data_9DZD
# 
_entry.id   9DZD 
# 
_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   9DZD         pdb_00009dzd 10.2210/pdb9dzd/pdb 
WWPDB D_1000289076 ?            ?                   
# 
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 2025-02-26 ? 
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' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation_author.name'    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DZD 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-16 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tham@wehi.edu.au 
_pdbx_contact_author.name_first         Wai-Hong 
_pdbx_contact_author.name_last          Tham 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7950-8699 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pymm, P.'   1 0000-0003-2722-4621 
'D Sa, J.'   2 0000-0002-4562-0241 
'Tham, W.H.' 3 0000-0001-7950-8699 
# 
_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                108290 
_citation.page_last                 108290 
_citation.title                     
'Stabilized designs of the malaria adhesin protein PvRBP2b for use as a potential diagnostic for Plasmodium vivax.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2025.108290 
_citation.pdbx_database_id_PubMed   39938801 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'D Sa, J.'           1  ? 
primary 'Krauss, L.'         2  ? 
primary 'Smith, L.'          3  ? 
primary 
;D'Andrea, L.
;
4  ? 
primary 'Chan, L.J.'         5  ? 
primary 'Abraham, A.'        6  ? 
primary 'Kiernan-Walker, N.' 7  ? 
primary 'Mazhari, R.'        8  ? 
primary 'Lamont, M.'         9  ? 
primary 'Lim, P.S.'          10 ? 
primary 'Sattabongkot, J.'   11 ? 
primary 'Lacerda, M.V.'      12 ? 
primary 'Wini, L.'           13 ? 
primary 'Mueller, I.'        14 ? 
primary 'Longley, R.J.'      15 ? 
primary 'Pymm, P.'           16 ? 
primary 'Fleishman, S.J.'    17 ? 
primary 'Tham, W.H.'         18 ? 
# 
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 'Reticulocyte-binding protein 2b' 39678.254 1   ? ? ? ? 
2 non-polymer syn GLYCEROL                          92.094    4   ? ? ? ? 
3 non-polymer nat 'DI(HYDROXYETHYL)ETHER'           106.120   1   ? ? ? ? 
4 water       nat water                             18.015    301 ? ? ? ? 
# 
_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       
;MSYYHHHHHHDYDIPTTENLYFQGAMGSTNTTDNIDYFDISDESNYYLISQLRPHFSNIYFFDEFKRYASYHTEIKRYED
IHKTKVNSLLNEASRAIGICNRLKNTLLGLINILENPQKFKTQRESYDVLLRQYEEKKEAFRGCLLNKNRKNLDQIKKIN
NEIRDLLERLKCSQDCQTNVYWDFIKIYLVDFKKMPLENYDTFIKQFKNSYLSYVDLIRKYEKQIDDPITLQAIKFVLKE
MGYIIDRFEYHLQKVKHAIDQITAIADGVKPKQVTKNELKEYYFNIGNYYAIFKFAKDQLNMLNKALIHKEKIVHNLLGE
LFGHLEERIS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSYYHHHHHHDYDIPTTENLYFQGAMGSTNTTDNIDYFDISDESNYYLISQLRPHFSNIYFFDEFKRYASYHTEIKRYED
IHKTKVNSLLNEASRAIGICNRLKNTLLGLINILENPQKFKTQRESYDVLLRQYEEKKEAFRGCLLNKNRKNLDQIKKIN
NEIRDLLERLKCSQDCQTNVYWDFIKIYLVDFKKMPLENYDTFIKQFKNSYLSYVDLIRKYEKQIDDPITLQAIKFVLKE
MGYIIDRFEYHLQKVKHAIDQITAIADGVKPKQVTKNELKEYYFNIGNYYAIFKFAKDQLNMLNKALIHKEKIVHNLLGE
LFGHLEERIS
;
_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 GLYCEROL                GOL 
3 'DI(HYDROXYETHYL)ETHER' PEG 
4 water                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   TYR n 
1 4   TYR n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  ASP n 
1 12  TYR n 
1 13  ASP n 
1 14  ILE n 
1 15  PRO n 
1 16  THR n 
1 17  THR n 
1 18  GLU n 
1 19  ASN n 
1 20  LEU n 
1 21  TYR n 
1 22  PHE n 
1 23  GLN n 
1 24  GLY n 
1 25  ALA n 
1 26  MET n 
1 27  GLY n 
1 28  SER n 
1 29  THR n 
1 30  ASN n 
1 31  THR n 
1 32  THR n 
1 33  ASP n 
1 34  ASN n 
1 35  ILE n 
1 36  ASP n 
1 37  TYR n 
1 38  PHE n 
1 39  ASP n 
1 40  ILE n 
1 41  SER n 
1 42  ASP n 
1 43  GLU n 
1 44  SER n 
1 45  ASN n 
1 46  TYR n 
1 47  TYR n 
1 48  LEU n 
1 49  ILE n 
1 50  SER n 
1 51  GLN n 
1 52  LEU n 
1 53  ARG n 
1 54  PRO n 
1 55  HIS n 
1 56  PHE n 
1 57  SER n 
1 58  ASN n 
1 59  ILE n 
1 60  TYR n 
1 61  PHE n 
1 62  PHE n 
1 63  ASP n 
1 64  GLU n 
1 65  PHE n 
1 66  LYS n 
1 67  ARG n 
1 68  TYR n 
1 69  ALA n 
1 70  SER n 
1 71  TYR n 
1 72  HIS n 
1 73  THR n 
1 74  GLU n 
1 75  ILE n 
1 76  LYS n 
1 77  ARG n 
1 78  TYR n 
1 79  GLU n 
1 80  ASP n 
1 81  ILE n 
1 82  HIS n 
1 83  LYS n 
1 84  THR n 
1 85  LYS n 
1 86  VAL n 
1 87  ASN n 
1 88  SER n 
1 89  LEU n 
1 90  LEU n 
1 91  ASN n 
1 92  GLU n 
1 93  ALA n 
1 94  SER n 
1 95  ARG n 
1 96  ALA n 
1 97  ILE n 
1 98  GLY n 
1 99  ILE n 
1 100 CYS n 
1 101 ASN n 
1 102 ARG n 
1 103 LEU n 
1 104 LYS n 
1 105 ASN n 
1 106 THR n 
1 107 LEU n 
1 108 LEU n 
1 109 GLY n 
1 110 LEU n 
1 111 ILE n 
1 112 ASN n 
1 113 ILE n 
1 114 LEU n 
1 115 GLU n 
1 116 ASN n 
1 117 PRO n 
1 118 GLN n 
1 119 LYS n 
1 120 PHE n 
1 121 LYS n 
1 122 THR n 
1 123 GLN n 
1 124 ARG n 
1 125 GLU n 
1 126 SER n 
1 127 TYR n 
1 128 ASP n 
1 129 VAL n 
1 130 LEU n 
1 131 LEU n 
1 132 ARG n 
1 133 GLN n 
1 134 TYR n 
1 135 GLU n 
1 136 GLU n 
1 137 LYS n 
1 138 LYS n 
1 139 GLU n 
1 140 ALA n 
1 141 PHE n 
1 142 ARG n 
1 143 GLY n 
1 144 CYS n 
1 145 LEU n 
1 146 LEU n 
1 147 ASN n 
1 148 LYS n 
1 149 ASN n 
1 150 ARG n 
1 151 LYS n 
1 152 ASN n 
1 153 LEU n 
1 154 ASP n 
1 155 GLN n 
1 156 ILE n 
1 157 LYS n 
1 158 LYS n 
1 159 ILE n 
1 160 ASN n 
1 161 ASN n 
1 162 GLU n 
1 163 ILE n 
1 164 ARG n 
1 165 ASP n 
1 166 LEU n 
1 167 LEU n 
1 168 GLU n 
1 169 ARG n 
1 170 LEU n 
1 171 LYS n 
1 172 CYS n 
1 173 SER n 
1 174 GLN n 
1 175 ASP n 
1 176 CYS n 
1 177 GLN n 
1 178 THR n 
1 179 ASN n 
1 180 VAL n 
1 181 TYR n 
1 182 TRP n 
1 183 ASP n 
1 184 PHE n 
1 185 ILE n 
1 186 LYS n 
1 187 ILE n 
1 188 TYR n 
1 189 LEU n 
1 190 VAL n 
1 191 ASP n 
1 192 PHE n 
1 193 LYS n 
1 194 LYS n 
1 195 MET n 
1 196 PRO n 
1 197 LEU n 
1 198 GLU n 
1 199 ASN n 
1 200 TYR n 
1 201 ASP n 
1 202 THR n 
1 203 PHE n 
1 204 ILE n 
1 205 LYS n 
1 206 GLN n 
1 207 PHE n 
1 208 LYS n 
1 209 ASN n 
1 210 SER n 
1 211 TYR n 
1 212 LEU n 
1 213 SER n 
1 214 TYR n 
1 215 VAL n 
1 216 ASP n 
1 217 LEU n 
1 218 ILE n 
1 219 ARG n 
1 220 LYS n 
1 221 TYR n 
1 222 GLU n 
1 223 LYS n 
1 224 GLN n 
1 225 ILE n 
1 226 ASP n 
1 227 ASP n 
1 228 PRO n 
1 229 ILE n 
1 230 THR n 
1 231 LEU n 
1 232 GLN n 
1 233 ALA n 
1 234 ILE n 
1 235 LYS n 
1 236 PHE n 
1 237 VAL n 
1 238 LEU n 
1 239 LYS n 
1 240 GLU n 
1 241 MET n 
1 242 GLY n 
1 243 TYR n 
1 244 ILE n 
1 245 ILE n 
1 246 ASP n 
1 247 ARG n 
1 248 PHE n 
1 249 GLU n 
1 250 TYR n 
1 251 HIS n 
1 252 LEU n 
1 253 GLN n 
1 254 LYS n 
1 255 VAL n 
1 256 LYS n 
1 257 HIS n 
1 258 ALA n 
1 259 ILE n 
1 260 ASP n 
1 261 GLN n 
1 262 ILE n 
1 263 THR n 
1 264 ALA n 
1 265 ILE n 
1 266 ALA n 
1 267 ASP n 
1 268 GLY n 
1 269 VAL n 
1 270 LYS n 
1 271 PRO n 
1 272 LYS n 
1 273 GLN n 
1 274 VAL n 
1 275 THR n 
1 276 LYS n 
1 277 ASN n 
1 278 GLU n 
1 279 LEU n 
1 280 LYS n 
1 281 GLU n 
1 282 TYR n 
1 283 TYR n 
1 284 PHE n 
1 285 ASN n 
1 286 ILE n 
1 287 GLY n 
1 288 ASN n 
1 289 TYR n 
1 290 TYR n 
1 291 ALA n 
1 292 ILE n 
1 293 PHE n 
1 294 LYS n 
1 295 PHE n 
1 296 ALA n 
1 297 LYS n 
1 298 ASP n 
1 299 GLN n 
1 300 LEU n 
1 301 ASN n 
1 302 MET n 
1 303 LEU n 
1 304 ASN n 
1 305 LYS n 
1 306 ALA n 
1 307 LEU n 
1 308 ILE n 
1 309 HIS n 
1 310 LYS n 
1 311 GLU n 
1 312 LYS n 
1 313 ILE n 
1 314 VAL n 
1 315 HIS n 
1 316 ASN n 
1 317 LEU n 
1 318 LEU n 
1 319 GLY n 
1 320 GLU n 
1 321 LEU n 
1 322 PHE n 
1 323 GLY n 
1 324 HIS n 
1 325 LEU n 
1 326 GLU n 
1 327 GLU n 
1 328 ARG n 
1 329 ILE n 
1 330 SER 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                   330 
_entity_src_gen.gene_src_common_name               'malaria parasite P. vivax' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Plasmodium vivax' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5855 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                 ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE              ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'         ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE               ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'         ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                 ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL                'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE               ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                   ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE              ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                 ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                  ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE              ?                               'C5 H11 N O2 S'  149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                               'C4 H10 O3'      106.120 
PHE 'L-peptide linking' y PHENYLALANINE           ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                 ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                  ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE               ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN              ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                  ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   TYR 3   3   ?   ?   ?   A . n 
A 1 4   TYR 4   4   ?   ?   ?   A . n 
A 1 5   HIS 5   5   ?   ?   ?   A . n 
A 1 6   HIS 6   6   ?   ?   ?   A . n 
A 1 7   HIS 7   7   ?   ?   ?   A . n 
A 1 8   HIS 8   8   ?   ?   ?   A . n 
A 1 9   HIS 9   9   ?   ?   ?   A . n 
A 1 10  HIS 10  10  ?   ?   ?   A . n 
A 1 11  ASP 11  11  ?   ?   ?   A . n 
A 1 12  TYR 12  12  ?   ?   ?   A . n 
A 1 13  ASP 13  13  ?   ?   ?   A . n 
A 1 14  ILE 14  14  ?   ?   ?   A . n 
A 1 15  PRO 15  15  ?   ?   ?   A . n 
A 1 16  THR 16  16  ?   ?   ?   A . n 
A 1 17  THR 17  17  ?   ?   ?   A . n 
A 1 18  GLU 18  18  ?   ?   ?   A . n 
A 1 19  ASN 19  19  ?   ?   ?   A . n 
A 1 20  LEU 20  20  ?   ?   ?   A . n 
A 1 21  TYR 21  21  ?   ?   ?   A . n 
A 1 22  PHE 22  22  ?   ?   ?   A . n 
A 1 23  GLN 23  23  ?   ?   ?   A . n 
A 1 24  GLY 24  24  ?   ?   ?   A . n 
A 1 25  ALA 25  25  ?   ?   ?   A . n 
A 1 26  MET 26  26  ?   ?   ?   A . n 
A 1 27  GLY 27  27  ?   ?   ?   A . n 
A 1 28  SER 28  28  ?   ?   ?   A . n 
A 1 29  THR 29  29  ?   ?   ?   A . n 
A 1 30  ASN 30  30  30  ASN ASN A . n 
A 1 31  THR 31  31  31  THR THR A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASN 34  34  34  ASN ASN A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  PHE 38  38  38  PHE PHE A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  ASP 42  42  42  ASP ASP A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  ASN 45  45  45  ASN ASN A . n 
A 1 46  TYR 46  46  46  TYR TYR A . n 
A 1 47  TYR 47  47  47  TYR TYR A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  GLN 51  51  51  GLN GLN A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  HIS 55  55  55  HIS HIS A . n 
A 1 56  PHE 56  56  56  PHE PHE A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  TYR 60  60  60  TYR TYR A . n 
A 1 61  PHE 61  61  61  PHE PHE A . n 
A 1 62  PHE 62  62  62  PHE PHE A . n 
A 1 63  ASP 63  63  63  ASP ASP A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  PHE 65  65  65  PHE PHE A . n 
A 1 66  LYS 66  66  66  LYS LYS A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  HIS 72  72  72  HIS HIS A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ARG 77  77  77  ARG ARG A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  ILE 81  81  81  ILE ILE A . n 
A 1 82  HIS 82  82  82  HIS HIS A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  SER 88  88  88  SER SER A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ASN 91  91  91  ASN ASN A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  ARG 95  95  95  ARG ARG A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  ILE 97  97  97  ILE ILE A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 CYS 100 100 100 CYS CYS A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 ASN 112 112 112 ASN ASN A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 PHE 120 120 120 PHE PHE A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 THR 122 122 122 THR THR A . n 
A 1 123 GLN 123 123 123 GLN GLN A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 GLN 133 133 133 GLN GLN A . n 
A 1 134 TYR 134 134 134 TYR TYR A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 PHE 141 141 141 PHE PHE A . n 
A 1 142 ARG 142 142 142 ARG ARG A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 CYS 144 144 144 CYS CYS A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 ASN 147 147 147 ASN ASN A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 ASN 149 149 149 ASN ASN A . n 
A 1 150 ARG 150 150 150 ARG ARG A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 GLN 155 155 155 GLN GLN A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 ASN 160 160 160 ASN ASN A . n 
A 1 161 ASN 161 161 161 ASN ASN A . n 
A 1 162 GLU 162 162 162 GLU GLU A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 ASP 165 165 165 ASP ASP A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 ARG 169 169 169 ARG ARG A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 CYS 172 172 172 CYS CYS A . n 
A 1 173 SER 173 173 173 SER SER A . n 
A 1 174 GLN 174 174 174 GLN GLN A . n 
A 1 175 ASP 175 175 175 ASP ASP A . n 
A 1 176 CYS 176 176 176 CYS CYS A . n 
A 1 177 GLN 177 177 177 GLN GLN A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 ASN 179 179 179 ASN ASN A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 TYR 181 181 181 TYR TYR A . n 
A 1 182 TRP 182 182 182 TRP TRP A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 PHE 184 184 184 PHE PHE A . n 
A 1 185 ILE 185 185 185 ILE ILE A . n 
A 1 186 LYS 186 186 186 LYS LYS A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 PHE 192 192 192 PHE PHE A . n 
A 1 193 LYS 193 193 193 LYS LYS A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 MET 195 195 195 MET MET A . n 
A 1 196 PRO 196 196 196 PRO PRO A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 GLU 198 198 198 GLU GLU A . n 
A 1 199 ASN 199 199 199 ASN ASN A . n 
A 1 200 TYR 200 200 200 TYR TYR A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 ILE 204 204 204 ILE ILE A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 GLN 206 206 206 GLN GLN A . n 
A 1 207 PHE 207 207 207 PHE PHE A . n 
A 1 208 LYS 208 208 208 LYS LYS A . n 
A 1 209 ASN 209 209 209 ASN ASN A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 TYR 211 211 211 TYR TYR A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 TYR 214 214 214 TYR TYR A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 ARG 219 219 219 ARG ARG A . n 
A 1 220 LYS 220 220 220 LYS LYS A . n 
A 1 221 TYR 221 221 221 TYR TYR A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 LYS 223 223 223 LYS LYS A . n 
A 1 224 GLN 224 224 224 GLN GLN A . n 
A 1 225 ILE 225 225 225 ILE ILE A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 ASP 227 227 227 ASP ASP A . n 
A 1 228 PRO 228 228 228 PRO PRO A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 THR 230 230 230 THR THR A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 GLN 232 232 232 GLN GLN A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 PHE 236 236 236 PHE PHE A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 LYS 239 239 239 LYS LYS A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 MET 241 241 241 MET MET A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 TYR 243 243 243 TYR TYR A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 ILE 245 245 245 ILE ILE A . n 
A 1 246 ASP 246 246 246 ASP ASP A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 GLU 249 249 249 GLU GLU A . n 
A 1 250 TYR 250 250 250 TYR TYR A . n 
A 1 251 HIS 251 251 251 HIS HIS A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 GLN 253 253 253 GLN GLN A . n 
A 1 254 LYS 254 254 254 LYS LYS A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 LYS 256 256 256 LYS LYS A . n 
A 1 257 HIS 257 257 257 HIS HIS A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 GLN 261 261 261 GLN GLN A . n 
A 1 262 ILE 262 262 262 ILE ILE A . n 
A 1 263 THR 263 263 263 THR THR A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 ILE 265 265 265 ILE ILE A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 ASP 267 267 267 ASP ASP A . n 
A 1 268 GLY 268 268 268 GLY GLY A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 LYS 270 270 270 LYS LYS A . n 
A 1 271 PRO 271 271 271 PRO PRO A . n 
A 1 272 LYS 272 272 272 LYS LYS A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 VAL 274 274 274 VAL VAL A . n 
A 1 275 THR 275 275 275 THR THR A . n 
A 1 276 LYS 276 276 276 LYS LYS A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLU 278 278 278 GLU GLU A . n 
A 1 279 LEU 279 279 279 LEU LEU A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 GLU 281 281 281 GLU GLU A . n 
A 1 282 TYR 282 282 282 TYR TYR A . n 
A 1 283 TYR 283 283 283 TYR TYR A . n 
A 1 284 PHE 284 284 284 PHE PHE A . n 
A 1 285 ASN 285 285 285 ASN ASN A . n 
A 1 286 ILE 286 286 286 ILE ILE A . n 
A 1 287 GLY 287 287 287 GLY GLY A . n 
A 1 288 ASN 288 288 288 ASN ASN A . n 
A 1 289 TYR 289 289 289 TYR TYR A . n 
A 1 290 TYR 290 290 290 TYR TYR A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ILE 292 292 292 ILE ILE A . n 
A 1 293 PHE 293 293 293 PHE PHE A . n 
A 1 294 LYS 294 294 294 LYS LYS A . n 
A 1 295 PHE 295 295 295 PHE PHE A . n 
A 1 296 ALA 296 296 296 ALA ALA A . n 
A 1 297 LYS 297 297 297 LYS LYS A . n 
A 1 298 ASP 298 298 298 ASP ASP A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 MET 302 302 302 MET MET A . n 
A 1 303 LEU 303 303 303 LEU LEU A . n 
A 1 304 ASN 304 304 304 ASN ASN A . n 
A 1 305 LYS 305 305 305 LYS LYS A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 LEU 307 307 307 LEU LEU A . n 
A 1 308 ILE 308 308 308 ILE ILE A . n 
A 1 309 HIS 309 309 309 HIS HIS A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 LYS 312 312 312 LYS LYS A . n 
A 1 313 ILE 313 313 313 ILE ILE A . n 
A 1 314 VAL 314 314 314 VAL VAL A . n 
A 1 315 HIS 315 315 315 HIS HIS A . n 
A 1 316 ASN 316 316 316 ASN ASN A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 LEU 321 321 321 LEU LEU A . n 
A 1 322 PHE 322 322 322 PHE PHE A . n 
A 1 323 GLY 323 323 323 GLY GLY A . n 
A 1 324 HIS 324 324 324 HIS HIS A . n 
A 1 325 LEU 325 325 325 LEU LEU A . n 
A 1 326 GLU 326 326 326 GLU GLU A . n 
A 1 327 GLU 327 327 327 GLU GLU A . n 
A 1 328 ARG 328 328 328 ARG ARG A . n 
A 1 329 ILE 329 329 329 ILE ILE A . n 
A 1 330 SER 330 330 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 GOL 1   401 401 GOL GOL A . 
C 2 GOL 1   402 403 GOL GOL A . 
D 2 GOL 1   403 404 GOL GOL A . 
E 2 GOL 1   404 405 GOL GOL A . 
F 3 PEG 1   405 406 PEG PEG A . 
G 4 HOH 1   501 185 HOH HOH A . 
G 4 HOH 2   502 174 HOH HOH A . 
G 4 HOH 3   503 266 HOH HOH A . 
G 4 HOH 4   504 108 HOH HOH A . 
G 4 HOH 5   505 246 HOH HOH A . 
G 4 HOH 6   506 217 HOH HOH A . 
G 4 HOH 7   507 320 HOH HOH A . 
G 4 HOH 8   508 72  HOH HOH A . 
G 4 HOH 9   509 172 HOH HOH A . 
G 4 HOH 10  510 78  HOH HOH A . 
G 4 HOH 11  511 157 HOH HOH A . 
G 4 HOH 12  512 86  HOH HOH A . 
G 4 HOH 13  513 13  HOH HOH A . 
G 4 HOH 14  514 186 HOH HOH A . 
G 4 HOH 15  515 278 HOH HOH A . 
G 4 HOH 16  516 156 HOH HOH A . 
G 4 HOH 17  517 23  HOH HOH A . 
G 4 HOH 18  518 128 HOH HOH A . 
G 4 HOH 19  519 139 HOH HOH A . 
G 4 HOH 20  520 26  HOH HOH A . 
G 4 HOH 21  521 289 HOH HOH A . 
G 4 HOH 22  522 308 HOH HOH A . 
G 4 HOH 23  523 24  HOH HOH A . 
G 4 HOH 24  524 114 HOH HOH A . 
G 4 HOH 25  525 298 HOH HOH A . 
G 4 HOH 26  526 201 HOH HOH A . 
G 4 HOH 27  527 90  HOH HOH A . 
G 4 HOH 28  528 51  HOH HOH A . 
G 4 HOH 29  529 136 HOH HOH A . 
G 4 HOH 30  530 183 HOH HOH A . 
G 4 HOH 31  531 300 HOH HOH A . 
G 4 HOH 32  532 243 HOH HOH A . 
G 4 HOH 33  533 161 HOH HOH A . 
G 4 HOH 34  534 35  HOH HOH A . 
G 4 HOH 35  535 99  HOH HOH A . 
G 4 HOH 36  536 2   HOH HOH A . 
G 4 HOH 37  537 126 HOH HOH A . 
G 4 HOH 38  538 94  HOH HOH A . 
G 4 HOH 39  539 58  HOH HOH A . 
G 4 HOH 40  540 241 HOH HOH A . 
G 4 HOH 41  541 148 HOH HOH A . 
G 4 HOH 42  542 159 HOH HOH A . 
G 4 HOH 43  543 192 HOH HOH A . 
G 4 HOH 44  544 10  HOH HOH A . 
G 4 HOH 45  545 39  HOH HOH A . 
G 4 HOH 46  546 12  HOH HOH A . 
G 4 HOH 47  547 60  HOH HOH A . 
G 4 HOH 48  548 135 HOH HOH A . 
G 4 HOH 49  549 6   HOH HOH A . 
G 4 HOH 50  550 64  HOH HOH A . 
G 4 HOH 51  551 4   HOH HOH A . 
G 4 HOH 52  552 15  HOH HOH A . 
G 4 HOH 53  553 40  HOH HOH A . 
G 4 HOH 54  554 1   HOH HOH A . 
G 4 HOH 55  555 44  HOH HOH A . 
G 4 HOH 56  556 25  HOH HOH A . 
G 4 HOH 57  557 176 HOH HOH A . 
G 4 HOH 58  558 168 HOH HOH A . 
G 4 HOH 59  559 36  HOH HOH A . 
G 4 HOH 60  560 272 HOH HOH A . 
G 4 HOH 61  561 82  HOH HOH A . 
G 4 HOH 62  562 216 HOH HOH A . 
G 4 HOH 63  563 37  HOH HOH A . 
G 4 HOH 64  564 291 HOH HOH A . 
G 4 HOH 65  565 313 HOH HOH A . 
G 4 HOH 66  566 282 HOH HOH A . 
G 4 HOH 67  567 123 HOH HOH A . 
G 4 HOH 68  568 97  HOH HOH A . 
G 4 HOH 69  569 32  HOH HOH A . 
G 4 HOH 70  570 303 HOH HOH A . 
G 4 HOH 71  571 29  HOH HOH A . 
G 4 HOH 72  572 28  HOH HOH A . 
G 4 HOH 73  573 71  HOH HOH A . 
G 4 HOH 74  574 75  HOH HOH A . 
G 4 HOH 75  575 21  HOH HOH A . 
G 4 HOH 76  576 140 HOH HOH A . 
G 4 HOH 77  577 142 HOH HOH A . 
G 4 HOH 78  578 96  HOH HOH A . 
G 4 HOH 79  579 321 HOH HOH A . 
G 4 HOH 80  580 138 HOH HOH A . 
G 4 HOH 81  581 93  HOH HOH A . 
G 4 HOH 82  582 19  HOH HOH A . 
G 4 HOH 83  583 209 HOH HOH A . 
G 4 HOH 84  584 179 HOH HOH A . 
G 4 HOH 85  585 77  HOH HOH A . 
G 4 HOH 86  586 31  HOH HOH A . 
G 4 HOH 87  587 67  HOH HOH A . 
G 4 HOH 88  588 252 HOH HOH A . 
G 4 HOH 89  589 83  HOH HOH A . 
G 4 HOH 90  590 119 HOH HOH A . 
G 4 HOH 91  591 125 HOH HOH A . 
G 4 HOH 92  592 173 HOH HOH A . 
G 4 HOH 93  593 304 HOH HOH A . 
G 4 HOH 94  594 235 HOH HOH A . 
G 4 HOH 95  595 283 HOH HOH A . 
G 4 HOH 96  596 134 HOH HOH A . 
G 4 HOH 97  597 311 HOH HOH A . 
G 4 HOH 98  598 73  HOH HOH A . 
G 4 HOH 99  599 47  HOH HOH A . 
G 4 HOH 100 600 163 HOH HOH A . 
G 4 HOH 101 601 254 HOH HOH A . 
G 4 HOH 102 602 84  HOH HOH A . 
G 4 HOH 103 603 153 HOH HOH A . 
G 4 HOH 104 604 106 HOH HOH A . 
G 4 HOH 105 605 111 HOH HOH A . 
G 4 HOH 106 606 5   HOH HOH A . 
G 4 HOH 107 607 212 HOH HOH A . 
G 4 HOH 108 608 273 HOH HOH A . 
G 4 HOH 109 609 34  HOH HOH A . 
G 4 HOH 110 610 124 HOH HOH A . 
G 4 HOH 111 611 14  HOH HOH A . 
G 4 HOH 112 612 285 HOH HOH A . 
G 4 HOH 113 613 91  HOH HOH A . 
G 4 HOH 114 614 165 HOH HOH A . 
G 4 HOH 115 615 80  HOH HOH A . 
G 4 HOH 116 616 221 HOH HOH A . 
G 4 HOH 117 617 20  HOH HOH A . 
G 4 HOH 118 618 238 HOH HOH A . 
G 4 HOH 119 619 113 HOH HOH A . 
G 4 HOH 120 620 297 HOH HOH A . 
G 4 HOH 121 621 8   HOH HOH A . 
G 4 HOH 122 622 42  HOH HOH A . 
G 4 HOH 123 623 247 HOH HOH A . 
G 4 HOH 124 624 143 HOH HOH A . 
G 4 HOH 125 625 18  HOH HOH A . 
G 4 HOH 126 626 227 HOH HOH A . 
G 4 HOH 127 627 231 HOH HOH A . 
G 4 HOH 128 628 79  HOH HOH A . 
G 4 HOH 129 629 112 HOH HOH A . 
G 4 HOH 130 630 323 HOH HOH A . 
G 4 HOH 131 631 54  HOH HOH A . 
G 4 HOH 132 632 33  HOH HOH A . 
G 4 HOH 133 633 22  HOH HOH A . 
G 4 HOH 134 634 260 HOH HOH A . 
G 4 HOH 135 635 70  HOH HOH A . 
G 4 HOH 136 636 170 HOH HOH A . 
G 4 HOH 137 637 225 HOH HOH A . 
G 4 HOH 138 638 52  HOH HOH A . 
G 4 HOH 139 639 43  HOH HOH A . 
G 4 HOH 140 640 242 HOH HOH A . 
G 4 HOH 141 641 158 HOH HOH A . 
G 4 HOH 142 642 115 HOH HOH A . 
G 4 HOH 143 643 17  HOH HOH A . 
G 4 HOH 144 644 45  HOH HOH A . 
G 4 HOH 145 645 276 HOH HOH A . 
G 4 HOH 146 646 16  HOH HOH A . 
G 4 HOH 147 647 121 HOH HOH A . 
G 4 HOH 148 648 309 HOH HOH A . 
G 4 HOH 149 649 253 HOH HOH A . 
G 4 HOH 150 650 30  HOH HOH A . 
G 4 HOH 151 651 267 HOH HOH A . 
G 4 HOH 152 652 3   HOH HOH A . 
G 4 HOH 153 653 166 HOH HOH A . 
G 4 HOH 154 654 50  HOH HOH A . 
G 4 HOH 155 655 49  HOH HOH A . 
G 4 HOH 156 656 249 HOH HOH A . 
G 4 HOH 157 657 137 HOH HOH A . 
G 4 HOH 158 658 178 HOH HOH A . 
G 4 HOH 159 659 223 HOH HOH A . 
G 4 HOH 160 660 229 HOH HOH A . 
G 4 HOH 161 661 169 HOH HOH A . 
G 4 HOH 162 662 118 HOH HOH A . 
G 4 HOH 163 663 248 HOH HOH A . 
G 4 HOH 164 664 256 HOH HOH A . 
G 4 HOH 165 665 150 HOH HOH A . 
G 4 HOH 166 666 89  HOH HOH A . 
G 4 HOH 167 667 187 HOH HOH A . 
G 4 HOH 168 668 263 HOH HOH A . 
G 4 HOH 169 669 103 HOH HOH A . 
G 4 HOH 170 670 167 HOH HOH A . 
G 4 HOH 171 671 213 HOH HOH A . 
G 4 HOH 172 672 41  HOH HOH A . 
G 4 HOH 173 673 207 HOH HOH A . 
G 4 HOH 174 674 318 HOH HOH A . 
G 4 HOH 175 675 218 HOH HOH A . 
G 4 HOH 176 676 81  HOH HOH A . 
G 4 HOH 177 677 105 HOH HOH A . 
G 4 HOH 178 678 63  HOH HOH A . 
G 4 HOH 179 679 61  HOH HOH A . 
G 4 HOH 180 680 122 HOH HOH A . 
G 4 HOH 181 681 104 HOH HOH A . 
G 4 HOH 182 682 7   HOH HOH A . 
G 4 HOH 183 683 87  HOH HOH A . 
G 4 HOH 184 684 302 HOH HOH A . 
G 4 HOH 185 685 177 HOH HOH A . 
G 4 HOH 186 686 288 HOH HOH A . 
G 4 HOH 187 687 110 HOH HOH A . 
G 4 HOH 188 688 131 HOH HOH A . 
G 4 HOH 189 689 190 HOH HOH A . 
G 4 HOH 190 690 171 HOH HOH A . 
G 4 HOH 191 691 258 HOH HOH A . 
G 4 HOH 192 692 224 HOH HOH A . 
G 4 HOH 193 693 46  HOH HOH A . 
G 4 HOH 194 694 27  HOH HOH A . 
G 4 HOH 195 695 301 HOH HOH A . 
G 4 HOH 196 696 189 HOH HOH A . 
G 4 HOH 197 697 265 HOH HOH A . 
G 4 HOH 198 698 296 HOH HOH A . 
G 4 HOH 199 699 11  HOH HOH A . 
G 4 HOH 200 700 57  HOH HOH A . 
G 4 HOH 201 701 307 HOH HOH A . 
G 4 HOH 202 702 144 HOH HOH A . 
G 4 HOH 203 703 188 HOH HOH A . 
G 4 HOH 204 704 107 HOH HOH A . 
G 4 HOH 205 705 55  HOH HOH A . 
G 4 HOH 206 706 69  HOH HOH A . 
G 4 HOH 207 707 293 HOH HOH A . 
G 4 HOH 208 708 164 HOH HOH A . 
G 4 HOH 209 709 290 HOH HOH A . 
G 4 HOH 210 710 182 HOH HOH A . 
G 4 HOH 211 711 275 HOH HOH A . 
G 4 HOH 212 712 53  HOH HOH A . 
G 4 HOH 213 713 100 HOH HOH A . 
G 4 HOH 214 714 193 HOH HOH A . 
G 4 HOH 215 715 228 HOH HOH A . 
G 4 HOH 216 716 59  HOH HOH A . 
G 4 HOH 217 717 271 HOH HOH A . 
G 4 HOH 218 718 147 HOH HOH A . 
G 4 HOH 219 719 230 HOH HOH A . 
G 4 HOH 220 720 151 HOH HOH A . 
G 4 HOH 221 721 197 HOH HOH A . 
G 4 HOH 222 722 38  HOH HOH A . 
G 4 HOH 223 723 65  HOH HOH A . 
G 4 HOH 224 724 175 HOH HOH A . 
G 4 HOH 225 725 277 HOH HOH A . 
G 4 HOH 226 726 48  HOH HOH A . 
G 4 HOH 227 727 219 HOH HOH A . 
G 4 HOH 228 728 120 HOH HOH A . 
G 4 HOH 229 729 269 HOH HOH A . 
G 4 HOH 230 730 322 HOH HOH A . 
G 4 HOH 231 731 160 HOH HOH A . 
G 4 HOH 232 732 280 HOH HOH A . 
G 4 HOH 233 733 250 HOH HOH A . 
G 4 HOH 234 734 146 HOH HOH A . 
G 4 HOH 235 735 244 HOH HOH A . 
G 4 HOH 236 736 240 HOH HOH A . 
G 4 HOH 237 737 56  HOH HOH A . 
G 4 HOH 238 738 208 HOH HOH A . 
G 4 HOH 239 739 257 HOH HOH A . 
G 4 HOH 240 740 204 HOH HOH A . 
G 4 HOH 241 741 195 HOH HOH A . 
G 4 HOH 242 742 234 HOH HOH A . 
G 4 HOH 243 743 76  HOH HOH A . 
G 4 HOH 244 744 154 HOH HOH A . 
G 4 HOH 245 745 232 HOH HOH A . 
G 4 HOH 246 746 184 HOH HOH A . 
G 4 HOH 247 747 259 HOH HOH A . 
G 4 HOH 248 748 141 HOH HOH A . 
G 4 HOH 249 749 220 HOH HOH A . 
G 4 HOH 250 750 284 HOH HOH A . 
G 4 HOH 251 751 312 HOH HOH A . 
G 4 HOH 252 752 95  HOH HOH A . 
G 4 HOH 253 753 116 HOH HOH A . 
G 4 HOH 254 754 180 HOH HOH A . 
G 4 HOH 255 755 255 HOH HOH A . 
G 4 HOH 256 756 199 HOH HOH A . 
G 4 HOH 257 757 245 HOH HOH A . 
G 4 HOH 258 758 191 HOH HOH A . 
G 4 HOH 259 759 315 HOH HOH A . 
G 4 HOH 260 760 101 HOH HOH A . 
G 4 HOH 261 761 200 HOH HOH A . 
G 4 HOH 262 762 68  HOH HOH A . 
G 4 HOH 263 763 222 HOH HOH A . 
G 4 HOH 264 764 129 HOH HOH A . 
G 4 HOH 265 765 145 HOH HOH A . 
G 4 HOH 266 766 226 HOH HOH A . 
G 4 HOH 267 767 270 HOH HOH A . 
G 4 HOH 268 768 294 HOH HOH A . 
G 4 HOH 269 769 268 HOH HOH A . 
G 4 HOH 270 770 196 HOH HOH A . 
G 4 HOH 271 771 237 HOH HOH A . 
G 4 HOH 272 772 310 HOH HOH A . 
G 4 HOH 273 773 261 HOH HOH A . 
G 4 HOH 274 774 109 HOH HOH A . 
G 4 HOH 275 775 305 HOH HOH A . 
G 4 HOH 276 776 127 HOH HOH A . 
G 4 HOH 277 777 198 HOH HOH A . 
G 4 HOH 278 778 236 HOH HOH A . 
G 4 HOH 279 779 210 HOH HOH A . 
G 4 HOH 280 780 251 HOH HOH A . 
G 4 HOH 281 781 306 HOH HOH A . 
G 4 HOH 282 782 292 HOH HOH A . 
G 4 HOH 283 783 102 HOH HOH A . 
G 4 HOH 284 784 264 HOH HOH A . 
G 4 HOH 285 785 233 HOH HOH A . 
G 4 HOH 286 786 206 HOH HOH A . 
G 4 HOH 287 787 203 HOH HOH A . 
G 4 HOH 288 788 117 HOH HOH A . 
G 4 HOH 289 789 314 HOH HOH A . 
G 4 HOH 290 790 317 HOH HOH A . 
G 4 HOH 291 791 299 HOH HOH A . 
G 4 HOH 292 792 62  HOH HOH A . 
G 4 HOH 293 793 181 HOH HOH A . 
G 4 HOH 294 794 205 HOH HOH A . 
G 4 HOH 295 795 74  HOH HOH A . 
G 4 HOH 296 796 88  HOH HOH A . 
G 4 HOH 297 797 274 HOH HOH A . 
G 4 HOH 298 798 316 HOH HOH A . 
G 4 HOH 299 799 149 HOH HOH A . 
G 4 HOH 300 800 262 HOH HOH A . 
G 4 HOH 301 801 202 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 102 ? CD  ? A ARG 102 CD  
2  1 Y 1 A ARG 102 ? NE  ? A ARG 102 NE  
3  1 Y 1 A ARG 102 ? CZ  ? A ARG 102 CZ  
4  1 Y 1 A ARG 102 ? NH1 ? A ARG 102 NH1 
5  1 Y 1 A ARG 102 ? NH2 ? A ARG 102 NH2 
6  1 Y 1 A GLN 118 ? CG  ? A GLN 118 CG  
7  1 Y 1 A GLN 118 ? CD  ? A GLN 118 CD  
8  1 Y 1 A GLN 118 ? OE1 ? A GLN 118 OE1 
9  1 Y 1 A GLN 118 ? NE2 ? A GLN 118 NE2 
10 1 Y 1 A LYS 171 ? CD  ? A LYS 171 CD  
11 1 Y 1 A LYS 171 ? CE  ? A LYS 171 CE  
12 1 Y 1 A LYS 171 ? NZ  ? A LYS 171 NZ  
13 1 Y 1 A LYS 193 ? CE  ? A LYS 193 CE  
14 1 Y 1 A LYS 193 ? NZ  ? A LYS 193 NZ  
15 1 Y 1 A LYS 235 ? CE  ? A LYS 235 CE  
16 1 Y 1 A LYS 235 ? NZ  ? A LYS 235 NZ  
17 1 Y 1 A LYS 272 ? CE  ? A LYS 272 CE  
18 1 Y 1 A LYS 272 ? NZ  ? A LYS 272 NZ  
# 
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  ? ? ? '(1.21.1_5286: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? 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                     9DZD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.423 
_cell.length_a_esd                 ? 
_cell.length_b                     46.423 
_cell.length_b_esd                 ? 
_cell.length_c                     361.005 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9DZD 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_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                   9DZD 
_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             2.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.82 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6 
_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    
;10 % Propan-2-ol 
10 % PEG MME 5000 
0.1 M Na Cacodylate pH 6
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-15 
_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   0.953647 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.953647 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DZD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.85 
_reflns.d_resolution_low                               46.04 
_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                                     35632 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.02 
_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                                0.082 
_reflns.pdbx_Rpim_I_all                                0.023 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       450878 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.078 
_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                                    1.85 
_reflns_shell.d_res_low                                     1.89 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2099 
_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                               13.4 
_reflns_shell.pdbx_chi_squared                              1.03 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.423 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.792 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.513 
_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                                 9DZD 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.85 
_refine.ls_d_res_low                             46.04 
_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                     35466 
_refine.ls_number_reflns_R_free                  1999 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 5.64 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1909 
_refine.ls_R_factor_R_free                       0.2216 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1890 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.08 
_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                            0.24 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        46.04 
_refine_hist.number_atoms_solvent             301 
_refine_hist.number_atoms_total               2862 
_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        2530 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_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' ? 0.008  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.817  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.414 ? 1014 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.048  ? 378  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 449  ? 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' 1.85 1.90  . . 137 2283 100.00 . . . . 0.3252 . . . . . . . . . . . 0.3982 
'X-RAY DIFFRACTION' 1.90 1.95  . . 140 2352 100.00 . . . . 0.2717 . . . . . . . . . . . 0.3373 
'X-RAY DIFFRACTION' 1.95 2.00  . . 139 2320 100.00 . . . . 0.2191 . . . . . . . . . . . 0.2845 
'X-RAY DIFFRACTION' 2.00 2.07  . . 139 2334 100.00 . . . . 0.2022 . . . . . . . . . . . 0.2399 
'X-RAY DIFFRACTION' 2.07 2.14  . . 139 2321 100.00 . . . . 0.1937 . . . . . . . . . . . 0.2328 
'X-RAY DIFFRACTION' 2.14 2.23  . . 141 2365 100.00 . . . . 0.1930 . . . . . . . . . . . 0.2365 
'X-RAY DIFFRACTION' 2.23 2.33  . . 141 2375 100.00 . . . . 0.1881 . . . . . . . . . . . 0.2391 
'X-RAY DIFFRACTION' 2.33 2.45  . . 141 2362 100.00 . . . . 0.1842 . . . . . . . . . . . 0.2400 
'X-RAY DIFFRACTION' 2.45 2.61  . . 141 2359 100.00 . . . . 0.1885 . . . . . . . . . . . 0.2360 
'X-RAY DIFFRACTION' 2.61 2.81  . . 142 2367 100.00 . . . . 0.1927 . . . . . . . . . . . 0.2250 
'X-RAY DIFFRACTION' 2.81 3.09  . . 144 2432 100.00 . . . . 0.1965 . . . . . . . . . . . 0.2062 
'X-RAY DIFFRACTION' 3.09 3.54  . . 146 2417 100.00 . . . . 0.1826 . . . . . . . . . . . 0.2401 
'X-RAY DIFFRACTION' 3.54 4.46  . . 148 2484 100.00 . . . . 0.1635 . . . . . . . . . . . 0.1919 
'X-RAY DIFFRACTION' 4.46 46.04 . . 161 2696 100.00 . . . . 0.1868 . . . . . . . . . . . 0.1939 
# 
_struct.entry_id                     9DZD 
_struct.title                        'PvRBP2b N-terminal domain stabilised mutant WHT2484' 
_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        9DZD 
_struct_keywords.text            'Malaria, Red Blood Cell, Reticulocyte Binding Protein, CELL ADHESION' 
_struct_keywords.pdbx_keywords   'CELL ADHESION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0U4ERT5_PLAVI 
_struct_ref.pdbx_db_accession          A0A0U4ERT5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TNTTDNIDYFDISDESNYYLISQLRPHFSNIYFFDEFKRYASYHTEIKRYEDIHKKKVNSLLNEASRAIGICNRAKNTVK
GLINILENPQKFKTQRESYDVKLRQYEEKKEAFRGCLLNKNRKNLDQIKKINNEIRDLLEQLKCSQYCQTNVYFDMIKIY
LVDFKKMPYENYDTFIKQYKNSYLSGVDMIRKIEKQIDNPVTINAIKFTQKEMGYIIDRFEYHLQKVKHSIDQVTALSDG
VKPKQVTKNRLKEYYFNIGNYYSIFKFGKDSLNMLNKALIHKEKIVHNLLGELFGHLEERIS
;
_struct_ref.pdbx_align_begin           169 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9DZD 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 29 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 330 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A0U4ERT5 
_struct_ref_seq.db_align_beg                  169 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  470 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       29 
_struct_ref_seq.pdbx_auth_seq_align_end       330 
# 
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 9DZD MET A 1   ? UNP A0A0U4ERT5 ?   ?   'initiating methionine' 1   1  
1 9DZD SER A 2   ? UNP A0A0U4ERT5 ?   ?   'expression tag'        2   2  
1 9DZD TYR A 3   ? UNP A0A0U4ERT5 ?   ?   'expression tag'        3   3  
1 9DZD TYR A 4   ? UNP A0A0U4ERT5 ?   ?   'expression tag'        4   4  
1 9DZD HIS A 5   ? UNP A0A0U4ERT5 ?   ?   'expression tag'        5   5  
1 9DZD HIS A 6   ? UNP A0A0U4ERT5 ?   ?   'expression tag'        6   6  
1 9DZD HIS A 7   ? UNP A0A0U4ERT5 ?   ?   'expression tag'        7   7  
1 9DZD HIS A 8   ? UNP A0A0U4ERT5 ?   ?   'expression tag'        8   8  
1 9DZD HIS A 9   ? UNP A0A0U4ERT5 ?   ?   'expression tag'        9   9  
1 9DZD HIS A 10  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        10  10 
1 9DZD ASP A 11  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        11  11 
1 9DZD TYR A 12  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        12  12 
1 9DZD ASP A 13  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        13  13 
1 9DZD ILE A 14  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        14  14 
1 9DZD PRO A 15  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        15  15 
1 9DZD THR A 16  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        16  16 
1 9DZD THR A 17  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        17  17 
1 9DZD GLU A 18  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        18  18 
1 9DZD ASN A 19  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        19  19 
1 9DZD LEU A 20  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        20  20 
1 9DZD TYR A 21  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        21  21 
1 9DZD PHE A 22  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        22  22 
1 9DZD GLN A 23  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        23  23 
1 9DZD GLY A 24  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        24  24 
1 9DZD ALA A 25  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        25  25 
1 9DZD MET A 26  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        26  26 
1 9DZD GLY A 27  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        27  27 
1 9DZD SER A 28  ? UNP A0A0U4ERT5 ?   ?   'expression tag'        28  28 
1 9DZD THR A 84  ? UNP A0A0U4ERT5 LYS 224 conflict                84  29 
1 9DZD LEU A 103 ? UNP A0A0U4ERT5 ALA 243 conflict                103 30 
1 9DZD LEU A 107 ? UNP A0A0U4ERT5 VAL 247 conflict                107 31 
1 9DZD LEU A 108 ? UNP A0A0U4ERT5 LYS 248 conflict                108 32 
1 9DZD LEU A 130 ? UNP A0A0U4ERT5 LYS 270 conflict                130 33 
1 9DZD ARG A 169 ? UNP A0A0U4ERT5 GLN 309 conflict                169 34 
1 9DZD ASP A 175 ? UNP A0A0U4ERT5 TYR 315 conflict                175 35 
1 9DZD TRP A 182 ? UNP A0A0U4ERT5 PHE 322 conflict                182 36 
1 9DZD PHE A 184 ? UNP A0A0U4ERT5 MET 324 conflict                184 37 
1 9DZD LEU A 197 ? UNP A0A0U4ERT5 TYR 337 conflict                197 38 
1 9DZD PHE A 207 ? UNP A0A0U4ERT5 TYR 347 conflict                207 39 
1 9DZD TYR A 214 ? UNP A0A0U4ERT5 GLY 354 conflict                214 40 
1 9DZD LEU A 217 ? UNP A0A0U4ERT5 MET 357 conflict                217 41 
1 9DZD TYR A 221 ? UNP A0A0U4ERT5 ILE 361 conflict                221 42 
1 9DZD ASP A 227 ? UNP A0A0U4ERT5 ASN 367 conflict                227 43 
1 9DZD ILE A 229 ? UNP A0A0U4ERT5 VAL 369 conflict                229 44 
1 9DZD LEU A 231 ? UNP A0A0U4ERT5 ILE 371 conflict                231 45 
1 9DZD GLN A 232 ? UNP A0A0U4ERT5 ASN 372 conflict                232 46 
1 9DZD VAL A 237 ? UNP A0A0U4ERT5 THR 377 conflict                237 47 
1 9DZD LEU A 238 ? UNP A0A0U4ERT5 GLN 378 conflict                238 48 
1 9DZD ALA A 258 ? UNP A0A0U4ERT5 SER 398 conflict                258 49 
1 9DZD ILE A 262 ? UNP A0A0U4ERT5 VAL 402 conflict                262 50 
1 9DZD ILE A 265 ? UNP A0A0U4ERT5 LEU 405 conflict                265 51 
1 9DZD ALA A 266 ? UNP A0A0U4ERT5 SER 406 conflict                266 52 
1 9DZD GLU A 278 ? UNP A0A0U4ERT5 ARG 418 conflict                278 53 
1 9DZD ALA A 291 ? UNP A0A0U4ERT5 SER 431 conflict                291 54 
1 9DZD ALA A 296 ? UNP A0A0U4ERT5 GLY 436 conflict                296 55 
1 9DZD GLN A 299 ? UNP A0A0U4ERT5 SER 439 conflict                299 56 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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 PHE A 56  ? SER A 70  ? PHE A 56  SER A 70  1 ? 15 
HELX_P HELX_P2  AA2 TYR A 71  ? LYS A 76  ? TYR A 71  LYS A 76  5 ? 6  
HELX_P HELX_P3  AA3 ARG A 77  ? CYS A 100 ? ARG A 77  CYS A 100 1 ? 24 
HELX_P HELX_P4  AA4 CYS A 100 ? ASN A 116 ? CYS A 100 ASN A 116 1 ? 17 
HELX_P HELX_P5  AA5 ASN A 116 ? THR A 122 ? ASN A 116 THR A 122 1 ? 7  
HELX_P HELX_P6  AA6 SER A 126 ? LYS A 148 ? SER A 126 LYS A 148 1 ? 23 
HELX_P HELX_P7  AA7 ASN A 149 ? GLU A 168 ? ASN A 149 GLU A 168 1 ? 20 
HELX_P HELX_P8  AA8 THR A 178 ? MET A 195 ? THR A 178 MET A 195 1 ? 18 
HELX_P HELX_P9  AA9 PRO A 196 ? ILE A 225 ? PRO A 196 ILE A 225 1 ? 30 
HELX_P HELX_P10 AB1 ASP A 227 ? GLY A 268 ? ASP A 227 GLY A 268 1 ? 42 
HELX_P HELX_P11 AB2 THR A 275 ? ILE A 329 ? THR A 275 ILE A 329 1 ? 55 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 100 SG ? ? ? 1_555 A CYS 144 SG ? ? A CYS 100 A CYS 144 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
disulf2 disulf ? ? A CYS 172 SG ? ? ? 1_555 A CYS 176 SG ? ? A CYS 172 A CYS 176 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 100 ? CYS A 144 ? CYS A 100 ? 1_555 CYS A 144 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 172 ? CYS A 176 ? CYS A 172 ? 1_555 CYS A 176 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ARG 
_struct_mon_prot_cis.label_seq_id           53 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ARG 
_struct_mon_prot_cis.auth_seq_id            53 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    54 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     54 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       10.95 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        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 ASP A 39 ? SER A 41 ? ASP A 39 SER A 41 
AA1 2 LEU A 48 ? SER A 50 ? LEU A 48 SER A 50 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   ILE 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    40 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    ILE 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     40 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   ILE 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    49 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    ILE 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     49 
# 
_pdbx_entry_details.entry_id                   9DZD 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O  A HOH 531 ? ? O A HOH 556 ? ? 1.96 
2 1 NZ A LYS 310 ? ? O A HOH 501 ? ? 2.15 
3 1 O  A HOH 631 ? ? O A HOH 727 ? ? 2.16 
# 
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 HIS A 55  ? ? 78.30   -32.65  
2 1 THR A 84  ? ? -95.71  -72.46  
3 1 SER A 173 ? ? -135.88 -66.16  
4 1 ASP A 227 ? ? -156.71 66.16   
5 1 LYS A 272 ? ? -101.73 -125.98 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     763 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   G 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_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         15.5950 
_pdbx_refine_tls.origin_y         5.2983 
_pdbx_refine_tls.origin_z         -27.0285 
_pdbx_refine_tls.T[1][1]          0.1422 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0284 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0087 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1340 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0001 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2320 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.5939 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.2148 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.5781 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.8999 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -1.0409 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          3.6495 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0126 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0087 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0262 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0030 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0102 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0292 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0379 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0604 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0306 
_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 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       801 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.89 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A SER 2   ? A SER 2   
3  1 Y 1 A TYR 3   ? A TYR 3   
4  1 Y 1 A TYR 4   ? A TYR 4   
5  1 Y 1 A HIS 5   ? A HIS 5   
6  1 Y 1 A HIS 6   ? A HIS 6   
7  1 Y 1 A HIS 7   ? A HIS 7   
8  1 Y 1 A HIS 8   ? A HIS 8   
9  1 Y 1 A HIS 9   ? A HIS 9   
10 1 Y 1 A HIS 10  ? A HIS 10  
11 1 Y 1 A ASP 11  ? A ASP 11  
12 1 Y 1 A TYR 12  ? A TYR 12  
13 1 Y 1 A ASP 13  ? A ASP 13  
14 1 Y 1 A ILE 14  ? A ILE 14  
15 1 Y 1 A PRO 15  ? A PRO 15  
16 1 Y 1 A THR 16  ? A THR 16  
17 1 Y 1 A THR 17  ? A THR 17  
18 1 Y 1 A GLU 18  ? A GLU 18  
19 1 Y 1 A ASN 19  ? A ASN 19  
20 1 Y 1 A LEU 20  ? A LEU 20  
21 1 Y 1 A TYR 21  ? A TYR 21  
22 1 Y 1 A PHE 22  ? A PHE 22  
23 1 Y 1 A GLN 23  ? A GLN 23  
24 1 Y 1 A GLY 24  ? A GLY 24  
25 1 Y 1 A ALA 25  ? A ALA 25  
26 1 Y 1 A MET 26  ? A MET 26  
27 1 Y 1 A GLY 27  ? A GLY 27  
28 1 Y 1 A SER 28  ? A SER 28  
29 1 Y 1 A THR 29  ? A THR 29  
30 1 Y 1 A SER 330 ? A SER 330 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
HOH O    O N N 172 
HOH H1   H N N 173 
HOH H2   H N N 174 
ILE N    N N N 175 
ILE CA   C N S 176 
ILE C    C N N 177 
ILE O    O N N 178 
ILE CB   C N S 179 
ILE CG1  C N N 180 
ILE CG2  C N N 181 
ILE CD1  C N N 182 
ILE OXT  O N N 183 
ILE H    H N N 184 
ILE H2   H N N 185 
ILE HA   H N N 186 
ILE HB   H N N 187 
ILE HG12 H N N 188 
ILE HG13 H N N 189 
ILE HG21 H N N 190 
ILE HG22 H N N 191 
ILE HG23 H N N 192 
ILE HD11 H N N 193 
ILE HD12 H N N 194 
ILE HD13 H N N 195 
ILE HXT  H N N 196 
LEU N    N N N 197 
LEU CA   C N S 198 
LEU C    C N N 199 
LEU O    O N N 200 
LEU CB   C N N 201 
LEU CG   C N N 202 
LEU CD1  C N N 203 
LEU CD2  C N N 204 
LEU OXT  O N N 205 
LEU H    H N N 206 
LEU H2   H N N 207 
LEU HA   H N N 208 
LEU HB2  H N N 209 
LEU HB3  H N N 210 
LEU HG   H N N 211 
LEU HD11 H N N 212 
LEU HD12 H N N 213 
LEU HD13 H N N 214 
LEU HD21 H N N 215 
LEU HD22 H N N 216 
LEU HD23 H N N 217 
LEU HXT  H N N 218 
LYS N    N N N 219 
LYS CA   C N S 220 
LYS C    C N N 221 
LYS O    O N N 222 
LYS CB   C N N 223 
LYS CG   C N N 224 
LYS CD   C N N 225 
LYS CE   C N N 226 
LYS NZ   N N N 227 
LYS OXT  O N N 228 
LYS H    H N N 229 
LYS H2   H N N 230 
LYS HA   H N N 231 
LYS HB2  H N N 232 
LYS HB3  H N N 233 
LYS HG2  H N N 234 
LYS HG3  H N N 235 
LYS HD2  H N N 236 
LYS HD3  H N N 237 
LYS HE2  H N N 238 
LYS HE3  H N N 239 
LYS HZ1  H N N 240 
LYS HZ2  H N N 241 
LYS HZ3  H N N 242 
LYS HXT  H N N 243 
MET N    N N N 244 
MET CA   C N S 245 
MET C    C N N 246 
MET O    O N N 247 
MET CB   C N N 248 
MET CG   C N N 249 
MET SD   S N N 250 
MET CE   C N N 251 
MET OXT  O N N 252 
MET H    H N N 253 
MET H2   H N N 254 
MET HA   H N N 255 
MET HB2  H N N 256 
MET HB3  H N N 257 
MET HG2  H N N 258 
MET HG3  H N N 259 
MET HE1  H N N 260 
MET HE2  H N N 261 
MET HE3  H N N 262 
MET HXT  H N N 263 
PEG C1   C N N 264 
PEG O1   O N N 265 
PEG C2   C N N 266 
PEG O2   O N N 267 
PEG C3   C N N 268 
PEG C4   C N N 269 
PEG O4   O N N 270 
PEG H11  H N N 271 
PEG H12  H N N 272 
PEG HO1  H N N 273 
PEG H21  H N N 274 
PEG H22  H N N 275 
PEG H31  H N N 276 
PEG H32  H N N 277 
PEG H41  H N N 278 
PEG H42  H N N 279 
PEG HO4  H N N 280 
PHE N    N N N 281 
PHE CA   C N S 282 
PHE C    C N N 283 
PHE O    O N N 284 
PHE CB   C N N 285 
PHE CG   C Y N 286 
PHE CD1  C Y N 287 
PHE CD2  C Y N 288 
PHE CE1  C Y N 289 
PHE CE2  C Y N 290 
PHE CZ   C Y N 291 
PHE OXT  O N N 292 
PHE H    H N N 293 
PHE H2   H N N 294 
PHE HA   H N N 295 
PHE HB2  H N N 296 
PHE HB3  H N N 297 
PHE HD1  H N N 298 
PHE HD2  H N N 299 
PHE HE1  H N N 300 
PHE HE2  H N N 301 
PHE HZ   H N N 302 
PHE HXT  H N N 303 
PRO N    N N N 304 
PRO CA   C N S 305 
PRO C    C N N 306 
PRO O    O N N 307 
PRO CB   C N N 308 
PRO CG   C N N 309 
PRO CD   C N N 310 
PRO OXT  O N N 311 
PRO H    H N N 312 
PRO HA   H N N 313 
PRO HB2  H N N 314 
PRO HB3  H N N 315 
PRO HG2  H N N 316 
PRO HG3  H N N 317 
PRO HD2  H N N 318 
PRO HD3  H N N 319 
PRO HXT  H N N 320 
SER N    N N N 321 
SER CA   C N S 322 
SER C    C N N 323 
SER O    O N N 324 
SER CB   C N N 325 
SER OG   O N N 326 
SER OXT  O N N 327 
SER H    H N N 328 
SER H2   H N N 329 
SER HA   H N N 330 
SER HB2  H N N 331 
SER HB3  H N N 332 
SER HG   H N N 333 
SER HXT  H N N 334 
THR N    N N N 335 
THR CA   C N S 336 
THR C    C N N 337 
THR O    O N N 338 
THR CB   C N R 339 
THR OG1  O N N 340 
THR CG2  C N N 341 
THR OXT  O N N 342 
THR H    H N N 343 
THR H2   H N N 344 
THR HA   H N N 345 
THR HB   H N N 346 
THR HG1  H N N 347 
THR HG21 H N N 348 
THR HG22 H N N 349 
THR HG23 H N N 350 
THR HXT  H N N 351 
TRP N    N N N 352 
TRP CA   C N S 353 
TRP C    C N N 354 
TRP O    O N N 355 
TRP CB   C N N 356 
TRP CG   C Y N 357 
TRP CD1  C Y N 358 
TRP CD2  C Y N 359 
TRP NE1  N Y N 360 
TRP CE2  C Y N 361 
TRP CE3  C Y N 362 
TRP CZ2  C Y N 363 
TRP CZ3  C Y N 364 
TRP CH2  C Y N 365 
TRP OXT  O N N 366 
TRP H    H N N 367 
TRP H2   H N N 368 
TRP HA   H N N 369 
TRP HB2  H N N 370 
TRP HB3  H N N 371 
TRP HD1  H N N 372 
TRP HE1  H N N 373 
TRP HE3  H N N 374 
TRP HZ2  H N N 375 
TRP HZ3  H N N 376 
TRP HH2  H N N 377 
TRP HXT  H N N 378 
TYR N    N N N 379 
TYR CA   C N S 380 
TYR C    C N N 381 
TYR O    O N N 382 
TYR CB   C N N 383 
TYR CG   C Y N 384 
TYR CD1  C Y N 385 
TYR CD2  C Y N 386 
TYR CE1  C Y N 387 
TYR CE2  C Y N 388 
TYR CZ   C Y N 389 
TYR OH   O N N 390 
TYR OXT  O N N 391 
TYR H    H N N 392 
TYR H2   H N N 393 
TYR HA   H N N 394 
TYR HB2  H N N 395 
TYR HB3  H N N 396 
TYR HD1  H N N 397 
TYR HD2  H N N 398 
TYR HE1  H N N 399 
TYR HE2  H N N 400 
TYR HH   H N N 401 
TYR HXT  H N N 402 
VAL N    N N N 403 
VAL CA   C N S 404 
VAL C    C N N 405 
VAL O    O N N 406 
VAL CB   C N N 407 
VAL CG1  C N N 408 
VAL CG2  C N N 409 
VAL OXT  O N N 410 
VAL H    H N N 411 
VAL H2   H N N 412 
VAL HA   H N N 413 
VAL HB   H N N 414 
VAL HG11 H N N 415 
VAL HG12 H N N 416 
VAL HG13 H N N 417 
VAL HG21 H N N 418 
VAL HG22 H N N 419 
VAL HG23 H N N 420 
VAL HXT  H N N 421 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PEG C1  O1   sing N N 250 
PEG C1  C2   sing N N 251 
PEG C1  H11  sing N N 252 
PEG C1  H12  sing N N 253 
PEG O1  HO1  sing N N 254 
PEG C2  O2   sing N N 255 
PEG C2  H21  sing N N 256 
PEG C2  H22  sing N N 257 
PEG O2  C3   sing N N 258 
PEG C3  C4   sing N N 259 
PEG C3  H31  sing N N 260 
PEG C3  H32  sing N N 261 
PEG C4  O4   sing N N 262 
PEG C4  H41  sing N N 263 
PEG C4  H42  sing N N 264 
PEG O4  HO4  sing N N 265 
PHE N   CA   sing N N 266 
PHE N   H    sing N N 267 
PHE N   H2   sing N N 268 
PHE CA  C    sing N N 269 
PHE CA  CB   sing N N 270 
PHE CA  HA   sing N N 271 
PHE C   O    doub N N 272 
PHE C   OXT  sing N N 273 
PHE CB  CG   sing N N 274 
PHE CB  HB2  sing N N 275 
PHE CB  HB3  sing N N 276 
PHE CG  CD1  doub Y N 277 
PHE CG  CD2  sing Y N 278 
PHE CD1 CE1  sing Y N 279 
PHE CD1 HD1  sing N N 280 
PHE CD2 CE2  doub Y N 281 
PHE CD2 HD2  sing N N 282 
PHE CE1 CZ   doub Y N 283 
PHE CE1 HE1  sing N N 284 
PHE CE2 CZ   sing Y N 285 
PHE CE2 HE2  sing N N 286 
PHE CZ  HZ   sing N N 287 
PHE OXT HXT  sing N N 288 
PRO N   CA   sing N N 289 
PRO N   CD   sing N N 290 
PRO N   H    sing N N 291 
PRO CA  C    sing N N 292 
PRO CA  CB   sing N N 293 
PRO CA  HA   sing N N 294 
PRO C   O    doub N N 295 
PRO C   OXT  sing N N 296 
PRO CB  CG   sing N N 297 
PRO CB  HB2  sing N N 298 
PRO CB  HB3  sing N N 299 
PRO CG  CD   sing N N 300 
PRO CG  HG2  sing N N 301 
PRO CG  HG3  sing N N 302 
PRO CD  HD2  sing N N 303 
PRO CD  HD3  sing N N 304 
PRO OXT HXT  sing N N 305 
SER N   CA   sing N N 306 
SER N   H    sing N N 307 
SER N   H2   sing N N 308 
SER CA  C    sing N N 309 
SER CA  CB   sing N N 310 
SER CA  HA   sing N N 311 
SER C   O    doub N N 312 
SER C   OXT  sing N N 313 
SER CB  OG   sing N N 314 
SER CB  HB2  sing N N 315 
SER CB  HB3  sing N N 316 
SER OG  HG   sing N N 317 
SER OXT HXT  sing N N 318 
THR N   CA   sing N N 319 
THR N   H    sing N N 320 
THR N   H2   sing N N 321 
THR CA  C    sing N N 322 
THR CA  CB   sing N N 323 
THR CA  HA   sing N N 324 
THR C   O    doub N N 325 
THR C   OXT  sing N N 326 
THR CB  OG1  sing N N 327 
THR CB  CG2  sing N N 328 
THR CB  HB   sing N N 329 
THR OG1 HG1  sing N N 330 
THR CG2 HG21 sing N N 331 
THR CG2 HG22 sing N N 332 
THR CG2 HG23 sing N N 333 
THR OXT HXT  sing N N 334 
TRP N   CA   sing N N 335 
TRP N   H    sing N N 336 
TRP N   H2   sing N N 337 
TRP CA  C    sing N N 338 
TRP CA  CB   sing N N 339 
TRP CA  HA   sing N N 340 
TRP C   O    doub N N 341 
TRP C   OXT  sing N N 342 
TRP CB  CG   sing N N 343 
TRP CB  HB2  sing N N 344 
TRP CB  HB3  sing N N 345 
TRP CG  CD1  doub Y N 346 
TRP CG  CD2  sing Y N 347 
TRP CD1 NE1  sing Y N 348 
TRP CD1 HD1  sing N N 349 
TRP CD2 CE2  doub Y N 350 
TRP CD2 CE3  sing Y N 351 
TRP NE1 CE2  sing Y N 352 
TRP NE1 HE1  sing N N 353 
TRP CE2 CZ2  sing Y N 354 
TRP CE3 CZ3  doub Y N 355 
TRP CE3 HE3  sing N N 356 
TRP CZ2 CH2  doub Y N 357 
TRP CZ2 HZ2  sing N N 358 
TRP CZ3 CH2  sing Y N 359 
TRP CZ3 HZ3  sing N N 360 
TRP CH2 HH2  sing N N 361 
TRP OXT HXT  sing N N 362 
TYR N   CA   sing N N 363 
TYR N   H    sing N N 364 
TYR N   H2   sing N N 365 
TYR CA  C    sing N N 366 
TYR CA  CB   sing N N 367 
TYR CA  HA   sing N N 368 
TYR C   O    doub N N 369 
TYR C   OXT  sing N N 370 
TYR CB  CG   sing N N 371 
TYR CB  HB2  sing N N 372 
TYR CB  HB3  sing N N 373 
TYR CG  CD1  doub Y N 374 
TYR CG  CD2  sing Y N 375 
TYR CD1 CE1  sing Y N 376 
TYR CD1 HD1  sing N N 377 
TYR CD2 CE2  doub Y N 378 
TYR CD2 HD2  sing N N 379 
TYR CE1 CZ   doub Y N 380 
TYR CE1 HE1  sing N N 381 
TYR CE2 CZ   sing Y N 382 
TYR CE2 HE2  sing N N 383 
TYR CZ  OH   sing N N 384 
TYR OH  HH   sing N N 385 
TYR OXT HXT  sing N N 386 
VAL N   CA   sing N N 387 
VAL N   H    sing N N 388 
VAL N   H2   sing N N 389 
VAL CA  C    sing N N 390 
VAL CA  CB   sing N N 391 
VAL CA  HA   sing N N 392 
VAL C   O    doub N N 393 
VAL C   OXT  sing N N 394 
VAL CB  CG1  sing N N 395 
VAL CB  CG2  sing N N 396 
VAL CB  HB   sing N N 397 
VAL CG1 HG11 sing N N 398 
VAL CG1 HG12 sing N N 399 
VAL CG1 HG13 sing N N 400 
VAL CG2 HG21 sing N N 401 
VAL CG2 HG22 sing N N 402 
VAL CG2 HG23 sing N N 403 
VAL OXT HXT  sing N N 404 
# 
_pdbx_audit_support.funding_organization   'National Health and Medical Research Council (NHMRC, Australia)' 
_pdbx_audit_support.country                Australia 
_pdbx_audit_support.grant_number           2016908 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DZD 
_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]   0.021541 
_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]   0.021541 
_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]   0.002770 
_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   . ASN A 1 30  ? 2.448  -8.335  -9.059  1.00 55.29 ? 30  ASN A N   1 
ATOM   2    C CA  . ASN A 1 30  ? 3.692  -7.875  -9.673  1.00 54.30 ? 30  ASN A CA  1 
ATOM   3    C C   . ASN A 1 30  ? 3.909  -6.380  -9.489  1.00 53.67 ? 30  ASN A C   1 
ATOM   4    O O   . ASN A 1 30  ? 3.000  -5.574  -9.698  1.00 53.65 ? 30  ASN A O   1 
ATOM   5    C CB  . ASN A 1 30  ? 3.722  -8.209  -11.170 1.00 55.73 ? 30  ASN A CB  1 
ATOM   6    C CG  . ASN A 1 30  ? 4.070  -9.663  -11.435 1.00 62.18 ? 30  ASN A CG  1 
ATOM   7    O OD1 . ASN A 1 30  ? 4.529  -10.377 -10.542 1.00 62.53 ? 30  ASN A OD1 1 
ATOM   8    N ND2 . ASN A 1 30  ? 3.866  -10.104 -12.673 1.00 66.03 ? 30  ASN A ND2 1 
ATOM   9    N N   . THR A 1 31  ? 5.134  -6.014  -9.111  1.00 47.51 ? 31  THR A N   1 
ATOM   10   C CA  . THR A 1 31  ? 5.465  -4.603  -8.959  1.00 45.94 ? 31  THR A CA  1 
ATOM   11   C C   . THR A 1 31  ? 5.848  -3.948  -10.279 1.00 42.36 ? 31  THR A C   1 
ATOM   12   O O   . THR A 1 31  ? 5.595  -2.754  -10.450 1.00 49.05 ? 31  THR A O   1 
ATOM   13   C CB  . THR A 1 31  ? 6.594  -4.429  -7.943  1.00 41.40 ? 31  THR A CB  1 
ATOM   14   O OG1 . THR A 1 31  ? 7.716  -5.228  -8.330  1.00 47.75 ? 31  THR A OG1 1 
ATOM   15   C CG2 . THR A 1 31  ? 6.108  -4.865  -6.561  1.00 47.33 ? 31  THR A CG2 1 
ATOM   16   N N   . THR A 1 32  ? 6.453  -4.693  -11.208 1.00 37.19 ? 32  THR A N   1 
ATOM   17   C CA  . THR A 1 32  ? 6.863  -4.180  -12.515 1.00 42.82 ? 32  THR A CA  1 
ATOM   18   C C   . THR A 1 32  ? 6.252  -5.054  -13.606 1.00 46.87 ? 32  THR A C   1 
ATOM   19   O O   . THR A 1 32  ? 6.349  -6.285  -13.545 1.00 41.63 ? 32  THR A O   1 
ATOM   20   C CB  . THR A 1 32  ? 8.398  -4.142  -12.647 1.00 38.41 ? 32  THR A CB  1 
ATOM   21   O OG1 . THR A 1 32  ? 8.936  -3.147  -11.755 1.00 38.37 ? 32  THR A OG1 1 
ATOM   22   C CG2 . THR A 1 32  ? 8.826  -3.805  -14.102 1.00 46.91 ? 32  THR A CG2 1 
ATOM   23   N N   . ASP A 1 33  ? 5.617  -4.415  -14.599 1.00 37.64 ? 33  ASP A N   1 
ATOM   24   C CA  . ASP A 1 33  ? 4.906  -5.128  -15.657 1.00 41.37 ? 33  ASP A CA  1 
ATOM   25   C C   . ASP A 1 33  ? 5.566  -5.024  -17.023 1.00 40.53 ? 33  ASP A C   1 
ATOM   26   O O   . ASP A 1 33  ? 5.238  -5.811  -17.916 1.00 38.23 ? 33  ASP A O   1 
ATOM   27   C CB  . ASP A 1 33  ? 3.462  -4.613  -15.763 1.00 51.08 ? 33  ASP A CB  1 
ATOM   28   C CG  . ASP A 1 33  ? 2.680  -4.802  -14.465 1.00 78.83 ? 33  ASP A CG  1 
ATOM   29   O OD1 . ASP A 1 33  ? 2.603  -5.953  -13.977 1.00 78.08 ? 33  ASP A OD1 1 
ATOM   30   O OD2 . ASP A 1 33  ? 2.162  -3.801  -13.920 1.00 75.59 ? 33  ASP A OD2 1 
ATOM   31   N N   . ASN A 1 34  ? 6.479  -4.084  -17.217 1.00 29.94 ? 34  ASN A N   1 
ATOM   32   C CA  . ASN A 1 34  ? 7.245  -4.067  -18.455 1.00 31.57 ? 34  ASN A CA  1 
ATOM   33   C C   . ASN A 1 34  ? 8.618  -3.482  -18.185 1.00 27.99 ? 34  ASN A C   1 
ATOM   34   O O   . ASN A 1 34  ? 8.799  -2.671  -17.267 1.00 31.03 ? 34  ASN A O   1 
ATOM   35   C CB  . ASN A 1 34  ? 6.557  -3.258  -19.549 1.00 41.88 ? 34  ASN A CB  1 
ATOM   36   C CG  . ASN A 1 34  ? 6.793  -1.786  -19.402 1.00 41.18 ? 34  ASN A CG  1 
ATOM   37   O OD1 . ASN A 1 34  ? 7.790  -1.248  -19.899 1.00 30.68 ? 34  ASN A OD1 1 
ATOM   38   N ND2 . ASN A 1 34  ? 5.894  -1.119  -18.694 1.00 46.68 ? 34  ASN A ND2 1 
ATOM   39   N N   . ILE A 1 35  ? 9.574  -3.874  -19.022 1.00 23.47 ? 35  ILE A N   1 
ATOM   40   C CA  . ILE A 1 35  ? 10.942 -3.389  -18.926 1.00 22.66 ? 35  ILE A CA  1 
ATOM   41   C C   . ILE A 1 35  ? 11.370 -2.749  -20.246 1.00 22.63 ? 35  ILE A C   1 
ATOM   42   O O   . ILE A 1 35  ? 12.489 -2.958  -20.719 1.00 20.32 ? 35  ILE A O   1 
ATOM   43   C CB  . ILE A 1 35  ? 11.884 -4.527  -18.509 1.00 23.42 ? 35  ILE A CB  1 
ATOM   44   C CG1 . ILE A 1 35  ? 11.688 -5.730  -19.441 1.00 32.98 ? 35  ILE A CG1 1 
ATOM   45   C CG2 . ILE A 1 35  ? 11.595 -4.873  -17.023 1.00 27.21 ? 35  ILE A CG2 1 
ATOM   46   C CD1 . ILE A 1 35  ? 12.722 -6.853  -19.224 1.00 41.63 ? 35  ILE A CD1 1 
ATOM   47   N N   . ASP A 1 36  ? 10.485 -1.929  -20.821 1.00 22.41 ? 36  ASP A N   1 
ATOM   48   C CA  . ASP A 1 36  ? 10.774 -1.233  -22.077 1.00 21.71 ? 36  ASP A CA  1 
ATOM   49   C C   . ASP A 1 36  ? 12.018 -0.356  -21.990 1.00 24.30 ? 36  ASP A C   1 
ATOM   50   O O   . ASP A 1 36  ? 12.538 0.073   -23.031 1.00 21.34 ? 36  ASP A O   1 
ATOM   51   C CB  . ASP A 1 36  ? 9.597  -0.330  -22.467 1.00 21.19 ? 36  ASP A CB  1 
ATOM   52   C CG  . ASP A 1 36  ? 8.353  -1.094  -22.895 1.00 31.24 ? 36  ASP A CG  1 
ATOM   53   O OD1 . ASP A 1 36  ? 8.445  -2.275  -23.289 1.00 31.94 ? 36  ASP A OD1 1 
ATOM   54   O OD2 . ASP A 1 36  ? 7.258  -0.478  -22.871 1.00 32.52 ? 36  ASP A OD2 1 
ATOM   55   N N   . TYR A 1 37  ? 12.491 -0.054  -20.777 1.00 21.53 ? 37  TYR A N   1 
ATOM   56   C CA  . TYR A 1 37  ? 13.566 0.918   -20.614 1.00 19.58 ? 37  TYR A CA  1 
ATOM   57   C C   . TYR A 1 37  ? 14.934 0.361   -20.962 1.00 20.38 ? 37  TYR A C   1 
ATOM   58   O O   . TYR A 1 37  ? 15.843 1.149   -21.218 1.00 22.86 ? 37  TYR A O   1 
ATOM   59   C CB  . TYR A 1 37  ? 13.583 1.473   -19.179 1.00 21.44 ? 37  TYR A CB  1 
ATOM   60   C CG  . TYR A 1 37  ? 13.517 0.411   -18.097 1.00 20.85 ? 37  TYR A CG  1 
ATOM   61   C CD1 . TYR A 1 37  ? 14.659 -0.258  -17.689 1.00 24.93 ? 37  TYR A CD1 1 
ATOM   62   C CD2 . TYR A 1 37  ? 12.305 0.096   -17.485 1.00 20.67 ? 37  TYR A CD2 1 
ATOM   63   C CE1 . TYR A 1 37  ? 14.604 -1.227  -16.689 1.00 20.95 ? 37  TYR A CE1 1 
ATOM   64   C CE2 . TYR A 1 37  ? 12.228 -0.872  -16.494 1.00 22.59 ? 37  TYR A CE2 1 
ATOM   65   C CZ  . TYR A 1 37  ? 13.385 -1.525  -16.103 1.00 25.60 ? 37  TYR A CZ  1 
ATOM   66   O OH  . TYR A 1 37  ? 13.321 -2.478  -15.124 1.00 33.38 ? 37  TYR A OH  1 
ATOM   67   N N   . PHE A 1 38  ? 15.117 -0.963  -21.001 1.00 21.08 ? 38  PHE A N   1 
ATOM   68   C CA  . PHE A 1 38  ? 16.396 -1.490  -21.459 1.00 21.18 ? 38  PHE A CA  1 
ATOM   69   C C   . PHE A 1 38  ? 16.576 -1.198  -22.945 1.00 21.48 ? 38  PHE A C   1 
ATOM   70   O O   . PHE A 1 38  ? 15.673 -1.461  -23.739 1.00 21.52 ? 38  PHE A O   1 
ATOM   71   C CB  . PHE A 1 38  ? 16.486 -3.001  -21.242 1.00 24.56 ? 38  PHE A CB  1 
ATOM   72   C CG  . PHE A 1 38  ? 16.566 -3.400  -19.803 1.00 20.83 ? 38  PHE A CG  1 
ATOM   73   C CD1 . PHE A 1 38  ? 17.628 -2.973  -19.011 1.00 19.63 ? 38  PHE A CD1 1 
ATOM   74   C CD2 . PHE A 1 38  ? 15.583 -4.198  -19.238 1.00 24.40 ? 38  PHE A CD2 1 
ATOM   75   C CE1 . PHE A 1 38  ? 17.705 -3.352  -17.670 1.00 23.52 ? 38  PHE A CE1 1 
ATOM   76   C CE2 . PHE A 1 38  ? 15.661 -4.567  -17.894 1.00 27.35 ? 38  PHE A CE2 1 
ATOM   77   C CZ  . PHE A 1 38  ? 16.719 -4.130  -17.116 1.00 22.91 ? 38  PHE A CZ  1 
ATOM   78   N N   . ASP A 1 39  ? 17.745 -0.675  -23.322 1.00 20.68 ? 39  ASP A N   1 
ATOM   79   C CA  . ASP A 1 39  ? 18.113 -0.549  -24.736 1.00 21.91 ? 39  ASP A CA  1 
ATOM   80   C C   . ASP A 1 39  ? 19.556 -1.016  -24.890 1.00 24.08 ? 39  ASP A C   1 
ATOM   81   O O   . ASP A 1 39  ? 20.207 -1.411  -23.917 1.00 24.34 ? 39  ASP A O   1 
ATOM   82   C CB  . ASP A 1 39  ? 17.872 0.885   -25.271 1.00 19.13 ? 39  ASP A CB  1 
ATOM   83   C CG  . ASP A 1 39  ? 18.753 1.957   -24.606 1.00 29.56 ? 39  ASP A CG  1 
ATOM   84   O OD1 . ASP A 1 39  ? 19.894 1.669   -24.224 1.00 31.52 ? 39  ASP A OD1 1 
ATOM   85   O OD2 . ASP A 1 39  ? 18.299 3.121   -24.457 1.00 26.50 ? 39  ASP A OD2 1 
ATOM   86   N N   . ILE A 1 40  ? 20.061 -1.009  -26.123 1.00 23.62 ? 40  ILE A N   1 
ATOM   87   C CA  . ILE A 1 40  ? 21.442 -1.427  -26.338 1.00 22.31 ? 40  ILE A CA  1 
ATOM   88   C C   . ILE A 1 40  ? 21.927 -0.831  -27.649 1.00 25.85 ? 40  ILE A C   1 
ATOM   89   O O   . ILE A 1 40  ? 21.171 -0.713  -28.617 1.00 25.17 ? 40  ILE A O   1 
ATOM   90   C CB  . ILE A 1 40  ? 21.576 -2.970  -26.318 1.00 28.93 ? 40  ILE A CB  1 
ATOM   91   C CG1 . ILE A 1 40  ? 23.056 -3.374  -26.382 1.00 29.39 ? 40  ILE A CG1 1 
ATOM   92   C CG2 . ILE A 1 40  ? 20.747 -3.607  -27.447 1.00 27.86 ? 40  ILE A CG2 1 
ATOM   93   C CD1 . ILE A 1 40  ? 23.333 -4.851  -26.075 1.00 32.29 ? 40  ILE A CD1 1 
ATOM   94   N N   . SER A 1 41  ? 23.197 -0.457  -27.676 1.00 27.51 ? 41  SER A N   1 
ATOM   95   C CA  . SER A 1 41  ? 23.813 -0.017  -28.909 1.00 26.46 ? 41  SER A CA  1 
ATOM   96   C C   . SER A 1 41  ? 24.742 -1.096  -29.435 1.00 28.62 ? 41  SER A C   1 
ATOM   97   O O   . SER A 1 41  ? 25.242 -1.940  -28.682 1.00 31.94 ? 41  SER A O   1 
ATOM   98   C CB  . SER A 1 41  ? 24.571 1.292   -28.695 1.00 35.05 ? 41  SER A CB  1 
ATOM   99   O OG  . SER A 1 41  ? 23.629 2.328   -28.462 1.00 37.15 ? 41  SER A OG  1 
ATOM   100  N N   . ASP A 1 42  ? 24.969 -1.057  -30.745 1.00 30.22 ? 42  ASP A N   1 
ATOM   101  C CA  . ASP A 1 42  ? 25.907 -1.988  -31.343 1.00 33.94 ? 42  ASP A CA  1 
ATOM   102  C C   . ASP A 1 42  ? 27.330 -1.591  -30.956 1.00 41.12 ? 42  ASP A C   1 
ATOM   103  O O   . ASP A 1 42  ? 27.576 -0.506  -30.411 1.00 36.68 ? 42  ASP A O   1 
ATOM   104  C CB  . ASP A 1 42  ? 25.743 -2.019  -32.861 1.00 34.86 ? 42  ASP A CB  1 
ATOM   105  C CG  . ASP A 1 42  ? 26.417 -0.854  -33.545 1.00 35.51 ? 42  ASP A CG  1 
ATOM   106  O OD1 . ASP A 1 42  ? 26.044 0.312   -33.280 1.00 37.18 ? 42  ASP A OD1 1 
ATOM   107  O OD2 . ASP A 1 42  ? 27.330 -1.109  -34.360 1.00 45.77 ? 42  ASP A OD2 1 
ATOM   108  N N   . GLU A 1 43  ? 28.281 -2.481  -31.266 1.00 35.02 ? 43  GLU A N   1 
ATOM   109  C CA  . GLU A 1 43  ? 29.639 -2.304  -30.761 1.00 42.30 ? 43  GLU A CA  1 
ATOM   110  C C   . GLU A 1 43  ? 30.300 -1.052  -31.326 1.00 42.27 ? 43  GLU A C   1 
ATOM   111  O O   . GLU A 1 43  ? 31.175 -0.468  -30.681 1.00 46.75 ? 43  GLU A O   1 
ATOM   112  C CB  . GLU A 1 43  ? 30.473 -3.547  -31.070 1.00 45.28 ? 43  GLU A CB  1 
ATOM   113  C CG  . GLU A 1 43  ? 30.097 -4.757  -30.229 1.00 39.07 ? 43  GLU A CG  1 
ATOM   114  C CD  . GLU A 1 43  ? 28.964 -5.589  -30.827 1.00 45.23 ? 43  GLU A CD  1 
ATOM   115  O OE1 . GLU A 1 43  ? 28.344 -5.151  -31.822 1.00 46.27 ? 43  GLU A OE1 1 
ATOM   116  O OE2 . GLU A 1 43  ? 28.693 -6.689  -30.294 1.00 49.69 ? 43  GLU A OE2 1 
ATOM   117  N N   . SER A 1 44  ? 29.898 -0.621  -32.516 1.00 47.48 ? 44  SER A N   1 
ATOM   118  C CA  . SER A 1 44  ? 30.454 0.583   -33.119 1.00 42.36 ? 44  SER A CA  1 
ATOM   119  C C   . SER A 1 44  ? 29.871 1.863   -32.532 1.00 41.70 ? 44  SER A C   1 
ATOM   120  O O   . SER A 1 44  ? 30.339 2.948   -32.887 1.00 41.96 ? 44  SER A O   1 
ATOM   121  C CB  . SER A 1 44  ? 30.211 0.567   -34.634 1.00 46.96 ? 44  SER A CB  1 
ATOM   122  O OG  . SER A 1 44  ? 28.822 0.732   -34.921 1.00 41.33 ? 44  SER A OG  1 
ATOM   123  N N   . ASN A 1 45  ? 28.853 1.757   -31.669 1.00 42.64 ? 45  ASN A N   1 
ATOM   124  C CA  . ASN A 1 45  ? 28.128 2.892   -31.095 1.00 40.44 ? 45  ASN A CA  1 
ATOM   125  C C   . ASN A 1 45  ? 27.388 3.710   -32.145 1.00 43.23 ? 45  ASN A C   1 
ATOM   126  O O   . ASN A 1 45  ? 27.043 4.874   -31.908 1.00 42.96 ? 45  ASN A O   1 
ATOM   127  C CB  . ASN A 1 45  ? 29.052 3.804   -30.283 1.00 54.41 ? 45  ASN A CB  1 
ATOM   128  C CG  . ASN A 1 45  ? 28.877 3.625   -28.796 1.00 62.67 ? 45  ASN A CG  1 
ATOM   129  O OD1 . ASN A 1 45  ? 28.800 2.499   -28.292 1.00 65.06 ? 45  ASN A OD1 1 
ATOM   130  N ND2 . ASN A 1 45  ? 28.802 4.739   -28.078 1.00 69.85 ? 45  ASN A ND2 1 
ATOM   131  N N   . TYR A 1 46  ? 27.115 3.119   -33.304 1.00 36.68 ? 46  TYR A N   1 
ATOM   132  C CA  . TYR A 1 46  ? 26.462 3.843   -34.377 1.00 33.00 ? 46  TYR A CA  1 
ATOM   133  C C   . TYR A 1 46  ? 24.942 3.688   -34.342 1.00 34.97 ? 46  TYR A C   1 
ATOM   134  O O   . TYR A 1 46  ? 24.213 4.632   -34.669 1.00 34.68 ? 46  TYR A O   1 
ATOM   135  C CB  . TYR A 1 46  ? 27.027 3.360   -35.717 1.00 39.10 ? 46  TYR A CB  1 
ATOM   136  C CG  . TYR A 1 46  ? 26.671 4.227   -36.887 1.00 36.20 ? 46  TYR A CG  1 
ATOM   137  C CD1 . TYR A 1 46  ? 25.673 3.848   -37.770 1.00 43.69 ? 46  TYR A CD1 1 
ATOM   138  C CD2 . TYR A 1 46  ? 27.329 5.423   -37.113 1.00 46.33 ? 46  TYR A CD2 1 
ATOM   139  C CE1 . TYR A 1 46  ? 25.334 4.632   -38.854 1.00 43.58 ? 46  TYR A CE1 1 
ATOM   140  C CE2 . TYR A 1 46  ? 27.000 6.221   -38.200 1.00 47.52 ? 46  TYR A CE2 1 
ATOM   141  C CZ  . TYR A 1 46  ? 26.000 5.818   -39.066 1.00 47.12 ? 46  TYR A CZ  1 
ATOM   142  O OH  . TYR A 1 46  ? 25.657 6.597   -40.144 1.00 55.23 ? 46  TYR A OH  1 
ATOM   143  N N   . TYR A 1 47  ? 24.450 2.508   -33.975 1.00 28.63 ? 47  TYR A N   1 
ATOM   144  C CA  . TYR A 1 47  ? 23.023 2.209   -33.947 1.00 26.38 ? 47  TYR A CA  1 
ATOM   145  C C   . TYR A 1 47  ? 22.575 1.979   -32.517 1.00 27.04 ? 47  TYR A C   1 
ATOM   146  O O   . TYR A 1 47  ? 23.261 1.299   -31.758 1.00 26.95 ? 47  TYR A O   1 
ATOM   147  C CB  . TYR A 1 47  ? 22.702 0.945   -34.732 1.00 27.65 ? 47  TYR A CB  1 
ATOM   148  C CG  . TYR A 1 47  ? 23.153 1.002   -36.166 1.00 26.32 ? 47  TYR A CG  1 
ATOM   149  C CD1 . TYR A 1 47  ? 22.443 1.749   -37.096 1.00 28.62 ? 47  TYR A CD1 1 
ATOM   150  C CD2 . TYR A 1 47  ? 24.269 0.300   -36.594 1.00 34.97 ? 47  TYR A CD2 1 
ATOM   151  C CE1 . TYR A 1 47  ? 22.840 1.799   -38.435 1.00 30.26 ? 47  TYR A CE1 1 
ATOM   152  C CE2 . TYR A 1 47  ? 24.680 0.348   -37.944 1.00 34.21 ? 47  TYR A CE2 1 
ATOM   153  C CZ  . TYR A 1 47  ? 23.956 1.094   -38.845 1.00 31.55 ? 47  TYR A CZ  1 
ATOM   154  O OH  . TYR A 1 47  ? 24.355 1.153   -40.173 1.00 34.88 ? 47  TYR A OH  1 
ATOM   155  N N   . LEU A 1 48  ? 21.399 2.489   -32.182 1.00 22.31 ? 48  LEU A N   1 
ATOM   156  C CA  . LEU A 1 48  ? 20.804 2.267   -30.871 1.00 26.02 ? 48  LEU A CA  1 
ATOM   157  C C   . LEU A 1 48  ? 19.497 1.528   -31.087 1.00 24.32 ? 48  LEU A C   1 
ATOM   158  O O   . LEU A 1 48  ? 18.629 1.995   -31.837 1.00 27.52 ? 48  LEU A O   1 
ATOM   159  C CB  . LEU A 1 48  ? 20.569 3.576   -30.121 1.00 26.02 ? 48  LEU A CB  1 
ATOM   160  C CG  . LEU A 1 48  ? 20.013 3.216   -28.733 1.00 30.93 ? 48  LEU A CG  1 
ATOM   161  C CD1 . LEU A 1 48  ? 20.732 3.955   -27.637 1.00 38.63 ? 48  LEU A CD1 1 
ATOM   162  C CD2 . LEU A 1 48  ? 18.508 3.444   -28.667 1.00 24.24 ? 48  LEU A CD2 1 
ATOM   163  N N   . ILE A 1 49  ? 19.363 0.384   -30.435 1.00 21.10 ? 49  ILE A N   1 
ATOM   164  C CA  . ILE A 1 49  ? 18.198 -0.475  -30.581 1.00 22.65 ? 49  ILE A CA  1 
ATOM   165  C C   . ILE A 1 49  ? 17.272 -0.247  -29.392 1.00 25.53 ? 49  ILE A C   1 
ATOM   166  O O   . ILE A 1 49  ? 17.688 -0.382  -28.238 1.00 21.79 ? 49  ILE A O   1 
ATOM   167  C CB  . ILE A 1 49  ? 18.627 -1.941  -30.687 1.00 24.38 ? 49  ILE A CB  1 
ATOM   168  C CG1 . ILE A 1 49  ? 19.515 -2.098  -31.934 1.00 33.30 ? 49  ILE A CG1 1 
ATOM   169  C CG2 . ILE A 1 49  ? 17.423 -2.853  -30.758 1.00 27.21 ? 49  ILE A CG2 1 
ATOM   170  C CD1 . ILE A 1 49  ? 20.185 -3.440  -32.050 1.00 33.80 ? 49  ILE A CD1 1 
ATOM   171  N N   . SER A 1 50  ? 16.019 0.086   -29.672 1.00 21.71 ? 50  SER A N   1 
ATOM   172  C CA  . SER A 1 50  ? 15.001 0.266   -28.647 1.00 19.13 ? 50  SER A CA  1 
ATOM   173  C C   . SER A 1 50  ? 13.959 -0.842  -28.745 1.00 19.62 ? 50  SER A C   1 
ATOM   174  O O   . SER A 1 50  ? 13.679 -1.358  -29.831 1.00 20.78 ? 50  SER A O   1 
ATOM   175  C CB  . SER A 1 50  ? 14.306 1.623   -28.818 1.00 20.56 ? 50  SER A CB  1 
ATOM   176  O OG  . SER A 1 50  ? 13.165 1.730   -27.965 1.00 21.48 ? 50  SER A OG  1 
ATOM   177  N N   . GLN A 1 51  ? 13.360 -1.190  -27.608 1.00 19.52 ? 51  GLN A N   1 
ATOM   178  C CA  . GLN A 1 51  ? 12.238 -2.118  -27.643 1.00 21.11 ? 51  GLN A CA  1 
ATOM   179  C C   . GLN A 1 51  ? 10.989 -1.482  -28.222 1.00 20.73 ? 51  GLN A C   1 
ATOM   180  O O   . GLN A 1 51  ? 10.066 -2.205  -28.620 1.00 20.31 ? 51  GLN A O   1 
ATOM   181  C CB  . GLN A 1 51  ? 11.944 -2.620  -26.226 1.00 16.41 ? 51  GLN A CB  1 
ATOM   182  C CG  . GLN A 1 51  ? 13.098 -3.414  -25.669 1.00 16.97 ? 51  GLN A CG  1 
ATOM   183  C CD  . GLN A 1 51  ? 12.798 -3.843  -24.255 1.00 20.04 ? 51  GLN A CD  1 
ATOM   184  O OE1 . GLN A 1 51  ? 11.882 -4.629  -24.032 1.00 19.50 ? 51  GLN A OE1 1 
ATOM   185  N NE2 . GLN A 1 51  ? 13.532 -3.289  -23.291 1.00 19.20 ? 51  GLN A NE2 1 
ATOM   186  N N   . LEU A 1 52  ? 10.919 -0.155  -28.243 1.00 18.85 ? 52  LEU A N   1 
ATOM   187  C CA  . LEU A 1 52  ? 9.769  0.534   -28.821 1.00 18.94 ? 52  LEU A CA  1 
ATOM   188  C C   . LEU A 1 52  ? 9.877  0.555   -30.348 1.00 19.96 ? 52  LEU A C   1 
ATOM   189  O O   . LEU A 1 52  ? 10.885 1.009   -30.893 1.00 17.56 ? 52  LEU A O   1 
ATOM   190  C CB  . LEU A 1 52  ? 9.698  1.966   -28.300 1.00 18.98 ? 52  LEU A CB  1 
ATOM   191  C CG  . LEU A 1 52  ? 9.582  2.176   -26.787 1.00 24.41 ? 52  LEU A CG  1 
ATOM   192  C CD1 . LEU A 1 52  ? 9.412  3.662   -26.493 1.00 24.20 ? 52  LEU A CD1 1 
ATOM   193  C CD2 . LEU A 1 52  ? 8.405  1.371   -26.263 1.00 24.60 ? 52  LEU A CD2 1 
ATOM   194  N N   . ARG A 1 53  ? 8.839  0.068   -31.023 1.00 16.73 ? 53  ARG A N   1 
ATOM   195  C CA  . ARG A 1 53  ? 8.757  0.207   -32.475 1.00 19.50 ? 53  ARG A CA  1 
ATOM   196  C C   . ARG A 1 53  ? 8.835  1.698   -32.818 1.00 22.91 ? 53  ARG A C   1 
ATOM   197  O O   . ARG A 1 53  ? 8.237  2.527   -32.106 1.00 21.37 ? 53  ARG A O   1 
ATOM   198  C CB  . ARG A 1 53  ? 7.434  -0.413  -32.943 1.00 22.91 ? 53  ARG A CB  1 
ATOM   199  C CG  . ARG A 1 53  ? 7.257  -0.619  -34.462 1.00 23.46 ? 53  ARG A CG  1 
ATOM   200  C CD  . ARG A 1 53  ? 5.850  -1.151  -34.756 1.00 23.85 ? 53  ARG A CD  1 
ATOM   201  N NE  . ARG A 1 53  ? 5.494  -1.184  -36.178 1.00 26.03 ? 53  ARG A NE  1 
ATOM   202  C CZ  . ARG A 1 53  ? 5.590  -2.260  -36.953 1.00 28.13 ? 53  ARG A CZ  1 
ATOM   203  N NH1 . ARG A 1 53  ? 6.134  -3.384  -36.510 1.00 31.59 ? 53  ARG A NH1 1 
ATOM   204  N NH2 . ARG A 1 53  ? 5.114  -2.213  -38.198 1.00 24.96 ? 53  ARG A NH2 1 
ATOM   205  N N   . PRO A 1 54  ? 9.575  2.100   -33.877 1.00 22.01 ? 54  PRO A N   1 
ATOM   206  C CA  . PRO A 1 54  ? 10.199 1.310   -34.950 1.00 20.90 ? 54  PRO A CA  1 
ATOM   207  C C   . PRO A 1 54  ? 11.605 0.825   -34.621 1.00 23.39 ? 54  PRO A C   1 
ATOM   208  O O   . PRO A 1 54  ? 12.303 0.440   -35.559 1.00 21.85 ? 54  PRO A O   1 
ATOM   209  C CB  . PRO A 1 54  ? 10.180 2.299   -36.144 1.00 21.13 ? 54  PRO A CB  1 
ATOM   210  C CG  . PRO A 1 54  ? 10.447 3.631   -35.476 1.00 25.82 ? 54  PRO A CG  1 
ATOM   211  C CD  . PRO A 1 54  ? 9.679  3.554   -34.153 1.00 23.76 ? 54  PRO A CD  1 
ATOM   212  N N   . HIS A 1 55  ? 12.043 0.861   -33.347 1.00 20.26 ? 55  HIS A N   1 
ATOM   213  C CA  . HIS A 1 55  ? 13.239 0.160   -32.860 1.00 20.34 ? 55  HIS A CA  1 
ATOM   214  C C   . HIS A 1 55  ? 14.571 0.830   -33.189 1.00 22.41 ? 55  HIS A C   1 
ATOM   215  O O   . HIS A 1 55  ? 15.524 0.720   -32.410 1.00 20.44 ? 55  HIS A O   1 
ATOM   216  C CB  . HIS A 1 55  ? 13.245 -1.285  -33.378 1.00 21.28 ? 55  HIS A CB  1 
ATOM   217  C CG  . HIS A 1 55  ? 11.992 -2.029  -33.044 1.00 19.05 ? 55  HIS A CG  1 
ATOM   218  N ND1 . HIS A 1 55  ? 11.558 -2.197  -31.744 1.00 19.33 ? 55  HIS A ND1 1 
ATOM   219  C CD2 . HIS A 1 55  ? 11.034 -2.565  -33.837 1.00 20.53 ? 55  HIS A CD2 1 
ATOM   220  C CE1 . HIS A 1 55  ? 10.406 -2.850  -31.755 1.00 24.64 ? 55  HIS A CE1 1 
ATOM   221  N NE2 . HIS A 1 55  ? 10.061 -3.070  -33.012 1.00 21.77 ? 55  HIS A NE2 1 
ATOM   222  N N   . PHE A 1 56  ? 14.670 1.513   -34.338 1.00 22.62 ? 56  PHE A N   1 
ATOM   223  C CA  . PHE A 1 56  ? 15.857 2.299   -34.669 1.00 23.89 ? 56  PHE A CA  1 
ATOM   224  C C   . PHE A 1 56  ? 15.400 3.649   -35.187 1.00 21.79 ? 56  PHE A C   1 
ATOM   225  O O   . PHE A 1 56  ? 14.455 3.709   -35.975 1.00 24.39 ? 56  PHE A O   1 
ATOM   226  C CB  . PHE A 1 56  ? 16.735 1.661   -35.787 1.00 27.71 ? 56  PHE A CB  1 
ATOM   227  C CG  . PHE A 1 56  ? 16.668 0.156   -35.864 1.00 26.24 ? 56  PHE A CG  1 
ATOM   228  C CD1 . PHE A 1 56  ? 17.419 -0.636  -35.017 1.00 31.77 ? 56  PHE A CD1 1 
ATOM   229  C CD2 . PHE A 1 56  ? 15.875 -0.461  -36.817 1.00 37.66 ? 56  PHE A CD2 1 
ATOM   230  C CE1 . PHE A 1 56  ? 17.364 -2.039  -35.108 1.00 30.19 ? 56  PHE A CE1 1 
ATOM   231  C CE2 . PHE A 1 56  ? 15.820 -1.848  -36.913 1.00 35.24 ? 56  PHE A CE2 1 
ATOM   232  C CZ  . PHE A 1 56  ? 16.560 -2.639  -36.050 1.00 33.66 ? 56  PHE A CZ  1 
ATOM   233  N N   . SER A 1 57  ? 16.105 4.720   -34.800 1.00 21.62 ? 57  SER A N   1 
ATOM   234  C CA  . SER A 1 57  ? 15.759 6.037   -35.353 1.00 23.02 ? 57  SER A CA  1 
ATOM   235  C C   . SER A 1 57  ? 15.923 6.053   -36.862 1.00 23.54 ? 57  SER A C   1 
ATOM   236  O O   . SER A 1 57  ? 15.257 6.837   -37.552 1.00 22.81 ? 57  SER A O   1 
ATOM   237  C CB  . SER A 1 57  ? 16.629 7.136   -34.739 1.00 24.24 ? 57  SER A CB  1 
ATOM   238  O OG  . SER A 1 57  ? 17.996 6.967   -35.101 1.00 28.26 ? 57  SER A OG  1 
ATOM   239  N N   . ASN A 1 58  ? 16.791 5.185   -37.395 1.00 24.35 ? 58  ASN A N   1 
ATOM   240  C CA  . ASN A 1 58  ? 17.033 5.181   -38.834 1.00 25.70 ? 58  ASN A CA  1 
ATOM   241  C C   . ASN A 1 58  ? 15.760 4.921   -39.620 1.00 28.61 ? 58  ASN A C   1 
ATOM   242  O O   . ASN A 1 58  ? 15.624 5.397   -40.756 1.00 25.74 ? 58  ASN A O   1 
ATOM   243  C CB  . ASN A 1 58  ? 18.087 4.126   -39.187 1.00 23.13 ? 58  ASN A CB  1 
ATOM   244  C CG  . ASN A 1 58  ? 19.285 4.191   -38.278 1.00 31.10 ? 58  ASN A CG  1 
ATOM   245  O OD1 . ASN A 1 58  ? 19.235 3.716   -37.149 1.00 29.53 ? 58  ASN A OD1 1 
ATOM   246  N ND2 . ASN A 1 58  ? 20.363 4.808   -38.750 1.00 28.87 ? 58  ASN A ND2 1 
ATOM   247  N N   . ILE A 1 59  ? 14.816 4.171   -39.043 1.00 22.72 ? 59  ILE A N   1 
ATOM   248  C CA  . ILE A 1 59  ? 13.550 3.939   -39.732 1.00 23.07 ? 59  ILE A CA  1 
ATOM   249  C C   . ILE A 1 59  ? 12.812 5.253   -39.930 1.00 24.74 ? 59  ILE A C   1 
ATOM   250  O O   . ILE A 1 59  ? 12.194 5.488   -40.980 1.00 26.70 ? 59  ILE A O   1 
ATOM   251  C CB  . ILE A 1 59  ? 12.678 2.933   -38.963 1.00 26.85 ? 59  ILE A CB  1 
ATOM   252  C CG1 . ILE A 1 59  ? 13.396 1.596   -38.793 1.00 30.88 ? 59  ILE A CG1 1 
ATOM   253  C CG2 . ILE A 1 59  ? 11.323 2.776   -39.659 1.00 23.23 ? 59  ILE A CG2 1 
ATOM   254  C CD1 . ILE A 1 59  ? 13.857 0.987   -40.067 1.00 27.38 ? 59  ILE A CD1 1 
ATOM   255  N N   . TYR A 1 60  ? 12.858 6.132   -38.926 1.00 23.67 ? 60  TYR A N   1 
ATOM   256  C CA  . TYR A 1 60  ? 12.236 7.439   -39.100 1.00 21.87 ? 60  TYR A CA  1 
ATOM   257  C C   . TYR A 1 60  ? 12.952 8.271   -40.160 1.00 23.63 ? 60  TYR A C   1 
ATOM   258  O O   . TYR A 1 60  ? 12.326 9.140   -40.775 1.00 27.31 ? 60  TYR A O   1 
ATOM   259  C CB  . TYR A 1 60  ? 12.195 8.197   -37.770 1.00 23.93 ? 60  TYR A CB  1 
ATOM   260  C CG  . TYR A 1 60  ? 11.059 7.765   -36.858 1.00 28.66 ? 60  TYR A CG  1 
ATOM   261  C CD1 . TYR A 1 60  ? 9.811  7.430   -37.384 1.00 25.67 ? 60  TYR A CD1 1 
ATOM   262  C CD2 . TYR A 1 60  ? 11.232 7.700   -35.481 1.00 25.49 ? 60  TYR A CD2 1 
ATOM   263  C CE1 . TYR A 1 60  ? 8.766  7.047   -36.556 1.00 28.38 ? 60  TYR A CE1 1 
ATOM   264  C CE2 . TYR A 1 60  ? 10.189 7.306   -34.637 1.00 28.99 ? 60  TYR A CE2 1 
ATOM   265  C CZ  . TYR A 1 60  ? 8.962  6.983   -35.187 1.00 28.72 ? 60  TYR A CZ  1 
ATOM   266  O OH  . TYR A 1 60  ? 7.920  6.594   -34.374 1.00 26.70 ? 60  TYR A OH  1 
ATOM   267  N N   . PHE A 1 61  ? 14.261 8.065   -40.364 1.00 23.43 ? 61  PHE A N   1 
ATOM   268  C CA  . PHE A 1 61  ? 14.898 8.718   -41.506 1.00 22.76 ? 61  PHE A CA  1 
ATOM   269  C C   . PHE A 1 61  ? 14.288 8.229   -42.820 1.00 26.23 ? 61  PHE A C   1 
ATOM   270  O O   . PHE A 1 61  ? 13.945 9.033   -43.696 1.00 26.14 ? 61  PHE A O   1 
ATOM   271  C CB  . PHE A 1 61  ? 16.412 8.508   -41.511 1.00 24.71 ? 61  PHE A CB  1 
ATOM   272  C CG  . PHE A 1 61  ? 17.045 8.917   -42.815 1.00 24.00 ? 61  PHE A CG  1 
ATOM   273  C CD1 . PHE A 1 61  ? 17.049 10.251  -43.207 1.00 28.24 ? 61  PHE A CD1 1 
ATOM   274  C CD2 . PHE A 1 61  ? 17.548 7.964   -43.686 1.00 26.69 ? 61  PHE A CD2 1 
ATOM   275  C CE1 . PHE A 1 61  ? 17.585 10.637  -44.453 1.00 27.06 ? 61  PHE A CE1 1 
ATOM   276  C CE2 . PHE A 1 61  ? 18.095 8.324   -44.929 1.00 27.52 ? 61  PHE A CE2 1 
ATOM   277  C CZ  . PHE A 1 61  ? 18.107 9.669   -45.322 1.00 29.78 ? 61  PHE A CZ  1 
ATOM   278  N N   . PHE A 1 62  ? 14.122 6.912   -42.975 1.00 25.48 ? 62  PHE A N   1 
ATOM   279  C CA  . PHE A 1 62  ? 13.486 6.426   -44.196 1.00 27.41 ? 62  PHE A CA  1 
ATOM   280  C C   . PHE A 1 62  ? 12.097 7.034   -44.350 1.00 29.26 ? 62  PHE A C   1 
ATOM   281  O O   . PHE A 1 62  ? 11.663 7.352   -45.472 1.00 28.28 ? 62  PHE A O   1 
ATOM   282  C CB  . PHE A 1 62  ? 13.424 4.883   -44.211 1.00 20.41 ? 62  PHE A CB  1 
ATOM   283  C CG  . PHE A 1 62  ? 14.776 4.204   -44.078 1.00 28.89 ? 62  PHE A CG  1 
ATOM   284  C CD1 . PHE A 1 62  ? 15.903 4.735   -44.693 1.00 28.18 ? 62  PHE A CD1 1 
ATOM   285  C CD2 . PHE A 1 62  ? 14.920 3.026   -43.342 1.00 25.07 ? 62  PHE A CD2 1 
ATOM   286  C CE1 . PHE A 1 62  ? 17.158 4.110   -44.580 1.00 30.94 ? 62  PHE A CE1 1 
ATOM   287  C CE2 . PHE A 1 62  ? 16.174 2.400   -43.215 1.00 25.08 ? 62  PHE A CE2 1 
ATOM   288  C CZ  . PHE A 1 62  ? 17.297 2.945   -43.834 1.00 23.85 ? 62  PHE A CZ  1 
ATOM   289  N N   . ASP A 1 63  ? 11.391 7.235   -43.227 1.00 26.22 ? 63  ASP A N   1 
ATOM   290  C CA  . ASP A 1 63  ? 10.079 7.880   -43.272 1.00 27.42 ? 63  ASP A CA  1 
ATOM   291  C C   . ASP A 1 63  ? 10.175 9.341   -43.716 1.00 25.92 ? 63  ASP A C   1 
ATOM   292  O O   . ASP A 1 63  ? 9.333  9.803   -44.494 1.00 28.38 ? 63  ASP A O   1 
ATOM   293  C CB  . ASP A 1 63  ? 9.388  7.817   -41.890 1.00 29.63 ? 63  ASP A CB  1 
ATOM   294  C CG  . ASP A 1 63  ? 8.983  6.387   -41.457 1.00 40.93 ? 63  ASP A CG  1 
ATOM   295  O OD1 . ASP A 1 63  ? 8.916  5.458   -42.295 1.00 36.85 ? 63  ASP A OD1 1 
ATOM   296  O OD2 . ASP A 1 63  ? 8.709  6.197   -40.249 1.00 38.24 ? 63  ASP A OD2 1 
ATOM   297  N N   . GLU A 1 64  ? 11.149 10.105  -43.179 1.00 28.54 ? 64  GLU A N   1 
ATOM   298  C CA  . GLU A 1 64  ? 11.343 11.503  -43.592 1.00 25.51 ? 64  GLU A CA  1 
ATOM   299  C C   . GLU A 1 64  ? 11.761 11.617  -45.048 1.00 23.16 ? 64  GLU A C   1 
ATOM   300  O O   . GLU A 1 64  ? 11.373 12.578  -45.733 1.00 24.57 ? 64  GLU A O   1 
ATOM   301  C CB  . GLU A 1 64  ? 12.423 12.206  -42.754 1.00 27.05 ? 64  GLU A CB  1 
ATOM   302  C CG  . GLU A 1 64  ? 11.962 12.850  -41.458 1.00 39.92 ? 64  GLU A CG  1 
ATOM   303  C CD  . GLU A 1 64  ? 10.634 13.568  -41.589 1.00 35.52 ? 64  GLU A CD  1 
ATOM   304  O OE1 . GLU A 1 64  ? 10.605 14.717  -42.095 1.00 33.07 ? 64  GLU A OE1 1 
ATOM   305  O OE2 . GLU A 1 64  ? 9.618  12.967  -41.184 1.00 41.36 ? 64  GLU A OE2 1 
ATOM   306  N N   . PHE A 1 65  ? 12.571 10.678  -45.538 1.00 24.32 ? 65  PHE A N   1 
ATOM   307  C CA  . PHE A 1 65  ? 12.965 10.768  -46.938 1.00 26.49 ? 65  PHE A CA  1 
ATOM   308  C C   . PHE A 1 65  ? 11.770 10.577  -47.862 1.00 26.21 ? 65  PHE A C   1 
ATOM   309  O O   . PHE A 1 65  ? 11.766 11.092  -48.987 1.00 26.83 ? 65  PHE A O   1 
ATOM   310  C CB  . PHE A 1 65  ? 14.062 9.756   -47.262 1.00 23.07 ? 65  PHE A CB  1 
ATOM   311  C CG  . PHE A 1 65  ? 14.660 9.975   -48.600 1.00 24.13 ? 65  PHE A CG  1 
ATOM   312  C CD1 . PHE A 1 65  ? 15.637 10.952  -48.780 1.00 23.12 ? 65  PHE A CD1 1 
ATOM   313  C CD2 . PHE A 1 65  ? 14.211 9.255   -49.690 1.00 26.23 ? 65  PHE A CD2 1 
ATOM   314  C CE1 . PHE A 1 65  ? 16.170 11.188  -50.034 1.00 27.88 ? 65  PHE A CE1 1 
ATOM   315  C CE2 . PHE A 1 65  ? 14.740 9.481   -50.964 1.00 34.95 ? 65  PHE A CE2 1 
ATOM   316  C CZ  . PHE A 1 65  ? 15.719 10.452  -51.130 1.00 30.46 ? 65  PHE A CZ  1 
ATOM   317  N N   . LYS A 1 66  ? 10.753 9.839   -47.416 1.00 27.70 ? 66  LYS A N   1 
ATOM   318  C CA  . LYS A 1 66  ? 9.518  9.755   -48.185 1.00 26.69 ? 66  LYS A CA  1 
ATOM   319  C C   . LYS A 1 66  ? 8.944  11.146  -48.430 1.00 26.99 ? 66  LYS A C   1 
ATOM   320  O O   . LYS A 1 66  ? 8.452  11.443  -49.524 1.00 31.47 ? 66  LYS A O   1 
ATOM   321  C CB  . LYS A 1 66  ? 8.503  8.873   -47.441 1.00 31.91 ? 66  LYS A CB  1 
ATOM   322  C CG  . LYS A 1 66  ? 7.425  8.318   -48.351 1.00 48.83 ? 66  LYS A CG  1 
ATOM   323  C CD  . LYS A 1 66  ? 6.435  7.383   -47.636 1.00 44.45 ? 66  LYS A CD  1 
ATOM   324  C CE  . LYS A 1 66  ? 5.417  6.843   -48.658 1.00 50.28 ? 66  LYS A CE  1 
ATOM   325  N NZ  . LYS A 1 66  ? 4.997  7.896   -49.648 1.00 54.59 ? 66  LYS A NZ  1 
ATOM   326  N N   . ARG A 1 67  ? 9.036  12.024  -47.421 1.00 31.57 ? 67  ARG A N   1 
ATOM   327  C CA  . ARG A 1 67  ? 8.530  13.390  -47.556 1.00 29.33 ? 67  ARG A CA  1 
ATOM   328  C C   . ARG A 1 67  ? 9.382  14.207  -48.524 1.00 24.93 ? 67  ARG A C   1 
ATOM   329  O O   . ARG A 1 67  ? 8.846  14.901  -49.397 1.00 30.29 ? 67  ARG A O   1 
ATOM   330  C CB  . ARG A 1 67  ? 8.463  14.062  -46.180 1.00 33.25 ? 67  ARG A CB  1 
ATOM   331  C CG  . ARG A 1 67  ? 7.516  13.344  -45.226 1.00 35.82 ? 67  ARG A CG  1 
ATOM   332  C CD  . ARG A 1 67  ? 6.705  14.337  -44.417 1.00 49.34 ? 67  ARG A CD  1 
ATOM   333  N NE  . ARG A 1 67  ? 7.484  14.826  -43.288 1.00 65.23 ? 67  ARG A NE  1 
ATOM   334  C CZ  . ARG A 1 67  ? 7.182  15.899  -42.572 1.00 56.47 ? 67  ARG A CZ  1 
ATOM   335  N NH1 . ARG A 1 67  ? 6.133  16.656  -42.867 1.00 55.07 ? 67  ARG A NH1 1 
ATOM   336  N NH2 . ARG A 1 67  ? 7.955  16.222  -41.538 1.00 39.92 ? 67  ARG A NH2 1 
ATOM   337  N N   . TYR A 1 68  ? 10.712 14.134  -48.395 1.00 24.98 ? 68  TYR A N   1 
ATOM   338  C CA  . TYR A 1 68  ? 11.575 14.839  -49.344 1.00 26.11 ? 68  TYR A CA  1 
ATOM   339  C C   . TYR A 1 68  ? 11.312 14.379  -50.775 1.00 26.92 ? 68  TYR A C   1 
ATOM   340  O O   . TYR A 1 68  ? 11.197 15.196  -51.696 1.00 27.35 ? 68  TYR A O   1 
ATOM   341  C CB  . TYR A 1 68  ? 13.056 14.627  -49.001 1.00 23.70 ? 68  TYR A CB  1 
ATOM   342  C CG  . TYR A 1 68  ? 13.464 14.881  -47.568 1.00 24.58 ? 68  TYR A CG  1 
ATOM   343  C CD1 . TYR A 1 68  ? 12.730 15.719  -46.734 1.00 27.06 ? 68  TYR A CD1 1 
ATOM   344  C CD2 . TYR A 1 68  ? 14.607 14.280  -47.052 1.00 23.81 ? 68  TYR A CD2 1 
ATOM   345  C CE1 . TYR A 1 68  ? 13.127 15.946  -45.411 1.00 24.75 ? 68  TYR A CE1 1 
ATOM   346  C CE2 . TYR A 1 68  ? 15.010 14.495  -45.745 1.00 21.74 ? 68  TYR A CE2 1 
ATOM   347  C CZ  . TYR A 1 68  ? 14.262 15.312  -44.926 1.00 23.33 ? 68  TYR A CZ  1 
ATOM   348  O OH  . TYR A 1 68  ? 14.686 15.498  -43.636 1.00 25.32 ? 68  TYR A OH  1 
ATOM   349  N N   . ALA A 1 69  ? 11.242 13.062  -50.987 1.00 27.98 ? 69  ALA A N   1 
ATOM   350  C CA  . ALA A 1 69  ? 11.162 12.547  -52.351 1.00 24.62 ? 69  ALA A CA  1 
ATOM   351  C C   . ALA A 1 69  ? 9.873  12.966  -53.046 1.00 31.89 ? 69  ALA A C   1 
ATOM   352  O O   . ALA A 1 69  ? 9.849  13.090  -54.281 1.00 33.38 ? 69  ALA A O   1 
ATOM   353  C CB  . ALA A 1 69  ? 11.305 11.024  -52.345 1.00 27.09 ? 69  ALA A CB  1 
ATOM   354  N N   . SER A 1 70  ? 8.801  13.216  -52.279 1.00 33.35 ? 70  SER A N   1 
ATOM   355  C CA  . SER A 1 70  ? 7.543  13.637  -52.885 1.00 30.76 ? 70  SER A CA  1 
ATOM   356  C C   . SER A 1 70  ? 7.611  15.040  -53.485 1.00 36.31 ? 70  SER A C   1 
ATOM   357  O O   . SER A 1 70  ? 6.670  15.450  -54.177 1.00 35.26 ? 70  SER A O   1 
ATOM   358  C CB  . SER A 1 70  ? 6.407  13.553  -51.854 1.00 35.65 ? 70  SER A CB  1 
ATOM   359  O OG  . SER A 1 70  ? 6.587  14.484  -50.797 1.00 36.80 ? 70  SER A OG  1 
ATOM   360  N N   . TYR A 1 71  ? 8.693  15.784  -53.265 1.00 34.82 ? 71  TYR A N   1 
ATOM   361  C CA  . TYR A 1 71  ? 8.864  17.083  -53.908 1.00 32.00 ? 71  TYR A CA  1 
ATOM   362  C C   . TYR A 1 71  ? 9.830  17.037  -55.079 1.00 38.28 ? 71  TYR A C   1 
ATOM   363  O O   . TYR A 1 71  ? 10.102 18.077  -55.689 1.00 39.91 ? 71  TYR A O   1 
ATOM   364  C CB  . TYR A 1 71  ? 9.323  18.133  -52.878 1.00 31.21 ? 71  TYR A CB  1 
ATOM   365  C CG  . TYR A 1 71  ? 8.263  18.387  -51.838 1.00 31.46 ? 71  TYR A CG  1 
ATOM   366  C CD1 . TYR A 1 71  ? 7.249  19.312  -52.063 1.00 35.67 ? 71  TYR A CD1 1 
ATOM   367  C CD2 . TYR A 1 71  ? 8.244  17.668  -50.652 1.00 36.11 ? 71  TYR A CD2 1 
ATOM   368  C CE1 . TYR A 1 71  ? 6.253  19.529  -51.113 1.00 45.19 ? 71  TYR A CE1 1 
ATOM   369  C CE2 . TYR A 1 71  ? 7.257  17.873  -49.701 1.00 38.56 ? 71  TYR A CE2 1 
ATOM   370  C CZ  . TYR A 1 71  ? 6.263  18.804  -49.941 1.00 39.59 ? 71  TYR A CZ  1 
ATOM   371  O OH  . TYR A 1 71  ? 5.282  19.009  -48.999 1.00 53.05 ? 71  TYR A OH  1 
ATOM   372  N N   . HIS A 1 72  ? 10.330 15.857  -55.436 1.00 30.17 ? 72  HIS A N   1 
ATOM   373  C CA  . HIS A 1 72  ? 11.250 15.708  -56.563 1.00 30.54 ? 72  HIS A CA  1 
ATOM   374  C C   . HIS A 1 72  ? 10.684 14.642  -57.494 1.00 37.20 ? 72  HIS A C   1 
ATOM   375  O O   . HIS A 1 72  ? 10.678 13.457  -57.148 1.00 35.54 ? 72  HIS A O   1 
ATOM   376  C CB  . HIS A 1 72  ? 12.653 15.333  -56.082 1.00 28.62 ? 72  HIS A CB  1 
ATOM   377  C CG  . HIS A 1 72  ? 13.290 16.372  -55.207 1.00 34.82 ? 72  HIS A CG  1 
ATOM   378  N ND1 . HIS A 1 72  ? 13.805 17.553  -55.704 1.00 37.32 ? 72  HIS A ND1 1 
ATOM   379  C CD2 . HIS A 1 72  ? 13.497 16.406  -53.870 1.00 34.28 ? 72  HIS A CD2 1 
ATOM   380  C CE1 . HIS A 1 72  ? 14.296 18.269  -54.706 1.00 36.20 ? 72  HIS A CE1 1 
ATOM   381  N NE2 . HIS A 1 72  ? 14.122 17.596  -53.583 1.00 30.49 ? 72  HIS A NE2 1 
ATOM   382  N N   . THR A 1 73  ? 10.212 15.061  -58.677 1.00 35.34 ? 73  THR A N   1 
ATOM   383  C CA  . THR A 1 73  ? 9.574  14.127  -59.602 1.00 34.91 ? 73  THR A CA  1 
ATOM   384  C C   . THR A 1 73  ? 10.497 12.964  -59.960 1.00 44.87 ? 73  THR A C   1 
ATOM   385  O O   . THR A 1 73  ? 10.042 11.822  -60.107 1.00 44.01 ? 73  THR A O   1 
ATOM   386  C CB  . THR A 1 73  ? 9.142  14.868  -60.876 1.00 46.46 ? 73  THR A CB  1 
ATOM   387  O OG1 . THR A 1 73  ? 8.111  15.814  -60.563 1.00 51.45 ? 73  THR A OG1 1 
ATOM   388  C CG2 . THR A 1 73  ? 8.606  13.897  -61.899 1.00 48.62 ? 73  THR A CG2 1 
ATOM   389  N N   . GLU A 1 74  ? 11.800 13.233  -60.096 1.00 36.87 ? 74  GLU A N   1 
ATOM   390  C CA  . GLU A 1 74  ? 12.737 12.206  -60.546 1.00 33.33 ? 74  GLU A CA  1 
ATOM   391  C C   . GLU A 1 74  ? 12.830 11.027  -59.583 1.00 34.41 ? 74  GLU A C   1 
ATOM   392  O O   . GLU A 1 74  ? 13.208 9.929   -59.999 1.00 34.80 ? 74  GLU A O   1 
ATOM   393  C CB  . GLU A 1 74  ? 14.131 12.800  -60.725 1.00 40.40 ? 74  GLU A CB  1 
ATOM   394  C CG  . GLU A 1 74  ? 14.189 14.037  -61.596 1.00 34.15 ? 74  GLU A CG  1 
ATOM   395  C CD  . GLU A 1 74  ? 14.253 15.318  -60.777 1.00 43.09 ? 74  GLU A CD  1 
ATOM   396  O OE1 . GLU A 1 74  ? 13.425 15.494  -59.849 1.00 36.93 ? 74  GLU A OE1 1 
ATOM   397  O OE2 . GLU A 1 74  ? 15.130 16.165  -61.075 1.00 41.29 ? 74  GLU A OE2 1 
ATOM   398  N N   . ILE A 1 75  ? 12.559 11.236  -58.298 1.00 32.71 ? 75  ILE A N   1 
ATOM   399  C CA  . ILE A 1 75  ? 12.769 10.181  -57.310 1.00 38.76 ? 75  ILE A CA  1 
ATOM   400  C C   . ILE A 1 75  ? 11.468 9.783   -56.613 1.00 33.12 ? 75  ILE A C   1 
ATOM   401  O O   . ILE A 1 75  ? 11.500 9.157   -55.550 1.00 32.05 ? 75  ILE A O   1 
ATOM   402  C CB  . ILE A 1 75  ? 13.850 10.571  -56.278 1.00 32.00 ? 75  ILE A CB  1 
ATOM   403  C CG1 . ILE A 1 75  ? 13.476 11.848  -55.522 1.00 33.02 ? 75  ILE A CG1 1 
ATOM   404  C CG2 . ILE A 1 75  ? 15.226 10.730  -56.933 1.00 33.15 ? 75  ILE A CG2 1 
ATOM   405  C CD1 . ILE A 1 75  ? 14.404 12.119  -54.344 1.00 31.45 ? 75  ILE A CD1 1 
ATOM   406  N N   . LYS A 1 76  ? 10.316 10.095  -57.211 1.00 34.48 ? 76  LYS A N   1 
ATOM   407  C CA  . LYS A 1 76  ? 9.055  9.764   -56.558 1.00 42.72 ? 76  LYS A CA  1 
ATOM   408  C C   . LYS A 1 76  ? 8.882  8.262   -56.331 1.00 40.70 ? 76  LYS A C   1 
ATOM   409  O O   . LYS A 1 76  ? 8.163  7.873   -55.404 1.00 39.13 ? 76  LYS A O   1 
ATOM   410  C CB  . LYS A 1 76  ? 7.882  10.335  -57.354 1.00 46.57 ? 76  LYS A CB  1 
ATOM   411  C CG  . LYS A 1 76  ? 7.613  11.807  -57.018 1.00 51.43 ? 76  LYS A CG  1 
ATOM   412  C CD  . LYS A 1 76  ? 6.412  12.375  -57.777 1.00 63.17 ? 76  LYS A CD  1 
ATOM   413  C CE  . LYS A 1 76  ? 6.144  13.819  -57.349 1.00 70.29 ? 76  LYS A CE  1 
ATOM   414  N NZ  . LYS A 1 76  ? 5.092  14.513  -58.154 1.00 65.51 ? 76  LYS A NZ  1 
ATOM   415  N N   . ARG A 1 77  ? 9.568  7.422   -57.114 1.00 35.55 ? 77  ARG A N   1 
ATOM   416  C CA  . ARG A 1 77  ? 9.571  5.970   -56.947 1.00 38.43 ? 77  ARG A CA  1 
ATOM   417  C C   . ARG A 1 77  ? 10.165 5.512   -55.619 1.00 35.95 ? 77  ARG A C   1 
ATOM   418  O O   . ARG A 1 77  ? 10.092 4.317   -55.297 1.00 33.17 ? 77  ARG A O   1 
ATOM   419  C CB  . ARG A 1 77  ? 10.357 5.327   -58.096 1.00 35.77 ? 77  ARG A CB  1 
ATOM   420  C CG  . ARG A 1 77  ? 11.866 5.461   -57.929 1.00 43.91 ? 77  ARG A CG  1 
ATOM   421  C CD  . ARG A 1 77  ? 12.627 4.881   -59.115 1.00 52.30 ? 77  ARG A CD  1 
ATOM   422  N NE  . ARG A 1 77  ? 12.354 5.632   -60.333 1.00 55.32 ? 77  ARG A NE  1 
ATOM   423  C CZ  . ARG A 1 77  ? 12.680 5.231   -61.554 1.00 71.00 ? 77  ARG A CZ  1 
ATOM   424  N NH1 . ARG A 1 77  ? 13.309 4.085   -61.761 1.00 64.99 ? 77  ARG A NH1 1 
ATOM   425  N NH2 . ARG A 1 77  ? 12.360 5.996   -62.595 1.00 54.94 ? 77  ARG A NH2 1 
ATOM   426  N N   . TYR A 1 78  ? 10.757 6.413   -54.835 1.00 30.89 ? 78  TYR A N   1 
ATOM   427  C CA  . TYR A 1 78  ? 11.119 6.029   -53.478 1.00 27.88 ? 78  TYR A CA  1 
ATOM   428  C C   . TYR A 1 78  ? 9.913  5.493   -52.706 1.00 36.46 ? 78  TYR A C   1 
ATOM   429  O O   . TYR A 1 78  ? 10.066 4.642   -51.819 1.00 29.72 ? 78  TYR A O   1 
ATOM   430  C CB  . TYR A 1 78  ? 11.731 7.208   -52.721 1.00 30.53 ? 78  TYR A CB  1 
ATOM   431  C CG  . TYR A 1 78  ? 12.007 6.825   -51.301 1.00 27.17 ? 78  TYR A CG  1 
ATOM   432  C CD1 . TYR A 1 78  ? 13.108 6.043   -50.990 1.00 27.99 ? 78  TYR A CD1 1 
ATOM   433  C CD2 . TYR A 1 78  ? 11.143 7.201   -50.265 1.00 28.88 ? 78  TYR A CD2 1 
ATOM   434  C CE1 . TYR A 1 78  ? 13.366 5.651   -49.680 1.00 25.52 ? 78  TYR A CE1 1 
ATOM   435  C CE2 . TYR A 1 78  ? 11.393 6.816   -48.947 1.00 25.55 ? 78  TYR A CE2 1 
ATOM   436  C CZ  . TYR A 1 78  ? 12.505 6.050   -48.668 1.00 25.23 ? 78  TYR A CZ  1 
ATOM   437  O OH  . TYR A 1 78  ? 12.790 5.659   -47.389 1.00 26.10 ? 78  TYR A OH  1 
ATOM   438  N N   . GLU A 1 79  ? 8.703  5.954   -53.037 1.00 32.01 ? 79  GLU A N   1 
ATOM   439  C CA  . GLU A 1 79  ? 7.532  5.441   -52.332 1.00 34.27 ? 79  GLU A CA  1 
ATOM   440  C C   . GLU A 1 79  ? 7.432  3.925   -52.462 1.00 32.48 ? 79  GLU A C   1 
ATOM   441  O O   . GLU A 1 79  ? 6.936  3.257   -51.551 1.00 32.70 ? 79  GLU A O   1 
ATOM   442  C CB  . GLU A 1 79  ? 6.260  6.121   -52.856 1.00 36.71 ? 79  GLU A CB  1 
ATOM   443  C CG  . GLU A 1 79  ? 5.910  5.749   -54.275 1.00 34.36 ? 79  GLU A CG  1 
ATOM   444  C CD  . GLU A 1 79  ? 4.607  6.375   -54.747 1.00 41.04 ? 79  GLU A CD  1 
ATOM   445  O OE1 . GLU A 1 79  ? 3.762  6.748   -53.899 1.00 43.26 ? 79  GLU A OE1 1 
ATOM   446  O OE2 . GLU A 1 79  ? 4.433  6.485   -55.971 1.00 41.87 ? 79  GLU A OE2 1 
ATOM   447  N N   . ASP A 1 80  ? 7.907  3.360   -53.577 1.00 32.08 ? 80  ASP A N   1 
ATOM   448  C CA  . ASP A 1 80  ? 7.869  1.912   -53.736 1.00 32.99 ? 80  ASP A CA  1 
ATOM   449  C C   . ASP A 1 80  ? 9.001  1.218   -52.982 1.00 38.62 ? 80  ASP A C   1 
ATOM   450  O O   . ASP A 1 80  ? 8.831  0.079   -52.528 1.00 38.11 ? 80  ASP A O   1 
ATOM   451  C CB  . ASP A 1 80  ? 7.902  1.560   -55.214 1.00 31.96 ? 80  ASP A CB  1 
ATOM   452  C CG  . ASP A 1 80  ? 6.693  2.103   -55.957 1.00 45.47 ? 80  ASP A CG  1 
ATOM   453  O OD1 . ASP A 1 80  ? 5.617  2.218   -55.323 1.00 47.48 ? 80  ASP A OD1 1 
ATOM   454  O OD2 . ASP A 1 80  ? 6.821  2.431   -57.152 1.00 44.53 ? 80  ASP A OD2 1 
ATOM   455  N N   . ILE A 1 81  ? 10.152 1.874   -52.838 1.00 29.06 ? 81  ILE A N   1 
ATOM   456  C CA  . ILE A 1 81  ? 11.196 1.325   -51.983 1.00 29.25 ? 81  ILE A CA  1 
ATOM   457  C C   . ILE A 1 81  ? 10.712 1.290   -50.546 1.00 29.78 ? 81  ILE A C   1 
ATOM   458  O O   . ILE A 1 81  ? 10.891 0.295   -49.831 1.00 33.68 ? 81  ILE A O   1 
ATOM   459  C CB  . ILE A 1 81  ? 12.489 2.152   -52.111 1.00 32.80 ? 81  ILE A CB  1 
ATOM   460  C CG1 . ILE A 1 81  ? 13.046 2.081   -53.545 1.00 32.63 ? 81  ILE A CG1 1 
ATOM   461  C CG2 . ILE A 1 81  ? 13.506 1.714   -51.050 1.00 31.17 ? 81  ILE A CG2 1 
ATOM   462  C CD1 . ILE A 1 81  ? 14.145 3.109   -53.795 1.00 36.90 ? 81  ILE A CD1 1 
ATOM   463  N N   . HIS A 1 82  ? 10.080 2.380   -50.105 1.00 27.18 ? 82  HIS A N   1 
ATOM   464  C CA  . HIS A 1 82  ? 9.614  2.468   -48.729 1.00 25.07 ? 82  HIS A CA  1 
ATOM   465  C C   . HIS A 1 82  ? 8.585  1.380   -48.433 1.00 33.39 ? 82  HIS A C   1 
ATOM   466  O O   . HIS A 1 82  ? 8.655  0.697   -47.399 1.00 33.12 ? 82  HIS A O   1 
ATOM   467  C CB  . HIS A 1 82  ? 9.031  3.863   -48.473 1.00 24.60 ? 82  HIS A CB  1 
ATOM   468  C CG  . HIS A 1 82  ? 8.755  4.145   -47.030 1.00 28.94 ? 82  HIS A CG  1 
ATOM   469  N ND1 . HIS A 1 82  ? 7.585  3.761   -46.410 1.00 36.74 ? 82  HIS A ND1 1 
ATOM   470  C CD2 . HIS A 1 82  ? 9.502  4.765   -46.083 1.00 25.80 ? 82  HIS A CD2 1 
ATOM   471  C CE1 . HIS A 1 82  ? 7.623  4.127   -45.140 1.00 39.22 ? 82  HIS A CE1 1 
ATOM   472  N NE2 . HIS A 1 82  ? 8.777  4.731   -44.913 1.00 35.02 ? 82  HIS A NE2 1 
ATOM   473  N N   . LYS A 1 83  ? 7.628  1.187   -49.333 1.00 31.47 ? 83  LYS A N   1 
ATOM   474  C CA  . LYS A 1 83  ? 6.564  0.251   -48.993 1.00 35.12 ? 83  LYS A CA  1 
ATOM   475  C C   . LYS A 1 83  ? 7.021  -1.204  -49.086 1.00 38.23 ? 83  LYS A C   1 
ATOM   476  O O   . LYS A 1 83  ? 6.378  -2.078  -48.493 1.00 41.52 ? 83  LYS A O   1 
ATOM   477  C CB  . LYS A 1 83  ? 5.344  0.507   -49.875 1.00 40.55 ? 83  LYS A CB  1 
ATOM   478  C CG  . LYS A 1 83  ? 5.476  0.004   -51.277 1.00 36.68 ? 83  LYS A CG  1 
ATOM   479  C CD  . LYS A 1 83  ? 4.388  0.601   -52.146 1.00 44.33 ? 83  LYS A CD  1 
ATOM   480  C CE  . LYS A 1 83  ? 4.349  -0.053  -53.504 1.00 42.70 ? 83  LYS A CE  1 
ATOM   481  N NZ  . LYS A 1 83  ? 3.278  0.517   -54.384 1.00 41.58 ? 83  LYS A NZ  1 
ATOM   482  N N   . THR A 1 84  ? 8.113  -1.483  -49.807 1.00 32.01 ? 84  THR A N   1 
ATOM   483  C CA  . THR A 1 84  ? 8.649  -2.841  -49.869 1.00 35.97 ? 84  THR A CA  1 
ATOM   484  C C   . THR A 1 84  ? 9.770  -3.031  -48.845 1.00 39.72 ? 84  THR A C   1 
ATOM   485  O O   . THR A 1 84  ? 9.577  -3.698  -47.821 1.00 35.11 ? 84  THR A O   1 
ATOM   486  C CB  . THR A 1 84  ? 9.152  -3.168  -51.276 1.00 35.36 ? 84  THR A CB  1 
ATOM   487  O OG1 . THR A 1 84  ? 10.099 -2.177  -51.692 1.00 40.87 ? 84  THR A OG1 1 
ATOM   488  C CG2 . THR A 1 84  ? 7.995  -3.184  -52.258 1.00 41.50 ? 84  THR A CG2 1 
ATOM   489  N N   . LYS A 1 85  ? 10.936 -2.431  -49.102 1.00 30.40 ? 85  LYS A N   1 
ATOM   490  C CA  . LYS A 1 85  ? 12.121 -2.709  -48.285 1.00 37.88 ? 85  LYS A CA  1 
ATOM   491  C C   . LYS A 1 85  ? 12.020 -2.113  -46.880 1.00 34.24 ? 85  LYS A C   1 
ATOM   492  O O   . LYS A 1 85  ? 12.439 -2.749  -45.901 1.00 27.36 ? 85  LYS A O   1 
ATOM   493  C CB  . LYS A 1 85  ? 13.374 -2.191  -48.999 1.00 28.65 ? 85  LYS A CB  1 
ATOM   494  C CG  . LYS A 1 85  ? 13.579 -2.821  -50.386 1.00 34.59 ? 85  LYS A CG  1 
ATOM   495  C CD  . LYS A 1 85  ? 15.046 -2.937  -50.741 1.00 47.44 ? 85  LYS A CD  1 
ATOM   496  C CE  . LYS A 1 85  ? 15.235 -3.417  -52.183 1.00 56.28 ? 85  LYS A CE  1 
ATOM   497  N NZ  . LYS A 1 85  ? 16.658 -3.743  -52.462 1.00 69.39 ? 85  LYS A NZ  1 
ATOM   498  N N   . VAL A 1 86  ? 11.517 -0.883  -46.747 1.00 26.54 ? 86  VAL A N   1 
ATOM   499  C CA  . VAL A 1 86  ? 11.479 -0.266  -45.419 1.00 25.13 ? 86  VAL A CA  1 
ATOM   500  C C   . VAL A 1 86  ? 10.443 -0.954  -44.534 1.00 25.88 ? 86  VAL A C   1 
ATOM   501  O O   . VAL A 1 86  ? 10.700 -1.244  -43.357 1.00 28.11 ? 86  VAL A O   1 
ATOM   502  C CB  . VAL A 1 86  ? 11.209 1.246   -45.524 1.00 27.46 ? 86  VAL A CB  1 
ATOM   503  C CG1 . VAL A 1 86  ? 10.995 1.839   -44.127 1.00 27.07 ? 86  VAL A CG1 1 
ATOM   504  C CG2 . VAL A 1 86  ? 12.359 1.952   -46.277 1.00 29.51 ? 86  VAL A CG2 1 
ATOM   505  N N   . ASN A 1 87  ? 9.252  -1.212  -45.083 1.00 31.94 ? 87  ASN A N   1 
ATOM   506  C CA  . ASN A 1 87  ? 8.223  -1.946  -44.347 1.00 37.83 ? 87  ASN A CA  1 
ATOM   507  C C   . ASN A 1 87  ? 8.699  -3.339  -43.939 1.00 34.32 ? 87  ASN A C   1 
ATOM   508  O O   . ASN A 1 87  ? 8.438  -3.786  -42.818 1.00 30.46 ? 87  ASN A O   1 
ATOM   509  C CB  . ASN A 1 87  ? 6.954  -2.060  -45.192 1.00 40.09 ? 87  ASN A CB  1 
ATOM   510  C CG  . ASN A 1 87  ? 5.834  -2.789  -44.466 1.00 54.45 ? 87  ASN A CG  1 
ATOM   511  O OD1 . ASN A 1 87  ? 5.534  -3.950  -44.759 1.00 58.94 ? 87  ASN A OD1 1 
ATOM   512  N ND2 . ASN A 1 87  ? 5.216  -2.112  -43.510 1.00 52.23 ? 87  ASN A ND2 1 
ATOM   513  N N   . SER A 1 88  ? 9.366  -4.058  -44.853 1.00 29.97 ? 88  SER A N   1 
ATOM   514  C CA  . SER A 1 88  ? 9.885  -5.387  -44.509 1.00 36.89 ? 88  SER A CA  1 
ATOM   515  C C   . SER A 1 88  ? 10.926 -5.313  -43.391 1.00 30.12 ? 88  SER A C   1 
ATOM   516  O O   . SER A 1 88  ? 10.915 -6.132  -42.461 1.00 31.29 ? 88  SER A O   1 
ATOM   517  C CB  . SER A 1 88  ? 10.488 -6.057  -45.743 1.00 36.17 ? 88  SER A CB  1 
ATOM   518  O OG  . SER A 1 88  ? 9.496  -6.266  -46.731 1.00 47.06 ? 88  SER A OG  1 
ATOM   519  N N   . LEU A 1 89  ? 11.841 -4.342  -43.475 1.00 30.62 ? 89  LEU A N   1 
ATOM   520  C CA  . LEU A 1 89  ? 12.849 -4.170  -42.441 1.00 26.22 ? 89  LEU A CA  1 
ATOM   521  C C   . LEU A 1 89  ? 12.202 -3.891  -41.091 1.00 31.40 ? 89  LEU A C   1 
ATOM   522  O O   . LEU A 1 89  ? 12.595 -4.467  -40.062 1.00 24.60 ? 89  LEU A O   1 
ATOM   523  C CB  . LEU A 1 89  ? 13.797 -3.031  -42.825 1.00 23.41 ? 89  LEU A CB  1 
ATOM   524  C CG  . LEU A 1 89  ? 14.728 -2.572  -41.684 1.00 24.83 ? 89  LEU A CG  1 
ATOM   525  C CD1 . LEU A 1 89  ? 15.643 -3.704  -41.259 1.00 26.81 ? 89  LEU A CD1 1 
ATOM   526  C CD2 . LEU A 1 89  ? 15.551 -1.370  -42.184 1.00 28.00 ? 89  LEU A CD2 1 
ATOM   527  N N   . LEU A 1 90  ? 11.210 -3.001  -41.075 1.00 25.29 ? 90  LEU A N   1 
ATOM   528  C CA  . LEU A 1 90  ? 10.520 -2.693  -39.835 1.00 25.78 ? 90  LEU A CA  1 
ATOM   529  C C   . LEU A 1 90  ? 9.851  -3.935  -39.247 1.00 26.44 ? 90  LEU A C   1 
ATOM   530  O O   . LEU A 1 90  ? 9.916  -4.177  -38.034 1.00 31.61 ? 90  LEU A O   1 
ATOM   531  C CB  . LEU A 1 90  ? 9.506  -1.579  -40.093 1.00 30.33 ? 90  LEU A CB  1 
ATOM   532  C CG  . LEU A 1 90  ? 8.629  -1.158  -38.904 1.00 28.02 ? 90  LEU A CG  1 
ATOM   533  C CD1 . LEU A 1 90  ? 9.442  -0.828  -37.657 1.00 30.28 ? 90  LEU A CD1 1 
ATOM   534  C CD2 . LEU A 1 90  ? 7.777  0.046   -39.343 1.00 29.62 ? 90  LEU A CD2 1 
ATOM   535  N N   . ASN A 1 91  ? 9.204  -4.737  -40.079 1.00 31.18 ? 91  ASN A N   1 
ATOM   536  C CA  . ASN A 1 91  ? 8.558  -5.920  -39.526 1.00 32.07 ? 91  ASN A CA  1 
ATOM   537  C C   . ASN A 1 91  ? 9.579  -6.964  -39.091 1.00 35.00 ? 91  ASN A C   1 
ATOM   538  O O   . ASN A 1 91  ? 9.348  -7.681  -38.104 1.00 28.80 ? 91  ASN A O   1 
ATOM   539  C CB  . ASN A 1 91  ? 7.571  -6.491  -40.535 1.00 31.36 ? 91  ASN A CB  1 
ATOM   540  C CG  . ASN A 1 91  ? 6.338  -5.618  -40.689 1.00 37.39 ? 91  ASN A CG  1 
ATOM   541  O OD1 . ASN A 1 91  ? 5.944  -4.901  -39.759 1.00 43.45 ? 91  ASN A OD1 1 
ATOM   542  N ND2 . ASN A 1 91  ? 5.730  -5.664  -41.855 1.00 44.30 ? 91  ASN A ND2 1 
ATOM   543  N N   . GLU A 1 92  ? 10.711 -7.051  -39.800 1.00 26.85 ? 92  GLU A N   1 
ATOM   544  C CA  . GLU A 1 92  ? 11.813 -7.907  -39.362 1.00 31.90 ? 92  GLU A CA  1 
ATOM   545  C C   . GLU A 1 92  ? 12.393 -7.432  -38.032 1.00 30.39 ? 92  GLU A C   1 
ATOM   546  O O   . GLU A 1 92  ? 12.802 -8.250  -37.197 1.00 28.48 ? 92  GLU A O   1 
ATOM   547  C CB  . GLU A 1 92  ? 12.913 -7.945  -40.426 1.00 29.41 ? 92  GLU A CB  1 
ATOM   548  C CG  . GLU A 1 92  ? 12.624 -8.875  -41.575 1.00 34.24 ? 92  GLU A CG  1 
ATOM   549  C CD  . GLU A 1 92  ? 12.369 -10.294 -41.095 1.00 57.22 ? 92  GLU A CD  1 
ATOM   550  O OE1 . GLU A 1 92  ? 13.233 -10.862 -40.390 1.00 48.30 ? 92  GLU A OE1 1 
ATOM   551  O OE2 . GLU A 1 92  ? 11.285 -10.829 -41.403 1.00 61.67 ? 92  GLU A OE2 1 
ATOM   552  N N   . ALA A 1 93  ? 12.478 -6.117  -37.833 1.00 26.39 ? 93  ALA A N   1 
ATOM   553  C CA  . ALA A 1 93  ? 12.962 -5.599  -36.558 1.00 26.93 ? 93  ALA A CA  1 
ATOM   554  C C   . ALA A 1 93  ? 12.012 -5.977  -35.428 1.00 28.77 ? 93  ALA A C   1 
ATOM   555  O O   . ALA A 1 93  ? 12.445 -6.423  -34.359 1.00 26.08 ? 93  ALA A O   1 
ATOM   556  C CB  . ALA A 1 93  ? 13.131 -4.080  -36.632 1.00 23.45 ? 93  ALA A CB  1 
ATOM   557  N N   . SER A 1 94  ? 10.704 -5.804  -35.646 1.00 27.17 ? 94  SER A N   1 
ATOM   558  C CA  . SER A 1 94  ? 9.751  -6.179  -34.599 1.00 28.92 ? 94  SER A CA  1 
ATOM   559  C C   . SER A 1 94  ? 9.801  -7.676  -34.336 1.00 29.12 ? 94  SER A C   1 
ATOM   560  O O   . SER A 1 94  ? 9.711  -8.117  -33.182 1.00 28.91 ? 94  SER A O   1 
ATOM   561  C CB  . SER A 1 94  ? 8.331  -5.739  -34.982 1.00 37.21 ? 94  SER A CB  1 
ATOM   562  O OG  . SER A 1 94  ? 8.139  -4.361  -34.630 1.00 43.62 ? 94  SER A OG  1 
ATOM   563  N N   . ARG A 1 95  ? 9.961  -8.470  -35.390 1.00 29.59 ? 95  ARG A N   1 
ATOM   564  C CA  . ARG A 1 95  ? 10.066 -9.913  -35.198 1.00 30.41 ? 95  ARG A CA  1 
ATOM   565  C C   . ARG A 1 95  ? 11.294 -10.263 -34.365 1.00 33.80 ? 95  ARG A C   1 
ATOM   566  O O   . ARG A 1 95  ? 11.217 -11.103 -33.454 1.00 29.81 ? 95  ARG A O   1 
ATOM   567  C CB  . ARG A 1 95  ? 10.105 -10.624 -36.551 1.00 34.04 ? 95  ARG A CB  1 
ATOM   568  C CG  . ARG A 1 95  ? 10.039 -12.145 -36.422 1.00 36.81 ? 95  ARG A CG  1 
ATOM   569  C CD  . ARG A 1 95  ? 9.981  -12.846 -37.776 1.00 49.59 ? 95  ARG A CD  1 
ATOM   570  N NE  . ARG A 1 95  ? 11.232 -12.706 -38.511 1.00 57.05 ? 95  ARG A NE  1 
ATOM   571  C CZ  . ARG A 1 95  ? 12.311 -13.447 -38.297 1.00 60.63 ? 95  ARG A CZ  1 
ATOM   572  N NH1 . ARG A 1 95  ? 12.328 -14.393 -37.371 1.00 60.97 ? 95  ARG A NH1 1 
ATOM   573  N NH2 . ARG A 1 95  ? 13.400 -13.234 -39.032 1.00 64.33 ? 95  ARG A NH2 1 
ATOM   574  N N   . ALA A 1 96  ? 12.432 -9.615  -34.649 1.00 30.65 ? 96  ALA A N   1 
ATOM   575  C CA  . ALA A 1 96  ? 13.656 -9.870  -33.886 1.00 32.64 ? 96  ALA A CA  1 
ATOM   576  C C   . ALA A 1 96  ? 13.475 -9.524  -32.415 1.00 31.58 ? 96  ALA A C   1 
ATOM   577  O O   . ALA A 1 96  ? 13.909 -10.269 -31.523 1.00 28.62 ? 96  ALA A O   1 
ATOM   578  C CB  . ALA A 1 96  ? 14.817 -9.069  -34.469 1.00 28.55 ? 96  ALA A CB  1 
ATOM   579  N N   . ILE A 1 97  ? 12.889 -8.360  -32.145 1.00 27.07 ? 97  ILE A N   1 
ATOM   580  C CA  . ILE A 1 97  ? 12.620 -7.971  -30.771 1.00 28.61 ? 97  ILE A CA  1 
ATOM   581  C C   . ILE A 1 97  ? 11.777 -9.035  -30.092 1.00 26.82 ? 97  ILE A C   1 
ATOM   582  O O   . ILE A 1 97  ? 12.024 -9.399  -28.934 1.00 28.33 ? 97  ILE A O   1 
ATOM   583  C CB  . ILE A 1 97  ? 11.942 -6.587  -30.731 1.00 29.84 ? 97  ILE A CB  1 
ATOM   584  C CG1 . ILE A 1 97  ? 12.914 -5.497  -31.213 1.00 26.41 ? 97  ILE A CG1 1 
ATOM   585  C CG2 . ILE A 1 97  ? 11.415 -6.272  -29.339 1.00 27.06 ? 97  ILE A CG2 1 
ATOM   586  C CD1 . ILE A 1 97  ? 14.108 -5.263  -30.289 1.00 26.95 ? 97  ILE A CD1 1 
ATOM   587  N N   . GLY A 1 98  ? 10.777 -9.560  -30.802 1.00 28.87 ? 98  GLY A N   1 
ATOM   588  C CA  . GLY A 1 98  ? 9.879  -10.529 -30.194 1.00 27.22 ? 98  GLY A CA  1 
ATOM   589  C C   . GLY A 1 98  ? 10.526 -11.871 -29.921 1.00 30.24 ? 98  GLY A C   1 
ATOM   590  O O   . GLY A 1 98  ? 10.063 -12.612 -29.049 1.00 30.19 ? 98  GLY A O   1 
ATOM   591  N N   . ILE A 1 99  ? 11.574 -12.224 -30.680 1.00 29.17 ? 99  ILE A N   1 
ATOM   592  C CA  . ILE A 1 99  ? 12.325 -13.444 -30.367 1.00 29.46 ? 99  ILE A CA  1 
ATOM   593  C C   . ILE A 1 99  ? 12.877 -13.385 -28.942 1.00 29.58 ? 99  ILE A C   1 
ATOM   594  O O   . ILE A 1 99  ? 13.048 -14.422 -28.287 1.00 31.65 ? 99  ILE A O   1 
ATOM   595  C CB  . ILE A 1 99  ? 13.445 -13.652 -31.409 1.00 29.17 ? 99  ILE A CB  1 
ATOM   596  C CG1 . ILE A 1 99  ? 12.851 -13.995 -32.786 1.00 30.74 ? 99  ILE A CG1 1 
ATOM   597  C CG2 . ILE A 1 99  ? 14.429 -14.737 -30.971 1.00 32.40 ? 99  ILE A CG2 1 
ATOM   598  C CD1 . ILE A 1 99  ? 13.865 -13.920 -33.905 1.00 39.41 ? 99  ILE A CD1 1 
ATOM   599  N N   . CYS A 1 100 ? 13.135 -12.188 -28.425 1.00 26.97 ? 100 CYS A N   1 
ATOM   600  C CA  . CYS A 1 100 ? 13.723 -12.066 -27.094 1.00 30.42 ? 100 CYS A CA  1 
ATOM   601  C C   . CYS A 1 100 ? 12.682 -12.079 -25.970 1.00 33.44 ? 100 CYS A C   1 
ATOM   602  O O   . CYS A 1 100 ? 13.039 -11.869 -24.800 1.00 28.23 ? 100 CYS A O   1 
ATOM   603  C CB  . CYS A 1 100 ? 14.574 -10.789 -27.027 1.00 27.85 ? 100 CYS A CB  1 
ATOM   604  S SG  . CYS A 1 100 ? 15.808 -10.698 -28.377 1.00 33.01 ? 100 CYS A SG  1 
ATOM   605  N N   . ASN A 1 101 ? 11.410 -12.344 -26.287 1.00 29.48 ? 101 ASN A N   1 
ATOM   606  C CA  . ASN A 1 101 ? 10.369 -12.220 -25.267 1.00 29.29 ? 101 ASN A CA  1 
ATOM   607  C C   . ASN A 1 101 ? 10.494 -13.276 -24.172 1.00 33.19 ? 101 ASN A C   1 
ATOM   608  O O   . ASN A 1 101 ? 10.061 -13.034 -23.038 1.00 27.33 ? 101 ASN A O   1 
ATOM   609  C CB  . ASN A 1 101 ? 8.986  -12.295 -25.911 1.00 33.59 ? 101 ASN A CB  1 
ATOM   610  C CG  . ASN A 1 101 ? 8.561  -10.974 -26.529 1.00 36.45 ? 101 ASN A CG  1 
ATOM   611  O OD1 . ASN A 1 101 ? 9.091  -9.908  -26.187 1.00 37.30 ? 101 ASN A OD1 1 
ATOM   612  N ND2 . ASN A 1 101 ? 7.578  -11.031 -27.419 1.00 38.94 ? 101 ASN A ND2 1 
ATOM   613  N N   . ARG A 1 102 ? 11.059 -14.448 -24.486 1.00 32.03 ? 102 ARG A N   1 
ATOM   614  C CA  . ARG A 1 102 ? 11.194 -15.480 -23.468 1.00 32.93 ? 102 ARG A CA  1 
ATOM   615  C C   . ARG A 1 102 ? 12.188 -15.048 -22.396 1.00 30.86 ? 102 ARG A C   1 
ATOM   616  O O   . ARG A 1 102 ? 11.911 -15.175 -21.200 1.00 30.94 ? 102 ARG A O   1 
ATOM   617  C CB  . ARG A 1 102 ? 11.610 -16.811 -24.092 1.00 35.50 ? 102 ARG A CB  1 
ATOM   618  C CG  . ARG A 1 102 ? 11.859 -17.896 -23.066 1.00 45.91 ? 102 ARG A CG  1 
ATOM   619  N N   . LEU A 1 103 ? 13.347 -14.526 -22.811 1.00 30.75 ? 103 LEU A N   1 
ATOM   620  C CA  . LEU A 1 103 ? 14.297 -13.942 -21.863 1.00 34.36 ? 103 LEU A CA  1 
ATOM   621  C C   . LEU A 1 103 ? 13.684 -12.762 -21.120 1.00 33.82 ? 103 LEU A C   1 
ATOM   622  O O   . LEU A 1 103 ? 13.946 -12.562 -19.927 1.00 31.36 ? 103 LEU A O   1 
ATOM   623  C CB  . LEU A 1 103 ? 15.557 -13.480 -22.599 1.00 27.72 ? 103 LEU A CB  1 
ATOM   624  C CG  . LEU A 1 103 ? 16.425 -14.562 -23.235 1.00 36.17 ? 103 LEU A CG  1 
ATOM   625  C CD1 . LEU A 1 103 ? 17.481 -13.947 -24.126 1.00 38.68 ? 103 LEU A CD1 1 
ATOM   626  C CD2 . LEU A 1 103 ? 17.071 -15.421 -22.152 1.00 36.18 ? 103 LEU A CD2 1 
ATOM   627  N N   . LYS A 1 104 ? 12.895 -11.944 -21.819 1.00 25.52 ? 104 LYS A N   1 
ATOM   628  C CA  . LYS A 1 104 ? 12.233 -10.828 -21.144 1.00 24.54 ? 104 LYS A CA  1 
ATOM   629  C C   . LYS A 1 104 ? 11.320 -11.314 -20.027 1.00 30.20 ? 104 LYS A C   1 
ATOM   630  O O   . LYS A 1 104 ? 11.305 -10.743 -18.931 1.00 29.40 ? 104 LYS A O   1 
ATOM   631  C CB  . LYS A 1 104 ? 11.431 -10.004 -22.150 1.00 27.51 ? 104 LYS A CB  1 
ATOM   632  C CG  . LYS A 1 104 ? 10.699 -8.854  -21.506 1.00 28.68 ? 104 LYS A CG  1 
ATOM   633  C CD  . LYS A 1 104 ? 10.137 -7.895  -22.541 1.00 33.11 ? 104 LYS A CD  1 
ATOM   634  C CE  . LYS A 1 104 ? 8.742  -8.306  -22.943 1.00 38.53 ? 104 LYS A CE  1 
ATOM   635  N NZ  . LYS A 1 104 ? 8.172  -7.242  -23.833 1.00 51.10 ? 104 LYS A NZ  1 
ATOM   636  N N   . ASN A 1 105 ? 10.536 -12.355 -20.290 1.00 25.62 ? 105 ASN A N   1 
ATOM   637  C CA  . ASN A 1 105 ? 9.614  -12.844 -19.273 1.00 25.72 ? 105 ASN A CA  1 
ATOM   638  C C   . ASN A 1 105 ? 10.365 -13.452 -18.100 1.00 32.08 ? 105 ASN A C   1 
ATOM   639  O O   . ASN A 1 105 ? 9.951  -13.286 -16.949 1.00 31.76 ? 105 ASN A O   1 
ATOM   640  C CB  . ASN A 1 105 ? 8.647  -13.856 -19.877 1.00 35.78 ? 105 ASN A CB  1 
ATOM   641  C CG  . ASN A 1 105 ? 7.651  -13.204 -20.826 1.00 43.17 ? 105 ASN A CG  1 
ATOM   642  O OD1 . ASN A 1 105 ? 7.273  -12.052 -20.635 1.00 45.09 ? 105 ASN A OD1 1 
ATOM   643  N ND2 . ASN A 1 105 ? 7.224  -13.940 -21.852 1.00 50.18 ? 105 ASN A ND2 1 
ATOM   644  N N   . THR A 1 106 ? 11.473 -14.147 -18.367 1.00 29.81 ? 106 THR A N   1 
ATOM   645  C CA  . THR A 1 106 ? 12.288 -14.668 -17.270 1.00 30.01 ? 106 THR A CA  1 
ATOM   646  C C   . THR A 1 106 ? 12.855 -13.529 -16.431 1.00 30.87 ? 106 THR A C   1 
ATOM   647  O O   . THR A 1 106 ? 12.845 -13.578 -15.192 1.00 29.26 ? 106 THR A O   1 
ATOM   648  C CB  . THR A 1 106 ? 13.422 -15.535 -17.812 1.00 35.84 ? 106 THR A CB  1 
ATOM   649  O OG1 . THR A 1 106 ? 12.869 -16.659 -18.510 1.00 38.10 ? 106 THR A OG1 1 
ATOM   650  C CG2 . THR A 1 106 ? 14.307 -16.019 -16.672 1.00 39.00 ? 106 THR A CG2 1 
ATOM   651  N N   . LEU A 1 107 ? 13.376 -12.504 -17.101 1.00 28.91 ? 107 LEU A N   1 
ATOM   652  C CA  . LEU A 1 107 ? 13.932 -11.339 -16.420 1.00 27.13 ? 107 LEU A CA  1 
ATOM   653  C C   . LEU A 1 107 ? 12.867 -10.609 -15.601 1.00 32.08 ? 107 LEU A C   1 
ATOM   654  O O   . LEU A 1 107 ? 13.131 -10.181 -14.471 1.00 25.53 ? 107 LEU A O   1 
ATOM   655  C CB  . LEU A 1 107 ? 14.558 -10.410 -17.464 1.00 27.71 ? 107 LEU A CB  1 
ATOM   656  C CG  . LEU A 1 107 ? 15.276 -9.137  -17.027 1.00 32.75 ? 107 LEU A CG  1 
ATOM   657  C CD1 . LEU A 1 107 ? 16.245 -9.449  -15.890 1.00 32.29 ? 107 LEU A CD1 1 
ATOM   658  C CD2 . LEU A 1 107 ? 16.004 -8.525  -18.236 1.00 28.91 ? 107 LEU A CD2 1 
ATOM   659  N N   . LEU A 1 108 ? 11.662 -10.431 -16.167 1.00 27.00 ? 108 LEU A N   1 
ATOM   660  C CA  . LEU A 1 108 ? 10.566 -9.837  -15.401 1.00 29.15 ? 108 LEU A CA  1 
ATOM   661  C C   . LEU A 1 108 ? 10.264 -10.638 -14.138 1.00 31.69 ? 108 LEU A C   1 
ATOM   662  O O   . LEU A 1 108 ? 9.948  -10.064 -13.081 1.00 30.05 ? 108 LEU A O   1 
ATOM   663  C CB  . LEU A 1 108 ? 9.318  -9.750  -16.273 1.00 28.35 ? 108 LEU A CB  1 
ATOM   664  C CG  . LEU A 1 108 ? 9.194  -8.515  -17.132 1.00 33.67 ? 108 LEU A CG  1 
ATOM   665  C CD1 . LEU A 1 108 ? 8.109  -8.761  -18.170 1.00 46.48 ? 108 LEU A CD1 1 
ATOM   666  C CD2 . LEU A 1 108 ? 8.855  -7.325  -16.245 1.00 29.72 ? 108 LEU A CD2 1 
ATOM   667  N N   . GLY A 1 109 ? 10.320 -11.968 -14.235 1.00 28.39 ? 109 GLY A N   1 
ATOM   668  C CA  . GLY A 1 109 ? 10.085 -12.795 -13.057 1.00 25.18 ? 109 GLY A CA  1 
ATOM   669  C C   . GLY A 1 109 ? 11.061 -12.498 -11.935 1.00 30.57 ? 109 GLY A C   1 
ATOM   670  O O   . GLY A 1 109 ? 10.666 -12.369 -10.769 1.00 30.84 ? 109 GLY A O   1 
ATOM   671  N N   . LEU A 1 110 ? 12.353 -12.394 -12.273 1.00 25.35 ? 110 LEU A N   1 
ATOM   672  C CA  . LEU A 1 110 ? 13.376 -12.109 -11.273 1.00 26.77 ? 110 LEU A CA  1 
ATOM   673  C C   . LEU A 1 110 ? 13.162 -10.733 -10.676 1.00 27.72 ? 110 LEU A C   1 
ATOM   674  O O   . LEU A 1 110 ? 13.193 -10.556 -9.451  1.00 25.89 ? 110 LEU A O   1 
ATOM   675  C CB  . LEU A 1 110 ? 14.775 -12.197 -11.894 1.00 26.96 ? 110 LEU A CB  1 
ATOM   676  C CG  . LEU A 1 110 ? 15.405 -13.567 -12.144 1.00 44.64 ? 110 LEU A CG  1 
ATOM   677  C CD1 . LEU A 1 110 ? 16.609 -13.427 -13.064 1.00 32.76 ? 110 LEU A CD1 1 
ATOM   678  C CD2 . LEU A 1 110 ? 15.788 -14.252 -10.798 1.00 39.84 ? 110 LEU A CD2 1 
ATOM   679  N N   . ILE A 1 111 ? 12.926 -9.742  -11.540 1.00 25.35 ? 111 ILE A N   1 
ATOM   680  C CA  . ILE A 1 111 ? 12.693 -8.382  -11.075 1.00 26.35 ? 111 ILE A CA  1 
ATOM   681  C C   . ILE A 1 111 ? 11.587 -8.352  -10.032 1.00 26.34 ? 111 ILE A C   1 
ATOM   682  O O   . ILE A 1 111 ? 11.699 -7.685  -8.998  1.00 23.67 ? 111 ILE A O   1 
ATOM   683  C CB  . ILE A 1 111 ? 12.366 -7.471  -12.269 1.00 25.59 ? 111 ILE A CB  1 
ATOM   684  C CG1 . ILE A 1 111 ? 13.647 -7.169  -13.034 1.00 25.38 ? 111 ILE A CG1 1 
ATOM   685  C CG2 . ILE A 1 111 ? 11.675 -6.191  -11.811 1.00 25.50 ? 111 ILE A CG2 1 
ATOM   686  C CD1 . ILE A 1 111 ? 13.396 -6.601  -14.443 1.00 26.69 ? 111 ILE A CD1 1 
ATOM   687  N N   . ASN A 1 112 ? 10.492 -9.061  -10.297 1.00 24.17 ? 112 ASN A N   1 
ATOM   688  C CA  . ASN A 1 112 ? 9.357  -9.000  -9.384  1.00 27.09 ? 112 ASN A CA  1 
ATOM   689  C C   . ASN A 1 112 ? 9.645  -9.688  -8.046  1.00 26.44 ? 112 ASN A C   1 
ATOM   690  O O   . ASN A 1 112 ? 9.081  -9.294  -7.018  1.00 28.84 ? 112 ASN A O   1 
ATOM   691  C CB  . ASN A 1 112 ? 8.129  -9.577  -10.084 1.00 29.02 ? 112 ASN A CB  1 
ATOM   692  C CG  . ASN A 1 112 ? 7.486  -8.556  -11.024 1.00 36.05 ? 112 ASN A CG  1 
ATOM   693  O OD1 . ASN A 1 112 ? 7.158  -7.447  -10.604 1.00 38.20 ? 112 ASN A OD1 1 
ATOM   694  N ND2 . ASN A 1 112 ? 7.349  -8.905  -12.299 1.00 39.32 ? 112 ASN A ND2 1 
ATOM   695  N N   . ILE A 1 113 ? 10.519 -10.693 -8.017  1.00 25.67 ? 113 ILE A N   1 
ATOM   696  C CA  . ILE A 1 113 ? 10.928 -11.228 -6.716  1.00 23.90 ? 113 ILE A CA  1 
ATOM   697  C C   . ILE A 1 113 ? 11.824 -10.224 -6.006  1.00 24.60 ? 113 ILE A C   1 
ATOM   698  O O   . ILE A 1 113 ? 11.673 -9.969  -4.799  1.00 26.63 ? 113 ILE A O   1 
ATOM   699  C CB  . ILE A 1 113 ? 11.629 -12.588 -6.885  1.00 25.81 ? 113 ILE A CB  1 
ATOM   700  C CG1 . ILE A 1 113 ? 10.648 -13.620 -7.445  1.00 30.29 ? 113 ILE A CG1 1 
ATOM   701  C CG2 . ILE A 1 113 ? 12.217 -13.074 -5.548  1.00 31.36 ? 113 ILE A CG2 1 
ATOM   702  C CD1 . ILE A 1 113 ? 11.325 -14.891 -7.955  1.00 32.68 ? 113 ILE A CD1 1 
ATOM   703  N N   . LEU A 1 114 ? 12.761 -9.625  -6.749  1.00 23.77 ? 114 LEU A N   1 
ATOM   704  C CA  . LEU A 1 114 ? 13.773 -8.778  -6.117  1.00 24.69 ? 114 LEU A CA  1 
ATOM   705  C C   . LEU A 1 114 ? 13.163 -7.504  -5.550  1.00 24.43 ? 114 LEU A C   1 
ATOM   706  O O   . LEU A 1 114 ? 13.627 -6.999  -4.522  1.00 23.45 ? 114 LEU A O   1 
ATOM   707  C CB  . LEU A 1 114 ? 14.870 -8.438  -7.124  1.00 21.41 ? 114 LEU A CB  1 
ATOM   708  C CG  . LEU A 1 114 ? 15.855 -9.579  -7.403  1.00 24.13 ? 114 LEU A CG  1 
ATOM   709  C CD1 . LEU A 1 114 ? 16.556 -9.382  -8.755  1.00 27.66 ? 114 LEU A CD1 1 
ATOM   710  C CD2 . LEU A 1 114 ? 16.864 -9.707  -6.264  1.00 27.52 ? 114 LEU A CD2 1 
ATOM   711  N N   . GLU A 1 115 ? 12.159 -6.943  -6.234  1.00 23.92 ? 115 GLU A N   1 
ATOM   712  C CA  . GLU A 1 115 ? 11.485 -5.721  -5.794  1.00 26.39 ? 115 GLU A CA  1 
ATOM   713  C C   . GLU A 1 115 ? 10.472 -5.939  -4.674  1.00 26.96 ? 115 GLU A C   1 
ATOM   714  O O   . GLU A 1 115 ? 10.028 -4.958  -4.070  1.00 27.69 ? 115 GLU A O   1 
ATOM   715  C CB  . GLU A 1 115 ? 10.733 -5.055  -6.964  1.00 23.19 ? 115 GLU A CB  1 
ATOM   716  C CG  . GLU A 1 115 ? 11.611 -4.544  -8.077  1.00 29.23 ? 115 GLU A CG  1 
ATOM   717  C CD  . GLU A 1 115 ? 10.814 -3.870  -9.191  1.00 27.62 ? 115 GLU A CD  1 
ATOM   718  O OE1 . GLU A 1 115 ? 9.603  -4.141  -9.349  1.00 27.57 ? 115 GLU A OE1 1 
ATOM   719  O OE2 . GLU A 1 115 ? 11.411 -3.050  -9.912  1.00 28.87 ? 115 GLU A OE2 1 
ATOM   720  N N   . ASN A 1 116 ? 10.051 -7.174  -4.414  1.00 28.12 ? 116 ASN A N   1 
ATOM   721  C CA  . ASN A 1 116 ? 8.866  -7.436  -3.591  1.00 27.89 ? 116 ASN A CA  1 
ATOM   722  C C   . ASN A 1 116 ? 9.234  -8.350  -2.430  1.00 26.74 ? 116 ASN A C   1 
ATOM   723  O O   . ASN A 1 116 ? 9.396  -9.567  -2.629  1.00 27.12 ? 116 ASN A O   1 
ATOM   724  C CB  . ASN A 1 116 ? 7.766  -8.064  -4.451  1.00 27.89 ? 116 ASN A CB  1 
ATOM   725  C CG  . ASN A 1 116 ? 6.448  -8.232  -3.713  1.00 40.35 ? 116 ASN A CG  1 
ATOM   726  O OD1 . ASN A 1 116 ? 6.411  -8.425  -2.491  1.00 36.53 ? 116 ASN A OD1 1 
ATOM   727  N ND2 . ASN A 1 116 ? 5.350  -8.175  -4.460  1.00 40.22 ? 116 ASN A ND2 1 
ATOM   728  N N   . PRO A 1 117 ? 9.358  -7.819  -1.201  1.00 29.02 ? 117 PRO A N   1 
ATOM   729  C CA  . PRO A 1 117 ? 9.741  -8.683  -0.067  1.00 30.85 ? 117 PRO A CA  1 
ATOM   730  C C   . PRO A 1 117 ? 8.825  -9.881  0.134   1.00 31.64 ? 117 PRO A C   1 
ATOM   731  O O   . PRO A 1 117 ? 9.306  -10.970 0.480   1.00 32.07 ? 117 PRO A O   1 
ATOM   732  C CB  . PRO A 1 117 ? 9.697  -7.713  1.126   1.00 30.55 ? 117 PRO A CB  1 
ATOM   733  C CG  . PRO A 1 117 ? 10.069 -6.391  0.510   1.00 27.98 ? 117 PRO A CG  1 
ATOM   734  C CD  . PRO A 1 117 ? 9.343  -6.392  -0.818  1.00 28.12 ? 117 PRO A CD  1 
ATOM   735  N N   . GLN A 1 118 ? 7.520  -9.717  -0.088  1.00 29.48 ? 118 GLN A N   1 
ATOM   736  C CA  . GLN A 1 118 ? 6.591  -10.831 0.103   1.00 36.77 ? 118 GLN A CA  1 
ATOM   737  C C   . GLN A 1 118 ? 6.904  -11.976 -0.857  1.00 37.13 ? 118 GLN A C   1 
ATOM   738  O O   . GLN A 1 118 ? 6.875  -13.148 -0.465  1.00 37.38 ? 118 GLN A O   1 
ATOM   739  C CB  . GLN A 1 118 ? 5.146  -10.353 -0.078  1.00 31.17 ? 118 GLN A CB  1 
ATOM   740  N N   . LYS A 1 119 ? 7.237  -11.654 -2.114  1.00 32.78 ? 119 LYS A N   1 
ATOM   741  C CA  . LYS A 1 119 ? 7.616  -12.698 -3.059  1.00 29.09 ? 119 LYS A CA  1 
ATOM   742  C C   . LYS A 1 119 ? 8.978  -13.291 -2.716  1.00 34.90 ? 119 LYS A C   1 
ATOM   743  O O   . LYS A 1 119 ? 9.190  -14.499 -2.873  1.00 35.41 ? 119 LYS A O   1 
ATOM   744  C CB  . LYS A 1 119 ? 7.607  -12.155 -4.490  1.00 29.62 ? 119 LYS A CB  1 
ATOM   745  C CG  . LYS A 1 119 ? 6.210  -11.968 -5.052  1.00 37.35 ? 119 LYS A CG  1 
ATOM   746  C CD  . LYS A 1 119 ? 6.257  -11.575 -6.529  1.00 37.35 ? 119 LYS A CD  1 
ATOM   747  C CE  . LYS A 1 119 ? 4.865  -11.557 -7.151  1.00 60.90 ? 119 LYS A CE  1 
ATOM   748  N NZ  . LYS A 1 119 ? 4.071  -10.371 -6.724  1.00 69.05 ? 119 LYS A NZ  1 
ATOM   749  N N   . PHE A 1 120 ? 9.916  -12.465 -2.248  1.00 28.97 ? 120 PHE A N   1 
ATOM   750  C CA  . PHE A 1 120 ? 11.208 -13.011 -1.838  1.00 33.08 ? 120 PHE A CA  1 
ATOM   751  C C   . PHE A 1 120 ? 11.057 -13.976 -0.664  1.00 29.39 ? 120 PHE A C   1 
ATOM   752  O O   . PHE A 1 120 ? 11.733 -15.013 -0.610  1.00 30.00 ? 120 PHE A O   1 
ATOM   753  C CB  . PHE A 1 120 ? 12.192 -11.890 -1.480  1.00 27.65 ? 120 PHE A CB  1 
ATOM   754  C CG  . PHE A 1 120 ? 13.483 -12.405 -0.883  1.00 26.94 ? 120 PHE A CG  1 
ATOM   755  C CD1 . PHE A 1 120 ? 14.410 -13.055 -1.683  1.00 31.54 ? 120 PHE A CD1 1 
ATOM   756  C CD2 . PHE A 1 120 ? 13.745 -12.270 0.477   1.00 31.04 ? 120 PHE A CD2 1 
ATOM   757  C CE1 . PHE A 1 120 ? 15.592 -13.574 -1.131  1.00 28.83 ? 120 PHE A CE1 1 
ATOM   758  C CE2 . PHE A 1 120 ? 14.921 -12.772 1.030   1.00 37.43 ? 120 PHE A CE2 1 
ATOM   759  C CZ  . PHE A 1 120 ? 15.847 -13.421 0.219   1.00 31.04 ? 120 PHE A CZ  1 
ATOM   760  N N   . LYS A 1 121 ? 10.175 -13.657 0.285   1.00 30.62 ? 121 LYS A N   1 
ATOM   761  C CA  . LYS A 1 121 ? 10.063 -14.486 1.481   1.00 31.83 ? 121 LYS A CA  1 
ATOM   762  C C   . LYS A 1 121 ? 9.411  -15.836 1.202   1.00 32.73 ? 121 LYS A C   1 
ATOM   763  O O   . LYS A 1 121 ? 9.552  -16.764 2.014   1.00 37.23 ? 121 LYS A O   1 
ATOM   764  C CB  . LYS A 1 121 ? 9.288  -13.725 2.566   1.00 34.27 ? 121 LYS A CB  1 
ATOM   765  C CG  . LYS A 1 121 ? 10.097 -12.580 3.164   1.00 40.54 ? 121 LYS A CG  1 
ATOM   766  C CD  . LYS A 1 121 ? 9.387  -11.888 4.324   1.00 44.88 ? 121 LYS A CD  1 
ATOM   767  C CE  . LYS A 1 121 ? 8.263  -11.007 3.824   1.00 45.05 ? 121 LYS A CE  1 
ATOM   768  N NZ  . LYS A 1 121 ? 7.665  -10.205 4.924   1.00 49.78 ? 121 LYS A NZ  1 
ATOM   769  N N   . THR A 1 122 ? 8.709  -15.974 0.083   1.00 29.07 ? 122 THR A N   1 
ATOM   770  C CA  . THR A 1 122 ? 8.013  -17.210 -0.258  1.00 37.35 ? 122 THR A CA  1 
ATOM   771  C C   . THR A 1 122 ? 8.716  -17.982 -1.375  1.00 43.30 ? 122 THR A C   1 
ATOM   772  O O   . THR A 1 122 ? 8.076  -18.707 -2.145  1.00 48.41 ? 122 THR A O   1 
ATOM   773  C CB  . THR A 1 122 ? 6.562  -16.914 -0.635  1.00 39.73 ? 122 THR A CB  1 
ATOM   774  O OG1 . THR A 1 122 ? 6.523  -15.920 -1.667  1.00 40.05 ? 122 THR A OG1 1 
ATOM   775  C CG2 . THR A 1 122 ? 5.794  -16.416 0.575   1.00 45.32 ? 122 THR A CG2 1 
ATOM   776  N N   . GLN A 1 123 ? 10.033 -17.822 -1.481  1.00 35.02 ? 123 GLN A N   1 
ATOM   777  C CA  . GLN A 1 123 ? 10.882 -18.692 -2.292  1.00 40.98 ? 123 GLN A CA  1 
ATOM   778  C C   . GLN A 1 123 ? 12.173 -18.889 -1.507  1.00 37.17 ? 123 GLN A C   1 
ATOM   779  O O   . GLN A 1 123 ? 12.328 -18.346 -0.408  1.00 37.98 ? 123 GLN A O   1 
ATOM   780  C CB  . GLN A 1 123 ? 11.097 -18.115 -3.703  1.00 38.24 ? 123 GLN A CB  1 
ATOM   781  C CG  . GLN A 1 123 ? 11.708 -16.715 -3.748  1.00 29.59 ? 123 GLN A CG  1 
ATOM   782  C CD  . GLN A 1 123 ? 13.209 -16.755 -3.576  1.00 40.91 ? 123 GLN A CD  1 
ATOM   783  O OE1 . GLN A 1 123 ? 13.913 -17.341 -4.403  1.00 34.15 ? 123 GLN A OE1 1 
ATOM   784  N NE2 . GLN A 1 123 ? 13.711 -16.167 -2.478  1.00 31.47 ? 123 GLN A NE2 1 
ATOM   785  N N   . ARG A 1 124 ? 13.117 -19.664 -2.048  1.00 37.76 ? 124 ARG A N   1 
ATOM   786  C CA  . ARG A 1 124 ? 14.241 -20.099 -1.224  1.00 40.08 ? 124 ARG A CA  1 
ATOM   787  C C   . ARG A 1 124 ? 15.630 -19.704 -1.718  1.00 38.18 ? 124 ARG A C   1 
ATOM   788  O O   . ARG A 1 124 ? 16.604 -19.982 -1.012  1.00 41.52 ? 124 ARG A O   1 
ATOM   789  C CB  . ARG A 1 124 ? 14.197 -21.625 -1.028  1.00 51.61 ? 124 ARG A CB  1 
ATOM   790  C CG  . ARG A 1 124 ? 12.996 -22.093 -0.207  1.00 59.30 ? 124 ARG A CG  1 
ATOM   791  C CD  . ARG A 1 124 ? 13.228 -23.465 0.408   1.00 56.75 ? 124 ARG A CD  1 
ATOM   792  N NE  . ARG A 1 124 ? 14.049 -23.386 1.609   1.00 71.01 ? 124 ARG A NE  1 
ATOM   793  C CZ  . ARG A 1 124 ? 14.642 -24.427 2.179   1.00 73.56 ? 124 ARG A CZ  1 
ATOM   794  N NH1 . ARG A 1 124 ? 14.552 -25.641 1.660   1.00 80.71 ? 124 ARG A NH1 1 
ATOM   795  N NH2 . ARG A 1 124 ? 15.344 -24.247 3.295   1.00 65.94 ? 124 ARG A NH2 1 
ATOM   796  N N   . GLU A 1 125 ? 15.763 -19.072 -2.881  1.00 38.20 ? 125 GLU A N   1 
ATOM   797  C CA  . GLU A 1 125 ? 17.068 -18.570 -3.295  1.00 43.31 ? 125 GLU A CA  1 
ATOM   798  C C   . GLU A 1 125 ? 17.472 -17.370 -2.451  1.00 39.67 ? 125 GLU A C   1 
ATOM   799  O O   . GLU A 1 125 ? 16.632 -16.538 -2.093  1.00 39.18 ? 125 GLU A O   1 
ATOM   800  C CB  . GLU A 1 125 ? 17.051 -18.163 -4.763  1.00 36.44 ? 125 GLU A CB  1 
ATOM   801  C CG  . GLU A 1 125 ? 16.767 -19.293 -5.717  1.00 56.05 ? 125 GLU A CG  1 
ATOM   802  C CD  . GLU A 1 125 ? 17.946 -20.244 -5.877  1.00 70.60 ? 125 GLU A CD  1 
ATOM   803  O OE1 . GLU A 1 125 ? 19.049 -19.943 -5.363  1.00 65.44 ? 125 GLU A OE1 1 
ATOM   804  O OE2 . GLU A 1 125 ? 17.765 -21.299 -6.520  1.00 81.15 ? 125 GLU A OE2 1 
ATOM   805  N N   . SER A 1 126 ? 18.768 -17.272 -2.148  1.00 35.33 ? 126 SER A N   1 
ATOM   806  C CA  . SER A 1 126 ? 19.274 -16.136 -1.386  1.00 34.70 ? 126 SER A CA  1 
ATOM   807  C C   . SER A 1 126 ? 19.146 -14.871 -2.219  1.00 33.98 ? 126 SER A C   1 
ATOM   808  O O   . SER A 1 126 ? 19.065 -14.918 -3.445  1.00 36.06 ? 126 SER A O   1 
ATOM   809  C CB  . SER A 1 126 ? 20.737 -16.344 -0.986  1.00 40.75 ? 126 SER A CB  1 
ATOM   810  O OG  . SER A 1 126 ? 21.606 -16.179 -2.102  1.00 43.62 ? 126 SER A OG  1 
ATOM   811  N N   . TYR A 1 127 ? 19.120 -13.722 -1.544  1.00 29.13 ? 127 TYR A N   1 
ATOM   812  C CA  . TYR A 1 127 ? 18.982 -12.479 -2.298  1.00 30.34 ? 127 TYR A CA  1 
ATOM   813  C C   . TYR A 1 127 ? 20.203 -12.248 -3.189  1.00 33.30 ? 127 TYR A C   1 
ATOM   814  O O   . TYR A 1 127 ? 20.081 -11.728 -4.311  1.00 32.17 ? 127 TYR A O   1 
ATOM   815  C CB  . TYR A 1 127 ? 18.747 -11.307 -1.336  1.00 28.75 ? 127 TYR A CB  1 
ATOM   816  C CG  . TYR A 1 127 ? 18.104 -10.124 -2.020  1.00 25.85 ? 127 TYR A CG  1 
ATOM   817  C CD1 . TYR A 1 127 ? 16.738 -10.090 -2.220  1.00 22.62 ? 127 TYR A CD1 1 
ATOM   818  C CD2 . TYR A 1 127 ? 18.862 -9.064  -2.482  1.00 25.60 ? 127 TYR A CD2 1 
ATOM   819  C CE1 . TYR A 1 127 ? 16.128 -9.026  -2.849  1.00 26.41 ? 127 TYR A CE1 1 
ATOM   820  C CE2 . TYR A 1 127 ? 18.273 -7.991  -3.117  1.00 29.19 ? 127 TYR A CE2 1 
ATOM   821  C CZ  . TYR A 1 127 ? 16.904 -7.975  -3.299  1.00 29.48 ? 127 TYR A CZ  1 
ATOM   822  O OH  . TYR A 1 127 ? 16.296 -6.923  -3.942  1.00 26.13 ? 127 TYR A OH  1 
ATOM   823  N N   . ASP A 1 128 ? 21.384 -12.677 -2.729  1.00 33.86 ? 128 ASP A N   1 
ATOM   824  C CA  . ASP A 1 128 ? 22.599 -12.521 -3.529  1.00 38.14 ? 128 ASP A CA  1 
ATOM   825  C C   . ASP A 1 128 ? 22.566 -13.378 -4.792  1.00 36.30 ? 128 ASP A C   1 
ATOM   826  O O   . ASP A 1 128 ? 23.016 -12.943 -5.856  1.00 36.97 ? 128 ASP A O   1 
ATOM   827  C CB  . ASP A 1 128 ? 23.834 -12.856 -2.683  1.00 37.26 ? 128 ASP A CB  1 
ATOM   828  C CG  . ASP A 1 128 ? 24.273 -11.686 -1.817  1.00 60.56 ? 128 ASP A CG  1 
ATOM   829  O OD1 . ASP A 1 128 ? 24.018 -10.523 -2.209  1.00 65.79 ? 128 ASP A OD1 1 
ATOM   830  O OD2 . ASP A 1 128 ? 24.872 -11.924 -0.749  1.00 79.31 ? 128 ASP A OD2 1 
ATOM   831  N N   . VAL A 1 129 ? 22.061 -14.606 -4.694  1.00 36.06 ? 129 VAL A N   1 
ATOM   832  C CA  . VAL A 1 129 ? 21.962 -15.454 -5.879  1.00 35.08 ? 129 VAL A CA  1 
ATOM   833  C C   . VAL A 1 129 ? 20.983 -14.855 -6.888  1.00 38.41 ? 129 VAL A C   1 
ATOM   834  O O   . VAL A 1 129 ? 21.243 -14.834 -8.099  1.00 33.38 ? 129 VAL A O   1 
ATOM   835  C CB  . VAL A 1 129 ? 21.557 -16.879 -5.466  1.00 37.26 ? 129 VAL A CB  1 
ATOM   836  C CG1 . VAL A 1 129 ? 21.120 -17.676 -6.693  1.00 45.69 ? 129 VAL A CG1 1 
ATOM   837  C CG2 . VAL A 1 129 ? 22.719 -17.567 -4.760  1.00 42.61 ? 129 VAL A CG2 1 
ATOM   838  N N   . LEU A 1 130 ? 19.852 -14.341 -6.404  1.00 27.45 ? 130 LEU A N   1 
ATOM   839  C CA  . LEU A 1 130 ? 18.883 -13.714 -7.304  1.00 28.65 ? 130 LEU A CA  1 
ATOM   840  C C   . LEU A 1 130 ? 19.455 -12.466 -7.965  1.00 36.06 ? 130 LEU A C   1 
ATOM   841  O O   . LEU A 1 130 ? 19.166 -12.190 -9.140  1.00 31.76 ? 130 LEU A O   1 
ATOM   842  C CB  . LEU A 1 130 ? 17.605 -13.364 -6.540  1.00 30.33 ? 130 LEU A CB  1 
ATOM   843  C CG  . LEU A 1 130 ? 16.794 -14.539 -5.988  1.00 33.57 ? 130 LEU A CG  1 
ATOM   844  C CD1 . LEU A 1 130 ? 15.679 -14.060 -5.062  1.00 31.95 ? 130 LEU A CD1 1 
ATOM   845  C CD2 . LEU A 1 130 ? 16.225 -15.360 -7.125  1.00 34.63 ? 130 LEU A CD2 1 
ATOM   846  N N   . LEU A 1 131 ? 20.240 -11.679 -7.224  1.00 33.05 ? 131 LEU A N   1 
ATOM   847  C CA  . LEU A 1 131 ? 20.864 -10.497 -7.819  1.00 32.25 ? 131 LEU A CA  1 
ATOM   848  C C   . LEU A 1 131 ? 21.840 -10.889 -8.921  1.00 29.71 ? 131 LEU A C   1 
ATOM   849  O O   . LEU A 1 131 ? 21.892 -10.242 -9.974  1.00 33.56 ? 131 LEU A O   1 
ATOM   850  C CB  . LEU A 1 131 ? 21.580 -9.670  -6.745  1.00 31.70 ? 131 LEU A CB  1 
ATOM   851  C CG  . LEU A 1 131 ? 20.748 -8.756  -5.843  1.00 29.72 ? 131 LEU A CG  1 
ATOM   852  C CD1 . LEU A 1 131 ? 21.614 -8.141  -4.741  1.00 32.63 ? 131 LEU A CD1 1 
ATOM   853  C CD2 . LEU A 1 131 ? 20.064 -7.648  -6.653  1.00 26.54 ? 131 LEU A CD2 1 
ATOM   854  N N   . ARG A 1 132 ? 22.627 -11.941 -8.699  1.00 32.03 ? 132 ARG A N   1 
ATOM   855  C CA  A ARG A 1 132 ? 23.536 -12.384 -9.750  0.50 33.77 ? 132 ARG A CA  1 
ATOM   856  C CA  B ARG A 1 132 ? 23.536 -12.419 -9.739  0.50 33.78 ? 132 ARG A CA  1 
ATOM   857  C C   . ARG A 1 132 ? 22.768 -12.873 -10.971 1.00 35.62 ? 132 ARG A C   1 
ATOM   858  O O   . ARG A 1 132 ? 23.150 -12.564 -12.108 1.00 35.44 ? 132 ARG A O   1 
ATOM   859  C CB  A ARG A 1 132 ? 24.474 -13.469 -9.220  0.50 38.04 ? 132 ARG A CB  1 
ATOM   860  C CB  B ARG A 1 132 ? 24.394 -13.566 -9.200  0.50 38.02 ? 132 ARG A CB  1 
ATOM   861  C CG  A ARG A 1 132 ? 25.539 -12.924 -8.288  0.50 42.42 ? 132 ARG A CG  1 
ATOM   862  C CG  B ARG A 1 132 ? 25.315 -14.186 -10.243 0.50 42.79 ? 132 ARG A CG  1 
ATOM   863  C CD  A ARG A 1 132 ? 26.653 -13.917 -8.026  0.50 43.52 ? 132 ARG A CD  1 
ATOM   864  C CD  B ARG A 1 132 ? 25.017 -15.663 -10.503 0.50 40.83 ? 132 ARG A CD  1 
ATOM   865  N NE  A ARG A 1 132 ? 26.925 -14.023 -6.600  0.50 42.27 ? 132 ARG A NE  1 
ATOM   866  N NE  B ARG A 1 132 ? 25.368 -16.511 -9.373  0.50 51.17 ? 132 ARG A NE  1 
ATOM   867  C CZ  A ARG A 1 132 ? 26.571 -15.059 -5.854  0.50 45.15 ? 132 ARG A CZ  1 
ATOM   868  C CZ  B ARG A 1 132 ? 24.566 -17.421 -8.839  0.50 48.11 ? 132 ARG A CZ  1 
ATOM   869  N NH1 A ARG A 1 132 ? 25.964 -16.112 -6.377  0.50 47.69 ? 132 ARG A NH1 1 
ATOM   870  N NH1 B ARG A 1 132 ? 23.365 -17.665 -9.340  0.50 48.07 ? 132 ARG A NH1 1 
ATOM   871  N NH2 A ARG A 1 132 ? 26.839 -15.041 -4.552  0.50 50.83 ? 132 ARG A NH2 1 
ATOM   872  N NH2 B ARG A 1 132 ? 24.979 -18.104 -7.775  0.50 48.44 ? 132 ARG A NH2 1 
ATOM   873  N N   . GLN A 1 133 ? 21.679 -13.625 -10.761 1.00 38.88 ? 133 GLN A N   1 
ATOM   874  C CA  . GLN A 1 133 ? 20.879 -14.097 -11.888 1.00 37.90 ? 133 GLN A CA  1 
ATOM   875  C C   . GLN A 1 133 ? 20.252 -12.930 -12.634 1.00 35.84 ? 133 GLN A C   1 
ATOM   876  O O   . GLN A 1 133 ? 20.160 -12.962 -13.867 1.00 29.62 ? 133 GLN A O   1 
ATOM   877  C CB  . GLN A 1 133 ? 19.798 -15.068 -11.409 1.00 36.35 ? 133 GLN A CB  1 
ATOM   878  C CG  . GLN A 1 133 ? 20.330 -16.382 -10.881 1.00 42.80 ? 133 GLN A CG  1 
ATOM   879  C CD  . GLN A 1 133 ? 19.266 -17.212 -10.186 1.00 47.72 ? 133 GLN A CD  1 
ATOM   880  O OE1 . GLN A 1 133 ? 18.124 -16.778 -10.022 1.00 52.14 ? 133 GLN A OE1 1 
ATOM   881  N NE2 . GLN A 1 133 ? 19.637 -18.410 -9.765  1.00 50.25 ? 133 GLN A NE2 1 
ATOM   882  N N   . TYR A 1 134 ? 19.834 -11.884 -11.909 1.00 31.32 ? 134 TYR A N   1 
ATOM   883  C CA  . TYR A 1 134 ? 19.338 -10.676 -12.569 1.00 33.28 ? 134 TYR A CA  1 
ATOM   884  C C   . TYR A 1 134 ? 20.393 -10.083 -13.500 1.00 33.02 ? 134 TYR A C   1 
ATOM   885  O O   . TYR A 1 134 ? 20.099 -9.739  -14.651 1.00 29.26 ? 134 TYR A O   1 
ATOM   886  C CB  . TYR A 1 134 ? 18.900 -9.635  -11.531 1.00 26.45 ? 134 TYR A CB  1 
ATOM   887  C CG  . TYR A 1 134 ? 18.690 -8.254  -12.127 1.00 26.44 ? 134 TYR A CG  1 
ATOM   888  C CD1 . TYR A 1 134 ? 17.476 -7.912  -12.727 1.00 25.26 ? 134 TYR A CD1 1 
ATOM   889  C CD2 . TYR A 1 134 ? 19.700 -7.287  -12.095 1.00 26.93 ? 134 TYR A CD2 1 
ATOM   890  C CE1 . TYR A 1 134 ? 17.283 -6.656  -13.291 1.00 27.03 ? 134 TYR A CE1 1 
ATOM   891  C CE2 . TYR A 1 134 ? 19.509 -6.020  -12.655 1.00 30.59 ? 134 TYR A CE2 1 
ATOM   892  C CZ  . TYR A 1 134 ? 18.298 -5.715  -13.255 1.00 31.84 ? 134 TYR A CZ  1 
ATOM   893  O OH  . TYR A 1 134 ? 18.079 -4.463  -13.812 1.00 26.13 ? 134 TYR A OH  1 
ATOM   894  N N   . GLU A 1 135 ? 21.623 -9.924  -13.007 1.00 30.75 ? 135 GLU A N   1 
ATOM   895  C CA  . GLU A 1 135 ? 22.687 -9.386  -13.852 1.00 34.88 ? 135 GLU A CA  1 
ATOM   896  C C   . GLU A 1 135 ? 22.894 -10.243 -15.094 1.00 35.55 ? 135 GLU A C   1 
ATOM   897  O O   . GLU A 1 135 ? 23.042 -9.720  -16.203 1.00 30.41 ? 135 GLU A O   1 
ATOM   898  C CB  . GLU A 1 135 ? 23.996 -9.283  -13.066 1.00 40.14 ? 135 GLU A CB  1 
ATOM   899  C CG  . GLU A 1 135 ? 24.008 -8.183  -12.029 1.00 43.35 ? 135 GLU A CG  1 
ATOM   900  C CD  . GLU A 1 135 ? 23.716 -6.805  -12.612 1.00 48.89 ? 135 GLU A CD  1 
ATOM   901  O OE1 . GLU A 1 135 ? 23.980 -6.573  -13.814 1.00 45.52 ? 135 GLU A OE1 1 
ATOM   902  O OE2 . GLU A 1 135 ? 23.222 -5.945  -11.859 1.00 49.42 ? 135 GLU A OE2 1 
ATOM   903  N N   . GLU A 1 136 ? 22.932 -11.565 -14.920 1.00 35.92 ? 136 GLU A N   1 
ATOM   904  C CA  . GLU A 1 136 ? 23.136 -12.451 -16.062 1.00 38.93 ? 136 GLU A CA  1 
ATOM   905  C C   . GLU A 1 136 ? 21.986 -12.344 -17.059 1.00 35.13 ? 136 GLU A C   1 
ATOM   906  O O   . GLU A 1 136 ? 22.208 -12.272 -18.275 1.00 30.57 ? 136 GLU A O   1 
ATOM   907  C CB  . GLU A 1 136 ? 23.307 -13.888 -15.575 1.00 36.04 ? 136 GLU A CB  1 
ATOM   908  C CG  . GLU A 1 136 ? 24.494 -14.057 -14.644 1.00 40.20 ? 136 GLU A CG  1 
ATOM   909  C CD  . GLU A 1 136 ? 24.647 -15.478 -14.111 1.00 63.72 ? 136 GLU A CD  1 
ATOM   910  O OE1 . GLU A 1 136 ? 23.690 -16.276 -14.238 1.00 56.18 ? 136 GLU A OE1 1 
ATOM   911  O OE2 . GLU A 1 136 ? 25.729 -15.791 -13.562 1.00 60.57 ? 136 GLU A OE2 1 
ATOM   912  N N   . LYS A 1 137 ? 20.745 -12.344 -16.566 1.00 32.98 ? 137 LYS A N   1 
ATOM   913  C CA  . LYS A 1 137 ? 19.610 -12.321 -17.483 1.00 36.01 ? 137 LYS A CA  1 
ATOM   914  C C   . LYS A 1 137 ? 19.437 -10.960 -18.121 1.00 33.98 ? 137 LYS A C   1 
ATOM   915  O O   . LYS A 1 137 ? 18.944 -10.870 -19.255 1.00 30.89 ? 137 LYS A O   1 
ATOM   916  C CB  . LYS A 1 137 ? 18.317 -12.724 -16.777 1.00 28.74 ? 137 LYS A CB  1 
ATOM   917  C CG  . LYS A 1 137 ? 18.281 -14.178 -16.338 1.00 41.12 ? 137 LYS A CG  1 
ATOM   918  C CD  . LYS A 1 137 ? 18.685 -15.128 -17.467 1.00 59.83 ? 137 LYS A CD  1 
ATOM   919  C CE  . LYS A 1 137 ? 17.494 -15.541 -18.327 1.00 62.41 ? 137 LYS A CE  1 
ATOM   920  N NZ  . LYS A 1 137 ? 17.818 -16.729 -19.175 1.00 57.38 ? 137 LYS A NZ  1 
ATOM   921  N N   . LYS A 1 138 ? 19.813 -9.889  -17.417 1.00 29.72 ? 138 LYS A N   1 
ATOM   922  C CA  . LYS A 1 138 ? 19.755 -8.564  -18.030 1.00 29.18 ? 138 LYS A CA  1 
ATOM   923  C C   . LYS A 1 138 ? 20.704 -8.477  -19.216 1.00 31.16 ? 138 LYS A C   1 
ATOM   924  O O   . LYS A 1 138 ? 20.355 -7.944  -20.278 1.00 28.86 ? 138 LYS A O   1 
ATOM   925  C CB  . LYS A 1 138 ? 20.099 -7.492  -16.995 1.00 26.99 ? 138 LYS A CB  1 
ATOM   926  C CG  . LYS A 1 138 ? 20.391 -6.107  -17.563 1.00 26.94 ? 138 LYS A CG  1 
ATOM   927  C CD  . LYS A 1 138 ? 20.754 -5.140  -16.432 1.00 29.42 ? 138 LYS A CD  1 
ATOM   928  C CE  . LYS A 1 138 ? 21.354 -3.859  -16.977 1.00 44.28 ? 138 LYS A CE  1 
ATOM   929  N NZ  . LYS A 1 138 ? 21.841 -2.960  -15.895 1.00 50.55 ? 138 LYS A NZ  1 
ATOM   930  N N   . GLU A 1 139 ? 21.915 -8.984  -19.052 1.00 30.45 ? 139 GLU A N   1 
ATOM   931  C CA  . GLU A 1 139 ? 22.864 -8.919  -20.156 1.00 35.91 ? 139 GLU A CA  1 
ATOM   932  C C   . GLU A 1 139 ? 22.501 -9.898  -21.266 1.00 33.19 ? 139 GLU A C   1 
ATOM   933  O O   . GLU A 1 139 ? 22.714 -9.592  -22.441 1.00 33.90 ? 139 GLU A O   1 
ATOM   934  C CB  . GLU A 1 139 ? 24.280 -9.155  -19.632 1.00 35.58 ? 139 GLU A CB  1 
ATOM   935  C CG  . GLU A 1 139 ? 24.771 -7.954  -18.819 1.00 41.65 ? 139 GLU A CG  1 
ATOM   936  C CD  . GLU A 1 139 ? 24.589 -6.633  -19.570 1.00 50.71 ? 139 GLU A CD  1 
ATOM   937  O OE1 . GLU A 1 139 ? 25.079 -6.535  -20.714 1.00 63.70 ? 139 GLU A OE1 1 
ATOM   938  O OE2 . GLU A 1 139 ? 23.954 -5.698  -19.028 1.00 42.68 ? 139 GLU A OE2 1 
ATOM   939  N N   . ALA A 1 140 ? 21.932 -11.059 -20.923 1.00 29.79 ? 140 ALA A N   1 
ATOM   940  C CA  . ALA A 1 140 ? 21.470 -11.981 -21.959 1.00 35.80 ? 140 ALA A CA  1 
ATOM   941  C C   . ALA A 1 140 ? 20.312 -11.379 -22.755 1.00 34.63 ? 140 ALA A C   1 
ATOM   942  O O   . ALA A 1 140 ? 20.222 -11.563 -23.978 1.00 31.08 ? 140 ALA A O   1 
ATOM   943  C CB  . ALA A 1 140 ? 21.051 -13.307 -21.332 1.00 32.12 ? 140 ALA A CB  1 
ATOM   944  N N   . PHE A 1 141 ? 19.409 -10.664 -22.077 1.00 30.19 ? 141 PHE A N   1 
ATOM   945  C CA  . PHE A 1 141 ? 18.284 -10.042 -22.774 1.00 31.12 ? 141 PHE A CA  1 
ATOM   946  C C   . PHE A 1 141 ? 18.748 -8.894  -23.658 1.00 31.37 ? 141 PHE A C   1 
ATOM   947  O O   . PHE A 1 141 ? 18.366 -8.810  -24.836 1.00 26.73 ? 141 PHE A O   1 
ATOM   948  C CB  . PHE A 1 141 ? 17.241 -9.545  -21.773 1.00 26.36 ? 141 PHE A CB  1 
ATOM   949  C CG  . PHE A 1 141 ? 16.124 -8.752  -22.406 1.00 27.10 ? 141 PHE A CG  1 
ATOM   950  C CD1 . PHE A 1 141 ? 15.242 -9.350  -23.295 1.00 25.74 ? 141 PHE A CD1 1 
ATOM   951  C CD2 . PHE A 1 141 ? 15.927 -7.421  -22.071 1.00 28.44 ? 141 PHE A CD2 1 
ATOM   952  C CE1 . PHE A 1 141 ? 14.197 -8.614  -23.877 1.00 22.70 ? 141 PHE A CE1 1 
ATOM   953  C CE2 . PHE A 1 141 ? 14.886 -6.689  -22.640 1.00 25.08 ? 141 PHE A CE2 1 
ATOM   954  C CZ  . PHE A 1 141 ? 14.030 -7.287  -23.548 1.00 25.78 ? 141 PHE A CZ  1 
ATOM   955  N N   . ARG A 1 142 ? 19.558 -7.984  -23.108 1.00 26.61 ? 142 ARG A N   1 
ATOM   956  C CA  . ARG A 1 142 ? 20.085 -6.907  -23.940 1.00 25.53 ? 142 ARG A CA  1 
ATOM   957  C C   . ARG A 1 142 ? 20.911 -7.468  -25.093 1.00 28.27 ? 142 ARG A C   1 
ATOM   958  O O   . ARG A 1 142 ? 20.822 -6.978  -26.225 1.00 27.24 ? 142 ARG A O   1 
ATOM   959  C CB  . ARG A 1 142 ? 20.919 -5.934  -23.108 1.00 28.92 ? 142 ARG A CB  1 
ATOM   960  C CG  . ARG A 1 142 ? 20.116 -5.143  -22.049 1.00 25.21 ? 142 ARG A CG  1 
ATOM   961  C CD  . ARG A 1 142 ? 20.999 -4.204  -21.235 1.00 27.19 ? 142 ARG A CD  1 
ATOM   962  N NE  . ARG A 1 142 ? 21.549 -3.110  -22.023 1.00 28.50 ? 142 ARG A NE  1 
ATOM   963  C CZ  . ARG A 1 142 ? 22.832 -2.972  -22.325 1.00 36.35 ? 142 ARG A CZ  1 
ATOM   964  N NH1 . ARG A 1 142 ? 23.745 -3.794  -21.837 1.00 32.18 ? 142 ARG A NH1 1 
ATOM   965  N NH2 . ARG A 1 142 ? 23.204 -1.994  -23.149 1.00 29.04 ? 142 ARG A NH2 1 
ATOM   966  N N   . GLY A 1 143 ? 21.713 -8.500  -24.827 1.00 29.57 ? 143 GLY A N   1 
ATOM   967  C CA  . GLY A 1 143 ? 22.469 -9.131  -25.899 1.00 32.51 ? 143 GLY A CA  1 
ATOM   968  C C   . GLY A 1 143 ? 21.584 -9.725  -26.981 1.00 32.71 ? 143 GLY A C   1 
ATOM   969  O O   . GLY A 1 143 ? 21.924 -9.683  -28.165 1.00 31.68 ? 143 GLY A O   1 
ATOM   970  N N   . CYS A 1 144 ? 20.442 -10.297 -26.592 1.00 30.37 ? 144 CYS A N   1 
ATOM   971  C CA  . CYS A 1 144 ? 19.511 -10.825 -27.585 1.00 28.91 ? 144 CYS A CA  1 
ATOM   972  C C   . CYS A 1 144 ? 18.957 -9.695  -28.451 1.00 29.12 ? 144 CYS A C   1 
ATOM   973  O O   . CYS A 1 144 ? 18.860 -9.834  -29.678 1.00 26.25 ? 144 CYS A O   1 
ATOM   974  C CB  . CYS A 1 144 ? 18.377 -11.589 -26.892 1.00 35.73 ? 144 CYS A CB  1 
ATOM   975  S SG  . CYS A 1 144 ? 17.057 -12.296 -27.986 1.00 37.42 ? 144 CYS A SG  1 
ATOM   976  N N   . LEU A 1 145 ? 18.600 -8.570  -27.838 1.00 26.62 ? 145 LEU A N   1 
ATOM   977  C CA  . LEU A 1 145 ? 18.077 -7.447  -28.622 1.00 24.52 ? 145 LEU A CA  1 
ATOM   978  C C   . LEU A 1 145 ? 19.060 -7.019  -29.707 1.00 31.13 ? 145 LEU A C   1 
ATOM   979  O O   . LEU A 1 145 ? 18.660 -6.667  -30.825 1.00 26.60 ? 145 LEU A O   1 
ATOM   980  C CB  . LEU A 1 145 ? 17.775 -6.256  -27.717 1.00 25.39 ? 145 LEU A CB  1 
ATOM   981  C CG  . LEU A 1 145 ? 16.729 -6.443  -26.634 1.00 26.14 ? 145 LEU A CG  1 
ATOM   982  C CD1 . LEU A 1 145 ? 16.606 -5.155  -25.868 1.00 23.86 ? 145 LEU A CD1 1 
ATOM   983  C CD2 . LEU A 1 145 ? 15.392 -6.863  -27.262 1.00 26.76 ? 145 LEU A CD2 1 
ATOM   984  N N   . LEU A 1 146 ? 20.351 -7.011  -29.386 1.00 27.25 ? 146 LEU A N   1 
ATOM   985  C CA  . LEU A 1 146 ? 21.348 -6.664  -30.391 1.00 25.40 ? 146 LEU A CA  1 
ATOM   986  C C   . LEU A 1 146 ? 21.583 -7.819  -31.363 1.00 30.21 ? 146 LEU A C   1 
ATOM   987  O O   . LEU A 1 146 ? 21.552 -7.632  -32.585 1.00 27.11 ? 146 LEU A O   1 
ATOM   988  C CB  . LEU A 1 146 ? 22.656 -6.270  -29.700 1.00 27.96 ? 146 LEU A CB  1 
ATOM   989  C CG  . LEU A 1 146 ? 23.857 -6.052  -30.625 1.00 32.69 ? 146 LEU A CG  1 
ATOM   990  C CD1 . LEU A 1 146 ? 23.557 -4.932  -31.606 1.00 28.45 ? 146 LEU A CD1 1 
ATOM   991  C CD2 . LEU A 1 146 ? 25.106 -5.736  -29.816 1.00 35.72 ? 146 LEU A CD2 1 
ATOM   992  N N   . ASN A 1 147 ? 21.820 -9.027  -30.836 1.00 25.42 ? 147 ASN A N   1 
ATOM   993  C CA  . ASN A 1 147 ? 22.229 -10.140 -31.693 1.00 26.34 ? 147 ASN A CA  1 
ATOM   994  C C   . ASN A 1 147 ? 21.186 -10.450 -32.763 1.00 32.82 ? 147 ASN A C   1 
ATOM   995  O O   . ASN A 1 147 ? 21.534 -10.689 -33.921 1.00 30.20 ? 147 ASN A O   1 
ATOM   996  C CB  . ASN A 1 147 ? 22.499 -11.385 -30.851 1.00 37.47 ? 147 ASN A CB  1 
ATOM   997  C CG  . ASN A 1 147 ? 23.819 -11.313 -30.113 1.00 41.84 ? 147 ASN A CG  1 
ATOM   998  O OD1 . ASN A 1 147 ? 24.683 -10.498 -30.442 1.00 46.54 ? 147 ASN A OD1 1 
ATOM   999  N ND2 . ASN A 1 147 ? 23.984 -12.169 -29.116 1.00 51.00 ? 147 ASN A ND2 1 
ATOM   1000 N N   . LYS A 1 148 ? 19.905 -10.472 -32.390 1.00 27.45 ? 148 LYS A N   1 
ATOM   1001 C CA  . LYS A 1 148 ? 18.862 -10.856 -33.335 1.00 27.46 ? 148 LYS A CA  1 
ATOM   1002 C C   . LYS A 1 148 ? 18.599 -9.769  -34.370 1.00 30.17 ? 148 LYS A C   1 
ATOM   1003 O O   . LYS A 1 148 ? 17.933 -10.039 -35.379 1.00 29.17 ? 148 LYS A O   1 
ATOM   1004 C CB  . LYS A 1 148 ? 17.568 -11.190 -32.575 1.00 28.09 ? 148 LYS A CB  1 
ATOM   1005 C CG  . LYS A 1 148 ? 17.658 -12.413 -31.655 1.00 27.10 ? 148 LYS A CG  1 
ATOM   1006 C CD  . LYS A 1 148 ? 17.943 -13.705 -32.454 1.00 33.66 ? 148 LYS A CD  1 
ATOM   1007 C CE  . LYS A 1 148 ? 18.301 -14.867 -31.517 1.00 33.29 ? 148 LYS A CE  1 
ATOM   1008 N NZ  . LYS A 1 148 ? 18.319 -16.159 -32.279 1.00 38.84 ? 148 LYS A NZ  1 
ATOM   1009 N N   . ASN A 1 149 ? 19.124 -8.566  -34.152 1.00 26.02 ? 149 ASN A N   1 
ATOM   1010 C CA  . ASN A 1 149 ? 18.958 -7.435  -35.056 1.00 22.72 ? 149 ASN A CA  1 
ATOM   1011 C C   . ASN A 1 149 ? 20.191 -7.138  -35.901 1.00 25.97 ? 149 ASN A C   1 
ATOM   1012 O O   . ASN A 1 149 ? 20.182 -6.162  -36.655 1.00 27.37 ? 149 ASN A O   1 
ATOM   1013 C CB  . ASN A 1 149 ? 18.577 -6.191  -34.260 1.00 24.68 ? 149 ASN A CB  1 
ATOM   1014 C CG  . ASN A 1 149 ? 17.095 -6.085  -34.069 1.00 29.24 ? 149 ASN A CG  1 
ATOM   1015 O OD1 . ASN A 1 149 ? 16.353 -5.947  -35.046 1.00 26.80 ? 149 ASN A OD1 1 
ATOM   1016 N ND2 . ASN A 1 149 ? 16.642 -6.178  -32.821 1.00 25.35 ? 149 ASN A ND2 1 
ATOM   1017 N N   . ARG A 1 150 ? 21.236 -7.963  -35.823 1.00 25.42 ? 150 ARG A N   1 
ATOM   1018 C CA  . ARG A 1 150 ? 22.455 -7.647  -36.553 1.00 25.95 ? 150 ARG A CA  1 
ATOM   1019 C C   . ARG A 1 150 ? 22.215 -7.606  -38.058 1.00 28.68 ? 150 ARG A C   1 
ATOM   1020 O O   . ARG A 1 150 ? 22.701 -6.696  -38.741 1.00 30.42 ? 150 ARG A O   1 
ATOM   1021 C CB  . ARG A 1 150 ? 23.551 -8.656  -36.212 1.00 30.79 ? 150 ARG A CB  1 
ATOM   1022 C CG  . ARG A 1 150 ? 23.994 -8.548  -34.768 1.00 33.60 ? 150 ARG A CG  1 
ATOM   1023 C CD  . ARG A 1 150 ? 25.241 -9.385  -34.520 1.00 41.14 ? 150 ARG A CD  1 
ATOM   1024 N NE  . ARG A 1 150 ? 25.594 -9.382  -33.102 1.00 42.98 ? 150 ARG A NE  1 
ATOM   1025 C CZ  . ARG A 1 150 ? 26.328 -8.448  -32.515 1.00 35.19 ? 150 ARG A CZ  1 
ATOM   1026 N NH1 . ARG A 1 150 ? 26.785 -7.402  -33.189 1.00 34.47 ? 150 ARG A NH1 1 
ATOM   1027 N NH2 . ARG A 1 150 ? 26.624 -8.578  -31.222 1.00 38.60 ? 150 ARG A NH2 1 
ATOM   1028 N N   . LYS A 1 151 ? 21.465 -8.574  -38.602 1.00 28.36 ? 151 LYS A N   1 
ATOM   1029 C CA  . LYS A 1 151 ? 21.200 -8.534  -40.040 1.00 26.45 ? 151 LYS A CA  1 
ATOM   1030 C C   . LYS A 1 151 ? 20.308 -7.353  -40.402 1.00 24.82 ? 151 LYS A C   1 
ATOM   1031 O O   . LYS A 1 151 ? 20.466 -6.777  -41.483 1.00 28.53 ? 151 LYS A O   1 
ATOM   1032 C CB  . LYS A 1 151 ? 20.586 -9.856  -40.524 1.00 28.36 ? 151 LYS A CB  1 
ATOM   1033 C CG  . LYS A 1 151 ? 21.549 -11.041 -40.404 1.00 32.63 ? 151 LYS A CG  1 
ATOM   1034 C CD  . LYS A 1 151 ? 21.124 -12.231 -41.237 1.00 41.59 ? 151 LYS A CD  1 
ATOM   1035 C CE  . LYS A 1 151 ? 20.037 -13.053 -40.569 1.00 43.14 ? 151 LYS A CE  1 
ATOM   1036 N NZ  . LYS A 1 151 ? 19.773 -14.284 -41.402 1.00 43.36 ? 151 LYS A NZ  1 
ATOM   1037 N N   . ASN A 1 152 ? 19.407 -6.945  -39.493 1.00 25.41 ? 152 ASN A N   1 
ATOM   1038 C CA  . ASN A 1 152 ? 18.606 -5.741  -39.721 1.00 24.81 ? 152 ASN A CA  1 
ATOM   1039 C C   . ASN A 1 152 ? 19.481 -4.496  -39.787 1.00 28.47 ? 152 ASN A C   1 
ATOM   1040 O O   . ASN A 1 152 ? 19.218 -3.591  -40.586 1.00 25.29 ? 152 ASN A O   1 
ATOM   1041 C CB  . ASN A 1 152 ? 17.544 -5.574  -38.623 1.00 22.97 ? 152 ASN A CB  1 
ATOM   1042 C CG  . ASN A 1 152 ? 16.462 -6.635  -38.719 1.00 27.04 ? 152 ASN A CG  1 
ATOM   1043 O OD1 . ASN A 1 152 ? 16.190 -7.132  -39.803 1.00 26.99 ? 152 ASN A OD1 1 
ATOM   1044 N ND2 . ASN A 1 152 ? 15.869 -7.005  -37.593 1.00 26.65 ? 152 ASN A ND2 1 
ATOM   1045 N N   . LEU A 1 153 ? 20.523 -4.425  -38.952 1.00 28.10 ? 153 LEU A N   1 
ATOM   1046 C CA  . LEU A 1 153 ? 21.434 -3.284  -39.033 1.00 25.33 ? 153 LEU A CA  1 
ATOM   1047 C C   . LEU A 1 153 ? 22.127 -3.230  -40.388 1.00 30.55 ? 153 LEU A C   1 
ATOM   1048 O O   . LEU A 1 153 ? 22.331 -2.148  -40.945 1.00 28.62 ? 153 LEU A O   1 
ATOM   1049 C CB  . LEU A 1 153 ? 22.466 -3.339  -37.899 1.00 30.03 ? 153 LEU A CB  1 
ATOM   1050 C CG  . LEU A 1 153 ? 21.902 -3.374  -36.475 1.00 27.21 ? 153 LEU A CG  1 
ATOM   1051 C CD1 . LEU A 1 153 ? 23.025 -3.505  -35.416 1.00 36.09 ? 153 LEU A CD1 1 
ATOM   1052 C CD2 . LEU A 1 153 ? 21.042 -2.151  -36.189 1.00 26.92 ? 153 LEU A CD2 1 
ATOM   1053 N N   . ASP A 1 154 ? 22.501 -4.391  -40.936 1.00 28.63 ? 154 ASP A N   1 
ATOM   1054 C CA  . ASP A 1 154 ? 23.095 -4.422  -42.266 1.00 34.43 ? 154 ASP A CA  1 
ATOM   1055 C C   . ASP A 1 154 ? 22.114 -3.909  -43.310 1.00 33.74 ? 154 ASP A C   1 
ATOM   1056 O O   . ASP A 1 154 ? 22.511 -3.241  -44.268 1.00 29.08 ? 154 ASP A O   1 
ATOM   1057 C CB  . ASP A 1 154 ? 23.534 -5.847  -42.616 1.00 31.21 ? 154 ASP A CB  1 
ATOM   1058 C CG  . ASP A 1 154 ? 24.763 -6.289  -41.838 1.00 48.30 ? 154 ASP A CG  1 
ATOM   1059 O OD1 . ASP A 1 154 ? 25.652 -5.442  -41.584 1.00 57.89 ? 154 ASP A OD1 1 
ATOM   1060 O OD2 . ASP A 1 154 ? 24.832 -7.485  -41.487 1.00 59.71 ? 154 ASP A OD2 1 
ATOM   1061 N N   . GLN A 1 155 ? 20.825 -4.205  -43.130 1.00 25.36 ? 155 GLN A N   1 
ATOM   1062 C CA  . GLN A 1 155 ? 19.824 -3.787  -44.105 1.00 25.32 ? 155 GLN A CA  1 
ATOM   1063 C C   . GLN A 1 155 ? 19.557 -2.283  -44.033 1.00 26.59 ? 155 GLN A C   1 
ATOM   1064 O O   . GLN A 1 155 ? 19.232 -1.665  -45.059 1.00 28.93 ? 155 GLN A O   1 
ATOM   1065 C CB  . GLN A 1 155 ? 18.547 -4.611  -43.903 1.00 26.98 ? 155 GLN A CB  1 
ATOM   1066 C CG  . GLN A 1 155 ? 17.435 -4.356  -44.916 1.00 30.57 ? 155 GLN A CG  1 
ATOM   1067 C CD  . GLN A 1 155 ? 17.770 -4.832  -46.340 1.00 40.75 ? 155 GLN A CD  1 
ATOM   1068 O OE1 . GLN A 1 155 ? 18.828 -5.420  -46.599 1.00 37.73 ? 155 GLN A OE1 1 
ATOM   1069 N NE2 . GLN A 1 155 ? 16.850 -4.582  -47.266 1.00 42.17 ? 155 GLN A NE2 1 
ATOM   1070 N N   . ILE A 1 156 ? 19.708 -1.668  -42.858 1.00 27.60 ? 156 ILE A N   1 
ATOM   1071 C CA  . ILE A 1 156 ? 19.682 -0.203  -42.782 1.00 23.95 ? 156 ILE A CA  1 
ATOM   1072 C C   . ILE A 1 156 ? 20.737 0.384   -43.709 1.00 23.65 ? 156 ILE A C   1 
ATOM   1073 O O   . ILE A 1 156 ? 20.467 1.292   -44.506 1.00 23.87 ? 156 ILE A O   1 
ATOM   1074 C CB  . ILE A 1 156 ? 19.901 0.265   -41.331 1.00 24.48 ? 156 ILE A CB  1 
ATOM   1075 C CG1 . ILE A 1 156 ? 18.759 -0.198  -40.427 1.00 21.62 ? 156 ILE A CG1 1 
ATOM   1076 C CG2 . ILE A 1 156 ? 20.035 1.792   -41.291 1.00 22.41 ? 156 ILE A CG2 1 
ATOM   1077 C CD1 . ILE A 1 156 ? 19.057 -0.006  -38.905 1.00 25.79 ? 156 ILE A CD1 1 
ATOM   1078 N N   . LYS A 1 157 ? 21.958 -0.130  -43.606 1.00 28.36 ? 157 LYS A N   1 
ATOM   1079 C CA  . LYS A 1 157 ? 23.051 0.359   -44.432 1.00 33.81 ? 157 LYS A CA  1 
ATOM   1080 C C   . LYS A 1 157 ? 22.760 0.148   -45.919 1.00 30.90 ? 157 LYS A C   1 
ATOM   1081 O O   . LYS A 1 157 ? 23.056 1.020   -46.744 1.00 30.12 ? 157 LYS A O   1 
ATOM   1082 C CB  . LYS A 1 157 ? 24.344 -0.341  -44.002 1.00 34.55 ? 157 LYS A CB  1 
ATOM   1083 C CG  . LYS A 1 157 ? 25.594 0.026   -44.795 1.00 50.45 ? 157 LYS A CG  1 
ATOM   1084 C CD  . LYS A 1 157 ? 26.835 -0.682  -44.232 1.00 49.16 ? 157 LYS A CD  1 
ATOM   1085 C CE  . LYS A 1 157 ? 28.018 -0.607  -45.222 1.00 56.26 ? 157 LYS A CE  1 
ATOM   1086 N NZ  . LYS A 1 157 ? 29.309 -1.158  -44.675 1.00 36.67 ? 157 LYS A NZ  1 
ATOM   1087 N N   . LYS A 1 158 ? 22.164 -1.000  -46.277 1.00 23.70 ? 158 LYS A N   1 
ATOM   1088 C CA  . LYS A 1 158 ? 21.833 -1.280  -47.679 1.00 26.67 ? 158 LYS A CA  1 
ATOM   1089 C C   . LYS A 1 158 ? 20.767 -0.321  -48.198 1.00 27.46 ? 158 LYS A C   1 
ATOM   1090 O O   . LYS A 1 158 ? 20.877 0.201   -49.315 1.00 26.58 ? 158 LYS A O   1 
ATOM   1091 C CB  . LYS A 1 158 ? 21.366 -2.733  -47.814 1.00 30.62 ? 158 LYS A CB  1 
ATOM   1092 C CG  . LYS A 1 158 ? 21.286 -3.298  -49.245 1.00 46.15 ? 158 LYS A CG  1 
ATOM   1093 C CD  . LYS A 1 158 ? 20.998 -4.814  -49.208 1.00 44.49 ? 158 LYS A CD  1 
ATOM   1094 C CE  . LYS A 1 158 ? 20.544 -5.343  -50.573 1.00 54.39 ? 158 LYS A CE  1 
ATOM   1095 N NZ  . LYS A 1 158 ? 21.566 -5.168  -51.636 1.00 70.86 ? 158 LYS A NZ  1 
ATOM   1096 N N   . ILE A 1 159 ? 19.738 -0.046  -47.396 1.00 24.64 ? 159 ILE A N   1 
ATOM   1097 C CA  . ILE A 1 159 ? 18.699 0.876   -47.859 1.00 28.93 ? 159 ILE A CA  1 
ATOM   1098 C C   . ILE A 1 159 ? 19.238 2.307   -47.944 1.00 27.40 ? 159 ILE A C   1 
ATOM   1099 O O   . ILE A 1 159 ? 18.929 3.044   -48.893 1.00 27.15 ? 159 ILE A O   1 
ATOM   1100 C CB  . ILE A 1 159 ? 17.455 0.772   -46.958 1.00 30.74 ? 159 ILE A CB  1 
ATOM   1101 C CG1 . ILE A 1 159 ? 16.800 -0.616  -47.121 1.00 25.76 ? 159 ILE A CG1 1 
ATOM   1102 C CG2 . ILE A 1 159 ? 16.439 1.895   -47.282 1.00 26.49 ? 159 ILE A CG2 1 
ATOM   1103 C CD1 . ILE A 1 159 ? 15.707 -0.861  -46.114 1.00 30.73 ? 159 ILE A CD1 1 
ATOM   1104 N N   . ASN A 1 160 ? 20.067 2.719   -46.974 1.00 24.51 ? 160 ASN A N   1 
ATOM   1105 C CA  . ASN A 1 160 ? 20.731 4.017   -47.087 1.00 23.45 ? 160 ASN A CA  1 
ATOM   1106 C C   . ASN A 1 160 ? 21.468 4.147   -48.421 1.00 29.19 ? 160 ASN A C   1 
ATOM   1107 O O   . ASN A 1 160 ? 21.409 5.188   -49.081 1.00 26.37 ? 160 ASN A O   1 
ATOM   1108 C CB  . ASN A 1 160 ? 21.721 4.211   -45.941 1.00 25.84 ? 160 ASN A CB  1 
ATOM   1109 C CG  . ASN A 1 160 ? 21.053 4.679   -44.661 1.00 33.53 ? 160 ASN A CG  1 
ATOM   1110 O OD1 . ASN A 1 160 ? 19.971 5.252   -44.686 1.00 35.92 ? 160 ASN A OD1 1 
ATOM   1111 N ND2 . ASN A 1 160 ? 21.710 4.456   -43.548 1.00 35.38 ? 160 ASN A ND2 1 
ATOM   1112 N N   . ASN A 1 161 ? 22.166 3.085   -48.813 1.00 29.01 ? 161 ASN A N   1 
ATOM   1113 C CA  . ASN A 1 161 ? 22.977 3.133   -50.059 1.00 33.09 ? 161 ASN A CA  1 
ATOM   1114 C C   . ASN A 1 161 ? 22.047 3.236   -51.270 1.00 33.75 ? 161 ASN A C   1 
ATOM   1115 O O   . ASN A 1 161 ? 22.370 3.970   -52.212 1.00 31.16 ? 161 ASN A O   1 
ATOM   1116 C CB  . ASN A 1 161 ? 23.960 1.971   -50.108 1.00 34.17 ? 161 ASN A CB  1 
ATOM   1117 C CG  . ASN A 1 161 ? 25.144 2.216   -49.207 1.00 46.16 ? 161 ASN A CG  1 
ATOM   1118 O OD1 . ASN A 1 161 ? 25.818 3.241   -49.339 1.00 62.41 ? 161 ASN A OD1 1 
ATOM   1119 N ND2 . ASN A 1 161 ? 25.403 1.307   -48.281 1.00 55.63 ? 161 ASN A ND2 1 
ATOM   1120 N N   . GLU A 1 162 ? 20.921 2.538   -51.221 1.00 30.12 ? 162 GLU A N   1 
ATOM   1121 C CA  . GLU A 1 162 ? 19.977 2.593   -52.324 1.00 29.15 ? 162 GLU A CA  1 
ATOM   1122 C C   . GLU A 1 162 ? 19.377 3.987   -52.468 1.00 23.07 ? 162 GLU A C   1 
ATOM   1123 O O   . GLU A 1 162 ? 19.106 4.440   -53.595 1.00 30.34 ? 162 GLU A O   1 
ATOM   1124 C CB  . GLU A 1 162 ? 18.902 1.535   -52.103 1.00 35.18 ? 162 GLU A CB  1 
ATOM   1125 C CG  . GLU A 1 162 ? 17.896 1.416   -53.212 1.00 46.09 ? 162 GLU A CG  1 
ATOM   1126 C CD  . GLU A 1 162 ? 17.153 0.097   -53.149 1.00 61.52 ? 162 GLU A CD  1 
ATOM   1127 O OE1 . GLU A 1 162 ? 17.559 -0.769  -52.341 1.00 51.36 ? 162 GLU A OE1 1 
ATOM   1128 O OE2 . GLU A 1 162 ? 16.173 -0.072  -53.910 1.00 66.87 ? 162 GLU A OE2 1 
ATOM   1129 N N   . ILE A 1 163 ? 19.166 4.675   -51.343 1.00 23.79 ? 163 ILE A N   1 
ATOM   1130 C CA  . ILE A 1 163 ? 18.678 6.047   -51.378 1.00 25.99 ? 163 ILE A CA  1 
ATOM   1131 C C   . ILE A 1 163 ? 19.724 6.960   -52.001 1.00 25.35 ? 163 ILE A C   1 
ATOM   1132 O O   . ILE A 1 163 ? 19.401 7.807   -52.840 1.00 29.84 ? 163 ILE A O   1 
ATOM   1133 C CB  . ILE A 1 163 ? 18.285 6.515   -49.964 1.00 26.36 ? 163 ILE A CB  1 
ATOM   1134 C CG1 . ILE A 1 163 ? 17.016 5.784   -49.505 1.00 27.99 ? 163 ILE A CG1 1 
ATOM   1135 C CG2 . ILE A 1 163 ? 18.107 8.045   -49.926 1.00 26.91 ? 163 ILE A CG2 1 
ATOM   1136 C CD1 . ILE A 1 163 ? 16.654 6.013   -48.031 1.00 29.08 ? 163 ILE A CD1 1 
ATOM   1137 N N   . ARG A 1 164 ? 20.991 6.794   -51.618 1.00 26.43 ? 164 ARG A N   1 
ATOM   1138 C CA  A ARG A 1 164 ? 22.046 7.607   -52.216 0.48 30.55 ? 164 ARG A CA  1 
ATOM   1139 C CA  B ARG A 1 164 ? 22.047 7.605   -52.215 0.52 30.75 ? 164 ARG A CA  1 
ATOM   1140 C C   . ARG A 1 164 ? 22.098 7.408   -53.726 1.00 29.72 ? 164 ARG A C   1 
ATOM   1141 O O   . ARG A 1 164 ? 22.245 8.379   -54.486 1.00 28.39 ? 164 ARG A O   1 
ATOM   1142 C CB  A ARG A 1 164 ? 23.395 7.276   -51.581 0.48 33.84 ? 164 ARG A CB  1 
ATOM   1143 C CB  B ARG A 1 164 ? 23.395 7.270   -51.573 0.52 33.42 ? 164 ARG A CB  1 
ATOM   1144 C CG  A ARG A 1 164 ? 23.525 7.774   -50.151 0.48 39.45 ? 164 ARG A CG  1 
ATOM   1145 C CG  B ARG A 1 164 ? 23.447 7.614   -50.086 0.52 39.45 ? 164 ARG A CG  1 
ATOM   1146 C CD  A ARG A 1 164 ? 24.947 7.632   -49.619 0.48 41.84 ? 164 ARG A CD  1 
ATOM   1147 C CD  B ARG A 1 164 ? 24.805 7.328   -49.435 0.52 43.27 ? 164 ARG A CD  1 
ATOM   1148 N NE  A ARG A 1 164 ? 25.077 8.250   -48.304 0.48 44.61 ? 164 ARG A NE  1 
ATOM   1149 N NE  B ARG A 1 164 ? 24.746 7.555   -47.993 0.52 47.73 ? 164 ARG A NE  1 
ATOM   1150 C CZ  A ARG A 1 164 ? 25.324 9.538   -48.107 0.48 43.43 ? 164 ARG A CZ  1 
ATOM   1151 C CZ  B ARG A 1 164 ? 24.800 6.601   -47.071 0.52 44.02 ? 164 ARG A CZ  1 
ATOM   1152 N NH1 A ARG A 1 164 ? 25.512 10.366  -49.121 0.48 42.16 ? 164 ARG A NH1 1 
ATOM   1153 N NH1 B ARG A 1 164 ? 25.024 5.338   -47.394 0.52 38.56 ? 164 ARG A NH1 1 
ATOM   1154 N NH2 A ARG A 1 164 ? 25.376 10.009  -46.862 0.48 39.04 ? 164 ARG A NH2 1 
ATOM   1155 N NH2 B ARG A 1 164 ? 24.621 6.923   -45.794 0.52 41.01 ? 164 ARG A NH2 1 
ATOM   1156 N N   . ASP A 1 165 ? 21.956 6.157   -54.181 1.00 25.92 ? 165 ASP A N   1 
ATOM   1157 C CA  . ASP A 1 165 ? 21.952 5.877   -55.617 1.00 30.61 ? 165 ASP A CA  1 
ATOM   1158 C C   . ASP A 1 165 ? 20.728 6.473   -56.307 1.00 31.29 ? 165 ASP A C   1 
ATOM   1159 O O   . ASP A 1 165 ? 20.825 6.992   -57.424 1.00 30.13 ? 165 ASP A O   1 
ATOM   1160 C CB  . ASP A 1 165 ? 22.012 4.368   -55.852 1.00 34.53 ? 165 ASP A CB  1 
ATOM   1161 C CG  . ASP A 1 165 ? 23.361 3.777   -55.500 1.00 47.94 ? 165 ASP A CG  1 
ATOM   1162 O OD1 . ASP A 1 165 ? 24.326 4.557   -55.321 1.00 50.69 ? 165 ASP A OD1 1 
ATOM   1163 O OD2 . ASP A 1 165 ? 23.458 2.534   -55.392 1.00 53.21 ? 165 ASP A OD2 1 
ATOM   1164 N N   . LEU A 1 166 ? 19.568 6.398   -55.661 1.00 30.43 ? 166 LEU A N   1 
ATOM   1165 C CA  . LEU A 1 166 ? 18.347 6.931   -56.252 1.00 30.17 ? 166 LEU A CA  1 
ATOM   1166 C C   . LEU A 1 166 ? 18.451 8.434   -56.467 1.00 26.88 ? 166 LEU A C   1 
ATOM   1167 O O   . LEU A 1 166 ? 17.980 8.958   -57.487 1.00 28.90 ? 166 LEU A O   1 
ATOM   1168 C CB  . LEU A 1 166 ? 17.156 6.596   -55.353 1.00 30.02 ? 166 LEU A CB  1 
ATOM   1169 C CG  . LEU A 1 166 ? 15.809 7.214   -55.703 1.00 32.47 ? 166 LEU A CG  1 
ATOM   1170 C CD1 . LEU A 1 166 ? 15.322 6.687   -57.040 1.00 36.06 ? 166 LEU A CD1 1 
ATOM   1171 C CD2 . LEU A 1 166 ? 14.801 6.919   -54.585 1.00 31.58 ? 166 LEU A CD2 1 
ATOM   1172 N N   . LEU A 1 167 ? 19.090 9.139   -55.527 1.00 30.83 ? 167 LEU A N   1 
ATOM   1173 C CA  . LEU A 1 167 ? 19.285 10.582  -55.648 1.00 30.54 ? 167 LEU A CA  1 
ATOM   1174 C C   . LEU A 1 167 ? 20.086 10.962  -56.892 1.00 30.42 ? 167 LEU A C   1 
ATOM   1175 O O   . LEU A 1 167 ? 19.986 12.105  -57.358 1.00 28.58 ? 167 LEU A O   1 
ATOM   1176 C CB  . LEU A 1 167 ? 19.963 11.111  -54.382 1.00 26.19 ? 167 LEU A CB  1 
ATOM   1177 C CG  . LEU A 1 167 ? 18.991 11.279  -53.208 1.00 29.22 ? 167 LEU A CG  1 
ATOM   1178 C CD1 . LEU A 1 167 ? 19.707 11.306  -51.854 1.00 28.67 ? 167 LEU A CD1 1 
ATOM   1179 C CD2 . LEU A 1 167 ? 18.157 12.541  -53.407 1.00 30.52 ? 167 LEU A CD2 1 
ATOM   1180 N N   . GLU A 1 168 ? 20.867 10.030  -57.447 1.00 30.59 ? 168 GLU A N   1 
ATOM   1181 C CA  . GLU A 1 168 ? 21.557 10.302  -58.707 1.00 32.17 ? 168 GLU A CA  1 
ATOM   1182 C C   . GLU A 1 168 ? 20.591 10.694  -59.814 1.00 37.50 ? 168 GLU A C   1 
ATOM   1183 O O   . GLU A 1 168 ? 20.983 11.393  -60.755 1.00 35.89 ? 168 GLU A O   1 
ATOM   1184 C CB  . GLU A 1 168 ? 22.367 9.082   -59.148 1.00 30.73 ? 168 GLU A CB  1 
ATOM   1185 C CG  . GLU A 1 168 ? 23.680 8.962   -58.431 1.00 47.51 ? 168 GLU A CG  1 
ATOM   1186 C CD  . GLU A 1 168 ? 24.559 10.159  -58.719 1.00 44.93 ? 168 GLU A CD  1 
ATOM   1187 O OE1 . GLU A 1 168 ? 24.851 10.392  -59.910 1.00 56.39 ? 168 GLU A OE1 1 
ATOM   1188 O OE2 . GLU A 1 168 ? 24.933 10.872  -57.770 1.00 58.53 ? 168 GLU A OE2 1 
ATOM   1189 N N   . ARG A 1 169 ? 19.335 10.244  -59.737 1.00 34.11 ? 169 ARG A N   1 
ATOM   1190 C CA  . ARG A 1 169 ? 18.373 10.505  -60.805 1.00 32.79 ? 169 ARG A CA  1 
ATOM   1191 C C   . ARG A 1 169 ? 17.898 11.948  -60.843 1.00 34.30 ? 169 ARG A C   1 
ATOM   1192 O O   . ARG A 1 169 ? 17.216 12.320  -61.796 1.00 31.97 ? 169 ARG A O   1 
ATOM   1193 C CB  . ARG A 1 169 ? 17.149 9.593   -60.668 1.00 33.17 ? 169 ARG A CB  1 
ATOM   1194 C CG  . ARG A 1 169 ? 17.453 8.120   -60.865 1.00 46.69 ? 169 ARG A CG  1 
ATOM   1195 C CD  . ARG A 1 169 ? 16.179 7.293   -60.803 1.00 53.36 ? 169 ARG A CD  1 
ATOM   1196 N NE  . ARG A 1 169 ? 16.457 5.865   -60.877 1.00 65.57 ? 169 ARG A NE  1 
ATOM   1197 C CZ  . ARG A 1 169 ? 16.531 5.180   -62.010 1.00 69.91 ? 169 ARG A CZ  1 
ATOM   1198 N NH1 . ARG A 1 169 ? 16.354 5.767   -63.181 1.00 53.17 ? 169 ARG A NH1 1 
ATOM   1199 N NH2 . ARG A 1 169 ? 16.790 3.875   -61.966 1.00 85.44 ? 169 ARG A NH2 1 
ATOM   1200 N N   . LEU A 1 170 ? 18.191 12.754  -59.823 1.00 34.01 ? 170 LEU A N   1 
ATOM   1201 C CA  . LEU A 1 170 ? 17.874 14.171  -59.906 1.00 30.03 ? 170 LEU A CA  1 
ATOM   1202 C C   . LEU A 1 170 ? 18.534 14.758  -61.145 1.00 31.37 ? 170 LEU A C   1 
ATOM   1203 O O   . LEU A 1 170 ? 19.688 14.451  -61.451 1.00 33.22 ? 170 LEU A O   1 
ATOM   1204 C CB  . LEU A 1 170 ? 18.357 14.903  -58.650 1.00 26.89 ? 170 LEU A CB  1 
ATOM   1205 C CG  . LEU A 1 170 ? 17.638 14.488  -57.374 1.00 31.54 ? 170 LEU A CG  1 
ATOM   1206 C CD1 . LEU A 1 170 ? 18.264 15.223  -56.215 1.00 32.84 ? 170 LEU A CD1 1 
ATOM   1207 C CD2 . LEU A 1 170 ? 16.138 14.795  -57.492 1.00 28.79 ? 170 LEU A CD2 1 
ATOM   1208 N N   . LYS A 1 171 ? 17.777 15.579  -61.876 1.00 30.72 ? 171 LYS A N   1 
ATOM   1209 C CA  . LYS A 1 171 ? 18.270 16.113  -63.142 1.00 35.19 ? 171 LYS A CA  1 
ATOM   1210 C C   . LYS A 1 171 ? 19.423 17.088  -62.919 1.00 38.39 ? 171 LYS A C   1 
ATOM   1211 O O   . LYS A 1 171 ? 20.390 17.106  -63.692 1.00 42.79 ? 171 LYS A O   1 
ATOM   1212 C CB  . LYS A 1 171 ? 17.120 16.783  -63.902 1.00 43.41 ? 171 LYS A CB  1 
ATOM   1213 C CG  . LYS A 1 171 ? 16.103 15.805  -64.507 1.00 41.59 ? 171 LYS A CG  1 
ATOM   1214 N N   . CYS A 1 172 ? 19.352 17.877  -61.856 1.00 33.87 ? 172 CYS A N   1 
ATOM   1215 C CA  . CYS A 1 172 ? 20.356 18.893  -61.582 1.00 38.18 ? 172 CYS A CA  1 
ATOM   1216 C C   . CYS A 1 172 ? 21.731 18.265  -61.356 1.00 33.33 ? 172 CYS A C   1 
ATOM   1217 O O   . CYS A 1 172 ? 21.866 17.077  -61.057 1.00 36.34 ? 172 CYS A O   1 
ATOM   1218 C CB  . CYS A 1 172 ? 19.946 19.714  -60.361 1.00 33.98 ? 172 CYS A CB  1 
ATOM   1219 S SG  . CYS A 1 172 ? 19.823 18.713  -58.809 1.00 35.22 ? 172 CYS A SG  1 
ATOM   1220 N N   . SER A 1 173 ? 22.766 19.083  -61.522 1.00 31.55 ? 173 SER A N   1 
ATOM   1221 C CA  . SER A 1 173 ? 24.122 18.611  -61.278 1.00 33.08 ? 173 SER A CA  1 
ATOM   1222 C C   . SER A 1 173 ? 24.896 19.655  -60.489 1.00 31.14 ? 173 SER A C   1 
ATOM   1223 O O   . SER A 1 173 ? 25.247 19.431  -59.327 1.00 29.18 ? 173 SER A O   1 
ATOM   1224 C CB  . SER A 1 173 ? 24.824 18.296  -62.598 1.00 38.95 ? 173 SER A CB  1 
ATOM   1225 O OG  . SER A 1 173 ? 26.125 17.809  -62.342 1.00 47.81 ? 173 SER A OG  1 
ATOM   1226 N N   . GLN A 1 174 ? 25.137 20.806  -61.108 1.00 28.12 ? 174 GLN A N   1 
ATOM   1227 C CA  . GLN A 1 174 ? 25.789 21.919  -60.437 1.00 32.97 ? 174 GLN A CA  1 
ATOM   1228 C C   . GLN A 1 174 ? 24.800 22.889  -59.814 1.00 37.88 ? 174 GLN A C   1 
ATOM   1229 O O   . GLN A 1 174 ? 25.214 23.768  -59.051 1.00 41.58 ? 174 GLN A O   1 
ATOM   1230 C CB  . GLN A 1 174 ? 26.674 22.677  -61.432 1.00 29.88 ? 174 GLN A CB  1 
ATOM   1231 C CG  . GLN A 1 174 ? 27.904 21.902  -61.873 1.00 33.84 ? 174 GLN A CG  1 
ATOM   1232 C CD  . GLN A 1 174 ? 29.013 21.937  -60.839 1.00 32.50 ? 174 GLN A CD  1 
ATOM   1233 O OE1 . GLN A 1 174 ? 29.323 20.927  -60.212 1.00 30.41 ? 174 GLN A OE1 1 
ATOM   1234 N NE2 . GLN A 1 174 ? 29.613 23.104  -60.658 1.00 31.68 ? 174 GLN A NE2 1 
ATOM   1235 N N   . ASP A 1 175 ? 23.512 22.739  -60.103 1.00 31.97 ? 175 ASP A N   1 
ATOM   1236 C CA  . ASP A 1 175 ? 22.531 23.801  -59.930 1.00 36.46 ? 175 ASP A CA  1 
ATOM   1237 C C   . ASP A 1 175 ? 21.325 23.316  -59.140 1.00 30.80 ? 175 ASP A C   1 
ATOM   1238 O O   . ASP A 1 175 ? 20.189 23.720  -59.407 1.00 35.81 ? 175 ASP A O   1 
ATOM   1239 C CB  . ASP A 1 175 ? 22.091 24.335  -61.296 1.00 44.34 ? 175 ASP A CB  1 
ATOM   1240 C CG  . ASP A 1 175 ? 21.534 23.224  -62.218 1.00 55.53 ? 175 ASP A CG  1 
ATOM   1241 O OD1 . ASP A 1 175 ? 21.949 22.041  -62.103 1.00 41.63 ? 175 ASP A OD1 1 
ATOM   1242 O OD2 . ASP A 1 175 ? 20.676 23.539  -63.072 1.00 63.36 ? 175 ASP A OD2 1 
ATOM   1243 N N   . CYS A 1 176 ? 21.538 22.442  -58.156 1.00 27.54 ? 176 CYS A N   1 
ATOM   1244 C CA  . CYS A 1 176 ? 20.420 21.876  -57.409 1.00 27.24 ? 176 CYS A CA  1 
ATOM   1245 C C   . CYS A 1 176 ? 19.878 22.900  -56.425 1.00 37.73 ? 176 CYS A C   1 
ATOM   1246 O O   . CYS A 1 176 ? 20.641 23.509  -55.669 1.00 33.44 ? 176 CYS A O   1 
ATOM   1247 C CB  . CYS A 1 176 ? 20.829 20.611  -56.654 1.00 25.20 ? 176 CYS A CB  1 
ATOM   1248 S SG  . CYS A 1 176 ? 21.469 19.286  -57.731 1.00 32.53 ? 176 CYS A SG  1 
ATOM   1249 N N   . GLN A 1 177 ? 18.562 23.075  -56.433 1.00 28.73 ? 177 GLN A N   1 
ATOM   1250 C CA  . GLN A 1 177 ? 17.893 24.009  -55.546 1.00 36.85 ? 177 GLN A CA  1 
ATOM   1251 C C   . GLN A 1 177 ? 17.786 23.428  -54.144 1.00 30.13 ? 177 GLN A C   1 
ATOM   1252 O O   . GLN A 1 177 ? 17.638 22.213  -53.959 1.00 28.46 ? 177 GLN A O   1 
ATOM   1253 C CB  . GLN A 1 177 ? 16.504 24.335  -56.079 1.00 34.71 ? 177 GLN A CB  1 
ATOM   1254 C CG  . GLN A 1 177 ? 16.543 24.993  -57.451 1.00 41.62 ? 177 GLN A CG  1 
ATOM   1255 C CD  . GLN A 1 177 ? 15.768 26.279  -57.463 1.00 63.72 ? 177 GLN A CD  1 
ATOM   1256 O OE1 . GLN A 1 177 ? 14.553 26.284  -57.248 1.00 65.33 ? 177 GLN A OE1 1 
ATOM   1257 N NE2 . GLN A 1 177 ? 16.465 27.388  -57.691 1.00 71.97 ? 177 GLN A NE2 1 
ATOM   1258 N N   . THR A 1 178 ? 17.863 24.315  -53.149 1.00 27.23 ? 178 THR A N   1 
ATOM   1259 C CA  . THR A 1 178 ? 17.814 23.926  -51.746 1.00 27.92 ? 178 THR A CA  1 
ATOM   1260 C C   . THR A 1 178 ? 16.541 24.402  -51.048 1.00 32.01 ? 178 THR A C   1 
ATOM   1261 O O   . THR A 1 178 ? 16.490 24.422  -49.821 1.00 32.00 ? 178 THR A O   1 
ATOM   1262 C CB  . THR A 1 178 ? 19.049 24.456  -51.011 1.00 34.04 ? 178 THR A CB  1 
ATOM   1263 O OG1 . THR A 1 178 ? 19.166 25.876  -51.194 1.00 31.05 ? 178 THR A OG1 1 
ATOM   1264 C CG2 . THR A 1 178 ? 20.299 23.792  -51.539 1.00 30.45 ? 178 THR A CG2 1 
ATOM   1265 N N   . ASN A 1 179 ? 15.509 24.794  -51.800 1.00 29.73 ? 179 ASN A N   1 
ATOM   1266 C CA  . ASN A 1 179 ? 14.318 25.354  -51.165 1.00 32.64 ? 179 ASN A CA  1 
ATOM   1267 C C   . ASN A 1 179 ? 13.563 24.311  -50.351 1.00 31.64 ? 179 ASN A C   1 
ATOM   1268 O O   . ASN A 1 179 ? 13.001 24.635  -49.299 1.00 30.11 ? 179 ASN A O   1 
ATOM   1269 C CB  . ASN A 1 179 ? 13.398 25.955  -52.211 1.00 35.24 ? 179 ASN A CB  1 
ATOM   1270 C CG  . ASN A 1 179 ? 12.941 24.927  -53.212 1.00 48.58 ? 179 ASN A CG  1 
ATOM   1271 O OD1 . ASN A 1 179 ? 13.754 24.171  -53.753 1.00 35.72 ? 179 ASN A OD1 1 
ATOM   1272 N ND2 . ASN A 1 179 ? 11.633 24.858  -53.436 1.00 45.53 ? 179 ASN A ND2 1 
ATOM   1273 N N   . VAL A 1 180 ? 13.497 23.068  -50.834 1.00 30.98 ? 180 VAL A N   1 
ATOM   1274 C CA  . VAL A 1 180 ? 12.811 22.020  -50.076 1.00 29.93 ? 180 VAL A CA  1 
ATOM   1275 C C   . VAL A 1 180 ? 13.556 21.732  -48.781 1.00 31.34 ? 180 VAL A C   1 
ATOM   1276 O O   . VAL A 1 180 ? 12.954 21.592  -47.707 1.00 29.51 ? 180 VAL A O   1 
ATOM   1277 C CB  . VAL A 1 180 ? 12.654 20.755  -50.942 1.00 29.03 ? 180 VAL A CB  1 
ATOM   1278 C CG1 . VAL A 1 180 ? 12.032 19.610  -50.145 1.00 26.47 ? 180 VAL A CG1 1 
ATOM   1279 C CG2 . VAL A 1 180 ? 11.829 21.084  -52.182 1.00 32.59 ? 180 VAL A CG2 1 
ATOM   1280 N N   . TYR A 1 181 ? 14.882 21.628  -48.866 1.00 26.53 ? 181 TYR A N   1 
ATOM   1281 C CA  . TYR A 1 181 ? 15.712 21.504  -47.669 1.00 28.66 ? 181 TYR A CA  1 
ATOM   1282 C C   . TYR A 1 181 ? 15.389 22.607  -46.661 1.00 23.46 ? 181 TYR A C   1 
ATOM   1283 O O   . TYR A 1 181 ? 15.065 22.340  -45.492 1.00 25.93 ? 181 TYR A O   1 
ATOM   1284 C CB  . TYR A 1 181 ? 17.169 21.558  -48.119 1.00 25.00 ? 181 TYR A CB  1 
ATOM   1285 C CG  . TYR A 1 181 ? 18.235 21.743  -47.076 1.00 26.76 ? 181 TYR A CG  1 
ATOM   1286 C CD1 . TYR A 1 181 ? 18.656 20.673  -46.284 1.00 22.90 ? 181 TYR A CD1 1 
ATOM   1287 C CD2 . TYR A 1 181 ? 18.906 22.969  -46.949 1.00 26.89 ? 181 TYR A CD2 1 
ATOM   1288 C CE1 . TYR A 1 181 ? 19.685 20.833  -45.351 1.00 28.02 ? 181 TYR A CE1 1 
ATOM   1289 C CE2 . TYR A 1 181 ? 19.931 23.132  -46.013 1.00 27.72 ? 181 TYR A CE2 1 
ATOM   1290 C CZ  . TYR A 1 181 ? 20.324 22.054  -45.231 1.00 23.63 ? 181 TYR A CZ  1 
ATOM   1291 O OH  . TYR A 1 181 ? 21.354 22.220  -44.316 1.00 28.77 ? 181 TYR A OH  1 
ATOM   1292 N N   . TRP A 1 182 ? 15.412 23.860  -47.121 1.00 26.06 ? 182 TRP A N   1 
ATOM   1293 C CA  . TRP A 1 182 ? 15.201 24.971  -46.198 1.00 32.99 ? 182 TRP A CA  1 
ATOM   1294 C C   . TRP A 1 182 ? 13.787 24.948  -45.633 1.00 34.47 ? 182 TRP A C   1 
ATOM   1295 O O   . TRP A 1 182 ? 13.587 25.228  -44.445 1.00 32.87 ? 182 TRP A O   1 
ATOM   1296 C CB  . TRP A 1 182 ? 15.492 26.298  -46.898 1.00 32.89 ? 182 TRP A CB  1 
ATOM   1297 C CG  . TRP A 1 182 ? 15.778 27.424  -45.934 1.00 42.29 ? 182 TRP A CG  1 
ATOM   1298 C CD1 . TRP A 1 182 ? 14.991 28.517  -45.679 1.00 44.79 ? 182 TRP A CD1 1 
ATOM   1299 C CD2 . TRP A 1 182 ? 16.941 27.565  -45.105 1.00 32.18 ? 182 TRP A CD2 1 
ATOM   1300 N NE1 . TRP A 1 182 ? 15.598 29.330  -44.749 1.00 43.92 ? 182 TRP A NE1 1 
ATOM   1301 C CE2 . TRP A 1 182 ? 16.793 28.766  -44.377 1.00 47.49 ? 182 TRP A CE2 1 
ATOM   1302 C CE3 . TRP A 1 182 ? 18.093 26.791  -44.910 1.00 30.22 ? 182 TRP A CE3 1 
ATOM   1303 C CZ2 . TRP A 1 182 ? 17.760 29.213  -43.462 1.00 41.64 ? 182 TRP A CZ2 1 
ATOM   1304 C CZ3 . TRP A 1 182 ? 19.046 27.233  -43.999 1.00 33.55 ? 182 TRP A CZ3 1 
ATOM   1305 C CH2 . TRP A 1 182 ? 18.874 28.429  -43.288 1.00 35.79 ? 182 TRP A CH2 1 
ATOM   1306 N N   . ASP A 1 183 ? 12.798 24.608  -46.468 1.00 32.78 ? 183 ASP A N   1 
ATOM   1307 C CA  . ASP A 1 183 ? 11.418 24.530  -45.995 1.00 30.68 ? 183 ASP A CA  1 
ATOM   1308 C C   . ASP A 1 183 ? 11.279 23.514  -44.876 1.00 36.79 ? 183 ASP A C   1 
ATOM   1309 O O   . ASP A 1 183 ? 10.536 23.736  -43.912 1.00 31.56 ? 183 ASP A O   1 
ATOM   1310 C CB  . ASP A 1 183 ? 10.474 24.148  -47.133 1.00 30.19 ? 183 ASP A CB  1 
ATOM   1311 C CG  . ASP A 1 183 ? 10.208 25.286  -48.097 1.00 42.26 ? 183 ASP A CG  1 
ATOM   1312 O OD1 . ASP A 1 183 ? 10.369 26.472  -47.727 1.00 41.27 ? 183 ASP A OD1 1 
ATOM   1313 O OD2 . ASP A 1 183 ? 9.810  24.981  -49.239 1.00 36.35 ? 183 ASP A OD2 1 
ATOM   1314 N N   . PHE A 1 184 ? 11.963 22.375  -44.996 1.00 26.53 ? 184 PHE A N   1 
ATOM   1315 C CA  . PHE A 1 184 ? 11.818 21.362  -43.963 1.00 24.90 ? 184 PHE A CA  1 
ATOM   1316 C C   . PHE A 1 184 ? 12.527 21.765  -42.675 1.00 28.98 ? 184 PHE A C   1 
ATOM   1317 O O   . PHE A 1 184 ? 12.024 21.476  -41.582 1.00 29.30 ? 184 PHE A O   1 
ATOM   1318 C CB  . PHE A 1 184 ? 12.297 20.003  -44.476 1.00 30.03 ? 184 PHE A CB  1 
ATOM   1319 C CG  . PHE A 1 184 ? 11.195 19.199  -45.118 1.00 30.02 ? 184 PHE A CG  1 
ATOM   1320 C CD1 . PHE A 1 184 ? 10.275 18.500  -44.334 1.00 35.39 ? 184 PHE A CD1 1 
ATOM   1321 C CD2 . PHE A 1 184 ? 11.039 19.193  -46.505 1.00 32.83 ? 184 PHE A CD2 1 
ATOM   1322 C CE1 . PHE A 1 184 ? 9.236  17.778  -44.929 1.00 36.47 ? 184 PHE A CE1 1 
ATOM   1323 C CE2 . PHE A 1 184 ? 10.011 18.484  -47.104 1.00 27.35 ? 184 PHE A CE2 1 
ATOM   1324 C CZ  . PHE A 1 184 ? 9.107  17.776  -46.323 1.00 32.24 ? 184 PHE A CZ  1 
ATOM   1325 N N   . ILE A 1 185 ? 13.647 22.483  -42.769 1.00 26.69 ? 185 ILE A N   1 
ATOM   1326 C CA  . ILE A 1 185 ? 14.265 23.022  -41.555 1.00 28.30 ? 185 ILE A CA  1 
ATOM   1327 C C   . ILE A 1 185 ? 13.278 23.918  -40.809 1.00 29.99 ? 185 ILE A C   1 
ATOM   1328 O O   . ILE A 1 185 ? 13.158 23.849  -39.576 1.00 31.00 ? 185 ILE A O   1 
ATOM   1329 C CB  . ILE A 1 185 ? 15.570 23.759  -41.915 1.00 32.26 ? 185 ILE A CB  1 
ATOM   1330 C CG1 . ILE A 1 185 ? 16.662 22.720  -42.233 1.00 30.90 ? 185 ILE A CG1 1 
ATOM   1331 C CG2 . ILE A 1 185 ? 16.014 24.667  -40.787 1.00 29.19 ? 185 ILE A CG2 1 
ATOM   1332 C CD1 . ILE A 1 185 ? 17.691 23.227  -43.204 1.00 32.12 ? 185 ILE A CD1 1 
ATOM   1333 N N   . LYS A 1 186 ? 12.540 24.758  -41.538 1.00 29.72 ? 186 LYS A N   1 
ATOM   1334 C CA  . LYS A 1 186 ? 11.569 25.631  -40.875 1.00 33.18 ? 186 LYS A CA  1 
ATOM   1335 C C   . LYS A 1 186 ? 10.460 24.823  -40.199 1.00 36.10 ? 186 LYS A C   1 
ATOM   1336 O O   . LYS A 1 186 ? 10.043 25.151  -39.080 1.00 35.20 ? 186 LYS A O   1 
ATOM   1337 C CB  . LYS A 1 186 ? 10.994 26.635  -41.869 1.00 31.31 ? 186 LYS A CB  1 
ATOM   1338 C CG  . LYS A 1 186 ? 12.063 27.538  -42.497 1.00 43.22 ? 186 LYS A CG  1 
ATOM   1339 C CD  . LYS A 1 186 ? 11.472 28.816  -43.082 1.00 52.63 ? 186 LYS A CD  1 
ATOM   1340 C CE  . LYS A 1 186 ? 10.860 28.580  -44.450 1.00 55.03 ? 186 LYS A CE  1 
ATOM   1341 N NZ  . LYS A 1 186 ? 11.218 29.701  -45.361 1.00 58.67 ? 186 LYS A NZ  1 
ATOM   1342 N N   . ILE A 1 187 ? 9.983  23.759  -40.855 1.00 33.52 ? 187 ILE A N   1 
ATOM   1343 C CA  . ILE A 1 187 ? 9.015  22.850  -40.237 1.00 39.68 ? 187 ILE A CA  1 
ATOM   1344 C C   . ILE A 1 187 ? 9.587  22.235  -38.966 1.00 32.84 ? 187 ILE A C   1 
ATOM   1345 O O   . ILE A 1 187 ? 8.908  22.132  -37.936 1.00 31.56 ? 187 ILE A O   1 
ATOM   1346 C CB  . ILE A 1 187 ? 8.608  21.743  -41.230 1.00 38.66 ? 187 ILE A CB  1 
ATOM   1347 C CG1 . ILE A 1 187 ? 7.823  22.316  -42.403 1.00 37.02 ? 187 ILE A CG1 1 
ATOM   1348 C CG2 . ILE A 1 187 ? 7.823  20.651  -40.502 1.00 40.66 ? 187 ILE A CG2 1 
ATOM   1349 C CD1 . ILE A 1 187 ? 7.542  21.276  -43.490 1.00 37.14 ? 187 ILE A CD1 1 
ATOM   1350 N N   . TYR A 1 188 ? 10.836 21.773  -39.032 1.00 29.05 ? 188 TYR A N   1 
ATOM   1351 C CA  . TYR A 1 188 ? 11.423 21.100  -37.877 1.00 25.54 ? 188 TYR A CA  1 
ATOM   1352 C C   . TYR A 1 188 ? 11.505 22.031  -36.675 1.00 27.09 ? 188 TYR A C   1 
ATOM   1353 O O   . TYR A 1 188 ? 11.232 21.614  -35.541 1.00 32.06 ? 188 TYR A O   1 
ATOM   1354 C CB  . TYR A 1 188 ? 12.801 20.572  -38.241 1.00 27.35 ? 188 TYR A CB  1 
ATOM   1355 C CG  . TYR A 1 188 ? 12.759 19.481  -39.291 1.00 29.86 ? 188 TYR A CG  1 
ATOM   1356 C CD1 . TYR A 1 188 ? 11.559 18.842  -39.621 1.00 26.21 ? 188 TYR A CD1 1 
ATOM   1357 C CD2 . TYR A 1 188 ? 13.924 19.076  -39.946 1.00 26.44 ? 188 TYR A CD2 1 
ATOM   1358 C CE1 . TYR A 1 188 ? 11.525 17.823  -40.591 1.00 28.74 ? 188 TYR A CE1 1 
ATOM   1359 C CE2 . TYR A 1 188 ? 13.895 18.072  -40.919 1.00 23.68 ? 188 TYR A CE2 1 
ATOM   1360 C CZ  . TYR A 1 188 ? 12.702 17.445  -41.227 1.00 27.78 ? 188 TYR A CZ  1 
ATOM   1361 O OH  . TYR A 1 188 ? 12.718 16.431  -42.173 1.00 26.46 ? 188 TYR A OH  1 
ATOM   1362 N N   . LEU A 1 189 ? 11.858 23.299  -36.904 1.00 31.20 ? 189 LEU A N   1 
ATOM   1363 C CA  . LEU A 1 189 ? 11.938 24.256  -35.797 1.00 31.43 ? 189 LEU A CA  1 
ATOM   1364 C C   . LEU A 1 189 ? 10.592 24.436  -35.108 1.00 36.75 ? 189 LEU A C   1 
ATOM   1365 O O   . LEU A 1 189 ? 10.542 24.602  -33.883 1.00 31.96 ? 189 LEU A O   1 
ATOM   1366 C CB  . LEU A 1 189 ? 12.446 25.610  -36.295 1.00 30.97 ? 189 LEU A CB  1 
ATOM   1367 C CG  . LEU A 1 189 ? 13.833 25.612  -36.926 1.00 44.58 ? 189 LEU A CG  1 
ATOM   1368 C CD1 . LEU A 1 189 ? 14.154 27.024  -37.399 1.00 47.75 ? 189 LEU A CD1 1 
ATOM   1369 C CD2 . LEU A 1 189 ? 14.861 25.119  -35.927 1.00 38.50 ? 189 LEU A CD2 1 
ATOM   1370 N N   . VAL A 1 190 ? 9.498  24.453  -35.881 1.00 34.01 ? 190 VAL A N   1 
ATOM   1371 C CA  . VAL A 1 190 ? 8.155  24.510  -35.294 1.00 36.92 ? 190 VAL A CA  1 
ATOM   1372 C C   . VAL A 1 190 ? 7.876  23.253  -34.483 1.00 34.01 ? 190 VAL A C   1 
ATOM   1373 O O   . VAL A 1 190 ? 7.368  23.319  -33.353 1.00 34.25 ? 190 VAL A O   1 
ATOM   1374 C CB  . VAL A 1 190 ? 7.083  24.704  -36.386 1.00 34.52 ? 190 VAL A CB  1 
ATOM   1375 C CG1 . VAL A 1 190 ? 5.664  24.569  -35.785 1.00 40.02 ? 190 VAL A CG1 1 
ATOM   1376 C CG2 . VAL A 1 190 ? 7.255  26.033  -37.094 1.00 38.97 ? 190 VAL A CG2 1 
ATOM   1377 N N   . ASP A 1 191 ? 8.196  22.081  -35.051 1.00 33.58 ? 191 ASP A N   1 
ATOM   1378 C CA  . ASP A 1 191 ? 8.007  20.826  -34.329 1.00 33.07 ? 191 ASP A CA  1 
ATOM   1379 C C   . ASP A 1 191 ? 8.816  20.787  -33.035 1.00 36.52 ? 191 ASP A C   1 
ATOM   1380 O O   . ASP A 1 191 ? 8.336  20.268  -32.022 1.00 34.79 ? 191 ASP A O   1 
ATOM   1381 C CB  . ASP A 1 191 ? 8.391  19.630  -35.206 1.00 32.55 ? 191 ASP A CB  1 
ATOM   1382 C CG  . ASP A 1 191 ? 7.438  19.422  -36.369 1.00 48.93 ? 191 ASP A CG  1 
ATOM   1383 O OD1 . ASP A 1 191 ? 6.402  20.119  -36.438 1.00 44.42 ? 191 ASP A OD1 1 
ATOM   1384 O OD2 . ASP A 1 191 ? 7.735  18.562  -37.221 1.00 38.99 ? 191 ASP A OD2 1 
ATOM   1385 N N   . PHE A 1 192 ? 10.052 21.315  -33.051 1.00 33.11 ? 192 PHE A N   1 
ATOM   1386 C CA  . PHE A 1 192 ? 10.888 21.304  -31.845 1.00 31.74 ? 192 PHE A CA  1 
ATOM   1387 C C   . PHE A 1 192 ? 10.203 22.009  -30.677 1.00 37.58 ? 192 PHE A C   1 
ATOM   1388 O O   . PHE A 1 192 ? 10.378 21.605  -29.522 1.00 44.11 ? 192 PHE A O   1 
ATOM   1389 C CB  . PHE A 1 192 ? 12.239 21.986  -32.100 1.00 35.21 ? 192 PHE A CB  1 
ATOM   1390 C CG  . PHE A 1 192 ? 13.144 21.247  -33.060 1.00 27.78 ? 192 PHE A CG  1 
ATOM   1391 C CD1 . PHE A 1 192 ? 12.945 19.903  -33.342 1.00 24.65 ? 192 PHE A CD1 1 
ATOM   1392 C CD2 . PHE A 1 192 ? 14.201 21.912  -33.676 1.00 31.18 ? 192 PHE A CD2 1 
ATOM   1393 C CE1 . PHE A 1 192 ? 13.799 19.220  -34.241 1.00 27.03 ? 192 PHE A CE1 1 
ATOM   1394 C CE2 . PHE A 1 192 ? 15.044 21.251  -34.570 1.00 29.05 ? 192 PHE A CE2 1 
ATOM   1395 C CZ  . PHE A 1 192 ? 14.841 19.898  -34.846 1.00 28.29 ? 192 PHE A CZ  1 
ATOM   1396 N N   . LYS A 1 193 ? 9.446  23.071  -30.954 1.00 40.56 ? 193 LYS A N   1 
ATOM   1397 C CA  . LYS A 1 193 ? 8.795  23.836  -29.894 1.00 41.64 ? 193 LYS A CA  1 
ATOM   1398 C C   . LYS A 1 193 ? 7.742  23.025  -29.159 1.00 51.42 ? 193 LYS A C   1 
ATOM   1399 O O   . LYS A 1 193 ? 7.446  23.325  -27.997 1.00 57.98 ? 193 LYS A O   1 
ATOM   1400 C CB  . LYS A 1 193 ? 8.144  25.094  -30.459 1.00 35.08 ? 193 LYS A CB  1 
ATOM   1401 C CG  . LYS A 1 193 ? 9.041  25.934  -31.359 1.00 59.55 ? 193 LYS A CG  1 
ATOM   1402 C CD  . LYS A 1 193 ? 10.197 26.557  -30.592 1.00 61.79 ? 193 LYS A CD  1 
ATOM   1403 N N   . LYS A 1 194 ? 7.177  22.003  -29.801 1.00 42.88 ? 194 LYS A N   1 
ATOM   1404 C CA  . LYS A 1 194 ? 6.160  21.200  -29.134 1.00 52.65 ? 194 LYS A CA  1 
ATOM   1405 C C   . LYS A 1 194 ? 6.755  20.320  -28.040 1.00 54.95 ? 194 LYS A C   1 
ATOM   1406 O O   . LYS A 1 194 ? 6.059  19.988  -27.075 1.00 71.58 ? 194 LYS A O   1 
ATOM   1407 C CB  . LYS A 1 194 ? 5.412  20.349  -30.158 1.00 50.02 ? 194 LYS A CB  1 
ATOM   1408 C CG  . LYS A 1 194 ? 4.585  21.161  -31.139 1.00 55.31 ? 194 LYS A CG  1 
ATOM   1409 C CD  . LYS A 1 194 ? 4.435  20.426  -32.462 1.00 53.22 ? 194 LYS A CD  1 
ATOM   1410 C CE  . LYS A 1 194 ? 3.695  21.285  -33.483 1.00 61.06 ? 194 LYS A CE  1 
ATOM   1411 N NZ  . LYS A 1 194 ? 3.572  20.595  -34.805 1.00 59.31 ? 194 LYS A NZ  1 
ATOM   1412 N N   . MET A 1 195 ? 8.023  19.943  -28.161 1.00 51.38 ? 195 MET A N   1 
ATOM   1413 C CA  . MET A 1 195 ? 8.618  19.031  -27.190 1.00 64.52 ? 195 MET A CA  1 
ATOM   1414 C C   . MET A 1 195 ? 8.821  19.735  -25.855 1.00 63.06 ? 195 MET A C   1 
ATOM   1415 O O   . MET A 1 195 ? 9.461  20.794  -25.809 1.00 51.15 ? 195 MET A O   1 
ATOM   1416 C CB  . MET A 1 195 ? 9.958  18.477  -27.673 1.00 59.54 ? 195 MET A CB  1 
ATOM   1417 C CG  . MET A 1 195 ? 10.751 17.870  -26.515 1.00 69.30 ? 195 MET A CG  1 
ATOM   1418 S SD  . MET A 1 195 ? 12.138 16.807  -26.939 1.00 70.58 ? 195 MET A SD  1 
ATOM   1419 C CE  . MET A 1 195 ? 11.317 15.542  -27.862 1.00 51.62 ? 195 MET A CE  1 
ATOM   1420 N N   . PRO A 1 196 ? 8.327  19.167  -24.750 1.00 87.78 ? 196 PRO A N   1 
ATOM   1421 C CA  . PRO A 1 196 ? 8.518  19.798  -23.437 1.00 83.34 ? 196 PRO A CA  1 
ATOM   1422 C C   . PRO A 1 196 ? 9.959  19.702  -22.960 1.00 75.64 ? 196 PRO A C   1 
ATOM   1423 O O   . PRO A 1 196 ? 10.244 19.003  -21.982 1.00 76.14 ? 196 PRO A O   1 
ATOM   1424 C CB  . PRO A 1 196 ? 7.576  19.004  -22.518 1.00 78.21 ? 196 PRO A CB  1 
ATOM   1425 C CG  . PRO A 1 196 ? 6.805  18.049  -23.422 1.00 77.11 ? 196 PRO A CG  1 
ATOM   1426 C CD  . PRO A 1 196 ? 7.630  17.874  -24.649 1.00 74.44 ? 196 PRO A CD  1 
ATOM   1427 N N   . LEU A 1 197 ? 10.872 20.410  -23.634 1.00 54.37 ? 197 LEU A N   1 
ATOM   1428 C CA  . LEU A 1 197 ? 12.296 20.236  -23.364 1.00 54.91 ? 197 LEU A CA  1 
ATOM   1429 C C   . LEU A 1 197 ? 12.672 20.802  -22.000 1.00 62.22 ? 197 LEU A C   1 
ATOM   1430 O O   . LEU A 1 197 ? 13.420 20.170  -21.243 1.00 59.52 ? 197 LEU A O   1 
ATOM   1431 C CB  . LEU A 1 197 ? 13.117 20.884  -24.481 1.00 56.42 ? 197 LEU A CB  1 
ATOM   1432 C CG  . LEU A 1 197 ? 14.474 20.257  -24.824 1.00 58.10 ? 197 LEU A CG  1 
ATOM   1433 C CD1 . LEU A 1 197 ? 14.347 18.781  -25.146 1.00 50.07 ? 197 LEU A CD1 1 
ATOM   1434 C CD2 . LEU A 1 197 ? 15.122 20.979  -25.984 1.00 46.48 ? 197 LEU A CD2 1 
ATOM   1435 N N   . GLU A 1 198 ? 12.144 21.979  -21.660 1.00 50.63 ? 198 GLU A N   1 
ATOM   1436 C CA  . GLU A 1 198 ? 12.382 22.538  -20.338 1.00 55.51 ? 198 GLU A CA  1 
ATOM   1437 C C   . GLU A 1 198 ? 11.765 21.660  -19.259 1.00 53.11 ? 198 GLU A C   1 
ATOM   1438 O O   . GLU A 1 198 ? 12.355 21.478  -18.189 1.00 47.27 ? 198 GLU A O   1 
ATOM   1439 C CB  . GLU A 1 198 ? 11.833 23.969  -20.264 1.00 52.95 ? 198 GLU A CB  1 
ATOM   1440 C CG  . GLU A 1 198 ? 12.035 24.654  -18.907 1.00 64.66 ? 198 GLU A CG  1 
ATOM   1441 C CD  . GLU A 1 198 ? 11.667 26.133  -18.914 1.00 68.56 ? 198 GLU A CD  1 
ATOM   1442 O OE1 . GLU A 1 198 ? 11.182 26.630  -19.957 1.00 60.44 ? 198 GLU A OE1 1 
ATOM   1443 O OE2 . GLU A 1 198 ? 11.872 26.798  -17.872 1.00 68.40 ? 198 GLU A OE2 1 
ATOM   1444 N N   . ASN A 1 199 ? 10.584 21.094  -19.527 1.00 51.36 ? 199 ASN A N   1 
ATOM   1445 C CA  . ASN A 1 199 ? 9.948  20.218  -18.548 1.00 58.11 ? 199 ASN A CA  1 
ATOM   1446 C C   . ASN A 1 199 ? 10.756 18.945  -18.323 1.00 48.90 ? 199 ASN A C   1 
ATOM   1447 O O   . ASN A 1 199 ? 10.795 18.431  -17.197 1.00 50.70 ? 199 ASN A O   1 
ATOM   1448 C CB  . ASN A 1 199 ? 8.524  19.873  -18.986 1.00 65.11 ? 199 ASN A CB  1 
ATOM   1449 C CG  . ASN A 1 199 ? 7.526  20.985  -18.676 1.00 73.07 ? 199 ASN A CG  1 
ATOM   1450 O OD1 . ASN A 1 199 ? 7.902  22.144  -18.466 1.00 72.48 ? 199 ASN A OD1 1 
ATOM   1451 N ND2 . ASN A 1 199 ? 6.244  20.633  -18.653 1.00 65.51 ? 199 ASN A ND2 1 
ATOM   1452 N N   . TYR A 1 200 ? 11.410 18.432  -19.368 1.00 45.88 ? 200 TYR A N   1 
ATOM   1453 C CA  . TYR A 1 200 ? 12.248 17.247  -19.205 1.00 43.96 ? 200 TYR A CA  1 
ATOM   1454 C C   . TYR A 1 200 ? 13.465 17.540  -18.345 1.00 42.64 ? 200 TYR A C   1 
ATOM   1455 O O   . TYR A 1 200 ? 13.842 16.718  -17.501 1.00 43.67 ? 200 TYR A O   1 
ATOM   1456 C CB  . TYR A 1 200 ? 12.676 16.710  -20.561 1.00 41.51 ? 200 TYR A CB  1 
ATOM   1457 C CG  . TYR A 1 200 ? 11.628 15.829  -21.175 1.00 50.48 ? 200 TYR A CG  1 
ATOM   1458 C CD1 . TYR A 1 200 ? 10.717 15.156  -20.374 1.00 62.62 ? 200 TYR A CD1 1 
ATOM   1459 C CD2 . TYR A 1 200 ? 11.536 15.675  -22.540 1.00 45.51 ? 200 TYR A CD2 1 
ATOM   1460 C CE1 . TYR A 1 200 ? 9.752  14.348  -20.922 1.00 60.49 ? 200 TYR A CE1 1 
ATOM   1461 C CE2 . TYR A 1 200 ? 10.569 14.872  -23.104 1.00 52.99 ? 200 TYR A CE2 1 
ATOM   1462 C CZ  . TYR A 1 200 ? 9.682  14.211  -22.289 1.00 39.92 ? 200 TYR A CZ  1 
ATOM   1463 O OH  . TYR A 1 200 ? 8.711  13.400  -22.824 1.00 57.32 ? 200 TYR A OH  1 
ATOM   1464 N N   . ASP A 1 201 ? 14.094 18.703  -18.544 1.00 43.02 ? 201 ASP A N   1 
ATOM   1465 C CA  . ASP A 1 201 ? 15.131 19.158  -17.621 1.00 42.12 ? 201 ASP A CA  1 
ATOM   1466 C C   . ASP A 1 201 ? 14.604 19.226  -16.195 1.00 49.42 ? 201 ASP A C   1 
ATOM   1467 O O   . ASP A 1 201 ? 15.245 18.733  -15.259 1.00 48.69 ? 201 ASP A O   1 
ATOM   1468 C CB  . ASP A 1 201 ? 15.656 20.525  -18.056 1.00 46.32 ? 201 ASP A CB  1 
ATOM   1469 C CG  . ASP A 1 201 ? 16.413 20.461  -19.356 1.00 49.87 ? 201 ASP A CG  1 
ATOM   1470 O OD1 . ASP A 1 201 ? 17.081 19.430  -19.587 1.00 43.90 ? 201 ASP A OD1 1 
ATOM   1471 O OD2 . ASP A 1 201 ? 16.335 21.431  -20.142 1.00 57.85 ? 201 ASP A OD2 1 
ATOM   1472 N N   . THR A 1 202 ? 13.440 19.852  -16.007 1.00 50.03 ? 202 THR A N   1 
ATOM   1473 C CA  . THR A 1 202 ? 12.855 19.934  -14.673 1.00 52.66 ? 202 THR A CA  1 
ATOM   1474 C C   . THR A 1 202 ? 12.604 18.549  -14.096 1.00 46.31 ? 202 THR A C   1 
ATOM   1475 O O   . THR A 1 202 ? 12.880 18.303  -12.917 1.00 50.90 ? 202 THR A O   1 
ATOM   1476 C CB  . THR A 1 202 ? 11.556 20.736  -14.715 1.00 50.77 ? 202 THR A CB  1 
ATOM   1477 O OG1 . THR A 1 202 ? 11.833 22.048  -15.213 1.00 59.20 ? 202 THR A OG1 1 
ATOM   1478 C CG2 . THR A 1 202 ? 10.942 20.838  -13.324 1.00 57.75 ? 202 THR A CG2 1 
ATOM   1479 N N   . PHE A 1 203 ? 12.103 17.624  -14.915 1.00 50.12 ? 203 PHE A N   1 
ATOM   1480 C CA  . PHE A 1 203 ? 11.771 16.304  -14.396 1.00 49.63 ? 203 PHE A CA  1 
ATOM   1481 C C   . PHE A 1 203 ? 13.009 15.530  -13.983 1.00 49.54 ? 203 PHE A C   1 
ATOM   1482 O O   . PHE A 1 203 ? 13.016 14.870  -12.937 1.00 43.28 ? 203 PHE A O   1 
ATOM   1483 C CB  . PHE A 1 203 ? 11.015 15.465  -15.411 1.00 50.11 ? 203 PHE A CB  1 
ATOM   1484 C CG  . PHE A 1 203 ? 10.974 14.023  -15.022 1.00 64.29 ? 203 PHE A CG  1 
ATOM   1485 C CD1 . PHE A 1 203 ? 10.250 13.623  -13.903 1.00 61.86 ? 203 PHE A CD1 1 
ATOM   1486 C CD2 . PHE A 1 203 ? 11.715 13.074  -15.713 1.00 53.13 ? 203 PHE A CD2 1 
ATOM   1487 C CE1 . PHE A 1 203 ? 10.227 12.297  -13.506 1.00 51.37 ? 203 PHE A CE1 1 
ATOM   1488 C CE2 . PHE A 1 203 ? 11.694 11.753  -15.317 1.00 51.98 ? 203 PHE A CE2 1 
ATOM   1489 C CZ  . PHE A 1 203 ? 10.948 11.367  -14.205 1.00 47.23 ? 203 PHE A CZ  1 
ATOM   1490 N N   . ILE A 1 204 ? 14.030 15.505  -14.840 1.00 41.38 ? 204 ILE A N   1 
ATOM   1491 C CA  . ILE A 1 204 ? 15.162 14.643  -14.527 1.00 44.16 ? 204 ILE A CA  1 
ATOM   1492 C C   . ILE A 1 204 ? 15.950 15.225  -13.356 1.00 40.73 ? 204 ILE A C   1 
ATOM   1493 O O   . ILE A 1 204 ? 16.527 14.475  -12.560 1.00 35.85 ? 204 ILE A O   1 
ATOM   1494 C CB  . ILE A 1 204 ? 16.024 14.398  -15.785 1.00 34.47 ? 204 ILE A CB  1 
ATOM   1495 C CG1 . ILE A 1 204 ? 16.906 13.158  -15.593 1.00 33.07 ? 204 ILE A CG1 1 
ATOM   1496 C CG2 . ILE A 1 204 ? 16.850 15.617  -16.131 1.00 33.19 ? 204 ILE A CG2 1 
ATOM   1497 C CD1 . ILE A 1 204 ? 16.122 11.883  -15.220 1.00 25.11 ? 204 ILE A CD1 1 
ATOM   1498 N N   . LYS A 1 205 ? 15.924 16.553  -13.183 1.00 38.92 ? 205 LYS A N   1 
ATOM   1499 C CA  . LYS A 1 205 ? 16.582 17.161  -12.027 1.00 48.30 ? 205 LYS A CA  1 
ATOM   1500 C C   . LYS A 1 205 ? 15.859 16.811  -10.731 1.00 49.65 ? 205 LYS A C   1 
ATOM   1501 O O   . LYS A 1 205 ? 16.488 16.358  -9.767  1.00 54.52 ? 205 LYS A O   1 
ATOM   1502 C CB  . LYS A 1 205 ? 16.677 18.677  -12.194 1.00 56.38 ? 205 LYS A CB  1 
ATOM   1503 C CG  . LYS A 1 205 ? 17.550 19.328  -11.126 1.00 68.90 ? 205 LYS A CG  1 
ATOM   1504 C CD  . LYS A 1 205 ? 17.905 20.774  -11.447 1.00 68.05 ? 205 LYS A CD  1 
ATOM   1505 C CE  . LYS A 1 205 ? 19.212 21.160  -10.760 1.00 73.63 ? 205 LYS A CE  1 
ATOM   1506 N NZ  . LYS A 1 205 ? 19.333 22.622  -10.508 1.00 65.34 ? 205 LYS A NZ  1 
ATOM   1507 N N   . GLN A 1 206 ? 14.539 17.039  -10.681 1.00 55.68 ? 206 GLN A N   1 
ATOM   1508 C CA  . GLN A 1 206 ? 13.738 16.585  -9.545  1.00 65.44 ? 206 GLN A CA  1 
ATOM   1509 C C   . GLN A 1 206 ? 14.025 15.135  -9.229  1.00 61.00 ? 206 GLN A C   1 
ATOM   1510 O O   . GLN A 1 206 ? 14.194 14.753  -8.066  1.00 62.45 ? 206 GLN A O   1 
ATOM   1511 C CB  . GLN A 1 206 ? 12.246 16.726  -9.844  1.00 66.07 ? 206 GLN A CB  1 
ATOM   1512 C CG  . GLN A 1 206 ? 11.690 18.099  -9.653  1.00 75.84 ? 206 GLN A CG  1 
ATOM   1513 C CD  . GLN A 1 206 ? 10.216 18.159  -9.976  1.00 82.06 ? 206 GLN A CD  1 
ATOM   1514 O OE1 . GLN A 1 206 ? 9.564  17.127  -10.141 1.00 88.00 ? 206 GLN A OE1 1 
ATOM   1515 N NE2 . GLN A 1 206 ? 9.682  19.368  -10.076 1.00 67.47 ? 206 GLN A NE2 1 
ATOM   1516 N N   . PHE A 1 207 ? 14.093 14.314  -10.264 1.00 50.32 ? 207 PHE A N   1 
ATOM   1517 C CA  . PHE A 1 207 ? 14.164 12.885  -10.053 1.00 47.81 ? 207 PHE A CA  1 
ATOM   1518 C C   . PHE A 1 207 ? 15.549 12.452  -9.607  1.00 47.77 ? 207 PHE A C   1 
ATOM   1519 O O   . PHE A 1 207 ? 15.685 11.548  -8.770  1.00 42.45 ? 207 PHE A O   1 
ATOM   1520 C CB  . PHE A 1 207 ? 13.774 12.171  -11.326 1.00 50.12 ? 207 PHE A CB  1 
ATOM   1521 C CG  . PHE A 1 207 ? 13.169 10.875  -11.072 1.00 51.66 ? 207 PHE A CG  1 
ATOM   1522 C CD1 . PHE A 1 207 ? 13.960 9.792   -10.735 1.00 51.05 ? 207 PHE A CD1 1 
ATOM   1523 C CD2 . PHE A 1 207 ? 11.799 10.736  -11.101 1.00 45.20 ? 207 PHE A CD2 1 
ATOM   1524 C CE1 . PHE A 1 207 ? 13.394 8.581   -10.470 1.00 59.80 ? 207 PHE A CE1 1 
ATOM   1525 C CE2 . PHE A 1 207 ? 11.232 9.531   -10.859 1.00 55.24 ? 207 PHE A CE2 1 
ATOM   1526 C CZ  . PHE A 1 207 ? 12.034 8.442   -10.533 1.00 66.36 ? 207 PHE A CZ  1 
ATOM   1527 N N   . LYS A 1 208 ? 16.585 13.059  -10.180 1.00 33.50 ? 208 LYS A N   1 
ATOM   1528 C CA  . LYS A 1 208 ? 17.945 12.735  -9.773  1.00 39.21 ? 208 LYS A CA  1 
ATOM   1529 C C   . LYS A 1 208 ? 18.178 13.145  -8.329  1.00 45.72 ? 208 LYS A C   1 
ATOM   1530 O O   . LYS A 1 208 ? 18.803 12.406  -7.562  1.00 38.94 ? 208 LYS A O   1 
ATOM   1531 C CB  . LYS A 1 208 ? 18.939 13.430  -10.700 1.00 44.55 ? 208 LYS A CB  1 
ATOM   1532 C CG  . LYS A 1 208 ? 20.234 12.685  -10.955 1.00 49.68 ? 208 LYS A CG  1 
ATOM   1533 C CD  . LYS A 1 208 ? 21.011 13.364  -12.096 1.00 44.11 ? 208 LYS A CD  1 
ATOM   1534 C CE  . LYS A 1 208 ? 22.477 12.948  -12.108 1.00 51.62 ? 208 LYS A CE  1 
ATOM   1535 N NZ  . LYS A 1 208 ? 22.697 11.630  -12.774 1.00 61.59 ? 208 LYS A NZ  1 
ATOM   1536 N N   . ASN A 1 209 ? 17.671 14.322  -7.943  1.00 41.79 ? 209 ASN A N   1 
ATOM   1537 C CA  . ASN A 1 209 ? 17.831 14.795  -6.569  1.00 46.59 ? 209 ASN A CA  1 
ATOM   1538 C C   . ASN A 1 209 ? 17.105 13.891  -5.586  1.00 43.02 ? 209 ASN A C   1 
ATOM   1539 O O   . ASN A 1 209 ? 17.655 13.542  -4.536  1.00 52.08 ? 209 ASN A O   1 
ATOM   1540 C CB  . ASN A 1 209 ? 17.329 16.235  -6.439  1.00 48.23 ? 209 ASN A CB  1 
ATOM   1541 C CG  . ASN A 1 209 ? 18.195 17.218  -7.190  1.00 69.31 ? 209 ASN A CG  1 
ATOM   1542 O OD1 . ASN A 1 209 ? 19.365 16.946  -7.460  1.00 79.04 ? 209 ASN A OD1 1 
ATOM   1543 N ND2 . ASN A 1 209 ? 17.625 18.371  -7.538  1.00 77.76 ? 209 ASN A ND2 1 
ATOM   1544 N N   . SER A 1 210 ? 15.873 13.490  -5.907  1.00 38.92 ? 210 SER A N   1 
ATOM   1545 C CA  . SER A 1 210 ? 15.148 12.587  -5.017  1.00 49.18 ? 210 SER A CA  1 
ATOM   1546 C C   . SER A 1 210 ? 15.824 11.217  -4.948  1.00 50.65 ? 210 SER A C   1 
ATOM   1547 O O   . SER A 1 210 ? 15.885 10.597  -3.876  1.00 42.03 ? 210 SER A O   1 
ATOM   1548 C CB  . SER A 1 210 ? 13.690 12.469  -5.465  1.00 46.51 ? 210 SER A CB  1 
ATOM   1549 O OG  . SER A 1 210 ? 13.457 11.284  -6.209  1.00 62.84 ? 210 SER A OG  1 
ATOM   1550 N N   . TYR A 1 211 ? 16.350 10.736  -6.076  1.00 33.91 ? 211 TYR A N   1 
ATOM   1551 C CA  . TYR A 1 211 ? 17.105 9.489   -6.081  1.00 29.91 ? 211 TYR A CA  1 
ATOM   1552 C C   . TYR A 1 211 ? 18.298 9.548   -5.124  1.00 33.08 ? 211 TYR A C   1 
ATOM   1553 O O   . TYR A 1 211 ? 18.494 8.647   -4.299  1.00 36.72 ? 211 TYR A O   1 
ATOM   1554 C CB  . TYR A 1 211 ? 17.570 9.200   -7.502  1.00 30.76 ? 211 TYR A CB  1 
ATOM   1555 C CG  . TYR A 1 211 ? 18.665 8.176   -7.624  1.00 29.89 ? 211 TYR A CG  1 
ATOM   1556 C CD1 . TYR A 1 211 ? 18.402 6.824   -7.442  1.00 33.75 ? 211 TYR A CD1 1 
ATOM   1557 C CD2 . TYR A 1 211 ? 19.952 8.552   -7.990  1.00 39.76 ? 211 TYR A CD2 1 
ATOM   1558 C CE1 . TYR A 1 211 ? 19.396 5.870   -7.591  1.00 32.37 ? 211 TYR A CE1 1 
ATOM   1559 C CE2 . TYR A 1 211 ? 20.961 7.602   -8.144  1.00 39.51 ? 211 TYR A CE2 1 
ATOM   1560 C CZ  . TYR A 1 211 ? 20.675 6.264   -7.939  1.00 40.97 ? 211 TYR A CZ  1 
ATOM   1561 O OH  . TYR A 1 211 ? 21.661 5.311   -8.074  1.00 46.28 ? 211 TYR A OH  1 
ATOM   1562 N N   . LEU A 1 212 ? 19.125 10.592  -5.243  1.00 33.24 ? 212 LEU A N   1 
ATOM   1563 C CA  . LEU A 1 212 ? 20.319 10.689  -4.402  1.00 45.70 ? 212 LEU A CA  1 
ATOM   1564 C C   . LEU A 1 212 ? 19.950 10.863  -2.938  1.00 41.95 ? 212 LEU A C   1 
ATOM   1565 O O   . LEU A 1 212 ? 20.685 10.406  -2.054  1.00 47.00 ? 212 LEU A O   1 
ATOM   1566 C CB  . LEU A 1 212 ? 21.215 11.843  -4.866  1.00 40.51 ? 212 LEU A CB  1 
ATOM   1567 C CG  . LEU A 1 212 ? 21.760 11.737  -6.293  1.00 51.45 ? 212 LEU A CG  1 
ATOM   1568 C CD1 . LEU A 1 212 ? 22.354 13.070  -6.725  1.00 58.50 ? 212 LEU A CD1 1 
ATOM   1569 C CD2 . LEU A 1 212 ? 22.793 10.623  -6.412  1.00 53.23 ? 212 LEU A CD2 1 
ATOM   1570 N N   . SER A 1 213 ? 18.812 11.499  -2.661  1.00 43.02 ? 213 SER A N   1 
ATOM   1571 C CA  . SER A 1 213 ? 18.342 11.591  -1.288  1.00 50.35 ? 213 SER A CA  1 
ATOM   1572 C C   . SER A 1 213 ? 17.980 10.214  -0.745  1.00 48.23 ? 213 SER A C   1 
ATOM   1573 O O   . SER A 1 213 ? 18.355 9.864   0.383   1.00 46.07 ? 213 SER A O   1 
ATOM   1574 C CB  . SER A 1 213 ? 17.146 12.541  -1.202  1.00 59.26 ? 213 SER A CB  1 
ATOM   1575 O OG  . SER A 1 213 ? 15.919 11.844  -1.385  1.00 64.03 ? 213 SER A OG  1 
ATOM   1576 N N   . TYR A 1 214 ? 17.243 9.417   -1.531  1.00 34.80 ? 214 TYR A N   1 
ATOM   1577 C CA  . TYR A 1 214 ? 16.889 8.068   -1.094  1.00 33.75 ? 214 TYR A CA  1 
ATOM   1578 C C   . TYR A 1 214 ? 18.130 7.223   -0.834  1.00 31.61 ? 214 TYR A C   1 
ATOM   1579 O O   . TYR A 1 214 ? 18.150 6.419   0.102   1.00 34.41 ? 214 TYR A O   1 
ATOM   1580 C CB  . TYR A 1 214 ? 16.034 7.338   -2.139  1.00 41.29 ? 214 TYR A CB  1 
ATOM   1581 C CG  . TYR A 1 214 ? 14.695 7.930   -2.519  1.00 51.66 ? 214 TYR A CG  1 
ATOM   1582 C CD1 . TYR A 1 214 ? 13.912 8.623   -1.606  1.00 46.80 ? 214 TYR A CD1 1 
ATOM   1583 C CD2 . TYR A 1 214 ? 14.206 7.760   -3.819  1.00 52.99 ? 214 TYR A CD2 1 
ATOM   1584 C CE1 . TYR A 1 214 ? 12.675 9.153   -1.986  1.00 52.73 ? 214 TYR A CE1 1 
ATOM   1585 C CE2 . TYR A 1 214 ? 12.983 8.279   -4.211  1.00 48.94 ? 214 TYR A CE2 1 
ATOM   1586 C CZ  . TYR A 1 214 ? 12.219 8.971   -3.297  1.00 64.61 ? 214 TYR A CZ  1 
ATOM   1587 O OH  . TYR A 1 214 ? 11.008 9.474   -3.725  1.00 55.35 ? 214 TYR A OH  1 
ATOM   1588 N N   . VAL A 1 215 ? 19.131 7.311   -1.718  1.00 32.36 ? 215 VAL A N   1 
ATOM   1589 C CA  . VAL A 1 215 ? 20.325 6.481   -1.575  1.00 36.59 ? 215 VAL A CA  1 
ATOM   1590 C C   . VAL A 1 215 ? 21.033 6.814   -0.271  1.00 44.77 ? 215 VAL A C   1 
ATOM   1591 O O   . VAL A 1 215 ? 21.421 5.926   0.502   1.00 37.75 ? 215 VAL A O   1 
ATOM   1592 C CB  . VAL A 1 215 ? 21.258 6.664   -2.789  1.00 33.41 ? 215 VAL A CB  1 
ATOM   1593 C CG1 . VAL A 1 215 ? 22.602 6.018   -2.534  1.00 42.35 ? 215 VAL A CG1 1 
ATOM   1594 C CG2 . VAL A 1 215 ? 20.639 6.086   -4.067  1.00 32.59 ? 215 VAL A CG2 1 
ATOM   1595 N N   . ASP A 1 216 ? 21.188 8.110   0.002   1.00 39.44 ? 216 ASP A N   1 
ATOM   1596 C CA  . ASP A 1 216 ? 21.824 8.530   1.243   1.00 48.25 ? 216 ASP A CA  1 
ATOM   1597 C C   . ASP A 1 216 ? 20.977 8.140   2.448   1.00 49.39 ? 216 ASP A C   1 
ATOM   1598 O O   . ASP A 1 216 ? 21.508 7.757   3.496   1.00 44.39 ? 216 ASP A O   1 
ATOM   1599 C CB  . ASP A 1 216 ? 22.070 10.037  1.211   1.00 45.54 ? 216 ASP A CB  1 
ATOM   1600 C CG  . ASP A 1 216 ? 23.063 10.478  2.268   1.00 64.35 ? 216 ASP A CG  1 
ATOM   1601 O OD1 . ASP A 1 216 ? 24.232 10.038  2.193   1.00 59.27 ? 216 ASP A OD1 1 
ATOM   1602 O OD2 . ASP A 1 216 ? 22.676 11.249  3.172   1.00 62.43 ? 216 ASP A OD2 1 
ATOM   1603 N N   . LEU A 1 217 ? 19.656 8.197   2.295   1.00 47.91 ? 217 LEU A N   1 
ATOM   1604 C CA  . LEU A 1 217 ? 18.739 7.858   3.375   1.00 34.47 ? 217 LEU A CA  1 
ATOM   1605 C C   . LEU A 1 217 ? 18.808 6.373   3.725   1.00 43.11 ? 217 LEU A C   1 
ATOM   1606 O O   . LEU A 1 217 ? 18.820 6.003   4.909   1.00 50.05 ? 217 LEU A O   1 
ATOM   1607 C CB  . LEU A 1 217 ? 17.328 8.243   2.946   1.00 51.31 ? 217 LEU A CB  1 
ATOM   1608 C CG  . LEU A 1 217 ? 16.194 8.502   3.928   1.00 58.97 ? 217 LEU A CG  1 
ATOM   1609 C CD1 . LEU A 1 217 ? 16.272 9.925   4.449   1.00 64.45 ? 217 LEU A CD1 1 
ATOM   1610 C CD2 . LEU A 1 217 ? 14.858 8.243   3.240   1.00 56.72 ? 217 LEU A CD2 1 
ATOM   1611 N N   . ILE A 1 218 ? 18.831 5.508   2.710   1.00 38.97 ? 218 ILE A N   1 
ATOM   1612 C CA  . ILE A 1 218 ? 18.949 4.072   2.946   1.00 37.73 ? 218 ILE A CA  1 
ATOM   1613 C C   . ILE A 1 218 ? 20.285 3.742   3.593   1.00 42.84 ? 218 ILE A C   1 
ATOM   1614 O O   . ILE A 1 218 ? 20.382 2.827   4.420   1.00 45.19 ? 218 ILE A O   1 
ATOM   1615 C CB  . ILE A 1 218 ? 18.758 3.301   1.628   1.00 38.51 ? 218 ILE A CB  1 
ATOM   1616 C CG1 . ILE A 1 218 ? 17.300 3.378   1.192   1.00 36.04 ? 218 ILE A CG1 1 
ATOM   1617 C CG2 . ILE A 1 218 ? 19.182 1.860   1.783   1.00 42.13 ? 218 ILE A CG2 1 
ATOM   1618 C CD1 . ILE A 1 218 ? 16.347 2.847   2.238   1.00 39.89 ? 218 ILE A CD1 1 
ATOM   1619 N N   . ARG A 1 219 ? 21.339 4.474   3.225   1.00 43.98 ? 219 ARG A N   1 
ATOM   1620 C CA  . ARG A 1 219 ? 22.636 4.240   3.851   1.00 49.02 ? 219 ARG A CA  1 
ATOM   1621 C C   . ARG A 1 219 ? 22.587 4.538   5.341   1.00 47.04 ? 219 ARG A C   1 
ATOM   1622 O O   . ARG A 1 219 ? 23.249 3.862   6.138   1.00 47.42 ? 219 ARG A O   1 
ATOM   1623 C CB  . ARG A 1 219 ? 23.709 5.078   3.166   1.00 46.26 ? 219 ARG A CB  1 
ATOM   1624 C CG  . ARG A 1 219 ? 24.125 4.511   1.833   1.00 46.07 ? 219 ARG A CG  1 
ATOM   1625 C CD  . ARG A 1 219 ? 25.413 5.130   1.337   1.00 65.41 ? 219 ARG A CD  1 
ATOM   1626 N NE  . ARG A 1 219 ? 25.235 6.522   0.949   1.00 56.27 ? 219 ARG A NE  1 
ATOM   1627 C CZ  . ARG A 1 219 ? 25.600 7.032   -0.217  1.00 56.48 ? 219 ARG A CZ  1 
ATOM   1628 N NH1 . ARG A 1 219 ? 26.152 6.280   -1.160  1.00 55.76 ? 219 ARG A NH1 1 
ATOM   1629 N NH2 . ARG A 1 219 ? 25.423 8.335   -0.436  1.00 49.01 ? 219 ARG A NH2 1 
ATOM   1630 N N   . LYS A 1 220 ? 21.814 5.552   5.739   1.00 41.00 ? 220 LYS A N   1 
ATOM   1631 C CA  . LYS A 1 220 ? 21.645 5.821   7.164   1.00 41.54 ? 220 LYS A CA  1 
ATOM   1632 C C   . LYS A 1 220 ? 20.754 4.774   7.823   1.00 52.76 ? 220 LYS A C   1 
ATOM   1633 O O   . LYS A 1 220 ? 21.042 4.317   8.937   1.00 44.36 ? 220 LYS A O   1 
ATOM   1634 C CB  . LYS A 1 220 ? 21.073 7.222   7.366   1.00 46.87 ? 220 LYS A CB  1 
ATOM   1635 C CG  . LYS A 1 220 ? 21.996 8.338   6.883   1.00 53.54 ? 220 LYS A CG  1 
ATOM   1636 C CD  . LYS A 1 220 ? 21.353 9.697   7.082   1.00 60.25 ? 220 LYS A CD  1 
ATOM   1637 C CE  . LYS A 1 220 ? 22.175 10.802  6.451   1.00 68.28 ? 220 LYS A CE  1 
ATOM   1638 N NZ  . LYS A 1 220 ? 21.454 12.112  6.453   1.00 70.64 ? 220 LYS A NZ  1 
ATOM   1639 N N   . TYR A 1 221 ? 19.679 4.366   7.143   1.00 51.00 ? 221 TYR A N   1 
ATOM   1640 C CA  . TYR A 1 221 ? 18.726 3.428   7.734   1.00 49.89 ? 221 TYR A CA  1 
ATOM   1641 C C   . TYR A 1 221 ? 19.353 2.066   7.990   1.00 40.14 ? 221 TYR A C   1 
ATOM   1642 O O   . TYR A 1 221 ? 19.000 1.391   8.966   1.00 54.21 ? 221 TYR A O   1 
ATOM   1643 C CB  . TYR A 1 221 ? 17.509 3.262   6.827   1.00 51.30 ? 221 TYR A CB  1 
ATOM   1644 C CG  . TYR A 1 221 ? 16.608 4.466   6.756   1.00 63.69 ? 221 TYR A CG  1 
ATOM   1645 C CD1 . TYR A 1 221 ? 16.551 5.392   7.798   1.00 67.62 ? 221 TYR A CD1 1 
ATOM   1646 C CD2 . TYR A 1 221 ? 15.807 4.675   5.645   1.00 64.23 ? 221 TYR A CD2 1 
ATOM   1647 C CE1 . TYR A 1 221 ? 15.718 6.496   7.723   1.00 65.87 ? 221 TYR A CE1 1 
ATOM   1648 C CE2 . TYR A 1 221 ? 14.973 5.762   5.562   1.00 69.24 ? 221 TYR A CE2 1 
ATOM   1649 C CZ  . TYR A 1 221 ? 14.931 6.674   6.599   1.00 76.42 ? 221 TYR A CZ  1 
ATOM   1650 O OH  . TYR A 1 221 ? 14.093 7.762   6.493   1.00 80.00 ? 221 TYR A OH  1 
ATOM   1651 N N   . GLU A 1 222 ? 20.264 1.633   7.113   1.00 41.05 ? 222 GLU A N   1 
ATOM   1652 C CA  . GLU A 1 222 ? 20.909 0.337   7.287   1.00 49.84 ? 222 GLU A CA  1 
ATOM   1653 C C   . GLU A 1 222 ? 21.554 0.210   8.663   1.00 49.16 ? 222 GLU A C   1 
ATOM   1654 O O   . GLU A 1 222 ? 21.691 -0.903  9.178   1.00 52.16 ? 222 GLU A O   1 
ATOM   1655 C CB  . GLU A 1 222 ? 21.953 0.114   6.190   1.00 52.13 ? 222 GLU A CB  1 
ATOM   1656 C CG  . GLU A 1 222 ? 21.369 -0.144  4.803   1.00 49.44 ? 222 GLU A CG  1 
ATOM   1657 C CD  . GLU A 1 222 ? 22.445 -0.316  3.751   1.00 62.32 ? 222 GLU A CD  1 
ATOM   1658 O OE1 . GLU A 1 222 ? 23.503 0.344   3.866   1.00 70.31 ? 222 GLU A OE1 1 
ATOM   1659 O OE2 . GLU A 1 222 ? 22.234 -1.114  2.811   1.00 67.52 ? 222 GLU A OE2 1 
ATOM   1660 N N   . LYS A 1 223 ? 21.933 1.334   9.278   1.00 57.31 ? 223 LYS A N   1 
ATOM   1661 C CA  . LYS A 1 223 ? 22.514 1.341   10.617  1.00 47.65 ? 223 LYS A CA  1 
ATOM   1662 C C   . LYS A 1 223 ? 21.484 1.549   11.719  1.00 52.94 ? 223 LYS A C   1 
ATOM   1663 O O   . LYS A 1 223 ? 21.734 1.159   12.864  1.00 59.92 ? 223 LYS A O   1 
ATOM   1664 C CB  . LYS A 1 223 ? 23.571 2.446   10.738  1.00 51.09 ? 223 LYS A CB  1 
ATOM   1665 C CG  . LYS A 1 223 ? 24.522 2.577   9.552   1.00 59.46 ? 223 LYS A CG  1 
ATOM   1666 C CD  . LYS A 1 223 ? 25.284 1.288   9.281   1.00 72.53 ? 223 LYS A CD  1 
ATOM   1667 C CE  . LYS A 1 223 ? 26.376 1.514   8.241   1.00 78.51 ? 223 LYS A CE  1 
ATOM   1668 N NZ  . LYS A 1 223 ? 26.665 0.292   7.438   1.00 76.61 ? 223 LYS A NZ  1 
ATOM   1669 N N   . GLN A 1 224 ? 20.344 2.168   11.412  1.00 47.99 ? 224 GLN A N   1 
ATOM   1670 C CA  . GLN A 1 224 ? 19.371 2.531   12.434  1.00 51.83 ? 224 GLN A CA  1 
ATOM   1671 C C   . GLN A 1 224 ? 18.191 1.575   12.514  1.00 51.42 ? 224 GLN A C   1 
ATOM   1672 O O   . GLN A 1 224 ? 17.482 1.571   13.527  1.00 48.17 ? 224 GLN A O   1 
ATOM   1673 C CB  . GLN A 1 224 ? 18.842 3.950   12.176  1.00 61.43 ? 224 GLN A CB  1 
ATOM   1674 C CG  . GLN A 1 224 ? 19.922 5.022   12.092  1.00 62.65 ? 224 GLN A CG  1 
ATOM   1675 C CD  . GLN A 1 224 ? 19.442 6.296   11.409  1.00 70.30 ? 224 GLN A CD  1 
ATOM   1676 O OE1 . GLN A 1 224 ? 18.245 6.491   11.189  1.00 69.82 ? 224 GLN A OE1 1 
ATOM   1677 N NE2 . GLN A 1 224 ? 20.382 7.166   11.064  1.00 66.77 ? 224 GLN A NE2 1 
ATOM   1678 N N   . ILE A 1 225 ? 17.966 0.767   11.481  1.00 44.65 ? 225 ILE A N   1 
ATOM   1679 C CA  . ILE A 1 225 ? 16.766 -0.048  11.357  1.00 43.99 ? 225 ILE A CA  1 
ATOM   1680 C C   . ILE A 1 225 ? 17.193 -1.475  11.048  1.00 55.15 ? 225 ILE A C   1 
ATOM   1681 O O   . ILE A 1 225 ? 17.992 -1.704  10.132  1.00 57.15 ? 225 ILE A O   1 
ATOM   1682 C CB  . ILE A 1 225 ? 15.837 0.494   10.250  1.00 53.69 ? 225 ILE A CB  1 
ATOM   1683 C CG1 . ILE A 1 225 ? 15.443 1.949   10.533  1.00 52.64 ? 225 ILE A CG1 1 
ATOM   1684 C CG2 . ILE A 1 225 ? 14.599 -0.376  10.090  1.00 47.29 ? 225 ILE A CG2 1 
ATOM   1685 C CD1 . ILE A 1 225 ? 14.643 2.593   9.404   1.00 56.42 ? 225 ILE A CD1 1 
ATOM   1686 N N   . ASP A 1 226 ? 16.649 -2.433  11.795  1.00 38.92 ? 226 ASP A N   1 
ATOM   1687 C CA  . ASP A 1 226 ? 16.945 -3.851  11.590  1.00 41.37 ? 226 ASP A CA  1 
ATOM   1688 C C   . ASP A 1 226 ? 15.841 -4.478  10.735  1.00 45.11 ? 226 ASP A C   1 
ATOM   1689 O O   . ASP A 1 226 ? 14.864 -5.049  11.232  1.00 37.10 ? 226 ASP A O   1 
ATOM   1690 C CB  . ASP A 1 226 ? 17.101 -4.555  12.936  1.00 47.83 ? 226 ASP A CB  1 
ATOM   1691 C CG  . ASP A 1 226 ? 17.168 -6.059  12.798  1.00 62.82 ? 226 ASP A CG  1 
ATOM   1692 O OD1 . ASP A 1 226 ? 17.778 -6.546  11.814  1.00 58.85 ? 226 ASP A OD1 1 
ATOM   1693 O OD2 . ASP A 1 226 ? 16.607 -6.751  13.673  1.00 63.73 ? 226 ASP A OD2 1 
ATOM   1694 N N   . ASP A 1 227 ? 16.013 -4.369  9.409   1.00 40.68 ? 227 ASP A N   1 
ATOM   1695 C CA  . ASP A 1 227 ? 15.026 -4.860  8.451   1.00 29.91 ? 227 ASP A CA  1 
ATOM   1696 C C   . ASP A 1 227 ? 15.704 -5.131  7.108   1.00 33.59 ? 227 ASP A C   1 
ATOM   1697 O O   . ASP A 1 227 ? 15.412 -4.448  6.116   1.00 30.36 ? 227 ASP A O   1 
ATOM   1698 C CB  . ASP A 1 227 ? 13.893 -3.840  8.302   1.00 31.88 ? 227 ASP A CB  1 
ATOM   1699 C CG  . ASP A 1 227 ? 12.709 -4.374  7.508   1.00 32.96 ? 227 ASP A CG  1 
ATOM   1700 O OD1 . ASP A 1 227 ? 12.807 -5.479  6.943   1.00 31.29 ? 227 ASP A OD1 1 
ATOM   1701 O OD2 . ASP A 1 227 ? 11.676 -3.675  7.433   1.00 36.38 ? 227 ASP A OD2 1 
ATOM   1702 N N   . PRO A 1 228 ? 16.608 -6.116  7.039   1.00 32.03 ? 228 PRO A N   1 
ATOM   1703 C CA  . PRO A 1 228 ? 17.371 -6.316  5.798   1.00 29.62 ? 228 PRO A CA  1 
ATOM   1704 C C   . PRO A 1 228 ? 16.526 -6.748  4.619   1.00 29.34 ? 228 PRO A C   1 
ATOM   1705 O O   . PRO A 1 228 ? 16.933 -6.488  3.483   1.00 29.19 ? 228 PRO A O   1 
ATOM   1706 C CB  . PRO A 1 228 ? 18.394 -7.401  6.176   1.00 32.11 ? 228 PRO A CB  1 
ATOM   1707 C CG  . PRO A 1 228 ? 17.796 -8.086  7.383   1.00 36.72 ? 228 PRO A CG  1 
ATOM   1708 C CD  . PRO A 1 228 ? 17.076 -7.003  8.127   1.00 39.15 ? 228 PRO A CD  1 
ATOM   1709 N N   . ILE A 1 229 ? 15.388 -7.417  4.840   1.00 30.04 ? 229 ILE A N   1 
ATOM   1710 C CA  . ILE A 1 229 ? 14.552 -7.848  3.722   1.00 28.94 ? 229 ILE A CA  1 
ATOM   1711 C C   . ILE A 1 229 ? 13.915 -6.649  3.030   1.00 31.05 ? 229 ILE A C   1 
ATOM   1712 O O   . ILE A 1 229 ? 13.863 -6.577  1.792   1.00 30.10 ? 229 ILE A O   1 
ATOM   1713 C CB  . ILE A 1 229 ? 13.481 -8.846  4.196   1.00 29.26 ? 229 ILE A CB  1 
ATOM   1714 C CG1 . ILE A 1 229 ? 14.132 -10.138 4.680   1.00 35.22 ? 229 ILE A CG1 1 
ATOM   1715 C CG2 . ILE A 1 229 ? 12.525 -9.167  3.046   1.00 29.60 ? 229 ILE A CG2 1 
ATOM   1716 C CD1 . ILE A 1 229 ? 13.166 -11.074 5.386   1.00 41.22 ? 229 ILE A CD1 1 
ATOM   1717 N N   . THR A 1 230 ? 13.401 -5.695  3.807   1.00 26.50 ? 230 THR A N   1 
ATOM   1718 C CA  . THR A 1 230 ? 12.837 -4.511  3.175   1.00 28.58 ? 230 THR A CA  1 
ATOM   1719 C C   . THR A 1 230 ? 13.939 -3.642  2.583   1.00 27.97 ? 230 THR A C   1 
ATOM   1720 O O   . THR A 1 230 ? 13.804 -3.136  1.462   1.00 24.95 ? 230 THR A O   1 
ATOM   1721 C CB  . THR A 1 230 ? 11.999 -3.714  4.170   1.00 25.37 ? 230 THR A CB  1 
ATOM   1722 O OG1 . THR A 1 230 ? 10.987 -4.560  4.744   1.00 30.81 ? 230 THR A OG1 1 
ATOM   1723 C CG2 . THR A 1 230 ? 11.328 -2.564  3.454   1.00 28.47 ? 230 THR A CG2 1 
ATOM   1724 N N   . LEU A 1 231 ? 15.047 -3.472  3.311   1.00 25.25 ? 231 LEU A N   1 
ATOM   1725 C CA  . LEU A 1 231 ? 16.095 -2.577  2.835   1.00 25.76 ? 231 LEU A CA  1 
ATOM   1726 C C   . LEU A 1 231 ? 16.739 -3.087  1.551   1.00 28.87 ? 231 LEU A C   1 
ATOM   1727 O O   . LEU A 1 231 ? 17.081 -2.289  0.675   1.00 25.85 ? 231 LEU A O   1 
ATOM   1728 C CB  . LEU A 1 231 ? 17.158 -2.374  3.912   1.00 29.54 ? 231 LEU A CB  1 
ATOM   1729 C CG  . LEU A 1 231 ? 16.638 -1.532  5.089   1.00 32.41 ? 231 LEU A CG  1 
ATOM   1730 C CD1 . LEU A 1 231 ? 17.536 -1.615  6.323   1.00 35.69 ? 231 LEU A CD1 1 
ATOM   1731 C CD2 . LEU A 1 231 ? 16.479 -0.098  4.591   1.00 30.95 ? 231 LEU A CD2 1 
ATOM   1732 N N   . GLN A 1 232 ? 16.957 -4.401  1.427   1.00 26.48 ? 232 GLN A N   1 
ATOM   1733 C CA  . GLN A 1 232 ? 17.631 -4.881  0.217   1.00 28.78 ? 232 GLN A CA  1 
ATOM   1734 C C   . GLN A 1 232 ? 16.769 -4.655  -1.019  1.00 30.20 ? 232 GLN A C   1 
ATOM   1735 O O   . GLN A 1 232 ? 17.282 -4.295  -2.096  1.00 25.98 ? 232 GLN A O   1 
ATOM   1736 C CB  . GLN A 1 232 ? 18.030 -6.350  0.378   1.00 26.97 ? 232 GLN A CB  1 
ATOM   1737 C CG  . GLN A 1 232 ? 16.904 -7.360  0.444   1.00 27.59 ? 232 GLN A CG  1 
ATOM   1738 C CD  . GLN A 1 232 ? 17.383 -8.721  0.960   1.00 33.95 ? 232 GLN A CD  1 
ATOM   1739 O OE1 . GLN A 1 232 ? 18.555 -8.887  1.300   1.00 33.99 ? 232 GLN A OE1 1 
ATOM   1740 N NE2 . GLN A 1 232 ? 16.478 -9.689  1.020   1.00 30.31 ? 232 GLN A NE2 1 
ATOM   1741 N N   . ALA A 1 233 ? 15.451 -4.809  -0.874  1.00 23.21 ? 233 ALA A N   1 
ATOM   1742 C CA  . ALA A 1 233 ? 14.547 -4.546  -1.985  1.00 25.06 ? 233 ALA A CA  1 
ATOM   1743 C C   . ALA A 1 233 ? 14.563 -3.069  -2.384  1.00 26.64 ? 233 ALA A C   1 
ATOM   1744 O O   . ALA A 1 233 ? 14.609 -2.738  -3.582  1.00 24.38 ? 233 ALA A O   1 
ATOM   1745 C CB  . ALA A 1 233 ? 13.135 -5.004  -1.619  1.00 23.58 ? 233 ALA A CB  1 
ATOM   1746 N N   . ILE A 1 234 ? 14.522 -2.165  -1.408  1.00 20.76 ? 234 ILE A N   1 
ATOM   1747 C CA  . ILE A 1 234 ? 14.623 -0.740  -1.731  1.00 20.58 ? 234 ILE A CA  1 
ATOM   1748 C C   . ILE A 1 234 ? 15.940 -0.452  -2.445  1.00 21.94 ? 234 ILE A C   1 
ATOM   1749 O O   . ILE A 1 234 ? 15.977 0.291   -3.438  1.00 23.84 ? 234 ILE A O   1 
ATOM   1750 C CB  . ILE A 1 234 ? 14.489 0.120   -0.460  1.00 25.21 ? 234 ILE A CB  1 
ATOM   1751 C CG1 . ILE A 1 234 ? 13.098 -0.045  0.181   1.00 22.13 ? 234 ILE A CG1 1 
ATOM   1752 C CG2 . ILE A 1 234 ? 14.814 1.578   -0.790  1.00 25.11 ? 234 ILE A CG2 1 
ATOM   1753 C CD1 . ILE A 1 234 ? 12.997 0.522   1.637   1.00 25.16 ? 234 ILE A CD1 1 
ATOM   1754 N N   . LYS A 1 235 ? 17.037 -1.029  -1.955  1.00 22.05 ? 235 LYS A N   1 
ATOM   1755 C CA  . LYS A 1 235 ? 18.328 -0.799  -2.604  1.00 25.86 ? 235 LYS A CA  1 
ATOM   1756 C C   . LYS A 1 235 ? 18.310 -1.289  -4.040  1.00 28.55 ? 235 LYS A C   1 
ATOM   1757 O O   . LYS A 1 235 ? 18.886 -0.655  -4.932  1.00 26.51 ? 235 LYS A O   1 
ATOM   1758 C CB  . LYS A 1 235 ? 19.461 -1.495  -1.834  1.00 23.32 ? 235 LYS A CB  1 
ATOM   1759 C CG  . LYS A 1 235 ? 19.759 -0.920  -0.497  1.00 40.29 ? 235 LYS A CG  1 
ATOM   1760 C CD  . LYS A 1 235 ? 21.007 -1.583  0.075   1.00 37.64 ? 235 LYS A CD  1 
ATOM   1761 N N   . PHE A 1 236 ? 17.664 -2.423  -4.287  1.00 22.44 ? 236 PHE A N   1 
ATOM   1762 C CA  . PHE A 1 236 ? 17.579 -2.910  -5.656  1.00 21.52 ? 236 PHE A CA  1 
ATOM   1763 C C   . PHE A 1 236 ? 16.761 -1.965  -6.532  1.00 23.71 ? 236 PHE A C   1 
ATOM   1764 O O   . PHE A 1 236 ? 17.163 -1.644  -7.665  1.00 22.46 ? 236 PHE A O   1 
ATOM   1765 C CB  . PHE A 1 236 ? 16.986 -4.314  -5.698  1.00 20.76 ? 236 PHE A CB  1 
ATOM   1766 C CG  . PHE A 1 236 ? 16.764 -4.807  -7.109  1.00 23.54 ? 236 PHE A CG  1 
ATOM   1767 C CD1 . PHE A 1 236 ? 17.846 -5.139  -7.905  1.00 26.76 ? 236 PHE A CD1 1 
ATOM   1768 C CD2 . PHE A 1 236 ? 15.495 -4.875  -7.637  1.00 22.56 ? 236 PHE A CD2 1 
ATOM   1769 C CE1 . PHE A 1 236 ? 17.661 -5.563  -9.231  1.00 26.01 ? 236 PHE A CE1 1 
ATOM   1770 C CE2 . PHE A 1 236 ? 15.292 -5.315  -8.961  1.00 27.41 ? 236 PHE A CE2 1 
ATOM   1771 C CZ  . PHE A 1 236 ? 16.392 -5.651  -9.749  1.00 23.90 ? 236 PHE A CZ  1 
ATOM   1772 N N   . VAL A 1 237 ? 15.612 -1.509  -6.031  1.00 22.59 ? 237 VAL A N   1 
ATOM   1773 C CA  . VAL A 1 237 ? 14.793 -0.600  -6.830  1.00 21.98 ? 237 VAL A CA  1 
ATOM   1774 C C   . VAL A 1 237 ? 15.567 0.677   -7.127  1.00 24.17 ? 237 VAL A C   1 
ATOM   1775 O O   . VAL A 1 237 ? 15.462 1.246   -8.221  1.00 21.94 ? 237 VAL A O   1 
ATOM   1776 C CB  . VAL A 1 237 ? 13.460 -0.305  -6.123  1.00 21.69 ? 237 VAL A CB  1 
ATOM   1777 C CG1 . VAL A 1 237 ? 12.672 0.745   -6.899  1.00 22.19 ? 237 VAL A CG1 1 
ATOM   1778 C CG2 . VAL A 1 237 ? 12.634 -1.587  -6.023  1.00 23.56 ? 237 VAL A CG2 1 
ATOM   1779 N N   . LEU A 1 238 ? 16.354 1.151   -6.158  1.00 22.56 ? 238 LEU A N   1 
ATOM   1780 C CA  . LEU A 1 238 ? 17.160 2.347   -6.406  1.00 28.59 ? 238 LEU A CA  1 
ATOM   1781 C C   . LEU A 1 238 ? 18.202 2.093   -7.484  1.00 24.08 ? 238 LEU A C   1 
ATOM   1782 O O   . LEU A 1 238 ? 18.470 2.968   -8.325  1.00 22.97 ? 238 LEU A O   1 
ATOM   1783 C CB  . LEU A 1 238 ? 17.825 2.811   -5.109  1.00 24.44 ? 238 LEU A CB  1 
ATOM   1784 C CG  . LEU A 1 238 ? 16.869 3.351   -4.045  1.00 21.78 ? 238 LEU A CG  1 
ATOM   1785 C CD1 . LEU A 1 238 ? 17.627 3.753   -2.762  1.00 23.37 ? 238 LEU A CD1 1 
ATOM   1786 C CD2 . LEU A 1 238 ? 16.080 4.530   -4.605  1.00 26.31 ? 238 LEU A CD2 1 
ATOM   1787 N N   . LYS A 1 239 ? 18.817 0.909   -7.462  1.00 23.67 ? 239 LYS A N   1 
ATOM   1788 C CA  . LYS A 1 239 ? 19.774 0.553   -8.506  1.00 22.84 ? 239 LYS A CA  1 
ATOM   1789 C C   . LYS A 1 239 ? 19.117 0.592   -9.884  1.00 25.77 ? 239 LYS A C   1 
ATOM   1790 O O   . LYS A 1 239 ? 19.692 1.125   -10.843 1.00 24.95 ? 239 LYS A O   1 
ATOM   1791 C CB  . LYS A 1 239 ? 20.357 -0.826  -8.195  1.00 29.32 ? 239 LYS A CB  1 
ATOM   1792 C CG  . LYS A 1 239 ? 21.116 -1.493  -9.326  1.00 33.10 ? 239 LYS A CG  1 
ATOM   1793 C CD  . LYS A 1 239 ? 21.411 -2.942  -8.941  1.00 42.36 ? 239 LYS A CD  1 
ATOM   1794 C CE  . LYS A 1 239 ? 21.747 -3.778  -10.170 1.00 61.28 ? 239 LYS A CE  1 
ATOM   1795 N NZ  . LYS A 1 239 ? 22.931 -3.254  -10.904 1.00 42.35 ? 239 LYS A NZ  1 
ATOM   1796 N N   . GLU A 1 240 ? 17.888 0.077   -9.992  1.00 23.79 ? 240 GLU A N   1 
ATOM   1797 C CA  . GLU A 1 240 ? 17.161 0.135   -11.261 1.00 21.35 ? 240 GLU A CA  1 
ATOM   1798 C C   . GLU A 1 240 ? 16.871 1.574   -11.656 1.00 27.32 ? 240 GLU A C   1 
ATOM   1799 O O   . GLU A 1 240 ? 17.026 1.949   -12.824 1.00 25.05 ? 240 GLU A O   1 
ATOM   1800 C CB  . GLU A 1 240 ? 15.836 -0.613  -11.148 1.00 24.81 ? 240 GLU A CB  1 
ATOM   1801 C CG  . GLU A 1 240 ? 15.922 -2.092  -10.804 1.00 25.06 ? 240 GLU A CG  1 
ATOM   1802 C CD  . GLU A 1 240 ? 14.528 -2.678  -10.708 1.00 35.57 ? 240 GLU A CD  1 
ATOM   1803 O OE1 . GLU A 1 240 ? 13.824 -2.340  -9.727  1.00 28.24 ? 240 GLU A OE1 1 
ATOM   1804 O OE2 . GLU A 1 240 ? 14.122 -3.436  -11.627 1.00 27.65 ? 240 GLU A OE2 1 
ATOM   1805 N N   . MET A 1 241 ? 16.412 2.376   -10.691 1.00 24.46 ? 241 MET A N   1 
ATOM   1806 C CA  . MET A 1 241 ? 16.162 3.789   -10.943 1.00 24.57 ? 241 MET A CA  1 
ATOM   1807 C C   . MET A 1 241 ? 17.402 4.478   -11.498 1.00 28.55 ? 241 MET A C   1 
ATOM   1808 O O   . MET A 1 241 ? 17.313 5.257   -12.454 1.00 26.63 ? 241 MET A O   1 
ATOM   1809 C CB  . MET A 1 241 ? 15.696 4.448   -9.647  1.00 24.82 ? 241 MET A CB  1 
ATOM   1810 C CG  . MET A 1 241 ? 15.150 5.838   -9.779  1.00 37.29 ? 241 MET A CG  1 
ATOM   1811 S SD  . MET A 1 241 ? 14.496 6.427   -8.170  1.00 36.30 ? 241 MET A SD  1 
ATOM   1812 C CE  . MET A 1 241 ? 13.242 5.233   -7.820  1.00 29.79 ? 241 MET A CE  1 
ATOM   1813 N N   . GLY A 1 242 ? 18.572 4.171   -10.938 1.00 26.77 ? 242 GLY A N   1 
ATOM   1814 C CA  . GLY A 1 242 ? 19.805 4.740   -11.455 1.00 31.81 ? 242 GLY A CA  1 
ATOM   1815 C C   . GLY A 1 242 ? 20.074 4.371   -12.901 1.00 26.69 ? 242 GLY A C   1 
ATOM   1816 O O   . GLY A 1 242 ? 20.533 5.211   -13.682 1.00 27.54 ? 242 GLY A O   1 
ATOM   1817 N N   . TYR A 1 243 ? 19.812 3.107   -13.281 1.00 24.73 ? 243 TYR A N   1 
ATOM   1818 C CA  . TYR A 1 243 ? 19.954 2.713   -14.686 1.00 27.29 ? 243 TYR A CA  1 
ATOM   1819 C C   . TYR A 1 243 ? 19.026 3.536   -15.578 1.00 23.89 ? 243 TYR A C   1 
ATOM   1820 O O   . TYR A 1 243 ? 19.443 4.058   -16.620 1.00 24.85 ? 243 TYR A O   1 
ATOM   1821 C CB  . TYR A 1 243 ? 19.685 1.202   -14.887 1.00 27.78 ? 243 TYR A CB  1 
ATOM   1822 C CG  . TYR A 1 243 ? 19.660 0.798   -16.379 1.00 25.60 ? 243 TYR A CG  1 
ATOM   1823 C CD1 . TYR A 1 243 ? 20.822 0.439   -17.051 1.00 36.94 ? 243 TYR A CD1 1 
ATOM   1824 C CD2 . TYR A 1 243 ? 18.475 0.800   -17.107 1.00 26.61 ? 243 TYR A CD2 1 
ATOM   1825 C CE1 . TYR A 1 243 ? 20.808 0.100   -18.439 1.00 33.71 ? 243 TYR A CE1 1 
ATOM   1826 C CE2 . TYR A 1 243 ? 18.446 0.471   -18.483 1.00 30.58 ? 243 TYR A CE2 1 
ATOM   1827 C CZ  . TYR A 1 243 ? 19.618 0.116   -19.143 1.00 35.56 ? 243 TYR A CZ  1 
ATOM   1828 O OH  . TYR A 1 243 ? 19.609 -0.208  -20.507 1.00 29.80 ? 243 TYR A OH  1 
ATOM   1829 N N   . ILE A 1 244 ? 17.759 3.667   -15.177 1.00 23.13 ? 244 ILE A N   1 
ATOM   1830 C CA  . ILE A 1 244 ? 16.773 4.369   -15.993 1.00 21.58 ? 244 ILE A CA  1 
ATOM   1831 C C   . ILE A 1 244 ? 17.086 5.860   -16.064 1.00 22.39 ? 244 ILE A C   1 
ATOM   1832 O O   . ILE A 1 244 ? 16.863 6.496   -17.097 1.00 21.34 ? 244 ILE A O   1 
ATOM   1833 C CB  . ILE A 1 244 ? 15.359 4.108   -15.441 1.00 22.34 ? 244 ILE A CB  1 
ATOM   1834 C CG1 . ILE A 1 244 ? 15.058 2.598   -15.441 1.00 23.28 ? 244 ILE A CG1 1 
ATOM   1835 C CG2 . ILE A 1 244 ? 14.306 4.830   -16.279 1.00 21.05 ? 244 ILE A CG2 1 
ATOM   1836 C CD1 . ILE A 1 244 ? 13.894 2.242   -14.480 1.00 25.95 ? 244 ILE A CD1 1 
ATOM   1837 N N   . ILE A 1 245 ? 17.581 6.446   -14.970 1.00 19.06 ? 245 ILE A N   1 
ATOM   1838 C CA  . ILE A 1 245 ? 18.009 7.850   -15.010 1.00 19.58 ? 245 ILE A CA  1 
ATOM   1839 C C   . ILE A 1 245 ? 19.115 8.029   -16.045 1.00 27.17 ? 245 ILE A C   1 
ATOM   1840 O O   . ILE A 1 245 ? 19.100 8.968   -16.844 1.00 23.63 ? 245 ILE A O   1 
ATOM   1841 C CB  . ILE A 1 245 ? 18.469 8.306   -13.618 1.00 26.02 ? 245 ILE A CB  1 
ATOM   1842 C CG1 . ILE A 1 245 ? 17.264 8.494   -12.699 1.00 22.70 ? 245 ILE A CG1 1 
ATOM   1843 C CG2 . ILE A 1 245 ? 19.312 9.578   -13.710 1.00 22.76 ? 245 ILE A CG2 1 
ATOM   1844 C CD1 . ILE A 1 245 ? 17.680 8.725   -11.220 1.00 21.83 ? 245 ILE A CD1 1 
ATOM   1845 N N   . ASP A 1 246 ? 20.100 7.132   -16.035 1.00 23.77 ? 246 ASP A N   1 
ATOM   1846 C CA  . ASP A 1 246 ? 21.169 7.203   -17.021 1.00 25.04 ? 246 ASP A CA  1 
ATOM   1847 C C   . ASP A 1 246 ? 20.616 7.136   -18.444 1.00 25.30 ? 246 ASP A C   1 
ATOM   1848 O O   . ASP A 1 246 ? 21.058 7.888   -19.320 1.00 25.44 ? 246 ASP A O   1 
ATOM   1849 C CB  . ASP A 1 246 ? 22.177 6.075   -16.789 1.00 25.49 ? 246 ASP A CB  1 
ATOM   1850 C CG  . ASP A 1 246 ? 23.225 6.005   -17.888 1.00 50.69 ? 246 ASP A CG  1 
ATOM   1851 O OD1 . ASP A 1 246 ? 24.152 6.845   -17.873 1.00 57.78 ? 246 ASP A OD1 1 
ATOM   1852 O OD2 . ASP A 1 246 ? 23.113 5.129   -18.780 1.00 46.92 ? 246 ASP A OD2 1 
ATOM   1853 N N   . ARG A 1 247 ? 19.654 6.243   -18.696 1.00 22.78 ? 247 ARG A N   1 
ATOM   1854 C CA  . ARG A 1 247 ? 19.064 6.168   -20.034 1.00 23.52 ? 247 ARG A CA  1 
ATOM   1855 C C   . ARG A 1 247 ? 18.353 7.464   -20.376 1.00 22.23 ? 247 ARG A C   1 
ATOM   1856 O O   . ARG A 1 247 ? 18.444 7.952   -21.508 1.00 24.02 ? 247 ARG A O   1 
ATOM   1857 C CB  . ARG A 1 247 ? 18.072 4.996   -20.152 1.00 20.40 ? 247 ARG A CB  1 
ATOM   1858 C CG  . ARG A 1 247 ? 18.660 3.583   -19.992 1.00 21.16 ? 247 ARG A CG  1 
ATOM   1859 C CD  . ARG A 1 247 ? 19.591 3.226   -21.164 1.00 29.10 ? 247 ARG A CD  1 
ATOM   1860 N NE  . ARG A 1 247 ? 20.891 3.863   -21.029 1.00 35.03 ? 247 ARG A NE  1 
ATOM   1861 C CZ  . ARG A 1 247 ? 21.611 4.328   -22.045 1.00 41.39 ? 247 ARG A CZ  1 
ATOM   1862 N NH1 . ARG A 1 247 ? 21.193 4.228   -23.298 1.00 39.04 ? 247 ARG A NH1 1 
ATOM   1863 N NH2 . ARG A 1 247 ? 22.774 4.921   -21.796 1.00 29.84 ? 247 ARG A NH2 1 
ATOM   1864 N N   . PHE A 1 248 ? 17.618 8.025   -19.416 1.00 20.29 ? 248 PHE A N   1 
ATOM   1865 C CA  . PHE A 1 248 ? 16.912 9.277   -19.673 1.00 22.42 ? 248 PHE A CA  1 
ATOM   1866 C C   . PHE A 1 248 ? 17.899 10.372  -20.060 1.00 24.18 ? 248 PHE A C   1 
ATOM   1867 O O   . PHE A 1 248 ? 17.717 11.065  -21.073 1.00 24.34 ? 248 PHE A O   1 
ATOM   1868 C CB  . PHE A 1 248 ? 16.098 9.679   -18.434 1.00 19.18 ? 248 PHE A CB  1 
ATOM   1869 C CG  . PHE A 1 248 ? 15.131 10.808  -18.673 1.00 22.33 ? 248 PHE A CG  1 
ATOM   1870 C CD1 . PHE A 1 248 ? 15.566 12.127  -18.737 1.00 23.06 ? 248 PHE A CD1 1 
ATOM   1871 C CD2 . PHE A 1 248 ? 13.783 10.550  -18.822 1.00 26.20 ? 248 PHE A CD2 1 
ATOM   1872 C CE1 . PHE A 1 248 ? 14.669 13.167  -18.946 1.00 24.32 ? 248 PHE A CE1 1 
ATOM   1873 C CE2 . PHE A 1 248 ? 12.900 11.582  -19.043 1.00 25.60 ? 248 PHE A CE2 1 
ATOM   1874 C CZ  . PHE A 1 248 ? 13.346 12.888  -19.104 1.00 28.69 ? 248 PHE A CZ  1 
ATOM   1875 N N   . GLU A 1 249 ? 18.967 10.529  -19.261 1.00 22.79 ? 249 GLU A N   1 
ATOM   1876 C CA  . GLU A 1 249 ? 19.979 11.548  -19.547 1.00 22.80 ? 249 GLU A CA  1 
ATOM   1877 C C   . GLU A 1 249 ? 20.617 11.324  -20.914 1.00 25.21 ? 249 GLU A C   1 
ATOM   1878 O O   . GLU A 1 249 ? 20.891 12.284  -21.655 1.00 25.42 ? 249 GLU A O   1 
ATOM   1879 C CB  . GLU A 1 249 ? 21.054 11.541  -18.457 1.00 24.25 ? 249 GLU A CB  1 
ATOM   1880 C CG  . GLU A 1 249 ? 20.559 12.013  -17.109 1.00 26.00 ? 249 GLU A CG  1 
ATOM   1881 C CD  . GLU A 1 249 ? 21.635 11.898  -16.036 1.00 40.81 ? 249 GLU A CD  1 
ATOM   1882 O OE1 . GLU A 1 249 ? 22.402 10.902  -16.046 1.00 43.28 ? 249 GLU A OE1 1 
ATOM   1883 O OE2 . GLU A 1 249 ? 21.717 12.802  -15.192 1.00 42.19 ? 249 GLU A OE2 1 
ATOM   1884 N N   . TYR A 1 250 ? 20.867 10.062  -21.258 1.00 21.77 ? 250 TYR A N   1 
ATOM   1885 C CA  . TYR A 1 250 ? 21.483 9.747   -22.543 1.00 24.96 ? 250 TYR A CA  1 
ATOM   1886 C C   . TYR A 1 250 ? 20.589 10.170  -23.708 1.00 24.16 ? 250 TYR A C   1 
ATOM   1887 O O   . TYR A 1 250 ? 21.048 10.788  -24.675 1.00 21.41 ? 250 TYR A O   1 
ATOM   1888 C CB  . TYR A 1 250 ? 21.783 8.251   -22.630 1.00 26.16 ? 250 TYR A CB  1 
ATOM   1889 C CG  . TYR A 1 250 ? 22.222 7.867   -24.029 1.00 28.36 ? 250 TYR A CG  1 
ATOM   1890 C CD1 . TYR A 1 250 ? 23.554 7.984   -24.408 1.00 33.03 ? 250 TYR A CD1 1 
ATOM   1891 C CD2 . TYR A 1 250 ? 21.301 7.414   -24.969 1.00 30.64 ? 250 TYR A CD2 1 
ATOM   1892 C CE1 . TYR A 1 250 ? 23.961 7.645   -25.690 1.00 37.09 ? 250 TYR A CE1 1 
ATOM   1893 C CE2 . TYR A 1 250 ? 21.689 7.088   -26.260 1.00 32.94 ? 250 TYR A CE2 1 
ATOM   1894 C CZ  . TYR A 1 250 ? 23.026 7.199   -26.612 1.00 49.51 ? 250 TYR A CZ  1 
ATOM   1895 O OH  . TYR A 1 250 ? 23.424 6.868   -27.891 1.00 56.95 ? 250 TYR A OH  1 
ATOM   1896 N N   . HIS A 1 251 ? 19.312 9.802   -23.653 1.00 21.84 ? 251 HIS A N   1 
ATOM   1897 C CA  . HIS A 1 251 ? 18.408 10.136  -24.749 1.00 23.67 ? 251 HIS A CA  1 
ATOM   1898 C C   . HIS A 1 251 ? 18.085 11.623  -24.779 1.00 27.27 ? 251 HIS A C   1 
ATOM   1899 O O   . HIS A 1 251 ? 17.836 12.187  -25.862 1.00 24.48 ? 251 HIS A O   1 
ATOM   1900 C CB  . HIS A 1 251 ? 17.145 9.288   -24.640 1.00 19.72 ? 251 HIS A CB  1 
ATOM   1901 C CG  . HIS A 1 251 ? 17.348 7.882   -25.104 1.00 22.08 ? 251 HIS A CG  1 
ATOM   1902 N ND1 . HIS A 1 251 ? 17.388 7.549   -26.441 1.00 21.52 ? 251 HIS A ND1 1 
ATOM   1903 C CD2 . HIS A 1 251 ? 17.587 6.735   -24.421 1.00 20.02 ? 251 HIS A CD2 1 
ATOM   1904 C CE1 . HIS A 1 251 ? 17.622 6.251   -26.564 1.00 25.82 ? 251 HIS A CE1 1 
ATOM   1905 N NE2 . HIS A 1 251 ? 17.748 5.733   -25.353 1.00 21.47 ? 251 HIS A NE2 1 
ATOM   1906 N N   . LEU A 1 252 ? 18.101 12.278  -23.613 1.00 20.79 ? 252 LEU A N   1 
ATOM   1907 C CA  . LEU A 1 252 ? 17.861 13.720  -23.560 1.00 24.10 ? 252 LEU A CA  1 
ATOM   1908 C C   . LEU A 1 252 ? 19.021 14.489  -24.186 1.00 25.22 ? 252 LEU A C   1 
ATOM   1909 O O   . LEU A 1 252 ? 18.808 15.453  -24.937 1.00 25.80 ? 252 LEU A O   1 
ATOM   1910 C CB  . LEU A 1 252 ? 17.635 14.162  -22.108 1.00 22.51 ? 252 LEU A CB  1 
ATOM   1911 C CG  . LEU A 1 252 ? 17.292 15.647  -21.922 1.00 30.69 ? 252 LEU A CG  1 
ATOM   1912 C CD1 . LEU A 1 252 ? 16.016 15.982  -22.674 1.00 26.51 ? 252 LEU A CD1 1 
ATOM   1913 C CD2 . LEU A 1 252 ? 17.170 16.005  -20.433 1.00 32.90 ? 252 LEU A CD2 1 
ATOM   1914 N N   . GLN A 1 253 ? 20.258 14.078  -23.891 1.00 23.43 ? 253 GLN A N   1 
ATOM   1915 C CA  . GLN A 1 253 ? 21.416 14.720  -24.507 1.00 23.94 ? 253 GLN A CA  1 
ATOM   1916 C C   . GLN A 1 253 ? 21.403 14.507  -26.023 1.00 26.55 ? 253 GLN A C   1 
ATOM   1917 O O   . GLN A 1 253 ? 21.764 15.406  -26.792 1.00 25.91 ? 253 GLN A O   1 
ATOM   1918 C CB  . GLN A 1 253 ? 22.695 14.172  -23.857 1.00 30.52 ? 253 GLN A CB  1 
ATOM   1919 C CG  . GLN A 1 253 ? 23.959 14.124  -24.726 1.00 47.22 ? 253 GLN A CG  1 
ATOM   1920 C CD  . GLN A 1 253 ? 23.970 12.983  -25.763 1.00 59.91 ? 253 GLN A CD  1 
ATOM   1921 O OE1 . GLN A 1 253 ? 23.675 11.792  -25.473 1.00 39.30 ? 253 GLN A OE1 1 
ATOM   1922 N NE2 . GLN A 1 253 ? 24.297 13.355  -26.991 1.00 52.80 ? 253 GLN A NE2 1 
ATOM   1923 N N   . LYS A 1 254 ? 20.966 13.326  -26.467 1.00 22.81 ? 254 LYS A N   1 
ATOM   1924 C CA  . LYS A 1 254 ? 20.939 13.021  -27.891 1.00 26.65 ? 254 LYS A CA  1 
ATOM   1925 C C   . LYS A 1 254 ? 19.930 13.891  -28.626 1.00 28.85 ? 254 LYS A C   1 
ATOM   1926 O O   . LYS A 1 254 ? 20.208 14.387  -29.730 1.00 24.73 ? 254 LYS A O   1 
ATOM   1927 C CB  . LYS A 1 254 ? 20.618 11.542  -28.088 1.00 29.51 ? 254 LYS A CB  1 
ATOM   1928 C CG  . LYS A 1 254 ? 20.814 11.046  -29.493 1.00 34.20 ? 254 LYS A CG  1 
ATOM   1929 C CD  . LYS A 1 254 ? 20.693 9.521   -29.538 1.00 37.26 ? 254 LYS A CD  1 
ATOM   1930 C CE  . LYS A 1 254 ? 20.994 8.987   -30.927 1.00 40.70 ? 254 LYS A CE  1 
ATOM   1931 N NZ  . LYS A 1 254 ? 20.990 7.507   -30.939 1.00 50.38 ? 254 LYS A NZ  1 
ATOM   1932 N N   . VAL A 1 255 ? 18.750 14.097  -28.041 1.00 22.50 ? 255 VAL A N   1 
ATOM   1933 C CA  . VAL A 1 255 ? 17.789 14.924  -28.762 1.00 32.94 ? 255 VAL A CA  1 
ATOM   1934 C C   . VAL A 1 255 ? 18.170 16.403  -28.677 1.00 27.57 ? 255 VAL A C   1 
ATOM   1935 O O   . VAL A 1 255 ? 17.963 17.149  -29.643 1.00 28.63 ? 255 VAL A O   1 
ATOM   1936 C CB  . VAL A 1 255 ? 16.353 14.662  -28.277 1.00 34.70 ? 255 VAL A CB  1 
ATOM   1937 C CG1 . VAL A 1 255 ? 16.169 15.060  -26.827 1.00 28.86 ? 255 VAL A CG1 1 
ATOM   1938 C CG2 . VAL A 1 255 ? 15.351 15.382  -29.199 1.00 33.30 ? 255 VAL A CG2 1 
ATOM   1939 N N   . LYS A 1 256 ? 18.749 16.853  -27.557 1.00 25.02 ? 256 LYS A N   1 
ATOM   1940 C CA  . LYS A 1 256 ? 19.216 18.239  -27.495 1.00 26.95 ? 256 LYS A CA  1 
ATOM   1941 C C   . LYS A 1 256 ? 20.286 18.486  -28.552 1.00 27.72 ? 256 LYS A C   1 
ATOM   1942 O O   . LYS A 1 256 ? 20.309 19.542  -29.202 1.00 26.24 ? 256 LYS A O   1 
ATOM   1943 C CB  . LYS A 1 256 ? 19.760 18.554  -26.104 1.00 29.71 ? 256 LYS A CB  1 
ATOM   1944 C CG  . LYS A 1 256 ? 18.679 18.772  -25.035 1.00 33.74 ? 256 LYS A CG  1 
ATOM   1945 C CD  . LYS A 1 256 ? 19.297 19.350  -23.770 1.00 41.31 ? 256 LYS A CD  1 
ATOM   1946 C CE  . LYS A 1 256 ? 18.315 19.360  -22.610 1.00 37.88 ? 256 LYS A CE  1 
ATOM   1947 N NZ  . LYS A 1 256 ? 19.047 19.591  -21.344 1.00 41.55 ? 256 LYS A NZ  1 
ATOM   1948 N N   . HIS A 1 257 ? 21.183 17.519  -28.734 1.00 24.99 ? 257 HIS A N   1 
ATOM   1949 C CA  . HIS A 1 257 ? 22.202 17.662  -29.766 1.00 28.51 ? 257 HIS A CA  1 
ATOM   1950 C C   . HIS A 1 257 ? 21.565 17.761  -31.148 1.00 25.34 ? 257 HIS A C   1 
ATOM   1951 O O   . HIS A 1 257 ? 21.978 18.587  -31.974 1.00 24.33 ? 257 HIS A O   1 
ATOM   1952 C CB  . HIS A 1 257 ? 23.174 16.484  -29.708 1.00 28.45 ? 257 HIS A CB  1 
ATOM   1953 C CG  . HIS A 1 257 ? 24.282 16.580  -30.709 1.00 31.44 ? 257 HIS A CG  1 
ATOM   1954 N ND1 . HIS A 1 257 ? 25.410 17.338  -30.489 1.00 35.13 ? 257 HIS A ND1 1 
ATOM   1955 C CD2 . HIS A 1 257 ? 24.423 16.037  -31.943 1.00 29.56 ? 257 HIS A CD2 1 
ATOM   1956 C CE1 . HIS A 1 257 ? 26.209 17.247  -31.539 1.00 35.39 ? 257 HIS A CE1 1 
ATOM   1957 N NE2 . HIS A 1 257 ? 25.635 16.461  -32.433 1.00 26.81 ? 257 HIS A NE2 1 
ATOM   1958 N N   . ALA A 1 258 ? 20.554 16.926  -31.419 1.00 23.01 ? 258 ALA A N   1 
ATOM   1959 C CA  . ALA A 1 258 ? 19.898 16.952  -32.726 1.00 22.26 ? 258 ALA A CA  1 
ATOM   1960 C C   . ALA A 1 258 ? 19.217 18.289  -32.975 1.00 27.21 ? 258 ALA A C   1 
ATOM   1961 O O   . ALA A 1 258 ? 19.313 18.850  -34.077 1.00 27.80 ? 258 ALA A O   1 
ATOM   1962 C CB  . ALA A 1 258 ? 18.882 15.815  -32.838 1.00 22.35 ? 258 ALA A CB  1 
ATOM   1963 N N   . ILE A 1 259 ? 18.511 18.808  -31.966 1.00 23.61 ? 259 ILE A N   1 
ATOM   1964 C CA  . ILE A 1 259 ? 17.863 20.117  -32.100 1.00 23.19 ? 259 ILE A CA  1 
ATOM   1965 C C   . ILE A 1 259 ? 18.903 21.210  -32.302 1.00 23.12 ? 259 ILE A C   1 
ATOM   1966 O O   . ILE A 1 259 ? 18.742 22.097  -33.154 1.00 25.96 ? 259 ILE A O   1 
ATOM   1967 C CB  . ILE A 1 259 ? 16.975 20.388  -30.863 1.00 27.54 ? 259 ILE A CB  1 
ATOM   1968 C CG1 . ILE A 1 259 ? 15.802 19.396  -30.843 1.00 24.22 ? 259 ILE A CG1 1 
ATOM   1969 C CG2 . ILE A 1 259 ? 16.466 21.854  -30.847 1.00 30.25 ? 259 ILE A CG2 1 
ATOM   1970 C CD1 . ILE A 1 259 ? 14.994 19.447  -29.564 1.00 29.36 ? 259 ILE A CD1 1 
ATOM   1971 N N   . ASP A 1 260 ? 19.987 21.174  -31.522 1.00 24.83 ? 260 ASP A N   1 
ATOM   1972 C CA  . ASP A 1 260 ? 21.034 22.188  -31.662 1.00 26.37 ? 260 ASP A CA  1 
ATOM   1973 C C   . ASP A 1 260 ? 21.633 22.192  -33.068 1.00 26.38 ? 260 ASP A C   1 
ATOM   1974 O O   . ASP A 1 260 ? 21.959 23.257  -33.619 1.00 27.24 ? 260 ASP A O   1 
ATOM   1975 C CB  . ASP A 1 260 ? 22.139 21.948  -30.635 1.00 30.46 ? 260 ASP A CB  1 
ATOM   1976 C CG  . ASP A 1 260 ? 21.704 22.254  -29.218 1.00 44.07 ? 260 ASP A CG  1 
ATOM   1977 O OD1 . ASP A 1 260 ? 20.608 22.831  -29.037 1.00 46.19 ? 260 ASP A OD1 1 
ATOM   1978 O OD2 . ASP A 1 260 ? 22.469 21.917  -28.282 1.00 43.57 ? 260 ASP A OD2 1 
ATOM   1979 N N   . GLN A 1 261 ? 21.819 21.012  -33.654 1.00 25.60 ? 261 GLN A N   1 
ATOM   1980 C CA  . GLN A 1 261 ? 22.440 20.944  -34.973 1.00 25.37 ? 261 GLN A CA  1 
ATOM   1981 C C   . GLN A 1 261 ? 21.528 21.548  -36.033 1.00 27.81 ? 261 GLN A C   1 
ATOM   1982 O O   . GLN A 1 261 ? 21.968 22.363  -36.852 1.00 27.49 ? 261 GLN A O   1 
ATOM   1983 C CB  . GLN A 1 261 ? 22.791 19.487  -35.304 1.00 27.95 ? 261 GLN A CB  1 
ATOM   1984 C CG  . GLN A 1 261 ? 23.931 18.958  -34.405 1.00 25.67 ? 261 GLN A CG  1 
ATOM   1985 C CD  . GLN A 1 261 ? 25.270 19.553  -34.814 1.00 36.17 ? 261 GLN A CD  1 
ATOM   1986 O OE1 . GLN A 1 261 ? 25.597 19.567  -35.988 1.00 38.55 ? 261 GLN A OE1 1 
ATOM   1987 N NE2 . GLN A 1 261 ? 26.029 20.065  -33.857 1.00 43.83 ? 261 GLN A NE2 1 
ATOM   1988 N N   . ILE A 1 262 ? 20.252 21.150  -36.041 1.00 24.22 ? 262 ILE A N   1 
ATOM   1989 C CA  . ILE A 1 262 ? 19.311 21.719  -37.007 1.00 24.26 ? 262 ILE A CA  1 
ATOM   1990 C C   . ILE A 1 262 ? 19.078 23.207  -36.730 1.00 25.75 ? 262 ILE A C   1 
ATOM   1991 O O   . ILE A 1 262 ? 18.927 24.008  -37.663 1.00 27.20 ? 262 ILE A O   1 
ATOM   1992 C CB  . ILE A 1 262 ? 17.998 20.903  -37.014 1.00 25.15 ? 262 ILE A CB  1 
ATOM   1993 C CG1 . ILE A 1 262 ? 18.240 19.552  -37.716 1.00 29.19 ? 262 ILE A CG1 1 
ATOM   1994 C CG2 . ILE A 1 262 ? 16.883 21.675  -37.726 1.00 30.41 ? 262 ILE A CG2 1 
ATOM   1995 C CD1 . ILE A 1 262 ? 17.113 18.545  -37.572 1.00 24.51 ? 262 ILE A CD1 1 
ATOM   1996 N N   . THR A 1 263 ? 19.086 23.619  -35.455 1.00 28.49 ? 263 THR A N   1 
ATOM   1997 C CA  . THR A 1 263 ? 18.921 25.045  -35.166 1.00 29.24 ? 263 THR A CA  1 
ATOM   1998 C C   . THR A 1 263 ? 20.105 25.854  -35.691 1.00 29.97 ? 263 THR A C   1 
ATOM   1999 O O   . THR A 1 263 ? 19.945 26.996  -36.149 1.00 29.27 ? 263 THR A O   1 
ATOM   2000 C CB  . THR A 1 263 ? 18.743 25.261  -33.667 1.00 31.84 ? 263 THR A CB  1 
ATOM   2001 O OG1 . THR A 1 263 ? 17.570 24.561  -33.235 1.00 30.55 ? 263 THR A OG1 1 
ATOM   2002 C CG2 . THR A 1 263 ? 18.604 26.770  -33.334 1.00 33.57 ? 263 THR A CG2 1 
ATOM   2003 N N   . ALA A 1 264 ? 21.311 25.286  -35.613 1.00 30.46 ? 264 ALA A N   1 
ATOM   2004 C CA  . ALA A 1 264 ? 22.486 26.001  -36.099 1.00 31.25 ? 264 ALA A CA  1 
ATOM   2005 C C   . ALA A 1 264 ? 22.442 26.157  -37.610 1.00 30.52 ? 264 ALA A C   1 
ATOM   2006 O O   . ALA A 1 264 ? 22.909 27.172  -38.141 1.00 33.06 ? 264 ALA A O   1 
ATOM   2007 C CB  . ALA A 1 264 ? 23.759 25.276  -35.664 1.00 32.29 ? 264 ALA A CB  1 
ATOM   2008 N N   . ILE A 1 265 ? 21.874 25.179  -38.317 1.00 28.02 ? 265 ILE A N   1 
ATOM   2009 C CA  . ILE A 1 265 ? 21.679 25.332  -39.760 1.00 30.34 ? 265 ILE A CA  1 
ATOM   2010 C C   . ILE A 1 265 ? 20.753 26.504  -40.036 1.00 30.12 ? 265 ILE A C   1 
ATOM   2011 O O   . ILE A 1 265 ? 21.043 27.367  -40.871 1.00 31.02 ? 265 ILE A O   1 
ATOM   2012 C CB  . ILE A 1 265 ? 21.118 24.040  -40.380 1.00 30.64 ? 265 ILE A CB  1 
ATOM   2013 C CG1 . ILE A 1 265 ? 22.142 22.912  -40.301 1.00 31.33 ? 265 ILE A CG1 1 
ATOM   2014 C CG2 . ILE A 1 265 ? 20.696 24.295  -41.822 1.00 29.51 ? 265 ILE A CG2 1 
ATOM   2015 C CD1 . ILE A 1 265 ? 21.581 21.539  -40.708 1.00 34.14 ? 265 ILE A CD1 1 
ATOM   2016 N N   . ALA A 1 266 ? 19.618 26.542  -39.336 1.00 33.56 ? 266 ALA A N   1 
ATOM   2017 C CA  . ALA A 1 266 ? 18.666 27.640  -39.500 1.00 33.85 ? 266 ALA A CA  1 
ATOM   2018 C C   . ALA A 1 266 ? 19.292 28.991  -39.171 1.00 30.85 ? 266 ALA A C   1 
ATOM   2019 O O   . ALA A 1 266 ? 18.933 30.012  -39.771 1.00 35.38 ? 266 ALA A O   1 
ATOM   2020 C CB  . ALA A 1 266 ? 17.446 27.386  -38.610 1.00 34.71 ? 266 ALA A CB  1 
ATOM   2021 N N   . ASP A 1 267 ? 20.201 29.029  -38.193 1.00 31.24 ? 267 ASP A N   1 
ATOM   2022 C CA  . ASP A 1 267 ? 20.836 30.285  -37.797 1.00 33.39 ? 267 ASP A CA  1 
ATOM   2023 C C   . ASP A 1 267 ? 22.061 30.624  -38.638 1.00 36.10 ? 267 ASP A C   1 
ATOM   2024 O O   . ASP A 1 267 ? 22.610 31.721  -38.494 1.00 38.28 ? 267 ASP A O   1 
ATOM   2025 C CB  . ASP A 1 267 ? 21.240 30.238  -36.314 1.00 34.16 ? 267 ASP A CB  1 
ATOM   2026 C CG  . ASP A 1 267 ? 20.046 30.387  -35.365 1.00 46.21 ? 267 ASP A CG  1 
ATOM   2027 O OD1 . ASP A 1 267 ? 19.006 30.936  -35.790 1.00 45.32 ? 267 ASP A OD1 1 
ATOM   2028 O OD2 . ASP A 1 267 ? 20.154 29.960  -34.189 1.00 39.45 ? 267 ASP A OD2 1 
ATOM   2029 N N   . GLY A 1 268 ? 22.508 29.715  -39.502 1.00 33.90 ? 268 GLY A N   1 
ATOM   2030 C CA  . GLY A 1 268 ? 23.697 29.923  -40.299 1.00 38.12 ? 268 GLY A CA  1 
ATOM   2031 C C   . GLY A 1 268 ? 23.394 30.454  -41.690 1.00 42.53 ? 268 GLY A C   1 
ATOM   2032 O O   . GLY A 1 268 ? 22.286 30.903  -41.995 1.00 39.24 ? 268 GLY A O   1 
ATOM   2033 N N   . VAL A 1 269 ? 24.420 30.392  -42.550 1.00 39.56 ? 269 VAL A N   1 
ATOM   2034 C CA  . VAL A 1 269 ? 24.285 30.894  -43.914 1.00 40.41 ? 269 VAL A CA  1 
ATOM   2035 C C   . VAL A 1 269 ? 23.244 30.074  -44.662 1.00 37.69 ? 269 VAL A C   1 
ATOM   2036 O O   . VAL A 1 269 ? 23.333 28.842  -44.745 1.00 37.05 ? 269 VAL A O   1 
ATOM   2037 C CB  . VAL A 1 269 ? 25.637 30.868  -44.648 1.00 45.84 ? 269 VAL A CB  1 
ATOM   2038 C CG1 . VAL A 1 269 ? 25.460 31.306  -46.116 1.00 44.77 ? 269 VAL A CG1 1 
ATOM   2039 C CG2 . VAL A 1 269 ? 26.647 31.762  -43.953 1.00 41.75 ? 269 VAL A CG2 1 
ATOM   2040 N N   . LYS A 1 270 ? 22.261 30.759  -45.227 1.00 39.19 ? 270 LYS A N   1 
ATOM   2041 C CA  . LYS A 1 270 ? 21.234 30.085  -46.004 1.00 38.16 ? 270 LYS A CA  1 
ATOM   2042 C C   . LYS A 1 270 ? 21.785 29.728  -47.391 1.00 31.89 ? 270 LYS A C   1 
ATOM   2043 O O   . LYS A 1 270 ? 22.211 30.625  -48.119 1.00 33.26 ? 270 LYS A O   1 
ATOM   2044 C CB  . LYS A 1 270 ? 20.006 30.965  -46.140 1.00 43.19 ? 270 LYS A CB  1 
ATOM   2045 C CG  . LYS A 1 270 ? 18.878 30.349  -46.946 1.00 41.56 ? 270 LYS A CG  1 
ATOM   2046 C CD  . LYS A 1 270 ? 17.801 31.388  -47.175 1.00 53.11 ? 270 LYS A CD  1 
ATOM   2047 C CE  . LYS A 1 270 ? 16.528 30.785  -47.718 1.00 55.52 ? 270 LYS A CE  1 
ATOM   2048 N NZ  . LYS A 1 270 ? 15.499 31.841  -47.960 1.00 66.35 ? 270 LYS A NZ  1 
ATOM   2049 N N   . PRO A 1 271 ? 21.773 28.461  -47.767 1.00 32.84 ? 271 PRO A N   1 
ATOM   2050 C CA  . PRO A 1 271 ? 22.346 28.085  -49.069 1.00 35.28 ? 271 PRO A CA  1 
ATOM   2051 C C   . PRO A 1 271 ? 21.492 28.583  -50.221 1.00 38.09 ? 271 PRO A C   1 
ATOM   2052 O O   . PRO A 1 271 ? 20.296 28.849  -50.092 1.00 36.20 ? 271 PRO A O   1 
ATOM   2053 C CB  . PRO A 1 271 ? 22.362 26.550  -49.016 1.00 32.97 ? 271 PRO A CB  1 
ATOM   2054 C CG  . PRO A 1 271 ? 21.283 26.186  -48.034 1.00 34.06 ? 271 PRO A CG  1 
ATOM   2055 C CD  . PRO A 1 271 ? 21.293 27.306  -47.004 1.00 28.65 ? 271 PRO A CD  1 
ATOM   2056 N N   . LYS A 1 272 ? 22.150 28.735  -51.365 1.00 32.00 ? 272 LYS A N   1 
ATOM   2057 C CA  . LYS A 1 272 ? 21.489 28.973  -52.643 1.00 31.31 ? 272 LYS A CA  1 
ATOM   2058 C C   . LYS A 1 272 ? 21.471 27.655  -53.414 1.00 29.90 ? 272 LYS A C   1 
ATOM   2059 O O   . LYS A 1 272 ? 21.000 26.656  -52.861 1.00 34.72 ? 272 LYS A O   1 
ATOM   2060 C CB  . LYS A 1 272 ? 22.152 30.159  -53.339 1.00 33.05 ? 272 LYS A CB  1 
ATOM   2061 C CG  . LYS A 1 272 ? 22.028 31.467  -52.544 1.00 39.70 ? 272 LYS A CG  1 
ATOM   2062 C CD  . LYS A 1 272 ? 22.575 32.652  -53.321 1.00 49.34 ? 272 LYS A CD  1 
ATOM   2063 N N   . GLN A 1 273 ? 21.962 27.584  -54.650 1.00 31.89 ? 273 GLN A N   1 
ATOM   2064 C CA  . GLN A 1 273 ? 22.054 26.306  -55.329 1.00 33.02 ? 273 GLN A CA  1 
ATOM   2065 C C   . GLN A 1 273 ? 23.357 25.604  -54.953 1.00 32.18 ? 273 GLN A C   1 
ATOM   2066 O O   . GLN A 1 273 ? 24.381 26.241  -54.670 1.00 31.55 ? 273 GLN A O   1 
ATOM   2067 C CB  . GLN A 1 273 ? 21.961 26.501  -56.845 1.00 35.98 ? 273 GLN A CB  1 
ATOM   2068 C CG  . GLN A 1 273 ? 20.663 27.173  -57.271 1.00 35.99 ? 273 GLN A CG  1 
ATOM   2069 C CD  . GLN A 1 273 ? 20.453 27.140  -58.780 1.00 61.67 ? 273 GLN A CD  1 
ATOM   2070 O OE1 . GLN A 1 273 ? 21.335 27.518  -59.550 1.00 59.98 ? 273 GLN A OE1 1 
ATOM   2071 N NE2 . GLN A 1 273 ? 19.280 26.675  -59.207 1.00 64.93 ? 273 GLN A NE2 1 
ATOM   2072 N N   . VAL A 1 274 ? 23.309 24.277  -54.954 1.00 27.40 ? 274 VAL A N   1 
ATOM   2073 C CA  . VAL A 1 274 ? 24.434 23.434  -54.553 1.00 28.25 ? 274 VAL A CA  1 
ATOM   2074 C C   . VAL A 1 274 ? 24.547 22.292  -55.554 1.00 27.75 ? 274 VAL A C   1 
ATOM   2075 O O   . VAL A 1 274 ? 23.668 22.096  -56.397 1.00 29.02 ? 274 VAL A O   1 
ATOM   2076 C CB  . VAL A 1 274 ? 24.267 22.875  -53.125 1.00 29.18 ? 274 VAL A CB  1 
ATOM   2077 C CG1 . VAL A 1 274 ? 24.234 24.014  -52.104 1.00 26.83 ? 274 VAL A CG1 1 
ATOM   2078 C CG2 . VAL A 1 274 ? 23.008 22.015  -53.054 1.00 24.98 ? 274 VAL A CG2 1 
ATOM   2079 N N   . THR A 1 275 ? 25.644 21.534  -55.456 1.00 26.43 ? 275 THR A N   1 
ATOM   2080 C CA  . THR A 1 275 ? 25.787 20.371  -56.317 1.00 26.07 ? 275 THR A CA  1 
ATOM   2081 C C   . THR A 1 275 ? 24.853 19.255  -55.845 1.00 25.95 ? 275 THR A C   1 
ATOM   2082 O O   . THR A 1 275 ? 24.386 19.223  -54.695 1.00 24.25 ? 275 THR A O   1 
ATOM   2083 C CB  . THR A 1 275 ? 27.216 19.822  -56.317 1.00 26.89 ? 275 THR A CB  1 
ATOM   2084 O OG1 . THR A 1 275 ? 27.532 19.348  -55.002 1.00 26.90 ? 275 THR A OG1 1 
ATOM   2085 C CG2 . THR A 1 275 ? 28.232 20.892  -56.714 1.00 27.95 ? 275 THR A CG2 1 
ATOM   2086 N N   . LYS A 1 276 ? 24.624 18.300  -56.746 1.00 25.55 ? 276 LYS A N   1 
ATOM   2087 C CA  . LYS A 1 276 ? 23.805 17.151  -56.391 1.00 31.13 ? 276 LYS A CA  1 
ATOM   2088 C C   . LYS A 1 276 ? 24.414 16.381  -55.222 1.00 26.44 ? 276 LYS A C   1 
ATOM   2089 O O   . LYS A 1 276 ? 23.692 15.924  -54.323 1.00 23.17 ? 276 LYS A O   1 
ATOM   2090 C CB  . LYS A 1 276 ? 23.618 16.257  -57.617 1.00 26.56 ? 276 LYS A CB  1 
ATOM   2091 C CG  . LYS A 1 276 ? 22.737 15.046  -57.322 1.00 31.66 ? 276 LYS A CG  1 
ATOM   2092 C CD  . LYS A 1 276 ? 22.056 14.567  -58.599 1.00 36.02 ? 276 LYS A CD  1 
ATOM   2093 C CE  . LYS A 1 276 ? 23.056 14.218  -59.671 1.00 30.16 ? 276 LYS A CE  1 
ATOM   2094 N NZ  . LYS A 1 276 ? 22.381 14.050  -61.012 1.00 32.14 ? 276 LYS A NZ  1 
ATOM   2095 N N   . ASN A 1 277 ? 25.743 16.253  -55.189 1.00 23.90 ? 277 ASN A N   1 
ATOM   2096 C CA  . ASN A 1 277 ? 26.368 15.543  -54.074 1.00 23.58 ? 277 ASN A CA  1 
ATOM   2097 C C   . ASN A 1 277 ? 26.118 16.272  -52.755 1.00 24.14 ? 277 ASN A C   1 
ATOM   2098 O O   . ASN A 1 277 ? 25.856 15.636  -51.725 1.00 22.88 ? 277 ASN A O   1 
ATOM   2099 C CB  . ASN A 1 277 ? 27.872 15.381  -54.320 1.00 24.59 ? 277 ASN A CB  1 
ATOM   2100 C CG  . ASN A 1 277 ? 28.193 14.225  -55.267 1.00 29.87 ? 277 ASN A CG  1 
ATOM   2101 O OD1 . ASN A 1 277 ? 27.428 13.263  -55.380 1.00 36.57 ? 277 ASN A OD1 1 
ATOM   2102 N ND2 . ASN A 1 277 ? 29.332 14.310  -55.933 1.00 27.69 ? 277 ASN A ND2 1 
ATOM   2103 N N   . GLU A 1 278 ? 26.169 17.611  -52.772 1.00 23.75 ? 278 GLU A N   1 
ATOM   2104 C CA  . GLU A 1 278 ? 25.871 18.382  -51.566 1.00 24.78 ? 278 GLU A CA  1 
ATOM   2105 C C   . GLU A 1 278 ? 24.436 18.176  -51.122 1.00 23.02 ? 278 GLU A C   1 
ATOM   2106 O O   . GLU A 1 278 ? 24.161 18.043  -49.924 1.00 24.10 ? 278 GLU A O   1 
ATOM   2107 C CB  . GLU A 1 278 ? 26.106 19.868  -51.807 1.00 26.07 ? 278 GLU A CB  1 
ATOM   2108 C CG  . GLU A 1 278 ? 27.533 20.295  -51.772 1.00 28.83 ? 278 GLU A CG  1 
ATOM   2109 C CD  . GLU A 1 278 ? 27.678 21.727  -52.225 1.00 27.74 ? 278 GLU A CD  1 
ATOM   2110 O OE1 . GLU A 1 278 ? 27.593 22.659  -51.382 1.00 29.94 ? 278 GLU A OE1 1 
ATOM   2111 O OE2 . GLU A 1 278 ? 27.852 21.909  -53.438 1.00 27.42 ? 278 GLU A OE2 1 
ATOM   2112 N N   . LEU A 1 279 ? 23.501 18.171  -52.073 1.00 22.69 ? 279 LEU A N   1 
ATOM   2113 C CA  . LEU A 1 279 ? 22.094 18.042  -51.703 1.00 23.56 ? 279 LEU A CA  1 
ATOM   2114 C C   . LEU A 1 279 ? 21.814 16.681  -51.081 1.00 23.50 ? 279 LEU A C   1 
ATOM   2115 O O   . LEU A 1 279 ? 21.018 16.580  -50.142 1.00 21.71 ? 279 LEU A O   1 
ATOM   2116 C CB  . LEU A 1 279 ? 21.188 18.286  -52.922 1.00 22.74 ? 279 LEU A CB  1 
ATOM   2117 C CG  . LEU A 1 279 ? 19.673 18.285  -52.636 1.00 27.04 ? 279 LEU A CG  1 
ATOM   2118 C CD1 . LEU A 1 279 ? 19.293 19.383  -51.604 1.00 27.78 ? 279 LEU A CD1 1 
ATOM   2119 C CD2 . LEU A 1 279 ? 18.848 18.437  -53.905 1.00 28.99 ? 279 LEU A CD2 1 
ATOM   2120 N N   . LYS A 1 280 ? 22.430 15.615  -51.606 1.00 23.66 ? 280 LYS A N   1 
ATOM   2121 C CA  . LYS A 1 280 ? 22.313 14.327  -50.930 1.00 24.44 ? 280 LYS A CA  1 
ATOM   2122 C C   . LYS A 1 280 ? 22.694 14.457  -49.469 1.00 27.34 ? 280 LYS A C   1 
ATOM   2123 O O   . LYS A 1 280 ? 21.958 14.013  -48.578 1.00 25.09 ? 280 LYS A O   1 
ATOM   2124 C CB  . LYS A 1 280 ? 23.195 13.269  -51.588 1.00 26.51 ? 280 LYS A CB  1 
ATOM   2125 C CG  . LYS A 1 280 ? 22.894 12.997  -53.049 1.00 24.67 ? 280 LYS A CG  1 
ATOM   2126 C CD  . LYS A 1 280 ? 23.654 11.731  -53.454 1.00 27.12 ? 280 LYS A CD  1 
ATOM   2127 C CE  . LYS A 1 280 ? 23.619 11.524  -54.958 1.00 31.91 ? 280 LYS A CE  1 
ATOM   2128 N NZ  . LYS A 1 280 ? 24.260 10.215  -55.256 1.00 32.48 ? 280 LYS A NZ  1 
ATOM   2129 N N   . GLU A 1 281 ? 23.852 15.062  -49.201 1.00 21.51 ? 281 GLU A N   1 
ATOM   2130 C CA  . GLU A 1 281 ? 24.313 15.119  -47.816 1.00 25.56 ? 281 GLU A CA  1 
ATOM   2131 C C   . GLU A 1 281 ? 23.390 15.984  -46.967 1.00 25.71 ? 281 GLU A C   1 
ATOM   2132 O O   . GLU A 1 281 ? 23.135 15.671  -45.798 1.00 23.19 ? 281 GLU A O   1 
ATOM   2133 C CB  . GLU A 1 281 ? 25.745 15.634  -47.759 1.00 28.72 ? 281 GLU A CB  1 
ATOM   2134 C CG  . GLU A 1 281 ? 26.756 14.677  -48.383 1.00 33.36 ? 281 GLU A CG  1 
ATOM   2135 C CD  . GLU A 1 281 ? 26.523 13.222  -47.971 1.00 47.36 ? 281 GLU A CD  1 
ATOM   2136 O OE1 . GLU A 1 281 ? 26.217 12.966  -46.783 1.00 54.26 ? 281 GLU A OE1 1 
ATOM   2137 O OE2 . GLU A 1 281 ? 26.633 12.331  -48.841 1.00 58.03 ? 281 GLU A OE2 1 
ATOM   2138 N N   . TYR A 1 282 ? 22.859 17.058  -47.552 1.00 23.03 ? 282 TYR A N   1 
ATOM   2139 C CA  . TYR A 1 282 ? 21.910 17.907  -46.837 1.00 22.37 ? 282 TYR A CA  1 
ATOM   2140 C C   . TYR A 1 282 ? 20.707 17.110  -46.359 1.00 24.85 ? 282 TYR A C   1 
ATOM   2141 O O   . TYR A 1 282 ? 20.288 17.223  -45.199 1.00 20.96 ? 282 TYR A O   1 
ATOM   2142 C CB  . TYR A 1 282 ? 21.444 19.047  -47.741 1.00 21.22 ? 282 TYR A CB  1 
ATOM   2143 C CG  . TYR A 1 282 ? 22.399 20.214  -47.911 1.00 22.80 ? 282 TYR A CG  1 
ATOM   2144 C CD1 . TYR A 1 282 ? 23.739 20.143  -47.528 1.00 31.16 ? 282 TYR A CD1 1 
ATOM   2145 C CD2 . TYR A 1 282 ? 21.954 21.402  -48.492 1.00 29.92 ? 282 TYR A CD2 1 
ATOM   2146 C CE1 . TYR A 1 282 ? 24.610 21.246  -47.705 1.00 30.95 ? 282 TYR A CE1 1 
ATOM   2147 C CE2 . TYR A 1 282 ? 22.814 22.496  -48.679 1.00 31.23 ? 282 TYR A CE2 1 
ATOM   2148 C CZ  . TYR A 1 282 ? 24.134 22.419  -48.277 1.00 29.52 ? 282 TYR A CZ  1 
ATOM   2149 O OH  . TYR A 1 282 ? 24.960 23.527  -48.464 1.00 31.53 ? 282 TYR A OH  1 
ATOM   2150 N N   . TYR A 1 283 ? 20.109 16.313  -47.250 1.00 20.26 ? 283 TYR A N   1 
ATOM   2151 C CA  . TYR A 1 283 ? 18.909 15.589  -46.846 1.00 21.30 ? 283 TYR A CA  1 
ATOM   2152 C C   . TYR A 1 283 ? 19.244 14.513  -45.824 1.00 23.47 ? 283 TYR A C   1 
ATOM   2153 O O   . TYR A 1 283 ? 18.467 14.262  -44.897 1.00 23.89 ? 283 TYR A O   1 
ATOM   2154 C CB  . TYR A 1 283 ? 18.235 14.968  -48.074 1.00 19.34 ? 283 TYR A CB  1 
ATOM   2155 C CG  . TYR A 1 283 ? 17.462 15.941  -48.950 1.00 20.85 ? 283 TYR A CG  1 
ATOM   2156 C CD1 . TYR A 1 283 ? 16.843 17.061  -48.411 1.00 26.04 ? 283 TYR A CD1 1 
ATOM   2157 C CD2 . TYR A 1 283 ? 17.341 15.717  -50.315 1.00 23.21 ? 283 TYR A CD2 1 
ATOM   2158 C CE1 . TYR A 1 283 ? 16.119 17.950  -49.230 1.00 27.02 ? 283 TYR A CE1 1 
ATOM   2159 C CE2 . TYR A 1 283 ? 16.634 16.582  -51.132 1.00 26.55 ? 283 TYR A CE2 1 
ATOM   2160 C CZ  . TYR A 1 283 ? 16.021 17.694  -50.583 1.00 27.38 ? 283 TYR A CZ  1 
ATOM   2161 O OH  . TYR A 1 283 ? 15.328 18.532  -51.426 1.00 26.05 ? 283 TYR A OH  1 
ATOM   2162 N N   . PHE A 1 284 ? 20.388 13.848  -45.986 1.00 22.60 ? 284 PHE A N   1 
ATOM   2163 C CA  . PHE A 1 284 ? 20.772 12.841  -45.010 1.00 20.43 ? 284 PHE A CA  1 
ATOM   2164 C C   . PHE A 1 284 ? 21.034 13.475  -43.647 1.00 26.19 ? 284 PHE A C   1 
ATOM   2165 O O   . PHE A 1 284 ? 20.705 12.877  -42.621 1.00 23.25 ? 284 PHE A O   1 
ATOM   2166 C CB  . PHE A 1 284 ? 22.010 12.071  -45.494 1.00 21.60 ? 284 PHE A CB  1 
ATOM   2167 C CG  . PHE A 1 284 ? 21.682 10.855  -46.311 1.00 26.20 ? 284 PHE A CG  1 
ATOM   2168 C CD1 . PHE A 1 284 ? 21.399 10.962  -47.657 1.00 30.44 ? 284 PHE A CD1 1 
ATOM   2169 C CD2 . PHE A 1 284 ? 21.637 9.603   -45.719 1.00 28.80 ? 284 PHE A CD2 1 
ATOM   2170 C CE1 . PHE A 1 284 ? 21.088 9.839   -48.411 1.00 39.49 ? 284 PHE A CE1 1 
ATOM   2171 C CE2 . PHE A 1 284 ? 21.321 8.473   -46.461 1.00 32.88 ? 284 PHE A CE2 1 
ATOM   2172 C CZ  . PHE A 1 284 ? 21.045 8.589   -47.805 1.00 35.80 ? 284 PHE A CZ  1 
ATOM   2173 N N   . ASN A 1 285 ? 21.584 14.698  -43.618 1.00 21.72 ? 285 ASN A N   1 
ATOM   2174 C CA  . ASN A 1 285 ? 21.909 15.349  -42.341 1.00 27.51 ? 285 ASN A CA  1 
ATOM   2175 C C   . ASN A 1 285 ? 20.649 15.751  -41.583 1.00 25.69 ? 285 ASN A C   1 
ATOM   2176 O O   . ASN A 1 285 ? 20.481 15.400  -40.399 1.00 22.32 ? 285 ASN A O   1 
ATOM   2177 C CB  . ASN A 1 285 ? 22.791 16.585  -42.578 1.00 21.84 ? 285 ASN A CB  1 
ATOM   2178 C CG  . ASN A 1 285 ? 23.394 17.147  -41.283 1.00 32.57 ? 285 ASN A CG  1 
ATOM   2179 O OD1 . ASN A 1 285 ? 23.926 16.408  -40.460 1.00 31.21 ? 285 ASN A OD1 1 
ATOM   2180 N ND2 . ASN A 1 285 ? 23.316 18.462  -41.111 1.00 29.97 ? 285 ASN A ND2 1 
ATOM   2181 N N   . ILE A 1 286 ? 19.756 16.509  -42.233 1.00 24.81 ? 286 ILE A N   1 
ATOM   2182 C CA  . ILE A 1 286 ? 18.571 16.965  -41.503 1.00 24.11 ? 286 ILE A CA  1 
ATOM   2183 C C   . ILE A 1 286 ? 17.584 15.824  -41.323 1.00 22.33 ? 286 ILE A C   1 
ATOM   2184 O O   . ILE A 1 286 ? 16.859 15.783  -40.319 1.00 21.44 ? 286 ILE A O   1 
ATOM   2185 C CB  . ILE A 1 286 ? 17.890 18.180  -42.171 1.00 20.41 ? 286 ILE A CB  1 
ATOM   2186 C CG1 . ILE A 1 286 ? 17.282 17.836  -43.546 1.00 22.13 ? 286 ILE A CG1 1 
ATOM   2187 C CG2 . ILE A 1 286 ? 18.867 19.369  -42.263 1.00 23.89 ? 286 ILE A CG2 1 
ATOM   2188 C CD1 . ILE A 1 286 ? 16.334 18.924  -44.070 1.00 24.65 ? 286 ILE A CD1 1 
ATOM   2189 N N   . GLY A 1 287 ? 17.531 14.878  -42.263 1.00 19.55 ? 287 GLY A N   1 
ATOM   2190 C CA  . GLY A 1 287 ? 16.640 13.739  -42.074 1.00 21.21 ? 287 GLY A CA  1 
ATOM   2191 C C   . GLY A 1 287 ? 17.052 12.888  -40.887 1.00 22.95 ? 287 GLY A C   1 
ATOM   2192 O O   . GLY A 1 287 ? 16.211 12.420  -40.107 1.00 24.32 ? 287 GLY A O   1 
ATOM   2193 N N   . ASN A 1 288 ? 18.351 12.679  -40.726 1.00 20.41 ? 288 ASN A N   1 
ATOM   2194 C CA  . ASN A 1 288 ? 18.785 11.818  -39.637 1.00 21.52 ? 288 ASN A CA  1 
ATOM   2195 C C   . ASN A 1 288 ? 18.664 12.514  -38.290 1.00 21.44 ? 288 ASN A C   1 
ATOM   2196 O O   . ASN A 1 288 ? 18.223 11.890  -37.318 1.00 21.91 ? 288 ASN A O   1 
ATOM   2197 C CB  . ASN A 1 288 ? 20.192 11.309  -39.917 1.00 24.81 ? 288 ASN A CB  1 
ATOM   2198 C CG  . ASN A 1 288 ? 20.155 9.991   -40.707 1.00 33.29 ? 288 ASN A CG  1 
ATOM   2199 O OD1 . ASN A 1 288 ? 19.713 8.955   -40.186 1.00 35.96 ? 288 ASN A OD1 1 
ATOM   2200 N ND2 . ASN A 1 288 ? 20.545 10.042  -41.978 1.00 34.05 ? 288 ASN A ND2 1 
ATOM   2201 N N   . TYR A 1 289 ? 18.968 13.815  -38.217 1.00 20.27 ? 289 TYR A N   1 
ATOM   2202 C CA  . TYR A 1 289 ? 18.798 14.511  -36.940 1.00 23.99 ? 289 TYR A CA  1 
ATOM   2203 C C   . TYR A 1 289 ? 17.325 14.699  -36.584 1.00 24.77 ? 289 TYR A C   1 
ATOM   2204 O O   . TYR A 1 289 ? 16.956 14.600  -35.405 1.00 23.91 ? 289 TYR A O   1 
ATOM   2205 C CB  . TYR A 1 289 ? 19.555 15.840  -36.958 1.00 24.26 ? 289 TYR A CB  1 
ATOM   2206 C CG  . TYR A 1 289 ? 21.000 15.651  -36.529 1.00 26.81 ? 289 TYR A CG  1 
ATOM   2207 C CD1 . TYR A 1 289 ? 21.308 14.889  -35.399 1.00 30.72 ? 289 TYR A CD1 1 
ATOM   2208 C CD2 . TYR A 1 289 ? 22.053 16.178  -37.265 1.00 25.89 ? 289 TYR A CD2 1 
ATOM   2209 C CE1 . TYR A 1 289 ? 22.625 14.695  -34.989 1.00 32.18 ? 289 TYR A CE1 1 
ATOM   2210 C CE2 . TYR A 1 289 ? 23.366 15.986  -36.868 1.00 31.81 ? 289 TYR A CE2 1 
ATOM   2211 C CZ  . TYR A 1 289 ? 23.646 15.240  -35.729 1.00 41.41 ? 289 TYR A CZ  1 
ATOM   2212 O OH  . TYR A 1 289 ? 24.944 15.032  -35.314 1.00 39.11 ? 289 TYR A OH  1 
ATOM   2213 N N   . TYR A 1 290 ? 16.456 14.934  -37.572 1.00 22.11 ? 290 TYR A N   1 
ATOM   2214 C CA  . TYR A 1 290 ? 15.031 14.980  -37.248 1.00 22.32 ? 290 TYR A CA  1 
ATOM   2215 C C   . TYR A 1 290 ? 14.510 13.609  -36.823 1.00 29.25 ? 290 TYR A C   1 
ATOM   2216 O O   . TYR A 1 290 ? 13.678 13.509  -35.899 1.00 23.37 ? 290 TYR A O   1 
ATOM   2217 C CB  . TYR A 1 290 ? 14.217 15.513  -38.429 1.00 22.30 ? 290 TYR A CB  1 
ATOM   2218 C CG  . TYR A 1 290 ? 12.764 15.692  -38.054 1.00 23.88 ? 290 TYR A CG  1 
ATOM   2219 C CD1 . TYR A 1 290 ? 12.368 16.750  -37.241 1.00 25.64 ? 290 TYR A CD1 1 
ATOM   2220 C CD2 . TYR A 1 290 ? 11.800 14.802  -38.485 1.00 23.74 ? 290 TYR A CD2 1 
ATOM   2221 C CE1 . TYR A 1 290 ? 11.061 16.928  -36.892 1.00 27.06 ? 290 TYR A CE1 1 
ATOM   2222 C CE2 . TYR A 1 290 ? 10.477 14.966  -38.129 1.00 31.39 ? 290 TYR A CE2 1 
ATOM   2223 C CZ  . TYR A 1 290 ? 10.118 16.031  -37.332 1.00 35.56 ? 290 TYR A CZ  1 
ATOM   2224 O OH  . TYR A 1 290 ? 8.805  16.209  -36.966 1.00 40.23 ? 290 TYR A OH  1 
ATOM   2225 N N   . ALA A 1 291 ? 14.992 12.542  -37.482 1.00 20.31 ? 291 ALA A N   1 
ATOM   2226 C CA  . ALA A 1 291 ? 14.659 11.177  -37.063 1.00 24.29 ? 291 ALA A CA  1 
ATOM   2227 C C   . ALA A 1 291 ? 15.072 10.916  -35.615 1.00 24.62 ? 291 ALA A C   1 
ATOM   2228 O O   . ALA A 1 291 ? 14.324 10.289  -34.846 1.00 22.44 ? 291 ALA A O   1 
ATOM   2229 C CB  . ALA A 1 291 ? 15.328 10.165  -38.009 1.00 21.20 ? 291 ALA A CB  1 
ATOM   2230 N N   . ILE A 1 292 ? 16.263 11.382  -35.224 1.00 19.92 ? 292 ILE A N   1 
ATOM   2231 C CA  . ILE A 1 292 ? 16.710 11.238  -33.838 1.00 25.30 ? 292 ILE A CA  1 
ATOM   2232 C C   . ILE A 1 292 ? 15.748 11.948  -32.891 1.00 30.68 ? 292 ILE A C   1 
ATOM   2233 O O   . ILE A 1 292 ? 15.364 11.402  -31.847 1.00 25.29 ? 292 ILE A O   1 
ATOM   2234 C CB  . ILE A 1 292 ? 18.152 11.759  -33.696 1.00 25.13 ? 292 ILE A CB  1 
ATOM   2235 C CG1 . ILE A 1 292 ? 19.120 10.765  -34.357 1.00 23.97 ? 292 ILE A CG1 1 
ATOM   2236 C CG2 . ILE A 1 292 ? 18.503 12.034  -32.215 1.00 26.44 ? 292 ILE A CG2 1 
ATOM   2237 C CD1 . ILE A 1 292 ? 20.499 11.316  -34.634 1.00 29.59 ? 292 ILE A CD1 1 
ATOM   2238 N N   . PHE A 1 293 ? 15.308 13.151  -33.263 1.00 22.20 ? 293 PHE A N   1 
ATOM   2239 C CA  . PHE A 1 293 ? 14.341 13.888  -32.453 1.00 25.57 ? 293 PHE A CA  1 
ATOM   2240 C C   . PHE A 1 293 ? 13.032 13.122  -32.318 1.00 24.61 ? 293 PHE A C   1 
ATOM   2241 O O   . PHE A 1 293 ? 12.499 12.974  -31.214 1.00 31.62 ? 293 PHE A O   1 
ATOM   2242 C CB  . PHE A 1 293 ? 14.103 15.271  -33.079 1.00 22.57 ? 293 PHE A CB  1 
ATOM   2243 C CG  . PHE A 1 293 ? 12.853 15.964  -32.601 1.00 25.17 ? 293 PHE A CG  1 
ATOM   2244 C CD1 . PHE A 1 293 ? 12.826 16.605  -31.362 1.00 28.25 ? 293 PHE A CD1 1 
ATOM   2245 C CD2 . PHE A 1 293 ? 11.719 16.000  -33.394 1.00 27.80 ? 293 PHE A CD2 1 
ATOM   2246 C CE1 . PHE A 1 293 ? 11.680 17.268  -30.925 1.00 31.31 ? 293 PHE A CE1 1 
ATOM   2247 C CE2 . PHE A 1 293 ? 10.575 16.656  -32.968 1.00 35.87 ? 293 PHE A CE2 1 
ATOM   2248 C CZ  . PHE A 1 293 ? 10.551 17.287  -31.733 1.00 36.53 ? 293 PHE A CZ  1 
ATOM   2249 N N   . LYS A 1 294 ? 12.493 12.636  -33.437 1.00 23.24 ? 294 LYS A N   1 
ATOM   2250 C CA  . LYS A 1 294 ? 11.205 11.952  -33.424 1.00 26.00 ? 294 LYS A CA  1 
ATOM   2251 C C   . LYS A 1 294 ? 11.277 10.682  -32.583 1.00 32.07 ? 294 LYS A C   1 
ATOM   2252 O O   . LYS A 1 294 ? 10.333 10.355  -31.849 1.00 29.38 ? 294 LYS A O   1 
ATOM   2253 C CB  . LYS A 1 294 ? 10.799 11.643  -34.868 1.00 31.33 ? 294 LYS A CB  1 
ATOM   2254 C CG  . LYS A 1 294 ? 9.373  11.206  -35.123 1.00 37.70 ? 294 LYS A CG  1 
ATOM   2255 C CD  . LYS A 1 294 ? 9.120  11.132  -36.642 1.00 35.88 ? 294 LYS A CD  1 
ATOM   2256 C CE  . LYS A 1 294 ? 7.694  10.702  -36.956 1.00 41.68 ? 294 LYS A CE  1 
ATOM   2257 N NZ  . LYS A 1 294 ? 7.430  10.402  -38.407 1.00 44.89 ? 294 LYS A NZ  1 
ATOM   2258 N N   . PHE A 1 295 ? 12.407 9.973   -32.663 1.00 21.30 ? 295 PHE A N   1 
ATOM   2259 C CA  . PHE A 1 295 ? 12.603 8.731   -31.914 1.00 28.58 ? 295 PHE A CA  1 
ATOM   2260 C C   . PHE A 1 295 ? 12.766 9.021   -30.420 1.00 34.31 ? 295 PHE A C   1 
ATOM   2261 O O   . PHE A 1 295 ? 12.255 8.283   -29.559 1.00 26.50 ? 295 PHE A O   1 
ATOM   2262 C CB  . PHE A 1 295 ? 13.845 8.041   -32.470 1.00 22.06 ? 295 PHE A CB  1 
ATOM   2263 C CG  . PHE A 1 295 ? 13.988 6.582   -32.101 1.00 28.08 ? 295 PHE A CG  1 
ATOM   2264 C CD1 . PHE A 1 295 ? 13.187 5.625   -32.699 1.00 27.32 ? 295 PHE A CD1 1 
ATOM   2265 C CD2 . PHE A 1 295 ? 14.979 6.173   -31.227 1.00 36.02 ? 295 PHE A CD2 1 
ATOM   2266 C CE1 . PHE A 1 295 ? 13.352 4.279   -32.407 1.00 28.26 ? 295 PHE A CE1 1 
ATOM   2267 C CE2 . PHE A 1 295 ? 15.153 4.817   -30.930 1.00 33.00 ? 295 PHE A CE2 1 
ATOM   2268 C CZ  . PHE A 1 295 ? 14.336 3.881   -31.528 1.00 24.58 ? 295 PHE A CZ  1 
ATOM   2269 N N   . ALA A 1 296 ? 13.491 10.092  -30.099 1.00 24.69 ? 296 ALA A N   1 
ATOM   2270 C CA  . ALA A 1 296 ? 13.698 10.471  -28.701 1.00 29.14 ? 296 ALA A CA  1 
ATOM   2271 C C   . ALA A 1 296 ? 12.396 10.857  -28.002 1.00 32.90 ? 296 ALA A C   1 
ATOM   2272 O O   . ALA A 1 296 ? 12.237 10.599  -26.797 1.00 35.46 ? 296 ALA A O   1 
ATOM   2273 C CB  . ALA A 1 296 ? 14.700 11.616  -28.623 1.00 33.05 ? 296 ALA A CB  1 
ATOM   2274 N N   . LYS A 1 297 ? 11.480 11.518  -28.717 1.00 36.06 ? 297 LYS A N   1 
ATOM   2275 C CA  . LYS A 1 297 ? 10.171 11.855  -28.158 1.00 42.74 ? 297 LYS A CA  1 
ATOM   2276 C C   . LYS A 1 297 ? 9.571  10.653  -27.446 1.00 40.54 ? 297 LYS A C   1 
ATOM   2277 O O   . LYS A 1 297 ? 9.211  10.712  -26.262 1.00 30.76 ? 297 LYS A O   1 
ATOM   2278 C CB  . LYS A 1 297 ? 9.208  12.307  -29.266 1.00 44.67 ? 297 LYS A CB  1 
ATOM   2279 C CG  . LYS A 1 297 ? 8.997  13.800  -29.443 1.00 54.07 ? 297 LYS A CG  1 
ATOM   2280 C CD  . LYS A 1 297 ? 7.740  14.076  -30.252 1.00 55.00 ? 297 LYS A CD  1 
ATOM   2281 C CE  . LYS A 1 297 ? 8.053  14.849  -31.523 1.00 60.62 ? 297 LYS A CE  1 
ATOM   2282 N NZ  . LYS A 1 297 ? 6.851  15.023  -32.383 1.00 69.16 ? 297 LYS A NZ  1 
ATOM   2283 N N   . ASP A 1 298 ? 9.454  9.545   -28.174 1.00 31.34 ? 298 ASP A N   1 
ATOM   2284 C CA  . ASP A 1 298 ? 8.785  8.381   -27.624 1.00 27.49 ? 298 ASP A CA  1 
ATOM   2285 C C   . ASP A 1 298 ? 9.646  7.709   -26.567 1.00 24.58 ? 298 ASP A C   1 
ATOM   2286 O O   . ASP A 1 298 ? 9.118  7.218   -25.564 1.00 23.55 ? 298 ASP A O   1 
ATOM   2287 C CB  . ASP A 1 298 ? 8.416  7.411   -28.749 1.00 28.93 ? 298 ASP A CB  1 
ATOM   2288 C CG  . ASP A 1 298 ? 7.311  7.974   -29.657 1.00 57.19 ? 298 ASP A CG  1 
ATOM   2289 O OD1 . ASP A 1 298 ? 6.128  7.922   -29.254 1.00 55.78 ? 298 ASP A OD1 1 
ATOM   2290 O OD2 . ASP A 1 298 ? 7.632  8.508   -30.748 1.00 48.15 ? 298 ASP A OD2 1 
ATOM   2291 N N   . GLN A 1 299 ? 10.968 7.683   -26.768 1.00 20.99 ? 299 GLN A N   1 
ATOM   2292 C CA  . GLN A 1 299 ? 11.824 7.004   -25.801 1.00 22.55 ? 299 GLN A CA  1 
ATOM   2293 C C   . GLN A 1 299 ? 11.801 7.736   -24.462 1.00 23.09 ? 299 GLN A C   1 
ATOM   2294 O O   . GLN A 1 299 ? 11.704 7.110   -23.402 1.00 18.07 ? 299 GLN A O   1 
ATOM   2295 C CB  . GLN A 1 299 ? 13.252 6.901   -26.319 1.00 16.98 ? 299 GLN A CB  1 
ATOM   2296 C CG  . GLN A 1 299 ? 14.075 5.810   -25.592 1.00 20.21 ? 299 GLN A CG  1 
ATOM   2297 C CD  . GLN A 1 299 ? 13.771 4.387   -26.094 1.00 19.81 ? 299 GLN A CD  1 
ATOM   2298 O OE1 . GLN A 1 299 ? 13.055 4.200   -27.084 1.00 21.16 ? 299 GLN A OE1 1 
ATOM   2299 N NE2 . GLN A 1 299 ? 14.332 3.385   -25.427 1.00 21.09 ? 299 GLN A NE2 1 
ATOM   2300 N N   . LEU A 1 300 ? 11.871 9.062   -24.503 1.00 17.97 ? 300 LEU A N   1 
ATOM   2301 C CA  . LEU A 1 300 ? 11.831 9.854   -23.276 1.00 22.84 ? 300 LEU A CA  1 
ATOM   2302 C C   . LEU A 1 300 ? 10.479 9.748   -22.579 1.00 23.56 ? 300 LEU A C   1 
ATOM   2303 O O   . LEU A 1 300 ? 10.414 9.714   -21.338 1.00 21.80 ? 300 LEU A O   1 
ATOM   2304 C CB  . LEU A 1 300 ? 12.192 11.305  -23.611 1.00 23.70 ? 300 LEU A CB  1 
ATOM   2305 C CG  . LEU A 1 300 ? 13.696 11.507  -23.852 1.00 21.54 ? 300 LEU A CG  1 
ATOM   2306 C CD1 . LEU A 1 300 ? 13.969 12.908  -24.417 1.00 25.75 ? 300 LEU A CD1 1 
ATOM   2307 C CD2 . LEU A 1 300 ? 14.478 11.336  -22.522 1.00 23.42 ? 300 LEU A CD2 1 
ATOM   2308 N N   . ASN A 1 301 ? 9.375  9.728   -23.335 1.00 20.00 ? 301 ASN A N   1 
ATOM   2309 C CA  A ASN A 1 301 ? 8.074  9.568   -22.693 0.49 26.19 ? 301 ASN A CA  1 
ATOM   2310 C CA  B ASN A 1 301 ? 8.079  9.570   -22.688 0.51 26.28 ? 301 ASN A CA  1 
ATOM   2311 C C   . ASN A 1 301 ? 7.992  8.234   -21.966 1.00 23.43 ? 301 ASN A C   1 
ATOM   2312 O O   . ASN A 1 301 ? 7.441  8.152   -20.866 1.00 22.20 ? 301 ASN A O   1 
ATOM   2313 C CB  A ASN A 1 301 ? 6.949  9.686   -23.720 0.49 27.66 ? 301 ASN A CB  1 
ATOM   2314 C CB  B ASN A 1 301 ? 6.951  9.701   -23.705 0.51 27.37 ? 301 ASN A CB  1 
ATOM   2315 C CG  A ASN A 1 301 ? 5.569  9.506   -23.105 0.49 32.78 ? 301 ASN A CG  1 
ATOM   2316 C CG  B ASN A 1 301 ? 6.826  11.107  -24.244 0.51 33.42 ? 301 ASN A CG  1 
ATOM   2317 O OD1 A ASN A 1 301 ? 5.105  10.342  -22.326 0.49 38.49 ? 301 ASN A OD1 1 
ATOM   2318 O OD1 B ASN A 1 301 ? 7.079  12.077  -23.530 0.51 37.08 ? 301 ASN A OD1 1 
ATOM   2319 N ND2 A ASN A 1 301 ? 4.897  8.424   -23.473 0.49 34.20 ? 301 ASN A ND2 1 
ATOM   2320 N ND2 B ASN A 1 301 ? 6.451  11.226  -25.507 0.51 30.19 ? 301 ASN A ND2 1 
ATOM   2321 N N   . MET A 1 302 ? 8.525  7.179   -22.581 1.00 20.16 ? 302 MET A N   1 
ATOM   2322 C CA  . MET A 1 302 ? 8.539  5.868   -21.951 1.00 21.27 ? 302 MET A CA  1 
ATOM   2323 C C   . MET A 1 302 ? 9.427  5.874   -20.704 1.00 20.98 ? 302 MET A C   1 
ATOM   2324 O O   . MET A 1 302 ? 9.054  5.331   -19.656 1.00 21.06 ? 302 MET A O   1 
ATOM   2325 C CB  . MET A 1 302 ? 9.015  4.829   -22.980 1.00 16.95 ? 302 MET A CB  1 
ATOM   2326 C CG  . MET A 1 302 ? 9.263  3.406   -22.411 1.00 19.36 ? 302 MET A CG  1 
ATOM   2327 S SD  . MET A 1 302 ? 10.874 3.202   -21.692 1.00 21.46 ? 302 MET A SD  1 
ATOM   2328 C CE  . MET A 1 302 ? 11.930 3.325   -23.177 1.00 18.13 ? 302 MET A CE  1 
ATOM   2329 N N   . LEU A 1 303 ? 10.598 6.503   -20.786 1.00 19.63 ? 303 LEU A N   1 
ATOM   2330 C CA  . LEU A 1 303 ? 11.503 6.515   -19.636 1.00 16.75 ? 303 LEU A CA  1 
ATOM   2331 C C   . LEU A 1 303 ? 10.949 7.366   -18.492 1.00 20.62 ? 303 LEU A C   1 
ATOM   2332 O O   . LEU A 1 303 ? 11.142 7.036   -17.316 1.00 21.83 ? 303 LEU A O   1 
ATOM   2333 C CB  . LEU A 1 303 ? 12.883 7.013   -20.063 1.00 19.92 ? 303 LEU A CB  1 
ATOM   2334 C CG  . LEU A 1 303 ? 13.625 6.043   -20.988 1.00 18.61 ? 303 LEU A CG  1 
ATOM   2335 C CD1 . LEU A 1 303 ? 14.806 6.766   -21.665 1.00 16.87 ? 303 LEU A CD1 1 
ATOM   2336 C CD2 . LEU A 1 303 ? 14.113 4.825   -20.205 1.00 17.90 ? 303 LEU A CD2 1 
ATOM   2337 N N   . ASN A 1 304 ? 10.266 8.463   -18.813 1.00 20.61 ? 304 ASN A N   1 
ATOM   2338 C CA  . ASN A 1 304 ? 9.583  9.240   -17.781 1.00 23.10 ? 304 ASN A CA  1 
ATOM   2339 C C   . ASN A 1 304 ? 8.557  8.382   -17.052 1.00 23.98 ? 304 ASN A C   1 
ATOM   2340 O O   . ASN A 1 304 ? 8.479  8.388   -15.813 1.00 22.97 ? 304 ASN A O   1 
ATOM   2341 C CB  . ASN A 1 304 ? 8.921  10.465  -18.418 1.00 24.52 ? 304 ASN A CB  1 
ATOM   2342 C CG  . ASN A 1 304 ? 8.086  11.261  -17.423 1.00 35.29 ? 304 ASN A CG  1 
ATOM   2343 O OD1 . ASN A 1 304 ? 6.893  11.459  -17.618 1.00 43.30 ? 304 ASN A OD1 1 
ATOM   2344 N ND2 . ASN A 1 304 ? 8.709  11.696  -16.341 1.00 30.59 ? 304 ASN A ND2 1 
ATOM   2345 N N   . LYS A 1 305 ? 7.759  7.627   -17.811 1.00 20.72 ? 305 LYS A N   1 
ATOM   2346 C CA  . LYS A 1 305 ? 6.798  6.711   -17.196 1.00 23.90 ? 305 LYS A CA  1 
ATOM   2347 C C   . LYS A 1 305 ? 7.495  5.644   -16.358 1.00 22.69 ? 305 LYS A C   1 
ATOM   2348 O O   . LYS A 1 305 ? 7.014  5.281   -15.272 1.00 24.33 ? 305 LYS A O   1 
ATOM   2349 C CB  . LYS A 1 305 ? 5.938  6.054   -18.276 1.00 29.89 ? 305 LYS A CB  1 
ATOM   2350 C CG  . LYS A 1 305 ? 4.784  5.246   -17.717 1.00 43.31 ? 305 LYS A CG  1 
ATOM   2351 C CD  . LYS A 1 305 ? 3.902  4.664   -18.811 1.00 54.48 ? 305 LYS A CD  1 
ATOM   2352 C CE  . LYS A 1 305 ? 2.747  3.879   -18.198 1.00 63.86 ? 305 LYS A CE  1 
ATOM   2353 N NZ  . LYS A 1 305 ? 2.343  2.725   -19.047 1.00 69.28 ? 305 LYS A NZ  1 
ATOM   2354 N N   . ALA A 1 306 ? 8.614  5.111   -16.850 1.00 20.10 ? 306 ALA A N   1 
ATOM   2355 C CA  . ALA A 1 306 ? 9.342  4.105   -16.086 1.00 19.71 ? 306 ALA A CA  1 
ATOM   2356 C C   . ALA A 1 306 ? 9.846  4.678   -14.769 1.00 22.15 ? 306 ALA A C   1 
ATOM   2357 O O   . ALA A 1 306 ? 9.832  3.996   -13.733 1.00 23.93 ? 306 ALA A O   1 
ATOM   2358 C CB  . ALA A 1 306 ? 10.506 3.553   -16.929 1.00 18.73 ? 306 ALA A CB  1 
ATOM   2359 N N   . LEU A 1 307 ? 10.272 5.940   -14.774 1.00 18.23 ? 307 LEU A N   1 
ATOM   2360 C CA  . LEU A 1 307 ? 10.790 6.523   -13.536 1.00 23.27 ? 307 LEU A CA  1 
ATOM   2361 C C   . LEU A 1 307 ? 9.664  6.809   -12.548 1.00 28.06 ? 307 LEU A C   1 
ATOM   2362 O O   . LEU A 1 307 ? 9.828  6.623   -11.337 1.00 26.50 ? 307 LEU A O   1 
ATOM   2363 C CB  . LEU A 1 307 ? 11.571 7.799   -13.849 1.00 23.64 ? 307 LEU A CB  1 
ATOM   2364 C CG  . LEU A 1 307 ? 12.942 7.544   -14.471 1.00 25.76 ? 307 LEU A CG  1 
ATOM   2365 C CD1 . LEU A 1 307 ? 13.556 8.835   -14.964 1.00 26.42 ? 307 LEU A CD1 1 
ATOM   2366 C CD2 . LEU A 1 307 ? 13.834 6.869   -13.436 1.00 27.42 ? 307 LEU A CD2 1 
ATOM   2367 N N   . ILE A 1 308 ? 8.516  7.252   -13.045 1.00 23.12 ? 308 ILE A N   1 
ATOM   2368 C CA  . ILE A 1 308 ? 7.361  7.464   -12.172 1.00 22.82 ? 308 ILE A CA  1 
ATOM   2369 C C   . ILE A 1 308 ? 6.923  6.145   -11.559 1.00 24.23 ? 308 ILE A C   1 
ATOM   2370 O O   . ILE A 1 308 ? 6.565  6.074   -10.372 1.00 28.35 ? 308 ILE A O   1 
ATOM   2371 C CB  . ILE A 1 308 ? 6.223  8.124   -12.968 1.00 25.72 ? 308 ILE A CB  1 
ATOM   2372 C CG1 . ILE A 1 308 ? 6.591  9.567   -13.306 1.00 26.33 ? 308 ILE A CG1 1 
ATOM   2373 C CG2 . ILE A 1 308 ? 4.912  8.060   -12.174 1.00 30.18 ? 308 ILE A CG2 1 
ATOM   2374 C CD1 . ILE A 1 308 ? 5.727  10.167  -14.395 1.00 35.49 ? 308 ILE A CD1 1 
ATOM   2375 N N   . HIS A 1 309 ? 6.983  5.071   -12.346 1.00 25.11 ? 309 HIS A N   1 
ATOM   2376 C CA  . HIS A 1 309 ? 6.635  3.763   -11.816 1.00 23.05 ? 309 HIS A CA  1 
ATOM   2377 C C   . HIS A 1 309 ? 7.598  3.347   -10.711 1.00 26.26 ? 309 HIS A C   1 
ATOM   2378 O O   . HIS A 1 309 ? 7.170  2.813   -9.674  1.00 22.12 ? 309 HIS A O   1 
ATOM   2379 C CB  . HIS A 1 309 ? 6.618  2.721   -12.928 1.00 24.39 ? 309 HIS A CB  1 
ATOM   2380 C CG  . HIS A 1 309 ? 6.227  1.366   -12.443 1.00 28.97 ? 309 HIS A CG  1 
ATOM   2381 N ND1 . HIS A 1 309 ? 4.941  1.069   -12.050 1.00 30.86 ? 309 HIS A ND1 1 
ATOM   2382 C CD2 . HIS A 1 309 ? 6.962  0.254   -12.217 1.00 29.80 ? 309 HIS A CD2 1 
ATOM   2383 C CE1 . HIS A 1 309 ? 4.894  -0.184  -11.634 1.00 34.54 ? 309 HIS A CE1 1 
ATOM   2384 N NE2 . HIS A 1 309 ? 6.104  -0.704  -11.738 1.00 35.10 ? 309 HIS A NE2 1 
ATOM   2385 N N   . LYS A 1 310 ? 8.902  3.589   -10.903 1.00 25.26 ? 310 LYS A N   1 
ATOM   2386 C CA  . LYS A 1 310 ? 9.874  3.251   -9.855  1.00 25.12 ? 310 LYS A CA  1 
ATOM   2387 C C   . LYS A 1 310 ? 9.649  4.076   -8.591  1.00 27.15 ? 310 LYS A C   1 
ATOM   2388 O O   . LYS A 1 310 ? 9.854  3.576   -7.479  1.00 25.97 ? 310 LYS A O   1 
ATOM   2389 C CB  . LYS A 1 310 ? 11.302 3.465   -10.353 1.00 28.12 ? 310 LYS A CB  1 
ATOM   2390 C CG  . LYS A 1 310 ? 11.710 2.494   -11.413 1.00 27.24 ? 310 LYS A CG  1 
ATOM   2391 C CD  . LYS A 1 310 ? 11.983 1.169   -10.755 1.00 40.16 ? 310 LYS A CD  1 
ATOM   2392 C CE  . LYS A 1 310 ? 12.361 0.146   -11.792 1.00 41.02 ? 310 LYS A CE  1 
ATOM   2393 N NZ  . LYS A 1 310 ? 11.183 -0.637  -12.241 1.00 35.87 ? 310 LYS A NZ  1 
ATOM   2394 N N   . GLU A 1 311 ? 9.282  5.352   -8.744  1.00 25.44 ? 311 GLU A N   1 
ATOM   2395 C CA  . GLU A 1 311 ? 8.976  6.188   -7.581  1.00 27.25 ? 311 GLU A CA  1 
ATOM   2396 C C   . GLU A 1 311 ? 7.848  5.592   -6.770  1.00 28.24 ? 311 GLU A C   1 
ATOM   2397 O O   . GLU A 1 311 ? 7.889  5.592   -5.530  1.00 24.67 ? 311 GLU A O   1 
ATOM   2398 C CB  . GLU A 1 311 ? 8.565  7.595   -8.007  1.00 34.10 ? 311 GLU A CB  1 
ATOM   2399 C CG  . GLU A 1 311 ? 9.685  8.510   -8.301  1.00 52.98 ? 311 GLU A CG  1 
ATOM   2400 C CD  . GLU A 1 311 ? 10.052 9.434   -7.166  1.00 51.95 ? 311 GLU A CD  1 
ATOM   2401 O OE1 . GLU A 1 311 ? 9.912  9.040   -5.992  1.00 53.76 ? 311 GLU A OE1 1 
ATOM   2402 O OE2 . GLU A 1 311 ? 10.494 10.563  -7.462  1.00 58.03 ? 311 GLU A OE2 1 
ATOM   2403 N N   . LYS A 1 312 ? 6.784  5.163   -7.457  1.00 21.60 ? 312 LYS A N   1 
ATOM   2404 C CA  . LYS A 1 312 ? 5.670  4.508   -6.779  1.00 29.29 ? 312 LYS A CA  1 
ATOM   2405 C C   . LYS A 1 312 ? 6.162  3.328   -5.953  1.00 26.24 ? 312 LYS A C   1 
ATOM   2406 O O   . LYS A 1 312 ? 5.815  3.193   -4.778  1.00 22.76 ? 312 LYS A O   1 
ATOM   2407 C CB  . LYS A 1 312 ? 4.628  4.041   -7.797  1.00 32.55 ? 312 LYS A CB  1 
ATOM   2408 C CG  . LYS A 1 312 ? 3.495  3.200   -7.186  1.00 31.97 ? 312 LYS A CG  1 
ATOM   2409 C CD  . LYS A 1 312 ? 2.777  2.394   -8.267  1.00 37.19 ? 312 LYS A CD  1 
ATOM   2410 C CE  . LYS A 1 312 ? 1.621  1.587   -7.704  1.00 49.34 ? 312 LYS A CE  1 
ATOM   2411 N NZ  . LYS A 1 312 ? 0.863  0.870   -8.773  1.00 51.20 ? 312 LYS A NZ  1 
ATOM   2412 N N   . ILE A 1 313 ? 6.973  2.456   -6.563  1.00 22.70 ? 313 ILE A N   1 
ATOM   2413 C CA  . ILE A 1 313 ? 7.447  1.264   -5.863  1.00 24.46 ? 313 ILE A CA  1 
ATOM   2414 C C   . ILE A 1 313 ? 8.288  1.645   -4.652  1.00 23.32 ? 313 ILE A C   1 
ATOM   2415 O O   . ILE A 1 313 ? 8.151  1.045   -3.577  1.00 22.66 ? 313 ILE A O   1 
ATOM   2416 C CB  . ILE A 1 313 ? 8.229  0.356   -6.833  1.00 26.98 ? 313 ILE A CB  1 
ATOM   2417 C CG1 . ILE A 1 313 ? 7.297  -0.155  -7.929  1.00 27.81 ? 313 ILE A CG1 1 
ATOM   2418 C CG2 . ILE A 1 313 ? 8.873  -0.815  -6.104  1.00 25.15 ? 313 ILE A CG2 1 
ATOM   2419 C CD1 . ILE A 1 313 ? 8.015  -0.960  -8.970  1.00 38.51 ? 313 ILE A CD1 1 
ATOM   2420 N N   . VAL A 1 314 ? 9.186  2.622   -4.815  1.00 21.98 ? 314 VAL A N   1 
ATOM   2421 C CA  . VAL A 1 314 ? 10.044 3.062   -3.706  1.00 21.29 ? 314 VAL A CA  1 
ATOM   2422 C C   . VAL A 1 314 ? 9.209  3.562   -2.538  1.00 21.74 ? 314 VAL A C   1 
ATOM   2423 O O   . VAL A 1 314 ? 9.449  3.204   -1.373  1.00 21.64 ? 314 VAL A O   1 
ATOM   2424 C CB  . VAL A 1 314 ? 11.016 4.162   -4.178  1.00 25.31 ? 314 VAL A CB  1 
ATOM   2425 C CG1 . VAL A 1 314 ? 11.643 4.869   -2.959  1.00 33.44 ? 314 VAL A CG1 1 
ATOM   2426 C CG2 . VAL A 1 314 ? 12.088 3.577   -5.036  1.00 32.89 ? 314 VAL A CG2 1 
ATOM   2427 N N   . HIS A 1 315 ? 8.231  4.424   -2.820  1.00 20.61 ? 315 HIS A N   1 
ATOM   2428 C CA  . HIS A 1 315 ? 7.425  4.963   -1.731  1.00 20.85 ? 315 HIS A CA  1 
ATOM   2429 C C   . HIS A 1 315 ? 6.628  3.871   -1.042  1.00 21.50 ? 315 HIS A C   1 
ATOM   2430 O O   . HIS A 1 315 ? 6.461  3.900   0.180   1.00 21.68 ? 315 HIS A O   1 
ATOM   2431 C CB  . HIS A 1 315 ? 6.509  6.075   -2.245  1.00 23.05 ? 315 HIS A CB  1 
ATOM   2432 C CG  . HIS A 1 315 ? 7.238  7.359   -2.476  1.00 23.75 ? 315 HIS A CG  1 
ATOM   2433 N ND1 . HIS A 1 315 ? 7.841  8.059   -1.452  1.00 26.88 ? 315 HIS A ND1 1 
ATOM   2434 C CD2 . HIS A 1 315 ? 7.505  8.045   -3.611  1.00 27.37 ? 315 HIS A CD2 1 
ATOM   2435 C CE1 . HIS A 1 315 ? 8.428  9.136   -1.944  1.00 35.02 ? 315 HIS A CE1 1 
ATOM   2436 N NE2 . HIS A 1 315 ? 8.233  9.155   -3.250  1.00 28.36 ? 315 HIS A NE2 1 
ATOM   2437 N N   . ASN A 1 316 ? 6.110  2.902   -1.801  1.00 24.18 ? 316 ASN A N   1 
ATOM   2438 C CA  . ASN A 1 316 ? 5.370  1.834   -1.136  1.00 21.98 ? 316 ASN A CA  1 
ATOM   2439 C C   . ASN A 1 316 ? 6.291  0.976   -0.275  1.00 22.29 ? 316 ASN A C   1 
ATOM   2440 O O   . ASN A 1 316 ? 5.889  0.533   0.807   1.00 22.94 ? 316 ASN A O   1 
ATOM   2441 C CB  . ASN A 1 316 ? 4.616  0.997   -2.176  1.00 22.67 ? 316 ASN A CB  1 
ATOM   2442 C CG  . ASN A 1 316 ? 3.381  1.717   -2.702  1.00 27.71 ? 316 ASN A CG  1 
ATOM   2443 O OD1 . ASN A 1 316 ? 2.843  2.615   -2.041  1.00 32.55 ? 316 ASN A OD1 1 
ATOM   2444 N ND2 . ASN A 1 316 ? 2.920  1.320   -3.864  1.00 27.95 ? 316 ASN A ND2 1 
ATOM   2445 N N   . LEU A 1 317 ? 7.525  0.731   -0.739  1.00 19.84 ? 317 LEU A N   1 
ATOM   2446 C CA  . LEU A 1 317 ? 8.495  0.003   0.074   1.00 20.40 ? 317 LEU A CA  1 
ATOM   2447 C C   . LEU A 1 317 ? 8.874  0.780   1.330   1.00 24.01 ? 317 LEU A C   1 
ATOM   2448 O O   . LEU A 1 317 ? 9.048  0.192   2.402   1.00 21.10 ? 317 LEU A O   1 
ATOM   2449 C CB  . LEU A 1 317 ? 9.735  -0.317  -0.757  1.00 20.06 ? 317 LEU A CB  1 
ATOM   2450 C CG  . LEU A 1 317 ? 9.546  -1.519  -1.694  1.00 25.64 ? 317 LEU A CG  1 
ATOM   2451 C CD1 . LEU A 1 317 ? 10.745 -1.665  -2.629  1.00 24.12 ? 317 LEU A CD1 1 
ATOM   2452 C CD2 . LEU A 1 317 ? 9.351  -2.804  -0.854  1.00 31.38 ? 317 LEU A CD2 1 
ATOM   2453 N N   . LEU A 1 318 ? 8.994  2.104   1.227   1.00 20.98 ? 318 LEU A N   1 
ATOM   2454 C CA  . LEU A 1 318 ? 9.267  2.913   2.412   1.00 22.87 ? 318 LEU A CA  1 
ATOM   2455 C C   . LEU A 1 318 ? 8.070  2.917   3.356   1.00 22.70 ? 318 LEU A C   1 
ATOM   2456 O O   . LEU A 1 318 ? 8.233  2.920   4.584   1.00 23.46 ? 318 LEU A O   1 
ATOM   2457 C CB  . LEU A 1 318 ? 9.643  4.333   1.984   1.00 22.72 ? 318 LEU A CB  1 
ATOM   2458 C CG  . LEU A 1 318 ? 11.009 4.446   1.307   1.00 26.76 ? 318 LEU A CG  1 
ATOM   2459 C CD1 . LEU A 1 318 ? 11.129 5.800   0.628   1.00 34.09 ? 318 LEU A CD1 1 
ATOM   2460 C CD2 . LEU A 1 318 ? 12.117 4.280   2.346   1.00 31.46 ? 318 LEU A CD2 1 
ATOM   2461 N N   . GLY A 1 319 ? 6.853  2.877   2.811   1.00 22.62 ? 319 GLY A N   1 
ATOM   2462 C CA  . GLY A 1 319 ? 5.699  2.649   3.677   1.00 23.40 ? 319 GLY A CA  1 
ATOM   2463 C C   . GLY A 1 319 ? 5.834  1.373   4.490   1.00 24.92 ? 319 GLY A C   1 
ATOM   2464 O O   . GLY A 1 319 ? 5.552  1.350   5.691   1.00 27.13 ? 319 GLY A O   1 
ATOM   2465 N N   . GLU A 1 320 ? 6.263  0.284   3.843   1.00 27.30 ? 320 GLU A N   1 
ATOM   2466 C CA  . GLU A 1 320 ? 6.455  -0.978  4.559   1.00 29.02 ? 320 GLU A CA  1 
ATOM   2467 C C   . GLU A 1 320 ? 7.563  -0.858  5.598   1.00 28.94 ? 320 GLU A C   1 
ATOM   2468 O O   . GLU A 1 320 ? 7.412  -1.306  6.741   1.00 28.72 ? 320 GLU A O   1 
ATOM   2469 C CB  . GLU A 1 320 ? 6.785  -2.104  3.569   1.00 30.53 ? 320 GLU A CB  1 
ATOM   2470 C CG  . GLU A 1 320 ? 5.715  -2.370  2.526   1.00 36.04 ? 320 GLU A CG  1 
ATOM   2471 C CD  . GLU A 1 320 ? 6.086  -3.512  1.567   1.00 47.49 ? 320 GLU A CD  1 
ATOM   2472 O OE1 . GLU A 1 320 ? 6.914  -4.374  1.933   1.00 44.66 ? 320 GLU A OE1 1 
ATOM   2473 O OE2 . GLU A 1 320 ? 5.545  -3.551  0.444   1.00 59.94 ? 320 GLU A OE2 1 
ATOM   2474 N N   . LEU A 1 321 ? 8.697  -0.271  5.206   1.00 24.65 ? 321 LEU A N   1 
ATOM   2475 C CA  . LEU A 1 321 ? 9.812  -0.071  6.130   1.00 24.18 ? 321 LEU A CA  1 
ATOM   2476 C C   . LEU A 1 321 ? 9.365  0.677   7.382   1.00 31.68 ? 321 LEU A C   1 
ATOM   2477 O O   . LEU A 1 321 ? 9.613  0.238   8.510   1.00 28.46 ? 321 LEU A O   1 
ATOM   2478 C CB  . LEU A 1 321 ? 10.941 0.694   5.423   1.00 26.61 ? 321 LEU A CB  1 
ATOM   2479 C CG  . LEU A 1 321 ? 12.242 0.904   6.209   1.00 34.94 ? 321 LEU A CG  1 
ATOM   2480 C CD1 . LEU A 1 321 ? 13.019 -0.424  6.325   1.00 29.83 ? 321 LEU A CD1 1 
ATOM   2481 C CD2 . LEU A 1 321 ? 13.098 1.988   5.571   1.00 29.74 ? 321 LEU A CD2 1 
ATOM   2482 N N   . PHE A 1 322 ? 8.696  1.815   7.208   1.00 26.12 ? 322 PHE A N   1 
ATOM   2483 C CA  . PHE A 1 322 ? 8.292  2.576   8.380   1.00 25.94 ? 322 PHE A CA  1 
ATOM   2484 C C   . PHE A 1 322 ? 7.191  1.877   9.172   1.00 27.06 ? 322 PHE A C   1 
ATOM   2485 O O   . PHE A 1 322 ? 7.160  1.975   10.411  1.00 33.84 ? 322 PHE A O   1 
ATOM   2486 C CB  . PHE A 1 322 ? 7.879  3.982   7.964   1.00 28.97 ? 322 PHE A CB  1 
ATOM   2487 C CG  . PHE A 1 322 ? 9.052  4.882   7.671   1.00 30.72 ? 322 PHE A CG  1 
ATOM   2488 C CD1 . PHE A 1 322 ? 9.861  5.330   8.708   1.00 44.58 ? 322 PHE A CD1 1 
ATOM   2489 C CD2 . PHE A 1 322 ? 9.344  5.282   6.378   1.00 37.29 ? 322 PHE A CD2 1 
ATOM   2490 C CE1 . PHE A 1 322 ? 10.949 6.158   8.449   1.00 51.45 ? 322 PHE A CE1 1 
ATOM   2491 C CE2 . PHE A 1 322 ? 10.433 6.110   6.118   1.00 44.34 ? 322 PHE A CE2 1 
ATOM   2492 C CZ  . PHE A 1 322 ? 11.232 6.545   7.157   1.00 47.27 ? 322 PHE A CZ  1 
ATOM   2493 N N   . GLY A 1 323 ? 6.319  1.128   8.504   1.00 29.27 ? 323 GLY A N   1 
ATOM   2494 C CA  . GLY A 1 323 ? 5.284  0.410   9.233   1.00 34.22 ? 323 GLY A CA  1 
ATOM   2495 C C   . GLY A 1 323 ? 5.857  -0.709  10.081  1.00 44.55 ? 323 GLY A C   1 
ATOM   2496 O O   . GLY A 1 323 ? 5.424  -0.922  11.220  1.00 43.91 ? 323 GLY A O   1 
ATOM   2497 N N   . HIS A 1 324 ? 6.850  -1.433  9.546   1.00 42.32 ? 324 HIS A N   1 
ATOM   2498 C CA  . HIS A 1 324 ? 7.554  -2.438  10.344  1.00 47.05 ? 324 HIS A CA  1 
ATOM   2499 C C   . HIS A 1 324 ? 8.290  -1.797  11.503  1.00 44.73 ? 324 HIS A C   1 
ATOM   2500 O O   . HIS A 1 324 ? 8.291  -2.331  12.619  1.00 46.43 ? 324 HIS A O   1 
ATOM   2501 C CB  . HIS A 1 324 ? 8.554  -3.219  9.490   1.00 39.34 ? 324 HIS A CB  1 
ATOM   2502 C CG  . HIS A 1 324 ? 7.923  -4.052  8.431   1.00 41.85 ? 324 HIS A CG  1 
ATOM   2503 N ND1 . HIS A 1 324 ? 8.633  -4.557  7.361   1.00 49.87 ? 324 HIS A ND1 1 
ATOM   2504 C CD2 . HIS A 1 324 ? 6.643  -4.459  8.261   1.00 56.48 ? 324 HIS A CD2 1 
ATOM   2505 C CE1 . HIS A 1 324 ? 7.816  -5.240  6.581   1.00 52.51 ? 324 HIS A CE1 1 
ATOM   2506 N NE2 . HIS A 1 324 ? 6.601  -5.191  7.099   1.00 52.19 ? 324 HIS A NE2 1 
ATOM   2507 N N   . LEU A 1 325 ? 8.955  -0.670  11.250  1.00 35.76 ? 325 LEU A N   1 
ATOM   2508 C CA  . LEU A 1 325 ? 9.683  0.003   12.315  1.00 40.82 ? 325 LEU A CA  1 
ATOM   2509 C C   . LEU A 1 325 ? 8.742  0.441   13.432  1.00 54.32 ? 325 LEU A C   1 
ATOM   2510 O O   . LEU A 1 325 ? 9.048  0.272   14.620  1.00 48.32 ? 325 LEU A O   1 
ATOM   2511 C CB  . LEU A 1 325 ? 10.441 1.191   11.740  1.00 35.84 ? 325 LEU A CB  1 
ATOM   2512 C CG  . LEU A 1 325 ? 11.159 2.103   12.722  1.00 40.66 ? 325 LEU A CG  1 
ATOM   2513 C CD1 . LEU A 1 325 ? 11.945 1.274   13.732  1.00 57.17 ? 325 LEU A CD1 1 
ATOM   2514 C CD2 . LEU A 1 325 ? 12.079 3.060   11.992  1.00 44.64 ? 325 LEU A CD2 1 
ATOM   2515 N N   . GLU A 1 326 ? 7.587  0.999   13.069  1.00 40.34 ? 326 GLU A N   1 
ATOM   2516 C CA  . GLU A 1 326 ? 6.593  1.353   14.076  1.00 43.74 ? 326 GLU A CA  1 
ATOM   2517 C C   . GLU A 1 326 ? 6.176  0.131   14.892  1.00 47.92 ? 326 GLU A C   1 
ATOM   2518 O O   . GLU A 1 326 ? 6.045  0.213   16.119  1.00 53.29 ? 326 GLU A O   1 
ATOM   2519 C CB  . GLU A 1 326 ? 5.383  1.995   13.397  1.00 42.21 ? 326 GLU A CB  1 
ATOM   2520 C CG  . GLU A 1 326 ? 4.432  2.679   14.342  1.00 56.73 ? 326 GLU A CG  1 
ATOM   2521 C CD  . GLU A 1 326 ? 3.130  3.073   13.676  1.00 53.62 ? 326 GLU A CD  1 
ATOM   2522 O OE1 . GLU A 1 326 ? 2.989  2.871   12.446  1.00 59.07 ? 326 GLU A OE1 1 
ATOM   2523 O OE2 . GLU A 1 326 ? 2.245  3.580   14.401  1.00 68.17 ? 326 GLU A OE2 1 
ATOM   2524 N N   . GLU A 1 327 ? 5.983  -1.016  14.227  1.00 49.03 ? 327 GLU A N   1 
ATOM   2525 C CA  . GLU A 1 327 ? 5.565  -2.238  14.914  1.00 57.13 ? 327 GLU A CA  1 
ATOM   2526 C C   . GLU A 1 327 ? 6.622  -2.718  15.901  1.00 59.43 ? 327 GLU A C   1 
ATOM   2527 O O   . GLU A 1 327 ? 6.291  -3.139  17.015  1.00 63.74 ? 327 GLU A O   1 
ATOM   2528 C CB  . GLU A 1 327 ? 5.259  -3.341  13.899  1.00 50.55 ? 327 GLU A CB  1 
ATOM   2529 C CG  . GLU A 1 327 ? 3.993  -3.126  13.082  1.00 62.67 ? 327 GLU A CG  1 
ATOM   2530 C CD  . GLU A 1 327 ? 4.033  -3.856  11.747  1.00 77.67 ? 327 GLU A CD  1 
ATOM   2531 O OE1 . GLU A 1 327 ? 4.849  -4.793  11.602  1.00 70.66 ? 327 GLU A OE1 1 
ATOM   2532 O OE2 . GLU A 1 327 ? 3.259  -3.483  10.837  1.00 92.61 ? 327 GLU A OE2 1 
ATOM   2533 N N   . ARG A 1 328 ? 7.894  -2.682  15.509  1.00 61.36 ? 328 ARG A N   1 
ATOM   2534 C CA  . ARG A 1 328 ? 8.976  -3.019  16.427  1.00 61.18 ? 328 ARG A CA  1 
ATOM   2535 C C   . ARG A 1 328 ? 9.270  -1.903  17.417  1.00 66.45 ? 328 ARG A C   1 
ATOM   2536 O O   . ARG A 1 328 ? 10.121 -2.084  18.296  1.00 74.44 ? 328 ARG A O   1 
ATOM   2537 C CB  . ARG A 1 328 ? 10.249 -3.372  15.649  1.00 61.58 ? 328 ARG A CB  1 
ATOM   2538 C CG  . ARG A 1 328 ? 10.087 -4.556  14.695  1.00 67.08 ? 328 ARG A CG  1 
ATOM   2539 C CD  . ARG A 1 328 ? 11.405 -4.923  14.031  1.00 61.44 ? 328 ARG A CD  1 
ATOM   2540 N NE  . ARG A 1 328 ? 12.029 -3.766  13.404  1.00 66.89 ? 328 ARG A NE  1 
ATOM   2541 C CZ  . ARG A 1 328 ? 11.833 -3.402  12.143  1.00 61.08 ? 328 ARG A CZ  1 
ATOM   2542 N NH1 . ARG A 1 328 ? 11.067 -4.113  11.331  1.00 55.32 ? 328 ARG A NH1 1 
ATOM   2543 N NH2 . ARG A 1 328 ? 12.415 -2.294  11.688  1.00 46.12 ? 328 ARG A NH2 1 
ATOM   2544 N N   . ILE A 1 329 ? 8.576  -0.774  17.305  1.00 73.35 ? 329 ILE A N   1 
ATOM   2545 C CA  . ILE A 1 329 ? 8.681  0.350   18.238  1.00 71.40 ? 329 ILE A CA  1 
ATOM   2546 C C   . ILE A 1 329 ? 10.082 0.948   18.209  1.00 69.67 ? 329 ILE A C   1 
ATOM   2547 O O   . ILE A 1 329 ? 10.316 1.952   17.533  1.00 73.00 ? 329 ILE A O   1 
ATOM   2548 C CB  . ILE A 1 329 ? 8.288  -0.059  19.671  1.00 69.92 ? 329 ILE A CB  1 
ATOM   2549 C CG1 . ILE A 1 329 ? 6.998  -0.884  19.665  1.00 69.41 ? 329 ILE A CG1 1 
ATOM   2550 C CG2 . ILE A 1 329 ? 8.128  1.172   20.541  1.00 62.23 ? 329 ILE A CG2 1 
ATOM   2551 C CD1 . ILE A 1 329 ? 5.768  -0.122  19.238  1.00 65.25 ? 329 ILE A CD1 1 
HETATM 2552 C C1  . GOL B 2 .   ? 7.156  21.052  -47.261 1.00 39.82 ? 401 GOL A C1  1 
HETATM 2553 O O1  . GOL B 2 .   ? 5.891  21.416  -46.747 1.00 43.75 ? 401 GOL A O1  1 
HETATM 2554 C C2  . GOL B 2 .   ? 7.494  21.965  -48.421 1.00 45.13 ? 401 GOL A C2  1 
HETATM 2555 O O2  . GOL B 2 .   ? 7.550  23.299  -47.951 1.00 49.41 ? 401 GOL A O2  1 
HETATM 2556 C C3  . GOL B 2 .   ? 8.791  21.541  -49.109 1.00 29.72 ? 401 GOL A C3  1 
HETATM 2557 O O3  . GOL B 2 .   ? 9.149  22.554  -50.018 1.00 38.34 ? 401 GOL A O3  1 
HETATM 2558 C C1  . GOL C 2 .   ? 7.842  18.688  -14.805 1.00 81.86 ? 402 GOL A C1  1 
HETATM 2559 O O1  . GOL C 2 .   ? 8.466  19.539  -15.739 1.00 76.10 ? 402 GOL A O1  1 
HETATM 2560 C C2  . GOL C 2 .   ? 8.146  17.256  -15.181 1.00 79.53 ? 402 GOL A C2  1 
HETATM 2561 O O2  . GOL C 2 .   ? 7.860  16.394  -14.100 1.00 82.35 ? 402 GOL A O2  1 
HETATM 2562 C C3  . GOL C 2 .   ? 7.434  16.841  -16.459 1.00 76.07 ? 402 GOL A C3  1 
HETATM 2563 O O3  . GOL C 2 .   ? 8.080  15.681  -16.938 1.00 74.42 ? 402 GOL A O3  1 
HETATM 2564 C C1  . GOL D 2 .   ? 16.586 29.037  -51.874 1.00 64.81 ? 403 GOL A C1  1 
HETATM 2565 O O1  . GOL D 2 .   ? 15.842 28.201  -52.728 1.00 69.87 ? 403 GOL A O1  1 
HETATM 2566 C C2  . GOL D 2 .   ? 16.222 28.771  -50.426 1.00 62.07 ? 403 GOL A C2  1 
HETATM 2567 O O2  . GOL D 2 .   ? 14.817 28.765  -50.244 1.00 63.79 ? 403 GOL A O2  1 
HETATM 2568 C C3  . GOL D 2 .   ? 16.855 27.485  -49.927 1.00 63.06 ? 403 GOL A C3  1 
HETATM 2569 O O3  . GOL D 2 .   ? 17.979 27.729  -49.106 1.00 54.19 ? 403 GOL A O3  1 
HETATM 2570 C C1  . GOL E 2 .   ? 15.766 20.075  -57.035 1.00 60.48 ? 404 GOL A C1  1 
HETATM 2571 O O1  . GOL E 2 .   ? 16.179 20.668  -55.808 1.00 36.89 ? 404 GOL A O1  1 
HETATM 2572 C C2  . GOL E 2 .   ? 16.741 20.297  -58.183 1.00 50.27 ? 404 GOL A C2  1 
HETATM 2573 O O2  . GOL E 2 .   ? 17.018 21.680  -58.284 1.00 47.08 ? 404 GOL A O2  1 
HETATM 2574 C C3  . GOL E 2 .   ? 16.159 19.796  -59.506 1.00 66.71 ? 404 GOL A C3  1 
HETATM 2575 O O3  . GOL E 2 .   ? 16.772 18.594  -59.953 1.00 52.06 ? 404 GOL A O3  1 
HETATM 2576 C C1  . PEG F 3 .   ? 6.939  14.438  -11.630 1.00 86.71 ? 405 PEG A C1  1 
HETATM 2577 O O1  . PEG F 3 .   ? 6.094  15.078  -10.697 1.00 90.40 ? 405 PEG A O1  1 
HETATM 2578 C C2  . PEG F 3 .   ? 7.793  13.402  -10.937 1.00 86.84 ? 405 PEG A C2  1 
HETATM 2579 O O2  . PEG F 3 .   ? 8.600  14.003  -9.956  1.00 90.76 ? 405 PEG A O2  1 
HETATM 2580 C C3  . PEG F 3 .   ? 9.478  13.093  -9.343  1.00 75.66 ? 405 PEG A C3  1 
HETATM 2581 C C4  . PEG F 3 .   ? 10.306 13.791  -8.289  1.00 79.05 ? 405 PEG A C4  1 
HETATM 2582 O O4  . PEG F 3 .   ? 11.094 12.851  -7.593  1.00 65.44 ? 405 PEG A O4  1 
HETATM 2583 O O   . HOH G 4 .   ? 11.721 -2.587  -12.968 1.00 41.48 ? 501 HOH A O   1 
HETATM 2584 O O   . HOH G 4 .   ? 9.159  -10.114 -40.766 1.00 47.10 ? 502 HOH A O   1 
HETATM 2585 O O   . HOH G 4 .   ? 5.202  -2.092  -1.401  1.00 42.54 ? 503 HOH A O   1 
HETATM 2586 O O   . HOH G 4 .   ? 21.518 1.190   -55.683 1.00 52.31 ? 504 HOH A O   1 
HETATM 2587 O O   . HOH G 4 .   ? 20.986 15.051  -15.889 1.00 44.55 ? 505 HOH A O   1 
HETATM 2588 O O   . HOH G 4 .   ? 27.189 11.204  -54.045 1.00 48.85 ? 506 HOH A O   1 
HETATM 2589 O O   . HOH G 4 .   ? 25.588 6.716   -19.875 1.00 56.87 ? 507 HOH A O   1 
HETATM 2590 O O   . HOH G 4 .   ? 26.367 12.880  -57.763 1.00 39.93 ? 508 HOH A O   1 
HETATM 2591 O O   . HOH G 4 .   ? 5.576  10.172  -19.878 1.00 41.09 ? 509 HOH A O   1 
HETATM 2592 O O   . HOH G 4 .   ? 24.560 13.102  -29.496 1.00 42.50 ? 510 HOH A O   1 
HETATM 2593 O O   . HOH G 4 .   ? 7.477  13.245  -39.856 1.00 45.82 ? 511 HOH A O   1 
HETATM 2594 O O   . HOH G 4 .   ? 26.448 26.718  -56.058 1.00 46.75 ? 512 HOH A O   1 
HETATM 2595 O O   . HOH G 4 .   ? 9.291  -12.706 -33.022 1.00 35.53 ? 513 HOH A O   1 
HETATM 2596 O O   . HOH G 4 .   ? 21.673 3.129   -18.152 1.00 37.80 ? 514 HOH A O   1 
HETATM 2597 O O   . HOH G 4 .   ? 12.632 -6.286  11.255  1.00 60.55 ? 515 HOH A O   1 
HETATM 2598 O O   . HOH G 4 .   ? 8.700  6.470   -31.862 1.00 37.09 ? 516 HOH A O   1 
HETATM 2599 O O   . HOH G 4 .   ? 22.177 1.645   -11.161 1.00 30.70 ? 517 HOH A O   1 
HETATM 2600 O O   . HOH G 4 .   ? 23.946 -16.962 -1.392  1.00 56.23 ? 518 HOH A O   1 
HETATM 2601 O O   . HOH G 4 .   ? 23.144 9.120   -14.352 1.00 46.68 ? 519 HOH A O   1 
HETATM 2602 O O   . HOH G 4 .   ? 24.775 28.647  -37.157 1.00 43.42 ? 520 HOH A O   1 
HETATM 2603 O O   . HOH G 4 .   ? 16.391 11.447  -64.074 1.00 46.07 ? 521 HOH A O   1 
HETATM 2604 O O   . HOH G 4 .   ? 5.128  17.112  -45.205 1.00 58.80 ? 522 HOH A O   1 
HETATM 2605 O O   . HOH G 4 .   ? 15.336 -3.602  -13.914 1.00 29.45 ? 523 HOH A O   1 
HETATM 2606 O O   . HOH G 4 .   ? 27.444 22.758  -48.785 1.00 34.90 ? 524 HOH A O   1 
HETATM 2607 O O   . HOH G 4 .   ? 27.264 -3.274  -27.713 1.00 44.07 ? 525 HOH A O   1 
HETATM 2608 O O   . HOH G 4 .   ? 25.507 20.570  -31.348 1.00 48.39 ? 526 HOH A O   1 
HETATM 2609 O O   . HOH G 4 .   ? 12.279 -15.627 -13.667 1.00 37.47 ? 527 HOH A O   1 
HETATM 2610 O O   . HOH G 4 .   ? 10.281 27.625  -38.261 1.00 40.45 ? 528 HOH A O   1 
HETATM 2611 O O   . HOH G 4 .   ? 7.736  9.546   -51.205 1.00 39.14 ? 529 HOH A O   1 
HETATM 2612 O O   . HOH G 4 .   ? 23.873 8.845   -19.565 1.00 43.30 ? 530 HOH A O   1 
HETATM 2613 O O   . HOH G 4 .   ? 22.369 0.874   -23.772 1.00 48.73 ? 531 HOH A O   1 
HETATM 2614 O O   . HOH G 4 .   ? 6.269  12.539  -21.058 1.00 40.46 ? 532 HOH A O   1 
HETATM 2615 O O   . HOH G 4 .   ? 11.450 -8.719  -26.283 1.00 30.49 ? 533 HOH A O   1 
HETATM 2616 O O   . HOH G 4 .   ? 23.602 3.017   -41.893 1.00 32.72 ? 534 HOH A O   1 
HETATM 2617 O O   . HOH G 4 .   ? 21.890 21.935  -25.690 1.00 49.78 ? 535 HOH A O   1 
HETATM 2618 O O   . HOH G 4 .   ? 16.084 3.420   -23.018 1.00 21.97 ? 536 HOH A O   1 
HETATM 2619 O O   . HOH G 4 .   ? 17.834 27.037  -54.055 1.00 40.46 ? 537 HOH A O   1 
HETATM 2620 O O   . HOH G 4 .   ? 12.541 25.647  -32.465 1.00 39.61 ? 538 HOH A O   1 
HETATM 2621 O O   . HOH G 4 .   ? 21.565 -13.425 -25.331 1.00 38.30 ? 539 HOH A O   1 
HETATM 2622 O O   . HOH G 4 .   ? 7.056  17.930  -32.077 1.00 51.59 ? 540 HOH A O   1 
HETATM 2623 O O   . HOH G 4 .   ? 8.053  22.922  -52.424 1.00 44.16 ? 541 HOH A O   1 
HETATM 2624 O O   . HOH G 4 .   ? 6.144  5.338   -57.670 1.00 40.60 ? 542 HOH A O   1 
HETATM 2625 O O   . HOH G 4 .   ? 25.073 7.156   -34.502 1.00 53.90 ? 543 HOH A O   1 
HETATM 2626 O O   . HOH G 4 .   ? 9.264  0.716   -18.843 1.00 29.13 ? 544 HOH A O   1 
HETATM 2627 O O   . HOH G 4 .   ? 14.179 -4.764  -46.243 1.00 33.97 ? 545 HOH A O   1 
HETATM 2628 O O   . HOH G 4 .   ? 22.057 28.313  -33.247 1.00 39.36 ? 546 HOH A O   1 
HETATM 2629 O O   . HOH G 4 .   ? 11.448 -1.684  9.229   1.00 36.52 ? 547 HOH A O   1 
HETATM 2630 O O   . HOH G 4 .   ? 26.942 13.186  -51.472 1.00 36.05 ? 548 HOH A O   1 
HETATM 2631 O O   . HOH G 4 .   ? 15.953 21.129  -51.775 1.00 28.71 ? 549 HOH A O   1 
HETATM 2632 O O   . HOH G 4 .   ? 9.902  26.474  -51.480 1.00 41.76 ? 550 HOH A O   1 
HETATM 2633 O O   . HOH G 4 .   ? 19.750 -4.957  -2.964  1.00 30.81 ? 551 HOH A O   1 
HETATM 2634 O O   . HOH G 4 .   ? 0.301  3.296   -1.440  1.00 29.96 ? 552 HOH A O   1 
HETATM 2635 O O   . HOH G 4 .   ? 9.698  -4.715  -22.446 1.00 33.26 ? 553 HOH A O   1 
HETATM 2636 O O   . HOH G 4 .   ? 14.114 0.206   -25.220 1.00 20.35 ? 554 HOH A O   1 
HETATM 2637 O O   . HOH G 4 .   ? 13.458 22.166  -55.539 1.00 37.04 ? 555 HOH A O   1 
HETATM 2638 O O   . HOH G 4 .   ? 21.746 0.656   -21.924 1.00 39.50 ? 556 HOH A O   1 
HETATM 2639 O O   . HOH G 4 .   ? 14.824 -17.597 -20.129 1.00 46.16 ? 557 HOH A O   1 
HETATM 2640 O O   . HOH G 4 .   ? 17.943 18.750  -15.479 1.00 39.35 ? 558 HOH A O   1 
HETATM 2641 O O   . HOH G 4 .   ? 23.223 33.946  -37.075 1.00 41.69 ? 559 HOH A O   1 
HETATM 2642 O O   . HOH G 4 .   ? 21.790 2.848   -6.944  1.00 42.37 ? 560 HOH A O   1 
HETATM 2643 O O   . HOH G 4 .   ? 13.794 -15.151 -25.775 1.00 32.81 ? 561 HOH A O   1 
HETATM 2644 O O   . HOH G 4 .   ? 28.297 18.415  -60.430 1.00 54.51 ? 562 HOH A O   1 
HETATM 2645 O O   . HOH G 4 .   ? 7.504  -3.946  -3.909  1.00 32.65 ? 563 HOH A O   1 
HETATM 2646 O O   . HOH G 4 .   ? 13.652 8.822   -62.450 1.00 58.34 ? 564 HOH A O   1 
HETATM 2647 O O   . HOH G 4 .   ? 25.294 -9.436  -28.007 1.00 51.17 ? 565 HOH A O   1 
HETATM 2648 O O   . HOH G 4 .   ? 5.273  -6.057  -37.382 1.00 46.08 ? 566 HOH A O   1 
HETATM 2649 O O   . HOH G 4 .   ? 11.203 8.087   -59.817 1.00 49.38 ? 567 HOH A O   1 
HETATM 2650 O O   . HOH G 4 .   ? 15.383 25.655  -32.023 1.00 43.47 ? 568 HOH A O   1 
HETATM 2651 O O   . HOH G 4 .   ? 13.889 17.937  -58.724 1.00 39.29 ? 569 HOH A O   1 
HETATM 2652 O O   . HOH G 4 .   ? 9.527  23.377  -15.822 1.00 67.22 ? 570 HOH A O   1 
HETATM 2653 O O   . HOH G 4 .   ? 16.252 -6.994  -42.531 1.00 34.67 ? 571 HOH A O   1 
HETATM 2654 O O   . HOH G 4 .   ? 22.910 26.901  -42.865 1.00 34.68 ? 572 HOH A O   1 
HETATM 2655 O O   . HOH G 4 .   ? 22.957 20.123  -43.589 1.00 32.08 ? 573 HOH A O   1 
HETATM 2656 O O   . HOH G 4 .   ? 21.080 0.984   -4.872  1.00 29.89 ? 574 HOH A O   1 
HETATM 2657 O O   . HOH G 4 .   ? 25.058 14.238  -44.456 1.00 35.21 ? 575 HOH A O   1 
HETATM 2658 O O   . HOH G 4 .   ? 10.104 10.692  -39.719 1.00 34.00 ? 576 HOH A O   1 
HETATM 2659 O O   . HOH G 4 .   ? 9.415  -8.347  -43.106 1.00 44.06 ? 577 HOH A O   1 
HETATM 2660 O O   . HOH G 4 .   ? 21.185 -6.701  -45.964 1.00 43.18 ? 578 HOH A O   1 
HETATM 2661 O O   . HOH G 4 .   ? 5.413  18.283  -19.832 1.00 64.62 ? 579 HOH A O   1 
HETATM 2662 O O   . HOH G 4 .   ? 14.389 -10.398 -37.884 1.00 45.37 ? 580 HOH A O   1 
HETATM 2663 O O   . HOH G 4 .   ? 7.877  4.028   -38.763 1.00 35.36 ? 581 HOH A O   1 
HETATM 2664 O O   . HOH G 4 .   ? 18.552 -9.238  -37.945 1.00 29.03 ? 582 HOH A O   1 
HETATM 2665 O O   . HOH G 4 .   ? 22.500 33.507  -45.271 1.00 45.65 ? 583 HOH A O   1 
HETATM 2666 O O   . HOH G 4 .   ? 24.582 -13.108 -19.405 1.00 42.15 ? 584 HOH A O   1 
HETATM 2667 O O   . HOH G 4 .   ? 18.246 -13.253 -43.456 1.00 48.21 ? 585 HOH A O   1 
HETATM 2668 O O   . HOH G 4 .   ? 6.824  -8.532  -37.379 1.00 42.19 ? 586 HOH A O   1 
HETATM 2669 O O   . HOH G 4 .   ? 8.181  -13.385 -10.122 1.00 33.70 ? 587 HOH A O   1 
HETATM 2670 O O   . HOH G 4 .   ? 6.617  9.782   -43.991 1.00 39.99 ? 588 HOH A O   1 
HETATM 2671 O O   . HOH G 4 .   ? 1.306  0.960   -52.500 1.00 39.02 ? 589 HOH A O   1 
HETATM 2672 O O   . HOH G 4 .   ? 22.088 7.229   -12.608 1.00 41.10 ? 590 HOH A O   1 
HETATM 2673 O O   . HOH G 4 .   ? 24.772 8.762   -62.145 1.00 55.80 ? 591 HOH A O   1 
HETATM 2674 O O   . HOH G 4 .   ? 24.475 4.538   -29.899 1.00 44.28 ? 592 HOH A O   1 
HETATM 2675 O O   . HOH G 4 .   ? 12.665 27.788  -48.797 1.00 55.32 ? 593 HOH A O   1 
HETATM 2676 O O   . HOH G 4 .   ? 28.715 0.421   -37.673 1.00 45.71 ? 594 HOH A O   1 
HETATM 2677 O O   . HOH G 4 .   ? 6.525  7.895   -39.170 1.00 38.35 ? 595 HOH A O   1 
HETATM 2678 O O   . HOH G 4 .   ? 10.198 22.896  -54.770 1.00 49.23 ? 596 HOH A O   1 
HETATM 2679 O O   . HOH G 4 .   ? 25.851 -12.080 -12.510 1.00 50.98 ? 597 HOH A O   1 
HETATM 2680 O O   . HOH G 4 .   ? 22.179 25.636  -32.209 1.00 37.96 ? 598 HOH A O   1 
HETATM 2681 O O   . HOH G 4 .   ? 13.885 -8.751  0.068   1.00 31.26 ? 599 HOH A O   1 
HETATM 2682 O O   . HOH G 4 .   ? 8.493  -5.681  3.805   1.00 44.68 ? 600 HOH A O   1 
HETATM 2683 O O   . HOH G 4 .   ? 18.433 21.819  -27.630 1.00 41.53 ? 601 HOH A O   1 
HETATM 2684 O O   . HOH G 4 .   ? 21.025 32.794  -49.394 1.00 48.96 ? 602 HOH A O   1 
HETATM 2685 O O   . HOH G 4 .   ? 6.226  -12.396 -11.428 1.00 47.16 ? 603 HOH A O   1 
HETATM 2686 O O   . HOH G 4 .   ? 6.051  -1.687  -14.932 1.00 40.51 ? 604 HOH A O   1 
HETATM 2687 O O   . HOH G 4 .   ? 25.330 27.438  -46.091 1.00 45.35 ? 605 HOH A O   1 
HETATM 2688 O O   . HOH G 4 .   ? 18.120 4.586   -32.731 1.00 25.80 ? 606 HOH A O   1 
HETATM 2689 O O   . HOH G 4 .   ? 18.672 31.069  -50.546 1.00 53.52 ? 607 HOH A O   1 
HETATM 2690 O O   . HOH G 4 .   ? 21.182 -8.300  0.573   1.00 47.08 ? 608 HOH A O   1 
HETATM 2691 O O   . HOH G 4 .   ? 6.469  6.345   -25.584 1.00 36.60 ? 609 HOH A O   1 
HETATM 2692 O O   . HOH G 4 .   ? 18.417 3.044   -55.910 1.00 37.46 ? 610 HOH A O   1 
HETATM 2693 O O   . HOH G 4 .   ? 10.587 -6.210  -25.931 1.00 26.62 ? 611 HOH A O   1 
HETATM 2694 O O   . HOH G 4 .   ? 27.233 25.555  -58.328 1.00 58.18 ? 612 HOH A O   1 
HETATM 2695 O O   . HOH G 4 .   ? 24.962 12.520  4.161   1.00 49.36 ? 613 HOH A O   1 
HETATM 2696 O O   . HOH G 4 .   ? 20.473 -19.503 -2.992  1.00 52.08 ? 614 HOH A O   1 
HETATM 2697 O O   . HOH G 4 .   ? 24.997 -3.727  -45.466 1.00 42.85 ? 615 HOH A O   1 
HETATM 2698 O O   . HOH G 4 .   ? 21.833 9.754   -10.880 1.00 56.50 ? 616 HOH A O   1 
HETATM 2699 O O   . HOH G 4 .   ? 22.679 24.667  -44.650 1.00 30.10 ? 617 HOH A O   1 
HETATM 2700 O O   . HOH G 4 .   ? 9.249  4.667   -30.599 1.00 37.64 ? 618 HOH A O   1 
HETATM 2701 O O   . HOH G 4 .   ? 9.872  1.133   -13.984 1.00 32.76 ? 619 HOH A O   1 
HETATM 2702 O O   . HOH G 4 .   ? 10.013 -17.056 -20.327 1.00 42.70 ? 620 HOH A O   1 
HETATM 2703 O O   . HOH G 4 .   ? 19.910 -2.341  -13.579 1.00 33.79 ? 621 HOH A O   1 
HETATM 2704 O O   . HOH G 4 .   ? 16.806 9.284   -30.678 1.00 31.18 ? 622 HOH A O   1 
HETATM 2705 O O   . HOH G 4 .   ? 4.605  19.582  -45.035 1.00 55.03 ? 623 HOH A O   1 
HETATM 2706 O O   . HOH G 4 .   ? 22.508 5.702   -36.643 1.00 42.56 ? 624 HOH A O   1 
HETATM 2707 O O   . HOH G 4 .   ? 21.309 14.765  -20.382 1.00 30.43 ? 625 HOH A O   1 
HETATM 2708 O O   . HOH G 4 .   ? 9.279  1.654   -58.303 1.00 47.84 ? 626 HOH A O   1 
HETATM 2709 O O   . HOH G 4 .   ? 7.579  3.144   -41.384 1.00 40.54 ? 627 HOH A O   1 
HETATM 2710 O O   . HOH G 4 .   ? 18.812 8.168   -37.524 1.00 35.03 ? 628 HOH A O   1 
HETATM 2711 O O   . HOH G 4 .   ? 19.399 -13.801 1.266   1.00 33.89 ? 629 HOH A O   1 
HETATM 2712 O O   . HOH G 4 .   ? 11.841 21.099  -9.501  1.00 59.23 ? 630 HOH A O   1 
HETATM 2713 O O   . HOH G 4 .   ? 24.704 20.246  -28.734 1.00 48.43 ? 631 HOH A O   1 
HETATM 2714 O O   . HOH G 4 .   ? 18.986 18.007  -18.052 1.00 39.04 ? 632 HOH A O   1 
HETATM 2715 O O   . HOH G 4 .   ? 12.329 -8.386  -2.420  1.00 26.10 ? 633 HOH A O   1 
HETATM 2716 O O   . HOH G 4 .   ? 16.537 29.542  -35.701 1.00 54.70 ? 634 HOH A O   1 
HETATM 2717 O O   . HOH G 4 .   ? 21.105 -8.212  -43.851 1.00 37.62 ? 635 HOH A O   1 
HETATM 2718 O O   . HOH G 4 .   ? 25.118 24.815  -45.934 1.00 40.65 ? 636 HOH A O   1 
HETATM 2719 O O   . HOH G 4 .   ? 29.086 24.867  -62.827 1.00 44.59 ? 637 HOH A O   1 
HETATM 2720 O O   . HOH G 4 .   ? 13.980 -8.022  7.443   1.00 35.41 ? 638 HOH A O   1 
HETATM 2721 O O   . HOH G 4 .   ? 3.958  -1.180  -4.753  1.00 36.41 ? 639 HOH A O   1 
HETATM 2722 O O   . HOH G 4 .   ? 25.333 -5.754  -38.189 1.00 42.61 ? 640 HOH A O   1 
HETATM 2723 O O   . HOH G 4 .   ? 7.240  10.050  -53.810 1.00 40.69 ? 641 HOH A O   1 
HETATM 2724 O O   . HOH G 4 .   ? 6.644  4.627   -36.001 1.00 36.54 ? 642 HOH A O   1 
HETATM 2725 O O   . HOH G 4 .   ? 8.380  -15.959 -5.188  1.00 40.96 ? 643 HOH A O   1 
HETATM 2726 O O   . HOH G 4 .   ? 8.217  25.367  -44.257 1.00 38.91 ? 644 HOH A O   1 
HETATM 2727 O O   . HOH G 4 .   ? 22.031 -0.958  -51.657 1.00 47.88 ? 645 HOH A O   1 
HETATM 2728 O O   . HOH G 4 .   ? 16.122 -12.114 -36.138 1.00 37.78 ? 646 HOH A O   1 
HETATM 2729 O O   . HOH G 4 .   ? 5.218  8.884   -26.584 1.00 39.94 ? 647 HOH A O   1 
HETATM 2730 O O   . HOH G 4 .   ? 4.826  16.532  -47.649 1.00 59.41 ? 648 HOH A O   1 
HETATM 2731 O O   . HOH G 4 .   ? 22.976 5.814   -32.107 1.00 49.99 ? 649 HOH A O   1 
HETATM 2732 O O   . HOH G 4 .   ? 22.162 13.623  -31.673 1.00 32.01 ? 650 HOH A O   1 
HETATM 2733 O O   . HOH G 4 .   ? 3.352  -9.536  -2.931  1.00 51.33 ? 651 HOH A O   1 
HETATM 2734 O O   . HOH G 4 .   ? 7.638  2.871   -19.295 1.00 23.13 ? 652 HOH A O   1 
HETATM 2735 O O   . HOH G 4 .   ? 25.140 -11.019 -5.869  1.00 49.53 ? 653 HOH A O   1 
HETATM 2736 O O   . HOH G 4 .   ? 12.838 -18.236 -6.906  1.00 37.52 ? 654 HOH A O   1 
HETATM 2737 O O   . HOH G 4 .   ? 18.838 33.395  -37.263 1.00 48.53 ? 655 HOH A O   1 
HETATM 2738 O O   . HOH G 4 .   ? 27.749 -3.655  -35.624 1.00 46.51 ? 656 HOH A O   1 
HETATM 2739 O O   . HOH G 4 .   ? 6.540  -7.994  -7.358  1.00 35.92 ? 657 HOH A O   1 
HETATM 2740 O O   . HOH G 4 .   ? 5.956  -5.212  -1.866  1.00 41.14 ? 658 HOH A O   1 
HETATM 2741 O O   . HOH G 4 .   ? 18.896 -4.000  8.650   1.00 46.44 ? 659 HOH A O   1 
HETATM 2742 O O   . HOH G 4 .   ? 2.934  -4.974  -41.881 1.00 48.76 ? 660 HOH A O   1 
HETATM 2743 O O   . HOH G 4 .   ? 27.044 10.449  -1.549  1.00 48.67 ? 661 HOH A O   1 
HETATM 2744 O O   . HOH G 4 .   ? 7.811  -7.149  -31.235 1.00 38.18 ? 662 HOH A O   1 
HETATM 2745 O O   . HOH G 4 .   ? 6.321  25.315  -49.629 1.00 50.65 ? 663 HOH A O   1 
HETATM 2746 O O   . HOH G 4 .   ? 8.395  22.021  -21.318 1.00 59.88 ? 664 HOH A O   1 
HETATM 2747 O O   . HOH G 4 .   ? 23.891 13.667  -39.521 1.00 37.67 ? 665 HOH A O   1 
HETATM 2748 O O   . HOH G 4 .   ? 11.561 5.448   -29.234 1.00 32.03 ? 666 HOH A O   1 
HETATM 2749 O O   . HOH G 4 .   ? 24.933 -0.318  -25.351 1.00 40.92 ? 667 HOH A O   1 
HETATM 2750 O O   . HOH G 4 .   ? 18.760 -17.858 -29.960 1.00 47.01 ? 668 HOH A O   1 
HETATM 2751 O O   . HOH G 4 .   ? 18.172 6.773   -30.889 1.00 35.60 ? 669 HOH A O   1 
HETATM 2752 O O   . HOH G 4 .   ? 22.675 -7.393  -9.391  1.00 43.52 ? 670 HOH A O   1 
HETATM 2753 O O   . HOH G 4 .   ? 11.186 20.779  -55.847 1.00 41.23 ? 671 HOH A O   1 
HETATM 2754 O O   . HOH G 4 .   ? 7.288  -13.352 -15.752 1.00 43.69 ? 672 HOH A O   1 
HETATM 2755 O O   . HOH G 4 .   ? 16.131 30.637  -40.315 1.00 56.87 ? 673 HOH A O   1 
HETATM 2756 O O   . HOH G 4 .   ? 17.354 22.836  -60.947 1.00 56.25 ? 674 HOH A O   1 
HETATM 2757 O O   . HOH G 4 .   ? 25.456 7.231   -54.970 1.00 51.52 ? 675 HOH A O   1 
HETATM 2758 O O   . HOH G 4 .   ? 20.684 7.091   -33.950 1.00 36.11 ? 676 HOH A O   1 
HETATM 2759 O O   . HOH G 4 .   ? 30.412 12.665  -58.102 1.00 40.71 ? 677 HOH A O   1 
HETATM 2760 O O   . HOH G 4 .   ? 6.231  1.763   -21.288 1.00 36.14 ? 678 HOH A O   1 
HETATM 2761 O O   . HOH G 4 .   ? 24.753 27.592  -52.090 1.00 40.28 ? 679 HOH A O   1 
HETATM 2762 O O   . HOH G 4 .   ? 23.552 -9.243  -43.464 1.00 39.62 ? 680 HOH A O   1 
HETATM 2763 O O   . HOH G 4 .   ? 25.078 -7.680  -23.430 1.00 50.93 ? 681 HOH A O   1 
HETATM 2764 O O   . HOH G 4 .   ? 20.262 4.291   -34.441 1.00 28.50 ? 682 HOH A O   1 
HETATM 2765 O O   . HOH G 4 .   ? 0.344  2.370   -4.866  1.00 44.17 ? 683 HOH A O   1 
HETATM 2766 O O   . HOH G 4 .   ? 26.394 15.084  -28.163 1.00 57.69 ? 684 HOH A O   1 
HETATM 2767 O O   . HOH G 4 .   ? 6.262  -6.880  0.493   1.00 46.96 ? 685 HOH A O   1 
HETATM 2768 O O   . HOH G 4 .   ? 24.195 26.824  -59.929 1.00 47.39 ? 686 HOH A O   1 
HETATM 2769 O O   . HOH G 4 .   ? 25.271 -2.167  -40.503 1.00 45.14 ? 687 HOH A O   1 
HETATM 2770 O O   . HOH G 4 .   ? 26.594 -6.424  -36.002 1.00 48.15 ? 688 HOH A O   1 
HETATM 2771 O O   . HOH G 4 .   ? 26.094 -2.474  -23.721 1.00 51.08 ? 689 HOH A O   1 
HETATM 2772 O O   . HOH G 4 .   ? 17.382 10.103  -27.989 1.00 32.64 ? 690 HOH A O   1 
HETATM 2773 O O   . HOH G 4 .   ? 14.168 23.438  -16.850 1.00 57.66 ? 691 HOH A O   1 
HETATM 2774 O O   . HOH G 4 .   ? 23.250 1.083   0.979   1.00 55.49 ? 692 HOH A O   1 
HETATM 2775 O O   . HOH G 4 .   ? 21.850 -13.019 0.207   1.00 39.67 ? 693 HOH A O   1 
HETATM 2776 O O   . HOH G 4 .   ? 27.471 16.536  -57.621 1.00 34.17 ? 694 HOH A O   1 
HETATM 2777 O O   . HOH G 4 .   ? 23.708 17.512  -25.894 1.00 42.11 ? 695 HOH A O   1 
HETATM 2778 O O   . HOH G 4 .   ? 23.711 4.447   -24.930 1.00 45.18 ? 696 HOH A O   1 
HETATM 2779 O O   . HOH G 4 .   ? 12.235 -17.225 -29.030 1.00 53.72 ? 697 HOH A O   1 
HETATM 2780 O O   . HOH G 4 .   ? 7.955  -16.862 -21.909 1.00 47.44 ? 698 HOH A O   1 
HETATM 2781 O O   . HOH G 4 .   ? 20.954 -11.109 -36.856 1.00 31.71 ? 699 HOH A O   1 
HETATM 2782 O O   . HOH G 4 .   ? 14.506 -1.584  13.763  1.00 45.50 ? 700 HOH A O   1 
HETATM 2783 O O   . HOH G 4 .   ? 25.305 -1.712  -48.010 1.00 50.62 ? 701 HOH A O   1 
HETATM 2784 O O   . HOH G 4 .   ? 24.599 21.722  -63.949 1.00 44.73 ? 702 HOH A O   1 
HETATM 2785 O O   . HOH G 4 .   ? 23.035 2.202   -25.486 1.00 47.03 ? 703 HOH A O   1 
HETATM 2786 O O   . HOH G 4 .   ? 28.784 18.859  -63.377 1.00 47.19 ? 704 HOH A O   1 
HETATM 2787 O O   . HOH G 4 .   ? 19.915 5.893   -41.555 1.00 38.65 ? 705 HOH A O   1 
HETATM 2788 O O   . HOH G 4 .   ? 5.234  -0.204  -25.132 1.00 38.68 ? 706 HOH A O   1 
HETATM 2789 O O   . HOH G 4 .   ? 23.346 29.718  -56.351 1.00 48.25 ? 707 HOH A O   1 
HETATM 2790 O O   . HOH G 4 .   ? 16.075 -16.902 0.908   1.00 43.16 ? 708 HOH A O   1 
HETATM 2791 O O   . HOH G 4 .   ? 20.399 12.447  -63.678 1.00 41.62 ? 709 HOH A O   1 
HETATM 2792 O O   . HOH G 4 .   ? 6.722  13.399  -14.710 1.00 52.13 ? 710 HOH A O   1 
HETATM 2793 O O   . HOH G 4 .   ? 8.240  -20.900 -4.320  1.00 56.56 ? 711 HOH A O   1 
HETATM 2794 O O   . HOH G 4 .   ? 13.571 -16.325 1.584   1.00 44.99 ? 712 HOH A O   1 
HETATM 2795 O O   . HOH G 4 .   ? 8.987  -4.822  -27.356 1.00 44.64 ? 713 HOH A O   1 
HETATM 2796 O O   . HOH G 4 .   ? 24.841 10.538  -28.248 1.00 42.11 ? 714 HOH A O   1 
HETATM 2797 O O   . HOH G 4 .   ? 6.866  -7.697  -43.957 1.00 44.39 ? 715 HOH A O   1 
HETATM 2798 O O   . HOH G 4 .   ? 20.804 17.015  -21.700 1.00 38.59 ? 716 HOH A O   1 
HETATM 2799 O O   . HOH G 4 .   ? 22.111 2.918   -0.105  1.00 52.33 ? 717 HOH A O   1 
HETATM 2800 O O   . HOH G 4 .   ? 6.687  -11.500 -14.005 1.00 42.16 ? 718 HOH A O   1 
HETATM 2801 O O   . HOH G 4 .   ? 6.579  0.887   -45.000 1.00 46.99 ? 719 HOH A O   1 
HETATM 2802 O O   . HOH G 4 .   ? 18.132 -11.770 2.782   1.00 41.52 ? 720 HOH A O   1 
HETATM 2803 O O   . HOH G 4 .   ? 26.794 28.489  -41.577 1.00 53.28 ? 721 HOH A O   1 
HETATM 2804 O O   . HOH G 4 .   ? 6.328  -1.603  -3.684  1.00 31.36 ? 722 HOH A O   1 
HETATM 2805 O O   . HOH G 4 .   ? 16.732 -10.325 -39.707 1.00 41.34 ? 723 HOH A O   1 
HETATM 2806 O O   . HOH G 4 .   ? 10.102 -15.506 -27.469 1.00 45.68 ? 724 HOH A O   1 
HETATM 2807 O O   . HOH G 4 .   ? 14.288 -3.648  15.737  1.00 62.65 ? 725 HOH A O   1 
HETATM 2808 O O   . HOH G 4 .   ? 8.248  0.268   -15.944 1.00 35.13 ? 726 HOH A O   1 
HETATM 2809 O O   . HOH G 4 .   ? 25.432 18.643  -27.487 1.00 51.83 ? 727 HOH A O   1 
HETATM 2810 O O   . HOH G 4 .   ? 16.802 -6.131  -50.216 1.00 53.33 ? 728 HOH A O   1 
HETATM 2811 O O   . HOH G 4 .   ? 5.062  -5.873  4.231   1.00 58.54 ? 729 HOH A O   1 
HETATM 2812 O O   . HOH G 4 .   ? 4.830  21.628  -24.475 1.00 72.04 ? 730 HOH A O   1 
HETATM 2813 O O   . HOH G 4 .   ? 11.235 -6.090  -49.543 1.00 46.49 ? 731 HOH A O   1 
HETATM 2814 O O   . HOH G 4 .   ? 25.263 30.200  -49.435 1.00 56.45 ? 732 HOH A O   1 
HETATM 2815 O O   . HOH G 4 .   ? 29.797 6.216   -33.406 1.00 49.38 ? 733 HOH A O   1 
HETATM 2816 O O   . HOH G 4 .   ? 14.088 -6.757  -44.261 1.00 35.75 ? 734 HOH A O   1 
HETATM 2817 O O   . HOH G 4 .   ? 11.735 -16.939 -35.189 1.00 59.75 ? 735 HOH A O   1 
HETATM 2818 O O   . HOH G 4 .   ? 2.747  -2.793  -40.619 1.00 43.44 ? 736 HOH A O   1 
HETATM 2819 O O   . HOH G 4 .   ? 25.160 4.026   -44.024 1.00 42.40 ? 737 HOH A O   1 
HETATM 2820 O O   . HOH G 4 .   ? 14.872 31.683  -42.318 1.00 57.82 ? 738 HOH A O   1 
HETATM 2821 O O   . HOH G 4 .   ? 6.316  24.636  -20.290 1.00 66.65 ? 739 HOH A O   1 
HETATM 2822 O O   . HOH G 4 .   ? 26.777 31.825  -40.402 1.00 59.32 ? 740 HOH A O   1 
HETATM 2823 O O   . HOH G 4 .   ? 25.258 24.757  -39.176 1.00 36.56 ? 741 HOH A O   1 
HETATM 2824 O O   . HOH G 4 .   ? 6.032  6.914   -43.719 1.00 43.80 ? 742 HOH A O   1 
HETATM 2825 O O   . HOH G 4 .   ? 22.338 -1.385  -5.061  1.00 37.13 ? 743 HOH A O   1 
HETATM 2826 O O   . HOH G 4 .   ? 2.783  -2.742  -19.187 1.00 61.00 ? 744 HOH A O   1 
HETATM 2827 O O   . HOH G 4 .   ? 5.390  5.474   -41.376 1.00 40.58 ? 745 HOH A O   1 
HETATM 2828 O O   . HOH G 4 .   ? 6.412  1.958   -16.847 1.00 44.31 ? 746 HOH A O   1 
HETATM 2829 O O   . HOH G 4 .   ? 19.426 17.241  -13.919 1.00 49.43 ? 747 HOH A O   1 
HETATM 2830 O O   . HOH G 4 .   ? 9.893  28.053  -35.366 1.00 51.05 ? 748 HOH A O   1 
HETATM 2831 O O   . HOH G 4 .   ? 24.432 11.068  -20.951 1.00 44.19 ? 749 HOH A O   1 
HETATM 2832 O O   . HOH G 4 .   ? 7.600  -4.834  -30.823 1.00 47.08 ? 750 HOH A O   1 
HETATM 2833 O O   . HOH G 4 .   ? 25.160 -12.642 -21.976 1.00 51.14 ? 751 HOH A O   1 
HETATM 2834 O O   . HOH G 4 .   ? 12.027 -15.960 -11.172 1.00 42.96 ? 752 HOH A O   1 
HETATM 2835 O O   . HOH G 4 .   ? 26.218 31.057  -37.733 1.00 57.94 ? 753 HOH A O   1 
HETATM 2836 O O   . HOH G 4 .   ? 21.568 -14.323 -32.653 1.00 41.07 ? 754 HOH A O   1 
HETATM 2837 O O   . HOH G 4 .   ? 13.509 22.899  -27.881 1.00 56.40 ? 755 HOH A O   1 
HETATM 2838 O O   . HOH G 4 .   ? 25.029 18.798  -44.768 1.00 48.96 ? 756 HOH A O   1 
HETATM 2839 O O   . HOH G 4 .   ? 17.016 -9.601  -42.579 1.00 55.24 ? 757 HOH A O   1 
HETATM 2840 O O   . HOH G 4 .   ? 24.161 11.270  -35.558 1.00 48.20 ? 758 HOH A O   1 
HETATM 2841 O O   . HOH G 4 .   ? 27.347 -5.826  -26.754 1.00 51.81 ? 759 HOH A O   1 
HETATM 2842 O O   . HOH G 4 .   ? 20.599 -13.927 -27.991 1.00 42.78 ? 760 HOH A O   1 
HETATM 2843 O O   . HOH G 4 .   ? 26.428 16.247  -43.801 1.00 45.98 ? 761 HOH A O   1 
HETATM 2844 O O   . HOH G 4 .   ? 21.102 -3.947  -5.386  1.00 33.20 ? 762 HOH A O   1 
HETATM 2845 O O   . HOH G 4 .   ? 10.727 10.727  0.000   0.50 43.08 ? 763 HOH A O   1 
HETATM 2846 O O   . HOH G 4 .   ? 24.795 12.891  -42.019 1.00 47.55 ? 764 HOH A O   1 
HETATM 2847 O O   . HOH G 4 .   ? 13.146 -6.425  -48.288 1.00 40.60 ? 765 HOH A O   1 
HETATM 2848 O O   . HOH G 4 .   ? 28.960 26.728  -59.161 1.00 48.44 ? 766 HOH A O   1 
HETATM 2849 O O   . HOH G 4 .   ? 3.347  -1.835  6.588   1.00 51.84 ? 767 HOH A O   1 
HETATM 2850 O O   . HOH G 4 .   ? 22.465 11.981  -37.648 1.00 35.45 ? 768 HOH A O   1 
HETATM 2851 O O   . HOH G 4 .   ? 3.369  -5.111  -2.840  1.00 47.16 ? 769 HOH A O   1 
HETATM 2852 O O   . HOH G 4 .   ? 26.905 26.876  -37.766 1.00 43.04 ? 770 HOH A O   1 
HETATM 2853 O O   . HOH G 4 .   ? 26.021 29.483  -52.210 1.00 49.15 ? 771 HOH A O   1 
HETATM 2854 O O   . HOH G 4 .   ? 24.797 28.808  -57.908 1.00 57.56 ? 772 HOH A O   1 
HETATM 2855 O O   . HOH G 4 .   ? 15.244 30.900  -37.313 1.00 60.98 ? 773 HOH A O   1 
HETATM 2856 O O   . HOH G 4 .   ? 18.372 -9.002  -44.224 1.00 54.25 ? 774 HOH A O   1 
HETATM 2857 O O   . HOH G 4 .   ? 7.330  25.434  -52.511 1.00 51.19 ? 775 HOH A O   1 
HETATM 2858 O O   . HOH G 4 .   ? 23.830 14.469  -19.735 1.00 49.14 ? 776 HOH A O   1 
HETATM 2859 O O   . HOH G 4 .   ? 25.166 21.905  -42.605 1.00 54.76 ? 777 HOH A O   1 
HETATM 2860 O O   . HOH G 4 .   ? 23.493 32.606  -34.099 1.00 51.81 ? 778 HOH A O   1 
HETATM 2861 O O   . HOH G 4 .   ? 20.087 34.422  -45.071 1.00 45.90 ? 779 HOH A O   1 
HETATM 2862 O O   . HOH G 4 .   ? 4.617  10.936  -54.280 1.00 49.69 ? 780 HOH A O   1 
HETATM 2863 O O   . HOH G 4 .   ? 5.705  27.126  -47.264 1.00 53.76 ? 781 HOH A O   1 
HETATM 2864 O O   . HOH G 4 .   ? 13.050 -8.954  -44.925 1.00 48.23 ? 782 HOH A O   1 
HETATM 2865 O O   . HOH G 4 .   ? 19.754 15.517  -17.964 1.00 37.86 ? 783 HOH A O   1 
HETATM 2866 O O   . HOH G 4 .   ? 18.320 -16.091 -27.819 1.00 56.50 ? 784 HOH A O   1 
HETATM 2867 O O   . HOH G 4 .   ? 5.703  2.329   -42.502 1.00 43.25 ? 785 HOH A O   1 
HETATM 2868 O O   . HOH G 4 .   ? 12.521 28.463  -32.694 1.00 53.31 ? 786 HOH A O   1 
HETATM 2869 O O   . HOH G 4 .   ? 24.616 28.809  -34.300 1.00 46.27 ? 787 HOH A O   1 
HETATM 2870 O O   . HOH G 4 .   ? 17.976 -16.405 2.265   1.00 48.80 ? 788 HOH A O   1 
HETATM 2871 O O   . HOH G 4 .   ? 26.010 -7.608  -26.209 1.00 55.95 ? 789 HOH A O   1 
HETATM 2872 O O   . HOH G 4 .   ? 25.137 -11.361 -38.269 1.00 56.63 ? 790 HOH A O   1 
HETATM 2873 O O   . HOH G 4 .   ? 1.524  2.864   -50.805 1.00 48.08 ? 791 HOH A O   1 
HETATM 2874 O O   . HOH G 4 .   ? 21.526 -5.964  -1.269  1.00 41.41 ? 792 HOH A O   1 
HETATM 2875 O O   . HOH G 4 .   ? 5.268  24.277  -39.893 1.00 44.84 ? 793 HOH A O   1 
HETATM 2876 O O   . HOH G 4 .   ? 15.441 28.727  -32.953 1.00 46.96 ? 794 HOH A O   1 
HETATM 2877 O O   . HOH G 4 .   ? 23.679 11.498  -32.476 1.00 39.27 ? 795 HOH A O   1 
HETATM 2878 O O   . HOH G 4 .   ? 23.043 -5.364  -6.691  1.00 44.08 ? 796 HOH A O   1 
HETATM 2879 O O   . HOH G 4 .   ? 9.853  -17.915 -6.945  1.00 47.52 ? 797 HOH A O   1 
HETATM 2880 O O   . HOH G 4 .   ? 20.536 -16.420 -24.786 1.00 54.58 ? 798 HOH A O   1 
HETATM 2881 O O   . HOH G 4 .   ? 22.539 2.350   -2.742  1.00 49.75 ? 799 HOH A O   1 
HETATM 2882 O O   . HOH G 4 .   ? 12.599 29.411  -38.988 1.00 55.75 ? 800 HOH A O   1 
HETATM 2883 O O   . HOH G 4 .   ? 26.632 27.041  -33.580 1.00 50.00 ? 801 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASN A 30  ? 0.6940 0.7111 0.6956 -0.0516 -0.0023 0.0534  30  ASN A N   
2    C CA  . ASN A 30  ? 0.6864 0.6863 0.6904 -0.0388 -0.0038 0.0459  30  ASN A CA  
3    C C   . ASN A 30  ? 0.6659 0.6849 0.6886 -0.0230 -0.0019 0.0433  30  ASN A C   
4    O O   . ASN A 30  ? 0.6521 0.6984 0.6880 -0.0220 0.0000  0.0468  30  ASN A O   
5    C CB  . ASN A 30  ? 0.7089 0.7000 0.7085 -0.0474 -0.0068 0.0444  30  ASN A CB  
6    C CG  . ASN A 30  ? 0.8119 0.7664 0.7845 -0.0583 -0.0077 0.0438  30  ASN A CG  
7    O OD1 . ASN A 30  ? 0.8282 0.7614 0.7864 -0.0557 -0.0060 0.0442  30  ASN A OD1 
8    N ND2 . ASN A 30  ? 0.8674 0.8116 0.8299 -0.0701 -0.0099 0.0432  30  ASN A ND2 
9    N N   . THR A 31  ? 0.5932 0.5972 0.6147 -0.0109 -0.0022 0.0377  31  THR A N   
10   C CA  . THR A 31  ? 0.5659 0.5805 0.5990 0.0015  -0.0006 0.0342  31  THR A CA  
11   C C   . THR A 31  ? 0.5176 0.5330 0.5589 0.0044  -0.0023 0.0308  31  THR A C   
12   O O   . THR A 31  ? 0.5951 0.6229 0.6455 0.0114  0.0000  0.0301  31  THR A O   
13   C CB  . THR A 31  ? 0.5148 0.5164 0.5419 0.0099  -0.0010 0.0304  31  THR A CB  
14   O OG1 . THR A 31  ? 0.6038 0.5867 0.6238 0.0103  -0.0044 0.0285  31  THR A OG1 
15   C CG2 . THR A 31  ? 0.5919 0.5952 0.6113 0.0082  0.0014  0.0340  31  THR A CG2 
16   N N   . THR A 32  ? 0.4590 0.4591 0.4949 0.0001  -0.0055 0.0290  32  THR A N   
17   C CA  . THR A 32  ? 0.5284 0.5281 0.5706 0.0022  -0.0071 0.0259  32  THR A CA  
18   C C   . THR A 32  ? 0.5828 0.5791 0.6189 -0.0101 -0.0089 0.0283  32  THR A C   
19   O O   . THR A 32  ? 0.5281 0.5053 0.5483 -0.0177 -0.0096 0.0291  32  THR A O   
20   C CB  . THR A 32  ? 0.4787 0.4625 0.5182 0.0102  -0.0086 0.0211  32  THR A CB  
21   O OG1 . THR A 32  ? 0.4748 0.4642 0.5191 0.0183  -0.0079 0.0188  32  THR A OG1 
22   C CG2 . THR A 32  ? 0.5855 0.5673 0.6296 0.0110  -0.0099 0.0185  32  THR A CG2 
23   N N   . ASP A 33  ? 0.4571 0.4700 0.5029 -0.0125 -0.0095 0.0296  33  ASP A N   
24   C CA  . ASP A 33  ? 0.5060 0.5202 0.5456 -0.0269 -0.0121 0.0325  33  ASP A CA  
25   C C   . ASP A 33  ? 0.4999 0.5025 0.5376 -0.0261 -0.0140 0.0284  33  ASP A C   
26   O O   . ASP A 33  ? 0.4777 0.4713 0.5033 -0.0390 -0.0162 0.0292  33  ASP A O   
27   C CB  . ASP A 33  ? 0.6132 0.6624 0.6650 -0.0325 -0.0118 0.0400  33  ASP A CB  
28   C CG  . ASP A 33  ? 0.9595 1.0231 1.0124 -0.0344 -0.0092 0.0453  33  ASP A CG  
29   O OD1 . ASP A 33  ? 0.9598 1.0088 0.9980 -0.0457 -0.0101 0.0463  33  ASP A OD1 
30   O OD2 . ASP A 33  ? 0.9063 0.9934 0.9724 -0.0239 -0.0054 0.0487  33  ASP A OD2 
31   N N   . ASN A 34  ? 0.3630 0.3644 0.4100 -0.0128 -0.0131 0.0241  34  ASN A N   
32   C CA  . ASN A 34  ? 0.3889 0.3778 0.4329 -0.0114 -0.0142 0.0204  34  ASN A CA  
33   C C   . ASN A 34  ? 0.3447 0.3257 0.3933 0.0020  -0.0130 0.0158  34  ASN A C   
34   O O   . ASN A 34  ? 0.3775 0.3673 0.4343 0.0092  -0.0118 0.0154  34  ASN A O   
35   C CB  . ASN A 34  ? 0.5096 0.5177 0.5638 -0.0138 -0.0155 0.0224  34  ASN A CB  
36   C CG  . ASN A 34  ? 0.4915 0.5127 0.5606 -0.0009 -0.0135 0.0215  34  ASN A CG  
37   O OD1 . ASN A 34  ? 0.3608 0.3731 0.4319 0.0060  -0.0132 0.0172  34  ASN A OD1 
38   N ND2 . ASN A 34  ? 0.5517 0.5928 0.6293 0.0026  -0.0112 0.0259  34  ASN A ND2 
39   N N   . ILE A 35  ? 0.2951 0.2600 0.3367 0.0044  -0.0130 0.0130  35  ILE A N   
40   C CA  . ILE A 35  ? 0.2841 0.2463 0.3306 0.0155  -0.0122 0.0102  35  ILE A CA  
41   C C   . ILE A 35  ? 0.2813 0.2457 0.3329 0.0173  -0.0124 0.0081  35  ILE A C   
42   O O   . ILE A 35  ? 0.2557 0.2118 0.3043 0.0232  -0.0113 0.0067  35  ILE A O   
43   C CB  . ILE A 35  ? 0.3044 0.2480 0.3376 0.0204  -0.0106 0.0106  35  ILE A CB  
44   C CG1 . ILE A 35  ? 0.4397 0.3599 0.4534 0.0148  -0.0091 0.0108  35  ILE A CG1 
45   C CG2 . ILE A 35  ? 0.3527 0.2975 0.3835 0.0202  -0.0106 0.0128  35  ILE A CG2 
46   C CD1 . ILE A 35  ? 0.5629 0.4595 0.5592 0.0238  -0.0054 0.0120  35  ILE A CD1 
47   N N   . ASP A 36  ? 0.2713 0.2490 0.3310 0.0136  -0.0133 0.0089  36  ASP A N   
48   C CA  . ASP A 36  ? 0.2600 0.2405 0.3244 0.0150  -0.0135 0.0075  36  ASP A CA  
49   C C   . ASP A 36  ? 0.2901 0.2719 0.3612 0.0231  -0.0126 0.0050  36  ASP A C   
50   O O   . ASP A 36  ? 0.2521 0.2335 0.3252 0.0246  -0.0124 0.0037  36  ASP A O   
51   C CB  . ASP A 36  ? 0.2448 0.2427 0.3177 0.0125  -0.0141 0.0104  36  ASP A CB  
52   C CG  . ASP A 36  ? 0.3716 0.3758 0.4394 0.0014  -0.0161 0.0144  36  ASP A CG  
53   O OD1 . ASP A 36  ? 0.3905 0.3791 0.4441 -0.0066 -0.0172 0.0135  36  ASP A OD1 
54   O OD2 . ASP A 36  ? 0.3781 0.4032 0.4543 0.0004  -0.0163 0.0193  36  ASP A OD2 
55   N N   . TYR A 37  ? 0.2533 0.2377 0.3270 0.0269  -0.0124 0.0045  37  TYR A N   
56   C CA  . TYR A 37  ? 0.2256 0.2141 0.3044 0.0306  -0.0125 0.0027  37  TYR A CA  
57   C C   . TYR A 37  ? 0.2365 0.2235 0.3142 0.0343  -0.0125 0.0030  37  TYR A C   
58   O O   . TYR A 37  ? 0.2641 0.2579 0.3466 0.0351  -0.0128 0.0024  37  TYR A O   
59   C CB  . TYR A 37  ? 0.2480 0.2398 0.3267 0.0312  -0.0126 0.0024  37  TYR A CB  
60   C CG  . TYR A 37  ? 0.2430 0.2324 0.3170 0.0317  -0.0131 0.0040  37  TYR A CG  
61   C CD1 . TYR A 37  ? 0.2953 0.2846 0.3672 0.0350  -0.0141 0.0052  37  TYR A CD1 
62   C CD2 . TYR A 37  ? 0.2414 0.2309 0.3130 0.0294  -0.0122 0.0055  37  TYR A CD2 
63   C CE1 . TYR A 37  ? 0.2482 0.2337 0.3140 0.0365  -0.0142 0.0074  37  TYR A CE1 
64   C CE2 . TYR A 37  ? 0.2690 0.2548 0.3347 0.0291  -0.0124 0.0073  37  TYR A CE2 
65   C CZ  . TYR A 37  ? 0.3096 0.2915 0.3716 0.0329  -0.0134 0.0080  37  TYR A CZ  
66   O OH  . TYR A 37  ? 0.4124 0.3890 0.4670 0.0336  -0.0133 0.0104  37  TYR A OH  
67   N N   . PHE A 38  ? 0.2512 0.2289 0.3208 0.0370  -0.0114 0.0045  38  PHE A N   
68   C CA  . PHE A 38  ? 0.2535 0.2304 0.3210 0.0441  -0.0095 0.0062  38  PHE A CA  
69   C C   . PHE A 38  ? 0.2577 0.2326 0.3256 0.0439  -0.0081 0.0049  38  PHE A C   
70   O O   . PHE A 38  ? 0.2638 0.2284 0.3254 0.0391  -0.0078 0.0035  38  PHE A O   
71   C CB  . PHE A 38  ? 0.3065 0.2670 0.3596 0.0492  -0.0068 0.0086  38  PHE A CB  
72   C CG  . PHE A 38  ? 0.2591 0.2218 0.3107 0.0515  -0.0077 0.0110  38  PHE A CG  
73   C CD1 . PHE A 38  ? 0.2350 0.2156 0.2951 0.0565  -0.0092 0.0136  38  PHE A CD1 
74   C CD2 . PHE A 38  ? 0.3126 0.2610 0.3533 0.0471  -0.0075 0.0111  38  PHE A CD2 
75   C CE1 . PHE A 38  ? 0.2841 0.2675 0.3419 0.0583  -0.0104 0.0163  38  PHE A CE1 
76   C CE2 . PHE A 38  ? 0.3502 0.3003 0.3888 0.0494  -0.0081 0.0136  38  PHE A CE2 
77   C CZ  . PHE A 38  ? 0.2854 0.2527 0.3325 0.0555  -0.0096 0.0160  38  PHE A CZ  
78   N N   . ASP A 39  ? 0.2414 0.2282 0.3162 0.0479  -0.0074 0.0061  39  ASP A N   
79   C CA  . ASP A 39  ? 0.2579 0.2428 0.3318 0.0494  -0.0051 0.0057  39  ASP A CA  
80   C C   . ASP A 39  ? 0.2824 0.2760 0.3568 0.0596  -0.0017 0.0100  39  ASP A C   
81   O O   . ASP A 39  ? 0.2820 0.2847 0.3581 0.0652  -0.0017 0.0137  39  ASP A O   
82   C CB  . ASP A 39  ? 0.2169 0.2102 0.2997 0.0426  -0.0072 0.0035  39  ASP A CB  
83   C CG  . ASP A 39  ? 0.3405 0.3503 0.4324 0.0401  -0.0091 0.0044  39  ASP A CG  
84   O OD1 . ASP A 39  ? 0.3600 0.3827 0.4551 0.0441  -0.0088 0.0079  39  ASP A OD1 
85   O OD2 . ASP A 39  ? 0.3011 0.3108 0.3949 0.0337  -0.0108 0.0023  39  ASP A OD2 
86   N N   . ILE A 40  ? 0.2774 0.2702 0.3499 0.0631  0.0017  0.0104  40  ILE A N   
87   C CA  . ILE A 40  ? 0.2562 0.2616 0.3300 0.0749  0.0062  0.0161  40  ILE A CA  
88   C C   . ILE A 40  ? 0.2977 0.3096 0.3749 0.0744  0.0084  0.0161  40  ILE A C   
89   O O   . ILE A 40  ? 0.2968 0.2926 0.3671 0.0694  0.0088  0.0118  40  ILE A O   
90   C CB  . ILE A 40  ? 0.3530 0.3376 0.4086 0.0878  0.0123  0.0188  40  ILE A CB  
91   C CG1 . ILE A 40  ? 0.3519 0.3547 0.4101 0.1040  0.0181  0.0270  40  ILE A CG1 
92   C CG2 . ILE A 40  ? 0.3568 0.3092 0.3925 0.0855  0.0157  0.0141  40  ILE A CG2 
93   C CD1 . ILE A 40  ? 0.4019 0.3845 0.4405 0.1206  0.0254  0.0316  40  ILE A CD1 
94   N N   . SER A 41  ? 0.3062 0.3447 0.3943 0.0790  0.0098  0.0217  41  SER A N   
95   C CA  . SER A 41  ? 0.2893 0.3362 0.3800 0.0802  0.0131  0.0231  41  SER A CA  
96   C C   . SER A 41  ? 0.3189 0.3670 0.4015 0.0981  0.0219  0.0293  41  SER A C   
97   O O   . SER A 41  ? 0.3603 0.4131 0.4403 0.1102  0.0247  0.0348  41  SER A O   
98   C CB  . SER A 41  ? 0.3824 0.4597 0.4897 0.0702  0.0089  0.0258  41  SER A CB  
99   O OG  . SER A 41  ? 0.4120 0.4791 0.5204 0.0556  0.0032  0.0195  41  SER A OG  
100  N N   . ASP A 42  ? 0.3428 0.3855 0.4199 0.1013  0.0269  0.0290  42  ASP A N   
101  C CA  . ASP A 42  ? 0.3930 0.4363 0.4604 0.1204  0.0370  0.0354  42  ASP A CA  
102  C C   . ASP A 42  ? 0.4620 0.5515 0.5489 0.1268  0.0381  0.0460  42  ASP A C   
103  O O   . ASP A 42  ? 0.3902 0.5078 0.4957 0.1127  0.0305  0.0470  42  ASP A O   
104  C CB  . ASP A 42  ? 0.4153 0.4396 0.4695 0.1213  0.0423  0.0320  42  ASP A CB  
105  C CG  . ASP A 42  ? 0.4081 0.4621 0.4793 0.1146  0.0412  0.0346  42  ASP A CG  
106  O OD1 . ASP A 42  ? 0.4208 0.4860 0.5058 0.0976  0.0328  0.0314  42  ASP A OD1 
107  O OD2 . ASP A 42  ? 0.5354 0.5998 0.6039 0.1268  0.0495  0.0403  42  ASP A OD2 
108  N N   . GLU A 43  ? 0.3844 0.4816 0.4647 0.1482  0.0482  0.0546  43  GLU A N   
109  C CA  . GLU A 43  ? 0.4562 0.5991 0.5519 0.1522  0.0483  0.0658  43  GLU A CA  
110  C C   . GLU A 43  ? 0.4360 0.6175 0.5528 0.1417  0.0457  0.0696  43  GLU A C   
111  O O   . GLU A 43  ? 0.4732 0.6962 0.6068 0.1341  0.0408  0.0770  43  GLU A O   
112  C CB  . GLU A 43  ? 0.5033 0.6380 0.5791 0.1708  0.0587  0.0726  43  GLU A CB  
113  C CG  . GLU A 43  ? 0.4407 0.5465 0.4972 0.1797  0.0608  0.0719  43  GLU A CG  
114  C CD  . GLU A 43  ? 0.5472 0.5962 0.5751 0.1819  0.0653  0.0623  43  GLU A CD  
115  O OE1 . GLU A 43  ? 0.5672 0.5991 0.5917 0.1755  0.0654  0.0552  43  GLU A OE1 
116  O OE2 . GLU A 43  ? 0.6200 0.6411 0.6270 0.1888  0.0686  0.0621  43  GLU A OE2 
117  N N   . SER A 44  ? 0.5090 0.6740 0.6209 0.1368  0.0479  0.0638  44  SER A N   
118  C CA  . SER A 44  ? 0.4295 0.6236 0.5564 0.1229  0.0451  0.0661  44  SER A CA  
119  C C   . SER A 44  ? 0.4177 0.6128 0.5539 0.0970  0.0332  0.0594  44  SER A C   
120  O O   . SER A 44  ? 0.4104 0.6272 0.5565 0.0826  0.0302  0.0613  44  SER A O   
121  C CB  . SER A 44  ? 0.4998 0.6708 0.6137 0.1261  0.0517  0.0618  44  SER A CB  
122  O OG  . SER A 44  ? 0.4470 0.5754 0.5479 0.1147  0.0470  0.0494  44  SER A OG  
123  N N   . ASN A 45  ? 0.4399 0.6098 0.5705 0.0910  0.0272  0.0519  45  ASN A N   
124  C CA  . ASN A 45  ? 0.4134 0.5756 0.5474 0.0697  0.0178  0.0449  45  ASN A CA  
125  C C   . ASN A 45  ? 0.4584 0.5980 0.5862 0.0593  0.0170  0.0377  45  ASN A C   
126  O O   . ASN A 45  ? 0.4553 0.5921 0.5850 0.0427  0.0112  0.0340  45  ASN A O   
127  C CB  . ASN A 45  ? 0.5731 0.7732 0.7211 0.0559  0.0119  0.0511  45  ASN A CB  
128  C CG  . ASN A 45  ? 0.6759 0.8797 0.8256 0.0529  0.0060  0.0511  45  ASN A CG  
129  O OD1 . ASN A 45  ? 0.7085 0.9082 0.8554 0.0684  0.0088  0.0534  45  ASN A OD1 
130  N ND2 . ASN A 45  ? 0.7649 0.9730 0.9160 0.0328  -0.0016 0.0485  45  ASN A ND2 
131  N N   . TYR A 46  ? 0.3851 0.5060 0.5026 0.0692  0.0233  0.0358  46  TYR A N   
132  C CA  . TYR A 46  ? 0.3466 0.4492 0.4582 0.0606  0.0227  0.0303  46  TYR A CA  
133  C C   . TYR A 46  ? 0.3866 0.4550 0.4872 0.0571  0.0193  0.0218  46  TYR A C   
134  O O   . TYR A 46  ? 0.3868 0.4447 0.4863 0.0463  0.0155  0.0179  46  TYR A O   
135  C CB  . TYR A 46  ? 0.4258 0.5291 0.5309 0.0715  0.0312  0.0334  46  TYR A CB  
136  C CG  . TYR A 46  ? 0.3935 0.4869 0.4948 0.0623  0.0309  0.0301  46  TYR A CG  
137  C CD1 . TYR A 46  ? 0.5040 0.5663 0.5898 0.0640  0.0321  0.0241  46  TYR A CD1 
138  C CD2 . TYR A 46  ? 0.5114 0.6264 0.6225 0.0504  0.0290  0.0336  46  TYR A CD2 
139  C CE1 . TYR A 46  ? 0.5065 0.5612 0.5883 0.0564  0.0317  0.0221  46  TYR A CE1 
140  C CE2 . TYR A 46  ? 0.5321 0.6358 0.6377 0.0427  0.0292  0.0312  46  TYR A CE2 
141  C CZ  . TYR A 46  ? 0.5413 0.6158 0.6332 0.0468  0.0306  0.0256  46  TYR A CZ  
142  O OH  . TYR A 46  ? 0.6491 0.7140 0.7353 0.0400  0.0305  0.0241  46  TYR A OH  
143  N N   . TYR A 47  ? 0.3150 0.3664 0.4062 0.0662  0.0209  0.0201  47  TYR A N   
144  C CA  . TYR A 47  ? 0.2996 0.3229 0.3800 0.0620  0.0178  0.0136  47  TYR A CA  
145  C C   . TYR A 47  ? 0.3069 0.3297 0.3909 0.0603  0.0134  0.0126  47  TYR A C   
146  O O   . TYR A 47  ? 0.3020 0.3340 0.3879 0.0686  0.0154  0.0165  47  TYR A O   
147  C CB  . TYR A 47  ? 0.3305 0.3289 0.3913 0.0706  0.0233  0.0118  47  TYR A CB  
148  C CG  . TYR A 47  ? 0.3170 0.3127 0.3703 0.0740  0.0288  0.0126  47  TYR A CG  
149  C CD1 . TYR A 47  ? 0.3493 0.3379 0.4004 0.0640  0.0258  0.0093  47  TYR A CD1 
150  C CD2 . TYR A 47  ? 0.4269 0.4275 0.4742 0.0885  0.0376  0.0174  47  TYR A CD2 
151  C CE1 . TYR A 47  ? 0.3740 0.3592 0.4167 0.0667  0.0308  0.0099  47  TYR A CE1 
152  C CE2 . TYR A 47  ? 0.4214 0.4186 0.4601 0.0922  0.0436  0.0182  47  TYR A CE2 
153  C CZ  . TYR A 47  ? 0.3911 0.3801 0.4275 0.0804  0.0398  0.0140  47  TYR A CZ  
154  O OH  . TYR A 47  ? 0.4376 0.4230 0.4646 0.0835  0.0456  0.0148  47  TYR A OH  
155  N N   . LEU A 48  ? 0.2506 0.2627 0.3344 0.0511  0.0082  0.0083  48  LEU A N   
156  C CA  . LEU A 48  ? 0.2980 0.3073 0.3834 0.0492  0.0046  0.0071  48  LEU A CA  
157  C C   . LEU A 48  ? 0.2877 0.2753 0.3612 0.0476  0.0038  0.0037  48  LEU A C   
158  O O   . LEU A 48  ? 0.3310 0.3124 0.4020 0.0416  0.0020  0.0017  48  LEU A O   
159  C CB  . LEU A 48  ? 0.2921 0.3099 0.3865 0.0399  -0.0001 0.0061  48  LEU A CB  
160  C CG  . LEU A 48  ? 0.3553 0.3702 0.4497 0.0396  -0.0029 0.0051  48  LEU A CG  
161  C CD1 . LEU A 48  ? 0.4455 0.4753 0.5469 0.0350  -0.0055 0.0066  48  LEU A CD1 
162  C CD2 . LEU A 48  ? 0.2763 0.2778 0.3668 0.0353  -0.0050 0.0020  48  LEU A CD2 
163  N N   . ILE A 49  ? 0.2529 0.2305 0.3182 0.0522  0.0050  0.0039  49  ILE A N   
164  C CA  . ILE A 49  ? 0.2845 0.2410 0.3352 0.0482  0.0042  0.0014  49  ILE A CA  
165  C C   . ILE A 49  ? 0.3176 0.2780 0.3746 0.0422  -0.0005 0.0007  49  ILE A C   
166  O O   . ILE A 49  ? 0.2663 0.2331 0.3284 0.0458  -0.0009 0.0022  49  ILE A O   
167  C CB  . ILE A 49  ? 0.3195 0.2558 0.3511 0.0566  0.0098  0.0022  49  ILE A CB  
168  C CG1 . ILE A 49  ? 0.4365 0.3686 0.4602 0.0642  0.0159  0.0031  49  ILE A CG1 
169  C CG2 . ILE A 49  ? 0.3699 0.2816 0.3824 0.0484  0.0086  -0.0005 49  ILE A CG2 
170  C CD1 . ILE A 49  ? 0.4568 0.3680 0.4595 0.0774  0.0241  0.0052  49  ILE A CD1 
171  N N   . SER A 50  ? 0.2699 0.2286 0.3263 0.0337  -0.0038 -0.0005 50  SER A N   
172  C CA  . SER A 50  ? 0.2339 0.1976 0.2952 0.0290  -0.0072 -0.0001 50  SER A CA  
173  C C   . SER A 50  ? 0.2491 0.2000 0.2964 0.0220  -0.0083 -0.0001 50  SER A C   
174  O O   . SER A 50  ? 0.2718 0.2114 0.3062 0.0172  -0.0079 -0.0008 50  SER A O   
175  C CB  . SER A 50  ? 0.2443 0.2207 0.3163 0.0259  -0.0094 0.0006  50  SER A CB  
176  O OG  . SER A 50  ? 0.2531 0.2351 0.3281 0.0228  -0.0114 0.0021  50  SER A OG  
177  N N   . GLN A 51  ? 0.2472 0.1994 0.2951 0.0196  -0.0098 0.0008  51  GLN A N   
178  C CA  . GLN A 51  ? 0.2746 0.2181 0.3096 0.0094  -0.0116 0.0017  51  GLN A CA  
179  C C   . GLN A 51  ? 0.2623 0.2220 0.3034 0.0007  -0.0153 0.0042  51  GLN A C   
180  O O   . GLN A 51  ? 0.2621 0.2182 0.2914 -0.0111 -0.0177 0.0057  51  GLN A O   
181  C CB  . GLN A 51  ? 0.2153 0.1582 0.2500 0.0090  -0.0119 0.0029  51  GLN A CB  
182  C CG  . GLN A 51  ? 0.2304 0.1577 0.2565 0.0181  -0.0082 0.0021  51  GLN A CG  
183  C CD  . GLN A 51  ? 0.2693 0.1968 0.2952 0.0178  -0.0088 0.0037  51  GLN A CD  
184  O OE1 . GLN A 51  ? 0.2696 0.1878 0.2836 0.0084  -0.0097 0.0047  51  GLN A OE1 
185  N NE2 . GLN A 51  ? 0.2506 0.1900 0.2889 0.0262  -0.0086 0.0042  51  GLN A NE2 
186  N N   . LEU A 52  ? 0.2271 0.2046 0.2845 0.0059  -0.0156 0.0056  52  LEU A N   
187  C CA  . LEU A 52  ? 0.2201 0.2156 0.2839 0.0015  -0.0181 0.0098  52  LEU A CA  
188  C C   . LEU A 52  ? 0.2366 0.2283 0.2936 -0.0023 -0.0190 0.0094  52  LEU A C   
189  O O   . LEU A 52  ? 0.2082 0.1929 0.2662 0.0041  -0.0167 0.0067  52  LEU A O   
190  C CB  . LEU A 52  ? 0.2111 0.2205 0.2896 0.0108  -0.0164 0.0116  52  LEU A CB  
191  C CG  . LEU A 52  ? 0.2770 0.2897 0.3608 0.0154  -0.0149 0.0119  52  LEU A CG  
192  C CD1 . LEU A 52  ? 0.2694 0.2894 0.3608 0.0242  -0.0122 0.0137  52  LEU A CD1 
193  C CD2 . LEU A 52  ? 0.2768 0.2992 0.3588 0.0082  -0.0168 0.0158  52  LEU A CD2 
194  N N   . ARG A 53  ? 0.1961 0.1940 0.2455 -0.0140 -0.0226 0.0126  53  ARG A N   
195  C CA  . ARG A 53  ? 0.2334 0.2312 0.2761 -0.0188 -0.0243 0.0132  53  ARG A CA  
196  C C   . ARG A 53  ? 0.2660 0.2798 0.3246 -0.0084 -0.0231 0.0159  53  ARG A C   
197  O O   . ARG A 53  ? 0.2362 0.2675 0.3081 -0.0022 -0.0226 0.0203  53  ARG A O   
198  C CB  . ARG A 53  ? 0.2756 0.2854 0.3095 -0.0352 -0.0297 0.0181  53  ARG A CB  
199  C CG  . ARG A 53  ? 0.2884 0.2946 0.3083 -0.0453 -0.0326 0.0184  53  ARG A CG  
200  C CD  . ARG A 53  ? 0.2893 0.3146 0.3021 -0.0644 -0.0392 0.0249  53  ARG A CD  
201  N NE  . ARG A 53  ? 0.3197 0.3489 0.3206 -0.0757 -0.0434 0.0270  53  ARG A NE  
202  C CZ  . ARG A 53  ? 0.3650 0.3676 0.3364 -0.0918 -0.0450 0.0227  53  ARG A CZ  
203  N NH1 . ARG A 53  ? 0.4283 0.3944 0.3777 -0.0959 -0.0417 0.0158  53  ARG A NH1 
204  N NH2 . ARG A 53  ? 0.3256 0.3364 0.2864 -0.1038 -0.0498 0.0256  53  ARG A NH2 
205  N N   . PRO A 54  ? 0.2584 0.2641 0.3137 -0.0053 -0.0216 0.0138  54  PRO A N   
206  C CA  . PRO A 54  ? 0.2565 0.2428 0.2947 -0.0106 -0.0211 0.0097  54  PRO A CA  
207  C C   . PRO A 54  ? 0.2968 0.2622 0.3296 -0.0031 -0.0160 0.0041  54  PRO A C   
208  O O   . PRO A 54  ? 0.2865 0.2369 0.3067 -0.0026 -0.0134 0.0014  54  PRO A O   
209  C CB  . PRO A 54  ? 0.2552 0.2507 0.2971 -0.0084 -0.0215 0.0123  54  PRO A CB  
210  C CG  . PRO A 54  ? 0.3053 0.3111 0.3647 0.0035  -0.0189 0.0141  54  PRO A CG  
211  C CD  . PRO A 54  ? 0.2729 0.2894 0.3403 0.0042  -0.0199 0.0166  54  PRO A CD  
212  N N   . HIS A 55  ? 0.2540 0.2201 0.2956 0.0036  -0.0142 0.0031  55  HIS A N   
213  C CA  . HIS A 55  ? 0.2621 0.2128 0.2980 0.0104  -0.0100 -0.0002 55  HIS A CA  
214  C C   . HIS A 55  ? 0.2850 0.2382 0.3282 0.0197  -0.0062 -0.0011 55  HIS A C   
215  O O   . HIS A 55  ? 0.2582 0.2122 0.3061 0.0268  -0.0037 -0.0014 55  HIS A O   
216  C CB  . HIS A 55  ? 0.2906 0.2165 0.3016 0.0053  -0.0082 -0.0024 55  HIS A CB  
217  C CG  . HIS A 55  ? 0.2668 0.1893 0.2675 -0.0075 -0.0123 -0.0013 55  HIS A CG  
218  N ND1 . HIS A 55  ? 0.2659 0.1950 0.2738 -0.0081 -0.0137 0.0002  55  HIS A ND1 
219  C CD2 . HIS A 55  ? 0.2930 0.2098 0.2774 -0.0221 -0.0158 -0.0006 55  HIS A CD2 
220  C CE1 . HIS A 55  ? 0.3371 0.2651 0.3339 -0.0224 -0.0175 0.0020  55  HIS A CE1 
221  N NE2 . HIS A 55  ? 0.3078 0.2293 0.2903 -0.0320 -0.0192 0.0017  55  HIS A NE2 
222  N N   . PHE A 56  ? 0.2863 0.2431 0.3302 0.0190  -0.0060 -0.0006 56  PHE A N   
223  C CA  . PHE A 56  ? 0.2978 0.2604 0.3494 0.0254  -0.0027 -0.0004 56  PHE A CA  
224  C C   . PHE A 56  ? 0.2649 0.2380 0.3250 0.0231  -0.0047 0.0016  56  PHE A C   
225  O O   . PHE A 56  ? 0.2994 0.2729 0.3545 0.0183  -0.0072 0.0030  56  PHE A O   
226  C CB  . PHE A 56  ? 0.3542 0.3055 0.3931 0.0290  0.0021  -0.0015 56  PHE A CB  
227  C CG  . PHE A 56  ? 0.3496 0.2793 0.3679 0.0296  0.0047  -0.0034 56  PHE A CG  
228  C CD1 . PHE A 56  ? 0.4227 0.3464 0.4380 0.0380  0.0086  -0.0032 56  PHE A CD1 
229  C CD2 . PHE A 56  ? 0.5062 0.4197 0.5049 0.0212  0.0036  -0.0050 56  PHE A CD2 
230  C CE1 . PHE A 56  ? 0.4199 0.3167 0.4106 0.0396  0.0124  -0.0047 56  PHE A CE1 
231  C CE2 . PHE A 56  ? 0.4933 0.3796 0.4663 0.0199  0.0067  -0.0073 56  PHE A CE2 
232  C CZ  . PHE A 56  ? 0.4784 0.3540 0.4464 0.0299  0.0117  -0.0072 56  PHE A CZ  
233  N N   . SER A 57  ? 0.2570 0.2375 0.3271 0.0259  -0.0035 0.0023  57  SER A N   
234  C CA  . SER A 57  ? 0.2724 0.2565 0.3456 0.0248  -0.0039 0.0045  57  SER A CA  
235  C C   . SER A 57  ? 0.2821 0.2636 0.3486 0.0236  -0.0028 0.0052  57  SER A C   
236  O O   . SER A 57  ? 0.2726 0.2560 0.3381 0.0225  -0.0038 0.0079  57  SER A O   
237  C CB  . SER A 57  ? 0.2852 0.2717 0.3641 0.0252  -0.0023 0.0046  57  SER A CB  
238  O OG  . SER A 57  ? 0.3346 0.3249 0.4144 0.0252  0.0002  0.0042  57  SER A OG  
239  N N   . ASN A 58  ? 0.2961 0.2728 0.3563 0.0250  0.0001  0.0034  58  ASN A N   
240  C CA  . ASN A 58  ? 0.3175 0.2901 0.3691 0.0243  0.0021  0.0038  58  ASN A CA  
241  C C   . ASN A 58  ? 0.3586 0.3275 0.4008 0.0188  -0.0016 0.0046  58  ASN A C   
242  O O   . ASN A 58  ? 0.3237 0.2930 0.3612 0.0169  -0.0016 0.0063  58  ASN A O   
243  C CB  . ASN A 58  ? 0.2902 0.2557 0.3330 0.0292  0.0073  0.0021  58  ASN A CB  
244  C CG  . ASN A 58  ? 0.3842 0.3601 0.4375 0.0349  0.0103  0.0031  58  ASN A CG  
245  O OD1 . ASN A 58  ? 0.3627 0.3394 0.4196 0.0367  0.0091  0.0026  58  ASN A OD1 
246  N ND2 . ASN A 58  ? 0.3506 0.3372 0.4092 0.0366  0.0137  0.0055  58  ASN A ND2 
247  N N   . ILE A 59  ? 0.2857 0.2529 0.3246 0.0149  -0.0050 0.0042  59  ILE A N   
248  C CA  . ILE A 59  ? 0.2920 0.2618 0.3228 0.0068  -0.0097 0.0065  59  ILE A CA  
249  C C   . ILE A 59  ? 0.3041 0.2902 0.3458 0.0084  -0.0121 0.0121  59  ILE A C   
250  O O   . ILE A 59  ? 0.3288 0.3206 0.3651 0.0045  -0.0146 0.0155  59  ILE A O   
251  C CB  . ILE A 59  ? 0.3421 0.3103 0.3679 0.0004  -0.0131 0.0060  59  ILE A CB  
252  C CG1 . ILE A 59  ? 0.4059 0.3519 0.4156 0.0003  -0.0095 0.0010  59  ILE A CG1 
253  C CG2 . ILE A 59  ? 0.2952 0.2733 0.3140 -0.0107 -0.0190 0.0101  59  ILE A CG2 
254  C CD1 . ILE A 59  ? 0.3746 0.3023 0.3633 -0.0019 -0.0064 -0.0016 59  ILE A CD1 
255  N N   . TYR A 60  ? 0.2842 0.2764 0.3388 0.0146  -0.0110 0.0135  60  TYR A N   
256  C CA  . TYR A 60  ? 0.2563 0.2578 0.3168 0.0191  -0.0111 0.0192  60  TYR A CA  
257  C C   . TYR A 60  ? 0.2818 0.2775 0.3384 0.0209  -0.0083 0.0199  60  TYR A C   
258  O O   . TYR A 60  ? 0.3268 0.3282 0.3828 0.0238  -0.0087 0.0255  60  TYR A O   
259  C CB  . TYR A 60  ? 0.2795 0.2813 0.3483 0.0254  -0.0090 0.0197  60  TYR A CB  
260  C CG  . TYR A 60  ? 0.3341 0.3472 0.4076 0.0255  -0.0116 0.0224  60  TYR A CG  
261  C CD1 . TYR A 60  ? 0.2909 0.3206 0.3639 0.0220  -0.0155 0.0283  60  TYR A CD1 
262  C CD2 . TYR A 60  ? 0.2935 0.3034 0.3715 0.0280  -0.0102 0.0198  60  TYR A CD2 
263  C CE1 . TYR A 60  ? 0.3185 0.3631 0.3968 0.0212  -0.0177 0.0320  60  TYR A CE1 
264  C CE2 . TYR A 60  ? 0.3327 0.3541 0.4148 0.0281  -0.0120 0.0228  60  TYR A CE2 
265  C CZ  . TYR A 60  ? 0.3230 0.3625 0.4058 0.0247  -0.0155 0.0291  60  TYR A CZ  
266  O OH  . TYR A 60  ? 0.2904 0.3458 0.3782 0.0238  -0.0172 0.0333  60  TYR A OH  
267  N N   . PHE A 61  ? 0.2832 0.2696 0.3375 0.0203  -0.0050 0.0154  61  PHE A N   
268  C CA  . PHE A 61  ? 0.2774 0.2603 0.3271 0.0204  -0.0024 0.0166  61  PHE A CA  
269  C C   . PHE A 61  ? 0.3242 0.3087 0.3638 0.0164  -0.0048 0.0183  61  PHE A C   
270  O O   . PHE A 61  ? 0.3231 0.3104 0.3598 0.0172  -0.0052 0.0229  61  PHE A O   
271  C CB  . PHE A 61  ? 0.3035 0.2819 0.3535 0.0204  0.0019  0.0129  61  PHE A CB  
272  C CG  . PHE A 61  ? 0.2973 0.2737 0.3411 0.0195  0.0049  0.0143  61  PHE A CG  
273  C CD1 . PHE A 61  ? 0.3516 0.3265 0.3950 0.0194  0.0059  0.0180  61  PHE A CD1 
274  C CD2 . PHE A 61  ? 0.3355 0.3083 0.3703 0.0192  0.0072  0.0122  61  PHE A CD2 
275  C CE1 . PHE A 61  ? 0.3395 0.3125 0.3762 0.0179  0.0087  0.0198  61  PHE A CE1 
276  C CE2 . PHE A 61  ? 0.3489 0.3201 0.3768 0.0187  0.0104  0.0137  61  PHE A CE2 
277  C CZ  . PHE A 61  ? 0.3762 0.3491 0.4063 0.0175  0.0107  0.0177  61  PHE A CZ  
278  N N   . PHE A 62  ? 0.3188 0.2993 0.3499 0.0115  -0.0065 0.0151  62  PHE A N   
279  C CA  . PHE A 62  ? 0.3481 0.3280 0.3653 0.0047  -0.0096 0.0165  62  PHE A CA  
280  C C   . PHE A 62  ? 0.3641 0.3618 0.3859 0.0029  -0.0151 0.0239  62  PHE A C   
281  O O   . PHE A 62  ? 0.3520 0.3556 0.3671 0.0001  -0.0173 0.0282  62  PHE A O   
282  C CB  . PHE A 62  ? 0.2691 0.2359 0.2705 -0.0024 -0.0103 0.0115  62  PHE A CB  
283  C CG  . PHE A 62  ? 0.3843 0.3342 0.3793 0.0031  -0.0034 0.0059  62  PHE A CG  
284  C CD1 . PHE A 62  ? 0.3753 0.3237 0.3717 0.0093  0.0022  0.0058  62  PHE A CD1 
285  C CD2 . PHE A 62  ? 0.3429 0.2799 0.3298 0.0028  -0.0020 0.0020  62  PHE A CD2 
286  C CE1 . PHE A 62  ? 0.4149 0.3539 0.4068 0.0163  0.0093  0.0027  62  PHE A CE1 
287  C CE2 . PHE A 62  ? 0.3495 0.2733 0.3303 0.0112  0.0055  -0.0013 62  PHE A CE2 
288  C CZ  . PHE A 62  ? 0.3316 0.2588 0.3160 0.0186  0.0112  -0.0005 62  PHE A CZ  
289  N N   . ASP A 63  ? 0.3181 0.3267 0.3515 0.0057  -0.0169 0.0266  63  ASP A N   
290  C CA  . ASP A 63  ? 0.3241 0.3542 0.3637 0.0076  -0.0207 0.0357  63  ASP A CA  
291  C C   . ASP A 63  ? 0.3034 0.3348 0.3464 0.0178  -0.0173 0.0413  63  ASP A C   
292  O O   . ASP A 63  ? 0.3301 0.3766 0.3717 0.0192  -0.0199 0.0496  63  ASP A O   
293  C CB  . ASP A 63  ? 0.3447 0.3854 0.3955 0.0108  -0.0215 0.0376  63  ASP A CB  
294  C CG  . ASP A 63  ? 0.4891 0.5311 0.5349 -0.0008 -0.0257 0.0343  63  ASP A CG  
295  O OD1 . ASP A 63  ? 0.4441 0.4806 0.4754 -0.0126 -0.0289 0.0321  63  ASP A OD1 
296  O OD2 . ASP A 63  ? 0.4512 0.4970 0.5048 0.0013  -0.0254 0.0340  63  ASP A OD2 
297  N N   . GLU A 64  ? 0.3408 0.3567 0.3868 0.0246  -0.0116 0.0379  64  GLU A N   
298  C CA  . GLU A 64  ? 0.3053 0.3149 0.3491 0.0326  -0.0075 0.0425  64  GLU A CA  
299  C C   . GLU A 64  ? 0.2798 0.2860 0.3144 0.0289  -0.0075 0.0434  64  GLU A C   
300  O O   . GLU A 64  ? 0.2983 0.3064 0.3289 0.0346  -0.0064 0.0506  64  GLU A O   
301  C CB  . GLU A 64  ? 0.3308 0.3218 0.3751 0.0354  -0.0020 0.0378  64  GLU A CB  
302  C CG  . GLU A 64  ? 0.4938 0.4815 0.5414 0.0429  0.0004  0.0396  64  GLU A CG  
303  C CD  . GLU A 64  ? 0.4351 0.4329 0.4816 0.0537  0.0010  0.0497  64  GLU A CD  
304  O OE1 . GLU A 64  ? 0.4107 0.3977 0.4481 0.0610  0.0052  0.0550  64  GLU A OE1 
305  O OE2 . GLU A 64  ? 0.5000 0.5175 0.5540 0.0550  -0.0025 0.0532  64  GLU A OE2 
306  N N   . PHE A 65  ? 0.2983 0.2980 0.3278 0.0210  -0.0077 0.0367  65  PHE A N   
307  C CA  . PHE A 65  ? 0.3305 0.3264 0.3496 0.0179  -0.0069 0.0375  65  PHE A CA  
308  C C   . PHE A 65  ? 0.3240 0.3349 0.3371 0.0144  -0.0127 0.0441  65  PHE A C   
309  O O   . PHE A 65  ? 0.3341 0.3456 0.3395 0.0146  -0.0125 0.0483  65  PHE A O   
310  C CB  . PHE A 65  ? 0.2931 0.2780 0.3054 0.0125  -0.0044 0.0296  65  PHE A CB  
311  C CG  . PHE A 65  ? 0.3121 0.2912 0.3136 0.0108  -0.0017 0.0302  65  PHE A CG  
312  C CD1 . PHE A 65  ? 0.3005 0.2740 0.3042 0.0141  0.0037  0.0311  65  PHE A CD1 
313  C CD2 . PHE A 65  ? 0.3435 0.3227 0.3306 0.0045  -0.0047 0.0303  65  PHE A CD2 
314  C CE1 . PHE A 65  ? 0.3654 0.3349 0.3591 0.0125  0.0065  0.0323  65  PHE A CE1 
315  C CE2 . PHE A 65  ? 0.4598 0.4331 0.4353 0.0032  -0.0019 0.0310  65  PHE A CE2 
316  C CZ  . PHE A 65  ? 0.4027 0.3721 0.3827 0.0080  0.0040  0.0322  65  PHE A CZ  
317  N N   . LYS A 66  ? 0.3372 0.3623 0.3529 0.0100  -0.0183 0.0458  66  LYS A N   
318  C CA  . LYS A 66  ? 0.3185 0.3653 0.3303 0.0053  -0.0248 0.0543  66  LYS A CA  
319  C C   . LYS A 66  ? 0.3162 0.3754 0.3337 0.0177  -0.0234 0.0654  66  LYS A C   
320  O O   . LYS A 66  ? 0.3711 0.4423 0.3822 0.0167  -0.0263 0.0728  66  LYS A O   
321  C CB  . LYS A 66  ? 0.3774 0.4413 0.3936 -0.0019 -0.0306 0.0558  66  LYS A CB  
322  C CG  . LYS A 66  ? 0.5875 0.6732 0.5947 -0.0147 -0.0389 0.0624  66  LYS A CG  
323  C CD  . LYS A 66  ? 0.5251 0.6290 0.5348 -0.0257 -0.0451 0.0643  66  LYS A CD  
324  C CE  . LYS A 66  ? 0.5953 0.7224 0.5930 -0.0426 -0.0544 0.0714  66  LYS A CE  
325  N NZ  . LYS A 66  ? 0.6418 0.7899 0.6424 -0.0349 -0.0557 0.0827  66  LYS A NZ  
326  N N   . ARG A 67  ? 0.3731 0.4267 0.3997 0.0301  -0.0182 0.0669  67  ARG A N   
327  C CA  . ARG A 67  ? 0.3433 0.4009 0.3704 0.0447  -0.0146 0.0775  67  ARG A CA  
328  C C   . ARG A 67  ? 0.2976 0.3358 0.3139 0.0467  -0.0102 0.0773  67  ARG A C   
329  O O   . ARG A 67  ? 0.3645 0.4110 0.3753 0.0530  -0.0104 0.0871  67  ARG A O   
330  C CB  . ARG A 67  ? 0.3936 0.4425 0.4271 0.0565  -0.0090 0.0778  67  ARG A CB  
331  C CG  . ARG A 67  ? 0.4151 0.4862 0.4597 0.0558  -0.0127 0.0799  67  ARG A CG  
332  C CD  . ARG A 67  ? 0.5832 0.6602 0.6313 0.0737  -0.0075 0.0893  67  ARG A CD  
333  N NE  . ARG A 67  ? 0.7952 0.8429 0.8405 0.0785  -0.0007 0.0816  67  ARG A NE  
334  C CZ  . ARG A 67  ? 0.6901 0.7255 0.7300 0.0944  0.0068  0.0867  67  ARG A CZ  
335  N NH1 . ARG A 67  ? 0.6683 0.7182 0.7059 0.1106  0.0098  0.1005  67  ARG A NH1 
336  N NH2 . ARG A 67  ? 0.4916 0.4990 0.5262 0.0944  0.0118  0.0784  67  ARG A NH2 
337  N N   . TYR A 68  ? 0.3072 0.3219 0.3202 0.0415  -0.0061 0.0672  68  TYR A N   
338  C CA  . TYR A 68  ? 0.3303 0.3288 0.3330 0.0411  -0.0020 0.0672  68  TYR A CA  
339  C C   . TYR A 68  ? 0.3395 0.3492 0.3342 0.0348  -0.0063 0.0701  68  TYR A C   
340  O O   . TYR A 68  ? 0.3481 0.3563 0.3346 0.0391  -0.0049 0.0772  68  TYR A O   
341  C CB  . TYR A 68  ? 0.3060 0.2861 0.3085 0.0344  0.0023  0.0569  68  TYR A CB  
342  C CG  . TYR A 68  ? 0.3182 0.2883 0.3273 0.0365  0.0054  0.0525  68  TYR A CG  
343  C CD1 . TYR A 68  ? 0.3509 0.3171 0.3603 0.0462  0.0073  0.0576  68  TYR A CD1 
344  C CD2 . TYR A 68  ? 0.3088 0.2735 0.3223 0.0295  0.0068  0.0439  68  TYR A CD2 
345  C CE1 . TYR A 68  ? 0.3247 0.2790 0.3367 0.0468  0.0102  0.0530  68  TYR A CE1 
346  C CE2 . TYR A 68  ? 0.2833 0.2408 0.3020 0.0298  0.0088  0.0403  68  TYR A CE2 
347  C CZ  . TYR A 68  ? 0.3060 0.2571 0.3232 0.0374  0.0102  0.0442  68  TYR A CZ  
348  O OH  . TYR A 68  ? 0.3336 0.2754 0.3529 0.0363  0.0121  0.0400  68  TYR A OH  
349  N N   . ALA A 69  ? 0.3505 0.3683 0.3443 0.0238  -0.0113 0.0646  69  ALA A N   
350  C CA  . ALA A 69  ? 0.3108 0.3329 0.2918 0.0153  -0.0149 0.0653  69  ALA A CA  
351  C C   . ALA A 69  ? 0.3957 0.4415 0.3747 0.0176  -0.0206 0.0778  69  ALA A C   
352  O O   . ALA A 69  ? 0.4176 0.4656 0.3849 0.0141  -0.0222 0.0815  69  ALA A O   
353  C CB  . ALA A 69  ? 0.3452 0.3644 0.3195 0.0028  -0.0182 0.0565  69  ALA A CB  
354  N N   . SER A 70  ? 0.4036 0.4696 0.3939 0.0245  -0.0233 0.0856  70  SER A N   
355  C CA  . SER A 70  ? 0.3607 0.4565 0.3515 0.0289  -0.0284 0.1001  70  SER A CA  
356  C C   . SER A 70  ? 0.4348 0.5241 0.4206 0.0436  -0.0230 0.1094  70  SER A C   
357  O O   . SER A 70  ? 0.4139 0.5277 0.3980 0.0490  -0.0266 0.1228  70  SER A O   
358  C CB  . SER A 70  ? 0.4091 0.5313 0.4141 0.0346  -0.0313 0.1074  70  SER A CB  
359  O OG  . SER A 70  ? 0.4257 0.5342 0.4381 0.0513  -0.0233 0.1083  70  SER A OG  
360  N N   . TYR A 71  ? 0.4280 0.4855 0.4097 0.0495  -0.0145 0.1037  71  TYR A N   
361  C CA  . TYR A 71  ? 0.4000 0.4443 0.3717 0.0609  -0.0088 0.1117  71  TYR A CA  
362  C C   . TYR A 71  ? 0.4889 0.5177 0.4479 0.0515  -0.0076 0.1068  71  TYR A C   
363  O O   . TYR A 71  ? 0.5177 0.5324 0.4662 0.0587  -0.0026 0.1127  71  TYR A O   
364  C CB  . TYR A 71  ? 0.3994 0.4163 0.3701 0.0729  0.0005  0.1106  71  TYR A CB  
365  C CG  . TYR A 71  ? 0.3950 0.4258 0.3744 0.0865  0.0011  0.1180  71  TYR A CG  
366  C CD1 . TYR A 71  ? 0.4459 0.4881 0.4211 0.1048  0.0037  0.1338  71  TYR A CD1 
367  C CD2 . TYR A 71  ? 0.4486 0.4833 0.4400 0.0822  -0.0003 0.1104  71  TYR A CD2 
368  C CE1 . TYR A 71  ? 0.5587 0.6165 0.5417 0.1195  0.0056  0.1419  71  TYR A CE1 
369  C CE2 . TYR A 71  ? 0.4722 0.5215 0.4714 0.0948  0.0008  0.1176  71  TYR A CE2 
370  C CZ  . TYR A 71  ? 0.4825 0.5440 0.4778 0.1138  0.0041  0.1334  71  TYR A CZ  
371  O OH  . TYR A 71  ? 0.6450 0.7230 0.6477 0.1285  0.0065  0.1417  71  TYR A OH  
372  N N   . HIS A 72  ? 0.3865 0.4162 0.3437 0.0364  -0.0113 0.0969  72  HIS A N   
373  C CA  . HIS A 72  ? 0.4001 0.4163 0.3442 0.0282  -0.0093 0.0923  72  HIS A CA  
374  C C   . HIS A 72  ? 0.4817 0.5148 0.4169 0.0161  -0.0174 0.0922  72  HIS A C   
375  O O   . HIS A 72  ? 0.4602 0.4948 0.3955 0.0059  -0.0208 0.0841  72  HIS A O   
376  C CB  . HIS A 72  ? 0.3825 0.3769 0.3281 0.0229  -0.0032 0.0796  72  HIS A CB  
377  C CG  . HIS A 72  ? 0.4650 0.4421 0.4158 0.0303  0.0039  0.0793  72  HIS A CG  
378  N ND1 . HIS A 72  ? 0.5052 0.4662 0.4465 0.0341  0.0097  0.0840  72  HIS A ND1 
379  C CD2 . HIS A 72  ? 0.4567 0.4279 0.4179 0.0327  0.0059  0.0748  72  HIS A CD2 
380  C CE1 . HIS A 72  ? 0.4957 0.4401 0.4397 0.0372  0.0150  0.0821  72  HIS A CE1 
381  N NE2 . HIS A 72  ? 0.4171 0.3681 0.3735 0.0367  0.0126  0.0765  72  HIS A NE2 
382  N N   . THR A 73  ? 0.4583 0.5017 0.3827 0.0163  -0.0203 0.1014  73  THR A N   
383  C CA  . THR A 73  ? 0.4512 0.5115 0.3637 0.0026  -0.0289 0.1026  73  THR A CA  
384  C C   . THR A 73  ? 0.5892 0.6283 0.4875 -0.0112 -0.0272 0.0885  73  THR A C   
385  O O   . THR A 73  ? 0.5798 0.6242 0.4682 -0.0249 -0.0336 0.0844  73  THR A O   
386  C CB  . THR A 73  ? 0.5974 0.6691 0.4987 0.0055  -0.0312 0.1146  73  THR A CB  
387  O OG1 . THR A 73  ? 0.6492 0.7441 0.5616 0.0201  -0.0329 0.1297  73  THR A OG1 
388  C CG2 . THR A 73  ? 0.6255 0.7116 0.5102 -0.0118 -0.0403 0.1148  73  THR A CG2 
389  N N   . GLU A 74  ? 0.4971 0.5116 0.3922 -0.0077 -0.0181 0.0815  74  GLU A N   
390  C CA  . GLU A 74  ? 0.4639 0.4587 0.3437 -0.0167 -0.0142 0.0700  74  GLU A CA  
391  C C   . GLU A 74  ? 0.4789 0.4672 0.3615 -0.0218 -0.0148 0.0603  74  GLU A C   
392  O O   . GLU A 74  ? 0.4952 0.4680 0.3590 -0.0304 -0.0134 0.0521  74  GLU A O   
393  C CB  . GLU A 74  ? 0.5594 0.5360 0.4397 -0.0103 -0.0036 0.0665  74  GLU A CB  
394  C CG  . GLU A 74  ? 0.4812 0.4589 0.3574 -0.0051 -0.0015 0.0758  74  GLU A CG  
395  C CD  . GLU A 74  ? 0.5896 0.5661 0.4814 0.0058  0.0020  0.0816  74  GLU A CD  
396  O OE1 . GLU A 74  ? 0.5040 0.4909 0.4083 0.0110  -0.0019 0.0852  74  GLU A OE1 
397  O OE2 . GLU A 74  ? 0.5720 0.5357 0.4610 0.0086  0.0092  0.0830  74  GLU A OE2 
398  N N   . ILE A 75  ? 0.4480 0.4439 0.3508 -0.0158 -0.0155 0.0609  75  ILE A N   
399  C CA  . ILE A 75  ? 0.5263 0.5141 0.4322 -0.0193 -0.0149 0.0519  75  ILE A CA  
400  C C   . ILE A 75  ? 0.4459 0.4531 0.3592 -0.0244 -0.0238 0.0557  75  ILE A C   
401  O O   . ILE A 75  ? 0.4312 0.4348 0.3519 -0.0250 -0.0236 0.0503  75  ILE A O   
402  C CB  . ILE A 75  ? 0.4387 0.4164 0.3609 -0.0095 -0.0069 0.0473  75  ILE A CB  
403  C CG1 . ILE A 75  ? 0.4418 0.4300 0.3827 0.0002  -0.0070 0.0547  75  ILE A CG1 
404  C CG2 . ILE A 75  ? 0.4608 0.4233 0.3755 -0.0070 0.0021  0.0434  75  ILE A CG2 
405  C CD1 . ILE A 75  ? 0.4204 0.3994 0.3751 0.0059  -0.0009 0.0497  75  ILE A CD1 
406  N N   . LYS A 76  ? 0.4562 0.4866 0.3671 -0.0283 -0.0317 0.0659  76  LYS A N   
407  C CA  . LYS A 76  ? 0.5492 0.6050 0.4690 -0.0333 -0.0400 0.0716  76  LYS A CA  
408  C C   . LYS A 76  ? 0.5317 0.5781 0.4368 -0.0502 -0.0440 0.0630  76  LYS A C   
409  O O   . LYS A 76  ? 0.5035 0.5643 0.4188 -0.0536 -0.0484 0.0646  76  LYS A O   
410  C CB  . LYS A 76  ? 0.5874 0.6753 0.5066 -0.0347 -0.0478 0.0860  76  LYS A CB  
411  C CG  . LYS A 76  ? 0.6380 0.7401 0.5759 -0.0145 -0.0442 0.0975  76  LYS A CG  
412  C CD  . LYS A 76  ? 0.7747 0.9126 0.7129 -0.0125 -0.0513 0.1142  76  LYS A CD  
413  C CE  . LYS A 76  ? 0.8574 1.0032 0.8101 0.0110  -0.0456 0.1259  76  LYS A CE  
414  N NZ  . LYS A 76  ? 0.7857 0.9654 0.7380 0.0180  -0.0504 0.1440  76  LYS A NZ  
415  N N   . ARG A 77  ? 0.4840 0.5033 0.3634 -0.0598 -0.0414 0.0540  77  ARG A N   
416  C CA  . ARG A 77  ? 0.5347 0.5333 0.3923 -0.0747 -0.0427 0.0446  77  ARG A CA  
417  C C   . ARG A 77  ? 0.5044 0.4879 0.3735 -0.0673 -0.0368 0.0368  77  ARG A C   
418  O O   . ARG A 77  ? 0.4811 0.4463 0.3328 -0.0782 -0.0375 0.0299  77  ARG A O   
419  C CB  . ARG A 77  ? 0.5226 0.4890 0.3473 -0.0812 -0.0377 0.0366  77  ARG A CB  
420  C CG  . ARG A 77  ? 0.6330 0.5743 0.4610 -0.0654 -0.0247 0.0291  77  ARG A CG  
421  C CD  . ARG A 77  ? 0.7602 0.6718 0.5551 -0.0691 -0.0183 0.0227  77  ARG A CD  
422  N NE  . ARG A 77  ? 0.7964 0.7205 0.5852 -0.0720 -0.0216 0.0295  77  ARG A NE  
423  C CZ  . ARG A 77  ? 1.0122 0.9161 0.7695 -0.0786 -0.0188 0.0262  77  ARG A CZ  
424  N NH1 . ARG A 77  ? 0.9585 0.8258 0.6851 -0.0819 -0.0115 0.0160  77  ARG A NH1 
425  N NH2 . ARG A 77  ? 0.8048 0.7237 0.5589 -0.0810 -0.0226 0.0336  77  ARG A NH2 
426  N N   . TYR A 78  ? 0.4300 0.4184 0.3252 -0.0502 -0.0310 0.0380  78  TYR A N   
427  C CA  . TYR A 78  ? 0.3901 0.3711 0.2981 -0.0445 -0.0276 0.0326  78  TYR A CA  
428  C C   . TYR A 78  ? 0.4916 0.4896 0.4042 -0.0542 -0.0357 0.0357  78  TYR A C   
429  O O   . TYR A 78  ? 0.4112 0.3963 0.3218 -0.0567 -0.0343 0.0296  78  TYR A O   
430  C CB  . TYR A 78  ? 0.4127 0.4004 0.3469 -0.0278 -0.0220 0.0349  78  TYR A CB  
431  C CG  . TYR A 78  ? 0.3673 0.3506 0.3143 -0.0233 -0.0197 0.0302  78  TYR A CG  
432  C CD1 . TYR A 78  ? 0.3876 0.3484 0.3274 -0.0210 -0.0129 0.0216  78  TYR A CD1 
433  C CD2 . TYR A 78  ? 0.3765 0.3790 0.3417 -0.0206 -0.0238 0.0353  78  TYR A CD2 
434  C CE1 . TYR A 78  ? 0.3537 0.3114 0.3044 -0.0168 -0.0111 0.0179  78  TYR A CE1 
435  C CE2 . TYR A 78  ? 0.3325 0.3303 0.3080 -0.0171 -0.0218 0.0308  78  TYR A CE2 
436  C CZ  . TYR A 78  ? 0.3382 0.3138 0.3066 -0.0158 -0.0159 0.0222  78  TYR A CZ  
437  O OH  . TYR A 78  ? 0.3473 0.3192 0.3252 -0.0120 -0.0140 0.0185  78  TYR A OH  
438  N N   . GLU A 79  ? 0.4230 0.4520 0.3414 -0.0597 -0.0441 0.0463  79  GLU A N   
439  C CA  . GLU A 79  ? 0.4425 0.4935 0.3661 -0.0700 -0.0519 0.0509  79  GLU A CA  
440  C C   . GLU A 79  ? 0.4368 0.4655 0.3317 -0.0904 -0.0548 0.0428  79  GLU A C   
441  O O   . GLU A 79  ? 0.4378 0.4697 0.3348 -0.0978 -0.0577 0.0419  79  GLU A O   
442  C CB  . GLU A 79  ? 0.4566 0.5494 0.3887 -0.0730 -0.0604 0.0655  79  GLU A CB  
443  C CG  . GLU A 79  ? 0.4344 0.5296 0.3416 -0.0897 -0.0667 0.0678  79  GLU A CG  
444  C CD  . GLU A 79  ? 0.4997 0.6431 0.4168 -0.0927 -0.0759 0.0844  79  GLU A CD  
445  O OE1 . GLU A 79  ? 0.5091 0.6857 0.4488 -0.0863 -0.0786 0.0940  79  GLU A OE1 
446  O OE2 . GLU A 79  ? 0.5133 0.6625 0.4149 -0.1007 -0.0801 0.0885  79  GLU A OE2 
447  N N   . ASP A 80  ? 0.4505 0.4529 0.3154 -0.0998 -0.0534 0.0369  80  ASP A N   
448  C CA  . ASP A 80  ? 0.4840 0.4555 0.3139 -0.1189 -0.0545 0.0285  80  ASP A CA  
449  C C   . ASP A 80  ? 0.5704 0.5033 0.3936 -0.1087 -0.0439 0.0172  80  ASP A C   
450  O O   . ASP A 80  ? 0.5784 0.4887 0.3807 -0.1204 -0.0442 0.0117  80  ASP A O   
451  C CB  . ASP A 80  ? 0.4881 0.4428 0.2834 -0.1326 -0.0562 0.0266  80  ASP A CB  
452  C CG  . ASP A 80  ? 0.6440 0.6402 0.4434 -0.1454 -0.0681 0.0389  80  ASP A CG  
453  O OD1 . ASP A 80  ? 0.6512 0.6841 0.4688 -0.1519 -0.0764 0.0479  80  ASP A OD1 
454  O OD2 . ASP A 80  ? 0.6372 0.6322 0.4227 -0.1478 -0.0689 0.0408  80  ASP A OD2 
455  N N   . ILE A 81  ? 0.4465 0.3721 0.2856 -0.0877 -0.0345 0.0146  81  ILE A N   
456  C CA  . ILE A 81  ? 0.4577 0.3570 0.2967 -0.0759 -0.0250 0.0067  81  ILE A CA  
457  C C   . ILE A 81  ? 0.4516 0.3666 0.3132 -0.0741 -0.0281 0.0086  81  ILE A C   
458  O O   . ILE A 81  ? 0.5125 0.4054 0.3619 -0.0765 -0.0254 0.0030  81  ILE A O   
459  C CB  . ILE A 81  ? 0.4979 0.3955 0.3528 -0.0558 -0.0155 0.0058  81  ILE A CB  
460  C CG1 . ILE A 81  ? 0.5100 0.3897 0.3400 -0.0569 -0.0110 0.0035  81  ILE A CG1 
461  C CG2 . ILE A 81  ? 0.4800 0.3622 0.3421 -0.0425 -0.0070 0.0004  81  ILE A CG2 
462  C CD1 . ILE A 81  ? 0.5553 0.4428 0.4039 -0.0402 -0.0034 0.0053  81  ILE A CD1 
463  N N   . HIS A 82  ? 0.3963 0.3477 0.2888 -0.0688 -0.0331 0.0170  82  HIS A N   
464  C CA  . HIS A 82  ? 0.3567 0.3245 0.2714 -0.0653 -0.0352 0.0194  82  HIS A CA  
465  C C   . HIS A 82  ? 0.4674 0.4353 0.3661 -0.0847 -0.0422 0.0197  82  HIS A C   
466  O O   . HIS A 82  ? 0.4678 0.4244 0.3663 -0.0852 -0.0405 0.0158  82  HIS A O   
467  C CB  . HIS A 82  ? 0.3288 0.3326 0.2732 -0.0554 -0.0382 0.0293  82  HIS A CB  
468  C CG  . HIS A 82  ? 0.3716 0.3891 0.3390 -0.0474 -0.0378 0.0313  82  HIS A CG  
469  N ND1 . HIS A 82  ? 0.4617 0.5002 0.4338 -0.0566 -0.0443 0.0365  82  HIS A ND1 
470  C CD2 . HIS A 82  ? 0.3272 0.3406 0.3125 -0.0321 -0.0318 0.0291  82  HIS A CD2 
471  C CE1 . HIS A 82  ? 0.4844 0.5295 0.4762 -0.0456 -0.0415 0.0370  82  HIS A CE1 
472  N NE2 . HIS A 82  ? 0.4343 0.4631 0.4332 -0.0314 -0.0342 0.0322  82  HIS A NE2 
473  N N   . LYS A 83  ? 0.4435 0.4247 0.3274 -0.1025 -0.0504 0.0247  83  LYS A N   
474  C CA  . LYS A 83  ? 0.4922 0.4796 0.3626 -0.1240 -0.0581 0.0266  83  LYS A CA  
475  C C   . LYS A 83  ? 0.5612 0.4995 0.3918 -0.1371 -0.0546 0.0158  83  LYS A C   
476  O O   . LYS A 83  ? 0.6086 0.5422 0.4267 -0.1531 -0.0586 0.0154  83  LYS A O   
477  C CB  . LYS A 83  ? 0.5501 0.5730 0.4175 -0.1411 -0.0691 0.0371  83  LYS A CB  
478  C CG  . LYS A 83  ? 0.5207 0.5211 0.3521 -0.1567 -0.0710 0.0334  83  LYS A CG  
479  C CD  . LYS A 83  ? 0.6009 0.6456 0.4377 -0.1680 -0.0816 0.0461  83  LYS A CD  
480  C CE  . LYS A 83  ? 0.6013 0.6240 0.3971 -0.1895 -0.0854 0.0426  83  LYS A CE  
481  N NZ  . LYS A 83  ? 0.5696 0.6398 0.3704 -0.2015 -0.0968 0.0563  83  LYS A NZ  
482  N N   . THR A 84  ? 0.5025 0.4030 0.3108 -0.1301 -0.0462 0.0076  84  THR A N   
483  C CA  . THR A 84  ? 0.5839 0.4319 0.3508 -0.1374 -0.0400 -0.0024 84  THR A CA  
484  C C   . THR A 84  ? 0.6347 0.4621 0.4123 -0.1154 -0.0291 -0.0079 84  THR A C   
485  O O   . THR A 84  ? 0.5802 0.3982 0.3558 -0.1183 -0.0289 -0.0095 84  THR A O   
486  C CB  . THR A 84  ? 0.5991 0.4151 0.3294 -0.1422 -0.0359 -0.0074 84  THR A CB  
487  O OG1 . THR A 84  ? 0.6585 0.4840 0.4103 -0.1199 -0.0293 -0.0067 84  THR A OG1 
488  C CG2 . THR A 84  ? 0.6768 0.5102 0.3899 -0.1683 -0.0478 -0.0021 84  THR A CG2 
489  N N   . LYS A 85  ? 0.5139 0.3375 0.3037 -0.0940 -0.0204 -0.0098 85  LYS A N   
490  C CA  . LYS A 85  ? 0.6131 0.4176 0.4086 -0.0738 -0.0096 -0.0142 85  LYS A CA  
491  C C   . LYS A 85  ? 0.5441 0.3782 0.3788 -0.0642 -0.0119 -0.0105 85  LYS A C   
492  O O   . LYS A 85  ? 0.4626 0.2812 0.2956 -0.0574 -0.0072 -0.0134 85  LYS A O   
493  C CB  . LYS A 85  ? 0.4969 0.2960 0.2955 -0.0558 -0.0002 -0.0156 85  LYS A CB  
494  C CG  . LYS A 85  ? 0.5975 0.3629 0.3539 -0.0629 0.0040  -0.0199 85  LYS A CG  
495  C CD  . LYS A 85  ? 0.7696 0.5148 0.5181 -0.0418 0.0180  -0.0229 85  LYS A CD  
496  C CE  . LYS A 85  ? 0.9062 0.6193 0.6130 -0.0474 0.0230  -0.0267 85  LYS A CE  
497  N NZ  . LYS A 85  ? 1.0839 0.7743 0.7782 -0.0252 0.0387  -0.0291 85  LYS A NZ  
498  N N   . VAL A 86  ? 0.4221 0.2962 0.2900 -0.0619 -0.0180 -0.0038 86  VAL A N   
499  C CA  . VAL A 86  ? 0.3854 0.2830 0.2865 -0.0518 -0.0188 -0.0007 86  VAL A CA  
500  C C   . VAL A 86  ? 0.3943 0.2962 0.2928 -0.0646 -0.0248 0.0006  86  VAL A C   
501  O O   . VAL A 86  ? 0.4209 0.3190 0.3284 -0.0579 -0.0222 -0.0010 86  VAL A O   
502  C CB  . VAL A 86  ? 0.3932 0.3258 0.3245 -0.0447 -0.0220 0.0062  86  VAL A CB  
503  C CG1 . VAL A 86  ? 0.3720 0.3248 0.3316 -0.0363 -0.0230 0.0092  86  VAL A CG1 
504  C CG2 . VAL A 86  ? 0.4198 0.3471 0.3542 -0.0325 -0.0154 0.0049  86  VAL A CG2 
505  N N   . ASN A 87  ? 0.4715 0.3842 0.3578 -0.0840 -0.0331 0.0045  87  ASN A N   
506  C CA  . ASN A 87  ? 0.5461 0.4644 0.4268 -0.0999 -0.0392 0.0066  87  ASN A CA  
507  C C   . ASN A 87  ? 0.5271 0.4006 0.3763 -0.1048 -0.0339 -0.0013 87  ASN A C   
508  O O   . ASN A 87  ? 0.4768 0.3498 0.3307 -0.1063 -0.0343 -0.0012 87  ASN A O   
509  C CB  . ASN A 87  ? 0.5720 0.5105 0.4407 -0.1229 -0.0493 0.0128  87  ASN A CB  
510  C CG  . ASN A 87  ? 0.7518 0.7019 0.6152 -0.1423 -0.0562 0.0166  87  ASN A CG  
511  O OD1 . ASN A 87  ? 0.8299 0.7525 0.6572 -0.1639 -0.0585 0.0129  87  ASN A OD1 
512  N ND2 . ASN A 87  ? 0.6994 0.6886 0.5964 -0.1352 -0.0590 0.0242  87  ASN A ND2 
513  N N   . SER A 88  ? 0.4971 0.3304 0.3112 -0.1070 -0.0283 -0.0078 88  SER A N   
514  C CA  . SER A 88  ? 0.6128 0.3971 0.3918 -0.1081 -0.0210 -0.0149 88  SER A CA  
515  C C   . SER A 88  ? 0.5218 0.3020 0.3206 -0.0840 -0.0126 -0.0166 88  SER A C   
516  O O   . SER A 88  ? 0.5465 0.3077 0.3348 -0.0848 -0.0103 -0.0183 88  SER A O   
517  C CB  . SER A 88  ? 0.6326 0.3729 0.3686 -0.1105 -0.0144 -0.0210 88  SER A CB  
518  O OG  . SER A 88  ? 0.7785 0.5191 0.4904 -0.1365 -0.0229 -0.0198 88  SER A OG  
519  N N   . LEU A 89  ? 0.5131 0.3113 0.3392 -0.0637 -0.0081 -0.0155 89  LEU A N   
520  C CA  . LEU A 89  ? 0.4494 0.2505 0.2962 -0.0427 -0.0013 -0.0159 89  LEU A CA  
521  C C   . LEU A 89  ? 0.4979 0.3243 0.3708 -0.0445 -0.0070 -0.0125 89  LEU A C   
522  O O   . LEU A 89  ? 0.4162 0.2305 0.2881 -0.0372 -0.0031 -0.0137 89  LEU A O   
523  C CB  . LEU A 89  ? 0.3984 0.2207 0.2706 -0.0261 0.0024  -0.0142 89  LEU A CB  
524  C CG  . LEU A 89  ? 0.4018 0.2395 0.3020 -0.0080 0.0067  -0.0127 89  LEU A CG  
525  C CD1 . LEU A 89  ? 0.4438 0.2514 0.3237 0.0034  0.0160  -0.0154 89  LEU A CD1 
526  C CD2 . LEU A 89  ? 0.4272 0.2869 0.3496 0.0028  0.0091  -0.0104 89  LEU A CD2 
527  N N   . LEU A 90  ? 0.4011 0.2630 0.2967 -0.0527 -0.0155 -0.0073 90  LEU A N   
528  C CA  . LEU A 90  ? 0.3913 0.2781 0.3103 -0.0537 -0.0201 -0.0034 90  LEU A CA  
529  C C   . LEU A 90  ? 0.4133 0.2814 0.3100 -0.0684 -0.0221 -0.0045 90  LEU A C   
530  O O   . LEU A 90  ? 0.4756 0.3441 0.3812 -0.0633 -0.0208 -0.0044 90  LEU A O   
531  C CB  . LEU A 90  ? 0.4280 0.3545 0.3699 -0.0585 -0.0274 0.0037  90  LEU A CB  
532  C CG  . LEU A 90  ? 0.3811 0.3369 0.3465 -0.0586 -0.0315 0.0093  90  LEU A CG  
533  C CD1 . LEU A 90  ? 0.4044 0.3586 0.3876 -0.0421 -0.0264 0.0071  90  LEU A CD1 
534  C CD2 . LEU A 90  ? 0.3822 0.3754 0.3679 -0.0578 -0.0364 0.0175  90  LEU A CD2 
535  N N   . ASN A 91  ? 0.4897 0.3399 0.3550 -0.0881 -0.0254 -0.0055 91  ASN A N   
536  C CA  . ASN A 91  ? 0.5163 0.3456 0.3565 -0.1051 -0.0274 -0.0065 91  ASN A CA  
537  C C   . ASN A 91  ? 0.5780 0.3597 0.3920 -0.0947 -0.0175 -0.0128 91  ASN A C   
538  O O   . ASN A 91  ? 0.5064 0.2755 0.3124 -0.0987 -0.0170 -0.0129 91  ASN A O   
539  C CB  . ASN A 91  ? 0.5199 0.3421 0.3298 -0.1328 -0.0343 -0.0055 91  ASN A CB  
540  C CG  . ASN A 91  ? 0.5690 0.4456 0.4060 -0.1443 -0.0449 0.0038  91  ASN A CG  
541  O OD1 . ASN A 91  ? 0.6219 0.5353 0.4937 -0.1357 -0.0470 0.0095  91  ASN A OD1 
542  N ND2 . ASN A 91  ? 0.6604 0.5424 0.4804 -0.1624 -0.0510 0.0060  91  ASN A ND2 
543  N N   . GLU A 92  ? 0.4878 0.2442 0.2883 -0.0800 -0.0091 -0.0171 92  GLU A N   
544  C CA  . GLU A 92  ? 0.5716 0.2888 0.3517 -0.0636 0.0020  -0.0210 92  GLU A CA  
545  C C   . GLU A 92  ? 0.5329 0.2738 0.3481 -0.0446 0.0040  -0.0183 92  GLU A C   
546  O O   . GLU A 92  ? 0.5209 0.2382 0.3229 -0.0371 0.0096  -0.0191 92  GLU A O   
547  C CB  . GLU A 92  ? 0.5532 0.2478 0.3166 -0.0491 0.0112  -0.0242 92  GLU A CB  
548  C CG  . GLU A 92  ? 0.6464 0.2960 0.3586 -0.0647 0.0135  -0.0287 92  GLU A CG  
549  C CD  . GLU A 92  ? 0.9689 0.5685 0.6369 -0.0743 0.0175  -0.0317 92  GLU A CD  
550  O OE1 . GLU A 92  ? 0.8663 0.4425 0.5265 -0.0545 0.0274  -0.0322 92  GLU A OE1 
551  O OE2 . GLU A 92  ? 1.0390 0.6242 0.6797 -0.1023 0.0104  -0.0329 92  GLU A OE2 
552  N N   . ALA A 93  ? 0.4538 0.2384 0.3104 -0.0366 0.0001  -0.0150 93  ALA A N   
553  C CA  . ALA A 93  ? 0.4429 0.2499 0.3304 -0.0220 0.0011  -0.0126 93  ALA A CA  
554  C C   . ALA A 93  ? 0.4634 0.2760 0.3537 -0.0327 -0.0040 -0.0107 93  ALA A C   
555  O O   . ALA A 93  ? 0.4316 0.2362 0.3230 -0.0238 -0.0005 -0.0106 93  ALA A O   
556  C CB  . ALA A 93  ? 0.3733 0.2200 0.2978 -0.0147 -0.0021 -0.0098 93  ALA A CB  
557  N N   . SER A 94  ? 0.4369 0.2664 0.3290 -0.0517 -0.0122 -0.0082 94  SER A N   
558  C CA  . SER A 94  ? 0.4553 0.2935 0.3502 -0.0629 -0.0167 -0.0054 94  SER A CA  
559  C C   . SER A 94  ? 0.4855 0.2793 0.3418 -0.0709 -0.0128 -0.0085 94  SER A C   
560  O O   . SER A 94  ? 0.4836 0.2735 0.3411 -0.0695 -0.0120 -0.0074 94  SER A O   
561  C CB  . SER A 94  ? 0.5469 0.4167 0.4505 -0.0818 -0.0259 -0.0001 94  SER A CB  
562  O OG  . SER A 94  ? 0.6013 0.5131 0.5432 -0.0709 -0.0283 0.0045  94  SER A OG  
563  N N   . ARG A 95  ? 0.5164 0.2727 0.3351 -0.0790 -0.0098 -0.0123 95  ARG A N   
564  C CA  . ARG A 95  ? 0.5588 0.2633 0.3332 -0.0856 -0.0043 -0.0155 95  ARG A CA  
565  C C   . ARG A 95  ? 0.6081 0.2934 0.3828 -0.0600 0.0055  -0.0164 95  ARG A C   
566  O O   . ARG A 95  ? 0.5702 0.2334 0.3289 -0.0611 0.0081  -0.0160 95  ARG A O   
567  C CB  . ARG A 95  ? 0.6336 0.2965 0.3631 -0.0971 -0.0014 -0.0200 95  ARG A CB  
568  C CG  . ARG A 95  ? 0.7074 0.3091 0.3822 -0.1080 0.0043  -0.0235 95  ARG A CG  
569  C CD  . ARG A 95  ? 0.8946 0.4636 0.5259 -0.1188 0.0074  -0.0267 95  ARG A CD  
570  N NE  . ARG A 95  ? 0.9972 0.5481 0.6224 -0.0946 0.0177  -0.0296 95  ARG A NE  
571  C CZ  . ARG A 95  ? 1.0579 0.5803 0.6655 -0.0707 0.0306  -0.0296 95  ARG A CZ  
572  N NH1 . ARG A 95  ? 1.0735 0.5777 0.6655 -0.0676 0.0348  -0.0277 95  ARG A NH1 
573  N NH2 . ARG A 95  ? 1.1078 0.6228 0.7137 -0.0494 0.0395  -0.0306 95  ARG A NH2 
574  N N   . ALA A 96  ? 0.5582 0.2548 0.3516 -0.0373 0.0109  -0.0167 96  ALA A N   
575  C CA  . ALA A 96  ? 0.5850 0.2727 0.3825 -0.0123 0.0197  -0.0155 96  ALA A CA  
576  C C   . ALA A 96  ? 0.5523 0.2684 0.3794 -0.0088 0.0156  -0.0120 96  ALA A C   
577  O O   . ALA A 96  ? 0.5248 0.2220 0.3406 0.0009  0.0208  -0.0106 96  ALA A O   
578  C CB  . ALA A 96  ? 0.5202 0.2266 0.3379 0.0077  0.0244  -0.0148 96  ALA A CB  
579  N N   . ILE A 97  ? 0.4679 0.2288 0.3320 -0.0146 0.0073  -0.0101 97  ILE A N   
580  C CA  . ILE A 97  ? 0.4702 0.2570 0.3600 -0.0125 0.0036  -0.0071 97  ILE A CA  
581  C C   . ILE A 97  ? 0.4626 0.2273 0.3292 -0.0267 0.0023  -0.0065 97  ILE A C   
582  O O   . ILE A 97  ? 0.4821 0.2434 0.3509 -0.0193 0.0044  -0.0048 97  ILE A O   
583  C CB  . ILE A 97  ? 0.4589 0.2906 0.3843 -0.0176 -0.0040 -0.0050 97  ILE A CB  
584  C CG1 . ILE A 97  ? 0.4018 0.2527 0.3491 -0.0031 -0.0021 -0.0053 97  ILE A CG1 
585  C CG2 . ILE A 97  ? 0.4096 0.2635 0.3550 -0.0184 -0.0075 -0.0021 97  ILE A CG2 
586  C CD1 . ILE A 97  ? 0.4010 0.2596 0.3632 0.0149  0.0020  -0.0042 97  ILE A CD1 
587  N N   . GLY A 98  ? 0.5015 0.2512 0.3441 -0.0487 -0.0013 -0.0076 98  GLY A N   
588  C CA  . GLY A 98  ? 0.4946 0.2255 0.3141 -0.0667 -0.0034 -0.0064 98  GLY A CA  
589  C C   . GLY A 98  ? 0.5645 0.2409 0.3434 -0.0607 0.0055  -0.0085 98  GLY A C   
590  O O   . GLY A 98  ? 0.5741 0.2351 0.3381 -0.0693 0.0054  -0.0069 98  GLY A O   
591  N N   . ILE A 99  ? 0.5685 0.2135 0.3262 -0.0454 0.0141  -0.0114 99  ILE A N   
592  C CA  . ILE A 99  ? 0.6024 0.1953 0.3214 -0.0328 0.0248  -0.0119 99  ILE A CA  
593  C C   . ILE A 99  ? 0.5912 0.2001 0.3324 -0.0146 0.0269  -0.0076 99  ILE A C   
594  O O   . ILE A 99  ? 0.6348 0.2161 0.3515 -0.0101 0.0325  -0.0060 99  ILE A O   
595  C CB  . ILE A 99  ? 0.6097 0.1853 0.3134 -0.0138 0.0344  -0.0136 99  ILE A CB  
596  C CG1 . ILE A 99  ? 0.6465 0.2017 0.3197 -0.0333 0.0330  -0.0177 99  ILE A CG1 
597  C CG2 . ILE A 99  ? 0.6656 0.2182 0.3475 0.0075  0.0458  -0.0108 99  ILE A CG2 
598  C CD1 . ILE A 99  ? 0.7624 0.3083 0.4268 -0.0161 0.0412  -0.0191 99  ILE A CD1 
599  N N   . CYS A 100 ? 0.5246 0.1861 0.3142 -0.0048 0.0220  -0.0053 100 CYS A N   
600  C CA  . CYS A 100 ? 0.5556 0.2344 0.3659 0.0116  0.0234  -0.0012 100 CYS A CA  
601  C C   . CYS A 100 ? 0.5857 0.2790 0.4058 -0.0035 0.0167  0.0006  100 CYS A C   
602  O O   . CYS A 100 ? 0.5074 0.2189 0.3465 0.0076  0.0165  0.0038  100 CYS A O   
603  C CB  . CYS A 100 ? 0.4937 0.2181 0.3463 0.0278  0.0217  0.0003  100 CYS A CB  
604  S SG  . CYS A 100 ? 0.5651 0.2796 0.4096 0.0452  0.0298  -0.0005 100 CYS A SG  
605  N N   . ASN A 101 ? 0.5422 0.2294 0.3486 -0.0290 0.0113  -0.0007 101 ASN A N   
606  C CA  . ASN A 101 ? 0.5276 0.2375 0.3480 -0.0433 0.0049  0.0022  101 ASN A CA  
607  C C   . ASN A 101 ? 0.5945 0.2745 0.3920 -0.0406 0.0094  0.0045  101 ASN A C   
608  O O   . ASN A 101 ? 0.5062 0.2097 0.3225 -0.0427 0.0060  0.0076  101 ASN A O   
609  C CB  . ASN A 101 ? 0.5831 0.2989 0.3942 -0.0722 -0.0021 0.0023  101 ASN A CB  
610  C CG  . ASN A 101 ? 0.5917 0.3549 0.4382 -0.0745 -0.0086 0.0029  101 ASN A CG  
611  O OD1 . ASN A 101 ? 0.5807 0.3753 0.4615 -0.0573 -0.0088 0.0035  101 ASN A OD1 
612  N ND2 . ASN A 101 ? 0.6249 0.3933 0.4613 -0.0967 -0.0140 0.0035  101 ASN A ND2 
613  N N   . ARG A 102 ? 0.6121 0.2381 0.3667 -0.0353 0.0178  0.0034  102 ARG A N   
614  C CA  . ARG A 102 ? 0.6429 0.2362 0.3720 -0.0314 0.0230  0.0063  102 ARG A CA  
615  C C   . ARG A 102 ? 0.5989 0.2172 0.3566 -0.0049 0.0253  0.0103  102 ARG A C   
616  O O   . ARG A 102 ? 0.5944 0.2219 0.3594 -0.0060 0.0235  0.0136  102 ARG A O   
617  C CB  . ARG A 102 ? 0.7050 0.2547 0.3892 -0.0275 0.0318  0.0042  102 ARG A CB  
618  C CG  . ARG A 102 ? 0.8518 0.3785 0.5139 -0.0195 0.0378  0.0073  102 ARG A CG  
619  N N   . LEU A 103 ? 0.5876 0.2193 0.3615 0.0177  0.0290  0.0105  103 LEU A N   
620  C CA  . LEU A 103 ? 0.6117 0.2768 0.4169 0.0395  0.0294  0.0149  103 LEU A CA  
621  C C   . LEU A 103 ? 0.5740 0.2900 0.4209 0.0302  0.0197  0.0147  103 LEU A C   
622  O O   . LEU A 103 ? 0.5313 0.2662 0.3940 0.0381  0.0184  0.0181  103 LEU A O   
623  C CB  . LEU A 103 ? 0.5197 0.1969 0.3366 0.0607  0.0340  0.0156  103 LEU A CB  
624  C CG  . LEU A 103 ? 0.6487 0.2928 0.4329 0.0756  0.0448  0.0170  103 LEU A CG  
625  C CD1 . LEU A 103 ? 0.6675 0.3337 0.4684 0.0912  0.0480  0.0176  103 LEU A CD1 
626  C CD2 . LEU A 103 ? 0.6535 0.2930 0.4283 0.0907  0.0502  0.0231  103 LEU A CD2 
627  N N   . LYS A 104 ? 0.4561 0.1942 0.3195 0.0150  0.0135  0.0111  104 LYS A N   
628  C CA  . LYS A 104 ? 0.4174 0.1993 0.3156 0.0079  0.0060  0.0115  104 LYS A CA  
629  C C   . LYS A 104 ? 0.4918 0.2716 0.3839 -0.0037 0.0040  0.0140  104 LYS A C   
630  O O   . LYS A 104 ? 0.4659 0.2716 0.3796 0.0010  0.0016  0.0160  104 LYS A O   
631  C CB  . LYS A 104 ? 0.4438 0.2460 0.3554 -0.0057 0.0009  0.0088  104 LYS A CB  
632  C CG  . LYS A 104 ? 0.4342 0.2779 0.3777 -0.0103 -0.0049 0.0101  104 LYS A CG  
633  C CD  . LYS A 104 ? 0.4776 0.3439 0.4365 -0.0174 -0.0087 0.0088  104 LYS A CD  
634  C CE  . LYS A 104 ? 0.5496 0.4169 0.4975 -0.0389 -0.0124 0.0107  104 LYS A CE  
635  N NZ  . LYS A 104 ? 0.6927 0.5893 0.6595 -0.0431 -0.0164 0.0114  104 LYS A NZ  
636  N N   . ASN A 105 ? 0.4548 0.2032 0.3156 -0.0204 0.0049  0.0141  105 ASN A N   
637  C CA  . ASN A 105 ? 0.4586 0.2061 0.3125 -0.0339 0.0029  0.0172  105 ASN A CA  
638  C C   . ASN A 105 ? 0.5476 0.2787 0.3924 -0.0186 0.0076  0.0203  105 ASN A C   
639  O O   . ASN A 105 ? 0.5334 0.2828 0.3906 -0.0209 0.0053  0.0231  105 ASN A O   
640  C CB  . ASN A 105 ? 0.6084 0.3242 0.4268 -0.0585 0.0026  0.0169  105 ASN A CB  
641  C CG  . ASN A 105 ? 0.6885 0.4319 0.5200 -0.0771 -0.0040 0.0161  105 ASN A CG  
642  O OD1 . ASN A 105 ? 0.6851 0.4750 0.5532 -0.0748 -0.0085 0.0175  105 ASN A OD1 
643  N ND2 . ASN A 105 ? 0.7980 0.5116 0.5971 -0.0954 -0.0041 0.0143  105 ASN A ND2 
644  N N   . THR A 106 ? 0.5372 0.2354 0.3601 -0.0017 0.0146  0.0206  106 THR A N   
645  C CA  . THR A 106 ? 0.5454 0.2329 0.3618 0.0162  0.0192  0.0253  106 THR A CA  
646  C C   . THR A 106 ? 0.5269 0.2623 0.3838 0.0293  0.0151  0.0270  106 THR A C   
647  O O   . THR A 106 ? 0.5012 0.2465 0.3641 0.0325  0.0141  0.0305  106 THR A O   
648  C CB  . THR A 106 ? 0.6422 0.2903 0.4291 0.0357  0.0287  0.0270  106 THR A CB  
649  O OG1 . THR A 106 ? 0.7040 0.2985 0.4450 0.0221  0.0334  0.0250  106 THR A OG1 
650  C CG2 . THR A 106 ? 0.6852 0.3287 0.4680 0.0569  0.0334  0.0339  106 THR A CG2 
651  N N   . LEU A 107 ? 0.4845 0.2475 0.3666 0.0360  0.0129  0.0245  107 LEU A N   
652  C CA  . LEU A 107 ? 0.4363 0.2416 0.3529 0.0452  0.0088  0.0253  107 LEU A CA  
653  C C   . LEU A 107 ? 0.4844 0.3152 0.4194 0.0317  0.0030  0.0242  107 LEU A C   
654  O O   . LEU A 107 ? 0.3904 0.2407 0.3390 0.0372  0.0011  0.0263  107 LEU A O   
655  C CB  . LEU A 107 ? 0.4312 0.2557 0.3660 0.0508  0.0079  0.0225  107 LEU A CB  
656  C CG  . LEU A 107 ? 0.4715 0.3354 0.4375 0.0582  0.0040  0.0228  107 LEU A CG  
657  C CD1 . LEU A 107 ? 0.4630 0.3340 0.4297 0.0723  0.0052  0.0287  107 LEU A CD1 
658  C CD2 . LEU A 107 ? 0.4165 0.2899 0.3921 0.0639  0.0048  0.0210  107 LEU A CD2 
659  N N   . LEU A 108 ? 0.4192 0.2524 0.3544 0.0143  0.0004  0.0217  108 LEU A N   
660  C CA  . LEU A 108 ? 0.4331 0.2909 0.3835 0.0033  -0.0035 0.0224  108 LEU A CA  
661  C C   . LEU A 108 ? 0.4733 0.3201 0.4105 0.0009  -0.0022 0.0262  108 LEU A C   
662  O O   . LEU A 108 ? 0.4402 0.3092 0.3922 0.0013  -0.0039 0.0275  108 LEU A O   
663  C CB  . LEU A 108 ? 0.4217 0.2847 0.3709 -0.0146 -0.0059 0.0216  108 LEU A CB  
664  C CG  . LEU A 108 ? 0.4727 0.3620 0.4446 -0.0137 -0.0086 0.0191  108 LEU A CG  
665  C CD1 . LEU A 108 ? 0.6377 0.5268 0.6016 -0.0313 -0.0108 0.0197  108 LEU A CD1 
666  C CD2 . LEU A 108 ? 0.4035 0.3254 0.4001 -0.0094 -0.0102 0.0200  108 LEU A CD2 
667  N N   . GLY A 109 ? 0.4544 0.2637 0.3606 -0.0021 0.0015  0.0280  109 GLY A N   
668  C CA  . GLY A 109 ? 0.4239 0.2185 0.3142 -0.0041 0.0034  0.0322  109 GLY A CA  
669  C C   . GLY A 109 ? 0.4839 0.2916 0.3861 0.0140  0.0038  0.0347  109 GLY A C   
670  O O   . GLY A 109 ? 0.4810 0.3017 0.3891 0.0115  0.0024  0.0371  109 GLY A O   
671  N N   . LEU A 110 ? 0.4171 0.2236 0.3223 0.0318  0.0057  0.0350  110 LEU A N   
672  C CA  . LEU A 110 ? 0.4257 0.2494 0.3421 0.0478  0.0052  0.0387  110 LEU A CA  
673  C C   . LEU A 110 ? 0.4149 0.2776 0.3607 0.0442  -0.0004 0.0361  110 LEU A C   
674  O O   . LEU A 110 ? 0.3862 0.2611 0.3365 0.0459  -0.0020 0.0384  110 LEU A O   
675  C CB  . LEU A 110 ? 0.4287 0.2508 0.3449 0.0664  0.0082  0.0409  110 LEU A CB  
676  C CG  . LEU A 110 ? 0.6761 0.4593 0.5606 0.0797  0.0160  0.0460  110 LEU A CG  
677  C CD1 . LEU A 110 ? 0.5226 0.3110 0.4113 0.0968  0.0195  0.0477  110 LEU A CD1 
678  C CD2 . LEU A 110 ? 0.6208 0.3985 0.4943 0.0901  0.0179  0.0536  110 LEU A CD2 
679  N N   . ILE A 111 ? 0.3736 0.2532 0.3365 0.0392  -0.0028 0.0312  111 ILE A N   
680  C CA  . ILE A 111 ? 0.3686 0.2785 0.3542 0.0364  -0.0066 0.0285  111 ILE A CA  
681  C C   . ILE A 111 ? 0.3670 0.2822 0.3518 0.0275  -0.0070 0.0295  111 ILE A C   
682  O O   . ILE A 111 ? 0.3251 0.2561 0.3181 0.0300  -0.0085 0.0295  111 ILE A O   
683  C CB  . ILE A 111 ? 0.3510 0.2716 0.3497 0.0316  -0.0079 0.0239  111 ILE A CB  
684  C CG1 . ILE A 111 ? 0.3453 0.2694 0.3498 0.0419  -0.0079 0.0232  111 ILE A CG1 
685  C CG2 . ILE A 111 ? 0.3368 0.2804 0.3517 0.0270  -0.0099 0.0216  111 ILE A CG2 
686  C CD1 . ILE A 111 ? 0.3587 0.2852 0.3701 0.0376  -0.0081 0.0194  111 ILE A CD1 
687  N N   . ASN A 112 ? 0.3474 0.2502 0.3209 0.0159  -0.0056 0.0306  112 ASN A N   
688  C CA  . ASN A 112 ? 0.3806 0.2935 0.3550 0.0067  -0.0054 0.0326  112 ASN A CA  
689  C C   . ASN A 112 ? 0.3795 0.2831 0.3420 0.0106  -0.0043 0.0365  112 ASN A C   
690  O O   . ASN A 112 ? 0.4034 0.3213 0.3710 0.0082  -0.0042 0.0377  112 ASN A O   
691  C CB  . ASN A 112 ? 0.4099 0.3170 0.3758 -0.0094 -0.0049 0.0341  112 ASN A CB  
692  C CG  . ASN A 112 ? 0.4852 0.4155 0.4691 -0.0137 -0.0066 0.0320  112 ASN A CG  
693  O OD1 . ASN A 112 ? 0.4985 0.4534 0.4996 -0.0096 -0.0066 0.0316  112 ASN A OD1 
694  N ND2 . ASN A 112 ? 0.5321 0.4523 0.5096 -0.0208 -0.0074 0.0309  112 ASN A ND2 
695  N N   . ILE A 113 ? 0.3836 0.2631 0.3289 0.0181  -0.0026 0.0391  113 ILE A N   
696  C CA  . ILE A 113 ? 0.3663 0.2401 0.3017 0.0246  -0.0018 0.0436  113 ILE A CA  
697  C C   . ILE A 113 ? 0.3612 0.2600 0.3135 0.0350  -0.0049 0.0428  113 ILE A C   
698  O O   . ILE A 113 ? 0.3830 0.2922 0.3365 0.0347  -0.0059 0.0443  113 ILE A O   
699  C CB  . ILE A 113 ? 0.4105 0.2502 0.3202 0.0325  0.0020  0.0481  113 ILE A CB  
700  C CG1 . ILE A 113 ? 0.4855 0.2943 0.3712 0.0177  0.0051  0.0486  113 ILE A CG1 
701  C CG2 . ILE A 113 ? 0.4846 0.3215 0.3853 0.0425  0.0027  0.0541  113 ILE A CG2 
702  C CD1 . ILE A 113 ? 0.5403 0.3064 0.3948 0.0258  0.0105  0.0516  113 ILE A CD1 
703  N N   . LEU A 114 ? 0.3436 0.2522 0.3073 0.0428  -0.0066 0.0406  114 LEU A N   
704  C CA  . LEU A 114 ? 0.3437 0.2748 0.3195 0.0504  -0.0102 0.0408  114 LEU A CA  
705  C C   . LEU A 114 ? 0.3303 0.2800 0.3180 0.0428  -0.0123 0.0361  114 LEU A C   
706  O O   . LEU A 114 ? 0.3133 0.2753 0.3022 0.0445  -0.0149 0.0367  114 LEU A O   
707  C CB  . LEU A 114 ? 0.2967 0.2355 0.2814 0.0583  -0.0112 0.0402  114 LEU A CB  
708  C CG  . LEU A 114 ? 0.3398 0.2650 0.3121 0.0720  -0.0081 0.0469  114 LEU A CG  
709  C CD1 . LEU A 114 ? 0.3817 0.3090 0.3604 0.0780  -0.0069 0.0457  114 LEU A CD1 
710  C CD2 . LEU A 114 ? 0.3775 0.3185 0.3496 0.0820  -0.0104 0.0539  114 LEU A CD2 
711  N N   . GLU A 115 ? 0.3208 0.2725 0.3154 0.0352  -0.0110 0.0319  115 GLU A N   
712  C CA  . GLU A 115 ? 0.3447 0.3105 0.3475 0.0309  -0.0109 0.0282  115 GLU A CA  
713  C C   . GLU A 115 ? 0.3541 0.3203 0.3500 0.0266  -0.0083 0.0304  115 GLU A C   
714  O O   . GLU A 115 ? 0.3592 0.3349 0.3579 0.0260  -0.0070 0.0281  115 GLU A O   
715  C CB  . GLU A 115 ? 0.2993 0.2697 0.3119 0.0270  -0.0095 0.0249  115 GLU A CB  
716  C CG  . GLU A 115 ? 0.3726 0.3449 0.3932 0.0304  -0.0115 0.0219  115 GLU A CG  
717  C CD  . GLU A 115 ? 0.3476 0.3247 0.3769 0.0268  -0.0101 0.0194  115 GLU A CD  
718  O OE1 . GLU A 115 ? 0.3465 0.3256 0.3755 0.0213  -0.0080 0.0214  115 GLU A OE1 
719  O OE2 . GLU A 115 ? 0.3599 0.3410 0.3963 0.0292  -0.0113 0.0163  115 GLU A OE2 
720  N N   . ASN A 116 ? 0.3765 0.3306 0.3613 0.0234  -0.0068 0.0350  116 ASN A N   
721  C CA  . ASN A 116 ? 0.3746 0.3312 0.3541 0.0167  -0.0037 0.0379  116 ASN A CA  
722  C C   . ASN A 116 ? 0.3685 0.3143 0.3333 0.0187  -0.0038 0.0424  116 ASN A C   
723  O O   . ASN A 116 ? 0.3840 0.3107 0.3357 0.0176  -0.0032 0.0462  116 ASN A O   
724  C CB  . ASN A 116 ? 0.3761 0.3295 0.3542 0.0063  -0.0019 0.0401  116 ASN A CB  
725  C CG  . ASN A 116 ? 0.5313 0.4950 0.5071 -0.0022 0.0014  0.0444  116 ASN A CG  
726  O OD1 . ASN A 116 ? 0.4854 0.4485 0.4539 -0.0008 0.0028  0.0467  116 ASN A OD1 
727  N ND2 . ASN A 116 ? 0.5233 0.4993 0.5054 -0.0114 0.0027  0.0463  116 ASN A ND2 
728  N N   . PRO A 117 ? 0.3949 0.3494 0.3582 0.0215  -0.0039 0.0423  117 PRO A N   
729  C CA  . PRO A 117 ? 0.4259 0.3713 0.3748 0.0238  -0.0043 0.0474  117 PRO A CA  
730  C C   . PRO A 117 ? 0.4450 0.3764 0.3808 0.0162  -0.0008 0.0526  117 PRO A C   
731  O O   . PRO A 117 ? 0.4616 0.3750 0.3820 0.0190  -0.0008 0.0575  117 PRO A O   
732  C CB  . PRO A 117 ? 0.4178 0.3763 0.3668 0.0249  -0.0043 0.0453  117 PRO A CB  
733  C CG  . PRO A 117 ? 0.3778 0.3465 0.3386 0.0268  -0.0060 0.0388  117 PRO A CG  
734  C CD  . PRO A 117 ? 0.3762 0.3451 0.3471 0.0235  -0.0038 0.0375  117 PRO A CD  
735  N N   . GLN A 118 ? 0.4134 0.3531 0.3536 0.0064  0.0023  0.0528  118 GLN A N   
736  C CA  . GLN A 118 ? 0.5138 0.4428 0.4406 -0.0048 0.0052  0.0584  118 GLN A CA  
737  C C   . GLN A 118 ? 0.5320 0.4340 0.4449 -0.0087 0.0046  0.0599  118 GLN A C   
738  O O   . GLN A 118 ? 0.5501 0.4285 0.4417 -0.0127 0.0063  0.0648  118 GLN A O   
739  C CB  . GLN A 118 ? 0.4320 0.3831 0.3692 -0.0150 0.0083  0.0596  118 GLN A CB  
740  N N   . LYS A 119 ? 0.4742 0.3758 0.3958 -0.0069 0.0029  0.0558  119 LYS A N   
741  C CA  . LYS A 119 ? 0.4428 0.3148 0.3476 -0.0089 0.0033  0.0567  119 LYS A CA  
742  C C   . LYS A 119 ? 0.5275 0.3792 0.4195 0.0066  0.0035  0.0588  119 LYS A C   
743  O O   . LYS A 119 ? 0.5532 0.3718 0.4202 0.0067  0.0064  0.0626  119 LYS A O   
744  C CB  . LYS A 119 ? 0.4434 0.3216 0.3604 -0.0107 0.0017  0.0519  119 LYS A CB  
745  C CG  . LYS A 119 ? 0.5343 0.4275 0.4575 -0.0276 0.0018  0.0524  119 LYS A CG  
746  C CD  . LYS A 119 ? 0.5304 0.4264 0.4621 -0.0295 0.0000  0.0484  119 LYS A CD  
747  C CE  . LYS A 119 ? 0.8221 0.7343 0.7575 -0.0478 -0.0005 0.0508  119 LYS A CE  
748  N NZ  . LYS A 119 ? 0.9039 0.8560 0.8635 -0.0457 0.0000  0.0521  119 LYS A NZ  
749  N N   . PHE A 120 ? 0.4411 0.3120 0.3477 0.0197  0.0008  0.0574  120 PHE A N   
750  C CA  . PHE A 120 ? 0.5000 0.3602 0.3967 0.0351  0.0006  0.0618  120 PHE A CA  
751  C C   . PHE A 120 ? 0.4656 0.3094 0.3416 0.0354  0.0030  0.0686  120 PHE A C   
752  O O   . PHE A 120 ? 0.4885 0.3071 0.3442 0.0453  0.0058  0.0744  120 PHE A O   
753  C CB  . PHE A 120 ? 0.4151 0.3044 0.3312 0.0449  -0.0039 0.0599  120 PHE A CB  
754  C CG  . PHE A 120 ? 0.4089 0.2973 0.3173 0.0601  -0.0048 0.0668  120 PHE A CG  
755  C CD1 . PHE A 120 ? 0.4737 0.3493 0.3753 0.0727  -0.0028 0.0706  120 PHE A CD1 
756  C CD2 . PHE A 120 ? 0.4574 0.3584 0.3638 0.0626  -0.0073 0.0705  120 PHE A CD2 
757  C CE1 . PHE A 120 ? 0.4406 0.3194 0.3354 0.0894  -0.0028 0.0793  120 PHE A CE1 
758  C CE2 . PHE A 120 ? 0.5392 0.4439 0.4389 0.0770  -0.0085 0.0787  120 PHE A CE2 
759  C CZ  . PHE A 120 ? 0.4630 0.3584 0.3579 0.0912  -0.0062 0.0837  120 PHE A CZ  
760  N N   . LYS A 121 ? 0.4760 0.3325 0.3549 0.0260  0.0028  0.0686  121 LYS A N   
761  C CA  . LYS A 121 ? 0.5021 0.3453 0.3620 0.0263  0.0049  0.0752  121 LYS A CA  
762  C C   . LYS A 121 ? 0.5347 0.3415 0.3673 0.0166  0.0096  0.0794  121 LYS A C   
763  O O   . LYS A 121 ? 0.6063 0.3918 0.4166 0.0196  0.0122  0.0860  121 LYS A O   
764  C CB  . LYS A 121 ? 0.5218 0.3891 0.3913 0.0191  0.0042  0.0740  121 LYS A CB  
765  C CG  . LYS A 121 ? 0.5873 0.4806 0.4723 0.0284  -0.0001 0.0710  121 LYS A CG  
766  C CD  . LYS A 121 ? 0.6357 0.5460 0.5234 0.0230  0.0007  0.0699  121 LYS A CD  
767  C CE  . LYS A 121 ? 0.6282 0.5535 0.5301 0.0143  0.0032  0.0647  121 LYS A CE  
768  N NZ  . LYS A 121 ? 0.6824 0.6235 0.5855 0.0128  0.0054  0.0635  121 LYS A NZ  
769  N N   . THR A 122 ? 0.4919 0.2896 0.3231 0.0041  0.0107  0.0760  122 THR A N   
770  C CA  . THR A 122 ? 0.6189 0.3799 0.4205 -0.0101 0.0147  0.0793  122 THR A CA  
771  C C   . THR A 122 ? 0.7135 0.4374 0.4944 -0.0035 0.0175  0.0789  122 THR A C   
772  O O   . THR A 122 ? 0.7950 0.4903 0.5541 -0.0190 0.0199  0.0784  122 THR A O   
773  C CB  . THR A 122 ? 0.6404 0.4184 0.4505 -0.0330 0.0140  0.0774  122 THR A CB  
774  O OG1 . THR A 122 ? 0.6281 0.4305 0.4633 -0.0326 0.0109  0.0712  122 THR A OG1 
775  C CG2 . THR A 122 ? 0.6974 0.5050 0.5198 -0.0384 0.0138  0.0799  122 THR A CG2 
776  N N   . GLN A 123 ? 0.6066 0.3315 0.3926 0.0188  0.0174  0.0796  123 GLN A N   
777  C CA  . GLN A 123 ? 0.7028 0.3896 0.4644 0.0316  0.0223  0.0818  123 GLN A CA  
778  C C   . GLN A 123 ? 0.6543 0.3440 0.4140 0.0569  0.0236  0.0889  123 GLN A C   
779  O O   . GLN A 123 ? 0.6489 0.3688 0.4252 0.0606  0.0196  0.0911  123 GLN A O   
780  C CB  . GLN A 123 ? 0.6608 0.3553 0.4367 0.0319  0.0209  0.0752  123 GLN A CB  
781  C CG  . GLN A 123 ? 0.5219 0.2649 0.3375 0.0416  0.0152  0.0713  123 GLN A CG  
782  C CD  . GLN A 123 ? 0.6627 0.4109 0.4808 0.0666  0.0161  0.0763  123 GLN A CD  
783  O OE1 . GLN A 123 ? 0.5900 0.3146 0.3930 0.0789  0.0208  0.0783  123 GLN A OE1 
784  N NE2 . GLN A 123 ? 0.5270 0.3067 0.3619 0.0744  0.0120  0.0793  123 GLN A NE2 
785  N N   . ARG A 124 ? 0.6790 0.3384 0.4171 0.0752  0.0294  0.0935  124 ARG A N   
786  C CA  . ARG A 124 ? 0.7111 0.3704 0.4413 0.0997  0.0318  0.1035  124 ARG A CA  
787  C C   . ARG A 124 ? 0.6739 0.3561 0.4205 0.1239  0.0317  0.1068  124 ARG A C   
788  O O   . ARG A 124 ? 0.7112 0.4076 0.4588 0.1429  0.0326  0.1149  124 ARG A O   
789  C CB  . ARG A 124 ? 0.8876 0.4970 0.5764 0.1030  0.0406  0.1079  124 ARG A CB  
790  C CG  . ARG A 124 ? 0.9985 0.5868 0.6678 0.0819  0.0407  0.1090  124 ARG A CG  
791  C CD  . ARG A 124 ? 0.9866 0.5439 0.6259 0.0887  0.0476  0.1127  124 ARG A CD  
792  N NE  . ARG A 124 ? 1.1559 0.7374 0.8047 0.1079  0.0461  0.1214  124 ARG A NE  
793  C CZ  . ARG A 124 ? 1.2005 0.7649 0.8295 0.1223  0.0520  0.1265  124 ARG A CZ  
794  N NH1 . ARG A 124 ? 1.3170 0.8367 0.9129 0.1216  0.0607  0.1234  124 ARG A NH1 
795  N NH2 . ARG A 124 ? 1.0909 0.6833 0.7315 0.1376  0.0493  0.1350  124 ARG A NH2 
796  N N   . GLU A 125 ? 0.6646 0.3589 0.4281 0.1218  0.0303  0.0999  125 GLU A N   
797  C CA  . GLU A 125 ? 0.7126 0.4370 0.4959 0.1426  0.0294  0.1035  125 GLU A CA  
798  C C   . GLU A 125 ? 0.6353 0.4170 0.4548 0.1413  0.0198  0.1034  125 GLU A C   
799  O O   . GLU A 125 ? 0.6172 0.4178 0.4538 0.1219  0.0136  0.0957  125 GLU A O   
800  C CB  . GLU A 125 ? 0.6238 0.3457 0.4150 0.1385  0.0303  0.0957  125 GLU A CB  
801  C CG  . GLU A 125 ? 0.8988 0.5730 0.6580 0.1352  0.0391  0.0917  125 GLU A CG  
802  C CD  . GLU A 125 ? 1.0894 0.7578 0.8351 0.1565  0.0476  0.0959  125 GLU A CD  
803  O OE1 . GLU A 125 ? 1.0054 0.7109 0.7702 0.1742  0.0463  0.1029  125 GLU A OE1 
804  O OE2 . GLU A 125 ? 1.2474 0.8745 0.9614 0.1549  0.0560  0.0925  125 GLU A OE2 
805  N N   . SER A 126 ? 0.5678 0.3774 0.3970 0.1621  0.0189  0.1127  126 SER A N   
806  C CA  . SER A 126 ? 0.5319 0.3951 0.3916 0.1591  0.0093  0.1131  126 SER A CA  
807  C C   . SER A 126 ? 0.5050 0.3939 0.3921 0.1459  0.0039  0.1025  126 SER A C   
808  O O   . SER A 126 ? 0.5368 0.4107 0.4228 0.1461  0.0076  0.0980  126 SER A O   
809  C CB  . SER A 126 ? 0.5973 0.4895 0.4615 0.1825  0.0092  0.1267  126 SER A CB  
810  O OG  . SER A 126 ? 0.6241 0.5319 0.5013 0.1903  0.0119  0.1253  126 SER A OG  
811  N N   . TYR A 127 ? 0.4244 0.3493 0.3330 0.1340  -0.0046 0.0984  127 TYR A N   
812  C CA  . TYR A 127 ? 0.4255 0.3707 0.3566 0.1217  -0.0091 0.0886  127 TYR A CA  
813  C C   . TYR A 127 ? 0.4517 0.4185 0.3951 0.1344  -0.0090 0.0928  127 TYR A C   
814  O O   . TYR A 127 ? 0.4343 0.4005 0.3875 0.1294  -0.0085 0.0860  127 TYR A O   
815  C CB  . TYR A 127 ? 0.3915 0.3645 0.3365 0.1072  -0.0168 0.0837  127 TYR A CB  
816  C CG  . TYR A 127 ? 0.3479 0.3266 0.3077 0.0921  -0.0191 0.0720  127 TYR A CG  
817  C CD1 . TYR A 127 ? 0.3154 0.2730 0.2709 0.0804  -0.0162 0.0647  127 TYR A CD1 
818  C CD2 . TYR A 127 ? 0.3299 0.3358 0.3069 0.0898  -0.0237 0.0696  127 TYR A CD2 
819  C CE1 . TYR A 127 ? 0.3572 0.3208 0.3253 0.0693  -0.0175 0.0556  127 TYR A CE1 
820  C CE2 . TYR A 127 ? 0.3714 0.3786 0.3589 0.0775  -0.0249 0.0596  127 TYR A CE2 
821  C CZ  . TYR A 127 ? 0.3836 0.3696 0.3668 0.0687  -0.0215 0.0529  127 TYR A CZ  
822  O OH  . TYR A 127 ? 0.3372 0.3255 0.3301 0.0591  -0.0218 0.0445  127 TYR A OH  
823  N N   . ASP A 128 ? 0.4522 0.4395 0.3950 0.1519  -0.0091 0.1054  128 ASP A N   
824  C CA  . ASP A 128 ? 0.4935 0.5069 0.4486 0.1658  -0.0083 0.1119  128 ASP A CA  
825  C C   . ASP A 128 ? 0.4867 0.4652 0.4271 0.1789  0.0019  0.1122  128 ASP A C   
826  O O   . ASP A 128 ? 0.4874 0.4775 0.4397 0.1804  0.0029  0.1097  128 ASP A O   
827  C CB  . ASP A 128 ? 0.4701 0.5177 0.4277 0.1816  -0.0101 0.1268  128 ASP A CB  
828  C CG  . ASP A 128 ? 0.7430 0.8382 0.7199 0.1679  -0.0220 0.1276  128 ASP A CG  
829  O OD1 . ASP A 128 ? 0.8006 0.9071 0.7921 0.1492  -0.0273 0.1168  128 ASP A OD1 
830  O OD2 . ASP A 128 ? 0.9732 1.0917 0.9485 0.1729  -0.0255 0.1374  128 ASP A OD2 
831  N N   . VAL A 129 ? 0.5077 0.4420 0.4204 0.1845  0.0100  0.1131  129 VAL A N   
832  C CA  . VAL A 129 ? 0.5140 0.4108 0.4082 0.1890  0.0200  0.1088  129 VAL A CA  
833  C C   . VAL A 129 ? 0.5617 0.4394 0.4584 0.1752  0.0185  0.0987  129 VAL A C   
834  O O   . VAL A 129 ? 0.4994 0.3717 0.3971 0.1769  0.0225  0.0946  129 VAL A O   
835  C CB  . VAL A 129 ? 0.5679 0.4197 0.4283 0.1934  0.0284  0.1109  129 VAL A CB  
836  C CG1 . VAL A 129 ? 0.6982 0.5038 0.5339 0.1915  0.0376  0.1042  129 VAL A CG1 
837  C CG2 . VAL A 129 ? 0.6306 0.5010 0.4876 0.2114  0.0326  0.1213  129 VAL A CG2 
838  N N   . LEU A 130 ? 0.4223 0.2970 0.3238 0.1541  0.0128  0.0905  130 LEU A N   
839  C CA  . LEU A 130 ? 0.4378 0.3043 0.3466 0.1350  0.0109  0.0784  130 LEU A CA  
840  C C   . LEU A 130 ? 0.5097 0.4134 0.4471 0.1326  0.0058  0.0745  130 LEU A C   
841  O O   . LEU A 130 ? 0.4571 0.3522 0.3973 0.1271  0.0073  0.0681  130 LEU A O   
842  C CB  . LEU A 130 ? 0.4591 0.3234 0.3700 0.1144  0.0064  0.0719  130 LEU A CB  
843  C CG  . LEU A 130 ? 0.5227 0.3483 0.4045 0.1107  0.0110  0.0744  130 LEU A CG  
844  C CD1 . LEU A 130 ? 0.4966 0.3319 0.3855 0.0924  0.0064  0.0701  130 LEU A CD1 
845  C CD2 . LEU A 130 ? 0.5585 0.3413 0.4162 0.1060  0.0174  0.0712  130 LEU A CD2 
846  N N   . LEU A 131 ? 0.4512 0.3960 0.4084 0.1345  -0.0005 0.0783  131 LEU A N   
847  C CA  . LEU A 131 ? 0.4218 0.4006 0.4029 0.1305  -0.0052 0.0755  131 LEU A CA  
848  C C   . LEU A 131 ? 0.3890 0.3700 0.3697 0.1473  0.0005  0.0811  131 LEU A C   
849  O O   . LEU A 131 ? 0.4322 0.4192 0.4238 0.1423  0.0002  0.0756  131 LEU A O   
850  C CB  . LEU A 131 ? 0.3959 0.4160 0.3927 0.1271  -0.0132 0.0795  131 LEU A CB  
851  C CG  . LEU A 131 ? 0.3675 0.3927 0.3691 0.1079  -0.0195 0.0716  131 LEU A CG  
852  C CD1 . LEU A 131 ? 0.3894 0.4512 0.3993 0.1053  -0.0269 0.0770  131 LEU A CD1 
853  C CD2 . LEU A 131 ? 0.3243 0.3475 0.3366 0.0930  -0.0212 0.0602  131 LEU A CD2 
854  N N   . ARG A 132 ? 0.4247 0.4007 0.3917 0.1688  0.0065  0.0927  132 ARG A N   
855  C CA  A ARG A 132 ? 0.4473 0.4242 0.4115 0.1812  0.0139  0.0955  132 ARG A CA  
856  C CA  B ARG A 132 ? 0.4479 0.4241 0.4115 0.1815  0.0141  0.0956  132 ARG A CA  
857  C C   . ARG A 132 ? 0.4918 0.4239 0.4376 0.1782  0.0208  0.0874  132 ARG A C   
858  O O   . ARG A 132 ? 0.4855 0.4232 0.4377 0.1791  0.0231  0.0845  132 ARG A O   
859  C CB  A ARG A 132 ? 0.5049 0.4845 0.4559 0.1972  0.0207  0.1051  132 ARG A CB  
860  C CB  B ARG A 132 ? 0.5070 0.4822 0.4555 0.1974  0.0213  0.1049  132 ARG A CB  
861  C CG  A ARG A 132 ? 0.5358 0.5686 0.5074 0.2000  0.0144  0.1142  132 ARG A CG  
862  C CG  B ARG A 132 ? 0.5713 0.5435 0.5112 0.2109  0.0314  0.1077  132 ARG A CG  
863  C CD  A ARG A 132 ? 0.5500 0.5922 0.5114 0.2182  0.0227  0.1248  132 ARG A CD  
864  C CD  B ARG A 132 ? 0.5755 0.4966 0.4792 0.2205  0.0432  0.1074  132 ARG A CD  
865  N NE  A ARG A 132 ? 0.5262 0.5900 0.4901 0.2198  0.0180  0.1325  132 ARG A NE  
866  N NE  B ARG A 132 ? 0.7111 0.6311 0.6020 0.2316  0.0465  0.1159  132 ARG A NE  
867  C CZ  A ARG A 132 ? 0.5794 0.6147 0.5215 0.2273  0.0227  0.1355  132 ARG A CZ  
868  C CZ  B ARG A 132 ? 0.6951 0.5733 0.5597 0.2302  0.0500  0.1143  132 ARG A CZ  
869  N NH1 A ARG A 132 ? 0.6382 0.6213 0.5524 0.2332  0.0326  0.1315  132 ARG A NH1 
870  N NH1 B ARG A 132 ? 0.7154 0.5490 0.5619 0.2173  0.0508  0.1049  132 ARG A NH1 
871  N NH2 A ARG A 132 ? 0.6421 0.7008 0.5884 0.2277  0.0174  0.1427  132 ARG A NH2 
872  N NH2 B ARG A 132 ? 0.7009 0.5830 0.5564 0.2410  0.0526  0.1227  132 ARG A NH2 
873  N N   . GLN A 133 ? 0.5559 0.4437 0.4775 0.1727  0.0236  0.0838  133 GLN A N   
874  C CA  . GLN A 133 ? 0.5646 0.4097 0.4658 0.1655  0.0290  0.0760  133 GLN A CA  
875  C C   . GLN A 133 ? 0.5280 0.3850 0.4489 0.1497  0.0229  0.0671  133 GLN A C   
876  O O   . GLN A 133 ? 0.4567 0.2976 0.3712 0.1487  0.0266  0.0627  133 GLN A O   
877  C CB  . GLN A 133 ? 0.5702 0.3695 0.4415 0.1573  0.0319  0.0742  133 GLN A CB  
878  C CG  . GLN A 133 ? 0.6665 0.4470 0.5129 0.1698  0.0398  0.0803  133 GLN A CG  
879  C CD  . GLN A 133 ? 0.7511 0.4918 0.5704 0.1594  0.0412  0.0793  133 GLN A CD  
880  O OE1 . GLN A 133 ? 0.8101 0.5405 0.6306 0.1421  0.0359  0.0749  133 GLN A OE1 
881  N NE2 . GLN A 133 ? 0.7990 0.5177 0.5928 0.1697  0.0489  0.0839  133 GLN A NE2 
882  N N   . TYR A 134 ? 0.4527 0.3402 0.3972 0.1346  0.0138  0.0629  134 TYR A N   
883  C CA  . TYR A 134 ? 0.4649 0.3696 0.4299 0.1185  0.0082  0.0539  134 TYR A CA  
884  C C   . TYR A 134 ? 0.4488 0.3770 0.4288 0.1270  0.0088  0.0555  134 TYR A C   
885  O O   . TYR A 134 ? 0.4031 0.3239 0.3849 0.1212  0.0098  0.0496  134 TYR A O   
886  C CB  . TYR A 134 ? 0.3632 0.2947 0.3469 0.1050  0.0001  0.0505  134 TYR A CB  
887  C CG  . TYR A 134 ? 0.3493 0.3017 0.3537 0.0931  -0.0047 0.0433  134 TYR A CG  
888  C CD1 . TYR A 134 ? 0.3388 0.2780 0.3429 0.0795  -0.0051 0.0357  134 TYR A CD1 
889  C CD2 . TYR A 134 ? 0.3383 0.3241 0.3610 0.0949  -0.0087 0.0451  134 TYR A CD2 
890  C CE1 . TYR A 134 ? 0.3502 0.3060 0.3708 0.0710  -0.0085 0.0301  134 TYR A CE1 
891  C CE2 . TYR A 134 ? 0.3753 0.3745 0.4125 0.0837  -0.0122 0.0386  134 TYR A CE2 
892  C CZ  . TYR A 134 ? 0.3971 0.3797 0.4328 0.0733  -0.0117 0.0311  134 TYR A CZ  
893  O OH  . TYR A 134 ? 0.3172 0.3106 0.3650 0.0644  -0.0143 0.0256  134 TYR A OH  
894  N N   . GLU A 135 ? 0.4057 0.3657 0.3971 0.1398  0.0079  0.0641  135 GLU A N   
895  C CA  . GLU A 135 ? 0.4440 0.4312 0.4502 0.1475  0.0086  0.0674  135 GLU A CA  
896  C C   . GLU A 135 ? 0.4681 0.4265 0.4561 0.1610  0.0185  0.0686  135 GLU A C   
897  O O   . GLU A 135 ? 0.3989 0.3622 0.3944 0.1585  0.0194  0.0649  135 GLU A O   
898  C CB  . GLU A 135 ? 0.4924 0.5213 0.5114 0.1597  0.0065  0.0793  135 GLU A CB  
899  C CG  . GLU A 135 ? 0.5161 0.5779 0.5532 0.1434  -0.0041 0.0775  135 GLU A CG  
900  C CD  . GLU A 135 ? 0.5770 0.6508 0.6298 0.1245  -0.0096 0.0679  135 GLU A CD  
901  O OE1 . GLU A 135 ? 0.5327 0.6070 0.5900 0.1266  -0.0066 0.0663  135 GLU A OE1 
902  O OE2 . GLU A 135 ? 0.5796 0.6601 0.6379 0.1082  -0.0164 0.0622  135 GLU A OE2 
903  N N   . GLU A 136 ? 0.4915 0.4199 0.4534 0.1696  0.0260  0.0714  136 GLU A N   
904  C CA  . GLU A 136 ? 0.5471 0.4458 0.4863 0.1763  0.0358  0.0698  136 GLU A CA  
905  C C   . GLU A 136 ? 0.5141 0.3785 0.4421 0.1631  0.0358  0.0599  136 GLU A C   
906  O O   . GLU A 136 ? 0.4594 0.3181 0.3841 0.1639  0.0396  0.0569  136 GLU A O   
907  C CB  . GLU A 136 ? 0.5301 0.3999 0.4395 0.1871  0.0441  0.0746  136 GLU A CB  
908  C CG  . GLU A 136 ? 0.5679 0.4727 0.4870 0.2015  0.0450  0.0856  136 GLU A CG  
909  C CD  . GLU A 136 ? 0.8857 0.7611 0.7742 0.2138  0.0540  0.0908  136 GLU A CD  
910  O OE1 . GLU A 136 ? 0.8158 0.6429 0.6759 0.2078  0.0578  0.0853  136 GLU A OE1 
911  O OE2 . GLU A 136 ? 0.8361 0.7373 0.7278 0.2287  0.0575  0.1007  136 GLU A OE2 
912  N N   . LYS A 137 ? 0.4969 0.3386 0.4176 0.1504  0.0318  0.0554  137 LYS A N   
913  C CA  . LYS A 137 ? 0.5492 0.3611 0.4577 0.1341  0.0314  0.0464  137 LYS A CA  
914  C C   . LYS A 137 ? 0.5032 0.3473 0.4407 0.1216  0.0245  0.0402  137 LYS A C   
915  O O   . LYS A 137 ? 0.4715 0.3001 0.4021 0.1131  0.0254  0.0344  137 LYS A O   
916  C CB  . LYS A 137 ? 0.4689 0.2589 0.3644 0.1166  0.0281  0.0426  137 LYS A CB  
917  C CG  . LYS A 137 ? 0.6529 0.3985 0.5110 0.1249  0.0359  0.0474  137 LYS A CG  
918  C CD  . LYS A 137 ? 0.9084 0.6258 0.7393 0.1297  0.0448  0.0456  137 LYS A CD  
919  C CE  . LYS A 137 ? 0.9631 0.6406 0.7678 0.1093  0.0452  0.0380  137 LYS A CE  
920  N NZ  . LYS A 137 ? 0.9233 0.5652 0.6915 0.1137  0.0549  0.0368  137 LYS A NZ  
921  N N   . LYS A 138 ? 0.4253 0.3116 0.3924 0.1193  0.0176  0.0414  138 LYS A N   
922  C CA  . LYS A 138 ? 0.4016 0.3145 0.3926 0.1088  0.0121  0.0361  138 LYS A CA  
923  C C   . LYS A 138 ? 0.4242 0.3429 0.4169 0.1198  0.0169  0.0382  138 LYS A C   
924  O O   . LYS A 138 ? 0.3948 0.3109 0.3910 0.1116  0.0162  0.0326  138 LYS A O   
925  C CB  . LYS A 138 ? 0.3532 0.3041 0.3684 0.1043  0.0048  0.0374  138 LYS A CB  
926  C CG  . LYS A 138 ? 0.3364 0.3143 0.3730 0.0965  0.0005  0.0340  138 LYS A CG  
927  C CD  . LYS A 138 ? 0.3523 0.3605 0.4050 0.0903  -0.0062 0.0352  138 LYS A CD  
928  C CE  . LYS A 138 ? 0.5267 0.5599 0.5958 0.0837  -0.0096 0.0336  138 LYS A CE  
929  N NZ  . LYS A 138 ? 0.5941 0.6533 0.6731 0.0759  -0.0158 0.0351  138 LYS A NZ  
930  N N   . GLU A 139 ? 0.4124 0.3414 0.4030 0.1392  0.0221  0.0472  139 GLU A N   
931  C CA  . GLU A 139 ? 0.4779 0.4159 0.4705 0.1512  0.0277  0.0505  139 GLU A CA  
932  C C   . GLU A 139 ? 0.4679 0.3624 0.4306 0.1526  0.0358  0.0464  139 GLU A C   
933  O O   . GLU A 139 ? 0.4766 0.3712 0.4401 0.1524  0.0383  0.0438  139 GLU A O   
934  C CB  . GLU A 139 ? 0.4603 0.4311 0.4606 0.1640  0.0299  0.0604  139 GLU A CB  
935  C CG  . GLU A 139 ? 0.5108 0.5300 0.5415 0.1583  0.0207  0.0641  139 GLU A CG  
936  C CD  . GLU A 139 ? 0.6137 0.6498 0.6632 0.1448  0.0155  0.0582  139 GLU A CD  
937  O OE1 . GLU A 139 ? 0.7770 0.8161 0.8273 0.1503  0.0202  0.0589  139 GLU A OE1 
938  O OE2 . GLU A 139 ? 0.5057 0.5496 0.5663 0.1265  0.0072  0.0517  139 GLU A OE2 
939  N N   . ALA A 140 ? 0.4469 0.3034 0.3814 0.1526  0.0398  0.0456  140 ALA A N   
940  C CA  . ALA A 140 ? 0.5489 0.3608 0.4505 0.1497  0.0467  0.0409  140 ALA A CA  
941  C C   . ALA A 140 ? 0.5395 0.3354 0.4408 0.1325  0.0421  0.0322  140 ALA A C   
942  O O   . ALA A 140 ? 0.5060 0.2827 0.3922 0.1296  0.0459  0.0283  140 ALA A O   
943  C CB  . ALA A 140 ? 0.5255 0.2999 0.3951 0.1501  0.0514  0.0419  140 ALA A CB  
944  N N   . PHE A 141 ? 0.4726 0.2830 0.3915 0.1166  0.0330  0.0287  141 PHE A N   
945  C CA  . PHE A 141 ? 0.4829 0.2926 0.4069 0.0952  0.0270  0.0208  141 PHE A CA  
946  C C   . PHE A 141 ? 0.4686 0.3073 0.4160 0.0952  0.0246  0.0191  141 PHE A C   
947  O O   . PHE A 141 ? 0.4170 0.2427 0.3558 0.0881  0.0254  0.0147  141 PHE A O   
948  C CB  . PHE A 141 ? 0.4126 0.2376 0.3514 0.0791  0.0186  0.0186  141 PHE A CB  
949  C CG  . PHE A 141 ? 0.4154 0.2497 0.3646 0.0602  0.0125  0.0129  141 PHE A CG  
950  C CD1 . PHE A 141 ? 0.4150 0.2215 0.3413 0.0474  0.0133  0.0095  141 PHE A CD1 
951  C CD2 . PHE A 141 ? 0.4106 0.2805 0.3897 0.0551  0.0062  0.0116  141 PHE A CD2 
952  C CE1 . PHE A 141 ? 0.3682 0.1890 0.3054 0.0308  0.0073  0.0062  141 PHE A CE1 
953  C CE2 . PHE A 141 ? 0.3620 0.2413 0.3498 0.0409  0.0017  0.0081  141 PHE A CE2 
954  C CZ  . PHE A 141 ? 0.3842 0.2422 0.3531 0.0294  0.0020  0.0060  141 PHE A CZ  
955  N N   . ARG A 142 ? 0.3860 0.2637 0.3615 0.1014  0.0214  0.0225  142 ARG A N   
956  C CA  . ARG A 142 ? 0.3572 0.2605 0.3522 0.1008  0.0198  0.0215  142 ARG A CA  
957  C C   . ARG A 142 ? 0.4014 0.2913 0.3816 0.1146  0.0285  0.0239  142 ARG A C   
958  O O   . ARG A 142 ? 0.3878 0.2777 0.3697 0.1096  0.0287  0.0204  142 ARG A O   
959  C CB  . ARG A 142 ? 0.3774 0.3220 0.3995 0.1032  0.0153  0.0256  142 ARG A CB  
960  C CG  . ARG A 142 ? 0.3217 0.2790 0.3573 0.0891  0.0072  0.0223  142 ARG A CG  
961  C CD  . ARG A 142 ? 0.3280 0.3210 0.3841 0.0893  0.0028  0.0259  142 ARG A CD  
962  N NE  . ARG A 142 ? 0.3332 0.3464 0.4033 0.0851  0.0013  0.0251  142 ARG A NE  
963  C CZ  . ARG A 142 ? 0.4221 0.4588 0.5003 0.0933  0.0033  0.0312  142 ARG A CZ  
964  N NH1 . ARG A 142 ? 0.3664 0.4138 0.4423 0.1079  0.0069  0.0396  142 ARG A NH1 
965  N NH2 . ARG A 142 ? 0.3212 0.3724 0.4096 0.0873  0.0023  0.0300  142 ARG A NH2 
966  N N   . GLY A 143 ? 0.4275 0.3048 0.3914 0.1335  0.0366  0.0306  143 GLY A N   
967  C CA  . GLY A 143 ? 0.4752 0.3388 0.4213 0.1457  0.0460  0.0327  143 GLY A CA  
968  C C   . GLY A 143 ? 0.5029 0.3212 0.4186 0.1370  0.0494  0.0255  143 GLY A C   
969  O O   . GLY A 143 ? 0.4942 0.3071 0.4024 0.1396  0.0540  0.0242  143 GLY A O   
970  N N   . CYS A 144 ? 0.4907 0.2764 0.3869 0.1250  0.0471  0.0212  144 CYS A N   
971  C CA  . CYS A 144 ? 0.4960 0.2405 0.3618 0.1114  0.0486  0.0145  144 CYS A CA  
972  C C   . CYS A 144 ? 0.4852 0.2506 0.3708 0.0958  0.0413  0.0092  144 CYS A C   
973  O O   . CYS A 144 ? 0.4613 0.2070 0.3292 0.0925  0.0445  0.0058  144 CYS A O   
974  C CB  . CYS A 144 ? 0.6001 0.3135 0.4440 0.0968  0.0458  0.0119  144 CYS A CB  
975  S SG  . CYS A 144 ? 0.6508 0.3165 0.4545 0.0719  0.0451  0.0042  144 CYS A SG  
976  N N   . LEU A 145 ? 0.4290 0.2333 0.3490 0.0862  0.0318  0.0086  145 LEU A N   
977  C CA  . LEU A 145 ? 0.3894 0.2144 0.3278 0.0730  0.0255  0.0047  145 LEU A CA  
978  C C   . LEU A 145 ? 0.4686 0.3027 0.4114 0.0834  0.0302  0.0057  145 LEU A C   
979  O O   . LEU A 145 ? 0.4141 0.2437 0.3529 0.0747  0.0290  0.0021  145 LEU A O   
980  C CB  . LEU A 145 ? 0.3767 0.2394 0.3486 0.0663  0.0171  0.0051  145 LEU A CB  
981  C CG  . LEU A 145 ? 0.3866 0.2477 0.3590 0.0555  0.0120  0.0044  145 LEU A CG  
982  C CD1 . LEU A 145 ? 0.3361 0.2320 0.3386 0.0522  0.0058  0.0048  145 LEU A CD1 
983  C CD2 . LEU A 145 ? 0.4070 0.2482 0.3617 0.0381  0.0094  0.0010  145 LEU A CD2 
984  N N   . LEU A 146 ? 0.4107 0.2617 0.3630 0.1015  0.0354  0.0116  146 LEU A N   
985  C CA  . LEU A 146 ? 0.3819 0.2447 0.3384 0.1122  0.0409  0.0140  146 LEU A CA  
986  C C   . LEU A 146 ? 0.4689 0.2905 0.3884 0.1228  0.0518  0.0136  146 LEU A C   
987  O O   . LEU A 146 ? 0.4355 0.2482 0.3462 0.1198  0.0541  0.0106  146 LEU A O   
988  C CB  . LEU A 146 ? 0.3940 0.2947 0.3737 0.1270  0.0426  0.0222  146 LEU A CB  
989  C CG  . LEU A 146 ? 0.4466 0.3645 0.4307 0.1407  0.0498  0.0273  146 LEU A CG  
990  C CD1 . LEU A 146 ? 0.3848 0.3147 0.3816 0.1267  0.0451  0.0225  146 LEU A CD1 
991  C CD2 . LEU A 146 ? 0.4630 0.4241 0.4703 0.1528  0.0504  0.0372  146 LEU A CD2 
992  N N   . ASN A 147 ? 0.4246 0.2210 0.3202 0.1334  0.0584  0.0166  147 ASN A N   
993  C CA  . ASN A 147 ? 0.4584 0.2235 0.3190 0.1407  0.0684  0.0170  147 ASN A CA  
994  C C   . ASN A 147 ? 0.5642 0.2881 0.3947 0.1249  0.0682  0.0088  147 ASN A C   
995  O O   . ASN A 147 ? 0.5421 0.2513 0.3539 0.1285  0.0746  0.0078  147 ASN A O   
996  C CB  . ASN A 147 ? 0.6126 0.3596 0.4517 0.1493  0.0738  0.0214  147 ASN A CB  
997  C CG  . ASN A 147 ? 0.6483 0.4334 0.5081 0.1678  0.0771  0.0313  147 ASN A CG  
998  O OD1 . ASN A 147 ? 0.6871 0.5094 0.5718 0.1748  0.0771  0.0355  147 ASN A OD1 
999  N ND2 . ASN A 147 ? 0.7707 0.5478 0.6194 0.1746  0.0797  0.0356  147 ASN A ND2 
1000 N N   . LYS A 148 ? 0.5043 0.2102 0.3283 0.1062  0.0607  0.0034  148 LYS A N   
1001 C CA  . LYS A 148 ? 0.5272 0.1961 0.3201 0.0869  0.0590  -0.0036 148 LYS A CA  
1002 C C   . LYS A 148 ? 0.5488 0.2385 0.3592 0.0770  0.0536  -0.0068 148 LYS A C   
1003 O O   . LYS A 148 ? 0.5534 0.2170 0.3379 0.0624  0.0528  -0.0117 148 LYS A O   
1004 C CB  . LYS A 148 ? 0.5436 0.1965 0.3274 0.0663  0.0513  -0.0065 148 LYS A CB  
1005 C CG  . LYS A 148 ? 0.5452 0.1771 0.3074 0.0707  0.0558  -0.0036 148 LYS A CG  
1006 C CD  . LYS A 148 ? 0.6571 0.2485 0.3732 0.0734  0.0658  -0.0042 148 LYS A CD  
1007 C CE  . LYS A 148 ? 0.6654 0.2385 0.3610 0.0836  0.0724  0.0002  148 LYS A CE  
1008 N NZ  . LYS A 148 ? 0.7691 0.2944 0.4122 0.0821  0.0818  -0.0008 148 LYS A NZ  
1009 N N   . ASN A 149 ? 0.4658 0.2044 0.3184 0.0827  0.0493  -0.0037 149 ASN A N   
1010 C CA  . ASN A 149 ? 0.4086 0.1730 0.2815 0.0739  0.0440  -0.0056 149 ASN A CA  
1011 C C   . ASN A 149 ? 0.4453 0.2196 0.3217 0.0908  0.0522  -0.0027 149 ASN A C   
1012 O O   . ASN A 149 ? 0.4503 0.2462 0.3434 0.0848  0.0485  -0.0035 149 ASN A O   
1013 C CB  . ASN A 149 ? 0.4052 0.2135 0.3190 0.0658  0.0335  -0.0044 149 ASN A CB  
1014 C CG  . ASN A 149 ? 0.4638 0.2702 0.3768 0.0447  0.0244  -0.0075 149 ASN A CG  
1015 O OD1 . ASN A 149 ? 0.4385 0.2382 0.3416 0.0315  0.0211  -0.0102 149 ASN A OD1 
1016 N ND2 . ASN A 149 ? 0.4087 0.2230 0.3316 0.0415  0.0203  -0.0063 149 ASN A ND2 
1017 N N   . ARG A 150 ? 0.4491 0.2080 0.3088 0.1124  0.0638  0.0016  150 ARG A N   
1018 C CA  . ARG A 150 ? 0.4479 0.2238 0.3145 0.1297  0.0722  0.0062  150 ARG A CA  
1019 C C   . ARG A 150 ? 0.4967 0.2513 0.3419 0.1232  0.0751  0.0015  150 ARG A C   
1020 O O   . ARG A 150 ? 0.5026 0.2855 0.3677 0.1243  0.0746  0.0031  150 ARG A O   
1021 C CB  . ARG A 150 ? 0.5145 0.2875 0.3678 0.1494  0.0824  0.0135  150 ARG A CB  
1022 C CG  . ARG A 150 ? 0.5311 0.3356 0.4101 0.1559  0.0788  0.0197  150 ARG A CG  
1023 C CD  . ARG A 150 ? 0.6268 0.4392 0.4971 0.1751  0.0883  0.0289  150 ARG A CD  
1024 N NE  . ARG A 150 ? 0.6344 0.4737 0.5250 0.1796  0.0844  0.0347  150 ARG A NE  
1025 C CZ  . ARG A 150 ? 0.5069 0.3962 0.4339 0.1825  0.0798  0.0407  150 ARG A CZ  
1026 N NH1 . ARG A 150 ? 0.4805 0.3999 0.4294 0.1810  0.0785  0.0419  150 ARG A NH1 
1027 N NH2 . ARG A 150 ? 0.5392 0.4484 0.4790 0.1857  0.0765  0.0458  150 ARG A NH2 
1028 N N   . LYS A 151 ? 0.5237 0.2276 0.3264 0.1147  0.0778  -0.0043 151 LYS A N   
1029 C CA  . LYS A 151 ? 0.5139 0.1971 0.2938 0.1064  0.0798  -0.0090 151 LYS A CA  
1030 C C   . LYS A 151 ? 0.4742 0.1878 0.2811 0.0840  0.0660  -0.0120 151 LYS A C   
1031 O O   . LYS A 151 ? 0.5179 0.2394 0.3266 0.0819  0.0666  -0.0128 151 LYS A O   
1032 C CB  . LYS A 151 ? 0.5738 0.2020 0.3016 0.0966  0.0836  -0.0136 151 LYS A CB  
1033 C CG  . LYS A 151 ? 0.6413 0.2532 0.3452 0.1152  0.0958  -0.0075 151 LYS A CG  
1034 C CD  . LYS A 151 ? 0.7906 0.3496 0.4401 0.1060  0.1014  -0.0107 151 LYS A CD  
1035 C CE  . LYS A 151 ? 0.8277 0.3577 0.4537 0.0872  0.0958  -0.0142 151 LYS A CE  
1036 N NZ  . LYS A 151 ? 0.8671 0.3444 0.4359 0.0793  0.1028  -0.0158 151 LYS A NZ  
1037 N N   . ASN A 152 ? 0.4681 0.2006 0.2967 0.0693  0.0545  -0.0126 152 ASN A N   
1038 C CA  . ASN A 152 ? 0.4405 0.2053 0.2969 0.0525  0.0428  -0.0135 152 ASN A CA  
1039 C C   . ASN A 152 ? 0.4611 0.2671 0.3534 0.0621  0.0427  -0.0094 152 ASN A C   
1040 O O   . ASN A 152 ? 0.4120 0.2336 0.3152 0.0541  0.0384  -0.0098 152 ASN A O   
1041 C CB  . ASN A 152 ? 0.4076 0.1855 0.2796 0.0388  0.0326  -0.0136 152 ASN A CB  
1042 C CG  . ASN A 152 ? 0.4825 0.2249 0.3199 0.0222  0.0302  -0.0173 152 ASN A CG  
1043 O OD1 . ASN A 152 ? 0.5017 0.2160 0.3077 0.0137  0.0322  -0.0205 152 ASN A OD1 
1044 N ND2 . ASN A 152 ? 0.4765 0.2188 0.3171 0.0162  0.0262  -0.0167 152 ASN A ND2 
1045 N N   . LEU A 153 ? 0.4444 0.2690 0.3544 0.0781  0.0472  -0.0047 153 LEU A N   
1046 C CA  . LEU A 153 ? 0.3862 0.2493 0.3267 0.0845  0.0473  -0.0003 153 LEU A CA  
1047 C C   . LEU A 153 ? 0.4579 0.3162 0.3865 0.0915  0.0551  0.0005  153 LEU A C   
1048 O O   . LEU A 153 ? 0.4195 0.3017 0.3663 0.0870  0.0523  0.0018  153 LEU A O   
1049 C CB  . LEU A 153 ? 0.4322 0.3182 0.3907 0.0988  0.0505  0.0058  153 LEU A CB  
1050 C CG  . LEU A 153 ? 0.3905 0.2826 0.3609 0.0932  0.0434  0.0054  153 LEU A CG  
1051 C CD1 . LEU A 153 ? 0.4900 0.4056 0.4756 0.1080  0.0469  0.0124  153 LEU A CD1 
1052 C CD2 . LEU A 153 ? 0.3727 0.2847 0.3656 0.0765  0.0325  0.0030  153 LEU A CD2 
1053 N N   . ASP A 154 ? 0.4559 0.2807 0.3512 0.1031  0.0657  0.0000  154 ASP A N   
1054 C CA  . ASP A 154 ? 0.5376 0.3535 0.4169 0.1104  0.0743  0.0004  154 ASP A CA  
1055 C C   . ASP A 154 ? 0.5346 0.3415 0.4060 0.0912  0.0672  -0.0050 154 ASP A C   
1056 O O   . ASP A 154 ? 0.4695 0.2892 0.3461 0.0917  0.0691  -0.0038 154 ASP A O   
1057 C CB  . ASP A 154 ? 0.5253 0.2978 0.3626 0.1267  0.0880  0.0002  154 ASP A CB  
1058 C CG  . ASP A 154 ? 0.7342 0.5217 0.5795 0.1518  0.0980  0.0086  154 ASP A CG  
1059 O OD1 . ASP A 154 ? 0.8281 0.6631 0.7083 0.1588  0.0976  0.0156  154 ASP A OD1 
1060 O OD2 . ASP A 154 ? 0.8975 0.6556 0.7156 0.1592  0.1037  0.0095  154 ASP A OD2 
1061 N N   . GLN A 155 ? 0.4388 0.2268 0.2980 0.0737  0.0587  -0.0101 155 GLN A N   
1062 C CA  . GLN A 155 ? 0.4428 0.2257 0.2936 0.0552  0.0513  -0.0137 155 GLN A CA  
1063 C C   . GLN A 155 ? 0.4324 0.2567 0.3212 0.0477  0.0421  -0.0109 155 GLN A C   
1064 O O   . GLN A 155 ? 0.4609 0.2900 0.3484 0.0397  0.0392  -0.0113 155 GLN A O   
1065 C CB  . GLN A 155 ? 0.4816 0.2362 0.3074 0.0379  0.0451  -0.0182 155 GLN A CB  
1066 C CG  . GLN A 155 ? 0.5328 0.2831 0.3458 0.0170  0.0370  -0.0207 155 GLN A CG  
1067 C CD  . GLN A 155 ? 0.6841 0.4036 0.4606 0.0175  0.0444  -0.0238 155 GLN A CD  
1068 O OE1 . GLN A 155 ? 0.6594 0.3571 0.4173 0.0350  0.0572  -0.0241 155 GLN A OE1 
1069 N NE2 . GLN A 155 ? 0.7062 0.4247 0.4712 -0.0013 0.0368  -0.0252 155 GLN A NE2 
1070 N N   . ILE A 156 ? 0.4257 0.2776 0.3455 0.0504  0.0380  -0.0080 156 ILE A N   
1071 C CA  . ILE A 156 ? 0.3580 0.2434 0.3089 0.0461  0.0320  -0.0051 156 ILE A CA  
1072 C C   . ILE A 156 ? 0.3490 0.2457 0.3041 0.0536  0.0382  -0.0023 156 ILE A C   
1073 O O   . ILE A 156 ? 0.3468 0.2527 0.3073 0.0466  0.0350  -0.0016 156 ILE A O   
1074 C CB  . ILE A 156 ? 0.3484 0.2561 0.3258 0.0491  0.0287  -0.0027 156 ILE A CB  
1075 C CG1 . ILE A 156 ? 0.3157 0.2152 0.2906 0.0408  0.0222  -0.0048 156 ILE A CG1 
1076 C CG2 . ILE A 156 ? 0.3045 0.2397 0.3073 0.0451  0.0244  0.0002  156 ILE A CG2 
1077 C CD1 . ILE A 156 ? 0.3563 0.2721 0.3515 0.0454  0.0205  -0.0029 156 ILE A CD1 
1078 N N   . LYS A 157 ? 0.4090 0.3070 0.3616 0.0687  0.0477  0.0004  157 LYS A N   
1079 C CA  . LYS A 157 ? 0.4714 0.3846 0.4288 0.0766  0.0547  0.0044  157 LYS A CA  
1080 C C   . LYS A 157 ? 0.4504 0.3413 0.3823 0.0734  0.0580  0.0015  157 LYS A C   
1081 O O   . LYS A 157 ? 0.4333 0.3384 0.3727 0.0707  0.0583  0.0036  157 LYS A O   
1082 C CB  . LYS A 157 ? 0.4782 0.3989 0.4356 0.0955  0.0652  0.0094  157 LYS A CB  
1083 C CG  . LYS A 157 ? 0.6709 0.6124 0.6337 0.1059  0.0741  0.0155  157 LYS A CG  
1084 C CD  . LYS A 157 ? 0.6486 0.6048 0.6143 0.1266  0.0843  0.0228  157 LYS A CD  
1085 C CE  . LYS A 157 ? 0.7338 0.7064 0.6974 0.1398  0.0960  0.0296  157 LYS A CE  
1086 N NZ  . LYS A 157 ? 0.4746 0.4729 0.4459 0.1617  0.1063  0.0398  157 LYS A NZ  
1087 N N   . LYS A 158 ? 0.3826 0.2366 0.2815 0.0720  0.0603  -0.0034 158 LYS A N   
1088 C CA  . LYS A 158 ? 0.4383 0.2674 0.3077 0.0668  0.0630  -0.0067 158 LYS A CA  
1089 C C   . LYS A 158 ? 0.4414 0.2818 0.3200 0.0486  0.0515  -0.0076 158 LYS A C   
1090 O O   . LYS A 158 ? 0.4311 0.2740 0.3048 0.0460  0.0526  -0.0069 158 LYS A O   
1091 C CB  . LYS A 158 ? 0.5176 0.3006 0.3453 0.0659  0.0671  -0.0120 158 LYS A CB  
1092 C CG  . LYS A 158 ? 0.7395 0.4878 0.5264 0.0632  0.0733  -0.0159 158 LYS A CG  
1093 C CD  . LYS A 158 ? 0.7515 0.4474 0.4915 0.0635  0.0795  -0.0211 158 LYS A CD  
1094 C CE  . LYS A 158 ? 0.9054 0.5618 0.5995 0.0525  0.0820  -0.0265 158 LYS A CE  
1095 N NZ  . LYS A 158 ? 1.1178 0.7723 0.8021 0.0676  0.0940  -0.0246 158 LYS A NZ  
1096 N N   . ILE A 159 ? 0.3983 0.2475 0.2906 0.0372  0.0409  -0.0083 159 ILE A N   
1097 C CA  . ILE A 159 ? 0.4449 0.3079 0.3464 0.0231  0.0309  -0.0071 159 ILE A CA  
1098 C C   . ILE A 159 ? 0.4064 0.2988 0.3360 0.0267  0.0304  -0.0024 159 ILE A C   
1099 O O   . ILE A 159 ? 0.4015 0.2996 0.3303 0.0210  0.0277  -0.0005 159 ILE A O   
1100 C CB  . ILE A 159 ? 0.4641 0.3314 0.3724 0.0121  0.0211  -0.0076 159 ILE A CB  
1101 C CG1 . ILE A 159 ? 0.4232 0.2583 0.2973 0.0030  0.0208  -0.0121 159 ILE A CG1 
1102 C CG2 . ILE A 159 ? 0.3977 0.2875 0.3213 0.0020  0.0117  -0.0037 159 ILE A CG2 
1103 C CD1 . ILE A 159 ? 0.4820 0.3230 0.3628 -0.0074 0.0124  -0.0118 159 ILE A CD1 
1104 N N   . ASN A 160 ? 0.3562 0.2664 0.3086 0.0351  0.0328  0.0000  160 ASN A N   
1105 C CA  . ASN A 160 ? 0.3281 0.2616 0.3015 0.0364  0.0333  0.0044  160 ASN A CA  
1106 C C   . ASN A 160 ? 0.4053 0.3366 0.3673 0.0397  0.0403  0.0059  160 ASN A C   
1107 O O   . ASN A 160 ? 0.3644 0.3051 0.3323 0.0348  0.0383  0.0086  160 ASN A O   
1108 C CB  . ASN A 160 ? 0.3456 0.2972 0.3390 0.0434  0.0360  0.0069  160 ASN A CB  
1109 C CG  . ASN A 160 ? 0.4348 0.3946 0.4447 0.0382  0.0284  0.0067  160 ASN A CG  
1110 O OD1 . ASN A 160 ? 0.4649 0.4233 0.4766 0.0305  0.0218  0.0063  160 ASN A OD1 
1111 N ND2 . ASN A 160 ? 0.4510 0.4210 0.4722 0.0434  0.0299  0.0077  160 ASN A ND2 
1112 N N   . ASN A 161 ? 0.4138 0.3310 0.3575 0.0494  0.0494  0.0046  161 ASN A N   
1113 C CA  . ASN A 161 ? 0.4696 0.3857 0.4019 0.0546  0.0575  0.0065  161 ASN A CA  
1114 C C   . ASN A 161 ? 0.4911 0.3892 0.4020 0.0446  0.0540  0.0038  161 ASN A C   
1115 O O   . ASN A 161 ? 0.4564 0.3612 0.3664 0.0433  0.0562  0.0064  161 ASN A O   
1116 C CB  . ASN A 161 ? 0.4928 0.3970 0.4085 0.0707  0.0699  0.0067  161 ASN A CB  
1117 C CG  . ASN A 161 ? 0.6262 0.5610 0.5668 0.0818  0.0749  0.0130  161 ASN A CG  
1118 O OD1 . ASN A 161 ? 0.8316 0.7657 0.7740 0.0909  0.0774  0.0136  161 ASN A OD1 
1119 N ND2 . ASN A 161 ? 0.7304 0.6936 0.6897 0.0796  0.0758  0.0185  161 ASN A ND2 
1120 N N   . GLU A 162 ? 0.4577 0.3353 0.3514 0.0360  0.0479  -0.0006 162 GLU A N   
1121 C CA  . GLU A 162 ? 0.4561 0.3215 0.3300 0.0239  0.0427  -0.0021 162 GLU A CA  
1122 C C   . GLU A 162 ? 0.3636 0.2534 0.2595 0.0162  0.0341  0.0026  162 GLU A C   
1123 O O   . GLU A 162 ? 0.4591 0.3484 0.3452 0.0109  0.0327  0.0043  162 GLU A O   
1124 C CB  . GLU A 162 ? 0.5477 0.3900 0.3990 0.0136  0.0373  -0.0068 162 GLU A CB  
1125 C CG  . GLU A 162 ? 0.6978 0.5285 0.5250 -0.0016 0.0311  -0.0080 162 GLU A CG  
1126 C CD  . GLU A 162 ? 0.9145 0.7143 0.7086 -0.0127 0.0289  -0.0133 162 GLU A CD  
1127 O OE1 . GLU A 162 ? 0.7941 0.5764 0.5810 -0.0054 0.0345  -0.0165 162 GLU A OE1 
1128 O OE2 . GLU A 162 ? 0.9913 0.7844 0.7651 -0.0295 0.0215  -0.0138 162 GLU A OE2 
1129 N N   . ILE A 163 ? 0.3575 0.2661 0.2804 0.0164  0.0291  0.0050  163 ILE A N   
1130 C CA  . ILE A 163 ? 0.3731 0.3003 0.3140 0.0123  0.0231  0.0101  163 ILE A CA  
1131 C C   . ILE A 163 ? 0.3600 0.2958 0.3072 0.0166  0.0292  0.0136  163 ILE A C   
1132 O O   . ILE A 163 ? 0.4164 0.3558 0.3616 0.0127  0.0270  0.0173  163 ILE A O   
1133 C CB  . ILE A 163 ? 0.3662 0.3060 0.3295 0.0128  0.0182  0.0114  163 ILE A CB  
1134 C CG1 . ILE A 163 ? 0.3902 0.3257 0.3475 0.0062  0.0110  0.0097  163 ILE A CG1 
1135 C CG2 . ILE A 163 ? 0.3633 0.3168 0.3421 0.0122  0.0156  0.0169  163 ILE A CG2 
1136 C CD1 . ILE A 163 ? 0.3942 0.3399 0.3708 0.0079  0.0075  0.0102  163 ILE A CD1 
1137 N N   . ARG A 164 ? 0.3695 0.3107 0.3240 0.0243  0.0369  0.0136  164 ARG A N   
1138 C CA  A ARG A 164 ? 0.4158 0.3687 0.3761 0.0265  0.0429  0.0178  164 ARG A CA  
1139 C CA  B ARG A 164 ? 0.4184 0.3714 0.3787 0.0265  0.0429  0.0178  164 ARG A CA  
1140 C C   . ARG A 164 ? 0.4162 0.3582 0.3549 0.0261  0.0469  0.0178  164 ARG A C   
1141 O O   . ARG A 164 ? 0.3968 0.3450 0.3369 0.0226  0.0473  0.0219  164 ARG A O   
1142 C CB  A ARG A 164 ? 0.4496 0.4156 0.4205 0.0349  0.0506  0.0192  164 ARG A CB  
1143 C CB  B ARG A 164 ? 0.4443 0.4103 0.4153 0.0349  0.0506  0.0191  164 ARG A CB  
1144 C CG  A ARG A 164 ? 0.5083 0.4891 0.5015 0.0330  0.0464  0.0204  164 ARG A CG  
1145 C CG  B ARG A 164 ? 0.5093 0.4883 0.5014 0.0336  0.0462  0.0197  164 ARG A CG  
1146 C CD  A ARG A 164 ? 0.5274 0.5292 0.5330 0.0394  0.0533  0.0241  164 ARG A CD  
1147 C CD  B ARG A 164 ? 0.5472 0.5456 0.5514 0.0410  0.0529  0.0229  164 ARG A CD  
1148 N NE  A ARG A 164 ? 0.5514 0.5674 0.5760 0.0342  0.0483  0.0255  164 ARG A NE  
1149 N NE  B ARG A 164 ? 0.5947 0.6031 0.6157 0.0383  0.0477  0.0228  164 ARG A NE  
1150 C CZ  A ARG A 164 ? 0.5298 0.5561 0.5642 0.0243  0.0456  0.0288  164 ARG A CZ  
1151 C CZ  B ARG A 164 ? 0.5473 0.5550 0.5704 0.0453  0.0482  0.0210  164 ARG A CZ  
1152 N NH1 A ARG A 164 ? 0.5155 0.5416 0.5447 0.0188  0.0475  0.0318  164 ARG A NH1 
1153 N NH1 B ARG A 164 ? 0.4868 0.4831 0.4952 0.0565  0.0547  0.0195  164 ARG A NH1 
1154 N NH2 A ARG A 164 ? 0.4675 0.5015 0.5142 0.0188  0.0412  0.0290  164 ARG A NH2 
1155 N NH2 B ARG A 164 ? 0.5018 0.5173 0.5389 0.0413  0.0426  0.0207  164 ARG A NH2 
1156 N N   . ASP A 165 ? 0.3823 0.3047 0.2978 0.0290  0.0502  0.0133  165 ASP A N   
1157 C CA  . ASP A 165 ? 0.4552 0.3628 0.3449 0.0278  0.0542  0.0125  165 ASP A CA  
1158 C C   . ASP A 165 ? 0.4665 0.3723 0.3499 0.0160  0.0445  0.0138  165 ASP A C   
1159 O O   . ASP A 165 ? 0.4549 0.3608 0.3292 0.0136  0.0460  0.0165  165 ASP A O   
1160 C CB  . ASP A 165 ? 0.5239 0.4039 0.3841 0.0326  0.0603  0.0067  165 ASP A CB  
1161 C CG  . ASP A 165 ? 0.6926 0.5747 0.5542 0.0487  0.0729  0.0076  165 ASP A CG  
1162 O OD1 . ASP A 165 ? 0.7109 0.6197 0.5954 0.0541  0.0770  0.0133  165 ASP A OD1 
1163 O OD2 . ASP A 165 ? 0.7754 0.6328 0.6138 0.0558  0.0790  0.0034  165 ASP A OD2 
1164 N N   . LEU A 166 ? 0.4538 0.3605 0.3420 0.0090  0.0348  0.0130  166 LEU A N   
1165 C CA  . LEU A 166 ? 0.4503 0.3616 0.3344 -0.0008 0.0253  0.0164  166 LEU A CA  
1166 C C   . LEU A 166 ? 0.3974 0.3253 0.2986 0.0007  0.0243  0.0234  166 LEU A C   
1167 O O   . LEU A 166 ? 0.4256 0.3552 0.3174 -0.0035 0.0214  0.0276  166 LEU A O   
1168 C CB  . LEU A 166 ? 0.4449 0.3605 0.3350 -0.0070 0.0160  0.0159  166 LEU A CB  
1169 C CG  . LEU A 166 ? 0.4705 0.4005 0.3627 -0.0152 0.0057  0.0220  166 LEU A CG  
1170 C CD1 . LEU A 166 ? 0.5286 0.4491 0.3922 -0.0254 0.0030  0.0217  166 LEU A CD1 
1171 C CD2 . LEU A 166 ? 0.4522 0.3920 0.3557 -0.0189 -0.0017 0.0226  166 LEU A CD2 
1172 N N   . LEU A 167 ? 0.4366 0.3749 0.3600 0.0061  0.0269  0.0251  167 LEU A N   
1173 C CA  . LEU A 167 ? 0.4260 0.3733 0.3609 0.0065  0.0272  0.0314  167 LEU A CA  
1174 C C   . LEU A 167 ? 0.4288 0.3740 0.3529 0.0064  0.0336  0.0338  167 LEU A C   
1175 O O   . LEU A 167 ? 0.4043 0.3521 0.3296 0.0048  0.0329  0.0397  167 LEU A O   
1176 C CB  . LEU A 167 ? 0.3617 0.3165 0.3169 0.0093  0.0293  0.0315  167 LEU A CB  
1177 C CG  . LEU A 167 ? 0.3953 0.3528 0.3620 0.0093  0.0225  0.0316  167 LEU A CG  
1178 C CD1 . LEU A 167 ? 0.3816 0.3438 0.3639 0.0113  0.0246  0.0293  167 LEU A CD1 
1179 C CD2 . LEU A 167 ? 0.4112 0.3695 0.3789 0.0091  0.0187  0.0383  167 LEU A CD2 
1180 N N   . GLU A 168 ? 0.4374 0.3762 0.3486 0.0092  0.0406  0.0300  168 GLU A N   
1181 C CA  . GLU A 168 ? 0.4623 0.3992 0.3607 0.0095  0.0472  0.0325  168 GLU A CA  
1182 C C   . GLU A 168 ? 0.5368 0.4683 0.4198 0.0036  0.0415  0.0356  168 GLU A C   
1183 O O   . GLU A 168 ? 0.5181 0.4507 0.3949 0.0027  0.0451  0.0400  168 GLU A O   
1184 C CB  . GLU A 168 ? 0.4528 0.3801 0.3348 0.0157  0.0565  0.0279  168 GLU A CB  
1185 C CG  . GLU A 168 ? 0.6557 0.5962 0.5531 0.0239  0.0651  0.0287  168 GLU A CG  
1186 C CD  . GLU A 168 ? 0.6128 0.5712 0.5231 0.0218  0.0691  0.0356  168 GLU A CD  
1187 O OE1 . GLU A 168 ? 0.7633 0.7191 0.6600 0.0212  0.0738  0.0381  168 GLU A OE1 
1188 O OE2 . GLU A 168 ? 0.7730 0.7464 0.7046 0.0192  0.0674  0.0384  168 GLU A OE2 
1189 N N   . ARG A 169 ? 0.4973 0.4252 0.3734 -0.0012 0.0326  0.0344  169 ARG A N   
1190 C CA  . ARG A 169 ? 0.4859 0.4134 0.3466 -0.0075 0.0263  0.0385  169 ARG A CA  
1191 C C   . ARG A 169 ? 0.4968 0.4362 0.3701 -0.0062 0.0223  0.0476  169 ARG A C   
1192 O O   . ARG A 169 ? 0.4702 0.4123 0.3320 -0.0095 0.0180  0.0531  169 ARG A O   
1193 C CB  . ARG A 169 ? 0.4949 0.4204 0.3450 -0.0152 0.0172  0.0360  169 ARG A CB  
1194 C CG  . ARG A 169 ? 0.6809 0.5857 0.5074 -0.0183 0.0211  0.0272  169 ARG A CG  
1195 C CD  . ARG A 169 ? 0.7710 0.6730 0.5833 -0.0304 0.0111  0.0255  169 ARG A CD  
1196 N NE  . ARG A 169 ? 0.9440 0.8186 0.7288 -0.0342 0.0156  0.0165  169 ARG A NE  
1197 C CZ  . ARG A 169 ? 1.0182 0.8706 0.7675 -0.0409 0.0184  0.0128  169 ARG A CZ  
1198 N NH1 . ARG A 169 ? 0.8079 0.6656 0.5469 -0.0453 0.0164  0.0173  169 ARG A NH1 
1199 N NH2 . ARG A 169 ? 1.2348 1.0561 0.9553 -0.0429 0.0239  0.0044  169 ARG A NH2 
1200 N N   . LEU A 170 ? 0.4846 0.4291 0.3784 -0.0016 0.0238  0.0496  170 LEU A N   
1201 C CA  . LEU A 170 ? 0.4314 0.3790 0.3307 0.0009  0.0226  0.0582  170 LEU A CA  
1202 C C   . LEU A 170 ? 0.4544 0.3969 0.3407 -0.0005 0.0280  0.0620  170 LEU A C   
1203 O O   . LEU A 170 ? 0.4798 0.4193 0.3631 -0.0015 0.0356  0.0584  170 LEU A O   
1204 C CB  . LEU A 170 ? 0.3861 0.3327 0.3027 0.0041  0.0254  0.0583  170 LEU A CB  
1205 C CG  . LEU A 170 ? 0.4392 0.3907 0.3686 0.0063  0.0202  0.0556  170 LEU A CG  
1206 C CD1 . LEU A 170 ? 0.4526 0.4002 0.3950 0.0080  0.0238  0.0551  170 LEU A CD1 
1207 C CD2 . LEU A 170 ? 0.4023 0.3614 0.3301 0.0091  0.0126  0.0625  170 LEU A CD2 
1208 N N   . LYS A 171 ? 0.4484 0.3920 0.3269 0.0004  0.0244  0.0704  171 LYS A N   
1209 C CA  . LYS A 171 ? 0.5116 0.4499 0.3754 -0.0013 0.0289  0.0747  171 LYS A CA  
1210 C C   . LYS A 171 ? 0.5527 0.4840 0.4218 -0.0014 0.0372  0.0765  171 LYS A C   
1211 O O   . LYS A 171 ? 0.6118 0.5410 0.4730 -0.0046 0.0440  0.0762  171 LYS A O   
1212 C CB  . LYS A 171 ? 0.6175 0.5602 0.4717 0.0008  0.0227  0.0847  171 LYS A CB  
1213 C CG  . LYS A 171 ? 0.5945 0.5478 0.4379 -0.0039 0.0141  0.0842  171 LYS A CG  
1214 N N   . CYS A 172 ? 0.4930 0.4203 0.3736 0.0009  0.0371  0.0786  172 CYS A N   
1215 C CA  . CYS A 172 ? 0.5503 0.4684 0.4321 -0.0028 0.0439  0.0809  172 CYS A CA  
1216 C C   . CYS A 172 ? 0.4833 0.4100 0.3731 -0.0082 0.0501  0.0747  172 CYS A C   
1217 O O   . CYS A 172 ? 0.5161 0.4522 0.4126 -0.0063 0.0495  0.0681  172 CYS A O   
1218 C CB  . CYS A 172 ? 0.4981 0.4064 0.3866 -0.0001 0.0425  0.0828  172 CYS A CB  
1219 S SG  . CYS A 172 ? 0.5036 0.4223 0.4124 0.0014  0.0387  0.0740  172 CYS A SG  
1220 N N   . SER A 173 ? 0.4624 0.3864 0.3499 -0.0150 0.0566  0.0782  173 SER A N   
1221 C CA  . SER A 173 ? 0.4736 0.4125 0.3707 -0.0199 0.0629  0.0751  173 SER A CA  
1222 C C   . SER A 173 ? 0.4483 0.3847 0.3503 -0.0299 0.0655  0.0781  173 SER A C   
1223 O O   . SER A 173 ? 0.4162 0.3605 0.3320 -0.0322 0.0645  0.0746  173 SER A O   
1224 C CB  . SER A 173 ? 0.5490 0.4950 0.4359 -0.0205 0.0694  0.0769  173 SER A CB  
1225 O OG  . SER A 173 ? 0.6513 0.6165 0.5488 -0.0226 0.0764  0.0756  173 SER A OG  
1226 N N   . GLN A 174 ? 0.4189 0.3426 0.3071 -0.0371 0.0687  0.0848  174 GLN A N   
1227 C CA  . GLN A 174 ? 0.4844 0.3986 0.3696 -0.0500 0.0711  0.0880  174 GLN A CA  
1228 C C   . GLN A 174 ? 0.5606 0.4446 0.4342 -0.0479 0.0675  0.0898  174 GLN A C   
1229 O O   . GLN A 174 ? 0.6145 0.4837 0.4817 -0.0588 0.0690  0.0911  174 GLN A O   
1230 C CB  . GLN A 174 ? 0.4499 0.3632 0.3223 -0.0611 0.0776  0.0948  174 GLN A CB  
1231 C CG  . GLN A 174 ? 0.4852 0.4313 0.3693 -0.0645 0.0834  0.0949  174 GLN A CG  
1232 C CD  . GLN A 174 ? 0.4562 0.4233 0.3552 -0.0766 0.0850  0.0950  174 GLN A CD  
1233 O OE1 . GLN A 174 ? 0.4159 0.4062 0.3331 -0.0705 0.0845  0.0908  174 GLN A OE1 
1234 N NE2 . GLN A 174 ? 0.4520 0.4104 0.3411 -0.0948 0.0869  0.1003  174 GLN A NE2 
1235 N N   . ASP A 175 ? 0.4902 0.3652 0.3594 -0.0343 0.0632  0.0906  175 ASP A N   
1236 C CA  . ASP A 175 ? 0.5621 0.4082 0.4150 -0.0282 0.0622  0.0960  175 ASP A CA  
1237 C C   . ASP A 175 ? 0.4864 0.3349 0.3489 -0.0150 0.0561  0.0934  175 ASP A C   
1238 O O   . ASP A 175 ? 0.5564 0.3947 0.4097 -0.0031 0.0541  0.0992  175 ASP A O   
1239 C CB  . ASP A 175 ? 0.6712 0.5074 0.5061 -0.0233 0.0638  0.1040  175 ASP A CB  
1240 C CG  . ASP A 175 ? 0.8029 0.6621 0.6449 -0.0149 0.0595  0.1027  175 ASP A CG  
1241 O OD1 . ASP A 175 ? 0.6144 0.4956 0.4716 -0.0166 0.0582  0.0954  175 ASP A OD1 
1242 O OD2 . ASP A 175 ? 0.9079 0.7617 0.7377 -0.0068 0.0576  0.1095  175 ASP A OD2 
1243 N N   . CYS A 176 ? 0.4336 0.2980 0.3148 -0.0163 0.0533  0.0858  176 CYS A N   
1244 C CA  . CYS A 176 ? 0.4246 0.2943 0.3159 -0.0051 0.0475  0.0833  176 CYS A CA  
1245 C C   . CYS A 176 ? 0.5690 0.4137 0.4509 -0.0010 0.0487  0.0861  176 CYS A C   
1246 O O   . CYS A 176 ? 0.5214 0.3510 0.3980 -0.0110 0.0522  0.0841  176 CYS A O   
1247 C CB  . CYS A 176 ? 0.3848 0.2763 0.2964 -0.0074 0.0448  0.0746  176 CYS A CB  
1248 S SG  . CYS A 176 ? 0.4679 0.3828 0.3852 -0.0091 0.0456  0.0708  176 CYS A SG  
1249 N N   . GLN A 177 ? 0.4574 0.2986 0.3357 0.0135  0.0461  0.0913  177 GLN A N   
1250 C CA  . GLN A 177 ? 0.5722 0.3886 0.4391 0.0221  0.0486  0.0951  177 GLN A CA  
1251 C C   . GLN A 177 ? 0.4797 0.3032 0.3618 0.0222  0.0458  0.0878  177 GLN A C   
1252 O O   . GLN A 177 ? 0.4426 0.2937 0.3451 0.0222  0.0403  0.0825  177 GLN A O   
1253 C CB  . GLN A 177 ? 0.5472 0.3646 0.4071 0.0403  0.0473  0.1053  177 GLN A CB  
1254 C CG  . GLN A 177 ? 0.6434 0.4520 0.4859 0.0417  0.0501  0.1138  177 GLN A CG  
1255 C CD  . GLN A 177 ? 0.9410 0.7203 0.7600 0.0570  0.0558  0.1250  177 GLN A CD  
1256 O OE1 . GLN A 177 ? 0.9570 0.7462 0.7790 0.0745  0.0540  0.1321  177 GLN A OE1 
1257 N NE2 . GLN A 177 ? 1.0661 0.8088 0.8598 0.0507  0.0634  0.1277  177 GLN A NE2 
1258 N N   . THR A 178 ? 0.4570 0.2520 0.3257 0.0217  0.0502  0.0876  178 THR A N   
1259 C CA  . THR A 178 ? 0.4615 0.2587 0.3408 0.0209  0.0484  0.0811  178 THR A CA  
1260 C C   . THR A 178 ? 0.5206 0.3038 0.3920 0.0389  0.0501  0.0860  178 THR A C   
1261 O O   . THR A 178 ? 0.5233 0.2974 0.3953 0.0389  0.0508  0.0816  178 THR A O   
1262 C CB  . THR A 178 ? 0.5487 0.3264 0.4183 0.0029  0.0518  0.0758  178 THR A CB  
1263 O OG1 . THR A 178 ? 0.5354 0.2716 0.3729 0.0004  0.0589  0.0812  178 THR A OG1 
1264 C CG2 . THR A 178 ? 0.4903 0.2928 0.3739 -0.0128 0.0500  0.0717  178 THR A CG2 
1265 N N   . ASN A 179 ? 0.4943 0.2773 0.3579 0.0551  0.0512  0.0961  179 ASN A N   
1266 C CA  . ASN A 179 ? 0.5383 0.3092 0.3928 0.0750  0.0547  0.1032  179 ASN A CA  
1267 C C   . ASN A 179 ? 0.5068 0.3095 0.3861 0.0811  0.0487  0.1002  179 ASN A C   
1268 O O   . ASN A 179 ? 0.4931 0.2837 0.3675 0.0915  0.0522  0.1013  179 ASN A O   
1269 C CB  . ASN A 179 ? 0.5752 0.3460 0.4178 0.0922  0.0571  0.1168  179 ASN A CB  
1270 C CG  . ASN A 179 ? 0.7220 0.5375 0.5864 0.0921  0.0483  0.1193  179 ASN A CG  
1271 O OD1 . ASN A 179 ? 0.5505 0.3809 0.4258 0.0760  0.0437  0.1119  179 ASN A OD1 
1272 N ND2 . ASN A 179 ? 0.6739 0.5122 0.5436 0.1099  0.0461  0.1302  179 ASN A ND2 
1273 N N   . VAL A 180 ? 0.4778 0.3188 0.3807 0.0751  0.0404  0.0970  180 VAL A N   
1274 C CA  . VAL A 180 ? 0.4477 0.3173 0.3721 0.0781  0.0344  0.0940  180 VAL A CA  
1275 C C   . VAL A 180 ? 0.4671 0.3266 0.3970 0.0686  0.0351  0.0833  180 VAL A C   
1276 O O   . VAL A 180 ? 0.4415 0.3033 0.3766 0.0758  0.0351  0.0827  180 VAL A O   
1277 C CB  . VAL A 180 ? 0.4188 0.3240 0.3603 0.0710  0.0259  0.0924  180 VAL A CB  
1278 C CG1 . VAL A 180 ? 0.3712 0.3025 0.3319 0.0706  0.0198  0.0886  180 VAL A CG1 
1279 C CG2 . VAL A 180 ? 0.4620 0.3796 0.3969 0.0799  0.0245  0.1041  180 VAL A CG2 
1280 N N   . TYR A 181 ? 0.4093 0.2603 0.3382 0.0522  0.0355  0.0755  181 TYR A N   
1281 C CA  . TYR A 181 ? 0.4385 0.2803 0.3702 0.0418  0.0363  0.0668  181 TYR A CA  
1282 C C   . TYR A 181 ? 0.3904 0.1988 0.3023 0.0485  0.0425  0.0687  181 TYR A C   
1283 O O   . TYR A 181 ? 0.4195 0.2288 0.3369 0.0516  0.0419  0.0653  181 TYR A O   
1284 C CB  . TYR A 181 ? 0.3941 0.2323 0.3234 0.0245  0.0373  0.0623  181 TYR A CB  
1285 C CG  . TYR A 181 ? 0.4207 0.2482 0.3478 0.0105  0.0386  0.0558  181 TYR A CG  
1286 C CD1 . TYR A 181 ? 0.3577 0.2077 0.3047 0.0053  0.0343  0.0490  181 TYR A CD1 
1287 C CD2 . TYR A 181 ? 0.4411 0.2364 0.3441 0.0004  0.0440  0.0569  181 TYR A CD2 
1288 C CE1 . TYR A 181 ? 0.4245 0.2700 0.3703 -0.0086 0.0347  0.0442  181 TYR A CE1 
1289 C CE2 . TYR A 181 ? 0.4548 0.2438 0.3546 -0.0163 0.0441  0.0516  181 TYR A CE2 
1290 C CZ  . TYR A 181 ? 0.3860 0.2031 0.3089 -0.0204 0.0391  0.0456  181 TYR A CZ  
1291 O OH  . TYR A 181 ? 0.4524 0.2680 0.3727 -0.0373 0.0385  0.0417  181 TYR A OH  
1292 N N   . TRP A 182 ? 0.4429 0.2187 0.3284 0.0517  0.0493  0.0747  182 TRP A N   
1293 C CA  . TRP A 182 ? 0.5534 0.2880 0.4120 0.0574  0.0571  0.0760  182 TRP A CA  
1294 C C   . TRP A 182 ? 0.5695 0.3097 0.4306 0.0803  0.0589  0.0821  182 TRP A C   
1295 O O   . TRP A 182 ? 0.5588 0.2800 0.4102 0.0842  0.0627  0.0794  182 TRP A O   
1296 C CB  . TRP A 182 ? 0.5769 0.2708 0.4020 0.0566  0.0649  0.0818  182 TRP A CB  
1297 C CG  . TRP A 182 ? 0.7250 0.3667 0.5150 0.0527  0.0731  0.0798  182 TRP A CG  
1298 C CD1 . TRP A 182 ? 0.7772 0.3855 0.5390 0.0692  0.0816  0.0847  182 TRP A CD1 
1299 C CD2 . TRP A 182 ? 0.6057 0.2305 0.3866 0.0287  0.0725  0.0705  182 TRP A CD2 
1300 N NE1 . TRP A 182 ? 0.7862 0.3600 0.5224 0.0557  0.0855  0.0765  182 TRP A NE1 
1301 C CE2 . TRP A 182 ? 0.8278 0.4047 0.5717 0.0305  0.0805  0.0696  182 TRP A CE2 
1302 C CE3 . TRP A 182 ? 0.5643 0.2172 0.3668 0.0061  0.0652  0.0625  182 TRP A CE3 
1303 C CZ2 . TRP A 182 ? 0.7671 0.3219 0.4932 0.0077  0.0805  0.0609  182 TRP A CZ2 
1304 C CZ3 . TRP A 182 ? 0.6199 0.2499 0.4051 -0.0151 0.0661  0.0563  182 TRP A CZ3 
1305 C CH2 . TRP A 182 ? 0.6811 0.2548 0.4241 -0.0159 0.0742  0.0565  182 TRP A CH2 
1306 N N   . ASP A 183 ? 0.5344 0.3030 0.4080 0.0949  0.0563  0.0909  183 ASP A N   
1307 C CA  . ASP A 183 ? 0.5009 0.2846 0.3803 0.1166  0.0576  0.0989  183 ASP A CA  
1308 C C   . ASP A 183 ? 0.5632 0.3699 0.4646 0.1122  0.0524  0.0913  183 ASP A C   
1309 O O   . ASP A 183 ? 0.5002 0.3015 0.3976 0.1258  0.0567  0.0941  183 ASP A O   
1310 C CB  . ASP A 183 ? 0.4776 0.2985 0.3709 0.1278  0.0531  0.1097  183 ASP A CB  
1311 C CG  . ASP A 183 ? 0.6457 0.4449 0.5152 0.1406  0.0599  0.1213  183 ASP A CG  
1312 O OD1 . ASP A 183 ? 0.6566 0.4135 0.4979 0.1458  0.0695  0.1213  183 ASP A OD1 
1313 O OD2 . ASP A 183 ? 0.5583 0.3858 0.4373 0.1430  0.0550  0.1285  183 ASP A OD2 
1314 N N   . PHE A 184 ? 0.4174 0.2496 0.3410 0.0948  0.0439  0.0825  184 PHE A N   
1315 C CA  . PHE A 184 ? 0.3833 0.2363 0.3265 0.0910  0.0390  0.0759  184 PHE A CA  
1316 C C   . PHE A 184 ? 0.4486 0.2723 0.3800 0.0841  0.0430  0.0679  184 PHE A C   
1317 O O   . PHE A 184 ? 0.4495 0.2775 0.3862 0.0897  0.0433  0.0663  184 PHE A O   
1318 C CB  . PHE A 184 ? 0.4302 0.3147 0.3961 0.0768  0.0300  0.0697  184 PHE A CB  
1319 C CG  . PHE A 184 ? 0.4131 0.3335 0.3940 0.0831  0.0240  0.0762  184 PHE A CG  
1320 C CD1 . PHE A 184 ? 0.4689 0.4120 0.4635 0.0883  0.0208  0.0775  184 PHE A CD1 
1321 C CD2 . PHE A 184 ? 0.4454 0.3772 0.4247 0.0827  0.0216  0.0818  184 PHE A CD2 
1322 C CE1 . PHE A 184 ? 0.4670 0.4452 0.4736 0.0907  0.0146  0.0845  184 PHE A CE1 
1323 C CE2 . PHE A 184 ? 0.3611 0.3267 0.3514 0.0856  0.0153  0.0883  184 PHE A CE2 
1324 C CZ  . PHE A 184 ? 0.4106 0.4000 0.4144 0.0887  0.0115  0.0899  184 PHE A CZ  
1325 N N   . ILE A 185 ? 0.4357 0.2294 0.3490 0.0712  0.0463  0.0636  185 ILE A N   
1326 C CA  . ILE A 185 ? 0.4721 0.2349 0.3684 0.0629  0.0502  0.0571  185 ILE A CA  
1327 C C   . ILE A 185 ? 0.5108 0.2443 0.3842 0.0815  0.0589  0.0625  185 ILE A C   
1328 O O   . ILE A 185 ? 0.5277 0.2524 0.3977 0.0823  0.0603  0.0581  185 ILE A O   
1329 C CB  . ILE A 185 ? 0.5375 0.2736 0.4145 0.0439  0.0524  0.0537  185 ILE A CB  
1330 C CG1 . ILE A 185 ? 0.5009 0.2702 0.4030 0.0260  0.0445  0.0475  185 ILE A CG1 
1331 C CG2 . ILE A 185 ? 0.5226 0.2164 0.3703 0.0357  0.0579  0.0494  185 ILE A CG2 
1332 C CD1 . ILE A 185 ? 0.5224 0.2834 0.4145 0.0117  0.0457  0.0484  185 ILE A CD1 
1333 N N   . LYS A 186 ? 0.5183 0.2364 0.3747 0.0985  0.0655  0.0727  186 LYS A N   
1334 C CA  . LYS A 186 ? 0.5750 0.2742 0.4114 0.1170  0.0740  0.0769  186 LYS A CA  
1335 C C   . LYS A 186 ? 0.5918 0.3277 0.4520 0.1311  0.0715  0.0798  186 LYS A C   
1336 O O   . LYS A 186 ? 0.5870 0.3131 0.4374 0.1365  0.0761  0.0769  186 LYS A O   
1337 C CB  . LYS A 186 ? 0.5596 0.2506 0.3794 0.1301  0.0800  0.0855  186 LYS A CB  
1338 C CG  . LYS A 186 ? 0.7322 0.3847 0.5252 0.1153  0.0832  0.0827  186 LYS A CG  
1339 C CD  . LYS A 186 ? 0.8671 0.4988 0.6338 0.1295  0.0921  0.0891  186 LYS A CD  
1340 C CE  . LYS A 186 ? 0.8826 0.5438 0.6646 0.1416  0.0894  0.1001  186 LYS A CE  
1341 N NZ  . LYS A 186 ? 0.9482 0.5785 0.7027 0.1402  0.0953  0.1029  186 LYS A NZ  
1342 N N   . ILE A 187 ? 0.5351 0.3135 0.4250 0.1357  0.0641  0.0857  187 ILE A N   
1343 C CA  . ILE A 187 ? 0.5920 0.4094 0.5063 0.1443  0.0602  0.0882  187 ILE A CA  
1344 C C   . ILE A 187 ? 0.5046 0.3179 0.4254 0.1317  0.0574  0.0768  187 ILE A C   
1345 O O   . ILE A 187 ? 0.4860 0.3045 0.4085 0.1407  0.0600  0.0773  187 ILE A O   
1346 C CB  . ILE A 187 ? 0.5525 0.4198 0.4964 0.1405  0.0499  0.0923  187 ILE A CB  
1347 C CG1 . ILE A 187 ? 0.5300 0.4078 0.4687 0.1560  0.0523  0.1064  187 ILE A CG1 
1348 C CG2 . ILE A 187 ? 0.5569 0.4628 0.5253 0.1420  0.0443  0.0926  187 ILE A CG2 
1349 C CD1 . ILE A 187 ? 0.5083 0.4317 0.4711 0.1472  0.0413  0.1091  187 ILE A CD1 
1350 N N   . TYR A 188 ? 0.4556 0.2661 0.3822 0.1092  0.0514  0.0661  188 TYR A N   
1351 C CA  . TYR A 188 ? 0.4074 0.2205 0.3427 0.0964  0.0476  0.0559  188 TYR A CA  
1352 C C   . TYR A 188 ? 0.4499 0.2219 0.3574 0.0998  0.0560  0.0532  188 TYR A C   
1353 O O   . TYR A 188 ? 0.5094 0.2866 0.4221 0.1016  0.0557  0.0499  188 TYR A O   
1354 C CB  . TYR A 188 ? 0.4255 0.2439 0.3697 0.0741  0.0411  0.0473  188 TYR A CB  
1355 C CG  . TYR A 188 ? 0.4365 0.2924 0.4056 0.0704  0.0334  0.0483  188 TYR A CG  
1356 C CD1 . TYR A 188 ? 0.3753 0.2610 0.3597 0.0817  0.0304  0.0549  188 TYR A CD1 
1357 C CD2 . TYR A 188 ? 0.3892 0.2509 0.3645 0.0547  0.0295  0.0432  188 TYR A CD2 
1358 C CE1 . TYR A 188 ? 0.3918 0.3069 0.3934 0.0755  0.0233  0.0551  188 TYR A CE1 
1359 C CE2 . TYR A 188 ? 0.3389 0.2292 0.3316 0.0520  0.0237  0.0436  188 TYR A CE2 
1360 C CZ  . TYR A 188 ? 0.3791 0.2932 0.3831 0.0614  0.0205  0.0489  188 TYR A CZ  
1361 O OH  . TYR A 188 ? 0.3508 0.2879 0.3666 0.0557  0.0148  0.0484  188 TYR A OH  
1362 N N   . LEU A 189 ? 0.5277 0.2556 0.4022 0.1004  0.0639  0.0546  189 LEU A N   
1363 C CA  . LEU A 189 ? 0.5536 0.2433 0.3973 0.0994  0.0712  0.0502  189 LEU A CA  
1364 C C   . LEU A 189 ? 0.6170 0.3189 0.4604 0.1198  0.0765  0.0548  189 LEU A C   
1365 O O   . LEU A 189 ? 0.5651 0.2529 0.3965 0.1186  0.0795  0.0498  189 LEU A O   
1366 C CB  . LEU A 189 ? 0.5724 0.2227 0.3818 0.0933  0.0774  0.0499  189 LEU A CB  
1367 C CG  . LEU A 189 ? 0.7507 0.3872 0.5559 0.0700  0.0733  0.0457  189 LEU A CG  
1368 C CD1 . LEU A 189 ? 0.8154 0.4143 0.5848 0.0654  0.0800  0.0464  189 LEU A CD1 
1369 C CD2 . LEU A 189 ? 0.6751 0.3062 0.4816 0.0484  0.0685  0.0364  189 LEU A CD2 
1370 N N   . VAL A 190 ? 0.5699 0.2981 0.4243 0.1377  0.0781  0.0651  190 VAL A N   
1371 C CA  . VAL A 190 ? 0.5989 0.3472 0.4567 0.1564  0.0830  0.0714  190 VAL A CA  
1372 C C   . VAL A 190 ? 0.5419 0.3227 0.4276 0.1543  0.0764  0.0691  190 VAL A C   
1373 O O   . VAL A 190 ? 0.5474 0.3265 0.4273 0.1601  0.0806  0.0680  190 VAL A O   
1374 C CB  . VAL A 190 ? 0.5563 0.3327 0.4226 0.1733  0.0850  0.0839  190 VAL A CB  
1375 C CG1 . VAL A 190 ? 0.6130 0.4198 0.4878 0.1908  0.0893  0.0919  190 VAL A CG1 
1376 C CG2 . VAL A 190 ? 0.6345 0.3762 0.4699 0.1781  0.0933  0.0867  190 VAL A CG2 
1377 N N   . ASP A 191 ? 0.5170 0.3272 0.4317 0.1462  0.0664  0.0688  191 ASP A N   
1378 C CA  . ASP A 191 ? 0.4922 0.3320 0.4324 0.1428  0.0600  0.0664  191 ASP A CA  
1379 C C   . ASP A 191 ? 0.5487 0.3613 0.4777 0.1321  0.0609  0.0557  191 ASP A C   
1380 O O   . ASP A 191 ? 0.5193 0.3458 0.4568 0.1350  0.0605  0.0545  191 ASP A O   
1381 C CB  . ASP A 191 ? 0.4654 0.3378 0.4336 0.1308  0.0490  0.0653  191 ASP A CB  
1382 C CG  . ASP A 191 ? 0.6568 0.5635 0.6389 0.1408  0.0465  0.0769  191 ASP A CG  
1383 O OD1 . ASP A 191 ? 0.6003 0.5129 0.5745 0.1568  0.0526  0.0861  191 ASP A OD1 
1384 O OD2 . ASP A 191 ? 0.5171 0.4480 0.5165 0.1276  0.0375  0.0747  191 ASP A OD2 
1385 N N   . PHE A 192 ? 0.5243 0.2998 0.4339 0.1179  0.0617  0.0483  192 PHE A N   
1386 C CA  . PHE A 192 ? 0.5183 0.2715 0.4162 0.1035  0.0611  0.0381  192 PHE A CA  
1387 C C   . PHE A 192 ? 0.6056 0.3404 0.4817 0.1134  0.0691  0.0379  192 PHE A C   
1388 O O   . PHE A 192 ? 0.6893 0.4213 0.5654 0.1082  0.0680  0.0323  192 PHE A O   
1389 C CB  . PHE A 192 ? 0.5800 0.3008 0.4568 0.0834  0.0606  0.0314  192 PHE A CB  
1390 C CG  . PHE A 192 ? 0.4682 0.2180 0.3693 0.0668  0.0509  0.0288  192 PHE A CG  
1391 C CD1 . PHE A 192 ? 0.4015 0.1972 0.3380 0.0664  0.0426  0.0289  192 PHE A CD1 
1392 C CD2 . PHE A 192 ? 0.5235 0.2521 0.4089 0.0515  0.0511  0.0265  192 PHE A CD2 
1393 C CE1 . PHE A 192 ? 0.4180 0.2362 0.3727 0.0532  0.0354  0.0265  192 PHE A CE1 
1394 C CE2 . PHE A 192 ? 0.4802 0.2365 0.3872 0.0382  0.0436  0.0249  192 PHE A CE2 
1395 C CZ  . PHE A 192 ? 0.4446 0.2447 0.3857 0.0404  0.0362  0.0248  192 PHE A CZ  
1396 N N   . LYS A 193 ? 0.6541 0.3766 0.5103 0.1271  0.0775  0.0441  193 LYS A N   
1397 C CA  . LYS A 193 ? 0.6826 0.3856 0.5139 0.1372  0.0869  0.0446  193 LYS A CA  
1398 C C   . LYS A 193 ? 0.7876 0.5258 0.6405 0.1492  0.0864  0.0487  193 LYS A C   
1399 O O   . LYS A 193 ? 0.8811 0.6044 0.7172 0.1531  0.0923  0.0467  193 LYS A O   
1400 C CB  . LYS A 193 ? 0.6144 0.2988 0.4197 0.1520  0.0974  0.0519  193 LYS A CB  
1401 C CG  . LYS A 193 ? 0.9421 0.5945 0.7261 0.1416  0.0983  0.0496  193 LYS A CG  
1402 C CD  . LYS A 193 ? 0.9962 0.6033 0.7482 0.1217  0.0995  0.0391  193 LYS A CD  
1403 N N   . LYS A 194 ? 0.6525 0.4365 0.5404 0.1537  0.0797  0.0546  194 LYS A N   
1404 C CA  . LYS A 194 ? 0.7573 0.5774 0.6656 0.1624  0.0787  0.0592  194 LYS A CA  
1405 C C   . LYS A 194 ? 0.7836 0.6034 0.7009 0.1508  0.0734  0.0504  194 LYS A C   
1406 O O   . LYS A 194 ? 0.9885 0.8217 0.9098 0.1571  0.0757  0.0520  194 LYS A O   
1407 C CB  . LYS A 194 ? 0.6970 0.5664 0.6372 0.1669  0.0722  0.0681  194 LYS A CB  
1408 C CG  . LYS A 194 ? 0.7638 0.6411 0.6967 0.1808  0.0778  0.0789  194 LYS A CG  
1409 C CD  . LYS A 194 ? 0.7166 0.6301 0.6755 0.1774  0.0690  0.0846  194 LYS A CD  
1410 C CE  . LYS A 194 ? 0.8166 0.7367 0.7667 0.1907  0.0746  0.0954  194 LYS A CE  
1411 N NZ  . LYS A 194 ? 0.7753 0.7299 0.7482 0.1861  0.0654  0.1011  194 LYS A NZ  
1412 N N   . MET A 195 ? 0.7424 0.5477 0.6621 0.1342  0.0671  0.0418  195 MET A N   
1413 C CA  . MET A 195 ? 0.9049 0.7124 0.8343 0.1236  0.0619  0.0343  195 MET A CA  
1414 C C   . MET A 195 ? 0.9076 0.6807 0.8078 0.1213  0.0681  0.0283  195 MET A C   
1415 O O   . MET A 195 ? 0.7800 0.5138 0.6496 0.1143  0.0723  0.0242  195 MET A O   
1416 C CB  . MET A 195 ? 0.8369 0.6480 0.7775 0.1012  0.0521  0.0263  195 MET A CB  
1417 C CG  . MET A 195 ? 0.9599 0.7704 0.9028 0.0857  0.0468  0.0173  195 MET A CG  
1418 S SD  . MET A 195 ? 0.9603 0.7949 0.9264 0.0627  0.0343  0.0107  195 MET A SD  
1419 C CE  . MET A 195 ? 0.6942 0.5734 0.6936 0.0695  0.0287  0.0165  195 MET A CE  
1420 N N   . PRO A 196 ? 1.2143 0.9999 1.1210 0.1252  0.0686  0.0278  196 PRO A N   
1421 C CA  . PRO A 196 ? 1.1792 0.9313 1.0562 0.1227  0.0744  0.0221  196 PRO A CA  
1422 C C   . PRO A 196 ? 1.0946 0.8199 0.9596 0.1011  0.0692  0.0112  196 PRO A C   
1423 O O   . PRO A 196 ? 1.0968 0.8285 0.9678 0.0936  0.0652  0.0063  196 PRO A O   
1424 C CB  . PRO A 196 ? 1.0994 0.8798 0.9925 0.1326  0.0752  0.0255  196 PRO A CB  
1425 C CG  . PRO A 196 ? 1.0568 0.8865 0.9867 0.1395  0.0699  0.0339  196 PRO A CG  
1426 C CD  . PRO A 196 ? 1.0193 0.8498 0.9595 0.1300  0.0633  0.0321  196 PRO A CD  
1427 N N   . LEU A 197 ? 0.8391 0.5391 0.6875 0.0886  0.0683  0.0080  197 LEU A N   
1428 C CA  . LEU A 197 ? 0.8507 0.5411 0.6947 0.0628  0.0603  -0.0007 197 LEU A CA  
1429 C C   . LEU A 197 ? 0.9675 0.6199 0.7766 0.0535  0.0640  -0.0075 197 LEU A C   
1430 O O   . LEU A 197 ? 0.9254 0.5925 0.7434 0.0366  0.0557  -0.0130 197 LEU A O   
1431 C CB  . LEU A 197 ? 0.8778 0.5535 0.7126 0.0511  0.0588  -0.0011 197 LEU A CB  
1432 C CG  . LEU A 197 ? 0.8840 0.5849 0.7387 0.0266  0.0469  -0.0055 197 LEU A CG  
1433 C CD1 . LEU A 197 ? 0.7495 0.5040 0.6491 0.0297  0.0382  -0.0036 197 LEU A CD1 
1434 C CD2 . LEU A 197 ? 0.7450 0.4316 0.5894 0.0176  0.0473  -0.0043 197 LEU A CD2 
1435 N N   . GLU A 198 ? 0.8412 0.4649 0.6178 0.0616  0.0736  -0.0058 198 GLU A N   
1436 C CA  . GLU A 198 ? 0.9245 0.5174 0.6674 0.0529  0.0771  -0.0113 198 GLU A CA  
1437 C C   . GLU A 198 ? 0.8832 0.4946 0.6403 0.0621  0.0770  -0.0116 198 GLU A C   
1438 O O   . GLU A 198 ? 0.8175 0.4169 0.5616 0.0477  0.0737  -0.0183 198 GLU A O   
1439 C CB  . GLU A 198 ? 0.9174 0.4742 0.6201 0.0628  0.0892  -0.0080 198 GLU A CB  
1440 C CG  . GLU A 198 ? 1.0920 0.6116 0.7533 0.0544  0.0943  -0.0130 198 GLU A CG  
1441 C CD  . GLU A 198 ? 1.1713 0.6476 0.7859 0.0617  0.1069  -0.0100 198 GLU A CD  
1442 O OE1 . GLU A 198 ? 1.0680 0.5448 0.6836 0.0753  0.1122  -0.0036 198 GLU A OE1 
1443 O OE2 . GLU A 198 ? 1.1946 0.6349 0.7692 0.0537  0.1119  -0.0136 198 GLU A OE2 
1444 N N   . ASN A 199 ? 0.8415 0.4847 0.6251 0.0845  0.0799  -0.0040 199 ASN A N   
1445 C CA  . ASN A 199 ? 0.9149 0.5792 0.7136 0.0932  0.0800  -0.0033 199 ASN A CA  
1446 C C   . ASN A 199 ? 0.7811 0.4699 0.6068 0.0778  0.0681  -0.0086 199 ASN A C   
1447 O O   . ASN A 199 ? 0.8018 0.4965 0.6280 0.0733  0.0659  -0.0119 199 ASN A O   
1448 C CB  . ASN A 199 ? 0.9833 0.6839 0.8067 0.1168  0.0844  0.0076  199 ASN A CB  
1449 C CG  . ASN A 199 ? 1.0993 0.7821 0.8949 0.1338  0.0972  0.0140  199 ASN A CG  
1450 O OD1 . ASN A 199 ? 1.1189 0.7591 0.8758 0.1295  0.1035  0.0110  199 ASN A OD1 
1451 N ND2 . ASN A 199 ? 0.9865 0.7023 0.8001 0.1526  0.1015  0.0236  199 ASN A ND2 
1452 N N   . TYR A 200 ? 0.7250 0.4408 0.5774 0.0667  0.0585  -0.0083 200 TYR A N   
1453 C CA  . TYR A 200 ? 0.6790 0.4306 0.5606 0.0500  0.0456  -0.0116 200 TYR A CA  
1454 C C   . TYR A 200 ? 0.6758 0.4079 0.5364 0.0278  0.0410  -0.0191 200 TYR A C   
1455 O O   . TYR A 200 ? 0.6782 0.4302 0.5507 0.0196  0.0344  -0.0215 200 TYR A O   
1456 C CB  . TYR A 200 ? 0.6289 0.4095 0.5389 0.0454  0.0384  -0.0092 200 TYR A CB  
1457 C CG  . TYR A 200 ? 0.7207 0.5364 0.6608 0.0604  0.0378  -0.0024 200 TYR A CG  
1458 C CD1 . TYR A 200 ? 0.8656 0.6980 0.8156 0.0703  0.0393  0.0002  200 TYR A CD1 
1459 C CD2 . TYR A 200 ? 0.6469 0.4790 0.6035 0.0631  0.0356  0.0016  200 TYR A CD2 
1460 C CE1 . TYR A 200 ? 0.8190 0.6848 0.7946 0.0804  0.0381  0.0069  200 TYR A CE1 
1461 C CE2 . TYR A 200 ? 0.7227 0.5868 0.7037 0.0736  0.0342  0.0079  200 TYR A CE2 
1462 C CZ  . TYR A 200 ? 0.5485 0.4297 0.5386 0.0813  0.0352  0.0106  200 TYR A CZ  
1463 O OH  . TYR A 200 ? 0.7503 0.6648 0.7629 0.0883  0.0332  0.0175  200 TYR A OH  
1464 N N   . ASP A 201 ? 0.7043 0.3981 0.5321 0.0166  0.0441  -0.0223 201 ASP A N   
1465 C CA  . ASP A 201 ? 0.7101 0.3806 0.5098 -0.0065 0.0406  -0.0289 201 ASP A CA  
1466 C C   . ASP A 201 ? 0.8164 0.4671 0.5942 -0.0016 0.0457  -0.0319 201 ASP A C   
1467 O O   . ASP A 201 ? 0.8025 0.4654 0.5821 -0.0164 0.0383  -0.0354 201 ASP A O   
1468 C CB  . ASP A 201 ? 0.7921 0.4159 0.5520 -0.0186 0.0454  -0.0314 201 ASP A CB  
1469 C CG  . ASP A 201 ? 0.8235 0.4682 0.6033 -0.0285 0.0392  -0.0290 201 ASP A CG  
1470 O OD1 . ASP A 201 ? 0.7199 0.4116 0.5363 -0.0367 0.0287  -0.0278 201 ASP A OD1 
1471 O OD2 . ASP A 201 ? 0.9425 0.5555 0.7000 -0.0269 0.0457  -0.0278 201 ASP A OD2 
1472 N N   . THR A 202 ? 0.8414 0.4621 0.5973 0.0203  0.0588  -0.0297 202 THR A N   
1473 C CA  . THR A 202 ? 0.8887 0.4897 0.6223 0.0278  0.0654  -0.0319 202 THR A CA  
1474 C C   . THR A 202 ? 0.7790 0.4291 0.5514 0.0311  0.0580  -0.0300 202 THR A C   
1475 O O   . THR A 202 ? 0.8420 0.4884 0.6034 0.0220  0.0555  -0.0341 202 THR A O   
1476 C CB  . THR A 202 ? 0.8739 0.4621 0.5929 0.0533  0.0792  -0.0250 202 THR A CB  
1477 O OG1 . THR A 202 ? 1.0022 0.5576 0.6894 0.0481  0.0843  -0.0244 202 THR A OG1 
1478 C CG2 . THR A 202 ? 0.9738 0.5485 0.6720 0.0610  0.0862  -0.0256 202 THR A CG2 
1479 N N   . PHE A 203 ? 0.7982 0.4927 0.6133 0.0426  0.0543  -0.0239 203 PHE A N   
1480 C CA  . PHE A 203 ? 0.7674 0.5032 0.6149 0.0460  0.0485  -0.0216 203 PHE A CA  
1481 C C   . PHE A 203 ? 0.7549 0.5116 0.6157 0.0243  0.0356  -0.0257 203 PHE A C   
1482 O O   . PHE A 203 ? 0.6707 0.4388 0.5351 0.0217  0.0326  -0.0269 203 PHE A O   
1483 C CB  . PHE A 203 ? 0.7475 0.5231 0.6334 0.0593  0.0467  -0.0143 203 PHE A CB  
1484 C CG  . PHE A 203 ? 0.9036 0.7187 0.8206 0.0563  0.0386  -0.0130 203 PHE A CG  
1485 C CD1 . PHE A 203 ? 0.8721 0.6915 0.7869 0.0638  0.0422  -0.0118 203 PHE A CD1 
1486 C CD2 . PHE A 203 ? 0.7432 0.5874 0.6879 0.0459  0.0281  -0.0130 203 PHE A CD2 
1487 C CE1 . PHE A 203 ? 0.7201 0.5718 0.6600 0.0602  0.0351  -0.0104 203 PHE A CE1 
1488 C CE2 . PHE A 203 ? 0.7112 0.5848 0.6788 0.0439  0.0219  -0.0116 203 PHE A CE2 
1489 C CZ  . PHE A 203 ? 0.6511 0.5276 0.6158 0.0504  0.0251  -0.0104 203 PHE A CZ  
1490 N N   . ILE A 204 ? 0.6445 0.4119 0.5159 0.0104  0.0281  -0.0265 204 ILE A N   
1491 C CA  . ILE A 204 ? 0.6642 0.4604 0.5534 -0.0062 0.0165  -0.0277 204 ILE A CA  
1492 C C   . ILE A 204 ? 0.6386 0.4124 0.4966 -0.0244 0.0143  -0.0329 204 ILE A C   
1493 O O   . ILE A 204 ? 0.5662 0.3621 0.4338 -0.0333 0.0067  -0.0330 204 ILE A O   
1494 C CB  . ILE A 204 ? 0.5270 0.3454 0.4375 -0.0141 0.0099  -0.0257 204 ILE A CB  
1495 C CG1 . ILE A 204 ? 0.4869 0.3450 0.4248 -0.0218 -0.0002 -0.0238 204 ILE A CG1 
1496 C CG2 . ILE A 204 ? 0.5288 0.3198 0.4125 -0.0300 0.0104  -0.0286 204 ILE A CG2 
1497 C CD1 . ILE A 204 ? 0.3709 0.2518 0.3314 -0.0080 -0.0007 -0.0210 204 ILE A CD1 
1498 N N   . LYS A 205 ? 0.6447 0.3722 0.4619 -0.0298 0.0213  -0.0369 205 LYS A N   
1499 C CA  . LYS A 205 ? 0.7847 0.4850 0.5654 -0.0491 0.0197  -0.0423 205 LYS A CA  
1500 C C   . LYS A 205 ? 0.8069 0.5012 0.5784 -0.0397 0.0236  -0.0437 205 LYS A C   
1501 O O   . LYS A 205 ? 0.8646 0.5721 0.6348 -0.0535 0.0160  -0.0452 205 LYS A O   
1502 C CB  . LYS A 205 ? 0.9218 0.5658 0.6544 -0.0575 0.0276  -0.0466 205 LYS A CB  
1503 C CG  . LYS A 205 ? 1.1039 0.7191 0.7950 -0.0845 0.0240  -0.0526 205 LYS A CG  
1504 C CD  . LYS A 205 ? 1.1255 0.6898 0.7703 -0.0985 0.0296  -0.0557 205 LYS A CD  
1505 C CE  . LYS A 205 ? 1.2023 0.7692 0.8261 -0.1322 0.0199  -0.0573 205 LYS A CE  
1506 N NZ  . LYS A 205 ? 1.1284 0.6507 0.7034 -0.1410 0.0278  -0.0571 205 LYS A NZ  
1507 N N   . GLN A 206 ? 0.8917 0.5677 0.6560 -0.0160 0.0356  -0.0421 206 GLN A N   
1508 C CA  . GLN A 206 ? 1.0160 0.6932 0.7773 -0.0041 0.0401  -0.0418 206 GLN A CA  
1509 C C   . GLN A 206 ? 0.9299 0.6573 0.7306 -0.0072 0.0293  -0.0389 206 GLN A C   
1510 O O   . GLN A 206 ? 0.9498 0.6800 0.7430 -0.0133 0.0263  -0.0406 206 GLN A O   
1511 C CB  . GLN A 206 ? 1.0248 0.6963 0.7893 0.0248  0.0532  -0.0368 206 GLN A CB  
1512 C CG  . GLN A 206 ? 1.1832 0.7985 0.8999 0.0350  0.0680  -0.0388 206 GLN A CG  
1513 C CD  . GLN A 206 ? 1.2575 0.8777 0.9826 0.0661  0.0808  -0.0311 206 GLN A CD  
1514 O OE1 . GLN A 206 ? 1.3043 0.9704 1.0691 0.0770  0.0779  -0.0249 206 GLN A OE1 
1515 N NE2 . GLN A 206 ? 1.0937 0.6818 0.7879 0.0771  0.0925  -0.0281 206 GLN A NE2 
1516 N N   . PHE A 207 ? 0.7690 0.5337 0.6091 -0.0027 0.0236  -0.0342 207 PHE A N   
1517 C CA  . PHE A 207 ? 0.7116 0.5185 0.5863 -0.0011 0.0159  -0.0305 207 PHE A CA  
1518 C C   . PHE A 207 ? 0.7038 0.5286 0.5826 -0.0210 0.0043  -0.0317 207 PHE A C   
1519 O O   . PHE A 207 ? 0.6264 0.4713 0.5154 -0.0220 -0.0004 -0.0301 207 PHE A O   
1520 C CB  . PHE A 207 ? 0.7201 0.5550 0.6293 0.0096  0.0146  -0.0254 207 PHE A CB  
1521 C CG  . PHE A 207 ? 0.7213 0.5853 0.6562 0.0185  0.0127  -0.0213 207 PHE A CG  
1522 C CD1 . PHE A 207 ? 0.6996 0.5886 0.6513 0.0105  0.0037  -0.0202 207 PHE A CD1 
1523 C CD2 . PHE A 207 ? 0.6370 0.5034 0.5770 0.0348  0.0203  -0.0175 207 PHE A CD2 
1524 C CE1 . PHE A 207 ? 0.7972 0.7073 0.7677 0.0178  0.0025  -0.0163 207 PHE A CE1 
1525 C CE2 . PHE A 207 ? 0.7485 0.6407 0.7097 0.0399  0.0183  -0.0134 207 PHE A CE2 
1526 C CZ  . PHE A 207 ? 0.8785 0.7895 0.8533 0.0309  0.0094  -0.0133 207 PHE A CZ  
1527 N N   . LYS A 208 ? 0.5267 0.3478 0.3985 -0.0365 -0.0003 -0.0332 208 LYS A N   
1528 C CA  . LYS A 208 ? 0.5901 0.4338 0.4657 -0.0560 -0.0113 -0.0324 208 LYS A CA  
1529 C C   . LYS A 208 ? 0.6894 0.5142 0.5335 -0.0689 -0.0125 -0.0362 208 LYS A C   
1530 O O   . LYS A 208 ? 0.5917 0.4430 0.4450 -0.0763 -0.0205 -0.0336 208 LYS A O   
1531 C CB  . LYS A 208 ? 0.6589 0.5027 0.5311 -0.0714 -0.0151 -0.0324 208 LYS A CB  
1532 C CG  . LYS A 208 ? 0.7005 0.5890 0.5982 -0.0826 -0.0260 -0.0271 208 LYS A CG  
1533 C CD  . LYS A 208 ? 0.6293 0.5195 0.5271 -0.0943 -0.0277 -0.0262 208 LYS A CD  
1534 C CE  . LYS A 208 ? 0.7050 0.6379 0.6184 -0.1106 -0.0383 -0.0202 208 LYS A CE  
1535 N NZ  . LYS A 208 ? 0.8038 0.7789 0.7574 -0.0948 -0.0407 -0.0133 208 LYS A NZ  
1536 N N   . ASN A 209 ? 0.6689 0.4460 0.4729 -0.0708 -0.0040 -0.0419 209 ASN A N   
1537 C CA  . ASN A 209 ? 0.7505 0.5020 0.5175 -0.0836 -0.0038 -0.0465 209 ASN A CA  
1538 C C   . ASN A 209 ? 0.6975 0.4620 0.4749 -0.0697 -0.0022 -0.0449 209 ASN A C   
1539 O O   . ASN A 209 ? 0.8111 0.5862 0.5813 -0.0819 -0.0090 -0.0450 209 ASN A O   
1540 C CB  . ASN A 209 ? 0.8085 0.4985 0.5257 -0.0849 0.0076  -0.0530 209 ASN A CB  
1541 C CG  . ASN A 209 ? 1.0885 0.7592 0.7858 -0.1049 0.0052  -0.0552 209 ASN A CG  
1542 O OD1 . ASN A 209 ? 1.1956 0.8986 0.9088 -0.1246 -0.0066 -0.0526 209 ASN A OD1 
1543 N ND2 . ASN A 209 ? 1.2249 0.8432 0.8863 -0.0993 0.0170  -0.0591 209 ASN A ND2 
1544 N N   . SER A 210 ? 0.6394 0.4058 0.4336 -0.0453 0.0064  -0.0425 210 SER A N   
1545 C CA  . SER A 210 ? 0.7609 0.5418 0.5660 -0.0331 0.0081  -0.0401 210 SER A CA  
1546 C C   . SER A 210 ? 0.7519 0.5800 0.5925 -0.0369 -0.0034 -0.0348 210 SER A C   
1547 O O   . SER A 210 ? 0.6398 0.4782 0.4791 -0.0388 -0.0066 -0.0337 210 SER A O   
1548 C CB  . SER A 210 ? 0.7242 0.5023 0.5408 -0.0082 0.0194  -0.0371 210 SER A CB  
1549 O OG  . SER A 210 ? 0.9036 0.7215 0.7626 0.0007  0.0150  -0.0311 210 SER A OG  
1550 N N   . TYR A 211 ? 0.5212 0.3761 0.3912 -0.0370 -0.0090 -0.0311 211 TYR A N   
1551 C CA  . TYR A 211 ? 0.4472 0.3427 0.3464 -0.0391 -0.0186 -0.0254 211 TYR A CA  
1552 C C   . TYR A 211 ? 0.4883 0.3942 0.3745 -0.0581 -0.0277 -0.0250 211 TYR A C   
1553 O O   . TYR A 211 ? 0.5248 0.4512 0.4192 -0.0569 -0.0323 -0.0212 211 TYR A O   
1554 C CB  . TYR A 211 ? 0.4426 0.3585 0.3678 -0.0370 -0.0215 -0.0222 211 TYR A CB  
1555 C CG  . TYR A 211 ? 0.4109 0.3650 0.3598 -0.0406 -0.0307 -0.0160 211 TYR A CG  
1556 C CD1 . TYR A 211 ? 0.4461 0.4206 0.4155 -0.0284 -0.0317 -0.0110 211 TYR A CD1 
1557 C CD2 . TYR A 211 ? 0.5303 0.5002 0.4800 -0.0554 -0.0375 -0.0141 211 TYR A CD2 
1558 C CE1 . TYR A 211 ? 0.4118 0.4182 0.4000 -0.0280 -0.0382 -0.0043 211 TYR A CE1 
1559 C CE2 . TYR A 211 ? 0.5068 0.5155 0.4790 -0.0552 -0.0445 -0.0065 211 TYR A CE2 
1560 C CZ  . TYR A 211 ? 0.5137 0.5388 0.5042 -0.0400 -0.0443 -0.0016 211 TYR A CZ  
1561 O OH  . TYR A 211 ? 0.5630 0.6231 0.5724 -0.0365 -0.0496 0.0069  211 TYR A OH  
1562 N N   . LEU A 212 ? 0.5014 0.3949 0.3665 -0.0769 -0.0309 -0.0281 212 LEU A N   
1563 C CA  . LEU A 212 ? 0.6582 0.5671 0.5110 -0.0985 -0.0409 -0.0265 212 LEU A CA  
1564 C C   . LEU A 212 ? 0.6275 0.5155 0.4511 -0.1031 -0.0395 -0.0301 212 LEU A C   
1565 O O   . LEU A 212 ? 0.6838 0.5952 0.5068 -0.1138 -0.0482 -0.0264 212 LEU A O   
1566 C CB  . LEU A 212 ? 0.6031 0.5007 0.4355 -0.1212 -0.0444 -0.0290 212 LEU A CB  
1567 C CG  . LEU A 212 ? 0.7247 0.6459 0.5844 -0.1196 -0.0466 -0.0248 212 LEU A CG  
1568 C CD1 . LEU A 212 ? 0.8311 0.7286 0.6630 -0.1418 -0.0472 -0.0288 212 LEU A CD1 
1569 C CD2 . LEU A 212 ? 0.7171 0.6945 0.6108 -0.1196 -0.0562 -0.0150 212 LEU A CD2 
1570 N N   . SER A 213 ? 0.6634 0.5089 0.4623 -0.0937 -0.0283 -0.0365 213 SER A N   
1571 C CA  . SER A 213 ? 0.7724 0.5969 0.5436 -0.0946 -0.0251 -0.0397 213 SER A CA  
1572 C C   . SER A 213 ? 0.7257 0.5820 0.5249 -0.0803 -0.0271 -0.0338 213 SER A C   
1573 O O   . SER A 213 ? 0.6987 0.5639 0.4879 -0.0886 -0.0326 -0.0324 213 SER A O   
1574 C CB  . SER A 213 ? 0.9127 0.6863 0.6526 -0.0831 -0.0104 -0.0464 213 SER A CB  
1575 O OG  . SER A 213 ? 0.9625 0.7444 0.7257 -0.0573 -0.0021 -0.0432 213 SER A OG  
1576 N N   . TYR A 214 ? 0.5396 0.4116 0.3713 -0.0600 -0.0229 -0.0299 214 TYR A N   
1577 C CA  . TYR A 214 ? 0.5095 0.4079 0.3651 -0.0477 -0.0244 -0.0240 214 TYR A CA  
1578 C C   . TYR A 214 ? 0.4645 0.4002 0.3364 -0.0566 -0.0365 -0.0174 214 TYR A C   
1579 O O   . TYR A 214 ? 0.4948 0.4440 0.3688 -0.0543 -0.0394 -0.0136 214 TYR A O   
1580 C CB  . TYR A 214 ? 0.5911 0.5007 0.4771 -0.0290 -0.0193 -0.0206 214 TYR A CB  
1581 C CG  . TYR A 214 ? 0.7331 0.6180 0.6119 -0.0158 -0.0074 -0.0236 214 TYR A CG  
1582 C CD1 . TYR A 214 ? 0.6908 0.5469 0.5406 -0.0124 0.0013  -0.0275 214 TYR A CD1 
1583 C CD2 . TYR A 214 ? 0.7398 0.6325 0.6410 -0.0055 -0.0044 -0.0215 214 TYR A CD2 
1584 C CE1 . TYR A 214 ? 0.7735 0.6118 0.6182 0.0029  0.0133  -0.0280 214 TYR A CE1 
1585 C CE2 . TYR A 214 ? 0.6952 0.5719 0.5922 0.0076  0.0062  -0.0222 214 TYR A CE2 
1586 C CZ  . TYR A 214 ? 0.9113 0.7625 0.7811 0.0128  0.0153  -0.0248 214 TYR A CZ  
1587 O OH  . TYR A 214 ? 0.7986 0.6387 0.6659 0.0286  0.0266  -0.0233 214 TYR A OH  
1588 N N   . VAL A 215 ? 0.4626 0.4183 0.3485 -0.0643 -0.0429 -0.0147 215 VAL A N   
1589 C CA  . VAL A 215 ? 0.4964 0.4932 0.4006 -0.0691 -0.0533 -0.0061 215 VAL A CA  
1590 C C   . VAL A 215 ? 0.6064 0.6077 0.4868 -0.0872 -0.0606 -0.0056 215 VAL A C   
1591 O O   . VAL A 215 ? 0.5065 0.5332 0.3946 -0.0848 -0.0660 0.0013  215 VAL A O   
1592 C CB  . VAL A 215 ? 0.4434 0.4613 0.3649 -0.0742 -0.0575 -0.0029 215 VAL A CB  
1593 C CG1 . VAL A 215 ? 0.5367 0.5997 0.4726 -0.0804 -0.0678 0.0073  215 VAL A CG1 
1594 C CG2 . VAL A 215 ? 0.4243 0.4428 0.3712 -0.0555 -0.0514 -0.0020 215 VAL A CG2 
1595 N N   . ASP A 216 ? 0.5590 0.5328 0.4068 -0.1060 -0.0605 -0.0128 216 ASP A N   
1596 C CA  . ASP A 216 ? 0.6804 0.6536 0.4993 -0.1269 -0.0676 -0.0134 216 ASP A CA  
1597 C C   . ASP A 216 ? 0.7053 0.6617 0.5096 -0.1183 -0.0631 -0.0154 216 ASP A C   
1598 O O   . ASP A 216 ? 0.6383 0.6130 0.4353 -0.1269 -0.0706 -0.0111 216 ASP A O   
1599 C CB  . ASP A 216 ? 0.6708 0.6083 0.4512 -0.1499 -0.0670 -0.0218 216 ASP A CB  
1600 C CG  . ASP A 216 ? 0.9158 0.8615 0.6679 -0.1784 -0.0776 -0.0208 216 ASP A CG  
1601 O OD1 . ASP A 216 ? 0.8283 0.8234 0.6003 -0.1893 -0.0894 -0.0112 216 ASP A OD1 
1602 O OD2 . ASP A 216 ? 0.9197 0.8236 0.6287 -0.1898 -0.0740 -0.0289 216 ASP A OD2 
1603 N N   . LEU A 217 ? 0.6979 0.6233 0.4993 -0.1006 -0.0510 -0.0207 217 LEU A N   
1604 C CA  . LEU A 217 ? 0.5375 0.4468 0.3254 -0.0911 -0.0450 -0.0223 217 LEU A CA  
1605 C C   . LEU A 217 ? 0.6251 0.5707 0.4420 -0.0790 -0.0494 -0.0130 217 LEU A C   
1606 O O   . LEU A 217 ? 0.7162 0.6648 0.5205 -0.0817 -0.0518 -0.0111 217 LEU A O   
1607 C CB  . LEU A 217 ? 0.7634 0.6395 0.5467 -0.0735 -0.0306 -0.0278 217 LEU A CB  
1608 C CG  . LEU A 217 ? 0.8796 0.7244 0.6366 -0.0648 -0.0199 -0.0321 217 LEU A CG  
1609 C CD1 . LEU A 217 ? 0.9805 0.7800 0.6882 -0.0789 -0.0154 -0.0410 217 LEU A CD1 
1610 C CD2 . LEU A 217 ? 0.8465 0.6864 0.6222 -0.0416 -0.0082 -0.0310 217 LEU A CD2 
1611 N N   . ILE A 218 ? 0.5529 0.5224 0.4053 -0.0654 -0.0497 -0.0072 218 ILE A N   
1612 C CA  . ILE A 218 ? 0.5196 0.5181 0.3957 -0.0534 -0.0530 0.0020  218 ILE A CA  
1613 C C   . ILE A 218 ? 0.5733 0.6047 0.4496 -0.0647 -0.0648 0.0097  218 ILE A C   
1614 O O   . ILE A 218 ? 0.5970 0.6438 0.4763 -0.0590 -0.0675 0.0164  218 ILE A O   
1615 C CB  . ILE A 218 ? 0.5147 0.5258 0.4225 -0.0381 -0.0503 0.0058  218 ILE A CB  
1616 C CG1 . ILE A 218 ? 0.4915 0.4772 0.4006 -0.0260 -0.0392 0.0007  218 ILE A CG1 
1617 C CG2 . ILE A 218 ? 0.5450 0.5836 0.4722 -0.0274 -0.0541 0.0161  218 ILE A CG2 
1618 C CD1 . ILE A 218 ? 0.5466 0.5225 0.4467 -0.0190 -0.0342 0.0014  218 ILE A CD1 
1619 N N   . ARG A 219 ? 0.5844 0.6293 0.4574 -0.0811 -0.0720 0.0101  219 ARG A N   
1620 C CA  . ARG A 219 ? 0.6354 0.7183 0.5088 -0.0937 -0.0839 0.0191  219 ARG A CA  
1621 C C   . ARG A 219 ? 0.6242 0.6963 0.4668 -0.1068 -0.0872 0.0169  219 ARG A C   
1622 O O   . ARG A 219 ? 0.6176 0.7209 0.4634 -0.1084 -0.0950 0.0263  219 ARG A O   
1623 C CB  . ARG A 219 ? 0.5946 0.6948 0.4684 -0.1121 -0.0908 0.0199  219 ARG A CB  
1624 C CG  . ARG A 219 ? 0.5720 0.6983 0.4801 -0.0987 -0.0902 0.0264  219 ARG A CG  
1625 C CD  . ARG A 219 ? 0.8053 0.9628 0.7172 -0.1173 -0.0989 0.0312  219 ARG A CD  
1626 N NE  . ARG A 219 ? 0.7086 0.8325 0.5969 -0.1363 -0.0969 0.0202  219 ARG A NE  
1627 C CZ  . ARG A 219 ? 0.7069 0.8343 0.6048 -0.1407 -0.0962 0.0194  219 ARG A CZ  
1628 N NH1 . ARG A 219 ? 0.6745 0.8383 0.6061 -0.1270 -0.0970 0.0286  219 ARG A NH1 
1629 N NH2 . ARG A 219 ? 0.6335 0.7249 0.5038 -0.1589 -0.0941 0.0095  219 ARG A NH2 
1630 N N   . LYS A 220 ? 0.5734 0.6007 0.3836 -0.1154 -0.0807 0.0051  220 LYS A N   
1631 C CA  . LYS A 220 ? 0.5969 0.6076 0.3737 -0.1263 -0.0820 0.0020  220 LYS A CA  
1632 C C   . LYS A 220 ? 0.7370 0.7456 0.5219 -0.1061 -0.0761 0.0051  220 LYS A C   
1633 O O   . LYS A 220 ? 0.6295 0.6515 0.4047 -0.1102 -0.0815 0.0100  220 LYS A O   
1634 C CB  . LYS A 220 ? 0.6958 0.6540 0.4311 -0.1392 -0.0748 -0.0113 220 LYS A CB  
1635 C CG  . LYS A 220 ? 0.7873 0.7415 0.5053 -0.1643 -0.0811 -0.0146 220 LYS A CG  
1636 C CD  . LYS A 220 ? 0.9084 0.8013 0.5794 -0.1744 -0.0717 -0.0279 220 LYS A CD  
1637 C CE  . LYS A 220 ? 1.0197 0.9025 0.6723 -0.1990 -0.0765 -0.0316 220 LYS A CE  
1638 N NZ  . LYS A 220 ? 1.0877 0.9030 0.6931 -0.2041 -0.0646 -0.0444 220 LYS A NZ  
1639 N N   . TYR A 221 ? 0.7140 0.7077 0.5163 -0.0855 -0.0655 0.0029  221 TYR A N   
1640 C CA  . TYR A 221 ? 0.6996 0.6886 0.5071 -0.0687 -0.0590 0.0055  221 TYR A CA  
1641 C C   . TYR A 221 ? 0.5564 0.5826 0.3863 -0.0606 -0.0661 0.0179  221 TYR A C   
1642 O O   . TYR A 221 ? 0.7367 0.7630 0.5600 -0.0553 -0.0652 0.0215  221 TYR A O   
1643 C CB  . TYR A 221 ? 0.7181 0.6896 0.5414 -0.0512 -0.0474 0.0022  221 TYR A CB  
1644 C CG  . TYR A 221 ? 0.8960 0.8286 0.6953 -0.0524 -0.0372 -0.0082 221 TYR A CG  
1645 C CD1 . TYR A 221 ? 0.9679 0.8734 0.7280 -0.0643 -0.0353 -0.0147 221 TYR A CD1 
1646 C CD2 . TYR A 221 ? 0.9016 0.8235 0.7152 -0.0407 -0.0288 -0.0109 221 TYR A CD2 
1647 C CE1 . TYR A 221 ? 0.9677 0.8333 0.7019 -0.0622 -0.0239 -0.0235 221 TYR A CE1 
1648 C CE2 . TYR A 221 ? 0.9839 0.8715 0.7754 -0.0384 -0.0184 -0.0186 221 TYR A CE2 
1649 C CZ  . TYR A 221 ? 1.0982 0.9562 0.8493 -0.0480 -0.0153 -0.0249 221 TYR A CZ  
1650 O OH  . TYR A 221 ? 1.1646 0.9845 0.8904 -0.0426 -0.0029 -0.0318 221 TYR A OH  
1651 N N   . GLU A 222 ? 0.5494 0.6059 0.4045 -0.0580 -0.0722 0.0251  222 GLU A N   
1652 C CA  . GLU A 222 ? 0.6432 0.7332 0.5174 -0.0469 -0.0774 0.0382  222 GLU A CA  
1653 C C   . GLU A 222 ? 0.6344 0.7421 0.4916 -0.0567 -0.0857 0.0443  222 GLU A C   
1654 O O   . GLU A 222 ? 0.6643 0.7884 0.5290 -0.0448 -0.0871 0.0543  222 GLU A O   
1655 C CB  . GLU A 222 ? 0.6535 0.7749 0.5524 -0.0439 -0.0825 0.0454  222 GLU A CB  
1656 C CG  . GLU A 222 ? 0.6170 0.7254 0.5360 -0.0301 -0.0745 0.0423  222 GLU A CG  
1657 C CD  . GLU A 222 ? 0.7627 0.9016 0.7034 -0.0271 -0.0788 0.0494  222 GLU A CD  
1658 O OE1 . GLU A 222 ? 0.8565 1.0205 0.7944 -0.0423 -0.0873 0.0524  222 GLU A OE1 
1659 O OE2 . GLU A 222 ? 0.8229 0.9607 0.7818 -0.0105 -0.0736 0.0525  222 GLU A OE2 
1660 N N   . LYS A 223 ? 0.7481 0.8500 0.5793 -0.0790 -0.0911 0.0385  223 LYS A N   
1661 C CA  . LYS A 223 ? 0.6277 0.7446 0.4382 -0.0922 -0.0997 0.0433  223 LYS A CA  
1662 C C   . LYS A 223 ? 0.7166 0.7970 0.4978 -0.0936 -0.0930 0.0355  223 LYS A C   
1663 O O   . LYS A 223 ? 0.8056 0.8976 0.5737 -0.0974 -0.0981 0.0411  223 LYS A O   
1664 C CB  . LYS A 223 ? 0.6724 0.8033 0.4655 -0.1200 -0.1103 0.0419  223 LYS A CB  
1665 C CG  . LYS A 223 ? 0.7594 0.9223 0.5776 -0.1227 -0.1156 0.0474  223 LYS A CG  
1666 C CD  . LYS A 223 ? 0.8973 1.1095 0.7492 -0.1042 -0.1200 0.0643  223 LYS A CD  
1667 C CE  . LYS A 223 ? 0.9532 1.2031 0.8268 -0.1093 -0.1260 0.0712  223 LYS A CE  
1668 N NZ  . LYS A 223 ? 0.9086 1.1859 0.8166 -0.0818 -0.1227 0.0833  223 LYS A NZ  
1669 N N   . GLN A 224 ? 0.6716 0.7102 0.4417 -0.0899 -0.0815 0.0235  224 GLN A N   
1670 C CA  . GLN A 224 ? 0.7422 0.7456 0.4816 -0.0911 -0.0737 0.0160  224 GLN A CA  
1671 C C   . GLN A 224 ? 0.7355 0.7297 0.4886 -0.0692 -0.0633 0.0181  224 GLN A C   
1672 O O   . GLN A 224 ? 0.7078 0.6831 0.4392 -0.0680 -0.0578 0.0155  224 GLN A O   
1673 C CB  . GLN A 224 ? 0.8870 0.8482 0.5987 -0.1007 -0.0660 0.0023  224 GLN A CB  
1674 C CG  . GLN A 224 ? 0.9093 0.8711 0.6002 -0.1263 -0.0753 -0.0013 224 GLN A CG  
1675 C CD  . GLN A 224 ? 1.0270 0.9466 0.6975 -0.1314 -0.0666 -0.0133 224 GLN A CD  
1676 O OE1 . GLN A 224 ? 1.0326 0.9208 0.6994 -0.1154 -0.0528 -0.0192 224 GLN A OE1 
1677 N NE2 . GLN A 224 ? 0.9866 0.9070 0.6434 -0.1535 -0.0743 -0.0158 224 GLN A NE2 
1678 N N   . ILE A 225 ? 0.6346 0.6411 0.4207 -0.0533 -0.0604 0.0228  225 ILE A N   
1679 C CA  . ILE A 225 ? 0.6261 0.6214 0.4240 -0.0359 -0.0502 0.0241  225 ILE A CA  
1680 C C   . ILE A 225 ? 0.7502 0.7715 0.5738 -0.0238 -0.0542 0.0359  225 ILE A C   
1681 O O   . ILE A 225 ? 0.7624 0.8032 0.6060 -0.0214 -0.0593 0.0403  225 ILE A O   
1682 C CB  . ILE A 225 ? 0.7525 0.7279 0.5596 -0.0292 -0.0404 0.0166  225 ILE A CB  
1683 C CG1 . ILE A 225 ? 0.7593 0.7043 0.5367 -0.0384 -0.0348 0.0056  225 ILE A CG1 
1684 C CG2 . ILE A 225 ? 0.6689 0.6387 0.4893 -0.0141 -0.0309 0.0193  225 ILE A CG2 
1685 C CD1 . ILE A 225 ? 0.8102 0.7378 0.5956 -0.0310 -0.0255 -0.0004 225 ILE A CD1 
1686 N N   . ASP A 226 ? 0.5463 0.5654 0.3672 -0.0154 -0.0509 0.0415  226 ASP A N   
1687 C CA  . ASP A 226 ? 0.5663 0.6011 0.4046 -0.0026 -0.0527 0.0529  226 ASP A CA  
1688 C C   . ASP A 226 ? 0.6142 0.6331 0.4667 0.0084  -0.0431 0.0518  226 ASP A C   
1689 O O   . ASP A 226 ? 0.5191 0.5250 0.3656 0.0126  -0.0364 0.0530  226 ASP A O   
1690 C CB  . ASP A 226 ? 0.6509 0.6919 0.4746 -0.0016 -0.0555 0.0608  226 ASP A CB  
1691 C CG  . ASP A 226 ? 0.8349 0.8817 0.6701 0.0136  -0.0543 0.0724  226 ASP A CG  
1692 O OD1 . ASP A 226 ? 0.7749 0.8332 0.6281 0.0220  -0.0561 0.0775  226 ASP A OD1 
1693 O OD2 . ASP A 226 ? 0.8535 0.8909 0.6772 0.0172  -0.0508 0.0764  226 ASP A OD2 
1694 N N   . ASP A 227 ? 0.5510 0.5727 0.4220 0.0117  -0.0427 0.0499  227 ASP A N   
1695 C CA  . ASP A 227 ? 0.4147 0.4230 0.2986 0.0191  -0.0348 0.0485  227 ASP A CA  
1696 C C   . ASP A 227 ? 0.4521 0.4694 0.3550 0.0245  -0.0373 0.0507  227 ASP A C   
1697 O O   . ASP A 227 ? 0.4096 0.4222 0.3217 0.0224  -0.0349 0.0441  227 ASP A O   
1698 C CB  . ASP A 227 ? 0.4466 0.4389 0.3257 0.0147  -0.0273 0.0387  227 ASP A CB  
1699 C CG  . ASP A 227 ? 0.4594 0.4428 0.3502 0.0205  -0.0193 0.0389  227 ASP A CG  
1700 O OD1 . ASP A 227 ? 0.4345 0.4193 0.3353 0.0258  -0.0199 0.0448  227 ASP A OD1 
1701 O OD2 . ASP A 227 ? 0.5064 0.4813 0.3947 0.0195  -0.0122 0.0335  227 ASP A OD2 
1702 N N   . PRO A 228 ? 0.4264 0.4562 0.3344 0.0328  -0.0413 0.0604  228 PRO A N   
1703 C CA  . PRO A 228 ? 0.3871 0.4269 0.3113 0.0392  -0.0431 0.0630  228 PRO A CA  
1704 C C   . PRO A 228 ? 0.3870 0.4080 0.3198 0.0439  -0.0361 0.0599  228 PRO A C   
1705 O O   . PRO A 228 ? 0.3793 0.4052 0.3246 0.0457  -0.0367 0.0580  228 PRO A O   
1706 C CB  . PRO A 228 ? 0.4140 0.4689 0.3372 0.0507  -0.0467 0.0761  228 PRO A CB  
1707 C CG  . PRO A 228 ? 0.4818 0.5246 0.3888 0.0520  -0.0444 0.0799  228 PRO A CG  
1708 C CD  . PRO A 228 ? 0.5175 0.5547 0.4151 0.0380  -0.0443 0.0704  228 PRO A CD  
1709 N N   . ILE A 229 ? 0.4047 0.4062 0.3305 0.0447  -0.0299 0.0598  229 ILE A N   
1710 C CA  . ILE A 229 ? 0.3940 0.3795 0.3261 0.0460  -0.0241 0.0574  229 ILE A CA  
1711 C C   . ILE A 229 ? 0.4173 0.4038 0.3587 0.0387  -0.0224 0.0479  229 ILE A C   
1712 O O   . ILE A 229 ? 0.4025 0.3867 0.3546 0.0398  -0.0212 0.0455  229 ILE A O   
1713 C CB  . ILE A 229 ? 0.4080 0.3753 0.3286 0.0451  -0.0185 0.0607  229 ILE A CB  
1714 C CG1 . ILE A 229 ? 0.4900 0.4499 0.3985 0.0544  -0.0190 0.0708  229 ILE A CG1 
1715 C CG2 . ILE A 229 ? 0.4151 0.3687 0.3407 0.0418  -0.0135 0.0579  229 ILE A CG2 
1716 C CD1 . ILE A 229 ? 0.5774 0.5184 0.4702 0.0514  -0.0140 0.0747  229 ILE A CD1 
1717 N N   . THR A 230 ? 0.3613 0.3491 0.2966 0.0323  -0.0213 0.0429  230 THR A N   
1718 C CA  . THR A 230 ? 0.3862 0.3725 0.3271 0.0282  -0.0185 0.0349  230 THR A CA  
1719 C C   . THR A 230 ? 0.3736 0.3689 0.3203 0.0261  -0.0239 0.0316  230 THR A C   
1720 O O   . THR A 230 ? 0.3323 0.3263 0.2892 0.0259  -0.0225 0.0277  230 THR A O   
1721 C CB  . THR A 230 ? 0.3516 0.3326 0.2798 0.0244  -0.0140 0.0310  230 THR A CB  
1722 O OG1 . THR A 230 ? 0.4235 0.4001 0.3472 0.0256  -0.0089 0.0353  230 THR A OG1 
1723 C CG2 . THR A 230 ? 0.3909 0.3677 0.3231 0.0236  -0.0091 0.0243  230 THR A CG2 
1724 N N   . LEU A 231 ? 0.3375 0.3441 0.2778 0.0233  -0.0304 0.0340  231 LEU A N   
1725 C CA  . LEU A 231 ? 0.3388 0.3569 0.2830 0.0179  -0.0361 0.0314  231 LEU A CA  
1726 C C   . LEU A 231 ? 0.3693 0.3969 0.3309 0.0244  -0.0376 0.0350  231 LEU A C   
1727 O O   . LEU A 231 ? 0.3275 0.3585 0.2962 0.0206  -0.0387 0.0309  231 LEU A O   
1728 C CB  . LEU A 231 ? 0.3853 0.4187 0.3185 0.0114  -0.0437 0.0350  231 LEU A CB  
1729 C CG  . LEU A 231 ? 0.4334 0.4536 0.3445 0.0020  -0.0423 0.0291  231 LEU A CG  
1730 C CD1 . LEU A 231 ? 0.4744 0.5095 0.3721 -0.0047 -0.0500 0.0341  231 LEU A CD1 
1731 C CD2 . LEU A 231 ? 0.4216 0.4286 0.3256 -0.0067 -0.0403 0.0195  231 LEU A CD2 
1732 N N   . GLN A 232 ? 0.3368 0.3666 0.3026 0.0346  -0.0370 0.0429  232 GLN A N   
1733 C CA  . GLN A 232 ? 0.3596 0.3959 0.3382 0.0424  -0.0373 0.0466  232 GLN A CA  
1734 C C   . GLN A 232 ? 0.3799 0.4013 0.3661 0.0417  -0.0322 0.0402  232 GLN A C   
1735 O O   . GLN A 232 ? 0.3209 0.3486 0.3175 0.0425  -0.0331 0.0387  232 GLN A O   
1736 C CB  . GLN A 232 ? 0.3381 0.3733 0.3135 0.0554  -0.0360 0.0567  232 GLN A CB  
1737 C CG  . GLN A 232 ? 0.3576 0.3667 0.3239 0.0586  -0.0296 0.0572  232 GLN A CG  
1738 C CD  . GLN A 232 ? 0.4435 0.4475 0.3991 0.0707  -0.0283 0.0679  232 GLN A CD  
1739 O OE1 . GLN A 232 ? 0.4369 0.4609 0.3939 0.0786  -0.0322 0.0757  232 GLN A OE1 
1740 N NE2 . GLN A 232 ? 0.4100 0.3881 0.3536 0.0719  -0.0227 0.0691  232 GLN A NE2 
1741 N N   . ALA A 233 ? 0.2987 0.3033 0.2800 0.0395  -0.0270 0.0369  233 ALA A N   
1742 C CA  . ALA A 233 ? 0.3229 0.3178 0.3114 0.0377  -0.0227 0.0319  233 ALA A CA  
1743 C C   . ALA A 233 ? 0.3400 0.3393 0.3330 0.0320  -0.0234 0.0249  233 ALA A C   
1744 O O   . ALA A 233 ? 0.3082 0.3076 0.3107 0.0323  -0.0228 0.0224  233 ALA A O   
1745 C CB  . ALA A 233 ? 0.3100 0.2931 0.2927 0.0354  -0.0175 0.0320  233 ALA A CB  
1746 N N   . ILE A 234 ? 0.2686 0.2682 0.2518 0.0265  -0.0241 0.0217  234 ILE A N   
1747 C CA  . ILE A 234 ? 0.2680 0.2651 0.2489 0.0207  -0.0241 0.0151  234 ILE A CA  
1748 C C   . ILE A 234 ? 0.2784 0.2883 0.2670 0.0181  -0.0299 0.0158  234 ILE A C   
1749 O O   . ILE A 234 ? 0.3014 0.3088 0.2954 0.0161  -0.0290 0.0120  234 ILE A O   
1750 C CB  . ILE A 234 ? 0.3354 0.3252 0.2973 0.0145  -0.0235 0.0115  234 ILE A CB  
1751 C CG1 . ILE A 234 ? 0.3023 0.2814 0.2571 0.0185  -0.0161 0.0112  234 ILE A CG1 
1752 C CG2 . ILE A 234 ? 0.3397 0.3213 0.2930 0.0072  -0.0237 0.0049  234 ILE A CG2 
1753 C CD1 . ILE A 234 ? 0.3509 0.3214 0.2836 0.0142  -0.0149 0.0088  234 ILE A CD1 
1754 N N   . LYS A 235 ? 0.2742 0.3002 0.2634 0.0186  -0.0356 0.0219  235 LYS A N   
1755 C CA  . LYS A 235 ? 0.3132 0.3581 0.3113 0.0166  -0.0410 0.0247  235 LYS A CA  
1756 C C   . LYS A 235 ? 0.3425 0.3869 0.3553 0.0248  -0.0380 0.0258  235 LYS A C   
1757 O O   . LYS A 235 ? 0.3119 0.3636 0.3319 0.0216  -0.0395 0.0242  235 LYS A O   
1758 C CB  . LYS A 235 ? 0.2732 0.3414 0.2715 0.0189  -0.0470 0.0339  235 LYS A CB  
1759 C CG  . LYS A 235 ? 0.4913 0.5651 0.4744 0.0079  -0.0519 0.0334  235 LYS A CG  
1760 C CD  . LYS A 235 ? 0.4462 0.5510 0.4329 0.0107  -0.0587 0.0446  235 LYS A CD  
1761 N N   . PHE A 236 ? 0.2680 0.3019 0.2828 0.0342  -0.0338 0.0285  236 PHE A N   
1762 C CA  . PHE A 236 ? 0.2550 0.2836 0.2789 0.0406  -0.0306 0.0288  236 PHE A CA  
1763 C C   . PHE A 236 ? 0.2848 0.3035 0.3125 0.0350  -0.0279 0.0214  236 PHE A C   
1764 O O   . PHE A 236 ? 0.2651 0.2874 0.3010 0.0355  -0.0279 0.0202  236 PHE A O   
1765 C CB  . PHE A 236 ? 0.2521 0.2657 0.2710 0.0486  -0.0265 0.0328  236 PHE A CB  
1766 C CG  . PHE A 236 ? 0.2896 0.2922 0.3125 0.0527  -0.0228 0.0321  236 PHE A CG  
1767 C CD1 . PHE A 236 ? 0.3262 0.3366 0.3540 0.0609  -0.0230 0.0361  236 PHE A CD1 
1768 C CD2 . PHE A 236 ? 0.2828 0.2701 0.3042 0.0480  -0.0193 0.0280  236 PHE A CD2 
1769 C CE1 . PHE A 236 ? 0.3208 0.3182 0.3491 0.0644  -0.0192 0.0349  236 PHE A CE1 
1770 C CE2 . PHE A 236 ? 0.3474 0.3241 0.3699 0.0497  -0.0167 0.0272  236 PHE A CE2 
1771 C CZ  . PHE A 236 ? 0.3013 0.2807 0.3260 0.0579  -0.0165 0.0301  236 PHE A CZ  
1772 N N   . VAL A 237 ? 0.2765 0.2840 0.2979 0.0311  -0.0248 0.0172  237 VAL A N   
1773 C CA  . VAL A 237 ? 0.2702 0.2702 0.2946 0.0285  -0.0214 0.0119  237 VAL A CA  
1774 C C   . VAL A 237 ? 0.2971 0.3006 0.3207 0.0228  -0.0238 0.0081  237 VAL A C   
1775 O O   . VAL A 237 ? 0.2678 0.2686 0.2971 0.0225  -0.0224 0.0055  237 VAL A O   
1776 C CB  . VAL A 237 ? 0.2720 0.2632 0.2890 0.0278  -0.0166 0.0100  237 VAL A CB  
1777 C CG1 . VAL A 237 ? 0.2793 0.2653 0.2984 0.0278  -0.0123 0.0061  237 VAL A CG1 
1778 C CG2 . VAL A 237 ? 0.2961 0.2850 0.3142 0.0304  -0.0143 0.0143  237 VAL A CG2 
1779 N N   . LEU A 238 ? 0.2779 0.2867 0.2924 0.0167  -0.0278 0.0080  238 LEU A N   
1780 C CA  . LEU A 238 ? 0.3553 0.3660 0.3652 0.0074  -0.0308 0.0047  238 LEU A CA  
1781 C C   . LEU A 238 ? 0.2876 0.3154 0.3118 0.0084  -0.0341 0.0082  238 LEU A C   
1782 O O   . LEU A 238 ? 0.2739 0.2996 0.2994 0.0034  -0.0340 0.0052  238 LEU A O   
1783 C CB  . LEU A 238 ? 0.3065 0.3209 0.3011 -0.0025 -0.0354 0.0046  238 LEU A CB  
1784 C CG  . LEU A 238 ? 0.2863 0.2798 0.2614 -0.0045 -0.0310 -0.0001 238 LEU A CG  
1785 C CD1 . LEU A 238 ? 0.3117 0.3080 0.2684 -0.0164 -0.0365 -0.0003 238 LEU A CD1 
1786 C CD2 . LEU A 238 ? 0.3546 0.3250 0.3201 -0.0049 -0.0245 -0.0066 238 LEU A CD2 
1787 N N   . LYS A 239 ? 0.2742 0.3177 0.3074 0.0159  -0.0362 0.0152  239 LYS A N   
1788 C CA  . LYS A 239 ? 0.2540 0.3139 0.3001 0.0204  -0.0376 0.0197  239 LYS A CA  
1789 C C   . LYS A 239 ? 0.2934 0.3400 0.3460 0.0246  -0.0328 0.0161  239 LYS A C   
1790 O O   . LYS A 239 ? 0.2784 0.3320 0.3374 0.0222  -0.0334 0.0157  239 LYS A O   
1791 C CB  . LYS A 239 ? 0.3303 0.4031 0.3804 0.0320  -0.0381 0.0285  239 LYS A CB  
1792 C CG  . LYS A 239 ? 0.3710 0.4547 0.4317 0.0426  -0.0363 0.0341  239 LYS A CG  
1793 C CD  . LYS A 239 ? 0.4886 0.5742 0.5468 0.0573  -0.0341 0.0425  239 LYS A CD  
1794 C CE  . LYS A 239 ? 0.7286 0.8098 0.7902 0.0708  -0.0288 0.0463  239 LYS A CE  
1795 N NZ  . LYS A 239 ? 0.4757 0.5843 0.5492 0.0714  -0.0305 0.0504  239 LYS A NZ  
1796 N N   . GLU A 240 ? 0.2747 0.3039 0.3252 0.0293  -0.0284 0.0140  240 GLU A N   
1797 C CA  . GLU A 240 ? 0.2457 0.2643 0.3012 0.0314  -0.0247 0.0111  240 GLU A CA  
1798 C C   . GLU A 240 ? 0.3236 0.3369 0.3775 0.0246  -0.0239 0.0057  240 GLU A C   
1799 O O   . GLU A 240 ? 0.2929 0.3062 0.3526 0.0245  -0.0231 0.0045  240 GLU A O   
1800 C CB  . GLU A 240 ? 0.2951 0.3003 0.3472 0.0343  -0.0210 0.0109  240 GLU A CB  
1801 C CG  . GLU A 240 ? 0.3007 0.3024 0.3490 0.0402  -0.0204 0.0159  240 GLU A CG  
1802 C CD  . GLU A 240 ? 0.4398 0.4287 0.4830 0.0384  -0.0172 0.0155  240 GLU A CD  
1803 O OE1 . GLU A 240 ? 0.3482 0.3372 0.3876 0.0353  -0.0166 0.0147  240 GLU A OE1 
1804 O OE2 . GLU A 240 ? 0.3432 0.3225 0.3848 0.0390  -0.0152 0.0163  240 GLU A OE2 
1805 N N   . MET A 241 ? 0.2936 0.2990 0.3368 0.0197  -0.0233 0.0025  241 MET A N   
1806 C CA  . MET A 241 ? 0.3015 0.2953 0.3367 0.0144  -0.0212 -0.0023 241 MET A CA  
1807 C C   . MET A 241 ? 0.3491 0.3505 0.3851 0.0067  -0.0250 -0.0027 241 MET A C   
1808 O O   . MET A 241 ? 0.3272 0.3213 0.3633 0.0051  -0.0229 -0.0051 241 MET A O   
1809 C CB  . MET A 241 ? 0.3147 0.2959 0.3326 0.0109  -0.0194 -0.0052 241 MET A CB  
1810 C CG  . MET A 241 ? 0.4844 0.4451 0.4876 0.0090  -0.0143 -0.0099 241 MET A CG  
1811 S SD  . MET A 241 ? 0.4863 0.4280 0.4648 0.0081  -0.0100 -0.0129 241 MET A SD  
1812 C CE  . MET A 241 ? 0.3966 0.3480 0.3872 0.0195  -0.0064 -0.0085 241 MET A CE  
1813 N N   . GLY A 242 ? 0.3204 0.3392 0.3576 0.0018  -0.0305 0.0008  242 GLY A N   
1814 C CA  . GLY A 242 ? 0.3786 0.4117 0.4184 -0.0069 -0.0345 0.0023  242 GLY A CA  
1815 C C   . GLY A 242 ? 0.3059 0.3474 0.3609 -0.0003 -0.0330 0.0046  242 GLY A C   
1816 O O   . GLY A 242 ? 0.3165 0.3587 0.3714 -0.0072 -0.0333 0.0033  242 GLY A O   
1817 N N   . TYR A 243 ? 0.2763 0.3218 0.3416 0.0122  -0.0309 0.0080  243 TYR A N   
1818 C CA  . TYR A 243 ? 0.3044 0.3525 0.3799 0.0189  -0.0284 0.0094  243 TYR A CA  
1819 C C   . TYR A 243 ? 0.2681 0.2982 0.3413 0.0168  -0.0251 0.0040  243 TYR A C   
1820 O O   . TYR A 243 ? 0.2782 0.3109 0.3552 0.0146  -0.0246 0.0036  243 TYR A O   
1821 C CB  . TYR A 243 ? 0.3101 0.3561 0.3892 0.0315  -0.0258 0.0131  243 TYR A CB  
1822 C CG  . TYR A 243 ? 0.2823 0.3239 0.3665 0.0377  -0.0223 0.0133  243 TYR A CG  
1823 C CD1 . TYR A 243 ? 0.4186 0.4759 0.5090 0.0434  -0.0218 0.0184  243 TYR A CD1 
1824 C CD2 . TYR A 243 ? 0.3018 0.3256 0.3838 0.0376  -0.0194 0.0092  243 TYR A CD2 
1825 C CE1 . TYR A 243 ? 0.3794 0.4300 0.4715 0.0491  -0.0178 0.0181  243 TYR A CE1 
1826 C CE2 . TYR A 243 ? 0.3531 0.3718 0.4371 0.0413  -0.0168 0.0091  243 TYR A CE2 
1827 C CZ  . TYR A 243 ? 0.4111 0.4409 0.4990 0.0472  -0.0157 0.0130  243 TYR A CZ  
1828 O OH  . TYR A 243 ? 0.3410 0.3634 0.4280 0.0511  -0.0124 0.0126  243 TYR A OH  
1829 N N   . ILE A 244 ? 0.2661 0.2799 0.3330 0.0182  -0.0223 0.0007  244 ILE A N   
1830 C CA  . ILE A 244 ? 0.2514 0.2517 0.3168 0.0191  -0.0186 -0.0024 244 ILE A CA  
1831 C C   . ILE A 244 ? 0.2679 0.2593 0.3234 0.0113  -0.0181 -0.0056 244 ILE A C   
1832 O O   . ILE A 244 ? 0.2567 0.2415 0.3127 0.0117  -0.0159 -0.0067 244 ILE A O   
1833 C CB  . ILE A 244 ? 0.2652 0.2565 0.3270 0.0236  -0.0153 -0.0028 244 ILE A CB  
1834 C CG1 . ILE A 244 ? 0.2735 0.2698 0.3412 0.0282  -0.0158 0.0004  244 ILE A CG1 
1835 C CG2 . ILE A 244 ? 0.2517 0.2349 0.3132 0.0264  -0.0112 -0.0038 244 ILE A CG2 
1836 C CD1 . ILE A 244 ? 0.3101 0.3025 0.3733 0.0297  -0.0137 0.0011  244 ILE A CD1 
1837 N N   . ILE A 245 ? 0.2308 0.2192 0.2743 0.0033  -0.0202 -0.0070 245 ILE A N   
1838 C CA  . ILE A 245 ? 0.2470 0.2219 0.2751 -0.0073 -0.0199 -0.0103 245 ILE A CA  
1839 C C   . ILE A 245 ? 0.3357 0.3246 0.3722 -0.0133 -0.0228 -0.0082 245 ILE A C   
1840 O O   . ILE A 245 ? 0.2972 0.2735 0.3271 -0.0172 -0.0205 -0.0101 245 ILE A O   
1841 C CB  . ILE A 245 ? 0.3360 0.3057 0.3467 -0.0179 -0.0226 -0.0120 245 ILE A CB  
1842 C CG1 . ILE A 245 ? 0.3056 0.2545 0.3025 -0.0116 -0.0174 -0.0149 245 ILE A CG1 
1843 C CG2 . ILE A 245 ? 0.3042 0.2633 0.2973 -0.0341 -0.0243 -0.0145 245 ILE A CG2 
1844 C CD1 . ILE A 245 ? 0.3023 0.2461 0.2809 -0.0215 -0.0202 -0.0166 245 ILE A CD1 
1845 N N   . ASP A 246 ? 0.2792 0.2947 0.3294 -0.0133 -0.0272 -0.0034 246 ASP A N   
1846 C CA  . ASP A 246 ? 0.2859 0.3197 0.3458 -0.0171 -0.0291 0.0000  246 ASP A CA  
1847 C C   . ASP A 246 ? 0.2893 0.3153 0.3567 -0.0087 -0.0248 -0.0009 246 ASP A C   
1848 O O   . ASP A 246 ? 0.2917 0.3171 0.3579 -0.0147 -0.0243 -0.0011 246 ASP A O   
1849 C CB  . ASP A 246 ? 0.2764 0.3417 0.3505 -0.0125 -0.0326 0.0071  246 ASP A CB  
1850 C CG  . ASP A 246 ? 0.5842 0.6717 0.6702 -0.0125 -0.0328 0.0121  246 ASP A CG  
1851 O OD1 . ASP A 246 ? 0.6704 0.7714 0.7534 -0.0268 -0.0363 0.0140  246 ASP A OD1 
1852 O OD2 . ASP A 246 ? 0.5321 0.6225 0.6283 0.0008  -0.0293 0.0143  246 ASP A OD2 
1853 N N   . ARG A 247 ? 0.2573 0.2775 0.3308 0.0035  -0.0220 -0.0011 247 ARG A N   
1854 C CA  . ARG A 247 ? 0.2672 0.2807 0.3459 0.0096  -0.0186 -0.0017 247 ARG A CA  
1855 C C   . ARG A 247 ? 0.2609 0.2547 0.3289 0.0062  -0.0158 -0.0051 247 ARG A C   
1856 O O   . ARG A 247 ? 0.2841 0.2752 0.3533 0.0056  -0.0142 -0.0051 247 ARG A O   
1857 C CB  . ARG A 247 ? 0.2274 0.2373 0.3106 0.0195  -0.0168 -0.0011 247 ARG A CB  
1858 C CG  . ARG A 247 ? 0.2313 0.2525 0.3202 0.0258  -0.0177 0.0027  247 ARG A CG  
1859 C CD  . ARG A 247 ? 0.3265 0.3576 0.4216 0.0294  -0.0166 0.0055  247 ARG A CD  
1860 N NE  . ARG A 247 ? 0.3943 0.4438 0.4931 0.0237  -0.0189 0.0082  247 ARG A NE  
1861 C CZ  . ARG A 247 ? 0.4705 0.5288 0.5734 0.0215  -0.0180 0.0096  247 ARG A CZ  
1862 N NH1 . ARG A 247 ? 0.4437 0.4924 0.5471 0.0255  -0.0148 0.0082  247 ARG A NH1 
1863 N NH2 . ARG A 247 ? 0.3164 0.3950 0.4223 0.0135  -0.0208 0.0131  247 ARG A NH2 
1864 N N   . PHE A 248 ? 0.2454 0.2241 0.3014 0.0054  -0.0141 -0.0076 248 PHE A N   
1865 C CA  . PHE A 248 ? 0.2845 0.2409 0.3264 0.0055  -0.0095 -0.0099 248 PHE A CA  
1866 C C   . PHE A 248 ? 0.3130 0.2617 0.3440 -0.0062 -0.0103 -0.0111 248 PHE A C   
1867 O O   . PHE A 248 ? 0.3196 0.2581 0.3470 -0.0053 -0.0073 -0.0111 248 PHE A O   
1868 C CB  . PHE A 248 ? 0.2537 0.1940 0.2809 0.0078  -0.0064 -0.0118 248 PHE A CB  
1869 C CG  . PHE A 248 ? 0.3068 0.2231 0.3185 0.0140  0.0007  -0.0126 248 PHE A CG  
1870 C CD1 . PHE A 248 ? 0.3316 0.2234 0.3212 0.0067  0.0033  -0.0152 248 PHE A CD1 
1871 C CD2 . PHE A 248 ? 0.3533 0.2718 0.3706 0.0271  0.0050  -0.0097 248 PHE A CD2 
1872 C CE1 . PHE A 248 ? 0.3622 0.2280 0.3340 0.0154  0.0114  -0.0149 248 PHE A CE1 
1873 C CE2 . PHE A 248 ? 0.3564 0.2563 0.3599 0.0359  0.0125  -0.0084 248 PHE A CE2 
1874 C CZ  . PHE A 248 ? 0.4129 0.2844 0.3927 0.0315  0.0162  -0.0110 248 PHE A CZ  
1875 N N   . GLU A 249 ? 0.2953 0.2505 0.3202 -0.0187 -0.0145 -0.0115 249 GLU A N   
1876 C CA  . GLU A 249 ? 0.3010 0.2514 0.3138 -0.0341 -0.0162 -0.0121 249 GLU A CA  
1877 C C   . GLU A 249 ? 0.3203 0.2888 0.3489 -0.0338 -0.0170 -0.0087 249 GLU A C   
1878 O O   . GLU A 249 ? 0.3303 0.2867 0.3489 -0.0413 -0.0153 -0.0092 249 GLU A O   
1879 C CB  . GLU A 249 ? 0.3168 0.2808 0.3239 -0.0491 -0.0222 -0.0113 249 GLU A CB  
1880 C CG  . GLU A 249 ? 0.3543 0.2949 0.3386 -0.0532 -0.0211 -0.0154 249 GLU A CG  
1881 C CD  . GLU A 249 ? 0.5376 0.4961 0.5171 -0.0690 -0.0283 -0.0138 249 GLU A CD  
1882 O OE1 . GLU A 249 ? 0.5488 0.5447 0.5508 -0.0673 -0.0335 -0.0082 249 GLU A OE1 
1883 O OE2 . GLU A 249 ? 0.5724 0.5072 0.5237 -0.0829 -0.0285 -0.0177 249 GLU A OE2 
1884 N N   . TYR A 250 ? 0.2606 0.2554 0.3110 -0.0249 -0.0189 -0.0051 250 TYR A N   
1885 C CA  . TYR A 250 ? 0.2911 0.3025 0.3550 -0.0227 -0.0187 -0.0017 250 TYR A CA  
1886 C C   . TYR A 250 ? 0.2878 0.2809 0.3493 -0.0160 -0.0141 -0.0035 250 TYR A C   
1887 O O   . TYR A 250 ? 0.2538 0.2461 0.3136 -0.0210 -0.0131 -0.0025 250 TYR A O   
1888 C CB  . TYR A 250 ? 0.2923 0.3274 0.3741 -0.0114 -0.0197 0.0022  250 TYR A CB  
1889 C CG  . TYR A 250 ? 0.3130 0.3593 0.4051 -0.0060 -0.0175 0.0051  250 TYR A CG  
1890 C CD1 . TYR A 250 ? 0.3619 0.4326 0.4605 -0.0118 -0.0187 0.0101  250 TYR A CD1 
1891 C CD2 . TYR A 250 ? 0.3454 0.3794 0.4396 0.0042  -0.0141 0.0035  250 TYR A CD2 
1892 C CE1 . TYR A 250 ? 0.4074 0.4878 0.5139 -0.0057 -0.0156 0.0130  250 TYR A CE1 
1893 C CE2 . TYR A 250 ? 0.3702 0.4112 0.4703 0.0086  -0.0117 0.0057  250 TYR A CE2 
1894 C CZ  . TYR A 250 ? 0.5707 0.6337 0.6767 0.0047  -0.0120 0.0102  250 TYR A CZ  
1895 O OH  . TYR A 250 ? 0.6612 0.7309 0.7718 0.0103  -0.0086 0.0126  250 TYR A OH  
1896 N N   . HIS A 251 ? 0.2621 0.2437 0.3241 -0.0049 -0.0116 -0.0050 251 HIS A N   
1897 C CA  . HIS A 251 ? 0.2896 0.2594 0.3506 0.0019  -0.0080 -0.0050 251 HIS A CA  
1898 C C   . HIS A 251 ? 0.3499 0.2944 0.3919 -0.0021 -0.0044 -0.0066 251 HIS A C   
1899 O O   . HIS A 251 ? 0.3182 0.2546 0.3573 0.0002  -0.0017 -0.0054 251 HIS A O   
1900 C CB  . HIS A 251 ? 0.2371 0.2075 0.3045 0.0130  -0.0069 -0.0045 251 HIS A CB  
1901 C CG  . HIS A 251 ? 0.2573 0.2438 0.3379 0.0173  -0.0088 -0.0029 251 HIS A CG  
1902 N ND1 . HIS A 251 ? 0.2473 0.2375 0.3327 0.0198  -0.0081 -0.0016 251 HIS A ND1 
1903 C CD2 . HIS A 251 ? 0.2262 0.2223 0.3122 0.0196  -0.0107 -0.0023 251 HIS A CD2 
1904 C CE1 . HIS A 251 ? 0.2971 0.2957 0.3883 0.0235  -0.0089 -0.0007 251 HIS A CE1 
1905 N NE2 . HIS A 251 ? 0.2408 0.2427 0.3325 0.0240  -0.0104 -0.0008 251 HIS A NE2 
1906 N N   . LEU A 252 ? 0.2785 0.2073 0.3040 -0.0078 -0.0038 -0.0090 252 LEU A N   
1907 C CA  . LEU A 252 ? 0.3396 0.2364 0.3397 -0.0117 0.0010  -0.0108 252 LEU A CA  
1908 C C   . LEU A 252 ? 0.3578 0.2510 0.3493 -0.0269 -0.0004 -0.0107 252 LEU A C   
1909 O O   . LEU A 252 ? 0.3774 0.2487 0.3544 -0.0269 0.0040  -0.0103 252 LEU A O   
1910 C CB  . LEU A 252 ? 0.3326 0.2099 0.3127 -0.0150 0.0026  -0.0140 252 LEU A CB  
1911 C CG  . LEU A 252 ? 0.4617 0.2967 0.4077 -0.0171 0.0095  -0.0162 252 LEU A CG  
1912 C CD1 . LEU A 252 ? 0.4132 0.2362 0.3580 0.0017  0.0169  -0.0130 252 LEU A CD1 
1913 C CD2 . LEU A 252 ? 0.5046 0.3183 0.4273 -0.0215 0.0112  -0.0199 252 LEU A CD2 
1914 N N   . GLN A 253 ? 0.3246 0.2411 0.3245 -0.0397 -0.0063 -0.0099 253 GLN A N   
1915 C CA  . GLN A 253 ? 0.3312 0.2523 0.3260 -0.0557 -0.0081 -0.0083 253 GLN A CA  
1916 C C   . GLN A 253 ? 0.3561 0.2876 0.3652 -0.0482 -0.0062 -0.0053 253 GLN A C   
1917 O O   . GLN A 253 ? 0.3559 0.2751 0.3535 -0.0565 -0.0043 -0.0046 253 GLN A O   
1918 C CB  . GLN A 253 ? 0.4001 0.3540 0.4054 -0.0686 -0.0149 -0.0057 253 GLN A CB  
1919 C CG  . GLN A 253 ? 0.5978 0.5810 0.6154 -0.0786 -0.0176 -0.0006 253 GLN A CG  
1920 C CD  . GLN A 253 ? 0.7407 0.7503 0.7853 -0.0620 -0.0164 0.0032  253 GLN A CD  
1921 O OE1 . GLN A 253 ? 0.4696 0.4940 0.5298 -0.0481 -0.0171 0.0040  253 GLN A OE1 
1922 N NE2 . GLN A 253 ? 0.6495 0.6609 0.6958 -0.0639 -0.0142 0.0053  253 GLN A NE2 
1923 N N   . LYS A 254 ? 0.2947 0.2460 0.3260 -0.0333 -0.0066 -0.0037 254 LYS A N   
1924 C CA  . LYS A 254 ? 0.3364 0.2969 0.3793 -0.0265 -0.0050 -0.0013 254 LYS A CA  
1925 C C   . LYS A 254 ? 0.3775 0.3112 0.4075 -0.0204 -0.0002 -0.0018 254 LYS A C   
1926 O O   . LYS A 254 ? 0.3272 0.2579 0.3547 -0.0229 0.0016  0.0001  254 LYS A O   
1927 C CB  . LYS A 254 ? 0.3593 0.3399 0.4220 -0.0135 -0.0061 -0.0001 254 LYS A CB  
1928 C CG  . LYS A 254 ? 0.4118 0.4034 0.4844 -0.0081 -0.0047 0.0022  254 LYS A CG  
1929 C CD  . LYS A 254 ? 0.4411 0.4477 0.5268 0.0023  -0.0054 0.0030  254 LYS A CD  
1930 C CE  . LYS A 254 ? 0.4804 0.4947 0.5715 0.0072  -0.0032 0.0050  254 LYS A CE  
1931 N NZ  . LYS A 254 ? 0.5983 0.6205 0.6954 0.0167  -0.0027 0.0055  254 LYS A NZ  
1932 N N   . VAL A 255 ? 0.3058 0.2216 0.3275 -0.0112 0.0025  -0.0031 255 VAL A N   
1933 C CA  . VAL A 255 ? 0.4491 0.3434 0.4591 -0.0026 0.0078  -0.0015 255 VAL A CA  
1934 C C   . VAL A 255 ? 0.4012 0.2632 0.3830 -0.0123 0.0117  -0.0024 255 VAL A C   
1935 O O   . VAL A 255 ? 0.4230 0.2699 0.3950 -0.0097 0.0156  -0.0001 255 VAL A O   
1936 C CB  . VAL A 255 ? 0.4722 0.3628 0.4834 0.0125  0.0104  -0.0004 255 VAL A CB  
1937 C CG1 . VAL A 255 ? 0.4092 0.2825 0.4049 0.0111  0.0124  -0.0033 255 VAL A CG1 
1938 C CG2 . VAL A 255 ? 0.4614 0.3390 0.4648 0.0242  0.0157  0.0039  255 VAL A CG2 
1939 N N   . LYS A 256 ? 0.3787 0.2275 0.3443 -0.0247 0.0109  -0.0057 256 LYS A N   
1940 C CA  . LYS A 256 ? 0.4256 0.2393 0.3590 -0.0381 0.0144  -0.0071 256 LYS A CA  
1941 C C   . LYS A 256 ? 0.4304 0.2551 0.3675 -0.0516 0.0121  -0.0049 256 LYS A C   
1942 O O   . LYS A 256 ? 0.4283 0.2250 0.3436 -0.0559 0.0167  -0.0038 256 LYS A O   
1943 C CB  . LYS A 256 ? 0.4711 0.2720 0.3858 -0.0531 0.0124  -0.0111 256 LYS A CB  
1944 C CG  . LYS A 256 ? 0.5365 0.3113 0.4342 -0.0410 0.0176  -0.0136 256 LYS A CG  
1945 C CD  . LYS A 256 ? 0.6493 0.4016 0.5186 -0.0594 0.0165  -0.0182 256 LYS A CD  
1946 C CE  . LYS A 256 ? 0.6173 0.3494 0.4727 -0.0469 0.0213  -0.0207 256 LYS A CE  
1947 N NZ  . LYS A 256 ? 0.6745 0.3955 0.5088 -0.0666 0.0177  -0.0252 256 LYS A NZ  
1948 N N   . HIS A 257 ? 0.3738 0.2387 0.3371 -0.0575 0.0059  -0.0034 257 HIS A N   
1949 C CA  . HIS A 257 ? 0.4109 0.2921 0.3804 -0.0684 0.0044  -0.0001 257 HIS A CA  
1950 C C   . HIS A 257 ? 0.3712 0.2466 0.3449 -0.0555 0.0085  0.0023  257 HIS A C   
1951 O O   . HIS A 257 ? 0.3668 0.2297 0.3278 -0.0639 0.0109  0.0043  257 HIS A O   
1952 C CB  . HIS A 257 ? 0.3851 0.3129 0.3829 -0.0713 -0.0013 0.0024  257 HIS A CB  
1953 C CG  . HIS A 257 ? 0.4131 0.3630 0.4187 -0.0814 -0.0020 0.0069  257 HIS A CG  
1954 N ND1 . HIS A 257 ? 0.4622 0.4166 0.4558 -0.1047 -0.0044 0.0090  257 HIS A ND1 
1955 C CD2 . HIS A 257 ? 0.3775 0.3460 0.3998 -0.0724 -0.0004 0.0101  257 HIS A CD2 
1956 C CE1 . HIS A 257 ? 0.4536 0.4321 0.4589 -0.1086 -0.0039 0.0140  257 HIS A CE1 
1957 N NE2 . HIS A 257 ? 0.3369 0.3228 0.3590 -0.0884 -0.0012 0.0145  257 HIS A NE2 
1958 N N   . ALA A 258 ? 0.3330 0.2180 0.3231 -0.0364 0.0091  0.0027  258 ALA A N   
1959 C CA  . ALA A 258 ? 0.3229 0.2061 0.3170 -0.0249 0.0120  0.0057  258 ALA A CA  
1960 C C   . ALA A 258 ? 0.4073 0.2522 0.3745 -0.0216 0.0182  0.0070  258 ALA A C   
1961 O O   . ALA A 258 ? 0.4197 0.2564 0.3802 -0.0221 0.0207  0.0100  258 ALA A O   
1962 C CB  . ALA A 258 ? 0.3119 0.2122 0.3251 -0.0084 0.0107  0.0062  258 ALA A CB  
1963 N N   . ILE A 259 ? 0.3760 0.1955 0.3256 -0.0166 0.0215  0.0053  259 ILE A N   
1964 C CA  . ILE A 259 ? 0.3949 0.1726 0.3136 -0.0106 0.0294  0.0072  259 ILE A CA  
1965 C C   . ILE A 259 ? 0.4118 0.1625 0.3039 -0.0303 0.0312  0.0062  259 ILE A C   
1966 O O   . ILE A 259 ? 0.4622 0.1882 0.3358 -0.0281 0.0364  0.0095  259 ILE A O   
1967 C CB  . ILE A 259 ? 0.4626 0.2181 0.3657 -0.0005 0.0338  0.0056  259 ILE A CB  
1968 C CG1 . ILE A 259 ? 0.4027 0.1862 0.3312 0.0191  0.0327  0.0085  259 ILE A CG1 
1969 C CG2 . ILE A 259 ? 0.5275 0.2314 0.3903 0.0058  0.0440  0.0075  259 ILE A CG2 
1970 C CD1 . ILE A 259 ? 0.4751 0.2464 0.3940 0.0289  0.0365  0.0074  259 ILE A CD1 
1971 N N   . ASP A 260 ? 0.4330 0.1888 0.3215 -0.0510 0.0266  0.0024  260 ASP A N   
1972 C CA  . ASP A 260 ? 0.4688 0.2023 0.3310 -0.0745 0.0273  0.0020  260 ASP A CA  
1973 C C   . ASP A 260 ? 0.4589 0.2103 0.3330 -0.0794 0.0264  0.0063  260 ASP A C   
1974 O O   . ASP A 260 ? 0.4888 0.2103 0.3361 -0.0902 0.0304  0.0079  260 ASP A O   
1975 C CB  . ASP A 260 ? 0.5147 0.2647 0.3779 -0.0972 0.0206  -0.0011 260 ASP A CB  
1976 C CG  . ASP A 260 ? 0.7043 0.4259 0.5444 -0.0981 0.0222  -0.0058 260 ASP A CG  
1977 O OD1 . ASP A 260 ? 0.7513 0.4343 0.5693 -0.0819 0.0301  -0.0065 260 ASP A OD1 
1978 O OD2 . ASP A 260 ? 0.6908 0.4301 0.5344 -0.1143 0.0160  -0.0080 260 ASP A OD2 
1979 N N   . GLN A 261 ? 0.4215 0.2189 0.3325 -0.0722 0.0217  0.0081  261 GLN A N   
1980 C CA  . GLN A 261 ? 0.4086 0.2246 0.3306 -0.0763 0.0213  0.0121  261 GLN A CA  
1981 C C   . GLN A 261 ? 0.4519 0.2430 0.3619 -0.0620 0.0272  0.0153  261 GLN A C   
1982 O O   . GLN A 261 ? 0.4584 0.2337 0.3524 -0.0712 0.0302  0.0181  261 GLN A O   
1983 C CB  . GLN A 261 ? 0.4123 0.2780 0.3719 -0.0694 0.0164  0.0132  261 GLN A CB  
1984 C CG  . GLN A 261 ? 0.3696 0.2649 0.3410 -0.0841 0.0109  0.0126  261 GLN A CG  
1985 C CD  . GLN A 261 ? 0.5008 0.4074 0.4661 -0.1065 0.0100  0.0163  261 GLN A CD  
1986 O OE1 . GLN A 261 ? 0.5253 0.4426 0.4968 -0.1058 0.0120  0.0199  261 GLN A OE1 
1987 N NE2 . GLN A 261 ? 0.6031 0.5076 0.5546 -0.1277 0.0069  0.0157  261 GLN A NE2 
1988 N N   . ILE A 262 ? 0.4041 0.1941 0.3219 -0.0399 0.0289  0.0159  262 ILE A N   
1989 C CA  . ILE A 262 ? 0.4145 0.1855 0.3218 -0.0247 0.0343  0.0207  262 ILE A CA  
1990 C C   . ILE A 262 ? 0.4648 0.1827 0.3308 -0.0265 0.0421  0.0217  262 ILE A C   
1991 O O   . ILE A 262 ? 0.4962 0.1923 0.3449 -0.0235 0.0470  0.0262  262 ILE A O   
1992 C CB  . ILE A 262 ? 0.4135 0.2024 0.3397 -0.0023 0.0335  0.0225  262 ILE A CB  
1993 C CG1 . ILE A 262 ? 0.4395 0.2715 0.3981 -0.0015 0.0273  0.0224  262 ILE A CG1 
1994 C CG2 . ILE A 262 ? 0.4922 0.2599 0.4032 0.0151  0.0398  0.0291  262 ILE A CG2 
1995 C CD1 . ILE A 262 ? 0.3668 0.2200 0.3444 0.0140  0.0247  0.0232  262 ILE A CD1 
1996 N N   . THR A 263 ? 0.5146 0.2074 0.3605 -0.0321 0.0439  0.0175  263 THR A N   
1997 C CA  . THR A 263 ? 0.5591 0.1934 0.3585 -0.0347 0.0526  0.0179  263 THR A CA  
1998 C C   . THR A 263 ? 0.5819 0.1975 0.3594 -0.0601 0.0527  0.0179  263 THR A C   
1999 O O   . THR A 263 ? 0.5976 0.1727 0.3418 -0.0591 0.0599  0.0205  263 THR A O   
2000 C CB  . THR A 263 ? 0.6068 0.2166 0.3864 -0.0372 0.0545  0.0128  263 THR A CB  
2001 O OG1 . THR A 263 ? 0.5779 0.2056 0.3771 -0.0128 0.0553  0.0140  263 THR A OG1 
2002 C CG2 . THR A 263 ? 0.6610 0.2209 0.3936 -0.0387 0.0627  0.0117  263 THR A CG2 
2003 N N   . ALA A 264 ? 0.5697 0.2205 0.3670 -0.0821 0.0447  0.0156  264 ALA A N   
2004 C CA  . ALA A 264 ? 0.5891 0.2300 0.3684 -0.1086 0.0441  0.0167  264 ALA A CA  
2005 C C   . ALA A 264 ? 0.5757 0.2225 0.3613 -0.1019 0.0467  0.0225  264 ALA A C   
2006 O O   . ALA A 264 ? 0.6284 0.2437 0.3842 -0.1163 0.0507  0.0249  264 ALA A O   
2007 C CB  . ALA A 264 ? 0.5788 0.2659 0.3822 -0.1311 0.0351  0.0151  264 ALA A CB  
2008 N N   . ILE A 265 ? 0.5199 0.2040 0.3408 -0.0813 0.0444  0.0249  265 ILE A N   
2009 C CA  . ILE A 265 ? 0.5471 0.2343 0.3714 -0.0728 0.0470  0.0305  265 ILE A CA  
2010 C C   . ILE A 265 ? 0.5740 0.2084 0.3619 -0.0596 0.0561  0.0343  265 ILE A C   
2011 O O   . ILE A 265 ? 0.6015 0.2107 0.3666 -0.0663 0.0606  0.0383  265 ILE A O   
2012 C CB  . ILE A 265 ? 0.5225 0.2551 0.3865 -0.0537 0.0428  0.0318  265 ILE A CB  
2013 C CG1 . ILE A 265 ? 0.5046 0.2854 0.4003 -0.0649 0.0359  0.0294  265 ILE A CG1 
2014 C CG2 . ILE A 265 ? 0.5095 0.2398 0.3719 -0.0430 0.0460  0.0379  265 ILE A CG2 
2015 C CD1 . ILE A 265 ? 0.5165 0.3351 0.4455 -0.0473 0.0321  0.0293  265 ILE A CD1 
2016 N N   . ALA A 266 ? 0.6254 0.2431 0.4068 -0.0393 0.0597  0.0341  266 ALA A N   
2017 C CA  . ALA A 266 ? 0.6556 0.2273 0.4030 -0.0216 0.0695  0.0388  266 ALA A CA  
2018 C C   . ALA A 266 ? 0.6430 0.1780 0.3513 -0.0381 0.0733  0.0347  266 ALA A C   
2019 O O   . ALA A 266 ? 0.7172 0.2263 0.4006 -0.0295 0.0798  0.0379  266 ALA A O   
2020 C CB  . ALA A 266 ? 0.6639 0.2384 0.4167 0.0020  0.0718  0.0385  266 ALA A CB  
2021 N N   . ASP A 267 ? 0.6515 0.1838 0.3518 -0.0616 0.0693  0.0278  267 ASP A N   
2022 C CA  . ASP A 267 ? 0.7036 0.2013 0.3636 -0.0796 0.0723  0.0236  267 ASP A CA  
2023 C C   . ASP A 267 ? 0.7375 0.2407 0.3933 -0.1052 0.0691  0.0249  267 ASP A C   
2024 O O   . ASP A 267 ? 0.7868 0.2607 0.4069 -0.1211 0.0715  0.0222  267 ASP A O   
2025 C CB  . ASP A 267 ? 0.7180 0.2117 0.3681 -0.0940 0.0690  0.0164  267 ASP A CB  
2026 C CG  . ASP A 267 ? 0.8810 0.3554 0.5191 -0.0703 0.0751  0.0146  267 ASP A CG  
2027 O OD1 . ASP A 267 ? 0.8803 0.3358 0.5057 -0.0458 0.0835  0.0188  267 ASP A OD1 
2028 O OD2 . ASP A 267 ? 0.7922 0.2729 0.4337 -0.0762 0.0718  0.0098  267 ASP A OD2 
2029 N N   . GLY A 268 ? 0.6863 0.2265 0.3755 -0.1102 0.0642  0.0292  268 GLY A N   
2030 C CA  . GLY A 268 ? 0.7347 0.2890 0.4248 -0.1343 0.0613  0.0315  268 GLY A CA  
2031 C C   . GLY A 268 ? 0.7978 0.3386 0.4794 -0.1241 0.0666  0.0377  268 GLY A C   
2032 O O   . GLY A 268 ? 0.7689 0.2845 0.4375 -0.0993 0.0730  0.0401  268 GLY A O   
2033 N N   . VAL A 269 ? 0.7501 0.3125 0.4405 -0.1435 0.0638  0.0410  269 VAL A N   
2034 C CA  . VAL A 269 ? 0.7672 0.3189 0.4492 -0.1371 0.0684  0.0471  269 VAL A CA  
2035 C C   . VAL A 269 ? 0.7208 0.2854 0.4259 -0.1098 0.0703  0.0529  269 VAL A C   
2036 O O   . VAL A 269 ? 0.6864 0.2934 0.4277 -0.1069 0.0654  0.0533  269 VAL A O   
2037 C CB  . VAL A 269 ? 0.8238 0.4033 0.5144 -0.1636 0.0649  0.0500  269 VAL A CB  
2038 C CG1 . VAL A 269 ? 0.8160 0.3857 0.4993 -0.1560 0.0698  0.0567  269 VAL A CG1 
2039 C CG2 . VAL A 269 ? 0.7846 0.3524 0.4495 -0.1910 0.0624  0.0451  269 VAL A CG2 
2040 N N   . LYS A 270 ? 0.7549 0.2919 0.4423 -0.0877 0.0764  0.0566  270 LYS A N   
2041 C CA  . LYS A 270 ? 0.7304 0.2821 0.4373 -0.0615 0.0775  0.0634  270 LYS A CA  
2042 C C   . LYS A 270 ? 0.6384 0.2141 0.3593 -0.0682 0.0762  0.0692  270 LYS A C   
2043 O O   . LYS A 270 ? 0.6696 0.2255 0.3687 -0.0773 0.0797  0.0720  270 LYS A O   
2044 C CB  . LYS A 270 ? 0.8109 0.3337 0.4963 -0.0351 0.0841  0.0666  270 LYS A CB  
2045 C CG  . LYS A 270 ? 0.7766 0.3204 0.4820 -0.0076 0.0843  0.0750  270 LYS A CG  
2046 C CD  . LYS A 270 ? 0.9387 0.4579 0.6212 0.0158  0.0914  0.0795  270 LYS A CD  
2047 C CE  . LYS A 270 ? 0.9527 0.5000 0.6570 0.0440  0.0905  0.0881  270 LYS A CE  
2048 N NZ  . LYS A 270 ? 1.1035 0.6315 0.7859 0.0666  0.0982  0.0936  270 LYS A NZ  
2049 N N   . PRO A 271 ? 0.6177 0.2488 0.3812 -0.0612 0.0693  0.0677  271 PRO A N   
2050 C CA  . PRO A 271 ? 0.6333 0.2944 0.4127 -0.0663 0.0675  0.0711  271 PRO A CA  
2051 C C   . PRO A 271 ? 0.6791 0.3232 0.4449 -0.0484 0.0719  0.0791  271 PRO A C   
2052 O O   . PRO A 271 ? 0.6644 0.2902 0.4209 -0.0264 0.0746  0.0828  271 PRO A O   
2053 C CB  . PRO A 271 ? 0.5711 0.2877 0.3939 -0.0596 0.0601  0.0668  271 PRO A CB  
2054 C CG  . PRO A 271 ? 0.5838 0.2973 0.4131 -0.0423 0.0584  0.0639  271 PRO A CG  
2055 C CD  . PRO A 271 ? 0.5425 0.2081 0.3380 -0.0497 0.0633  0.0627  271 PRO A CD  
2056 N N   . LYS A 272 ? 0.5999 0.2520 0.3640 -0.0581 0.0729  0.0830  272 LYS A N   
2057 C CA  . LYS A 272 ? 0.5946 0.2428 0.3523 -0.0427 0.0754  0.0909  272 LYS A CA  
2058 C C   . LYS A 272 ? 0.5470 0.2481 0.3411 -0.0365 0.0691  0.0896  272 LYS A C   
2059 O O   . LYS A 272 ? 0.5906 0.3189 0.4097 -0.0271 0.0638  0.0849  272 LYS A O   
2060 C CB  . LYS A 272 ? 0.6399 0.2521 0.3637 -0.0576 0.0820  0.0963  272 LYS A CB  
2061 C CG  . LYS A 272 ? 0.7558 0.3126 0.4403 -0.0614 0.0880  0.0957  272 LYS A CG  
2062 C CD  . LYS A 272 ? 0.8948 0.4272 0.5525 -0.0727 0.0919  0.0978  272 LYS A CD  
2063 N N   . GLN A 273 ? 0.5671 0.2818 0.3628 -0.0416 0.0699  0.0932  273 GLN A N   
2064 C CA  . GLN A 273 ? 0.5566 0.3163 0.3817 -0.0374 0.0649  0.0908  273 GLN A CA  
2065 C C   . GLN A 273 ? 0.5298 0.3188 0.3742 -0.0546 0.0634  0.0848  273 GLN A C   
2066 O O   . GLN A 273 ? 0.5284 0.3083 0.3622 -0.0739 0.0664  0.0852  273 GLN A O   
2067 C CB  . GLN A 273 ? 0.5963 0.3577 0.4130 -0.0336 0.0670  0.0977  273 GLN A CB  
2068 C CG  . GLN A 273 ? 0.6102 0.3483 0.4090 -0.0147 0.0683  0.1057  273 GLN A CG  
2069 C CD  . GLN A 273 ? 0.9338 0.6813 0.7282 -0.0094 0.0685  0.1124  273 GLN A CD  
2070 O OE1 . GLN A 273 ? 0.9173 0.6602 0.7016 -0.0220 0.0723  0.1146  273 GLN A OE1 
2071 N NE2 . GLN A 273 ? 0.9673 0.7305 0.7692 0.0082  0.0641  0.1163  273 GLN A NE2 
2072 N N   . VAL A 274 ? 0.4483 0.2731 0.3195 -0.0476 0.0590  0.0802  274 VAL A N   
2073 C CA  . VAL A 274 ? 0.4417 0.2983 0.3333 -0.0581 0.0581  0.0756  274 VAL A CA  
2074 C C   . VAL A 274 ? 0.4205 0.3067 0.3271 -0.0502 0.0577  0.0748  274 VAL A C   
2075 O O   . VAL A 274 ? 0.4394 0.3217 0.3414 -0.0385 0.0565  0.0766  274 VAL A O   
2076 C CB  . VAL A 274 ? 0.4463 0.3103 0.3523 -0.0562 0.0540  0.0693  274 VAL A CB  
2077 C CG1 . VAL A 274 ? 0.4338 0.2650 0.3206 -0.0655 0.0552  0.0695  274 VAL A CG1 
2078 C CG2 . VAL A 274 ? 0.3875 0.2574 0.3042 -0.0373 0.0496  0.0667  274 VAL A CG2 
2079 N N   . THR A 275 ? 0.3885 0.3044 0.3111 -0.0565 0.0591  0.0727  275 THR A N   
2080 C CA  . THR A 275 ? 0.3730 0.3121 0.3056 -0.0475 0.0603  0.0713  275 THR A CA  
2081 C C   . THR A 275 ? 0.3664 0.3099 0.3096 -0.0337 0.0552  0.0653  275 THR A C   
2082 O O   . THR A 275 ? 0.3446 0.2829 0.2939 -0.0321 0.0513  0.0621  275 THR A O   
2083 C CB  . THR A 275 ? 0.3683 0.3390 0.3142 -0.0543 0.0649  0.0722  275 THR A CB  
2084 O OG1 . THR A 275 ? 0.3588 0.3433 0.3201 -0.0556 0.0623  0.0686  275 THR A OG1 
2085 C CG2 . THR A 275 ? 0.3843 0.3564 0.3211 -0.0714 0.0696  0.0790  275 THR A CG2 
2086 N N   . LYS A 276 ? 0.3584 0.3108 0.3015 -0.0252 0.0558  0.0638  276 LYS A N   
2087 C CA  . LYS A 276 ? 0.4258 0.3815 0.3754 -0.0151 0.0512  0.0582  276 LYS A CA  
2088 C C   . LYS A 276 ? 0.3560 0.3266 0.3218 -0.0147 0.0513  0.0537  276 LYS A C   
2089 O O   . LYS A 276 ? 0.3135 0.2811 0.2856 -0.0102 0.0464  0.0497  276 LYS A O   
2090 C CB  . LYS A 276 ? 0.3699 0.3286 0.3107 -0.0093 0.0527  0.0571  276 LYS A CB  
2091 C CG  . LYS A 276 ? 0.4342 0.3924 0.3763 -0.0021 0.0478  0.0513  276 LYS A CG  
2092 C CD  . LYS A 276 ? 0.4972 0.4492 0.4224 0.0001  0.0464  0.0515  276 LYS A CD  
2093 C CE  . LYS A 276 ? 0.4250 0.3804 0.3404 0.0003  0.0545  0.0518  276 LYS A CE  
2094 N NZ  . LYS A 276 ? 0.4599 0.4063 0.3550 0.0001  0.0528  0.0530  276 LYS A NZ  
2095 N N   . ASN A 277 ? 0.3153 0.3046 0.2882 -0.0192 0.0570  0.0554  277 ASN A N   
2096 C CA  . ASN A 277 ? 0.3001 0.3072 0.2887 -0.0177 0.0572  0.0529  277 ASN A CA  
2097 C C   . ASN A 277 ? 0.3077 0.3078 0.3018 -0.0251 0.0521  0.0521  277 ASN A C   
2098 O O   . ASN A 277 ? 0.2873 0.2910 0.2910 -0.0207 0.0488  0.0480  277 ASN A O   
2099 C CB  . ASN A 277 ? 0.3011 0.3359 0.2972 -0.0208 0.0646  0.0576  277 ASN A CB  
2100 C CG  . ASN A 277 ? 0.3667 0.4097 0.3586 -0.0081 0.0713  0.0570  277 ASN A CG  
2101 O OD1 . ASN A 277 ? 0.4581 0.4880 0.4436 0.0022  0.0698  0.0515  277 ASN A OD1 
2102 N ND2 . ASN A 277 ? 0.3316 0.3956 0.3248 -0.0094 0.0792  0.0630  277 ASN A ND2 
2103 N N   . GLU A 278 ? 0.3104 0.2968 0.2951 -0.0364 0.0519  0.0558  278 GLU A N   
2104 C CA  . GLU A 278 ? 0.3289 0.3008 0.3118 -0.0435 0.0481  0.0546  278 GLU A CA  
2105 C C   . GLU A 278 ? 0.3134 0.2671 0.2942 -0.0323 0.0432  0.0508  278 GLU A C   
2106 O O   . GLU A 278 ? 0.3256 0.2774 0.3125 -0.0318 0.0399  0.0475  278 GLU A O   
2107 C CB  . GLU A 278 ? 0.3580 0.3094 0.3232 -0.0571 0.0501  0.0593  278 GLU A CB  
2108 C CG  . GLU A 278 ? 0.3863 0.3559 0.3533 -0.0743 0.0533  0.0635  278 GLU A CG  
2109 C CD  . GLU A 278 ? 0.3888 0.3324 0.3328 -0.0886 0.0559  0.0683  278 GLU A CD  
2110 O OE1 . GLU A 278 ? 0.4296 0.3487 0.3592 -0.1000 0.0545  0.0678  278 GLU A OE1 
2111 O OE2 . GLU A 278 ? 0.3867 0.3310 0.3241 -0.0882 0.0597  0.0724  278 GLU A OE2 
2112 N N   . LEU A 279 ? 0.3157 0.2584 0.2878 -0.0239 0.0425  0.0521  279 LEU A N   
2113 C CA  . LEU A 279 ? 0.3312 0.2623 0.3019 -0.0139 0.0378  0.0507  279 LEU A CA  
2114 C C   . LEU A 279 ? 0.3208 0.2667 0.3055 -0.0076 0.0344  0.0451  279 LEU A C   
2115 O O   . LEU A 279 ? 0.2982 0.2397 0.2870 -0.0034 0.0307  0.0431  279 LEU A O   
2116 C CB  . LEU A 279 ? 0.3274 0.2503 0.2864 -0.0073 0.0372  0.0550  279 LEU A CB  
2117 C CG  . LEU A 279 ? 0.3843 0.3011 0.3421 0.0030  0.0324  0.0565  279 LEU A CG  
2118 C CD1 . LEU A 279 ? 0.4024 0.2992 0.3538 0.0045  0.0334  0.0587  279 LEU A CD1 
2119 C CD2 . LEU A 279 ? 0.4127 0.3287 0.3602 0.0087  0.0310  0.0623  279 LEU A CD2 
2120 N N   . LYS A 280 ? 0.3160 0.2774 0.3057 -0.0059 0.0364  0.0429  280 LYS A N   
2121 C CA  . LYS A 280 ? 0.3195 0.2903 0.3187 -0.0004 0.0344  0.0377  280 LYS A CA  
2122 C C   . LYS A 280 ? 0.3509 0.3265 0.3614 -0.0035 0.0332  0.0360  280 LYS A C   
2123 O O   . LYS A 280 ? 0.3216 0.2946 0.3370 0.0005  0.0291  0.0328  280 LYS A O   
2124 C CB  . LYS A 280 ? 0.3416 0.3246 0.3409 0.0029  0.0395  0.0364  280 LYS A CB  
2125 C CG  . LYS A 280 ? 0.3252 0.3019 0.3101 0.0053  0.0413  0.0372  280 LYS A CG  
2126 C CD  . LYS A 280 ? 0.3553 0.3386 0.3367 0.0116  0.0473  0.0346  280 LYS A CD  
2127 C CE  . LYS A 280 ? 0.4241 0.4003 0.3880 0.0128  0.0509  0.0355  280 LYS A CE  
2128 N NZ  . LYS A 280 ? 0.4340 0.4103 0.3898 0.0212  0.0579  0.0325  280 LYS A NZ  
2129 N N   . GLU A 281 ? 0.2732 0.2572 0.2870 -0.0120 0.0363  0.0384  281 GLU A N   
2130 C CA  . GLU A 281 ? 0.3188 0.3101 0.3421 -0.0169 0.0346  0.0370  281 GLU A CA  
2131 C C   . GLU A 281 ? 0.3301 0.2999 0.3469 -0.0190 0.0308  0.0359  281 GLU A C   
2132 O O   . GLU A 281 ? 0.2957 0.2663 0.3190 -0.0175 0.0279  0.0328  281 GLU A O   
2133 C CB  . GLU A 281 ? 0.3519 0.3604 0.3788 -0.0286 0.0380  0.0411  281 GLU A CB  
2134 C CG  . GLU A 281 ? 0.3988 0.4342 0.4344 -0.0233 0.0431  0.0435  281 GLU A CG  
2135 C CD  . GLU A 281 ? 0.5712 0.6136 0.6146 -0.0094 0.0429  0.0396  281 GLU A CD  
2136 O OE1 . GLU A 281 ? 0.6566 0.6984 0.7066 -0.0087 0.0388  0.0367  281 GLU A OE1 
2137 O OE2 . GLU A 281 ? 0.7066 0.7520 0.7465 0.0006  0.0474  0.0394  281 GLU A OE2 
2138 N N   . TYR A 282 ? 0.3078 0.2571 0.3101 -0.0207 0.0318  0.0389  282 TYR A N   
2139 C CA  . TYR A 282 ? 0.3107 0.2363 0.3030 -0.0187 0.0302  0.0390  282 TYR A CA  
2140 C C   . TYR A 282 ? 0.3387 0.2669 0.3386 -0.0066 0.0263  0.0365  282 TYR A C   
2141 O O   . TYR A 282 ? 0.2913 0.2128 0.2924 -0.0051 0.0247  0.0344  282 TYR A O   
2142 C CB  . TYR A 282 ? 0.3097 0.2130 0.2836 -0.0180 0.0330  0.0442  282 TYR A CB  
2143 C CG  . TYR A 282 ? 0.3396 0.2285 0.2984 -0.0324 0.0371  0.0471  282 TYR A CG  
2144 C CD1 . TYR A 282 ? 0.4382 0.3429 0.4031 -0.0471 0.0377  0.0462  282 TYR A CD1 
2145 C CD2 . TYR A 282 ? 0.4467 0.3067 0.3833 -0.0317 0.0405  0.0520  282 TYR A CD2 
2146 C CE1 . TYR A 282 ? 0.4448 0.3373 0.3937 -0.0641 0.0409  0.0496  282 TYR A CE1 
2147 C CE2 . TYR A 282 ? 0.4755 0.3174 0.3937 -0.0471 0.0445  0.0548  282 TYR A CE2 
2148 C CZ  . TYR A 282 ? 0.4464 0.3047 0.3706 -0.0648 0.0443  0.0534  282 TYR A CZ  
2149 O OH  . TYR A 282 ? 0.4844 0.3254 0.3883 -0.0835 0.0478  0.0568  282 TYR A OH  
2150 N N   . TYR A 283 ? 0.2764 0.2137 0.2795 0.0008  0.0247  0.0369  283 TYR A N   
2151 C CA  . TYR A 283 ? 0.2865 0.2276 0.2950 0.0094  0.0204  0.0355  283 TYR A CA  
2152 C C   . TYR A 283 ? 0.3060 0.2588 0.3270 0.0089  0.0185  0.0301  283 TYR A C   
2153 O O   . TYR A 283 ? 0.3100 0.2623 0.3353 0.0128  0.0157  0.0287  283 TYR A O   
2154 C CB  . TYR A 283 ? 0.2605 0.2084 0.2660 0.0135  0.0184  0.0374  283 TYR A CB  
2155 C CG  . TYR A 283 ? 0.2862 0.2256 0.2804 0.0174  0.0188  0.0443  283 TYR A CG  
2156 C CD1 . TYR A 283 ? 0.3587 0.2842 0.3466 0.0226  0.0201  0.0488  283 TYR A CD1 
2157 C CD2 . TYR A 283 ? 0.3169 0.2607 0.3043 0.0172  0.0183  0.0469  283 TYR A CD2 
2158 C CE1 . TYR A 283 ? 0.3777 0.2952 0.3537 0.0292  0.0214  0.0568  283 TYR A CE1 
2159 C CE2 . TYR A 283 ? 0.3645 0.3028 0.3416 0.0217  0.0184  0.0544  283 TYR A CE2 
2160 C CZ  . TYR A 283 ? 0.3808 0.3067 0.3528 0.0285  0.0200  0.0598  283 TYR A CZ  
2161 O OH  . TYR A 283 ? 0.3696 0.2903 0.3301 0.0355  0.0209  0.0686  283 TYR A OH  
2162 N N   . PHE A 284 ? 0.2893 0.2537 0.3156 0.0053  0.0207  0.0279  284 PHE A N   
2163 C CA  . PHE A 284 ? 0.2548 0.2298 0.2915 0.0067  0.0197  0.0240  284 PHE A CA  
2164 C C   . PHE A 284 ? 0.3271 0.2999 0.3679 0.0020  0.0187  0.0233  284 PHE A C   
2165 O O   . PHE A 284 ? 0.2869 0.2624 0.3341 0.0048  0.0161  0.0205  284 PHE A O   
2166 C CB  . PHE A 284 ? 0.2636 0.2530 0.3040 0.0068  0.0238  0.0239  284 PHE A CB  
2167 C CG  . PHE A 284 ? 0.3241 0.3123 0.3588 0.0135  0.0248  0.0218  284 PHE A CG  
2168 C CD1 . PHE A 284 ? 0.3836 0.3657 0.4073 0.0136  0.0260  0.0233  284 PHE A CD1 
2169 C CD2 . PHE A 284 ? 0.3558 0.3457 0.3926 0.0189  0.0245  0.0185  284 PHE A CD2 
2170 C CE1 . PHE A 284 ? 0.5034 0.4802 0.5167 0.0176  0.0269  0.0209  284 PHE A CE1 
2171 C CE2 . PHE A 284 ? 0.4142 0.3959 0.4393 0.0234  0.0260  0.0161  284 PHE A CE2 
2172 C CZ  . PHE A 284 ? 0.4577 0.4323 0.4702 0.0220  0.0270  0.0170  284 PHE A CZ  
2173 N N   . ASN A 285 ? 0.2754 0.2405 0.3094 -0.0064 0.0206  0.0258  285 ASN A N   
2174 C CA  . ASN A 285 ? 0.3512 0.3104 0.3836 -0.0138 0.0197  0.0247  285 ASN A CA  
2175 C C   . ASN A 285 ? 0.3365 0.2769 0.3624 -0.0078 0.0181  0.0235  285 ASN A C   
2176 O O   . ASN A 285 ? 0.2915 0.2339 0.3225 -0.0069 0.0160  0.0207  285 ASN A O   
2177 C CB  . ASN A 285 ? 0.2860 0.2370 0.3069 -0.0273 0.0224  0.0277  285 ASN A CB  
2178 C CG  . ASN A 285 ? 0.4244 0.3717 0.4411 -0.0396 0.0211  0.0264  285 ASN A CG  
2179 O OD1 . ASN A 285 ? 0.3963 0.3638 0.4258 -0.0412 0.0187  0.0249  285 ASN A OD1 
2180 N ND2 . ASN A 285 ? 0.4079 0.3272 0.4036 -0.0488 0.0230  0.0273  285 ASN A ND2 
2181 N N   . ILE A 286 ? 0.3350 0.2583 0.3492 -0.0024 0.0197  0.0267  286 ILE A N   
2182 C CA  . ILE A 286 ? 0.3337 0.2414 0.3411 0.0059  0.0198  0.0274  286 ILE A CA  
2183 C C   . ILE A 286 ? 0.3014 0.2252 0.3220 0.0155  0.0160  0.0266  286 ILE A C   
2184 O O   . ILE A 286 ? 0.2908 0.2115 0.3125 0.0207  0.0153  0.0259  286 ILE A O   
2185 C CB  . ILE A 286 ? 0.3004 0.1853 0.2897 0.0115  0.0237  0.0330  286 ILE A CB  
2186 C CG1 . ILE A 286 ? 0.3171 0.2136 0.3100 0.0187  0.0226  0.0374  286 ILE A CG1 
2187 C CG2 . ILE A 286 ? 0.3582 0.2205 0.3288 -0.0007 0.0278  0.0336  286 ILE A CG2 
2188 C CD1 . ILE A 286 ? 0.3605 0.2387 0.3373 0.0290  0.0262  0.0448  286 ILE A CD1 
2189 N N   . GLY A 287 ? 0.2582 0.1979 0.2866 0.0170  0.0139  0.0267  287 GLY A N   
2190 C CA  . GLY A 287 ? 0.2720 0.2246 0.3091 0.0222  0.0100  0.0256  287 GLY A CA  
2191 C C   . GLY A 287 ? 0.2889 0.2480 0.3351 0.0201  0.0084  0.0207  287 GLY A C   
2192 O O   . GLY A 287 ? 0.3036 0.2662 0.3542 0.0240  0.0061  0.0201  287 GLY A O   
2193 N N   . ASN A 288 ? 0.2542 0.2176 0.3037 0.0143  0.0099  0.0181  288 ASN A N   
2194 C CA  . ASN A 288 ? 0.2626 0.2345 0.3207 0.0137  0.0085  0.0146  288 ASN A CA  
2195 C C   . ASN A 288 ? 0.2646 0.2288 0.3213 0.0116  0.0080  0.0137  288 ASN A C   
2196 O O   . ASN A 288 ? 0.2677 0.2351 0.3296 0.0145  0.0059  0.0117  288 ASN A O   
2197 C CB  . ASN A 288 ? 0.2985 0.2828 0.3613 0.0104  0.0106  0.0142  288 ASN A CB  
2198 C CG  . ASN A 288 ? 0.4042 0.3937 0.4670 0.0161  0.0114  0.0132  288 ASN A CG  
2199 O OD1 . ASN A 288 ? 0.4375 0.4270 0.5019 0.0200  0.0098  0.0109  288 ASN A OD1 
2200 N ND2 . ASN A 288 ? 0.4153 0.4054 0.4730 0.0160  0.0143  0.0148  288 ASN A ND2 
2201 N N   . TYR A 289 ? 0.2577 0.2082 0.3042 0.0063  0.0102  0.0151  289 TYR A N   
2202 C CA  . TYR A 289 ? 0.3118 0.2487 0.3509 0.0039  0.0105  0.0137  289 TYR A CA  
2203 C C   . TYR A 289 ? 0.3264 0.2532 0.3615 0.0148  0.0111  0.0151  289 TYR A C   
2204 O O   . TYR A 289 ? 0.3167 0.2403 0.3516 0.0168  0.0106  0.0132  289 TYR A O   
2205 C CB  . TYR A 289 ? 0.3264 0.2457 0.3496 -0.0068 0.0133  0.0145  289 TYR A CB  
2206 C CG  . TYR A 289 ? 0.3518 0.2866 0.3804 -0.0202 0.0116  0.0134  289 TYR A CG  
2207 C CD1 . TYR A 289 ? 0.3931 0.3424 0.4318 -0.0213 0.0085  0.0111  289 TYR A CD1 
2208 C CD2 . TYR A 289 ? 0.3399 0.2791 0.3647 -0.0313 0.0130  0.0159  289 TYR A CD2 
2209 C CE1 . TYR A 289 ? 0.4027 0.3723 0.4478 -0.0324 0.0066  0.0120  289 TYR A CE1 
2210 C CE2 . TYR A 289 ? 0.4053 0.3662 0.4371 -0.0435 0.0112  0.0168  289 TYR A CE2 
2211 C CZ  . TYR A 289 ? 0.5179 0.4952 0.5603 -0.0435 0.0079  0.0152  289 TYR A CZ  
2212 O OH  . TYR A 289 ? 0.4770 0.4815 0.5276 -0.0546 0.0058  0.0180  289 TYR A OH  
2213 N N   . TYR A 290 ? 0.2942 0.2192 0.3265 0.0224  0.0122  0.0193  290 TYR A N   
2214 C CA  . TYR A 290 ? 0.2971 0.2219 0.3289 0.0339  0.0126  0.0227  290 TYR A CA  
2215 C C   . TYR A 290 ? 0.3731 0.3185 0.4199 0.0355  0.0082  0.0211  290 TYR A C   
2216 O O   . TYR A 290 ? 0.2974 0.2447 0.3459 0.0412  0.0082  0.0220  290 TYR A O   
2217 C CB  . TYR A 290 ? 0.2990 0.2230 0.3254 0.0417  0.0143  0.0295  290 TYR A CB  
2218 C CG  . TYR A 290 ? 0.3175 0.2462 0.3438 0.0549  0.0155  0.0355  290 TYR A CG  
2219 C CD1 . TYR A 290 ? 0.3516 0.2591 0.3635 0.0633  0.0215  0.0378  290 TYR A CD1 
2220 C CD2 . TYR A 290 ? 0.3031 0.2574 0.3416 0.0583  0.0111  0.0393  290 TYR A CD2 
2221 C CE1 . TYR A 290 ? 0.3671 0.2819 0.3792 0.0779  0.0240  0.0447  290 TYR A CE1 
2222 C CE2 . TYR A 290 ? 0.3956 0.3611 0.4360 0.0699  0.0122  0.0466  290 TYR A CE2 
2223 C CZ  . TYR A 290 ? 0.4584 0.4057 0.4869 0.0812  0.0191  0.0497  290 TYR A CZ  
2224 O OH  . TYR A 290 ? 0.5123 0.4735 0.5429 0.0954  0.0216  0.0584  290 TYR A OH  
2225 N N   . ALA A 291 ? 0.2526 0.2114 0.3076 0.0307  0.0050  0.0189  291 ALA A N   
2226 C CA  . ALA A 291 ? 0.2957 0.2675 0.3597 0.0302  0.0014  0.0166  291 ALA A CA  
2227 C C   . ALA A 291 ? 0.2992 0.2695 0.3667 0.0287  0.0012  0.0129  291 ALA A C   
2228 O O   . ALA A 291 ? 0.2683 0.2442 0.3400 0.0311  -0.0006 0.0128  291 ALA A O   
2229 C CB  . ALA A 291 ? 0.2541 0.2318 0.3194 0.0260  0.0002  0.0144  291 ALA A CB  
2230 N N   . ILE A 292 ? 0.2423 0.2069 0.3077 0.0235  0.0027  0.0104  292 ILE A N   
2231 C CA  . ILE A 292 ? 0.3098 0.2741 0.3772 0.0209  0.0021  0.0075  292 ILE A CA  
2232 C C   . ILE A 292 ? 0.3840 0.3370 0.4446 0.0253  0.0036  0.0083  292 ILE A C   
2233 O O   . ILE A 292 ? 0.3133 0.2701 0.3776 0.0272  0.0023  0.0069  292 ILE A O   
2234 C CB  . ILE A 292 ? 0.3086 0.2726 0.3736 0.0119  0.0028  0.0063  292 ILE A CB  
2235 C CG1 . ILE A 292 ? 0.2853 0.2662 0.3594 0.0110  0.0022  0.0065  292 ILE A CG1 
2236 C CG2 . ILE A 292 ? 0.3275 0.2877 0.3893 0.0070  0.0019  0.0041  292 ILE A CG2 
2237 C CD1 . ILE A 292 ? 0.3541 0.3422 0.4278 0.0025  0.0034  0.0079  292 ILE A CD1 
2238 N N   . PHE A 293 ? 0.2856 0.2234 0.3345 0.0286  0.0072  0.0111  293 PHE A N   
2239 C CA  . PHE A 293 ? 0.3361 0.2605 0.3751 0.0365  0.0108  0.0130  293 PHE A CA  
2240 C C   . PHE A 293 ? 0.3147 0.2562 0.3641 0.0456  0.0094  0.0166  293 PHE A C   
2241 O O   . PHE A 293 ? 0.4034 0.3452 0.4529 0.0494  0.0103  0.0163  293 PHE A O   
2242 C CB  . PHE A 293 ? 0.3110 0.2139 0.3327 0.0411  0.0163  0.0168  293 PHE A CB  
2243 C CG  . PHE A 293 ? 0.3511 0.2428 0.3623 0.0554  0.0218  0.0217  293 PHE A CG  
2244 C CD1 . PHE A 293 ? 0.4031 0.2723 0.3981 0.0569  0.0263  0.0193  293 PHE A CD1 
2245 C CD2 . PHE A 293 ? 0.3788 0.2831 0.3946 0.0676  0.0231  0.0294  293 PHE A CD2 
2246 C CE1 . PHE A 293 ? 0.4498 0.3071 0.4326 0.0731  0.0333  0.0246  293 PHE A CE1 
2247 C CE2 . PHE A 293 ? 0.4860 0.3843 0.4927 0.0835  0.0293  0.0359  293 PHE A CE2 
2248 C CZ  . PHE A 293 ? 0.5080 0.3819 0.4980 0.0875  0.0351  0.0336  293 PHE A CZ  
2249 N N   . LYS A 294 ? 0.2898 0.2465 0.3468 0.0476  0.0071  0.0203  294 LYS A N   
2250 C CA  . LYS A 294 ? 0.3153 0.2917 0.3809 0.0530  0.0050  0.0251  294 LYS A CA  
2251 C C   . LYS A 294 ? 0.3859 0.3723 0.4602 0.0473  0.0012  0.0211  294 LYS A C   
2252 O O   . LYS A 294 ? 0.3471 0.3437 0.4253 0.0511  0.0010  0.0239  294 LYS A O   
2253 C CB  . LYS A 294 ? 0.3771 0.3671 0.4461 0.0519  0.0021  0.0294  294 LYS A CB  
2254 C CG  . LYS A 294 ? 0.4478 0.4615 0.5232 0.0557  -0.0004 0.0369  294 LYS A CG  
2255 C CD  . LYS A 294 ? 0.4215 0.4456 0.4963 0.0531  -0.0033 0.0413  294 LYS A CD  
2256 C CE  . LYS A 294 ? 0.4831 0.5364 0.5641 0.0540  -0.0070 0.0503  294 LYS A CE  
2257 N NZ  . LYS A 294 ? 0.5203 0.5861 0.5993 0.0476  -0.0116 0.0540  294 LYS A NZ  
2258 N N   . PHE A 295 ? 0.2498 0.2334 0.3262 0.0393  -0.0012 0.0154  295 PHE A N   
2259 C CA  . PHE A 295 ? 0.3383 0.3276 0.4200 0.0352  -0.0040 0.0119  295 PHE A CA  
2260 C C   . PHE A 295 ? 0.4133 0.3966 0.4938 0.0367  -0.0025 0.0098  295 PHE A C   
2261 O O   . PHE A 295 ? 0.3112 0.3006 0.3951 0.0369  -0.0038 0.0097  295 PHE A O   
2262 C CB  . PHE A 295 ? 0.2563 0.2436 0.3384 0.0299  -0.0051 0.0081  295 PHE A CB  
2263 C CG  . PHE A 295 ? 0.3311 0.3213 0.4147 0.0275  -0.0071 0.0058  295 PHE A CG  
2264 C CD1 . PHE A 295 ? 0.3214 0.3147 0.4019 0.0247  -0.0093 0.0070  295 PHE A CD1 
2265 C CD2 . PHE A 295 ? 0.4315 0.4203 0.5168 0.0274  -0.0067 0.0031  295 PHE A CD2 
2266 C CE1 . PHE A 295 ? 0.3364 0.3251 0.4124 0.0220  -0.0102 0.0048  295 PHE A CE1 
2267 C CE2 . PHE A 295 ? 0.3942 0.3821 0.4778 0.0273  -0.0074 0.0018  295 PHE A CE2 
2268 C CZ  . PHE A 295 ? 0.2906 0.2754 0.3679 0.0247  -0.0087 0.0023  295 PHE A CZ  
2269 N N   . ALA A 296 ? 0.2984 0.2682 0.3716 0.0360  0.0002  0.0080  296 ALA A N   
2270 C CA  . ALA A 296 ? 0.3596 0.3205 0.4272 0.0356  0.0016  0.0056  296 ALA A CA  
2271 C C   . ALA A 296 ? 0.4092 0.3680 0.4729 0.0444  0.0049  0.0089  296 ALA A C   
2272 O O   . ALA A 296 ? 0.4422 0.4002 0.5048 0.0449  0.0052  0.0073  296 ALA A O   
2273 C CB  . ALA A 296 ? 0.4188 0.3628 0.4743 0.0299  0.0037  0.0033  296 ALA A CB  
2274 N N   . LYS A 297 ? 0.4502 0.4090 0.5109 0.0526  0.0081  0.0143  297 LYS A N   
2275 C CA  . LYS A 297 ? 0.5342 0.4970 0.5926 0.0640  0.0123  0.0198  297 LYS A CA  
2276 C C   . LYS A 297 ? 0.4958 0.4784 0.5660 0.0622  0.0090  0.0205  297 LYS A C   
2277 O O   . LYS A 297 ? 0.3740 0.3538 0.4408 0.0661  0.0117  0.0203  297 LYS A O   
2278 C CB  . LYS A 297 ? 0.5546 0.5279 0.6146 0.0730  0.0143  0.0281  297 LYS A CB  
2279 C CG  . LYS A 297 ? 0.6867 0.6384 0.7294 0.0845  0.0222  0.0319  297 LYS A CG  
2280 C CD  . LYS A 297 ? 0.6906 0.6617 0.7377 0.0975  0.0246  0.0430  297 LYS A CD  
2281 C CE  . LYS A 297 ? 0.7677 0.7282 0.8072 0.0991  0.0259  0.0455  297 LYS A CE  
2282 N NZ  . LYS A 297 ? 0.8658 0.8508 0.9113 0.1112  0.0270  0.0576  297 LYS A NZ  
2283 N N   . ASP A 298 ? 0.3698 0.3698 0.4511 0.0556  0.0034  0.0212  298 ASP A N   
2284 C CA  . ASP A 298 ? 0.3129 0.3296 0.4021 0.0521  0.0003  0.0226  298 ASP A CA  
2285 C C   . ASP A 298 ? 0.2795 0.2869 0.3676 0.0464  -0.0013 0.0161  298 ASP A C   
2286 O O   . ASP A 298 ? 0.2638 0.2772 0.3537 0.0468  -0.0012 0.0170  298 ASP A O   
2287 C CB  . ASP A 298 ? 0.3242 0.3560 0.4190 0.0444  -0.0049 0.0249  298 ASP A CB  
2288 C CG  . ASP A 298 ? 0.6753 0.7248 0.7729 0.0497  -0.0043 0.0338  298 ASP A CG  
2289 O OD1 . ASP A 298 ? 0.6489 0.7190 0.7515 0.0537  -0.0035 0.0412  298 ASP A OD1 
2290 O OD2 . ASP A 298 ? 0.5633 0.6083 0.6581 0.0507  -0.0042 0.0344  298 ASP A OD2 
2291 N N   . GLN A 299 ? 0.2387 0.2343 0.3244 0.0415  -0.0027 0.0106  299 GLN A N   
2292 C CA  . GLN A 299 ? 0.2598 0.2514 0.3455 0.0372  -0.0045 0.0062  299 GLN A CA  
2293 C C   . GLN A 299 ? 0.2718 0.2548 0.3508 0.0401  -0.0016 0.0049  299 GLN A C   
2294 O O   . GLN A 299 ? 0.2071 0.1926 0.2868 0.0393  -0.0025 0.0041  299 GLN A O   
2295 C CB  . GLN A 299 ? 0.1909 0.1778 0.2765 0.0327  -0.0060 0.0027  299 GLN A CB  
2296 C CG  . GLN A 299 ? 0.2303 0.2197 0.3180 0.0301  -0.0082 0.0006  299 GLN A CG  
2297 C CD  . GLN A 299 ? 0.2240 0.2162 0.3126 0.0294  -0.0098 0.0014  299 GLN A CD  
2298 O OE1 . GLN A 299 ? 0.2407 0.2344 0.3286 0.0281  -0.0102 0.0031  299 GLN A OE1 
2299 N NE2 . GLN A 299 ? 0.2410 0.2320 0.3284 0.0296  -0.0105 0.0007  299 GLN A NE2 
2300 N N   . LEU A 300 ? 0.2146 0.1843 0.2839 0.0433  0.0023  0.0048  300 LEU A N   
2301 C CA  . LEU A 300 ? 0.2855 0.2404 0.3421 0.0456  0.0061  0.0031  300 LEU A CA  
2302 C C   . LEU A 300 ? 0.2922 0.2538 0.3492 0.0547  0.0098  0.0073  300 LEU A C   
2303 O O   . LEU A 300 ? 0.2738 0.2299 0.3244 0.0552  0.0113  0.0056  300 LEU A O   
2304 C CB  . LEU A 300 ? 0.3092 0.2418 0.3494 0.0463  0.0105  0.0021  300 LEU A CB  
2305 C CG  . LEU A 300 ? 0.2850 0.2114 0.3219 0.0339  0.0069  -0.0022 300 LEU A CG  
2306 C CD1 . LEU A 300 ? 0.3520 0.2552 0.3712 0.0325  0.0112  -0.0024 300 LEU A CD1 
2307 C CD2 . LEU A 300 ? 0.3118 0.2350 0.3429 0.0256  0.0044  -0.0061 300 LEU A CD2 
2308 N N   . ASN A 301 ? 0.2401 0.2158 0.3039 0.0619  0.0114  0.0137  301 ASN A N   
2309 C CA  A ASN A 301 ? 0.3129 0.3025 0.3795 0.0703  0.0149  0.0197  301 ASN A CA  
2310 C CA  B ASN A 301 ? 0.3142 0.3037 0.3808 0.0703  0.0149  0.0196  301 ASN A CA  
2311 C C   . ASN A 301 ? 0.2704 0.2737 0.3461 0.0629  0.0103  0.0185  301 ASN A C   
2312 O O   . ASN A 301 ? 0.2549 0.2607 0.3280 0.0668  0.0132  0.0200  301 ASN A O   
2313 C CB  A ASN A 301 ? 0.3219 0.3324 0.3967 0.0774  0.0161  0.0285  301 ASN A CB  
2314 C CB  B ASN A 301 ? 0.3184 0.3286 0.3930 0.0775  0.0162  0.0285  301 ASN A CB  
2315 C CG  A ASN A 301 ? 0.3775 0.4105 0.4576 0.0859  0.0197  0.0369  301 ASN A CG  
2316 C CG  B ASN A 301 ? 0.4040 0.3992 0.4667 0.0890  0.0229  0.0316  301 ASN A CG  
2317 O OD1 A ASN A 301 ? 0.4561 0.4806 0.5259 0.0987  0.0278  0.0397  301 ASN A OD1 
2318 O OD1 B ASN A 301 ? 0.4649 0.4340 0.5098 0.0954  0.0294  0.0291  301 ASN A OD1 
2319 N ND2 A ASN A 301 ? 0.3813 0.4426 0.4754 0.0785  0.0143  0.0416  301 ASN A ND2 
2320 N ND2 B ASN A 301 ? 0.3565 0.3649 0.4257 0.0911  0.0215  0.0370  301 ASN A ND2 
2321 N N   . MET A 302 ? 0.2242 0.2338 0.3078 0.0529  0.0038  0.0162  302 MET A N   
2322 C CA  . MET A 302 ? 0.2346 0.2510 0.3224 0.0459  0.0001  0.0151  302 MET A CA  
2323 C C   . MET A 302 ? 0.2377 0.2405 0.3190 0.0447  0.0002  0.0099  302 MET A C   
2324 O O   . MET A 302 ? 0.2378 0.2441 0.3184 0.0444  0.0005  0.0107  302 MET A O   
2325 C CB  . MET A 302 ? 0.1781 0.1964 0.2697 0.0374  -0.0051 0.0137  302 MET A CB  
2326 C CG  . MET A 302 ? 0.2095 0.2262 0.2999 0.0305  -0.0083 0.0120  302 MET A CG  
2327 S SD  . MET A 302 ? 0.2423 0.2445 0.3287 0.0307  -0.0091 0.0062  302 MET A SD  
2328 C CE  . MET A 302 ? 0.2015 0.1988 0.2886 0.0296  -0.0103 0.0040  302 MET A CE  
2329 N N   . LEU A 303 ? 0.2270 0.2160 0.3027 0.0429  -0.0002 0.0053  303 LEU A N   
2330 C CA  . LEU A 303 ? 0.1958 0.1758 0.2648 0.0395  -0.0012 0.0012  303 LEU A CA  
2331 C C   . LEU A 303 ? 0.2521 0.2221 0.3092 0.0444  0.0038  0.0011  303 LEU A C   
2332 O O   . LEU A 303 ? 0.2696 0.2376 0.3222 0.0423  0.0031  -0.0005 303 LEU A O   
2333 C CB  . LEU A 303 ? 0.2394 0.2122 0.3054 0.0340  -0.0034 -0.0023 303 LEU A CB  
2334 C CG  . LEU A 303 ? 0.2163 0.1986 0.2922 0.0309  -0.0073 -0.0020 303 LEU A CG  
2335 C CD1 . LEU A 303 ? 0.1957 0.1752 0.2701 0.0266  -0.0081 -0.0036 303 LEU A CD1 
2336 C CD2 . LEU A 303 ? 0.2043 0.1927 0.2831 0.0296  -0.0102 -0.0018 303 LEU A CD2 
2337 N N   . ASN A 304 ? 0.2572 0.2191 0.3068 0.0519  0.0096  0.0031  304 ASN A N   
2338 C CA  . ASN A 304 ? 0.2977 0.2476 0.3326 0.0598  0.0166  0.0039  304 ASN A CA  
2339 C C   . ASN A 304 ? 0.3001 0.2680 0.3432 0.0639  0.0176  0.0083  304 ASN A C   
2340 O O   . ASN A 304 ? 0.2926 0.2537 0.3264 0.0648  0.0199  0.0068  304 ASN A O   
2341 C CB  . ASN A 304 ? 0.3226 0.2615 0.3477 0.0709  0.0241  0.0074  304 ASN A CB  
2342 C CG  . ASN A 304 ? 0.4696 0.3944 0.4769 0.0832  0.0337  0.0096  304 ASN A CG  
2343 O OD1 . ASN A 304 ? 0.5658 0.5030 0.5765 0.0969  0.0398  0.0172  304 ASN A OD1 
2344 N ND2 . ASN A 304 ? 0.4249 0.3254 0.4121 0.0786  0.0353  0.0036  304 ASN A ND2 
2345 N N   . LYS A 305 ? 0.2457 0.2369 0.3047 0.0646  0.0156  0.0139  305 LYS A N   
2346 C CA  . LYS A 305 ? 0.2768 0.2877 0.3437 0.0648  0.0156  0.0188  305 LYS A CA  
2347 C C   . LYS A 305 ? 0.2624 0.2704 0.3295 0.0554  0.0105  0.0146  305 LYS A C   
2348 O O   . LYS A 305 ? 0.2826 0.2947 0.3473 0.0565  0.0125  0.0162  305 LYS A O   
2349 C CB  . LYS A 305 ? 0.3395 0.3755 0.4208 0.0624  0.0128  0.0254  305 LYS A CB  
2350 C CG  . LYS A 305 ? 0.4993 0.5588 0.5875 0.0610  0.0134  0.0323  305 LYS A CG  
2351 C CD  . LYS A 305 ? 0.6280 0.7140 0.7279 0.0552  0.0098  0.0396  305 LYS A CD  
2352 C CE  . LYS A 305 ? 0.7361 0.8483 0.8418 0.0509  0.0101  0.0474  305 LYS A CE  
2353 N NZ  . LYS A 305 ? 0.7976 0.9258 0.9088 0.0347  0.0030  0.0507  305 LYS A NZ  
2354 N N   . ALA A 306 ? 0.2307 0.2328 0.3004 0.0475  0.0046  0.0102  306 ALA A N   
2355 C CA  . ALA A 306 ? 0.2269 0.2264 0.2958 0.0412  0.0005  0.0076  306 ALA A CA  
2356 C C   . ALA A 306 ? 0.2655 0.2533 0.3228 0.0423  0.0021  0.0043  306 ALA A C   
2357 O O   . ALA A 306 ? 0.2884 0.2777 0.3433 0.0405  0.0012  0.0046  306 ALA A O   
2358 C CB  . ALA A 306 ? 0.2142 0.2106 0.2868 0.0361  -0.0045 0.0049  306 ALA A CB  
2359 N N   . LEU A 307 ? 0.2239 0.1977 0.2709 0.0440  0.0047  0.0011  307 LEU A N   
2360 C CA  . LEU A 307 ? 0.2980 0.2572 0.3291 0.0420  0.0059  -0.0026 307 LEU A CA  
2361 C C   . LEU A 307 ? 0.3627 0.3188 0.3846 0.0498  0.0128  -0.0004 307 LEU A C   
2362 O O   . LEU A 307 ? 0.3476 0.2989 0.3604 0.0476  0.0127  -0.0020 307 LEU A O   
2363 C CB  . LEU A 307 ? 0.3133 0.2540 0.3307 0.0388  0.0069  -0.0067 307 LEU A CB  
2364 C CG  . LEU A 307 ? 0.3361 0.2823 0.3604 0.0292  -0.0001 -0.0087 307 LEU A CG  
2365 C CD1 . LEU A 307 ? 0.3546 0.2837 0.3656 0.0243  0.0013  -0.0117 307 LEU A CD1 
2366 C CD2 . LEU A 307 ? 0.3552 0.3082 0.3786 0.0222  -0.0055 -0.0095 307 LEU A CD2 
2367 N N   . ILE A 308 ? 0.2977 0.2587 0.3220 0.0596  0.0190  0.0042  308 ILE A N   
2368 C CA  . ILE A 308 ? 0.2952 0.2589 0.3129 0.0695  0.0268  0.0083  308 ILE A CA  
2369 C C   . ILE A 308 ? 0.3026 0.2862 0.3318 0.0654  0.0236  0.0116  308 ILE A C   
2370 O O   . ILE A 308 ? 0.3584 0.3399 0.3788 0.0680  0.0272  0.0122  308 ILE A O   
2371 C CB  . ILE A 308 ? 0.3277 0.3005 0.3489 0.0824  0.0339  0.0151  308 ILE A CB  
2372 C CG1 . ILE A 308 ? 0.3514 0.2958 0.3532 0.0886  0.0396  0.0119  308 ILE A CG1 
2373 C CG2 . ILE A 308 ? 0.3794 0.3670 0.4002 0.0934  0.0418  0.0224  308 ILE A CG2 
2374 C CD1 . ILE A 308 ? 0.4625 0.4163 0.4697 0.1010  0.0450  0.0191  308 ILE A CD1 
2375 N N   . HIS A 309 ? 0.3029 0.3027 0.3486 0.0582  0.0171  0.0136  309 HIS A N   
2376 C CA  . HIS A 309 ? 0.2702 0.2832 0.3225 0.0523  0.0140  0.0166  309 HIS A CA  
2377 C C   . HIS A 309 ? 0.3180 0.3185 0.3613 0.0473  0.0108  0.0121  309 HIS A C   
2378 O O   . HIS A 309 ? 0.2655 0.2698 0.3053 0.0469  0.0122  0.0142  309 HIS A O   
2379 C CB  . HIS A 309 ? 0.2794 0.3035 0.3439 0.0443  0.0082  0.0187  309 HIS A CB  
2380 C CG  . HIS A 309 ? 0.3341 0.3661 0.4003 0.0367  0.0057  0.0220  309 HIS A CG  
2381 N ND1 . HIS A 309 ? 0.3509 0.4013 0.4203 0.0363  0.0090  0.0289  309 HIS A ND1 
2382 C CD2 . HIS A 309 ? 0.3489 0.3717 0.4118 0.0298  0.0010  0.0199  309 HIS A CD2 
2383 C CE1 . HIS A 309 ? 0.3984 0.4485 0.4654 0.0270  0.0059  0.0303  309 HIS A CE1 
2384 N NE2 . HIS A 309 ? 0.4135 0.4448 0.4754 0.0240  0.0014  0.0249  309 HIS A NE2 
2385 N N   . LYS A 310 ? 0.3106 0.2989 0.3502 0.0433  0.0064  0.0067  310 LYS A N   
2386 C CA  . LYS A 310 ? 0.3138 0.2952 0.3454 0.0387  0.0027  0.0039  310 LYS A CA  
2387 C C   . LYS A 310 ? 0.3490 0.3190 0.3635 0.0413  0.0074  0.0019  310 LYS A C   
2388 O O   . LYS A 310 ? 0.3364 0.3058 0.3446 0.0388  0.0059  0.0020  310 LYS A O   
2389 C CB  . LYS A 310 ? 0.3532 0.3301 0.3851 0.0337  -0.0028 0.0003  310 LYS A CB  
2390 C CG  . LYS A 310 ? 0.3349 0.3203 0.3798 0.0322  -0.0069 0.0022  310 LYS A CG  
2391 C CD  . LYS A 310 ? 0.4972 0.4863 0.5425 0.0311  -0.0097 0.0050  310 LYS A CD  
2392 C CE  . LYS A 310 ? 0.5051 0.4960 0.5574 0.0311  -0.0120 0.0069  310 LYS A CE  
2393 N NZ  . LYS A 310 ? 0.4392 0.4304 0.4933 0.0297  -0.0101 0.0097  310 LYS A NZ  
2394 N N   . GLU A 311 ? 0.3350 0.2927 0.3389 0.0467  0.0135  0.0001  311 GLU A N   
2395 C CA  . GLU A 311 ? 0.3708 0.3116 0.3528 0.0506  0.0200  -0.0020 311 GLU A CA  
2396 C C   . GLU A 311 ? 0.3787 0.3313 0.3629 0.0568  0.0249  0.0031  311 GLU A C   
2397 O O   . GLU A 311 ? 0.3410 0.2854 0.3108 0.0560  0.0267  0.0017  311 GLU A O   
2398 C CB  . GLU A 311 ? 0.4686 0.3908 0.4361 0.0589  0.0282  -0.0033 311 GLU A CB  
2399 C CG  . GLU A 311 ? 0.7200 0.6203 0.6726 0.0508  0.0255  -0.0095 311 GLU A CG  
2400 C CD  . GLU A 311 ? 0.7280 0.5982 0.6477 0.0470  0.0293  -0.0149 311 GLU A CD  
2401 O OE1 . GLU A 311 ? 0.7533 0.6238 0.6653 0.0461  0.0297  -0.0151 311 GLU A OE1 
2402 O OE2 . GLU A 311 ? 0.8206 0.6646 0.7196 0.0438  0.0318  -0.0191 311 GLU A OE2 
2403 N N   . LYS A 312 ? 0.2824 0.2553 0.2831 0.0624  0.0275  0.0096  312 LYS A N   
2404 C CA  . LYS A 312 ? 0.3725 0.3627 0.3778 0.0660  0.0316  0.0160  312 LYS A CA  
2405 C C   . LYS A 312 ? 0.3328 0.3254 0.3389 0.0565  0.0254  0.0154  312 LYS A C   
2406 O O   . LYS A 312 ? 0.2923 0.2837 0.2887 0.0582  0.0290  0.0166  312 LYS A O   
2407 C CB  . LYS A 312 ? 0.3984 0.4151 0.4231 0.0678  0.0323  0.0239  312 LYS A CB  
2408 C CG  . LYS A 312 ? 0.3810 0.4212 0.4125 0.0673  0.0351  0.0318  312 LYS A CG  
2409 C CD  . LYS A 312 ? 0.4321 0.4987 0.4823 0.0606  0.0313  0.0388  312 LYS A CD  
2410 C CE  . LYS A 312 ? 0.5754 0.6679 0.6315 0.0570  0.0338  0.0477  312 LYS A CE  
2411 N NZ  . LYS A 312 ? 0.5852 0.7041 0.6562 0.0473  0.0297  0.0550  312 LYS A NZ  
2412 N N   . ILE A 313 ? 0.2838 0.2789 0.2998 0.0478  0.0169  0.0141  313 ILE A N   
2413 C CA  . ILE A 313 ? 0.3060 0.3020 0.3215 0.0411  0.0117  0.0149  313 ILE A CA  
2414 C C   . ILE A 313 ? 0.3014 0.2839 0.3009 0.0400  0.0106  0.0107  313 ILE A C   
2415 O O   . ILE A 313 ? 0.2949 0.2782 0.2880 0.0386  0.0108  0.0127  313 ILE A O   
2416 C CB  . ILE A 313 ? 0.3343 0.3314 0.3596 0.0353  0.0046  0.0147  313 ILE A CB  
2417 C CG1 . ILE A 313 ? 0.3370 0.3460 0.3738 0.0333  0.0053  0.0191  313 ILE A CG1 
2418 C CG2 . ILE A 313 ? 0.3137 0.3074 0.3346 0.0313  0.0003  0.0161  313 ILE A CG2 
2419 C CD1 . ILE A 313 ? 0.4722 0.4771 0.5141 0.0285  -0.0002 0.0183  313 ILE A CD1 
2420 N N   . VAL A 314 ? 0.2912 0.2613 0.2826 0.0388  0.0090  0.0053  314 VAL A N   
2421 C CA  . VAL A 314 ? 0.2925 0.2505 0.2660 0.0343  0.0068  0.0013  314 VAL A CA  
2422 C C   . VAL A 314 ? 0.3072 0.2558 0.2632 0.0390  0.0145  0.0011  314 VAL A C   
2423 O O   . VAL A 314 ? 0.3102 0.2566 0.2555 0.0357  0.0130  0.0011  314 VAL A O   
2424 C CB  . VAL A 314 ? 0.3503 0.2960 0.3154 0.0295  0.0043  -0.0042 314 VAL A CB  
2425 C CG1 . VAL A 314 ? 0.4669 0.3969 0.4069 0.0227  0.0035  -0.0085 314 VAL A CG1 
2426 C CG2 . VAL A 314 ? 0.4372 0.3950 0.4176 0.0244  -0.0039 -0.0033 314 VAL A CG2 
2427 N N   . HIS A 315 ? 0.2964 0.2391 0.2476 0.0480  0.0236  0.0014  315 HIS A N   
2428 C CA  . HIS A 315 ? 0.3093 0.2416 0.2413 0.0553  0.0330  0.0017  315 HIS A CA  
2429 C C   . HIS A 315 ? 0.3084 0.2594 0.2492 0.0568  0.0345  0.0081  315 HIS A C   
2430 O O   . HIS A 315 ? 0.3185 0.2622 0.2429 0.0577  0.0380  0.0077  315 HIS A O   
2431 C CB  . HIS A 315 ? 0.3422 0.2662 0.2674 0.0683  0.0440  0.0028  315 HIS A CB  
2432 C CG  . HIS A 315 ? 0.3685 0.2623 0.2716 0.0666  0.0454  -0.0043 315 HIS A CG  
2433 N ND1 . HIS A 315 ? 0.4283 0.2932 0.2997 0.0610  0.0467  -0.0107 315 HIS A ND1 
2434 C CD2 . HIS A 315 ? 0.4160 0.3023 0.3215 0.0675  0.0452  -0.0060 315 HIS A CD2 
2435 C CE1 . HIS A 315 ? 0.5457 0.3852 0.3996 0.0575  0.0474  -0.0161 315 HIS A CE1 
2436 N NE2 . HIS A 315 ? 0.4503 0.3023 0.3250 0.0622  0.0468  -0.0132 315 HIS A NE2 
2437 N N   . ASN A 316 ? 0.3271 0.3007 0.2910 0.0558  0.0319  0.0140  316 ASN A N   
2438 C CA  . ASN A 316 ? 0.2921 0.2815 0.2615 0.0543  0.0330  0.0203  316 ASN A CA  
2439 C C   . ASN A 316 ? 0.3002 0.2834 0.2632 0.0458  0.0257  0.0186  316 ASN A C   
2440 O O   . ASN A 316 ? 0.3104 0.2956 0.2655 0.0456  0.0284  0.0215  316 ASN A O   
2441 C CB  . ASN A 316 ? 0.2860 0.2981 0.2771 0.0516  0.0315  0.0269  316 ASN A CB  
2442 C CG  . ASN A 316 ? 0.3425 0.3702 0.3400 0.0615  0.0402  0.0322  316 ASN A CG  
2443 O OD1 . ASN A 316 ? 0.4093 0.4328 0.3945 0.0726  0.0496  0.0330  316 ASN A OD1 
2444 N ND2 . ASN A 316 ? 0.3337 0.3795 0.3487 0.0582  0.0376  0.0367  316 ASN A ND2 
2445 N N   . LEU A 317 ? 0.2699 0.2477 0.2364 0.0397  0.0170  0.0152  317 LEU A N   
2446 C CA  . LEU A 317 ? 0.2801 0.2547 0.2401 0.0340  0.0102  0.0151  317 LEU A CA  
2447 C C   . LEU A 317 ? 0.3374 0.2993 0.2754 0.0331  0.0115  0.0111  317 LEU A C   
2448 O O   . LEU A 317 ? 0.3035 0.2656 0.2327 0.0307  0.0098  0.0132  317 LEU A O   
2449 C CB  . LEU A 317 ? 0.2725 0.2482 0.2414 0.0302  0.0018  0.0138  317 LEU A CB  
2450 C CG  . LEU A 317 ? 0.3357 0.3188 0.3197 0.0297  -0.0003 0.0184  317 LEU A CG  
2451 C CD1 . LEU A 317 ? 0.3137 0.2973 0.3054 0.0289  -0.0065 0.0171  317 LEU A CD1 
2452 C CD2 . LEU A 317 ? 0.4099 0.3933 0.3890 0.0281  -0.0009 0.0239  317 LEU A CD2 
2453 N N   . LEU A 318 ? 0.3080 0.2558 0.2334 0.0344  0.0149  0.0055  318 LEU A N   
2454 C CA  . LEU A 318 ? 0.3471 0.2770 0.2451 0.0319  0.0172  0.0010  318 LEU A CA  
2455 C C   . LEU A 318 ? 0.3494 0.2768 0.2363 0.0396  0.0272  0.0036  318 LEU A C   
2456 O O   . LEU A 318 ? 0.3683 0.2872 0.2359 0.0367  0.0277  0.0025  318 LEU A O   
2457 C CB  . LEU A 318 ? 0.3572 0.2664 0.2395 0.0304  0.0195  -0.0058 318 LEU A CB  
2458 C CG  . LEU A 318 ? 0.4055 0.3175 0.2936 0.0198  0.0090  -0.0085 318 LEU A CG  
2459 C CD1 . LEU A 318 ? 0.5096 0.4009 0.3846 0.0189  0.0128  -0.0142 318 LEU A CD1 
2460 C CD2 . LEU A 318 ? 0.4696 0.3822 0.3436 0.0079  0.0006  -0.0095 318 LEU A CD2 
2461 N N   . GLY A 319 ? 0.3407 0.2788 0.2401 0.0492  0.0352  0.0081  319 GLY A N   
2462 C CA  . GLY A 319 ? 0.3502 0.2949 0.2441 0.0563  0.0444  0.0132  319 GLY A CA  
2463 C C   . GLY A 319 ? 0.3646 0.3201 0.2622 0.0495  0.0391  0.0174  319 GLY A C   
2464 O O   . GLY A 319 ? 0.3998 0.3502 0.2808 0.0507  0.0435  0.0182  319 GLY A O   
2465 N N   . GLU A 320 ? 0.3841 0.3522 0.3009 0.0428  0.0304  0.0204  320 GLU A N   
2466 C CA  . GLU A 320 ? 0.4039 0.3777 0.3211 0.0372  0.0258  0.0250  320 GLU A CA  
2467 C C   . GLU A 320 ? 0.4129 0.3746 0.3119 0.0327  0.0202  0.0214  320 GLU A C   
2468 O O   . GLU A 320 ? 0.4144 0.3753 0.3016 0.0316  0.0213  0.0241  320 GLU A O   
2469 C CB  . GLU A 320 ? 0.4141 0.3963 0.3498 0.0324  0.0187  0.0285  320 GLU A CB  
2470 C CG  . GLU A 320 ? 0.4737 0.4695 0.4261 0.0330  0.0225  0.0327  320 GLU A CG  
2471 C CD  . GLU A 320 ? 0.6144 0.6115 0.5783 0.0268  0.0160  0.0353  320 GLU A CD  
2472 O OE1 . GLU A 320 ? 0.5832 0.5720 0.5415 0.0240  0.0106  0.0364  320 GLU A OE1 
2473 O OE2 . GLU A 320 ? 0.7653 0.7706 0.7417 0.0254  0.0167  0.0367  320 GLU A OE2 
2474 N N   . LEU A 321 ? 0.3617 0.3166 0.2582 0.0290  0.0136  0.0162  321 LEU A N   
2475 C CA  . LEU A 321 ? 0.3637 0.3119 0.2430 0.0222  0.0069  0.0137  321 LEU A CA  
2476 C C   . LEU A 321 ? 0.4729 0.4060 0.3250 0.0225  0.0136  0.0104  321 LEU A C   
2477 O O   . LEU A 321 ? 0.4364 0.3695 0.2757 0.0190  0.0112  0.0125  321 LEU A O   
2478 C CB  . LEU A 321 ? 0.3953 0.3405 0.2751 0.0165  0.0002  0.0087  321 LEU A CB  
2479 C CG  . LEU A 321 ? 0.5058 0.4514 0.3704 0.0063  -0.0088 0.0074  321 LEU A CG  
2480 C CD1 . LEU A 321 ? 0.4298 0.3954 0.3082 0.0065  -0.0172 0.0154  321 LEU A CD1 
2481 C CD2 . LEU A 321 ? 0.4436 0.3833 0.3032 -0.0017 -0.0129 0.0016  321 LEU A CD2 
2482 N N   . PHE A 322 ? 0.4111 0.3295 0.2518 0.0277  0.0228  0.0057  322 PHE A N   
2483 C CA  . PHE A 322 ? 0.4257 0.3244 0.2354 0.0295  0.0308  0.0022  322 PHE A CA  
2484 C C   . PHE A 322 ? 0.4365 0.3446 0.2469 0.0367  0.0385  0.0085  322 PHE A C   
2485 O O   . PHE A 322 ? 0.5338 0.4313 0.3204 0.0351  0.0412  0.0076  322 PHE A O   
2486 C CB  . PHE A 322 ? 0.4773 0.3530 0.2703 0.0358  0.0403  -0.0037 322 PHE A CB  
2487 C CG  . PHE A 322 ? 0.5110 0.3680 0.2882 0.0245  0.0335  -0.0113 322 PHE A CG  
2488 C CD1 . PHE A 322 ? 0.7030 0.5418 0.4489 0.0121  0.0291  -0.0163 322 PHE A CD1 
2489 C CD2 . PHE A 322 ? 0.5888 0.4472 0.3808 0.0244  0.0311  -0.0130 322 PHE A CD2 
2490 C CE1 . PHE A 322 ? 0.8004 0.6242 0.5301 -0.0019 0.0221  -0.0226 322 PHE A CE1 
2491 C CE2 . PHE A 322 ? 0.6885 0.5310 0.4651 0.0119  0.0247  -0.0193 322 PHE A CE2 
2492 C CZ  . PHE A 322 ? 0.7416 0.5674 0.4871 -0.0020 0.0201  -0.0239 322 PHE A CZ  
2493 N N   . GLY A 323 ? 0.4492 0.3779 0.2851 0.0425  0.0416  0.0153  323 GLY A N   
2494 C CA  . GLY A 323 ? 0.5072 0.4483 0.3445 0.0466  0.0484  0.0224  323 GLY A CA  
2495 C C   . GLY A 323 ? 0.6375 0.5829 0.4723 0.0384  0.0405  0.0259  323 GLY A C   
2496 O O   . GLY A 323 ? 0.6350 0.5787 0.4548 0.0393  0.0453  0.0284  323 GLY A O   
2497 N N   . HIS A 324 ? 0.6032 0.5538 0.4511 0.0316  0.0289  0.0267  324 HIS A N   
2498 C CA  . HIS A 324 ? 0.6638 0.6168 0.5068 0.0260  0.0213  0.0308  324 HIS A CA  
2499 C C   . HIS A 324 ? 0.6474 0.5881 0.4641 0.0218  0.0186  0.0264  324 HIS A C   
2500 O O   . HIS A 324 ? 0.6733 0.6139 0.4770 0.0200  0.0182  0.0300  324 HIS A O   
2501 C CB  . HIS A 324 ? 0.5583 0.5183 0.4181 0.0229  0.0110  0.0331  324 HIS A CB  
2502 C CG  . HIS A 324 ? 0.5805 0.5485 0.4609 0.0245  0.0126  0.0377  324 HIS A CG  
2503 N ND1 . HIS A 324 ? 0.6765 0.6470 0.5714 0.0239  0.0061  0.0386  324 HIS A ND1 
2504 C CD2 . HIS A 324 ? 0.7614 0.7359 0.6486 0.0254  0.0200  0.0420  324 HIS A CD2 
2505 C CE1 . HIS A 324 ? 0.7046 0.6787 0.6118 0.0235  0.0093  0.0423  324 HIS A CE1 
2506 N NE2 . HIS A 324 ? 0.7003 0.6788 0.6039 0.0233  0.0172  0.0447  324 HIS A NE2 
2507 N N   . LEU A 325 ? 0.5410 0.4705 0.3474 0.0184  0.0162  0.0188  325 LEU A N   
2508 C CA  . LEU A 325 ? 0.6192 0.5352 0.3964 0.0106  0.0128  0.0141  325 LEU A CA  
2509 C C   . LEU A 325 ? 0.8039 0.7045 0.5553 0.0148  0.0241  0.0125  325 LEU A C   
2510 O O   . LEU A 325 ? 0.7364 0.6326 0.4671 0.0096  0.0217  0.0132  325 LEU A O   
2511 C CB  . LEU A 325 ? 0.5634 0.4669 0.3314 0.0041  0.0094  0.0062  325 LEU A CB  
2512 C CG  . LEU A 325 ? 0.6427 0.5273 0.3749 -0.0078 0.0062  -0.0001 325 LEU A CG  
2513 C CD1 . LEU A 325 ? 0.8485 0.7481 0.5757 -0.0156 -0.0039 0.0055  325 LEU A CD1 
2514 C CD2 . LEU A 325 ? 0.6975 0.5741 0.4244 -0.0180 0.0001  -0.0062 325 LEU A CD2 
2515 N N   . GLU A 326 ? 0.6289 0.5229 0.3809 0.0253  0.0369  0.0112  326 GLU A N   
2516 C CA  . GLU A 326 ? 0.6834 0.5659 0.4126 0.0327  0.0497  0.0114  326 GLU A CA  
2517 C C   . GLU A 326 ? 0.7287 0.6280 0.4641 0.0326  0.0496  0.0198  326 GLU A C   
2518 O O   . GLU A 326 ? 0.8086 0.6977 0.5185 0.0318  0.0534  0.0195  326 GLU A O   
2519 C CB  . GLU A 326 ? 0.6621 0.5439 0.3977 0.0470  0.0638  0.0120  326 GLU A CB  
2520 C CG  . GLU A 326 ? 0.8608 0.7268 0.5680 0.0579  0.0795  0.0115  326 GLU A CG  
2521 C CD  . GLU A 326 ? 0.8136 0.6902 0.5334 0.0749  0.0938  0.0163  326 GLU A CD  
2522 O OE1 . GLU A 326 ? 0.8666 0.7614 0.6163 0.0764  0.0905  0.0192  326 GLU A OE1 
2523 O OE2 . GLU A 326 ? 1.0078 0.8758 0.7067 0.0875  0.1086  0.0180  326 GLU A OE2 
2524 N N   . GLU A 327 ? 0.7251 0.6471 0.4909 0.0325  0.0453  0.0273  327 GLU A N   
2525 C CA  . GLU A 327 ? 0.8219 0.7567 0.5920 0.0312  0.0454  0.0359  327 GLU A CA  
2526 C C   . GLU A 327 ? 0.8580 0.7878 0.6122 0.0232  0.0356  0.0365  327 GLU A C   
2527 O O   . GLU A 327 ? 0.9178 0.8468 0.6573 0.0228  0.0388  0.0404  327 GLU A O   
2528 C CB  . GLU A 327 ? 0.7224 0.6754 0.5226 0.0302  0.0422  0.0429  327 GLU A CB  
2529 C CG  . GLU A 327 ? 0.8661 0.8321 0.6830 0.0365  0.0520  0.0456  327 GLU A CG  
2530 C CD  . GLU A 327 ? 1.0432 1.0210 0.8867 0.0328  0.0462  0.0488  327 GLU A CD  
2531 O OE1 . GLU A 327 ? 0.9539 0.9292 0.8016 0.0267  0.0367  0.0508  327 GLU A OE1 
2532 O OE2 . GLU A 327 ? 1.2239 1.2129 1.0822 0.0367  0.0515  0.0497  327 GLU A OE2 
2533 N N   . ARG A 328 ? 0.8813 0.8111 0.6391 0.0171  0.0236  0.0340  328 ARG A N   
2534 C CA  . ARG A 328 ? 0.8838 0.8141 0.6268 0.0099  0.0136  0.0358  328 ARG A CA  
2535 C C   . ARG A 328 ? 0.9677 0.8805 0.6768 0.0040  0.0147  0.0285  328 ARG A C   
2536 O O   . ARG A 328 ? 1.0736 0.9881 0.7668 -0.0038 0.0063  0.0301  328 ARG A O   
2537 C CB  . ARG A 328 ? 0.8794 0.8215 0.6389 0.0061  0.0008  0.0377  328 ARG A CB  
2538 C CG  . ARG A 328 ? 0.9361 0.8897 0.7230 0.0118  -0.0003 0.0449  328 ARG A CG  
2539 C CD  . ARG A 328 ? 0.8565 0.8215 0.6564 0.0108  -0.0116 0.0478  328 ARG A CD  
2540 N NE  . ARG A 328 ? 0.9252 0.8901 0.7264 0.0060  -0.0153 0.0400  328 ARG A NE  
2541 C CZ  . ARG A 328 ? 0.8462 0.8103 0.6644 0.0084  -0.0132 0.0362  328 ARG A CZ  
2542 N NH1 . ARG A 328 ? 0.7668 0.7321 0.6030 0.0148  -0.0082 0.0393  328 ARG A NH1 
2543 N NH2 . ARG A 328 ? 0.6586 0.6200 0.4737 0.0028  -0.0163 0.0292  328 ARG A NH2 
2544 N N   . ILE A 329 ? 1.0657 0.9605 0.7609 0.0077  0.0253  0.0210  329 ILE A N   
2545 C CA  . ILE A 329 ? 1.0628 0.9318 0.7185 0.0029  0.0294  0.0131  329 ILE A CA  
2546 C C   . ILE A 329 ? 1.0473 0.9106 0.6893 -0.0120 0.0165  0.0077  329 ILE A C   
2547 O O   . ILE A 329 ? 1.0966 0.9450 0.7321 -0.0151 0.0173  0.0004  329 ILE A O   
2548 C CB  . ILE A 329 ? 1.0528 0.9180 0.6858 0.0030  0.0336  0.0165  329 ILE A CB  
2549 C CG1 . ILE A 329 ? 1.0356 0.9146 0.6871 0.0151  0.0443  0.0244  329 ILE A CG1 
2550 C CG2 . ILE A 329 ? 0.9812 0.8136 0.5696 0.0006  0.0419  0.0076  329 ILE A CG2 
2551 C CD1 . ILE A 329 ? 0.9856 0.8567 0.6367 0.0278  0.0604  0.0221  329 ILE A CD1 
2552 C C1  . GOL B .   ? 0.5241 0.4963 0.4925 0.1413  0.0291  0.1264  401 GOL A C1  
2553 O O1  . GOL B .   ? 0.5671 0.5576 0.5377 0.1624  0.0329  0.1394  401 GOL A O1  
2554 C C2  . GOL B .   ? 0.6040 0.5566 0.5542 0.1451  0.0330  0.1322  401 GOL A C2  
2555 O O2  . GOL B .   ? 0.6800 0.5915 0.6059 0.1610  0.0449  0.1365  401 GOL A O2  
2556 C C3  . GOL B .   ? 0.4134 0.3534 0.3626 0.1232  0.0291  0.1203  401 GOL A C3  
2557 O O3  . GOL B .   ? 0.5373 0.4529 0.4665 0.1274  0.0345  0.1257  401 GOL A O3  
2558 C C1  . GOL C .   ? 1.2049 0.8981 1.0073 0.1200  0.0906  -0.0007 402 GOL A C1  
2559 O O1  . GOL C .   ? 1.1437 0.8153 0.9322 0.1122  0.0899  -0.0023 402 GOL A O1  
2560 C C2  . GOL C .   ? 1.1480 0.8818 0.9920 0.1131  0.0791  -0.0012 402 GOL A C2  
2561 O O2  . GOL C .   ? 1.1733 0.9272 1.0282 0.1122  0.0768  -0.0017 402 GOL A O2  
2562 C C3  . GOL C .   ? 1.0809 0.8522 0.9572 0.1245  0.0776  0.0080  402 GOL A C3  
2563 O O3  . GOL C .   ? 1.0370 0.8436 0.9469 0.1077  0.0635  0.0057  402 GOL A O3  
2564 C C1  . GOL D .   ? 1.0239 0.6586 0.7798 0.0489  0.0786  0.1083  403 GOL A C1  
2565 O O1  . GOL D .   ? 1.0652 0.7431 0.8465 0.0614  0.0724  0.1131  403 GOL A O1  
2566 C C2  . GOL D .   ? 0.9880 0.6205 0.7499 0.0534  0.0782  0.1026  403 GOL A C2  
2567 O O2  . GOL D .   ? 1.0064 0.6461 0.7711 0.0804  0.0797  0.1105  403 GOL A O2  
2568 C C3  . GOL D .   ? 0.9753 0.6487 0.7720 0.0384  0.0692  0.0918  403 GOL A C3  
2569 O O3  . GOL D .   ? 0.8721 0.5273 0.6595 0.0167  0.0702  0.0837  403 GOL A O3  
2570 C C1  . GOL E .   ? 0.8245 0.7376 0.7361 0.0320  0.0258  0.0907  404 GOL A C1  
2571 O O1  . GOL E .   ? 0.5307 0.4268 0.4443 0.0321  0.0299  0.0878  404 GOL A O1  
2572 C C2  . GOL E .   ? 0.7011 0.6073 0.6016 0.0242  0.0299  0.0908  404 GOL A C2  
2573 O O2  . GOL E .   ? 0.6736 0.5558 0.5594 0.0260  0.0360  0.0971  404 GOL A O2  
2574 C C3  . GOL E .   ? 0.9066 0.8276 0.8005 0.0248  0.0255  0.0948  404 GOL A C3  
2575 O O3  . GOL E .   ? 0.7169 0.6481 0.6132 0.0161  0.0245  0.0866  404 GOL A O3  
2576 C C1  . PEG F .   ? 1.2056 1.0055 1.0833 0.1138  0.0742  -0.0001 405 PEG A C1  
2577 O O1  . PEG F .   ? 1.2682 1.0469 1.1195 0.1307  0.0878  0.0023  405 PEG A O1  
2578 C C2  . PEG F .   ? 1.1981 1.0129 1.0884 0.0946  0.0622  -0.0056 405 PEG A C2  
2579 O O2  . PEG F .   ? 1.2705 1.0497 1.1281 0.0835  0.0627  -0.0137 405 PEG A O2  
2580 C C3  . PEG F .   ? 1.0703 0.8654 0.9392 0.0661  0.0513  -0.0176 405 PEG A C3  
2581 C C4  . PEG F .   ? 1.1374 0.8968 0.9694 0.0526  0.0512  -0.0254 405 PEG A C4  
2582 O O4  . PEG F .   ? 0.9539 0.7341 0.7983 0.0376  0.0402  -0.0274 405 PEG A O4  
2583 O O   . HOH G .   ? 0.5156 0.4957 0.5645 0.0286  -0.0120 0.0127  501 HOH A O   
2584 O O   . HOH G .   ? 0.8187 0.4730 0.4981 -0.1384 -0.0115 -0.0247 502 HOH A O   
2585 O O   . HOH G .   ? 0.5360 0.5506 0.5297 0.0315  0.0190  0.0328  503 HOH A O   
2586 O O   . HOH G .   ? 0.7962 0.6035 0.5880 0.0365  0.0686  -0.0068 504 HOH A O   
2587 O O   . HOH G .   ? 0.6429 0.5049 0.5449 -0.0906 -0.0174 -0.0256 505 HOH A O   
2588 O O   . HOH G .   ? 0.6108 0.6416 0.6037 0.0192  0.0692  0.0436  506 HOH A O   
2589 O O   . HOH G .   ? 0.6402 0.7769 0.7436 -0.0235 -0.0340 0.0227  507 HOH A O   
2590 O O   . HOH G .   ? 0.5220 0.5221 0.4729 0.0080  0.0720  0.0495  508 HOH A O   
2591 O O   . HOH G .   ? 0.5023 0.5025 0.5563 0.0971  0.0317  0.0311  509 HOH A O   
2592 O O   . HOH G .   ? 0.5092 0.5340 0.5714 -0.0534 -0.0088 0.0099  510 HOH A O   
2593 O O   . HOH G .   ? 0.5430 0.5910 0.6072 0.0719  -0.0013 0.0667  511 HOH A O   
2594 O O   . HOH G .   ? 0.7164 0.5165 0.5435 -0.1043 0.0727  0.0919  512 HOH A O   
2595 O O   . HOH G .   ? 0.6728 0.2981 0.3790 -0.1077 0.0008  -0.0155 513 HOH A O   
2596 O O   . HOH G .   ? 0.4231 0.4939 0.5190 0.0221  -0.0253 0.0137  514 HOH A O   
2597 O O   . HOH G .   ? 0.8236 0.8054 0.6716 0.0210  -0.0207 0.0554  515 HOH A O   
2598 O O   . HOH G .   ? 0.4264 0.4646 0.5182 0.0299  -0.0126 0.0256  516 HOH A O   
2599 O O   . HOH G .   ? 0.3320 0.4324 0.4020 0.0146  -0.0411 0.0247  517 HOH A O   
2600 O O   . HOH G .   ? 0.7645 0.7230 0.6489 0.2186  0.0165  0.1424  518 HOH A O   
2601 O O   . HOH G .   ? 0.5700 0.6129 0.5907 -0.0626 -0.0420 -0.0003 519 HOH A O   
2602 O O   . HOH G .   ? 0.7804 0.3775 0.4918 -0.1650 0.0466  0.0190  520 HOH A O   
2603 O O   . HOH G .   ? 0.6662 0.6012 0.4830 -0.0228 0.0123  0.0540  521 HOH A O   
2604 O O   . HOH G .   ? 0.7047 0.7904 0.7390 0.1170  0.0049  0.1202  522 HOH A O   
2605 O O   . HOH G .   ? 0.3648 0.3420 0.4122 0.0453  -0.0144 0.0159  523 HOH A O   
2606 O O   . HOH G .   ? 0.4957 0.4036 0.4269 -0.1092 0.0477  0.0603  524 HOH A O   
2607 O O   . HOH G .   ? 0.5001 0.5907 0.5834 0.1425  0.0342  0.0540  525 HOH A O   
2608 O O   . HOH G .   ? 0.6844 0.5501 0.6043 -0.1383 0.0039  0.0075  526 HOH A O   
2609 O O   . HOH G .   ? 0.6414 0.3298 0.4525 0.0266  0.0204  0.0378  527 HOH A O   
2610 O O   . HOH G .   ? 0.7036 0.3490 0.4843 0.1382  0.0943  0.0720  528 HOH A O   
2611 O O   . HOH G .   ? 0.4714 0.5573 0.4583 -0.0131 -0.0392 0.0713  529 HOH A O   
2612 O O   . HOH G .   ? 0.5023 0.5718 0.5710 -0.0416 -0.0322 0.0070  530 HOH A O   
2613 O O   . HOH G .   ? 0.5632 0.6216 0.6665 0.0567  -0.0068 0.0191  531 HOH A O   
2614 O O   . HOH G .   ? 0.5199 0.4730 0.5445 0.1095  0.0410  0.0294  532 HOH A O   
2615 O O   . HOH G .   ? 0.4794 0.2875 0.3915 -0.0159 -0.0016 0.0009  533 HOH A O   
2616 O O   . HOH G .   ? 0.4085 0.3956 0.4389 0.0638  0.0395  0.0120  534 HOH A O   
2617 O O   . HOH G .   ? 0.7894 0.4980 0.6038 -0.1165 0.0159  -0.0162 535 HOH A O   
2618 O O   . HOH G .   ? 0.2497 0.2469 0.3384 0.0306  -0.0120 -0.0002 536 HOH A O   
2619 O O   . HOH G .   ? 0.6698 0.3899 0.4776 0.0259  0.0645  0.1030  537 HOH A O   
2620 O O   . HOH G .   ? 0.7022 0.3196 0.4834 0.0826  0.0814  0.0327  538 HOH A O   
2621 O O   . HOH G .   ? 0.6274 0.3651 0.4628 0.1509  0.0652  0.0325  539 HOH A O   
2622 O O   . HOH G .   ? 0.6847 0.5966 0.6791 0.1368  0.0475  0.0616  540 HOH A O   
2623 O O   . HOH G .   ? 0.6012 0.5525 0.5243 0.1396  0.0298  0.1481  541 HOH A O   
2624 O O   . HOH G .   ? 0.5413 0.6151 0.3862 -0.1167 -0.0729 0.0669  542 HOH A O   
2625 O O   . HOH G .   ? 0.6188 0.6997 0.7293 0.0222  0.0103  0.0208  543 HOH A O   
2626 O O   . HOH G .   ? 0.3398 0.3481 0.4189 0.0235  -0.0098 0.0115  544 HOH A O   
2627 O O   . HOH G .   ? 0.5944 0.3309 0.3654 -0.0419 0.0134  -0.0241 545 HOH A O   
2628 O O   . HOH G .   ? 0.7556 0.2992 0.4409 -0.1190 0.0530  0.0043  546 HOH A O   
2629 O O   . HOH G .   ? 0.5275 0.4846 0.3754 0.0111  -0.0076 0.0231  547 HOH A O   
2630 O O   . HOH G .   ? 0.4373 0.4754 0.4570 -0.0031 0.0552  0.0451  548 HOH A O   
2631 O O   . HOH G .   ? 0.4307 0.3019 0.3583 0.0380  0.0328  0.0779  549 HOH A O   
2632 O O   . HOH G .   ? 0.6471 0.4480 0.4916 0.1528  0.0617  0.1454  550 HOH A O   
2633 O O   . HOH G .   ? 0.3652 0.4292 0.3761 0.0567  -0.0386 0.0522  551 HOH A O   
2634 O O   . HOH G .   ? 0.3632 0.4250 0.3502 0.0958  0.0712  0.0497  552 HOH A O   
2635 O O   . HOH G .   ? 0.4348 0.3741 0.4550 -0.0077 -0.0142 0.0098  553 HOH A O   
2636 O O   . HOH G .   ? 0.2427 0.2170 0.3136 0.0286  -0.0105 0.0015  554 HOH A O   
2637 O O   . HOH G .   ? 0.5379 0.4307 0.4389 0.0655  0.0295  0.1103  555 HOH A O   
2638 O O   . HOH G .   ? 0.4485 0.5032 0.5489 0.0533  -0.0111 0.0181  556 HOH A O   
2639 O O   . HOH G .   ? 0.8229 0.3941 0.5367 0.0551  0.0486  0.0234  557 HOH A O   
2640 O O   . HOH G .   ? 0.6754 0.3627 0.4572 -0.0676 0.0184  -0.0389 558 HOH A O   
2641 O O   . HOH G .   ? 0.8857 0.2822 0.4162 -0.1476 0.0783  0.0123  559 HOH A O   
2642 O O   . HOH G .   ? 0.4978 0.5876 0.5246 -0.0142 -0.0516 0.0194  560 HOH A O   
2643 O O   . HOH G .   ? 0.6453 0.2297 0.3716 0.0148  0.0379  0.0024  561 HOH A O   
2644 O O   . HOH G .   ? 0.7143 0.7144 0.6425 -0.0389 0.0822  0.0792  562 HOH A O   
2645 O O   . HOH G .   ? 0.4138 0.4078 0.4191 0.0214  0.0020  0.0294  563 HOH A O   
2646 O O   . HOH G .   ? 0.8211 0.7665 0.6293 -0.0468 -0.0112 0.0461  564 HOH A O   
2647 O O   . HOH G .   ? 0.7030 0.5974 0.6439 0.1761  0.0643  0.0447  565 HOH A O   
2648 O O   . HOH G .   ? 0.6563 0.5653 0.5290 -0.1442 -0.0470 0.0111  566 HOH A O   
2649 O O   . HOH G .   ? 0.6820 0.6687 0.5256 -0.0565 -0.0307 0.0512  567 HOH A O   
2650 O O   . HOH G .   ? 0.7672 0.3539 0.5305 0.0267  0.0708  0.0173  568 HOH A O   
2651 O O   . HOH G .   ? 0.5387 0.5023 0.4518 0.0292  0.0091  0.0942  569 HOH A O   
2652 O O   . HOH G .   ? 1.1125 0.6591 0.7825 0.0956  0.1075  -0.0077 570 HOH A O   
2653 O O   . HOH G .   ? 0.6203 0.3091 0.3880 0.0046  0.0361  -0.0251 571 HOH A O   
2654 O O   . HOH G .   ? 0.6192 0.2848 0.4138 -0.0936 0.0545  0.0431  572 HOH A O   
2655 O O   . HOH G .   ? 0.4563 0.3404 0.4223 -0.0488 0.0307  0.0354  573 HOH A O   
2656 O O   . HOH G .   ? 0.3425 0.4311 0.3620 0.0009  -0.0511 0.0262  574 HOH A O   
2657 O O   . HOH G .   ? 0.4244 0.4403 0.4730 -0.0207 0.0285  0.0319  575 HOH A O   
2658 O O   . HOH G .   ? 0.4017 0.4237 0.4666 0.0393  -0.0082 0.0397  576 HOH A O   
2659 O O   . HOH G .   ? 0.7576 0.4551 0.4612 -0.1332 -0.0160 -0.0231 577 HOH A O   
2660 O O   . HOH G .   ? 0.7432 0.4148 0.4826 0.0829  0.0844  -0.0192 578 HOH A O   
2661 O O   . HOH G .   ? 0.9159 0.7278 0.8113 0.1563  0.0863  0.0332  579 HOH A O   
2662 O O   . HOH G .   ? 0.7944 0.4132 0.5164 -0.0167 0.0321  -0.0249 580 HOH A O   
2663 O O   . HOH G .   ? 0.4165 0.4629 0.4640 -0.0159 -0.0306 0.0303  581 HOH A O   
2664 O O   . HOH G .   ? 0.5543 0.2188 0.3299 0.0646  0.0582  -0.0151 582 HOH A O   
2665 O O   . HOH G .   ? 0.8900 0.3459 0.4984 -0.0984 0.0869  0.0531  583 HOH A O   
2666 O O   . HOH G .   ? 0.6025 0.4818 0.5172 0.1936  0.0551  0.0685  584 HOH A O   
2667 O O   . HOH G .   ? 0.9367 0.4042 0.4910 0.0383  0.0889  -0.0276 585 HOH A O   
2668 O O   . HOH G .   ? 0.6730 0.4645 0.4654 -0.1466 -0.0327 -0.0052 586 HOH A O   
2669 O O   . HOH G .   ? 0.5282 0.3385 0.4138 -0.0250 0.0020  0.0412  587 HOH A O   
2670 O O   . HOH G .   ? 0.4540 0.5563 0.5090 0.0214  -0.0282 0.0685  588 HOH A O   
2671 O O   . HOH G .   ? 0.4884 0.6491 0.3452 -0.2027 -0.1080 0.0780  589 HOH A O   
2672 O O   . HOH G .   ? 0.4951 0.5426 0.5240 -0.0406 -0.0417 0.0015  590 HOH A O   
2673 O O   . HOH G .   ? 0.7860 0.7072 0.6269 0.0278  0.0843  0.0322  591 HOH A O   
2674 O O   . HOH G .   ? 0.4931 0.5793 0.6102 0.0381  0.0021  0.0203  592 HOH A O   
2675 O O   . HOH G .   ? 0.8731 0.5583 0.6704 0.1151  0.0762  0.1143  593 HOH A O   
2676 O O   . HOH G .   ? 0.5232 0.6170 0.5967 0.1242  0.0606  0.0453  594 HOH A O   
2677 O O   . HOH G .   ? 0.4289 0.5221 0.5060 0.0194  -0.0250 0.0534  595 HOH A O   
2678 O O   . HOH G .   ? 0.6804 0.6048 0.5853 0.1084  0.0277  0.1371  596 HOH A O   
2679 O O   . HOH G .   ? 0.6469 0.6626 0.6276 0.1974  0.0255  0.0986  597 HOH A O   
2680 O O   . HOH G .   ? 0.6895 0.3068 0.4460 -0.1184 0.0397  0.0024  598 HOH A O   
2681 O O   . HOH G .   ? 0.4262 0.3845 0.3769 0.0502  -0.0163 0.0531  599 HOH A O   
2682 O O   . HOH G .   ? 0.5957 0.5706 0.5314 0.0236  0.0028  0.0407  600 HOH A O   
2683 O O   . HOH G .   ? 0.6858 0.3726 0.5198 -0.0407 0.0350  -0.0080 601 HOH A O   
2684 O O   . HOH G .   ? 0.9068 0.4008 0.5529 -0.0502 0.0916  0.0799  602 HOH A O   
2685 O O   . HOH G .   ? 0.6770 0.5293 0.5854 -0.0526 -0.0035 0.0398  603 HOH A O   
2686 O O   . HOH G .   ? 0.4796 0.5117 0.5480 0.0094  -0.0061 0.0258  604 HOH A O   
2687 O O   . HOH G .   ? 0.7403 0.4444 0.5385 -0.1308 0.0564  0.0559  605 HOH A O   
2688 O O   . HOH G .   ? 0.3022 0.2938 0.3843 0.0315  -0.0012 0.0018  606 HOH A O   
2689 O O   . HOH G .   ? 0.9299 0.4782 0.6254 0.0056  0.0888  0.0953  607 HOH A O   
2690 O O   . HOH G .   ? 0.5753 0.6586 0.5548 0.0897  -0.0410 0.0874  608 HOH A O   
2691 O O   . HOH G .   ? 0.4105 0.4678 0.5122 0.0477  -0.0023 0.0313  609 HOH A O   
2692 O O   . HOH G .   ? 0.5866 0.4310 0.4055 -0.0030 0.0343  -0.0017 610 HOH A O   
2693 O O   . HOH G .   ? 0.3849 0.2684 0.3581 -0.0163 -0.0109 0.0037  611 HOH A O   
2694 O O   . HOH G .   ? 0.8363 0.6899 0.6843 -0.0983 0.0762  0.0967  612 HOH A O   
2695 O O   . HOH G .   ? 0.7633 0.6876 0.4248 -0.2547 -0.0953 -0.0254 613 HOH A O   
2696 O O   . HOH G .   ? 0.8027 0.5789 0.5971 0.1961  0.0383  0.1206  614 HOH A O   
2697 O O   . HOH G .   ? 0.6469 0.4724 0.5088 0.1303  0.0953  0.0058  615 HOH A O   
2698 O O   . HOH G .   ? 0.7290 0.7214 0.6964 -0.0736 -0.0421 -0.0107 616 HOH A O   
2699 O O   . HOH G .   ? 0.5075 0.2636 0.3727 -0.0691 0.0471  0.0462  617 HOH A O   
2700 O O   . HOH G .   ? 0.4381 0.4656 0.5265 0.0206  -0.0148 0.0184  618 HOH A O   
2701 O O   . HOH G .   ? 0.3935 0.3934 0.4580 0.0317  -0.0058 0.0090  619 HOH A O   
2702 O O   . HOH G .   ? 0.7819 0.3536 0.4870 -0.0477 0.0226  0.0158  620 HOH A O   
2703 O O   . HOH G .   ? 0.3912 0.4322 0.4606 0.0576  -0.0219 0.0265  621 HOH A O   
2704 O O   . HOH G .   ? 0.3758 0.3537 0.4553 0.0213  -0.0028 0.0022  622 HOH A O   
2705 O O   . HOH G .   ? 0.6766 0.7290 0.6854 0.1573  0.0234  0.1377  623 HOH A O   
2706 O O   . HOH G .   ? 0.5021 0.5274 0.5875 0.0365  0.0139  0.0113  624 HOH A O   
2707 O O   . HOH G .   ? 0.4324 0.3325 0.3913 -0.0718 -0.0136 -0.0160 625 HOH A O   
2708 O O   . HOH G .   ? 0.7249 0.6312 0.4616 -0.1345 -0.0470 0.0193  626 HOH A O   
2709 O O   . HOH G .   ? 0.4949 0.5347 0.5108 -0.0380 -0.0373 0.0306  627 HOH A O   
2710 O O   . HOH G .   ? 0.4225 0.4123 0.4962 0.0223  0.0044  0.0073  628 HOH A O   
2711 O O   . HOH G .   ? 0.4776 0.4308 0.3792 0.1343  -0.0123 0.1099  629 HOH A O   
2712 O O   . HOH G .   ? 1.0382 0.5534 0.6590 0.0287  0.0861  -0.0413 630 HOH A O   
2713 O O   . HOH G .   ? 0.6967 0.5415 0.6018 -0.1354 0.0006  -0.0009 631 HOH A O   
2714 O O   . HOH G .   ? 0.6306 0.3805 0.4723 -0.0705 0.0086  -0.0307 632 HOH A O   
2715 O O   . HOH G .   ? 0.3604 0.3059 0.3253 0.0395  -0.0110 0.0438  633 HOH A O   
2716 O O   . HOH G .   ? 0.9682 0.4665 0.6436 0.0109  0.0869  0.0276  634 HOH A O   
2717 O O   . HOH G .   ? 0.6873 0.3294 0.4129 0.0933  0.0879  -0.0180 635 HOH A O   
2718 O O   . HOH G .   ? 0.6266 0.4196 0.4982 -0.1056 0.0468  0.0511  636 HOH A O   
2719 O O   . HOH G .   ? 0.6465 0.5576 0.4902 -0.1005 0.0926  0.1119  637 HOH A O   
2720 O O   . HOH G .   ? 0.4878 0.4744 0.3832 0.0390  -0.0249 0.0635  638 HOH A O   
2721 O O   . HOH G .   ? 0.4380 0.4808 0.4646 0.0334  0.0205  0.0362  639 HOH A O   
2722 O O   . HOH G .   ? 0.6126 0.4765 0.5297 0.1584  0.0842  0.0207  640 HOH A O   
2723 O O   . HOH G .   ? 0.4933 0.5954 0.4572 -0.0212 -0.0456 0.0830  641 HOH A O   
2724 O O   . HOH G .   ? 0.4126 0.4883 0.4875 -0.0030 -0.0284 0.0377  642 HOH A O   
2725 O O   . HOH G .   ? 0.6540 0.4176 0.4847 -0.0153 0.0105  0.0604  643 HOH A O   
2726 O O   . HOH G .   ? 0.5990 0.4045 0.4748 0.1682  0.0699  0.1153  644 HOH A O   
2727 O O   . HOH G .   ? 0.7369 0.5329 0.5494 0.0600  0.0736  -0.0096 645 HOH A O   
2728 O O   . HOH G .   ? 0.7201 0.2973 0.4183 0.0244  0.0522  -0.0199 646 HOH A O   
2729 O O   . HOH G .   ? 0.4502 0.5183 0.5493 0.0741  0.0082  0.0452  647 HOH A O   
2730 O O   . HOH G .   ? 0.7016 0.8215 0.7341 0.1016  -0.0073 0.1283  648 HOH A O   
2731 O O   . HOH G .   ? 0.5810 0.6319 0.6864 0.0297  0.0036  0.0125  649 HOH A O   
2732 O O   . HOH G .   ? 0.3964 0.3718 0.4478 -0.0302 -0.0001 0.0060  650 HOH A O   
2733 O O   . HOH G .   ? 0.6661 0.6522 0.6320 -0.0322 0.0079  0.0591  651 HOH A O   
2734 O O   . HOH G .   ? 0.2536 0.2834 0.3419 0.0334  -0.0040 0.0173  652 HOH A O   
2735 O O   . HOH G .   ? 0.5953 0.6893 0.5971 0.1754  -0.0102 0.1167  653 HOH A O   
2736 O O   . HOH G .   ? 0.6661 0.3272 0.4322 0.0566  0.0276  0.0689  654 HOH A O   
2737 O O   . HOH G .   ? 0.9676 0.3528 0.5235 -0.0399 0.0993  0.0239  655 HOH A O   
2738 O O   . HOH G .   ? 0.5809 0.5893 0.5969 0.1659  0.0731  0.0434  656 HOH A O   
2739 O O   . HOH G .   ? 0.4716 0.4317 0.4617 -0.0090 -0.0027 0.0386  657 HOH A O   
2740 O O   . HOH G .   ? 0.5244 0.5238 0.5149 0.0143  0.0080  0.0391  658 HOH A O   
2741 O O   . HOH G .   ? 0.6003 0.6752 0.4890 0.0065  -0.0615 0.0597  659 HOH A O   
2742 O O   . HOH G .   ? 0.6730 0.6555 0.5240 -0.1972 -0.0723 0.0281  660 HOH A O   
2743 O O   . HOH G .   ? 0.6368 0.7315 0.4811 -0.2093 -0.1033 0.0074  661 HOH A O   
2744 O O   . HOH G .   ? 0.5602 0.4221 0.4683 -0.0816 -0.0236 0.0030  662 HOH A O   
2745 O O   . HOH G .   ? 0.7066 0.6141 0.6040 0.1891  0.0558  0.1574  663 HOH A O   
2746 O O   . HOH G .   ? 0.9370 0.6070 0.7314 0.1258  0.0937  0.0165  664 HOH A O   
2747 O O   . HOH G .   ? 0.4542 0.4612 0.5158 -0.0215 0.0152  0.0213  665 HOH A O   
2748 O O   . HOH G .   ? 0.3751 0.3782 0.4638 0.0286  -0.0099 0.0091  666 HOH A O   
2749 O O   . HOH G .   ? 0.4512 0.5439 0.5596 0.0829  0.0048  0.0342  667 HOH A O   
2750 O O   . HOH G .   ? 0.8867 0.3916 0.5078 0.1001  0.0902  0.0082  668 HOH A O   
2751 O O   . HOH G .   ? 0.4216 0.4190 0.5118 0.0243  -0.0041 0.0018  669 HOH A O   
2752 O O   . HOH G .   ? 0.5176 0.5820 0.5539 0.1158  -0.0172 0.0701  670 HOH A O   
2753 O O   . HOH G .   ? 0.5628 0.5185 0.4852 0.0761  0.0151  0.1204  671 HOH A O   
2754 O O   . HOH G .   ? 0.6715 0.4536 0.5350 -0.0607 -0.0023 0.0288  672 HOH A O   
2755 O O   . HOH G .   ? 0.9943 0.4955 0.6712 0.0333  0.0934  0.0505  673 HOH A O   
2756 O O   . HOH G .   ? 0.8051 0.6740 0.6583 0.0243  0.0413  0.1110  674 HOH A O   
2757 O O   . HOH G .   ? 0.6845 0.6514 0.6215 0.0457  0.0739  0.0259  675 HOH A O   
2758 O O   . HOH G .   ? 0.4225 0.4360 0.5136 0.0236  0.0027  0.0064  676 HOH A O   
2759 O O   . HOH G .   ? 0.4984 0.5757 0.4729 0.0139  0.0987  0.0661  677 HOH A O   
2760 O O   . HOH G .   ? 0.4085 0.4620 0.5027 0.0198  -0.0092 0.0253  678 HOH A O   
2761 O O   . HOH G .   ? 0.6668 0.3938 0.4700 -0.0970 0.0675  0.0794  679 HOH A O   
2762 O O   . HOH G .   ? 0.7099 0.3628 0.4325 0.1408  0.1110  -0.0033 680 HOH A O   
2763 O O   . HOH G .   ? 0.6456 0.6300 0.6596 0.1610  0.0366  0.0531  681 HOH A O   
2764 O O   . HOH G .   ? 0.3340 0.3350 0.4140 0.0380  0.0064  0.0049  682 HOH A O   
2765 O O   . HOH G .   ? 0.5153 0.6132 0.5495 0.0775  0.0532  0.0545  683 HOH A O   
2766 O O   . HOH G .   ? 0.7108 0.7378 0.7432 -0.1007 -0.0155 0.0123  684 HOH A O   
2767 O O   . HOH G .   ? 0.6124 0.5953 0.5764 0.0109  0.0078  0.0459  685 HOH A O   
2768 O O   . HOH G .   ? 0.7378 0.5215 0.5412 -0.0608 0.0759  0.1072  686 HOH A O   
2769 O O   . HOH G .   ? 0.6040 0.5361 0.5750 0.1225  0.0691  0.0173  687 HOH A O   
2770 O O   . HOH G .   ? 0.6620 0.5664 0.6010 0.1755  0.0844  0.0342  688 HOH A O   
2771 O O   . HOH G .   ? 0.5768 0.6853 0.6788 0.1131  0.0107  0.0498  689 HOH A O   
2772 O O   . HOH G .   ? 0.4003 0.3692 0.4708 0.0140  -0.0036 -0.0012 690 HOH A O   
2773 O O   . HOH G .   ? 1.0034 0.5252 0.6620 0.0031  0.0741  -0.0303 691 HOH A O   
2774 O O   . HOH G .   ? 0.6649 0.8126 0.6308 -0.0360 -0.0783 0.0430  692 HOH A O   
2775 O O   . HOH G .   ? 0.5187 0.5368 0.4517 0.1551  -0.0175 0.1206  693 HOH A O   
2776 O O   . HOH G .   ? 0.4435 0.4522 0.4027 -0.0238 0.0715  0.0650  694 HOH A O   
2777 O O   . HOH G .   ? 0.5850 0.4799 0.5353 -0.1054 -0.0081 -0.0056 695 HOH A O   
2778 O O   . HOH G .   ? 0.5033 0.5933 0.6201 0.0262  -0.0123 0.0179  696 HOH A O   
2779 O O   . HOH G .   ? 0.9751 0.4735 0.5927 -0.0356 0.0415  -0.0094 697 HOH A O   
2780 O O   . HOH G .   ? 0.8401 0.4268 0.5357 -0.0997 0.0106  0.0117  698 HOH A O   
2781 O O   . HOH G .   ? 0.6007 0.2502 0.3540 0.1135  0.0819  -0.0023 699 HOH A O   
2782 O O   . HOH G .   ? 0.6616 0.6328 0.4345 -0.0190 -0.0340 0.0298  700 HOH A O   
2783 O O   . HOH G .   ? 0.7303 0.5874 0.6057 0.1158  0.0939  0.0069  701 HOH A O   
2784 O O   . HOH G .   ? 0.6480 0.5526 0.4990 -0.0347 0.0728  0.0967  702 HOH A O   
2785 O O   . HOH G .   ? 0.5355 0.6054 0.6459 0.0494  -0.0055 0.0186  703 HOH A O   
2786 O O   . HOH G .   ? 0.6330 0.6294 0.5304 -0.0395 0.0937  0.0883  704 HOH A O   
2787 O O   . HOH G .   ? 0.4819 0.4602 0.5264 0.0303  0.0152  0.0069  705 HOH A O   
2788 O O   . HOH G .   ? 0.4419 0.5049 0.5230 -0.0145 -0.0216 0.0304  706 HOH A O   
2789 O O   . HOH G .   ? 0.8107 0.4723 0.5503 -0.0697 0.0822  0.1055  707 HOH A O   
2790 O O   . HOH G .   ? 0.6681 0.4793 0.4925 0.1161  0.0093  0.1052  708 HOH A O   
2791 O O   . HOH G .   ? 0.6054 0.5306 0.4455 -0.0048 0.0439  0.0499  709 HOH A O   
2792 O O   . HOH G .   ? 0.7237 0.5897 0.6674 0.1123  0.0604  0.0105  710 HOH A O   
2793 O O   . HOH G .   ? 0.9598 0.5475 0.6419 -0.0302 0.0298  0.0776  711 HOH A O   
2794 O O   . HOH G .   ? 0.6912 0.4994 0.5188 0.0765  0.0072  0.0930  712 HOH A O   
2795 O O   . HOH G .   ? 0.5930 0.5174 0.5859 -0.0321 -0.0186 0.0070  713 HOH A O   
2796 O O   . HOH G .   ? 0.4799 0.5482 0.5720 -0.0324 -0.0122 0.0133  714 HOH A O   
2797 O O   . HOH G .   ? 0.7349 0.5014 0.4502 -0.1818 -0.0409 -0.0113 715 HOH A O   
2798 O O   . HOH G .   ? 0.5722 0.4067 0.4874 -0.0771 -0.0026 -0.0190 716 HOH A O   
2799 O O   . HOH G .   ? 0.6475 0.7429 0.5980 -0.0490 -0.0699 0.0235  717 HOH A O   
2800 O O   . HOH G .   ? 0.6081 0.4652 0.5288 -0.0506 -0.0064 0.0324  718 HOH A O   
2801 O O   . HOH G .   ? 0.6093 0.6260 0.5500 -0.0909 -0.0511 0.0290  719 HOH A O   
2802 O O   . HOH G .   ? 0.5594 0.5410 0.4772 0.0991  -0.0233 0.0941  720 HOH A O   
2803 O O   . HOH G .   ? 0.8697 0.5347 0.6202 -0.1898 0.0474  0.0396  721 HOH A O   
2804 O O   . HOH G .   ? 0.3913 0.3999 0.4005 0.0311  0.0115  0.0265  722 HOH A O   
2805 O O   . HOH G .   ? 0.7583 0.3524 0.4602 0.0236  0.0537  -0.0258 723 HOH A O   
2806 O O   . HOH G .   ? 0.8272 0.3966 0.5116 -0.0730 0.0180  -0.0054 724 HOH A O   
2807 O O   . HOH G .   ? 0.8781 0.8618 0.6404 -0.0106 -0.0354 0.0465  725 HOH A O   
2808 O O   . HOH G .   ? 0.4156 0.4302 0.4892 0.0247  -0.0064 0.0152  726 HOH A O   
2809 O O   . HOH G .   ? 0.7071 0.6136 0.6488 -0.1355 -0.0091 0.0008  727 HOH A O   
2810 O O   . HOH G .   ? 0.9131 0.5415 0.5715 -0.0170 0.0486  -0.0354 728 HOH A O   
2811 O O   . HOH G .   ? 0.7630 0.7591 0.7023 0.0170  0.0200  0.0494  729 HOH A O   
2812 O O   . HOH G .   ? 1.0295 0.8154 0.8921 0.1795  0.0991  0.0539  730 HOH A O   
2813 O O   . HOH G .   ? 0.8040 0.4942 0.4681 -0.1204 -0.0075 -0.0283 731 HOH A O   
2814 O O   . HOH G .   ? 0.9363 0.5517 0.6566 -0.1368 0.0743  0.0748  732 HOH A O   
2815 O O   . HOH G .   ? 0.5061 0.7153 0.6547 0.0309  0.0163  0.0513  733 HOH A O   
2816 O O   . HOH G .   ? 0.6429 0.3312 0.3841 -0.0416 0.0189  -0.0279 734 HOH A O   
2817 O O   . HOH G .   ? 1.0935 0.5456 0.6313 -0.0756 0.0415  -0.0234 735 HOH A O   
2818 O O   . HOH G .   ? 0.5555 0.6107 0.4844 -0.1563 -0.0695 0.0403  736 HOH A O   
2819 O O   . HOH G .   ? 0.5239 0.5326 0.5544 0.0665  0.0498  0.0190  737 HOH A O   
2820 O O   . HOH G .   ? 1.0128 0.5074 0.6766 0.0661  0.1031  0.0659  738 HOH A O   
2821 O O   . HOH G .   ? 1.0681 0.6814 0.7829 0.1657  0.1263  0.0306  739 HOH A O   
2822 O O   . HOH G .   ? 1.0208 0.5716 0.6616 -0.2079 0.0547  0.0287  740 HOH A O   
2823 O O   . HOH G .   ? 0.5939 0.3530 0.4423 -0.1378 0.0338  0.0285  741 HOH A O   
2824 O O   . HOH G .   ? 0.5041 0.6129 0.5471 -0.0131 -0.0398 0.0598  742 HOH A O   
2825 O O   . HOH G .   ? 0.4155 0.5405 0.4548 0.0275  -0.0517 0.0456  743 HOH A O   
2826 O O   . HOH G .   ? 0.7182 0.8063 0.7934 -0.0305 -0.0162 0.0436  744 HOH A O   
2827 O O   . HOH G .   ? 0.4587 0.5726 0.5105 -0.0218 -0.0415 0.0556  745 HOH A O   
2828 O O   . HOH G .   ? 0.5193 0.5606 0.6039 0.0324  -0.0008 0.0224  746 HOH A O   
2829 O O   . HOH G .   ? 0.7731 0.5227 0.5822 -0.0928 -0.0007 -0.0386 747 HOH A O   
2830 O O   . HOH G .   ? 0.8587 0.4716 0.6093 0.1406  0.1037  0.0614  748 HOH A O   
2831 O O   . HOH G .   ? 0.5274 0.5757 0.5758 -0.0660 -0.0305 0.0041  749 HOH A O   
2832 O O   . HOH G .   ? 0.6306 0.5592 0.5990 -0.0628 -0.0268 0.0088  750 HOH A O   
2833 O O   . HOH G .   ? 0.7184 0.5948 0.6301 0.1959  0.0627  0.0638  751 HOH A O   
2834 O O   . HOH G .   ? 0.7056 0.4067 0.5199 0.0291  0.0189  0.0459  752 HOH A O   
2835 O O   . HOH G .   ? 1.0021 0.5535 0.6459 -0.2031 0.0495  0.0183  753 HOH A O   
2836 O O   . HOH G .   ? 0.7390 0.3608 0.4606 0.1394  0.0918  0.0135  754 HOH A O   
2837 O O   . HOH G .   ? 0.8968 0.5388 0.7074 0.0530  0.0660  0.0093  755 HOH A O   
2838 O O   . HOH G .   ? 0.6394 0.5859 0.6351 -0.0582 0.0311  0.0387  756 HOH A O   
2839 O O   . HOH G .   ? 0.9445 0.5308 0.6236 0.0178  0.0572  -0.0306 757 HOH A O   
2840 O O   . HOH G .   ? 0.5678 0.6080 0.6556 -0.0127 0.0065  0.0166  758 HOH A O   
2841 O O   . HOH G .   ? 0.6259 0.6731 0.6696 0.1657  0.0445  0.0587  759 HOH A O   
2842 O O   . HOH G .   ? 0.7217 0.3967 0.5071 0.1325  0.0712  0.0201  760 HOH A O   
2843 O O   . HOH G .   ? 0.5637 0.5805 0.6027 -0.0499 0.0285  0.0373  761 HOH A O   
2844 O O   . HOH G .   ? 0.3792 0.4676 0.4146 0.0570  -0.0397 0.0508  762 HOH A O   
2845 O O   . HOH G .   ? 0.5826 0.5826 0.4715 0.0223  0.0367  -0.0367 763 HOH A O   
2846 O O   . HOH G .   ? 0.5712 0.5989 0.6367 -0.0136 0.0225  0.0264  764 HOH A O   
2847 O O   . HOH G .   ? 0.7331 0.3986 0.4110 -0.0786 0.0119  -0.0321 765 HOH A O   
2848 O O   . HOH G .   ? 0.7186 0.5743 0.5476 -0.1302 0.0843  0.1063  766 HOH A O   
2849 O O   . HOH G .   ? 0.6868 0.6878 0.5951 0.0444  0.0476  0.0412  767 HOH A O   
2850 O O   . HOH G .   ? 0.4233 0.4280 0.4956 -0.0055 0.0099  0.0147  768 HOH A O   
2851 O O   . HOH G .   ? 0.5829 0.6192 0.5897 0.0049  0.0152  0.0486  769 HOH A O   
2852 O O   . HOH G .   ? 0.7179 0.4215 0.4959 -0.1989 0.0331  0.0262  770 HOH A O   
2853 O O   . HOH G .   ? 0.8127 0.4895 0.5654 -0.1342 0.0748  0.0848  771 HOH A O   
2854 O O   . HOH G .   ? 0.9009 0.6195 0.6667 -0.0861 0.0812  0.1066  772 HOH A O   
2855 O O   . HOH G .   ? 1.0633 0.5393 0.7144 0.0437  0.1002  0.0400  773 HOH A O   
2856 O O   . HOH G .   ? 0.9313 0.5218 0.6080 0.0390  0.0692  -0.0299 774 HOH A O   
2857 O O   . HOH G .   ? 0.7192 0.6233 0.6026 0.1761  0.0487  0.1669  775 HOH A O   
2858 O O   . HOH G .   ? 0.6477 0.6033 0.6162 -0.1052 -0.0276 -0.0095 776 HOH A O   
2859 O O   . HOH G .   ? 0.7589 0.6267 0.6952 -0.0945 0.0321  0.0371  777 HOH A O   
2860 O O   . HOH G .   ? 0.9970 0.4252 0.5463 -0.1619 0.0670  0.0018  778 HOH A O   
2861 O O   . HOH G .   ? 0.9178 0.3284 0.4976 -0.0439 0.1004  0.0572  779 HOH A O   
2862 O O   . HOH G .   ? 0.5756 0.7579 0.5545 -0.0167 -0.0587 0.1143  780 HOH A O   
2863 O O   . HOH G .   ? 0.7760 0.6274 0.6392 0.2113  0.0788  0.1500  781 HOH A O   
2864 O O   . HOH G .   ? 0.8597 0.4635 0.5093 -0.0747 0.0200  -0.0358 782 HOH A O   
2865 O O   . HOH G .   ? 0.5622 0.4029 0.4736 -0.0664 -0.0062 -0.0245 783 HOH A O   
2866 O O   . HOH G .   ? 0.9543 0.5336 0.6588 0.0965  0.0716  0.0109  784 HOH A O   
2867 O O   . HOH G .   ? 0.5247 0.5947 0.5240 -0.0662 -0.0498 0.0406  785 HOH A O   
2868 O O   . HOH G .   ? 0.9291 0.4666 0.6297 0.0858  0.0999  0.0341  786 HOH A O   
2869 O O   . HOH G .   ? 0.8328 0.4083 0.5168 -0.1729 0.0431  0.0072  787 HOH A O   
2870 O O   . HOH G .   ? 0.7148 0.5827 0.5568 0.1397  0.0017  0.1189  788 HOH A O   
2871 O O   . HOH G .   ? 0.7150 0.6931 0.7176 0.1697  0.0490  0.0522  789 HOH A O   
2872 O O   . HOH G .   ? 0.8973 0.5972 0.6573 0.1798  0.1134  0.0212  790 HOH A O   
2873 O O   . HOH G .   ? 0.5676 0.7652 0.4941 -0.1500 -0.0965 0.0874  791 HOH A O   
2874 O O   . HOH G .   ? 0.4880 0.5918 0.4935 0.0688  -0.0458 0.0718  792 HOH A O   
2875 O O   . HOH G .   ? 0.6437 0.5102 0.5498 0.1956  0.0769  0.1135  793 HOH A O   
2876 O O   . HOH G .   ? 0.8655 0.3722 0.5467 0.0264  0.0880  0.0206  794 HOH A O   
2877 O O   . HOH G .   ? 0.4590 0.4904 0.5427 -0.0210 -0.0009 0.0119  795 HOH A O   
2878 O O   . HOH G .   ? 0.5031 0.6207 0.5509 0.0853  -0.0358 0.0686  796 HOH A O   
2879 O O   . HOH G .   ? 0.7870 0.4607 0.5577 0.0000  0.0202  0.0613  797 HOH A O   
2880 O O   . HOH G .   ? 0.8971 0.5345 0.6423 0.1448  0.0780  0.0309  798 HOH A O   
2881 O O   . HOH G .   ? 0.5947 0.7087 0.5868 -0.0308 -0.0654 0.0281  799 HOH A O   
2882 O O   . HOH G .   ? 0.9449 0.5073 0.6662 0.1013  0.0987  0.0618  800 HOH A O   
2883 O O   . HOH G .   ? 0.8276 0.5023 0.5700 -0.2099 0.0247  0.0093  801 HOH A O   
# 
