHE   A CD1 
1495 C CD2 . PHE   A 194 ? 0.4732 0.4763 0.4979 0.0186  -0.0190 -0.0104 190 PHE   A CD2 
1496 C CE1 . PHE   A 194 ? 0.4413 0.4309 0.4723 0.0249  -0.0182 -0.0072 190 PHE   A CE1 
1497 C CE2 . PHE   A 194 ? 0.5434 0.5446 0.5676 0.0242  -0.0169 -0.0135 190 PHE   A CE2 
1498 C CZ  . PHE   A 194 ? 0.3933 0.3883 0.4213 0.0280  -0.0171 -0.0121 190 PHE   A CZ  
1499 N N   . ILE   A 195 ? 0.4145 0.4309 0.4466 0.0173  -0.0201 0.0059  191 ILE   A N   
1500 C CA  . ILE   A 195 ? 0.4425 0.4629 0.4687 0.0162  -0.0175 0.0076  191 ILE   A CA  
1501 C C   . ILE   A 195 ? 0.4254 0.4498 0.4540 0.0179  -0.0135 0.0024  191 ILE   A C   
1502 O O   . ILE   A 195 ? 0.4347 0.4576 0.4701 0.0205  -0.0129 0.0015  191 ILE   A O   
1503 C CB  . ILE   A 195 ? 0.3825 0.4002 0.4081 0.0149  -0.0172 0.0140  191 ILE   A CB  
1504 C CG1 . ILE   A 195 ? 0.4348 0.4480 0.4579 0.0164  -0.0223 0.0181  191 ILE   A CG1 
1505 C CG2 . ILE   A 195 ? 0.4719 0.4925 0.4889 0.0106  -0.0134 0.0156  191 ILE   A CG2 
1506 C CD1 . ILE   A 195 ? 0.5089 0.5226 0.5210 0.0164  -0.0256 0.0189  191 ILE   A CD1 
1507 N N   . ASN   A 196 ? 0.4148 0.4450 0.4373 0.0172  -0.0112 -0.0017 192 ASN   A N   
1508 C CA  . ASN   A 196 ? 0.4528 0.4912 0.4783 0.0201  -0.0072 -0.0080 192 ASN   A CA  
1509 C C   . ASN   A 196 ? 0.4283 0.4757 0.4581 0.0173  -0.0036 -0.0056 192 ASN   A C   
1510 O O   . ASN   A 196 ? 0.3839 0.4322 0.4071 0.0106  -0.0018 -0.0005 192 ASN   A O   
1511 C CB  . ASN   A 196 ? 0.4172 0.4622 0.4346 0.0193  -0.0047 -0.0137 192 ASN   A CB  
1512 C CG  . ASN   A 196 ? 0.4639 0.5004 0.4778 0.0227  -0.0077 -0.0192 192 ASN   A CG  
1513 O OD1 . ASN   A 196 ? 0.4519 0.4784 0.4697 0.0266  -0.0103 -0.0210 192 ASN   A OD1 
1514 N ND2 . ASN   A 196 ? 0.4249 0.4639 0.4291 0.0201  -0.0074 -0.0220 192 ASN   A ND2 
1515 N N   . HIS   A 197 ? 0.3981 0.4507 0.4374 0.0221  -0.0031 -0.0094 193 HIS   A N   
1516 C CA  . HIS   A 197 ? 0.4345 0.4977 0.4798 0.0185  -0.0002 -0.0082 193 HIS   A CA  
1517 C C   . HIS   A 197 ? 0.3792 0.4589 0.4341 0.0246  0.0015  -0.0171 193 HIS   A C   
1518 O O   . HIS   A 197 ? 0.3773 0.4663 0.4402 0.0236  0.0020  -0.0175 193 HIS   A O   
1519 C CB  . HIS   A 197 ? 0.3283 0.3806 0.3766 0.0177  -0.0036 -0.0016 193 HIS   A CB  
1520 C CG  . HIS   A 197 ? 0.3285 0.3709 0.3808 0.0253  -0.0081 -0.0028 193 HIS   A CG  
1521 N ND1 . HIS   A 197 ? 0.3468 0.3765 0.3944 0.0270  -0.0109 -0.0020 193 HIS   A ND1 
1522 C CD2 . HIS   A 197 ? 0.3496 0.3921 0.4080 0.0307  -0.0102 -0.0047 193 HIS   A CD2 
1523 C CE1 . HIS   A 197 ? 0.4012 0.4214 0.4503 0.0318  -0.0137 -0.0029 193 HIS   A CE1 
1524 N NE2 . HIS   A 197 ? 0.4262 0.4530 0.4810 0.0350  -0.0138 -0.0041 193 HIS   A NE2 
1525 N N   . ASN   A 198 ? 0.2734 0.3576 0.3279 0.0316  0.0018  -0.0251 194 ASN   A N   
1526 C CA  . ASN   A 198 ? 0.3182 0.4203 0.3820 0.0404  0.0027  -0.0355 194 ASN   A CA  
1527 C C   . ASN   A 198 ? 0.3735 0.4704 0.4444 0.0496  -0.0032 -0.0359 194 ASN   A C   
1528 O O   . ASN   A 198 ? 0.3700 0.4858 0.4512 0.0555  -0.0034 -0.0429 194 ASN   A O   
1529 C CB  . ASN   A 198 ? 0.2719 0.4014 0.3413 0.0325  0.0099  -0.0397 194 ASN   A CB  
1530 C CG  . ASN   A 198 ? 0.3436 0.4796 0.4035 0.0254  0.0161  -0.0417 194 ASN   A CG  
1531 O OD1 . ASN   A 198 ? 0.3257 0.4606 0.3818 0.0323  0.0158  -0.0481 194 ASN   A OD1 
1532 N ND2 . ASN   A 198 ? 0.4217 0.5618 0.4749 0.0111  0.0215  -0.0361 194 ASN   A ND2 
1533 N N   . ALA   A 199 ? 0.3013 0.3740 0.3664 0.0506  -0.0081 -0.0290 195 ALA   A N   
1534 C CA  . ALA   A 199 ? 0.3687 0.4296 0.4347 0.0597  -0.0142 -0.0290 195 ALA   A CA  
1535 C C   . ALA   A 199 ? 0.3519 0.4275 0.4279 0.0593  -0.0149 -0.0286 195 ALA   A C   
1536 O O   . ALA   A 199 ? 0.3984 0.4769 0.4781 0.0699  -0.0197 -0.0331 195 ALA   A O   
1537 C CB  . ALA   A 199 ? 0.3456 0.4015 0.4085 0.0739  -0.0178 -0.0378 195 ALA   A CB  
1538 N N   . VAL   A 200 ? 0.3342 0.4177 0.4129 0.0473  -0.0108 -0.0234 196 VAL   A N   
1539 C CA  . VAL   A 200 ? 0.4326 0.5278 0.5192 0.0440  -0.0111 -0.0228 196 VAL   A CA  
1540 C C   . VAL   A 200 ? 0.4972 0.5757 0.5784 0.0351  -0.0112 -0.0129 196 VAL   A C   
1541 O O   . VAL   A 200 ? 0.3551 0.4286 0.4306 0.0263  -0.0076 -0.0080 196 VAL   A O   
1542 C CB  . VAL   A 200 ? 0.4250 0.5492 0.5201 0.0367  -0.0051 -0.0286 196 VAL   A CB  
1543 C CG1 . VAL   A 200 ? 0.4185 0.5537 0.5209 0.0312  -0.0056 -0.0283 196 VAL   A CG1 
1544 C CG2 . VAL   A 200 ? 0.4716 0.6169 0.5742 0.0470  -0.0048 -0.0405 196 VAL   A CG2 
1545 N N   . LEU   A 201 ? 0.3394 0.4088 0.4208 0.0384  -0.0156 -0.0103 197 LEU   A N   
1546 C CA  . LEU   A 201 ? 0.3164 0.3718 0.3936 0.0317  -0.0158 -0.0026 197 LEU   A CA  
1547 C C   . LEU   A 201 ? 0.4011 0.4674 0.4840 0.0270  -0.0157 -0.0034 197 LEU   A C   
1548 O O   . LEU   A 201 ? 0.4019 0.4784 0.4906 0.0332  -0.0192 -0.0082 197 LEU   A O   
1549 C CB  . LEU   A 201 ? 0.4122 0.4474 0.4830 0.0371  -0.0200 0.0007  197 LEU   A CB  
1550 C CG  . LEU   A 201 ? 0.4642 0.4887 0.5323 0.0323  -0.0204 0.0064  197 LEU   A CG  
1551 C CD1 . LEU   A 201 ? 0.4771 0.4960 0.5424 0.0254  -0.0174 0.0109  197 LEU   A CD1 
1552 C CD2 . LEU   A 201 ? 0.4793 0.4876 0.5405 0.0370  -0.0239 0.0080  197 LEU   A CD2 
1553 N N   . TYR   A 202 ? 0.3422 0.4052 0.4222 0.0166  -0.0123 0.0009  198 TYR   A N   
1554 C CA  . TYR   A 202 ? 0.3368 0.4066 0.4198 0.0094  -0.0116 0.0003  198 TYR   A CA  
1555 C C   . TYR   A 202 ? 0.4424 0.4932 0.5199 0.0094  -0.0143 0.0057  198 TYR   A C   
1556 O O   . TYR   A 202 ? 0.4153 0.4513 0.4855 0.0054  -0.0128 0.0111  198 TYR   A O   
1557 C CB  . TYR   A 202 ? 0.3330 0.4083 0.4127 -0.0034 -0.0057 0.0009  198 TYR   A CB  
1558 C CG  . TYR   A 202 ? 0.3907 0.4870 0.4751 -0.0050 -0.0015 -0.0052 198 TYR   A CG  
1559 C CD1 . TYR   A 202 ? 0.3035 0.4274 0.3998 -0.0057 -0.0005 -0.0141 198 TYR   A CD1 
1560 C CD2 . TYR   A 202 ? 0.3058 0.3968 0.3832 -0.0056 0.0013  -0.0031 198 TYR   A CD2 
1561 C CE1 . TYR   A 202 ? 0.4018 0.5484 0.5036 -0.0069 0.0041  -0.0213 198 TYR   A CE1 
1562 C CE2 . TYR   A 202 ? 0.3988 0.5097 0.4795 -0.0073 0.0058  -0.0094 198 TYR   A CE2 
1563 C CZ  . TYR   A 202 ? 0.3936 0.5329 0.4870 -0.0079 0.0077  -0.0188 198 TYR   A CZ  
1564 O OH  . TYR   A 202 ? 0.5281 0.6905 0.6259 -0.0093 0.0129  -0.0267 198 TYR   A OH  
1565 N N   . LYS   A 203 ? 0.3916 0.4433 0.4716 0.0149  -0.0185 0.0038  199 LYS   A N   
1566 C CA  . LYS   A 203 ? 0.4562 0.4924 0.5308 0.0147  -0.0205 0.0077  199 LYS   A CA  
1567 C C   . LYS   A 203 ? 0.4861 0.5258 0.5612 0.0062  -0.0196 0.0066  199 LYS   A C   
1568 O O   . LYS   A 203 ? 0.4393 0.4949 0.5205 0.0054  -0.0214 0.0013  199 LYS   A O   
1569 C CB  . LYS   A 203 ? 0.5322 0.5641 0.6049 0.0239  -0.0255 0.0067  199 LYS   A CB  
1570 C CG  . LYS   A 203 ? 0.6608 0.6806 0.7282 0.0297  -0.0261 0.0089  199 LYS   A CG  
1571 C CD  . LYS   A 203 ? 0.5758 0.5865 0.6365 0.0377  -0.0311 0.0085  199 LYS   A CD  
1572 C CE  . LYS   A 203 ? 0.6863 0.6837 0.7393 0.0348  -0.0313 0.0122  199 LYS   A CE  
1573 N NZ  . LYS   A 203 ? 0.5459 0.5327 0.5957 0.0301  -0.0270 0.0158  199 LYS   A NZ  
1574 N N   . VAL   A 204 ? 0.4335 0.4584 0.5017 0.0003  -0.0173 0.0108  200 VAL   A N   
1575 C CA  . VAL   A 204 ? 0.4219 0.4435 0.4867 -0.0088 -0.0161 0.0100  200 VAL   A CA  
1576 C C   . VAL   A 204 ? 0.4868 0.4974 0.5480 -0.0054 -0.0190 0.0105  200 VAL   A C   
1577 O O   . VAL   A 204 ? 0.4761 0.4718 0.5320 -0.0017 -0.0188 0.0140  200 VAL   A O   
1578 C CB  . VAL   A 204 ? 0.4904 0.4978 0.5459 -0.0164 -0.0125 0.0140  200 VAL   A CB  
1579 C CG1 . VAL   A 204 ? 0.4516 0.4485 0.4998 -0.0259 -0.0117 0.0134  200 VAL   A CG1 
1580 C CG2 . VAL   A 204 ? 0.4130 0.4320 0.4697 -0.0217 -0.0089 0.0133  200 VAL   A CG2 
1581 N N   . PHE   A 205 ? 0.3654 0.3854 0.4296 -0.0067 -0.0216 0.0062  201 PHE   A N   
1582 C CA  . PHE   A 205 ? 0.4021 0.4129 0.4612 -0.0045 -0.0242 0.0059  201 PHE   A CA  
1583 C C   . PHE   A 205 ? 0.4820 0.4848 0.5356 -0.0142 -0.0227 0.0043  201 PHE   A C   
1584 O O   . PHE   A 205 ? 0.4002 0.4149 0.4571 -0.0227 -0.0225 0.0001  201 PHE   A O   
1585 C CB  . PHE   A 205 ? 0.3711 0.3947 0.4337 0.0014  -0.0295 0.0022  201 PHE   A CB  
1586 C CG  . PHE   A 205 ? 0.4373 0.4591 0.4992 0.0118  -0.0317 0.0044  201 PHE   A CG  
1587 C CD1 . PHE   A 205 ? 0.4697 0.4756 0.5228 0.0158  -0.0319 0.0080  201 PHE   A CD1 
1588 C CD2 . PHE   A 205 ? 0.3971 0.4323 0.4658 0.0168  -0.0333 0.0022  201 PHE   A CD2 
1589 C CE1 . PHE   A 205 ? 0.5042 0.5047 0.5535 0.0230  -0.0335 0.0101  201 PHE   A CE1 
1590 C CE2 . PHE   A 205 ? 0.4508 0.4794 0.5158 0.0261  -0.0357 0.0040  201 PHE   A CE2 
1591 C CZ  . PHE   A 205 ? 0.5084 0.5181 0.5627 0.0284  -0.0358 0.0083  201 PHE   A CZ  
1592 N N   . VAL   A 206 ? 0.4878 0.4711 0.5329 -0.0132 -0.0217 0.0067  202 VAL   A N   
1593 C CA  . VAL   A 206 ? 0.4797 0.4485 0.5162 -0.0210 -0.0204 0.0053  202 VAL   A CA  
1594 C C   . VAL   A 206 ? 0.4589 0.4234 0.4913 -0.0191 -0.0227 0.0020  202 VAL   A C   
1595 O O   . VAL   A 206 ? 0.5292 0.4899 0.5603 -0.0110 -0.0232 0.0031  202 VAL   A O   
1596 C CB  . VAL   A 206 ? 0.5004 0.4482 0.5284 -0.0194 -0.0183 0.0096  202 VAL   A CB  
1597 C CG1 . VAL   A 206 ? 0.5334 0.4608 0.5489 -0.0267 -0.0177 0.0080  202 VAL   A CG1 
1598 C CG2 . VAL   A 206 ? 0.4396 0.3912 0.4693 -0.0211 -0.0164 0.0133  202 VAL   A CG2 
1599 N N   . VAL   A 207 ? 0.4546 0.4206 0.4843 -0.0281 -0.0236 -0.0027 203 VAL   A N   
1600 C CA  . VAL   A 207 ? 0.5399 0.4998 0.5631 -0.0280 -0.0257 -0.0067 203 VAL   A CA  
1601 C C   . VAL   A 207 ? 0.5881 0.5300 0.6009 -0.0385 -0.0239 -0.0094 203 VAL   A C   
1602 O O   . VAL   A 207 ? 0.5620 0.5112 0.5751 -0.0502 -0.0243 -0.0137 203 VAL   A O   
1603 C CB  . VAL   A 207 ? 0.5414 0.5219 0.5700 -0.0282 -0.0303 -0.0112 203 VAL   A CB  
1604 C CG1 . VAL   A 207 ? 0.5334 0.5062 0.5528 -0.0290 -0.0325 -0.0155 203 VAL   A CG1 
1605 C CG2 . VAL   A 207 ? 0.4633 0.4552 0.4979 -0.0173 -0.0327 -0.0081 203 VAL   A CG2 
1606 N N   . GLY   A 208 ? 0.6018 0.5199 0.6047 -0.0343 -0.0221 -0.0075 204 GLY   A N   
1607 C CA  . GLY   A 208 ? 0.5674 0.4611 0.5565 -0.0425 -0.0210 -0.0094 204 GLY   A CA  
1608 C C   . GLY   A 208 ? 0.7411 0.6292 0.7265 -0.0527 -0.0187 -0.0061 204 GLY   A C   
1609 O O   . GLY   A 208 ? 0.6141 0.4988 0.6003 -0.0474 -0.0176 -0.0003 204 GLY   A O   
1610 N N   . GLU   A 209 ? 0.6735 0.5615 0.6541 -0.0687 -0.0177 -0.0100 205 GLU   A N   
1611 C CA  . GLU   A 209 ? 0.7855 0.6685 0.7603 -0.0821 -0.0142 -0.0075 205 GLU   A CA  
1612 C C   . GLU   A 209 ? 0.8089 0.7280 0.8014 -0.0863 -0.0128 -0.0084 205 GLU   A C   
1613 O O   . GLU   A 209 ? 0.9279 0.8483 0.9197 -0.0900 -0.0096 -0.0042 205 GLU   A O   
1614 C CB  . GLU   A 209 ? 1.0323 0.8962 0.9913 -0.1002 -0.0126 -0.0121 205 GLU   A CB  
1615 C CG  . GLU   A 209 ? 1.0881 0.9081 1.0244 -0.0966 -0.0136 -0.0107 205 GLU   A CG  
1616 C CD  . GLU   A 209 ? 1.4809 1.2775 1.3984 -0.1159 -0.0121 -0.0154 205 GLU   A CD  
1617 O OE1 . GLU   A 209 ? 1.5556 1.3751 1.4804 -0.1329 -0.0101 -0.0208 205 GLU   A OE1 
1618 O OE2 . GLU   A 209 ? 1.4843 1.2398 1.3795 -0.1140 -0.0131 -0.0145 205 GLU   A OE2 
1619 N N   . SER   A 210 ? 0.7054 0.6536 0.7125 -0.0849 -0.0157 -0.0142 206 SER   A N   
1620 C CA  . SER   A 210 ? 0.6539 0.6376 0.6785 -0.0854 -0.0157 -0.0165 206 SER   A CA  
1621 C C   . SER   A 210 ? 0.6354 0.6254 0.6683 -0.0687 -0.0168 -0.0109 206 SER   A C   
1622 O O   . SER   A 210 ? 0.6105 0.5885 0.6408 -0.0560 -0.0192 -0.0077 206 SER   A O   
1623 C CB  . SER   A 210 ? 0.6988 0.7106 0.7350 -0.0866 -0.0203 -0.0250 206 SER   A CB  
1624 O OG  . SER   A 210 ? 0.7205 0.7295 0.7572 -0.0716 -0.0254 -0.0241 206 SER   A OG  
1625 N N   . TYR   A 211 ? 0.5614 0.5711 0.6037 -0.0700 -0.0146 -0.0107 207 TYR   A N   
1626 C CA  . TYR   A 211 ? 0.4682 0.4837 0.5175 -0.0560 -0.0154 -0.0063 207 TYR   A CA  
1627 C C   . TYR   A 211 ? 0.4910 0.5406 0.5562 -0.0547 -0.0161 -0.0115 207 TYR   A C   
1628 O O   . TYR   A 211 ? 0.4519 0.5211 0.5226 -0.0669 -0.0137 -0.0176 207 TYR   A O   
1629 C CB  . TYR   A 211 ? 0.5400 0.5348 0.5793 -0.0564 -0.0116 0.0009  207 TYR   A CB  
1630 C CG  . TYR   A 211 ? 0.5068 0.5064 0.5426 -0.0710 -0.0061 0.0004  207 TYR   A CG  
1631 C CD1 . TYR   A 211 ? 0.6724 0.6566 0.6948 -0.0875 -0.0030 -0.0006 207 TYR   A CD1 
1632 C CD2 . TYR   A 211 ? 0.5430 0.5611 0.5868 -0.0694 -0.0036 0.0005  207 TYR   A CD2 
1633 C CE1 . TYR   A 211 ? 0.7767 0.7640 0.7930 -0.1035 0.0031  -0.0009 207 TYR   A CE1 
1634 C CE2 . TYR   A 211 ? 0.5725 0.5963 0.6118 -0.0841 0.0024  -0.0003 207 TYR   A CE2 
1635 C CZ  . TYR   A 211 ? 0.6948 0.7032 0.7199 -0.1019 0.0061  -0.0008 207 TYR   A CZ  
1636 O OH  . TYR   A 211 ? 0.7658 0.7785 0.7836 -0.1190 0.0131  -0.0014 207 TYR   A OH  
1637 N N   . THR   A 212 ? 0.4603 0.5170 0.5324 -0.0400 -0.0191 -0.0098 208 THR   A N   
1638 C CA  . THR   A 212 ? 0.5470 0.6331 0.6330 -0.0343 -0.0210 -0.0151 208 THR   A CA  
1639 C C   . THR   A 212 ? 0.4791 0.5610 0.5655 -0.0258 -0.0192 -0.0105 208 THR   A C   
1640 O O   . THR   A 212 ? 0.5068 0.5697 0.5870 -0.0168 -0.0207 -0.0047 208 THR   A O   
1641 C CB  . THR   A 212 ? 0.6088 0.7063 0.7003 -0.0228 -0.0289 -0.0190 208 THR   A CB  
1642 O OG1 . THR   A 212 ? 0.6514 0.7465 0.7389 -0.0299 -0.0311 -0.0221 208 THR   A OG1 
1643 C CG2 . THR   A 212 ? 0.5927 0.7237 0.6990 -0.0173 -0.0319 -0.0271 208 THR   A CG2 
1644 N N   . VAL   A 213 ? 0.4004 0.5016 0.4940 -0.0296 -0.0155 -0.0141 209 VAL   A N   
1645 C CA  . VAL   A 213 ? 0.4107 0.5111 0.5050 -0.0224 -0.0137 -0.0114 209 VAL   A CA  
1646 C C   . VAL   A 213 ? 0.5259 0.6479 0.6319 -0.0089 -0.0186 -0.0177 209 VAL   A C   
1647 O O   . VAL   A 213 ? 0.4785 0.6299 0.5963 -0.0104 -0.0189 -0.0265 209 VAL   A O   
1648 C CB  . VAL   A 213 ? 0.4762 0.5817 0.5678 -0.0350 -0.0061 -0.0114 209 VAL   A CB  
1649 C CG1 . VAL   A 213 ? 0.4069 0.5071 0.4961 -0.0275 -0.0046 -0.0080 209 VAL   A CG1 
1650 C CG2 . VAL   A 213 ? 0.3271 0.4084 0.4039 -0.0486 -0.0026 -0.0059 209 VAL   A CG2 
1651 N N   . VAL   A 214 ? 0.4529 0.5604 0.5549 0.0044  -0.0225 -0.0138 210 VAL   A N   
1652 C CA  . VAL   A 214 ? 0.4926 0.6112 0.6002 0.0192  -0.0284 -0.0186 210 VAL   A CA  
1653 C C   . VAL   A 214 ? 0.4902 0.6045 0.5965 0.0249  -0.0259 -0.0174 210 VAL   A C   
1654 O O   . VAL   A 214 ? 0.5119 0.6038 0.6089 0.0239  -0.0239 -0.0103 210 VAL   A O   
1655 C CB  . VAL   A 214 ? 0.6181 0.7191 0.7177 0.0290  -0.0355 -0.0153 210 VAL   A CB  
1656 C CG1 . VAL   A 214 ? 0.5396 0.6432 0.6394 0.0453  -0.0421 -0.0187 210 VAL   A CG1 
1657 C CG2 . VAL   A 214 ? 0.4588 0.5671 0.5598 0.0242  -0.0386 -0.0180 210 VAL   A CG2 
1658 N N   . GLN   A 215 ? 0.4384 0.5760 0.5543 0.0309  -0.0263 -0.0256 211 GLN   A N   
1659 C CA  . GLN   A 215 ? 0.5348 0.6705 0.6494 0.0367  -0.0240 -0.0264 211 GLN   A CA  
1660 C C   . GLN   A 215 ? 0.4752 0.5960 0.5841 0.0534  -0.0314 -0.0265 211 GLN   A C   
1661 O O   . GLN   A 215 ? 0.5998 0.7299 0.7124 0.0648  -0.0384 -0.0320 211 GLN   A O   
1662 C CB  . GLN   A 215 ? 0.4546 0.6237 0.5816 0.0346  -0.0198 -0.0365 211 GLN   A CB  
1663 C CG  . GLN   A 215 ? 0.5040 0.6752 0.6307 0.0432  -0.0184 -0.0402 211 GLN   A CG  
1664 C CD  . GLN   A 215 ? 0.6666 0.8699 0.8034 0.0359  -0.0109 -0.0489 211 GLN   A CD  
1665 O OE1 . GLN   A 215 ? 0.6213 0.8427 0.7636 0.0217  -0.0059 -0.0511 211 GLN   A OE1 
1666 N NE2 . GLN   A 215 ? 0.6800 0.8899 0.8178 0.0445  -0.0096 -0.0546 211 GLN   A NE2 
1667 N N   . ARG   A 216 ? 0.5212 0.6178 0.6193 0.0547  -0.0303 -0.0205 212 ARG   A N   
1668 C CA  . ARG   A 216 ? 0.4382 0.5122 0.5256 0.0665  -0.0361 -0.0187 212 ARG   A CA  
1669 C C   . ARG   A 216 ? 0.4605 0.5279 0.5441 0.0708  -0.0342 -0.0206 212 ARG   A C   
1670 O O   . ARG   A 216 ? 0.4352 0.5105 0.5220 0.0627  -0.0279 -0.0206 212 ARG   A O   
1671 C CB  . ARG   A 216 ? 0.4603 0.5080 0.5362 0.0610  -0.0364 -0.0095 212 ARG   A CB  
1672 C CG  . ARG   A 216 ? 0.4746 0.5249 0.5514 0.0578  -0.0388 -0.0078 212 ARG   A CG  
1673 C CD  . ARG   A 216 ? 0.6080 0.6562 0.6803 0.0704  -0.0475 -0.0109 212 ARG   A CD  
1674 N NE  . ARG   A 216 ? 0.7544 0.7990 0.8230 0.0673  -0.0503 -0.0083 212 ARG   A NE  
1675 C CZ  . ARG   A 216 ? 0.7199 0.7405 0.7749 0.0644  -0.0504 -0.0016 212 ARG   A CZ  
1676 N NH1 . ARG   A 216 ? 0.6661 0.6654 0.7109 0.0632  -0.0477 0.0031  212 ARG   A NH1 
1677 N NH2 . ARG   A 216 ? 0.7536 0.7732 0.8052 0.0617  -0.0527 -0.0003 212 ARG   A NH2 
1678 N N   . PRO   A 217 ? 0.4574 0.5078 0.5315 0.0833  -0.0399 -0.0223 213 PRO   A N   
1679 C CA  . PRO   A 217 ? 0.4490 0.4875 0.5163 0.0863  -0.0382 -0.0239 213 PRO   A CA  
1680 C C   . PRO   A 217 ? 0.4207 0.4392 0.4794 0.0747  -0.0340 -0.0158 213 PRO   A C   
1681 O O   . PRO   A 217 ? 0.3896 0.3972 0.4444 0.0680  -0.0338 -0.0090 213 PRO   A O   
1682 C CB  . PRO   A 217 ? 0.4958 0.5146 0.5512 0.1021  -0.0465 -0.0269 213 PRO   A CB  
1683 C CG  . PRO   A 217 ? 0.5814 0.6121 0.6417 0.1101  -0.0529 -0.0293 213 PRO   A CG  
1684 C CD  . PRO   A 217 ? 0.4671 0.5076 0.5344 0.0959  -0.0488 -0.0235 213 PRO   A CD  
1685 N N   . SER   A 218 ? 0.3918 0.4077 0.4480 0.0730  -0.0307 -0.0176 214 SER   A N   
1686 C CA  . SER   A 218 ? 0.3205 0.3233 0.3707 0.0625  -0.0272 -0.0118 214 SER   A CA  
1687 C C   . SER   A 218 ? 0.4835 0.4758 0.5259 0.0652  -0.0269 -0.0157 214 SER   A C   
1688 O O   . SER   A 218 ? 0.5252 0.5170 0.5654 0.0758  -0.0295 -0.0227 214 SER   A O   
1689 C CB  . SER   A 218 ? 0.3833 0.4026 0.4418 0.0519  -0.0220 -0.0086 214 SER   A CB  
1690 O OG  . SER   A 218 ? 0.4507 0.4591 0.5042 0.0441  -0.0202 -0.0035 214 SER   A OG  
1691 N N   . LEU   A 219 ? 0.4096 0.3939 0.4477 0.0560  -0.0243 -0.0121 215 LEU   A N   
1692 C CA  . LEU   A 219 ? 0.4894 0.4629 0.5191 0.0561  -0.0240 -0.0160 215 LEU   A CA  
1693 C C   . LEU   A 219 ? 0.3699 0.3621 0.4049 0.0585  -0.0211 -0.0222 215 LEU   A C   
1694 O O   . LEU   A 219 ? 0.3616 0.3732 0.4046 0.0532  -0.0175 -0.0206 215 LEU   A O   
1695 C CB  . LEU   A 219 ? 0.4020 0.3678 0.4279 0.0449  -0.0223 -0.0115 215 LEU   A CB  
1696 C CG  . LEU   A 219 ? 0.4374 0.3865 0.4574 0.0398  -0.0234 -0.0066 215 LEU   A CG  
1697 C CD1 . LEU   A 219 ? 0.5471 0.4989 0.5684 0.0291  -0.0212 -0.0044 215 LEU   A CD1 
1698 C CD2 . LEU   A 219 ? 0.5103 0.4331 0.5150 0.0440  -0.0264 -0.0090 215 LEU   A CD2 
1699 N N   . LYS   A 220 ? 0.3701 0.3542 0.3980 0.0659  -0.0225 -0.0294 216 LYS   A N   
1700 C CA  . LYS   A 220 ? 0.4495 0.4515 0.4810 0.0687  -0.0192 -0.0369 216 LYS   A CA  
1701 C C   . LYS   A 220 ? 0.4627 0.4683 0.4913 0.0576  -0.0156 -0.0345 216 LYS   A C   
1702 O O   . LYS   A 220 ? 0.3593 0.3555 0.3850 0.0492  -0.0163 -0.0280 216 LYS   A O   
1703 C CB  . LYS   A 220 ? 0.3717 0.3615 0.3950 0.0813  -0.0222 -0.0463 216 LYS   A CB  
1704 C CG  . LYS   A 220 ? 0.5135 0.4732 0.5206 0.0783  -0.0244 -0.0463 216 LYS   A CG  
1705 C CD  . LYS   A 220 ? 0.7491 0.6910 0.7450 0.0921  -0.0282 -0.0557 216 LYS   A CD  
1706 C CE  . LYS   A 220 ? 0.8588 0.7691 0.8364 0.0864  -0.0296 -0.0564 216 LYS   A CE  
1707 N NZ  . LYS   A 220 ? 1.0160 0.9023 0.9788 0.1006  -0.0340 -0.0656 216 LYS   A NZ  
1708 N N   . ASN   A 221 ? 0.4482 0.4694 0.4774 0.0581  -0.0119 -0.0406 217 ASN   A N   
1709 C CA  . ASN   A 221 ? 0.4172 0.4423 0.4413 0.0488  -0.0093 -0.0387 217 ASN   A CA  
1710 C C   . ASN   A 221 ? 0.4618 0.4688 0.4746 0.0486  -0.0117 -0.0428 217 ASN   A C   
1711 O O   . ASN   A 221 ? 0.4364 0.4312 0.4436 0.0570  -0.0135 -0.0502 217 ASN   A O   
1712 C CB  . ASN   A 221 ? 0.5123 0.5604 0.5384 0.0477  -0.0037 -0.0436 217 ASN   A CB  
1713 C CG  . ASN   A 221 ? 0.5088 0.5750 0.5442 0.0436  -0.0003 -0.0396 217 ASN   A CG  
1714 O OD1 . ASN   A 221 ? 0.3833 0.4442 0.4214 0.0389  -0.0020 -0.0311 217 ASN   A OD1 
1715 N ND2 . ASN   A 221 ? 0.4125 0.5011 0.4525 0.0447  0.0049  -0.0467 217 ASN   A ND2 
1716 N N   . PHE   A 222 ? 0.5033 0.5080 0.5119 0.0393  -0.0123 -0.0384 218 PHE   A N   
1717 C CA  . PHE   A 222 ? 0.5408 0.5331 0.5391 0.0361  -0.0141 -0.0429 218 PHE   A CA  
1718 C C   . PHE   A 222 ? 0.5172 0.5231 0.5116 0.0300  -0.0127 -0.0430 218 PHE   A C   
1719 O O   . PHE   A 222 ? 0.5661 0.5859 0.5639 0.0269  -0.0109 -0.0372 218 PHE   A O   
1720 C CB  . PHE   A 222 ? 0.5956 0.5720 0.5921 0.0297  -0.0175 -0.0388 218 PHE   A CB  
1721 C CG  . PHE   A 222 ? 0.4554 0.4146 0.4514 0.0342  -0.0191 -0.0375 218 PHE   A CG  
1722 C CD1 . PHE   A 222 ? 0.4517 0.3890 0.4364 0.0397  -0.0208 -0.0439 218 PHE   A CD1 
1723 C CD2 . PHE   A 222 ? 0.5287 0.4911 0.5327 0.0333  -0.0193 -0.0300 218 PHE   A CD2 
1724 C CE1 . PHE   A 222 ? 0.5469 0.4647 0.5271 0.0444  -0.0231 -0.0420 218 PHE   A CE1 
1725 C CE2 . PHE   A 222 ? 0.4107 0.3565 0.4117 0.0373  -0.0211 -0.0285 218 PHE   A CE2 
1726 C CZ  . PHE   A 222 ? 0.4520 0.3749 0.4403 0.0429  -0.0233 -0.0341 218 PHE   A CZ  
1727 N N   . SER   A 223 ? 0.5950 0.5942 0.5795 0.0281  -0.0138 -0.0496 219 SER   A N   
1728 C CA  . SER   A 223 ? 0.6738 0.6844 0.6516 0.0227  -0.0135 -0.0502 219 SER   A CA  
1729 C C   . SER   A 223 ? 0.7765 0.7922 0.7571 0.0159  -0.0171 -0.0414 219 SER   A C   
1730 O O   . SER   A 223 ? 0.7778 0.7863 0.7625 0.0127  -0.0205 -0.0393 219 SER   A O   
1731 C CB  . SER   A 223 ? 0.7147 0.7157 0.6812 0.0214  -0.0150 -0.0597 219 SER   A CB  
1732 O OG  . SER   A 223 ? 0.9442 0.9564 0.9026 0.0163  -0.0155 -0.0605 219 SER   A OG  
1733 N N   . ALA   A 224 ? 0.7841 0.8118 0.7612 0.0139  -0.0162 -0.0366 220 ALA   A N   
1734 C CA  . ALA   A 224 ? 0.8832 0.9144 0.8600 0.0101  -0.0210 -0.0291 220 ALA   A CA  
1735 C C   . ALA   A 224 ? 0.8249 0.8564 0.7957 0.0064  -0.0263 -0.0337 220 ALA   A C   
1736 O O   . ALA   A 224 ? 0.8677 0.8986 0.8292 0.0054  -0.0255 -0.0413 220 ALA   A O   
1737 C CB  . ALA   A 224 ? 0.6371 0.6753 0.6061 0.0089  -0.0193 -0.0227 220 ALA   A CB  
1738 N N   . GLY   A 225 ? 0.8539 0.8882 0.8305 0.0044  -0.0318 -0.0303 221 GLY   A N   
1739 C CA  . GLY   A 225 ? 0.9017 0.9403 0.8759 0.0001  -0.0373 -0.0359 221 GLY   A CA  
1740 C C   . GLY   A 225 ? 0.9607 0.9907 0.9400 -0.0046 -0.0363 -0.0427 221 GLY   A C   
1741 O O   . GLY   A 225 ? 0.9347 0.9556 0.9211 -0.0037 -0.0331 -0.0405 221 GLY   A O   
1742 N N   . THR   A 226 ? 0.9795 1.0101 0.9529 -0.0105 -0.0390 -0.0510 222 THR   A N   
1743 C CA  . THR   A 226 ? 0.9534 0.9725 0.9278 -0.0178 -0.0381 -0.0577 222 THR   A CA  
1744 C C   . THR   A 226 ? 0.9537 0.9525 0.9174 -0.0155 -0.0336 -0.0636 222 THR   A C   
1745 O O   . THR   A 226 ? 0.9856 0.9851 0.9396 -0.0121 -0.0327 -0.0678 222 THR   A O   
1746 C CB  . THR   A 226 ? 0.8870 0.9169 0.8600 -0.0269 -0.0433 -0.0651 222 THR   A CB  
1747 O OG1 . THR   A 226 ? 0.8532 0.9049 0.8367 -0.0259 -0.0488 -0.0608 222 THR   A OG1 
1748 C CG2 . THR   A 226 ? 0.6519 0.6686 0.6247 -0.0378 -0.0414 -0.0717 222 THR   A CG2 
1749 N N   . SER   A 227 ? 0.9806 0.9607 0.9446 -0.0167 -0.0309 -0.0641 223 SER   A N   
1750 C CA  . SER   A 227 ? 0.9331 0.8896 0.8855 -0.0129 -0.0282 -0.0703 223 SER   A CA  
1751 C C   . SER   A 227 ? 0.7724 0.7078 0.7157 -0.0237 -0.0289 -0.0765 223 SER   A C   
1752 O O   . SER   A 227 ? 0.8346 0.7750 0.7838 -0.0343 -0.0299 -0.0748 223 SER   A O   
1753 C CB  . SER   A 227 ? 0.7943 0.7422 0.7508 -0.0026 -0.0252 -0.0651 223 SER   A CB  
1754 O OG  . SER   A 227 ? 0.9467 0.9121 0.9088 0.0057  -0.0234 -0.0617 223 SER   A OG  
1755 N N   . ASP   A 228 ? 0.8791 0.7902 0.8070 -0.0213 -0.0280 -0.0845 224 ASP   A N   
1756 C CA  . ASP   A 228 ? 0.8046 0.6869 0.7183 -0.0317 -0.0282 -0.0904 224 ASP   A CA  
1757 C C   . ASP   A 228 ? 0.8390 0.6945 0.7477 -0.0289 -0.0267 -0.0854 224 ASP   A C   
1758 O O   . ASP   A 228 ? 1.0701 0.8908 0.9600 -0.0326 -0.0267 -0.0902 224 ASP   A O   
1759 C CB  . ASP   A 228 ? 0.8710 0.7349 0.7668 -0.0298 -0.0287 -0.1019 224 ASP   A CB  
1760 C CG  . ASP   A 228 ? 0.8850 0.7266 0.7657 -0.0465 -0.0297 -0.1097 224 ASP   A CG  
1761 O OD1 . ASP   A 228 ? 1.0849 0.9470 0.9715 -0.0600 -0.0313 -0.1122 224 ASP   A OD1 
1762 O OD2 . ASP   A 228 ? 1.1255 0.9286 0.9876 -0.0461 -0.0291 -0.1136 224 ASP   A OD2 
1763 N N   . ARG   A 229 ? 0.7651 0.6336 0.6876 -0.0226 -0.0258 -0.0758 225 ARG   A N   
1764 C CA  . ARG   A 229 ? 0.7676 0.6132 0.6852 -0.0173 -0.0251 -0.0706 225 ARG   A CA  
1765 C C   . ARG   A 229 ? 0.7995 0.6395 0.7173 -0.0322 -0.0237 -0.0660 225 ARG   A C   
1766 O O   . ARG   A 229 ? 0.7482 0.6155 0.6807 -0.0411 -0.0232 -0.0637 225 ARG   A O   
1767 C CB  . ARG   A 229 ? 0.6426 0.5063 0.5745 -0.0027 -0.0247 -0.0639 225 ARG   A CB  
1768 C CG  . ARG   A 229 ? 0.7839 0.6261 0.7105 0.0059  -0.0252 -0.0594 225 ARG   A CG  
1769 C CD  . ARG   A 229 ? 0.7242 0.5890 0.6666 0.0187  -0.0248 -0.0543 225 ARG   A CD  
1770 N NE  . ARG   A 229 ? 0.7258 0.5973 0.6683 0.0320  -0.0249 -0.0609 225 ARG   A NE  
1771 C CZ  . ARG   A 229 ? 0.9610 0.8161 0.8958 0.0461  -0.0268 -0.0652 225 ARG   A CZ  
1772 N NH1 . ARG   A 229 ? 1.0501 0.9174 0.9874 0.0578  -0.0261 -0.0728 225 ARG   A NH1 
1773 N NH2 . ARG   A 229 ? 1.0485 0.8753 0.9722 0.0490  -0.0297 -0.0622 225 ARG   A NH2 
1774 N N   . GLU   A 230 ? 0.7065 0.5106 0.6067 -0.0344 -0.0233 -0.0651 226 GLU   A N   
1775 C CA  . GLU   A 230 ? 0.8052 0.6014 0.7024 -0.0495 -0.0208 -0.0606 226 GLU   A CA  
1776 C C   . GLU   A 230 ? 0.6809 0.4984 0.5956 -0.0436 -0.0198 -0.0512 226 GLU   A C   
1777 O O   . GLU   A 230 ? 0.6417 0.4655 0.5635 -0.0272 -0.0215 -0.0474 226 GLU   A O   
1778 C CB  . GLU   A 230 ? 0.9625 0.7089 0.8308 -0.0533 -0.0208 -0.0612 226 GLU   A CB  
1779 C CG  . GLU   A 230 ? 1.0620 0.7795 0.9087 -0.0574 -0.0222 -0.0709 226 GLU   A CG  
1780 C CD  . GLU   A 230 ? 1.2597 0.9551 1.0950 -0.0355 -0.0263 -0.0741 226 GLU   A CD  
1781 O OE1 . GLU   A 230 ? 1.0667 0.7860 0.9190 -0.0180 -0.0277 -0.0712 226 GLU   A OE1 
1782 O OE2 . GLU   A 230 ? 1.3699 1.0243 1.1789 -0.0360 -0.0281 -0.0802 226 GLU   A OE2 
1783 N N   . SER   A 231 ? 0.5574 0.3874 0.4793 -0.0578 -0.0168 -0.0486 227 SER   A N   
1784 C CA  . SER   A 231 ? 0.5603 0.4090 0.4973 -0.0534 -0.0156 -0.0406 227 SER   A CA  
1785 C C   . SER   A 231 ? 0.7150 0.5345 0.6384 -0.0446 -0.0161 -0.0347 227 SER   A C   
1786 O O   . SER   A 231 ? 0.5853 0.3673 0.4847 -0.0492 -0.0161 -0.0356 227 SER   A O   
1787 C CB  . SER   A 231 ? 0.5678 0.4342 0.5132 -0.0706 -0.0118 -0.0410 227 SER   A CB  
1788 O OG  . SER   A 231 ? 0.4576 0.3604 0.4217 -0.0730 -0.0132 -0.0453 227 SER   A OG  
1789 N N   . ILE   A 232 ? 0.5081 0.3435 0.4450 -0.0321 -0.0172 -0.0287 228 ILE   A N   
1790 C CA  . ILE   A 232 ? 0.5553 0.3694 0.4822 -0.0206 -0.0192 -0.0237 228 ILE   A CA  
1791 C C   . ILE   A 232 ? 0.5381 0.3617 0.4720 -0.0252 -0.0167 -0.0170 228 ILE   A C   
1792 O O   . ILE   A 232 ? 0.4673 0.3227 0.4221 -0.0238 -0.0156 -0.0150 228 ILE   A O   
1793 C CB  . ILE   A 232 ? 0.6526 0.4781 0.5888 -0.0015 -0.0227 -0.0243 228 ILE   A CB  
1794 C CG1 . ILE   A 232 ? 0.5687 0.3788 0.4935 0.0048  -0.0250 -0.0320 228 ILE   A CG1 
1795 C CG2 . ILE   A 232 ? 0.6501 0.4650 0.5826 0.0102  -0.0253 -0.0192 228 ILE   A CG2 
1796 C CD1 . ILE   A 232 ? 0.5236 0.3566 0.4620 0.0194  -0.0264 -0.0350 228 ILE   A CD1 
1797 N N   . PHE   A 233 ? 0.5695 0.3633 0.4835 -0.0303 -0.0160 -0.0136 229 PHE   A N   
1798 C CA  . PHE   A 233 ? 0.5859 0.3843 0.5021 -0.0342 -0.0135 -0.0075 229 PHE   A CA  
1799 C C   . PHE   A 233 ? 0.5572 0.3452 0.4693 -0.0172 -0.0183 -0.0027 229 PHE   A C   
1800 O O   . PHE   A 233 ? 0.6187 0.3777 0.5127 -0.0075 -0.0230 -0.0032 229 PHE   A O   
1801 C CB  . PHE   A 233 ? 0.6483 0.4208 0.5426 -0.0526 -0.0091 -0.0066 229 PHE   A CB  
1802 C CG  . PHE   A 233 ? 0.5729 0.3637 0.4750 -0.0717 -0.0035 -0.0123 229 PHE   A CG  
1803 C CD1 . PHE   A 233 ? 0.6216 0.4011 0.5150 -0.0793 -0.0038 -0.0188 229 PHE   A CD1 
1804 C CD2 . PHE   A 233 ? 0.6394 0.4605 0.5582 -0.0815 0.0016  -0.0123 229 PHE   A CD2 
1805 C CE1 . PHE   A 233 ? 0.6630 0.4628 0.5648 -0.0973 0.0007  -0.0251 229 PHE   A CE1 
1806 C CE2 . PHE   A 233 ? 0.6421 0.4850 0.5704 -0.0980 0.0060  -0.0191 229 PHE   A CE2 
1807 C CZ  . PHE   A 233 ? 0.7208 0.5540 0.6410 -0.1063 0.0054  -0.0254 229 PHE   A CZ  
1808 N N   . PHE   A 234 ? 0.4970 0.3090 0.4258 -0.0132 -0.0176 0.0012  230 PHE   A N   
1809 C CA  . PHE   A 234 ? 0.5125 0.3216 0.4410 0.0021  -0.0224 0.0047  230 PHE   A CA  
1810 C C   . PHE   A 234 ? 0.5949 0.4180 0.5313 -0.0014 -0.0199 0.0096  230 PHE   A C   
1811 O O   . PHE   A 234 ? 0.4893 0.3283 0.4345 -0.0134 -0.0146 0.0095  230 PHE   A O   
1812 C CB  . PHE   A 234 ? 0.5607 0.3919 0.5068 0.0163  -0.0256 0.0015  230 PHE   A CB  
1813 C CG  . PHE   A 234 ? 0.4649 0.3319 0.4352 0.0134  -0.0224 0.0016  230 PHE   A CG  
1814 C CD1 . PHE   A 234 ? 0.4896 0.3700 0.4676 0.0053  -0.0197 -0.0017 230 PHE   A CD1 
1815 C CD2 . PHE   A 234 ? 0.4664 0.3515 0.4497 0.0191  -0.0230 0.0047  230 PHE   A CD2 
1816 C CE1 . PHE   A 234 ? 0.4806 0.3898 0.4773 0.0045  -0.0182 -0.0011 230 PHE   A CE1 
1817 C CE2 . PHE   A 234 ? 0.4955 0.4075 0.4968 0.0168  -0.0207 0.0052  230 PHE   A CE2 
1818 C CZ  . PHE   A 234 ? 0.4588 0.3817 0.4660 0.0103  -0.0186 0.0026  230 PHE   A CZ  
1819 N N   . ASN   A 235 ? 0.5722 0.3908 0.5057 0.0101  -0.0243 0.0127  231 ASN   A N   
1820 C CA  . ASN   A 235 ? 0.5192 0.3501 0.4593 0.0091  -0.0230 0.0167  231 ASN   A CA  
1821 C C   . ASN   A 235 ? 0.4961 0.3537 0.4571 0.0208  -0.0258 0.0157  231 ASN   A C   
1822 O O   . ASN   A 235 ? 0.4938 0.3483 0.4533 0.0336  -0.0315 0.0144  231 ASN   A O   
1823 C CB  . ASN   A 235 ? 0.5844 0.3857 0.4998 0.0107  -0.0261 0.0211  231 ASN   A CB  
1824 C CG  . ASN   A 235 ? 0.6509 0.4634 0.5703 0.0075  -0.0240 0.0246  231 ASN   A CG  
1825 O OD1 . ASN   A 235 ? 0.5264 0.3599 0.4618 0.0160  -0.0264 0.0244  231 ASN   A OD1 
1826 N ND2 . ASN   A 235 ? 0.6697 0.4681 0.5734 -0.0060 -0.0190 0.0271  231 ASN   A ND2 
1827 N N   . SER   A 236 ? 0.4737 0.3572 0.4533 0.0162  -0.0220 0.0158  232 SER   A N   
1828 C CA  . SER   A 236 ? 0.4861 0.3926 0.4833 0.0240  -0.0236 0.0150  232 SER   A CA  
1829 C C   . SER   A 236 ? 0.4924 0.3978 0.4876 0.0321  -0.0278 0.0166  232 SER   A C   
1830 O O   . SER   A 236 ? 0.5415 0.4600 0.5459 0.0405  -0.0308 0.0143  232 SER   A O   
1831 C CB  . SER   A 236 ? 0.5231 0.4505 0.5353 0.0177  -0.0196 0.0154  232 SER   A CB  
1832 O OG  . SER   A 236 ? 0.5008 0.4262 0.5100 0.0116  -0.0169 0.0175  232 SER   A OG  
1833 N N   . HIS   A 237 ? 0.5075 0.3995 0.4905 0.0289  -0.0279 0.0198  233 HIS   A N   
1834 C CA  . HIS   A 237 ? 0.5338 0.4241 0.5129 0.0368  -0.0329 0.0210  233 HIS   A CA  
1835 C C   . HIS   A 237 ? 0.5623 0.4380 0.5302 0.0492  -0.0402 0.0193  233 HIS   A C   
1836 O O   . HIS   A 237 ? 0.6053 0.4935 0.5806 0.0597  -0.0454 0.0167  233 HIS   A O   
1837 C CB  . HIS   A 237 ? 0.5593 0.4369 0.5247 0.0301  -0.0312 0.0248  233 HIS   A CB  
1838 C CG  . HIS   A 237 ? 0.5903 0.4675 0.5511 0.0375  -0.0368 0.0259  233 HIS   A CG  
1839 N ND1 . HIS   A 237 ? 0.8526 0.7082 0.7938 0.0460  -0.0441 0.0273  233 HIS   A ND1 
1840 C CD2 . HIS   A 237 ? 0.7275 0.6226 0.6997 0.0379  -0.0370 0.0253  233 HIS   A CD2 
1841 C CE1 . HIS   A 237 ? 0.8279 0.6911 0.7699 0.0516  -0.0487 0.0273  233 HIS   A CE1 
1842 N NE2 . HIS   A 237 ? 0.7585 0.6455 0.7193 0.0459  -0.0442 0.0259  233 HIS   A NE2 
1843 N N   . ASN   A 238 ? 0.4410 0.2904 0.3906 0.0483  -0.0410 0.0198  234 ASN   A N   
1844 C CA  . ASN   A 238 ? 0.5971 0.4285 0.5335 0.0623  -0.0488 0.0175  234 ASN   A CA  
1845 C C   . ASN   A 238 ? 0.6599 0.5127 0.6142 0.0717  -0.0501 0.0109  234 ASN   A C   
1846 O O   . ASN   A 238 ? 0.5543 0.4117 0.5100 0.0866  -0.0570 0.0069  234 ASN   A O   
1847 C CB  . ASN   A 238 ? 0.6351 0.4282 0.5443 0.0575  -0.0488 0.0196  234 ASN   A CB  
1848 C CG  . ASN   A 238 ? 0.7661 0.5338 0.6518 0.0493  -0.0482 0.0260  234 ASN   A CG  
1849 O OD1 . ASN   A 238 ? 0.7176 0.4944 0.6056 0.0508  -0.0497 0.0285  234 ASN   A OD1 
1850 N ND2 . ASN   A 238 ? 0.6907 0.4258 0.5521 0.0392  -0.0456 0.0283  234 ASN   A ND2 
1851 N N   . VAL   A 239 ? 0.6233 0.4914 0.5911 0.0634  -0.0438 0.0092  235 VAL   A N   
1852 C CA  . VAL   A 239 ? 0.6678 0.5551 0.6498 0.0703  -0.0438 0.0030  235 VAL   A CA  
1853 C C   . VAL   A 239 ? 0.6405 0.5593 0.6421 0.0752  -0.0445 0.0006  235 VAL   A C   
1854 O O   . VAL   A 239 ? 0.5290 0.4625 0.5386 0.0856  -0.0473 -0.0058 235 VAL   A O   
1855 C CB  . VAL   A 239 ? 0.5696 0.4635 0.5580 0.0592  -0.0374 0.0024  235 VAL   A CB  
1856 C CG1 . VAL   A 239 ? 0.6078 0.5255 0.6113 0.0641  -0.0362 -0.0033 235 VAL   A CG1 
1857 C CG2 . VAL   A 239 ? 0.6578 0.5223 0.6271 0.0545  -0.0371 0.0023  235 VAL   A CG2 
1858 N N   . SER   A 240 ? 0.5862 0.5162 0.5954 0.0672  -0.0418 0.0046  236 SER   A N   
1859 C CA  . SER   A 240 ? 0.5554 0.5136 0.5819 0.0677  -0.0411 0.0025  236 SER   A CA  
1860 C C   . SER   A 240 ? 0.6725 0.6328 0.6974 0.0729  -0.0464 0.0029  236 SER   A C   
1861 O O   . SER   A 240 ? 0.7085 0.6902 0.7461 0.0703  -0.0455 0.0015  236 SER   A O   
1862 C CB  . SER   A 240 ? 0.3944 0.3636 0.4303 0.0552  -0.0346 0.0059  236 SER   A CB  
1863 O OG  . SER   A 240 ? 0.7838 0.7432 0.8141 0.0491  -0.0336 0.0108  236 SER   A OG  
1864 N N   . LYS   A 241 ? 0.6845 0.6212 0.6916 0.0796  -0.0522 0.0047  237 LYS   A N   
1865 C CA  . LYS   A 241 ? 0.8074 0.7435 0.8093 0.0865  -0.0590 0.0050  237 LYS   A CA  
1866 C C   . LYS   A 241 ? 1.0552 1.0205 1.0737 0.0971  -0.0634 -0.0032 237 LYS   A C   
1867 O O   . LYS   A 241 ? 0.9422 0.9191 0.9696 0.1011  -0.0618 -0.0085 237 LYS   A O   
1868 C CB  . LYS   A 241 ? 0.7598 0.6601 0.7350 0.0930  -0.0649 0.0084  237 LYS   A CB  
1869 C CG  . LYS   A 241 ? 0.9739 0.8624 0.9346 0.0963  -0.0710 0.0118  237 LYS   A CG  
1870 C CD  . LYS   A 241 ? 0.9690 0.8177 0.9000 0.0920  -0.0713 0.0186  237 LYS   A CD  
1871 C CE  . LYS   A 241 ? 0.8687 0.6899 0.7823 0.1010  -0.0757 0.0176  237 LYS   A CE  
1872 N NZ  . LYS   A 241 ? 0.9272 0.7050 0.8057 0.0986  -0.0785 0.0243  237 LYS   A NZ  
1873 N N   . PRO   A 242 ? 0.9395 0.9208 0.9636 0.1011  -0.0686 -0.0056 238 PRO   A N   
1874 C CA  . PRO   A 242 ? 0.9153 0.9328 0.9602 0.1065  -0.0702 -0.0148 238 PRO   A CA  
1875 C C   . PRO   A 242 ? 1.0983 1.1200 1.1450 0.1212  -0.0741 -0.0221 238 PRO   A C   
1876 O O   . PRO   A 242 ? 1.1905 1.2435 1.2557 0.1225  -0.0716 -0.0303 238 PRO   A O   
1877 C CB  . PRO   A 242 ? 0.8376 0.8656 0.8828 0.1119  -0.0781 -0.0170 238 PRO   A CB  
1878 C CG  . PRO   A 242 ? 1.0244 1.0190 1.0463 0.1125  -0.0819 -0.0091 238 PRO   A CG  
1879 C CD  . PRO   A 242 ? 0.9872 0.9520 0.9950 0.1058  -0.0758 -0.0022 238 PRO   A CD  
1880 N N   . GLU   A 243 ? 0.9824 0.9710 1.0082 0.1313  -0.0795 -0.0195 239 GLU   A N   
1881 C CA  . GLU   A 243 ? 1.1479 1.1314 1.1710 0.1441  -0.0820 -0.0257 239 GLU   A CA  
1882 C C   . GLU   A 243 ? 1.3067 1.2443 1.3030 0.1442  -0.0828 -0.0191 239 GLU   A C   
1883 O O   . GLU   A 243 ? 1.3379 1.2455 1.3117 0.1512  -0.0904 -0.0148 239 GLU   A O   
1884 C CB  . GLU   A 243 ? 1.2154 1.2150 1.2430 0.1654  -0.0930 -0.0355 239 GLU   A CB  
1885 C CG  . GLU   A 243 ? 1.4012 1.4521 1.4586 0.1658  -0.0899 -0.0467 239 GLU   A CG  
1886 C CD  . GLU   A 243 ? 1.5263 1.5884 1.5936 0.1603  -0.0805 -0.0509 239 GLU   A CD  
1887 O OE1 . GLU   A 243 ? 1.5688 1.6023 1.6210 0.1652  -0.0807 -0.0493 239 GLU   A OE1 
1888 O OE2 . GLU   A 243 ? 1.4523 1.5497 1.5402 0.1498  -0.0728 -0.0554 239 GLU   A OE2 
1889 N N   . SER   A 244 ? 1.2456 1.1774 1.2429 0.1352  -0.0750 -0.0184 240 SER   A N   
1890 C CA  . SER   A 244 ? 1.2406 1.1352 1.2159 0.1373  -0.0758 -0.0166 240 SER   A CA  
1891 C C   . SER   A 244 ? 1.2922 1.1945 1.2723 0.1515  -0.0782 -0.0269 240 SER   A C   
1892 O O   . SER   A 244 ? 1.3317 1.2711 1.3348 0.1523  -0.0744 -0.0341 240 SER   A O   
1893 C CB  . SER   A 244 ? 1.0095 0.8942 0.9827 0.1175  -0.0659 -0.0104 240 SER   A CB  
1894 O OG  . SER   A 244 ? 1.1241 0.9750 1.0770 0.1173  -0.0661 -0.0101 240 SER   A OG  
1895 N N   . SER   A 245 ? 1.3476 1.2132 1.3042 0.1623  -0.0842 -0.0279 241 SER   A N   
1896 C CA  . SER   A 245 ? 1.3114 1.1757 1.2677 0.1739  -0.0852 -0.0374 241 SER   A CA  
1897 C C   . SER   A 245 ? 1.2473 1.0718 1.1814 0.1629  -0.0813 -0.0328 241 SER   A C   
1898 O O   . SER   A 245 ? 1.0892 0.8691 0.9940 0.1666  -0.0871 -0.0287 241 SER   A O   
1899 C CB  . SER   A 245 ? 1.4537 1.3107 1.4016 0.2006  -0.0978 -0.0456 241 SER   A CB  
1900 O OG  . SER   A 245 ? 1.4047 1.3083 1.3786 0.2101  -0.1004 -0.0532 241 SER   A OG  
1901 N N   . SER   A 246 ? 1.2090 1.0489 1.1553 0.1483  -0.0717 -0.0334 242 SER   A N   
1902 C CA  . SER   A 246 ? 1.0400 0.8501 0.9696 0.1344  -0.0670 -0.0297 242 SER   A CA  
1903 C C   . SER   A 246 ? 0.9875 0.8090 0.9244 0.1357  -0.0631 -0.0385 242 SER   A C   
1904 O O   . SER   A 246 ? 0.9980 0.8565 0.9565 0.1417  -0.0609 -0.0454 242 SER   A O   
1905 C CB  . SER   A 246 ? 1.1103 0.9276 1.0460 0.1122  -0.0592 -0.0206 242 SER   A CB  
1906 O OG  . SER   A 246 ? 1.1536 0.9633 1.0832 0.1104  -0.0619 -0.0133 242 SER   A OG  
1907 N N   . VAL   A 247 ? 0.9364 0.7256 0.8538 0.1285  -0.0617 -0.0385 243 VAL   A N   
1908 C CA  . VAL   A 247 ? 0.9393 0.7374 0.8616 0.1259  -0.0572 -0.0460 243 VAL   A CA  
1909 C C   . VAL   A 247 ? 0.9302 0.7666 0.8759 0.1107  -0.0486 -0.0437 243 VAL   A C   
1910 O O   . VAL   A 247 ? 1.0685 0.9244 1.0236 0.1104  -0.0448 -0.0502 243 VAL   A O   
1911 C CB  . VAL   A 247 ? 1.1039 0.8573 0.9986 0.1181  -0.0575 -0.0460 243 VAL   A CB  
1912 C CG1 . VAL   A 247 ? 1.0903 0.8333 0.9795 0.0955  -0.0525 -0.0363 243 VAL   A CG1 
1913 C CG2 . VAL   A 247 ? 1.1479 0.9077 1.0448 0.1175  -0.0541 -0.0554 243 VAL   A CG2 
1914 N N   . LEU   A 248 ? 0.8656 0.7119 0.8191 0.0988  -0.0459 -0.0346 244 LEU   A N   
1915 C CA  . LEU   A 248 ? 0.7163 0.5947 0.6894 0.0861  -0.0392 -0.0316 244 LEU   A CA  
1916 C C   . LEU   A 248 ? 0.6473 0.5614 0.6411 0.0920  -0.0383 -0.0329 244 LEU   A C   
1917 O O   . LEU   A 248 ? 0.6329 0.5725 0.6403 0.0839  -0.0329 -0.0322 244 LEU   A O   
1918 C CB  . LEU   A 248 ? 0.6851 0.5560 0.6558 0.0707  -0.0366 -0.0224 244 LEU   A CB  
1919 C CG  . LEU   A 248 ? 0.7612 0.5978 0.7109 0.0612  -0.0367 -0.0207 244 LEU   A CG  
1920 C CD1 . LEU   A 248 ? 0.5706 0.4092 0.5224 0.0458  -0.0329 -0.0133 244 LEU   A CD1 
1921 C CD2 . LEU   A 248 ? 0.7694 0.6027 0.7151 0.0566  -0.0346 -0.0269 244 LEU   A CD2 
1922 N N   . THR   A 249 ? 0.7314 0.6471 0.7262 0.1054  -0.0437 -0.0349 245 THR   A N   
1923 C CA  . THR   A 249 ? 0.6784 0.6295 0.6930 0.1093  -0.0428 -0.0372 245 THR   A CA  
1924 C C   . THR   A 249 ? 0.6522 0.6277 0.6771 0.1199  -0.0418 -0.0486 245 THR   A C   
1925 O O   . THR   A 249 ? 0.5078 0.5171 0.5498 0.1153  -0.0368 -0.0510 245 THR   A O   
1926 C CB  . THR   A 249 ? 0.7556 0.7011 0.7678 0.1181  -0.0496 -0.0348 245 THR   A CB  
1927 O OG1 . THR   A 249 ? 0.8458 0.7807 0.8540 0.1054  -0.0480 -0.0246 245 THR   A OG1 
1928 C CG2 . THR   A 249 ? 0.7467 0.7295 0.7786 0.1254  -0.0504 -0.0409 245 THR   A CG2 
1929 N N   . GLU   A 250 ? 0.5256 0.4838 0.5390 0.1332  -0.0460 -0.0563 246 GLU   A N   
1930 C CA  . GLU   A 250 ? 0.6409 0.6228 0.6635 0.1449  -0.0449 -0.0691 246 GLU   A CA  
1931 C C   . GLU   A 250 ? 0.5826 0.5847 0.6128 0.1318  -0.0356 -0.0707 246 GLU   A C   
1932 O O   . GLU   A 250 ? 0.6106 0.5929 0.6285 0.1259  -0.0338 -0.0701 246 GLU   A O   
1933 C CB  . GLU   A 250 ? 0.6170 0.5690 0.6217 0.1622  -0.0517 -0.0768 246 GLU   A CB  
1934 C CG  . GLU   A 250 ? 0.7456 0.6981 0.7502 0.1845  -0.0614 -0.0832 246 GLU   A CG  
1935 C CD  . GLU   A 250 ? 1.0285 0.9502 1.0139 0.2039  -0.0686 -0.0922 246 GLU   A CD  
1936 O OE1 . GLU   A 250 ? 0.9758 0.8592 0.9399 0.1973  -0.0680 -0.0889 246 GLU   A OE1 
1937 O OE2 . GLU   A 250 ? 0.9220 0.8578 0.9132 0.2260  -0.0752 -0.1033 246 GLU   A OE2 
1938 N N   . LEU   A 251 ? 0.4741 0.5143 0.5224 0.1263  -0.0299 -0.0727 247 LEU   A N   
1939 C CA  . LEU   A 251 ? 0.5291 0.5872 0.5813 0.1138  -0.0213 -0.0737 247 LEU   A CA  
1940 C C   . LEU   A 251 ? 0.5194 0.5864 0.5701 0.1241  -0.0195 -0.0871 247 LEU   A C   
1941 O O   . LEU   A 251 ? 0.5613 0.6433 0.6190 0.1401  -0.0222 -0.0981 247 LEU   A O   
1942 C CB  . LEU   A 251 ? 0.4720 0.5640 0.5401 0.1033  -0.0153 -0.0716 247 LEU   A CB  
1943 C CG  . LEU   A 251 ? 0.4796 0.5858 0.5476 0.0878  -0.0066 -0.0695 247 LEU   A CG  
1944 C CD1 . LEU   A 251 ? 0.3407 0.4234 0.3984 0.0751  -0.0067 -0.0570 247 LEU   A CD1 
1945 C CD2 . LEU   A 251 ? 0.4022 0.5423 0.4836 0.0794  -0.0004 -0.0708 247 LEU   A CD2 
1946 N N   . ASP   A 252 ? 0.5901 0.6488 0.6313 0.1156  -0.0152 -0.0869 248 ASP   A N   
1947 C CA  . ASP   A 252 ? 0.6383 0.7056 0.6767 0.1238  -0.0126 -0.1001 248 ASP   A CA  
1948 C C   . ASP   A 252 ? 0.5053 0.6170 0.5592 0.1215  -0.0046 -0.1079 248 ASP   A C   
1949 O O   . ASP   A 252 ? 0.6044 0.7365 0.6661 0.1358  -0.0044 -0.1216 248 ASP   A O   
1950 C CB  . ASP   A 252 ? 0.6518 0.6990 0.6750 0.1138  -0.0105 -0.0978 248 ASP   A CB  
1951 C CG  . ASP   A 252 ? 0.9003 0.9049 0.9070 0.1154  -0.0174 -0.0934 248 ASP   A CG  
1952 O OD1 . ASP   A 252 ? 0.9530 0.9377 0.9515 0.1309  -0.0232 -0.1002 248 ASP   A OD1 
1953 O OD2 . ASP   A 252 ? 0.8945 0.8853 0.8954 0.1011  -0.0171 -0.0834 248 ASP   A OD2 
1954 N N   . LYS   A 253 ? 0.5176 0.6442 0.5751 0.1034  0.0020  -0.0997 249 LYS   A N   
1955 C CA  . LYS   A 253 ? 0.5874 0.7531 0.6558 0.0961  0.0111  -0.1055 249 LYS   A CA  
1956 C C   . LYS   A 253 ? 0.4880 0.6565 0.5562 0.0766  0.0152  -0.0920 249 LYS   A C   
1957 O O   . LYS   A 253 ? 0.4283 0.5705 0.4871 0.0694  0.0118  -0.0800 249 LYS   A O   
1958 C CB  . LYS   A 253 ? 0.5521 0.7280 0.6131 0.0955  0.0175  -0.1153 249 LYS   A CB  
1959 C CG  . LYS   A 253 ? 0.6257 0.7753 0.6686 0.0850  0.0175  -0.1072 249 LYS   A CG  
1960 C CD  . LYS   A 253 ? 0.6559 0.8137 0.6899 0.0862  0.0228  -0.1184 249 LYS   A CD  
1961 C CE  . LYS   A 253 ? 0.7819 0.9739 0.8187 0.0736  0.0338  -0.1211 249 LYS   A CE  
1962 N NZ  . LYS   A 253 ? 0.8123 0.9960 0.8390 0.0543  0.0362  -0.1060 249 LYS   A NZ  
1963 N N   . ILE   A 254 ? 0.5674 0.7681 0.6455 0.0679  0.0226  -0.0950 250 ILE   A N   
1964 C CA  . ILE   A 254 ? 0.5068 0.7075 0.5808 0.0486  0.0272  -0.0831 250 ILE   A CA  
1965 C C   . ILE   A 254 ? 0.5116 0.7019 0.5682 0.0377  0.0316  -0.0786 250 ILE   A C   
1966 O O   . ILE   A 254 ? 0.6285 0.8332 0.6811 0.0382  0.0372  -0.0881 250 ILE   A O   
1967 C CB  . ILE   A 254 ? 0.6241 0.8604 0.7108 0.0400  0.0345  -0.0884 250 ILE   A CB  
1968 C CG1 . ILE   A 254 ? 0.5874 0.8354 0.6917 0.0513  0.0286  -0.0929 250 ILE   A CG1 
1969 C CG2 . ILE   A 254 ? 0.5060 0.7361 0.5833 0.0191  0.0395  -0.0759 250 ILE   A CG2 
1970 C CD1 . ILE   A 254 ? 0.6215 0.9129 0.7421 0.0457  0.0354  -0.1034 250 ILE   A CD1 
1971 N N   . GLU   A 255 ? 0.4672 0.6332 0.5128 0.0286  0.0286  -0.0649 251 GLU   A N   
1972 C CA  . GLU   A 255 ? 0.5448 0.6990 0.5726 0.0197  0.0305  -0.0597 251 GLU   A CA  
1973 C C   . GLU   A 255 ? 0.6042 0.7493 0.6232 0.0053  0.0317  -0.0465 251 GLU   A C   
1974 O O   . GLU   A 255 ? 0.5885 0.7201 0.6117 0.0055  0.0265  -0.0383 251 GLU   A O   
1975 C CB  . GLU   A 255 ? 0.5865 0.7152 0.6071 0.0275  0.0229  -0.0581 251 GLU   A CB  
1976 C CG  . GLU   A 255 ? 0.7344 0.8659 0.7561 0.0400  0.0224  -0.0714 251 GLU   A CG  
1977 C CD  . GLU   A 255 ? 1.0053 1.1107 1.0261 0.0499  0.0138  -0.0708 251 GLU   A CD  
1978 O OE1 . GLU   A 255 ? 0.9314 1.0324 0.9617 0.0579  0.0097  -0.0706 251 GLU   A OE1 
1979 O OE2 . GLU   A 255 ? 1.2522 1.3411 1.2614 0.0488  0.0112  -0.0709 251 GLU   A OE2 
1980 N N   . GLY   A 256 ? 0.5227 0.6736 0.5273 -0.0069 0.0383  -0.0448 252 GLY   A N   
1981 C CA  . GLY   A 256 ? 0.4832 0.6202 0.4740 -0.0200 0.0388  -0.0321 252 GLY   A CA  
1982 C C   . GLY   A 256 ? 0.4875 0.6354 0.4864 -0.0285 0.0433  -0.0306 252 GLY   A C   
1983 O O   . GLY   A 256 ? 0.5397 0.7146 0.5526 -0.0285 0.0491  -0.0407 252 GLY   A O   
1984 N N   . VAL   A 257 ? 0.4713 0.5985 0.4612 -0.0355 0.0402  -0.0185 253 VAL   A N   
1985 C CA  . VAL   A 257 ? 0.5466 0.6792 0.5408 -0.0456 0.0440  -0.0162 253 VAL   A CA  
1986 C C   . VAL   A 257 ? 0.5636 0.7065 0.5817 -0.0350 0.0398  -0.0213 253 VAL   A C   
1987 O O   . VAL   A 257 ? 0.5272 0.6559 0.5514 -0.0228 0.0315  -0.0188 253 VAL   A O   
1988 C CB  . VAL   A 257 ? 0.6479 0.7504 0.6230 -0.0542 0.0408  -0.0023 253 VAL   A CB  
1989 C CG1 . VAL   A 257 ? 0.5857 0.6910 0.5623 -0.0667 0.0453  -0.0005 253 VAL   A CG1 
1990 C CG2 . VAL   A 257 ? 0.6895 0.7782 0.6373 -0.0626 0.0430  0.0034  253 VAL   A CG2 
1991 N N   . PHE   A 258 ? 0.5046 0.6733 0.5355 -0.0404 0.0455  -0.0289 254 PHE   A N   
1992 C CA  . PHE   A 258 ? 0.6837 0.8646 0.7360 -0.0306 0.0411  -0.0342 254 PHE   A CA  
1993 C C   . PHE   A 258 ? 0.5343 0.7287 0.5906 -0.0452 0.0463  -0.0347 254 PHE   A C   
1994 O O   . PHE   A 258 ? 0.7056 0.9337 0.7748 -0.0491 0.0524  -0.0459 254 PHE   A O   
1995 C CB  . PHE   A 258 ? 0.5709 0.7768 0.6393 -0.0161 0.0408  -0.0481 254 PHE   A CB  
1996 C CG  . PHE   A 258 ? 0.7644 0.9747 0.8501 -0.0019 0.0332  -0.0522 254 PHE   A CG  
1997 C CD1 . PHE   A 258 ? 0.6930 0.8758 0.7764 0.0037  0.0249  -0.0428 254 PHE   A CD1 
1998 C CD2 . PHE   A 258 ? 0.7376 0.9804 0.8412 0.0066  0.0340  -0.0659 254 PHE   A CD2 
1999 C CE1 . PHE   A 258 ? 0.7130 0.8975 0.8086 0.0160  0.0180  -0.0459 254 PHE   A CE1 
2000 C CE2 . PHE   A 258 ? 0.6417 0.8861 0.7581 0.0210  0.0256  -0.0691 254 PHE   A CE2 
2001 C CZ  . PHE   A 258 ? 0.6211 0.8348 0.7321 0.0251  0.0177  -0.0585 254 PHE   A CZ  
2002 N N   . GLU   A 259 ? 0.5746 0.7433 0.6195 -0.0534 0.0440  -0.0235 255 GLU   A N   
2003 C CA  . GLU   A 259 ? 0.6330 0.8073 0.6782 -0.0686 0.0481  -0.0228 255 GLU   A CA  
2004 C C   . GLU   A 259 ? 0.6389 0.8031 0.6945 -0.0608 0.0400  -0.0200 255 GLU   A C   
2005 O O   . GLU   A 259 ? 0.6668 0.8137 0.7246 -0.0462 0.0319  -0.0159 255 GLU   A O   
2006 C CB  . GLU   A 259 ? 0.4619 0.6106 0.4800 -0.0868 0.0528  -0.0124 255 GLU   A CB  
2007 C CG  . GLU   A 259 ? 0.6384 0.7987 0.6429 -0.0992 0.0627  -0.0154 255 GLU   A CG  
2008 C CD  . GLU   A 259 ? 0.8788 1.0773 0.8945 -0.1138 0.0733  -0.0271 255 GLU   A CD  
2009 O OE1 . GLU   A 259 ? 0.9579 1.1634 0.9821 -0.1218 0.0738  -0.0289 255 GLU   A OE1 
2010 O OE2 . GLU   A 259 ? 0.9945 1.2181 1.0111 -0.1176 0.0812  -0.0355 255 GLU   A OE2 
2011 N N   . ARG   A 260 ? 0.6386 0.8138 0.6994 -0.0716 0.0428  -0.0226 256 ARG   A N   
2012 C CA  . ARG   A 260 ? 0.6201 0.7886 0.6900 -0.0660 0.0358  -0.0212 256 ARG   A CA  
2013 C C   . ARG   A 260 ? 0.4946 0.6267 0.5453 -0.0752 0.0344  -0.0093 256 ARG   A C   
2014 O O   . ARG   A 260 ? 0.6803 0.7991 0.7120 -0.0908 0.0402  -0.0044 256 ARG   A O   
2015 C CB  . ARG   A 260 ? 0.7779 0.9817 0.8656 -0.0721 0.0387  -0.0325 256 ARG   A CB  
2016 C CG  . ARG   A 260 ? 0.8443 1.0863 0.9503 -0.0621 0.0403  -0.0458 256 ARG   A CG  
2017 C CD  . ARG   A 260 ? 0.9883 1.2271 1.1052 -0.0377 0.0302  -0.0476 256 ARG   A CD  
2018 N NE  . ARG   A 260 ? 1.3392 1.6029 1.4665 -0.0257 0.0313  -0.0584 256 ARG   A NE  
2019 C CZ  . ARG   A 260 ? 1.1819 1.4438 1.3166 -0.0045 0.0232  -0.0621 256 ARG   A CZ  
2020 N NH1 . ARG   A 260 ? 0.8272 1.0653 0.9600 0.0055  0.0141  -0.0555 256 ARG   A NH1 
2021 N NH2 . ARG   A 260 ? 1.0363 1.3187 1.1784 0.0065  0.0243  -0.0726 256 ARG   A NH2 
2022 N N   . PRO   A 261 ? 0.5485 0.6624 0.6017 -0.0652 0.0265  -0.0047 257 PRO   A N   
2023 C CA  . PRO   A 261 ? 0.5610 0.6388 0.5958 -0.0696 0.0240  0.0060  257 PRO   A CA  
2024 C C   . PRO   A 261 ? 0.6468 0.7176 0.6696 -0.0894 0.0294  0.0070  257 PRO   A C   
2025 O O   . PRO   A 261 ? 0.5956 0.6905 0.6297 -0.0985 0.0329  -0.0009 257 PRO   A O   
2026 C CB  . PRO   A 261 ? 0.6235 0.6932 0.6681 -0.0558 0.0159  0.0070  257 PRO   A CB  
2027 C CG  . PRO   A 261 ? 0.5551 0.6559 0.6205 -0.0498 0.0148  -0.0028 257 PRO   A CG  
2028 C CD  . PRO   A 261 ? 0.5958 0.7206 0.6669 -0.0496 0.0196  -0.0094 257 PRO   A CD  
2029 N N   . SER   A 262 ? 0.7503 0.7870 0.7486 -0.0962 0.0296  0.0165  258 SER   A N   
2030 C CA  . SER   A 262 ? 0.7243 0.7434 0.7046 -0.1154 0.0340  0.0192  258 SER   A CA  
2031 C C   . SER   A 262 ? 0.6551 0.6632 0.6402 -0.1130 0.0289  0.0189  258 SER   A C   
2032 O O   . SER   A 262 ? 0.6725 0.6616 0.6575 -0.0982 0.0215  0.0235  258 SER   A O   
2033 C CB  . SER   A 262 ? 0.5680 0.5482 0.5167 -0.1205 0.0340  0.0301  258 SER   A CB  
2034 O OG  . SER   A 262 ? 0.6652 0.6156 0.5927 -0.1348 0.0353  0.0344  258 SER   A OG  
2035 N N   . ASP   A 263 ? 0.7099 0.7322 0.6997 -0.1282 0.0333  0.0125  259 ASP   A N   
2036 C CA  . ASP   A 263 ? 0.6540 0.6663 0.6468 -0.1277 0.0288  0.0113  259 ASP   A CA  
2037 C C   . ASP   A 263 ? 0.7517 0.7157 0.7170 -0.1308 0.0262  0.0206  259 ASP   A C   
2038 O O   . ASP   A 263 ? 0.5698 0.5183 0.5361 -0.1218 0.0202  0.0216  259 ASP   A O   
2039 C CB  . ASP   A 263 ? 0.7088 0.7490 0.7119 -0.1452 0.0339  0.0013  259 ASP   A CB  
2040 C CG  . ASP   A 263 ? 0.8523 0.8870 0.8605 -0.1439 0.0287  -0.0015 259 ASP   A CG  
2041 O OD1 . ASP   A 263 ? 0.8834 0.9377 0.9120 -0.1282 0.0226  -0.0059 259 ASP   A OD1 
2042 O OD2 . ASP   A 263 ? 1.0660 1.0743 1.0555 -0.1590 0.0306  0.0007  259 ASP   A OD2 
2043 N N   . GLU   A 264 ? 0.7254 0.6642 0.6645 -0.1426 0.0304  0.0272  260 GLU   A N   
2044 C CA  . GLU   A 264 ? 0.7000 0.5889 0.6097 -0.1429 0.0266  0.0363  260 GLU   A CA  
2045 C C   . GLU   A 264 ? 0.7995 0.6726 0.7104 -0.1185 0.0175  0.0419  260 GLU   A C   
2046 O O   . GLU   A 264 ? 0.6637 0.5082 0.5649 -0.1102 0.0115  0.0450  260 GLU   A O   
2047 C CB  . GLU   A 264 ? 0.6681 0.5315 0.5458 -0.1611 0.0327  0.0426  260 GLU   A CB  
2048 C CG  . GLU   A 264 ? 0.9597 0.7669 0.8019 -0.1646 0.0289  0.0512  260 GLU   A CG  
2049 C CD  . GLU   A 264 ? 1.1280 0.9027 0.9359 -0.1705 0.0302  0.0610  260 GLU   A CD  
2050 O OE1 . GLU   A 264 ? 1.2067 0.9362 0.9885 -0.1606 0.0226  0.0693  260 GLU   A OE1 
2051 O OE2 . GLU   A 264 ? 1.0002 0.7947 0.8061 -0.1843 0.0384  0.0599  260 GLU   A OE2 
2052 N N   . VAL   A 265 ? 0.6307 0.5236 0.5535 -0.1070 0.0166  0.0423  261 VAL   A N   
2053 C CA  . VAL   A 265 ? 0.6578 0.5407 0.5834 -0.0857 0.0085  0.0463  261 VAL   A CA  
2054 C C   . VAL   A 265 ? 0.6512 0.5450 0.5979 -0.0728 0.0038  0.0418  261 VAL   A C   
2055 O O   . VAL   A 265 ? 0.4593 0.3338 0.4019 -0.0603 -0.0024 0.0445  261 VAL   A O   
2056 C CB  . VAL   A 265 ? 0.5604 0.4637 0.4941 -0.0788 0.0092  0.0464  261 VAL   A CB  
2057 C CG1 . VAL   A 265 ? 0.4450 0.3474 0.3883 -0.0581 0.0014  0.0479  261 VAL   A CG1 
2058 C CG2 . VAL   A 265 ? 0.6910 0.5765 0.5982 -0.0894 0.0126  0.0524  261 VAL   A CG2 
2059 N N   . ILE   A 266 ? 0.6303 0.5556 0.5987 -0.0755 0.0064  0.0343  262 ILE   A N   
2060 C CA  . ILE   A 266 ? 0.5855 0.5206 0.5712 -0.0643 0.0020  0.0303  262 ILE   A CA  
2061 C C   . ILE   A 266 ? 0.6349 0.5456 0.6095 -0.0677 0.0000  0.0307  262 ILE   A C   
2062 O O   . ILE   A 266 ? 0.6214 0.5228 0.5988 -0.0554 -0.0048 0.0309  262 ILE   A O   
2063 C CB  . ILE   A 266 ? 0.4918 0.4635 0.4995 -0.0660 0.0041  0.0223  262 ILE   A CB  
2064 C CG1 . ILE   A 266 ? 0.5701 0.5621 0.5895 -0.0567 0.0042  0.0213  262 ILE   A CG1 
2065 C CG2 . ILE   A 266 ? 0.5472 0.5240 0.5663 -0.0589 -0.0002 0.0185  262 ILE   A CG2 
2066 C CD1 . ILE   A 266 ? 0.4975 0.5241 0.5330 -0.0607 0.0075  0.0131  262 ILE   A CD1 
2067 N N   . ARG   A 267 ? 0.6083 0.5079 0.5692 -0.0852 0.0041  0.0301  263 ARG   A N   
2068 C CA  . ARG   A 267 ? 0.7040 0.5780 0.6523 -0.0899 0.0024  0.0295  263 ARG   A CA  
2069 C C   . ARG   A 267 ? 0.6611 0.4953 0.5882 -0.0798 -0.0025 0.0363  263 ARG   A C   
2070 O O   . ARG   A 267 ? 0.6213 0.4424 0.5483 -0.0695 -0.0070 0.0349  263 ARG   A O   
2071 C CB  . ARG   A 267 ? 0.6520 0.5222 0.5884 -0.1137 0.0085  0.0269  263 ARG   A CB  
2072 C CG  . ARG   A 267 ? 0.7113 0.6228 0.6706 -0.1224 0.0117  0.0175  263 ARG   A CG  
2073 C CD  . ARG   A 267 ? 0.6364 0.5459 0.5844 -0.1480 0.0181  0.0135  263 ARG   A CD  
2074 N NE  . ARG   A 267 ? 0.7248 0.6348 0.6608 -0.1626 0.0253  0.0163  263 ARG   A NE  
2075 C CZ  . ARG   A 267 ? 0.8481 0.7189 0.7523 -0.1764 0.0285  0.0229  263 ARG   A CZ  
2076 N NH1 . ARG   A 267 ? 0.9471 0.7743 0.8290 -0.1759 0.0245  0.0270  263 ARG   A NH1 
2077 N NH2 . ARG   A 267 ? 0.8227 0.6961 0.7151 -0.1905 0.0357  0.0253  263 ARG   A NH2 
2078 N N   . GLU   A 268 ? 0.6427 0.4581 0.5511 -0.0817 -0.0021 0.0431  264 GLU   A N   
2079 C CA  . GLU   A 268 ? 0.8230 0.6009 0.7102 -0.0697 -0.0084 0.0492  264 GLU   A CA  
2080 C C   . GLU   A 268 ? 0.7225 0.5130 0.6270 -0.0471 -0.0145 0.0483  264 GLU   A C   
2081 O O   . GLU   A 268 ? 0.7586 0.5267 0.6545 -0.0340 -0.0204 0.0491  264 GLU   A O   
2082 C CB  . GLU   A 268 ? 0.8739 0.6303 0.7359 -0.0764 -0.0073 0.0569  264 GLU   A CB  
2083 C CG  . GLU   A 268 ? 1.2683 0.9734 1.0963 -0.0721 -0.0131 0.0633  264 GLU   A CG  
2084 C CD  . GLU   A 268 ? 1.3581 1.0395 1.1571 -0.0794 -0.0125 0.0718  264 GLU   A CD  
2085 O OE1 . GLU   A 268 ? 1.1614 0.8115 0.9395 -0.0653 -0.0205 0.0777  264 GLU   A OE1 
2086 O OE2 . GLU   A 268 ? 1.3021 0.9972 1.0987 -0.0988 -0.0040 0.0720  264 GLU   A OE2 
2087 N N   . LEU   A 269 ? 0.7165 0.5425 0.6446 -0.0425 -0.0130 0.0458  265 LEU   A N   
2088 C CA  . LEU   A 269 ? 0.6518 0.4912 0.5961 -0.0244 -0.0176 0.0442  265 LEU   A CA  
2089 C C   . LEU   A 269 ? 0.7668 0.6135 0.7242 -0.0193 -0.0186 0.0385  265 LEU   A C   
2090 O O   . LEU   A 269 ? 0.5392 0.3831 0.5007 -0.0055 -0.0226 0.0371  265 LEU   A O   
2091 C CB  . LEU   A 269 ? 0.7105 0.5806 0.6720 -0.0227 -0.0156 0.0433  265 LEU   A CB  
2092 C CG  . LEU   A 269 ? 0.8142 0.6949 0.7865 -0.0073 -0.0198 0.0432  265 LEU   A CG  
2093 C CD1 . LEU   A 269 ? 0.7676 0.6642 0.7436 -0.0090 -0.0181 0.0445  265 LEU   A CD1 
2094 C CD2 . LEU   A 269 ? 0.7331 0.6320 0.7250 -0.0007 -0.0201 0.0379  265 LEU   A CD2 
2095 N N   . SER   A 270 ? 0.6512 0.5094 0.6152 -0.0304 -0.0148 0.0345  266 SER   A N   
2096 C CA  . SER   A 270 ? 0.6807 0.5447 0.6543 -0.0266 -0.0159 0.0291  266 SER   A CA  
2097 C C   . SER   A 270 ? 0.6891 0.5219 0.6461 -0.0236 -0.0186 0.0287  266 SER   A C   
2098 O O   . SER   A 270 ? 0.5868 0.4197 0.5493 -0.0128 -0.0210 0.0252  266 SER   A O   
2099 C CB  . SER   A 270 ? 0.6451 0.5287 0.6279 -0.0390 -0.0125 0.0245  266 SER   A CB  
2100 O OG  . SER   A 270 ? 0.8343 0.7191 0.8214 -0.0368 -0.0140 0.0196  266 SER   A OG  
2101 N N   . ARG   A 271 ? 0.5827 0.3871 0.5176 -0.0333 -0.0181 0.0318  267 ARG   A N   
2102 C CA  . ARG   A 271 ? 0.6760 0.4448 0.5914 -0.0294 -0.0215 0.0313  267 ARG   A CA  
2103 C C   . ARG   A 271 ? 0.7610 0.5186 0.6736 -0.0090 -0.0274 0.0328  267 ARG   A C   
2104 O O   . ARG   A 271 ? 0.7273 0.4745 0.6386 0.0022  -0.0306 0.0285  267 ARG   A O   
2105 C CB  . ARG   A 271 ? 0.7518 0.4877 0.6396 -0.0452 -0.0197 0.0353  267 ARG   A CB  
2106 C CG  . ARG   A 271 ? 0.8407 0.5304 0.7016 -0.0386 -0.0247 0.0364  267 ARG   A CG  
2107 C CD  . ARG   A 271 ? 0.9763 0.6284 0.8052 -0.0561 -0.0227 0.0416  267 ARG   A CD  
2108 N NE  . ARG   A 271 ? 1.1058 0.7504 0.9225 -0.0560 -0.0233 0.0499  267 ARG   A NE  
2109 C CZ  . ARG   A 271 ? 1.3826 0.9867 1.1708 -0.0470 -0.0294 0.0562  267 ARG   A CZ  
2110 N NH1 . ARG   A 271 ? 1.3382 0.9049 1.1079 -0.0363 -0.0354 0.0546  267 ARG   A NH1 
2111 N NH2 . ARG   A 271 ? 1.4291 1.0291 1.2061 -0.0477 -0.0300 0.0636  267 ARG   A NH2 
2112 N N   . ALA   A 272 ? 0.6884 0.4508 0.6009 -0.0036 -0.0292 0.0379  268 ALA   A N   
2113 C CA  . ALA   A 272 ? 0.8084 0.5639 0.7192 0.0159  -0.0357 0.0385  268 ALA   A CA  
2114 C C   . ALA   A 272 ? 0.6590 0.4447 0.5952 0.0281  -0.0360 0.0321  268 ALA   A C   
2115 O O   . ALA   A 272 ? 0.6438 0.4257 0.5808 0.0443  -0.0408 0.0290  268 ALA   A O   
2116 C CB  . ALA   A 272 ? 0.5999 0.3565 0.5049 0.0173  -0.0376 0.0450  268 ALA   A CB  
2117 N N   . LEU   A 273 ? 0.5762 0.3916 0.5318 0.0208  -0.0310 0.0297  269 LEU   A N   
2118 C CA  . LEU   A 273 ? 0.5969 0.4370 0.5723 0.0295  -0.0303 0.0241  269 LEU   A CA  
2119 C C   . LEU   A 273 ? 0.7025 0.5354 0.6765 0.0309  -0.0297 0.0181  269 LEU   A C   
2120 O O   . LEU   A 273 ? 0.6079 0.4495 0.5899 0.0420  -0.0305 0.0128  269 LEU   A O   
2121 C CB  . LEU   A 273 ? 0.5648 0.4339 0.5571 0.0222  -0.0262 0.0243  269 LEU   A CB  
2122 C CG  . LEU   A 273 ? 0.7158 0.6012 0.7168 0.0267  -0.0270 0.0267  269 LEU   A CG  
2123 C CD1 . LEU   A 273 ? 0.6514 0.5572 0.6632 0.0183  -0.0233 0.0274  269 LEU   A CD1 
2124 C CD2 . LEU   A 273 ? 0.4899 0.3880 0.5017 0.0389  -0.0288 0.0225  269 LEU   A CD2 
2125 N N   . ARG   A 274 ? 0.5971 0.4160 0.5610 0.0190  -0.0278 0.0179  270 ARG   A N   
2126 C CA  . ARG   A 274 ? 0.7307 0.5403 0.6907 0.0196  -0.0275 0.0117  270 ARG   A CA  
2127 C C   . ARG   A 274 ? 0.7350 0.5148 0.6790 0.0314  -0.0319 0.0095  270 ARG   A C   
2128 O O   . ARG   A 274 ? 0.7981 0.5770 0.7437 0.0398  -0.0322 0.0025  270 ARG   A O   
2129 C CB  . ARG   A 274 ? 0.6816 0.4852 0.6349 0.0025  -0.0248 0.0111  270 ARG   A CB  
2130 C CG  . ARG   A 274 ? 0.6556 0.4894 0.6247 -0.0071 -0.0216 0.0120  270 ARG   A CG  
2131 C CD  . ARG   A 274 ? 0.7905 0.6252 0.7566 -0.0219 -0.0199 0.0086  270 ARG   A CD  
2132 N NE  . ARG   A 274 ? 0.8893 0.7081 0.8417 -0.0360 -0.0184 0.0114  270 ARG   A NE  
2133 C CZ  . ARG   A 274 ? 0.8238 0.6104 0.7555 -0.0428 -0.0188 0.0106  270 ARG   A CZ  
2134 N NH1 . ARG   A 274 ? 0.9048 0.6725 0.8284 -0.0348 -0.0212 0.0064  270 ARG   A NH1 
2135 N NH2 . ARG   A 274 ? 0.9721 0.7444 0.8898 -0.0583 -0.0164 0.0136  270 ARG   A NH2 
2136 N N   . GLN   A 275 ? 0.7212 0.4755 0.6479 0.0331  -0.0355 0.0150  271 GLN   A N   
2137 C CA  . GLN   A 275 ? 0.7378 0.4601 0.6465 0.0471  -0.0415 0.0131  271 GLN   A CA  
2138 C C   . GLN   A 275 ? 0.7212 0.4617 0.6437 0.0678  -0.0453 0.0091  271 GLN   A C   
2139 O O   . GLN   A 275 ? 0.8986 0.6291 0.8175 0.0826  -0.0488 0.0022  271 GLN   A O   
2140 C CB  . GLN   A 275 ? 0.6911 0.3769 0.5728 0.0423  -0.0449 0.0210  271 GLN   A CB  
2141 C CG  . GLN   A 275 ? 0.8913 0.5436 0.7498 0.0255  -0.0427 0.0220  271 GLN   A CG  
2142 C CD  . GLN   A 275 ? 1.0665 0.6830 0.8961 0.0171  -0.0446 0.0309  271 GLN   A CD  
2143 O OE1 . GLN   A 275 ? 0.9241 0.5310 0.7454 0.0292  -0.0501 0.0358  271 GLN   A OE1 
2144 N NE2 . GLN   A 275 ? 1.2352 0.8324 1.0483 -0.0048 -0.0401 0.0326  271 GLN   A NE2 
2145 N N   . ALA   A 276 ? 0.7581 0.5269 0.6968 0.0690  -0.0447 0.0121  272 ALA   A N   
2146 C CA  . ALA   A 276 ? 0.7828 0.5713 0.7348 0.0867  -0.0486 0.0079  272 ALA   A CA  
2147 C C   . ALA   A 276 ? 0.7369 0.5563 0.7103 0.0905  -0.0441 -0.0011 272 ALA   A C   
2148 O O   . ALA   A 276 ? 0.7982 0.6303 0.7802 0.1061  -0.0468 -0.0082 272 ALA   A O   
2149 C CB  . ALA   A 276 ? 0.7286 0.5354 0.6887 0.0849  -0.0494 0.0137  272 ALA   A CB  
2150 N N   . LEU   A 277 ? 0.6487 0.4812 0.6299 0.0767  -0.0374 -0.0014 273 LEU   A N   
2151 C CA  . LEU   A 277 ? 0.7199 0.5800 0.7178 0.0777  -0.0325 -0.0086 273 LEU   A CA  
2152 C C   . LEU   A 277 ? 0.6298 0.4812 0.6219 0.0725  -0.0292 -0.0135 273 LEU   A C   
2153 O O   . LEU   A 277 ? 0.8173 0.6876 0.8192 0.0747  -0.0253 -0.0203 273 LEU   A O   
2154 C CB  . LEU   A 277 ? 0.7558 0.6428 0.7683 0.0674  -0.0281 -0.0048 273 LEU   A CB  
2155 C CG  . LEU   A 277 ? 0.6716 0.5768 0.6948 0.0722  -0.0299 -0.0029 273 LEU   A CG  
2156 C CD1 . LEU   A 277 ? 0.4982 0.4220 0.5310 0.0606  -0.0255 0.0009  273 LEU   A CD1 
2157 C CD2 . LEU   A 277 ? 0.5229 0.4470 0.5574 0.0851  -0.0304 -0.0116 273 LEU   A CD2 
2158 N N   . GLY   A 278 ? 0.7305 0.5545 0.7061 0.0644  -0.0304 -0.0107 274 GLY   A N   
2159 C CA  . GLY   A 278 ? 0.6313 0.4507 0.6024 0.0564  -0.0272 -0.0152 274 GLY   A CA  
2160 C C   . GLY   A 278 ? 0.7415 0.5851 0.7240 0.0441  -0.0227 -0.0134 274 GLY   A C   
2161 O O   . GLY   A 278 ? 0.6872 0.5321 0.6674 0.0387  -0.0205 -0.0178 274 GLY   A O   
2162 N N   . VAL   A 279 ? 0.7196 0.5808 0.7126 0.0406  -0.0220 -0.0075 275 VAL   A N   
2163 C CA  . VAL   A 279 ? 0.6226 0.5043 0.6247 0.0314  -0.0190 -0.0057 275 VAL   A CA  
2164 C C   . VAL   A 279 ? 0.6119 0.4862 0.6078 0.0187  -0.0196 -0.0027 275 VAL   A C   
2165 O O   . VAL   A 279 ? 0.6868 0.5450 0.6742 0.0144  -0.0213 0.0006  275 VAL   A O   
2166 C CB  . VAL   A 279 ? 0.6113 0.5124 0.6256 0.0334  -0.0183 -0.0016 275 VAL   A CB  
2167 C CG1 . VAL   A 279 ? 0.5747 0.4685 0.5863 0.0307  -0.0207 0.0048  275 VAL   A CG1 
2168 C CG2 . VAL   A 279 ? 0.6909 0.6099 0.7122 0.0270  -0.0157 -0.0007 275 VAL   A CG2 
2169 N N   . SER   A 280 ? 0.6834 0.5699 0.6826 0.0122  -0.0184 -0.0045 276 SER   A N   
2170 C CA  . SER   A 280 ? 0.5758 0.4632 0.5728 0.0004  -0.0193 -0.0036 276 SER   A CA  
2171 C C   . SER   A 280 ? 0.6304 0.5405 0.6372 -0.0025 -0.0195 -0.0021 276 SER   A C   
2172 O O   . SER   A 280 ? 0.5421 0.4591 0.5506 -0.0108 -0.0207 -0.0019 276 SER   A O   
2173 C CB  . SER   A 280 ? 0.6359 0.5101 0.6222 -0.0049 -0.0199 -0.0094 276 SER   A CB  
2174 O OG  . SER   A 280 ? 0.6370 0.5211 0.6247 -0.0019 -0.0193 -0.0137 276 SER   A OG  
2175 N N   . LEU   A 281 ? 0.6072 0.5285 0.6196 0.0039  -0.0185 -0.0015 277 LEU   A N   
2176 C CA  . LEU   A 281 ? 0.5790 0.5162 0.5970 0.0030  -0.0195 0.0006  277 LEU   A CA  
2177 C C   . LEU   A 281 ? 0.6565 0.5997 0.6814 0.0078  -0.0182 0.0047  277 LEU   A C   
2178 O O   . LEU   A 281 ? 0.5830 0.5275 0.6084 0.0124  -0.0159 0.0042  277 LEU   A O   
2179 C CB  . LEU   A 281 ? 0.5972 0.5374 0.6100 0.0041  -0.0196 -0.0022 277 LEU   A CB  
2180 C CG  . LEU   A 281 ? 0.5997 0.5385 0.6056 -0.0009 -0.0222 -0.0066 277 LEU   A CG  
2181 C CD1 . LEU   A 281 ? 0.6390 0.5888 0.6495 -0.0060 -0.0265 -0.0063 277 LEU   A CD1 
2182 C CD2 . LEU   A 281 ? 0.8289 0.7530 0.8278 -0.0029 -0.0209 -0.0113 277 LEU   A CD2 
2183 N N   . PHE   A 282 ? 0.5141 0.4622 0.5440 0.0059  -0.0191 0.0079  278 PHE   A N   
2184 C CA  . PHE   A 282 ? 0.6038 0.5567 0.6393 0.0100  -0.0181 0.0112  278 PHE   A CA  
2185 C C   . PHE   A 282 ? 0.5314 0.4930 0.5717 0.0073  -0.0193 0.0134  278 PHE   A C   
2186 O O   . PHE   A 282 ? 0.4820 0.4474 0.5226 0.0020  -0.0204 0.0120  278 PHE   A O   
2187 C CB  . PHE   A 282 ? 0.5676 0.5118 0.6020 0.0137  -0.0172 0.0118  278 PHE   A CB  
2188 C CG  . PHE   A 282 ? 0.4590 0.3921 0.4881 0.0099  -0.0182 0.0133  278 PHE   A CG  
2189 C CD1 . PHE   A 282 ? 0.5696 0.4887 0.5900 0.0066  -0.0187 0.0108  278 PHE   A CD1 
2190 C CD2 . PHE   A 282 ? 0.4668 0.4010 0.4968 0.0086  -0.0184 0.0170  278 PHE   A CD2 
2191 C CE1 . PHE   A 282 ? 0.5831 0.4875 0.5947 0.0010  -0.0191 0.0126  278 PHE   A CE1 
2192 C CE2 . PHE   A 282 ? 0.5161 0.4375 0.5374 0.0031  -0.0186 0.0190  278 PHE   A CE2 
2193 C CZ  . PHE   A 282 ? 0.6370 0.5422 0.6483 -0.0012 -0.0189 0.0170  278 PHE   A CZ  
2194 N N   . GLY   A 283 ? 0.5109 0.4773 0.5553 0.0106  -0.0188 0.0157  279 GLY   A N   
2195 C CA  . GLY   A 283 ? 0.6226 0.5978 0.6716 0.0096  -0.0194 0.0168  279 GLY   A CA  
2196 C C   . GLY   A 283 ? 0.5433 0.5173 0.5937 0.0111  -0.0182 0.0194  279 GLY   A C   
2197 O O   . GLY   A 283 ? 0.5266 0.4972 0.5768 0.0148  -0.0176 0.0200  279 GLY   A O   
2198 N N   . ILE   A 284 ? 0.5490 0.5277 0.6005 0.0077  -0.0177 0.0201  280 ILE   A N   
2199 C CA  . ILE   A 284 ? 0.4584 0.4358 0.5089 0.0084  -0.0169 0.0226  280 ILE   A CA  
2200 C C   . ILE   A 284 ? 0.4418 0.4313 0.4973 0.0091  -0.0165 0.0215  280 ILE   A C   
2201 O O   . ILE   A 284 ? 0.4507 0.4502 0.5093 0.0060  -0.0161 0.0191  280 ILE   A O   
2202 C CB  . ILE   A 284 ? 0.5171 0.4850 0.5598 0.0027  -0.0160 0.0247  280 ILE   A CB  
2203 C CG1 . ILE   A 284 ? 0.6211 0.5754 0.6574 0.0013  -0.0166 0.0241  280 ILE   A CG1 
2204 C CG2 . ILE   A 284 ? 0.5341 0.4956 0.5718 0.0057  -0.0166 0.0279  280 ILE   A CG2 
2205 C CD1 . ILE   A 284 ? 0.6517 0.5904 0.6758 -0.0055 -0.0159 0.0264  280 ILE   A CD1 
2206 N N   . ASP   A 285 ? 0.4179 0.4078 0.4744 0.0133  -0.0168 0.0222  281 ASP   A N   
2207 C CA  . ASP   A 285 ? 0.4850 0.4832 0.5443 0.0149  -0.0166 0.0207  281 ASP   A CA  
2208 C C   . ASP   A 285 ? 0.4243 0.4237 0.4805 0.0120  -0.0151 0.0221  281 ASP   A C   
2209 O O   . ASP   A 285 ? 0.5541 0.5470 0.6066 0.0131  -0.0158 0.0246  281 ASP   A O   
2210 C CB  . ASP   A 285 ? 0.4404 0.4357 0.4998 0.0192  -0.0176 0.0201  281 ASP   A CB  
2211 C CG  . ASP   A 285 ? 0.7484 0.7400 0.8065 0.0213  -0.0190 0.0191  281 ASP   A CG  
2212 O OD1 . ASP   A 285 ? 0.6481 0.6434 0.7073 0.0214  -0.0202 0.0178  281 ASP   A OD1 
2213 O OD2 . ASP   A 285 ? 0.8008 0.7859 0.8557 0.0220  -0.0189 0.0194  281 ASP   A OD2 
2214 N N   . ILE   A 286 ? 0.3877 0.3969 0.4451 0.0084  -0.0131 0.0201  282 ILE   A N   
2215 C CA  . ILE   A 286 ? 0.4166 0.4264 0.4680 0.0034  -0.0106 0.0217  282 ILE   A CA  
2216 C C   . ILE   A 286 ? 0.3745 0.3980 0.4298 0.0050  -0.0089 0.0175  282 ILE   A C   
2217 O O   . ILE   A 286 ? 0.4212 0.4575 0.4841 0.0071  -0.0087 0.0125  282 ILE   A O   
2218 C CB  . ILE   A 286 ? 0.3652 0.3734 0.4115 -0.0061 -0.0079 0.0227  282 ILE   A CB  
2219 C CG1 . ILE   A 286 ? 0.4655 0.4544 0.5035 -0.0067 -0.0099 0.0271  282 ILE   A CG1 
2220 C CG2 . ILE   A 286 ? 0.4843 0.4957 0.5228 -0.0134 -0.0040 0.0234  282 ILE   A CG2 
2221 C CD1 . ILE   A 286 ? 0.3679 0.3494 0.3976 -0.0172 -0.0075 0.0280  282 ILE   A CD1 
2222 N N   . ILE   A 287 ? 0.3321 0.3534 0.3816 0.0051  -0.0084 0.0188  283 ILE   A N   
2223 C CA  . ILE   A 287 ? 0.4474 0.4806 0.4982 0.0060  -0.0061 0.0143  283 ILE   A CA  
2224 C C   . ILE   A 287 ? 0.4088 0.4420 0.4491 -0.0020 -0.0026 0.0166  283 ILE   A C   
2225 O O   . ILE   A 287 ? 0.4474 0.4663 0.4771 -0.0055 -0.0037 0.0226  283 ILE   A O   
2226 C CB  . ILE   A 287 ? 0.4034 0.4329 0.4547 0.0130  -0.0089 0.0126  283 ILE   A CB  
2227 C CG1 . ILE   A 287 ? 0.3021 0.3203 0.3466 0.0126  -0.0113 0.0174  283 ILE   A CG1 
2228 C CG2 . ILE   A 287 ? 0.3888 0.4154 0.4463 0.0193  -0.0117 0.0105  283 ILE   A CG2 
2229 C CD1 . ILE   A 287 ? 0.3169 0.3338 0.3612 0.0164  -0.0134 0.0148  283 ILE   A CD1 
2230 N N   . ILE   A 288 ? 0.3625 0.4108 0.4039 -0.0042 0.0016  0.0114  284 ILE   A N   
2231 C CA  . ILE   A 288 ? 0.3276 0.3774 0.3570 -0.0135 0.0063  0.0130  284 ILE   A CA  
2232 C C   . ILE   A 288 ? 0.3936 0.4421 0.4167 -0.0096 0.0054  0.0121  284 ILE   A C   
2233 O O   . ILE   A 288 ? 0.3611 0.4222 0.3911 -0.0043 0.0064  0.0051  284 ILE   A O   
2234 C CB  . ILE   A 288 ? 0.5586 0.6302 0.5934 -0.0211 0.0130  0.0064  284 ILE   A CB  
2235 C CG1 . ILE   A 288 ? 0.4760 0.5495 0.5165 -0.0266 0.0135  0.0067  284 ILE   A CG1 
2236 C CG2 . ILE   A 288 ? 0.3905 0.4630 0.4099 -0.0328 0.0192  0.0080  284 ILE   A CG2 
2237 C CD1 . ILE   A 288 ? 0.4267 0.4775 0.4515 -0.0360 0.0135  0.0153  284 ILE   A CD1 
2238 N N   . ASN   A 289 ? 0.4050 0.4374 0.4139 -0.0112 0.0027  0.0188  285 ASN   A N   
2239 C CA  . ASN   A 289 ? 0.3981 0.4292 0.3984 -0.0089 0.0012  0.0184  285 ASN   A CA  
2240 C C   . ASN   A 289 ? 0.4787 0.5241 0.4738 -0.0150 0.0081  0.0133  285 ASN   A C   
2241 O O   . ASN   A 289 ? 0.3480 0.3908 0.3293 -0.0253 0.0126  0.0167  285 ASN   A O   
2242 C CB  . ASN   A 289 ? 0.4335 0.4458 0.4176 -0.0097 -0.0035 0.0266  285 ASN   A CB  
2243 C CG  . ASN   A 289 ? 0.5796 0.5908 0.5582 -0.0045 -0.0082 0.0257  285 ASN   A CG  
2244 O OD1 . ASN   A 289 ? 0.5463 0.5675 0.5233 -0.0054 -0.0054 0.0206  285 ASN   A OD1 
2245 N ND2 . ASN   A 289 ? 0.4871 0.4879 0.4634 0.0012  -0.0155 0.0297  285 ASN   A ND2 
2246 N N   . ASN   A 290 ? 0.3443 0.4034 0.3484 -0.0091 0.0093  0.0049  286 ASN   A N   
2247 C CA  . ASN   A 290 ? 0.4920 0.5685 0.4935 -0.0130 0.0162  -0.0024 286 ASN   A CA  
2248 C C   . ASN   A 290 ? 0.5999 0.6701 0.5818 -0.0180 0.0172  0.0002  286 ASN   A C   
2249 O O   . ASN   A 290 ? 0.5532 0.6370 0.5303 -0.0212 0.0230  -0.0061 286 ASN   A O   
2250 C CB  . ASN   A 290 ? 0.3987 0.4876 0.4139 -0.0024 0.0158  -0.0128 286 ASN   A CB  
2251 C CG  . ASN   A 290 ? 0.4725 0.5505 0.4826 0.0043  0.0108  -0.0141 286 ASN   A CG  
2252 O OD1 . ASN   A 290 ? 0.4398 0.5031 0.4415 0.0030  0.0061  -0.0073 286 ASN   A OD1 
2253 N ND2 . ASN   A 290 ? 0.4812 0.5670 0.4964 0.0117  0.0115  -0.0238 286 ASN   A ND2 
2254 N N   . GLN   A 291 ? 0.5536 0.6041 0.5241 -0.0177 0.0109  0.0091  287 GLN   A N   
2255 C CA  . GLN   A 291 ? 0.6778 0.7196 0.6300 -0.0187 0.0080  0.0120  287 GLN   A CA  
2256 C C   . GLN   A 291 ? 0.7972 0.8199 0.7280 -0.0253 0.0060  0.0228  287 GLN   A C   
2257 O O   . GLN   A 291 ? 0.9619 0.9764 0.8725 -0.0274 0.0040  0.0260  287 GLN   A O   
2258 C CB  . GLN   A 291 ? 0.7827 0.8203 0.7420 -0.0086 -0.0001 0.0102  287 GLN   A CB  
2259 C CG  . GLN   A 291 ? 1.0956 1.1244 1.0398 -0.0070 -0.0067 0.0132  287 GLN   A CG  
2260 C CD  . GLN   A 291 ? 1.1811 1.2141 1.1073 -0.0125 -0.0028 0.0109  287 GLN   A CD  
2261 O OE1 . GLN   A 291 ? 1.2686 1.2905 1.1735 -0.0163 -0.0053 0.0177  287 GLN   A OE1 
2262 N NE2 . GLN   A 291 ? 1.0535 1.1010 0.9861 -0.0122 0.0029  0.0011  287 GLN   A NE2 
2263 N N   . THR   A 292 ? 0.7883 0.8014 0.7208 -0.0282 0.0060  0.0282  288 THR   A N   
2264 C CA  . THR   A 292 ? 0.7380 0.7316 0.6474 -0.0377 0.0070  0.0371  288 THR   A CA  
2265 C C   . THR   A 292 ? 0.5851 0.5820 0.4985 -0.0483 0.0145  0.0369  288 THR   A C   
2266 O O   . THR   A 292 ? 0.6813 0.6632 0.5727 -0.0605 0.0182  0.0428  288 THR   A O   
2267 C CB  . THR   A 292 ? 0.6824 0.6519 0.5828 -0.0298 -0.0035 0.0455  288 THR   A CB  
2268 O OG1 . THR   A 292 ? 0.5657 0.5371 0.4869 -0.0230 -0.0063 0.0441  288 THR   A OG1 
2269 C CG2 . THR   A 292 ? 0.7476 0.7158 0.6429 -0.0202 -0.0117 0.0454  288 THR   A CG2 
2270 N N   . GLY   A 293 ? 0.6807 0.6956 0.6194 -0.0448 0.0164  0.0301  289 GLY   A N   
2271 C CA  . GLY   A 293 ? 0.4082 0.4291 0.3532 -0.0541 0.0222  0.0287  289 GLY   A CA  
2272 C C   . GLY   A 293 ? 0.5644 0.5669 0.5113 -0.0516 0.0168  0.0344  289 GLY   A C   
2273 O O   . GLY   A 293 ? 0.5442 0.5511 0.4967 -0.0595 0.0208  0.0329  289 GLY   A O   
2274 N N   . GLN   A 294 ? 0.4269 0.4116 0.3705 -0.0407 0.0079  0.0397  290 GLN   A N   
2275 C CA  . GLN   A 294 ? 0.4340 0.3988 0.3755 -0.0378 0.0028  0.0450  290 GLN   A CA  
2276 C C   . GLN   A 294 ? 0.4710 0.4488 0.4375 -0.0305 0.0013  0.0398  290 GLN   A C   
2277 O O   . GLN   A 294 ? 0.3458 0.3424 0.3293 -0.0240 0.0014  0.0336  290 GLN   A O   
2278 C CB  . GLN   A 294 ? 0.5147 0.4588 0.4432 -0.0278 -0.0064 0.0512  290 GLN   A CB  
2279 C CG  . GLN   A 294 ? 0.5931 0.5155 0.4907 -0.0339 -0.0071 0.0584  290 GLN   A CG  
2280 C CD  . GLN   A 294 ? 0.6826 0.5933 0.5706 -0.0211 -0.0174 0.0621  290 GLN   A CD  
2281 O OE1 . GLN   A 294 ? 0.6940 0.6222 0.5967 -0.0126 -0.0205 0.0572  290 GLN   A OE1 
2282 N NE2 . GLN   A 294 ? 0.6212 0.5019 0.4838 -0.0195 -0.0232 0.0701  290 GLN   A NE2 
2283 N N   . HIS   A 295 ? 0.4075 0.3721 0.3732 -0.0316 -0.0004 0.0426  291 HIS   A N   
2284 C CA  . HIS   A 295 ? 0.4939 0.4662 0.4789 -0.0247 -0.0026 0.0389  291 HIS   A CA  
2285 C C   . HIS   A 295 ? 0.4766 0.4429 0.4663 -0.0116 -0.0098 0.0402  291 HIS   A C   
2286 O O   . HIS   A 295 ? 0.5881 0.5360 0.5653 -0.0077 -0.0146 0.0451  291 HIS   A O   
2287 C CB  . HIS   A 295 ? 0.4896 0.4498 0.4705 -0.0313 -0.0017 0.0407  291 HIS   A CB  
2288 C CG  . HIS   A 295 ? 0.4490 0.4213 0.4303 -0.0455 0.0057  0.0372  291 HIS   A CG  
2289 N ND1 . HIS   A 295 ? 0.5088 0.4812 0.4755 -0.0578 0.0115  0.0383  291 HIS   A ND1 
2290 C CD2 . HIS   A 295 ? 0.4351 0.4223 0.4297 -0.0500 0.0083  0.0317  291 HIS   A CD2 
2291 C CE1 . HIS   A 295 ? 0.3872 0.3762 0.3600 -0.0701 0.0181  0.0331  291 HIS   A CE1 
2292 N NE2 . HIS   A 295 ? 0.5521 0.5509 0.5423 -0.0650 0.0156  0.0288  291 HIS   A NE2 
2293 N N   . ALA   A 296 ? 0.5110 0.4926 0.5175 -0.0049 -0.0106 0.0352  292 ALA   A N   
2294 C CA  . ALA   A 296 ? 0.5583 0.5386 0.5708 0.0047  -0.0159 0.0348  292 ALA   A CA  
2295 C C   . ALA   A 296 ? 0.5263 0.5089 0.5512 0.0080  -0.0164 0.0326  292 ALA   A C   
2296 O O   . ALA   A 296 ? 0.4884 0.4818 0.5233 0.0079  -0.0143 0.0286  292 ALA   A O   
2297 C CB  . ALA   A 296 ? 0.3653 0.3575 0.3826 0.0077  -0.0161 0.0311  292 ALA   A CB  
2298 N N   . VAL   A 297 ? 0.4265 0.3981 0.4492 0.0118  -0.0197 0.0347  293 VAL   A N   
2299 C CA  . VAL   A 297 ? 0.4575 0.4311 0.4901 0.0150  -0.0201 0.0323  293 VAL   A CA  
2300 C C   . VAL   A 297 ? 0.5195 0.5014 0.5604 0.0205  -0.0220 0.0294  293 VAL   A C   
2301 O O   . VAL   A 297 ? 0.6062 0.5876 0.6455 0.0251  -0.0255 0.0297  293 VAL   A O   
2302 C CB  . VAL   A 297 ? 0.5798 0.5388 0.6061 0.0167  -0.0221 0.0344  293 VAL   A CB  
2303 C CG1 . VAL   A 297 ? 0.4768 0.4395 0.5127 0.0200  -0.0220 0.0312  293 VAL   A CG1 
2304 C CG2 . VAL   A 297 ? 0.5566 0.5052 0.5728 0.0084  -0.0196 0.0369  293 VAL   A CG2 
2305 N N   . ILE   A 298 ? 0.4553 0.4447 0.5041 0.0198  -0.0200 0.0263  294 ILE   A N   
2306 C CA  . ILE   A 298 ? 0.4595 0.4548 0.5135 0.0217  -0.0207 0.0234  294 ILE   A CA  
2307 C C   . ILE   A 298 ? 0.6072 0.6024 0.6660 0.0225  -0.0201 0.0216  294 ILE   A C   
2308 O O   . ILE   A 298 ? 0.5039 0.5044 0.5663 0.0225  -0.0203 0.0189  294 ILE   A O   
2309 C CB  . ILE   A 298 ? 0.5703 0.5692 0.6250 0.0201  -0.0191 0.0210  294 ILE   A CB  
2310 C CG1 . ILE   A 298 ? 0.3401 0.3388 0.3959 0.0195  -0.0174 0.0205  294 ILE   A CG1 
2311 C CG2 . ILE   A 298 ? 0.4422 0.4442 0.4923 0.0195  -0.0195 0.0210  294 ILE   A CG2 
2312 C CD1 . ILE   A 298 ? 0.3979 0.3982 0.4541 0.0212  -0.0171 0.0171  294 ILE   A CD1 
2313 N N   . ASP   A 299 ? 0.5909 0.5815 0.6494 0.0220  -0.0191 0.0224  295 ASP   A N   
2314 C CA  . ASP   A 299 ? 0.5430 0.5333 0.6040 0.0222  -0.0179 0.0206  295 ASP   A CA  
2315 C C   . ASP   A 299 ? 0.5746 0.5586 0.6332 0.0223  -0.0178 0.0216  295 ASP   A C   
2316 O O   . ASP   A 299 ? 0.5719 0.5529 0.6278 0.0202  -0.0180 0.0232  295 ASP   A O   
2317 C CB  . ASP   A 299 ? 0.4674 0.4569 0.5275 0.0196  -0.0163 0.0193  295 ASP   A CB  
2318 C CG  . ASP   A 299 ? 0.6825 0.6756 0.7435 0.0174  -0.0156 0.0170  295 ASP   A CG  
2319 O OD1 . ASP   A 299 ? 0.4324 0.4327 0.4976 0.0172  -0.0152 0.0148  295 ASP   A OD1 
2320 O OD2 . ASP   A 299 ? 0.6174 0.6067 0.6749 0.0160  -0.0156 0.0166  295 ASP   A OD2 
2321 N N   . ILE   A 300 ? 0.5547 0.5383 0.6145 0.0240  -0.0172 0.0196  296 ILE   A N   
2322 C CA  . ILE   A 300 ? 0.4200 0.3969 0.4767 0.0239  -0.0169 0.0193  296 ILE   A CA  
2323 C C   . ILE   A 300 ? 0.6030 0.5817 0.6596 0.0220  -0.0146 0.0171  296 ILE   A C   
2324 O O   . ILE   A 300 ? 0.6161 0.6007 0.6749 0.0212  -0.0127 0.0151  296 ILE   A O   
2325 C CB  . ILE   A 300 ? 0.4806 0.4521 0.5356 0.0289  -0.0185 0.0181  296 ILE   A CB  
2326 C CG1 . ILE   A 300 ? 0.5210 0.4882 0.5725 0.0315  -0.0216 0.0209  296 ILE   A CG1 
2327 C CG2 . ILE   A 300 ? 0.5426 0.5033 0.5918 0.0277  -0.0184 0.0177  296 ILE   A CG2 
2328 C CD1 . ILE   A 300 ? 0.6358 0.5923 0.6791 0.0265  -0.0217 0.0247  296 ILE   A CD1 
2329 N N   . ASN   A 301 ? 0.5779 0.5518 0.6305 0.0201  -0.0148 0.0173  297 ASN   A N   
2330 C CA  . ASN   A 301 ? 0.6524 0.6253 0.7010 0.0182  -0.0134 0.0161  297 ASN   A CA  
2331 C C   . ASN   A 301 ? 0.6649 0.6334 0.7100 0.0182  -0.0131 0.0138  297 ASN   A C   
2332 O O   . ASN   A 301 ? 0.5945 0.5590 0.6381 0.0173  -0.0151 0.0142  297 ASN   A O   
2333 C CB  . ASN   A 301 ? 0.6845 0.6561 0.7298 0.0172  -0.0155 0.0179  297 ASN   A CB  
2334 C CG  . ASN   A 301 ? 0.8168 0.7913 0.8652 0.0181  -0.0163 0.0193  297 ASN   A CG  
2335 O OD1 . ASN   A 301 ? 0.7815 0.7560 0.8295 0.0173  -0.0148 0.0192  297 ASN   A OD1 
2336 N ND2 . ASN   A 301 ? 0.7512 0.7294 0.8025 0.0187  -0.0182 0.0197  297 ASN   A ND2 
2337 N N   . ALA   A 302 ? 0.6274 0.5972 0.6705 0.0182  -0.0101 0.0108  298 ALA   A N   
2338 C CA  . ALA   A 302 ? 0.6586 0.6241 0.6971 0.0185  -0.0095 0.0076  298 ALA   A CA  
2339 C C   . ALA   A 302 ? 0.5343 0.4961 0.5643 0.0149  -0.0105 0.0085  298 ALA   A C   
2340 O O   . ALA   A 302 ? 0.6458 0.6076 0.6705 0.0126  -0.0091 0.0097  298 ALA   A O   
2341 C CB  . ALA   A 302 ? 0.6091 0.5805 0.6493 0.0205  -0.0053 0.0025  298 ALA   A CB  
2342 N N   . PHE   A 303 ? 0.5934 0.5508 0.6205 0.0141  -0.0132 0.0076  299 PHE   A N   
2343 C CA  . PHE   A 303 ? 0.5922 0.5480 0.6117 0.0119  -0.0160 0.0075  299 PHE   A CA  
2344 C C   . PHE   A 303 ? 0.6507 0.6077 0.6673 0.0125  -0.0181 0.0110  299 PHE   A C   
2345 O O   . PHE   A 303 ? 0.5817 0.5341 0.5886 0.0116  -0.0167 0.0118  299 PHE   A O   
2346 C CB  . PHE   A 303 ? 0.5931 0.5452 0.6038 0.0107  -0.0135 0.0038  299 PHE   A CB  
2347 C CG  . PHE   A 303 ? 0.6690 0.6187 0.6698 0.0088  -0.0173 0.0031  299 PHE   A CG  
2348 C CD1 . PHE   A 303 ? 0.7985 0.7516 0.8022 0.0082  -0.0228 0.0032  299 PHE   A CD1 
2349 C CD2 . PHE   A 303 ? 0.7726 0.7185 0.7609 0.0073  -0.0154 0.0016  299 PHE   A CD2 
2350 C CE1 . PHE   A 303 ? 0.8109 0.7649 0.8065 0.0074  -0.0275 0.0016  299 PHE   A CE1 
2351 C CE2 . PHE   A 303 ? 0.7524 0.6957 0.7298 0.0063  -0.0200 0.0011  299 PHE   A CE2 
2352 C CZ  . PHE   A 303 ? 0.7241 0.6720 0.7058 0.0070  -0.0267 0.0009  299 PHE   A CZ  
2353 N N   . PRO   A 304 ? 0.5916 0.5530 0.6144 0.0140  -0.0212 0.0129  300 PRO   A N   
2354 C CA  . PRO   A 304 ? 0.5223 0.4825 0.5417 0.0167  -0.0236 0.0156  300 PRO   A CA  
2355 C C   . PRO   A 304 ? 0.6288 0.5862 0.6385 0.0193  -0.0291 0.0155  300 PRO   A C   
2356 O O   . PRO   A 304 ? 0.6639 0.6207 0.6682 0.0178  -0.0305 0.0134  300 PRO   A O   
2357 C CB  . PRO   A 304 ? 0.5692 0.5373 0.5994 0.0183  -0.0248 0.0160  300 PRO   A CB  
2358 C CG  . PRO   A 304 ? 0.5919 0.5656 0.6279 0.0152  -0.0250 0.0136  300 PRO   A CG  
2359 C CD  . PRO   A 304 ? 0.5366 0.5032 0.5684 0.0130  -0.0220 0.0123  300 PRO   A CD  
2360 N N   . GLY   A 305 ? 0.6661 0.6208 0.6722 0.0242  -0.0331 0.0173  301 GLY   A N   
2361 C CA  . GLY   A 305 ? 0.7296 0.6802 0.7247 0.0295  -0.0402 0.0172  301 GLY   A CA  
2362 C C   . GLY   A 305 ? 0.6074 0.5745 0.6123 0.0330  -0.0462 0.0130  301 GLY   A C   
2363 O O   . GLY   A 305 ? 0.7320 0.6994 0.7289 0.0372  -0.0528 0.0115  301 GLY   A O   
2364 N N   . TYR   A 306 ? 0.5960 0.5776 0.6171 0.0307  -0.0439 0.0105  302 TYR   A N   
2365 C CA  . TYR   A 306 ? 0.6692 0.6706 0.7013 0.0313  -0.0480 0.0053  302 TYR   A CA  
2366 C C   . TYR   A 306 ? 0.8322 0.8396 0.8620 0.0423  -0.0566 0.0030  302 TYR   A C   
2367 O O   . TYR   A 306 ? 0.8246 0.8457 0.8569 0.0449  -0.0629 -0.0018 302 TYR   A O   
2368 C CB  . TYR   A 306 ? 0.6225 0.6281 0.6542 0.0246  -0.0483 0.0021  302 TYR   A CB  
2369 C CG  . TYR   A 306 ? 0.6000 0.5978 0.6327 0.0160  -0.0411 0.0032  302 TYR   A CG  
2370 C CD1 . TYR   A 306 ? 0.4493 0.4546 0.4917 0.0093  -0.0377 0.0014  302 TYR   A CD1 
2371 C CD2 . TYR   A 306 ? 0.5797 0.5622 0.6023 0.0149  -0.0377 0.0056  302 TYR   A CD2 
2372 C CE1 . TYR   A 306 ? 0.5049 0.4987 0.5451 0.0035  -0.0325 0.0026  302 TYR   A CE1 
2373 C CE2 . TYR   A 306 ? 0.5294 0.5053 0.5532 0.0098  -0.0322 0.0054  302 TYR   A CE2 
2374 C CZ  . TYR   A 306 ? 0.5383 0.5181 0.5701 0.0051  -0.0303 0.0042  302 TYR   A CZ  
2375 O OH  . TYR   A 306 ? 0.4521 0.4212 0.4820 0.0021  -0.0262 0.0042  302 TYR   A OH  
2376 N N   . GLU   A 307 ? 0.9257 0.9223 0.9501 0.0492  -0.0574 0.0059  303 GLU   A N   
2377 C CA  . GLU   A 307 ? 0.9789 0.9730 0.9958 0.0622  -0.0664 0.0045  303 GLU   A CA  
2378 C C   . GLU   A 307 ? 1.0100 1.0333 1.0435 0.0683  -0.0717 -0.0036 303 GLU   A C   
2379 O O   . GLU   A 307 ? 0.9682 1.0065 1.0160 0.0674  -0.0680 -0.0068 303 GLU   A O   
2380 C CB  . GLU   A 307 ? 1.0280 1.0036 1.0364 0.0670  -0.0652 0.0082  303 GLU   A CB  
2381 C CG  . GLU   A 307 ? 1.1342 1.1066 1.1362 0.0826  -0.0747 0.0055  303 GLU   A CG  
2382 C CD  . GLU   A 307 ? 1.1487 1.0929 1.1344 0.0861  -0.0740 0.0100  303 GLU   A CD  
2383 O OE1 . GLU   A 307 ? 0.9491 0.8818 0.9322 0.0753  -0.0656 0.0144  303 GLU   A OE1 
2384 O OE2 . GLU   A 307 ? 1.1599 1.0930 1.1346 0.0998  -0.0824 0.0086  303 GLU   A OE2 
2385 N N   . GLY   A 308 ? 0.9134 0.9469 0.9450 0.0741  -0.0802 -0.0078 304 GLY   A N   
2386 C CA  . GLY   A 308 ? 0.8484 0.9141 0.8966 0.0808  -0.0863 -0.0173 304 GLY   A CA  
2387 C C   . GLY   A 308 ? 0.8325 0.9258 0.9015 0.0674  -0.0791 -0.0228 304 GLY   A C   
2388 O O   . GLY   A 308 ? 0.8773 1.0018 0.9628 0.0702  -0.0817 -0.0317 304 GLY   A O   
2389 N N   . VAL   A 309 ? 0.8575 0.9395 0.9249 0.0528  -0.0701 -0.0180 305 VAL   A N   
2390 C CA  . VAL   A 309 ? 0.7592 0.8598 0.8404 0.0386  -0.0636 -0.0221 305 VAL   A CA  
2391 C C   . VAL   A 309 ? 0.6187 0.7448 0.7079 0.0359  -0.0692 -0.0308 305 VAL   A C   
2392 O O   . VAL   A 309 ? 0.6574 0.7770 0.7369 0.0382  -0.0752 -0.0307 305 VAL   A O   
2393 C CB  . VAL   A 309 ? 0.6507 0.7293 0.7242 0.0264  -0.0554 -0.0156 305 VAL   A CB  
2394 C CG1 . VAL   A 309 ? 0.6061 0.6975 0.6879 0.0114  -0.0503 -0.0196 305 VAL   A CG1 
2395 C CG2 . VAL   A 309 ? 0.7079 0.7711 0.7790 0.0274  -0.0495 -0.0094 305 VAL   A CG2 
2396 N N   . SER   A 310 ? 0.7294 0.8862 0.8358 0.0300  -0.0670 -0.0389 306 SER   A N   
2397 C CA  . SER   A 310 ? 0.5777 0.7652 0.6949 0.0254  -0.0718 -0.0492 306 SER   A CA  
2398 C C   . SER   A 310 ? 0.6202 0.7971 0.7307 0.0089  -0.0680 -0.0481 306 SER   A C   
2399 O O   . SER   A 310 ? 0.6672 0.8314 0.7754 -0.0052 -0.0586 -0.0444 306 SER   A O   
2400 C CB  . SER   A 310 ? 0.4813 0.7055 0.6187 0.0198  -0.0678 -0.0586 306 SER   A CB  
2401 O OG  . SER   A 310 ? 0.6236 0.8845 0.7744 0.0178  -0.0738 -0.0707 306 SER   A OG  
2402 N N   . GLU   A 311 ? 0.5500 0.7293 0.6549 0.0118  -0.0761 -0.0513 307 GLU   A N   
2403 C CA  . GLU   A 311 ? 0.6262 0.8017 0.7262 -0.0033 -0.0744 -0.0537 307 GLU   A CA  
2404 C C   . GLU   A 311 ? 0.6220 0.7580 0.7043 -0.0079 -0.0683 -0.0440 307 GLU   A C   
2405 O O   . GLU   A 311 ? 0.5967 0.7228 0.6750 -0.0227 -0.0626 -0.0446 307 GLU   A O   
2406 C CB  . GLU   A 311 ? 0.6257 0.8250 0.7396 -0.0220 -0.0677 -0.0615 307 GLU   A CB  
2407 C CG  . GLU   A 311 ? 0.8110 1.0251 0.9263 -0.0353 -0.0704 -0.0704 307 GLU   A CG  
2408 C CD  . GLU   A 311 ? 0.8754 1.1188 1.0056 -0.0542 -0.0642 -0.0796 307 GLU   A CD  
2409 O OE1 . GLU   A 311 ? 0.7793 1.0516 0.9182 -0.0625 -0.0685 -0.0909 307 GLU   A OE1 
2410 O OE2 . GLU   A 311 ? 0.9395 1.1775 1.0717 -0.0616 -0.0548 -0.0760 307 GLU   A OE2 
2411 N N   . PHE   A 312 ? 0.5746 0.6878 0.6453 0.0046  -0.0697 -0.0359 308 PHE   A N   
2412 C CA  . PHE   A 312 ? 0.6159 0.6968 0.6726 0.0012  -0.0634 -0.0279 308 PHE   A CA  
2413 C C   . PHE   A 312 ? 0.5628 0.6328 0.6068 -0.0027 -0.0658 -0.0296 308 PHE   A C   
2414 O O   . PHE   A 312 ? 0.5526 0.6054 0.5902 -0.0118 -0.0596 -0.0282 308 PHE   A O   
2415 C CB  . PHE   A 312 ? 0.5960 0.6592 0.6447 0.0134  -0.0634 -0.0200 308 PHE   A CB  
2416 C CG  . PHE   A 312 ? 0.5761 0.6117 0.6098 0.0122  -0.0590 -0.0138 308 PHE   A CG  
2417 C CD1 . PHE   A 312 ? 0.5989 0.6218 0.6328 0.0042  -0.0506 -0.0113 308 PHE   A CD1 
2418 C CD2 . PHE   A 312 ? 0.6319 0.6546 0.6500 0.0193  -0.0634 -0.0111 308 PHE   A CD2 
2419 C CE1 . PHE   A 312 ? 0.6157 0.6180 0.6381 0.0043  -0.0466 -0.0075 308 PHE   A CE1 
2420 C CE2 . PHE   A 312 ? 0.6629 0.6643 0.6682 0.0169  -0.0581 -0.0068 308 PHE   A CE2 
2421 C CZ  . PHE   A 312 ? 0.5572 0.5506 0.5663 0.0099  -0.0496 -0.0057 308 PHE   A CZ  
2422 N N   . PHE   A 313 ? 0.5422 0.6208 0.5809 0.0049  -0.0752 -0.0327 309 PHE   A N   
2423 C CA  . PHE   A 313 ? 0.6335 0.7029 0.6587 0.0011  -0.0779 -0.0350 309 PHE   A CA  
2424 C C   . PHE   A 313 ? 0.5930 0.6718 0.6243 -0.0146 -0.0752 -0.0426 309 PHE   A C   
2425 O O   . PHE   A 313 ? 0.5245 0.5857 0.5444 -0.0219 -0.0719 -0.0432 309 PHE   A O   
2426 C CB  . PHE   A 313 ? 0.5538 0.6327 0.5714 0.0125  -0.0900 -0.0374 309 PHE   A CB  
2427 C CG  . PHE   A 313 ? 0.5514 0.6079 0.5517 0.0252  -0.0924 -0.0289 309 PHE   A CG  
2428 C CD1 . PHE   A 313 ? 0.5359 0.5697 0.5309 0.0244  -0.0833 -0.0208 309 PHE   A CD1 
2429 C CD2 . PHE   A 313 ? 0.5252 0.5828 0.5130 0.0373  -0.1040 -0.0291 309 PHE   A CD2 
2430 C CE1 . PHE   A 313 ? 0.5302 0.5432 0.5080 0.0330  -0.0845 -0.0135 309 PHE   A CE1 
2431 C CE2 . PHE   A 313 ? 0.5954 0.6277 0.5629 0.0470  -0.1058 -0.0207 309 PHE   A CE2 
2432 C CZ  . PHE   A 313 ? 0.5578 0.5679 0.5205 0.0435  -0.0954 -0.0130 309 PHE   A CZ  
2433 N N   . THR   A 314 ? 0.5358 0.6418 0.5839 -0.0208 -0.0761 -0.0493 310 THR   A N   
2434 C CA  . THR   A 314 ? 0.5201 0.6340 0.5724 -0.0388 -0.0728 -0.0569 310 THR   A CA  
2435 C C   . THR   A 314 ? 0.6349 0.7221 0.6815 -0.0494 -0.0618 -0.0519 310 THR   A C   
2436 O O   . THR   A 314 ? 0.5252 0.5964 0.5620 -0.0607 -0.0589 -0.0546 310 THR   A O   
2437 C CB  . THR   A 314 ? 0.5337 0.6864 0.6059 -0.0442 -0.0753 -0.0659 310 THR   A CB  
2438 O OG1 . THR   A 314 ? 0.7595 0.9372 0.8373 -0.0298 -0.0870 -0.0706 310 THR   A OG1 
2439 C CG2 . THR   A 314 ? 0.6915 0.8536 0.7659 -0.0652 -0.0725 -0.0750 310 THR   A CG2 
2440 N N   . ASP   A 315 ? 0.5488 0.6295 0.6000 -0.0453 -0.0564 -0.0451 311 ASP   A N   
2441 C CA  . ASP   A 315 ? 0.5482 0.6024 0.5922 -0.0527 -0.0476 -0.0398 311 ASP   A CA  
2442 C C   . ASP   A 315 ? 0.5642 0.5888 0.5928 -0.0469 -0.0462 -0.0353 311 ASP   A C   
2443 O O   . ASP   A 315 ? 0.5116 0.5129 0.5313 -0.0531 -0.0409 -0.0340 311 ASP   A O   
2444 C CB  . ASP   A 315 ? 0.5852 0.6412 0.6369 -0.0483 -0.0433 -0.0339 311 ASP   A CB  
2445 C CG  . ASP   A 315 ? 0.6025 0.6868 0.6686 -0.0570 -0.0421 -0.0394 311 ASP   A CG  
2446 O OD1 . ASP   A 315 ? 0.6874 0.7821 0.7550 -0.0720 -0.0413 -0.0466 311 ASP   A OD1 
2447 O OD2 . ASP   A 315 ? 0.7097 0.8066 0.7852 -0.0496 -0.0415 -0.0372 311 ASP   A OD2 
2448 N N   . LEU   A 316 ? 0.5388 0.5633 0.5626 -0.0350 -0.0508 -0.0335 312 LEU   A N   
2449 C CA  . LEU   A 316 ? 0.6046 0.6050 0.6144 -0.0304 -0.0482 -0.0303 312 LEU   A CA  
2450 C C   . LEU   A 316 ? 0.5880 0.5803 0.5871 -0.0380 -0.0493 -0.0369 312 LEU   A C   
2451 O O   . LEU   A 316 ? 0.6110 0.5812 0.6005 -0.0397 -0.0444 -0.0369 312 LEU   A O   
2452 C CB  . LEU   A 316 ? 0.7155 0.7160 0.7205 -0.0177 -0.0514 -0.0256 312 LEU   A CB  
2453 C CG  . LEU   A 316 ? 0.6252 0.6047 0.6179 -0.0135 -0.0466 -0.0220 312 LEU   A CG  
2454 C CD1 . LEU   A 316 ? 0.6745 0.6412 0.6710 -0.0146 -0.0390 -0.0189 312 LEU   A CD1 
2455 C CD2 . LEU   A 316 ? 0.5380 0.5163 0.5241 -0.0040 -0.0488 -0.0168 312 LEU   A CD2 
2456 N N   . LEU   A 317 ? 0.5918 0.6019 0.5920 -0.0417 -0.0561 -0.0436 313 LEU   A N   
2457 C CA  . LEU   A 317 ? 0.5809 0.5842 0.5715 -0.0519 -0.0569 -0.0514 313 LEU   A CA  
2458 C C   . LEU   A 317 ? 0.5822 0.5717 0.5723 -0.0655 -0.0509 -0.0537 313 LEU   A C   
2459 O O   . LEU   A 317 ? 0.6809 0.6451 0.6578 -0.0688 -0.0473 -0.0555 313 LEU   A O   
2460 C CB  . LEU   A 317 ? 0.6624 0.6915 0.6564 -0.0552 -0.0659 -0.0594 313 LEU   A CB  
2461 C CG  . LEU   A 317 ? 0.8114 0.8470 0.7965 -0.0445 -0.0742 -0.0597 313 LEU   A CG  
2462 C CD1 . LEU   A 317 ? 0.8173 0.8834 0.8098 -0.0476 -0.0841 -0.0685 313 LEU   A CD1 
2463 C CD2 . LEU   A 317 ? 0.6942 0.7061 0.6605 -0.0470 -0.0714 -0.0616 313 LEU   A CD2 
2464 N N   . ASN   A 318 ? 0.5624 0.5668 0.5646 -0.0737 -0.0496 -0.0544 314 ASN   A N   
2465 C CA  . ASN   A 318 ? 0.6611 0.6495 0.6585 -0.0891 -0.0439 -0.0563 314 ASN   A CA  
2466 C C   . ASN   A 318 ? 0.5767 0.5303 0.5627 -0.0839 -0.0380 -0.0495 314 ASN   A C   
2467 O O   . ASN   A 318 ? 0.6861 0.6134 0.6588 -0.0929 -0.0348 -0.0517 314 ASN   A O   
2468 C CB  . ASN   A 318 ? 0.5869 0.5982 0.5986 -0.0986 -0.0422 -0.0572 314 ASN   A CB  
2469 C CG  . ASN   A 318 ? 0.7464 0.7964 0.7712 -0.1038 -0.0485 -0.0664 314 ASN   A CG  
2470 O OD1 . ASN   A 318 ? 0.7403 0.7947 0.7601 -0.1080 -0.0534 -0.0738 314 ASN   A OD1 
2471 N ND2 . ASN   A 318 ? 0.8242 0.9040 0.8662 -0.1029 -0.0489 -0.0671 314 ASN   A ND2 
2472 N N   . HIS   A 319 ? 0.6575 0.6098 0.6475 -0.0690 -0.0370 -0.0420 315 HIS   A N   
2473 C CA  . HIS   A 319 ? 0.6630 0.5873 0.6441 -0.0619 -0.0325 -0.0371 315 HIS   A CA  
2474 C C   . HIS   A 319 ? 0.7165 0.6233 0.6844 -0.0573 -0.0326 -0.0413 315 HIS   A C   
2475 O O   . HIS   A 319 ? 0.5956 0.4754 0.5518 -0.0578 -0.0298 -0.0425 315 HIS   A O   
2476 C CB  . HIS   A 319 ? 0.5666 0.4985 0.5567 -0.0488 -0.0313 -0.0293 315 HIS   A CB  
2477 C CG  . HIS   A 319 ? 0.7005 0.6100 0.6844 -0.0405 -0.0275 -0.0253 315 HIS   A CG  
2478 N ND1 . HIS   A 319 ? 0.6583 0.5424 0.6318 -0.0446 -0.0251 -0.0255 315 HIS   A ND1 
2479 C CD2 . HIS   A 319 ? 0.5778 0.4872 0.5641 -0.0282 -0.0260 -0.0216 315 HIS   A CD2 
2480 C CE1 . HIS   A 319 ? 0.6353 0.5066 0.6065 -0.0331 -0.0233 -0.0226 315 HIS   A CE1 
2481 N NE2 . HIS   A 319 ? 0.6948 0.5832 0.6749 -0.0240 -0.0233 -0.0206 315 HIS   A NE2 
2482 N N   . ILE   A 320 ? 0.5889 0.5096 0.5569 -0.0523 -0.0361 -0.0438 316 ILE   A N   
2483 C CA  . ILE   A 320 ? 0.6577 0.5642 0.6123 -0.0488 -0.0357 -0.0487 316 ILE   A CA  
2484 C C   . ILE   A 320 ? 0.7574 0.6497 0.7009 -0.0610 -0.0365 -0.0571 316 ILE   A C   
2485 O O   . ILE   A 320 ? 0.7237 0.5921 0.6542 -0.0593 -0.0339 -0.0611 316 ILE   A O   
2486 C CB  . ILE   A 320 ? 0.6357 0.5591 0.5894 -0.0425 -0.0395 -0.0489 316 ILE   A CB  
2487 C CG1 . ILE   A 320 ? 0.5473 0.4772 0.5074 -0.0313 -0.0376 -0.0407 316 ILE   A CG1 
2488 C CG2 . ILE   A 320 ? 0.5990 0.5100 0.5371 -0.0414 -0.0387 -0.0553 316 ILE   A CG2 
2489 C CD1 . ILE   A 320 ? 0.6518 0.5950 0.6082 -0.0261 -0.0421 -0.0392 316 ILE   A CD1 
2490 N N   . ALA   A 321 ? 0.7259 0.6332 0.6742 -0.0737 -0.0400 -0.0608 317 ALA   A N   
2491 C CA  . ALA   A 321 ? 0.7160 0.6095 0.6531 -0.0886 -0.0404 -0.0693 317 ALA   A CA  
2492 C C   . ALA   A 321 ? 0.7407 0.6033 0.6688 -0.0949 -0.0353 -0.0673 317 ALA   A C   
2493 O O   . ALA   A 321 ? 0.8892 0.7245 0.8006 -0.1019 -0.0344 -0.0733 317 ALA   A O   
2494 C CB  . ALA   A 321 ? 0.5985 0.5210 0.5452 -0.1019 -0.0451 -0.0748 317 ALA   A CB  
2495 N N   . THR   A 322 ? 0.8425 0.7061 0.7788 -0.0920 -0.0325 -0.0591 318 THR   A N   
2496 C CA  . THR   A 322 ? 0.8447 0.6767 0.7692 -0.0974 -0.0287 -0.0561 318 THR   A CA  
2497 C C   . THR   A 322 ? 0.9207 0.7202 0.8312 -0.0838 -0.0273 -0.0557 318 THR   A C   
2498 O O   . THR   A 322 ? 1.0368 0.8019 0.9284 -0.0890 -0.0265 -0.0593 318 THR   A O   
2499 C CB  . THR   A 322 ? 0.9022 0.7454 0.8382 -0.0964 -0.0264 -0.0474 318 THR   A CB  
2500 O OG1 . THR   A 322 ? 0.9132 0.7843 0.8604 -0.1112 -0.0269 -0.0499 318 THR   A OG1 
2501 C CG2 . THR   A 322 ? 0.9878 0.7944 0.9081 -0.0982 -0.0232 -0.0426 318 THR   A CG2 
2502 N N   . VAL   A 323 ? 0.8847 0.6947 0.8038 -0.0663 -0.0270 -0.0523 319 VAL   A N   
2503 C CA  . VAL   A 323 ? 0.9184 0.7048 0.8279 -0.0520 -0.0254 -0.0534 319 VAL   A CA  
2504 C C   . VAL   A 323 ? 0.9408 0.7122 0.8360 -0.0526 -0.0261 -0.0636 319 VAL   A C   
2505 O O   . VAL   A 323 ? 0.9896 0.7336 0.8721 -0.0438 -0.0251 -0.0673 319 VAL   A O   
2506 C CB  . VAL   A 323 ? 0.8598 0.6662 0.7831 -0.0360 -0.0241 -0.0488 319 VAL   A CB  
2507 C CG1 . VAL   A 323 ? 0.7880 0.6041 0.7229 -0.0344 -0.0235 -0.0395 319 VAL   A CG1 
2508 C CG2 . VAL   A 323 ? 0.6780 0.5119 0.6088 -0.0357 -0.0252 -0.0509 319 VAL   A CG2 
2509 N N   . LEU   A 324 ? 0.9221 0.7113 0.8187 -0.0617 -0.0282 -0.0689 320 LEU   A N   
2510 C CA  . LEU   A 324 ? 0.9237 0.6992 0.8054 -0.0639 -0.0290 -0.0792 320 LEU   A CA  
2511 C C   . LEU   A 324 ? 1.1203 0.8658 0.9848 -0.0790 -0.0298 -0.0850 320 LEU   A C   
2512 O O   . LEU   A 324 ? 1.2201 0.9443 1.0683 -0.0796 -0.0301 -0.0941 320 LEU   A O   
2513 C CB  . LEU   A 324 ? 0.9725 0.7778 0.8598 -0.0677 -0.0321 -0.0828 320 LEU   A CB  
2514 C CG  . LEU   A 324 ? 0.8556 0.6813 0.7508 -0.0534 -0.0310 -0.0793 320 LEU   A CG  
2515 C CD1 . LEU   A 324 ? 0.6251 0.4789 0.5247 -0.0577 -0.0358 -0.0799 320 LEU   A CD1 
2516 C CD2 . LEU   A 324 ? 0.9129 0.7226 0.7962 -0.0429 -0.0274 -0.0857 320 LEU   A CD2 
2517 N N   . GLN   A 325 ? 1.1720 0.9142 1.0380 -0.0922 -0.0296 -0.0803 321 GLN   A N   
2518 C CA  . GLN   A 325 ? 1.1711 0.8814 1.0179 -0.1095 -0.0293 -0.0849 321 GLN   A CA  
2519 C C   . GLN   A 325 ? 1.2043 0.8678 1.0315 -0.1016 -0.0278 -0.0824 321 GLN   A C   
2520 O O   . GLN   A 325 ? 1.4058 1.0343 1.2120 -0.1158 -0.0276 -0.0849 321 GLN   A O   
2521 C CB  . GLN   A 325 ? 1.1056 0.8339 0.9611 -0.1292 -0.0288 -0.0816 321 GLN   A CB  
2522 C CG  . GLN   A 325 ? 0.9625 0.7324 0.8328 -0.1400 -0.0319 -0.0876 321 GLN   A CG  
2523 C CD  . GLN   A 325 ? 0.9601 0.7528 0.8416 -0.1585 -0.0308 -0.0862 321 GLN   A CD  
2524 O OE1 . GLN   A 325 ? 0.9829 0.7693 0.8662 -0.1597 -0.0273 -0.0782 321 GLN   A OE1 
2525 N NE2 . GLN   A 325 ? 0.8248 0.6464 0.7140 -0.1728 -0.0339 -0.0948 321 GLN   A NE2 
2526 N N   . GLY   A 326 ? 1.1442 0.8057 0.9765 -0.0798 -0.0273 -0.0780 322 GLY   A N   
2527 C CA  . GLY   A 326 ? 1.1752 0.7948 0.9897 -0.0684 -0.0276 -0.0762 322 GLY   A CA  
2528 C C   . GLY   A 326 ? 1.2512 0.8546 1.0567 -0.0505 -0.0282 -0.0851 322 GLY   A C   
2529 O O   . GLY   A 326 ? 1.2948 0.9227 1.1092 -0.0464 -0.0274 -0.0914 322 GLY   A O   
2530 S S   . SO4   B .   ? 0.7363 0.5647 0.6450 -0.0291 -0.0040 0.0297  401 SO4   A S   
2531 O O1  . SO4   B .   ? 0.7855 0.6240 0.7071 -0.0322 -0.0023 0.0256  401 SO4   A O1  
2532 O O2  . SO4   B .   ? 0.8239 0.6812 0.7538 -0.0259 -0.0022 0.0276  401 SO4   A O2  
2533 O O3  . SO4   B .   ? 0.8981 0.7052 0.7814 -0.0441 0.0018  0.0317  401 SO4   A O3  
2534 O O4  . SO4   B .   ? 0.9486 0.7588 0.8469 -0.0143 -0.0135 0.0328  401 SO4   A O4  
2535 C C1  . A1A7Y C .   ? 0.3958 0.3998 0.4409 0.0225  -0.0173 0.0061  402 A1A7Y A C1  
2536 C C2  . A1A7Y C .   ? 0.4766 0.4710 0.5251 0.0216  -0.0182 0.0095  402 A1A7Y A C2  
2537 C C3  . A1A7Y C .   ? 0.4517 0.4507 0.5020 0.0188  -0.0189 0.0111  402 A1A7Y A C3  
2538 C C7  . A1A7Y C .   ? 0.5564 0.5442 0.6047 0.0313  -0.0198 0.0080  402 A1A7Y A C7  
2539 N N2  . A1A7Y C .   ? 0.4261 0.4236 0.4728 0.0244  -0.0177 0.0064  402 A1A7Y A N2  
2540 C C4  . A1A7Y C .   ? 0.4449 0.4499 0.4931 0.0185  -0.0197 0.0107  402 A1A7Y A C4  
2541 N N1  . A1A7Y C .   ? 0.4105 0.4172 0.4552 0.0196  -0.0185 0.0085  402 A1A7Y A N1  
2542 C C5  . A1A7Y C .   ? 0.4782 0.4676 0.5294 0.0182  -0.0180 0.0125  402 A1A7Y A C5  
2543 C C6  . A1A7Y C .   ? 0.5871 0.5663 0.6320 0.0259  -0.0193 0.0099  402 A1A7Y A C6  
2544 C C10 . A1A7Y C .   ? 0.4790 0.4433 0.5143 0.0274  -0.0205 0.0070  402 A1A7Y A C10 
2545 C C8  . A1A7Y C .   ? 0.5498 0.5264 0.5927 0.0365  -0.0226 0.0071  402 A1A7Y A C8  
2546 C C9  . A1A7Y C .   ? 0.6084 0.5678 0.6408 0.0353  -0.0232 0.0061  402 A1A7Y A C9  
2547 N N3  . A1A7Y C .   ? 0.5371 0.5242 0.5853 0.0217  -0.0183 0.0107  402 A1A7Y A N3  
2548 N N4  . A1A7Y C .   ? 0.5292 0.5263 0.5824 0.0173  -0.0188 0.0124  402 A1A7Y A N4  
2549 N N5  . A1A7Y C .   ? 0.3789 0.3886 0.4275 0.0180  -0.0221 0.0119  402 A1A7Y A N5  
2550 O O   . HOH   D .   ? 0.6528 0.6299 0.7010 0.0173  -0.0167 0.0158  501 HOH   A O   
2551 O O   . HOH   D .   ? 0.6259 0.7590 0.7559 0.0156  -0.0051 -0.0333 502 HOH   A O   
2552 O O   . HOH   D .   ? 0.5932 0.5368 0.6131 0.0191  -0.0095 -0.0049 503 HOH   A O   
2553 O O   . HOH   D .   ? 0.6661 0.6393 0.7093 0.0071  -0.0096 0.0161  504 HOH   A O   
2554 O O   . HOH   D .   ? 0.6348 0.5694 0.5722 -0.0173 0.0126  0.0039  505 HOH   A O   
2555 O O   . HOH   D .   ? 1.2349 0.7246 0.9697 0.0677  -0.0767 0.0522  506 HOH   A O   
2556 O O   . HOH   D .   ? 0.7385 0.6175 0.5048 -0.0043 -0.0576 -0.0076 507 HOH   A O   
2557 O O   . HOH   D .   ? 0.3691 0.4479 0.4331 0.0101  0.0013  -0.0045 508 HOH   A O   
2558 O O   . HOH   D .   ? 0.6308 0.5801 0.6382 0.0175  -0.0020 -0.0142 509 HOH   A O   
2559 O O   . HOH   D .   ? 1.2082 0.9884 1.1068 0.1617  -0.0932 -0.0141 510 HOH   A O   
2560 O O   . HOH   D .   ? 0.8680 0.7270 0.7244 0.0291  0.0218  -0.1390 511 HOH   A O   
2561 O O   . HOH   D .   ? 0.4740 0.5265 0.5423 0.0976  -0.0323 -0.0412 512 HOH   A O   
2562 O O   . HOH   D .   ? 1.1237 0.6681 0.7756 -0.0449 -0.0436 0.1155  513 HOH   A O   
2563 O O   . HOH   D .   ? 0.5376 0.5249 0.5771 0.0563  -0.0459 0.0243  514 HOH   A O   
2564 O O   . HOH   D .   ? 0.5044 0.5208 0.5595 0.0404  -0.0385 0.0183  515 HOH   A O   
2565 O O   . HOH   D .   ? 0.3857 0.3536 0.4122 -0.0295 0.0019  0.0041  516 HOH   A O   
2566 O O   . HOH   D .   ? 0.6475 0.4591 0.5640 -0.0535 -0.0030 0.0047  517 HOH   A O   
2567 O O   . HOH   D .   ? 0.6538 0.8852 0.7514 -0.0812 -0.0615 -0.1046 518 HOH   A O   
2568 O O   . HOH   D .   ? 0.7022 0.6890 0.6867 0.0030  -0.0248 -0.0440 519 HOH   A O   
2569 O O   . HOH   D .   ? 0.7212 0.6207 0.4963 0.0191  -0.0958 -0.0073 520 HOH   A O   
2570 O O   . HOH   D .   ? 0.4673 0.4898 0.4896 0.0830  -0.0127 -0.0654 521 HOH   A O   
2571 O O   . HOH   D .   ? 0.5920 0.4326 0.5284 0.0776  0.0024  -0.1035 522 HOH   A O   
2572 O O   . HOH   D .   ? 0.7108 0.5212 0.6497 0.0469  -0.0126 -0.0636 523 HOH   A O   
2573 O O   . HOH   D .   ? 0.4581 0.5644 0.5005 -0.0049 0.0172  -0.0134 524 HOH   A O   
2574 O O   . HOH   D .   ? 0.6690 0.6280 0.6910 -0.0085 -0.0009 0.0147  525 HOH   A O   
2575 O O   . HOH   D .   ? 0.3567 0.3968 0.4024 0.0399  -0.0091 -0.0194 526 HOH   A O   
2576 O O   . HOH   D .   ? 0.5729 0.4383 0.4965 -0.0917 -0.0190 -0.0747 527 HOH   A O   
2577 O O   . HOH   D .   ? 0.5623 0.4754 0.5260 -0.0594 -0.0201 -0.0539 528 HOH   A O   
2578 O O   . HOH   D .   ? 0.8026 0.8245 0.7709 -0.0864 0.0684  -0.0223 529 HOH   A O   
2579 O O   . HOH   D .   ? 0.6263 0.3950 0.5268 0.0356  -0.0377 0.0105  530 HOH   A O   
2580 O O   . HOH   D .   ? 0.6553 0.4811 0.5644 -0.0992 -0.0117 -0.0608 531 HOH   A O   
2581 O O   . HOH   D .   ? 0.6315 1.0409 0.8669 -0.0454 -0.0310 -0.1250 532 HOH   A O   
2582 O O   . HOH   D .   ? 0.6675 0.4836 0.5925 -0.0902 -0.0047 0.0235  533 HOH   A O   
2583 O O   . HOH   D .   ? 0.8235 0.7513 0.7640 -0.0245 0.0146  0.0117  534 HOH   A O   
2584 O O   . HOH   D .   ? 0.7434 0.7237 0.7895 0.0213  -0.0241 0.0175  535 HOH   A O   
2585 O O   . HOH   D .   ? 0.6464 0.6244 0.6610 -0.0760 -0.0300 -0.0319 536 HOH   A O   
2586 O O   . HOH   D .   ? 0.7183 0.8182 0.8046 0.0625  -0.0642 -0.0221 537 HOH   A O   
2587 O O   . HOH   D .   ? 0.8570 0.8123 0.8764 0.0850  0.0071  -0.0763 538 HOH   A O   
2588 O O   . HOH   D .   ? 0.4581 0.4848 0.4638 0.0136  -0.0214 -0.0066 539 HOH   A O   
2589 O O   . HOH   D .   ? 0.5965 0.6592 0.5926 -0.0632 -0.0497 -0.0833 540 HOH   A O   
2590 O O   . HOH   D .   ? 0.5587 0.5957 0.5756 0.0126  -0.0365 -0.0045 541 HOH   A O   
2591 O O   . HOH   D .   ? 0.8133 0.6459 0.6798 -0.1288 -0.0484 -0.1170 542 HOH   A O   
2592 O O   . HOH   D .   ? 0.7052 0.7888 0.7107 -0.0040 -0.0589 -0.0372 543 HOH   A O   
2593 O O   . HOH   D .   ? 0.8294 0.6751 0.7564 0.0966  -0.0323 -0.0874 544 HOH   A O   
2594 O O   . HOH   D .   ? 0.5490 0.6875 0.6241 -0.0075 0.0168  -0.0205 545 HOH   A O   
2595 O O   . HOH   D .   ? 1.2287 0.6375 0.8960 0.0421  -0.0768 0.0681  546 HOH   A O   
2596 O O   . HOH   D .   ? 0.5515 0.5828 0.5497 0.0111  -0.0148 0.0014  547 HOH   A O   
2597 O O   . HOH   D .   ? 0.8553 0.7658 0.6138 -0.0252 -0.0647 -0.0609 548 HOH   A O   
2598 O O   . HOH   D .   ? 0.9375 0.7009 0.8255 -0.1423 -0.0035 -0.0033 549 HOH   A O   
2599 O O   . HOH   D .   ? 0.6423 0.6037 0.6687 0.0116  -0.0105 0.0162  550 HOH   A O   
2600 O O   . HOH   D .   ? 0.6004 0.6165 0.5990 0.0250  -0.0419 0.0209  551 HOH   A O   
2601 O O   . HOH   D .   ? 1.1130 0.9057 1.0178 0.1298  -0.0828 0.0015  552 HOH   A O   
2602 O O   . HOH   D .   ? 0.7519 0.4769 0.6158 -0.0029 -0.0263 0.0148  553 HOH   A O   
2603 O O   . HOH   D .   ? 0.7095 0.7246 0.6551 -0.1842 0.0561  0.0131  554 HOH   A O   
2604 O O   . HOH   D .   ? 0.8367 0.6975 0.7591 0.0053  -0.0211 0.0334  555 HOH   A O   
2605 O O   . HOH   D .   ? 0.6656 0.7706 0.6738 -0.1694 0.0552  -0.0096 556 HOH   A O   
2606 O O   . HOH   D .   ? 0.5952 0.5593 0.6252 0.0255  -0.0265 0.0193  557 HOH   A O   
2607 O O   . HOH   D .   ? 0.5316 0.7475 0.6807 0.0424  -0.0363 -0.0517 558 HOH   A O   
2608 O O   . HOH   D .   ? 0.5782 0.5533 0.5925 -0.0827 0.0086  -0.0219 559 HOH   A O   
2609 O O   . HOH   D .   ? 0.6066 0.5534 0.5688 0.0452  -0.0169 -0.0721 560 HOH   A O   
2610 O O   . HOH   D .   ? 0.6971 0.6644 0.7192 0.0382  -0.0395 0.0160  561 HOH   A O   
2611 O O   . HOH   D .   ? 1.3450 1.0011 1.0511 0.1011  -0.1149 0.0600  562 HOH   A O   
# 
