data_9N2M
# 
_entry.id   9N2M 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9N2M         pdb_00009n2m 10.2210/pdb9n2m/pdb 
WWPDB D_1000292355 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-02 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9N2M 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              j-brunzelle@northwestern.edu 
_pdbx_contact_author.name_first         Joseph 
_pdbx_contact_author.name_last          Brunzelle 
_pdbx_contact_author.name_mi            S 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9197-0018 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Brunzelle, J.S.' 1 0000-0001-9197-0018 
'Shuvalova, L.'   2 0000-0003-1702-6998 
'Roy, S.M.'       3 0000-0001-9096-0491 
'Watterson, D.M.' 4 0000-0001-7605-5866 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal Structure of Human DAPK1 Catalytic Subunit Complexed with Compound MW01-30-047SRM' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Brunzelle, J.S.' 1 0000-0001-9197-0018 
primary 'Shuvalova, L.'   2 0000-0003-1702-6998 
primary 'Roy, S.M.'       3 0000-0001-9096-0491 
primary 'Watterson, D.M.' 4 0000-0001-7605-5866 
# 
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 'Death-associated protein kinase 1'                             33665.188 1   2.7.11.1 ? ? ? 
2 non-polymer syn 'SULFATE ION'                                                   96.063    1   ?        ? ? ? 
3 non-polymer syn '5-(pyridin-4-yl)-3-[4-(pyridin-4-yl)piperazin-1-yl]pyridazine' 318.376   1   ?        ? ? ? 
4 water       nat water                                                           18.015    232 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'DAP kinase 1' 
# 
_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       
;TVFRQENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHE
VYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIID
FGLAHKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYF
SNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWIKPKDTQQALSSAWSHPQFE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;TVFRQENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHE
VYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIID
FGLAHKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYF
SNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWIKPKDTQQALSSAWSHPQFE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                                   SO4   
3 '5-(pyridin-4-yl)-3-[4-(pyridin-4-yl)piperazin-1-yl]pyridazine' A1BVM 
4 water                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   VAL n 
1 3   PHE n 
1 4   ARG n 
1 5   GLN n 
1 6   GLU n 
1 7   ASN n 
1 8   VAL n 
1 9   ASP n 
1 10  ASP n 
1 11  TYR n 
1 12  TYR n 
1 13  ASP n 
1 14  THR n 
1 15  GLY n 
1 16  GLU n 
1 17  GLU n 
1 18  LEU n 
1 19  GLY n 
1 20  SER n 
1 21  GLY n 
1 22  GLN n 
1 23  PHE n 
1 24  ALA n 
1 25  VAL n 
1 26  VAL n 
1 27  LYS n 
1 28  LYS n 
1 29  CYS n 
1 30  ARG n 
1 31  GLU n 
1 32  LYS n 
1 33  SER n 
1 34  THR n 
1 35  GLY n 
1 36  LEU n 
1 37  GLN n 
1 38  TYR n 
1 39  ALA n 
1 40  ALA n 
1 41  LYS n 
1 42  PHE n 
1 43  ILE n 
1 44  LYS n 
1 45  LYS n 
1 46  ARG n 
1 47  ARG n 
1 48  THR n 
1 49  LYS n 
1 50  SER n 
1 51  SER n 
1 52  ARG n 
1 53  ARG n 
1 54  GLY n 
1 55  VAL n 
1 56  SER n 
1 57  ARG n 
1 58  GLU n 
1 59  ASP n 
1 60  ILE n 
1 61  GLU n 
1 62  ARG n 
1 63  GLU n 
1 64  VAL n 
1 65  SER n 
1 66  ILE n 
1 67  LEU n 
1 68  LYS n 
1 69  GLU n 
1 70  ILE n 
1 71  GLN n 
1 72  HIS n 
1 73  PRO n 
1 74  ASN n 
1 75  VAL n 
1 76  ILE n 
1 77  THR n 
1 78  LEU n 
1 79  HIS n 
1 80  GLU n 
1 81  VAL n 
1 82  TYR n 
1 83  GLU n 
1 84  ASN n 
1 85  LYS n 
1 86  THR n 
1 87  ASP n 
1 88  VAL n 
1 89  ILE n 
1 90  LEU n 
1 91  ILE n 
1 92  LEU n 
1 93  GLU n 
1 94  LEU n 
1 95  VAL n 
1 96  ALA n 
1 97  GLY n 
1 98  GLY n 
1 99  GLU n 
1 100 LEU n 
1 101 PHE n 
1 102 ASP n 
1 103 PHE n 
1 104 LEU n 
1 105 ALA n 
1 106 GLU n 
1 107 LYS n 
1 108 GLU n 
1 109 SER n 
1 110 LEU n 
1 111 THR n 
1 112 GLU n 
1 113 GLU n 
1 114 GLU n 
1 115 ALA n 
1 116 THR n 
1 117 GLU n 
1 118 PHE n 
1 119 LEU n 
1 120 LYS n 
1 121 GLN n 
1 122 ILE n 
1 123 LEU n 
1 124 ASN n 
1 125 GLY n 
1 126 VAL n 
1 127 TYR n 
1 128 TYR n 
1 129 LEU n 
1 130 HIS n 
1 131 SER n 
1 132 LEU n 
1 133 GLN n 
1 134 ILE n 
1 135 ALA n 
1 136 HIS n 
1 137 PHE n 
1 138 ASP n 
1 139 LEU n 
1 140 LYS n 
1 141 PRO n 
1 142 GLU n 
1 143 ASN n 
1 144 ILE n 
1 145 MET n 
1 146 LEU n 
1 147 LEU n 
1 148 ASP n 
1 149 ARG n 
1 150 ASN n 
1 151 VAL n 
1 152 PRO n 
1 153 LYS n 
1 154 PRO n 
1 155 ARG n 
1 156 ILE n 
1 157 LYS n 
1 158 ILE n 
1 159 ILE n 
1 160 ASP n 
1 161 PHE n 
1 162 GLY n 
1 163 LEU n 
1 164 ALA n 
1 165 HIS n 
1 166 LYS n 
1 167 ILE n 
1 168 ASP n 
1 169 PHE n 
1 170 GLY n 
1 171 ASN n 
1 172 GLU n 
1 173 PHE n 
1 174 LYS n 
1 175 ASN n 
1 176 ILE n 
1 177 PHE n 
1 178 GLY n 
1 179 THR n 
1 180 PRO n 
1 181 GLU n 
1 182 PHE n 
1 183 VAL n 
1 184 ALA n 
1 185 PRO n 
1 186 GLU n 
1 187 ILE n 
1 188 VAL n 
1 189 ASN n 
1 190 TYR n 
1 191 GLU n 
1 192 PRO n 
1 193 LEU n 
1 194 GLY n 
1 195 LEU n 
1 196 GLU n 
1 197 ALA n 
1 198 ASP n 
1 199 MET n 
1 200 TRP n 
1 201 SER n 
1 202 ILE n 
1 203 GLY n 
1 204 VAL n 
1 205 ILE n 
1 206 THR n 
1 207 TYR n 
1 208 ILE n 
1 209 LEU n 
1 210 LEU n 
1 211 SER n 
1 212 GLY n 
1 213 ALA n 
1 214 SER n 
1 215 PRO n 
1 216 PHE n 
1 217 LEU n 
1 218 GLY n 
1 219 ASP n 
1 220 THR n 
1 221 LYS n 
1 222 GLN n 
1 223 GLU n 
1 224 THR n 
1 225 LEU n 
1 226 ALA n 
1 227 ASN n 
1 228 VAL n 
1 229 SER n 
1 230 ALA n 
1 231 VAL n 
1 232 ASN n 
1 233 TYR n 
1 234 GLU n 
1 235 PHE n 
1 236 GLU n 
1 237 ASP n 
1 238 GLU n 
1 239 TYR n 
1 240 PHE n 
1 241 SER n 
1 242 ASN n 
1 243 THR n 
1 244 SER n 
1 245 ALA n 
1 246 LEU n 
1 247 ALA n 
1 248 LYS n 
1 249 ASP n 
1 250 PHE n 
1 251 ILE n 
1 252 ARG n 
1 253 ARG n 
1 254 LEU n 
1 255 LEU n 
1 256 VAL n 
1 257 LYS n 
1 258 ASP n 
1 259 PRO n 
1 260 LYS n 
1 261 LYS n 
1 262 ARG n 
1 263 MET n 
1 264 THR n 
1 265 ILE n 
1 266 GLN n 
1 267 ASP n 
1 268 SER n 
1 269 LEU n 
1 270 GLN n 
1 271 HIS n 
1 272 PRO n 
1 273 TRP n 
1 274 ILE n 
1 275 LYS n 
1 276 PRO n 
1 277 LYS n 
1 278 ASP n 
1 279 THR n 
1 280 GLN n 
1 281 GLN n 
1 282 ALA n 
1 283 LEU n 
1 284 SER n 
1 285 SER n 
1 286 ALA n 
1 287 TRP n 
1 288 SER n 
1 289 HIS n 
1 290 PRO n 
1 291 GLN n 
1 292 PHE n 
1 293 GLU 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                   293 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DAPK1, DAPK' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pASK-IBA3 
_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 
A1BVM non-polymer         . '5-(pyridin-4-yl)-3-[4-(pyridin-4-yl)piperazin-1-yl]pyridazine' ? 'C18 H18 N6'     318.376 
ALA   'L-peptide linking' y ALANINE                                                         ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                        ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                      ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                 ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                        ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                       ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                 ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                         ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                       ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                           ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                      ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                         ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                          ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                      ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                   ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                         ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                          ? 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                                   ? 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                                       ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                      ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                        ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   THR 1   2   2   THR THR A . n 
A 1 2   VAL 2   3   3   VAL VAL A . n 
A 1 3   PHE 3   4   4   PHE PHE A . n 
A 1 4   ARG 4   5   5   ARG ARG A . n 
A 1 5   GLN 5   6   6   GLN GLN A . n 
A 1 6   GLU 6   7   7   GLU GLU A . n 
A 1 7   ASN 7   8   8   ASN ASN A . n 
A 1 8   VAL 8   9   9   VAL VAL A . n 
A 1 9   ASP 9   10  10  ASP ASP A . n 
A 1 10  ASP 10  11  11  ASP ASP A . n 
A 1 11  TYR 11  12  12  TYR TYR A . n 
A 1 12  TYR 12  13  13  TYR TYR A . n 
A 1 13  ASP 13  14  14  ASP ASP A . n 
A 1 14  THR 14  15  15  THR THR A . n 
A 1 15  GLY 15  16  16  GLY GLY A . n 
A 1 16  GLU 16  17  17  GLU GLU A . n 
A 1 17  GLU 17  18  18  GLU GLU A . n 
A 1 18  LEU 18  19  19  LEU LEU A . n 
A 1 19  GLY 19  20  20  GLY GLY A . n 
A 1 20  SER 20  21  21  SER SER A . n 
A 1 21  GLY 21  22  22  GLY GLY A . n 
A 1 22  GLN 22  23  23  GLN GLN A . n 
A 1 23  PHE 23  24  24  PHE PHE A . n 
A 1 24  ALA 24  25  25  ALA ALA A . n 
A 1 25  VAL 25  26  26  VAL VAL A . n 
A 1 26  VAL 26  27  27  VAL VAL A . n 
A 1 27  LYS 27  28  28  LYS LYS A . n 
A 1 28  LYS 28  29  29  LYS LYS A . n 
A 1 29  CYS 29  30  30  CYS CYS A . n 
A 1 30  ARG 30  31  31  ARG ARG A . n 
A 1 31  GLU 31  32  32  GLU GLU A . n 
A 1 32  LYS 32  33  33  LYS LYS A . n 
A 1 33  SER 33  34  34  SER SER A . n 
A 1 34  THR 34  35  35  THR THR A . n 
A 1 35  GLY 35  36  36  GLY GLY A . n 
A 1 36  LEU 36  37  37  LEU LEU A . n 
A 1 37  GLN 37  38  38  GLN GLN A . n 
A 1 38  TYR 38  39  39  TYR TYR A . n 
A 1 39  ALA 39  40  40  ALA ALA A . n 
A 1 40  ALA 40  41  41  ALA ALA A . n 
A 1 41  LYS 41  42  42  LYS LYS A . n 
A 1 42  PHE 42  43  43  PHE PHE A . n 
A 1 43  ILE 43  44  44  ILE ILE A . n 
A 1 44  LYS 44  45  45  LYS LYS A . n 
A 1 45  LYS 45  46  46  LYS LYS A . n 
A 1 46  ARG 46  47  47  ARG ARG A . n 
A 1 47  ARG 47  48  48  ARG ARG A . n 
A 1 48  THR 48  49  49  THR THR A . n 
A 1 49  LYS 49  50  50  LYS LYS A . n 
A 1 50  SER 50  51  51  SER SER A . n 
A 1 51  SER 51  52  52  SER SER A . n 
A 1 52  ARG 52  53  53  ARG ARG A . n 
A 1 53  ARG 53  54  54  ARG ARG A . n 
A 1 54  GLY 54  55  55  GLY GLY A . n 
A 1 55  VAL 55  56  56  VAL VAL A . n 
A 1 56  SER 56  57  57  SER SER A . n 
A 1 57  ARG 57  58  58  ARG ARG A . n 
A 1 58  GLU 58  59  59  GLU GLU A . n 
A 1 59  ASP 59  60  60  ASP ASP A . n 
A 1 60  ILE 60  61  61  ILE ILE A . n 
A 1 61  GLU 61  62  62  GLU GLU A . n 
A 1 62  ARG 62  63  63  ARG ARG A . n 
A 1 63  GLU 63  64  64  GLU GLU A . n 
A 1 64  VAL 64  65  65  VAL VAL A . n 
A 1 65  SER 65  66  66  SER SER A . n 
A 1 66  ILE 66  67  67  ILE ILE A . n 
A 1 67  LEU 67  68  68  LEU LEU A . n 
A 1 68  LYS 68  69  69  LYS LYS A . n 
A 1 69  GLU 69  70  70  GLU GLU A . n 
A 1 70  ILE 70  71  71  ILE ILE A . n 
A 1 71  GLN 71  72  72  GLN GLN A . n 
A 1 72  HIS 72  73  73  HIS HIS A . n 
A 1 73  PRO 73  74  74  PRO PRO A . n 
A 1 74  ASN 74  75  75  ASN ASN A . n 
A 1 75  VAL 75  76  76  VAL VAL A . n 
A 1 76  ILE 76  77  77  ILE ILE A . n 
A 1 77  THR 77  78  78  THR THR A . n 
A 1 78  LEU 78  79  79  LEU LEU A . n 
A 1 79  HIS 79  80  80  HIS HIS A . n 
A 1 80  GLU 80  81  81  GLU GLU A . n 
A 1 81  VAL 81  82  82  VAL VAL A . n 
A 1 82  TYR 82  83  83  TYR TYR A . n 
A 1 83  GLU 83  84  84  GLU GLU A . n 
A 1 84  ASN 84  85  85  ASN ASN A . n 
A 1 85  LYS 85  86  86  LYS LYS A . n 
A 1 86  THR 86  87  87  THR THR A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  VAL 88  89  89  VAL VAL A . n 
A 1 89  ILE 89  90  90  ILE ILE A . n 
A 1 90  LEU 90  91  91  LEU LEU A . n 
A 1 91  ILE 91  92  92  ILE ILE A . n 
A 1 92  LEU 92  93  93  LEU LEU A . n 
A 1 93  GLU 93  94  94  GLU GLU A . n 
A 1 94  LEU 94  95  95  LEU LEU A . n 
A 1 95  VAL 95  96  96  VAL VAL A . n 
A 1 96  ALA 96  97  97  ALA ALA A . n 
A 1 97  GLY 97  98  98  GLY GLY A . n 
A 1 98  GLY 98  99  99  GLY GLY A . n 
A 1 99  GLU 99  100 100 GLU GLU A . n 
A 1 100 LEU 100 101 101 LEU LEU A . n 
A 1 101 PHE 101 102 102 PHE PHE A . n 
A 1 102 ASP 102 103 103 ASP ASP A . n 
A 1 103 PHE 103 104 104 PHE PHE A . n 
A 1 104 LEU 104 105 105 LEU LEU A . n 
A 1 105 ALA 105 106 106 ALA ALA A . n 
A 1 106 GLU 106 107 107 GLU GLU A . n 
A 1 107 LYS 107 108 108 LYS LYS A . n 
A 1 108 GLU 108 109 109 GLU GLU A . n 
A 1 109 SER 109 110 110 SER SER A . n 
A 1 110 LEU 110 111 111 LEU LEU A . n 
A 1 111 THR 111 112 112 THR THR A . n 
A 1 112 GLU 112 113 113 GLU GLU A . n 
A 1 113 GLU 113 114 114 GLU GLU A . n 
A 1 114 GLU 114 115 115 GLU GLU A . n 
A 1 115 ALA 115 116 116 ALA ALA A . n 
A 1 116 THR 116 117 117 THR THR A . n 
A 1 117 GLU 117 118 118 GLU GLU A . n 
A 1 118 PHE 118 119 119 PHE PHE A . n 
A 1 119 LEU 119 120 120 LEU LEU A . n 
A 1 120 LYS 120 121 121 LYS LYS A . n 
A 1 121 GLN 121 122 122 GLN GLN A . n 
A 1 122 ILE 122 123 123 ILE ILE A . n 
A 1 123 LEU 123 124 124 LEU LEU A . n 
A 1 124 ASN 124 125 125 ASN ASN A . n 
A 1 125 GLY 125 126 126 GLY GLY A . n 
A 1 126 VAL 126 127 127 VAL VAL A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 TYR 128 129 129 TYR TYR A . n 
A 1 129 LEU 129 130 130 LEU LEU A . n 
A 1 130 HIS 130 131 131 HIS HIS A . n 
A 1 131 SER 131 132 132 SER SER A . n 
A 1 132 LEU 132 133 133 LEU LEU A . n 
A 1 133 GLN 133 134 134 GLN GLN A . n 
A 1 134 ILE 134 135 135 ILE ILE A . n 
A 1 135 ALA 135 136 136 ALA ALA A . n 
A 1 136 HIS 136 137 137 HIS HIS A . n 
A 1 137 PHE 137 138 138 PHE PHE A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 LEU 139 140 140 LEU LEU A . n 
A 1 140 LYS 140 141 141 LYS LYS A . n 
A 1 141 PRO 141 142 142 PRO PRO A . n 
A 1 142 GLU 142 143 143 GLU GLU A . n 
A 1 143 ASN 143 144 144 ASN ASN A . n 
A 1 144 ILE 144 145 145 ILE ILE A . n 
A 1 145 MET 145 146 146 MET MET A . n 
A 1 146 LEU 146 147 147 LEU LEU A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 ASP 148 149 149 ASP ASP A . n 
A 1 149 ARG 149 150 150 ARG ARG A . n 
A 1 150 ASN 150 151 151 ASN ASN A . n 
A 1 151 VAL 151 152 152 VAL VAL A . n 
A 1 152 PRO 152 153 153 PRO PRO A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 ARG 155 156 156 ARG ARG A . n 
A 1 156 ILE 156 157 157 ILE ILE A . n 
A 1 157 LYS 157 158 158 LYS LYS A . n 
A 1 158 ILE 158 159 159 ILE ILE A . n 
A 1 159 ILE 159 160 160 ILE ILE A . n 
A 1 160 ASP 160 161 161 ASP ASP A . n 
A 1 161 PHE 161 162 162 PHE PHE A . n 
A 1 162 GLY 162 163 163 GLY GLY A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ALA 164 165 165 ALA ALA A . n 
A 1 165 HIS 165 166 166 HIS HIS A . n 
A 1 166 LYS 166 167 167 LYS LYS A . n 
A 1 167 ILE 167 168 168 ILE ILE A . n 
A 1 168 ASP 168 169 169 ASP ASP A . n 
A 1 169 PHE 169 170 170 PHE PHE A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 ASN 171 172 172 ASN ASN A . n 
A 1 172 GLU 172 173 173 GLU GLU A . n 
A 1 173 PHE 173 174 174 PHE PHE A . n 
A 1 174 LYS 174 175 175 LYS LYS A . n 
A 1 175 ASN 175 176 176 ASN ASN A . n 
A 1 176 ILE 176 177 177 ILE ILE A . n 
A 1 177 PHE 177 178 178 PHE PHE A . n 
A 1 178 GLY 178 179 179 GLY GLY A . n 
A 1 179 THR 179 180 180 THR THR A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 GLU 181 182 182 GLU GLU A . n 
A 1 182 PHE 182 183 183 PHE PHE A . n 
A 1 183 VAL 183 184 184 VAL VAL A . n 
A 1 184 ALA 184 185 185 ALA ALA A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 ILE 187 188 188 ILE ILE A . n 
A 1 188 VAL 188 189 189 VAL VAL A . n 
A 1 189 ASN 189 190 190 ASN ASN A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 GLU 191 192 192 GLU GLU A . n 
A 1 192 PRO 192 193 193 PRO PRO A . n 
A 1 193 LEU 193 194 194 LEU LEU A . n 
A 1 194 GLY 194 195 195 GLY GLY A . n 
A 1 195 LEU 195 196 196 LEU LEU A . n 
A 1 196 GLU 196 197 197 GLU GLU A . n 
A 1 197 ALA 197 198 198 ALA ALA A . n 
A 1 198 ASP 198 199 199 ASP ASP A . n 
A 1 199 MET 199 200 200 MET MET A . n 
A 1 200 TRP 200 201 201 TRP TRP A . n 
A 1 201 SER 201 202 202 SER SER A . n 
A 1 202 ILE 202 203 203 ILE ILE A . n 
A 1 203 GLY 203 204 204 GLY GLY A . n 
A 1 204 VAL 204 205 205 VAL VAL A . n 
A 1 205 ILE 205 206 206 ILE ILE A . n 
A 1 206 THR 206 207 207 THR THR A . n 
A 1 207 TYR 207 208 208 TYR TYR A . n 
A 1 208 ILE 208 209 209 ILE ILE A . n 
A 1 209 LEU 209 210 210 LEU LEU A . n 
A 1 210 LEU 210 211 211 LEU LEU A . n 
A 1 211 SER 211 212 212 SER SER A . n 
A 1 212 GLY 212 213 213 GLY GLY A . n 
A 1 213 ALA 213 214 214 ALA ALA A . n 
A 1 214 SER 214 215 215 SER SER A . n 
A 1 215 PRO 215 216 216 PRO PRO A . n 
A 1 216 PHE 216 217 217 PHE PHE A . n 
A 1 217 LEU 217 218 218 LEU LEU A . n 
A 1 218 GLY 218 219 219 GLY GLY A . n 
A 1 219 ASP 219 220 220 ASP ASP A . n 
A 1 220 THR 220 221 221 THR THR A . n 
A 1 221 LYS 221 222 222 LYS LYS A . n 
A 1 222 GLN 222 223 223 GLN GLN A . n 
A 1 223 GLU 223 224 224 GLU GLU A . n 
A 1 224 THR 224 225 225 THR THR A . n 
A 1 225 LEU 225 226 226 LEU LEU A . n 
A 1 226 ALA 226 227 227 ALA ALA A . n 
A 1 227 ASN 227 228 228 ASN ASN A . n 
A 1 228 VAL 228 229 229 VAL VAL A . n 
A 1 229 SER 229 230 230 SER SER A . n 
A 1 230 ALA 230 231 231 ALA ALA A . n 
A 1 231 VAL 231 232 232 VAL VAL A . n 
A 1 232 ASN 232 233 233 ASN ASN A . n 
A 1 233 TYR 233 234 234 TYR TYR A . n 
A 1 234 GLU 234 235 235 GLU GLU A . n 
A 1 235 PHE 235 236 236 PHE PHE A . n 
A 1 236 GLU 236 237 237 GLU GLU A . n 
A 1 237 ASP 237 238 238 ASP ASP A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 TYR 239 240 240 TYR TYR A . n 
A 1 240 PHE 240 241 241 PHE PHE A . n 
A 1 241 SER 241 242 242 SER SER A . n 
A 1 242 ASN 242 243 243 ASN ASN A . n 
A 1 243 THR 243 244 244 THR THR A . n 
A 1 244 SER 244 245 245 SER SER A . n 
A 1 245 ALA 245 246 246 ALA ALA A . n 
A 1 246 LEU 246 247 247 LEU LEU A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 LYS 248 249 249 LYS LYS A . n 
A 1 249 ASP 249 250 250 ASP ASP A . n 
A 1 250 PHE 250 251 251 PHE PHE A . n 
A 1 251 ILE 251 252 252 ILE ILE A . n 
A 1 252 ARG 252 253 253 ARG ARG A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 LEU 254 255 255 LEU LEU A . n 
A 1 255 LEU 255 256 256 LEU LEU A . n 
A 1 256 VAL 256 257 257 VAL VAL A . n 
A 1 257 LYS 257 258 258 LYS LYS A . n 
A 1 258 ASP 258 259 259 ASP ASP A . n 
A 1 259 PRO 259 260 260 PRO PRO A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
A 1 261 LYS 261 262 262 LYS LYS A . n 
A 1 262 ARG 262 263 263 ARG ARG A . n 
A 1 263 MET 263 264 264 MET MET A . n 
A 1 264 THR 264 265 265 THR THR A . n 
A 1 265 ILE 265 266 266 ILE ILE A . n 
A 1 266 GLN 266 267 267 GLN GLN A . n 
A 1 267 ASP 267 268 268 ASP ASP A . n 
A 1 268 SER 268 269 269 SER SER A . n 
A 1 269 LEU 269 270 270 LEU LEU A . n 
A 1 270 GLN 270 271 271 GLN GLN A . n 
A 1 271 HIS 271 272 272 HIS HIS A . n 
A 1 272 PRO 272 273 273 PRO PRO A . n 
A 1 273 TRP 273 274 274 TRP TRP A . n 
A 1 274 ILE 274 275 275 ILE ILE A . n 
A 1 275 LYS 275 276 276 LYS LYS A . n 
A 1 276 PRO 276 277 277 PRO PRO A . n 
A 1 277 LYS 277 278 ?   ?   ?   A . n 
A 1 278 ASP 278 279 ?   ?   ?   A . n 
A 1 279 THR 279 280 ?   ?   ?   A . n 
A 1 280 GLN 280 281 ?   ?   ?   A . n 
A 1 281 GLN 281 282 ?   ?   ?   A . n 
A 1 282 ALA 282 283 ?   ?   ?   A . n 
A 1 283 LEU 283 284 ?   ?   ?   A . n 
A 1 284 SER 284 285 ?   ?   ?   A . n 
A 1 285 SER 285 286 ?   ?   ?   A . n 
A 1 286 ALA 286 287 ?   ?   ?   A . n 
A 1 287 TRP 287 288 ?   ?   ?   A . n 
A 1 288 SER 288 289 ?   ?   ?   A . n 
A 1 289 HIS 289 290 ?   ?   ?   A . n 
A 1 290 PRO 290 291 291 PRO PRO A . n 
A 1 291 GLN 291 292 292 GLN GLN A . n 
A 1 292 PHE 292 293 293 PHE PHE A . n 
A 1 293 GLU 293 294 294 GLU GLU A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 SO4   1   301 1   SO4   SO4 A . 
C 3 A1BVM 1   302 301 A1BVM D22 A . 
D 4 HOH   1   401 56  HOH   HOH A . 
D 4 HOH   2   402 263 HOH   HOH A . 
D 4 HOH   3   403 99  HOH   HOH A . 
D 4 HOH   4   404 96  HOH   HOH A . 
D 4 HOH   5   405 130 HOH   HOH A . 
D 4 HOH   6   406 256 HOH   HOH A . 
D 4 HOH   7   407 182 HOH   HOH A . 
D 4 HOH   8   408 184 HOH   HOH A . 
D 4 HOH   9   409 271 HOH   HOH A . 
D 4 HOH   10  410 123 HOH   HOH A . 
D 4 HOH   11  411 266 HOH   HOH A . 
D 4 HOH   12  412 76  HOH   HOH A . 
D 4 HOH   13  413 64  HOH   HOH A . 
D 4 HOH   14  414 258 HOH   HOH A . 
D 4 HOH   15  415 277 HOH   HOH A . 
D 4 HOH   16  416 177 HOH   HOH A . 
D 4 HOH   17  417 77  HOH   HOH A . 
D 4 HOH   18  418 249 HOH   HOH A . 
D 4 HOH   19  419 151 HOH   HOH A . 
D 4 HOH   20  420 111 HOH   HOH A . 
D 4 HOH   21  421 38  HOH   HOH A . 
D 4 HOH   22  422 138 HOH   HOH A . 
D 4 HOH   23  423 27  HOH   HOH A . 
D 4 HOH   24  424 51  HOH   HOH A . 
D 4 HOH   25  425 174 HOH   HOH A . 
D 4 HOH   26  426 18  HOH   HOH A . 
D 4 HOH   27  427 59  HOH   HOH A . 
D 4 HOH   28  428 145 HOH   HOH A . 
D 4 HOH   29  429 23  HOH   HOH A . 
D 4 HOH   30  430 16  HOH   HOH A . 
D 4 HOH   31  431 124 HOH   HOH A . 
D 4 HOH   32  432 53  HOH   HOH A . 
D 4 HOH   33  433 269 HOH   HOH A . 
D 4 HOH   34  434 211 HOH   HOH A . 
D 4 HOH   35  435 35  HOH   HOH A . 
D 4 HOH   36  436 172 HOH   HOH A . 
D 4 HOH   37  437 268 HOH   HOH A . 
D 4 HOH   38  438 131 HOH   HOH A . 
D 4 HOH   39  439 83  HOH   HOH A . 
D 4 HOH   40  440 229 HOH   HOH A . 
D 4 HOH   41  441 252 HOH   HOH A . 
D 4 HOH   42  442 216 HOH   HOH A . 
D 4 HOH   43  443 69  HOH   HOH A . 
D 4 HOH   44  444 36  HOH   HOH A . 
D 4 HOH   45  445 255 HOH   HOH A . 
D 4 HOH   46  446 197 HOH   HOH A . 
D 4 HOH   47  447 203 HOH   HOH A . 
D 4 HOH   48  448 201 HOH   HOH A . 
D 4 HOH   49  449 45  HOH   HOH A . 
D 4 HOH   50  450 141 HOH   HOH A . 
D 4 HOH   51  451 117 HOH   HOH A . 
D 4 HOH   52  452 91  HOH   HOH A . 
D 4 HOH   53  453 267 HOH   HOH A . 
D 4 HOH   54  454 100 HOH   HOH A . 
D 4 HOH   55  455 227 HOH   HOH A . 
D 4 HOH   56  456 14  HOH   HOH A . 
D 4 HOH   57  457 21  HOH   HOH A . 
D 4 HOH   58  458 65  HOH   HOH A . 
D 4 HOH   59  459 5   HOH   HOH A . 
D 4 HOH   60  460 25  HOH   HOH A . 
D 4 HOH   61  461 210 HOH   HOH A . 
D 4 HOH   62  462 12  HOH   HOH A . 
D 4 HOH   63  463 19  HOH   HOH A . 
D 4 HOH   64  464 270 HOH   HOH A . 
D 4 HOH   65  465 180 HOH   HOH A . 
D 4 HOH   66  466 40  HOH   HOH A . 
D 4 HOH   67  467 101 HOH   HOH A . 
D 4 HOH   68  468 162 HOH   HOH A . 
D 4 HOH   69  469 144 HOH   HOH A . 
D 4 HOH   70  470 70  HOH   HOH A . 
D 4 HOH   71  471 260 HOH   HOH A . 
D 4 HOH   72  472 71  HOH   HOH A . 
D 4 HOH   73  473 106 HOH   HOH A . 
D 4 HOH   74  474 11  HOH   HOH A . 
D 4 HOH   75  475 254 HOH   HOH A . 
D 4 HOH   76  476 31  HOH   HOH A . 
D 4 HOH   77  477 1   HOH   HOH A . 
D 4 HOH   78  478 13  HOH   HOH A . 
D 4 HOH   79  479 118 HOH   HOH A . 
D 4 HOH   80  480 208 HOH   HOH A . 
D 4 HOH   81  481 82  HOH   HOH A . 
D 4 HOH   82  482 61  HOH   HOH A . 
D 4 HOH   83  483 29  HOH   HOH A . 
D 4 HOH   84  484 159 HOH   HOH A . 
D 4 HOH   85  485 169 HOH   HOH A . 
D 4 HOH   86  486 220 HOH   HOH A . 
D 4 HOH   87  487 48  HOH   HOH A . 
D 4 HOH   88  488 33  HOH   HOH A . 
D 4 HOH   89  489 6   HOH   HOH A . 
D 4 HOH   90  490 94  HOH   HOH A . 
D 4 HOH   91  491 134 HOH   HOH A . 
D 4 HOH   92  492 44  HOH   HOH A . 
D 4 HOH   93  493 264 HOH   HOH A . 
D 4 HOH   94  494 223 HOH   HOH A . 
D 4 HOH   95  495 175 HOH   HOH A . 
D 4 HOH   96  496 152 HOH   HOH A . 
D 4 HOH   97  497 128 HOH   HOH A . 
D 4 HOH   98  498 248 HOH   HOH A . 
D 4 HOH   99  499 2   HOH   HOH A . 
D 4 HOH   100 500 50  HOH   HOH A . 
D 4 HOH   101 501 78  HOH   HOH A . 
D 4 HOH   102 502 39  HOH   HOH A . 
D 4 HOH   103 503 9   HOH   HOH A . 
D 4 HOH   104 504 171 HOH   HOH A . 
D 4 HOH   105 505 7   HOH   HOH A . 
D 4 HOH   106 506 60  HOH   HOH A . 
D 4 HOH   107 507 81  HOH   HOH A . 
D 4 HOH   108 508 191 HOH   HOH A . 
D 4 HOH   109 509 165 HOH   HOH A . 
D 4 HOH   110 510 185 HOH   HOH A . 
D 4 HOH   111 511 115 HOH   HOH A . 
D 4 HOH   112 512 129 HOH   HOH A . 
D 4 HOH   113 513 132 HOH   HOH A . 
D 4 HOH   114 514 26  HOH   HOH A . 
D 4 HOH   115 515 55  HOH   HOH A . 
D 4 HOH   116 516 47  HOH   HOH A . 
D 4 HOH   117 517 157 HOH   HOH A . 
D 4 HOH   118 518 66  HOH   HOH A . 
D 4 HOH   119 519 190 HOH   HOH A . 
D 4 HOH   120 520 215 HOH   HOH A . 
D 4 HOH   121 521 28  HOH   HOH A . 
D 4 HOH   122 522 57  HOH   HOH A . 
D 4 HOH   123 523 24  HOH   HOH A . 
D 4 HOH   124 524 74  HOH   HOH A . 
D 4 HOH   125 525 265 HOH   HOH A . 
D 4 HOH   126 526 15  HOH   HOH A . 
D 4 HOH   127 527 116 HOH   HOH A . 
D 4 HOH   128 528 113 HOH   HOH A . 
D 4 HOH   129 529 73  HOH   HOH A . 
D 4 HOH   130 530 52  HOH   HOH A . 
D 4 HOH   131 531 49  HOH   HOH A . 
D 4 HOH   132 532 68  HOH   HOH A . 
D 4 HOH   133 533 42  HOH   HOH A . 
D 4 HOH   134 534 173 HOH   HOH A . 
D 4 HOH   135 535 46  HOH   HOH A . 
D 4 HOH   136 536 212 HOH   HOH A . 
D 4 HOH   137 537 41  HOH   HOH A . 
D 4 HOH   138 538 156 HOH   HOH A . 
D 4 HOH   139 539 119 HOH   HOH A . 
D 4 HOH   140 540 110 HOH   HOH A . 
D 4 HOH   141 541 92  HOH   HOH A . 
D 4 HOH   142 542 168 HOH   HOH A . 
D 4 HOH   143 543 143 HOH   HOH A . 
D 4 HOH   144 544 103 HOH   HOH A . 
D 4 HOH   145 545 3   HOH   HOH A . 
D 4 HOH   146 546 4   HOH   HOH A . 
D 4 HOH   147 547 108 HOH   HOH A . 
D 4 HOH   148 548 37  HOH   HOH A . 
D 4 HOH   149 549 205 HOH   HOH A . 
D 4 HOH   150 550 84  HOH   HOH A . 
D 4 HOH   151 551 219 HOH   HOH A . 
D 4 HOH   152 552 109 HOH   HOH A . 
D 4 HOH   153 553 181 HOH   HOH A . 
D 4 HOH   154 554 104 HOH   HOH A . 
D 4 HOH   155 555 253 HOH   HOH A . 
D 4 HOH   156 556 192 HOH   HOH A . 
D 4 HOH   157 557 32  HOH   HOH A . 
D 4 HOH   158 558 98  HOH   HOH A . 
D 4 HOH   159 559 207 HOH   HOH A . 
D 4 HOH   160 560 149 HOH   HOH A . 
D 4 HOH   161 561 95  HOH   HOH A . 
D 4 HOH   162 562 107 HOH   HOH A . 
D 4 HOH   163 563 125 HOH   HOH A . 
D 4 HOH   164 564 167 HOH   HOH A . 
D 4 HOH   165 565 250 HOH   HOH A . 
D 4 HOH   166 566 257 HOH   HOH A . 
D 4 HOH   167 567 97  HOH   HOH A . 
D 4 HOH   168 568 62  HOH   HOH A . 
D 4 HOH   169 569 274 HOH   HOH A . 
D 4 HOH   170 570 20  HOH   HOH A . 
D 4 HOH   171 571 105 HOH   HOH A . 
D 4 HOH   172 572 79  HOH   HOH A . 
D 4 HOH   173 573 34  HOH   HOH A . 
D 4 HOH   174 574 214 HOH   HOH A . 
D 4 HOH   175 575 90  HOH   HOH A . 
D 4 HOH   176 576 72  HOH   HOH A . 
D 4 HOH   177 577 114 HOH   HOH A . 
D 4 HOH   178 578 112 HOH   HOH A . 
D 4 HOH   179 579 88  HOH   HOH A . 
D 4 HOH   180 580 276 HOH   HOH A . 
D 4 HOH   181 581 272 HOH   HOH A . 
D 4 HOH   182 582 176 HOH   HOH A . 
D 4 HOH   183 583 67  HOH   HOH A . 
D 4 HOH   184 584 17  HOH   HOH A . 
D 4 HOH   185 585 137 HOH   HOH A . 
D 4 HOH   186 586 179 HOH   HOH A . 
D 4 HOH   187 587 231 HOH   HOH A . 
D 4 HOH   188 588 193 HOH   HOH A . 
D 4 HOH   189 589 30  HOH   HOH A . 
D 4 HOH   190 590 199 HOH   HOH A . 
D 4 HOH   191 591 261 HOH   HOH A . 
D 4 HOH   192 592 178 HOH   HOH A . 
D 4 HOH   193 593 122 HOH   HOH A . 
D 4 HOH   194 594 136 HOH   HOH A . 
D 4 HOH   195 595 75  HOH   HOH A . 
D 4 HOH   196 596 58  HOH   HOH A . 
D 4 HOH   197 597 224 HOH   HOH A . 
D 4 HOH   198 598 273 HOH   HOH A . 
D 4 HOH   199 599 198 HOH   HOH A . 
D 4 HOH   200 600 8   HOH   HOH A . 
D 4 HOH   201 601 234 HOH   HOH A . 
D 4 HOH   202 602 236 HOH   HOH A . 
D 4 HOH   203 603 239 HOH   HOH A . 
D 4 HOH   204 604 204 HOH   HOH A . 
D 4 HOH   205 605 235 HOH   HOH A . 
D 4 HOH   206 606 259 HOH   HOH A . 
D 4 HOH   207 607 237 HOH   HOH A . 
D 4 HOH   208 608 80  HOH   HOH A . 
D 4 HOH   209 609 54  HOH   HOH A . 
D 4 HOH   210 610 121 HOH   HOH A . 
D 4 HOH   211 611 154 HOH   HOH A . 
D 4 HOH   212 612 213 HOH   HOH A . 
D 4 HOH   213 613 232 HOH   HOH A . 
D 4 HOH   214 614 170 HOH   HOH A . 
D 4 HOH   215 615 244 HOH   HOH A . 
D 4 HOH   216 616 85  HOH   HOH A . 
D 4 HOH   217 617 153 HOH   HOH A . 
D 4 HOH   218 618 147 HOH   HOH A . 
D 4 HOH   219 619 206 HOH   HOH A . 
D 4 HOH   220 620 161 HOH   HOH A . 
D 4 HOH   221 621 86  HOH   HOH A . 
D 4 HOH   222 622 10  HOH   HOH A . 
D 4 HOH   223 623 251 HOH   HOH A . 
D 4 HOH   224 624 233 HOH   HOH A . 
D 4 HOH   225 625 139 HOH   HOH A . 
D 4 HOH   226 626 120 HOH   HOH A . 
D 4 HOH   227 627 262 HOH   HOH A . 
D 4 HOH   228 628 238 HOH   HOH A . 
D 4 HOH   229 629 228 HOH   HOH A . 
D 4 HOH   230 630 89  HOH   HOH A . 
D 4 HOH   231 631 240 HOH   HOH A . 
D 4 HOH   232 632 160 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.8                2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? .                    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                     9N2M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.300 
_cell.length_a_esd                 ? 
_cell.length_b                     63.080 
_cell.length_b_esd                 ? 
_cell.length_c                     88.120 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9N2M 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9N2M 
_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             1.95 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.08 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '2M LiSO4, 5% DMSO' 
_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                      'Bi-morph KB' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-07-07 
_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                    'DCM Si 111' 
_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   1.12705 
_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                        'APS BEAMLINE 21-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.12705 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9N2M 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.35 
_reflns.d_resolution_low                               32.24 
_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                                     57668 
_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                           98.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.96 
_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                                0.062 
_reflns.pdbx_Rpim_I_all                                0.023 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       417722 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.057 
_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                                    1.35 
_reflns_shell.d_res_low                                     1.39 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           29308 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4079 
_reflns_shell.percent_possible_obs                          95.6 
_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                               7.2 
_reflns_shell.pdbx_chi_squared                              0.86 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     5.6 
_reflns_shell.pdbx_Rrim_I_all                               0.349 
_reflns_shell.pdbx_Rpim_I_all                               0.127 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.960 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.324 
_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                                 9N2M 
_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                            1.35 
_refine.ls_d_res_low                             31.54 
_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                     57605 
_refine.ls_number_reflns_R_free                  2855 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.35 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1461 
_refine.ls_R_factor_R_free                       0.1768 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1444 
_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                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          SIR 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            Random 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_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                 15.70 
_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                            0.10 
_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.pdbx_number_atoms_protein        2274 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             232 
_refine_hist.number_atoms_total               2535 
_refine_hist.d_res_high                       1.35 
_refine_hist.d_res_low                        31.54 
# 
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' ? 0.009 ? 2431 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.088 ? 3302 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.685 ? 351  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.094 ? 367  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010 ? 442  ? 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' 1.35 1.37  . . 124 2630 95.00  . . . . 0.1426 . . . . . . . . . . . 0.2058 
'X-RAY DIFFRACTION' 1.37 1.40  . . 140 2626 96.00  . . . . 0.1325 . . . . . . . . . . . 0.1808 
'X-RAY DIFFRACTION' 1.40 1.43  . . 146 2659 97.00  . . . . 0.1250 . . . . . . . . . . . 0.2092 
'X-RAY DIFFRACTION' 1.43 1.45  . . 133 2685 98.00  . . . . 0.1259 . . . . . . . . . . . 0.1627 
'X-RAY DIFFRACTION' 1.45 1.49  . . 152 2687 97.00  . . . . 0.1186 . . . . . . . . . . . 0.1649 
'X-RAY DIFFRACTION' 1.49 1.52  . . 135 2723 99.00  . . . . 0.1170 . . . . . . . . . . . 0.1705 
'X-RAY DIFFRACTION' 1.52 1.56  . . 134 2731 99.00  . . . . 0.1195 . . . . . . . . . . . 0.1831 
'X-RAY DIFFRACTION' 1.56 1.60  . . 153 2705 99.00  . . . . 0.1150 . . . . . . . . . . . 0.1819 
'X-RAY DIFFRACTION' 1.60 1.65  . . 152 2707 99.00  . . . . 0.1177 . . . . . . . . . . . 0.1641 
'X-RAY DIFFRACTION' 1.65 1.70  . . 129 2735 98.00  . . . . 0.1220 . . . . . . . . . . . 0.1586 
'X-RAY DIFFRACTION' 1.70 1.76  . . 153 2745 99.00  . . . . 0.1253 . . . . . . . . . . . 0.1653 
'X-RAY DIFFRACTION' 1.76 1.83  . . 151 2757 100.00 . . . . 0.1337 . . . . . . . . . . . 0.1785 
'X-RAY DIFFRACTION' 1.83 1.92  . . 153 2754 100.00 . . . . 0.1304 . . . . . . . . . . . 0.1579 
'X-RAY DIFFRACTION' 1.92 2.02  . . 141 2764 100.00 . . . . 0.1288 . . . . . . . . . . . 0.1673 
'X-RAY DIFFRACTION' 2.02 2.14  . . 126 2815 100.00 . . . . 0.1304 . . . . . . . . . . . 0.1409 
'X-RAY DIFFRACTION' 2.14 2.31  . . 143 2782 100.00 . . . . 0.1381 . . . . . . . . . . . 0.1783 
'X-RAY DIFFRACTION' 2.31 2.54  . . 155 2810 100.00 . . . . 0.1472 . . . . . . . . . . . 0.1850 
'X-RAY DIFFRACTION' 2.54 2.91  . . 111 2781 98.00  . . . . 0.1642 . . . . . . . . . . . 0.1915 
'X-RAY DIFFRACTION' 2.91 3.66  . . 157 2860 100.00 . . . . 0.1577 . . . . . . . . . . . 0.1800 
'X-RAY DIFFRACTION' 3.66 31.54 . . 167 2794 94.00  . . . . 0.1598 . . . . . . . . . . . 0.1820 
# 
_struct.entry_id                     9N2M 
_struct.title                        'Crystal Structure of Human DAPK1 Catalytic Subunit Complexed with Compound MW01-30-047SRM' 
_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        9N2M 
_struct_keywords.text            'DAPK1, DAPK1 catalytic subunit, MW01-30-047SRM, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DAPK1_HUMAN 
_struct_ref.pdbx_db_accession          P53355 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TVFRQENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHE
VYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIID
FGLAHKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYF
SNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWIKPKDTQQALS
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9N2M 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 284 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P53355 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  285 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       285 
# 
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 9N2M SER A 285 ? UNP P53355 ? ? 'expression tag' 286 1 
1 9N2M ALA A 286 ? UNP P53355 ? ? 'expression tag' 287 2 
1 9N2M TRP A 287 ? UNP P53355 ? ? 'expression tag' 288 3 
1 9N2M SER A 288 ? UNP P53355 ? ? 'expression tag' 289 4 
1 9N2M HIS A 289 ? UNP P53355 ? ? 'expression tag' 290 5 
1 9N2M PRO A 290 ? UNP P53355 ? ? 'expression tag' 291 6 
1 9N2M GLN A 291 ? UNP P53355 ? ? 'expression tag' 292 7 
1 9N2M PHE A 292 ? UNP P53355 ? ? 'expression tag' 293 8 
1 9N2M GLU A 293 ? UNP P53355 ? ? 'expression tag' 294 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PQS 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 ASN A 7   ? ASP A 10  ? ASN A 8   ASP A 11  5 ? 4  
HELX_P HELX_P2  AA2 SER A 56  ? ILE A 70  ? SER A 57  ILE A 71  1 ? 15 
HELX_P HELX_P3  AA3 GLU A 99  ? GLU A 108 ? GLU A 100 GLU A 109 1 ? 10 
HELX_P HELX_P4  AA4 THR A 111 ? LEU A 132 ? THR A 112 LEU A 133 1 ? 22 
HELX_P HELX_P5  AA5 LYS A 140 ? GLU A 142 ? LYS A 141 GLU A 143 5 ? 3  
HELX_P HELX_P6  AA6 THR A 179 ? VAL A 183 ? THR A 180 VAL A 184 5 ? 5  
HELX_P HELX_P7  AA7 ALA A 184 ? ASN A 189 ? ALA A 185 ASN A 190 1 ? 6  
HELX_P HELX_P8  AA8 LEU A 195 ? GLY A 212 ? LEU A 196 GLY A 213 1 ? 18 
HELX_P HELX_P9  AA9 THR A 220 ? ALA A 230 ? THR A 221 ALA A 231 1 ? 11 
HELX_P HELX_P10 AB1 GLU A 236 ? SER A 241 ? GLU A 237 SER A 242 1 ? 6  
HELX_P HELX_P11 AB2 SER A 244 ? LEU A 255 ? SER A 245 LEU A 256 1 ? 12 
HELX_P HELX_P12 AB3 ASP A 258 ? ARG A 262 ? ASP A 259 ARG A 263 5 ? 5  
HELX_P HELX_P13 AB4 THR A 264 ? HIS A 271 ? THR A 265 HIS A 272 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 12  ? LEU A 18  ? TYR A 13  LEU A 19  
AA1 2 ALA A 24  ? GLU A 31  ? ALA A 25  GLU A 32  
AA1 3 GLN A 37  ? LYS A 44  ? GLN A 38  LYS A 45  
AA1 4 ASP A 87  ? GLU A 93  ? ASP A 88  GLU A 94  
AA1 5 LEU A 78  ? GLU A 83  ? LEU A 79  GLU A 84  
AA2 1 ILE A 134 ? ALA A 135 ? ILE A 135 ALA A 136 
AA2 2 HIS A 165 ? LYS A 166 ? HIS A 166 LYS A 167 
AA3 1 ILE A 144 ? LEU A 146 ? ILE A 145 LEU A 147 
AA3 2 ILE A 156 ? ILE A 158 ? ILE A 157 ILE A 159 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLU A 16  ? N GLU A 17  O LYS A 28  ? O LYS A 29  
AA1 2 3 N LYS A 27  ? N LYS A 28  O ALA A 40  ? O ALA A 41  
AA1 3 4 N ILE A 43  ? N ILE A 44  O VAL A 88  ? O VAL A 89  
AA1 4 5 O ILE A 89  ? O ILE A 90  N TYR A 82  ? N TYR A 83  
AA2 1 2 N ALA A 135 ? N ALA A 136 O HIS A 165 ? O HIS A 166 
AA3 1 2 N MET A 145 ? N MET A 146 O LYS A 157 ? O LYS A 158 
# 
_pdbx_entry_details.entry_id                   9N2M 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 51  ? ? -93.68  30.38   
2 1 GLU A 109 ? ? 75.82   -67.84  
3 1 ASP A 139 ? ? -145.67 37.91   
4 1 ASP A 161 ? A 52.35   87.35   
5 1 ASP A 161 ? B 64.66   85.99   
6 1 LYS A 175 ? ? -159.29 -157.53 
# 
_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                       632 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.95 
_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 LYS 278 ? A LYS 277 
2  1 Y 1 A ASP 279 ? A ASP 278 
3  1 Y 1 A THR 280 ? A THR 279 
4  1 Y 1 A GLN 281 ? A GLN 280 
5  1 Y 1 A GLN 282 ? A GLN 281 
6  1 Y 1 A ALA 283 ? A ALA 282 
7  1 Y 1 A LEU 284 ? A LEU 283 
8  1 Y 1 A SER 285 ? A SER 284 
9  1 Y 1 A SER 286 ? A SER 285 
10 1 Y 1 A ALA 287 ? A ALA 286 
11 1 Y 1 A TRP 288 ? A TRP 287 
12 1 Y 1 A SER 289 ? A SER 288 
13 1 Y 1 A HIS 290 ? A HIS 289 
# 
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 
A1BVM C2   C Y N 1   
A1BVM C3   C Y N 2   
A1BVM C4   C N N 3   
A1BVM C5   C N N 4   
A1BVM C6   C Y N 5   
A1BVM C7   C Y N 6   
A1BVM C8   C Y N 7   
A1BVM C10  C Y N 8   
A1BVM C17  C Y N 9   
A1BVM C16  C Y N 10  
A1BVM C15  C Y N 11  
A1BVM C14  C Y N 12  
A1BVM C13  C Y N 13  
A1BVM C12  C N N 14  
A1BVM C11  C N N 15  
A1BVM C1   C Y N 16  
A1BVM N    N N N 17  
A1BVM C    C Y N 18  
A1BVM C9   C Y N 19  
A1BVM N1   N N N 20  
A1BVM N2   N Y N 21  
A1BVM N3   N Y N 22  
A1BVM N4   N Y N 23  
A1BVM N5   N Y N 24  
A1BVM H1   H N N 25  
A1BVM H2   H N N 26  
A1BVM H3   H N N 27  
A1BVM H4   H N N 28  
A1BVM H5   H N N 29  
A1BVM H6   H N N 30  
A1BVM H7   H N N 31  
A1BVM H8   H N N 32  
A1BVM H9   H N N 33  
A1BVM H10  H N N 34  
A1BVM H11  H N N 35  
A1BVM H12  H N N 36  
A1BVM H13  H N N 37  
A1BVM H14  H N N 38  
A1BVM H15  H N N 39  
A1BVM H16  H N N 40  
A1BVM H17  H N N 41  
A1BVM H18  H N N 42  
ALA   N    N N N 43  
ALA   CA   C N S 44  
ALA   C    C N N 45  
ALA   O    O N N 46  
ALA   CB   C N N 47  
ALA   OXT  O N N 48  
ALA   H    H N N 49  
ALA   H2   H N N 50  
ALA   HA   H N N 51  
ALA   HB1  H N N 52  
ALA   HB2  H N N 53  
ALA   HB3  H N N 54  
ALA   HXT  H N N 55  
ARG   N    N N N 56  
ARG   CA   C N S 57  
ARG   C    C N N 58  
ARG   O    O N N 59  
ARG   CB   C N N 60  
ARG   CG   C N N 61  
ARG   CD   C N N 62  
ARG   NE   N N N 63  
ARG   CZ   C N N 64  
ARG   NH1  N N N 65  
ARG   NH2  N N N 66  
ARG   OXT  O N N 67  
ARG   H    H N N 68  
ARG   H2   H N N 69  
ARG   HA   H N N 70  
ARG   HB2  H N N 71  
ARG   HB3  H N N 72  
ARG   HG2  H N N 73  
ARG   HG3  H N N 74  
ARG   HD2  H N N 75  
ARG   HD3  H N N 76  
ARG   HE   H N N 77  
ARG   HH11 H N N 78  
ARG   HH12 H N N 79  
ARG   HH21 H N N 80  
ARG   HH22 H N N 81  
ARG   HXT  H N N 82  
ASN   N    N N N 83  
ASN   CA   C N S 84  
ASN   C    C N N 85  
ASN   O    O N N 86  
ASN   CB   C N N 87  
ASN   CG   C N N 88  
ASN   OD1  O N N 89  
ASN   ND2  N N N 90  
ASN   OXT  O N N 91  
ASN   H    H N N 92  
ASN   H2   H N N 93  
ASN   HA   H N N 94  
ASN   HB2  H N N 95  
ASN   HB3  H N N 96  
ASN   HD21 H N N 97  
ASN   HD22 H N N 98  
ASN   HXT  H N N 99  
ASP   N    N N N 100 
ASP   CA   C N S 101 
ASP   C    C N N 102 
ASP   O    O N N 103 
ASP   CB   C N N 104 
ASP   CG   C N N 105 
ASP   OD1  O N N 106 
ASP   OD2  O N N 107 
ASP   OXT  O N N 108 
ASP   H    H N N 109 
ASP   H2   H N N 110 
ASP   HA   H N N 111 
ASP   HB2  H N N 112 
ASP   HB3  H N N 113 
ASP   HD2  H N N 114 
ASP   HXT  H N N 115 
CYS   N    N N N 116 
CYS   CA   C N R 117 
CYS   C    C N N 118 
CYS   O    O N N 119 
CYS   CB   C N N 120 
CYS   SG   S N N 121 
CYS   OXT  O N N 122 
CYS   H    H N N 123 
CYS   H2   H N N 124 
CYS   HA   H N N 125 
CYS   HB2  H N N 126 
CYS   HB3  H N N 127 
CYS   HG   H N N 128 
CYS   HXT  H N N 129 
GLN   N    N N N 130 
GLN   CA   C N S 131 
GLN   C    C N N 132 
GLN   O    O N N 133 
GLN   CB   C N N 134 
GLN   CG   C N N 135 
GLN   CD   C N N 136 
GLN   OE1  O N N 137 
GLN   NE2  N N N 138 
GLN   OXT  O N N 139 
GLN   H    H N N 140 
GLN   H2   H N N 141 
GLN   HA   H N N 142 
GLN   HB2  H N N 143 
GLN   HB3  H N N 144 
GLN   HG2  H N N 145 
GLN   HG3  H N N 146 
GLN   HE21 H N N 147 
GLN   HE22 H N N 148 
GLN   HXT  H N N 149 
GLU   N    N N N 150 
GLU   CA   C N S 151 
GLU   C    C N N 152 
GLU   O    O N N 153 
GLU   CB   C N N 154 
GLU   CG   C N N 155 
GLU   CD   C N N 156 
GLU   OE1  O N N 157 
GLU   OE2  O N N 158 
GLU   OXT  O N N 159 
GLU   H    H N N 160 
GLU   H2   H N N 161 
GLU   HA   H N N 162 
GLU   HB2  H N N 163 
GLU   HB3  H N N 164 
GLU   HG2  H N N 165 
GLU   HG3  H N N 166 
GLU   HE2  H N N 167 
GLU   HXT  H N N 168 
GLY   N    N N N 169 
GLY   CA   C N N 170 
GLY   C    C N N 171 
GLY   O    O N N 172 
GLY   OXT  O N N 173 
GLY   H    H N N 174 
GLY   H2   H N N 175 
GLY   HA2  H N N 176 
GLY   HA3  H N N 177 
GLY   HXT  H N N 178 
HIS   N    N N N 179 
HIS   CA   C N S 180 
HIS   C    C N N 181 
HIS   O    O N N 182 
HIS   CB   C N N 183 
HIS   CG   C Y N 184 
HIS   ND1  N Y N 185 
HIS   CD2  C Y N 186 
HIS   CE1  C Y N 187 
HIS   NE2  N Y N 188 
HIS   OXT  O N N 189 
HIS   H    H N N 190 
HIS   H2   H N N 191 
HIS   HA   H N N 192 
HIS   HB2  H N N 193 
HIS   HB3  H N N 194 
HIS   HD1  H N N 195 
HIS   HD2  H N N 196 
HIS   HE1  H N N 197 
HIS   HE2  H N N 198 
HIS   HXT  H N N 199 
HOH   O    O N N 200 
HOH   H1   H N N 201 
HOH   H2   H N N 202 
ILE   N    N N N 203 
ILE   CA   C N S 204 
ILE   C    C N N 205 
ILE   O    O N N 206 
ILE   CB   C N S 207 
ILE   CG1  C N N 208 
ILE   CG2  C N N 209 
ILE   CD1  C N N 210 
ILE   OXT  O N N 211 
ILE   H    H N N 212 
ILE   H2   H N N 213 
ILE   HA   H N N 214 
ILE   HB   H N N 215 
ILE   HG12 H N N 216 
ILE   HG13 H N N 217 
ILE   HG21 H N N 218 
ILE   HG22 H N N 219 
ILE   HG23 H N N 220 
ILE   HD11 H N N 221 
ILE   HD12 H N N 222 
ILE   HD13 H N N 223 
ILE   HXT  H N N 224 
LEU   N    N N N 225 
LEU   CA   C N S 226 
LEU   C    C N N 227 
LEU   O    O N N 228 
LEU   CB   C N N 229 
LEU   CG   C N N 230 
LEU   CD1  C N N 231 
LEU   CD2  C N N 232 
LEU   OXT  O N N 233 
LEU   H    H N N 234 
LEU   H2   H N N 235 
LEU   HA   H N N 236 
LEU   HB2  H N N 237 
LEU   HB3  H N N 238 
LEU   HG   H N N 239 
LEU   HD11 H N N 240 
LEU   HD12 H N N 241 
LEU   HD13 H N N 242 
LEU   HD21 H N N 243 
LEU   HD22 H N N 244 
LEU   HD23 H N N 245 
LEU   HXT  H N N 246 
LYS   N    N N N 247 
LYS   CA   C N S 248 
LYS   C    C N N 249 
LYS   O    O N N 250 
LYS   CB   C N N 251 
LYS   CG   C N N 252 
LYS   CD   C N N 253 
LYS   CE   C N N 254 
LYS   NZ   N N N 255 
LYS   OXT  O N N 256 
LYS   H    H N N 257 
LYS   H2   H N N 258 
LYS   HA   H N N 259 
LYS   HB2  H N N 260 
LYS   HB3  H N N 261 
LYS   HG2  H N N 262 
LYS   HG3  H N N 263 
LYS   HD2  H N N 264 
LYS   HD3  H N N 265 
LYS   HE2  H N N 266 
LYS   HE3  H N N 267 
LYS   HZ1  H N N 268 
LYS   HZ2  H N N 269 
LYS   HZ3  H N N 270 
LYS   HXT  H N N 271 
MET   N    N N N 272 
MET   CA   C N S 273 
MET   C    C N N 274 
MET   O    O N N 275 
MET   CB   C N N 276 
MET   CG   C N N 277 
MET   SD   S N N 278 
MET   CE   C N N 279 
MET   OXT  O N N 280 
MET   H    H N N 281 
MET   H2   H N N 282 
MET   HA   H N N 283 
MET   HB2  H N N 284 
MET   HB3  H N N 285 
MET   HG2  H N N 286 
MET   HG3  H N N 287 
MET   HE1  H N N 288 
MET   HE2  H N N 289 
MET   HE3  H N N 290 
MET   HXT  H N N 291 
PHE   N    N N N 292 
PHE   CA   C N S 293 
PHE   C    C N N 294 
PHE   O    O N N 295 
PHE   CB   C N N 296 
PHE   CG   C Y N 297 
PHE   CD1  C Y N 298 
PHE   CD2  C Y N 299 
PHE   CE1  C Y N 300 
PHE   CE2  C Y N 301 
PHE   CZ   C Y N 302 
PHE   OXT  O N N 303 
PHE   H    H N N 304 
PHE   H2   H N N 305 
PHE   HA   H N N 306 
PHE   HB2  H N N 307 
PHE   HB3  H N N 308 
PHE   HD1  H N N 309 
PHE   HD2  H N N 310 
PHE   HE1  H N N 311 
PHE   HE2  H N N 312 
PHE   HZ   H N N 313 
PHE   HXT  H N N 314 
PRO   N    N N N 315 
PRO   CA   C N S 316 
PRO   C    C N N 317 
PRO   O    O N N 318 
PRO   CB   C N N 319 
PRO   CG   C N N 320 
PRO   CD   C N N 321 
PRO   OXT  O N N 322 
PRO   H    H N N 323 
PRO   HA   H N N 324 
PRO   HB2  H N N 325 
PRO   HB3  H N N 326 
PRO   HG2  H N N 327 
PRO   HG3  H N N 328 
PRO   HD2  H N N 329 
PRO   HD3  H N N 330 
PRO   HXT  H N N 331 
SER   N    N N N 332 
SER   CA   C N S 333 
SER   C    C N N 334 
SER   O    O N N 335 
SER   CB   C N N 336 
SER   OG   O N N 337 
SER   OXT  O N N 338 
SER   H    H N N 339 
SER   H2   H N N 340 
SER   HA   H N N 341 
SER   HB2  H N N 342 
SER   HB3  H N N 343 
SER   HG   H N N 344 
SER   HXT  H N N 345 
SO4   S    S N N 346 
SO4   O1   O N N 347 
SO4   O2   O N N 348 
SO4   O3   O N N 349 
SO4   O4   O N N 350 
THR   N    N N N 351 
THR   CA   C N S 352 
THR   C    C N N 353 
THR   O    O N N 354 
THR   CB   C N R 355 
THR   OG1  O N N 356 
THR   CG2  C N N 357 
THR   OXT  O N N 358 
THR   H    H N N 359 
THR   H2   H N N 360 
THR   HA   H N N 361 
THR   HB   H N N 362 
THR   HG1  H N N 363 
THR   HG21 H N N 364 
THR   HG22 H N N 365 
THR   HG23 H N N 366 
THR   HXT  H N N 367 
TRP   N    N N N 368 
TRP   CA   C N S 369 
TRP   C    C N N 370 
TRP   O    O N N 371 
TRP   CB   C N N 372 
TRP   CG   C Y N 373 
TRP   CD1  C Y N 374 
TRP   CD2  C Y N 375 
TRP   NE1  N Y N 376 
TRP   CE2  C Y N 377 
TRP   CE3  C Y N 378 
TRP   CZ2  C Y N 379 
TRP   CZ3  C Y N 380 
TRP   CH2  C Y N 381 
TRP   OXT  O N N 382 
TRP   H    H N N 383 
TRP   H2   H N N 384 
TRP   HA   H N N 385 
TRP   HB2  H N N 386 
TRP   HB3  H N N 387 
TRP   HD1  H N N 388 
TRP   HE1  H N N 389 
TRP   HE3  H N N 390 
TRP   HZ2  H N N 391 
TRP   HZ3  H N N 392 
TRP   HH2  H N N 393 
TRP   HXT  H N N 394 
TYR   N    N N N 395 
TYR   CA   C N S 396 
TYR   C    C N N 397 
TYR   O    O N N 398 
TYR   CB   C N N 399 
TYR   CG   C Y N 400 
TYR   CD1  C Y N 401 
TYR   CD2  C Y N 402 
TYR   CE1  C Y N 403 
TYR   CE2  C Y N 404 
TYR   CZ   C Y N 405 
TYR   OH   O N N 406 
TYR   OXT  O N N 407 
TYR   H    H N N 408 
TYR   H2   H N N 409 
TYR   HA   H N N 410 
TYR   HB2  H N N 411 
TYR   HB3  H N N 412 
TYR   HD1  H N N 413 
TYR   HD2  H N N 414 
TYR   HE1  H N N 415 
TYR   HE2  H N N 416 
TYR   HH   H N N 417 
TYR   HXT  H N N 418 
VAL   N    N N N 419 
VAL   CA   C N S 420 
VAL   C    C N N 421 
VAL   O    O N N 422 
VAL   CB   C N N 423 
VAL   CG1  C N N 424 
VAL   CG2  C N N 425 
VAL   OXT  O N N 426 
VAL   H    H N N 427 
VAL   H2   H N N 428 
VAL   HA   H N N 429 
VAL   HB   H N N 430 
VAL   HG11 H N N 431 
VAL   HG12 H N N 432 
VAL   HG13 H N N 433 
VAL   HG21 H N N 434 
VAL   HG22 H N N 435 
VAL   HG23 H N N 436 
VAL   HXT  H N N 437 
# 
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 
A1BVM C15 C14  doub Y N 1   
A1BVM C15 N5   sing Y N 2   
A1BVM C14 C    sing Y N 3   
A1BVM C13 N4   doub Y N 4   
A1BVM C13 C1   sing Y N 5   
A1BVM N4  N3   sing Y N 6   
A1BVM N5  C16  doub Y N 7   
A1BVM C   C1   sing N N 8   
A1BVM C   C17  doub Y N 9   
A1BVM C1  C2   doub Y N 10  
A1BVM N3  C3   doub Y N 11  
A1BVM C16 C17  sing Y N 12  
A1BVM C2  C3   sing Y N 13  
A1BVM C3  N    sing N N 14  
A1BVM N   C12  sing N N 15  
A1BVM N   C4   sing N N 16  
A1BVM C12 C11  sing N N 17  
A1BVM C4  C5   sing N N 18  
A1BVM C11 N1   sing N N 19  
A1BVM N1  C5   sing N N 20  
A1BVM N1  C6   sing N N 21  
A1BVM C6  C7   doub Y N 22  
A1BVM C6  C10  sing Y N 23  
A1BVM C7  C8   sing Y N 24  
A1BVM C10 C9   doub Y N 25  
A1BVM C8  N2   doub Y N 26  
A1BVM C9  N2   sing Y N 27  
A1BVM C2  H1   sing N N 28  
A1BVM C4  H2   sing N N 29  
A1BVM C4  H3   sing N N 30  
A1BVM C5  H4   sing N N 31  
A1BVM C5  H5   sing N N 32  
A1BVM C7  H6   sing N N 33  
A1BVM C8  H7   sing N N 34  
A1BVM C10 H8   sing N N 35  
A1BVM C17 H9   sing N N 36  
A1BVM C16 H10  sing N N 37  
A1BVM C15 H11  sing N N 38  
A1BVM C14 H12  sing N N 39  
A1BVM C13 H13  sing N N 40  
A1BVM C12 H14  sing N N 41  
A1BVM C12 H15  sing N N 42  
A1BVM C11 H16  sing N N 43  
A1BVM C11 H17  sing N N 44  
A1BVM C9  H18  sing N N 45  
ALA   N   CA   sing N N 46  
ALA   N   H    sing N N 47  
ALA   N   H2   sing N N 48  
ALA   CA  C    sing N N 49  
ALA   CA  CB   sing N N 50  
ALA   CA  HA   sing N N 51  
ALA   C   O    doub N N 52  
ALA   C   OXT  sing N N 53  
ALA   CB  HB1  sing N N 54  
ALA   CB  HB2  sing N N 55  
ALA   CB  HB3  sing N N 56  
ALA   OXT HXT  sing N N 57  
ARG   N   CA   sing N N 58  
ARG   N   H    sing N N 59  
ARG   N   H2   sing N N 60  
ARG   CA  C    sing N N 61  
ARG   CA  CB   sing N N 62  
ARG   CA  HA   sing N N 63  
ARG   C   O    doub N N 64  
ARG   C   OXT  sing N N 65  
ARG   CB  CG   sing N N 66  
ARG   CB  HB2  sing N N 67  
ARG   CB  HB3  sing N N 68  
ARG   CG  CD   sing N N 69  
ARG   CG  HG2  sing N N 70  
ARG   CG  HG3  sing N N 71  
ARG   CD  NE   sing N N 72  
ARG   CD  HD2  sing N N 73  
ARG   CD  HD3  sing N N 74  
ARG   NE  CZ   sing N N 75  
ARG   NE  HE   sing N N 76  
ARG   CZ  NH1  sing N N 77  
ARG   CZ  NH2  doub N N 78  
ARG   NH1 HH11 sing N N 79  
ARG   NH1 HH12 sing N N 80  
ARG   NH2 HH21 sing N N 81  
ARG   NH2 HH22 sing N N 82  
ARG   OXT HXT  sing N N 83  
ASN   N   CA   sing N N 84  
ASN   N   H    sing N N 85  
ASN   N   H2   sing N N 86  
ASN   CA  C    sing N N 87  
ASN   CA  CB   sing N N 88  
ASN   CA  HA   sing N N 89  
ASN   C   O    doub N N 90  
ASN   C   OXT  sing N N 91  
ASN   CB  CG   sing N N 92  
ASN   CB  HB2  sing N N 93  
ASN   CB  HB3  sing N N 94  
ASN   CG  OD1  doub N N 95  
ASN   CG  ND2  sing N N 96  
ASN   ND2 HD21 sing N N 97  
ASN   ND2 HD22 sing N N 98  
ASN   OXT HXT  sing N N 99  
ASP   N   CA   sing N N 100 
ASP   N   H    sing N N 101 
ASP   N   H2   sing N N 102 
ASP   CA  C    sing N N 103 
ASP   CA  CB   sing N N 104 
ASP   CA  HA   sing N N 105 
ASP   C   O    doub N N 106 
ASP   C   OXT  sing N N 107 
ASP   CB  CG   sing N N 108 
ASP   CB  HB2  sing N N 109 
ASP   CB  HB3  sing N N 110 
ASP   CG  OD1  doub N N 111 
ASP   CG  OD2  sing N N 112 
ASP   OD2 HD2  sing N N 113 
ASP   OXT HXT  sing N N 114 
CYS   N   CA   sing N N 115 
CYS   N   H    sing N N 116 
CYS   N   H2   sing N N 117 
CYS   CA  C    sing N N 118 
CYS   CA  CB   sing N N 119 
CYS   CA  HA   sing N N 120 
CYS   C   O    doub N N 121 
CYS   C   OXT  sing N N 122 
CYS   CB  SG   sing N N 123 
CYS   CB  HB2  sing N N 124 
CYS   CB  HB3  sing N N 125 
CYS   SG  HG   sing N N 126 
CYS   OXT HXT  sing N N 127 
GLN   N   CA   sing N N 128 
GLN   N   H    sing N N 129 
GLN   N   H2   sing N N 130 
GLN   CA  C    sing N N 131 
GLN   CA  CB   sing N N 132 
GLN   CA  HA   sing N N 133 
GLN   C   O    doub N N 134 
GLN   C   OXT  sing N N 135 
GLN   CB  CG   sing N N 136 
GLN   CB  HB2  sing N N 137 
GLN   CB  HB3  sing N N 138 
GLN   CG  CD   sing N N 139 
GLN   CG  HG2  sing N N 140 
GLN   CG  HG3  sing N N 141 
GLN   CD  OE1  doub N N 142 
GLN   CD  NE2  sing N N 143 
GLN   NE2 HE21 sing N N 144 
GLN   NE2 HE22 sing N N 145 
GLN   OXT HXT  sing N N 146 
GLU   N   CA   sing N N 147 
GLU   N   H    sing N N 148 
GLU   N   H2   sing N N 149 
GLU   CA  C    sing N N 150 
GLU   CA  CB   sing N N 151 
GLU   CA  HA   sing N N 152 
GLU   C   O    doub N N 153 
GLU   C   OXT  sing N N 154 
GLU   CB  CG   sing N N 155 
GLU   CB  HB2  sing N N 156 
GLU   CB  HB3  sing N N 157 
GLU   CG  CD   sing N N 158 
GLU   CG  HG2  sing N N 159 
GLU   CG  HG3  sing N N 160 
GLU   CD  OE1  doub N N 161 
GLU   CD  OE2  sing N N 162 
GLU   OE2 HE2  sing N N 163 
GLU   OXT HXT  sing N N 164 
GLY   N   CA   sing N N 165 
GLY   N   H    sing N N 166 
GLY   N   H2   sing N N 167 
GLY   CA  C    sing N N 168 
GLY   CA  HA2  sing N N 169 
GLY   CA  HA3  sing N N 170 
GLY   C   O    doub N N 171 
GLY   C   OXT  sing N N 172 
GLY   OXT HXT  sing N N 173 
HIS   N   CA   sing N N 174 
HIS   N   H    sing N N 175 
HIS   N   H2   sing N N 176 
HIS   CA  C    sing N N 177 
HIS   CA  CB   sing N N 178 
HIS   CA  HA   sing N N 179 
HIS   C   O    doub N N 180 
HIS   C   OXT  sing N N 181 
HIS   CB  CG   sing N N 182 
HIS   CB  HB2  sing N N 183 
HIS   CB  HB3  sing N N 184 
HIS   CG  ND1  sing Y N 185 
HIS   CG  CD2  doub Y N 186 
HIS   ND1 CE1  doub Y N 187 
HIS   ND1 HD1  sing N N 188 
HIS   CD2 NE2  sing Y N 189 
HIS   CD2 HD2  sing N N 190 
HIS   CE1 NE2  sing Y N 191 
HIS   CE1 HE1  sing N N 192 
HIS   NE2 HE2  sing N N 193 
HIS   OXT HXT  sing N N 194 
HOH   O   H1   sing N N 195 
HOH   O   H2   sing N N 196 
ILE   N   CA   sing N N 197 
ILE   N   H    sing N N 198 
ILE   N   H2   sing N N 199 
ILE   CA  C    sing N N 200 
ILE   CA  CB   sing N N 201 
ILE   CA  HA   sing N N 202 
ILE   C   O    doub N N 203 
ILE   C   OXT  sing N N 204 
ILE   CB  CG1  sing N N 205 
ILE   CB  CG2  sing N N 206 
ILE   CB  HB   sing N N 207 
ILE   CG1 CD1  sing N N 208 
ILE   CG1 HG12 sing N N 209 
ILE   CG1 HG13 sing N N 210 
ILE   CG2 HG21 sing N N 211 
ILE   CG2 HG22 sing N N 212 
ILE   CG2 HG23 sing N N 213 
ILE   CD1 HD11 sing N N 214 
ILE   CD1 HD12 sing N N 215 
ILE   CD1 HD13 sing N N 216 
ILE   OXT HXT  sing N N 217 
LEU   N   CA   sing N N 218 
LEU   N   H    sing N N 219 
LEU   N   H2   sing N N 220 
LEU   CA  C    sing N N 221 
LEU   CA  CB   sing N N 222 
LEU   CA  HA   sing N N 223 
LEU   C   O    doub N N 224 
LEU   C   OXT  sing N N 225 
LEU   CB  CG   sing N N 226 
LEU   CB  HB2  sing N N 227 
LEU   CB  HB3  sing N N 228 
LEU   CG  CD1  sing N N 229 
LEU   CG  CD2  sing N N 230 
LEU   CG  HG   sing N N 231 
LEU   CD1 HD11 sing N N 232 
LEU   CD1 HD12 sing N N 233 
LEU   CD1 HD13 sing N N 234 
LEU   CD2 HD21 sing N N 235 
LEU   CD2 HD22 sing N N 236 
LEU   CD2 HD23 sing N N 237 
LEU   OXT HXT  sing N N 238 
LYS   N   CA   sing N N 239 
LYS   N   H    sing N N 240 
LYS   N   H2   sing N N 241 
LYS   CA  C    sing N N 242 
LYS   CA  CB   sing N N 243 
LYS   CA  HA   sing N N 244 
LYS   C   O    doub N N 245 
LYS   C   OXT  sing N N 246 
LYS   CB  CG   sing N N 247 
LYS   CB  HB2  sing N N 248 
LYS   CB  HB3  sing N N 249 
LYS   CG  CD   sing N N 250 
LYS   CG  HG2  sing N N 251 
LYS   CG  HG3  sing N N 252 
LYS   CD  CE   sing N N 253 
LYS   CD  HD2  sing N N 254 
LYS   CD  HD3  sing N N 255 
LYS   CE  NZ   sing N N 256 
LYS   CE  HE2  sing N N 257 
LYS   CE  HE3  sing N N 258 
LYS   NZ  HZ1  sing N N 259 
LYS   NZ  HZ2  sing N N 260 
LYS   NZ  HZ3  sing N N 261 
LYS   OXT HXT  sing N N 262 
MET   N   CA   sing N N 263 
MET   N   H    sing N N 264 
MET   N   H2   sing N N 265 
MET   CA  C    sing N N 266 
MET   CA  CB   sing N N 267 
MET   CA  HA   sing N N 268 
MET   C   O    doub N N 269 
MET   C   OXT  sing N N 270 
MET   CB  CG   sing N N 271 
MET   CB  HB2  sing N N 272 
MET   CB  HB3  sing N N 273 
MET   CG  SD   sing N N 274 
MET   CG  HG2  sing N N 275 
MET   CG  HG3  sing N N 276 
MET   SD  CE   sing N N 277 
MET   CE  HE1  sing N N 278 
MET   CE  HE2  sing N N 279 
MET   CE  HE3  sing N N 280 
MET   OXT HXT  sing N N 281 
PHE   N   CA   sing N N 282 
PHE   N   H    sing N N 283 
PHE   N   H2   sing N N 284 
PHE   CA  C    sing N N 285 
PHE   CA  CB   sing N N 286 
PHE   CA  HA   sing N N 287 
PHE   C   O    doub N N 288 
PHE   C   OXT  sing N N 289 
PHE   CB  CG   sing N N 290 
PHE   CB  HB2  sing N N 291 
PHE   CB  HB3  sing N N 292 
PHE   CG  CD1  doub Y N 293 
PHE   CG  CD2  sing Y N 294 
PHE   CD1 CE1  sing Y N 295 
PHE   CD1 HD1  sing N N 296 
PHE   CD2 CE2  doub Y N 297 
PHE   CD2 HD2  sing N N 298 
PHE   CE1 CZ   doub Y N 299 
PHE   CE1 HE1  sing N N 300 
PHE   CE2 CZ   sing Y N 301 
PHE   CE2 HE2  sing N N 302 
PHE   CZ  HZ   sing N N 303 
PHE   OXT HXT  sing N N 304 
PRO   N   CA   sing N N 305 
PRO   N   CD   sing N N 306 
PRO   N   H    sing N N 307 
PRO   CA  C    sing N N 308 
PRO   CA  CB   sing N N 309 
PRO   CA  HA   sing N N 310 
PRO   C   O    doub N N 311 
PRO   C   OXT  sing N N 312 
PRO   CB  CG   sing N N 313 
PRO   CB  HB2  sing N N 314 
PRO   CB  HB3  sing N N 315 
PRO   CG  CD   sing N N 316 
PRO   CG  HG2  sing N N 317 
PRO   CG  HG3  sing N N 318 
PRO   CD  HD2  sing N N 319 
PRO   CD  HD3  sing N N 320 
PRO   OXT HXT  sing N N 321 
SER   N   CA   sing N N 322 
SER   N   H    sing N N 323 
SER   N   H2   sing N N 324 
SER   CA  C    sing N N 325 
SER   CA  CB   sing N N 326 
SER   CA  HA   sing N N 327 
SER   C   O    doub N N 328 
SER   C   OXT  sing N N 329 
SER   CB  OG   sing N N 330 
SER   CB  HB2  sing N N 331 
SER   CB  HB3  sing N N 332 
SER   OG  HG   sing N N 333 
SER   OXT HXT  sing N N 334 
SO4   S   O1   doub N N 335 
SO4   S   O2   doub N N 336 
SO4   S   O3   sing N N 337 
SO4   S   O4   sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9N2M 
_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]   0.021142 
_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]   0.015853 
_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]   0.011348 
_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   . THR   A 1 1   ? 32.981 34.148 -9.534  1.00 30.42  ? 2   THR   A N   1 
ATOM   2    C CA  . THR   A 1 1   ? 31.742 33.417 -9.799  1.00 28.62  ? 2   THR   A CA  1 
ATOM   3    C C   . THR   A 1 1   ? 30.564 34.262 -9.343  1.00 23.40  ? 2   THR   A C   1 
ATOM   4    O O   . THR   A 1 1   ? 30.569 34.824 -8.244  1.00 27.47  ? 2   THR   A O   1 
ATOM   5    C CB  . THR   A 1 1   ? 31.733 32.085 -9.015  1.00 35.43  ? 2   THR   A CB  1 
ATOM   6    O OG1 . THR   A 1 1   ? 32.774 31.236 -9.515  1.00 39.77  ? 2   THR   A OG1 1 
ATOM   7    C CG2 . THR   A 1 1   ? 30.391 31.368 -9.145  1.00 36.38  ? 2   THR   A CG2 1 
ATOM   8    N N   . VAL   A 1 2   ? 29.531 34.355 -10.153 1.00 16.73  ? 3   VAL   A N   1 
ATOM   9    C CA  . VAL   A 1 2   ? 28.399 35.179 -9.784  1.00 17.72  ? 3   VAL   A CA  1 
ATOM   10   C C   . VAL   A 1 2   ? 27.269 34.252 -9.359  1.00 19.00  ? 3   VAL   A C   1 
ATOM   11   O O   . VAL   A 1 2   ? 27.269 33.056 -9.668  1.00 23.05  ? 3   VAL   A O   1 
ATOM   12   C CB  . VAL   A 1 2   ? 27.981 36.178 -10.885 1.00 22.55  ? 3   VAL   A CB  1 
ATOM   13   C CG1 . VAL   A 1 2   ? 29.227 36.858 -11.461 1.00 21.35  ? 3   VAL   A CG1 1 
ATOM   14   C CG2 . VAL   A 1 2   ? 27.177 35.509 -11.960 1.00 26.66  ? 3   VAL   A CG2 1 
ATOM   15   N N   . PHE   A 1 3   ? 26.338 34.787 -8.578  1.00 16.40  ? 4   PHE   A N   1 
ATOM   16   C CA  . PHE   A 1 3   ? 25.255 34.003 -7.994  1.00 16.78  ? 4   PHE   A CA  1 
ATOM   17   C C   . PHE   A 1 3   ? 23.926 34.556 -8.502  1.00 17.42  ? 4   PHE   A C   1 
ATOM   18   O O   . PHE   A 1 3   ? 23.899 35.553 -9.222  1.00 17.11  ? 4   PHE   A O   1 
ATOM   19   C CB  . PHE   A 1 3   ? 25.352 34.034 -6.467  1.00 18.00  ? 4   PHE   A CB  1 
ATOM   20   C CG  . PHE   A 1 3   ? 26.703 33.600 -5.940  1.00 19.23  ? 4   PHE   A CG  1 
ATOM   21   C CD1 . PHE   A 1 3   ? 27.193 32.335 -6.209  1.00 21.17  ? 4   PHE   A CD1 1 
ATOM   22   C CD2 . PHE   A 1 3   ? 27.475 34.464 -5.173  1.00 20.43  ? 4   PHE   A CD2 1 
ATOM   23   C CE1 . PHE   A 1 3   ? 28.424 31.925 -5.728  1.00 21.62  ? 4   PHE   A CE1 1 
ATOM   24   C CE2 . PHE   A 1 3   ? 28.722 34.058 -4.672  1.00 22.29  ? 4   PHE   A CE2 1 
ATOM   25   C CZ  . PHE   A 1 3   ? 29.194 32.789 -4.965  1.00 22.41  ? 4   PHE   A CZ  1 
ATOM   26   N N   . ARG   A 1 4   ? 22.821 33.903 -8.124  1.00 18.63  ? 5   ARG   A N   1 
ATOM   27   C CA  . ARG   A 1 4   ? 21.495 34.320 -8.585  1.00 17.46  ? 5   ARG   A CA  1 
ATOM   28   C C   . ARG   A 1 4   ? 21.184 35.716 -8.073  1.00 15.51  ? 5   ARG   A C   1 
ATOM   29   O O   . ARG   A 1 4   ? 21.257 35.980 -6.867  1.00 18.21  ? 5   ARG   A O   1 
ATOM   30   C CB  . ARG   A 1 4   ? 20.446 33.366 -8.017  1.00 20.34  ? 5   ARG   A CB  1 
ATOM   31   C CG  . ARG   A 1 4   ? 20.533 31.961 -8.524  1.00 24.04  ? 5   ARG   A CG  1 
ATOM   32   C CD  . ARG   A 1 4   ? 19.258 31.203 -8.228  1.00 26.40  ? 5   ARG   A CD  1 
ATOM   33   N NE  . ARG   A 1 4   ? 18.118 31.820 -8.901  1.00 29.01  ? 5   ARG   A NE  1 
ATOM   34   C CZ  . ARG   A 1 4   ? 16.948 31.222 -9.062  1.00 30.66  ? 5   ARG   A CZ  1 
ATOM   35   N NH1 . ARG   A 1 4   ? 16.731 30.001 -8.603  1.00 30.89  ? 5   ARG   A NH1 1 
ATOM   36   N NH2 . ARG   A 1 4   ? 15.978 31.857 -9.715  1.00 31.59  ? 5   ARG   A NH2 1 
ATOM   37   N N   . GLN   A 1 5   ? 20.789 36.608 -8.971  1.00 15.42  ? 6   GLN   A N   1 
ATOM   38   C CA  . GLN   A 1 5   ? 20.574 37.992 -8.575  1.00 16.91  ? 6   GLN   A CA  1 
ATOM   39   C C   . GLN   A 1 5   ? 19.112 38.416 -8.537  1.00 18.96  ? 6   GLN   A C   1 
ATOM   40   O O   . GLN   A 1 5   ? 18.823 39.586 -8.253  1.00 20.59  ? 6   GLN   A O   1 
ATOM   41   C CB  . GLN   A 1 5   ? 21.455 38.955 -9.365  1.00 19.21  ? 6   GLN   A CB  1 
ATOM   42   C CG  . GLN   A 1 5   ? 22.910 38.802 -8.925  1.00 18.99  ? 6   GLN   A CG  1 
ATOM   43   C CD  . GLN   A 1 5   ? 23.877 39.395 -9.894  1.00 19.25  ? 6   GLN   A CD  1 
ATOM   44   O OE1 . GLN   A 1 5   ? 23.491 40.167 -10.767 1.00 22.73  ? 6   GLN   A OE1 1 
ATOM   45   N NE2 . GLN   A 1 5   ? 25.144 39.044 -9.758  1.00 19.60  ? 6   GLN   A NE2 1 
ATOM   46   N N   . GLU   A 1 6   ? 18.177 37.502 -8.765  1.00 19.81  ? 7   GLU   A N   1 
ATOM   47   C CA  . GLU   A 1 6   ? 16.793 37.810 -8.447  1.00 21.64  ? 7   GLU   A CA  1 
ATOM   48   C C   . GLU   A 1 6   ? 16.650 38.026 -6.942  1.00 21.91  ? 7   GLU   A C   1 
ATOM   49   O O   . GLU   A 1 6   ? 17.439 37.525 -6.141  1.00 22.51  ? 7   GLU   A O   1 
ATOM   50   C CB  . GLU   A 1 6   ? 15.900 36.643 -8.833  1.00 25.02  ? 7   GLU   A CB  1 
ATOM   51   C CG  . GLU   A 1 6   ? 15.887 36.398 -10.307 1.00 31.23  ? 7   GLU   A CG  1 
ATOM   52   C CD  . GLU   A 1 6   ? 16.343 35.001 -10.628 1.00 38.53  ? 7   GLU   A CD  1 
ATOM   53   O OE1 . GLU   A 1 6   ? 15.501 34.209 -11.105 1.00 40.60  ? 7   GLU   A OE1 1 
ATOM   54   O OE2 . GLU   A 1 6   ? 17.537 34.695 -10.373 1.00 40.10  ? 7   GLU   A OE2 1 
ATOM   55   N N   . ASN   A 1 7   ? 15.629 38.790 -6.557  1.00 23.15  ? 8   ASN   A N   1 
ATOM   56   C CA  . ASN   A 1 7   ? 15.378 39.015 -5.140  1.00 23.55  ? 8   ASN   A CA  1 
ATOM   57   C C   . ASN   A 1 7   ? 15.009 37.698 -4.485  1.00 21.20  ? 8   ASN   A C   1 
ATOM   58   O O   . ASN   A 1 7   ? 14.076 37.013 -4.917  1.00 20.15  ? 8   ASN   A O   1 
ATOM   59   C CB  . ASN   A 1 7   ? 14.215 39.988 -4.931  1.00 27.24  ? 8   ASN   A CB  1 
ATOM   60   C CG  . ASN   A 1 7   ? 14.278 40.691 -3.574  1.00 31.38  ? 8   ASN   A CG  1 
ATOM   61   O OD1 . ASN   A 1 7   ? 14.161 40.046 -2.522  1.00 32.16  ? 8   ASN   A OD1 1 
ATOM   62   N ND2 . ASN   A 1 7   ? 14.368 42.021 -3.595  1.00 34.73  ? 8   ASN   A ND2 1 
ATOM   63   N N   . VAL   A 1 8   ? 15.722 37.362 -3.415  1.00 20.77  ? 9   VAL   A N   1 
ATOM   64   C CA  . VAL   A 1 8   ? 15.448 36.117 -2.720  1.00 20.25  ? 9   VAL   A CA  1 
ATOM   65   C C   . VAL   A 1 8   ? 14.021 36.083 -2.190  1.00 20.25  ? 9   VAL   A C   1 
ATOM   66   O O   . VAL   A 1 8   ? 13.407 35.011 -2.130  1.00 19.34  ? 9   VAL   A O   1 
ATOM   67   C CB  . VAL   A 1 8   ? 16.542 35.868 -1.666  1.00 24.68  ? 9   VAL   A CB  1 
ATOM   68   C CG1 . VAL   A 1 8   ? 16.411 36.830 -0.531  1.00 24.82  ? 9   VAL   A CG1 1 
ATOM   69   C CG2 . VAL   A 1 8   ? 16.520 34.428 -1.215  1.00 26.23  ? 9   VAL   A CG2 1 
ATOM   70   N N   . ASP   A 1 9   ? 13.460 37.248 -1.841  1.00 20.65  ? 10  ASP   A N   1 
ATOM   71   C CA  . ASP   A 1 9   ? 12.090 37.328 -1.354  1.00 24.14  ? 10  ASP   A CA  1 
ATOM   72   C C   . ASP   A 1 9   ? 11.071 36.946 -2.412  1.00 22.91  ? 10  ASP   A C   1 
ATOM   73   O O   . ASP   A 1 9   ? 9.919  36.684 -2.061  1.00 24.36  ? 10  ASP   A O   1 
ATOM   74   C CB  . ASP   A 1 9   ? 11.768 38.749 -0.885  1.00 32.16  ? 10  ASP   A CB  1 
ATOM   75   C CG  . ASP   A 1 9   ? 12.604 39.172 0.300   1.00 41.51  ? 10  ASP   A CG  1 
ATOM   76   O OD1 . ASP   A 1 9   ? 12.824 38.331 1.198   1.00 45.08  ? 10  ASP   A OD1 1 
ATOM   77   O OD2 . ASP   A 1 9   ? 13.024 40.351 0.344   1.00 45.02  ? 10  ASP   A OD2 1 
ATOM   78   N N   . ASP   A 1 10  ? 11.453 36.937 -3.693  1.00 22.32  ? 11  ASP   A N   1 
ATOM   79   C CA  . ASP   A 1 10  ? 10.545 36.448 -4.730  1.00 23.01  ? 11  ASP   A CA  1 
ATOM   80   C C   . ASP   A 1 10  ? 10.375 34.936 -4.670  1.00 20.76  ? 11  ASP   A C   1 
ATOM   81   O O   . ASP   A 1 10  ? 9.395  34.410 -5.208  1.00 22.64  ? 11  ASP   A O   1 
ATOM   82   C CB  . ASP   A 1 10  ? 11.030 36.833 -6.131  1.00 28.32  ? 11  ASP   A CB  1 
ATOM   83   C CG  . ASP   A 1 10  ? 10.959 38.333 -6.410  1.00 35.34  ? 11  ASP   A CG  1 
ATOM   84   O OD1 . ASP   A 1 10  ? 10.361 39.080 -5.605  1.00 38.27  ? 11  ASP   A OD1 1 
ATOM   85   O OD2 . ASP   A 1 10  ? 11.470 38.745 -7.474  1.00 37.46  ? 11  ASP   A OD2 1 
ATOM   86   N N   . TYR   A 1 11  ? 11.309 34.234 -4.027  1.00 18.53  ? 12  TYR   A N   1 
ATOM   87   C CA  . TYR   A 1 11  ? 11.356 32.783 -4.042  1.00 17.32  ? 12  TYR   A CA  1 
ATOM   88   C C   . TYR   A 1 11  ? 11.204 32.157 -2.674  1.00 17.04  ? 12  TYR   A C   1 
ATOM   89   O O   . TYR   A 1 11  ? 10.860 30.974 -2.592  1.00 17.49  ? 12  TYR   A O   1 
ATOM   90   C CB  . TYR   A 1 11  ? 12.673 32.307 -4.688  1.00 18.30  ? 12  TYR   A CB  1 
ATOM   91   C CG  . TYR   A 1 11  ? 12.684 32.646 -6.158  1.00 19.96  ? 12  TYR   A CG  1 
ATOM   92   C CD1 . TYR   A 1 11  ? 11.957 31.887 -7.075  1.00 24.43  ? 12  TYR   A CD1 1 
ATOM   93   C CD2 . TYR   A 1 11  ? 13.317 33.790 -6.615  1.00 22.39  ? 12  TYR   A CD2 1 
ATOM   94   C CE1 . TYR   A 1 11  ? 11.925 32.219 -8.424  1.00 27.20  ? 12  TYR   A CE1 1 
ATOM   95   C CE2 . TYR   A 1 11  ? 13.285 34.127 -7.956  1.00 25.54  ? 12  TYR   A CE2 1 
ATOM   96   C CZ  . TYR   A 1 11  ? 12.588 33.338 -8.852  1.00 27.29  ? 12  TYR   A CZ  1 
ATOM   97   O OH  . TYR   A 1 11  ? 12.558 33.685 -10.185 1.00 31.54  ? 12  TYR   A OH  1 
ATOM   98   N N   . TYR   A 1 12  ? 11.458 32.907 -1.608  1.00 16.69  ? 13  TYR   A N   1 
ATOM   99   C CA  . TYR   A 1 12  ? 11.408 32.387 -0.254  1.00 16.22  ? 13  TYR   A CA  1 
ATOM   100  C C   . TYR   A 1 12  ? 10.703 33.392 0.636   1.00 17.78  ? 13  TYR   A C   1 
ATOM   101  O O   . TYR   A 1 12  ? 10.783 34.601 0.407   1.00 20.58  ? 13  TYR   A O   1 
ATOM   102  C CB  . TYR   A 1 12  ? 12.827 32.180 0.300   1.00 16.34  ? 13  TYR   A CB  1 
ATOM   103  C CG  . TYR   A 1 12  ? 13.611 31.118 -0.415  1.00 14.89  ? 13  TYR   A CG  1 
ATOM   104  C CD1 . TYR   A 1 12  ? 14.288 31.400 -1.588  1.00 15.35  ? 13  TYR   A CD1 1 
ATOM   105  C CD2 . TYR   A 1 12  ? 13.687 29.813 0.101   1.00 16.06  ? 13  TYR   A CD2 1 
ATOM   106  C CE1 . TYR   A 1 12  ? 14.991 30.418 -2.249  1.00 15.97  ? 13  TYR   A CE1 1 
ATOM   107  C CE2 . TYR   A 1 12  ? 14.391 28.834 -0.554  1.00 15.36  ? 13  TYR   A CE2 1 
ATOM   108  C CZ  . TYR   A 1 12  ? 15.043 29.136 -1.729  1.00 15.23  ? 13  TYR   A CZ  1 
ATOM   109  O OH  . TYR   A 1 12  ? 15.760 28.146 -2.365  1.00 18.15  ? 13  TYR   A OH  1 
ATOM   110  N N   . ASP   A 1 13  ? 9.980  32.882 1.630   1.00 17.09  ? 14  ASP   A N   1 
ATOM   111  C CA  . ASP   A 1 13  ? 9.467  33.700 2.721   1.00 17.37  ? 14  ASP   A CA  1 
ATOM   112  C C   . ASP   A 1 13  ? 10.288 33.395 3.963   1.00 17.34  ? 14  ASP   A C   1 
ATOM   113  O O   . ASP   A 1 13  ? 10.508 32.230 4.287   1.00 19.74  ? 14  ASP   A O   1 
ATOM   114  C CB  . ASP   A 1 13  ? 8.000  33.395 3.014   1.00 18.75  ? 14  ASP   A CB  1 
ATOM   115  C CG  . ASP   A 1 13  ? 7.101  33.769 1.859   1.00 22.33  ? 14  ASP   A CG  1 
ATOM   116  O OD1 . ASP   A 1 13  ? 6.951  34.991 1.621   1.00 25.42  ? 14  ASP   A OD1 1 
ATOM   117  O OD2 . ASP   A 1 13  ? 6.469  32.871 1.267   1.00 22.56  ? 14  ASP   A OD2 1 
ATOM   118  N N   . THR   A 1 14  ? 10.743 34.425 4.643   1.00 18.66  ? 15  THR   A N   1 
ATOM   119  C CA  . THR   A 1 14  ? 11.543 34.198 5.834   1.00 18.76  ? 15  THR   A CA  1 
ATOM   120  C C   . THR   A 1 14  ? 10.670 34.228 7.086   1.00 19.06  ? 15  THR   A C   1 
ATOM   121  O O   . THR   A 1 14  ? 9.548  34.748 7.098   1.00 21.64  ? 15  THR   A O   1 
ATOM   122  C CB  . THR   A 1 14  ? 12.674 35.226 5.951   1.00 22.81  ? 15  THR   A CB  1 
ATOM   123  O OG1 . THR   A 1 14  ? 12.124 36.545 6.049   1.00 24.49  ? 15  THR   A OG1 1 
ATOM   124  C CG2 . THR   A 1 14  ? 13.582 35.162 4.723   1.00 25.01  ? 15  THR   A CG2 1 
ATOM   125  N N   . GLY   A 1 15  ? 11.210 33.661 8.153   1.00 17.80  ? 16  GLY   A N   1 
ATOM   126  C CA  . GLY   A 1 15  ? 10.542 33.666 9.442   1.00 19.30  ? 16  GLY   A CA  1 
ATOM   127  C C   . GLY   A 1 15  ? 11.484 34.053 10.566  1.00 18.73  ? 16  GLY   A C   1 
ATOM   128  O O   . GLY   A 1 15  ? 12.154 35.085 10.496  1.00 20.37  ? 16  GLY   A O   1 
ATOM   129  N N   . GLU   A 1 16  ? 11.589 33.177 11.563  1.00 18.22  ? 17  GLU   A N   1 
ATOM   130  C CA  . GLU   A 1 16  ? 12.377 33.420 12.767  1.00 17.88  ? 17  GLU   A CA  1 
ATOM   131  C C   . GLU   A 1 16  ? 13.860 33.604 12.442  1.00 17.14  ? 17  GLU   A C   1 
ATOM   132  O O   . GLU   A 1 16  ? 14.434 32.858 11.655  1.00 17.92  ? 17  GLU   A O   1 
ATOM   133  C CB  . GLU   A 1 16  ? 12.266 32.155 13.633  1.00 21.46  ? 17  GLU   A CB  1 
ATOM   134  C CG  . GLU   A 1 16  ? 12.791 32.260 15.024  1.00 26.63  ? 17  GLU   A CG  1 
ATOM   135  C CD  . GLU   A 1 16  ? 12.956 30.902 15.695  1.00 30.04  ? 17  GLU   A CD  1 
ATOM   136  O OE1 . GLU   A 1 16  ? 12.267 29.931 15.300  1.00 28.88  ? 17  GLU   A OE1 1 
ATOM   137  O OE2 . GLU   A 1 16  ? 13.648 30.855 16.736  1.00 32.71  ? 17  GLU   A OE2 1 
ATOM   138  N N   . GLU   A 1 17  ? 14.507 34.580 13.077  1.00 16.91  ? 18  GLU   A N   1 
ATOM   139  C CA  . GLU   A 1 17  ? 15.965 34.622 13.088  1.00 17.95  ? 18  GLU   A CA  1 
ATOM   140  C C   . GLU   A 1 17  ? 16.498 33.588 14.053  1.00 18.84  ? 18  GLU   A C   1 
ATOM   141  O O   . GLU   A 1 17  ? 16.067 33.536 15.205  1.00 23.51  ? 18  GLU   A O   1 
ATOM   142  C CB  . GLU   A 1 17  ? 16.506 35.987 13.515  1.00 20.67  ? 18  GLU   A CB  1 
ATOM   143  C CG  . GLU   A 1 17  ? 18.004 36.109 13.224  1.00 23.30  ? 18  GLU   A CG  1 
ATOM   144  C CD  . GLU   A 1 17  ? 18.639 37.451 13.515  1.00 27.07  ? 18  GLU   A CD  1 
ATOM   145  O OE1 . GLU   A 1 17  ? 17.916 38.403 13.773  1.00 25.07  ? 18  GLU   A OE1 1 
ATOM   146  O OE2 . GLU   A 1 17  ? 19.901 37.546 13.496  1.00 30.68  ? 18  GLU   A OE2 1 
ATOM   147  N N   . LEU   A 1 18  ? 17.480 32.816 13.611  1.00 18.33  ? 19  LEU   A N   1 
ATOM   148  C CA  . LEU   A 1 18  ? 18.114 31.813 14.449  1.00 21.05  ? 19  LEU   A CA  1 
ATOM   149  C C   . LEU   A 1 18  ? 19.404 32.364 15.042  1.00 23.53  ? 19  LEU   A C   1 
ATOM   150  O O   . LEU   A 1 18  ? 19.920 33.398 14.614  1.00 23.69  ? 19  LEU   A O   1 
ATOM   151  C CB  . LEU   A 1 18  ? 18.413 30.573 13.615  1.00 22.16  ? 19  LEU   A CB  1 
ATOM   152  C CG  . LEU   A 1 18  ? 17.171 29.929 13.003  1.00 23.90  ? 19  LEU   A CG  1 
ATOM   153  C CD1 . LEU   A 1 18  ? 17.605 28.681 12.301  1.00 24.86  ? 19  LEU   A CD1 1 
ATOM   154  C CD2 . LEU   A 1 18  ? 16.117 29.597 14.060  1.00 25.51  ? 19  LEU   A CD2 1 
ATOM   155  N N   . GLY   A 1 19  ? 19.934 31.646 16.031  1.00 25.46  ? 20  GLY   A N   1 
ATOM   156  C CA  . GLY   A 1 19  ? 21.203 32.048 16.616  1.00 29.56  ? 20  GLY   A CA  1 
ATOM   157  C C   . GLY   A 1 19  ? 22.326 32.006 15.594  1.00 32.53  ? 20  GLY   A C   1 
ATOM   158  O O   . GLY   A 1 19  ? 22.371 31.133 14.722  1.00 32.59  ? 20  GLY   A O   1 
ATOM   159  N N   . SER   A 1 20  ? 23.237 32.969 15.692  1.00 35.69  ? 21  SER   A N   1 
ATOM   160  C CA  . SER   A 1 20  ? 24.372 33.025 14.778  1.00 38.51  ? 21  SER   A CA  1 
ATOM   161  C C   . SER   A 1 20  ? 25.515 33.771 15.453  1.00 40.72  ? 21  SER   A C   1 
ATOM   162  O O   . SER   A 1 20  ? 25.408 34.213 16.601  1.00 40.28  ? 21  SER   A O   1 
ATOM   163  C CB  . SER   A 1 20  ? 23.993 33.707 13.462  1.00 39.06  ? 21  SER   A CB  1 
ATOM   164  O OG  . SER   A 1 20  ? 23.750 35.086 13.672  1.00 39.11  ? 21  SER   A OG  1 
ATOM   165  N N   . GLY   A 1 21  ? 26.617 33.908 14.718  1.00 42.99  ? 22  GLY   A N   1 
ATOM   166  C CA  . GLY   A 1 21  ? 27.727 34.725 15.155  1.00 45.31  ? 22  GLY   A CA  1 
ATOM   167  C C   . GLY   A 1 21  ? 27.501 36.193 14.846  1.00 48.16  ? 22  GLY   A C   1 
ATOM   168  O O   . GLY   A 1 21  ? 26.522 36.592 14.219  1.00 47.62  ? 22  GLY   A O   1 
ATOM   169  N N   . GLN   A 1 22  ? 28.452 37.017 15.291  1.00 50.78  ? 23  GLN   A N   1 
ATOM   170  C CA  . GLN   A 1 22  ? 28.305 38.463 15.166  1.00 53.43  ? 23  GLN   A CA  1 
ATOM   171  C C   . GLN   A 1 22  ? 28.219 38.925 13.722  1.00 53.87  ? 23  GLN   A C   1 
ATOM   172  O O   . GLN   A 1 22  ? 27.708 40.020 13.469  1.00 55.17  ? 23  GLN   A O   1 
ATOM   173  C CB  . GLN   A 1 22  ? 29.528 39.167 15.734  1.00 55.04  ? 23  GLN   A CB  1 
ATOM   174  C CG  . GLN   A 1 22  ? 30.039 38.629 17.018  1.00 56.72  ? 23  GLN   A CG  1 
ATOM   175  C CD  . GLN   A 1 22  ? 31.344 39.293 17.385  1.00 57.57  ? 23  GLN   A CD  1 
ATOM   176  O OE1 . GLN   A 1 22  ? 31.582 40.447 17.027  1.00 58.02  ? 23  GLN   A OE1 1 
ATOM   177  N NE2 . GLN   A 1 22  ? 32.204 38.567 18.082  1.00 58.09  ? 23  GLN   A NE2 1 
ATOM   178  N N   . PHE   A 1 23  ? 28.729 38.137 12.780  1.00 53.69  ? 24  PHE   A N   1 
ATOM   179  C CA  . PHE   A 1 23  ? 29.007 38.636 11.438  1.00 52.84  ? 24  PHE   A CA  1 
ATOM   180  C C   . PHE   A 1 23  ? 27.964 38.255 10.394  1.00 48.43  ? 24  PHE   A C   1 
ATOM   181  O O   . PHE   A 1 23  ? 27.739 39.028 9.457   1.00 49.25  ? 24  PHE   A O   1 
ATOM   182  C CB  . PHE   A 1 23  ? 30.402 38.180 11.004  1.00 57.20  ? 24  PHE   A CB  1 
ATOM   183  C CG  . PHE   A 1 23  ? 31.484 38.568 11.983  1.00 60.72  ? 24  PHE   A CG  1 
ATOM   184  C CD1 . PHE   A 1 23  ? 31.727 39.902 12.276  1.00 62.02  ? 24  PHE   A CD1 1 
ATOM   185  C CD2 . PHE   A 1 23  ? 32.229 37.599 12.637  1.00 61.91  ? 24  PHE   A CD2 1 
ATOM   186  C CE1 . PHE   A 1 23  ? 32.712 40.264 13.186  1.00 62.73  ? 24  PHE   A CE1 1 
ATOM   187  C CE2 . PHE   A 1 23  ? 33.211 37.954 13.546  1.00 62.97  ? 24  PHE   A CE2 1 
ATOM   188  C CZ  . PHE   A 1 23  ? 33.452 39.288 13.821  1.00 62.92  ? 24  PHE   A CZ  1 
ATOM   189  N N   . ALA   A 1 24  ? 27.323 37.098 10.510  1.00 42.04  ? 25  ALA   A N   1 
ATOM   190  C CA  . ALA   A 1 24  ? 26.273 36.719 9.574   1.00 35.41  ? 25  ALA   A CA  1 
ATOM   191  C C   . ALA   A 1 24  ? 24.934 36.720 10.298  1.00 29.61  ? 25  ALA   A C   1 
ATOM   192  O O   . ALA   A 1 24  ? 24.874 36.738 11.526  1.00 30.96  ? 25  ALA   A O   1 
ATOM   193  C CB  . ALA   A 1 24  ? 26.549 35.339 8.960   1.00 35.30  ? 25  ALA   A CB  1 
ATOM   194  N N   . VAL   A 1 25  ? 23.854 36.715 9.523   1.00 22.74  ? 26  VAL   A N   1 
ATOM   195  C CA  . VAL   A 1 25  ? 22.497 36.584 10.041  1.00 19.92  ? 26  VAL   A CA  1 
ATOM   196  C C   . VAL   A 1 25  ? 21.909 35.321 9.448   1.00 17.89  ? 26  VAL   A C   1 
ATOM   197  O O   . VAL   A 1 25  ? 22.090 35.054 8.262   1.00 20.51  ? 26  VAL   A O   1 
ATOM   198  C CB  . VAL   A 1 25  ? 21.645 37.808 9.646   1.00 22.19  ? 26  VAL   A CB  1 
ATOM   199  C CG1 . VAL   A 1 25  ? 20.187 37.629 10.093  1.00 23.66  ? 26  VAL   A CG1 1 
ATOM   200  C CG2 . VAL   A 1 25  ? 22.243 39.071 10.247  1.00 24.45  ? 26  VAL   A CG2 1 
ATOM   201  N N   . VAL   A 1 26  ? 21.221 34.532 10.261  1.00 16.39  ? 27  VAL   A N   1 
ATOM   202  C CA  . VAL   A 1 26  ? 20.604 33.295 9.798   1.00 16.42  ? 27  VAL   A CA  1 
ATOM   203  C C   . VAL   A 1 26  ? 19.116 33.361 10.095  1.00 16.45  ? 27  VAL   A C   1 
ATOM   204  O O   . VAL   A 1 26  ? 18.725 33.629 11.237  1.00 17.69  ? 27  VAL   A O   1 
ATOM   205  C CB  . VAL   A 1 26  ? 21.237 32.063 10.470  1.00 18.72  ? 27  VAL   A CB  1 
ATOM   206  C CG1 . VAL   A 1 26  ? 20.555 30.782 10.000  1.00 21.53  ? 27  VAL   A CG1 1 
ATOM   207  C CG2 . VAL   A 1 26  ? 22.716 32.010 10.175  1.00 19.53  ? 27  VAL   A CG2 1 
ATOM   208  N N   . LYS   A 1 27  ? 18.285 33.095 9.085   1.00 17.03  ? 28  LYS   A N   1 
ATOM   209  C CA  . LYS   A 1 27  ? 16.838 33.086 9.260   1.00 17.05  ? 28  LYS   A CA  1 
ATOM   210  C C   . LYS   A 1 27  ? 16.239 31.788 8.747   1.00 17.22  ? 28  LYS   A C   1 
ATOM   211  O O   . LYS   A 1 27  ? 16.657 31.276 7.717   1.00 19.94  ? 28  LYS   A O   1 
ATOM   212  C CB  . LYS   A 1 27  ? 16.198 34.236 8.490   1.00 19.94  ? 28  LYS   A CB  1 
ATOM   213  C CG  . LYS   A 1 27  ? 16.579 35.581 9.047   1.00 24.08  ? 28  LYS   A CG  1 
ATOM   214  C CD  . LYS   A 1 27  ? 15.839 36.672 8.340   1.00 25.39  ? 28  LYS   A CD  1 
ATOM   215  C CE  . LYS   A 1 27  ? 16.189 38.025 8.928   1.00 28.00  ? 28  LYS   A CE  1 
ATOM   216  N NZ  . LYS   A 1 27  ? 15.341 39.054 8.280   1.00 30.87  ? 28  LYS   A NZ  1 
ATOM   217  N N   . LYS   A 1 28  ? 15.246 31.270 9.456   1.00 15.99  ? 29  LYS   A N   1 
ATOM   218  C CA  . LYS   A 1 28  ? 14.411 30.239 8.869   1.00 16.47  ? 29  LYS   A CA  1 
ATOM   219  C C   . LYS   A 1 28  ? 13.703 30.795 7.646   1.00 16.33  ? 29  LYS   A C   1 
ATOM   220  O O   . LYS   A 1 28  ? 13.329 31.967 7.595   1.00 17.27  ? 29  LYS   A O   1 
ATOM   221  C CB  . LYS   A 1 28  ? 13.375 29.753 9.879   1.00 19.28  ? 29  LYS   A CB  1 
ATOM   222  C CG  . LYS   A 1 28  ? 13.939 28.905 10.990  1.00 25.76  ? 29  LYS   A CG  1 
ATOM   223  C CD  . LYS   A 1 28  ? 12.826 28.376 11.889  1.00 32.24  ? 29  LYS   A CD  1 
ATOM   224  C CE  . LYS   A 1 28  ? 11.905 27.428 11.138  1.00 36.53  ? 29  LYS   A CE  1 
ATOM   225  N NZ  . LYS   A 1 28  ? 10.657 28.096 10.647  1.00 40.25  ? 29  LYS   A NZ  1 
ATOM   226  N N   . CYS   A 1 29  ? 13.519 29.942 6.642   1.00 15.53  ? 30  CYS   A N   1 
ATOM   227  C CA  . CYS   A 1 29  ? 12.786 30.366 5.470   1.00 16.65  ? 30  CYS   A CA  1 
ATOM   228  C C   . CYS   A 1 29  ? 12.056 29.181 4.857   1.00 15.51  ? 30  CYS   A C   1 
ATOM   229  O O   . CYS   A 1 29  ? 12.271 28.015 5.218   1.00 15.67  ? 30  CYS   A O   1 
ATOM   230  C CB  . CYS   A 1 29  ? 13.698 31.115 4.489   1.00 17.93  ? 30  CYS   A CB  1 
ATOM   231  S SG  . CYS   A 1 29  ? 14.898 30.059 3.660   1.00 18.28  ? 30  CYS   A SG  1 
ATOM   232  N N   . ARG   A 1 30  ? 11.159 29.507 3.937   1.00 16.59  ? 31  ARG   A N   1 
ATOM   233  C CA  . ARG   A 1 30  ? 10.345 28.516 3.255   1.00 16.20  ? 31  ARG   A CA  1 
ATOM   234  C C   . ARG   A 1 30  ? 10.333 28.828 1.767   1.00 15.22  ? 31  ARG   A C   1 
ATOM   235  O O   . ARG   A 1 30  ? 10.038 29.959 1.356   1.00 15.63  ? 31  ARG   A O   1 
ATOM   236  C CB  . ARG   A 1 30  ? 8.918  28.540 3.790   1.00 16.73  ? 31  ARG   A CB  1 
ATOM   237  C CG  . ARG   A 1 30  ? 7.980  27.582 3.071   1.00 17.14  ? 31  ARG   A CG  1 
ATOM   238  C CD  . ARG   A 1 30  ? 6.586  27.826 3.583   1.00 17.86  ? 31  ARG   A CD  1 
ATOM   239  N NE  . ARG   A 1 30  ? 5.557  26.980 2.987   1.00 18.02  ? 31  ARG   A NE  1 
ATOM   240  C CZ  . ARG   A 1 30  ? 4.889  27.262 1.873   1.00 17.75  ? 31  ARG   A CZ  1 
ATOM   241  N NH1 . ARG   A 1 30  ? 5.162  28.342 1.155   1.00 19.93  ? 31  ARG   A NH1 1 
ATOM   242  N NH2 . ARG   A 1 30  ? 3.915  26.446 1.480   1.00 19.31  ? 31  ARG   A NH2 1 
ATOM   243  N N   . GLU   A 1 31  ? 10.670 27.834 0.961   1.00 15.21  ? 32  GLU   A N   1 
ATOM   244  C CA  . GLU   A 1 31  ? 10.664 28.041 -0.480  1.00 15.28  ? 32  GLU   A CA  1 
ATOM   245  C C   . GLU   A 1 31  ? 9.223  28.036 -0.998  1.00 16.17  ? 32  GLU   A C   1 
ATOM   246  O O   . GLU   A 1 31  ? 8.449  27.110 -0.723  1.00 17.10  ? 32  GLU   A O   1 
ATOM   247  C CB  . GLU   A 1 31  ? 11.452 26.934 -1.142  1.00 16.20  ? 32  GLU   A CB  1 
ATOM   248  C CG  . GLU   A 1 31  ? 11.586 27.109 -2.625  1.00 18.05  ? 32  GLU   A CG  1 
ATOM   249  C CD  . GLU   A 1 31  ? 12.545 26.133 -3.213  1.00 23.39  ? 32  GLU   A CD  1 
ATOM   250  O OE1 . GLU   A 1 31  ? 12.459 24.961 -2.787  1.00 26.73  ? 32  GLU   A OE1 1 
ATOM   251  O OE2 . GLU   A 1 31  ? 13.292 26.495 -4.148  1.00 23.19  ? 32  GLU   A OE2 1 
ATOM   252  N N   . LYS   A 1 32  ? 8.860  29.077 -1.753  1.00 16.37  ? 33  LYS   A N   1 
ATOM   253  C CA  . LYS   A 1 32  ? 7.476  29.222 -2.194  1.00 17.55  ? 33  LYS   A CA  1 
ATOM   254  C C   . LYS   A 1 32  ? 7.033  28.081 -3.101  1.00 18.89  ? 33  LYS   A C   1 
ATOM   255  O O   . LYS   A 1 32  ? 5.876  27.648 -3.031  1.00 20.49  ? 33  LYS   A O   1 
ATOM   256  C CB  . LYS   A 1 32  ? 7.268  30.568 -2.896  1.00 18.74  ? 33  LYS   A CB  1 
ATOM   257  C CG  . LYS   A 1 32  ? 7.438  31.776 -1.987  1.00 20.11  ? 33  LYS   A CG  1 
ATOM   258  C CD  . LYS   A 1 32  ? 7.253  33.053 -2.788  1.00 22.63  ? 33  LYS   A CD  1 
ATOM   259  C CE  . LYS   A 1 32  ? 7.566  34.297 -1.971  1.00 25.02  ? 33  LYS   A CE  1 
ATOM   260  N NZ  . LYS   A 1 32  ? 7.240  35.544 -2.729  1.00 28.67  ? 33  LYS   A NZ  1 
ATOM   261  N N   . SER   A 1 33  ? 7.917  27.605 -3.989  1.00 19.65  ? 34  SER   A N   1 
ATOM   262  C CA  . SER   A 1 33  ? 7.498  26.628 -4.994  1.00 20.57  ? 34  SER   A CA  1 
ATOM   263  C C   . SER   A 1 33  ? 7.294  25.217 -4.443  1.00 21.03  ? 34  SER   A C   1 
ATOM   264  O O   . SER   A 1 33  ? 6.585  24.419 -5.069  1.00 23.28  ? 34  SER   A O   1 
ATOM   265  C CB  . SER   A 1 33  ? 8.525  26.572 -6.124  1.00 21.52  ? 34  SER   A CB  1 
ATOM   266  O OG  . SER   A 1 33  ? 9.792  26.195 -5.608  1.00 23.19  ? 34  SER   A OG  1 
ATOM   267  N N   . THR   A 1 34  ? 7.898  24.875 -3.302  1.00 19.30  ? 35  THR   A N   1 
ATOM   268  C CA  . THR   A 1 34  ? 7.879  23.515 -2.793  1.00 18.33  ? 35  THR   A CA  1 
ATOM   269  C C   . THR   A 1 34  ? 7.342  23.414 -1.381  1.00 17.97  ? 35  THR   A C   1 
ATOM   270  O O   . THR   A 1 34  ? 7.048  22.297 -0.935  1.00 19.43  ? 35  THR   A O   1 
ATOM   271  C CB  . THR   A 1 34  ? 9.301  22.933 -2.755  1.00 18.66  ? 35  THR   A CB  1 
ATOM   272  O OG1 . THR   A 1 34  ? 10.103 23.739 -1.866  1.00 18.86  ? 35  THR   A OG1 1 
ATOM   273  C CG2 . THR   A 1 34  ? 9.954  22.860 -4.140  1.00 21.22  ? 35  THR   A CG2 1 
ATOM   274  N N   . GLY   A 1 35  ? 7.253  24.524 -0.650  1.00 16.85  ? 36  GLY   A N   1 
ATOM   275  C CA  . GLY   A 1 35  ? 6.928  24.479 0.761   1.00 16.97  ? 36  GLY   A CA  1 
ATOM   276  C C   . GLY   A 1 35  ? 8.040  23.968 1.651   1.00 15.52  ? 36  GLY   A C   1 
ATOM   277  O O   . GLY   A 1 35  ? 7.827  23.858 2.864   1.00 17.17  ? 36  GLY   A O   1 
ATOM   278  N N   . LEU   A 1 36  ? 9.201  23.624 1.094   1.00 15.13  ? 37  LEU   A N   1 
ATOM   279  C CA  . LEU   A 1 36  ? 10.285 23.074 1.885   1.00 15.41  ? 37  LEU   A CA  1 
ATOM   280  C C   . LEU   A 1 36  ? 10.972 24.178 2.675   1.00 13.96  ? 37  LEU   A C   1 
ATOM   281  O O   . LEU   A 1 36  ? 11.100 25.328 2.223   1.00 15.46  ? 37  LEU   A O   1 
ATOM   282  C CB  . LEU   A 1 36  ? 11.284 22.349 0.980   1.00 16.00  ? 37  LEU   A CB  1 
ATOM   283  C CG  . LEU   A 1 36  ? 10.738 21.064 0.336   1.00 16.09  ? 37  LEU   A CG  1 
ATOM   284  C CD1 . LEU   A 1 36  ? 11.720 20.513 -0.682  1.00 18.49  ? 37  LEU   A CD1 1 
ATOM   285  C CD2 . LEU   A 1 36  ? 10.387 20.014 1.392   1.00 17.67  ? 37  LEU   A CD2 1 
ATOM   286  N N   . GLN   A 1 37  ? 11.427 23.817 3.867   1.00 16.41  ? 38  GLN   A N   1 
ATOM   287  C CA  . GLN   A 1 37  ? 12.034 24.768 4.781   1.00 15.95  ? 38  GLN   A CA  1 
ATOM   288  C C   . GLN   A 1 37  ? 13.551 24.677 4.762   1.00 15.24  ? 38  GLN   A C   1 
ATOM   289  O O   . GLN   A 1 37  ? 14.121 23.589 4.616   1.00 17.19  ? 38  GLN   A O   1 
ATOM   290  C CB  . GLN   A 1 37  ? 11.495 24.567 6.194   1.00 19.11  ? 38  GLN   A CB  1 
ATOM   291  C CG  . GLN   A 1 37  ? 9.958  24.623 6.239   1.00 23.78  ? 38  GLN   A CG  1 
ATOM   292  C CD  . GLN   A 1 37  ? 9.398  24.491 7.633   1.00 30.19  ? 38  GLN   A CD  1 
ATOM   293  O OE1 . GLN   A 1 37  ? 9.694  25.300 8.507   1.00 31.69  ? 38  GLN   A OE1 1 
ATOM   294  N NE2 . GLN   A 1 37  ? 8.575  23.473 7.847   1.00 34.91  ? 38  GLN   A NE2 1 
ATOM   295  N N   . TYR   A 1 38  ? 14.194 25.834 4.892   1.00 14.80  ? 39  TYR   A N   1 
ATOM   296  C CA  . TYR   A 1 38  ? 15.636 25.991 4.802   1.00 14.56  ? 39  TYR   A CA  1 
ATOM   297  C C   . TYR   A 1 38  ? 16.076 27.012 5.840   1.00 14.23  ? 39  TYR   A C   1 
ATOM   298  O O   . TYR   A 1 38  ? 15.250 27.660 6.489   1.00 15.26  ? 39  TYR   A O   1 
ATOM   299  C CB  . TYR   A 1 38  ? 16.026 26.493 3.398   1.00 14.31  ? 39  TYR   A CB  1 
ATOM   300  C CG  . TYR   A 1 38  ? 15.756 25.452 2.336   1.00 13.49  ? 39  TYR   A CG  1 
ATOM   301  C CD1 . TYR   A 1 38  ? 16.630 24.393 2.153   1.00 14.83  ? 39  TYR   A CD1 1 
ATOM   302  C CD2 . TYR   A 1 38  ? 14.599 25.495 1.560   1.00 14.12  ? 39  TYR   A CD2 1 
ATOM   303  C CE1 . TYR   A 1 38  ? 16.369 23.413 1.216   1.00 15.65  ? 39  TYR   A CE1 1 
ATOM   304  C CE2 . TYR   A 1 38  ? 14.342 24.518 0.605   1.00 14.16  ? 39  TYR   A CE2 1 
ATOM   305  C CZ  . TYR   A 1 38  ? 15.229 23.476 0.456   1.00 15.85  ? 39  TYR   A CZ  1 
ATOM   306  O OH  . TYR   A 1 38  ? 15.003 22.479 -0.460  1.00 19.18  ? 39  TYR   A OH  1 
ATOM   307  N N   . ALA   A 1 39  ? 17.389 27.172 5.964   1.00 13.99  ? 40  ALA   A N   1 
ATOM   308  C CA  . ALA   A 1 39  ? 17.965 28.272 6.715   1.00 14.88  ? 40  ALA   A CA  1 
ATOM   309  C C   . ALA   A 1 39  ? 18.696 29.169 5.730   1.00 15.76  ? 40  ALA   A C   1 
ATOM   310  O O   . ALA   A 1 39  ? 19.520 28.694 4.956   1.00 19.23  ? 40  ALA   A O   1 
ATOM   311  C CB  . ALA   A 1 39  ? 18.955 27.753 7.757   1.00 16.74  ? 40  ALA   A CB  1 
ATOM   312  N N   . ALA   A 1 40  ? 18.392 30.458 5.750   1.00 14.74  ? 41  ALA   A N   1 
ATOM   313  C CA  . ALA   A 1 40  ? 19.055 31.424 4.889   1.00 15.27  ? 41  ALA   A CA  1 
ATOM   314  C C   . ALA   A 1 40  ? 20.136 32.142 5.687   1.00 16.43  ? 41  ALA   A C   1 
ATOM   315  O O   . ALA   A 1 40  ? 19.841 32.782 6.706   1.00 17.49  ? 41  ALA   A O   1 
ATOM   316  C CB  . ALA   A 1 40  ? 18.047 32.430 4.349   1.00 17.62  ? 41  ALA   A CB  1 
ATOM   317  N N   . LYS   A 1 41  ? 21.383 32.025 5.239   1.00 15.69  ? 42  LYS   A N   1 
ATOM   318  C CA  . LYS   A 1 41  ? 22.504 32.698 5.874   1.00 15.57  ? 42  LYS   A CA  1 
ATOM   319  C C   . LYS   A 1 41  ? 22.913 33.892 5.017   1.00 16.29  ? 42  LYS   A C   1 
ATOM   320  O O   . LYS   A 1 41  ? 23.352 33.722 3.873   1.00 16.81  ? 42  LYS   A O   1 
ATOM   321  C CB  . LYS   A 1 41  ? 23.680 31.739 6.062   1.00 16.65  ? 42  LYS   A CB  1 
ATOM   322  C CG  . LYS   A 1 41  ? 24.912 32.391 6.659   1.00 19.76  ? 42  LYS   A CG  1 
ATOM   323  C CD  . LYS   A 1 41  ? 26.047 31.379 6.763   1.00 24.10  ? 42  LYS   A CD  1 
ATOM   324  C CE  . LYS   A 1 41  ? 27.327 32.028 7.295   1.00 27.69  ? 42  LYS   A CE  1 
ATOM   325  N NZ  . LYS   A 1 41  ? 28.495 31.087 7.350   1.00 30.18  ? 42  LYS   A NZ  1 
ATOM   326  N N   . PHE   A 1 42  ? 22.829 35.083 5.592   1.00 16.91  ? 43  PHE   A N   1 
ATOM   327  C CA  . PHE   A 1 42  ? 23.133 36.335 4.902   1.00 18.49  ? 43  PHE   A CA  1 
ATOM   328  C C   . PHE   A 1 42  ? 24.543 36.751 5.302   1.00 18.32  ? 43  PHE   A C   1 
ATOM   329  O O   . PHE   A 1 42  ? 24.789 37.084 6.466   1.00 22.20  ? 43  PHE   A O   1 
ATOM   330  C CB  . PHE   A 1 42  ? 22.149 37.426 5.327   1.00 19.70  ? 43  PHE   A CB  1 
ATOM   331  C CG  . PHE   A 1 42  ? 20.722 37.136 4.956   1.00 20.50  ? 43  PHE   A CG  1 
ATOM   332  C CD1 . PHE   A 1 42  ? 19.982 36.210 5.681   1.00 21.64  ? 43  PHE   A CD1 1 
ATOM   333  C CD2 . PHE   A 1 42  ? 20.116 37.786 3.889   1.00 22.75  ? 43  PHE   A CD2 1 
ATOM   334  C CE1 . PHE   A 1 42  ? 18.658 35.942 5.349   1.00 22.84  ? 43  PHE   A CE1 1 
ATOM   335  C CE2 . PHE   A 1 42  ? 18.804 37.518 3.553   1.00 23.41  ? 43  PHE   A CE2 1 
ATOM   336  C CZ  . PHE   A 1 42  ? 18.078 36.592 4.284   1.00 22.41  ? 43  PHE   A CZ  1 
ATOM   337  N N   . ILE   A 1 43  ? 25.462 36.742 4.347   1.00 18.22  ? 44  ILE   A N   1 
ATOM   338  C CA  . ILE   A 1 43  ? 26.852 37.126 4.565   1.00 18.01  ? 44  ILE   A CA  1 
ATOM   339  C C   . ILE   A 1 43  ? 27.028 38.535 4.013   1.00 18.04  ? 44  ILE   A C   1 
ATOM   340  O O   . ILE   A 1 43  ? 26.748 38.788 2.836   1.00 18.59  ? 44  ILE   A O   1 
ATOM   341  C CB  . ILE   A 1 43  ? 27.798 36.141 3.858   1.00 19.34  ? 44  ILE   A CB  1 
ATOM   342  C CG1 . ILE   A 1 43  ? 27.535 34.698 4.306   1.00 22.96  ? 44  ILE   A CG1 1 
ATOM   343  C CG2 . ILE   A 1 43  ? 29.236 36.557 4.054   1.00 20.86  ? 44  ILE   A CG2 1 
ATOM   344  C CD1 . ILE   A 1 43  ? 28.322 33.693 3.516   1.00 25.13  ? 44  ILE   A CD1 1 
ATOM   345  N N   . LYS   A 1 44  ? 27.503 39.459 4.838   1.00 18.91  ? 45  LYS   A N   1 
ATOM   346  C CA  . LYS   A 1 44  ? 27.659 40.843 4.404   1.00 20.09  ? 45  LYS   A CA  1 
ATOM   347  C C   . LYS   A 1 44  ? 28.872 40.999 3.501   1.00 19.03  ? 45  LYS   A C   1 
ATOM   348  O O   . LYS   A 1 44  ? 29.985 40.599 3.853   1.00 20.51  ? 45  LYS   A O   1 
ATOM   349  C CB  . LYS   A 1 44  ? 27.768 41.779 5.607   1.00 24.04  ? 45  LYS   A CB  1 
ATOM   350  C CG  . LYS   A 1 44  ? 26.410 42.049 6.212   1.00 31.83  ? 45  LYS   A CG  1 
ATOM   351  C CD  . LYS   A 1 44  ? 25.760 43.245 5.540   1.00 38.16  ? 45  LYS   A CD  1 
ATOM   352  C CE  . LYS   A 1 44  ? 24.317 43.400 6.007   1.00 41.57  ? 45  LYS   A CE  1 
ATOM   353  N NZ  . LYS   A 1 44  ? 23.442 43.941 4.933   1.00 43.04  ? 45  LYS   A NZ  1 
ATOM   354  N N   . LYS   A 1 45  ? 28.658 41.601 2.336   1.00 18.88  ? 46  LYS   A N   1 
ATOM   355  C CA  . LYS   A 1 45  ? 29.744 41.842 1.400   1.00 18.09  ? 46  LYS   A CA  1 
ATOM   356  C C   . LYS   A 1 45  ? 30.588 43.030 1.844   1.00 19.20  ? 46  LYS   A C   1 
ATOM   357  O O   . LYS   A 1 45  ? 30.129 43.920 2.569   1.00 20.51  ? 46  LYS   A O   1 
ATOM   358  C CB  . LYS   A 1 45  ? 29.179 42.167 0.018   1.00 17.56  ? 46  LYS   A CB  1 
ATOM   359  C CG  . LYS   A 1 45  ? 28.528 40.999 -0.676  1.00 18.02  ? 46  LYS   A CG  1 
ATOM   360  C CD  . LYS   A 1 45  ? 27.953 41.416 -2.037  1.00 18.30  ? 46  LYS   A CD  1 
ATOM   361  C CE  . LYS   A 1 45  ? 27.576 40.202 -2.856  1.00 18.54  ? 46  LYS   A CE  1 
ATOM   362  N NZ  . LYS   A 1 45  ? 26.956 40.623 -4.144  1.00 19.12  ? 46  LYS   A NZ  1 
ATOM   363  N N   . ARG   A 1 46  ? 31.835 43.041 1.382   1.00 21.10  ? 47  ARG   A N   1 
ATOM   364  C CA  . ARG   A 1 46  ? 32.686 44.210 1.551   1.00 24.85  ? 47  ARG   A CA  1 
ATOM   365  C C   . ARG   A 1 46  ? 32.184 45.363 0.690   1.00 26.54  ? 47  ARG   A C   1 
ATOM   366  O O   . ARG   A 1 46  ? 31.809 45.180 -0.474  1.00 28.82  ? 47  ARG   A O   1 
ATOM   367  C CB  . ARG   A 1 46  ? 34.131 43.891 1.173   1.00 30.28  ? 47  ARG   A CB  1 
ATOM   368  C CG  . ARG   A 1 46  ? 34.887 43.086 2.205   1.00 35.62  ? 47  ARG   A CG  1 
ATOM   369  C CD  . ARG   A 1 46  ? 36.276 43.672 2.424   1.00 41.24  ? 47  ARG   A CD  1 
ATOM   370  N NE  . ARG   A 1 46  ? 37.202 42.725 3.035   1.00 46.96  ? 47  ARG   A NE  1 
ATOM   371  C CZ  . ARG   A 1 46  ? 38.342 42.327 2.483   1.00 50.57  ? 47  ARG   A CZ  1 
ATOM   372  N NH1 . ARG   A 1 46  ? 38.733 42.776 1.298   1.00 51.81  ? 47  ARG   A NH1 1 
ATOM   373  N NH2 . ARG   A 1 46  ? 39.110 41.456 3.135   1.00 51.91  ? 47  ARG   A NH2 1 
ATOM   374  N N   . ARG   A 1 47  ? 32.184 46.560 1.270   1.00 29.23  ? 48  ARG   A N   1 
ATOM   375  C CA  . ARG   A 1 47  ? 31.687 47.761 0.606   1.00 34.32  ? 48  ARG   A CA  1 
ATOM   376  C C   . ARG   A 1 47  ? 32.748 48.436 -0.248  1.00 33.73  ? 48  ARG   A C   1 
ATOM   377  O O   . ARG   A 1 47  ? 32.403 49.188 -1.171  1.00 32.50  ? 48  ARG   A O   1 
ATOM   378  C CB  . ARG   A 1 47  ? 31.218 48.768 1.666   1.00 40.08  ? 48  ARG   A CB  1 
ATOM   379  C CG  . ARG   A 1 47  ? 29.720 48.787 1.929   1.00 45.41  ? 48  ARG   A CG  1 
ATOM   380  C CD  . ARG   A 1 47  ? 29.130 47.385 1.918   1.00 49.50  ? 48  ARG   A CD  1 
ATOM   381  N NE  . ARG   A 1 47  ? 27.819 47.307 2.555   1.00 53.20  ? 48  ARG   A NE  1 
ATOM   382  C CZ  . ARG   A 1 47  ? 27.182 46.175 2.829   1.00 54.55  ? 48  ARG   A CZ  1 
ATOM   383  N NH1 . ARG   A 1 47  ? 27.660 45.000 2.446   1.00 53.31  ? 48  ARG   A NH1 1 
ATOM   384  N NH2 . ARG   A 1 47  ? 26.030 46.223 3.492   1.00 55.65  ? 48  ARG   A NH2 1 
ATOM   385  N N   . THR   A 1 48  ? 34.027 48.219 0.061   1.00 36.23  ? 49  THR   A N   1 
ATOM   386  C CA  . THR   A 1 48  ? 35.149 48.753 -0.706  1.00 40.36  ? 49  THR   A CA  1 
ATOM   387  C C   . THR   A 1 48  ? 36.265 47.717 -0.696  1.00 45.82  ? 49  THR   A C   1 
ATOM   388  O O   . THR   A 1 48  ? 36.206 46.722 0.027   1.00 46.72  ? 49  THR   A O   1 
ATOM   389  C CB  . THR   A 1 48  ? 35.683 50.090 -0.144  1.00 41.33  ? 49  THR   A CB  1 
ATOM   390  O OG1 . THR   A 1 48  ? 36.358 49.857 1.097   1.00 41.52  ? 49  THR   A OG1 1 
ATOM   391  C CG2 . THR   A 1 48  ? 34.567 51.114 0.068   1.00 41.13  ? 49  THR   A CG2 1 
ATOM   392  N N   . LYS   A 1 49  ? 37.302 47.958 -1.500  1.00 51.55  ? 50  LYS   A N   1 
ATOM   393  C CA  . LYS   A 1 49  ? 38.366 46.965 -1.621  1.00 57.99  ? 50  LYS   A CA  1 
ATOM   394  C C   . LYS   A 1 49  ? 39.207 46.890 -0.349  1.00 61.45  ? 50  LYS   A C   1 
ATOM   395  O O   . LYS   A 1 49  ? 39.534 45.794 0.121   1.00 62.23  ? 50  LYS   A O   1 
ATOM   396  C CB  . LYS   A 1 49  ? 39.237 47.267 -2.842  1.00 61.18  ? 50  LYS   A CB  1 
ATOM   397  C CG  . LYS   A 1 49  ? 40.197 46.146 -3.240  1.00 63.94  ? 50  LYS   A CG  1 
ATOM   398  C CD  . LYS   A 1 49  ? 41.095 46.593 -4.394  1.00 66.11  ? 50  LYS   A CD  1 
ATOM   399  C CE  . LYS   A 1 49  ? 41.959 45.458 -4.947  1.00 67.80  ? 50  LYS   A CE  1 
ATOM   400  N NZ  . LYS   A 1 49  ? 41.161 44.402 -5.639  1.00 68.74  ? 50  LYS   A NZ  1 
ATOM   401  N N   . SER   A 1 50  ? 39.560 48.042 0.228   1.00 63.49  ? 51  SER   A N   1 
ATOM   402  C CA  . SER   A 1 50  ? 40.402 48.099 1.418   1.00 65.05  ? 51  SER   A CA  1 
ATOM   403  C C   . SER   A 1 50  ? 39.598 48.156 2.711   1.00 64.55  ? 51  SER   A C   1 
ATOM   404  O O   . SER   A 1 50  ? 40.060 48.743 3.699   1.00 64.86  ? 51  SER   A O   1 
ATOM   405  C CB  . SER   A 1 50  ? 41.370 49.281 1.333   1.00 66.55  ? 51  SER   A CB  1 
ATOM   406  O OG  . SER   A 1 50  ? 40.692 50.512 1.524   1.00 67.05  ? 51  SER   A OG  1 
ATOM   407  N N   . SER   A 1 51  ? 38.412 47.561 2.736   1.00 63.27  ? 52  SER   A N   1 
ATOM   408  C CA  . SER   A 1 51  ? 37.549 47.636 3.903   1.00 61.99  ? 52  SER   A CA  1 
ATOM   409  C C   . SER   A 1 51  ? 37.812 46.473 4.848   1.00 61.71  ? 52  SER   A C   1 
ATOM   410  O O   . SER   A 1 51  ? 38.199 45.377 4.432   1.00 61.33  ? 52  SER   A O   1 
ATOM   411  C CB  . SER   A 1 51  ? 36.078 47.627 3.490   1.00 61.17  ? 52  SER   A CB  1 
ATOM   412  O OG  . SER   A 1 51  ? 35.241 47.738 4.626   1.00 60.43  ? 52  SER   A OG  1 
ATOM   413  N N   . ARG   A 1 52  ? 37.591 46.726 6.135   1.00 61.82  ? 53  ARG   A N   1 
ATOM   414  C CA  . ARG   A 1 52  ? 37.720 45.700 7.160   1.00 62.38  ? 53  ARG   A CA  1 
ATOM   415  C C   . ARG   A 1 52  ? 36.401 45.022 7.502   1.00 59.72  ? 53  ARG   A C   1 
ATOM   416  O O   . ARG   A 1 52  ? 36.407 43.871 7.949   1.00 60.21  ? 53  ARG   A O   1 
ATOM   417  C CB  . ARG   A 1 52  ? 38.359 46.296 8.421   1.00 65.48  ? 53  ARG   A CB  1 
ATOM   418  C CG  . ARG   A 1 52  ? 37.506 47.327 9.155   1.00 68.40  ? 53  ARG   A CG  1 
ATOM   419  C CD  . ARG   A 1 52  ? 38.350 48.101 10.166  1.00 70.98  ? 53  ARG   A CD  1 
ATOM   420  N NE  . ARG   A 1 52  ? 37.567 49.013 10.993  1.00 72.97  ? 53  ARG   A NE  1 
ATOM   421  C CZ  . ARG   A 1 52  ? 36.759 48.636 11.976  1.00 74.13  ? 53  ARG   A CZ  1 
ATOM   422  N NH1 . ARG   A 1 52  ? 36.605 47.360 12.295  1.00 74.58  ? 53  ARG   A NH1 1 
ATOM   423  N NH2 . ARG   A 1 52  ? 36.092 49.562 12.658  1.00 74.44  ? 53  ARG   A NH2 1 
ATOM   424  N N   . ARG   A 1 53  ? 35.276 45.696 7.289   1.00 56.45  ? 54  ARG   A N   1 
ATOM   425  C CA  . ARG   A 1 53  ? 33.973 45.123 7.571   1.00 53.02  ? 54  ARG   A CA  1 
ATOM   426  C C   . ARG   A 1 53  ? 33.499 44.326 6.359   1.00 43.32  ? 54  ARG   A C   1 
ATOM   427  O O   . ARG   A 1 53  ? 33.893 44.591 5.220   1.00 43.05  ? 54  ARG   A O   1 
ATOM   428  C CB  . ARG   A 1 53  ? 32.968 46.231 7.893   1.00 59.36  ? 54  ARG   A CB  1 
ATOM   429  C CG  . ARG   A 1 53  ? 31.658 45.751 8.510   1.00 65.26  ? 54  ARG   A CG  1 
ATOM   430  C CD  . ARG   A 1 53  ? 30.487 45.926 7.556   1.00 70.16  ? 54  ARG   A CD  1 
ATOM   431  N NE  . ARG   A 1 53  ? 29.206 45.918 8.254   1.00 74.18  ? 54  ARG   A NE  1 
ATOM   432  C CZ  . ARG   A 1 53  ? 28.125 46.568 7.841   1.00 76.96  ? 54  ARG   A CZ  1 
ATOM   433  N NH1 . ARG   A 1 53  ? 28.125 47.268 6.718   1.00 77.93  ? 54  ARG   A NH1 1 
ATOM   434  N NH2 . ARG   A 1 53  ? 27.015 46.511 8.573   1.00 77.72  ? 54  ARG   A NH2 1 
ATOM   435  N N   . GLY   A 1 54  ? 32.654 43.336 6.615   1.00 35.39  ? 55  GLY   A N   1 
ATOM   436  C CA  . GLY   A 1 54  ? 32.180 42.461 5.564   1.00 30.19  ? 55  GLY   A CA  1 
ATOM   437  C C   . GLY   A 1 54  ? 33.202 41.398 5.216   1.00 25.50  ? 55  GLY   A C   1 
ATOM   438  O O   . GLY   A 1 54  ? 34.331 41.375 5.712   1.00 26.41  ? 55  GLY   A O   1 
ATOM   439  N N   . VAL   A 1 55  ? 32.785 40.485 4.350   1.00 20.90  ? 56  VAL   A N   1 
ATOM   440  C CA  . VAL   A 1 55  ? 33.603 39.345 3.959   1.00 19.47  ? 56  VAL   A CA  1 
ATOM   441  C C   . VAL   A 1 55  ? 34.030 39.572 2.514   1.00 18.60  ? 56  VAL   A C   1 
ATOM   442  O O   . VAL   A 1 55  ? 33.203 39.934 1.671   1.00 19.63  ? 56  VAL   A O   1 
ATOM   443  C CB  . VAL   A 1 55  ? 32.823 38.028 4.124   1.00 19.67  ? 56  VAL   A CB  1 
ATOM   444  C CG1 . VAL   A 1 55  ? 33.707 36.846 3.745   1.00 20.59  ? 56  VAL   A CG1 1 
ATOM   445  C CG2 . VAL   A 1 55  ? 32.256 37.907 5.557   1.00 20.57  ? 56  VAL   A CG2 1 
ATOM   446  N N   . SER   A 1 56  ? 35.317 39.391 2.238   1.00 20.24  ? 57  SER   A N   1 
ATOM   447  C CA  . SER   A 1 56  ? 35.824 39.581 0.884   1.00 19.96  ? 57  SER   A CA  1 
ATOM   448  C C   . SER   A 1 56  ? 35.201 38.579 -0.071  1.00 18.41  ? 57  SER   A C   1 
ATOM   449  O O   . SER   A 1 56  ? 34.807 37.476 0.311   1.00 17.88  ? 57  SER   A O   1 
ATOM   450  C CB  . SER   A 1 56  ? 37.338 39.408 0.860   1.00 21.62  ? 57  SER   A CB  1 
ATOM   451  O OG  . SER   A 1 56  ? 37.681 38.030 0.956   1.00 21.72  ? 57  SER   A OG  1 
ATOM   452  N N   . ARG   A 1 57  ? 35.110 38.980 -1.338  1.00 19.41  ? 58  ARG   A N   1 
ATOM   453  C CA  . ARG   A 1 57  ? 34.543 38.095 -2.342  1.00 20.77  ? 58  ARG   A CA  1 
ATOM   454  C C   . ARG   A 1 57  ? 35.315 36.785 -2.421  1.00 19.68  ? 58  ARG   A C   1 
ATOM   455  O O   . ARG   A 1 57  ? 34.720 35.707 -2.551  1.00 19.50  ? 58  ARG   A O   1 
ATOM   456  C CB  . ARG   A 1 57  ? 34.587 38.800 -3.687  1.00 24.09  ? 58  ARG   A CB  1 
ATOM   457  C CG  . ARG   A 1 57  ? 34.030 37.963 -4.760  1.00 26.86  ? 58  ARG   A CG  1 
ATOM   458  C CD  . ARG   A 1 57  ? 32.655 38.447 -5.008  1.00 28.67  ? 58  ARG   A CD  1 
ATOM   459  N NE  . ARG   A 1 57  ? 31.800 37.576 -5.801  1.00 26.33  ? 58  ARG   A NE  1 
ATOM   460  C CZ  . ARG   A 1 57  ? 30.504 37.805 -5.929  1.00 22.85  ? 58  ARG   A CZ  1 
ATOM   461  N NH1 . ARG   A 1 57  ? 29.940 38.856 -5.354  1.00 25.03  ? 58  ARG   A NH1 1 
ATOM   462  N NH2 . ARG   A 1 57  ? 29.761 36.960 -6.640  1.00 21.39  ? 58  ARG   A NH2 1 
ATOM   463  N N   . GLU   A 1 58  ? 36.643 36.857 -2.341  1.00 19.20  ? 59  GLU   A N   1 
ATOM   464  C CA  . GLU   A 1 58  ? 37.447 35.645 -2.370  1.00 21.47  ? 59  GLU   A CA  1 
ATOM   465  C C   . GLU   A 1 58  ? 37.042 34.702 -1.249  1.00 19.24  ? 59  GLU   A C   1 
ATOM   466  O O   . GLU   A 1 58  ? 36.922 33.485 -1.461  1.00 19.39  ? 59  GLU   A O   1 
ATOM   467  C CB  . GLU   A 1 58  ? 38.919 36.012 -2.240  1.00 26.46  ? 59  GLU   A CB  1 
ATOM   468  C CG  . GLU   A 1 58  ? 39.867 34.839 -2.290  1.00 33.46  ? 59  GLU   A CG  1 
ATOM   469  C CD  . GLU   A 1 58  ? 41.284 35.274 -2.606  1.00 40.10  ? 59  GLU   A CD  1 
ATOM   470  O OE1 . GLU   A 1 58  ? 42.068 35.476 -1.660  1.00 42.29  ? 59  GLU   A OE1 1 
ATOM   471  O OE2 . GLU   A 1 58  ? 41.600 35.430 -3.800  1.00 43.75  ? 59  GLU   A OE2 1 
ATOM   472  N N   . ASP   A 1 59  ? 36.811 35.252 -0.050  1.00 17.49  ? 60  ASP   A N   1 
ATOM   473  C CA  . ASP   A 1 59  ? 36.456 34.419 1.092   1.00 16.98  ? 60  ASP   A CA  1 
ATOM   474  C C   . ASP   A 1 59  ? 35.054 33.839 0.944   1.00 15.94  ? 60  ASP   A C   1 
ATOM   475  O O   . ASP   A 1 59  ? 34.825 32.684 1.307   1.00 16.61  ? 60  ASP   A O   1 
ATOM   476  C CB  . ASP   A 1 59  ? 36.571 35.223 2.387   1.00 18.77  ? 60  ASP   A CB  1 
ATOM   477  C CG  . ASP   A 1 59  ? 38.006 35.438 2.824   1.00 22.69  ? 60  ASP   A CG  1 
ATOM   478  O OD1 . ASP   A 1 59  ? 38.916 34.887 2.174   1.00 23.39  ? 60  ASP   A OD1 1 
ATOM   479  O OD2 . ASP   A 1 59  ? 38.210 36.150 3.840   1.00 25.48  ? 60  ASP   A OD2 1 
ATOM   480  N N   . ILE   A 1 60  ? 34.096 34.620 0.427   1.00 16.19  ? 61  ILE   A N   1 
ATOM   481  C CA  . ILE   A 1 60  ? 32.754 34.082 0.215   1.00 16.83  ? 61  ILE   A CA  1 
ATOM   482  C C   . ILE   A 1 60  ? 32.799 32.958 -0.806  1.00 16.20  ? 61  ILE   A C   1 
ATOM   483  O O   . ILE   A 1 60  ? 32.184 31.902 -0.623  1.00 17.12  ? 61  ILE   A O   1 
ATOM   484  C CB  . ILE   A 1 60  ? 31.778 35.188 -0.214  1.00 17.77  ? 61  ILE   A CB  1 
ATOM   485  C CG1 . ILE   A 1 60  ? 31.666 36.259 0.868   1.00 18.60  ? 61  ILE   A CG1 1 
ATOM   486  C CG2 . ILE   A 1 60  ? 30.406 34.581 -0.496  1.00 20.82  ? 61  ILE   A CG2 1 
ATOM   487  C CD1 . ILE   A 1 60  ? 30.824 37.437 0.491   1.00 20.80  ? 61  ILE   A CD1 1 
ATOM   488  N N   . GLU   A 1 61  ? 33.507 33.184 -1.917  1.00 16.92  ? 62  GLU   A N   1 
ATOM   489  C CA  . GLU   A 1 61  ? 33.582 32.184 -2.978  1.00 17.20  ? 62  GLU   A CA  1 
ATOM   490  C C   . GLU   A 1 61  ? 34.234 30.893 -2.496  1.00 16.66  ? 62  GLU   A C   1 
ATOM   491  O O   . GLU   A 1 61  ? 33.835 29.798 -2.918  1.00 17.04  ? 62  GLU   A O   1 
ATOM   492  C CB  . GLU   A 1 61  ? 34.294 32.764 -4.201  1.00 18.75  ? 62  GLU   A CB  1 
ATOM   493  C CG  . GLU   A 1 61  ? 33.412 33.812 -4.908  1.00 22.80  ? 62  GLU   A CG  1 
ATOM   494  C CD  . GLU   A 1 61  ? 34.056 34.467 -6.119  1.00 27.13  ? 62  GLU   A CD  1 
ATOM   495  O OE1 . GLU   A 1 61  ? 35.145 34.020 -6.519  1.00 31.21  ? 62  GLU   A OE1 1 
ATOM   496  O OE2 . GLU   A 1 61  ? 33.435 35.385 -6.714  1.00 27.28  ? 62  GLU   A OE2 1 
ATOM   497  N N   . ARG   A 1 62  ? 35.242 30.995 -1.614  1.00 16.93  ? 63  ARG   A N   1 
ATOM   498  C CA  . ARG   A 1 62  ? 35.870 29.799 -1.059  1.00 16.72  ? 63  ARG   A CA  1 
ATOM   499  C C   . ARG   A 1 62  ? 34.869 28.989 -0.248  1.00 16.75  ? 63  ARG   A C   1 
ATOM   500  O O   . ARG   A 1 62  ? 34.770 27.769 -0.402  1.00 16.73  ? 63  ARG   A O   1 
ATOM   501  C CB  . ARG   A 1 62  ? 37.070 30.174 -0.190  1.00 17.53  ? 63  ARG   A CB  1 
ATOM   502  C CG  . ARG   A 1 62  ? 37.790 28.943 0.367   1.00 18.97  ? 63  ARG   A CG  1 
ATOM   503  C CD  . ARG   A 1 62  ? 38.925 29.337 1.306   1.00 19.88  ? 63  ARG   A CD  1 
ATOM   504  N NE  . ARG   A 1 62  ? 39.900 30.139 0.583   1.00 21.38  ? 63  ARG   A NE  1 
ATOM   505  C CZ  . ARG   A 1 62  ? 40.057 31.442 0.757   1.00 23.25  ? 63  ARG   A CZ  1 
ATOM   506  N NH1 . ARG   A 1 62  ? 39.324 32.110 1.629   1.00 23.82  ? 63  ARG   A NH1 1 
ATOM   507  N NH2 . ARG   A 1 62  ? 40.960 32.090 0.027   1.00 25.03  ? 63  ARG   A NH2 1 
ATOM   508  N N   . GLU   A 1 63  ? 34.096 29.662 0.603   1.00 15.54  ? 64  GLU   A N   1 
ATOM   509  C CA  . GLU   A 1 63  ? 33.106 28.980 1.423   1.00 16.11  ? 64  GLU   A CA  1 
ATOM   510  C C   . GLU   A 1 63  ? 32.058 28.298 0.549   1.00 15.86  ? 64  GLU   A C   1 
ATOM   511  O O   . GLU   A 1 63  ? 31.726 27.121 0.759   1.00 16.07  ? 64  GLU   A O   1 
ATOM   512  C CB  . GLU   A 1 63  ? 32.499 29.955 2.436   1.00 17.36  ? 64  GLU   A CB  1 
ATOM   513  C CG  . GLU   A 1 63  ? 31.391 29.357 3.289   1.00 18.62  ? 64  GLU   A CG  1 
ATOM   514  C CD  . GLU   A 1 63  ? 30.758 30.335 4.304   1.00 22.98  ? 64  GLU   A CD  1 
ATOM   515  O OE1 . GLU   A 1 63  ? 31.255 31.464 4.474   1.00 25.95  ? 64  GLU   A OE1 1 
ATOM   516  O OE2 . GLU   A 1 63  ? 29.762 29.962 4.938   1.00 26.53  ? 64  GLU   A OE2 1 
ATOM   517  N N   . VAL   A 1 64  ? 31.562 29.006 -0.479  1.00 14.25  ? 65  VAL   A N   1 
ATOM   518  C CA  . VAL   A 1 64  ? 30.557 28.424 -1.367  1.00 14.62  ? 65  VAL   A CA  1 
ATOM   519  C C   . VAL   A 1 64  ? 31.125 27.223 -2.115  1.00 15.37  ? 65  VAL   A C   1 
ATOM   520  O O   . VAL   A 1 64  ? 30.465 26.183 -2.232  1.00 15.99  ? 65  VAL   A O   1 
ATOM   521  C CB  . VAL   A 1 64  ? 30.012 29.497 -2.325  1.00 15.50  ? 65  VAL   A CB  1 
ATOM   522  C CG1 . VAL   A 1 64  ? 29.172 28.845 -3.405  1.00 16.46  ? 65  VAL   A CG1 1 
ATOM   523  C CG2 . VAL   A 1 64  ? 29.202 30.509 -1.545  1.00 16.03  ? 65  VAL   A CG2 1 
ATOM   524  N N   . SER   A 1 65  ? 32.363 27.328 -2.606  1.00 15.22  ? 66  SER   A N   1 
ATOM   525  C CA  A SER   A 1 65  ? 32.956 26.227 -3.362  0.54 15.94  ? 66  SER   A CA  1 
ATOM   526  C CA  B SER   A 1 65  ? 32.924 26.217 -3.367  0.46 16.68  ? 66  SER   A CA  1 
ATOM   527  C C   . SER   A 1 65  ? 33.088 24.983 -2.488  1.00 15.00  ? 66  SER   A C   1 
ATOM   528  O O   . SER   A 1 65  ? 32.824 23.859 -2.938  1.00 16.92  ? 66  SER   A O   1 
ATOM   529  C CB  A SER   A 1 65  ? 34.334 26.649 -3.874  0.54 17.58  ? 66  SER   A CB  1 
ATOM   530  C CB  B SER   A 1 65  ? 34.255 26.618 -3.995  0.46 19.88  ? 66  SER   A CB  1 
ATOM   531  O OG  A SER   A 1 65  ? 35.003 25.572 -4.508  0.54 20.76  ? 66  SER   A OG  1 
ATOM   532  O OG  B SER   A 1 65  ? 35.229 26.830 -3.002  0.46 22.69  ? 66  SER   A OG  1 
ATOM   533  N N   . ILE   A 1 66  ? 33.495 25.172 -1.223  1.00 14.49  ? 67  ILE   A N   1 
ATOM   534  C CA  A ILE   A 1 66  ? 33.619 24.026 -0.331  0.60 14.84  ? 67  ILE   A CA  1 
ATOM   535  C CA  B ILE   A 1 66  ? 33.613 24.065 -0.267  0.40 15.07  ? 67  ILE   A CA  1 
ATOM   536  C C   . ILE   A 1 66  ? 32.251 23.423 -0.034  1.00 14.92  ? 67  ILE   A C   1 
ATOM   537  O O   . ILE   A 1 66  ? 32.083 22.196 -0.102  1.00 15.46  ? 67  ILE   A O   1 
ATOM   538  C CB  A ILE   A 1 66  ? 34.400 24.412 0.933   0.60 14.92  ? 67  ILE   A CB  1 
ATOM   539  C CB  B ILE   A 1 66  ? 34.204 24.587 1.059   0.40 15.67  ? 67  ILE   A CB  1 
ATOM   540  C CG1 A ILE   A 1 66  ? 35.878 24.508 0.560   0.60 16.28  ? 67  ILE   A CG1 1 
ATOM   541  C CG1 B ILE   A 1 66  ? 35.674 24.989 0.898   0.40 17.97  ? 67  ILE   A CG1 1 
ATOM   542  C CG2 A ILE   A 1 66  ? 34.220 23.372 2.039   0.60 17.51  ? 67  ILE   A CG2 1 
ATOM   543  C CG2 B ILE   A 1 66  ? 34.025 23.573 2.201   0.40 16.79  ? 67  ILE   A CG2 1 
ATOM   544  C CD1 A ILE   A 1 66  ? 36.689 25.201 1.597   0.60 15.81  ? 67  ILE   A CD1 1 
ATOM   545  C CD1 B ILE   A 1 66  ? 36.614 23.827 0.772   0.40 19.59  ? 67  ILE   A CD1 1 
ATOM   546  N N   . LEU   A 1 67  ? 31.250 24.260 0.265   1.00 14.29  ? 68  LEU   A N   1 
ATOM   547  C CA  . LEU   A 1 67  ? 29.911 23.744 0.517   1.00 15.93  ? 68  LEU   A CA  1 
ATOM   548  C C   . LEU   A 1 67  ? 29.393 22.949 -0.676  1.00 16.10  ? 68  LEU   A C   1 
ATOM   549  O O   . LEU   A 1 67  ? 28.739 21.912 -0.502  1.00 17.04  ? 68  LEU   A O   1 
ATOM   550  C CB  . LEU   A 1 67  ? 28.965 24.899 0.857   1.00 16.58  ? 68  LEU   A CB  1 
ATOM   551  C CG  . LEU   A 1 67  ? 29.165 25.507 2.239   1.00 17.89  ? 68  LEU   A CG  1 
ATOM   552  C CD1 . LEU   A 1 67  ? 28.343 26.777 2.372   1.00 19.06  ? 68  LEU   A CD1 1 
ATOM   553  C CD2 . LEU   A 1 67  ? 28.769 24.491 3.304   1.00 21.36  ? 68  LEU   A CD2 1 
ATOM   554  N N   . LYS   A 1 68  ? 29.661 23.421 -1.899  1.00 15.73  ? 69  LYS   A N   1 
ATOM   555  C CA  . LYS   A 1 68  ? 29.141 22.733 -3.076  1.00 17.27  ? 69  LYS   A CA  1 
ATOM   556  C C   . LYS   A 1 68  ? 29.753 21.349 -3.234  1.00 17.57  ? 69  LYS   A C   1 
ATOM   557  O O   . LYS   A 1 68  ? 29.103 20.450 -3.775  1.00 22.21  ? 69  LYS   A O   1 
ATOM   558  C CB  . LYS   A 1 68  ? 29.409 23.563 -4.327  1.00 18.64  ? 69  LYS   A CB  1 
ATOM   559  C CG  . LYS   A 1 68  ? 28.424 24.677 -4.500  1.00 21.15  ? 69  LYS   A CG  1 
ATOM   560  C CD  . LYS   A 1 68  ? 28.791 25.622 -5.640  1.00 25.18  ? 69  LYS   A CD  1 
ATOM   561  C CE  . LYS   A 1 68  ? 27.663 26.614 -5.849  1.00 28.53  ? 69  LYS   A CE  1 
ATOM   562  N NZ  . LYS   A 1 68  ? 27.949 27.684 -6.859  1.00 32.16  ? 69  LYS   A NZ  1 
ATOM   563  N N   . GLU   A 1 69  ? 30.989 21.154 -2.778  1.00 16.79  ? 70  GLU   A N   1 
ATOM   564  C CA  . GLU   A 1 69  ? 31.667 19.881 -2.969  1.00 19.44  ? 70  GLU   A CA  1 
ATOM   565  C C   . GLU   A 1 69  ? 31.200 18.820 -1.976  1.00 19.20  ? 70  GLU   A C   1 
ATOM   566  O O   . GLU   A 1 69  ? 31.226 17.631 -2.283  1.00 22.13  ? 70  GLU   A O   1 
ATOM   567  C CB  . GLU   A 1 69  ? 33.181 20.093 -2.825  1.00 24.88  ? 70  GLU   A CB  1 
ATOM   568  C CG  . GLU   A 1 69  ? 34.021 18.838 -2.967  1.00 30.02  ? 70  GLU   A CG  1 
ATOM   569  C CD  . GLU   A 1 69  ? 35.516 19.131 -2.918  1.00 33.61  ? 70  GLU   A CD  1 
ATOM   570  O OE1 . GLU   A 1 69  ? 35.903 20.322 -2.907  1.00 35.30  ? 70  GLU   A OE1 1 
ATOM   571  O OE2 . GLU   A 1 69  ? 36.296 18.158 -2.967  1.00 36.48  ? 70  GLU   A OE2 1 
ATOM   572  N N   . ILE   A 1 70  ? 30.758 19.213 -0.801  1.00 17.98  ? 71  ILE   A N   1 
ATOM   573  C CA  A ILE   A 1 70  ? 30.539 18.250 0.275   0.55 17.38  ? 71  ILE   A CA  1 
ATOM   574  C CA  B ILE   A 1 70  ? 30.530 18.287 0.303   0.45 17.83  ? 71  ILE   A CA  1 
ATOM   575  C C   . ILE   A 1 70  ? 29.104 17.741 0.259   1.00 17.35  ? 71  ILE   A C   1 
ATOM   576  O O   . ILE   A 1 70  ? 28.148 18.499 0.104   1.00 18.81  ? 71  ILE   A O   1 
ATOM   577  C CB  A ILE   A 1 70  ? 30.946 18.829 1.648   0.55 15.57  ? 71  ILE   A CB  1 
ATOM   578  C CB  B ILE   A 1 70  ? 30.779 18.998 1.638   0.45 17.25  ? 71  ILE   A CB  1 
ATOM   579  C CG1 A ILE   A 1 70  ? 30.106 20.056 2.027   0.55 16.43  ? 71  ILE   A CG1 1 
ATOM   580  C CG1 B ILE   A 1 70  ? 32.203 19.529 1.745   0.45 18.07  ? 71  ILE   A CG1 1 
ATOM   581  C CG2 A ILE   A 1 70  ? 32.428 19.172 1.653   0.55 16.49  ? 71  ILE   A CG2 1 
ATOM   582  C CG2 B ILE   A 1 70  ? 30.558 18.066 2.720   0.45 17.78  ? 71  ILE   A CG2 1 
ATOM   583  C CD1 A ILE   A 1 70  ? 30.620 20.785 3.255   0.55 18.52  ? 71  ILE   A CD1 1 
ATOM   584  C CD1 B ILE   A 1 70  ? 32.352 20.538 2.874   0.45 18.39  ? 71  ILE   A CD1 1 
ATOM   585  N N   . GLN   A 1 71  ? 28.955 16.422 0.410   1.00 16.72  ? 72  GLN   A N   1 
ATOM   586  C CA  . GLN   A 1 71  ? 27.657 15.763 0.601   1.00 18.00  ? 72  GLN   A CA  1 
ATOM   587  C C   . GLN   A 1 71  ? 27.845 14.594 1.568   1.00 17.12  ? 72  GLN   A C   1 
ATOM   588  O O   . GLN   A 1 71  ? 28.370 13.547 1.187   1.00 18.40  ? 72  GLN   A O   1 
ATOM   589  C CB  . GLN   A 1 71  ? 27.047 15.270 -0.709  1.00 25.35  ? 72  GLN   A CB  1 
ATOM   590  C CG  . GLN   A 1 71  ? 27.276 16.151 -1.941  1.00 34.33  ? 72  GLN   A CG  1 
ATOM   591  C CD  . GLN   A 1 71  ? 26.585 15.625 -3.185  1.00 40.65  ? 72  GLN   A CD  1 
ATOM   592  O OE1 . GLN   A 1 71  ? 27.236 15.129 -4.107  1.00 41.93  ? 72  GLN   A OE1 1 
ATOM   593  N NE2 . GLN   A 1 71  ? 25.257 15.699 -3.204  1.00 42.49  ? 72  GLN   A NE2 1 
ATOM   594  N N   . HIS   A 1 72  ? 27.385 14.762 2.812   1.00 15.50  ? 73  HIS   A N   1 
ATOM   595  C CA  . HIS   A 1 72  ? 27.581 13.759 3.856   1.00 14.55  ? 73  HIS   A CA  1 
ATOM   596  C C   . HIS   A 1 72  ? 26.562 14.017 4.952   1.00 15.05  ? 73  HIS   A C   1 
ATOM   597  O O   . HIS   A 1 72  ? 26.269 15.183 5.230   1.00 16.30  ? 73  HIS   A O   1 
ATOM   598  C CB  . HIS   A 1 72  ? 29.007 13.859 4.428   1.00 14.53  ? 73  HIS   A CB  1 
ATOM   599  C CG  . HIS   A 1 72  ? 29.324 12.802 5.438   1.00 14.42  ? 73  HIS   A CG  1 
ATOM   600  N ND1 . HIS   A 1 72  ? 28.979 12.920 6.776   1.00 14.84  ? 73  HIS   A ND1 1 
ATOM   601  C CD2 . HIS   A 1 72  ? 29.926 11.597 5.307   1.00 15.74  ? 73  HIS   A CD2 1 
ATOM   602  C CE1 . HIS   A 1 72  ? 29.360 11.828 7.413   1.00 15.57  ? 73  HIS   A CE1 1 
ATOM   603  N NE2 . HIS   A 1 72  ? 29.943 11.015 6.547   1.00 16.36  ? 73  HIS   A NE2 1 
ATOM   604  N N   . PRO   A 1 73  ? 26.026 12.980 5.600   1.00 15.47  ? 74  PRO   A N   1 
ATOM   605  C CA  . PRO   A 1 73  ? 24.984 13.218 6.618   1.00 17.95  ? 74  PRO   A CA  1 
ATOM   606  C C   . PRO   A 1 73  ? 25.404 14.122 7.756   1.00 14.91  ? 74  PRO   A C   1 
ATOM   607  O O   . PRO   A 1 73  ? 24.525 14.725 8.381   1.00 17.53  ? 74  PRO   A O   1 
ATOM   608  C CB  . PRO   A 1 73  ? 24.658 11.814 7.135   1.00 20.97  ? 74  PRO   A CB  1 
ATOM   609  C CG  . PRO   A 1 73  ? 25.074 10.889 6.059   1.00 20.94  ? 74  PRO   A CG  1 
ATOM   610  C CD  . PRO   A 1 73  ? 26.210 11.543 5.317   1.00 16.59  ? 74  PRO   A CD  1 
ATOM   611  N N   . ASN   A 1 74  ? 26.693 14.208 8.082   1.00 13.95  ? 75  ASN   A N   1 
ATOM   612  C CA  . ASN   A 1 74  ? 27.119 15.002 9.230   1.00 13.92  ? 75  ASN   A CA  1 
ATOM   613  C C   . ASN   A 1 74  ? 27.652 16.371 8.844   1.00 13.59  ? 75  ASN   A C   1 
ATOM   614  O O   . ASN   A 1 74  ? 28.267 17.046 9.672   1.00 14.29  ? 75  ASN   A O   1 
ATOM   615  C CB  . ASN   A 1 74  ? 28.091 14.227 10.122  1.00 14.78  ? 75  ASN   A CB  1 
ATOM   616  C CG  . ASN   A 1 74  ? 27.483 12.958 10.638  1.00 16.07  ? 75  ASN   A CG  1 
ATOM   617  O OD1 . ASN   A 1 74  ? 27.960 11.869 10.320  1.00 18.92  ? 75  ASN   A OD1 1 
ATOM   618  N ND2 . ASN   A 1 74  ? 26.424 13.080 11.441  1.00 16.68  ? 75  ASN   A ND2 1 
ATOM   619  N N   . VAL   A 1 75  ? 27.391 16.821 7.624   1.00 13.34  ? 76  VAL   A N   1 
ATOM   620  C CA  A VAL   A 1 75  ? 27.721 18.174 7.217   0.53 14.05  ? 76  VAL   A CA  1 
ATOM   621  C CA  B VAL   A 1 75  ? 27.713 18.184 7.232   0.47 13.83  ? 76  VAL   A CA  1 
ATOM   622  C C   . VAL   A 1 75  ? 26.490 18.800 6.577   1.00 14.61  ? 76  VAL   A C   1 
ATOM   623  O O   . VAL   A 1 75  ? 25.700 18.118 5.913   1.00 16.25  ? 76  VAL   A O   1 
ATOM   624  C CB  A VAL   A 1 75  ? 28.913 18.195 6.247   0.53 14.96  ? 76  VAL   A CB  1 
ATOM   625  C CB  B VAL   A 1 75  ? 28.918 18.258 6.284   0.47 14.06  ? 76  VAL   A CB  1 
ATOM   626  C CG1 A VAL   A 1 75  ? 29.255 19.589 5.944   0.53 16.78  ? 76  VAL   A CG1 1 
ATOM   627  C CG1 B VAL   A 1 75  ? 30.146 17.598 6.911   0.47 14.94  ? 76  VAL   A CG1 1 
ATOM   628  C CG2 A VAL   A 1 75  ? 30.121 17.460 6.837   0.53 16.02  ? 76  VAL   A CG2 1 
ATOM   629  C CG2 B VAL   A 1 75  ? 28.554 17.566 5.022   0.47 15.47  ? 76  VAL   A CG2 1 
ATOM   630  N N   . ILE   A 1 76  ? 26.339 20.113 6.766   1.00 15.25  ? 77  ILE   A N   1 
ATOM   631  C CA  . ILE   A 1 76  ? 25.174 20.819 6.236   1.00 16.78  ? 77  ILE   A CA  1 
ATOM   632  C C   . ILE   A 1 76  ? 25.229 20.843 4.707   1.00 17.60  ? 77  ILE   A C   1 
ATOM   633  O O   . ILE   A 1 76  ? 26.312 20.933 4.111   1.00 21.49  ? 77  ILE   A O   1 
ATOM   634  C CB  . ILE   A 1 76  ? 25.111 22.221 6.876   1.00 18.46  ? 77  ILE   A CB  1 
ATOM   635  C CG1 . ILE   A 1 76  ? 23.802 22.913 6.526   1.00 20.55  ? 77  ILE   A CG1 1 
ATOM   636  C CG2 . ILE   A 1 76  ? 26.258 23.120 6.388   1.00 20.07  ? 77  ILE   A CG2 1 
ATOM   637  C CD1 . ILE   A 1 76  ? 23.655 24.258 7.195   1.00 23.89  ? 77  ILE   A CD1 1 
ATOM   638  N N   . THR   A 1 77  ? 24.058 20.690 4.069   1.00 17.60  ? 78  THR   A N   1 
ATOM   639  C CA  . THR   A 1 77  ? 23.893 20.740 2.612   1.00 18.40  ? 78  THR   A CA  1 
ATOM   640  C C   . THR   A 1 77  ? 23.580 22.169 2.157   1.00 17.41  ? 78  THR   A C   1 
ATOM   641  O O   . THR   A 1 77  ? 22.711 22.840 2.731   1.00 22.63  ? 78  THR   A O   1 
ATOM   642  C CB  . THR   A 1 77  ? 22.707 19.840 2.218   1.00 19.90  ? 78  THR   A CB  1 
ATOM   643  O OG1 . THR   A 1 77  ? 23.024 18.472 2.534   1.00 24.13  ? 78  THR   A OG1 1 
ATOM   644  C CG2 . THR   A 1 77  ? 22.388 19.944 0.714   1.00 23.60  ? 78  THR   A CG2 1 
ATOM   645  N N   . LEU   A 1 78  ? 24.252 22.625 1.094   1.00 14.64  ? 79  LEU   A N   1 
ATOM   646  C CA  . LEU   A 1 78  ? 23.929 23.896 0.453   1.00 14.71  ? 79  LEU   A CA  1 
ATOM   647  C C   . LEU   A 1 78  ? 22.928 23.668 -0.675  1.00 13.85  ? 79  LEU   A C   1 
ATOM   648  O O   . LEU   A 1 78  ? 23.153 22.829 -1.549  1.00 17.57  ? 79  LEU   A O   1 
ATOM   649  C CB  . LEU   A 1 78  ? 25.201 24.542 -0.086  1.00 15.48  ? 79  LEU   A CB  1 
ATOM   650  C CG  . LEU   A 1 78  ? 25.006 25.828 -0.892  1.00 16.47  ? 79  LEU   A CG  1 
ATOM   651  C CD1 . LEU   A 1 78  ? 24.457 26.954 -0.052  1.00 17.44  ? 79  LEU   A CD1 1 
ATOM   652  C CD2 . LEU   A 1 78  ? 26.323 26.226 -1.533  1.00 19.04  ? 79  LEU   A CD2 1 
ATOM   653  N N   . HIS   A 1 79  ? 21.826 24.410 -0.658  1.00 13.83  ? 80  HIS   A N   1 
ATOM   654  C CA  . HIS   A 1 79  ? 20.767 24.276 -1.649  1.00 15.09  ? 80  HIS   A CA  1 
ATOM   655  C C   . HIS   A 1 79  ? 20.904 25.250 -2.816  1.00 15.81  ? 80  HIS   A C   1 
ATOM   656  O O   . HIS   A 1 79  ? 20.806 24.841 -3.977  1.00 17.85  ? 80  HIS   A O   1 
ATOM   657  C CB  . HIS   A 1 79  ? 19.408 24.459 -0.959  1.00 15.48  ? 80  HIS   A CB  1 
ATOM   658  C CG  . HIS   A 1 79  ? 18.253 24.274 -1.880  1.00 20.08  ? 80  HIS   A CG  1 
ATOM   659  N ND1 . HIS   A 1 79  ? 17.273 25.226 -2.076  1.00 25.46  ? 80  HIS   A ND1 1 
ATOM   660  C CD2 . HIS   A 1 79  ? 17.925 23.225 -2.667  1.00 22.15  ? 80  HIS   A CD2 1 
ATOM   661  C CE1 . HIS   A 1 79  ? 16.395 24.772 -2.952  1.00 25.16  ? 80  HIS   A CE1 1 
ATOM   662  N NE2 . HIS   A 1 79  ? 16.770 23.562 -3.331  1.00 25.97  ? 80  HIS   A NE2 1 
ATOM   663  N N   . GLU   A 1 80  ? 21.124 26.532 -2.539  1.00 15.34  ? 81  GLU   A N   1 
ATOM   664  C CA  . GLU   A 1 80  ? 21.196 27.557 -3.575  1.00 16.49  ? 81  GLU   A CA  1 
ATOM   665  C C   . GLU   A 1 80  ? 21.964 28.732 -3.012  1.00 14.05  ? 81  GLU   A C   1 
ATOM   666  O O   . GLU   A 1 80  ? 22.076 28.879 -1.784  1.00 14.39  ? 81  GLU   A O   1 
ATOM   667  C CB  . GLU   A 1 80  ? 19.805 28.138 -3.908  1.00 22.82  ? 81  GLU   A CB  1 
ATOM   668  C CG  . GLU   A 1 80  ? 18.761 27.307 -4.579  1.00 28.56  ? 81  GLU   A CG  1 
ATOM   669  C CD  . GLU   A 1 80  ? 17.767 28.209 -5.294  1.00 28.50  ? 81  GLU   A CD  1 
ATOM   670  O OE1 . GLU   A 1 80  ? 18.066 28.558 -6.452  1.00 29.15  ? 81  GLU   A OE1 1 
ATOM   671  O OE2 . GLU   A 1 80  ? 16.721 28.600 -4.722  1.00 29.02  ? 81  GLU   A OE2 1 
ATOM   672  N N   . VAL   A 1 81  ? 22.422 29.611 -3.904  1.00 14.66  ? 82  VAL   A N   1 
ATOM   673  C CA  . VAL   A 1 81  ? 23.093 30.850 -3.510  1.00 14.85  ? 82  VAL   A CA  1 
ATOM   674  C C   . VAL   A 1 81  ? 22.496 32.015 -4.286  1.00 14.68  ? 82  VAL   A C   1 
ATOM   675  O O   . VAL   A 1 81  ? 22.422 31.980 -5.522  1.00 16.66  ? 82  VAL   A O   1 
ATOM   676  C CB  . VAL   A 1 81  ? 24.616 30.806 -3.728  1.00 15.24  ? 82  VAL   A CB  1 
ATOM   677  C CG1 . VAL   A 1 81  ? 25.256 32.066 -3.178  1.00 16.84  ? 82  VAL   A CG1 1 
ATOM   678  C CG2 . VAL   A 1 81  ? 25.222 29.583 -3.084  1.00 17.37  ? 82  VAL   A CG2 1 
ATOM   679  N N   . TYR   A 1 82  ? 22.110 33.059 -3.567  1.00 15.23  ? 83  TYR   A N   1 
ATOM   680  C CA  . TYR   A 1 82  ? 21.648 34.314 -4.144  1.00 15.71  ? 83  TYR   A CA  1 
ATOM   681  C C   . TYR   A 1 82  ? 22.596 35.424 -3.732  1.00 15.82  ? 83  TYR   A C   1 
ATOM   682  O O   . TYR   A 1 82  ? 23.362 35.285 -2.773  1.00 16.75  ? 83  TYR   A O   1 
ATOM   683  C CB  . TYR   A 1 82  ? 20.238 34.684 -3.648  1.00 15.52  ? 83  TYR   A CB  1 
ATOM   684  C CG  . TYR   A 1 82  ? 19.148 33.804 -4.183  1.00 16.78  ? 83  TYR   A CG  1 
ATOM   685  C CD1 . TYR   A 1 82  ? 18.948 32.527 -3.669  1.00 17.49  ? 83  TYR   A CD1 1 
ATOM   686  C CD2 . TYR   A 1 82  ? 18.282 34.253 -5.179  1.00 17.02  ? 83  TYR   A CD2 1 
ATOM   687  C CE1 . TYR   A 1 82  ? 17.953 31.715 -4.153  1.00 19.86  ? 83  TYR   A CE1 1 
ATOM   688  C CE2 . TYR   A 1 82  ? 17.278 33.435 -5.680  1.00 18.77  ? 83  TYR   A CE2 1 
ATOM   689  C CZ  . TYR   A 1 82  ? 17.126 32.156 -5.146  1.00 18.42  ? 83  TYR   A CZ  1 
ATOM   690  O OH  . TYR   A 1 82  ? 16.127 31.327 -5.615  1.00 21.97  ? 83  TYR   A OH  1 
ATOM   691  N N   . GLU   A 1 83  ? 22.504 36.553 -4.427  1.00 16.24  ? 84  GLU   A N   1 
ATOM   692  C CA  . GLU   A 1 83  ? 23.289 37.701 -4.017  1.00 16.35  ? 84  GLU   A CA  1 
ATOM   693  C C   . GLU   A 1 83  ? 22.608 38.995 -4.424  1.00 17.82  ? 84  GLU   A C   1 
ATOM   694  O O   . GLU   A 1 83  ? 21.833 39.035 -5.382  1.00 17.95  ? 84  GLU   A O   1 
ATOM   695  C CB  . GLU   A 1 83  ? 24.721 37.583 -4.536  1.00 17.06  ? 84  GLU   A CB  1 
ATOM   696  C CG  . GLU   A 1 83  ? 24.879 37.955 -5.997  1.00 16.96  ? 84  GLU   A CG  1 
ATOM   697  C CD  . GLU   A 1 83  ? 26.336 37.923 -6.451  1.00 17.90  ? 84  GLU   A CD  1 
ATOM   698  O OE1 . GLU   A 1 83  ? 26.640 37.423 -7.546  1.00 18.01  ? 84  GLU   A OE1 1 
ATOM   699  O OE2 . GLU   A 1 83  ? 27.220 38.325 -5.670  1.00 19.74  ? 84  GLU   A OE2 1 
ATOM   700  N N   . ASN   A 1 84  ? 22.900 40.049 -3.672  1.00 17.86  ? 85  ASN   A N   1 
ATOM   701  C CA  . ASN   A 1 84  ? 22.465 41.405 -4.011  1.00 19.46  ? 85  ASN   A CA  1 
ATOM   702  C C   . ASN   A 1 84  ? 23.604 42.350 -3.652  1.00 20.92  ? 85  ASN   A C   1 
ATOM   703  O O   . ASN   A 1 84  ? 24.704 41.905 -3.313  1.00 21.04  ? 85  ASN   A O   1 
ATOM   704  C CB  . ASN   A 1 84  ? 21.113 41.726 -3.360  1.00 19.21  ? 85  ASN   A CB  1 
ATOM   705  C CG  . ASN   A 1 84  ? 21.167 41.725 -1.846  1.00 20.77  ? 85  ASN   A CG  1 
ATOM   706  O OD1 . ASN   A 1 84  ? 22.210 41.979 -1.228  1.00 21.32  ? 85  ASN   A OD1 1 
ATOM   707  N ND2 . ASN   A 1 84  ? 20.047 41.402 -1.238  1.00 25.14  ? 85  ASN   A ND2 1 
ATOM   708  N N   . LYS   A 1 85  ? 23.351 43.660 -3.722  1.00 22.25  ? 86  LYS   A N   1 
ATOM   709  C CA  . LYS   A 1 85  ? 24.437 44.614 -3.522  1.00 24.41  ? 86  LYS   A CA  1 
ATOM   710  C C   . LYS   A 1 85  ? 25.093 44.466 -2.155  1.00 22.79  ? 86  LYS   A C   1 
ATOM   711  O O   . LYS   A 1 85  ? 26.299 44.705 -2.020  1.00 23.57  ? 86  LYS   A O   1 
ATOM   712  C CB  . LYS   A 1 85  ? 23.925 46.043 -3.706  1.00 29.49  ? 86  LYS   A CB  1 
ATOM   713  C CG  . LYS   A 1 85  ? 23.699 46.448 -5.156  1.00 34.70  ? 86  LYS   A CG  1 
ATOM   714  C CD  . LYS   A 1 85  ? 24.961 46.287 -6.009  1.00 37.71  ? 86  LYS   A CD  1 
ATOM   715  C CE  . LYS   A 1 85  ? 26.087 47.212 -5.556  1.00 40.19  ? 86  LYS   A CE  1 
ATOM   716  N NZ  . LYS   A 1 85  ? 25.965 48.577 -6.122  1.00 41.86  ? 86  LYS   A NZ  1 
ATOM   717  N N   . THR   A 1 86  ? 24.323 44.088 -1.128  1.00 20.37  ? 87  THR   A N   1 
ATOM   718  C CA  . THR   A 1 86  ? 24.838 44.075 0.264   1.00 21.76  ? 87  THR   A CA  1 
ATOM   719  C C   . THR   A 1 86  ? 25.209 42.702 0.777   1.00 20.71  ? 87  THR   A C   1 
ATOM   720  O O   . THR   A 1 86  ? 26.058 42.626 1.659   1.00 21.24  ? 87  THR   A O   1 
ATOM   721  C CB  . THR   A 1 86  ? 23.727 44.646 1.145   1.00 25.08  ? 87  THR   A CB  1 
ATOM   722  O OG1 . THR   A 1 86  ? 22.573 43.826 1.016   1.00 28.63  ? 87  THR   A OG1 1 
ATOM   723  C CG2 . THR   A 1 86  ? 23.378 46.070 0.755   1.00 25.81  ? 87  THR   A CG2 1 
ATOM   724  N N   . ASP   A 1 87  ? 24.612 41.657 0.227   1.00 19.49  ? 88  ASP   A N   1 
ATOM   725  C CA  . ASP   A 1 87  ? 24.817 40.330 0.838   1.00 19.07  ? 88  ASP   A CA  1 
ATOM   726  C C   . ASP   A 1 87  ? 24.897 39.162 -0.131  1.00 16.74  ? 88  ASP   A C   1 
ATOM   727  O O   . ASP   A 1 87  ? 24.378 39.265 -1.241  1.00 18.34  ? 88  ASP   A O   1 
ATOM   728  C CB  . ASP   A 1 87  ? 23.604 39.958 1.676   1.00 23.09  ? 88  ASP   A CB  1 
ATOM   729  C CG  . ASP   A 1 87  ? 23.367 40.799 2.919   1.00 30.57  ? 88  ASP   A CG  1 
ATOM   730  O OD1 . ASP   A 1 87  ? 22.397 41.573 2.916   1.00 36.11  ? 88  ASP   A OD1 1 
ATOM   731  O OD2 . ASP   A 1 87  ? 24.132 40.644 3.886   1.00 32.85  ? 88  ASP   A OD2 1 
ATOM   732  N N   . VAL   A 1 88  ? 25.588 38.120 0.289   1.00 16.12  ? 89  VAL   A N   1 
ATOM   733  C CA  . VAL   A 1 88  ? 25.508 36.822 -0.422  1.00 16.74  ? 89  VAL   A CA  1 
ATOM   734  C C   . VAL   A 1 88  ? 24.585 36.014 0.505   1.00 16.19  ? 89  VAL   A C   1 
ATOM   735  O O   . VAL   A 1 88  ? 24.796 36.072 1.733   1.00 19.19  ? 89  VAL   A O   1 
ATOM   736  C CB  . VAL   A 1 88  ? 26.848 36.111 -0.666  1.00 17.41  ? 89  VAL   A CB  1 
ATOM   737  C CG1 . VAL   A 1 88  ? 26.646 34.688 -1.161  1.00 19.17  ? 89  VAL   A CG1 1 
ATOM   738  C CG2 . VAL   A 1 88  ? 27.715 36.890 -1.646  1.00 18.22  ? 89  VAL   A CG2 1 
ATOM   739  N N   . ILE   A 1 89  ? 23.587 35.334 -0.027  1.00 15.26  ? 90  ILE   A N   1 
ATOM   740  C CA  . ILE   A 1 89  ? 22.587 34.620 0.756   1.00 15.01  ? 90  ILE   A CA  1 
ATOM   741  C C   . ILE   A 1 89  ? 22.710 33.144 0.430   1.00 14.58  ? 90  ILE   A C   1 
ATOM   742  O O   . ILE   A 1 89  ? 22.423 32.726 -0.703  1.00 15.38  ? 90  ILE   A O   1 
ATOM   743  C CB  . ILE   A 1 89  ? 21.161 35.124 0.504   1.00 16.87  ? 90  ILE   A CB  1 
ATOM   744  C CG1 . ILE   A 1 89  ? 21.103 36.641 0.650   1.00 18.25  ? 90  ILE   A CG1 1 
ATOM   745  C CG2 . ILE   A 1 89  ? 20.172 34.411 1.442   1.00 18.68  ? 90  ILE   A CG2 1 
ATOM   746  C CD1 . ILE   A 1 89  ? 20.950 37.397 -0.646  1.00 22.65  ? 90  ILE   A CD1 1 
ATOM   747  N N   . LEU   A 1 90  ? 23.151 32.358 1.413   1.00 14.45  ? 91  LEU   A N   1 
ATOM   748  C CA  . LEU   A 1 90  ? 23.241 30.915 1.251   1.00 14.86  ? 91  LEU   A CA  1 
ATOM   749  C C   . LEU   A 1 90  ? 21.932 30.310 1.716   1.00 14.32  ? 91  LEU   A C   1 
ATOM   750  O O   . LEU   A 1 90  ? 21.518 30.531 2.860   1.00 16.67  ? 91  LEU   A O   1 
ATOM   751  C CB  . LEU   A 1 90  ? 24.365 30.326 2.098   1.00 16.54  ? 91  LEU   A CB  1 
ATOM   752  C CG  . LEU   A 1 90  ? 25.742 30.969 2.035   1.00 19.60  ? 91  LEU   A CG  1 
ATOM   753  C CD1 . LEU   A 1 90  ? 26.713 30.160 2.885   1.00 21.33  ? 91  LEU   A CD1 1 
ATOM   754  C CD2 . LEU   A 1 90  ? 26.204 31.052 0.616   1.00 21.73  ? 91  LEU   A CD2 1 
ATOM   755  N N   . ILE   A 1 91  ? 21.320 29.502 0.862   1.00 13.20  ? 92  ILE   A N   1 
ATOM   756  C CA  . ILE   A 1 91  ? 20.128 28.753 1.259   1.00 13.63  ? 92  ILE   A CA  1 
ATOM   757  C C   . ILE   A 1 91  ? 20.623 27.377 1.653   1.00 12.81  ? 92  ILE   A C   1 
ATOM   758  O O   . ILE   A 1 91  ? 21.058 26.607 0.791   1.00 14.17  ? 92  ILE   A O   1 
ATOM   759  C CB  . ILE   A 1 91  ? 19.076 28.667 0.144   1.00 14.89  ? 92  ILE   A CB  1 
ATOM   760  C CG1 . ILE   A 1 91  ? 18.701 30.055 -0.404  1.00 16.11  ? 92  ILE   A CG1 1 
ATOM   761  C CG2 . ILE   A 1 91  ? 17.858 27.875 0.646   1.00 15.77  ? 92  ILE   A CG2 1 
ATOM   762  C CD1 . ILE   A 1 91  ? 18.095 31.027 0.620   1.00 18.08  ? 92  ILE   A CD1 1 
ATOM   763  N N   . LEU   A 1 92  ? 20.605 27.094 2.956   1.00 14.04  ? 93  LEU   A N   1 
ATOM   764  C CA  . LEU   A 1 92  ? 21.169 25.895 3.545   1.00 14.66  ? 93  LEU   A CA  1 
ATOM   765  C C   . LEU   A 1 92  ? 20.075 24.982 4.070   1.00 13.98  ? 93  LEU   A C   1 
ATOM   766  O O   . LEU   A 1 92  ? 18.986 25.411 4.431   1.00 14.54  ? 93  LEU   A O   1 
ATOM   767  C CB  . LEU   A 1 92  ? 22.065 26.264 4.737   1.00 16.54  ? 93  LEU   A CB  1 
ATOM   768  C CG  . LEU   A 1 92  ? 23.248 27.172 4.423   1.00 18.64  ? 93  LEU   A CG  1 
ATOM   769  C CD1 . LEU   A 1 92  ? 23.737 27.804 5.706   1.00 22.00  ? 93  LEU   A CD1 1 
ATOM   770  C CD2 . LEU   A 1 92  ? 24.353 26.339 3.794   1.00 19.39  ? 93  LEU   A CD2 1 
ATOM   771  N N   . GLU   A 1 93  ? 20.411 23.712 4.162   1.00 15.74  ? 94  GLU   A N   1 
ATOM   772  C CA  . GLU   A 1 93  ? 19.571 22.768 4.874   1.00 16.81  ? 94  GLU   A CA  1 
ATOM   773  C C   . GLU   A 1 93  ? 19.266 23.293 6.281   1.00 16.44  ? 94  GLU   A C   1 
ATOM   774  O O   . GLU   A 1 93  ? 20.160 23.780 6.984   1.00 19.04  ? 94  GLU   A O   1 
ATOM   775  C CB  . GLU   A 1 93  ? 20.368 21.462 4.947   1.00 20.42  ? 94  GLU   A CB  1 
ATOM   776  C CG  . GLU   A 1 93  ? 19.764 20.361 5.723   1.00 21.65  ? 94  GLU   A CG  1 
ATOM   777  C CD  . GLU   A 1 93  ? 20.647 19.128 5.767   1.00 23.13  ? 94  GLU   A CD  1 
ATOM   778  O OE1 . GLU   A 1 93  ? 21.898 19.206 5.583   1.00 21.98  ? 94  GLU   A OE1 1 
ATOM   779  O OE2 . GLU   A 1 93  ? 20.061 18.051 5.921   1.00 27.37  ? 94  GLU   A OE2 1 
ATOM   780  N N   . LEU   A 1 94  ? 18.005 23.194 6.678   1.00 16.72  ? 95  LEU   A N   1 
ATOM   781  C CA  . LEU   A 1 94  ? 17.583 23.638 8.033   1.00 16.84  ? 95  LEU   A CA  1 
ATOM   782  C C   . LEU   A 1 94  ? 17.937 22.569 9.075   1.00 19.09  ? 95  LEU   A C   1 
ATOM   783  O O   . LEU   A 1 94  ? 17.573 21.407 8.881   1.00 21.71  ? 95  LEU   A O   1 
ATOM   784  C CB  . LEU   A 1 94  ? 16.082 23.910 8.052   1.00 17.84  ? 95  LEU   A CB  1 
ATOM   785  C CG  . LEU   A 1 94  ? 15.488 24.321 9.402   1.00 18.80  ? 95  LEU   A CG  1 
ATOM   786  C CD1 . LEU   A 1 94  ? 16.102 25.620 9.881   1.00 19.88  ? 95  LEU   A CD1 1 
ATOM   787  C CD2 . LEU   A 1 94  ? 13.982 24.448 9.317   1.00 21.31  ? 95  LEU   A CD2 1 
ATOM   788  N N   . VAL   A 1 95  ? 18.667 22.976 10.100  1.00 18.18  ? 96  VAL   A N   1 
ATOM   789  C CA  . VAL   A 1 95  ? 18.984 22.061 11.235  1.00 19.66  ? 96  VAL   A CA  1 
ATOM   790  C C   . VAL   A 1 95  ? 18.263 22.704 12.431  1.00 21.74  ? 96  VAL   A C   1 
ATOM   791  O O   . VAL   A 1 95  ? 18.744 23.718 12.921  1.00 24.39  ? 96  VAL   A O   1 
ATOM   792  C CB  . VAL   A 1 95  ? 20.505 21.910 11.363  1.00 20.07  ? 96  VAL   A CB  1 
ATOM   793  C CG1 . VAL   A 1 95  ? 20.869 20.836 12.380  1.00 22.39  ? 96  VAL   A CG1 1 
ATOM   794  C CG2 . VAL   A 1 95  ? 21.138 21.577 10.017  1.00 21.92  ? 96  VAL   A CG2 1 
ATOM   795  N N   . ALA   A 1 96  ? 17.174 22.089 12.882  1.00 22.55  ? 97  ALA   A N   1 
ATOM   796  C CA  . ALA   A 1 96  ? 16.273 22.787 13.831  1.00 25.36  ? 97  ALA   A CA  1 
ATOM   797  C C   . ALA   A 1 96  ? 16.435 22.443 15.312  1.00 24.37  ? 97  ALA   A C   1 
ATOM   798  O O   . ALA   A 1 96  ? 15.655 23.001 16.099  1.00 26.59  ? 97  ALA   A O   1 
ATOM   799  C CB  . ALA   A 1 96  ? 14.866 22.495 13.383  1.00 27.28  ? 97  ALA   A CB  1 
ATOM   800  N N   . GLY   A 1 97  ? 17.402 21.622 15.691  1.00 22.00  ? 98  GLY   A N   1 
ATOM   801  C CA  . GLY   A 1 97  ? 17.501 21.196 17.102  1.00 21.72  ? 98  GLY   A CA  1 
ATOM   802  C C   . GLY   A 1 97  ? 18.472 22.030 17.905  1.00 22.15  ? 98  GLY   A C   1 
ATOM   803  O O   . GLY   A 1 97  ? 18.799 21.634 19.027  1.00 23.57  ? 98  GLY   A O   1 
ATOM   804  N N   . GLY   A 1 98  ? 18.950 23.121 17.338  1.00 22.75  ? 99  GLY   A N   1 
ATOM   805  C CA  . GLY   A 1 98  ? 19.829 24.019 18.087  1.00 23.59  ? 99  GLY   A CA  1 
ATOM   806  C C   . GLY   A 1 98  ? 21.285 23.611 18.097  1.00 23.34  ? 99  GLY   A C   1 
ATOM   807  O O   . GLY   A 1 98  ? 21.610 22.551 17.557  1.00 23.22  ? 99  GLY   A O   1 
ATOM   808  N N   . GLU   A 1 99  ? 22.102 24.410 18.766  1.00 25.29  ? 100 GLU   A N   1 
ATOM   809  C CA  . GLU   A 1 99  ? 23.537 24.209 18.808  1.00 26.27  ? 100 GLU   A CA  1 
ATOM   810  C C   . GLU   A 1 99  ? 23.882 23.173 19.866  1.00 23.19  ? 100 GLU   A C   1 
ATOM   811  O O   . GLU   A 1 99  ? 23.233 23.075 20.914  1.00 23.74  ? 100 GLU   A O   1 
ATOM   812  C CB  . GLU   A 1 99  ? 24.208 25.506 19.257  1.00 30.87  ? 100 GLU   A CB  1 
ATOM   813  C CG  . GLU   A 1 99  ? 24.305 26.602 18.214  1.00 35.20  ? 100 GLU   A CG  1 
ATOM   814  C CD  . GLU   A 1 99  ? 24.531 27.946 18.888  1.00 39.98  ? 100 GLU   A CD  1 
ATOM   815  O OE1 . GLU   A 1 99  ? 25.274 27.995 19.893  1.00 39.87  ? 100 GLU   A OE1 1 
ATOM   816  O OE2 . GLU   A 1 99  ? 23.915 28.943 18.453  1.00 44.12  ? 100 GLU   A OE2 1 
ATOM   817  N N   . LEU   A 1 100 ? 24.953 22.432 19.614  1.00 22.98  ? 101 LEU   A N   1 
ATOM   818  C CA  . LEU   A 1 100 ? 25.503 21.578 20.652  1.00 22.86  ? 101 LEU   A CA  1 
ATOM   819  C C   . LEU   A 1 100 ? 25.911 22.399 21.871  1.00 23.97  ? 101 LEU   A C   1 
ATOM   820  O O   . LEU   A 1 100 ? 25.758 21.937 23.003  1.00 25.08  ? 101 LEU   A O   1 
ATOM   821  C CB  . LEU   A 1 100 ? 26.672 20.775 20.091  1.00 22.76  ? 101 LEU   A CB  1 
ATOM   822  C CG  . LEU   A 1 100 ? 27.390 19.841 21.071  1.00 23.02  ? 101 LEU   A CG  1 
ATOM   823  C CD1 . LEU   A 1 100 ? 26.454 18.755 21.575  1.00 23.41  ? 101 LEU   A CD1 1 
ATOM   824  C CD2 . LEU   A 1 100 ? 28.583 19.239 20.364  1.00 22.60  ? 101 LEU   A CD2 1 
ATOM   825  N N   . PHE   A 1 101 ? 26.399 23.628 21.658  1.00 23.56  ? 102 PHE   A N   1 
ATOM   826  C CA  . PHE   A 1 101 ? 26.703 24.533 22.765  1.00 25.08  ? 102 PHE   A CA  1 
ATOM   827  C C   . PHE   A 1 101 ? 25.515 24.682 23.722  1.00 25.79  ? 102 PHE   A C   1 
ATOM   828  O O   . PHE   A 1 101 ? 25.665 24.638 24.954  1.00 25.44  ? 102 PHE   A O   1 
ATOM   829  C CB  . PHE   A 1 101 ? 27.084 25.897 22.183  1.00 26.11  ? 102 PHE   A CB  1 
ATOM   830  C CG  . PHE   A 1 101 ? 27.385 26.935 23.221  1.00 26.61  ? 102 PHE   A CG  1 
ATOM   831  C CD1 . PHE   A 1 101 ? 28.658 27.047 23.751  1.00 28.41  ? 102 PHE   A CD1 1 
ATOM   832  C CD2 . PHE   A 1 101 ? 26.393 27.789 23.681  1.00 28.83  ? 102 PHE   A CD2 1 
ATOM   833  C CE1 . PHE   A 1 101 ? 28.940 28.001 24.714  1.00 29.83  ? 102 PHE   A CE1 1 
ATOM   834  C CE2 . PHE   A 1 101 ? 26.668 28.742 24.650  1.00 29.90  ? 102 PHE   A CE2 1 
ATOM   835  C CZ  . PHE   A 1 101 ? 27.943 28.847 25.167  1.00 30.49  ? 102 PHE   A CZ  1 
ATOM   836  N N   . ASP   A 1 102 ? 24.324 24.903 23.174  1.00 28.45  ? 103 ASP   A N   1 
ATOM   837  C CA  . ASP   A 1 102 ? 23.164 25.147 24.022  1.00 30.50  ? 103 ASP   A CA  1 
ATOM   838  C C   . ASP   A 1 102 ? 22.665 23.861 24.670  1.00 29.01  ? 103 ASP   A C   1 
ATOM   839  O O   . ASP   A 1 102 ? 22.160 23.891 25.797  1.00 30.41  ? 103 ASP   A O   1 
ATOM   840  C CB  . ASP   A 1 102 ? 22.084 25.803 23.168  1.00 35.04  ? 103 ASP   A CB  1 
ATOM   841  C CG  . ASP   A 1 102 ? 22.356 27.279 22.937  1.00 41.30  ? 103 ASP   A CG  1 
ATOM   842  O OD1 . ASP   A 1 102 ? 22.990 27.911 23.810  1.00 44.15  ? 103 ASP   A OD1 1 
ATOM   843  O OD2 . ASP   A 1 102 ? 21.974 27.799 21.868  1.00 44.04  ? 103 ASP   A OD2 1 
ATOM   844  N N   . PHE   A 1 103 ? 22.824 22.733 23.979  1.00 26.90  ? 104 PHE   A N   1 
ATOM   845  C CA  . PHE   A 1 103 ? 22.490 21.428 24.537  1.00 27.11  ? 104 PHE   A CA  1 
ATOM   846  C C   . PHE   A 1 103 ? 23.372 21.104 25.735  1.00 25.91  ? 104 PHE   A C   1 
ATOM   847  O O   . PHE   A 1 103 ? 22.882 20.640 26.776  1.00 26.90  ? 104 PHE   A O   1 
ATOM   848  C CB  . PHE   A 1 103 ? 22.584 20.400 23.395  1.00 25.40  ? 104 PHE   A CB  1 
ATOM   849  C CG  . PHE   A 1 103 ? 22.172 19.004 23.769  1.00 26.22  ? 104 PHE   A CG  1 
ATOM   850  C CD1 . PHE   A 1 103 ? 23.084 18.128 24.350  1.00 27.94  ? 104 PHE   A CD1 1 
ATOM   851  C CD2 . PHE   A 1 103 ? 20.843 18.612 23.675  1.00 27.29  ? 104 PHE   A CD2 1 
ATOM   852  C CE1 . PHE   A 1 103 ? 22.707 16.845 24.711  1.00 28.86  ? 104 PHE   A CE1 1 
ATOM   853  C CE2 . PHE   A 1 103 ? 20.457 17.349 24.061  1.00 29.43  ? 104 PHE   A CE2 1 
ATOM   854  C CZ  . PHE   A 1 103 ? 21.388 16.462 24.584  1.00 29.38  ? 104 PHE   A CZ  1 
ATOM   855  N N   . LEU   A 1 104 ? 24.669 21.396 25.624  1.00 26.19  ? 105 LEU   A N   1 
ATOM   856  C CA  . LEU   A 1 104 ? 25.609 21.159 26.712  1.00 29.52  ? 105 LEU   A CA  1 
ATOM   857  C C   . LEU   A 1 104 ? 25.325 22.075 27.887  1.00 32.72  ? 105 LEU   A C   1 
ATOM   858  O O   . LEU   A 1 104 ? 25.487 21.676 29.048  1.00 32.53  ? 105 LEU   A O   1 
ATOM   859  C CB  . LEU   A 1 104 ? 27.018 21.433 26.204  1.00 29.06  ? 105 LEU   A CB  1 
ATOM   860  C CG  . LEU   A 1 104 ? 27.464 20.474 25.118  1.00 30.68  ? 105 LEU   A CG  1 
ATOM   861  C CD1 . LEU   A 1 104 ? 28.819 20.892 24.559  1.00 30.38  ? 105 LEU   A CD1 1 
ATOM   862  C CD2 . LEU   A 1 104 ? 27.503 19.073 25.703  1.00 30.93  ? 105 LEU   A CD2 1 
ATOM   863  N N   . ALA   A 1 105 ? 24.943 23.321 27.608  1.00 35.74  ? 106 ALA   A N   1 
ATOM   864  C CA  . ALA   A 1 105 ? 24.623 24.237 28.696  1.00 39.76  ? 106 ALA   A CA  1 
ATOM   865  C C   . ALA   A 1 105 ? 23.461 23.713 29.529  1.00 42.89  ? 106 ALA   A C   1 
ATOM   866  O O   . ALA   A 1 105 ? 23.394 23.976 30.736  1.00 43.75  ? 106 ALA   A O   1 
ATOM   867  C CB  . ALA   A 1 105 ? 24.330 25.630 28.140  1.00 40.73  ? 106 ALA   A CB  1 
ATOM   868  N N   . GLU   A 1 106 ? 22.595 22.903 28.936  1.00 45.87  ? 107 GLU   A N   1 
ATOM   869  C CA  . GLU   A 1 106 ? 21.424 22.361 29.673  1.00 50.15  ? 107 GLU   A CA  1 
ATOM   870  C C   . GLU   A 1 106 ? 21.858 21.148 30.500  1.00 49.37  ? 107 GLU   A C   1 
ATOM   871  O O   . GLU   A 1 106 ? 21.383 21.007 31.632  1.00 48.47  ? 107 GLU   A O   1 
ATOM   872  C CB  . GLU   A 1 106 ? 20.327 21.960 28.693  1.00 56.59  ? 107 GLU   A CB  1 
ATOM   873  C CG  . GLU   A 1 106 ? 19.074 21.389 29.349  1.00 63.05  ? 107 GLU   A CG  1 
ATOM   874  C CD  . GLU   A 1 106 ? 17.985 21.071 28.338  1.00 68.40  ? 107 GLU   A CD  1 
ATOM   875  O OE1 . GLU   A 1 106 ? 18.225 21.276 27.132  1.00 71.09  ? 107 GLU   A OE1 1 
ATOM   876  O OE2 . GLU   A 1 106 ? 16.895 20.626 28.748  1.00 69.76  ? 107 GLU   A OE2 1 
ATOM   877  N N   . LYS   A 1 107 ? 22.756 20.328 29.970  1.00 49.73  ? 108 LYS   A N   1 
ATOM   878  C CA  . LYS   A 1 107 ? 23.135 19.077 30.666  1.00 50.20  ? 108 LYS   A CA  1 
ATOM   879  C C   . LYS   A 1 107 ? 24.319 19.282 31.619  1.00 48.16  ? 108 LYS   A C   1 
ATOM   880  O O   . LYS   A 1 107 ? 24.555 18.372 32.429  1.00 47.04  ? 108 LYS   A O   1 
ATOM   881  C CB  . LYS   A 1 107 ? 23.479 18.069 29.568  1.00 52.25  ? 108 LYS   A CB  1 
ATOM   882  C CG  . LYS   A 1 107 ? 22.277 17.673 28.731  1.00 54.48  ? 108 LYS   A CG  1 
ATOM   883  C CD  . LYS   A 1 107 ? 22.461 16.404 27.914  1.00 56.20  ? 108 LYS   A CD  1 
ATOM   884  C CE  . LYS   A 1 107 ? 22.375 15.136 28.688  1.00 57.48  ? 108 LYS   A CE  1 
ATOM   885  N NZ  . LYS   A 1 107 ? 22.407 13.996 27.767  1.00 58.26  ? 108 LYS   A NZ  1 
ATOM   886  N N   . GLU   A 1 108 ? 25.029 20.401 31.514  1.00 47.64  ? 109 GLU   A N   1 
ATOM   887  C CA  . GLU   A 1 108 ? 26.245 20.665 32.329  1.00 47.78  ? 109 GLU   A CA  1 
ATOM   888  C C   . GLU   A 1 108 ? 27.421 19.843 31.776  1.00 40.40  ? 109 GLU   A C   1 
ATOM   889  O O   . GLU   A 1 108 ? 28.386 20.456 31.299  1.00 39.71  ? 109 GLU   A O   1 
ATOM   890  C CB  . GLU   A 1 108 ? 26.033 20.392 33.821  1.00 55.19  ? 109 GLU   A CB  1 
ATOM   891  C CG  . GLU   A 1 108 ? 27.114 21.008 34.702  1.00 62.18  ? 109 GLU   A CG  1 
ATOM   892  C CD  . GLU   A 1 108 ? 26.549 21.698 35.930  1.00 67.60  ? 109 GLU   A CD  1 
ATOM   893  O OE1 . GLU   A 1 108 ? 25.906 21.017 36.757  1.00 69.42  ? 109 GLU   A OE1 1 
ATOM   894  O OE2 . GLU   A 1 108 ? 26.738 22.927 36.046  1.00 69.60  ? 109 GLU   A OE2 1 
ATOM   895  N N   . SER   A 1 109 ? 27.362 18.515 31.903  1.00 34.44  ? 110 SER   A N   1 
ATOM   896  C CA  . SER   A 1 109 ? 28.405 17.622 31.331  1.00 30.16  ? 110 SER   A CA  1 
ATOM   897  C C   . SER   A 1 109 ? 27.730 16.367 30.781  1.00 26.23  ? 110 SER   A C   1 
ATOM   898  O O   . SER   A 1 109 ? 26.611 16.060 31.206  1.00 26.97  ? 110 SER   A O   1 
ATOM   899  C CB  . SER   A 1 109 ? 29.481 17.246 32.315  1.00 30.37  ? 110 SER   A CB  1 
ATOM   900  O OG  . SER   A 1 109 ? 28.966 16.418 33.347  1.00 33.27  ? 110 SER   A OG  1 
ATOM   901  N N   . LEU   A 1 110 ? 28.400 15.712 29.845  1.00 20.88  ? 111 LEU   A N   1 
ATOM   902  C CA  . LEU   A 1 110 ? 27.878 14.476 29.285  1.00 20.28  ? 111 LEU   A CA  1 
ATOM   903  C C   . LEU   A 1 110 ? 28.617 13.276 29.864  1.00 21.38  ? 111 LEU   A C   1 
ATOM   904  O O   . LEU   A 1 110 ? 29.806 13.353 30.195  1.00 21.55  ? 111 LEU   A O   1 
ATOM   905  C CB  . LEU   A 1 110 ? 28.074 14.467 27.773  1.00 20.21  ? 111 LEU   A CB  1 
ATOM   906  C CG  . LEU   A 1 110 ? 27.437 15.613 26.994  1.00 20.46  ? 111 LEU   A CG  1 
ATOM   907  C CD1 . LEU   A 1 110 ? 27.613 15.394 25.518  1.00 21.87  ? 111 LEU   A CD1 1 
ATOM   908  C CD2 . LEU   A 1 110 ? 25.968 15.767 27.335  1.00 23.60  ? 111 LEU   A CD2 1 
ATOM   909  N N   . THR   A 1 111 ? 27.896 12.161 29.997  1.00 21.58  ? 112 THR   A N   1 
ATOM   910  C CA  . THR   A 1 111 ? 28.535 10.877 30.267  1.00 20.90  ? 112 THR   A CA  1 
ATOM   911  C C   . THR   A 1 111 ? 29.470 10.497 29.122  1.00 19.66  ? 112 THR   A C   1 
ATOM   912  O O   . THR   A 1 111 ? 29.397 11.042 28.027  1.00 18.18  ? 112 THR   A O   1 
ATOM   913  C CB  . THR   A 1 111 ? 27.468 9.801  30.486  1.00 21.74  ? 112 THR   A CB  1 
ATOM   914  O OG1 . THR   A 1 111 ? 26.884 9.430  29.222  1.00 21.49  ? 112 THR   A OG1 1 
ATOM   915  C CG2 . THR   A 1 111 ? 26.378 10.266 31.443  1.00 24.10  ? 112 THR   A CG2 1 
ATOM   916  N N   . GLU   A 1 112 ? 30.382 9.566  29.386  1.00 18.62  ? 113 GLU   A N   1 
ATOM   917  C CA  . GLU   A 1 112 ? 31.273 9.103  28.327  1.00 18.74  ? 113 GLU   A CA  1 
ATOM   918  C C   . GLU   A 1 112 ? 30.477 8.495  27.183  1.00 17.90  ? 113 GLU   A C   1 
ATOM   919  O O   . GLU   A 1 112 ? 30.800 8.715  26.012  1.00 19.44  ? 113 GLU   A O   1 
ATOM   920  C CB  . GLU   A 1 112 ? 32.295 8.103  28.857  1.00 18.21  ? 113 GLU   A CB  1 
ATOM   921  C CG  . GLU   A 1 112 ? 33.433 8.743  29.596  1.00 19.94  ? 113 GLU   A CG  1 
ATOM   922  C CD  . GLU   A 1 112 ? 34.375 7.729  30.121  1.00 19.02  ? 113 GLU   A CD  1 
ATOM   923  O OE1 . GLU   A 1 112 ? 34.939 6.981  29.279  1.00 18.60  ? 113 GLU   A OE1 1 
ATOM   924  O OE2 . GLU   A 1 112 ? 34.589 7.679  31.352  1.00 21.50  ? 113 GLU   A OE2 1 
ATOM   925  N N   . GLU   A 1 113 ? 29.411 7.758  27.488  1.00 18.39  ? 114 GLU   A N   1 
ATOM   926  C CA  . GLU   A 1 113 ? 28.616 7.185  26.412  1.00 19.40  ? 114 GLU   A CA  1 
ATOM   927  C C   . GLU   A 1 113 ? 27.907 8.267  25.605  1.00 18.68  ? 114 GLU   A C   1 
ATOM   928  O O   . GLU   A 1 113 ? 27.884 8.203  24.375  1.00 19.27  ? 114 GLU   A O   1 
ATOM   929  C CB  . GLU   A 1 113 ? 27.629 6.167  26.972  1.00 23.12  ? 114 GLU   A CB  1 
ATOM   930  C CG  . GLU   A 1 113 ? 28.283 4.858  27.408  1.00 27.61  ? 114 GLU   A CG  1 
ATOM   931  C CD  . GLU   A 1 113 ? 28.617 3.964  26.231  1.00 34.35  ? 114 GLU   A CD  1 
ATOM   932  O OE1 . GLU   A 1 113 ? 27.684 3.616  25.479  1.00 38.23  ? 114 GLU   A OE1 1 
ATOM   933  O OE2 . GLU   A 1 113 ? 29.799 3.611  26.047  1.00 36.59  ? 114 GLU   A OE2 1 
ATOM   934  N N   . GLU   A 1 114 ? 27.329 9.275  26.277  1.00 16.75  ? 115 GLU   A N   1 
ATOM   935  C CA  . GLU   A 1 114 ? 26.667 10.372 25.566  1.00 18.63  ? 115 GLU   A CA  1 
ATOM   936  C C   . GLU   A 1 114 ? 27.682 11.153 24.745  1.00 17.57  ? 115 GLU   A C   1 
ATOM   937  O O   . GLU   A 1 114 ? 27.424 11.510 23.589  1.00 18.72  ? 115 GLU   A O   1 
ATOM   938  C CB  . GLU   A 1 114 ? 26.003 11.298 26.592  1.00 20.69  ? 115 GLU   A CB  1 
ATOM   939  C CG  . GLU   A 1 114 ? 24.669 10.815 27.138  1.00 25.44  ? 115 GLU   A CG  1 
ATOM   940  C CD  . GLU   A 1 114 ? 24.277 11.478 28.458  1.00 30.09  ? 115 GLU   A CD  1 
ATOM   941  O OE1 . GLU   A 1 114 ? 25.019 12.355 28.970  1.00 26.93  ? 115 GLU   A OE1 1 
ATOM   942  O OE2 . GLU   A 1 114 ? 23.209 11.121 28.974  1.00 32.81  ? 115 GLU   A OE2 1 
ATOM   943  N N   . ALA   A 1 115 ? 28.846 11.429 25.329  1.00 17.18  ? 116 ALA   A N   1 
ATOM   944  C CA  . ALA   A 1 115 ? 29.895 12.141 24.613  1.00 17.32  ? 116 ALA   A CA  1 
ATOM   945  C C   . ALA   A 1 115 ? 30.347 11.356 23.391  1.00 16.85  ? 116 ALA   A C   1 
ATOM   946  O O   . ALA   A 1 115 ? 30.534 11.940 22.318  1.00 18.84  ? 116 ALA   A O   1 
ATOM   947  C CB  . ALA   A 1 115 ? 31.082 12.422 25.540  1.00 18.37  ? 116 ALA   A CB  1 
ATOM   948  N N   . THR   A 1 116 ? 30.535 10.038 23.528  1.00 17.85  ? 117 THR   A N   1 
ATOM   949  C CA  A THR   A 1 116 ? 31.012 9.288  22.369  0.55 17.92  ? 117 THR   A CA  1 
ATOM   950  C CA  B THR   A 1 116 ? 30.989 9.225  22.401  0.45 17.21  ? 117 THR   A CA  1 
ATOM   951  C C   . THR   A 1 116 ? 29.960 9.190  21.283  1.00 18.16  ? 117 THR   A C   1 
ATOM   952  O O   . THR   A 1 116 ? 30.321 9.138  20.102  1.00 18.66  ? 117 THR   A O   1 
ATOM   953  C CB  A THR   A 1 116 ? 31.591 7.916  22.726  0.55 18.88  ? 117 THR   A CB  1 
ATOM   954  C CB  B THR   A 1 116 ? 31.332 7.813  22.884  0.45 17.03  ? 117 THR   A CB  1 
ATOM   955  O OG1 A THR   A 1 116 ? 30.620 7.118  23.399  0.55 20.35  ? 117 THR   A OG1 1 
ATOM   956  O OG1 B THR   A 1 116 ? 32.275 7.901  23.960  0.45 18.61  ? 117 THR   A OG1 1 
ATOM   957  C CG2 A THR   A 1 116 ? 32.809 8.086  23.575  0.55 18.41  ? 117 THR   A CG2 1 
ATOM   958  C CG2 B THR   A 1 116 ? 31.928 6.985  21.751  0.45 18.41  ? 117 THR   A CG2 1 
ATOM   959  N N   . GLU   A 1 117 ? 28.675 9.214  21.637  1.00 16.98  ? 118 GLU   A N   1 
ATOM   960  C CA  . GLU   A 1 117 ? 27.639 9.197  20.613  1.00 19.37  ? 118 GLU   A CA  1 
ATOM   961  C C   . GLU   A 1 117 ? 27.711 10.455 19.759  1.00 19.66  ? 118 GLU   A C   1 
ATOM   962  O O   . GLU   A 1 117 ? 27.545 10.391 18.535  1.00 19.48  ? 118 GLU   A O   1 
ATOM   963  C CB  . GLU   A 1 117 ? 26.267 9.056  21.268  1.00 24.95  ? 118 GLU   A CB  1 
ATOM   964  C CG  . GLU   A 1 117 ? 25.941 7.611  21.597  1.00 33.12  ? 118 GLU   A CG  1 
ATOM   965  C CD  . GLU   A 1 117 ? 25.825 6.742  20.349  1.00 42.62  ? 118 GLU   A CD  1 
ATOM   966  O OE1 . GLU   A 1 117 ? 26.716 5.889  20.129  1.00 45.82  ? 118 GLU   A OE1 1 
ATOM   967  O OE2 . GLU   A 1 117 ? 24.858 6.928  19.577  1.00 45.42  ? 118 GLU   A OE2 1 
ATOM   968  N N   . PHE   A 1 118 ? 27.960 11.611 20.378  1.00 16.60  ? 119 PHE   A N   1 
ATOM   969  C CA  . PHE   A 1 118 ? 28.172 12.833 19.602  1.00 17.44  ? 119 PHE   A CA  1 
ATOM   970  C C   . PHE   A 1 118 ? 29.497 12.785 18.871  1.00 16.50  ? 119 PHE   A C   1 
ATOM   971  O O   . PHE   A 1 118 ? 29.578 13.139 17.686  1.00 16.72  ? 119 PHE   A O   1 
ATOM   972  C CB  . PHE   A 1 118 ? 28.188 14.054 20.521  1.00 17.96  ? 119 PHE   A CB  1 
ATOM   973  C CG  . PHE   A 1 118 ? 26.832 14.530 20.932  1.00 18.09  ? 119 PHE   A CG  1 
ATOM   974  C CD1 . PHE   A 1 118 ? 25.919 14.999 19.992  1.00 19.68  ? 119 PHE   A CD1 1 
ATOM   975  C CD2 . PHE   A 1 118 ? 26.470 14.535 22.263  1.00 19.46  ? 119 PHE   A CD2 1 
ATOM   976  C CE1 . PHE   A 1 118 ? 24.680 15.451 20.389  1.00 21.35  ? 119 PHE   A CE1 1 
ATOM   977  C CE2 . PHE   A 1 118 ? 25.225 14.986 22.657  1.00 21.00  ? 119 PHE   A CE2 1 
ATOM   978  C CZ  . PHE   A 1 118 ? 24.329 15.433 21.725  1.00 21.36  ? 119 PHE   A CZ  1 
ATOM   979  N N   . LEU   A 1 119 ? 30.559 12.394 19.579  1.00 15.95  ? 120 LEU   A N   1 
ATOM   980  C CA  A LEU   A 1 119 ? 31.888 12.439 18.980  0.49 16.74  ? 120 LEU   A CA  1 
ATOM   981  C CA  B LEU   A 1 119 ? 31.897 12.416 19.005  0.51 17.66  ? 120 LEU   A CA  1 
ATOM   982  C C   . LEU   A 1 119 ? 32.000 11.522 17.778  1.00 16.74  ? 120 LEU   A C   1 
ATOM   983  O O   . LEU   A 1 119 ? 32.652 11.882 16.798  1.00 18.49  ? 120 LEU   A O   1 
ATOM   984  C CB  A LEU   A 1 119 ? 32.964 12.110 20.003  0.49 16.73  ? 120 LEU   A CB  1 
ATOM   985  C CB  B LEU   A 1 119 ? 32.914 12.021 20.075  0.51 19.57  ? 120 LEU   A CB  1 
ATOM   986  C CG  A LEU   A 1 119 ? 33.311 13.295 20.874  0.49 16.33  ? 120 LEU   A CG  1 
ATOM   987  C CG  B LEU   A 1 119 ? 34.392 12.188 19.765  0.51 20.60  ? 120 LEU   A CG  1 
ATOM   988  C CD1 A LEU   A 1 119 ? 34.239 12.791 21.945  0.49 17.71  ? 120 LEU   A CD1 1 
ATOM   989  C CD1 B LEU   A 1 119 ? 34.734 13.628 19.426  0.51 19.89  ? 120 LEU   A CD1 1 
ATOM   990  C CD2 A LEU   A 1 119 ? 33.954 14.429 20.085  0.49 16.17  ? 120 LEU   A CD2 1 
ATOM   991  C CD2 B LEU   A 1 119 ? 35.176 11.714 20.964  0.51 20.05  ? 120 LEU   A CD2 1 
ATOM   992  N N   . LYS   A 1 120 ? 31.371 10.340 17.819  1.00 16.50  ? 121 LYS   A N   1 
ATOM   993  C CA  . LYS   A 1 120 ? 31.421 9.477  16.640  1.00 16.54  ? 121 LYS   A CA  1 
ATOM   994  C C   . LYS   A 1 120 ? 30.899 10.183 15.400  1.00 15.77  ? 121 LYS   A C   1 
ATOM   995  O O   . LYS   A 1 120 ? 31.476 10.041 14.313  1.00 16.27  ? 121 LYS   A O   1 
ATOM   996  C CB  . LYS   A 1 120 ? 30.643 8.186  16.863  1.00 21.45  ? 121 LYS   A CB  1 
ATOM   997  C CG  . LYS   A 1 120 ? 30.898 7.261  15.717  1.00 32.00  ? 121 LYS   A CG  1 
ATOM   998  C CD  . LYS   A 1 120 ? 32.221 6.577  15.790  1.00 40.37  ? 121 LYS   A CD  1 
ATOM   999  C CE  . LYS   A 1 120 ? 32.764 6.499  14.369  1.00 45.70  ? 121 LYS   A CE  1 
ATOM   1000 N NZ  . LYS   A 1 120 ? 32.528 5.219  13.662  1.00 48.62  ? 121 LYS   A NZ  1 
ATOM   1001 N N   . GLN   A 1 121 ? 29.823 10.956 15.542  1.00 15.54  ? 122 GLN   A N   1 
ATOM   1002 C CA  . GLN   A 1 121 ? 29.269 11.664 14.395  1.00 15.00  ? 122 GLN   A CA  1 
ATOM   1003 C C   . GLN   A 1 121 ? 30.191 12.788 13.946  1.00 14.77  ? 122 GLN   A C   1 
ATOM   1004 O O   . GLN   A 1 121 ? 30.353 13.010 12.740  1.00 14.68  ? 122 GLN   A O   1 
ATOM   1005 C CB  . GLN   A 1 121 ? 27.902 12.221 14.759  1.00 14.89  ? 122 GLN   A CB  1 
ATOM   1006 C CG  . GLN   A 1 121 ? 26.910 11.178 15.186  1.00 16.64  ? 122 GLN   A CG  1 
ATOM   1007 C CD  . GLN   A 1 121 ? 25.604 11.826 15.536  1.00 17.19  ? 122 GLN   A CD  1 
ATOM   1008 O OE1 . GLN   A 1 121 ? 24.904 12.322 14.668  1.00 17.45  ? 122 GLN   A OE1 1 
ATOM   1009 N NE2 . GLN   A 1 121 ? 25.330 11.944 16.833  1.00 18.56  ? 122 GLN   A NE2 1 
ATOM   1010 N N   . ILE   A 1 122 ? 30.750 13.554 14.896  1.00 13.56  ? 123 ILE   A N   1 
ATOM   1011 C CA  . ILE   A 1 122 ? 31.713 14.600 14.549  1.00 13.24  ? 123 ILE   A CA  1 
ATOM   1012 C C   . ILE   A 1 122 ? 32.905 13.994 13.822  1.00 12.19  ? 123 ILE   A C   1 
ATOM   1013 O O   . ILE   A 1 122 ? 33.353 14.506 12.779  1.00 13.13  ? 123 ILE   A O   1 
ATOM   1014 C CB  . ILE   A 1 122 ? 32.141 15.372 15.812  1.00 14.44  ? 123 ILE   A CB  1 
ATOM   1015 C CG1 . ILE   A 1 122 ? 30.933 16.065 16.465  1.00 15.54  ? 123 ILE   A CG1 1 
ATOM   1016 C CG2 . ILE   A 1 122 ? 33.245 16.359 15.481  1.00 16.33  ? 123 ILE   A CG2 1 
ATOM   1017 C CD1 . ILE   A 1 122 ? 31.223 16.597 17.893  1.00 17.84  ? 123 ILE   A CD1 1 
ATOM   1018 N N   . LEU   A 1 123 ? 33.441 12.893 14.356  1.00 12.29  ? 124 LEU   A N   1 
ATOM   1019 C CA  . LEU   A 1 123 ? 34.582 12.253 13.723  1.00 12.45  ? 124 LEU   A CA  1 
ATOM   1020 C C   . LEU   A 1 123 ? 34.225 11.751 12.330  1.00 11.83  ? 124 LEU   A C   1 
ATOM   1021 O O   . LEU   A 1 123 ? 35.055 11.825 11.415  1.00 12.71  ? 124 LEU   A O   1 
ATOM   1022 C CB  . LEU   A 1 123 ? 35.094 11.100 14.591  1.00 12.42  ? 124 LEU   A CB  1 
ATOM   1023 C CG  . LEU   A 1 123 ? 35.678 11.443 15.970  1.00 14.12  ? 124 LEU   A CG  1 
ATOM   1024 C CD1 . LEU   A 1 123 ? 36.059 10.169 16.689  1.00 16.02  ? 124 LEU   A CD1 1 
ATOM   1025 C CD2 . LEU   A 1 123 ? 36.896 12.360 15.844  1.00 15.84  ? 124 LEU   A CD2 1 
ATOM   1026 N N   . ASN   A 1 124 ? 33.008 11.223 12.144  1.00 12.36  ? 125 ASN   A N   1 
ATOM   1027 C CA  . ASN   A 1 124 ? 32.620 10.759 10.810  1.00 12.66  ? 125 ASN   A CA  1 
ATOM   1028 C C   . ASN   A 1 124 ? 32.567 11.927 9.831   1.00 12.89  ? 125 ASN   A C   1 
ATOM   1029 O O   . ASN   A 1 124 ? 33.008 11.802 8.682   1.00 13.27  ? 125 ASN   A O   1 
ATOM   1030 C CB  . ASN   A 1 124 ? 31.283 10.018 10.837  1.00 14.31  ? 125 ASN   A CB  1 
ATOM   1031 C CG  . ASN   A 1 124 ? 31.382 8.660  11.509  1.00 16.91  ? 125 ASN   A CG  1 
ATOM   1032 O OD1 . ASN   A 1 124 ? 32.475 8.110  11.659  1.00 19.02  ? 125 ASN   A OD1 1 
ATOM   1033 N ND2 . ASN   A 1 124 ? 30.243 8.112  11.911  1.00 19.55  ? 125 ASN   A ND2 1 
ATOM   1034 N N   . GLY   A 1 125 ? 32.026 13.074 10.257  1.00 12.79  ? 126 GLY   A N   1 
ATOM   1035 C CA  . GLY   A 1 125 ? 31.978 14.229 9.376   1.00 12.34  ? 126 GLY   A CA  1 
ATOM   1036 C C   . GLY   A 1 125 ? 33.372 14.750 9.076   1.00 11.51  ? 126 GLY   A C   1 
ATOM   1037 O O   . GLY   A 1 125 ? 33.693 15.083 7.924   1.00 12.40  ? 126 GLY   A O   1 
ATOM   1038 N N   . VAL   A 1 126 ? 34.234 14.811 10.094  1.00 11.92  ? 127 VAL   A N   1 
ATOM   1039 C CA  . VAL   A 1 126 ? 35.598 15.286 9.861   1.00 11.74  ? 127 VAL   A CA  1 
ATOM   1040 C C   . VAL   A 1 126 ? 36.381 14.291 9.021   1.00 11.72  ? 127 VAL   A C   1 
ATOM   1041 O O   . VAL   A 1 126 ? 37.220 14.688 8.195   1.00 11.59  ? 127 VAL   A O   1 
ATOM   1042 C CB  . VAL   A 1 126 ? 36.296 15.638 11.192  1.00 11.71  ? 127 VAL   A CB  1 
ATOM   1043 C CG1 . VAL   A 1 126 ? 37.759 15.987 10.959  1.00 13.75  ? 127 VAL   A CG1 1 
ATOM   1044 C CG2 . VAL   A 1 126 ? 35.570 16.783 11.832  1.00 12.30  ? 127 VAL   A CG2 1 
ATOM   1045 N N   . TYR   A 1 127 ? 36.117 12.996 9.182   1.00 11.77  ? 128 TYR   A N   1 
ATOM   1046 C CA  . TYR   A 1 127 ? 36.786 12.030 8.314   1.00 11.86  ? 128 TYR   A CA  1 
ATOM   1047 C C   . TYR   A 1 127 ? 36.438 12.268 6.850   1.00 11.66  ? 128 TYR   A C   1 
ATOM   1048 O O   . TYR   A 1 127 ? 37.320 12.250 5.990   1.00 11.95  ? 128 TYR   A O   1 
ATOM   1049 C CB  . TYR   A 1 127 ? 36.373 10.615 8.710   1.00 13.73  ? 128 TYR   A CB  1 
ATOM   1050 C CG  . TYR   A 1 127 ? 36.941 9.534  7.820   1.00 13.14  ? 128 TYR   A CG  1 
ATOM   1051 C CD1 . TYR   A 1 127 ? 38.282 9.227  7.845   1.00 16.94  ? 128 TYR   A CD1 1 
ATOM   1052 C CD2 . TYR   A 1 127 ? 36.129 8.826  6.946   1.00 15.62  ? 128 TYR   A CD2 1 
ATOM   1053 C CE1 . TYR   A 1 127 ? 38.807 8.234  7.050   1.00 17.55  ? 128 TYR   A CE1 1 
ATOM   1054 C CE2 . TYR   A 1 127 ? 36.645 7.827  6.150   1.00 17.04  ? 128 TYR   A CE2 1 
ATOM   1055 C CZ  . TYR   A 1 127 ? 37.981 7.537  6.210   1.00 16.76  ? 128 TYR   A CZ  1 
ATOM   1056 O OH  . TYR   A 1 127 ? 38.475 6.527  5.432   1.00 20.07  ? 128 TYR   A OH  1 
ATOM   1057 N N   . TYR   A 1 128 ? 35.177 12.545 6.564   1.00 11.60  ? 129 TYR   A N   1 
ATOM   1058 C CA  . TYR   A 1 128 ? 34.788 12.902 5.212   1.00 12.18  ? 129 TYR   A CA  1 
ATOM   1059 C C   . TYR   A 1 128 ? 35.534 14.156 4.726   1.00 12.50  ? 129 TYR   A C   1 
ATOM   1060 O O   . TYR   A 1 128 ? 36.117 14.168 3.627   1.00 13.47  ? 129 TYR   A O   1 
ATOM   1061 C CB  . TYR   A 1 128 ? 33.266 13.061 5.178   1.00 12.54  ? 129 TYR   A CB  1 
ATOM   1062 C CG  . TYR   A 1 128 ? 32.744 13.519 3.855   1.00 13.28  ? 129 TYR   A CG  1 
ATOM   1063 C CD1 . TYR   A 1 128 ? 32.431 12.611 2.844   1.00 14.81  ? 129 TYR   A CD1 1 
ATOM   1064 C CD2 . TYR   A 1 128 ? 32.579 14.852 3.616   1.00 15.94  ? 129 TYR   A CD2 1 
ATOM   1065 C CE1 . TYR   A 1 128 ? 31.957 13.054 1.586   1.00 14.31  ? 129 TYR   A CE1 1 
ATOM   1066 C CE2 . TYR   A 1 128 ? 32.120 15.296 2.393   1.00 17.38  ? 129 TYR   A CE2 1 
ATOM   1067 C CZ  . TYR   A 1 128 ? 31.820 14.411 1.379   1.00 16.17  ? 129 TYR   A CZ  1 
ATOM   1068 O OH  . TYR   A 1 128 ? 31.345 14.918 0.179   1.00 18.79  ? 129 TYR   A OH  1 
ATOM   1069 N N   . LEU   A 1 129 ? 35.530 15.227 5.528   1.00 11.72  ? 130 LEU   A N   1 
ATOM   1070 C CA  . LEU   A 1 129 ? 36.187 16.472 5.122   1.00 12.04  ? 130 LEU   A CA  1 
ATOM   1071 C C   . LEU   A 1 129 ? 37.670 16.249 4.899   1.00 12.26  ? 130 LEU   A C   1 
ATOM   1072 O O   . LEU   A 1 129 ? 38.226 16.649 3.871   1.00 12.90  ? 130 LEU   A O   1 
ATOM   1073 C CB  . LEU   A 1 129 ? 35.990 17.552 6.193   1.00 13.40  ? 130 LEU   A CB  1 
ATOM   1074 C CG  . LEU   A 1 129 ? 34.544 17.994 6.405   1.00 13.53  ? 130 LEU   A CG  1 
ATOM   1075 C CD1 . LEU   A 1 129 ? 34.485 18.950 7.572   1.00 16.73  ? 130 LEU   A CD1 1 
ATOM   1076 C CD2 . LEU   A 1 129 ? 33.965 18.640 5.141   1.00 15.98  ? 130 LEU   A CD2 1 
ATOM   1077 N N   . HIS   A 1 130 ? 38.332 15.595 5.850   1.00 12.07  ? 131 HIS   A N   1 
ATOM   1078 C CA  . HIS   A 1 130 ? 39.770 15.386 5.705   1.00 12.94  ? 131 HIS   A CA  1 
ATOM   1079 C C   . HIS   A 1 130 ? 40.097 14.482 4.530   1.00 12.64  ? 131 HIS   A C   1 
ATOM   1080 O O   . HIS   A 1 130 ? 41.148 14.653 3.902   1.00 13.61  ? 131 HIS   A O   1 
ATOM   1081 C CB  . HIS   A 1 130 ? 40.358 14.847 7.005   1.00 11.77  ? 131 HIS   A CB  1 
ATOM   1082 C CG  . HIS   A 1 130 ? 40.442 15.884 8.068   1.00 11.66  ? 131 HIS   A CG  1 
ATOM   1083 N ND1 . HIS   A 1 130 ? 41.123 15.698 9.250   1.00 12.40  ? 131 HIS   A ND1 1 
ATOM   1084 C CD2 . HIS   A 1 130 ? 39.938 17.142 8.107   1.00 11.83  ? 131 HIS   A CD2 1 
ATOM   1085 C CE1 . HIS   A 1 130 ? 41.021 16.796 9.978   1.00 12.22  ? 131 HIS   A CE1 1 
ATOM   1086 N NE2 . HIS   A 1 130 ? 40.316 17.692 9.307   1.00 11.80  ? 131 HIS   A NE2 1 
ATOM   1087 N N   . SER   A 1 131 ? 39.207 13.539 4.204   1.00 12.59  ? 132 SER   A N   1 
ATOM   1088 C CA  . SER   A 1 131 ? 39.397 12.698 3.022   1.00 14.62  ? 132 SER   A CA  1 
ATOM   1089 C C   . SER   A 1 131 ? 39.403 13.517 1.743   1.00 15.08  ? 132 SER   A C   1 
ATOM   1090 O O   . SER   A 1 131 ? 40.040 13.116 0.764   1.00 17.55  ? 132 SER   A O   1 
ATOM   1091 C CB  . SER   A 1 131 ? 38.314 11.630 2.964   1.00 15.84  ? 132 SER   A CB  1 
ATOM   1092 O OG  . SER   A 1 131 ? 38.453 10.706 4.036   1.00 17.61  ? 132 SER   A OG  1 
ATOM   1093 N N   . LEU   A 1 132 ? 38.705 14.654 1.733   1.00 15.31  ? 133 LEU   A N   1 
ATOM   1094 C CA  . LEU   A 1 132 ? 38.689 15.594 0.624   1.00 16.40  ? 133 LEU   A CA  1 
ATOM   1095 C C   . LEU   A 1 132 ? 39.751 16.675 0.781   1.00 15.87  ? 133 LEU   A C   1 
ATOM   1096 O O   . LEU   A 1 132 ? 39.766 17.639 0.004   1.00 18.50  ? 133 LEU   A O   1 
ATOM   1097 C CB  . LEU   A 1 132 ? 37.302 16.228 0.545   1.00 17.43  ? 133 LEU   A CB  1 
ATOM   1098 C CG  . LEU   A 1 132 ? 36.193 15.270 0.093   1.00 19.56  ? 133 LEU   A CG  1 
ATOM   1099 C CD1 . LEU   A 1 132 ? 34.880 16.019 0.050   1.00 21.62  ? 133 LEU   A CD1 1 
ATOM   1100 C CD2 . LEU   A 1 132 ? 36.482 14.671 -1.281  1.00 20.85  ? 133 LEU   A CD2 1 
ATOM   1101 N N   . GLN   A 1 133 ? 40.630 16.553 1.786   1.00 15.83  ? 134 GLN   A N   1 
ATOM   1102 C CA  . GLN   A 1 133 ? 41.669 17.544 2.063   1.00 15.34  ? 134 GLN   A CA  1 
ATOM   1103 C C   . GLN   A 1 133 ? 41.084 18.900 2.445   1.00 15.61  ? 134 GLN   A C   1 
ATOM   1104 O O   . GLN   A 1 133 ? 41.675 19.944 2.169   1.00 18.08  ? 134 GLN   A O   1 
ATOM   1105 C CB  . GLN   A 1 133 ? 42.710 17.670 0.944   1.00 19.69  ? 134 GLN   A CB  1 
ATOM   1106 C CG  . GLN   A 1 133 ? 43.496 16.393 0.722   1.00 23.31  ? 134 GLN   A CG  1 
ATOM   1107 C CD  . GLN   A 1 133 ? 44.433 16.068 1.888   1.00 30.85  ? 134 GLN   A CD  1 
ATOM   1108 O OE1 . GLN   A 1 133 ? 44.382 14.971 2.442   1.00 33.73  ? 134 GLN   A OE1 1 
ATOM   1109 N NE2 . GLN   A 1 133 ? 45.219 17.050 2.323   1.00 33.29  ? 134 GLN   A NE2 1 
ATOM   1110 N N   . ILE   A 1 134 ? 39.919 18.901 3.093   1.00 13.66  ? 135 ILE   A N   1 
ATOM   1111 C CA  . ILE   A 1 134 ? 39.295 20.124 3.574   1.00 13.43  ? 135 ILE   A CA  1 
ATOM   1112 C C   . ILE   A 1 134 ? 39.547 20.219 5.074   1.00 12.87  ? 135 ILE   A C   1 
ATOM   1113 O O   . ILE   A 1 134 ? 39.126 19.341 5.844   1.00 13.86  ? 135 ILE   A O   1 
ATOM   1114 C CB  . ILE   A 1 134 ? 37.787 20.142 3.269   1.00 15.04  ? 135 ILE   A CB  1 
ATOM   1115 C CG1 . ILE   A 1 134 ? 37.531 20.163 1.753   1.00 17.12  ? 135 ILE   A CG1 1 
ATOM   1116 C CG2 . ILE   A 1 134 ? 37.163 21.350 3.939   1.00 15.75  ? 135 ILE   A CG2 1 
ATOM   1117 C CD1 . ILE   A 1 134 ? 36.106 19.854 1.394   1.00 18.96  ? 135 ILE   A CD1 1 
ATOM   1118 N N   . ALA   A 1 135 ? 40.232 21.281 5.479   1.00 12.66  ? 136 ALA   A N   1 
ATOM   1119 C CA  . ALA   A 1 135 ? 40.355 21.629 6.888   1.00 12.86  ? 136 ALA   A CA  1 
ATOM   1120 C C   . ALA   A 1 135 ? 39.221 22.577 7.235   1.00 12.65  ? 136 ALA   A C   1 
ATOM   1121 O O   . ALA   A 1 135 ? 38.972 23.541 6.503   1.00 14.32  ? 136 ALA   A O   1 
ATOM   1122 C CB  . ALA   A 1 135 ? 41.691 22.322 7.148   1.00 14.58  ? 136 ALA   A CB  1 
ATOM   1123 N N   . HIS   A 1 136 ? 38.542 22.309 8.345   1.00 12.57  ? 137 HIS   A N   1 
ATOM   1124 C CA  . HIS   A 1 136 ? 37.423 23.158 8.744   1.00 13.11  ? 137 HIS   A CA  1 
ATOM   1125 C C   . HIS   A 1 136 ? 37.920 24.450 9.389   1.00 13.31  ? 137 HIS   A C   1 
ATOM   1126 O O   . HIS   A 1 136 ? 37.432 25.547 9.077   1.00 14.22  ? 137 HIS   A O   1 
ATOM   1127 C CB  . HIS   A 1 136 ? 36.512 22.388 9.703   1.00 13.72  ? 137 HIS   A CB  1 
ATOM   1128 C CG  . HIS   A 1 136 ? 35.287 23.144 10.094  1.00 12.97  ? 137 HIS   A CG  1 
ATOM   1129 N ND1 . HIS   A 1 136 ? 35.294 24.108 11.082  1.00 13.79  ? 137 HIS   A ND1 1 
ATOM   1130 C CD2 . HIS   A 1 136 ? 34.027 23.123 9.588   1.00 15.13  ? 137 HIS   A CD2 1 
ATOM   1131 C CE1 . HIS   A 1 136 ? 34.077 24.612 11.194  1.00 15.02  ? 137 HIS   A CE1 1 
ATOM   1132 N NE2 . HIS   A 1 136 ? 33.291 24.039 10.295  1.00 16.71  ? 137 HIS   A NE2 1 
ATOM   1133 N N   . PHE   A 1 137 ? 38.895 24.329 10.295  1.00 12.67  ? 138 PHE   A N   1 
ATOM   1134 C CA  . PHE   A 1 137 ? 39.571 25.419 10.986  1.00 13.81  ? 138 PHE   A CA  1 
ATOM   1135 C C   . PHE   A 1 137 ? 38.709 26.174 11.995  1.00 14.04  ? 138 PHE   A C   1 
ATOM   1136 O O   . PHE   A 1 137 ? 39.202 27.124 12.587  1.00 18.54  ? 138 PHE   A O   1 
ATOM   1137 C CB  . PHE   A 1 137 ? 40.254 26.409 10.030  1.00 14.33  ? 138 PHE   A CB  1 
ATOM   1138 C CG  . PHE   A 1 137 ? 41.475 25.866 9.324   1.00 13.98  ? 138 PHE   A CG  1 
ATOM   1139 C CD1 . PHE   A 1 137 ? 42.411 25.080 9.991   1.00 15.59  ? 138 PHE   A CD1 1 
ATOM   1140 C CD2 . PHE   A 1 137 ? 41.714 26.210 8.003   1.00 14.43  ? 138 PHE   A CD2 1 
ATOM   1141 C CE1 . PHE   A 1 137 ? 43.548 24.630 9.337   1.00 16.18  ? 138 PHE   A CE1 1 
ATOM   1142 C CE2 . PHE   A 1 137 ? 42.834 25.765 7.346   1.00 15.20  ? 138 PHE   A CE2 1 
ATOM   1143 C CZ  . PHE   A 1 137 ? 43.774 24.987 8.005   1.00 14.75  ? 138 PHE   A CZ  1 
ATOM   1144 N N   . ASP   A 1 138 ? 37.469 25.764 12.251  1.00 13.33  ? 139 ASP   A N   1 
ATOM   1145 C CA  . ASP   A 1 138 ? 36.644 26.473 13.223  1.00 16.16  ? 139 ASP   A CA  1 
ATOM   1146 C C   . ASP   A 1 138 ? 35.733 25.493 13.971  1.00 13.93  ? 139 ASP   A C   1 
ATOM   1147 O O   . ASP   A 1 138 ? 34.575 25.808 14.267  1.00 16.03  ? 139 ASP   A O   1 
ATOM   1148 C CB  . ASP   A 1 138 ? 35.846 27.563 12.489  1.00 21.59  ? 139 ASP   A CB  1 
ATOM   1149 C CG  . ASP   A 1 138 ? 35.264 28.629 13.390  1.00 26.65  ? 139 ASP   A CG  1 
ATOM   1150 O OD1 . ASP   A 1 138 ? 35.827 28.922 14.472  1.00 26.30  ? 139 ASP   A OD1 1 
ATOM   1151 O OD2 . ASP   A 1 138 ? 34.276 29.270 12.924  1.00 29.08  ? 139 ASP   A OD2 1 
ATOM   1152 N N   . LEU   A 1 139 ? 36.232 24.298 14.285  1.00 13.10  ? 140 LEU   A N   1 
ATOM   1153 C CA  . LEU   A 1 139 ? 35.403 23.328 15.001  1.00 12.96  ? 140 LEU   A CA  1 
ATOM   1154 C C   . LEU   A 1 139 ? 35.246 23.748 16.460  1.00 13.34  ? 140 LEU   A C   1 
ATOM   1155 O O   . LEU   A 1 139 ? 36.237 24.005 17.158  1.00 15.19  ? 140 LEU   A O   1 
ATOM   1156 C CB  . LEU   A 1 139 ? 36.013 21.933 14.933  1.00 13.41  ? 140 LEU   A CB  1 
ATOM   1157 C CG  . LEU   A 1 139 ? 36.059 21.327 13.531  1.00 12.55  ? 140 LEU   A CG  1 
ATOM   1158 C CD1 . LEU   A 1 139 ? 36.888 20.064 13.541  1.00 15.08  ? 140 LEU   A CD1 1 
ATOM   1159 C CD2 . LEU   A 1 139 ? 34.676 21.037 12.955  1.00 14.75  ? 140 LEU   A CD2 1 
ATOM   1160 N N   . LYS   A 1 140 ? 33.997 23.840 16.902  1.00 14.38  ? 141 LYS   A N   1 
ATOM   1161 C CA  . LYS   A 1 140 ? 33.632 24.198 18.269  1.00 15.46  ? 141 LYS   A CA  1 
ATOM   1162 C C   . LYS   A 1 140 ? 32.144 23.874 18.444  1.00 15.64  ? 141 LYS   A C   1 
ATOM   1163 O O   . LYS   A 1 140 ? 31.435 23.734 17.448  1.00 15.33  ? 141 LYS   A O   1 
ATOM   1164 C CB  . LYS   A 1 140 ? 33.880 25.688 18.539  1.00 16.17  ? 141 LYS   A CB  1 
ATOM   1165 C CG  . LYS   A 1 140 ? 33.144 26.623 17.579  1.00 17.52  ? 141 LYS   A CG  1 
ATOM   1166 C CD  . LYS   A 1 140 ? 33.478 28.074 17.907  1.00 21.01  ? 141 LYS   A CD  1 
ATOM   1167 C CE  . LYS   A 1 140 ? 32.745 29.037 16.985  1.00 22.17  ? 141 LYS   A CE  1 
ATOM   1168 N NZ  . LYS   A 1 140 ? 32.982 30.462 17.393  1.00 25.38  ? 141 LYS   A NZ  1 
ATOM   1169 N N   . PRO   A 1 141 ? 31.650 23.764 19.695  1.00 16.28  ? 142 PRO   A N   1 
ATOM   1170 C CA  . PRO   A 1 141 ? 30.241 23.363 19.910  1.00 17.97  ? 142 PRO   A CA  1 
ATOM   1171 C C   . PRO   A 1 141 ? 29.213 24.256 19.231  1.00 16.98  ? 142 PRO   A C   1 
ATOM   1172 O O   . PRO   A 1 141 ? 28.145 23.765 18.834  1.00 19.04  ? 142 PRO   A O   1 
ATOM   1173 C CB  . PRO   A 1 141 ? 30.099 23.349 21.446  1.00 19.04  ? 142 PRO   A CB  1 
ATOM   1174 C CG  . PRO   A 1 141 ? 31.452 23.013 21.911  1.00 20.37  ? 142 PRO   A CG  1 
ATOM   1175 C CD  . PRO   A 1 141 ? 32.391 23.774 20.974  1.00 18.45  ? 142 PRO   A CD  1 
ATOM   1176 N N   . GLU   A 1 142 ? 29.494 25.557 19.086  1.00 16.06  ? 143 GLU   A N   1 
ATOM   1177 C CA  . GLU   A 1 142 ? 28.534 26.444 18.428  1.00 17.91  ? 143 GLU   A CA  1 
ATOM   1178 C C   . GLU   A 1 142 ? 28.382 26.132 16.946  1.00 17.10  ? 143 GLU   A C   1 
ATOM   1179 O O   . GLU   A 1 142 ? 27.363 26.504 16.344  1.00 18.86  ? 143 GLU   A O   1 
ATOM   1180 C CB  . GLU   A 1 142 ? 29.005 27.887 18.593  1.00 22.60  ? 143 GLU   A CB  1 
ATOM   1181 C CG  . GLU   A 1 142 ? 28.917 28.352 20.019  1.00 26.90  ? 143 GLU   A CG  1 
ATOM   1182 C CD  . GLU   A 1 142 ? 30.246 28.182 20.791  1.00 30.72  ? 143 GLU   A CD  1 
ATOM   1183 O OE1 . GLU   A 1 142 ? 31.055 27.232 20.514  1.00 29.65  ? 143 GLU   A OE1 1 
ATOM   1184 O OE2 . GLU   A 1 142 ? 30.456 28.991 21.720  1.00 36.94  ? 143 GLU   A OE2 1 
ATOM   1185 N N   . ASN   A 1 143 ? 29.375 25.486 16.339  1.00 15.78  ? 144 ASN   A N   1 
ATOM   1186 C CA  . ASN   A 1 143 ? 29.340 25.135 14.922  1.00 15.68  ? 144 ASN   A CA  1 
ATOM   1187 C C   . ASN   A 1 143 ? 28.859 23.714 14.683  1.00 17.76  ? 144 ASN   A C   1 
ATOM   1188 O O   . ASN   A 1 143 ? 29.020 23.186 13.587  1.00 18.70  ? 144 ASN   A O   1 
ATOM   1189 C CB  . ASN   A 1 143 ? 30.697 25.382 14.267  1.00 15.90  ? 144 ASN   A CB  1 
ATOM   1190 C CG  . ASN   A 1 143 ? 30.926 26.841 14.009  1.00 16.65  ? 144 ASN   A CG  1 
ATOM   1191 O OD1 . ASN   A 1 143 ? 29.960 27.620 13.941  1.00 19.99  ? 144 ASN   A OD1 1 
ATOM   1192 N ND2 . ASN   A 1 143 ? 32.177 27.233 13.855  1.00 17.00  ? 144 ASN   A ND2 1 
ATOM   1193 N N   . ILE   A 1 144 ? 28.276 23.083 15.692  1.00 16.89  ? 145 ILE   A N   1 
ATOM   1194 C CA  A ILE   A 1 144 ? 27.684 21.765 15.553  0.50 18.54  ? 145 ILE   A CA  1 
ATOM   1195 C CA  B ILE   A 1 144 ? 27.700 21.740 15.599  0.50 18.19  ? 145 ILE   A CA  1 
ATOM   1196 C C   . ILE   A 1 144 ? 26.238 21.880 15.976  1.00 19.58  ? 145 ILE   A C   1 
ATOM   1197 O O   . ILE   A 1 144 ? 25.936 22.328 17.093  1.00 22.05  ? 145 ILE   A O   1 
ATOM   1198 C CB  A ILE   A 1 144 ? 28.422 20.734 16.403  0.50 18.11  ? 145 ILE   A CB  1 
ATOM   1199 C CB  B ILE   A 1 144 ? 28.370 20.770 16.585  0.50 19.18  ? 145 ILE   A CB  1 
ATOM   1200 C CG1 A ILE   A 1 144 ? 29.859 20.637 15.913  0.50 22.95  ? 145 ILE   A CG1 1 
ATOM   1201 C CG1 B ILE   A 1 144 ? 29.890 20.758 16.449  0.50 22.64  ? 145 ILE   A CG1 1 
ATOM   1202 C CG2 A ILE   A 1 144 ? 27.705 19.391 16.350  0.50 21.02  ? 145 ILE   A CG2 1 
ATOM   1203 C CG2 B ILE   A 1 144 ? 27.812 19.364 16.415  0.50 24.42  ? 145 ILE   A CG2 1 
ATOM   1204 C CD1 A ILE   A 1 144 ? 30.750 20.068 16.921  0.50 15.61  ? 145 ILE   A CD1 1 
ATOM   1205 C CD1 B ILE   A 1 144 ? 30.340 20.222 15.136  0.50 19.32  ? 145 ILE   A CD1 1 
ATOM   1206 N N   . MET   A 1 145 ? 25.341 21.500 15.087  1.00 17.02  ? 146 MET   A N   1 
ATOM   1207 C CA  A MET   A 1 145 ? 23.906 21.638 15.303  0.53 16.97  ? 146 MET   A CA  1 
ATOM   1208 C CA  B MET   A 1 145 ? 23.921 21.631 15.362  0.47 17.19  ? 146 MET   A CA  1 
ATOM   1209 C C   . MET   A 1 145 ? 23.230 20.274 15.372  1.00 16.70  ? 146 MET   A C   1 
ATOM   1210 O O   . MET   A 1 145 ? 23.648 19.329 14.699  1.00 17.11  ? 146 MET   A O   1 
ATOM   1211 C CB  A MET   A 1 145 ? 23.232 22.459 14.190  0.53 21.47  ? 146 MET   A CB  1 
ATOM   1212 C CB  B MET   A 1 145 ? 23.252 22.573 14.371  0.47 21.64  ? 146 MET   A CB  1 
ATOM   1213 C CG  A MET   A 1 145 ? 23.908 23.770 13.923  0.53 24.73  ? 146 MET   A CG  1 
ATOM   1214 C CG  B MET   A 1 145 ? 23.852 23.951 14.412  0.47 23.99  ? 146 MET   A CG  1 
ATOM   1215 S SD  A MET   A 1 145 ? 23.170 25.015 14.983  0.53 25.53  ? 146 MET   A SD  1 
ATOM   1216 S SD  B MET   A 1 145 ? 22.762 25.215 13.771  0.47 25.19  ? 146 MET   A SD  1 
ATOM   1217 C CE  A MET   A 1 145 ? 21.427 24.790 14.657  0.53 26.86  ? 146 MET   A CE  1 
ATOM   1218 C CE  B MET   A 1 145 ? 21.341 25.011 14.828  0.47 25.36  ? 146 MET   A CE  1 
ATOM   1219 N N   . LEU   A 1 146 ? 22.165 20.197 16.162  1.00 16.94  ? 147 LEU   A N   1 
ATOM   1220 C CA  . LEU   A 1 146 ? 21.398 18.978 16.361  1.00 18.82  ? 147 LEU   A CA  1 
ATOM   1221 C C   . LEU   A 1 146 ? 20.189 18.992 15.441  1.00 19.30  ? 147 LEU   A C   1 
ATOM   1222 O O   . LEU   A 1 146 ? 19.540 20.025 15.276  1.00 20.66  ? 147 LEU   A O   1 
ATOM   1223 C CB  . LEU   A 1 146 ? 20.921 18.873 17.816  1.00 19.50  ? 147 LEU   A CB  1 
ATOM   1224 C CG  . LEU   A 1 146 ? 21.968 18.414 18.845  1.00 21.93  ? 147 LEU   A CG  1 
ATOM   1225 C CD1 . LEU   A 1 146 ? 23.150 19.350 18.964  1.00 23.62  ? 147 LEU   A CD1 1 
ATOM   1226 C CD2 . LEU   A 1 146 ? 21.304 18.274 20.208  1.00 23.11  ? 147 LEU   A CD2 1 
ATOM   1227 N N   . LEU   A 1 147 ? 19.887 17.841 14.851  1.00 20.44  ? 148 LEU   A N   1 
ATOM   1228 C CA  . LEU   A 1 147 ? 18.692 17.751 14.015  1.00 22.71  ? 148 LEU   A CA  1 
ATOM   1229 C C   . LEU   A 1 147 ? 17.431 17.824 14.862  1.00 24.38  ? 148 LEU   A C   1 
ATOM   1230 O O   . LEU   A 1 147 ? 16.450 18.469 14.474  1.00 26.87  ? 148 LEU   A O   1 
ATOM   1231 C CB  . LEU   A 1 147 ? 18.709 16.460 13.199  1.00 24.76  ? 148 LEU   A CB  1 
ATOM   1232 C CG  . LEU   A 1 147 ? 19.534 16.483 11.909  1.00 25.05  ? 148 LEU   A CG  1 
ATOM   1233 C CD1 . LEU   A 1 147 ? 21.030 16.631 12.196  1.00 25.80  ? 148 LEU   A CD1 1 
ATOM   1234 C CD2 . LEU   A 1 147 ? 19.271 15.226 11.097  1.00 27.72  ? 148 LEU   A CD2 1 
ATOM   1235 N N   . ASP   A 1 148 ? 17.449 17.183 16.029  1.00 25.60  ? 149 ASP   A N   1 
ATOM   1236 C CA  . ASP   A 1 148 ? 16.302 17.145 16.929  1.00 27.82  ? 149 ASP   A CA  1 
ATOM   1237 C C   . ASP   A 1 148 ? 16.878 16.938 18.320  1.00 28.68  ? 149 ASP   A C   1 
ATOM   1238 O O   . ASP   A 1 148 ? 17.551 15.932 18.561  1.00 29.32  ? 149 ASP   A O   1 
ATOM   1239 C CB  . ASP   A 1 148 ? 15.389 15.974 16.538  1.00 31.23  ? 149 ASP   A CB  1 
ATOM   1240 C CG  . ASP   A 1 148 ? 14.137 15.864 17.397  1.00 34.09  ? 149 ASP   A CG  1 
ATOM   1241 O OD1 . ASP   A 1 148 ? 14.048 16.485 18.479  1.00 35.96  ? 149 ASP   A OD1 1 
ATOM   1242 O OD2 . ASP   A 1 148 ? 13.221 15.140 16.958  1.00 36.00  ? 149 ASP   A OD2 1 
ATOM   1243 N N   . ARG   A 1 149 ? 16.630 17.876 19.233  1.00 31.53  ? 150 ARG   A N   1 
ATOM   1244 C CA  . ARG   A 1 149 ? 17.287 17.797 20.529  1.00 35.37  ? 150 ARG   A CA  1 
ATOM   1245 C C   . ARG   A 1 149 ? 16.493 16.988 21.539  1.00 37.76  ? 150 ARG   A C   1 
ATOM   1246 O O   . ARG   A 1 149 ? 16.933 16.861 22.685  1.00 38.65  ? 150 ARG   A O   1 
ATOM   1247 C CB  . ARG   A 1 149 ? 17.601 19.189 21.099  1.00 36.53  ? 150 ARG   A CB  1 
ATOM   1248 C CG  . ARG   A 1 149 ? 16.381 19.979 21.567  1.00 39.79  ? 150 ARG   A CG  1 
ATOM   1249 C CD  . ARG   A 1 149 ? 16.736 21.438 21.815  1.00 44.19  ? 150 ARG   A CD  1 
ATOM   1250 N NE  . ARG   A 1 149 ? 15.576 22.311 21.680  1.00 48.62  ? 150 ARG   A NE  1 
ATOM   1251 C CZ  . ARG   A 1 149 ? 15.216 23.228 22.568  1.00 52.56  ? 150 ARG   A CZ  1 
ATOM   1252 N NH1 . ARG   A 1 149 ? 15.898 23.411 23.687  1.00 53.81  ? 150 ARG   A NH1 1 
ATOM   1253 N NH2 . ARG   A 1 149 ? 14.141 23.975 22.331  1.00 53.94  ? 150 ARG   A NH2 1 
ATOM   1254 N N   . ASN   A 1 150 ? 15.355 16.423 21.135  1.00 37.76  ? 151 ASN   A N   1 
ATOM   1255 C CA  . ASN   A 1 150 ? 14.437 15.754 22.044  1.00 38.98  ? 151 ASN   A CA  1 
ATOM   1256 C C   . ASN   A 1 150 ? 14.508 14.231 21.971  1.00 40.37  ? 151 ASN   A C   1 
ATOM   1257 O O   . ASN   A 1 150 ? 13.702 13.558 22.616  1.00 43.20  ? 151 ASN   A O   1 
ATOM   1258 C CB  . ASN   A 1 150 ? 13.000 16.235 21.803  1.00 40.93  ? 151 ASN   A CB  1 
ATOM   1259 C CG  . ASN   A 1 150 ? 12.824 17.712 22.098  1.00 44.41  ? 151 ASN   A CG  1 
ATOM   1260 O OD1 . ASN   A 1 150 ? 13.122 18.177 23.199  1.00 45.77  ? 151 ASN   A OD1 1 
ATOM   1261 N ND2 . ASN   A 1 150 ? 12.360 18.463 21.104  1.00 45.79  ? 151 ASN   A ND2 1 
ATOM   1262 N N   . VAL   A 1 151 ? 15.448 13.675 21.217  1.00 38.16  ? 152 VAL   A N   1 
ATOM   1263 C CA  . VAL   A 1 151 ? 15.634 12.227 21.122  1.00 35.69  ? 152 VAL   A CA  1 
ATOM   1264 C C   . VAL   A 1 151 ? 16.777 11.814 22.045  1.00 37.00  ? 152 VAL   A C   1 
ATOM   1265 O O   . VAL   A 1 151 ? 17.625 12.652 22.390  1.00 37.62  ? 152 VAL   A O   1 
ATOM   1266 C CB  . VAL   A 1 151 ? 15.865 11.785 19.665  1.00 33.15  ? 152 VAL   A CB  1 
ATOM   1267 C CG1 . VAL   A 1 151 ? 14.654 12.154 18.797  1.00 33.79  ? 152 VAL   A CG1 1 
ATOM   1268 C CG2 . VAL   A 1 151 ? 17.148 12.390 19.116  1.00 33.66  ? 152 VAL   A CG2 1 
ATOM   1269 N N   . PRO   A 1 152 ? 16.834 10.551 22.486  1.00 37.68  ? 153 PRO   A N   1 
ATOM   1270 C CA  . PRO   A 1 152 ? 17.919 10.154 23.406  1.00 37.57  ? 153 PRO   A CA  1 
ATOM   1271 C C   . PRO   A 1 152 ? 19.326 10.286 22.843  1.00 36.90  ? 153 PRO   A C   1 
ATOM   1272 O O   . PRO   A 1 152 ? 20.256 10.549 23.614  1.00 38.40  ? 153 PRO   A O   1 
ATOM   1273 C CB  . PRO   A 1 152 ? 17.577 8.709  23.801  1.00 39.14  ? 153 PRO   A CB  1 
ATOM   1274 C CG  . PRO   A 1 152 ? 16.243 8.397  23.194  1.00 39.96  ? 153 PRO   A CG  1 
ATOM   1275 C CD  . PRO   A 1 152 ? 15.864 9.469  22.226  1.00 38.37  ? 153 PRO   A CD  1 
ATOM   1276 N N   . LYS   A 1 153 ? 19.522 10.124 21.534  1.00 34.12  ? 154 LYS   A N   1 
ATOM   1277 C CA  . LYS   A 1 153 ? 20.853 10.159 20.921  1.00 32.40  ? 154 LYS   A CA  1 
ATOM   1278 C C   . LYS   A 1 153 ? 20.823 11.145 19.757  1.00 28.12  ? 154 LYS   A C   1 
ATOM   1279 O O   . LYS   A 1 153 ? 20.749 10.745 18.584  1.00 27.88  ? 154 LYS   A O   1 
ATOM   1280 C CB  . LYS   A 1 153 ? 21.277 8.767  20.449  1.00 35.98  ? 154 LYS   A CB  1 
ATOM   1281 C CG  . LYS   A 1 153 ? 21.622 7.784  21.567  1.00 40.48  ? 154 LYS   A CG  1 
ATOM   1282 C CD  . LYS   A 1 153 ? 21.705 6.360  21.032  1.00 45.32  ? 154 LYS   A CD  1 
ATOM   1283 C CE  . LYS   A 1 153 ? 20.348 5.661  21.076  1.00 49.30  ? 154 LYS   A CE  1 
ATOM   1284 N NZ  . LYS   A 1 153 ? 19.488 5.994  19.897  1.00 51.49  ? 154 LYS   A NZ  1 
ATOM   1285 N N   . PRO   A 1 154 ? 20.880 12.444 20.039  1.00 24.45  ? 155 PRO   A N   1 
ATOM   1286 C CA  . PRO   A 1 154 ? 20.669 13.431 18.968  1.00 23.62  ? 155 PRO   A CA  1 
ATOM   1287 C C   . PRO   A 1 154 ? 21.688 13.311 17.840  1.00 22.23  ? 155 PRO   A C   1 
ATOM   1288 O O   . PRO   A 1 154 ? 22.879 13.082 18.067  1.00 21.92  ? 155 PRO   A O   1 
ATOM   1289 C CB  . PRO   A 1 154 ? 20.790 14.770 19.705  1.00 23.98  ? 155 PRO   A CB  1 
ATOM   1290 C CG  . PRO   A 1 154 ? 20.365 14.444 21.119  1.00 25.64  ? 155 PRO   A CG  1 
ATOM   1291 C CD  . PRO   A 1 154 ? 20.982 13.092 21.362  1.00 26.10  ? 155 PRO   A CD  1 
ATOM   1292 N N   . ARG   A 1 155 ? 21.203 13.468 16.607  1.00 20.90  ? 156 ARG   A N   1 
ATOM   1293 C CA  . ARG   A 1 155 ? 22.062 13.437 15.428  1.00 20.01  ? 156 ARG   A CA  1 
ATOM   1294 C C   . ARG   A 1 155 ? 22.554 14.851 15.145  1.00 17.88  ? 156 ARG   A C   1 
ATOM   1295 O O   . ARG   A 1 155 ? 21.872 15.830 15.472  1.00 19.17  ? 156 ARG   A O   1 
ATOM   1296 C CB  . ARG   A 1 155 ? 21.258 12.945 14.228  1.00 21.80  ? 156 ARG   A CB  1 
ATOM   1297 C CG  . ARG   A 1 155 ? 20.696 11.534 14.436  1.00 25.27  ? 156 ARG   A CG  1 
ATOM   1298 C CD  . ARG   A 1 155 ? 21.779 10.472 14.596  1.00 29.13  ? 156 ARG   A CD  1 
ATOM   1299 N NE  . ARG   A 1 155 ? 22.177 10.249 15.984  1.00 31.89  ? 156 ARG   A NE  1 
ATOM   1300 C CZ  . ARG   A 1 155 ? 23.231 9.525  16.342  1.00 34.43  ? 156 ARG   A CZ  1 
ATOM   1301 N NH1 . ARG   A 1 155 ? 23.962 8.880  15.445  1.00 34.43  ? 156 ARG   A NH1 1 
ATOM   1302 N NH2 . ARG   A 1 155 ? 23.562 9.447  17.631  1.00 35.49  ? 156 ARG   A NH2 1 
ATOM   1303 N N   . ILE   A 1 156 ? 23.765 14.963 14.572  1.00 15.65  ? 157 ILE   A N   1 
ATOM   1304 C CA  . ILE   A 1 156 ? 24.372 16.283 14.407  1.00 15.53  ? 157 ILE   A CA  1 
ATOM   1305 C C   . ILE   A 1 156 ? 24.870 16.551 12.992  1.00 14.96  ? 157 ILE   A C   1 
ATOM   1306 O O   . ILE   A 1 156 ? 25.144 15.638 12.210  1.00 15.93  ? 157 ILE   A O   1 
ATOM   1307 C CB  . ILE   A 1 156 ? 25.495 16.575 15.418  1.00 17.06  ? 157 ILE   A CB  1 
ATOM   1308 C CG1 . ILE   A 1 156 ? 26.669 15.597 15.230  1.00 17.99  ? 157 ILE   A CG1 1 
ATOM   1309 C CG2 . ILE   A 1 156 ? 24.950 16.520 16.833  1.00 20.14  ? 157 ILE   A CG2 1 
ATOM   1310 C CD1 . ILE   A 1 156 ? 27.729 16.034 14.142  1.00 18.18  ? 157 ILE   A CD1 1 
ATOM   1311 N N   . LYS   A 1 157 ? 25.066 17.837 12.716  1.00 14.41  ? 158 LYS   A N   1 
ATOM   1312 C CA  . LYS   A 1 157 ? 25.681 18.308 11.484  1.00 15.11  ? 158 LYS   A CA  1 
ATOM   1313 C C   . LYS   A 1 157 ? 26.657 19.424 11.806  1.00 14.22  ? 158 LYS   A C   1 
ATOM   1314 O O   . LYS   A 1 157 ? 26.379 20.289 12.644  1.00 14.92  ? 158 LYS   A O   1 
ATOM   1315 C CB  . LYS   A 1 157 ? 24.654 18.809 10.451  1.00 16.96  ? 158 LYS   A CB  1 
ATOM   1316 C CG  . LYS   A 1 157 ? 23.923 17.657 9.744   1.00 19.62  ? 158 LYS   A CG  1 
ATOM   1317 C CD  . LYS   A 1 157 ? 22.773 18.129 8.896   1.00 20.15  ? 158 LYS   A CD  1 
ATOM   1318 C CE  . LYS   A 1 157 ? 22.132 16.964 8.111   1.00 21.85  ? 158 LYS   A CE  1 
ATOM   1319 N NZ  . LYS   A 1 157 ? 22.837 16.747 6.804   1.00 24.27  ? 158 LYS   A NZ  1 
ATOM   1320 N N   . ILE   A 1 158 ? 27.814 19.376 11.159  1.00 13.35  ? 159 ILE   A N   1 
ATOM   1321 C CA  . ILE   A 1 158 ? 28.768 20.467 11.229  1.00 13.71  ? 159 ILE   A CA  1 
ATOM   1322 C C   . ILE   A 1 158 ? 28.309 21.572 10.306  1.00 16.61  ? 159 ILE   A C   1 
ATOM   1323 O O   . ILE   A 1 158 ? 27.933 21.327 9.137   1.00 15.34  ? 159 ILE   A O   1 
ATOM   1324 C CB  . ILE   A 1 158 ? 30.154 19.988 10.786  1.00 15.16  ? 159 ILE   A CB  1 
ATOM   1325 C CG1 . ILE   A 1 158 ? 30.634 18.859 11.691  1.00 16.63  ? 159 ILE   A CG1 1 
ATOM   1326 C CG2 . ILE   A 1 158 ? 31.134 21.168 10.720  1.00 18.03  ? 159 ILE   A CG2 1 
ATOM   1327 C CD1 . ILE   A 1 158 ? 31.835 18.091 11.124  1.00 18.82  ? 159 ILE   A CD1 1 
ATOM   1328 N N   A ILE   A 1 159 ? 28.271 22.784 10.846  0.50 16.76  ? 160 ILE   A N   1 
ATOM   1329 N N   B ILE   A 1 159 ? 28.419 22.809 10.774  0.50 26.28  ? 160 ILE   A N   1 
ATOM   1330 C CA  A ILE   A 1 159 ? 27.945 23.961 10.065  0.50 29.43  ? 160 ILE   A CA  1 
ATOM   1331 C CA  B ILE   A 1 159 ? 28.120 23.939 9.927   0.50 34.09  ? 160 ILE   A CA  1 
ATOM   1332 C C   A ILE   A 1 159 ? 29.123 24.906 9.953   0.50 40.79  ? 160 ILE   A C   1 
ATOM   1333 C C   B ILE   A 1 159 ? 29.258 24.957 10.030  0.50 13.81  ? 160 ILE   A C   1 
ATOM   1334 O O   A ILE   A 1 159 ? 30.193 24.699 10.537  0.50 58.67  ? 160 ILE   A O   1 
ATOM   1335 O O   B ILE   A 1 159 ? 30.289 24.738 10.682  0.50 13.95  ? 160 ILE   A O   1 
ATOM   1336 C CB  A ILE   A 1 159 ? 26.793 24.750 10.694  0.50 18.82  ? 160 ILE   A CB  1 
ATOM   1337 C CB  B ILE   A 1 159 ? 26.735 24.549 10.234  0.50 30.05  ? 160 ILE   A CB  1 
ATOM   1338 C CG1 A ILE   A 1 159 ? 27.206 25.274 12.070  0.50 15.26  ? 160 ILE   A CG1 1 
ATOM   1339 C CG1 B ILE   A 1 159 ? 25.656 23.495 10.053  0.50 31.65  ? 160 ILE   A CG1 1 
ATOM   1340 C CG2 A ILE   A 1 159 ? 25.554 23.903 10.776  0.50 11.27  ? 160 ILE   A CG2 1 
ATOM   1341 C CG2 B ILE   A 1 159 ? 26.321 25.533 9.134   0.50 23.60  ? 160 ILE   A CG2 1 
ATOM   1342 C CD1 A ILE   A 1 159 ? 26.296 26.203 12.501  0.50 14.52  ? 160 ILE   A CD1 1 
ATOM   1343 C CD1 B ILE   A 1 159 ? 25.154 22.868 11.316  0.50 40.93  ? 160 ILE   A CD1 1 
ATOM   1344 N N   A ASP   A 1 160 ? 28.871 25.979 9.224   0.50 36.66  ? 161 ASP   A N   1 
ATOM   1345 N N   B ASP   A 1 160 ? 29.063 26.061 9.336   0.50 14.60  ? 161 ASP   A N   1 
ATOM   1346 C CA  A ASP   A 1 160 ? 29.683 27.170 9.057   0.50 32.34  ? 161 ASP   A CA  1 
ATOM   1347 C CA  B ASP   A 1 160 ? 29.950 27.198 9.294   0.50 19.78  ? 161 ASP   A CA  1 
ATOM   1348 C C   A ASP   A 1 160 ? 31.124 26.925 8.648   0.50 25.63  ? 161 ASP   A C   1 
ATOM   1349 C C   B ASP   A 1 160 ? 31.252 26.782 8.661   0.50 20.17  ? 161 ASP   A C   1 
ATOM   1350 O O   A ASP   A 1 160 ? 32.054 26.888 9.466   0.50 27.21  ? 161 ASP   A O   1 
ATOM   1351 O O   B ASP   A 1 160 ? 32.202 26.379 9.344   0.50 23.72  ? 161 ASP   A O   1 
ATOM   1352 C CB  A ASP   A 1 160 ? 29.629 28.123 10.229  0.50 33.50  ? 161 ASP   A CB  1 
ATOM   1353 C CB  B ASP   A 1 160 ? 30.185 27.891 10.632  0.50 23.23  ? 161 ASP   A CB  1 
ATOM   1354 C CG  A ASP   A 1 160 ? 30.004 29.504 9.796   0.50 34.73  ? 161 ASP   A CG  1 
ATOM   1355 C CG  B ASP   A 1 160 ? 30.642 29.310 10.419  0.50 28.04  ? 161 ASP   A CG  1 
ATOM   1356 O OD1 A ASP   A 1 160 ? 31.207 29.778 9.621   0.50 34.12  ? 161 ASP   A OD1 1 
ATOM   1357 O OD1 B ASP   A 1 160 ? 31.746 29.468 9.850   0.50 29.97  ? 161 ASP   A OD1 1 
ATOM   1358 O OD2 A ASP   A 1 160 ? 29.075 30.303 9.597   0.50 35.70  ? 161 ASP   A OD2 1 
ATOM   1359 O OD2 B ASP   A 1 160 ? 29.921 30.250 10.796  0.50 30.05  ? 161 ASP   A OD2 1 
ATOM   1360 N N   . PHE   A 1 161 ? 31.284 26.842 7.343   1.00 18.31  ? 162 PHE   A N   1 
ATOM   1361 C CA  . PHE   A 1 161 ? 32.512 26.599 6.631   1.00 15.91  ? 162 PHE   A CA  1 
ATOM   1362 C C   . PHE   A 1 161 ? 33.220 27.890 6.260   1.00 16.89  ? 162 PHE   A C   1 
ATOM   1363 O O   . PHE   A 1 161 ? 33.990 27.909 5.306   1.00 16.96  ? 162 PHE   A O   1 
ATOM   1364 C CB  . PHE   A 1 161 ? 32.169 25.703 5.444   1.00 15.97  ? 162 PHE   A CB  1 
ATOM   1365 C CG  . PHE   A 1 161 ? 31.950 24.296 5.870   1.00 15.00  ? 162 PHE   A CG  1 
ATOM   1366 C CD1 . PHE   A 1 161 ? 30.732 23.912 6.423   1.00 18.12  ? 162 PHE   A CD1 1 
ATOM   1367 C CD2 . PHE   A 1 161 ? 32.965 23.364 5.782   1.00 15.62  ? 162 PHE   A CD2 1 
ATOM   1368 C CE1 . PHE   A 1 161 ? 30.552 22.615 6.898   1.00 19.37  ? 162 PHE   A CE1 1 
ATOM   1369 C CE2 . PHE   A 1 161 ? 32.789 22.083 6.236   1.00 17.57  ? 162 PHE   A CE2 1 
ATOM   1370 C CZ  . PHE   A 1 161 ? 31.590 21.703 6.797   1.00 18.42  ? 162 PHE   A CZ  1 
ATOM   1371 N N   . GLY   A 1 162 ? 33.008 28.962 7.034   1.00 17.02  ? 163 GLY   A N   1 
ATOM   1372 C CA  . GLY   A 1 162 ? 33.588 30.257 6.722   1.00 17.54  ? 163 GLY   A CA  1 
ATOM   1373 C C   . GLY   A 1 162 ? 35.094 30.359 6.871   1.00 17.17  ? 163 GLY   A C   1 
ATOM   1374 O O   . GLY   A 1 162 ? 35.685 31.297 6.335   1.00 19.69  ? 163 GLY   A O   1 
ATOM   1375 N N   . LEU   A 1 163 ? 35.736 29.418 7.556   1.00 15.68  ? 164 LEU   A N   1 
ATOM   1376 C CA  . LEU   A 1 163 ? 37.195 29.387 7.635   1.00 16.08  ? 164 LEU   A CA  1 
ATOM   1377 C C   . LEU   A 1 163 ? 37.787 28.198 6.894   1.00 15.15  ? 164 LEU   A C   1 
ATOM   1378 O O   . LEU   A 1 163 ? 39.011 28.041 6.868   1.00 15.87  ? 164 LEU   A O   1 
ATOM   1379 C CB  . LEU   A 1 163 ? 37.665 29.379 9.098   1.00 19.53  ? 164 LEU   A CB  1 
ATOM   1380 C CG  . LEU   A 1 163 ? 37.613 30.680 9.884   1.00 25.01  ? 164 LEU   A CG  1 
ATOM   1381 C CD1 . LEU   A 1 163 ? 38.393 30.490 11.183  1.00 26.02  ? 164 LEU   A CD1 1 
ATOM   1382 C CD2 . LEU   A 1 163 ? 38.164 31.836 9.067   1.00 27.91  ? 164 LEU   A CD2 1 
ATOM   1383 N N   . ALA   A 1 164 ? 36.951 27.351 6.306   1.00 13.96  ? 165 ALA   A N   1 
ATOM   1384 C CA  . ALA   A 1 164 ? 37.434 26.100 5.742   1.00 13.25  ? 165 ALA   A CA  1 
ATOM   1385 C C   . ALA   A 1 164 ? 38.300 26.357 4.512   1.00 13.43  ? 165 ALA   A C   1 
ATOM   1386 O O   . ALA   A 1 164 ? 38.038 27.272 3.708   1.00 15.15  ? 165 ALA   A O   1 
ATOM   1387 C CB  . ALA   A 1 164 ? 36.252 25.198 5.395   1.00 14.13  ? 165 ALA   A CB  1 
ATOM   1388 N N   . HIS   A 1 165 ? 39.329 25.523 4.342   1.00 13.31  ? 166 HIS   A N   1 
ATOM   1389 C CA  . HIS   A 1 165 ? 40.200 25.641 3.181   1.00 13.85  ? 166 HIS   A CA  1 
ATOM   1390 C C   . HIS   A 1 165 ? 40.540 24.257 2.661   1.00 14.32  ? 166 HIS   A C   1 
ATOM   1391 O O   . HIS   A 1 165 ? 40.718 23.304 3.432   1.00 14.25  ? 166 HIS   A O   1 
ATOM   1392 C CB  . HIS   A 1 165 ? 41.540 26.271 3.552   1.00 15.41  ? 166 HIS   A CB  1 
ATOM   1393 C CG  . HIS   A 1 165 ? 41.511 27.752 3.693   1.00 16.68  ? 166 HIS   A CG  1 
ATOM   1394 N ND1 . HIS   A 1 165 ? 40.835 28.399 4.704   1.00 16.46  ? 166 HIS   A ND1 1 
ATOM   1395 C CD2 . HIS   A 1 165 ? 42.091 28.721 2.944   1.00 17.79  ? 166 HIS   A CD2 1 
ATOM   1396 C CE1 . HIS   A 1 165 ? 40.996 29.706 4.567   1.00 17.89  ? 166 HIS   A CE1 1 
ATOM   1397 N NE2 . HIS   A 1 165 ? 41.752 29.927 3.506   1.00 19.26  ? 166 HIS   A NE2 1 
ATOM   1398 N N   . LYS   A 1 166 ? 40.681 24.175 1.346   1.00 16.35  ? 167 LYS   A N   1 
ATOM   1399 C CA  . LYS   A 1 166 ? 41.283 23.011 0.730   1.00 18.48  ? 167 LYS   A CA  1 
ATOM   1400 C C   . LYS   A 1 166 ? 42.789 23.039 0.965   1.00 19.37  ? 167 LYS   A C   1 
ATOM   1401 O O   . LYS   A 1 166 ? 43.447 24.064 0.744   1.00 24.06  ? 167 LYS   A O   1 
ATOM   1402 C CB  . LYS   A 1 166 ? 41.003 23.049 -0.766  1.00 25.78  ? 167 LYS   A CB  1 
ATOM   1403 C CG  . LYS   A 1 166 ? 39.724 22.351 -1.112  1.00 32.04  ? 167 LYS   A CG  1 
ATOM   1404 C CD  . LYS   A 1 166 ? 40.014 20.871 -1.305  1.00 36.02  ? 167 LYS   A CD  1 
ATOM   1405 C CE  . LYS   A 1 166 ? 38.877 20.186 -2.026  1.00 38.43  ? 167 LYS   A CE  1 
ATOM   1406 N NZ  . LYS   A 1 166 ? 38.744 20.768 -3.370  1.00 40.33  ? 167 LYS   A NZ  1 
ATOM   1407 N N   . ILE   A 1 167 ? 43.334 21.915 1.400   1.00 17.13  ? 168 ILE   A N   1 
ATOM   1408 C CA  . ILE   A 1 167 ? 44.749 21.820 1.748   1.00 19.79  ? 168 ILE   A CA  1 
ATOM   1409 C C   . ILE   A 1 167 ? 45.385 20.874 0.743   1.00 23.88  ? 168 ILE   A C   1 
ATOM   1410 O O   . ILE   A 1 167 ? 45.523 19.676 1.011   1.00 28.01  ? 168 ILE   A O   1 
ATOM   1411 C CB  . ILE   A 1 167 ? 44.950 21.273 3.182   1.00 20.25  ? 168 ILE   A CB  1 
ATOM   1412 C CG1 . ILE   A 1 167 ? 44.103 22.006 4.234   1.00 22.99  ? 168 ILE   A CG1 1 
ATOM   1413 C CG2 . ILE   A 1 167 ? 46.419 21.367 3.580   1.00 22.19  ? 168 ILE   A CG2 1 
ATOM   1414 C CD1 . ILE   A 1 167 ? 44.454 23.441 4.401   1.00 24.24  ? 168 ILE   A CD1 1 
ATOM   1415 N N   . ASP   A 1 168 ? 45.773 21.389 -0.412  1.00 23.43  ? 169 ASP   A N   1 
ATOM   1416 C CA  . ASP   A 1 168 ? 46.298 20.505 -1.442  1.00 24.77  ? 169 ASP   A CA  1 
ATOM   1417 C C   . ASP   A 1 168 ? 47.828 20.442 -1.443  1.00 21.48  ? 169 ASP   A C   1 
ATOM   1418 O O   . ASP   A 1 168 ? 48.417 19.597 -2.145  1.00 21.20  ? 169 ASP   A O   1 
ATOM   1419 C CB  . ASP   A 1 168 ? 45.771 20.970 -2.797  1.00 31.44  ? 169 ASP   A CB  1 
ATOM   1420 C CG  . ASP   A 1 168 ? 44.356 20.465 -3.062  1.00 37.72  ? 169 ASP   A CG  1 
ATOM   1421 O OD1 . ASP   A 1 168 ? 43.949 19.466 -2.416  1.00 38.20  ? 169 ASP   A OD1 1 
ATOM   1422 O OD2 . ASP   A 1 168 ? 43.650 21.079 -3.893  1.00 40.67  ? 169 ASP   A OD2 1 
ATOM   1423 N N   . PHE   A 1 169 ? 48.492 21.307 -0.675  1.00 20.84  ? 170 PHE   A N   1 
ATOM   1424 C CA  . PHE   A 1 169 ? 49.940 21.288 -0.554  1.00 22.19  ? 170 PHE   A CA  1 
ATOM   1425 C C   . PHE   A 1 169 ? 50.343 20.934 0.869   1.00 21.70  ? 170 PHE   A C   1 
ATOM   1426 O O   . PHE   A 1 169 ? 51.383 21.390 1.349   1.00 25.75  ? 170 PHE   A O   1 
ATOM   1427 C CB  . PHE   A 1 169 ? 50.541 22.642 -0.944  1.00 25.90  ? 170 PHE   A CB  1 
ATOM   1428 C CG  . PHE   A 1 169 ? 50.369 23.002 -2.394  1.00 32.63  ? 170 PHE   A CG  1 
ATOM   1429 C CD1 . PHE   A 1 169 ? 51.324 22.664 -3.338  1.00 32.79  ? 170 PHE   A CD1 1 
ATOM   1430 C CD2 . PHE   A 1 169 ? 49.247 23.700 -2.810  1.00 36.80  ? 170 PHE   A CD2 1 
ATOM   1431 C CE1 . PHE   A 1 169 ? 51.157 23.009 -4.668  1.00 36.56  ? 170 PHE   A CE1 1 
ATOM   1432 C CE2 . PHE   A 1 169 ? 49.073 24.046 -4.142  1.00 38.61  ? 170 PHE   A CE2 1 
ATOM   1433 C CZ  . PHE   A 1 169 ? 50.030 23.699 -5.071  1.00 38.06  ? 170 PHE   A CZ  1 
ATOM   1434 N N   . GLY   A 1 170 ? 49.489 20.201 1.593   1.00 20.96  ? 171 GLY   A N   1 
ATOM   1435 C CA  . GLY   A 1 170 ? 49.810 19.812 2.960   1.00 21.92  ? 171 GLY   A CA  1 
ATOM   1436 C C   . GLY   A 1 170 ? 49.556 20.847 4.043   1.00 19.77  ? 171 GLY   A C   1 
ATOM   1437 O O   . GLY   A 1 170 ? 49.234 20.485 5.182   1.00 19.93  ? 171 GLY   A O   1 
ATOM   1438 N N   . ASN   A 1 171 ? 49.654 22.137 3.716   1.00 18.22  ? 172 ASN   A N   1 
ATOM   1439 C CA  . ASN   A 1 171 ? 49.443 23.177 4.708   1.00 16.28  ? 172 ASN   A CA  1 
ATOM   1440 C C   . ASN   A 1 171 ? 49.084 24.466 3.984   1.00 16.62  ? 172 ASN   A C   1 
ATOM   1441 O O   . ASN   A 1 171 ? 49.340 24.614 2.786   1.00 18.64  ? 172 ASN   A O   1 
ATOM   1442 C CB  . ASN   A 1 171 ? 50.678 23.350 5.591   1.00 16.87  ? 172 ASN   A CB  1 
ATOM   1443 C CG  . ASN   A 1 171 ? 51.846 23.924 4.816   1.00 19.47  ? 172 ASN   A CG  1 
ATOM   1444 O OD1 . ASN   A 1 171 ? 51.868 25.109 4.510   1.00 20.47  ? 172 ASN   A OD1 1 
ATOM   1445 N ND2 . ASN   A 1 171 ? 52.818 23.082 4.478   1.00 21.75  ? 172 ASN   A ND2 1 
ATOM   1446 N N   . GLU   A 1 172 ? 48.464 25.383 4.717   1.00 16.53  ? 173 GLU   A N   1 
ATOM   1447 C CA  . GLU   A 1 172 ? 48.181 26.749 4.293   1.00 18.12  ? 173 GLU   A CA  1 
ATOM   1448 C C   . GLU   A 1 172 ? 48.859 27.738 5.219   1.00 17.68  ? 173 GLU   A C   1 
ATOM   1449 O O   . GLU   A 1 172 ? 48.921 27.519 6.427   1.00 19.00  ? 173 GLU   A O   1 
ATOM   1450 C CB  . GLU   A 1 172 ? 46.680 27.059 4.338   1.00 24.82  ? 173 GLU   A CB  1 
ATOM   1451 C CG  . GLU   A 1 172 ? 45.862 26.231 3.440   1.00 32.04  ? 173 GLU   A CG  1 
ATOM   1452 C CD  . GLU   A 1 172 ? 45.793 26.795 2.038   1.00 38.33  ? 173 GLU   A CD  1 
ATOM   1453 O OE1 . GLU   A 1 172 ? 46.284 27.926 1.805   1.00 37.57  ? 173 GLU   A OE1 1 
ATOM   1454 O OE2 . GLU   A 1 172 ? 45.264 26.086 1.158   1.00 42.24  ? 173 GLU   A OE2 1 
ATOM   1455 N N   . PHE   A 1 173 ? 49.342 28.831 4.654   1.00 18.61  ? 174 PHE   A N   1 
ATOM   1456 C CA  . PHE   A 1 173 ? 50.055 29.839 5.476   1.00 20.42  ? 174 PHE   A CA  1 
ATOM   1457 C C   . PHE   A 1 173 ? 49.509 31.205 5.140   1.00 24.58  ? 174 PHE   A C   1 
ATOM   1458 O O   . PHE   A 1 173 ? 50.014 31.872 4.227   1.00 27.66  ? 174 PHE   A O   1 
ATOM   1459 C CB  . PHE   A 1 173 ? 51.545 29.742 5.158   1.00 20.51  ? 174 PHE   A CB  1 
ATOM   1460 C CG  . PHE   A 1 173 ? 52.491 30.539 6.044   1.00 22.59  ? 174 PHE   A CG  1 
ATOM   1461 C CD1 . PHE   A 1 173 ? 52.279 30.640 7.412   1.00 24.63  ? 174 PHE   A CD1 1 
ATOM   1462 C CD2 . PHE   A 1 173 ? 53.592 31.186 5.500   1.00 25.78  ? 174 PHE   A CD2 1 
ATOM   1463 C CE1 . PHE   A 1 173 ? 53.152 31.362 8.208   1.00 26.62  ? 174 PHE   A CE1 1 
ATOM   1464 C CE2 . PHE   A 1 173 ? 54.461 31.903 6.302   1.00 28.56  ? 174 PHE   A CE2 1 
ATOM   1465 C CZ  . PHE   A 1 173 ? 54.238 31.992 7.654   1.00 28.78  ? 174 PHE   A CZ  1 
ATOM   1466 N N   . LYS   A 1 174 ? 48.473 31.613 5.857   1.00 24.24  ? 175 LYS   A N   1 
ATOM   1467 C CA  . LYS   A 1 174 ? 47.830 32.905 5.547   1.00 25.95  ? 175 LYS   A CA  1 
ATOM   1468 C C   . LYS   A 1 174 ? 47.041 33.400 6.761   1.00 27.13  ? 175 LYS   A C   1 
ATOM   1469 O O   . LYS   A 1 174 ? 47.354 32.973 7.873   1.00 28.76  ? 175 LYS   A O   1 
ATOM   1470 C CB  . LYS   A 1 174 ? 46.886 32.692 4.368   1.00 26.01  ? 175 LYS   A CB  1 
ATOM   1471 C CG  . LYS   A 1 174 ? 46.041 31.442 4.471   1.00 26.03  ? 175 LYS   A CG  1 
ATOM   1472 C CD  . LYS   A 1 174 ? 45.022 31.380 3.345   1.00 26.74  ? 175 LYS   A CD  1 
ATOM   1473 C CE  . LYS   A 1 174 ? 44.028 32.481 3.495   1.00 29.27  ? 175 LYS   A CE  1 
ATOM   1474 N NZ  . LYS   A 1 174 ? 42.944 32.351 2.521   1.00 29.28  ? 175 LYS   A NZ  1 
ATOM   1475 N N   . ASN   A 1 175 ? 46.063 34.267 6.517   1.00 28.94  ? 176 ASN   A N   1 
ATOM   1476 C CA  . ASN   A 1 175 ? 45.247 34.868 7.609   1.00 33.55  ? 176 ASN   A CA  1 
ATOM   1477 C C   . ASN   A 1 175 ? 44.155 33.887 8.018   1.00 31.16  ? 176 ASN   A C   1 
ATOM   1478 O O   . ASN   A 1 175 ? 43.064 33.956 7.438   1.00 33.64  ? 176 ASN   A O   1 
ATOM   1479 C CB  . ASN   A 1 175 ? 44.630 36.197 7.183   1.00 42.05  ? 176 ASN   A CB  1 
ATOM   1480 C CG  . ASN   A 1 175 ? 43.844 36.861 8.287   1.00 49.94  ? 176 ASN   A CG  1 
ATOM   1481 O OD1 . ASN   A 1 175 ? 43.904 36.432 9.444   1.00 52.73  ? 176 ASN   A OD1 1 
ATOM   1482 N ND2 . ASN   A 1 175 ? 43.119 37.918 7.957   1.00 52.33  ? 176 ASN   A ND2 1 
ATOM   1483 N N   . ILE   A 1 176 ? 44.486 32.996 8.948   1.00 25.11  ? 177 ILE   A N   1 
ATOM   1484 C CA  . ILE   A 1 176 ? 43.517 32.011 9.425   1.00 21.51  ? 177 ILE   A CA  1 
ATOM   1485 C C   . ILE   A 1 176 ? 43.595 31.947 10.945  1.00 19.48  ? 177 ILE   A C   1 
ATOM   1486 O O   . ILE   A 1 176 ? 44.607 31.505 11.505  1.00 19.60  ? 177 ILE   A O   1 
ATOM   1487 C CB  . ILE   A 1 176 ? 43.723 30.608 8.828   1.00 17.77  ? 177 ILE   A CB  1 
ATOM   1488 C CG1 . ILE   A 1 176 ? 43.551 30.613 7.301   1.00 18.10  ? 177 ILE   A CG1 1 
ATOM   1489 C CG2 . ILE   A 1 176 ? 42.765 29.628 9.488   1.00 19.49  ? 177 ILE   A CG2 1 
ATOM   1490 C CD1 . ILE   A 1 176 ? 43.976 29.318 6.660   1.00 19.64  ? 177 ILE   A CD1 1 
ATOM   1491 N N   . PHE   A 1 177 ? 42.518 32.347 11.612  1.00 17.19  ? 178 PHE   A N   1 
ATOM   1492 C CA  . PHE   A 1 177 ? 42.501 32.343 13.067  1.00 17.31  ? 178 PHE   A CA  1 
ATOM   1493 C C   . PHE   A 1 177 ? 41.058 32.159 13.525  1.00 19.07  ? 178 PHE   A C   1 
ATOM   1494 O O   . PHE   A 1 177 ? 40.193 32.980 13.210  1.00 22.99  ? 178 PHE   A O   1 
ATOM   1495 C CB  . PHE   A 1 177 ? 43.083 33.653 13.594  1.00 18.29  ? 178 PHE   A CB  1 
ATOM   1496 C CG  . PHE   A 1 177 ? 43.828 33.507 14.899  1.00 16.97  ? 178 PHE   A CG  1 
ATOM   1497 C CD1 . PHE   A 1 177 ? 43.148 33.148 16.060  1.00 17.79  ? 178 PHE   A CD1 1 
ATOM   1498 C CD2 . PHE   A 1 177 ? 45.199 33.760 14.970  1.00 17.73  ? 178 PHE   A CD2 1 
ATOM   1499 C CE1 . PHE   A 1 177 ? 43.823 33.046 17.279  1.00 18.90  ? 178 PHE   A CE1 1 
ATOM   1500 C CE2 . PHE   A 1 177 ? 45.881 33.652 16.192  1.00 17.85  ? 178 PHE   A CE2 1 
ATOM   1501 C CZ  . PHE   A 1 177 ? 45.181 33.293 17.346  1.00 18.49  ? 178 PHE   A CZ  1 
ATOM   1502 N N   . GLY   A 1 178 ? 40.793 31.090 14.264  1.00 20.02  ? 179 GLY   A N   1 
ATOM   1503 C CA  . GLY   A 1 178 ? 39.477 30.818 14.820  1.00 21.17  ? 179 GLY   A CA  1 
ATOM   1504 C C   . GLY   A 1 178 ? 39.293 31.381 16.222  1.00 22.39  ? 179 GLY   A C   1 
ATOM   1505 O O   . GLY   A 1 178 ? 39.933 32.359 16.618  1.00 23.25  ? 179 GLY   A O   1 
ATOM   1506 N N   . THR   A 1 179 ? 38.425 30.725 17.004  1.00 20.93  ? 180 THR   A N   1 
ATOM   1507 C CA  . THR   A 1 179 ? 38.079 31.181 18.351  1.00 21.18  ? 180 THR   A CA  1 
ATOM   1508 C C   . THR   A 1 179 ? 39.162 30.751 19.335  1.00 17.80  ? 180 THR   A C   1 
ATOM   1509 O O   . THR   A 1 179 ? 39.508 29.564 19.377  1.00 16.64  ? 180 THR   A O   1 
ATOM   1510 C CB  . THR   A 1 179 ? 36.741 30.575 18.742  1.00 24.37  ? 180 THR   A CB  1 
ATOM   1511 O OG1 . THR   A 1 179 ? 35.736 31.110 17.875  1.00 28.56  ? 180 THR   A OG1 1 
ATOM   1512 C CG2 . THR   A 1 179 ? 36.371 30.892 20.189  1.00 26.43  ? 180 THR   A CG2 1 
ATOM   1513 N N   . PRO   A 1 180 ? 39.690 31.673 20.162  1.00 18.25  ? 181 PRO   A N   1 
ATOM   1514 C CA  . PRO   A 1 180 ? 40.871 31.351 20.991  1.00 17.01  ? 181 PRO   A CA  1 
ATOM   1515 C C   . PRO   A 1 180 ? 40.804 30.063 21.795  1.00 15.57  ? 181 PRO   A C   1 
ATOM   1516 O O   . PRO   A 1 180 ? 41.792 29.321 21.818  1.00 15.48  ? 181 PRO   A O   1 
ATOM   1517 C CB  . PRO   A 1 180 ? 41.013 32.597 21.867  1.00 19.26  ? 181 PRO   A CB  1 
ATOM   1518 C CG  . PRO   A 1 180 ? 40.579 33.693 20.928  1.00 21.18  ? 181 PRO   A CG  1 
ATOM   1519 C CD  . PRO   A 1 180 ? 39.419 33.125 20.157  1.00 21.31  ? 181 PRO   A CD  1 
ATOM   1520 N N   . GLU   A 1 181 ? 39.675 29.768 22.442  1.00 14.90  ? 182 GLU   A N   1 
ATOM   1521 C CA  . GLU   A 1 181 ? 39.602 28.565 23.263  1.00 15.00  ? 182 GLU   A CA  1 
ATOM   1522 C C   . GLU   A 1 181 ? 39.814 27.280 22.477  1.00 13.17  ? 182 GLU   A C   1 
ATOM   1523 O O   . GLU   A 1 181 ? 40.147 26.258 23.086  1.00 13.26  ? 182 GLU   A O   1 
ATOM   1524 C CB  . GLU   A 1 181 ? 38.237 28.433 23.946  1.00 19.25  ? 182 GLU   A CB  1 
ATOM   1525 C CG  . GLU   A 1 181 ? 38.033 29.248 25.159  1.00 25.04  ? 182 GLU   A CG  1 
ATOM   1526 C CD  . GLU   A 1 181 ? 36.577 29.251 25.500  1.00 29.47  ? 182 GLU   A CD  1 
ATOM   1527 O OE1 . GLU   A 1 181 ? 36.089 28.265 26.098  1.00 30.49  ? 182 GLU   A OE1 1 
ATOM   1528 O OE2 . GLU   A 1 181 ? 35.905 30.205 25.086  1.00 32.51  ? 182 GLU   A OE2 1 
ATOM   1529 N N   . PHE   A 1 182 ? 39.600 27.298 21.152  1.00 12.45  ? 183 PHE   A N   1 
ATOM   1530 C CA  . PHE   A 1 182 ? 39.568 26.087 20.338  1.00 13.18  ? 183 PHE   A CA  1 
ATOM   1531 C C   . PHE   A 1 182 ? 40.704 25.977 19.338  1.00 12.96  ? 183 PHE   A C   1 
ATOM   1532 O O   . PHE   A 1 182 ? 40.851 24.917 18.722  1.00 15.71  ? 183 PHE   A O   1 
ATOM   1533 C CB  . PHE   A 1 182 ? 38.223 25.990 19.603  1.00 14.77  ? 183 PHE   A CB  1 
ATOM   1534 C CG  . PHE   A 1 182 ? 37.078 25.826 20.533  1.00 16.40  ? 183 PHE   A CG  1 
ATOM   1535 C CD1 . PHE   A 1 182 ? 36.735 24.566 21.002  1.00 18.05  ? 183 PHE   A CD1 1 
ATOM   1536 C CD2 . PHE   A 1 182 ? 36.387 26.931 20.998  1.00 16.85  ? 183 PHE   A CD2 1 
ATOM   1537 C CE1 . PHE   A 1 182 ? 35.694 24.399 21.885  1.00 19.37  ? 183 PHE   A CE1 1 
ATOM   1538 C CE2 . PHE   A 1 182 ? 35.343 26.777 21.911  1.00 19.54  ? 183 PHE   A CE2 1 
ATOM   1539 C CZ  . PHE   A 1 182 ? 35.009 25.510 22.365  1.00 20.80  ? 183 PHE   A CZ  1 
ATOM   1540 N N   . VAL   A 1 183 ? 41.523 27.010 19.175  1.00 12.46  ? 184 VAL   A N   1 
ATOM   1541 C CA  . VAL   A 1 183 ? 42.553 26.987 18.148  1.00 12.38  ? 184 VAL   A CA  1 
ATOM   1542 C C   . VAL   A 1 183 ? 43.772 26.213 18.632  1.00 12.47  ? 184 VAL   A C   1 
ATOM   1543 O O   . VAL   A 1 183 ? 44.153 26.257 19.807  1.00 13.72  ? 184 VAL   A O   1 
ATOM   1544 C CB  . VAL   A 1 183 ? 42.944 28.406 17.683  1.00 13.97  ? 184 VAL   A CB  1 
ATOM   1545 C CG1 . VAL   A 1 183 ? 41.786 29.099 16.995  1.00 16.65  ? 184 VAL   A CG1 1 
ATOM   1546 C CG2 . VAL   A 1 183 ? 43.543 29.247 18.815  1.00 15.50  ? 184 VAL   A CG2 1 
ATOM   1547 N N   . ALA   A 1 184 ? 44.451 25.586 17.685  1.00 12.90  ? 185 ALA   A N   1 
ATOM   1548 C CA  . ALA   A 1 184 ? 45.668 24.839 17.957  1.00 12.56  ? 185 ALA   A CA  1 
ATOM   1549 C C   . ALA   A 1 184 ? 46.861 25.782 18.142  1.00 12.31  ? 185 ALA   A C   1 
ATOM   1550 O O   . ALA   A 1 184 ? 46.830 26.940 17.697  1.00 12.68  ? 185 ALA   A O   1 
ATOM   1551 C CB  . ALA   A 1 184 ? 45.937 23.893 16.784  1.00 13.73  ? 185 ALA   A CB  1 
ATOM   1552 N N   . PRO   A 1 185 ? 47.947 25.297 18.769  1.00 12.47  ? 186 PRO   A N   1 
ATOM   1553 C CA  . PRO   A 1 185 ? 49.133 26.158 18.951  1.00 13.32  ? 186 PRO   A CA  1 
ATOM   1554 C C   . PRO   A 1 185 ? 49.673 26.722 17.656  1.00 13.39  ? 186 PRO   A C   1 
ATOM   1555 O O   . PRO   A 1 185 ? 50.157 27.861 17.642  1.00 14.46  ? 186 PRO   A O   1 
ATOM   1556 C CB  . PRO   A 1 185 ? 50.144 25.245 19.657  1.00 14.67  ? 186 PRO   A CB  1 
ATOM   1557 C CG  . PRO   A 1 185 ? 49.276 24.247 20.389  1.00 15.03  ? 186 PRO   A CG  1 
ATOM   1558 C CD  . PRO   A 1 185 ? 48.064 24.010 19.487  1.00 13.72  ? 186 PRO   A CD  1 
ATOM   1559 N N   . GLU   A 1 186 ? 49.615 25.962 16.553  1.00 13.33  ? 187 GLU   A N   1 
ATOM   1560 C CA  . GLU   A 1 186 ? 50.148 26.497 15.303  1.00 13.56  ? 187 GLU   A CA  1 
ATOM   1561 C C   . GLU   A 1 186 ? 49.335 27.687 14.806  1.00 12.30  ? 187 GLU   A C   1 
ATOM   1562 O O   . GLU   A 1 186 ? 49.890 28.560 14.126  1.00 14.53  ? 187 GLU   A O   1 
ATOM   1563 C CB  . GLU   A 1 186 ? 50.249 25.400 14.226  1.00 13.53  ? 187 GLU   A CB  1 
ATOM   1564 C CG  . GLU   A 1 186 ? 48.954 24.638 13.911  1.00 14.81  ? 187 GLU   A CG  1 
ATOM   1565 C CD  . GLU   A 1 186 ? 48.720 23.389 14.728  1.00 13.70  ? 187 GLU   A CD  1 
ATOM   1566 O OE1 . GLU   A 1 186 ? 49.180 23.322 15.903  1.00 14.18  ? 187 GLU   A OE1 1 
ATOM   1567 O OE2 . GLU   A 1 186 ? 48.057 22.473 14.185  1.00 14.33  ? 187 GLU   A OE2 1 
ATOM   1568 N N   . ILE   A 1 187 ? 48.040 27.759 15.148  1.00 12.62  ? 188 ILE   A N   1 
ATOM   1569 C CA  . ILE   A 1 187 ? 47.255 28.954 14.832  1.00 13.08  ? 188 ILE   A CA  1 
ATOM   1570 C C   . ILE   A 1 187 ? 47.730 30.133 15.678  1.00 13.75  ? 188 ILE   A C   1 
ATOM   1571 O O   . ILE   A 1 187 ? 47.981 31.235 15.168  1.00 14.32  ? 188 ILE   A O   1 
ATOM   1572 C CB  . ILE   A 1 187 ? 45.740 28.683 14.988  1.00 13.33  ? 188 ILE   A CB  1 
ATOM   1573 C CG1 . ILE   A 1 187 ? 45.294 27.648 13.941  1.00 14.94  ? 188 ILE   A CG1 1 
ATOM   1574 C CG2 . ILE   A 1 187 ? 44.950 29.988 14.896  1.00 15.24  ? 188 ILE   A CG2 1 
ATOM   1575 C CD1 . ILE   A 1 187 ? 43.812 27.315 13.942  1.00 16.26  ? 188 ILE   A CD1 1 
ATOM   1576 N N   . VAL   A 1 188 ? 47.862 29.906 16.991  1.00 13.47  ? 189 VAL   A N   1 
ATOM   1577 C CA  . VAL   A 1 188 ? 48.307 30.950 17.910  1.00 13.70  ? 189 VAL   A CA  1 
ATOM   1578 C C   . VAL   A 1 188 ? 49.648 31.520 17.474  1.00 13.86  ? 189 VAL   A C   1 
ATOM   1579 O O   . VAL   A 1 188 ? 49.899 32.723 17.610  1.00 14.85  ? 189 VAL   A O   1 
ATOM   1580 C CB  . VAL   A 1 188 ? 48.399 30.378 19.342  1.00 14.58  ? 189 VAL   A CB  1 
ATOM   1581 C CG1 . VAL   A 1 188 ? 48.960 31.441 20.312  1.00 15.48  ? 189 VAL   A CG1 1 
ATOM   1582 C CG2 . VAL   A 1 188 ? 47.038 29.866 19.807  1.00 15.93  ? 189 VAL   A CG2 1 
ATOM   1583 N N   . ASN   A 1 189 ? 50.537 30.655 16.992  1.00 13.79  ? 190 ASN   A N   1 
ATOM   1584 C CA  . ASN   A 1 189 ? 51.894 31.030 16.625  1.00 14.93  ? 190 ASN   A CA  1 
ATOM   1585 C C   . ASN   A 1 189 ? 52.025 31.449 15.161  1.00 15.24  ? 190 ASN   A C   1 
ATOM   1586 O O   . ASN   A 1 189 ? 53.145 31.702 14.704  1.00 16.39  ? 190 ASN   A O   1 
ATOM   1587 C CB  . ASN   A 1 189 ? 52.864 29.897 16.966  1.00 15.09  ? 190 ASN   A CB  1 
ATOM   1588 C CG  . ASN   A 1 189 ? 53.155 29.822 18.451  1.00 15.83  ? 190 ASN   A CG  1 
ATOM   1589 O OD1 . ASN   A 1 189 ? 54.036 30.503 18.940  1.00 18.77  ? 190 ASN   A OD1 1 
ATOM   1590 N ND2 . ASN   A 1 189 ? 52.390 29.016 19.184  1.00 17.28  ? 190 ASN   A ND2 1 
ATOM   1591 N N   . TYR   A 1 190 ? 50.911 31.514 14.416  1.00 14.27  ? 191 TYR   A N   1 
ATOM   1592 C CA  . TYR   A 1 190 ? 50.921 31.978 13.023  1.00 14.49  ? 191 TYR   A CA  1 
ATOM   1593 C C   . TYR   A 1 190 ? 51.849 31.131 12.146  1.00 14.05  ? 191 TYR   A C   1 
ATOM   1594 O O   . TYR   A 1 190 ? 52.574 31.646 11.290  1.00 17.22  ? 191 TYR   A O   1 
ATOM   1595 C CB  . TYR   A 1 190 ? 51.242 33.472 12.917  1.00 15.06  ? 191 TYR   A CB  1 
ATOM   1596 C CG  . TYR   A 1 190 ? 50.248 34.352 13.626  1.00 14.79  ? 191 TYR   A CG  1 
ATOM   1597 C CD1 . TYR   A 1 190 ? 49.118 34.828 12.961  1.00 16.58  ? 191 TYR   A CD1 1 
ATOM   1598 C CD2 . TYR   A 1 190 ? 50.450 34.745 14.947  1.00 15.44  ? 191 TYR   A CD2 1 
ATOM   1599 C CE1 . TYR   A 1 190 ? 48.207 35.662 13.605  1.00 17.09  ? 191 TYR   A CE1 1 
ATOM   1600 C CE2 . TYR   A 1 190 ? 49.560 35.570 15.587  1.00 16.22  ? 191 TYR   A CE2 1 
ATOM   1601 C CZ  . TYR   A 1 190 ? 48.440 36.023 14.919  1.00 16.60  ? 191 TYR   A CZ  1 
ATOM   1602 O OH  . TYR   A 1 190 ? 47.545 36.843 15.556  1.00 19.14  ? 191 TYR   A OH  1 
ATOM   1603 N N   . GLU   A 1 191 ? 51.797 29.833 12.324  1.00 14.16  ? 192 GLU   A N   1 
ATOM   1604 C CA  . GLU   A 1 191 ? 52.586 28.865 11.589  1.00 15.34  ? 192 GLU   A CA  1 
ATOM   1605 C C   . GLU   A 1 191 ? 51.741 28.241 10.481  1.00 15.77  ? 192 GLU   A C   1 
ATOM   1606 O O   . GLU   A 1 191 ? 50.516 28.365 10.471  1.00 16.20  ? 192 GLU   A O   1 
ATOM   1607 C CB  . GLU   A 1 191 ? 53.044 27.793 12.586  1.00 17.26  ? 192 GLU   A CB  1 
ATOM   1608 C CG  . GLU   A 1 191 ? 54.240 28.319 13.378  1.00 22.26  ? 192 GLU   A CG  1 
ATOM   1609 C CD  . GLU   A 1 191 ? 54.522 27.618 14.687  1.00 28.41  ? 192 GLU   A CD  1 
ATOM   1610 O OE1 . GLU   A 1 191 ? 53.819 26.657 15.059  1.00 29.55  ? 192 GLU   A OE1 1 
ATOM   1611 O OE2 . GLU   A 1 191 ? 55.522 28.011 15.329  1.00 31.12  ? 192 GLU   A OE2 1 
ATOM   1612 N N   . PRO   A 1 192 ? 52.360 27.575 9.510   1.00 16.55  ? 193 PRO   A N   1 
ATOM   1613 C CA  . PRO   A 1 192 ? 51.559 26.861 8.502   1.00 16.37  ? 193 PRO   A CA  1 
ATOM   1614 C C   . PRO   A 1 192 ? 50.602 25.862 9.150   1.00 15.73  ? 193 PRO   A C   1 
ATOM   1615 O O   . PRO   A 1 192 ? 50.909 25.238 10.171  1.00 17.25  ? 193 PRO   A O   1 
ATOM   1616 C CB  . PRO   A 1 192 ? 52.613 26.169 7.635   1.00 18.66  ? 193 PRO   A CB  1 
ATOM   1617 C CG  . PRO   A 1 192 ? 53.876 27.050 7.813   1.00 18.90  ? 193 PRO   A CG  1 
ATOM   1618 C CD  . PRO   A 1 192 ? 53.809 27.487 9.256   1.00 18.10  ? 193 PRO   A CD  1 
ATOM   1619 N N   . LEU   A 1 193 ? 49.415 25.751 8.565   1.00 14.36  ? 194 LEU   A N   1 
ATOM   1620 C CA  . LEU   A 1 193 ? 48.294 25.029 9.152   1.00 13.82  ? 194 LEU   A CA  1 
ATOM   1621 C C   . LEU   A 1 193 ? 47.831 23.909 8.234   1.00 13.71  ? 194 LEU   A C   1 
ATOM   1622 O O   . LEU   A 1 193 ? 47.727 24.093 7.020   1.00 15.40  ? 194 LEU   A O   1 
ATOM   1623 C CB  . LEU   A 1 193 ? 47.095 25.963 9.328   1.00 14.18  ? 194 LEU   A CB  1 
ATOM   1624 C CG  . LEU   A 1 193 ? 47.346 27.247 10.127  1.00 14.43  ? 194 LEU   A CG  1 
ATOM   1625 C CD1 . LEU   A 1 193 ? 46.033 28.040 10.211  1.00 15.63  ? 194 LEU   A CD1 1 
ATOM   1626 C CD2 . LEU   A 1 193 ? 47.876 26.941 11.543  1.00 15.55  ? 194 LEU   A CD2 1 
ATOM   1627 N N   . GLY   A 1 194 ? 47.461 22.775 8.808   1.00 15.59  ? 195 GLY   A N   1 
ATOM   1628 C CA  . GLY   A 1 194 ? 46.903 21.702 8.003   1.00 16.13  ? 195 GLY   A CA  1 
ATOM   1629 C C   . GLY   A 1 194 ? 45.739 21.038 8.702   1.00 14.16  ? 195 GLY   A C   1 
ATOM   1630 O O   . GLY   A 1 194 ? 45.167 21.616 9.650   1.00 15.32  ? 195 GLY   A O   1 
ATOM   1631 N N   . LEU   A 1 195 ? 45.392 19.823 8.261   1.00 13.56  ? 196 LEU   A N   1 
ATOM   1632 C CA  . LEU   A 1 195 ? 44.298 19.082 8.861   1.00 13.45  ? 196 LEU   A CA  1 
ATOM   1633 C C   . LEU   A 1 195 ? 44.513 18.832 10.348  1.00 12.33  ? 196 LEU   A C   1 
ATOM   1634 O O   . LEU   A 1 195 ? 43.524 18.647 11.072  1.00 13.10  ? 196 LEU   A O   1 
ATOM   1635 C CB  . LEU   A 1 195 ? 44.177 17.740 8.152   1.00 13.59  ? 196 LEU   A CB  1 
ATOM   1636 C CG  . LEU   A 1 195 ? 43.997 17.771 6.616   1.00 14.82  ? 196 LEU   A CG  1 
ATOM   1637 C CD1 . LEU   A 1 195 ? 43.846 16.368 6.119   1.00 16.45  ? 196 LEU   A CD1 1 
ATOM   1638 C CD2 . LEU   A 1 195 ? 42.793 18.620 6.234   1.00 16.45  ? 196 LEU   A CD2 1 
ATOM   1639 N N   . GLU   A 1 196 ? 45.767 18.871 10.817  1.00 13.91  ? 197 GLU   A N   1 
ATOM   1640 C CA  . GLU   A 1 196 ? 46.055 18.571 12.217  1.00 13.04  ? 197 GLU   A CA  1 
ATOM   1641 C C   . GLU   A 1 196 ? 45.383 19.571 13.146  1.00 12.36  ? 197 GLU   A C   1 
ATOM   1642 O O   . GLU   A 1 196 ? 45.041 19.225 14.283  1.00 12.61  ? 197 GLU   A O   1 
ATOM   1643 C CB  . GLU   A 1 196 ? 47.566 18.512 12.484  1.00 14.40  ? 197 GLU   A CB  1 
ATOM   1644 C CG  . GLU   A 1 196 ? 48.341 17.615 11.534  1.00 16.64  ? 197 GLU   A CG  1 
ATOM   1645 C CD  . GLU   A 1 196 ? 48.798 18.276 10.249  1.00 23.74  ? 197 GLU   A CD  1 
ATOM   1646 O OE1 . GLU   A 1 196 ? 48.351 19.389 9.908   1.00 25.22  ? 197 GLU   A OE1 1 
ATOM   1647 O OE2 . GLU   A 1 196 ? 49.640 17.659 9.579   1.00 30.47  ? 197 GLU   A OE2 1 
ATOM   1648 N N   . ALA   A 1 197 ? 45.196 20.816 12.700  1.00 12.34  ? 198 ALA   A N   1 
ATOM   1649 C CA  . ALA   A 1 197 ? 44.572 21.813 13.570  1.00 11.82  ? 198 ALA   A CA  1 
ATOM   1650 C C   . ALA   A 1 197 ? 43.166 21.387 13.991  1.00 11.37  ? 198 ALA   A C   1 
ATOM   1651 O O   . ALA   A 1 197 ? 42.754 21.611 15.136  1.00 12.16  ? 198 ALA   A O   1 
ATOM   1652 C CB  . ALA   A 1 197 ? 44.542 23.175 12.863  1.00 14.00  ? 198 ALA   A CB  1 
ATOM   1653 N N   . ASP   A 1 198 ? 42.419 20.747 13.087  1.00 11.51  ? 199 ASP   A N   1 
ATOM   1654 C CA  . ASP   A 1 198 ? 41.073 20.278 13.424  1.00 11.29  ? 199 ASP   A CA  1 
ATOM   1655 C C   . ASP   A 1 198 ? 41.128 19.198 14.495  1.00 11.00  ? 199 ASP   A C   1 
ATOM   1656 O O   . ASP   A 1 198 ? 40.220 19.089 15.332  1.00 11.67  ? 199 ASP   A O   1 
ATOM   1657 C CB  . ASP   A 1 198 ? 40.380 19.699 12.188  1.00 11.89  ? 199 ASP   A CB  1 
ATOM   1658 C CG  . ASP   A 1 198 ? 39.902 20.734 11.223  1.00 12.38  ? 199 ASP   A CG  1 
ATOM   1659 O OD1 . ASP   A 1 198 ? 39.721 21.917 11.574  1.00 13.06  ? 199 ASP   A OD1 1 
ATOM   1660 O OD2 . ASP   A 1 198 ? 39.621 20.315 10.077  1.00 13.22  ? 199 ASP   A OD2 1 
ATOM   1661 N N   . MET   A 1 199 ? 42.156 18.353 14.452  1.00 10.60  ? 200 MET   A N   1 
ATOM   1662 C CA  . MET   A 1 199 ? 42.287 17.311 15.460  1.00 10.42  ? 200 MET   A CA  1 
ATOM   1663 C C   . MET   A 1 199 ? 42.502 17.876 16.860  1.00 10.62  ? 200 MET   A C   1 
ATOM   1664 O O   . MET   A 1 199 ? 41.944 17.342 17.837  1.00 11.51  ? 200 MET   A O   1 
ATOM   1665 C CB  . MET   A 1 199 ? 43.316 16.272 15.049  1.00 12.35  ? 200 MET   A CB  1 
ATOM   1666 C CG  . MET   A 1 199 ? 43.094 15.555 13.699  1.00 12.37  ? 200 MET   A CG  1 
ATOM   1667 S SD  . MET   A 1 199 ? 41.355 14.998 13.515  1.00 12.63  ? 200 MET   A SD  1 
ATOM   1668 C CE  . MET   A 1 199 ? 41.315 13.800 14.867  1.00 13.28  ? 200 MET   A CE  1 
ATOM   1669 N N   . TRP   A 1 200 ? 43.297 18.936 16.983  1.00 11.01  ? 201 TRP   A N   1 
ATOM   1670 C CA  . TRP   A 1 200 ? 43.422 19.622 18.266  1.00 11.67  ? 201 TRP   A CA  1 
ATOM   1671 C C   . TRP   A 1 200 ? 42.052 20.106 18.730  1.00 10.40  ? 201 TRP   A C   1 
ATOM   1672 O O   . TRP   A 1 200 ? 41.662 19.891 19.888  1.00 11.09  ? 201 TRP   A O   1 
ATOM   1673 C CB  . TRP   A 1 200 ? 44.415 20.772 18.118  1.00 12.29  ? 201 TRP   A CB  1 
ATOM   1674 C CG  . TRP   A 1 200 ? 44.473 21.669 19.303  1.00 11.95  ? 201 TRP   A CG  1 
ATOM   1675 C CD1 . TRP   A 1 200 ? 43.541 22.605 19.683  1.00 12.50  ? 201 TRP   A CD1 1 
ATOM   1676 C CD2 . TRP   A 1 200 ? 45.490 21.676 20.311  1.00 11.83  ? 201 TRP   A CD2 1 
ATOM   1677 N NE1 . TRP   A 1 200 ? 43.926 23.197 20.854  1.00 12.99  ? 201 TRP   A NE1 1 
ATOM   1678 C CE2 . TRP   A 1 200 ? 45.127 22.667 21.253  1.00 12.85  ? 201 TRP   A CE2 1 
ATOM   1679 C CE3 . TRP   A 1 200 ? 46.694 20.970 20.484  1.00 12.67  ? 201 TRP   A CE3 1 
ATOM   1680 C CZ2 . TRP   A 1 200 ? 45.921 22.973 22.368  1.00 13.82  ? 201 TRP   A CZ2 1 
ATOM   1681 C CZ3 . TRP   A 1 200 ? 47.489 21.268 21.606  1.00 13.94  ? 201 TRP   A CZ3 1 
ATOM   1682 C CH2 . TRP   A 1 200 ? 47.098 22.271 22.525  1.00 14.30  ? 201 TRP   A CH2 1 
ATOM   1683 N N   . SER   A 1 201 ? 41.293 20.753 17.837  1.00 10.92  ? 202 SER   A N   1 
ATOM   1684 C CA  . SER   A 1 201 ? 39.990 21.282 18.244  1.00 11.13  ? 202 SER   A CA  1 
ATOM   1685 C C   . SER   A 1 201 ? 39.063 20.180 18.720  1.00 10.82  ? 202 SER   A C   1 
ATOM   1686 O O   . SER   A 1 201 ? 38.282 20.389 19.655  1.00 11.81  ? 202 SER   A O   1 
ATOM   1687 C CB  . SER   A 1 201 ? 39.346 22.066 17.099  1.00 12.92  ? 202 SER   A CB  1 
ATOM   1688 O OG  . SER   A 1 201 ? 40.211 23.083 16.640  1.00 14.04  ? 202 SER   A OG  1 
ATOM   1689 N N   . ILE   A 1 202 ? 39.125 19.004 18.081  1.00 10.83  ? 203 ILE   A N   1 
ATOM   1690 C CA  . ILE   A 1 202 ? 38.345 17.861 18.546  1.00 11.63  ? 203 ILE   A CA  1 
ATOM   1691 C C   . ILE   A 1 202 ? 38.748 17.459 19.966  1.00 11.88  ? 203 ILE   A C   1 
ATOM   1692 O O   . ILE   A 1 202 ? 37.885 17.084 20.779  1.00 12.94  ? 203 ILE   A O   1 
ATOM   1693 C CB  . ILE   A 1 202 ? 38.435 16.696 17.542  1.00 12.74  ? 203 ILE   A CB  1 
ATOM   1694 C CG1 . ILE   A 1 202 ? 37.662 17.056 16.259  1.00 12.99  ? 203 ILE   A CG1 1 
ATOM   1695 C CG2 . ILE   A 1 202 ? 37.901 15.384 18.180  1.00 14.04  ? 203 ILE   A CG2 1 
ATOM   1696 C CD1 . ILE   A 1 202 ? 38.010 16.202 15.073  1.00 15.58  ? 203 ILE   A CD1 1 
ATOM   1697 N N   . GLY   A 1 203 ? 40.050 17.514 20.288  1.00 11.52  ? 204 GLY   A N   1 
ATOM   1698 C CA  . GLY   A 1 203 ? 40.474 17.272 21.668  1.00 12.06  ? 204 GLY   A CA  1 
ATOM   1699 C C   . GLY   A 1 203 ? 39.853 18.246 22.647  1.00 11.32  ? 204 GLY   A C   1 
ATOM   1700 O O   . GLY   A 1 203 ? 39.408 17.855 23.736  1.00 11.92  ? 204 GLY   A O   1 
ATOM   1701 N N   . VAL   A 1 204 ? 39.804 19.532 22.278  1.00 11.03  ? 205 VAL   A N   1 
ATOM   1702 C CA  . VAL   A 1 204 ? 39.198 20.533 23.150  1.00 11.30  ? 205 VAL   A CA  1 
ATOM   1703 C C   . VAL   A 1 204 ? 37.718 20.231 23.330  1.00 10.82  ? 205 VAL   A C   1 
ATOM   1704 O O   . VAL   A 1 204 ? 37.195 20.256 24.451  1.00 12.26  ? 205 VAL   A O   1 
ATOM   1705 C CB  . VAL   A 1 204 ? 39.436 21.952 22.592  1.00 11.05  ? 205 VAL   A CB  1 
ATOM   1706 C CG1 . VAL   A 1 204 ? 38.711 22.985 23.459  1.00 12.53  ? 205 VAL   A CG1 1 
ATOM   1707 C CG2 . VAL   A 1 204 ? 40.918 22.248 22.492  1.00 12.89  ? 205 VAL   A CG2 1 
ATOM   1708 N N   . ILE   A 1 205 ? 37.009 19.977 22.220  1.00 11.26  ? 206 ILE   A N   1 
ATOM   1709 C CA  . ILE   A 1 205 ? 35.587 19.655 22.284  1.00 11.99  ? 206 ILE   A CA  1 
ATOM   1710 C C   . ILE   A 1 205 ? 35.359 18.462 23.203  1.00 11.98  ? 206 ILE   A C   1 
ATOM   1711 O O   . ILE   A 1 205 ? 34.432 18.471 24.018  1.00 12.76  ? 206 ILE   A O   1 
ATOM   1712 C CB  . ILE   A 1 205 ? 35.025 19.412 20.867  1.00 12.46  ? 206 ILE   A CB  1 
ATOM   1713 C CG1 . ILE   A 1 205 ? 34.993 20.717 20.078  1.00 13.76  ? 206 ILE   A CG1 1 
ATOM   1714 C CG2 . ILE   A 1 205 ? 33.624 18.779 20.946  1.00 14.40  ? 206 ILE   A CG2 1 
ATOM   1715 C CD1 . ILE   A 1 205 ? 34.807 20.480 18.573  1.00 16.49  ? 206 ILE   A CD1 1 
ATOM   1716 N N   . THR   A 1 206 ? 36.175 17.413 23.068  1.00 11.52  ? 207 THR   A N   1 
ATOM   1717 C CA  . THR   A 1 206 ? 35.992 16.213 23.889  1.00 12.60  ? 207 THR   A CA  1 
ATOM   1718 C C   . THR   A 1 206 ? 36.163 16.532 25.378  1.00 12.16  ? 207 THR   A C   1 
ATOM   1719 O O   . THR   A 1 206 ? 35.363 16.092 26.219  1.00 13.04  ? 207 THR   A O   1 
ATOM   1720 C CB  . THR   A 1 206 ? 36.967 15.110 23.448  1.00 12.91  ? 207 THR   A CB  1 
ATOM   1721 O OG1 . THR   A 1 206 ? 36.759 14.840 22.060  1.00 13.82  ? 207 THR   A OG1 1 
ATOM   1722 C CG2 . THR   A 1 206 ? 36.703 13.824 24.229  1.00 14.39  ? 207 THR   A CG2 1 
ATOM   1723 N N   . TYR   A 1 207 ? 37.188 17.318 25.710  1.00 11.82  ? 208 TYR   A N   1 
ATOM   1724 C CA  . TYR   A 1 207 ? 37.386 17.742 27.090  1.00 12.39  ? 208 TYR   A CA  1 
ATOM   1725 C C   . TYR   A 1 207 ? 36.144 18.450 27.622  1.00 12.50  ? 208 TYR   A C   1 
ATOM   1726 O O   . TYR   A 1 207 ? 35.672 18.160 28.731  1.00 13.75  ? 208 TYR   A O   1 
ATOM   1727 C CB  . TYR   A 1 207 ? 38.645 18.609 27.144  1.00 12.22  ? 208 TYR   A CB  1 
ATOM   1728 C CG  . TYR   A 1 207 ? 39.084 19.042 28.529  1.00 13.11  ? 208 TYR   A CG  1 
ATOM   1729 C CD1 . TYR   A 1 207 ? 38.358 19.992 29.247  1.00 14.27  ? 208 TYR   A CD1 1 
ATOM   1730 C CD2 . TYR   A 1 207 ? 40.257 18.551 29.085  1.00 13.25  ? 208 TYR   A CD2 1 
ATOM   1731 C CE1 . TYR   A 1 207 ? 38.772 20.413 30.502  1.00 15.39  ? 208 TYR   A CE1 1 
ATOM   1732 C CE2 . TYR   A 1 207 ? 40.681 18.967 30.345  1.00 14.59  ? 208 TYR   A CE2 1 
ATOM   1733 C CZ  . TYR   A 1 207 ? 39.937 19.910 31.036  1.00 15.57  ? 208 TYR   A CZ  1 
ATOM   1734 O OH  . TYR   A 1 207 ? 40.338 20.345 32.290  1.00 18.30  ? 208 TYR   A OH  1 
ATOM   1735 N N   . ILE   A 1 208 ? 35.589 19.374 26.839  1.00 12.36  ? 209 ILE   A N   1 
ATOM   1736 C CA  . ILE   A 1 208 ? 34.408 20.131 27.261  1.00 13.07  ? 209 ILE   A CA  1 
ATOM   1737 C C   . ILE   A 1 208 ? 33.203 19.220 27.414  1.00 14.66  ? 209 ILE   A C   1 
ATOM   1738 O O   . ILE   A 1 208 ? 32.448 19.329 28.386  1.00 15.44  ? 209 ILE   A O   1 
ATOM   1739 C CB  . ILE   A 1 208 ? 34.121 21.265 26.256  1.00 14.43  ? 209 ILE   A CB  1 
ATOM   1740 C CG1 . ILE   A 1 208 ? 35.212 22.328 26.311  1.00 15.60  ? 209 ILE   A CG1 1 
ATOM   1741 C CG2 . ILE   A 1 208 ? 32.712 21.846 26.458  1.00 18.58  ? 209 ILE   A CG2 1 
ATOM   1742 C CD1 . ILE   A 1 208 ? 35.135 23.302 25.170  1.00 16.96  ? 209 ILE   A CD1 1 
ATOM   1743 N N   . LEU   A 1 209 ? 33.005 18.298 26.471  1.00 14.03  ? 210 LEU   A N   1 
ATOM   1744 C CA  . LEU   A 1 209 ? 31.847 17.410 26.557  1.00 15.17  ? 210 LEU   A CA  1 
ATOM   1745 C C   . LEU   A 1 209 ? 31.851 16.630 27.862  1.00 15.92  ? 210 LEU   A C   1 
ATOM   1746 O O   . LEU   A 1 209 ? 30.796 16.445 28.482  1.00 17.52  ? 210 LEU   A O   1 
ATOM   1747 C CB  . LEU   A 1 209 ? 31.844 16.420 25.393  1.00 17.37  ? 210 LEU   A CB  1 
ATOM   1748 C CG  . LEU   A 1 209 ? 31.586 17.002 24.012  1.00 18.98  ? 210 LEU   A CG  1 
ATOM   1749 C CD1 . LEU   A 1 209 ? 31.582 15.898 22.990  1.00 22.36  ? 210 LEU   A CD1 1 
ATOM   1750 C CD2 . LEU   A 1 209 ? 30.276 17.729 23.983  1.00 22.40  ? 210 LEU   A CD2 1 
ATOM   1751 N N   . LEU   A 1 210 ? 33.034 16.168 28.300  1.00 14.81  ? 211 LEU   A N   1 
ATOM   1752 C CA  . LEU   A 1 210 ? 33.114 15.305 29.470  1.00 15.22  ? 211 LEU   A CA  1 
ATOM   1753 C C   . LEU   A 1 210 ? 33.090 16.072 30.782  1.00 16.74  ? 211 LEU   A C   1 
ATOM   1754 O O   . LEU   A 1 210 ? 32.718 15.506 31.816  1.00 18.22  ? 211 LEU   A O   1 
ATOM   1755 C CB  . LEU   A 1 210 ? 34.384 14.471 29.399  1.00 15.96  ? 211 LEU   A CB  1 
ATOM   1756 C CG  . LEU   A 1 210 ? 34.427 13.450 28.258  1.00 16.36  ? 211 LEU   A CG  1 
ATOM   1757 C CD1 . LEU   A 1 210 ? 35.771 12.750 28.189  1.00 18.12  ? 211 LEU   A CD1 1 
ATOM   1758 C CD2 . LEU   A 1 210 ? 33.296 12.446 28.415  1.00 18.66  ? 211 LEU   A CD2 1 
ATOM   1759 N N   . SER   A 1 211 ? 33.470 17.337 30.779  1.00 17.23  ? 212 SER   A N   1 
ATOM   1760 C CA  . SER   A 1 211 ? 33.671 18.070 32.019  1.00 18.14  ? 212 SER   A CA  1 
ATOM   1761 C C   . SER   A 1 211 ? 32.787 19.290 32.172  1.00 17.45  ? 212 SER   A C   1 
ATOM   1762 O O   . SER   A 1 211 ? 32.583 19.741 33.310  1.00 19.14  ? 212 SER   A O   1 
ATOM   1763 C CB  . SER   A 1 211 ? 35.135 18.523 32.129  1.00 17.79  ? 212 SER   A CB  1 
ATOM   1764 O OG  . SER   A 1 211 ? 35.408 19.536 31.169  1.00 16.66  ? 212 SER   A OG  1 
ATOM   1765 N N   . GLY   A 1 212 ? 32.276 19.850 31.079  1.00 16.24  ? 213 GLY   A N   1 
ATOM   1766 C CA  . GLY   A 1 212 ? 31.639 21.148 31.145  1.00 18.55  ? 213 GLY   A CA  1 
ATOM   1767 C C   . GLY   A 1 212 ? 32.585 22.310 31.297  1.00 18.25  ? 213 GLY   A C   1 
ATOM   1768 O O   . GLY   A 1 212 ? 32.126 23.440 31.485  1.00 22.23  ? 213 GLY   A O   1 
ATOM   1769 N N   . ALA   A 1 213 ? 33.885 22.074 31.239  1.00 16.81  ? 214 ALA   A N   1 
ATOM   1770 C CA  . ALA   A 1 213 ? 34.896 23.099 31.433  1.00 17.15  ? 214 ALA   A CA  1 
ATOM   1771 C C   . ALA   A 1 213 ? 35.796 23.153 30.210  1.00 16.46  ? 214 ALA   A C   1 
ATOM   1772 O O   . ALA   A 1 213 ? 36.004 22.146 29.517  1.00 17.17  ? 214 ALA   A O   1 
ATOM   1773 C CB  . ALA   A 1 213 ? 35.767 22.789 32.665  1.00 19.52  ? 214 ALA   A CB  1 
ATOM   1774 N N   . SER   A 1 214 ? 36.330 24.325 29.964  1.00 17.26  ? 215 SER   A N   1 
ATOM   1775 C CA  . SER   A 1 214 ? 37.180 24.569 28.800  1.00 16.95  ? 215 SER   A CA  1 
ATOM   1776 C C   . SER   A 1 214 ? 38.650 24.460 29.207  1.00 17.49  ? 215 SER   A C   1 
ATOM   1777 O O   . SER   A 1 214 ? 39.070 25.119 30.167  1.00 20.29  ? 215 SER   A O   1 
ATOM   1778 C CB  . SER   A 1 214 ? 36.867 25.970 28.299  1.00 19.09  ? 215 SER   A CB  1 
ATOM   1779 O OG  . SER   A 1 214 ? 37.560 26.264 27.111  1.00 20.53  ? 215 SER   A OG  1 
ATOM   1780 N N   . PRO   A 1 215 ? 39.472 23.654 28.516  1.00 15.40  ? 216 PRO   A N   1 
ATOM   1781 C CA  . PRO   A 1 215 ? 40.792 23.285 29.071  1.00 15.29  ? 216 PRO   A CA  1 
ATOM   1782 C C   . PRO   A 1 215 ? 41.802 24.415 29.133  1.00 13.28  ? 216 PRO   A C   1 
ATOM   1783 O O   . PRO   A 1 215 ? 42.668 24.393 30.020  1.00 14.82  ? 216 PRO   A O   1 
ATOM   1784 C CB  . PRO   A 1 215 ? 41.270 22.145 28.157  1.00 15.40  ? 216 PRO   A CB  1 
ATOM   1785 C CG  . PRO   A 1 215 ? 40.468 22.337 26.855  1.00 15.84  ? 216 PRO   A CG  1 
ATOM   1786 C CD  . PRO   A 1 215 ? 39.112 22.855 27.338  1.00 14.95  ? 216 PRO   A CD  1 
ATOM   1787 N N   . PHE   A 1 216 ? 41.750 25.393 28.219  1.00 13.51  ? 217 PHE   A N   1 
ATOM   1788 C CA  . PHE   A 1 216 ? 42.763 26.445 28.144  1.00 13.12  ? 217 PHE   A CA  1 
ATOM   1789 C C   . PHE   A 1 216 ? 42.229 27.818 28.503  1.00 13.21  ? 217 PHE   A C   1 
ATOM   1790 O O   . PHE   A 1 216 ? 42.982 28.794 28.432  1.00 14.27  ? 217 PHE   A O   1 
ATOM   1791 C CB  . PHE   A 1 216 ? 43.369 26.490 26.732  1.00 14.61  ? 217 PHE   A CB  1 
ATOM   1792 C CG  . PHE   A 1 216 ? 43.992 25.189 26.342  1.00 12.90  ? 217 PHE   A CG  1 
ATOM   1793 C CD1 . PHE   A 1 216 ? 45.199 24.800 26.901  1.00 14.28  ? 217 PHE   A CD1 1 
ATOM   1794 C CD2 . PHE   A 1 216 ? 43.356 24.320 25.460  1.00 14.04  ? 217 PHE   A CD2 1 
ATOM   1795 C CE1 . PHE   A 1 216 ? 45.771 23.573 26.575  1.00 14.93  ? 217 PHE   A CE1 1 
ATOM   1796 C CE2 . PHE   A 1 216 ? 43.902 23.113 25.128  1.00 14.32  ? 217 PHE   A CE2 1 
ATOM   1797 C CZ  . PHE   A 1 216 ? 45.128 22.725 25.682  1.00 14.01  ? 217 PHE   A CZ  1 
ATOM   1798 N N   . LEU   A 1 217 ? 40.950 27.928 28.843  1.00 14.54  ? 218 LEU   A N   1 
ATOM   1799 C CA  . LEU   A 1 217 ? 40.313 29.237 28.946  1.00 15.85  ? 218 LEU   A CA  1 
ATOM   1800 C C   . LEU   A 1 217 ? 40.903 30.053 30.088  1.00 16.30  ? 218 LEU   A C   1 
ATOM   1801 O O   . LEU   A 1 217 ? 40.906 29.604 31.229  1.00 18.65  ? 218 LEU   A O   1 
ATOM   1802 C CB  . LEU   A 1 217 ? 38.813 29.053 29.155  1.00 17.68  ? 218 LEU   A CB  1 
ATOM   1803 C CG  . LEU   A 1 217 ? 38.013 30.350 29.376  1.00 20.76  ? 218 LEU   A CG  1 
ATOM   1804 C CD1 . LEU   A 1 217 ? 38.047 31.261 28.166  1.00 23.19  ? 218 LEU   A CD1 1 
ATOM   1805 C CD2 . LEU   A 1 217 ? 36.565 29.993 29.755  1.00 23.72  ? 218 LEU   A CD2 1 
ATOM   1806 N N   . GLY   A 1 218 ? 41.380 31.258 29.773  1.00 16.23  ? 219 GLY   A N   1 
ATOM   1807 C CA  . GLY   A 1 218 ? 41.826 32.215 30.756  1.00 18.88  ? 219 GLY   A CA  1 
ATOM   1808 C C   . GLY   A 1 218 ? 40.834 33.351 30.912  1.00 20.56  ? 219 GLY   A C   1 
ATOM   1809 O O   . GLY   A 1 218 ? 39.728 33.328 30.371  1.00 22.15  ? 219 GLY   A O   1 
ATOM   1810 N N   . ASP   A 1 219 ? 41.239 34.385 31.644  1.00 22.96  ? 220 ASP   A N   1 
ATOM   1811 C CA  . ASP   A 1 219 ? 40.294 35.504 31.918  1.00 25.37  ? 220 ASP   A CA  1 
ATOM   1812 C C   . ASP   A 1 219 ? 40.283 36.506 30.768  1.00 23.07  ? 220 ASP   A C   1 
ATOM   1813 O O   . ASP   A 1 219 ? 39.376 37.339 30.734  1.00 25.02  ? 220 ASP   A O   1 
ATOM   1814 C CB  . ASP   A 1 219 ? 40.632 36.208 33.216  1.00 32.69  ? 220 ASP   A CB  1 
ATOM   1815 C CG  . ASP   A 1 219 ? 40.324 35.405 34.465  1.00 41.11  ? 220 ASP   A CG  1 
ATOM   1816 O OD1 . ASP   A 1 219 ? 39.268 34.743 34.483  1.00 44.46  ? 220 ASP   A OD1 1 
ATOM   1817 O OD2 . ASP   A 1 219 ? 41.148 35.453 35.393  1.00 46.23  ? 220 ASP   A OD2 1 
ATOM   1818 N N   . THR   A 1 220 ? 41.243 36.399 29.862  1.00 19.21  ? 221 THR   A N   1 
ATOM   1819 C CA  . THR   A 1 220 ? 41.314 37.276 28.701  1.00 17.68  ? 221 THR   A CA  1 
ATOM   1820 C C   . THR   A 1 220 ? 41.719 36.427 27.513  1.00 16.81  ? 221 THR   A C   1 
ATOM   1821 O O   . THR   A 1 220 ? 42.256 35.326 27.674  1.00 16.62  ? 221 THR   A O   1 
ATOM   1822 C CB  . THR   A 1 220 ? 42.379 38.368 28.891  1.00 18.06  ? 221 THR   A CB  1 
ATOM   1823 O OG1 . THR   A 1 220 ? 43.681 37.760 29.017  1.00 19.00  ? 221 THR   A OG1 1 
ATOM   1824 C CG2 . THR   A 1 220 ? 42.077 39.203 30.113  1.00 21.84  ? 221 THR   A CG2 1 
ATOM   1825 N N   . LYS   A 1 221 ? 41.504 36.973 26.310  1.00 17.62  ? 222 LYS   A N   1 
ATOM   1826 C CA  . LYS   A 1 221 ? 41.896 36.245 25.100  1.00 16.93  ? 222 LYS   A CA  1 
ATOM   1827 C C   . LYS   A 1 221 ? 43.395 35.970 25.096  1.00 16.32  ? 222 LYS   A C   1 
ATOM   1828 O O   . LYS   A 1 221 ? 43.825 34.877 24.713  1.00 16.05  ? 222 LYS   A O   1 
ATOM   1829 C CB  . LYS   A 1 221 ? 41.524 37.062 23.867  1.00 21.18  ? 222 LYS   A CB  1 
ATOM   1830 C CG  . LYS   A 1 221 ? 40.060 36.963 23.507  1.00 25.75  ? 222 LYS   A CG  1 
ATOM   1831 C CD  . LYS   A 1 221 ? 39.758 37.810 22.276  1.00 29.50  ? 222 LYS   A CD  1 
ATOM   1832 C CE  . LYS   A 1 221 ? 38.273 37.801 21.955  1.00 33.90  ? 222 LYS   A CE  1 
ATOM   1833 N NZ  . LYS   A 1 221 ? 37.986 38.479 20.663  1.00 36.91  ? 222 LYS   A NZ  1 
ATOM   1834 N N   . GLN   A 1 222 ? 44.210 36.956 25.501  1.00 16.51  ? 223 GLN   A N   1 
ATOM   1835 C CA  . GLN   A 1 222 ? 45.664 36.751 25.477  1.00 17.08  ? 223 GLN   A CA  1 
ATOM   1836 C C   . GLN   A 1 222 ? 46.081 35.632 26.426  1.00 16.86  ? 223 GLN   A C   1 
ATOM   1837 O O   . GLN   A 1 222 ? 46.983 34.850 26.112  1.00 17.40  ? 223 GLN   A O   1 
ATOM   1838 C CB  . GLN   A 1 222 ? 46.416 38.063 25.775  1.00 19.43  ? 223 GLN   A CB  1 
ATOM   1839 C CG  . GLN   A 1 222 ? 46.116 38.588 27.186  1.00 19.91  ? 223 GLN   A CG  1 
ATOM   1840 C CD  . GLN   A 1 222 ? 45.112 39.732 27.181  1.00 20.06  ? 223 GLN   A CD  1 
ATOM   1841 O OE1 . GLN   A 1 222 ? 44.131 39.679 26.432  1.00 19.89  ? 223 GLN   A OE1 1 
ATOM   1842 N NE2 . GLN   A 1 222 ? 45.207 40.614 28.181  1.00 20.17  ? 223 GLN   A NE2 1 
ATOM   1843 N N   . GLU   A 1 223 ? 45.430 35.528 27.584  1.00 16.37  ? 224 GLU   A N   1 
ATOM   1844 C CA  A GLU   A 1 223 ? 45.748 34.441 28.501  0.52 16.42  ? 224 GLU   A CA  1 
ATOM   1845 C CA  B GLU   A 1 223 ? 45.746 34.437 28.503  0.48 15.83  ? 224 GLU   A CA  1 
ATOM   1846 C C   . GLU   A 1 223 ? 45.365 33.090 27.905  1.00 15.72  ? 224 GLU   A C   1 
ATOM   1847 O O   . GLU   A 1 223 ? 46.135 32.132 27.988  1.00 15.53  ? 224 GLU   A O   1 
ATOM   1848 C CB  A GLU   A 1 223 ? 45.054 34.696 29.835  0.52 19.80  ? 224 GLU   A CB  1 
ATOM   1849 C CB  B GLU   A 1 223 ? 45.048 34.643 29.849  0.48 17.99  ? 224 GLU   A CB  1 
ATOM   1850 C CG  A GLU   A 1 223 ? 45.622 33.945 31.000  0.52 24.57  ? 224 GLU   A CG  1 
ATOM   1851 C CG  B GLU   A 1 223 ? 45.670 35.698 30.744  0.48 21.76  ? 224 GLU   A CG  1 
ATOM   1852 C CD  A GLU   A 1 223 ? 45.068 34.466 32.328  0.52 26.81  ? 224 GLU   A CD  1 
ATOM   1853 C CD  B GLU   A 1 223 ? 44.876 35.899 32.027  0.48 27.12  ? 224 GLU   A CD  1 
ATOM   1854 O OE1 A GLU   A 1 223 ? 45.443 35.593 32.767  0.52 26.66  ? 224 GLU   A OE1 1 
ATOM   1855 O OE1 B GLU   A 1 223 ? 43.913 35.136 32.264  0.48 29.68  ? 224 GLU   A OE1 1 
ATOM   1856 O OE2 A GLU   A 1 223 ? 44.206 33.771 32.912  0.52 29.18  ? 224 GLU   A OE2 1 
ATOM   1857 O OE2 B GLU   A 1 223 ? 45.218 36.800 32.811  0.48 30.30  ? 224 GLU   A OE2 1 
ATOM   1858 N N   . THR   A 1 224 ? 44.182 32.999 27.290  1.00 14.28  ? 225 THR   A N   1 
ATOM   1859 C CA  . THR   A 1 224 ? 43.786 31.749 26.642  1.00 13.98  ? 225 THR   A CA  1 
ATOM   1860 C C   . THR   A 1 224 ? 44.807 31.342 25.590  1.00 13.81  ? 225 THR   A C   1 
ATOM   1861 O O   . THR   A 1 224 ? 45.223 30.178 25.526  1.00 14.42  ? 225 THR   A O   1 
ATOM   1862 C CB  . THR   A 1 224 ? 42.408 31.923 26.004  1.00 13.85  ? 225 THR   A CB  1 
ATOM   1863 O OG1 . THR   A 1 224 ? 41.469 32.227 27.040  1.00 14.97  ? 225 THR   A OG1 1 
ATOM   1864 C CG2 . THR   A 1 224 ? 41.987 30.641 25.299  1.00 15.50  ? 225 THR   A CG2 1 
ATOM   1865 N N   . LEU   A 1 225 ? 45.216 32.298 24.750  1.00 13.90  ? 226 LEU   A N   1 
ATOM   1866 C CA  . LEU   A 1 225 ? 46.140 31.992 23.663  1.00 14.40  ? 226 LEU   A CA  1 
ATOM   1867 C C   . LEU   A 1 225 ? 47.498 31.568 24.196  1.00 14.63  ? 226 LEU   A C   1 
ATOM   1868 O O   . LEU   A 1 225 ? 48.113 30.631 23.672  1.00 15.40  ? 226 LEU   A O   1 
ATOM   1869 C CB  . LEU   A 1 225 ? 46.272 33.217 22.752  1.00 15.41  ? 226 LEU   A CB  1 
ATOM   1870 C CG  . LEU   A 1 225 ? 44.995 33.604 21.993  1.00 15.81  ? 226 LEU   A CG  1 
ATOM   1871 C CD1 . LEU   A 1 225 ? 45.156 34.951 21.308  1.00 17.73  ? 226 LEU   A CD1 1 
ATOM   1872 C CD2 . LEU   A 1 225 ? 44.606 32.553 20.960  1.00 17.93  ? 226 LEU   A CD2 1 
ATOM   1873 N N   . ALA   A 1 226 ? 47.974 32.233 25.253  1.00 15.02  ? 227 ALA   A N   1 
ATOM   1874 C CA  . ALA   A 1 226 ? 49.219 31.807 25.881  1.00 16.12  ? 227 ALA   A CA  1 
ATOM   1875 C C   . ALA   A 1 226 ? 49.084 30.410 26.475  1.00 15.37  ? 227 ALA   A C   1 
ATOM   1876 O O   . ALA   A 1 226 ? 50.015 29.601 26.386  1.00 17.17  ? 227 ALA   A O   1 
ATOM   1877 C CB  . ALA   A 1 226 ? 49.641 32.817 26.947  1.00 18.60  ? 227 ALA   A CB  1 
ATOM   1878 N N   . ASN   A 1 227 ? 47.923 30.096 27.057  1.00 14.24  ? 228 ASN   A N   1 
ATOM   1879 C CA  . ASN   A 1 227 ? 47.700 28.760 27.607  1.00 14.36  ? 228 ASN   A CA  1 
ATOM   1880 C C   . ASN   A 1 227 ? 47.714 27.701 26.511  1.00 14.23  ? 228 ASN   A C   1 
ATOM   1881 O O   . ASN   A 1 227 ? 48.315 26.628 26.676  1.00 14.86  ? 228 ASN   A O   1 
ATOM   1882 C CB  . ASN   A 1 227 ? 46.359 28.705 28.345  1.00 14.03  ? 228 ASN   A CB  1 
ATOM   1883 C CG  . ASN   A 1 227 ? 46.375 29.441 29.655  1.00 15.54  ? 228 ASN   A CG  1 
ATOM   1884 O OD1 . ASN   A 1 227 ? 47.437 29.702 30.228  1.00 18.27  ? 228 ASN   A OD1 1 
ATOM   1885 N ND2 . ASN   A 1 227 ? 45.182 29.763 30.156  1.00 16.53  ? 228 ASN   A ND2 1 
ATOM   1886 N N   . VAL   A 1 228 ? 47.071 27.990 25.372  1.00 13.28  ? 229 VAL   A N   1 
ATOM   1887 C CA  . VAL   A 1 228 ? 47.082 27.042 24.254  1.00 13.38  ? 229 VAL   A CA  1 
ATOM   1888 C C   . VAL   A 1 228 ? 48.518 26.797 23.800  1.00 14.16  ? 229 VAL   A C   1 
ATOM   1889 O O   . VAL   A 1 228 ? 48.958 25.655 23.621  1.00 15.00  ? 229 VAL   A O   1 
ATOM   1890 C CB  . VAL   A 1 228 ? 46.235 27.601 23.095  1.00 13.54  ? 229 VAL   A CB  1 
ATOM   1891 C CG1 . VAL   A 1 228 ? 46.494 26.815 21.803  1.00 14.28  ? 229 VAL   A CG1 1 
ATOM   1892 C CG2 . VAL   A 1 228 ? 44.748 27.609 23.441  1.00 13.55  ? 229 VAL   A CG2 1 
ATOM   1893 N N   . SER   A 1 229 ? 49.274 27.873 23.615  1.00 14.08  ? 230 SER   A N   1 
ATOM   1894 C CA  . SER   A 1 229 ? 50.624 27.723 23.083  1.00 15.66  ? 230 SER   A CA  1 
ATOM   1895 C C   . SER   A 1 229 ? 51.517 26.896 24.011  1.00 16.16  ? 230 SER   A C   1 
ATOM   1896 O O   . SER   A 1 229 ? 52.382 26.141 23.541  1.00 17.71  ? 230 SER   A O   1 
ATOM   1897 C CB  . SER   A 1 229 ? 51.220 29.098 22.794  1.00 16.80  ? 230 SER   A CB  1 
ATOM   1898 O OG  . SER   A 1 229 ? 52.468 28.967 22.116  1.00 18.31  ? 230 SER   A OG  1 
ATOM   1899 N N   . ALA   A 1 230 ? 51.316 27.013 25.327  1.00 16.09  ? 231 ALA   A N   1 
ATOM   1900 C CA  . ALA   A 1 230 ? 52.066 26.269 26.334  1.00 17.26  ? 231 ALA   A CA  1 
ATOM   1901 C C   . ALA   A 1 230 ? 51.486 24.889 26.631  1.00 17.57  ? 231 ALA   A C   1 
ATOM   1902 O O   . ALA   A 1 230 ? 52.041 24.165 27.464  1.00 20.43  ? 231 ALA   A O   1 
ATOM   1903 C CB  . ALA   A 1 230 ? 52.118 27.090 27.627  1.00 19.77  ? 231 ALA   A CB  1 
ATOM   1904 N N   . VAL   A 1 231 ? 50.359 24.542 26.009  1.00 16.01  ? 232 VAL   A N   1 
ATOM   1905 C CA  . VAL   A 1 231 ? 49.640 23.268 26.324  1.00 16.54  ? 232 VAL   A CA  1 
ATOM   1906 C C   . VAL   A 1 231 ? 49.376 23.261 27.843  1.00 16.97  ? 232 VAL   A C   1 
ATOM   1907 O O   . VAL   A 1 231 ? 49.619 22.250 28.500  1.00 18.09  ? 232 VAL   A O   1 
ATOM   1908 C CB  . VAL   A 1 231 ? 50.326 21.997 25.781  1.00 17.96  ? 232 VAL   A CB  1 
ATOM   1909 C CG1 . VAL   A 1 231 ? 49.352 20.826 25.721  1.00 18.60  ? 232 VAL   A CG1 1 
ATOM   1910 C CG2 . VAL   A 1 231 ? 50.893 22.246 24.391  1.00 18.89  ? 232 VAL   A CG2 1 
ATOM   1911 N N   . ASN   A 1 232 ? 48.828 24.372 28.322  1.00 15.96  ? 233 ASN   A N   1 
ATOM   1912 C CA  . ASN   A 1 232 ? 48.540 24.550 29.770  1.00 16.32  ? 233 ASN   A CA  1 
ATOM   1913 C C   . ASN   A 1 232 ? 47.131 24.057 30.089  1.00 15.93  ? 233 ASN   A C   1 
ATOM   1914 O O   . ASN   A 1 232 ? 46.208 24.859 30.151  1.00 17.17  ? 233 ASN   A O   1 
ATOM   1915 C CB  . ASN   A 1 232 ? 48.773 26.009 30.139  1.00 17.39  ? 233 ASN   A CB  1 
ATOM   1916 C CG  . ASN   A 1 232 ? 48.701 26.307 31.619  1.00 18.09  ? 233 ASN   A CG  1 
ATOM   1917 O OD1 . ASN   A 1 232 ? 49.730 26.564 32.248  1.00 21.29  ? 233 ASN   A OD1 1 
ATOM   1918 N ND2 . ASN   A 1 232 ? 47.506 26.307 32.188  1.00 18.43  ? 233 ASN   A ND2 1 
ATOM   1919 N N   . TYR   A 1 233 ? 46.999 22.748 30.233  1.00 15.14  ? 234 TYR   A N   1 
ATOM   1920 C CA  . TYR   A 1 233 ? 45.711 22.164 30.663  1.00 15.89  ? 234 TYR   A CA  1 
ATOM   1921 C C   . TYR   A 1 233 ? 45.981 20.976 31.580  1.00 16.99  ? 234 TYR   A C   1 
ATOM   1922 O O   . TYR   A 1 233 ? 47.062 20.391 31.559  1.00 17.61  ? 234 TYR   A O   1 
ATOM   1923 C CB  . TYR   A 1 233 ? 44.859 21.707 29.472  1.00 16.12  ? 234 TYR   A CB  1 
ATOM   1924 C CG  . TYR   A 1 233 ? 45.192 20.315 28.957  1.00 15.33  ? 234 TYR   A CG  1 
ATOM   1925 C CD1 . TYR   A 1 233 ? 46.272 20.113 28.110  1.00 15.25  ? 234 TYR   A CD1 1 
ATOM   1926 C CD2 . TYR   A 1 233 ? 44.427 19.212 29.312  1.00 16.64  ? 234 TYR   A CD2 1 
ATOM   1927 C CE1 . TYR   A 1 233 ? 46.595 18.852 27.642  1.00 16.11  ? 234 TYR   A CE1 1 
ATOM   1928 C CE2 . TYR   A 1 233 ? 44.738 17.946 28.849  1.00 17.88  ? 234 TYR   A CE2 1 
ATOM   1929 C CZ  . TYR   A 1 233 ? 45.823 17.768 28.012  1.00 15.86  ? 234 TYR   A CZ  1 
ATOM   1930 O OH  . TYR   A 1 233 ? 46.143 16.530 27.550  1.00 20.12  ? 234 TYR   A OH  1 
ATOM   1931 N N   . GLU   A 1 234 ? 44.983 20.648 32.387  1.00 16.13  ? 235 GLU   A N   1 
ATOM   1932 C CA  . GLU   A 1 234 ? 45.079 19.427 33.180  1.00 18.85  ? 235 GLU   A CA  1 
ATOM   1933 C C   . GLU   A 1 234 ? 43.697 18.807 33.351  1.00 16.51  ? 235 GLU   A C   1 
ATOM   1934 O O   . GLU   A 1 234 ? 42.672 19.487 33.238  1.00 17.26  ? 235 GLU   A O   1 
ATOM   1935 C CB  . GLU   A 1 234 ? 45.762 19.621 34.528  1.00 25.21  ? 235 GLU   A CB  1 
ATOM   1936 C CG  . GLU   A 1 234 ? 45.202 20.718 35.353  1.00 30.18  ? 235 GLU   A CG  1 
ATOM   1937 C CD  . GLU   A 1 234 ? 46.065 21.031 36.572  1.00 34.67  ? 235 GLU   A CD  1 
ATOM   1938 O OE1 . GLU   A 1 234 ? 47.259 20.657 36.581  1.00 38.84  ? 235 GLU   A OE1 1 
ATOM   1939 O OE2 . GLU   A 1 234 ? 45.574 21.710 37.497  1.00 36.48  ? 235 GLU   A OE2 1 
ATOM   1940 N N   . PHE   A 1 235 ? 43.668 17.504 33.650  1.00 16.62  ? 236 PHE   A N   1 
ATOM   1941 C CA  . PHE   A 1 235 ? 42.399 16.805 33.921  1.00 16.30  ? 236 PHE   A CA  1 
ATOM   1942 C C   . PHE   A 1 235 ? 42.060 16.980 35.398  1.00 18.56  ? 236 PHE   A C   1 
ATOM   1943 O O   . PHE   A 1 235 ? 42.386 16.134 36.240  1.00 21.02  ? 236 PHE   A O   1 
ATOM   1944 C CB  . PHE   A 1 235 ? 42.527 15.324 33.614  1.00 16.71  ? 236 PHE   A CB  1 
ATOM   1945 C CG  . PHE   A 1 235 ? 42.764 15.025 32.159  1.00 15.48  ? 236 PHE   A CG  1 
ATOM   1946 C CD1 . PHE   A 1 235 ? 41.772 15.269 31.216  1.00 16.04  ? 236 PHE   A CD1 1 
ATOM   1947 C CD2 . PHE   A 1 235 ? 43.964 14.489 31.729  1.00 17.63  ? 236 PHE   A CD2 1 
ATOM   1948 C CE1 . PHE   A 1 235 ? 41.983 14.981 29.871  1.00 16.49  ? 236 PHE   A CE1 1 
ATOM   1949 C CE2 . PHE   A 1 235 ? 44.173 14.196 30.389  1.00 18.47  ? 236 PHE   A CE2 1 
ATOM   1950 C CZ  . PHE   A 1 235 ? 43.186 14.450 29.462  1.00 17.44  ? 236 PHE   A CZ  1 
ATOM   1951 N N   . GLU   A 1 236 ? 41.386 18.075 35.723  1.00 17.88  ? 237 GLU   A N   1 
ATOM   1952 C CA  . GLU   A 1 236 ? 41.030 18.373 37.116  1.00 17.41  ? 237 GLU   A CA  1 
ATOM   1953 C C   . GLU   A 1 236 ? 40.221 17.245 37.731  1.00 17.08  ? 237 GLU   A C   1 
ATOM   1954 O O   . GLU   A 1 236 ? 39.221 16.790 37.163  1.00 17.71  ? 237 GLU   A O   1 
ATOM   1955 C CB  . GLU   A 1 236 ? 40.203 19.656 37.173  1.00 20.38  ? 237 GLU   A CB  1 
ATOM   1956 C CG  . GLU   A 1 236 ? 40.912 20.901 36.686  1.00 22.03  ? 237 GLU   A CG  1 
ATOM   1957 C CD  . GLU   A 1 236 ? 42.148 21.226 37.478  1.00 22.48  ? 237 GLU   A CD  1 
ATOM   1958 O OE1 . GLU   A 1 236 ? 42.293 20.755 38.630  1.00 24.54  ? 237 GLU   A OE1 1 
ATOM   1959 O OE2 . GLU   A 1 236 ? 43.006 21.947 36.933  1.00 24.06  ? 237 GLU   A OE2 1 
ATOM   1960 N N   . ASP   A 1 237 ? 40.660 16.789 38.910  1.00 18.72  ? 238 ASP   A N   1 
ATOM   1961 C CA  . ASP   A 1 237 ? 39.996 15.657 39.553  1.00 19.03  ? 238 ASP   A CA  1 
ATOM   1962 C C   . ASP   A 1 237 ? 38.517 15.939 39.803  1.00 18.24  ? 238 ASP   A C   1 
ATOM   1963 O O   . ASP   A 1 237 ? 37.685 15.028 39.734  1.00 20.23  ? 238 ASP   A O   1 
ATOM   1964 C CB  . ASP   A 1 237 ? 40.697 15.338 40.876  1.00 22.99  ? 238 ASP   A CB  1 
ATOM   1965 C CG  . ASP   A 1 237 ? 41.934 14.495 40.686  1.00 30.19  ? 238 ASP   A CG  1 
ATOM   1966 O OD1 . ASP   A 1 237 ? 42.793 14.481 41.592  1.00 33.80  ? 238 ASP   A OD1 1 
ATOM   1967 O OD2 . ASP   A 1 237 ? 42.042 13.837 39.637  1.00 33.07  ? 238 ASP   A OD2 1 
ATOM   1968 N N   . GLU   A 1 238 ? 38.172 17.185 40.134  1.00 16.76  ? 239 GLU   A N   1 
ATOM   1969 C CA  . GLU   A 1 238 ? 36.774 17.504 40.406  1.00 19.02  ? 239 GLU   A CA  1 
ATOM   1970 C C   . GLU   A 1 238 ? 35.878 17.164 39.223  1.00 19.45  ? 239 GLU   A C   1 
ATOM   1971 O O   . GLU   A 1 238 ? 34.717 16.778 39.418  1.00 21.72  ? 239 GLU   A O   1 
ATOM   1972 C CB  . GLU   A 1 238 ? 36.601 18.966 40.808  1.00 19.94  ? 239 GLU   A CB  1 
ATOM   1973 C CG  . GLU   A 1 238 ? 35.220 19.208 41.388  1.00 22.32  ? 239 GLU   A CG  1 
ATOM   1974 C CD  . GLU   A 1 238 ? 34.968 20.641 41.776  1.00 23.89  ? 239 GLU   A CD  1 
ATOM   1975 O OE1 . GLU   A 1 238 ? 35.942 21.341 42.116  1.00 22.80  ? 239 GLU   A OE1 1 
ATOM   1976 O OE2 . GLU   A 1 238 ? 33.778 21.063 41.734  1.00 27.06  ? 239 GLU   A OE2 1 
ATOM   1977 N N   . TYR   A 1 239 ? 36.391 17.301 37.995  1.00 18.24  ? 240 TYR   A N   1 
ATOM   1978 C CA  . TYR   A 1 239 ? 35.631 16.971 36.798  1.00 18.54  ? 240 TYR   A CA  1 
ATOM   1979 C C   . TYR   A 1 239 ? 35.893 15.557 36.288  1.00 17.92  ? 240 TYR   A C   1 
ATOM   1980 O O   . TYR   A 1 239 ? 34.989 14.935 35.719  1.00 20.74  ? 240 TYR   A O   1 
ATOM   1981 C CB  . TYR   A 1 239 ? 35.986 17.963 35.683  1.00 21.06  ? 240 TYR   A CB  1 
ATOM   1982 C CG  . TYR   A 1 239 ? 35.827 19.414 36.082  1.00 25.01  ? 240 TYR   A CG  1 
ATOM   1983 C CD1 . TYR   A 1 239 ? 34.837 19.804 36.977  1.00 29.78  ? 240 TYR   A CD1 1 
ATOM   1984 C CD2 . TYR   A 1 239 ? 36.676 20.399 35.576  1.00 27.07  ? 240 TYR   A CD2 1 
ATOM   1985 C CE1 . TYR   A 1 239 ? 34.680 21.123 37.355  1.00 32.05  ? 240 TYR   A CE1 1 
ATOM   1986 C CE2 . TYR   A 1 239 ? 36.518 21.734 35.941  1.00 29.81  ? 240 TYR   A CE2 1 
ATOM   1987 C CZ  . TYR   A 1 239 ? 35.515 22.084 36.832  1.00 31.74  ? 240 TYR   A CZ  1 
ATOM   1988 O OH  . TYR   A 1 239 ? 35.343 23.393 37.223  1.00 33.85  ? 240 TYR   A OH  1 
ATOM   1989 N N   . PHE   A 1 240 ? 37.094 15.016 36.502  1.00 17.51  ? 241 PHE   A N   1 
ATOM   1990 C CA  . PHE   A 1 240 ? 37.531 13.830 35.777  1.00 17.96  ? 241 PHE   A CA  1 
ATOM   1991 C C   . PHE   A 1 240 ? 37.848 12.630 36.669  1.00 20.09  ? 241 PHE   A C   1 
ATOM   1992 O O   . PHE   A 1 240 ? 38.310 11.606 36.154  1.00 21.17  ? 241 PHE   A O   1 
ATOM   1993 C CB  . PHE   A 1 240 ? 38.784 14.152 34.953  1.00 16.71  ? 241 PHE   A CB  1 
ATOM   1994 C CG  . PHE   A 1 240 ? 38.528 15.012 33.738  1.00 15.91  ? 241 PHE   A CG  1 
ATOM   1995 C CD1 . PHE   A 1 240 ? 38.097 14.453 32.544  1.00 17.89  ? 241 PHE   A CD1 1 
ATOM   1996 C CD2 . PHE   A 1 240 ? 38.734 16.376 33.791  1.00 16.04  ? 241 PHE   A CD2 1 
ATOM   1997 C CE1 . PHE   A 1 240 ? 37.867 15.254 31.415  1.00 18.65  ? 241 PHE   A CE1 1 
ATOM   1998 C CE2 . PHE   A 1 240 ? 38.523 17.185 32.672  1.00 17.65  ? 241 PHE   A CE2 1 
ATOM   1999 C CZ  . PHE   A 1 240 ? 38.090 16.612 31.481  1.00 18.09  ? 241 PHE   A CZ  1 
ATOM   2000 N N   . SER   A 1 241 ? 37.612 12.708 37.986  1.00 22.31  ? 242 SER   A N   1 
ATOM   2001 C CA  . SER   A 1 241 ? 38.040 11.631 38.885  1.00 25.09  ? 242 SER   A CA  1 
ATOM   2002 C C   . SER   A 1 241 ? 37.398 10.297 38.529  1.00 26.07  ? 242 SER   A C   1 
ATOM   2003 O O   . SER   A 1 241 ? 37.960 9.237  38.836  1.00 28.17  ? 242 SER   A O   1 
ATOM   2004 C CB  . SER   A 1 241 ? 37.731 11.986 40.343  1.00 27.72  ? 242 SER   A CB  1 
ATOM   2005 O OG  . SER   A 1 241 ? 36.326 12.037 40.575  1.00 29.68  ? 242 SER   A OG  1 
ATOM   2006 N N   . ASN   A 1 242 ? 36.212 10.323 37.918  1.00 25.42  ? 243 ASN   A N   1 
ATOM   2007 C CA  . ASN   A 1 242 ? 35.499 9.107  37.551  1.00 28.18  ? 243 ASN   A CA  1 
ATOM   2008 C C   . ASN   A 1 242 ? 35.477 8.865  36.049  1.00 25.04  ? 243 ASN   A C   1 
ATOM   2009 O O   . ASN   A 1 242 ? 34.746 7.989  35.576  1.00 26.25  ? 243 ASN   A O   1 
ATOM   2010 C CB  . ASN   A 1 242 ? 34.084 9.173  38.108  1.00 33.57  ? 243 ASN   A CB  1 
ATOM   2011 C CG  . ASN   A 1 242 ? 34.063 9.015  39.596  1.00 39.50  ? 243 ASN   A CG  1 
ATOM   2012 O OD1 . ASN   A 1 242 ? 34.864 8.270  40.159  1.00 42.25  ? 243 ASN   A OD1 1 
ATOM   2013 N ND2 . ASN   A 1 242 ? 33.207 9.769  40.252  1.00 41.86  ? 243 ASN   A ND2 1 
ATOM   2014 N N   . THR   A 1 243 ? 36.263 9.620  35.295  1.00 22.02  ? 244 THR   A N   1 
ATOM   2015 C CA  . THR   A 1 243 ? 36.374 9.441  33.852  1.00 19.33  ? 244 THR   A CA  1 
ATOM   2016 C C   . THR   A 1 243 ? 37.378 8.343  33.552  1.00 17.70  ? 244 THR   A C   1 
ATOM   2017 O O   . THR   A 1 243 ? 38.417 8.245  34.207  1.00 19.96  ? 244 THR   A O   1 
ATOM   2018 C CB  . THR   A 1 243 ? 36.852 10.747 33.233  1.00 19.21  ? 244 THR   A CB  1 
ATOM   2019 O OG1 . THR   A 1 243 ? 35.925 11.772 33.571  1.00 22.30  ? 244 THR   A OG1 1 
ATOM   2020 C CG2 . THR   A 1 243 ? 36.946 10.634 31.688  1.00 19.41  ? 244 THR   A CG2 1 
ATOM   2021 N N   . SER   A 1 244 ? 37.074 7.510  32.551  1.00 16.43  ? 245 SER   A N   1 
ATOM   2022 C CA  . SER   A 1 244 ? 37.949 6.385  32.254  1.00 16.37  ? 245 SER   A CA  1 
ATOM   2023 C C   . SER   A 1 244 ? 39.322 6.854  31.773  1.00 14.33  ? 245 SER   A C   1 
ATOM   2024 O O   . SER   A 1 244 ? 39.483 7.904  31.140  1.00 14.34  ? 245 SER   A O   1 
ATOM   2025 C CB  . SER   A 1 244 ? 37.317 5.464  31.210  1.00 16.81  ? 245 SER   A CB  1 
ATOM   2026 O OG  . SER   A 1 244 ? 37.373 6.054  29.913  1.00 17.56  ? 245 SER   A OG  1 
ATOM   2027 N N   . ALA   A 1 245 ? 40.322 6.036  32.061  1.00 14.99  ? 246 ALA   A N   1 
ATOM   2028 C CA  . ALA   A 1 245 ? 41.668 6.304  31.568  1.00 15.89  ? 246 ALA   A CA  1 
ATOM   2029 C C   . ALA   A 1 245 ? 41.718 6.358  30.052  1.00 15.25  ? 246 ALA   A C   1 
ATOM   2030 O O   . ALA   A 1 245 ? 42.484 7.148  29.501  1.00 15.31  ? 246 ALA   A O   1 
ATOM   2031 C CB  . ALA   A 1 245 ? 42.644 5.252  32.100  1.00 18.14  ? 246 ALA   A CB  1 
ATOM   2032 N N   . LEU   A 1 246 ? 40.908 5.546  29.364  1.00 15.41  ? 247 LEU   A N   1 
ATOM   2033 C CA  . LEU   A 1 246 ? 40.932 5.564  27.900  1.00 15.27  ? 247 LEU   A CA  1 
ATOM   2034 C C   . LEU   A 1 246 ? 40.421 6.873  27.348  1.00 14.16  ? 247 LEU   A C   1 
ATOM   2035 O O   . LEU   A 1 246 ? 40.908 7.333  26.316  1.00 15.25  ? 247 LEU   A O   1 
ATOM   2036 C CB  . LEU   A 1 246 ? 40.080 4.448  27.334  1.00 18.99  ? 247 LEU   A CB  1 
ATOM   2037 C CG  . LEU   A 1 246 ? 40.771 3.186  26.866  1.00 19.72  ? 247 LEU   A CG  1 
ATOM   2038 C CD1 . LEU   A 1 246 ? 39.740 2.312  26.211  1.00 20.00  ? 247 LEU   A CD1 1 
ATOM   2039 C CD2 . LEU   A 1 246 ? 41.967 3.463  25.907  1.00 18.42  ? 247 LEU   A CD2 1 
ATOM   2040 N N   . ALA   A 1 247 ? 39.417 7.478  27.993  1.00 13.63  ? 248 ALA   A N   1 
ATOM   2041 C CA  . ALA   A 1 247 ? 38.948 8.784  27.540  1.00 14.34  ? 248 ALA   A CA  1 
ATOM   2042 C C   . ALA   A 1 247 ? 40.043 9.831  27.678  1.00 14.00  ? 248 ALA   A C   1 
ATOM   2043 O O   . ALA   A 1 247 ? 40.243 10.670 26.787  1.00 14.51  ? 248 ALA   A O   1 
ATOM   2044 C CB  . ALA   A 1 247 ? 37.707 9.208  28.320  1.00 15.06  ? 248 ALA   A CB  1 
ATOM   2045 N N   . LYS   A 1 248 ? 40.746 9.820  28.811  1.00 14.19  ? 249 LYS   A N   1 
ATOM   2046 C CA  . LYS   A 1 248 ? 41.866 10.742 28.996  1.00 14.44  ? 249 LYS   A CA  1 
ATOM   2047 C C   . LYS   A 1 248 ? 42.964 10.485 27.966  1.00 13.84  ? 249 LYS   A C   1 
ATOM   2048 O O   . LYS   A 1 248 ? 43.566 11.434 27.453  1.00 14.94  ? 249 LYS   A O   1 
ATOM   2049 C CB  . LYS   A 1 248 ? 42.407 10.654 30.425  1.00 15.50  ? 249 LYS   A CB  1 
ATOM   2050 C CG  . LYS   A 1 248 ? 41.437 11.110 31.487  1.00 17.76  ? 249 LYS   A CG  1 
ATOM   2051 C CD  . LYS   A 1 248 ? 42.105 10.944 32.868  1.00 23.38  ? 249 LYS   A CD  1 
ATOM   2052 C CE  . LYS   A 1 248 ? 41.314 11.594 33.951  1.00 27.32  ? 249 LYS   A CE  1 
ATOM   2053 N NZ  . LYS   A 1 248 ? 41.986 11.275 35.235  1.00 30.93  ? 249 LYS   A NZ  1 
ATOM   2054 N N   . ASP   A 1 249 ? 43.223 9.218  27.644  1.00 13.86  ? 250 ASP   A N   1 
ATOM   2055 C CA  . ASP   A 1 249 ? 44.242 8.848  26.628  1.00 13.41  ? 250 ASP   A CA  1 
ATOM   2056 C C   . ASP   A 1 249 ? 43.852 9.487  25.286  1.00 12.85  ? 250 ASP   A C   1 
ATOM   2057 O O   . ASP   A 1 249 ? 44.720 10.062 24.636  1.00 13.42  ? 250 ASP   A O   1 
ATOM   2058 C CB  . ASP   A 1 249 ? 44.364 7.332  26.568  1.00 14.67  ? 250 ASP   A CB  1 
ATOM   2059 C CG  . ASP   A 1 249 ? 45.374 6.746  25.591  1.00 16.16  ? 250 ASP   A CG  1 
ATOM   2060 O OD1 . ASP   A 1 249 ? 45.168 6.891  24.377  1.00 15.31  ? 250 ASP   A OD1 1 
ATOM   2061 O OD2 . ASP   A 1 249 ? 46.335 6.104  26.055  1.00 18.58  ? 250 ASP   A OD2 1 
ATOM   2062 N N   . PHE   A 1 250 ? 42.584 9.360  24.918  1.00 12.94  ? 251 PHE   A N   1 
ATOM   2063 C CA  . PHE   A 1 250 ? 42.111 9.947  23.662  1.00 12.66  ? 251 PHE   A CA  1 
ATOM   2064 C C   . PHE   A 1 250 ? 42.410 11.446 23.617  1.00 12.22  ? 251 PHE   A C   1 
ATOM   2065 O O   . PHE   A 1 250 ? 42.993 11.954 22.647  1.00 12.96  ? 251 PHE   A O   1 
ATOM   2066 C CB  . PHE   A 1 250 ? 40.605 9.662  23.563  1.00 13.45  ? 251 PHE   A CB  1 
ATOM   2067 C CG  . PHE   A 1 250 ? 39.951 10.146 22.295  1.00 13.51  ? 251 PHE   A CG  1 
ATOM   2068 C CD1 . PHE   A 1 250 ? 39.960 9.375  21.143  1.00 14.09  ? 251 PHE   A CD1 1 
ATOM   2069 C CD2 . PHE   A 1 250 ? 39.331 11.386 22.264  1.00 14.06  ? 251 PHE   A CD2 1 
ATOM   2070 C CE1 . PHE   A 1 250 ? 39.349 9.846  19.976  1.00 14.90  ? 251 PHE   A CE1 1 
ATOM   2071 C CE2 . PHE   A 1 250 ? 38.706 11.849 21.120  1.00 14.96  ? 251 PHE   A CE2 1 
ATOM   2072 C CZ  . PHE   A 1 250 ? 38.720 11.075 19.977  1.00 14.90  ? 251 PHE   A CZ  1 
ATOM   2073 N N   . ILE   A 1 251 ? 41.999 12.180 24.656  1.00 12.87  ? 252 ILE   A N   1 
ATOM   2074 C CA  . ILE   A 1 251 ? 42.229 13.623 24.680  1.00 12.68  ? 252 ILE   A CA  1 
ATOM   2075 C C   . ILE   A 1 251 ? 43.724 13.928 24.654  1.00 12.74  ? 252 ILE   A C   1 
ATOM   2076 O O   . ILE   A 1 251 ? 44.190 14.824 23.932  1.00 12.92  ? 252 ILE   A O   1 
ATOM   2077 C CB  . ILE   A 1 251 ? 41.537 14.262 25.904  1.00 13.24  ? 252 ILE   A CB  1 
ATOM   2078 C CG1 . ILE   A 1 251 ? 40.019 14.137 25.787  1.00 13.94  ? 252 ILE   A CG1 1 
ATOM   2079 C CG2 . ILE   A 1 251 ? 41.997 15.698 26.095  1.00 14.47  ? 252 ILE   A CG2 1 
ATOM   2080 C CD1 . ILE   A 1 251 ? 39.318 14.443 27.119  1.00 15.24  ? 252 ILE   A CD1 1 
ATOM   2081 N N   . ARG   A 1 252 ? 44.495 13.189 25.450  1.00 13.51  ? 253 ARG   A N   1 
ATOM   2082 C CA  . ARG   A 1 252 ? 45.918 13.456 25.574  1.00 15.23  ? 253 ARG   A CA  1 
ATOM   2083 C C   . ARG   A 1 252 ? 46.632 13.321 24.248  1.00 14.43  ? 253 ARG   A C   1 
ATOM   2084 O O   . ARG   A 1 252 ? 47.611 14.027 24.010  1.00 16.48  ? 253 ARG   A O   1 
ATOM   2085 C CB  . ARG   A 1 252 ? 46.555 12.498 26.588  1.00 17.12  ? 253 ARG   A CB  1 
ATOM   2086 C CG  . ARG   A 1 252 ? 47.840 13.024 27.144  1.00 25.92  ? 253 ARG   A CG  1 
ATOM   2087 C CD  . ARG   A 1 252 ? 48.351 12.216 28.315  1.00 30.65  ? 253 ARG   A CD  1 
ATOM   2088 N NE  . ARG   A 1 252 ? 47.316 11.515 29.069  1.00 35.33  ? 253 ARG   A NE  1 
ATOM   2089 C CZ  . ARG   A 1 252 ? 46.976 11.818 30.317  1.00 39.10  ? 253 ARG   A CZ  1 
ATOM   2090 N NH1 . ARG   A 1 252 ? 47.462 12.889 30.924  1.00 41.90  ? 253 ARG   A NH1 1 
ATOM   2091 N NH2 . ARG   A 1 252 ? 46.151 11.011 30.984  1.00 39.91  ? 253 ARG   A NH2 1 
ATOM   2092 N N   . ARG   A 1 253 ? 46.169 12.410 23.381  1.00 13.32  ? 254 ARG   A N   1 
ATOM   2093 C CA  . ARG   A 1 253 ? 46.811 12.208 22.085  1.00 13.95  ? 254 ARG   A CA  1 
ATOM   2094 C C   . ARG   A 1 253 ? 46.392 13.229 21.033  1.00 12.68  ? 254 ARG   A C   1 
ATOM   2095 O O   . ARG   A 1 253 ? 46.979 13.248 19.943  1.00 14.14  ? 254 ARG   A O   1 
ATOM   2096 C CB  . ARG   A 1 253 ? 46.549 10.787 21.597  1.00 15.63  ? 254 ARG   A CB  1 
ATOM   2097 C CG  . ARG   A 1 253 ? 47.223 9.748  22.483  1.00 16.37  ? 254 ARG   A CG  1 
ATOM   2098 C CD  . ARG   A 1 253 ? 47.009 8.342  21.944  1.00 18.15  ? 254 ARG   A CD  1 
ATOM   2099 N NE  . ARG   A 1 253 ? 47.399 7.325  22.909  1.00 18.50  ? 254 ARG   A NE  1 
ATOM   2100 C CZ  . ARG   A 1 253 ? 48.648 6.976  23.174  1.00 19.63  ? 254 ARG   A CZ  1 
ATOM   2101 N NH1 . ARG   A 1 253 ? 49.654 7.351  22.388  1.00 22.17  ? 254 ARG   A NH1 1 
ATOM   2102 N NH2 . ARG   A 1 253 ? 48.894 6.227  24.247  1.00 20.65  ? 254 ARG   A NH2 1 
ATOM   2103 N N   . LEU   A 1 254 ? 45.395 14.060 21.327  1.00 12.65  ? 255 LEU   A N   1 
ATOM   2104 C CA  . LEU   A 1 254 ? 44.983 15.155 20.456  1.00 12.11  ? 255 LEU   A CA  1 
ATOM   2105 C C   . LEU   A 1 254 ? 45.564 16.490 20.900  1.00 12.03  ? 255 LEU   A C   1 
ATOM   2106 O O   . LEU   A 1 254 ? 45.913 17.324 20.063  1.00 13.13  ? 255 LEU   A O   1 
ATOM   2107 C CB  . LEU   A 1 254 ? 43.453 15.248 20.425  1.00 11.85  ? 255 LEU   A CB  1 
ATOM   2108 C CG  . LEU   A 1 254 ? 42.783 14.041 19.777  1.00 12.47  ? 255 LEU   A CG  1 
ATOM   2109 C CD1 . LEU   A 1 254 ? 41.285 14.018 20.068  1.00 14.59  ? 255 LEU   A CD1 1 
ATOM   2110 C CD2 . LEU   A 1 254 ? 43.059 13.993 18.278  1.00 14.26  ? 255 LEU   A CD2 1 
ATOM   2111 N N   . LEU   A 1 255 ? 45.693 16.725 22.208  1.00 12.94  ? 256 LEU   A N   1 
ATOM   2112 C CA  . LEU   A 1 255 ? 46.187 18.008 22.721  1.00 12.13  ? 256 LEU   A CA  1 
ATOM   2113 C C   . LEU   A 1 255 ? 47.709 17.946 22.822  1.00 13.97  ? 256 LEU   A C   1 
ATOM   2114 O O   . LEU   A 1 255 ? 48.304 17.973 23.893  1.00 15.49  ? 256 LEU   A O   1 
ATOM   2115 C CB  . LEU   A 1 255 ? 45.515 18.343 24.047  1.00 13.22  ? 256 LEU   A CB  1 
ATOM   2116 C CG  . LEU   A 1 255 ? 43.993 18.517 23.942  1.00 12.98  ? 256 LEU   A CG  1 
ATOM   2117 C CD1 . LEU   A 1 255 ? 43.439 18.935 25.299  1.00 15.31  ? 256 LEU   A CD1 1 
ATOM   2118 C CD2 . LEU   A 1 255 ? 43.611 19.523 22.872  1.00 14.37  ? 256 LEU   A CD2 1 
ATOM   2119 N N   . VAL   A 1 256 ? 48.323 17.850 21.649  1.00 13.81  ? 257 VAL   A N   1 
ATOM   2120 C CA  . VAL   A 1 256 ? 49.759 17.681 21.471  1.00 15.13  ? 257 VAL   A CA  1 
ATOM   2121 C C   . VAL   A 1 256 ? 50.257 18.874 20.668  1.00 14.52  ? 257 VAL   A C   1 
ATOM   2122 O O   . VAL   A 1 256 ? 49.703 19.171 19.602  1.00 15.68  ? 257 VAL   A O   1 
ATOM   2123 C CB  . VAL   A 1 256 ? 50.052 16.363 20.725  1.00 16.72  ? 257 VAL   A CB  1 
ATOM   2124 C CG1 . VAL   A 1 256 ? 51.538 16.247 20.371  1.00 20.20  ? 257 VAL   A CG1 1 
ATOM   2125 C CG2 . VAL   A 1 256 ? 49.597 15.191 21.577  1.00 18.15  ? 257 VAL   A CG2 1 
ATOM   2126 N N   . LYS   A 1 257 ? 51.313 19.535 21.145  1.00 14.77  ? 258 LYS   A N   1 
ATOM   2127 C CA  A LYS   A 1 257 ? 51.756 20.757 20.477  0.50 16.00  ? 258 LYS   A CA  1 
ATOM   2128 C CA  B LYS   A 1 257 ? 51.768 20.756 20.481  0.50 15.31  ? 258 LYS   A CA  1 
ATOM   2129 C C   . LYS   A 1 257 ? 52.270 20.478 19.067  1.00 15.85  ? 258 LYS   A C   1 
ATOM   2130 O O   . LYS   A 1 257 ? 51.918 21.198 18.120  1.00 17.02  ? 258 LYS   A O   1 
ATOM   2131 C CB  A LYS   A 1 257 ? 52.794 21.519 21.306  0.50 19.24  ? 258 LYS   A CB  1 
ATOM   2132 C CB  B LYS   A 1 257 ? 52.845 21.464 21.304  0.50 17.33  ? 258 LYS   A CB  1 
ATOM   2133 C CG  A LYS   A 1 257 ? 53.155 22.885 20.688  0.50 21.90  ? 258 LYS   A CG  1 
ATOM   2134 C CG  B LYS   A 1 257 ? 53.287 22.783 20.665  0.50 19.11  ? 258 LYS   A CG  1 
ATOM   2135 C CD  A LYS   A 1 257 ? 54.310 23.579 21.407  0.50 24.78  ? 258 LYS   A CD  1 
ATOM   2136 C CD  B LYS   A 1 257 ? 53.939 23.726 21.669  0.50 21.17  ? 258 LYS   A CD  1 
ATOM   2137 C CE  A LYS   A 1 257 ? 54.624 24.948 20.784  0.50 25.62  ? 258 LYS   A CE  1 
ATOM   2138 C CE  B LYS   A 1 257 ? 54.230 25.081 21.020  0.50 21.22  ? 258 LYS   A CE  1 
ATOM   2139 N NZ  A LYS   A 1 257 ? 53.574 25.999 20.974  0.50 25.14  ? 258 LYS   A NZ  1 
ATOM   2140 N NZ  B LYS   A 1 257 ? 54.688 26.140 21.972  0.50 22.16  ? 258 LYS   A NZ  1 
ATOM   2141 N N   . ASP   A 1 258 ? 53.121 19.466 18.909  1.00 15.90  ? 259 ASP   A N   1 
ATOM   2142 C CA  . ASP   A 1 258 ? 53.695 19.191 17.591  1.00 17.59  ? 259 ASP   A CA  1 
ATOM   2143 C C   . ASP   A 1 258 ? 52.610 18.594 16.702  1.00 16.80  ? 259 ASP   A C   1 
ATOM   2144 O O   . ASP   A 1 258 ? 52.139 17.485 16.979  1.00 17.32  ? 259 ASP   A O   1 
ATOM   2145 C CB  . ASP   A 1 258 ? 54.882 18.238 17.747  1.00 20.13  ? 259 ASP   A CB  1 
ATOM   2146 C CG  . ASP   A 1 258 ? 55.591 17.941 16.432  1.00 23.22  ? 259 ASP   A CG  1 
ATOM   2147 O OD1 . ASP   A 1 258 ? 55.047 18.248 15.358  1.00 24.13  ? 259 ASP   A OD1 1 
ATOM   2148 O OD2 . ASP   A 1 258 ? 56.735 17.428 16.487  1.00 26.88  ? 259 ASP   A OD2 1 
ATOM   2149 N N   . PRO   A 1 259 ? 52.192 19.269 15.625  1.00 16.40  ? 260 PRO   A N   1 
ATOM   2150 C CA  . PRO   A 1 259 ? 51.109 18.706 14.808  1.00 17.40  ? 260 PRO   A CA  1 
ATOM   2151 C C   . PRO   A 1 259 ? 51.427 17.342 14.246  1.00 17.31  ? 260 PRO   A C   1 
ATOM   2152 O O   . PRO   A 1 259 ? 50.504 16.552 14.042  1.00 19.14  ? 260 PRO   A O   1 
ATOM   2153 C CB  . PRO   A 1 259 ? 50.907 19.743 13.690  1.00 18.72  ? 260 PRO   A CB  1 
ATOM   2154 C CG  . PRO   A 1 259 ? 51.692 20.914 14.062  1.00 20.18  ? 260 PRO   A CG  1 
ATOM   2155 C CD  . PRO   A 1 259 ? 52.681 20.563 15.110  1.00 18.17  ? 260 PRO   A CD  1 
ATOM   2156 N N   . LYS   A 1 260 ? 52.697 17.056 13.954  1.00 18.48  ? 261 LYS   A N   1 
ATOM   2157 C CA  . LYS   A 1 260 ? 53.057 15.762 13.383  1.00 21.48  ? 261 LYS   A CA  1 
ATOM   2158 C C   . LYS   A 1 260 ? 52.899 14.609 14.356  1.00 20.41  ? 261 LYS   A C   1 
ATOM   2159 O O   . LYS   A 1 260 ? 52.777 13.463 13.922  1.00 23.55  ? 261 LYS   A O   1 
ATOM   2160 C CB  . LYS   A 1 260 ? 54.492 15.794 12.871  1.00 26.36  ? 261 LYS   A CB  1 
ATOM   2161 C CG  . LYS   A 1 260 ? 54.828 17.065 12.092  1.00 32.69  ? 261 LYS   A CG  1 
ATOM   2162 C CD  . LYS   A 1 260 ? 55.937 16.866 11.084  1.00 38.52  ? 261 LYS   A CD  1 
ATOM   2163 C CE  . LYS   A 1 260 ? 57.310 17.115 11.678  1.00 41.28  ? 261 LYS   A CE  1 
ATOM   2164 N NZ  . LYS   A 1 260 ? 58.290 17.457 10.589  1.00 43.06  ? 261 LYS   A NZ  1 
ATOM   2165 N N   . LYS   A 1 261 ? 52.874 14.882 15.658  1.00 17.64  ? 262 LYS   A N   1 
ATOM   2166 C CA  . LYS   A 1 261 ? 52.737 13.831 16.649  1.00 17.53  ? 262 LYS   A CA  1 
ATOM   2167 C C   . LYS   A 1 261 ? 51.308 13.671 17.149  1.00 16.22  ? 262 LYS   A C   1 
ATOM   2168 O O   . LYS   A 1 261 ? 51.019 12.726 17.885  1.00 18.36  ? 262 LYS   A O   1 
ATOM   2169 C CB  . LYS   A 1 261 ? 53.705 14.107 17.806  1.00 22.22  ? 262 LYS   A CB  1 
ATOM   2170 C CG  . LYS   A 1 261 ? 55.170 13.984 17.337  1.00 28.30  ? 262 LYS   A CG  1 
ATOM   2171 C CD  . LYS   A 1 261 ? 56.179 14.265 18.422  1.00 33.35  ? 262 LYS   A CD  1 
ATOM   2172 C CE  . LYS   A 1 261 ? 57.607 14.101 17.888  1.00 36.00  ? 262 LYS   A CE  1 
ATOM   2173 N NZ  . LYS   A 1 261 ? 58.646 14.396 18.917  1.00 38.37  ? 262 LYS   A NZ  1 
ATOM   2174 N N   . ARG   A 1 262 ? 50.409 14.541 16.727  1.00 15.32  ? 263 ARG   A N   1 
ATOM   2175 C CA  . ARG   A 1 262 ? 49.010 14.489 17.092  1.00 15.67  ? 263 ARG   A CA  1 
ATOM   2176 C C   . ARG   A 1 262 ? 48.322 13.340 16.351  1.00 14.83  ? 263 ARG   A C   1 
ATOM   2177 O O   . ARG   A 1 262 ? 48.701 12.976 15.245  1.00 15.93  ? 263 ARG   A O   1 
ATOM   2178 C CB  . ARG   A 1 262 ? 48.437 15.858 16.713  1.00 17.89  ? 263 ARG   A CB  1 
ATOM   2179 C CG  . ARG   A 1 262 ? 47.174 16.308 17.377  1.00 18.87  ? 263 ARG   A CG  1 
ATOM   2180 C CD  . ARG   A 1 262 ? 46.860 17.738 16.950  1.00 16.10  ? 263 ARG   A CD  1 
ATOM   2181 N NE  . ARG   A 1 262 ? 47.805 18.762 17.421  1.00 13.47  ? 263 ARG   A NE  1 
ATOM   2182 C CZ  . ARG   A 1 262 ? 47.996 19.936 16.820  1.00 13.40  ? 263 ARG   A CZ  1 
ATOM   2183 N NH1 . ARG   A 1 262 ? 47.305 20.288 15.744  1.00 13.28  ? 263 ARG   A NH1 1 
ATOM   2184 N NH2 . ARG   A 1 262 ? 48.950 20.753 17.261  1.00 14.63  ? 263 ARG   A NH2 1 
ATOM   2185 N N   . MET   A 1 263 ? 47.306 12.752 16.972  1.00 14.93  ? 264 MET   A N   1 
ATOM   2186 C CA  . MET   A 1 263 ? 46.495 11.754 16.283  1.00 16.01  ? 264 MET   A CA  1 
ATOM   2187 C C   . MET   A 1 263 ? 45.812 12.366 15.061  1.00 14.29  ? 264 MET   A C   1 
ATOM   2188 O O   . MET   A 1 263 ? 45.321 13.490 15.107  1.00 14.17  ? 264 MET   A O   1 
ATOM   2189 C CB  . MET   A 1 263 ? 45.404 11.276 17.244  1.00 20.13  ? 264 MET   A CB  1 
ATOM   2190 C CG  . MET   A 1 263 ? 45.765 10.032 17.966  1.00 20.86  ? 264 MET   A CG  1 
ATOM   2191 S SD  . MET   A 1 263 ? 44.377 9.093  18.643  1.00 17.01  ? 264 MET   A SD  1 
ATOM   2192 C CE  . MET   A 1 263 ? 43.244 10.299 19.320  1.00 16.64  ? 264 MET   A CE  1 
ATOM   2193 N N   . THR   A 1 264 ? 45.772 11.604 13.968  1.00 14.45  ? 265 THR   A N   1 
ATOM   2194 C CA  . THR   A 1 264 ? 45.018 11.987 12.784  1.00 13.38  ? 265 THR   A CA  1 
ATOM   2195 C C   . THR   A 1 264 ? 43.569 11.545 12.922  1.00 13.24  ? 265 THR   A C   1 
ATOM   2196 O O   . THR   A 1 264 ? 43.201 10.813 13.838  1.00 13.62  ? 265 THR   A O   1 
ATOM   2197 C CB  . THR   A 1 264 ? 45.602 11.321 11.538  1.00 14.86  ? 265 THR   A CB  1 
ATOM   2198 O OG1 . THR   A 1 264 ? 45.413 9.909  11.684  1.00 16.03  ? 265 THR   A OG1 1 
ATOM   2199 C CG2 . THR   A 1 264 ? 47.071 11.662 11.332  1.00 16.63  ? 265 THR   A CG2 1 
ATOM   2200 N N   . ILE   A 1 265 ? 42.736 11.954 11.964  1.00 12.23  ? 266 ILE   A N   1 
ATOM   2201 C CA  . ILE   A 1 265 ? 41.337 11.522 12.013  1.00 12.23  ? 266 ILE   A CA  1 
ATOM   2202 C C   . ILE   A 1 265 ? 41.236 10.005 11.914  1.00 12.61  ? 266 ILE   A C   1 
ATOM   2203 O O   . ILE   A 1 265 ? 40.421 9.385  12.604  1.00 13.05  ? 266 ILE   A O   1 
ATOM   2204 C CB  . ILE   A 1 265 ? 40.486 12.256 10.956  1.00 12.36  ? 266 ILE   A CB  1 
ATOM   2205 C CG1 . ILE   A 1 265 ? 38.995 12.035 11.199  1.00 13.40  ? 266 ILE   A CG1 1 
ATOM   2206 C CG2 . ILE   A 1 265 ? 40.851 11.860 9.524   1.00 13.93  ? 266 ILE   A CG2 1 
ATOM   2207 C CD1 . ILE   A 1 265 ? 38.500 12.566 12.555  1.00 14.88  ? 266 ILE   A CD1 1 
ATOM   2208 N N   . GLN   A 1 266 ? 42.061 9.370  11.064  1.00 13.17  ? 267 GLN   A N   1 
ATOM   2209 C CA  . GLN   A 1 266 ? 42.032 7.908  10.985  1.00 13.76  ? 267 GLN   A CA  1 
ATOM   2210 C C   . GLN   A 1 266 ? 42.456 7.262  12.292  1.00 14.59  ? 267 GLN   A C   1 
ATOM   2211 O O   . GLN   A 1 266 ? 41.843 6.280  12.724  1.00 16.31  ? 267 GLN   A O   1 
ATOM   2212 C CB  . GLN   A 1 266 ? 42.877 7.396  9.812   1.00 16.59  ? 267 GLN   A CB  1 
ATOM   2213 C CG  . GLN   A 1 266 ? 42.361 7.868  8.464   1.00 21.30  ? 267 GLN   A CG  1 
ATOM   2214 C CD  . GLN   A 1 266 ? 43.030 7.201  7.290   1.00 29.67  ? 267 GLN   A CD  1 
ATOM   2215 O OE1 . GLN   A 1 266 ? 43.836 6.278  7.448   1.00 33.93  ? 267 GLN   A OE1 1 
ATOM   2216 N NE2 . GLN   A 1 266 ? 42.704 7.665  6.095   1.00 32.99  ? 267 GLN   A NE2 1 
ATOM   2217 N N   . ASP   A 1 267 ? 43.489 7.803  12.940  1.00 14.33  ? 268 ASP   A N   1 
ATOM   2218 C CA  . ASP   A 1 267 ? 43.895 7.297  14.248  1.00 15.85  ? 268 ASP   A CA  1 
ATOM   2219 C C   . ASP   A 1 267 ? 42.753 7.415  15.240  1.00 14.98  ? 268 ASP   A C   1 
ATOM   2220 O O   . ASP   A 1 267 ? 42.525 6.509  16.056  1.00 15.87  ? 268 ASP   A O   1 
ATOM   2221 C CB  . ASP   A 1 267 ? 45.056 8.133  14.808  1.00 16.63  ? 268 ASP   A CB  1 
ATOM   2222 C CG  . ASP   A 1 267 ? 46.358 7.964  14.076  1.00 19.65  ? 268 ASP   A CG  1 
ATOM   2223 O OD1 . ASP   A 1 267 ? 46.638 6.870  13.532  1.00 21.75  ? 268 ASP   A OD1 1 
ATOM   2224 O OD2 . ASP   A 1 267 ? 47.146 8.952  14.114  1.00 19.36  ? 268 ASP   A OD2 1 
ATOM   2225 N N   . SER   A 1 268 ? 42.025 8.532  15.198  1.00 13.79  ? 269 SER   A N   1 
ATOM   2226 C CA  A SER   A 1 268 ? 40.990 8.764  16.202  0.50 13.55  ? 269 SER   A CA  1 
ATOM   2227 C CA  B SER   A 1 268 ? 40.995 8.757  16.206  0.50 14.92  ? 269 SER   A CA  1 
ATOM   2228 C C   . SER   A 1 268 ? 39.873 7.739  16.087  1.00 14.51  ? 269 SER   A C   1 
ATOM   2229 O O   . SER   A 1 268 ? 39.303 7.315  17.103  1.00 15.32  ? 269 SER   A O   1 
ATOM   2230 C CB  A SER   A 1 268 ? 40.471 10.206 16.120  0.50 12.85  ? 269 SER   A CB  1 
ATOM   2231 C CB  B SER   A 1 268 ? 40.460 10.173 16.070  0.50 17.13  ? 269 SER   A CB  1 
ATOM   2232 O OG  A SER   A 1 268 ? 39.594 10.430 15.021  0.50 11.39  ? 269 SER   A OG  1 
ATOM   2233 O OG  B SER   A 1 268 ? 41.509 11.075 16.343  0.50 18.90  ? 269 SER   A OG  1 
ATOM   2234 N N   . LEU   A 1 269 ? 39.547 7.325  14.857  1.00 14.98  ? 270 LEU   A N   1 
ATOM   2235 C CA  . LEU   A 1 269 ? 38.502 6.335  14.639  1.00 16.01  ? 270 LEU   A CA  1 
ATOM   2236 C C   . LEU   A 1 269 ? 38.930 4.928  15.052  1.00 17.74  ? 270 LEU   A C   1 
ATOM   2237 O O   . LEU   A 1 269 ? 38.065 4.087  15.329  1.00 20.45  ? 270 LEU   A O   1 
ATOM   2238 C CB  . LEU   A 1 269 ? 38.107 6.357  13.157  1.00 18.29  ? 270 LEU   A CB  1 
ATOM   2239 C CG  . LEU   A 1 269 ? 37.286 7.613  12.853  1.00 20.28  ? 270 LEU   A CG  1 
ATOM   2240 C CD1 . LEU   A 1 269 ? 37.190 7.903  11.372  1.00 23.96  ? 270 LEU   A CD1 1 
ATOM   2241 C CD2 . LEU   A 1 269 ? 35.880 7.470  13.411  1.00 20.64  ? 270 LEU   A CD2 1 
ATOM   2242 N N   . GLN   A 1 270 ? 40.230 4.642  15.087  1.00 16.72  ? 271 GLN   A N   1 
ATOM   2243 C CA  . GLN   A 1 270 ? 40.724 3.345  15.542  1.00 19.10  ? 271 GLN   A CA  1 
ATOM   2244 C C   . GLN   A 1 270 ? 41.078 3.333  17.016  1.00 18.48  ? 271 GLN   A C   1 
ATOM   2245 O O   . GLN   A 1 270 ? 41.400 2.263  17.559  1.00 20.05  ? 271 GLN   A O   1 
ATOM   2246 C CB  . GLN   A 1 270 ? 41.987 2.950  14.768  1.00 21.37  ? 271 GLN   A CB  1 
ATOM   2247 C CG  . GLN   A 1 270 ? 41.770 2.811  13.270  1.00 22.83  ? 271 GLN   A CG  1 
ATOM   2248 C CD  . GLN   A 1 270 ? 40.644 1.855  12.963  1.00 25.93  ? 271 GLN   A CD  1 
ATOM   2249 O OE1 . GLN   A 1 270 ? 40.601 0.737  13.478  1.00 28.43  ? 271 GLN   A OE1 1 
ATOM   2250 N NE2 . GLN   A 1 270 ? 39.714 2.294  12.123  1.00 27.49  ? 271 GLN   A NE2 1 
ATOM   2251 N N   . HIS   A 1 271 ? 41.059 4.483  17.670  1.00 17.56  ? 272 HIS   A N   1 
ATOM   2252 C CA  . HIS   A 1 271 ? 41.453 4.537  19.068  1.00 16.55  ? 272 HIS   A CA  1 
ATOM   2253 C C   . HIS   A 1 271 ? 40.504 3.664  19.890  1.00 16.28  ? 272 HIS   A C   1 
ATOM   2254 O O   . HIS   A 1 271 ? 39.285 3.680  19.663  1.00 18.11  ? 272 HIS   A O   1 
ATOM   2255 C CB  . HIS   A 1 271 ? 41.357 5.987  19.541  1.00 16.27  ? 272 HIS   A CB  1 
ATOM   2256 C CG  . HIS   A 1 271 ? 41.860 6.203  20.931  1.00 14.31  ? 272 HIS   A CG  1 
ATOM   2257 N ND1 . HIS   A 1 271 ? 41.129 5.867  22.051  1.00 14.73  ? 272 HIS   A ND1 1 
ATOM   2258 C CD2 . HIS   A 1 271 ? 43.056 6.660  21.381  1.00 14.89  ? 272 HIS   A CD2 1 
ATOM   2259 C CE1 . HIS   A 1 271 ? 41.837 6.143  23.135  1.00 14.38  ? 272 HIS   A CE1 1 
ATOM   2260 N NE2 . HIS   A 1 271 ? 43.002 6.642  22.763  1.00 14.45  ? 272 HIS   A NE2 1 
ATOM   2261 N N   . PRO   A 1 272 ? 41.011 2.900  20.863  1.00 17.35  ? 273 PRO   A N   1 
ATOM   2262 C CA  . PRO   A 1 272 ? 40.132 1.971  21.592  1.00 18.84  ? 273 PRO   A CA  1 
ATOM   2263 C C   . PRO   A 1 272 ? 38.955 2.612  22.313  1.00 19.09  ? 273 PRO   A C   1 
ATOM   2264 O O   . PRO   A 1 272 ? 37.966 1.917  22.566  1.00 21.79  ? 273 PRO   A O   1 
ATOM   2265 C CB  . PRO   A 1 272 ? 41.086 1.272  22.576  1.00 20.37  ? 273 PRO   A CB  1 
ATOM   2266 C CG  . PRO   A 1 272 ? 42.440 1.374  21.918  1.00 22.37  ? 273 PRO   A CG  1 
ATOM   2267 C CD  . PRO   A 1 272 ? 42.433 2.703  21.214  1.00 19.20  ? 273 PRO   A CD  1 
ATOM   2268 N N   . TRP   A 1 273 ? 39.000 3.909  22.644  1.00 17.97  ? 274 TRP   A N   1 
ATOM   2269 C CA  . TRP   A 1 273 ? 37.822 4.535  23.254  1.00 18.57  ? 274 TRP   A CA  1 
ATOM   2270 C C   . TRP   A 1 273 ? 36.678 4.659  22.252  1.00 20.54  ? 274 TRP   A C   1 
ATOM   2271 O O   . TRP   A 1 273 ? 35.511 4.665  22.658  1.00 23.16  ? 274 TRP   A O   1 
ATOM   2272 C CB  . TRP   A 1 273 ? 38.185 5.924  23.787  1.00 17.40  ? 274 TRP   A CB  1 
ATOM   2273 C CG  . TRP   A 1 273 ? 37.171 6.579  24.699  1.00 16.03  ? 274 TRP   A CG  1 
ATOM   2274 C CD1 . TRP   A 1 273 ? 36.608 6.045  25.831  1.00 17.87  ? 274 TRP   A CD1 1 
ATOM   2275 C CD2 . TRP   A 1 273 ? 36.621 7.898  24.566  1.00 16.22  ? 274 TRP   A CD2 1 
ATOM   2276 N NE1 . TRP   A 1 273 ? 35.738 6.954  26.399  1.00 17.69  ? 274 TRP   A NE1 1 
ATOM   2277 C CE2 . TRP   A 1 273 ? 35.736 8.101  25.645  1.00 16.33  ? 274 TRP   A CE2 1 
ATOM   2278 C CE3 . TRP   A 1 273 ? 36.804 8.934  23.643  1.00 15.86  ? 274 TRP   A CE3 1 
ATOM   2279 C CZ2 . TRP   A 1 273 ? 35.031 9.294  25.822  1.00 16.64  ? 274 TRP   A CZ2 1 
ATOM   2280 C CZ3 . TRP   A 1 273 ? 36.114 10.115 23.830  1.00 17.31  ? 274 TRP   A CZ3 1 
ATOM   2281 C CH2 . TRP   A 1 273 ? 35.238 10.288 24.907  1.00 17.51  ? 274 TRP   A CH2 1 
ATOM   2282 N N   . ILE   A 1 274 ? 36.993 4.761  20.959  1.00 21.08  ? 275 ILE   A N   1 
ATOM   2283 C CA  . ILE   A 1 274 ? 36.007 5.027  19.906  1.00 21.97  ? 275 ILE   A CA  1 
ATOM   2284 C C   . ILE   A 1 274 ? 35.626 3.771  19.136  1.00 26.93  ? 275 ILE   A C   1 
ATOM   2285 O O   . ILE   A 1 274 ? 34.456 3.584  18.805  1.00 28.42  ? 275 ILE   A O   1 
ATOM   2286 C CB  . ILE   A 1 274 ? 36.544 6.101  18.929  1.00 20.71  ? 275 ILE   A CB  1 
ATOM   2287 C CG1 . ILE   A 1 274 ? 36.728 7.448  19.612  1.00 20.30  ? 275 ILE   A CG1 1 
ATOM   2288 C CG2 . ILE   A 1 274 ? 35.671 6.188  17.667  1.00 21.38  ? 275 ILE   A CG2 1 
ATOM   2289 C CD1 . ILE   A 1 274 ? 35.461 8.067  20.134  1.00 22.17  ? 275 ILE   A CD1 1 
ATOM   2290 N N   . LYS   A 1 275 ? 36.608 2.955  18.771  1.00 29.45  ? 276 LYS   A N   1 
ATOM   2291 C CA  . LYS   A 1 275 ? 36.363 1.844  17.866  1.00 35.34  ? 276 LYS   A CA  1 
ATOM   2292 C C   . LYS   A 1 275 ? 35.336 0.901  18.481  1.00 41.41  ? 276 LYS   A C   1 
ATOM   2293 O O   . LYS   A 1 275 ? 35.461 0.543  19.659  1.00 42.87  ? 276 LYS   A O   1 
ATOM   2294 C CB  . LYS   A 1 275 ? 37.662 1.088  17.609  1.00 35.45  ? 276 LYS   A CB  1 
ATOM   2295 C CG  . LYS   A 1 275 ? 37.531 0.003  16.568  1.00 36.61  ? 276 LYS   A CG  1 
ATOM   2296 C CD  . LYS   A 1 275 ? 38.874 -0.309 15.972  1.00 38.59  ? 276 LYS   A CD  1 
ATOM   2297 C CE  . LYS   A 1 275 ? 38.873 -1.635 15.265  1.00 40.77  ? 276 LYS   A CE  1 
ATOM   2298 N NZ  . LYS   A 1 275 ? 40.250 -2.175 15.221  1.00 42.14  ? 276 LYS   A NZ  1 
ATOM   2299 N N   . PRO   A 1 276 ? 34.306 0.483  17.726  1.00 47.26  ? 277 PRO   A N   1 
ATOM   2300 C CA  . PRO   A 1 276 ? 33.254 -0.415 18.214  1.00 50.67  ? 277 PRO   A CA  1 
ATOM   2301 C C   . PRO   A 1 276 ? 33.710 -1.869 18.243  1.00 52.59  ? 277 PRO   A C   1 
ATOM   2302 O O   . PRO   A 1 276 ? 34.912 -2.110 18.342  1.00 53.52  ? 277 PRO   A O   1 
ATOM   2303 C CB  . PRO   A 1 276 ? 32.141 -0.234 17.178  1.00 51.52  ? 277 PRO   A CB  1 
ATOM   2304 C CG  . PRO   A 1 276 ? 32.863 0.101  15.923  1.00 50.61  ? 277 PRO   A CG  1 
ATOM   2305 C CD  . PRO   A 1 276 ? 34.064 0.918  16.340  1.00 48.77  ? 277 PRO   A CD  1 
ATOM   2306 N N   . PRO   A 1 290 ? 39.261 39.256 15.649  1.00 63.41  ? 291 PRO   A N   1 
ATOM   2307 C CA  . PRO   A 1 290 ? 38.854 37.904 16.054  1.00 62.20  ? 291 PRO   A CA  1 
ATOM   2308 C C   . PRO   A 1 290 ? 39.616 37.442 17.293  1.00 58.62  ? 291 PRO   A C   1 
ATOM   2309 O O   . PRO   A 1 290 ? 39.020 37.144 18.333  1.00 59.30  ? 291 PRO   A O   1 
ATOM   2310 C CB  . PRO   A 1 290 ? 39.248 37.040 14.847  1.00 63.90  ? 291 PRO   A CB  1 
ATOM   2311 C CG  . PRO   A 1 290 ? 39.436 38.004 13.707  1.00 64.44  ? 291 PRO   A CG  1 
ATOM   2312 C CD  . PRO   A 1 290 ? 39.932 39.265 14.340  1.00 64.26  ? 291 PRO   A CD  1 
ATOM   2313 N N   . GLN   A 1 291 ? 40.938 37.385 17.171  1.00 53.12  ? 292 GLN   A N   1 
ATOM   2314 C CA  . GLN   A 1 291 ? 41.798 36.964 18.264  1.00 47.41  ? 292 GLN   A CA  1 
ATOM   2315 C C   . GLN   A 1 291 ? 42.217 38.109 19.175  1.00 43.63  ? 292 GLN   A C   1 
ATOM   2316 O O   . GLN   A 1 291 ? 42.896 37.860 20.170  1.00 40.77  ? 292 GLN   A O   1 
ATOM   2317 C CB  . GLN   A 1 291 ? 43.038 36.241 17.727  1.00 44.70  ? 292 GLN   A CB  1 
ATOM   2318 C CG  . GLN   A 1 291 ? 44.010 37.088 16.912  1.00 41.18  ? 292 GLN   A CG  1 
ATOM   2319 C CD  . GLN   A 1 291 ? 43.677 37.116 15.422  1.00 38.25  ? 292 GLN   A CD  1 
ATOM   2320 O OE1 . GLN   A 1 291 ? 42.512 37.220 15.039  1.00 38.60  ? 292 GLN   A OE1 1 
ATOM   2321 N NE2 . GLN   A 1 291 ? 44.702 37.019 14.577  1.00 35.93  ? 292 GLN   A NE2 1 
ATOM   2322 N N   . PHE   A 1 292 ? 41.810 39.340 18.876  1.00 43.34  ? 293 PHE   A N   1 
ATOM   2323 C CA  . PHE   A 1 292 ? 42.237 40.517 19.618  1.00 43.84  ? 293 PHE   A CA  1 
ATOM   2324 C C   . PHE   A 1 292 ? 41.072 41.083 20.418  1.00 49.58  ? 293 PHE   A C   1 
ATOM   2325 O O   . PHE   A 1 292 ? 39.949 41.181 19.912  1.00 49.57  ? 293 PHE   A O   1 
ATOM   2326 C CB  . PHE   A 1 292 ? 42.788 41.575 18.655  1.00 40.26  ? 293 PHE   A CB  1 
ATOM   2327 C CG  . PHE   A 1 292 ? 44.039 41.140 17.942  1.00 36.35  ? 293 PHE   A CG  1 
ATOM   2328 C CD1 . PHE   A 1 292 ? 45.250 41.093 18.611  1.00 34.57  ? 293 PHE   A CD1 1 
ATOM   2329 C CD2 . PHE   A 1 292 ? 43.994 40.733 16.616  1.00 35.51  ? 293 PHE   A CD2 1 
ATOM   2330 C CE1 . PHE   A 1 292 ? 46.401 40.669 17.966  1.00 34.37  ? 293 PHE   A CE1 1 
ATOM   2331 C CE2 . PHE   A 1 292 ? 45.141 40.307 15.965  1.00 34.48  ? 293 PHE   A CE2 1 
ATOM   2332 C CZ  . PHE   A 1 292 ? 46.348 40.274 16.643  1.00 34.46  ? 293 PHE   A CZ  1 
ATOM   2333 N N   . GLU   A 1 293 ? 41.344 41.444 21.672  1.00 53.19  ? 294 GLU   A N   1 
ATOM   2334 C CA  . GLU   A 1 293 ? 40.326 42.042 22.529  1.00 56.88  ? 294 GLU   A CA  1 
ATOM   2335 C C   . GLU   A 1 293 ? 40.004 43.446 22.031  1.00 58.47  ? 294 GLU   A C   1 
ATOM   2336 O O   . GLU   A 1 293 ? 40.856 44.338 22.066  1.00 58.62  ? 294 GLU   A O   1 
ATOM   2337 C CB  . GLU   A 1 293 ? 40.799 42.094 23.988  1.00 58.41  ? 294 GLU   A CB  1 
ATOM   2338 C CG  . GLU   A 1 293 ? 41.067 40.729 24.620  1.00 59.52  ? 294 GLU   A CG  1 
ATOM   2339 C CD  . GLU   A 1 293 ? 39.895 40.214 25.445  1.00 59.98  ? 294 GLU   A CD  1 
ATOM   2340 O OE1 . GLU   A 1 293 ? 38.751 40.653 25.195  1.00 61.62  ? 294 GLU   A OE1 1 
ATOM   2341 O OE2 . GLU   A 1 293 ? 40.112 39.366 26.336  1.00 58.09  ? 294 GLU   A OE2 1 
HETATM 2342 S S   . SO4   B 2 .   ? 46.066 12.105 34.674  1.00 106.41 ? 301 SO4   A S   1 
HETATM 2343 O O1  . SO4   B 2 .   ? 46.850 13.087 33.928  1.00 64.29  ? 301 SO4   A O1  1 
HETATM 2344 O O2  . SO4   B 2 .   ? 45.624 11.032 33.787  1.00 70.46  ? 301 SO4   A O2  1 
HETATM 2345 O O3  . SO4   B 2 .   ? 46.886 11.541 35.743  1.00 77.68  ? 301 SO4   A O3  1 
HETATM 2346 O O4  . SO4   B 2 .   ? 44.898 12.766 35.246  1.00 46.53  ? 301 SO4   A O4  1 
HETATM 2347 C C2  . A1BVM C 3 .   ? 23.807 28.376 12.188  1.00 25.83  ? 302 A1BVM A C2  1 
HETATM 2348 C C3  . A1BVM C 3 .   ? 24.972 29.133 12.296  1.00 28.11  ? 302 A1BVM A C3  1 
HETATM 2349 C C4  . A1BVM C 3 .   ? 25.132 28.741 14.723  1.00 33.63  ? 302 A1BVM A C4  1 
HETATM 2350 C C5  . A1BVM C 3 .   ? 25.350 29.617 15.940  1.00 36.06  ? 302 A1BVM A C5  1 
HETATM 2351 C C6  . A1BVM C 3 .   ? 27.153 30.956 16.976  1.00 45.37  ? 302 A1BVM A C6  1 
HETATM 2352 C C7  . A1BVM C 3 .   ? 28.474 31.382 17.024  1.00 48.65  ? 302 A1BVM A C7  1 
HETATM 2353 C C8  . A1BVM C 3 .   ? 28.905 32.119 18.111  1.00 51.12  ? 302 A1BVM A C8  1 
HETATM 2354 C C10 . A1BVM C 3 .   ? 26.331 31.292 18.044  1.00 48.49  ? 302 A1BVM A C10 1 
HETATM 2355 C C17 . A1BVM C 3 .   ? 21.150 27.102 11.629  1.00 22.54  ? 302 A1BVM A C17 1 
HETATM 2356 C C16 . A1BVM C 3 .   ? 20.077 26.264 11.394  1.00 22.42  ? 302 A1BVM A C16 1 
HETATM 2357 C C15 . A1BVM C 3 .   ? 20.963 25.548 9.420   1.00 22.39  ? 302 A1BVM A C15 1 
HETATM 2358 C C14 . A1BVM C 3 .   ? 22.074 26.350 9.570   1.00 23.85  ? 302 A1BVM A C14 1 
HETATM 2359 C C13 . A1BVM C 3 .   ? 24.157 28.455 9.850   1.00 27.58  ? 302 A1BVM A C13 1 
HETATM 2360 C C12 . A1BVM C 3 .   ? 26.984 29.757 13.523  1.00 33.94  ? 302 A1BVM A C12 1 
HETATM 2361 C C11 . A1BVM C 3 .   ? 27.558 29.625 14.920  1.00 35.70  ? 302 A1BVM A C11 1 
HETATM 2362 C C1  . A1BVM C 3 .   ? 23.381 28.012 10.913  1.00 24.35  ? 302 A1BVM A C1  1 
HETATM 2363 N N   . A1BVM C 3 .   ? 25.552 29.437 13.506  1.00 31.63  ? 302 A1BVM A N   1 
HETATM 2364 C C   . A1BVM C 3 .   ? 22.191 27.151 10.703  1.00 21.79  ? 302 A1BVM A C   1 
HETATM 2365 C C9  . A1BVM C 3 .   ? 26.851 32.034 19.087  1.00 50.78  ? 302 A1BVM A C9  1 
HETATM 2366 N N1  . A1BVM C 3 .   ? 26.663 30.260 15.886  1.00 38.29  ? 302 A1BVM A N1  1 
HETATM 2367 N N2  . A1BVM C 3 .   ? 28.119 32.454 19.139  1.00 51.88  ? 302 A1BVM A N2  1 
HETATM 2368 N N3  . A1BVM C 3 .   ? 25.659 29.538 11.238  1.00 28.19  ? 302 A1BVM A N3  1 
HETATM 2369 N N4  . A1BVM C 3 .   ? 25.250 29.191 10.006  1.00 28.18  ? 302 A1BVM A N4  1 
HETATM 2370 N N5  . A1BVM C 3 .   ? 19.967 25.490 10.308  1.00 22.32  ? 302 A1BVM A N5  1 
HETATM 2371 O O   . HOH   D 4 .   ? 28.312 38.615 7.435   0.50 38.11  ? 401 HOH   A O   1 
HETATM 2372 O O   A HOH   D 4 .   ? 33.733 29.514 10.728  0.50 40.87  ? 402 HOH   A O   1 
HETATM 2373 O O   B HOH   D 4 .   ? 33.038 27.980 10.389  0.50 40.87  ? 402 HOH   A O   1 
HETATM 2374 O O   . HOH   D 4 .   ? 13.600 22.949 -2.570  1.00 28.33  ? 403 HOH   A O   1 
HETATM 2375 O O   . HOH   D 4 .   ? 37.355 28.408 16.172  1.00 37.64  ? 404 HOH   A O   1 
HETATM 2376 O O   . HOH   D 4 .   ? 48.411 28.963 1.896   1.00 38.71  ? 405 HOH   A O   1 
HETATM 2377 O O   . HOH   D 4 .   ? 19.923 27.727 -7.666  1.00 42.14  ? 406 HOH   A O   1 
HETATM 2378 O O   . HOH   D 4 .   ? 37.274 26.349 -1.855  1.00 55.18  ? 407 HOH   A O   1 
HETATM 2379 O O   . HOH   D 4 .   ? 39.971 35.012 37.435  1.00 48.31  ? 408 HOH   A O   1 
HETATM 2380 O O   . HOH   D 4 .   ? 45.311 36.240 11.449  1.00 43.59  ? 409 HOH   A O   1 
HETATM 2381 O O   . HOH   D 4 .   ? 20.036 40.964 -6.530  1.00 44.10  ? 410 HOH   A O   1 
HETATM 2382 O O   . HOH   D 4 .   ? 35.920 25.381 35.785  1.00 40.58  ? 411 HOH   A O   1 
HETATM 2383 O O   . HOH   D 4 .   ? 44.989 31.389 32.607  1.00 26.80  ? 412 HOH   A O   1 
HETATM 2384 O O   . HOH   D 4 .   ? 21.287 35.221 13.097  1.00 23.34  ? 413 HOH   A O   1 
HETATM 2385 O O   . HOH   D 4 .   ? 47.568 18.181 1.177   1.00 36.50  ? 414 HOH   A O   1 
HETATM 2386 O O   . HOH   D 4 .   ? 30.504 30.162 13.287  1.00 38.24  ? 415 HOH   A O   1 
HETATM 2387 O O   . HOH   D 4 .   ? 12.487 28.243 -5.847  1.00 44.38  ? 416 HOH   A O   1 
HETATM 2388 O O   . HOH   D 4 .   ? 29.032 27.671 5.840   1.00 25.80  ? 417 HOH   A O   1 
HETATM 2389 O O   . HOH   D 4 .   ? 33.649 5.722  32.726  1.00 62.21  ? 418 HOH   A O   1 
HETATM 2390 O O   . HOH   D 4 .   ? 46.856 17.107 4.328   1.00 41.80  ? 419 HOH   A O   1 
HETATM 2391 O O   . HOH   D 4 .   ? 53.709 24.113 14.584  1.00 34.34  ? 420 HOH   A O   1 
HETATM 2392 O O   . HOH   D 4 .   ? 31.707 13.032 31.938  1.00 26.56  ? 421 HOH   A O   1 
HETATM 2393 O O   . HOH   D 4 .   ? 58.250 17.225 18.597  1.00 54.55  ? 422 HOH   A O   1 
HETATM 2394 O O   . HOH   D 4 .   ? 30.371 13.205 -1.545  1.00 39.28  ? 423 HOH   A O   1 
HETATM 2395 O O   . HOH   D 4 .   ? 16.124 21.900 4.882   1.00 20.24  ? 424 HOH   A O   1 
HETATM 2396 O O   . HOH   D 4 .   ? 25.207 7.429  29.583  1.00 32.07  ? 425 HOH   A O   1 
HETATM 2397 O O   . HOH   D 4 .   ? 36.545 23.956 -3.105  1.00 46.51  ? 426 HOH   A O   1 
HETATM 2398 O O   . HOH   D 4 .   ? 27.769 9.515  11.495  1.00 29.90  ? 427 HOH   A O   1 
HETATM 2399 O O   . HOH   D 4 .   ? 56.380 19.691 13.590  1.00 40.85  ? 428 HOH   A O   1 
HETATM 2400 O O   . HOH   D 4 .   ? 7.195  30.328 1.332   1.00 19.14  ? 429 HOH   A O   1 
HETATM 2401 O O   . HOH   D 4 .   ? 48.209 16.260 25.918  1.00 21.33  ? 430 HOH   A O   1 
HETATM 2402 O O   . HOH   D 4 .   ? 34.211 30.869 -7.308  1.00 48.67  ? 431 HOH   A O   1 
HETATM 2403 O O   . HOH   D 4 .   ? 21.520 28.695 15.358  1.00 44.68  ? 432 HOH   A O   1 
HETATM 2404 O O   . HOH   D 4 .   ? 47.838 15.510 30.646  1.00 50.01  ? 433 HOH   A O   1 
HETATM 2405 O O   . HOH   D 4 .   ? 19.159 9.148  17.166  1.00 41.33  ? 434 HOH   A O   1 
HETATM 2406 O O   . HOH   D 4 .   ? 49.207 14.482 12.973  1.00 17.66  ? 435 HOH   A O   1 
HETATM 2407 O O   . HOH   D 4 .   ? 35.694 3.501  14.257  1.00 33.61  ? 436 HOH   A O   1 
HETATM 2408 O O   . HOH   D 4 .   ? 8.240  32.994 -7.151  1.00 36.64  ? 437 HOH   A O   1 
HETATM 2409 O O   A HOH   D 4 .   ? 25.205 16.738 3.339   0.48 17.11  ? 438 HOH   A O   1 
HETATM 2410 O O   B HOH   D 4 .   ? 26.360 17.605 2.972   0.52 25.61  ? 438 HOH   A O   1 
HETATM 2411 O O   . HOH   D 4 .   ? 50.903 22.636 10.774  1.00 45.36  ? 439 HOH   A O   1 
HETATM 2412 O O   . HOH   D 4 .   ? 45.644 5.511  11.458  1.00 46.26  ? 440 HOH   A O   1 
HETATM 2413 O O   . HOH   D 4 .   ? 34.852 32.305 26.359  1.00 42.42  ? 441 HOH   A O   1 
HETATM 2414 O O   . HOH   D 4 .   ? 26.077 29.211 -8.006  1.00 56.34  ? 442 HOH   A O   1 
HETATM 2415 O O   . HOH   D 4 .   ? 6.769  20.945 1.364   1.00 22.88  ? 443 HOH   A O   1 
HETATM 2416 O O   . HOH   D 4 .   ? 32.622 15.699 34.716  1.00 26.58  ? 444 HOH   A O   1 
HETATM 2417 O O   . HOH   D 4 .   ? 40.340 37.835 1.247   1.00 36.73  ? 445 HOH   A O   1 
HETATM 2418 O O   . HOH   D 4 .   ? 17.399 17.834 6.184   1.00 45.47  ? 446 HOH   A O   1 
HETATM 2419 O O   . HOH   D 4 .   ? 31.010 4.000  23.683  1.00 51.34  ? 447 HOH   A O   1 
HETATM 2420 O O   . HOH   D 4 .   ? 33.694 7.276  9.413   1.00 48.18  ? 448 HOH   A O   1 
HETATM 2421 O O   . HOH   D 4 .   ? 51.945 23.562 16.831  1.00 25.63  ? 449 HOH   A O   1 
HETATM 2422 O O   . HOH   D 4 .   ? 13.761 39.688 -8.529  1.00 45.31  ? 450 HOH   A O   1 
HETATM 2423 O O   . HOH   D 4 .   ? 11.497 37.029 8.623   1.00 27.58  ? 451 HOH   A O   1 
HETATM 2424 O O   . HOH   D 4 .   ? 37.129 38.584 4.275   1.00 25.15  ? 452 HOH   A O   1 
HETATM 2425 O O   . HOH   D 4 .   ? 34.623 13.950 39.721  1.00 41.04  ? 453 HOH   A O   1 
HETATM 2426 O O   . HOH   D 4 .   ? 41.507 13.519 36.997  1.00 40.13  ? 454 HOH   A O   1 
HETATM 2427 O O   . HOH   D 4 .   ? 37.523 32.810 -6.016  1.00 46.33  ? 455 HOH   A O   1 
HETATM 2428 O O   . HOH   D 4 .   ? 48.864 30.525 10.425  1.00 17.84  ? 456 HOH   A O   1 
HETATM 2429 O O   . HOH   D 4 .   ? 49.389 11.803 19.859  1.00 19.15  ? 457 HOH   A O   1 
HETATM 2430 O O   . HOH   D 4 .   ? 54.297 29.799 23.954  1.00 30.03  ? 458 HOH   A O   1 
HETATM 2431 O O   . HOH   D 4 .   ? 48.170 22.110 11.488  1.00 20.15  ? 459 HOH   A O   1 
HETATM 2432 O O   . HOH   D 4 .   ? 24.559 11.003 12.307  1.00 26.70  ? 460 HOH   A O   1 
HETATM 2433 O O   . HOH   D 4 .   ? 5.503  20.421 -2.180  1.00 41.58  ? 461 HOH   A O   1 
HETATM 2434 O O   . HOH   D 4 .   ? 10.489 27.753 7.607   1.00 39.26  ? 462 HOH   A O   1 
HETATM 2435 O O   . HOH   D 4 .   ? 39.552 33.541 25.597  1.00 24.46  ? 463 HOH   A O   1 
HETATM 2436 O O   . HOH   D 4 .   ? 26.762 8.100  17.235  1.00 118.39 ? 464 HOH   A O   1 
HETATM 2437 O O   . HOH   D 4 .   ? 15.115 32.895 17.849  1.00 46.48  ? 465 HOH   A O   1 
HETATM 2438 O O   . HOH   D 4 .   ? 35.870 28.959 3.511   1.00 17.19  ? 466 HOH   A O   1 
HETATM 2439 O O   . HOH   D 4 .   ? 46.892 8.432  9.890   1.00 35.02  ? 467 HOH   A O   1 
HETATM 2440 O O   . HOH   D 4 .   ? 24.136 11.545 19.978  1.00 33.08  ? 468 HOH   A O   1 
HETATM 2441 O O   . HOH   D 4 .   ? 9.007  25.206 11.175  1.00 54.67  ? 469 HOH   A O   1 
HETATM 2442 O O   . HOH   D 4 .   ? 53.055 26.015 17.630  1.00 27.82  ? 470 HOH   A O   1 
HETATM 2443 O O   . HOH   D 4 .   ? 33.549 11.114 32.328  1.00 41.46  ? 471 HOH   A O   1 
HETATM 2444 O O   . HOH   D 4 .   ? 32.892 23.228 -5.633  1.00 24.49  ? 472 HOH   A O   1 
HETATM 2445 O O   . HOH   D 4 .   ? 16.069 20.188 6.901   1.00 27.47  ? 473 HOH   A O   1 
HETATM 2446 O O   . HOH   D 4 .   ? 40.010 25.750 25.923  1.00 14.71  ? 474 HOH   A O   1 
HETATM 2447 O O   . HOH   D 4 .   ? 56.500 30.926 17.745  1.00 28.06  ? 475 HOH   A O   1 
HETATM 2448 O O   . HOH   D 4 .   ? 47.627 29.910 7.875   1.00 19.80  ? 476 HOH   A O   1 
HETATM 2449 O O   . HOH   D 4 .   ? 42.630 25.403 21.962  1.00 13.54  ? 477 HOH   A O   1 
HETATM 2450 O O   . HOH   D 4 .   ? 47.232 31.580 12.404  1.00 15.67  ? 478 HOH   A O   1 
HETATM 2451 O O   . HOH   D 4 .   ? 35.632 31.738 15.173  1.00 48.13  ? 479 HOH   A O   1 
HETATM 2452 O O   . HOH   D 4 .   ? 32.169 4.715  26.980  1.00 38.96  ? 480 HOH   A O   1 
HETATM 2453 O O   . HOH   D 4 .   ? 38.011 32.007 -3.544  1.00 28.36  ? 481 HOH   A O   1 
HETATM 2454 O O   . HOH   D 4 .   ? 20.551 22.228 21.100  1.00 29.46  ? 482 HOH   A O   1 
HETATM 2455 O O   . HOH   D 4 .   ? 15.113 20.183 1.103   1.00 27.16  ? 483 HOH   A O   1 
HETATM 2456 O O   . HOH   D 4 .   ? 31.956 18.157 35.507  1.00 37.49  ? 484 HOH   A O   1 
HETATM 2457 O O   . HOH   D 4 .   ? 27.762 25.178 26.703  1.00 54.60  ? 485 HOH   A O   1 
HETATM 2458 O O   . HOH   D 4 .   ? 13.933 13.001 15.319  1.00 49.81  ? 486 HOH   A O   1 
HETATM 2459 O O   . HOH   D 4 .   ? 44.832 5.396  17.156  1.00 29.13  ? 487 HOH   A O   1 
HETATM 2460 O O   . HOH   D 4 .   ? 10.224 29.415 -4.816  1.00 21.04  ? 488 HOH   A O   1 
HETATM 2461 O O   . HOH   D 4 .   ? 46.526 15.329 13.390  1.00 15.78  ? 489 HOH   A O   1 
HETATM 2462 O O   . HOH   D 4 .   ? 18.560 14.350 16.462  1.00 24.66  ? 490 HOH   A O   1 
HETATM 2463 O O   . HOH   D 4 .   ? 8.698  36.837 0.468   1.00 37.95  ? 491 HOH   A O   1 
HETATM 2464 O O   . HOH   D 4 .   ? 49.855 9.112  20.230  1.00 27.12  ? 492 HOH   A O   1 
HETATM 2465 O O   . HOH   D 4 .   ? 20.726 16.973 3.069   1.00 37.40  ? 493 HOH   A O   1 
HETATM 2466 O O   . HOH   D 4 .   ? 32.614 46.796 4.070   1.00 44.86  ? 494 HOH   A O   1 
HETATM 2467 O O   . HOH   D 4 .   ? 18.107 25.186 15.222  1.00 32.61  ? 495 HOH   A O   1 
HETATM 2468 O O   . HOH   D 4 .   ? 50.162 20.568 8.123   1.00 40.99  ? 496 HOH   A O   1 
HETATM 2469 O O   . HOH   D 4 .   ? 19.944 41.068 1.654   1.00 30.49  ? 497 HOH   A O   1 
HETATM 2470 O O   . HOH   D 4 .   ? 55.937 31.661 14.982  1.00 36.07  ? 498 HOH   A O   1 
HETATM 2471 O O   . HOH   D 4 .   ? 39.006 23.338 13.890  1.00 13.85  ? 499 HOH   A O   1 
HETATM 2472 O O   . HOH   D 4 .   ? 3.966  28.972 -1.451  1.00 33.62  ? 500 HOH   A O   1 
HETATM 2473 O O   . HOH   D 4 .   ? 47.595 23.652 0.796   1.00 31.07  ? 501 HOH   A O   1 
HETATM 2474 O O   . HOH   D 4 .   ? 30.915 43.927 -2.833  1.00 21.08  ? 502 HOH   A O   1 
HETATM 2475 O O   . HOH   D 4 .   ? 32.513 41.095 -0.801  1.00 23.04  ? 503 HOH   A O   1 
HETATM 2476 O O   . HOH   D 4 .   ? 33.174 5.301  24.575  1.00 40.78  ? 504 HOH   A O   1 
HETATM 2477 O O   . HOH   D 4 .   ? 43.284 14.033 9.969   1.00 14.35  ? 505 HOH   A O   1 
HETATM 2478 O O   . HOH   D 4 .   ? 40.041 26.347 -0.337  1.00 31.21  ? 506 HOH   A O   1 
HETATM 2479 O O   . HOH   D 4 .   ? 34.531 12.233 36.406  1.00 29.04  ? 507 HOH   A O   1 
HETATM 2480 O O   . HOH   D 4 .   ? 31.934 22.101 34.724  1.00 49.24  ? 508 HOH   A O   1 
HETATM 2481 O O   . HOH   D 4 .   ? 33.011 24.155 38.632  1.00 40.75  ? 509 HOH   A O   1 
HETATM 2482 O O   . HOH   D 4 .   ? 37.818 32.997 5.577   1.00 43.41  ? 510 HOH   A O   1 
HETATM 2483 O O   . HOH   D 4 .   ? 40.544 4.712  10.755  1.00 25.47  ? 511 HOH   A O   1 
HETATM 2484 O O   . HOH   D 4 .   ? 50.639 11.163 14.249  1.00 36.08  ? 512 HOH   A O   1 
HETATM 2485 O O   . HOH   D 4 .   ? 17.777 8.720  19.780  1.00 45.65  ? 513 HOH   A O   1 
HETATM 2486 O O   . HOH   D 4 .   ? 2.195  26.886 -0.744  1.00 39.58  ? 514 HOH   A O   1 
HETATM 2487 O O   . HOH   D 4 .   ? 40.571 25.970 14.800  1.00 30.54  ? 515 HOH   A O   1 
HETATM 2488 O O   . HOH   D 4 .   ? 34.947 26.941 8.818   1.00 19.18  ? 516 HOH   A O   1 
HETATM 2489 O O   . HOH   D 4 .   ? 49.554 21.272 32.649  1.00 41.44  ? 517 HOH   A O   1 
HETATM 2490 O O   . HOH   D 4 .   ? 52.704 18.647 23.483  1.00 25.18  ? 518 HOH   A O   1 
HETATM 2491 O O   . HOH   D 4 .   ? 38.396 6.286  36.294  1.00 46.54  ? 519 HOH   A O   1 
HETATM 2492 O O   . HOH   D 4 .   ? 57.274 29.658 13.773  1.00 40.69  ? 520 HOH   A O   1 
HETATM 2493 O O   . HOH   D 4 .   ? 32.590 9.226  7.500   1.00 25.95  ? 521 HOH   A O   1 
HETATM 2494 O O   . HOH   D 4 .   ? 47.388 18.673 6.417   1.00 26.12  ? 522 HOH   A O   1 
HETATM 2495 O O   . HOH   D 4 .   ? 43.139 22.936 32.445  1.00 20.49  ? 523 HOH   A O   1 
HETATM 2496 O O   . HOH   D 4 .   ? 30.300 8.296  7.396   1.00 31.50  ? 524 HOH   A O   1 
HETATM 2497 O O   . HOH   D 4 .   ? 50.228 12.883 24.340  1.00 34.13  ? 525 HOH   A O   1 
HETATM 2498 O O   A HOH   D 4 .   ? 34.463 33.765 5.505   0.50 26.67  ? 526 HOH   A O   1 
HETATM 2499 O O   B HOH   D 4 .   ? 33.086 33.236 3.792   0.50 26.37  ? 526 HOH   A O   1 
HETATM 2500 O O   . HOH   D 4 .   ? 26.087 20.807 -0.360  1.00 29.21  ? 527 HOH   A O   1 
HETATM 2501 O O   . HOH   D 4 .   ? 46.839 33.783 10.585  1.00 38.20  ? 528 HOH   A O   1 
HETATM 2502 O O   . HOH   D 4 .   ? 37.901 26.734 32.242  1.00 27.91  ? 529 HOH   A O   1 
HETATM 2503 O O   . HOH   D 4 .   ? 23.870 30.847 -7.737  1.00 25.94  ? 530 HOH   A O   1 
HETATM 2504 O O   . HOH   D 4 .   ? 36.667 31.513 3.185   1.00 27.26  ? 531 HOH   A O   1 
HETATM 2505 O O   . HOH   D 4 .   ? 42.604 18.414 40.278  1.00 22.52  ? 532 HOH   A O   1 
HETATM 2506 O O   . HOH   D 4 .   ? 45.056 7.893  30.582  1.00 33.61  ? 533 HOH   A O   1 
HETATM 2507 O O   . HOH   D 4 .   ? 32.982 37.033 -9.383  1.00 57.43  ? 534 HOH   A O   1 
HETATM 2508 O O   . HOH   D 4 .   ? 54.444 18.133 21.111  1.00 24.89  ? 535 HOH   A O   1 
HETATM 2509 O O   . HOH   D 4 .   ? 48.739 18.124 30.907  1.00 50.62  ? 536 HOH   A O   1 
HETATM 2510 O O   . HOH   D 4 .   ? 31.212 33.503 6.528   1.00 42.80  ? 537 HOH   A O   1 
HETATM 2511 O O   . HOH   D 4 .   ? 16.293 19.484 11.766  1.00 31.94  ? 538 HOH   A O   1 
HETATM 2512 O O   . HOH   D 4 .   ? 39.625 23.140 32.601  1.00 39.51  ? 539 HOH   A O   1 
HETATM 2513 O O   . HOH   D 4 .   ? 49.657 31.569 30.168  1.00 56.95  ? 540 HOH   A O   1 
HETATM 2514 O O   . HOH   D 4 .   ? 38.345 25.861 16.414  1.00 21.82  ? 541 HOH   A O   1 
HETATM 2515 O O   . HOH   D 4 .   ? 40.916 34.262 10.125  1.00 26.01  ? 542 HOH   A O   1 
HETATM 2516 O O   . HOH   D 4 .   ? 30.399 8.465  32.080  1.00 48.54  ? 543 HOH   A O   1 
HETATM 2517 O O   . HOH   D 4 .   ? 21.848 28.607 -6.576  1.00 39.40  ? 544 HOH   A O   1 
HETATM 2518 O O   . HOH   D 4 .   ? 45.891 4.418  14.932  1.00 29.29  ? 545 HOH   A O   1 
HETATM 2519 O O   . HOH   D 4 .   ? 42.730 24.504 15.551  1.00 16.57  ? 546 HOH   A O   1 
HETATM 2520 O O   . HOH   D 4 .   ? 32.688 8.846  33.243  1.00 35.73  ? 547 HOH   A O   1 
HETATM 2521 O O   . HOH   D 4 .   ? 13.106 36.012 15.211  1.00 22.44  ? 548 HOH   A O   1 
HETATM 2522 O O   . HOH   D 4 .   ? 55.603 28.923 20.842  1.00 48.64  ? 549 HOH   A O   1 
HETATM 2523 O O   . HOH   D 4 .   ? 10.453 21.283 4.964   1.00 33.10  ? 550 HOH   A O   1 
HETATM 2524 O O   . HOH   D 4 .   ? 14.655 19.801 18.247  1.00 43.77  ? 551 HOH   A O   1 
HETATM 2525 O O   . HOH   D 4 .   ? 23.053 13.630 10.666  1.00 46.62  ? 552 HOH   A O   1 
HETATM 2526 O O   . HOH   D 4 .   ? 10.618 36.829 2.968   1.00 51.93  ? 553 HOH   A O   1 
HETATM 2527 O O   . HOH   D 4 .   ? 9.622  30.998 11.517  1.00 29.32  ? 554 HOH   A O   1 
HETATM 2528 O O   . HOH   D 4 .   ? 46.217 16.142 34.174  1.00 32.17  ? 555 HOH   A O   1 
HETATM 2529 O O   . HOH   D 4 .   ? 35.929 39.171 6.820   1.00 40.44  ? 556 HOH   A O   1 
HETATM 2530 O O   . HOH   D 4 .   ? 32.217 30.057 -5.369  1.00 24.84  ? 557 HOH   A O   1 
HETATM 2531 O O   . HOH   D 4 .   ? 28.514 39.257 -8.898  1.00 22.38  ? 558 HOH   A O   1 
HETATM 2532 O O   . HOH   D 4 .   ? 43.007 16.801 43.404  1.00 54.34  ? 559 HOH   A O   1 
HETATM 2533 O O   . HOH   D 4 .   ? 52.473 10.465 16.649  1.00 54.74  ? 560 HOH   A O   1 
HETATM 2534 O O   . HOH   D 4 .   ? 43.030 12.727 5.129   1.00 39.71  ? 561 HOH   A O   1 
HETATM 2535 O O   . HOH   D 4 .   ? 24.547 11.649 22.874  1.00 29.56  ? 562 HOH   A O   1 
HETATM 2536 O O   . HOH   D 4 .   ? 37.984 31.985 23.475  1.00 25.18  ? 563 HOH   A O   1 
HETATM 2537 O O   . HOH   D 4 .   ? 37.986 -0.707 21.152  1.00 50.15  ? 564 HOH   A O   1 
HETATM 2538 O O   . HOH   D 4 .   ? 50.057 32.593 9.072   1.00 42.55  ? 565 HOH   A O   1 
HETATM 2539 O O   . HOH   D 4 .   ? 40.496 39.955 5.322   1.00 47.10  ? 566 HOH   A O   1 
HETATM 2540 O O   . HOH   D 4 .   ? 39.657 2.996  30.314  1.00 23.95  ? 567 HOH   A O   1 
HETATM 2541 O O   . HOH   D 4 .   ? 35.365 26.651 31.589  1.00 28.83  ? 568 HOH   A O   1 
HETATM 2542 O O   . HOH   D 4 .   ? 43.876 10.247 8.842   1.00 21.48  ? 569 HOH   A O   1 
HETATM 2543 O O   . HOH   D 4 .   ? 38.081 39.468 -2.708  1.00 23.73  ? 570 HOH   A O   1 
HETATM 2544 O O   . HOH   D 4 .   ? 52.642 30.978 25.896  1.00 40.71  ? 571 HOH   A O   1 
HETATM 2545 O O   . HOH   D 4 .   ? 24.104 39.963 7.033   1.00 46.20  ? 572 HOH   A O   1 
HETATM 2546 O O   . HOH   D 4 .   ? 43.931 42.989 21.604  1.00 30.60  ? 573 HOH   A O   1 
HETATM 2547 O O   . HOH   D 4 .   ? 18.470 18.564 9.508   1.00 66.16  ? 574 HOH   A O   1 
HETATM 2548 O O   A HOH   D 4 .   ? 17.961 39.265 -2.610  0.50 29.73  ? 575 HOH   A O   1 
HETATM 2549 O O   B HOH   D 4 .   ? 19.281 38.086 -4.345  0.50 22.53  ? 575 HOH   A O   1 
HETATM 2550 O O   . HOH   D 4 .   ? 26.733 28.064 7.576   1.00 44.58  ? 576 HOH   A O   1 
HETATM 2551 O O   . HOH   D 4 .   ? 31.083 40.894 -3.333  1.00 26.11  ? 577 HOH   A O   1 
HETATM 2552 O O   . HOH   D 4 .   ? 53.199 23.931 11.791  1.00 44.29  ? 578 HOH   A O   1 
HETATM 2553 O O   . HOH   D 4 .   ? 18.082 29.495 17.276  1.00 50.30  ? 579 HOH   A O   1 
HETATM 2554 O O   . HOH   D 4 .   ? 9.473  30.031 8.510   1.00 41.33  ? 580 HOH   A O   1 
HETATM 2555 O O   . HOH   D 4 .   ? 36.763 35.513 19.773  1.00 47.44  ? 581 HOH   A O   1 
HETATM 2556 O O   . HOH   D 4 .   ? 29.414 20.193 28.206  1.00 50.04  ? 582 HOH   A O   1 
HETATM 2557 O O   . HOH   D 4 .   ? 22.256 35.400 17.461  1.00 33.66  ? 583 HOH   A O   1 
HETATM 2558 O O   . HOH   D 4 .   ? 46.276 3.100  25.059  1.00 19.76  ? 584 HOH   A O   1 
HETATM 2559 O O   . HOH   D 4 .   ? 21.842 14.134 5.251   1.00 53.57  ? 585 HOH   A O   1 
HETATM 2560 O O   . HOH   D 4 .   ? 7.942  20.946 4.189   1.00 43.00  ? 586 HOH   A O   1 
HETATM 2561 O O   . HOH   D 4 .   ? 50.490 19.245 29.246  1.00 64.14  ? 587 HOH   A O   1 
HETATM 2562 O O   . HOH   D 4 .   ? 12.295 31.010 -11.964 1.00 55.52  ? 588 HOH   A O   1 
HETATM 2563 O O   . HOH   D 4 .   ? 45.519 4.239  22.534  1.00 22.53  ? 589 HOH   A O   1 
HETATM 2564 O O   . HOH   D 4 .   ? 32.021 42.119 9.586   1.00 56.99  ? 590 HOH   A O   1 
HETATM 2565 O O   . HOH   D 4 .   ? 25.302 8.039  12.550  1.00 48.34  ? 591 HOH   A O   1 
HETATM 2566 O O   . HOH   D 4 .   ? 22.863 12.850 24.689  1.00 41.63  ? 592 HOH   A O   1 
HETATM 2567 O O   . HOH   D 4 .   ? 31.426 39.007 -8.848  1.00 43.57  ? 593 HOH   A O   1 
HETATM 2568 O O   . HOH   D 4 .   ? 36.603 3.354  27.989  1.00 47.23  ? 594 HOH   A O   1 
HETATM 2569 O O   . HOH   D 4 .   ? 38.139 35.154 27.970  1.00 53.68  ? 595 HOH   A O   1 
HETATM 2570 O O   . HOH   D 4 .   ? 47.552 15.021 8.962   1.00 32.56  ? 596 HOH   A O   1 
HETATM 2571 O O   . HOH   D 4 .   ? 49.114 31.590 0.922   1.00 60.57  ? 597 HOH   A O   1 
HETATM 2572 O O   . HOH   D 4 .   ? 30.866 35.402 17.145  1.00 56.96  ? 598 HOH   A O   1 
HETATM 2573 O O   . HOH   D 4 .   ? 33.397 24.687 34.445  1.00 56.44  ? 599 HOH   A O   1 
HETATM 2574 O O   . HOH   D 4 .   ? 45.493 15.357 10.795  1.00 15.40  ? 600 HOH   A O   1 
HETATM 2575 O O   . HOH   D 4 .   ? 23.593 14.261 3.109   1.00 30.58  ? 601 HOH   A O   1 
HETATM 2576 O O   . HOH   D 4 .   ? 39.020 5.027  8.595   1.00 59.38  ? 602 HOH   A O   1 
HETATM 2577 O O   . HOH   D 4 .   ? 39.173 -3.751 18.232  1.00 52.86  ? 603 HOH   A O   1 
HETATM 2578 O O   . HOH   D 4 .   ? 35.206 4.143  11.503  1.00 59.14  ? 604 HOH   A O   1 
HETATM 2579 O O   . HOH   D 4 .   ? 19.550 21.631 1.148   1.00 35.09  ? 605 HOH   A O   1 
HETATM 2580 O O   . HOH   D 4 .   ? 31.217 34.498 14.929  1.00 45.31  ? 606 HOH   A O   1 
HETATM 2581 O O   . HOH   D 4 .   ? 7.306  35.447 10.033  1.00 25.68  ? 607 HOH   A O   1 
HETATM 2582 O O   . HOH   D 4 .   ? 49.824 13.922 10.425  1.00 38.59  ? 608 HOH   A O   1 
HETATM 2583 O O   . HOH   D 4 .   ? 8.530  30.398 -6.735  1.00 31.47  ? 609 HOH   A O   1 
HETATM 2584 O O   . HOH   D 4 .   ? 31.755 21.074 -6.692  1.00 39.46  ? 610 HOH   A O   1 
HETATM 2585 O O   . HOH   D 4 .   ? 50.277 9.859  11.780  1.00 49.56  ? 611 HOH   A O   1 
HETATM 2586 O O   . HOH   D 4 .   ? 23.945 8.827  23.870  1.00 53.42  ? 612 HOH   A O   1 
HETATM 2587 O O   . HOH   D 4 .   ? 7.540  33.066 11.347  1.00 22.55  ? 613 HOH   A O   1 
HETATM 2588 O O   . HOH   D 4 .   ? 34.051 32.604 22.318  1.00 53.98  ? 614 HOH   A O   1 
HETATM 2589 O O   . HOH   D 4 .   ? 18.863 20.720 -1.168  1.00 53.31  ? 615 HOH   A O   1 
HETATM 2590 O O   . HOH   D 4 .   ? 40.607 39.353 -1.854  1.00 37.17  ? 616 HOH   A O   1 
HETATM 2591 O O   . HOH   D 4 .   ? 30.198 35.658 7.629   1.00 43.36  ? 617 HOH   A O   1 
HETATM 2592 O O   . HOH   D 4 .   ? 17.026 12.922 15.022  1.00 53.31  ? 618 HOH   A O   1 
HETATM 2593 O O   . HOH   D 4 .   ? 12.234 24.456 12.636  1.00 56.24  ? 619 HOH   A O   1 
HETATM 2594 O O   . HOH   D 4 .   ? 36.802 34.284 22.384  1.00 54.51  ? 620 HOH   A O   1 
HETATM 2595 O O   . HOH   D 4 .   ? 17.535 20.569 2.752   1.00 30.39  ? 621 HOH   A O   1 
HETATM 2596 O O   . HOH   D 4 .   ? 44.160 12.677 7.727   1.00 21.00  ? 622 HOH   A O   1 
HETATM 2597 O O   . HOH   D 4 .   ? 45.277 2.550  13.309  1.00 38.60  ? 623 HOH   A O   1 
HETATM 2598 O O   . HOH   D 4 .   ? 45.377 4.165  19.643  1.00 22.19  ? 624 HOH   A O   1 
HETATM 2599 O O   . HOH   D 4 .   ? 3.595  31.941 -2.283  1.00 52.91  ? 625 HOH   A O   1 
HETATM 2600 O O   . HOH   D 4 .   ? 54.335 20.576 24.690  1.00 45.14  ? 626 HOH   A O   1 
HETATM 2601 O O   . HOH   D 4 .   ? 9.343  29.517 -9.086  1.00 39.15  ? 627 HOH   A O   1 
HETATM 2602 O O   . HOH   D 4 .   ? 29.189 9.862  34.232  1.00 48.30  ? 628 HOH   A O   1 
HETATM 2603 O O   . HOH   D 4 .   ? 36.116 35.780 24.437  1.00 57.25  ? 629 HOH   A O   1 
HETATM 2604 O O   . HOH   D 4 .   ? 46.775 13.357 7.168   1.00 44.08  ? 630 HOH   A O   1 
HETATM 2605 O O   . HOH   D 4 .   ? 17.166 12.696 12.396  1.00 49.17  ? 631 HOH   A O   1 
HETATM 2606 O O   . HOH   D 4 .   ? 45.479 4.383  34.524  1.00 30.97  ? 632 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   . THR   A 1   ? 0.3389 0.4331 0.3840 0.0323  -0.0787 -0.0898 2   THR   A N   
2    C CA  . THR   A 1   ? 0.3437 0.3811 0.3625 0.0780  -0.0870 -0.0623 2   THR   A CA  
3    C C   . THR   A 1   ? 0.3063 0.3189 0.2639 0.0739  -0.0718 -0.0858 2   THR   A C   
4    O O   . THR   A 1   ? 0.4154 0.3750 0.2535 0.0953  -0.0674 -0.1129 2   THR   A O   
5    C CB  . THR   A 1   ? 0.5038 0.3987 0.4436 0.1060  -0.0359 -0.0441 2   THR   A CB  
6    O OG1 . THR   A 1   ? 0.5959 0.4347 0.4804 0.1030  -0.0109 -0.0434 2   THR   A OG1 
7    C CG2 . THR   A 1   ? 0.5496 0.3769 0.4557 0.1018  -0.0385 -0.0407 2   THR   A CG2 
15   N N   . PHE   A 3   ? 0.2501 0.2049 0.1684 -0.0214 -0.0084 0.0483  4   PHE   A N   
16   C CA  . PHE   A 3   ? 0.2581 0.2126 0.1667 -0.0094 -0.0040 0.0521  4   PHE   A CA  
17   C C   . PHE   A 3   ? 0.2631 0.2062 0.1927 -0.0101 -0.0027 0.0331  4   PHE   A C   
18   O O   . PHE   A 3   ? 0.2749 0.2301 0.1453 -0.0074 -0.0087 0.0452  4   PHE   A O   
19   C CB  . PHE   A 3   ? 0.2612 0.2456 0.1771 0.0031  -0.0089 0.0509  4   PHE   A CB  
20   C CG  . PHE   A 3   ? 0.2673 0.2828 0.1806 0.0378  0.0124  0.0903  4   PHE   A CG  
21   C CD1 . PHE   A 3   ? 0.2805 0.3160 0.2077 0.0554  0.0190  0.1113  4   PHE   A CD1 
22   C CD2 . PHE   A 3   ? 0.2538 0.3134 0.2091 0.0127  -0.0171 0.0911  4   PHE   A CD2 
23   C CE1 . PHE   A 3   ? 0.2614 0.3456 0.2145 0.0521  0.0131  0.0967  4   PHE   A CE1 
24   C CE2 . PHE   A 3   ? 0.2896 0.3235 0.2339 0.0067  -0.0062 0.1126  4   PHE   A CE2 
25   C CZ  . PHE   A 3   ? 0.2735 0.3494 0.2284 0.0133  0.0075  0.1091  4   PHE   A CZ  
26   N N   . ARG   A 4   ? 0.2523 0.2228 0.2326 -0.0129 -0.0260 0.0382  5   ARG   A N   
27   C CA  . ARG   A 4   ? 0.2365 0.2032 0.2238 -0.0010 -0.0253 0.0325  5   ARG   A CA  
28   C C   . ARG   A 4   ? 0.2363 0.1874 0.1655 -0.0058 -0.0205 0.0431  5   ARG   A C   
29   O O   . ARG   A 4   ? 0.3245 0.2118 0.1557 -0.0110 -0.0225 0.0323  5   ARG   A O   
30   C CB  . ARG   A 4   ? 0.2634 0.2374 0.2718 -0.0201 -0.0355 0.0291  5   ARG   A CB  
31   C CG  . ARG   A 4   ? 0.3310 0.2841 0.2982 -0.0288 -0.0409 0.0301  5   ARG   A CG  
32   C CD  . ARG   A 4   ? 0.3733 0.3085 0.3215 -0.0680 -0.0754 0.0424  5   ARG   A CD  
33   N NE  . ARG   A 4   ? 0.4217 0.3280 0.3525 -0.0732 -0.0762 0.0198  5   ARG   A NE  
34   C CZ  . ARG   A 4   ? 0.4723 0.3338 0.3587 -0.0359 -0.0984 -0.0122 5   ARG   A CZ  
35   N NH1 . ARG   A 4   ? 0.4946 0.3320 0.3472 -0.0462 -0.0872 -0.0167 5   ARG   A NH1 
36   N NH2 . ARG   A 4   ? 0.4859 0.3374 0.3769 0.0034  -0.0942 -0.0269 5   ARG   A NH2 
37   N N   . GLN   A 5   ? 0.2427 0.1776 0.1656 -0.0027 -0.0038 0.0214  6   GLN   A N   
38   C CA  . GLN   A 5   ? 0.2727 0.1824 0.1874 -0.0193 0.0262  0.0475  6   GLN   A CA  
39   C C   . GLN   A 5   ? 0.2796 0.1992 0.2415 0.0130  -0.0023 0.0617  6   GLN   A C   
40   O O   . GLN   A 5   ? 0.3075 0.2125 0.2624 0.0118  0.0021  0.0521  6   GLN   A O   
41   C CB  . GLN   A 5   ? 0.3044 0.2127 0.2127 0.0000  -0.0017 0.0323  6   GLN   A CB  
42   C CG  . GLN   A 5   ? 0.2787 0.2364 0.2065 -0.0108 -0.0107 0.0295  6   GLN   A CG  
43   C CD  . GLN   A 5   ? 0.2969 0.2212 0.2133 -0.0225 0.0055  0.0481  6   GLN   A CD  
44   O OE1 . GLN   A 5   ? 0.3466 0.2714 0.2454 -0.0066 -0.0113 0.0730  6   GLN   A OE1 
45   N NE2 . GLN   A 5   ? 0.2886 0.2311 0.2249 -0.0214 0.0200  0.0181  6   GLN   A NE2 
46   N N   . GLU   A 6   ? 0.2490 0.2327 0.2709 -0.0045 0.0169  0.0624  7   GLU   A N   
47   C CA  . GLU   A 6   ? 0.2532 0.2769 0.2920 0.0061  0.0350  0.0637  7   GLU   A CA  
48   C C   . GLU   A 6   ? 0.2812 0.2687 0.2826 0.0216  0.0263  0.0696  7   GLU   A C   
49   O O   . GLU   A 6   ? 0.3048 0.2645 0.2861 0.0456  0.0297  0.0848  7   GLU   A O   
50   C CB  . GLU   A 6   ? 0.3041 0.3087 0.3379 0.0185  0.0140  0.0275  7   GLU   A CB  
51   C CG  . GLU   A 6   ? 0.4049 0.3800 0.4017 0.0256  0.0497  -0.0149 7   GLU   A CG  
52   C CD  . GLU   A 6   ? 0.5294 0.4614 0.4732 0.0129  0.0487  -0.0197 7   GLU   A CD  
53   O OE1 . GLU   A 6   ? 0.5586 0.4949 0.4891 -0.0185 0.0159  -0.0339 7   GLU   A OE1 
54   O OE2 . GLU   A 6   ? 0.5600 0.4633 0.5001 0.0209  0.0717  -0.0283 7   GLU   A OE2 
55   N N   . ASN   A 7   ? 0.2953 0.2811 0.3031 0.0094  0.0356  0.0792  8   ASN   A N   
56   C CA  . ASN   A 7   ? 0.3040 0.2697 0.3212 0.0215  0.0492  0.0688  8   ASN   A CA  
57   C C   . ASN   A 7   ? 0.2888 0.2355 0.2814 0.0189  0.0172  0.0380  8   ASN   A C   
58   O O   . ASN   A 7   ? 0.2790 0.2193 0.2673 -0.0051 0.0259  0.0322  8   ASN   A O   
59   C CB  . ASN   A 7   ? 0.3626 0.2917 0.3806 0.0526  0.0540  0.0871  8   ASN   A CB  
60   C CG  . ASN   A 7   ? 0.4320 0.3281 0.4323 0.0379  0.0494  0.0905  8   ASN   A CG  
61   O OD1 . ASN   A 7   ? 0.4403 0.3295 0.4523 -0.0068 0.0420  0.0834  8   ASN   A OD1 
62   N ND2 . ASN   A 7   ? 0.4713 0.3758 0.4727 0.0587  0.0475  0.0556  8   ASN   A ND2 
63   N N   . VAL   A 8   ? 0.2887 0.2252 0.2753 0.0098  0.0287  0.0329  9   VAL   A N   
64   C CA  . VAL   A 8   ? 0.2888 0.2131 0.2674 0.0009  0.0051  0.0128  9   VAL   A CA  
65   C C   . VAL   A 8   ? 0.3039 0.2122 0.2532 -0.0057 0.0223  0.0223  9   VAL   A C   
66   O O   . VAL   A 8   ? 0.3134 0.2060 0.2154 -0.0238 0.0219  0.0114  9   VAL   A O   
67   C CB  . VAL   A 8   ? 0.4099 0.2368 0.2909 -0.0168 -0.0036 0.0305  9   VAL   A CB  
68   C CG1 . VAL   A 8   ? 0.3863 0.2646 0.2923 0.0379  0.0441  0.0154  9   VAL   A CG1 
69   C CG2 . VAL   A 8   ? 0.4338 0.2412 0.3216 -0.0043 -0.0192 0.0406  9   VAL   A CG2 
70   N N   . ASP   A 9   ? 0.2841 0.2254 0.2752 -0.0002 0.0197  0.0179  10  ASP   A N   
71   C CA  . ASP   A 9   ? 0.3417 0.2582 0.3174 0.0123  0.0666  0.0020  10  ASP   A CA  
72   C C   . ASP   A 9   ? 0.2965 0.2464 0.3277 0.0450  0.0366  0.0324  10  ASP   A C   
73   O O   . ASP   A 9   ? 0.3029 0.2728 0.3500 0.0493  0.0410  0.0199  10  ASP   A O   
74   C CB  . ASP   A 9   ? 0.4589 0.3724 0.3907 0.0122  0.0924  -0.0101 10  ASP   A CB  
75   C CG  . ASP   A 9   ? 0.6303 0.4953 0.4518 -0.0416 0.0752  -0.0091 10  ASP   A CG  
76   O OD1 . ASP   A 9   ? 0.6923 0.5359 0.4846 -0.0587 0.0625  -0.0237 10  ASP   A OD1 
77   O OD2 . ASP   A 9   ? 0.6925 0.5299 0.4880 -0.0628 0.0609  -0.0028 10  ASP   A OD2 
78   N N   . ASP   A 10  ? 0.3242 0.2183 0.3054 0.0632  0.0042  0.0425  11  ASP   A N   
79   C CA  . ASP   A 10  ? 0.3355 0.2483 0.2906 0.0162  -0.0012 0.0761  11  ASP   A CA  
80   C C   . ASP   A 10  ? 0.2851 0.2390 0.2647 0.0328  0.0056  0.0527  11  ASP   A C   
81   O O   . ASP   A 10  ? 0.2981 0.2596 0.3026 0.0197  -0.0200 0.0538  11  ASP   A O   
82   C CB  . ASP   A 10  ? 0.4528 0.3062 0.3169 0.0057  -0.0582 0.1163  11  ASP   A CB  
83   C CG  . ASP   A 10  ? 0.5713 0.3971 0.3743 0.0085  -0.0995 0.1246  11  ASP   A CG  
84   O OD1 . ASP   A 10  ? 0.6647 0.3916 0.3979 0.0311  -0.1192 0.1227  11  ASP   A OD1 
85   O OD2 . ASP   A 10  ? 0.5829 0.4283 0.4121 -0.0166 -0.1328 0.1358  11  ASP   A OD2 
86   N N   . TYR   A 11  ? 0.2627 0.2271 0.2142 0.0305  0.0265  0.0622  12  TYR   A N   
87   C CA  . TYR   A 11  ? 0.2508 0.2164 0.1908 0.0170  0.0168  0.0256  12  TYR   A CA  
88   C C   . TYR   A 11  ? 0.2537 0.2020 0.1917 0.0057  0.0144  0.0011  12  TYR   A C   
89   O O   . TYR   A 11  ? 0.2488 0.2212 0.1947 0.0148  -0.0117 0.0098  12  TYR   A O   
90   C CB  . TYR   A 11  ? 0.2517 0.2511 0.1926 0.0208  0.0145  0.0434  12  TYR   A CB  
91   C CG  . TYR   A 11  ? 0.2719 0.2777 0.2087 -0.0219 -0.0021 0.0619  12  TYR   A CG  
92   C CD1 . TYR   A 11  ? 0.3831 0.3314 0.2137 -0.0293 0.0084  0.0557  12  TYR   A CD1 
93   C CD2 . TYR   A 11  ? 0.2978 0.3192 0.2339 -0.0357 0.0383  0.0551  12  TYR   A CD2 
94   C CE1 . TYR   A 11  ? 0.4415 0.3605 0.2315 -0.0253 0.0281  0.0574  12  TYR   A CE1 
95   C CE2 . TYR   A 11  ? 0.3769 0.3520 0.2416 -0.0345 0.0370  0.0665  12  TYR   A CE2 
96   C CZ  . TYR   A 11  ? 0.4389 0.3739 0.2240 -0.0327 0.0444  0.0819  12  TYR   A CZ  
97   O OH  . TYR   A 11  ? 0.5297 0.4302 0.2385 -0.0276 0.0473  0.0947  12  TYR   A OH  
98   N N   . TYR   A 12  ? 0.2621 0.1869 0.1853 0.0201  0.0176  -0.0003 13  TYR   A N   
99   C CA  . TYR   A 12  ? 0.2505 0.1937 0.1721 0.0163  0.0187  0.0107  13  TYR   A CA  
100  C C   . TYR   A 12  ? 0.2850 0.1939 0.1964 0.0329  0.0296  0.0146  13  TYR   A C   
101  O O   . TYR   A 12  ? 0.3581 0.1988 0.2250 0.0340  0.0384  0.0133  13  TYR   A O   
102  C CB  . TYR   A 12  ? 0.2288 0.2234 0.1687 -0.0033 -0.0073 0.0014  13  TYR   A CB  
103  C CG  . TYR   A 12  ? 0.2060 0.1989 0.1607 0.0160  0.0140  0.0154  13  TYR   A CG  
104  C CD1 . TYR   A 12  ? 0.2194 0.2108 0.1531 -0.0005 0.0118  0.0066  13  TYR   A CD1 
105  C CD2 . TYR   A 12  ? 0.2060 0.2205 0.1835 0.0089  -0.0133 0.0078  13  TYR   A CD2 
106  C CE1 . TYR   A 12  ? 0.2227 0.2148 0.1692 0.0260  -0.0167 -0.0001 13  TYR   A CE1 
107  C CE2 . TYR   A 12  ? 0.1671 0.2282 0.1882 0.0110  0.0091  0.0039  13  TYR   A CE2 
108  C CZ  . TYR   A 12  ? 0.1825 0.2156 0.1805 0.0229  0.0090  0.0029  13  TYR   A CZ  
109  O OH  . TYR   A 12  ? 0.2371 0.2482 0.2042 0.0317  -0.0031 -0.0126 13  TYR   A OH  
110  N N   . ASP   A 13  ? 0.2494 0.2052 0.1947 0.0329  0.0233  0.0069  14  ASP   A N   
111  C CA  . ASP   A 13  ? 0.2542 0.1916 0.2141 0.0482  0.0126  0.0023  14  ASP   A CA  
112  C C   . ASP   A 13  ? 0.2733 0.1786 0.2068 0.0263  -0.0159 0.0020  14  ASP   A C   
113  O O   . ASP   A 13  ? 0.3277 0.1856 0.2369 0.0260  -0.0448 0.0043  14  ASP   A O   
114  C CB  . ASP   A 13  ? 0.2307 0.2350 0.2468 0.0561  -0.0100 -0.0133 14  ASP   A CB  
115  C CG  . ASP   A 13  ? 0.3036 0.2469 0.2979 0.0770  -0.0018 0.0027  14  ASP   A CG  
116  O OD1 . ASP   A 13  ? 0.3762 0.2499 0.3399 0.0500  -0.0171 0.0308  14  ASP   A OD1 
117  O OD2 . ASP   A 13  ? 0.2981 0.2606 0.2985 0.0524  0.0100  0.0078  14  ASP   A OD2 
118  N N   . THR   A 14  ? 0.3172 0.1716 0.2201 0.0389  -0.0103 0.0239  15  THR   A N   
119  C CA  . THR   A 14  ? 0.2926 0.2001 0.2203 0.0120  0.0212  -0.0180 15  THR   A CA  
120  C C   . THR   A 14  ? 0.2811 0.2083 0.2347 0.0303  0.0570  -0.0359 15  THR   A C   
121  O O   . THR   A 14  ? 0.3073 0.2400 0.2750 0.0381  0.0380  -0.0293 15  THR   A O   
122  C CB  . THR   A 14  ? 0.3608 0.2373 0.2685 -0.0089 0.0472  -0.0197 15  THR   A CB  
123  O OG1 . THR   A 14  ? 0.4060 0.2405 0.2839 -0.0229 0.0053  -0.0078 15  THR   A OG1 
124  C CG2 . THR   A 14  ? 0.3809 0.2789 0.2905 -0.0459 0.0554  -0.0069 15  THR   A CG2 
125  N N   . GLY   A 15  ? 0.2550 0.2195 0.2017 0.0238  0.0367  -0.0219 16  GLY   A N   
126  C CA  . GLY   A 15  ? 0.2959 0.2418 0.1954 0.0132  0.0438  -0.0201 16  GLY   A CA  
127  C C   . GLY   A 15  ? 0.2927 0.2196 0.1995 0.0061  0.0240  -0.0280 16  GLY   A C   
128  O O   . GLY   A 15  ? 0.3308 0.2302 0.2131 -0.0182 0.0342  -0.0387 16  GLY   A O   
129  N N   . GLU   A 16  ? 0.2705 0.2253 0.1965 0.0138  0.0379  -0.0317 17  GLU   A N   
130  C CA  . GLU   A 16  ? 0.2535 0.2220 0.2039 0.0245  0.0514  -0.0286 17  GLU   A CA  
131  C C   . GLU   A 16  ? 0.2582 0.1929 0.2002 0.0008  0.0450  -0.0508 17  GLU   A C   
132  O O   . GLU   A 16  ? 0.2627 0.2155 0.2027 -0.0057 0.0681  -0.0767 17  GLU   A O   
133  C CB  . GLU   A 16  ? 0.3142 0.2704 0.2308 -0.0396 0.0535  0.0022  17  GLU   A CB  
134  C CG  . GLU   A 16  ? 0.4250 0.3076 0.2794 -0.0200 0.0678  0.0029  17  GLU   A CG  
135  C CD  . GLU   A 16  ? 0.5188 0.3282 0.2943 -0.0121 0.0775  0.0202  17  GLU   A CD  
136  O OE1 . GLU   A 16  ? 0.4987 0.3069 0.2918 -0.0007 0.0632  0.0274  17  GLU   A OE1 
137  O OE2 . GLU   A 16  ? 0.5914 0.3608 0.2905 0.0111  0.0787  0.0014  17  GLU   A OE2 
138  N N   . GLU   A 17  ? 0.2622 0.1967 0.1838 -0.0201 0.0341  -0.0546 18  GLU   A N   
139  C CA  . GLU   A 17  ? 0.2672 0.2149 0.1999 -0.0217 0.0161  -0.0541 18  GLU   A CA  
140  C C   . GLU   A 17  ? 0.2876 0.2462 0.1820 0.0080  0.0223  -0.0081 18  GLU   A C   
141  O O   . GLU   A 17  ? 0.3490 0.3408 0.2034 0.0714  0.0645  0.0082  18  GLU   A O   
142  C CB  . GLU   A 17  ? 0.3294 0.2076 0.2484 -0.0528 0.0379  -0.0781 18  GLU   A CB  
143  C CG  . GLU   A 17  ? 0.3779 0.2312 0.2760 -0.0690 0.0677  -0.0754 18  GLU   A CG  
144  C CD  . GLU   A 17  ? 0.4359 0.3021 0.2904 -0.0748 0.0759  -0.0509 18  GLU   A CD  
145  O OE1 . GLU   A 17  ? 0.4046 0.2653 0.2827 -0.0293 0.0962  -0.0645 18  GLU   A OE1 
146  O OE2 . GLU   A 17  ? 0.5114 0.3504 0.3039 -0.1059 0.0469  -0.0551 18  GLU   A OE2 
147  N N   . LEU   A 18  ? 0.2907 0.2150 0.1909 0.0117  0.0035  0.0136  19  LEU   A N   
148  C CA  . LEU   A 18  ? 0.3218 0.2260 0.2520 0.0230  -0.0109 0.0138  19  LEU   A CA  
149  C C   . LEU   A 18  ? 0.3677 0.2472 0.2793 0.0063  -0.0570 0.0056  19  LEU   A C   
150  O O   . LEU   A 18  ? 0.3655 0.2489 0.2855 -0.0207 -0.0429 0.0052  19  LEU   A O   
151  C CB  . LEU   A 18  ? 0.3215 0.2329 0.2875 0.0201  0.0022  -0.0004 19  LEU   A CB  
152  C CG  . LEU   A 18  ? 0.3369 0.2523 0.3189 -0.0158 0.0336  -0.0173 19  LEU   A CG  
153  C CD1 . LEU   A 18  ? 0.3763 0.2285 0.3397 0.0028  0.0222  -0.0384 19  LEU   A CD1 
154  C CD2 . LEU   A 18  ? 0.3627 0.2734 0.3330 -0.0427 0.0627  -0.0078 19  LEU   A CD2 
155  N N   . GLY   A 19  ? 0.3872 0.2723 0.3081 0.0302  -0.0826 0.0052  20  GLY   A N   
156  C CA  . GLY   A 19  ? 0.4221 0.3399 0.3611 0.0031  -0.1023 -0.0009 20  GLY   A CA  
157  C C   . GLY   A 19  ? 0.4303 0.4011 0.4044 -0.0027 -0.1181 -0.0006 20  GLY   A C   
158  O O   . GLY   A 19  ? 0.4126 0.4091 0.4164 0.0260  -0.0931 -0.0344 20  GLY   A O   
159  N N   . SER   A 20  ? 0.4630 0.4510 0.4422 -0.0330 -0.1409 0.0371  21  SER   A N   
160  C CA  . SER   A 20  ? 0.5055 0.4846 0.4730 -0.0712 -0.1686 0.0748  21  SER   A CA  
161  C C   . SER   A 20  ? 0.5510 0.4940 0.5021 -0.0905 -0.1885 0.0944  21  SER   A C   
162  O O   . SER   A 20  ? 0.5532 0.4691 0.5080 -0.0820 -0.1784 0.1079  21  SER   A O   
163  C CB  . SER   A 20  ? 0.5079 0.4990 0.4771 -0.0691 -0.1599 0.0903  21  SER   A CB  
164  O OG  . SER   A 20  ? 0.4954 0.5110 0.4795 -0.0504 -0.1517 0.1009  21  SER   A OG  
165  N N   . GLY   A 21  ? 0.5861 0.5217 0.5258 -0.1502 -0.1938 0.0844  22  GLY   A N   
166  C CA  . GLY   A 21  ? 0.6201 0.5665 0.5349 -0.1828 -0.2198 0.0550  22  GLY   A CA  
167  C C   . GLY   A 21  ? 0.6745 0.6101 0.5454 -0.1958 -0.2221 0.0326  22  GLY   A C   
168  O O   . GLY   A 21  ? 0.6752 0.5976 0.5365 -0.2071 -0.2267 0.0284  22  GLY   A O   
169  N N   . GLN   A 22  ? 0.7004 0.6736 0.5555 -0.1853 -0.2449 0.0178  23  GLN   A N   
170  C CA  . GLN   A 22  ? 0.7134 0.7443 0.5723 -0.1664 -0.2537 0.0010  23  GLN   A CA  
171  C C   . GLN   A 22  ? 0.7310 0.7611 0.5547 -0.1391 -0.2674 0.0109  23  GLN   A C   
172  O O   . GLN   A 22  ? 0.7673 0.7703 0.5585 -0.1241 -0.2658 0.0047  23  GLN   A O   
173  C CB  . GLN   A 22  ? 0.7005 0.7885 0.6021 -0.1868 -0.2416 -0.0225 23  GLN   A CB  
174  C CG  . GLN   A 22  ? 0.6917 0.8333 0.6302 -0.1946 -0.2231 -0.0351 23  GLN   A CG  
175  C CD  . GLN   A 22  ? 0.6745 0.8663 0.6465 -0.2118 -0.2140 -0.0418 23  GLN   A CD  
176  O OE1 . GLN   A 22  ? 0.6763 0.8749 0.6533 -0.2219 -0.2131 -0.0466 23  GLN   A OE1 
177  N NE2 . GLN   A 22  ? 0.6734 0.8834 0.6505 -0.2001 -0.2070 -0.0361 23  GLN   A NE2 
178  N N   . PHE   A 23  ? 0.7128 0.7713 0.5560 -0.1212 -0.2396 0.0193  24  PHE   A N   
179  C CA  . PHE   A 23  ? 0.6781 0.7882 0.5414 -0.1003 -0.2386 0.0211  24  PHE   A CA  
180  C C   . PHE   A 23  ? 0.6310 0.6993 0.5099 -0.0591 -0.1918 0.0255  24  PHE   A C   
181  O O   . PHE   A 23  ? 0.6574 0.7046 0.5093 -0.0083 -0.1974 0.0565  24  PHE   A O   
182  C CB  . PHE   A 23  ? 0.7151 0.8855 0.5729 -0.1049 -0.2462 0.0209  24  PHE   A CB  
183  C CG  . PHE   A 23  ? 0.7265 0.9731 0.6074 -0.1156 -0.2614 0.0137  24  PHE   A CG  
184  C CD1 . PHE   A 23  ? 0.7293 1.0079 0.6194 -0.1270 -0.2730 0.0077  24  PHE   A CD1 
185  C CD2 . PHE   A 23  ? 0.7239 1.0099 0.6185 -0.1143 -0.2758 0.0141  24  PHE   A CD2 
186  C CE1 . PHE   A 23  ? 0.7241 1.0309 0.6284 -0.1314 -0.2708 0.0112  24  PHE   A CE1 
187  C CE2 . PHE   A 23  ? 0.7306 1.0325 0.6296 -0.1200 -0.2676 0.0077  24  PHE   A CE2 
188  C CZ  . PHE   A 23  ? 0.7206 1.0384 0.6316 -0.1318 -0.2684 0.0074  24  PHE   A CZ  
189  N N   . ALA   A 24  ? 0.5378 0.5908 0.4688 -0.0736 -0.1485 0.0125  25  ALA   A N   
190  C CA  . ALA   A 24  ? 0.4593 0.4772 0.4090 -0.0725 -0.1076 -0.0270 25  ALA   A CA  
191  C C   . ALA   A 24  ? 0.3818 0.3823 0.3611 -0.0528 -0.0693 -0.0316 25  ALA   A C   
192  O O   . ALA   A 24  ? 0.4152 0.3896 0.3715 -0.0487 -0.0977 -0.0492 25  ALA   A O   
193  C CB  . ALA   A 24  ? 0.4566 0.4791 0.4054 -0.0755 -0.1136 -0.0388 25  ALA   A CB  
194  N N   . VAL   A 25  ? 0.3030 0.2731 0.2879 -0.0578 -0.0051 -0.0334 26  VAL   A N   
195  C CA  . VAL   A 25  ? 0.2993 0.2174 0.2403 -0.0515 0.0379  -0.0554 26  VAL   A CA  
196  C C   . VAL   A 25  ? 0.2691 0.2116 0.1989 -0.0397 0.0336  -0.0340 26  VAL   A C   
197  O O   . VAL   A 25  ? 0.3418 0.2547 0.1828 -0.0576 0.0840  -0.0406 26  VAL   A O   
198  C CB  . VAL   A 25  ? 0.3543 0.2175 0.2714 -0.0358 0.0411  -0.0576 26  VAL   A CB  
199  C CG1 . VAL   A 25  ? 0.3584 0.2442 0.2964 0.0050  0.0713  -0.0542 26  VAL   A CG1 
200  C CG2 . VAL   A 25  ? 0.4152 0.2278 0.2859 -0.0161 0.0219  -0.0693 26  VAL   A CG2 
201  N N   . VAL   A 26  ? 0.2368 0.2026 0.1836 -0.0210 0.0178  -0.0187 27  VAL   A N   
202  C CA  . VAL   A 26  ? 0.2425 0.2006 0.1807 -0.0201 0.0009  -0.0265 27  VAL   A CA  
203  C C   . VAL   A 26  ? 0.2464 0.2020 0.1768 -0.0210 0.0168  -0.0473 27  VAL   A C   
204  O O   . VAL   A 26  ? 0.2814 0.2142 0.1767 -0.0281 0.0382  -0.0535 27  VAL   A O   
205  C CB  . VAL   A 26  ? 0.2792 0.1982 0.2340 -0.0092 0.0072  -0.0335 27  VAL   A CB  
206  C CG1 . VAL   A 26  ? 0.3149 0.2304 0.2728 -0.0463 0.0149  -0.0340 27  VAL   A CG1 
207  C CG2 . VAL   A 26  ? 0.2676 0.2249 0.2494 0.0122  -0.0025 -0.0100 27  VAL   A CG2 
208  N N   . LYS   A 27  ? 0.2251 0.2316 0.1903 -0.0227 0.0154  -0.0533 28  LYS   A N   
209  C CA  . LYS   A 27  ? 0.2373 0.2062 0.2045 -0.0155 0.0251  -0.0646 28  LYS   A CA  
210  C C   . LYS   A 27  ? 0.2413 0.2125 0.2006 -0.0182 0.0345  -0.0747 28  LYS   A C   
211  O O   . LYS   A 27  ? 0.2822 0.2636 0.2120 -0.0126 0.0698  -0.0962 28  LYS   A O   
212  C CB  . LYS   A 27  ? 0.2743 0.2168 0.2666 0.0097  0.0021  -0.0538 28  LYS   A CB  
213  C CG  . LYS   A 27  ? 0.3677 0.2465 0.3008 0.0132  -0.0094 -0.0392 28  LYS   A CG  
214  C CD  . LYS   A 27  ? 0.4091 0.2475 0.3080 0.0356  -0.0257 -0.0169 28  LYS   A CD  
215  C CE  . LYS   A 27  ? 0.4826 0.2561 0.3253 0.0543  -0.0191 -0.0103 28  LYS   A CE  
216  N NZ  . LYS   A 27  ? 0.5399 0.2922 0.3410 0.0590  -0.0524 -0.0071 28  LYS   A NZ  
217  N N   . LYS   A 28  ? 0.2385 0.1976 0.1713 -0.0173 0.0212  -0.0487 29  LYS   A N   
218  C CA  . LYS   A 28  ? 0.2554 0.1987 0.1717 -0.0154 0.0154  -0.0469 29  LYS   A CA  
219  C C   . LYS   A 28  ? 0.2702 0.1643 0.1858 0.0256  -0.0080 -0.0450 29  LYS   A C   
220  O O   . LYS   A 28  ? 0.2644 0.1826 0.2091 0.0272  -0.0026 -0.0411 29  LYS   A O   
221  C CB  . LYS   A 28  ? 0.2368 0.2588 0.2370 -0.0243 0.0444  -0.0444 29  LYS   A CB  
222  C CG  . LYS   A 28  ? 0.3130 0.3467 0.3193 -0.0124 0.0422  -0.0524 29  LYS   A CG  
223  C CD  . LYS   A 28  ? 0.3972 0.4318 0.3960 -0.0215 0.0608  -0.0435 29  LYS   A CD  
224  C CE  . LYS   A 28  ? 0.4649 0.4880 0.4351 -0.0020 0.0604  -0.0371 29  LYS   A CE  
225  N NZ  . LYS   A 28  ? 0.5347 0.5223 0.4724 0.0031  0.0706  -0.0372 29  LYS   A NZ  
226  N N   . CYS   A 29  ? 0.2490 0.1697 0.1712 0.0274  -0.0166 -0.0348 30  CYS   A N   
227  C CA  . CYS   A 29  ? 0.2803 0.1660 0.1864 0.0100  -0.0251 -0.0241 30  CYS   A CA  
228  C C   . CYS   A 29  ? 0.2563 0.1485 0.1844 0.0320  -0.0131 -0.0173 30  CYS   A C   
229  O O   . CYS   A 29  ? 0.2504 0.1662 0.1787 0.0293  -0.0142 -0.0063 30  CYS   A O   
230  C CB  . CYS   A 29  ? 0.2882 0.2038 0.1894 0.0162  0.0081  -0.0287 30  CYS   A CB  
231  S SG  . CYS   A 29  ? 0.2908 0.2190 0.1849 0.0157  0.0017  -0.0146 30  CYS   A SG  
232  N N   . ARG   A 30  ? 0.2762 0.1693 0.1851 0.0191  -0.0291 -0.0125 31  ARG   A N   
233  C CA  . ARG   A 30  ? 0.2735 0.1693 0.1726 0.0082  -0.0089 -0.0151 31  ARG   A CA  
234  C C   . ARG   A 30  ? 0.2353 0.1597 0.1834 0.0316  -0.0133 0.0084  31  ARG   A C   
235  O O   . ARG   A 30  ? 0.2398 0.1613 0.1928 0.0187  -0.0126 0.0090  31  ARG   A O   
236  C CB  . ARG   A 30  ? 0.2556 0.2012 0.1787 -0.0159 0.0000  -0.0097 31  ARG   A CB  
237  C CG  . ARG   A 30  ? 0.2714 0.1990 0.1809 -0.0161 0.0194  -0.0165 31  ARG   A CG  
238  C CD  . ARG   A 30  ? 0.2508 0.2145 0.2135 -0.0158 0.0404  -0.0091 31  ARG   A CD  
239  N NE  . ARG   A 30  ? 0.2528 0.2173 0.2148 0.0084  0.0252  -0.0203 31  ARG   A NE  
240  C CZ  . ARG   A 30  ? 0.2222 0.2131 0.2393 -0.0521 0.0389  0.0240  31  ARG   A CZ  
241  N NH1 . ARG   A 30  ? 0.2502 0.2354 0.2716 -0.0412 0.0261  0.0551  31  ARG   A NH1 
242  N NH2 . ARG   A 30  ? 0.2466 0.2184 0.2686 -0.0469 0.0286  0.0133  31  ARG   A NH2 
243  N N   . GLU   A 31  ? 0.2376 0.1687 0.1714 0.0170  -0.0215 -0.0146 32  GLU   A N   
244  C CA  . GLU   A 31  ? 0.2262 0.1826 0.1719 0.0210  -0.0205 -0.0232 32  GLU   A CA  
245  C C   . GLU   A 31  ? 0.2505 0.1872 0.1766 -0.0143 -0.0190 0.0005  32  GLU   A C   
246  O O   . GLU   A 31  ? 0.2427 0.2062 0.2007 -0.0096 -0.0263 0.0158  32  GLU   A O   
247  C CB  . GLU   A 31  ? 0.2470 0.1833 0.1852 0.0133  0.0051  -0.0249 32  GLU   A CB  
248  C CG  . GLU   A 31  ? 0.3020 0.1941 0.1897 0.0188  -0.0013 -0.0506 32  GLU   A CG  
249  C CD  . GLU   A 31  ? 0.4339 0.2241 0.2309 0.0339  0.0268  -0.0591 32  GLU   A CD  
250  O OE1 . GLU   A 31  ? 0.5175 0.2583 0.2398 0.0716  0.0254  -0.0395 32  GLU   A OE1 
251  O OE2 . GLU   A 31  ? 0.3546 0.2260 0.3005 -0.0103 0.0513  -0.0837 32  GLU   A OE2 
252  N N   . LYS   A 32  ? 0.2267 0.2174 0.1779 0.0265  -0.0215 0.0259  33  LYS   A N   
253  C CA  . LYS   A 32  ? 0.2291 0.2384 0.1991 0.0154  -0.0294 0.0391  33  LYS   A CA  
254  C C   . LYS   A 32  ? 0.2476 0.2672 0.2029 0.0123  -0.0241 0.0413  33  LYS   A C   
255  O O   . LYS   A 32  ? 0.2500 0.2883 0.2402 -0.0258 -0.0342 0.0476  33  LYS   A O   
256  C CB  . LYS   A 32  ? 0.2481 0.2252 0.2389 0.0104  -0.0508 0.0526  33  LYS   A CB  
257  C CG  . LYS   A 32  ? 0.2647 0.2270 0.2722 0.0148  -0.0417 0.0452  33  LYS   A CG  
258  C CD  . LYS   A 32  ? 0.3183 0.2318 0.3097 0.0252  -0.0474 0.0627  33  LYS   A CD  
259  C CE  . LYS   A 32  ? 0.3803 0.2310 0.3394 0.0389  -0.0281 0.0850  33  LYS   A CE  
260  N NZ  . LYS   A 32  ? 0.4429 0.2728 0.3735 0.0505  -0.0269 0.0751  33  LYS   A NZ  
261  N N   . SER   A 33  ? 0.2847 0.2627 0.1993 -0.0003 -0.0606 0.0258  34  SER   A N   
262  C CA  . SER   A 33  ? 0.3235 0.2647 0.1933 -0.0360 -0.0488 0.0129  34  SER   A CA  
263  C C   . SER   A 33  ? 0.3435 0.2586 0.1971 -0.0778 -0.0441 -0.0089 34  SER   A C   
264  O O   . SER   A 33  ? 0.3606 0.3058 0.2181 -0.1344 -0.0414 0.0021  34  SER   A O   
265  C CB  . SER   A 33  ? 0.3244 0.2768 0.2166 -0.0587 -0.0370 0.0091  34  SER   A CB  
266  O OG  . SER   A 33  ? 0.3514 0.2850 0.2446 -0.0702 -0.0150 -0.0128 34  SER   A OG  
267  N N   . THR   A 34  ? 0.3106 0.2322 0.1905 -0.0560 -0.0151 0.0025  35  THR   A N   
268  C CA  . THR   A 34  ? 0.2631 0.2457 0.1875 -0.0528 -0.0123 -0.0245 35  THR   A CA  
269  C C   . THR   A 34  ? 0.2498 0.2301 0.2029 -0.0469 -0.0025 -0.0293 35  THR   A C   
270  O O   . THR   A 34  ? 0.2719 0.2322 0.2340 -0.0612 -0.0008 -0.0145 35  THR   A O   
271  C CB  . THR   A 34  ? 0.2797 0.2431 0.1862 -0.0303 -0.0024 -0.0583 35  THR   A CB  
272  O OG1 . THR   A 34  ? 0.3166 0.2187 0.1812 -0.0452 -0.0138 -0.0426 35  THR   A OG1 
273  C CG2 . THR   A 34  ? 0.3403 0.2654 0.2004 -0.0639 -0.0233 -0.0588 35  THR   A CG2 
274  N N   . GLY   A 35  ? 0.2191 0.2174 0.2039 -0.0164 -0.0104 -0.0209 36  GLY   A N   
275  C CA  . GLY   A 35  ? 0.2264 0.2161 0.2023 0.0232  -0.0086 -0.0232 36  GLY   A CA  
276  C C   . GLY   A 35  ? 0.1808 0.2023 0.2067 0.0128  0.0096  -0.0255 36  GLY   A C   
277  O O   . GLY   A 35  ? 0.2097 0.2293 0.2133 -0.0052 0.0221  -0.0106 36  GLY   A O   
278  N N   . LEU   A 36  ? 0.2017 0.1749 0.1983 0.0013  -0.0216 -0.0278 37  LEU   A N   
279  C CA  . LEU   A 36  ? 0.2233 0.1738 0.1883 0.0071  -0.0090 -0.0410 37  LEU   A CA  
280  C C   . LEU   A 36  ? 0.2050 0.1453 0.1801 0.0304  0.0076  -0.0174 37  LEU   A C   
281  O O   . LEU   A 36  ? 0.2372 0.1631 0.1869 0.0096  -0.0009 -0.0092 37  LEU   A O   
282  C CB  . LEU   A 36  ? 0.2275 0.1715 0.2088 0.0196  0.0079  -0.0494 37  LEU   A CB  
283  C CG  . LEU   A 36  ? 0.2376 0.1666 0.2071 0.0015  -0.0055 -0.0442 37  LEU   A CG  
284  C CD1 . LEU   A 36  ? 0.2580 0.2031 0.2415 0.0301  0.0075  -0.0704 37  LEU   A CD1 
285  C CD2 . LEU   A 36  ? 0.2918 0.1560 0.2237 0.0068  -0.0232 -0.0249 37  LEU   A CD2 
286  N N   . GLN   A 37  ? 0.2433 0.1727 0.2075 0.0188  -0.0148 -0.0045 38  GLN   A N   
287  C CA  . GLN   A 37  ? 0.2480 0.1687 0.1892 -0.0014 0.0026  -0.0055 38  GLN   A CA  
288  C C   . GLN   A 37  ? 0.2477 0.1592 0.1724 0.0103  -0.0035 0.0076  38  GLN   A C   
289  O O   . GLN   A 37  ? 0.2613 0.1662 0.2254 0.0082  -0.0044 0.0100  38  GLN   A O   
290  C CB  . GLN   A 37  ? 0.2490 0.2332 0.2438 0.0041  0.0306  -0.0221 38  GLN   A CB  
291  C CG  . GLN   A 37  ? 0.3297 0.2621 0.3117 0.0061  0.0643  -0.0299 38  GLN   A CG  
292  C CD  . GLN   A 37  ? 0.4834 0.2899 0.3738 0.0125  0.0825  -0.0215 38  GLN   A CD  
293  O OE1 . GLN   A 37  ? 0.5329 0.3125 0.3586 0.0308  0.0880  -0.0390 38  GLN   A OE1 
294  N NE2 . GLN   A 37  ? 0.5590 0.3392 0.4284 0.0225  0.0926  -0.0155 38  GLN   A NE2 
295  N N   . TYR   A 38  ? 0.2454 0.1706 0.1465 0.0100  -0.0150 -0.0042 39  TYR   A N   
296  C CA  . TYR   A 38  ? 0.2379 0.1811 0.1341 0.0083  -0.0149 -0.0143 39  TYR   A CA  
297  C C   . TYR   A 38  ? 0.2156 0.1765 0.1488 0.0412  -0.0110 -0.0045 39  TYR   A C   
298  O O   . TYR   A 38  ? 0.2242 0.1967 0.1588 0.0472  -0.0057 -0.0162 39  TYR   A O   
299  C CB  . TYR   A 38  ? 0.2675 0.1583 0.1180 -0.0025 0.0154  -0.0075 39  TYR   A CB  
300  C CG  . TYR   A 38  ? 0.2352 0.1403 0.1369 0.0125  -0.0086 -0.0269 39  TYR   A CG  
301  C CD1 . TYR   A 38  ? 0.2411 0.1690 0.1532 0.0163  -0.0243 -0.0381 39  TYR   A CD1 
302  C CD2 . TYR   A 38  ? 0.2312 0.1689 0.1362 0.0060  -0.0040 -0.0115 39  TYR   A CD2 
303  C CE1 . TYR   A 38  ? 0.2418 0.1894 0.1633 0.0284  -0.0104 -0.0413 39  TYR   A CE1 
304  C CE2 . TYR   A 38  ? 0.2273 0.1641 0.1467 0.0163  -0.0028 -0.0156 39  TYR   A CE2 
305  C CZ  . TYR   A 38  ? 0.2745 0.1723 0.1556 0.0337  -0.0313 -0.0409 39  TYR   A CZ  
306  O OH  . TYR   A 38  ? 0.3279 0.2018 0.1990 0.0555  -0.0472 -0.0818 39  TYR   A OH  
307  N N   . ALA   A 39  ? 0.2224 0.1712 0.1381 0.0151  -0.0081 -0.0115 40  ALA   A N   
308  C CA  . ALA   A 39  ? 0.2399 0.1691 0.1565 -0.0071 -0.0143 -0.0146 40  ALA   A CA  
309  C C   . ALA   A 39  ? 0.2817 0.1672 0.1499 0.0071  0.0233  -0.0339 40  ALA   A C   
310  O O   . ALA   A 39  ? 0.3524 0.1773 0.2009 0.0343  0.0938  -0.0295 40  ALA   A O   
311  C CB  . ALA   A 39  ? 0.2792 0.1947 0.1622 0.0142  -0.0234 -0.0051 40  ALA   A CB  
312  N N   . ALA   A 40  ? 0.2660 0.1524 0.1415 -0.0051 0.0212  -0.0119 41  ALA   A N   
313  C CA  . ALA   A 40  ? 0.2752 0.1564 0.1484 -0.0053 0.0322  -0.0203 41  ALA   A CA  
314  C C   . ALA   A 40  ? 0.2818 0.1973 0.1452 -0.0090 0.0215  -0.0195 41  ALA   A C   
315  O O   . ALA   A 40  ? 0.2892 0.2109 0.1644 -0.0269 0.0441  -0.0348 41  ALA   A O   
316  C CB  . ALA   A 40  ? 0.2972 0.1893 0.1830 0.0284  0.0267  0.0009  41  ALA   A CB  
317  N N   . LYS   A 41  ? 0.2635 0.1814 0.1515 -0.0067 0.0288  -0.0364 42  LYS   A N   
318  C CA  . LYS   A 41  ? 0.2588 0.1792 0.1535 0.0021  0.0249  -0.0210 42  LYS   A CA  
319  C C   . LYS   A 41  ? 0.2713 0.1998 0.1477 0.0011  0.0124  -0.0203 42  LYS   A C   
320  O O   . LYS   A 41  ? 0.2789 0.2195 0.1403 -0.0041 0.0153  -0.0188 42  LYS   A O   
321  C CB  . LYS   A 41  ? 0.2637 0.1982 0.1707 0.0063  -0.0057 -0.0152 42  LYS   A CB  
322  C CG  . LYS   A 41  ? 0.2990 0.2237 0.2281 0.0096  -0.0293 0.0156  42  LYS   A CG  
323  C CD  . LYS   A 41  ? 0.3460 0.3010 0.2686 0.0429  -0.0785 0.0331  42  LYS   A CD  
324  C CE  . LYS   A 41  ? 0.3887 0.3536 0.3099 0.0555  -0.0707 0.0356  42  LYS   A CE  
325  N NZ  . LYS   A 41  ? 0.4329 0.3838 0.3301 0.0541  -0.0573 0.0242  42  LYS   A NZ  
326  N N   . PHE   A 42  ? 0.2989 0.1882 0.1554 -0.0123 0.0484  -0.0203 43  PHE   A N   
327  C CA  . PHE   A 42  ? 0.3321 0.1825 0.1879 -0.0249 0.0650  -0.0222 43  PHE   A CA  
328  C C   . PHE   A 42  ? 0.3022 0.2180 0.1758 -0.0341 0.0418  -0.0154 43  PHE   A C   
329  O O   . PHE   A 42  ? 0.3685 0.2780 0.1970 -0.0801 0.0621  -0.0561 43  PHE   A O   
330  C CB  . PHE   A 42  ? 0.3315 0.1983 0.2188 -0.0201 0.0783  -0.0355 43  PHE   A CB  
331  C CG  . PHE   A 42  ? 0.2906 0.2311 0.2572 -0.0039 0.0675  -0.0324 43  PHE   A CG  
332  C CD1 . PHE   A 42  ? 0.2877 0.2454 0.2892 -0.0147 0.0768  -0.0491 43  PHE   A CD1 
333  C CD2 . PHE   A 42  ? 0.2989 0.2714 0.2939 0.0218  0.0560  -0.0343 43  PHE   A CD2 
334  C CE1 . PHE   A 42  ? 0.2950 0.2685 0.3042 0.0019  0.0637  -0.0451 43  PHE   A CE1 
335  C CE2 . PHE   A 42  ? 0.3007 0.2777 0.3109 0.0380  0.0635  -0.0390 43  PHE   A CE2 
336  C CZ  . PHE   A 42  ? 0.2856 0.2639 0.3019 0.0204  0.0619  -0.0477 43  PHE   A CZ  
337  N N   . ILE   A 43  ? 0.2820 0.2283 0.1820 -0.0663 0.0296  0.0226  44  ILE   A N   
338  C CA  . ILE   A 43  ? 0.2821 0.2212 0.1810 -0.0440 0.0070  0.0110  44  ILE   A CA  
339  C C   . ILE   A 43  ? 0.2949 0.2336 0.1570 -0.0480 -0.0003 0.0055  44  ILE   A C   
340  O O   . ILE   A 43  ? 0.3139 0.2405 0.1520 -0.0308 -0.0198 0.0210  44  ILE   A O   
341  C CB  . ILE   A 43  ? 0.2839 0.2347 0.2161 -0.0400 -0.0016 0.0179  44  ILE   A CB  
342  C CG1 . ILE   A 43  ? 0.3302 0.2873 0.2550 -0.0006 0.0043  0.0252  44  ILE   A CG1 
343  C CG2 . ILE   A 43  ? 0.3046 0.2612 0.2266 -0.0233 -0.0160 0.0178  44  ILE   A CG2 
344  C CD1 . ILE   A 43  ? 0.3322 0.3237 0.2990 0.0245  -0.0022 0.0270  44  ILE   A CD1 
345  N N   . LYS   A 44  ? 0.3220 0.2406 0.1559 -0.0656 -0.0037 0.0010  45  LYS   A N   
346  C CA  . LYS   A 44  ? 0.3201 0.2736 0.1694 -0.0648 -0.0065 -0.0210 45  LYS   A CA  
347  C C   . LYS   A 44  ? 0.3046 0.2579 0.1607 -0.0674 -0.0238 -0.0161 45  LYS   A C   
348  O O   . LYS   A 44  ? 0.3160 0.2808 0.1826 -0.0443 -0.0222 0.0195  45  LYS   A O   
349  C CB  . LYS   A 44  ? 0.3662 0.3513 0.1958 -0.0169 0.0037  -0.0554 45  LYS   A CB  
350  C CG  . LYS   A 44  ? 0.5152 0.4273 0.2670 0.0454  0.0033  -0.0611 45  LYS   A CG  
351  C CD  . LYS   A 44  ? 0.6337 0.4960 0.3202 0.1023  -0.0141 -0.0485 45  LYS   A CD  
352  C CE  . LYS   A 44  ? 0.6909 0.5428 0.3458 0.1256  -0.0108 -0.0431 45  LYS   A CE  
353  N NZ  . LYS   A 44  ? 0.7293 0.5602 0.3459 0.1215  -0.0310 -0.0492 45  LYS   A NZ  
354  N N   . LYS   A 45  ? 0.3203 0.2442 0.1526 -0.0718 -0.0051 -0.0017 46  LYS   A N   
355  C CA  . LYS   A 45  ? 0.3023 0.2383 0.1470 -0.0643 -0.0156 -0.0046 46  LYS   A CA  
356  C C   . LYS   A 45  ? 0.3115 0.2319 0.1862 -0.0627 -0.0151 -0.0051 46  LYS   A C   
357  O O   . LYS   A 45  ? 0.3380 0.2349 0.2064 -0.0599 0.0030  0.0062  46  LYS   A O   
358  C CB  . LYS   A 45  ? 0.2981 0.2324 0.1368 -0.0467 -0.0391 0.0123  46  LYS   A CB  
359  C CG  . LYS   A 45  ? 0.3087 0.2365 0.1396 -0.0720 -0.0300 0.0022  46  LYS   A CG  
360  C CD  . LYS   A 45  ? 0.3386 0.2263 0.1304 -0.0493 -0.0366 -0.0026 46  LYS   A CD  
361  C CE  . LYS   A 45  ? 0.3213 0.2409 0.1424 -0.0484 -0.0226 0.0123  46  LYS   A CE  
362  N NZ  . LYS   A 45  ? 0.3283 0.2565 0.1417 -0.0058 -0.0053 0.0132  46  LYS   A NZ  
363  N N   . ARG   A 46  ? 0.3154 0.2655 0.2208 -0.0976 -0.0207 -0.0002 47  ARG   A N   
364  C CA  . ARG   A 46  ? 0.3716 0.3186 0.2541 -0.1287 -0.0133 -0.0150 47  ARG   A CA  
365  C C   . ARG   A 46  ? 0.4515 0.3392 0.2177 -0.1409 -0.0303 0.0106  47  ARG   A C   
366  O O   . ARG   A 46  ? 0.5089 0.3811 0.2049 -0.1440 -0.0251 -0.0179 47  ARG   A O   
367  C CB  . ARG   A 46  ? 0.4055 0.3713 0.3738 -0.1414 -0.0107 -0.0261 47  ARG   A CB  
368  C CG  . ARG   A 46  ? 0.4549 0.4140 0.4845 -0.1475 -0.0254 -0.0300 47  ARG   A CG  
369  C CD  . ARG   A 46  ? 0.5339 0.4513 0.5817 -0.1804 -0.0388 -0.0334 47  ARG   A CD  
370  N NE  . ARG   A 46  ? 0.6315 0.4922 0.6605 -0.1849 -0.0344 -0.0318 47  ARG   A NE  
371  C CZ  . ARG   A 46  ? 0.6781 0.5254 0.7180 -0.2050 -0.0326 -0.0312 47  ARG   A CZ  
372  N NH1 . ARG   A 46  ? 0.7029 0.5222 0.7434 -0.2069 -0.0307 -0.0300 47  ARG   A NH1 
373  N NH2 . ARG   A 46  ? 0.6911 0.5482 0.7332 -0.2172 -0.0444 -0.0355 47  ARG   A NH2 
374  N N   . ARG   A 47  ? 0.5359 0.3372 0.2378 -0.1495 -0.0608 0.0292  48  ARG   A N   
375  C CA  . ARG   A 47  ? 0.6184 0.3986 0.2870 -0.1656 -0.0601 0.0378  48  ARG   A CA  
376  C C   . ARG   A 47  ? 0.6261 0.3865 0.2690 -0.1856 -0.0771 0.0251  48  ARG   A C   
377  O O   . ARG   A 47  ? 0.6099 0.3584 0.2664 -0.1498 -0.1137 0.0653  48  ARG   A O   
378  C CB  . ARG   A 47  ? 0.6564 0.5006 0.3659 -0.1938 -0.0460 0.0509  48  ARG   A CB  
379  C CG  . ARG   A 47  ? 0.6739 0.6075 0.4438 -0.2195 -0.0490 0.0684  48  ARG   A CG  
380  C CD  . ARG   A 47  ? 0.6801 0.6959 0.5048 -0.2465 -0.0390 0.0969  48  ARG   A CD  
381  N NE  . ARG   A 47  ? 0.6849 0.7797 0.5566 -0.2467 -0.0411 0.1071  48  ARG   A NE  
382  C CZ  . ARG   A 47  ? 0.6569 0.8277 0.5880 -0.2591 -0.0510 0.1133  48  ARG   A CZ  
383  N NH1 . ARG   A 47  ? 0.6118 0.8246 0.5892 -0.2702 -0.0610 0.1020  48  ARG   A NH1 
384  N NH2 . ARG   A 47  ? 0.6610 0.8542 0.5994 -0.2535 -0.0461 0.1159  48  ARG   A NH2 
385  N N   . THR   A 48  ? 0.6553 0.4302 0.2912 -0.1936 -0.0490 0.0160  49  THR   A N   
386  C CA  . THR   A 48  ? 0.7235 0.4788 0.3313 -0.2299 -0.0363 -0.0171 49  THR   A CA  
387  C C   . THR   A 48  ? 0.7893 0.5567 0.3950 -0.2271 -0.0030 -0.0403 49  THR   A C   
388  O O   . THR   A 48  ? 0.8016 0.5665 0.4071 -0.1774 -0.0016 -0.0239 49  THR   A O   
389  C CB  . THR   A 48  ? 0.7606 0.4773 0.3324 -0.2119 -0.0579 -0.0330 49  THR   A CB  
390  O OG1 . THR   A 48  ? 0.7661 0.4841 0.3272 -0.1856 -0.0710 -0.0338 49  THR   A OG1 
391  C CG2 . THR   A 48  ? 0.7673 0.4648 0.3306 -0.2141 -0.0612 -0.0428 49  THR   A CG2 
392  N N   . LYS   A 49  ? 0.8667 0.6338 0.4583 -0.2428 0.0215  -0.0663 50  LYS   A N   
393  C CA  . LYS   A 49  ? 0.9584 0.7163 0.5289 -0.2344 0.0600  -0.0736 50  LYS   A CA  
394  C C   . LYS   A 49  ? 0.9928 0.7726 0.5694 -0.2125 0.0615  -0.0535 50  LYS   A C   
395  O O   . LYS   A 49  ? 1.0038 0.7825 0.5781 -0.2032 0.0693  -0.0374 50  LYS   A O   
396  C CB  . LYS   A 49  ? 1.0195 0.7447 0.5606 -0.2344 0.0934  -0.1022 50  LYS   A CB  
397  C CG  . LYS   A 49  ? 1.0775 0.7652 0.5867 -0.2361 0.1153  -0.1260 50  LYS   A CG  
398  C CD  . LYS   A 49  ? 1.1281 0.7749 0.6089 -0.2422 0.1339  -0.1460 50  LYS   A CD  
399  C CE  . LYS   A 49  ? 1.1691 0.7800 0.6270 -0.2488 0.1416  -0.1592 50  LYS   A CE  
400  N NZ  . LYS   A 49  ? 1.1939 0.7839 0.6340 -0.2512 0.1447  -0.1663 50  LYS   A NZ  
401  N N   . SER   A 50  ? 1.0096 0.8122 0.5906 -0.2026 0.0556  -0.0538 51  SER   A N   
402  C CA  . SER   A 50  ? 1.0222 0.8411 0.6084 -0.1902 0.0508  -0.0491 51  SER   A CA  
403  C C   . SER   A 50  ? 0.9888 0.8473 0.6165 -0.1619 0.0351  -0.0547 51  SER   A C   
404  O O   . SER   A 50  ? 0.9872 0.8549 0.6223 -0.1658 0.0316  -0.0543 51  SER   A O   
405  C CB  . SER   A 50  ? 1.0633 0.8525 0.6126 -0.2008 0.0548  -0.0462 51  SER   A CB  
406  O OG  . SER   A 50  ? 1.0775 0.8567 0.6132 -0.2094 0.0566  -0.0466 51  SER   A OG  
407  N N   . SER   A 51  ? 0.9483 0.8388 0.6168 -0.1325 0.0195  -0.0607 52  SER   A N   
408  C CA  . SER   A 51  ? 0.9182 0.8218 0.6152 -0.1031 -0.0012 -0.0736 52  SER   A CA  
409  C C   . SER   A 51  ? 0.9284 0.8093 0.6072 -0.0927 -0.0447 -0.0933 52  SER   A C   
410  O O   . SER   A 51  ? 0.9174 0.8085 0.6045 -0.0746 -0.0656 -0.0982 52  SER   A O   
411  C CB  . SER   A 51  ? 0.8917 0.8150 0.6174 -0.0873 0.0178  -0.0676 52  SER   A CB  
412  O OG  . SER   A 51  ? 0.8723 0.8062 0.6175 -0.0829 0.0265  -0.0648 52  SER   A OG  
413  N N   . ARG   A 52  ? 0.9575 0.7931 0.5982 -0.1016 -0.0665 -0.1087 53  ARG   A N   
414  C CA  . ARG   A 52  ? 0.9988 0.7797 0.5915 -0.1107 -0.0809 -0.1217 53  ARG   A CA  
415  C C   . ARG   A 52  ? 0.9898 0.7224 0.5570 -0.1097 -0.0906 -0.1199 53  ARG   A C   
416  O O   . ARG   A 52  ? 1.0091 0.7217 0.5569 -0.1112 -0.0964 -0.1354 53  ARG   A O   
417  C CB  . ARG   A 52  ? 1.0544 0.8209 0.6127 -0.1176 -0.0839 -0.1384 53  ARG   A CB  
418  C CG  . ARG   A 52  ? 1.1055 0.8596 0.6338 -0.1253 -0.0792 -0.1516 53  ARG   A CG  
419  C CD  . ARG   A 52  ? 1.1523 0.8957 0.6489 -0.1343 -0.0713 -0.1628 53  ARG   A CD  
420  N NE  . ARG   A 52  ? 1.1843 0.9260 0.6621 -0.1484 -0.0632 -0.1676 53  ARG   A NE  
421  C CZ  . ARG   A 52  ? 1.2021 0.9470 0.6676 -0.1603 -0.0545 -0.1696 53  ARG   A CZ  
422  N NH1 . ARG   A 52  ? 1.2056 0.9565 0.6715 -0.1662 -0.0497 -0.1659 53  ARG   A NH1 
423  N NH2 . ARG   A 52  ? 1.2088 0.9518 0.6678 -0.1655 -0.0573 -0.1727 53  ARG   A NH2 
424  N N   . ARG   A 53  ? 0.9521 0.6704 0.5224 -0.1133 -0.0962 -0.1037 54  ARG   A N   
425  C CA  . ARG   A 53  ? 0.8995 0.6246 0.4904 -0.1046 -0.0915 -0.0828 54  ARG   A CA  
426  C C   . ARG   A 53  ? 0.7590 0.5012 0.3859 -0.1322 -0.0970 -0.0855 54  ARG   A C   
427  O O   . ARG   A 53  ? 0.7514 0.4811 0.4032 -0.1752 -0.0883 -0.0534 54  ARG   A O   
428  C CB  . ARG   A 53  ? 0.9864 0.7054 0.5635 -0.0496 -0.0657 -0.0409 54  ARG   A CB  
429  C CG  . ARG   A 53  ? 1.0592 0.7893 0.6310 0.0087  -0.0421 0.0008  54  ARG   A CG  
430  C CD  . ARG   A 53  ? 1.1151 0.8623 0.6885 0.0532  -0.0252 0.0391  54  ARG   A CD  
431  N NE  . ARG   A 53  ? 1.1597 0.9224 0.7366 0.0860  -0.0153 0.0688  54  ARG   A NE  
432  C CZ  . ARG   A 53  ? 1.1875 0.9655 0.7712 0.1104  -0.0073 0.0892  54  ARG   A CZ  
433  N NH1 . ARG   A 53  ? 1.1973 0.9809 0.7828 0.1204  -0.0092 0.0966  54  ARG   A NH1 
434  N NH2 . ARG   A 53  ? 1.1940 0.9782 0.7807 0.1179  -0.0009 0.0947  54  ARG   A NH2 
435  N N   . GLY   A 54  ? 0.6278 0.4210 0.2958 -0.0834 -0.0955 -0.0683 55  GLY   A N   
436  C CA  . GLY   A 54  ? 0.5330 0.3552 0.2590 -0.0522 -0.0873 -0.0511 55  GLY   A CA  
437  C C   . GLY   A 54  ? 0.4347 0.3115 0.2226 -0.0362 -0.0714 -0.0250 55  GLY   A C   
438  O O   . GLY   A 54  ? 0.4268 0.3345 0.2423 -0.0616 -0.0787 -0.0176 55  GLY   A O   
439  N N   . VAL   A 55  ? 0.3369 0.2655 0.1918 -0.0093 -0.0029 0.0028  56  VAL   A N   
440  C CA  . VAL   A 55  ? 0.2957 0.2543 0.1896 -0.0258 -0.0112 0.0213  56  VAL   A CA  
441  C C   . VAL   A 55  ? 0.2760 0.2387 0.1920 -0.0168 -0.0242 0.0262  56  VAL   A C   
442  O O   . VAL   A 55  ? 0.3047 0.2529 0.1880 -0.0059 -0.0224 0.0277  56  VAL   A O   
443  C CB  . VAL   A 55  ? 0.3161 0.2458 0.1854 -0.0096 -0.0052 0.0364  56  VAL   A CB  
444  C CG1 . VAL   A 55  ? 0.3149 0.2468 0.2207 -0.0114 -0.0062 0.0500  56  VAL   A CG1 
445  C CG2 . VAL   A 55  ? 0.3187 0.2894 0.1735 -0.0068 0.0055  0.0043  56  VAL   A CG2 
446  N N   . SER   A 56  ? 0.3017 0.2544 0.2131 -0.0156 -0.0084 0.0168  57  SER   A N   
447  C CA  . SER   A 56  ? 0.2962 0.2333 0.2289 -0.0115 -0.0263 0.0230  57  SER   A CA  
448  C C   . SER   A 56  ? 0.2715 0.2199 0.2081 -0.0027 -0.0257 0.0510  57  SER   A C   
449  O O   . SER   A 56  ? 0.2627 0.2074 0.2092 -0.0030 -0.0012 0.0290  57  SER   A O   
450  C CB  . SER   A 56  ? 0.3113 0.2359 0.2741 0.0015  -0.0235 0.0396  57  SER   A CB  
451  O OG  . SER   A 56  ? 0.3258 0.2124 0.2871 -0.0027 -0.0179 0.0471  57  SER   A OG  
452  N N   . ARG   A 57  ? 0.2902 0.2448 0.2023 -0.0104 -0.0245 0.0342  58  ARG   A N   
453  C CA  . ARG   A 57  ? 0.3391 0.2369 0.2131 0.0102  -0.0439 0.0569  58  ARG   A CA  
454  C C   . ARG   A 57  ? 0.3071 0.2433 0.1973 -0.0115 -0.0257 0.0587  58  ARG   A C   
455  O O   . ARG   A 57  ? 0.3012 0.2506 0.1892 -0.0114 -0.0394 0.0435  58  ARG   A O   
456  C CB  . ARG   A 57  ? 0.4089 0.2745 0.2318 -0.0033 -0.0672 0.0621  58  ARG   A CB  
457  C CG  . ARG   A 57  ? 0.4407 0.3220 0.2580 0.0016  -0.0766 0.0186  58  ARG   A CG  
458  C CD  . ARG   A 57  ? 0.4109 0.3703 0.3079 0.0106  -0.0529 -0.0476 58  ARG   A CD  
459  N NE  . ARG   A 57  ? 0.3502 0.3643 0.2860 0.0488  -0.0796 -0.0626 58  ARG   A NE  
460  C CZ  . ARG   A 57  ? 0.2922 0.3206 0.2553 0.0727  -0.0630 -0.0380 58  ARG   A CZ  
461  N NH1 . ARG   A 57  ? 0.3649 0.3270 0.2592 0.0760  -0.0542 -0.0487 58  ARG   A NH1 
462  N NH2 . ARG   A 57  ? 0.3114 0.2847 0.2167 -0.0038 -0.0409 -0.0111 58  ARG   A NH2 
463  N N   . GLU   A 58  ? 0.2849 0.2419 0.2028 -0.0004 -0.0131 0.0525  59  GLU   A N   
464  C CA  . GLU   A 58  ? 0.3009 0.2796 0.2355 -0.0276 -0.0017 0.0700  59  GLU   A CA  
465  C C   . GLU   A 58  ? 0.2803 0.2462 0.2044 -0.0129 -0.0058 0.0722  59  GLU   A C   
466  O O   . GLU   A 58  ? 0.2709 0.2583 0.2075 -0.0018 -0.0043 0.0687  59  GLU   A O   
467  C CB  . GLU   A 58  ? 0.3312 0.3867 0.2875 -0.0439 0.0179  0.0854  59  GLU   A CB  
468  C CG  . GLU   A 58  ? 0.4087 0.4986 0.3638 -0.0669 0.0468  0.0798  59  GLU   A CG  
469  C CD  . GLU   A 58  ? 0.4941 0.6095 0.4199 -0.0712 0.0476  0.0686  59  GLU   A CD  
470  O OE1 . GLU   A 58  ? 0.5149 0.6497 0.4422 -0.0788 0.0368  0.0651  59  GLU   A OE1 
471  O OE2 . GLU   A 58  ? 0.5430 0.6571 0.4621 -0.0456 0.0258  0.0536  59  GLU   A OE2 
472  N N   . ASP   A 59  ? 0.2593 0.2305 0.1749 -0.0076 -0.0256 0.0636  60  ASP   A N   
473  C CA  . ASP   A 59  ? 0.2443 0.2186 0.1822 -0.0148 -0.0284 0.0502  60  ASP   A CA  
474  C C   . ASP   A 59  ? 0.2236 0.2121 0.1700 -0.0044 -0.0075 0.0573  60  ASP   A C   
475  O O   . ASP   A 59  ? 0.2257 0.2023 0.2032 -0.0160 -0.0182 0.0470  60  ASP   A O   
476  C CB  . ASP   A 59  ? 0.2763 0.2411 0.1958 -0.0329 -0.0473 0.0364  60  ASP   A CB  
477  C CG  . ASP   A 59  ? 0.3334 0.2768 0.2519 0.0020  -0.0502 0.0279  60  ASP   A CG  
478  O OD1 . ASP   A 59  ? 0.3054 0.3024 0.2809 -0.0125 -0.0628 0.0342  60  ASP   A OD1 
479  O OD2 . ASP   A 59  ? 0.3830 0.3077 0.2775 -0.0128 -0.0753 0.0096  60  ASP   A OD2 
480  N N   . ILE   A 60  ? 0.2345 0.2218 0.1587 0.0028  -0.0292 0.0268  61  ILE   A N   
481  C CA  . ILE   A 60  ? 0.2536 0.2103 0.1756 0.0075  -0.0363 0.0121  61  ILE   A CA  
482  C C   . ILE   A 60  ? 0.2341 0.2200 0.1614 0.0046  -0.0222 0.0195  61  ILE   A C   
483  O O   . ILE   A 60  ? 0.2573 0.2050 0.1881 0.0200  -0.0115 0.0157  61  ILE   A O   
484  C CB  . ILE   A 60  ? 0.2322 0.2191 0.2239 -0.0070 -0.0627 -0.0088 61  ILE   A CB  
485  C CG1 . ILE   A 60  ? 0.3011 0.1877 0.2181 0.0220  -0.0284 0.0009  61  ILE   A CG1 
486  C CG2 . ILE   A 60  ? 0.2664 0.2572 0.2674 0.0000  -0.0746 0.0005  61  ILE   A CG2 
487  C CD1 . ILE   A 60  ? 0.3505 0.1937 0.2460 0.0160  -0.0492 -0.0189 61  ILE   A CD1 
488  N N   . GLU   A 61  ? 0.2748 0.2275 0.1405 0.0265  -0.0195 0.0384  62  GLU   A N   
489  C CA  . GLU   A 61  ? 0.2710 0.2368 0.1456 0.0227  -0.0188 0.0258  62  GLU   A CA  
490  C C   . GLU   A 61  ? 0.2620 0.2207 0.1502 0.0316  -0.0049 0.0316  62  GLU   A C   
491  O O   . GLU   A 61  ? 0.2742 0.1993 0.1738 0.0124  -0.0035 0.0185  62  GLU   A O   
492  C CB  . GLU   A 61  ? 0.3020 0.2475 0.1630 0.0388  -0.0205 0.0368  62  GLU   A CB  
493  C CG  . GLU   A 61  ? 0.3718 0.2926 0.2018 0.0631  -0.0115 0.0545  62  GLU   A CG  
494  C CD  . GLU   A 61  ? 0.4209 0.3581 0.2519 0.1107  0.0147  0.0530  62  GLU   A CD  
495  O OE1 . GLU   A 61  ? 0.4811 0.4154 0.2892 0.1041  0.0555  0.0775  62  GLU   A OE1 
496  O OE2 . GLU   A 61  ? 0.4216 0.3582 0.2567 0.1260  -0.0268 0.0118  62  GLU   A OE2 
497  N N   . ARG   A 62  ? 0.2456 0.2372 0.1605 0.0443  -0.0222 0.0440  63  ARG   A N   
498  C CA  . ARG   A 62  ? 0.2281 0.2259 0.1814 0.0164  -0.0085 0.0486  63  ARG   A CA  
499  C C   . ARG   A 62  ? 0.2663 0.2093 0.1608 0.0003  -0.0011 0.0391  63  ARG   A C   
500  O O   . ARG   A 62  ? 0.2681 0.2107 0.1569 0.0122  -0.0146 0.0365  63  ARG   A O   
501  C CB  . ARG   A 62  ? 0.2258 0.2341 0.2061 0.0087  -0.0231 0.0652  63  ARG   A CB  
502  C CG  . ARG   A 62  ? 0.2295 0.2408 0.2505 0.0211  -0.0300 0.0547  63  ARG   A CG  
503  C CD  . ARG   A 62  ? 0.2338 0.2445 0.2770 -0.0233 -0.0314 0.0715  63  ARG   A CD  
504  N NE  . ARG   A 62  ? 0.2650 0.2756 0.2718 -0.0306 -0.0338 0.0855  63  ARG   A NE  
505  C CZ  . ARG   A 62  ? 0.3025 0.2913 0.2898 -0.0548 -0.0330 0.0968  63  ARG   A CZ  
506  N NH1 . ARG   A 62  ? 0.3273 0.2863 0.2914 -0.0551 -0.0623 0.0881  63  ARG   A NH1 
507  N NH2 . ARG   A 62  ? 0.3018 0.3179 0.3313 -0.0860 -0.0348 0.1064  63  ARG   A NH2 
508  N N   . GLU   A 63  ? 0.2215 0.2347 0.1341 0.0048  -0.0019 0.0417  64  GLU   A N   
509  C CA  . GLU   A 63  ? 0.2300 0.2460 0.1361 0.0039  -0.0416 0.0199  64  GLU   A CA  
510  C C   . GLU   A 63  ? 0.2393 0.2325 0.1307 0.0064  -0.0309 0.0042  64  GLU   A C   
511  O O   . GLU   A 63  ? 0.2447 0.2171 0.1488 0.0026  -0.0014 0.0104  64  GLU   A O   
512  C CB  . GLU   A 63  ? 0.2435 0.2527 0.1632 -0.0060 -0.0078 0.0191  64  GLU   A CB  
513  C CG  . GLU   A 63  ? 0.2347 0.3181 0.1545 -0.0185 0.0067  -0.0036 64  GLU   A CG  
514  C CD  . GLU   A 63  ? 0.2533 0.3986 0.2212 -0.0172 0.0167  -0.0179 64  GLU   A CD  
515  O OE1 . GLU   A 63  ? 0.2929 0.4366 0.2566 0.0134  -0.0188 -0.0347 64  GLU   A OE1 
516  O OE2 . GLU   A 63  ? 0.3316 0.4380 0.2384 -0.0446 -0.0113 -0.0471 64  GLU   A OE2 
517  N N   . VAL   A 64  ? 0.1946 0.2285 0.1181 -0.0002 -0.0266 0.0103  65  VAL   A N   
518  C CA  . VAL   A 64  ? 0.2323 0.1963 0.1271 0.0170  -0.0311 0.0092  65  VAL   A CA  
519  C C   . VAL   A 64  ? 0.2378 0.2151 0.1310 0.0357  -0.0112 0.0009  65  VAL   A C   
520  O O   . VAL   A 64  ? 0.2602 0.2151 0.1322 0.0039  -0.0250 -0.0025 65  VAL   A O   
521  C CB  . VAL   A 64  ? 0.2467 0.2134 0.1287 0.0300  -0.0303 0.0212  65  VAL   A CB  
522  C CG1 . VAL   A 64  ? 0.2678 0.2287 0.1290 0.0327  -0.0434 0.0125  65  VAL   A CG1 
523  C CG2 . VAL   A 64  ? 0.2375 0.2246 0.1471 0.0337  -0.0142 0.0034  65  VAL   A CG2 
524  N N   . SER   A 65  ? 0.2384 0.2043 0.1356 0.0311  -0.0090 0.0086  66  SER   A N   
525  C CA  A SER   A 65  ? 0.2525 0.2256 0.1277 0.0176  0.0012  0.0277  66  SER   A CA  
526  C CA  B SER   A 65  ? 0.2590 0.2267 0.1480 0.0041  0.0056  0.0171  66  SER   A CA  
527  C C   . SER   A 65  ? 0.2234 0.2124 0.1340 0.0219  -0.0099 0.0272  66  SER   A C   
528  O O   . SER   A 65  ? 0.2631 0.2155 0.1644 0.0002  -0.0006 0.0210  66  SER   A O   
529  C CB  A SER   A 65  ? 0.2862 0.2440 0.1377 0.0410  0.0179  0.0330  66  SER   A CB  
530  C CB  B SER   A 65  ? 0.3120 0.2518 0.1916 -0.0088 0.0327  0.0049  66  SER   A CB  
531  O OG  A SER   A 65  ? 0.3323 0.2828 0.1739 0.0045  0.0134  0.0155  66  SER   A OG  
532  O OG  B SER   A 65  ? 0.3650 0.2674 0.2297 -0.0611 0.0308  0.0032  66  SER   A OG  
533  N N   . ILE   A 66  ? 0.2124 0.2169 0.1212 0.0252  -0.0139 0.0246  67  ILE   A N   
534  C CA  A ILE   A 66  ? 0.2136 0.2165 0.1335 0.0246  -0.0118 0.0170  67  ILE   A CA  
535  C CA  B ILE   A 66  ? 0.2278 0.2024 0.1425 0.0403  0.0111  0.0332  67  ILE   A CA  
536  C C   . ILE   A 66  ? 0.2109 0.2093 0.1465 0.0384  0.0072  0.0103  67  ILE   A C   
537  O O   . ILE   A 66  ? 0.2588 0.1893 0.1395 0.0208  0.0064  -0.0066 67  ILE   A O   
538  C CB  A ILE   A 66  ? 0.1938 0.2319 0.1414 0.0052  -0.0357 0.0287  67  ILE   A CB  
539  C CB  B ILE   A 66  ? 0.2436 0.1890 0.1626 0.0439  0.0300  0.0755  67  ILE   A CB  
540  C CG1 A ILE   A 66  ? 0.2043 0.2530 0.1614 0.0235  -0.0313 0.0234  67  ILE   A CG1 
541  C CG1 B ILE   A 66  ? 0.2838 0.1873 0.2118 0.0382  0.0282  0.0810  67  ILE   A CG1 
542  C CG2 A ILE   A 66  ? 0.2746 0.2297 0.1609 0.0163  -0.0534 0.0238  67  ILE   A CG2 
543  C CG2 B ILE   A 66  ? 0.2863 0.1794 0.1722 0.0599  0.0385  0.0881  67  ILE   A CG2 
544  C CD1 A ILE   A 66  ? 0.2129 0.2592 0.1285 0.0314  -0.0320 0.0182  67  ILE   A CD1 
545  C CD1 B ILE   A 66  ? 0.3081 0.1963 0.2400 0.0541  0.0238  0.0696  67  ILE   A CD1 
546  N N   . LEU   A 67  ? 0.1938 0.2198 0.1293 0.0286  -0.0086 0.0112  68  LEU   A N   
547  C CA  . LEU   A 67  ? 0.1934 0.2464 0.1653 0.0211  0.0072  -0.0149 68  LEU   A CA  
548  C C   . LEU   A 67  ? 0.2098 0.2475 0.1546 0.0075  0.0003  0.0071  68  LEU   A C   
549  O O   . LEU   A 67  ? 0.2675 0.2166 0.1633 -0.0105 0.0148  -0.0040 68  LEU   A O   
550  C CB  . LEU   A 67  ? 0.2087 0.2725 0.1487 0.0244  0.0102  -0.0328 68  LEU   A CB  
551  C CG  . LEU   A 67  ? 0.2365 0.2711 0.1719 0.0061  0.0186  -0.0360 68  LEU   A CG  
552  C CD1 . LEU   A 67  ? 0.2343 0.2819 0.2081 0.0256  0.0442  -0.0522 68  LEU   A CD1 
553  C CD2 . LEU   A 67  ? 0.3137 0.3059 0.1921 -0.0218 0.0265  -0.0236 68  LEU   A CD2 
554  N N   . LYS   A 68  ? 0.2306 0.2280 0.1390 -0.0140 -0.0224 -0.0063 69  LYS   A N   
555  C CA  . LYS   A 68  ? 0.2817 0.2160 0.1585 -0.0036 -0.0145 0.0086  69  LYS   A CA  
556  C C   . LYS   A 68  ? 0.3025 0.2062 0.1588 -0.0018 -0.0282 -0.0042 69  LYS   A C   
557  O O   . LYS   A 68  ? 0.3785 0.2347 0.2304 -0.0171 -0.0504 -0.0531 69  LYS   A O   
558  C CB  . LYS   A 68  ? 0.2869 0.2350 0.1866 0.0188  -0.0240 0.0154  69  LYS   A CB  
559  C CG  . LYS   A 68  ? 0.3245 0.2670 0.2120 0.0326  -0.0362 0.0111  69  LYS   A CG  
560  C CD  . LYS   A 68  ? 0.3966 0.3097 0.2504 0.0329  -0.0453 0.0471  69  LYS   A CD  
561  C CE  . LYS   A 68  ? 0.4238 0.3811 0.2793 0.0276  -0.0758 0.0484  69  LYS   A CE  
562  N NZ  . LYS   A 68  ? 0.4686 0.4521 0.3013 0.0264  -0.0966 0.0577  69  LYS   A NZ  
563  N N   . GLU   A 69  ? 0.2941 0.1996 0.1443 0.0130  0.0159  -0.0092 70  GLU   A N   
564  C CA  . GLU   A 69  ? 0.3356 0.2110 0.1921 0.0112  0.0141  -0.0051 70  GLU   A CA  
565  C C   . GLU   A 69  ? 0.3567 0.1953 0.1777 -0.0031 -0.0104 -0.0201 70  GLU   A C   
566  O O   . GLU   A 69  ? 0.4218 0.1970 0.2222 0.0112  0.0019  -0.0272 70  GLU   A O   
567  C CB  . GLU   A 69  ? 0.3965 0.2678 0.2810 0.0623  0.0177  -0.0072 70  GLU   A CB  
568  C CG  . GLU   A 69  ? 0.4407 0.3607 0.3394 0.0466  0.0142  0.0069  70  GLU   A CG  
569  C CD  . GLU   A 69  ? 0.4700 0.4353 0.3719 0.0838  0.0206  0.0154  70  GLU   A CD  
570  O OE1 . GLU   A 69  ? 0.4888 0.4784 0.3740 0.0435  0.0193  -0.0051 70  GLU   A OE1 
571  O OE2 . GLU   A 69  ? 0.5026 0.4842 0.3993 0.0961  0.0164  0.0358  70  GLU   A OE2 
572  N N   . ILE   A 70  ? 0.3463 0.1910 0.1459 0.0015  -0.0232 0.0085  71  ILE   A N   
573  C CA  A ILE   A 70  ? 0.3320 0.1839 0.1444 -0.0143 -0.0327 0.0112  71  ILE   A CA  
574  C CA  B ILE   A 70  ? 0.3184 0.1999 0.1591 -0.0102 -0.0469 0.0031  71  ILE   A CA  
575  C C   . ILE   A 70  ? 0.3272 0.1851 0.1470 -0.0221 -0.0280 -0.0019 71  ILE   A C   
576  O O   . ILE   A 70  ? 0.3503 0.1852 0.1793 0.0114  -0.0186 0.0000  71  ILE   A O   
577  C CB  A ILE   A 70  ? 0.2942 0.1677 0.1297 -0.0027 0.0056  0.0287  71  ILE   A CB  
578  C CB  B ILE   A 70  ? 0.2629 0.2165 0.1761 0.0013  -0.0503 0.0015  71  ILE   A CB  
579  C CG1 A ILE   A 70  ? 0.3698 0.1482 0.1061 -0.0065 0.0010  0.0144  71  ILE   A CG1 
580  C CG1 B ILE   A 70  ? 0.2572 0.2261 0.2032 -0.0385 -0.0690 0.0086  71  ILE   A CG1 
581  C CG2 A ILE   A 70  ? 0.2722 0.1808 0.1737 -0.0086 -0.0071 0.0301  71  ILE   A CG2 
582  C CG2 B ILE   A 70  ? 0.2685 0.2344 0.1727 0.0178  -0.0682 -0.0200 71  ILE   A CG2 
583  C CD1 A ILE   A 70  ? 0.4213 0.1663 0.1161 -0.0338 -0.0195 0.0161  71  ILE   A CD1 
584  C CD1 B ILE   A 70  ? 0.2408 0.2550 0.2030 -0.0748 -0.0515 0.0104  71  ILE   A CD1 
585  N N   . GLN   A 71  ? 0.3069 0.1746 0.1540 -0.0222 -0.0512 0.0169  72  GLN   A N   
586  C CA  . GLN   A 71  ? 0.3014 0.2137 0.1689 -0.0426 -0.0494 0.0293  72  GLN   A CA  
587  C C   . GLN   A 71  ? 0.2797 0.2052 0.1658 -0.0108 -0.0295 0.0082  72  GLN   A C   
588  O O   . GLN   A 71  ? 0.2883 0.2299 0.1808 0.0329  -0.0225 -0.0071 72  GLN   A O   
589  C CB  . GLN   A 71  ? 0.4223 0.3238 0.2171 -0.0655 -0.0919 0.0216  72  GLN   A CB  
590  C CG  . GLN   A 71  ? 0.5547 0.4510 0.2987 -0.0837 -0.0804 -0.0040 72  GLN   A CG  
591  C CD  . GLN   A 71  ? 0.6268 0.5589 0.3587 -0.1166 -0.0838 -0.0478 72  GLN   A CD  
592  O OE1 . GLN   A 71  ? 0.6659 0.5747 0.3526 -0.1373 -0.0480 -0.0666 72  GLN   A OE1 
593  N NE2 . GLN   A 71  ? 0.6326 0.5915 0.3902 -0.1295 -0.1148 -0.0805 72  GLN   A NE2 
594  N N   . HIS   A 72  ? 0.2490 0.1845 0.1553 0.0069  -0.0270 -0.0038 73  HIS   A N   
595  C CA  . HIS   A 72  ? 0.2221 0.1745 0.1561 0.0019  -0.0205 -0.0064 73  HIS   A CA  
596  C C   . HIS   A 72  ? 0.2203 0.1806 0.1710 -0.0079 -0.0189 -0.0182 73  HIS   A C   
597  O O   . HIS   A 72  ? 0.2530 0.1982 0.1683 0.0200  -0.0386 -0.0222 73  HIS   A O   
598  C CB  . HIS   A 72  ? 0.2011 0.1907 0.1602 -0.0256 -0.0296 0.0134  73  HIS   A CB  
599  C CG  . HIS   A 72  ? 0.2198 0.1794 0.1487 0.0113  -0.0130 -0.0123 73  HIS   A CG  
600  N ND1 . HIS   A 72  ? 0.2185 0.1898 0.1556 -0.0043 -0.0166 -0.0049 73  HIS   A ND1 
601  C CD2 . HIS   A 72  ? 0.2394 0.1908 0.1678 0.0099  -0.0175 0.0081  73  HIS   A CD2 
602  C CE1 . HIS   A 72  ? 0.2370 0.1838 0.1706 0.0074  -0.0165 -0.0033 73  HIS   A CE1 
603  N NE2 . HIS   A 72  ? 0.2652 0.1941 0.1622 0.0000  -0.0148 0.0081  73  HIS   A NE2 
604  N N   . PRO   A 73  ? 0.2178 0.2045 0.1655 -0.0193 -0.0037 -0.0370 74  PRO   A N   
605  C CA  . PRO   A 73  ? 0.2490 0.2369 0.1959 -0.0355 0.0171  -0.0451 74  PRO   A CA  
606  C C   . PRO   A 73  ? 0.1960 0.1979 0.1727 0.0037  -0.0013 -0.0271 74  PRO   A C   
607  O O   . PRO   A 73  ? 0.2223 0.2351 0.2085 -0.0129 0.0045  -0.0447 74  PRO   A O   
608  C CB  . PRO   A 73  ? 0.3178 0.2565 0.2223 -0.0866 0.0603  -0.0406 74  PRO   A CB  
609  C CG  . PRO   A 73  ? 0.3114 0.2541 0.2300 -0.0546 0.0415  -0.0337 74  PRO   A CG  
610  C CD  . PRO   A 73  ? 0.2396 0.2007 0.1901 -0.0482 0.0090  -0.0153 74  PRO   A CD  
611  N N   . ASN   A 74  ? 0.2129 0.1620 0.1550 -0.0031 -0.0183 0.0048  75  ASN   A N   
612  C CA  . ASN   A 74  ? 0.2268 0.1478 0.1544 -0.0055 -0.0322 0.0008  75  ASN   A CA  
613  C C   . ASN   A 74  ? 0.2166 0.1563 0.1434 -0.0254 -0.0091 0.0102  75  ASN   A C   
614  O O   . ASN   A 74  ? 0.2265 0.1644 0.1521 -0.0165 -0.0063 -0.0144 75  ASN   A O   
615  C CB  . ASN   A 74  ? 0.2267 0.1731 0.1618 -0.0095 -0.0299 0.0234  75  ASN   A CB  
616  C CG  . ASN   A 74  ? 0.2524 0.1920 0.1662 -0.0188 0.0062  -0.0027 75  ASN   A CG  
617  O OD1 . ASN   A 74  ? 0.3184 0.2140 0.1863 0.0004  0.0037  -0.0100 75  ASN   A OD1 
618  N ND2 . ASN   A 74  ? 0.2513 0.2088 0.1736 -0.0112 0.0104  0.0166  75  ASN   A ND2 
619  N N   . VAL   A 75  ? 0.1999 0.1581 0.1490 0.0040  -0.0035 0.0245  76  VAL   A N   
620  C CA  A VAL   A 75  ? 0.2024 0.1727 0.1587 -0.0004 0.0029  0.0044  76  VAL   A CA  
621  C CA  B VAL   A 75  ? 0.2071 0.1669 0.1516 0.0044  0.0095  0.0099  76  VAL   A CA  
622  C C   . VAL   A 75  ? 0.2170 0.1768 0.1612 0.0172  -0.0030 0.0096  76  VAL   A C   
623  O O   . VAL   A 75  ? 0.2416 0.1966 0.1792 0.0382  -0.0299 -0.0170 76  VAL   A O   
624  C CB  A VAL   A 75  ? 0.2117 0.1878 0.1690 -0.0203 -0.0052 -0.0071 76  VAL   A CB  
625  C CB  B VAL   A 75  ? 0.2193 0.1673 0.1476 -0.0051 0.0132  0.0064  76  VAL   A CB  
626  C CG1 A VAL   A 75  ? 0.2369 0.2056 0.1952 -0.0077 0.0011  -0.0273 76  VAL   A CG1 
627  C CG1 B VAL   A 75  ? 0.2093 0.1873 0.1709 0.0178  0.0027  0.0026  76  VAL   A CG1 
628  C CG2 A VAL   A 75  ? 0.2211 0.2057 0.1819 0.0127  -0.0153 -0.0227 76  VAL   A CG2 
629  C CG2 B VAL   A 75  ? 0.2534 0.1759 0.1585 0.0041  0.0225  -0.0202 76  VAL   A CG2 
630  N N   . ILE   A 76  ? 0.2257 0.1685 0.1851 0.0031  0.0024  0.0352  77  ILE   A N   
631  C CA  . ILE   A 76  ? 0.2460 0.1756 0.2161 0.0387  0.0046  0.0375  77  ILE   A CA  
632  C C   . ILE   A 76  ? 0.2275 0.2325 0.2086 0.0421  0.0204  0.0442  77  ILE   A C   
633  O O   . ILE   A 76  ? 0.2873 0.3235 0.2056 -0.0247 0.0140  0.0857  77  ILE   A O   
634  C CB  . ILE   A 76  ? 0.2475 0.1845 0.2694 0.0115  0.0027  0.0333  77  ILE   A CB  
635  C CG1 . ILE   A 76  ? 0.2750 0.2034 0.3025 0.0636  -0.0035 0.0188  77  ILE   A CG1 
636  C CG2 . ILE   A 76  ? 0.2689 0.2142 0.2793 0.0469  -0.0298 0.0414  77  ILE   A CG2 
637  C CD1 . ILE   A 76  ? 0.3343 0.2509 0.3225 0.0807  0.0085  0.0014  77  ILE   A CD1 
638  N N   . THR   A 77  ? 0.2485 0.2130 0.2074 0.0683  -0.0018 0.0618  78  THR   A N   
639  C CA  . THR   A 77  ? 0.2670 0.2134 0.2188 0.0368  -0.0188 0.0639  78  THR   A CA  
640  C C   . THR   A 77  ? 0.2583 0.1962 0.2068 0.0807  0.0178  0.0294  78  THR   A C   
641  O O   . THR   A 77  ? 0.3608 0.2431 0.2559 0.1214  0.0752  0.0767  78  THR   A O   
642  C CB  . THR   A 77  ? 0.3190 0.1963 0.2409 0.0058  -0.0636 0.0446  78  THR   A CB  
643  O OG1 . THR   A 77  ? 0.3775 0.2270 0.3121 -0.0100 -0.0768 0.0384  78  THR   A OG1 
644  C CG2 . THR   A 77  ? 0.3668 0.2640 0.2658 -0.0253 -0.0573 0.0486  78  THR   A CG2 
645  N N   . LEU   A 78  ? 0.2315 0.1586 0.1660 0.0290  -0.0055 0.0175  79  LEU   A N   
646  C CA  . LEU   A 78  ? 0.2117 0.1814 0.1659 0.0252  -0.0048 0.0087  79  LEU   A CA  
647  C C   . LEU   A 78  ? 0.2089 0.1469 0.1705 0.0310  -0.0369 -0.0125 79  LEU   A C   
648  O O   . LEU   A 78  ? 0.2573 0.2174 0.1929 0.0552  -0.0275 -0.0345 79  LEU   A O   
649  C CB  . LEU   A 78  ? 0.2151 0.1768 0.1963 0.0093  0.0160  0.0313  79  LEU   A CB  
650  C CG  . LEU   A 78  ? 0.2058 0.2081 0.2120 0.0195  0.0251  0.0338  79  LEU   A CG  
651  C CD1 . LEU   A 78  ? 0.2402 0.2121 0.2103 0.0308  -0.0047 0.0431  79  LEU   A CD1 
652  C CD2 . LEU   A 78  ? 0.2085 0.2623 0.2525 0.0175  0.0482  0.0533  79  LEU   A CD2 
653  N N   . HIS   A 79  ? 0.1840 0.1903 0.1513 0.0300  -0.0397 -0.0070 80  HIS   A N   
654  C CA  . HIS   A 79  ? 0.1924 0.1940 0.1869 0.0150  -0.0282 0.0150  80  HIS   A CA  
655  C C   . HIS   A 79  ? 0.2471 0.2023 0.1514 0.0232  -0.0224 -0.0018 80  HIS   A C   
656  O O   . HIS   A 79  ? 0.2999 0.2295 0.1489 0.0155  -0.0200 -0.0236 80  HIS   A O   
657  C CB  . HIS   A 79  ? 0.1494 0.2264 0.2123 0.0277  -0.0183 0.0067  80  HIS   A CB  
658  C CG  . HIS   A 79  ? 0.1980 0.2884 0.2767 0.0185  -0.0101 0.0076  80  HIS   A CG  
659  N ND1 . HIS   A 79  ? 0.3225 0.3365 0.3084 -0.0032 -0.0266 0.0017  80  HIS   A ND1 
660  C CD2 . HIS   A 79  ? 0.2713 0.2906 0.2799 -0.0146 -0.0465 -0.0402 80  HIS   A CD2 
661  C CE1 . HIS   A 79  ? 0.2878 0.3520 0.3162 -0.0216 -0.0535 -0.0099 80  HIS   A CE1 
662  N NE2 . HIS   A 79  ? 0.2997 0.3753 0.3118 -0.0316 -0.0507 -0.0345 80  HIS   A NE2 
663  N N   . GLU   A 80  ? 0.2290 0.1965 0.1574 -0.0159 -0.0188 0.0186  81  GLU   A N   
664  C CA  . GLU   A 80  ? 0.2449 0.2264 0.1551 -0.0379 -0.0269 0.0317  81  GLU   A CA  
665  C C   . GLU   A 80  ? 0.2069 0.1906 0.1365 -0.0060 0.0084  0.0326  81  GLU   A C   
666  O O   . GLU   A 80  ? 0.2261 0.1962 0.1247 -0.0074 0.0159  0.0015  81  GLU   A O   
667  C CB  . GLU   A 80  ? 0.3664 0.3047 0.1961 -0.0025 -0.0408 0.0354  81  GLU   A CB  
668  C CG  . GLU   A 80  ? 0.4325 0.3881 0.2645 0.0558  -0.0006 0.0469  81  GLU   A CG  
669  C CD  . GLU   A 80  ? 0.4310 0.3879 0.2641 0.0748  -0.0029 0.0206  81  GLU   A CD  
670  O OE1 . GLU   A 80  ? 0.4328 0.3956 0.2793 0.0509  -0.0202 0.0159  81  GLU   A OE1 
671  O OE2 . GLU   A 80  ? 0.4711 0.3713 0.2603 0.0938  0.0625  -0.0016 81  GLU   A OE2 
672  N N   . VAL   A 81  ? 0.2180 0.1838 0.1553 -0.0229 -0.0041 0.0037  82  VAL   A N   
673  C CA  . VAL   A 81  ? 0.2159 0.1914 0.1568 0.0055  0.0049  0.0201  82  VAL   A CA  
674  C C   . VAL   A 81  ? 0.2186 0.2079 0.1313 0.0212  0.0074  0.0291  82  VAL   A C   
675  O O   . VAL   A 81  ? 0.2459 0.2511 0.1360 0.0164  0.0130  0.0331  82  VAL   A O   
676  C CB  . VAL   A 81  ? 0.2073 0.2144 0.1573 0.0059  -0.0074 0.0311  82  VAL   A CB  
677  C CG1 . VAL   A 81  ? 0.2510 0.2166 0.1724 0.0083  -0.0159 0.0378  82  VAL   A CG1 
678  C CG2 . VAL   A 81  ? 0.2340 0.2376 0.1884 0.0233  -0.0135 0.0467  82  VAL   A CG2 
679  N N   . TYR   A 82  ? 0.2361 0.1997 0.1430 0.0204  0.0007  0.0305  83  TYR   A N   
680  C CA  . TYR   A 82  ? 0.2404 0.1954 0.1612 -0.0058 0.0083  0.0334  83  TYR   A CA  
681  C C   . TYR   A 82  ? 0.2809 0.1935 0.1267 0.0136  0.0031  0.0350  83  TYR   A C   
682  O O   . TYR   A 82  ? 0.2842 0.2199 0.1323 0.0206  -0.0067 0.0299  83  TYR   A O   
683  C CB  . TYR   A 82  ? 0.2194 0.2028 0.1675 0.0189  0.0248  0.0250  83  TYR   A CB  
684  C CG  . TYR   A 82  ? 0.2430 0.2186 0.1761 -0.0043 0.0085  0.0428  83  TYR   A CG  
685  C CD1 . TYR   A 82  ? 0.2381 0.2241 0.2024 -0.0032 0.0506  0.0194  83  TYR   A CD1 
686  C CD2 . TYR   A 82  ? 0.1902 0.2664 0.1902 -0.0036 0.0068  0.0472  83  TYR   A CD2 
687  C CE1 . TYR   A 82  ? 0.2607 0.2639 0.2301 0.0119  0.0352  0.0156  83  TYR   A CE1 
688  C CE2 . TYR   A 82  ? 0.2461 0.2644 0.2028 -0.0467 0.0104  0.0456  83  TYR   A CE2 
689  C CZ  . TYR   A 82  ? 0.2360 0.2472 0.2168 -0.0349 0.0062  0.0298  83  TYR   A CZ  
690  O OH  . TYR   A 82  ? 0.2719 0.3017 0.2611 -0.0346 0.0063  -0.0017 83  TYR   A OH  
691  N N   . GLU   A 83  ? 0.2614 0.2157 0.1399 0.0005  0.0012  0.0295  84  GLU   A N   
692  C CA  . GLU   A 83  ? 0.2560 0.2061 0.1590 0.0006  0.0050  0.0396  84  GLU   A CA  
693  C C   . GLU   A 83  ? 0.2836 0.2082 0.1854 -0.0023 0.0044  0.0395  84  GLU   A C   
694  O O   . GLU   A 83  ? 0.2979 0.1998 0.1844 0.0004  -0.0076 0.0332  84  GLU   A O   
695  C CB  . GLU   A 83  ? 0.2392 0.2554 0.1535 -0.0024 0.0174  0.0208  84  GLU   A CB  
696  C CG  . GLU   A 83  ? 0.2513 0.2639 0.1291 -0.0043 0.0078  0.0231  84  GLU   A CG  
697  C CD  . GLU   A 83  ? 0.2750 0.2517 0.1535 -0.0130 0.0196  -0.0172 84  GLU   A CD  
698  O OE1 . GLU   A 83  ? 0.2922 0.2179 0.1741 -0.0081 0.0190  -0.0029 84  GLU   A OE1 
699  O OE2 . GLU   A 83  ? 0.2934 0.2780 0.1787 -0.0202 0.0122  -0.0076 84  GLU   A OE2 
700  N N   . ASN   A 84  ? 0.3042 0.1874 0.1870 0.0151  0.0024  0.0326  85  ASN   A N   
701  C CA  . ASN   A 84  ? 0.3072 0.2102 0.2219 0.0008  0.0051  0.0310  85  ASN   A CA  
702  C C   . ASN   A 84  ? 0.3510 0.2232 0.2208 -0.0076 0.0064  0.0305  85  ASN   A C   
703  O O   . ASN   A 84  ? 0.3365 0.2415 0.2214 -0.0096 -0.0127 0.0207  85  ASN   A O   
704  C CB  . ASN   A 84  ? 0.2682 0.2413 0.2204 0.0066  0.0102  0.0159  85  ASN   A CB  
705  C CG  . ASN   A 84  ? 0.2670 0.2769 0.2454 0.0060  0.0085  0.0009  85  ASN   A CG  
706  O OD1 . ASN   A 84  ? 0.2825 0.2775 0.2499 0.0052  -0.0052 0.0042  85  ASN   A OD1 
707  N ND2 . ASN   A 84  ? 0.3232 0.3603 0.2717 0.0142  0.0231  -0.0105 85  ASN   A ND2 
708  N N   . LYS   A 85  ? 0.4007 0.2217 0.2231 -0.0040 0.0101  0.0547  86  LYS   A N   
709  C CA  . LYS   A 85  ? 0.4227 0.2458 0.2592 0.0132  0.0092  0.0252  86  LYS   A CA  
710  C C   . LYS   A 85  ? 0.3912 0.2297 0.2449 -0.0149 0.0200  0.0127  86  LYS   A C   
711  O O   . LYS   A 85  ? 0.4091 0.2514 0.2350 -0.0126 0.0461  -0.0090 86  LYS   A O   
712  C CB  . LYS   A 85  ? 0.4912 0.3128 0.3163 0.0197  -0.0342 0.0427  86  LYS   A CB  
713  C CG  . LYS   A 85  ? 0.5476 0.3968 0.3742 0.0177  -0.0512 0.0182  86  LYS   A CG  
714  C CD  . LYS   A 85  ? 0.5677 0.4450 0.4202 0.0359  -0.0499 0.0082  86  LYS   A CD  
715  C CE  . LYS   A 85  ? 0.5910 0.4759 0.4600 0.0585  -0.0413 0.0128  86  LYS   A CE  
716  N NZ  . LYS   A 85  ? 0.6120 0.4987 0.4799 0.0852  -0.0453 0.0134  86  LYS   A NZ  
717  N N   . THR   A 86  ? 0.3364 0.2123 0.2255 0.0197  0.0177  0.0136  87  THR   A N   
718  C CA  . THR   A 86  ? 0.3772 0.2187 0.2310 0.0484  0.0232  0.0052  87  THR   A CA  
719  C C   . THR   A 86  ? 0.3436 0.2304 0.2129 0.0240  0.0325  0.0057  87  THR   A C   
720  O O   . THR   A 86  ? 0.3441 0.2480 0.2148 0.0125  0.0035  -0.0084 87  THR   A O   
721  C CB  . THR   A 86  ? 0.4328 0.2556 0.2644 0.0635  0.0318  -0.0160 87  THR   A CB  
722  O OG1 . THR   A 86  ? 0.4803 0.3131 0.2944 0.0888  0.0398  -0.0197 87  THR   A OG1 
723  C CG2 . THR   A 86  ? 0.4557 0.2569 0.2680 0.0864  0.0422  -0.0134 87  THR   A CG2 
724  N N   . ASP   A 87  ? 0.3278 0.2196 0.1930 0.0162  0.0201  0.0087  88  ASP   A N   
725  C CA  . ASP   A 87  ? 0.3056 0.2221 0.1968 0.0141  0.0146  0.0143  88  ASP   A CA  
726  C C   . ASP   A 87  ? 0.2741 0.1928 0.1691 0.0004  -0.0330 0.0292  88  ASP   A C   
727  O O   . ASP   A 87  ? 0.2852 0.2341 0.1775 0.0285  -0.0288 0.0115  88  ASP   A O   
728  C CB  . ASP   A 87  ? 0.3569 0.2785 0.2419 0.0321  0.0432  -0.0072 88  ASP   A CB  
729  C CG  . ASP   A 87  ? 0.4846 0.3750 0.3020 0.1021  0.0282  -0.0128 88  ASP   A CG  
730  O OD1 . ASP   A 87  ? 0.5609 0.4496 0.3615 0.1110  0.0104  -0.0133 88  ASP   A OD1 
731  O OD2 . ASP   A 87  ? 0.5306 0.4084 0.3092 0.1270  0.0344  -0.0331 88  ASP   A OD2 
732  N N   . VAL   A 88  ? 0.2743 0.1889 0.1493 -0.0238 -0.0374 0.0133  89  VAL   A N   
733  C CA  . VAL   A 88  ? 0.2715 0.1929 0.1717 -0.0256 -0.0012 0.0095  89  VAL   A CA  
734  C C   . VAL   A 88  ? 0.2559 0.2146 0.1447 -0.0171 -0.0185 0.0165  89  VAL   A C   
735  O O   . VAL   A 88  ? 0.3017 0.2715 0.1559 -0.0435 -0.0389 0.0268  89  VAL   A O   
736  C CB  . VAL   A 88  ? 0.2448 0.2038 0.2130 -0.0206 -0.0080 0.0196  89  VAL   A CB  
737  C CG1 . VAL   A 88  ? 0.2728 0.2239 0.2316 -0.0116 -0.0151 -0.0223 89  VAL   A CG1 
738  C CG2 . VAL   A 88  ? 0.2633 0.2218 0.2071 -0.0205 0.0225  0.0335  89  VAL   A CG2 
739  N N   . ILE   A 89  ? 0.2250 0.1944 0.1604 -0.0083 -0.0080 0.0051  90  ILE   A N   
740  C CA  . ILE   A 89  ? 0.2212 0.1889 0.1603 -0.0039 0.0193  -0.0051 90  ILE   A CA  
741  C C   . ILE   A 89  ? 0.2300 0.1951 0.1290 0.0018  0.0037  0.0047  90  ILE   A C   
742  O O   . ILE   A 89  ? 0.2455 0.2056 0.1334 -0.0063 -0.0061 0.0131  90  ILE   A O   
743  C CB  . ILE   A 89  ? 0.2478 0.2038 0.1893 -0.0067 0.0110  0.0119  90  ILE   A CB  
744  C CG1 . ILE   A 89  ? 0.2756 0.2035 0.2146 0.0160  -0.0018 0.0233  90  ILE   A CG1 
745  C CG2 . ILE   A 89  ? 0.2681 0.2506 0.1912 0.0042  0.0184  0.0132  90  ILE   A CG2 
746  C CD1 . ILE   A 89  ? 0.3803 0.2296 0.2509 0.0150  0.0299  0.0193  90  ILE   A CD1 
747  N N   . LEU   A 90  ? 0.2251 0.1750 0.1487 0.0211  0.0085  0.0141  91  LEU   A N   
748  C CA  . LEU   A 90  ? 0.2195 0.1956 0.1495 0.0336  -0.0011 0.0081  91  LEU   A CA  
749  C C   . LEU   A 90  ? 0.2309 0.1858 0.1275 0.0071  0.0084  -0.0183 91  LEU   A C   
750  O O   . LEU   A 90  ? 0.2762 0.2232 0.1340 -0.0106 0.0214  -0.0372 91  LEU   A O   
751  C CB  . LEU   A 90  ? 0.2039 0.2434 0.1810 0.0203  -0.0083 0.0050  91  LEU   A CB  
752  C CG  . LEU   A 90  ? 0.2265 0.2839 0.2342 0.0118  0.0009  0.0442  91  LEU   A CG  
753  C CD1 . LEU   A 90  ? 0.2548 0.2889 0.2666 0.0250  -0.0487 0.0714  91  LEU   A CD1 
754  C CD2 . LEU   A 90  ? 0.2666 0.3210 0.2381 -0.0054 -0.0022 0.0295  91  LEU   A CD2 
755  N N   . ILE   A 91  ? 0.2029 0.1647 0.1340 0.0181  0.0064  0.0064  92  ILE   A N   
756  C CA  . ILE   A 91  ? 0.1940 0.1788 0.1450 0.0234  0.0063  -0.0039 92  ILE   A CA  
757  C C   . ILE   A 91  ? 0.1952 0.1644 0.1272 0.0450  0.0063  -0.0088 92  ILE   A C   
758  O O   . ILE   A 91  ? 0.2335 0.1623 0.1425 0.0382  0.0001  -0.0229 92  ILE   A O   
759  C CB  . ILE   A 91  ? 0.1978 0.2024 0.1655 0.0064  -0.0150 0.0287  92  ILE   A CB  
760  C CG1 . ILE   A 91  ? 0.2576 0.1937 0.1607 0.0206  -0.0125 0.0028  92  ILE   A CG1 
761  C CG2 . ILE   A 91  ? 0.1904 0.2390 0.1699 -0.0136 0.0126  0.0338  92  ILE   A CG2 
762  C CD1 . ILE   A 91  ? 0.2971 0.2047 0.1849 0.0477  -0.0143 -0.0093 92  ILE   A CD1 
763  N N   . LEU   A 92  ? 0.2219 0.1704 0.1411 0.0291  0.0006  0.0137  93  LEU   A N   
764  C CA  . LEU   A 92  ? 0.2393 0.1644 0.1532 0.0248  -0.0238 0.0228  93  LEU   A CA  
765  C C   . LEU   A 92  ? 0.2438 0.1462 0.1412 0.0256  -0.0092 0.0077  93  LEU   A C   
766  O O   . LEU   A 92  ? 0.2343 0.1718 0.1463 0.0470  -0.0032 -0.0079 93  LEU   A O   
767  C CB  . LEU   A 92  ? 0.2439 0.1964 0.1881 0.0201  -0.0265 0.0112  93  LEU   A CB  
768  C CG  . LEU   A 92  ? 0.2405 0.2423 0.2255 0.0152  -0.0041 -0.0105 93  LEU   A CG  
769  C CD1 . LEU   A 92  ? 0.3325 0.2544 0.2491 0.0145  -0.0194 -0.0425 93  LEU   A CD1 
770  C CD2 . LEU   A 92  ? 0.2470 0.2503 0.2394 0.0246  0.0271  -0.0495 93  LEU   A CD2 
771  N N   . GLU   A 93  ? 0.2888 0.1589 0.1505 0.0533  -0.0094 0.0273  94  GLU   A N   
772  C CA  . GLU   A 93  ? 0.3266 0.1421 0.1701 0.0355  0.0162  0.0104  94  GLU   A CA  
773  C C   . GLU   A 93  ? 0.2889 0.1843 0.1516 0.0162  -0.0109 0.0217  94  GLU   A C   
774  O O   . GLU   A 93  ? 0.3097 0.2521 0.1617 -0.0336 -0.0260 0.0270  94  GLU   A O   
775  C CB  . GLU   A 93  ? 0.3867 0.1612 0.2281 0.0500  0.0249  0.0105  94  GLU   A CB  
776  C CG  . GLU   A 93  ? 0.3747 0.1794 0.2684 0.0481  0.0197  0.0288  94  GLU   A CG  
777  C CD  . GLU   A 93  ? 0.3362 0.2282 0.3146 0.0388  0.0054  0.0532  94  GLU   A CD  
778  O OE1 . GLU   A 93  ? 0.3163 0.2193 0.2995 -0.0073 0.0268  0.0514  94  GLU   A OE1 
779  O OE2 . GLU   A 93  ? 0.3824 0.2807 0.3767 0.0290  -0.0122 0.0322  94  GLU   A OE2 
780  N N   . LEU   A 94  ? 0.2952 0.1975 0.1424 0.0427  0.0001  -0.0025 95  LEU   A N   
781  C CA  . LEU   A 94  ? 0.2761 0.2069 0.1570 0.0249  -0.0007 0.0000  95  LEU   A CA  
782  C C   . LEU   A 94  ? 0.3063 0.2386 0.1806 -0.0001 -0.0162 0.0188  95  LEU   A C   
783  O O   . LEU   A 94  ? 0.3595 0.2628 0.2025 -0.0095 -0.0443 0.0525  95  LEU   A O   
784  C CB  . LEU   A 94  ? 0.3043 0.2234 0.1502 0.0228  -0.0020 -0.0067 95  LEU   A CB  
785  C CG  . LEU   A 94  ? 0.2960 0.2431 0.1750 0.0203  0.0000  -0.0199 95  LEU   A CG  
786  C CD1 . LEU   A 94  ? 0.3321 0.2182 0.2049 0.0131  -0.0042 -0.0260 95  LEU   A CD1 
787  C CD2 . LEU   A 94  ? 0.3037 0.2987 0.2072 -0.0038 0.0032  -0.0167 95  LEU   A CD2 
788  N N   . VAL   A 95  ? 0.2661 0.2501 0.1746 0.0168  -0.0182 0.0349  96  VAL   A N   
789  C CA  . VAL   A 95  ? 0.2810 0.2872 0.1786 0.0357  -0.0108 0.0399  96  VAL   A CA  
790  C C   . VAL   A 95  ? 0.2917 0.3277 0.2066 0.0322  0.0115  0.0454  96  VAL   A C   
791  O O   . VAL   A 95  ? 0.3749 0.3342 0.2176 0.0229  -0.0067 0.0327  96  VAL   A O   
792  C CB  . VAL   A 95  ? 0.2937 0.2850 0.1840 0.0398  -0.0086 0.0460  96  VAL   A CB  
793  C CG1 . VAL   A 95  ? 0.3378 0.2989 0.2141 0.0530  0.0034  0.0502  96  VAL   A CG1 
794  C CG2 . VAL   A 95  ? 0.3161 0.3120 0.2046 0.0453  -0.0084 0.0268  96  VAL   A CG2 
795  N N   . ALA   A 96  ? 0.2697 0.3769 0.2103 0.0647  0.0293  0.0525  97  ALA   A N   
796  C CA  . ALA   A 96  ? 0.2845 0.4333 0.2457 0.0612  0.0207  0.0417  97  ALA   A CA  
797  C C   . ALA   A 96  ? 0.2747 0.4171 0.2339 0.0735  0.0296  0.0333  97  ALA   A C   
798  O O   . ALA   A 96  ? 0.3200 0.4392 0.2512 0.1037  0.0244  0.0315  97  ALA   A O   
799  C CB  . ALA   A 96  ? 0.3006 0.4708 0.2651 0.0496  0.0200  0.0431  97  ALA   A CB  
800  N N   . GLY   A 97  ? 0.2480 0.3834 0.2044 0.0610  0.0163  0.0219  98  GLY   A N   
801  C CA  . GLY   A 97  ? 0.2372 0.3939 0.1944 0.0375  0.0434  0.0271  98  GLY   A CA  
802  C C   . GLY   A 97  ? 0.2368 0.4046 0.2004 0.0288  0.0320  0.0340  98  GLY   A C   
803  O O   . GLY   A 97  ? 0.2673 0.4231 0.2050 0.0359  0.0307  0.0264  98  GLY   A O   
804  N N   . GLY   A 98  ? 0.2528 0.4019 0.2097 0.0487  0.0099  0.0258  99  GLY   A N   
805  C CA  . GLY   A 98  ? 0.2514 0.4210 0.2240 0.0626  0.0267  -0.0177 99  GLY   A CA  
806  C C   . GLY   A 98  ? 0.2434 0.4189 0.2245 0.0864  0.0356  -0.0443 99  GLY   A C   
807  O O   . GLY   A 98  ? 0.2446 0.3889 0.2488 0.0816  0.0413  -0.0402 99  GLY   A O   
808  N N   . GLU   A 99  ? 0.2840 0.4281 0.2488 0.0730  0.0259  -0.0458 100 GLU   A N   
809  C CA  . GLU   A 99  ? 0.3146 0.4302 0.2534 0.0535  0.0411  -0.0329 100 GLU   A CA  
810  C C   . GLU   A 99  ? 0.2624 0.3929 0.2259 0.0697  0.0521  -0.0167 100 GLU   A C   
811  O O   . GLU   A 99  ? 0.2829 0.4018 0.2171 0.0619  0.0531  -0.0277 100 GLU   A O   
812  C CB  . GLU   A 99  ? 0.3868 0.4829 0.3031 0.0778  0.0084  0.0091  100 GLU   A CB  
813  C CG  . GLU   A 99  ? 0.4681 0.5247 0.3447 0.0989  -0.0207 0.0140  100 GLU   A CG  
814  C CD  . GLU   A 99  ? 0.5559 0.5680 0.3953 0.1306  -0.0311 0.0117  100 GLU   A CD  
815  O OE1 . GLU   A 99  ? 0.5456 0.5680 0.4011 0.1565  -0.0265 -0.0056 100 GLU   A OE1 
816  O OE2 . GLU   A 99  ? 0.6346 0.6157 0.4262 0.1122  -0.0454 0.0146  100 GLU   A OE2 
817  N N   . LEU   A 100 ? 0.2802 0.3497 0.2433 0.0493  0.0406  0.0032  101 LEU   A N   
818  C CA  . LEU   A 100 ? 0.3031 0.3380 0.2273 0.0553  0.0495  -0.0123 101 LEU   A CA  
819  C C   . LEU   A 100 ? 0.3309 0.3523 0.2275 0.0208  0.0691  -0.0164 101 LEU   A C   
820  O O   . LEU   A 100 ? 0.3560 0.3832 0.2136 0.0079  0.0774  0.0071  101 LEU   A O   
821  C CB  . LEU   A 100 ? 0.2999 0.3093 0.2556 0.0686  0.0438  -0.0026 101 LEU   A CB  
822  C CG  . LEU   A 100 ? 0.2904 0.3216 0.2628 0.0148  0.0375  0.0138  101 LEU   A CG  
823  C CD1 . LEU   A 100 ? 0.2958 0.3054 0.2883 -0.0244 0.0591  0.0213  101 LEU   A CD1 
824  C CD2 . LEU   A 100 ? 0.2690 0.3359 0.2536 0.0662  0.0444  -0.0090 101 LEU   A CD2 
825  N N   . PHE   A 101 ? 0.3246 0.3375 0.2332 0.0112  0.0566  -0.0413 102 PHE   A N   
826  C CA  . PHE   A 101 ? 0.3631 0.3456 0.2444 -0.0069 0.0780  -0.0473 102 PHE   A CA  
827  C C   . PHE   A 101 ? 0.3615 0.3889 0.2294 0.0099  0.0808  -0.0407 102 PHE   A C   
828  O O   . PHE   A 101 ? 0.3719 0.3796 0.2151 -0.0036 0.0754  -0.0458 102 PHE   A O   
829  C CB  . PHE   A 101 ? 0.3720 0.3307 0.2893 -0.0071 0.0583  -0.0625 102 PHE   A CB  
830  C CG  . PHE   A 101 ? 0.3761 0.3218 0.3130 0.0044  0.0526  -0.0806 102 PHE   A CG  
831  C CD1 . PHE   A 101 ? 0.3980 0.3407 0.3407 -0.0234 0.0359  -0.0791 102 PHE   A CD1 
832  C CD2 . PHE   A 101 ? 0.4128 0.3441 0.3385 0.0131  0.0442  -0.0966 102 PHE   A CD2 
833  C CE1 . PHE   A 101 ? 0.4250 0.3557 0.3525 -0.0042 0.0349  -0.0909 102 PHE   A CE1 
834  C CE2 . PHE   A 101 ? 0.4252 0.3616 0.3493 0.0014  0.0193  -0.1002 102 PHE   A CE2 
835  C CZ  . PHE   A 101 ? 0.4359 0.3650 0.3575 -0.0113 0.0183  -0.0987 102 PHE   A CZ  
836  N N   . ASP   A 102 ? 0.3864 0.4325 0.2620 0.0557  0.1006  -0.0252 103 ASP   A N   
837  C CA  . ASP   A 102 ? 0.3995 0.4737 0.2855 0.0862  0.1109  -0.0012 103 ASP   A CA  
838  C C   . ASP   A 102 ? 0.3860 0.4702 0.2462 0.0648  0.0741  -0.0176 103 ASP   A C   
839  O O   . ASP   A 102 ? 0.3992 0.4954 0.2610 0.0297  0.0960  -0.0361 103 ASP   A O   
840  C CB  . ASP   A 102 ? 0.4669 0.5242 0.3403 0.1425  0.1140  0.0145  103 ASP   A CB  
841  C CG  . ASP   A 102 ? 0.5920 0.5841 0.3933 0.1596  0.1117  0.0325  103 ASP   A CG  
842  O OD1 . ASP   A 102 ? 0.6429 0.6089 0.4258 0.1598  0.1122  0.0406  103 ASP   A OD1 
843  O OD2 . ASP   A 102 ? 0.6538 0.5948 0.4248 0.1557  0.1018  0.0489  103 ASP   A OD2 
844  N N   . PHE   A 103 ? 0.3630 0.4365 0.2225 0.0356  0.0549  -0.0032 104 PHE   A N   
845  C CA  . PHE   A 103 ? 0.3873 0.4462 0.1965 0.0099  0.0442  0.0002  104 PHE   A CA  
846  C C   . PHE   A 103 ? 0.3550 0.4425 0.1870 -0.0076 0.0652  0.0202  104 PHE   A C   
847  O O   . PHE   A 103 ? 0.3685 0.4477 0.2059 -0.0160 0.0403  0.0054  104 PHE   A O   
848  C CB  . PHE   A 103 ? 0.3455 0.4403 0.1793 0.0016  0.0564  0.0166  104 PHE   A CB  
849  C CG  . PHE   A 103 ? 0.3524 0.4643 0.1793 -0.0076 0.0471  0.0473  104 PHE   A CG  
850  C CD1 . PHE   A 103 ? 0.3871 0.4768 0.1978 0.0048  0.0532  0.0460  104 PHE   A CD1 
851  C CD2 . PHE   A 103 ? 0.3601 0.4778 0.1992 -0.0055 0.0557  0.0434  104 PHE   A CD2 
852  C CE1 . PHE   A 103 ? 0.4083 0.4792 0.2090 0.0116  0.0338  0.0546  104 PHE   A CE1 
853  C CE2 . PHE   A 103 ? 0.4103 0.4931 0.2149 0.0037  0.0516  0.0460  104 PHE   A CE2 
854  C CZ  . PHE   A 103 ? 0.4172 0.4891 0.2102 -0.0022 0.0510  0.0506  104 PHE   A CZ  
855  N N   . LEU   A 104 ? 0.3199 0.4531 0.2221 -0.0017 0.0266  0.0352  105 LEU   A N   
856  C CA  . LEU   A 104 ? 0.3896 0.4817 0.2503 0.0057  0.0499  0.0273  105 LEU   A CA  
857  C C   . LEU   A 104 ? 0.4536 0.5279 0.2618 -0.0127 0.0650  -0.0031 105 LEU   A C   
858  O O   . LEU   A 104 ? 0.4581 0.5265 0.2514 -0.0233 0.0505  0.0160  105 LEU   A O   
859  C CB  . LEU   A 104 ? 0.3810 0.4543 0.2688 0.0229  0.0600  0.0624  105 LEU   A CB  
860  C CG  . LEU   A 104 ? 0.4299 0.4291 0.3067 0.0529  0.0369  0.0722  105 LEU   A CG  
861  C CD1 . LEU   A 104 ? 0.4144 0.4261 0.3139 0.0574  0.0340  0.0637  105 LEU   A CD1 
862  C CD2 . LEU   A 104 ? 0.4382 0.4208 0.3160 0.0608  0.0190  0.0857  105 LEU   A CD2 
863  N N   . ALA   A 105 ? 0.5111 0.5629 0.2839 -0.0149 0.0975  -0.0359 106 ALA   A N   
864  C CA  . ALA   A 105 ? 0.5678 0.6088 0.3340 -0.0192 0.1501  -0.0502 106 ALA   A CA  
865  C C   . ALA   A 105 ? 0.5969 0.6559 0.3767 -0.0498 0.2048  -0.0397 106 ALA   A C   
866  O O   . ALA   A 105 ? 0.6261 0.6708 0.3654 -0.0645 0.1958  -0.0482 106 ALA   A O   
867  C CB  . ALA   A 105 ? 0.5957 0.6104 0.3417 -0.0108 0.1404  -0.0562 106 ALA   A CB  
868  N N   . GLU   A 106 ? 0.6218 0.6873 0.4336 -0.0822 0.2416  -0.0238 107 GLU   A N   
869  C CA  . GLU   A 106 ? 0.6876 0.7210 0.4969 -0.1141 0.2409  -0.0096 107 GLU   A CA  
870  C C   . GLU   A 106 ? 0.6807 0.6808 0.5143 -0.0998 0.2008  -0.0005 107 GLU   A C   
871  O O   . GLU   A 106 ? 0.6637 0.6784 0.4995 -0.1107 0.2067  0.0096  107 GLU   A O   
872  C CB  . GLU   A 106 ? 0.8032 0.7921 0.5551 -0.1538 0.2448  -0.0074 107 GLU   A CB  
873  C CG  . GLU   A 106 ? 0.9405 0.8534 0.6016 -0.1847 0.2358  -0.0047 107 GLU   A CG  
874  C CD  . GLU   A 106 ? 1.0597 0.8990 0.6401 -0.2084 0.2331  -0.0059 107 GLU   A CD  
875  O OE1 . GLU   A 106 ? 1.1277 0.9173 0.6561 -0.2095 0.2245  -0.0059 107 GLU   A OE1 
876  O OE2 . GLU   A 106 ? 1.0808 0.9147 0.6550 -0.2180 0.2330  -0.0060 107 GLU   A OE2 
877  N N   . LYS   A 107 ? 0.7112 0.6395 0.5386 -0.0570 0.1401  -0.0053 108 LYS   A N   
878  C CA  . LYS   A 107 ? 0.7430 0.6090 0.5553 -0.0126 0.1073  -0.0088 108 LYS   A CA  
879  C C   . LYS   A 107 ? 0.7173 0.5735 0.5390 0.0061  0.1170  -0.0323 108 LYS   A C   
880  O O   . LYS   A 107 ? 0.6849 0.5652 0.5373 -0.0093 0.1298  -0.0293 108 LYS   A O   
881  C CB  . LYS   A 107 ? 0.7893 0.6170 0.5788 0.0218  0.0762  0.0010  108 LYS   A CB  
882  C CG  . LYS   A 107 ? 0.8417 0.6301 0.5980 0.0500  0.0499  0.0140  108 LYS   A CG  
883  C CD  . LYS   A 107 ? 0.8813 0.6370 0.6170 0.0720  0.0290  0.0246  108 LYS   A CD  
884  C CE  . LYS   A 107 ? 0.9085 0.6451 0.6304 0.0820  0.0165  0.0303  108 LYS   A CE  
885  N NZ  . LYS   A 107 ? 0.9238 0.6538 0.6360 0.0818  0.0074  0.0348  108 LYS   A NZ  
886  N N   . GLU   A 108 ? 0.7329 0.5528 0.5244 0.0400  0.1183  -0.0537 109 GLU   A N   
887  C CA  . GLU   A 108 ? 0.7547 0.5395 0.5212 0.0435  0.1078  -0.0730 109 GLU   A CA  
888  C C   . GLU   A 108 ? 0.6263 0.4445 0.4643 0.0601  0.0997  -0.0551 109 GLU   A C   
889  O O   . GLU   A 108 ? 0.6102 0.4227 0.4760 0.0636  0.0625  -0.0302 109 GLU   A O   
890  C CB  . GLU   A 108 ? 0.9016 0.6268 0.5684 0.0273  0.1089  -0.1071 109 GLU   A CB  
891  C CG  . GLU   A 108 ? 1.0383 0.7062 0.6179 0.0039  0.1025  -0.1357 109 GLU   A CG  
892  C CD  . GLU   A 108 ? 1.1434 0.7685 0.6564 -0.0218 0.0946  -0.1566 109 GLU   A CD  
893  O OE1 . GLU   A 108 ? 1.1791 0.7910 0.6677 -0.0276 0.1011  -0.1671 109 GLU   A OE1 
894  O OE2 . GLU   A 108 ? 1.1802 0.7915 0.6729 -0.0316 0.0924  -0.1591 109 GLU   A OE2 
895  N N   . SER   A 109 ? 0.5256 0.3823 0.4007 0.0403  0.1172  -0.0519 110 SER   A N   
896  C CA  . SER   A 109 ? 0.4779 0.3294 0.3387 0.0182  0.1012  -0.0232 110 SER   A CA  
897  C C   . SER   A 109 ? 0.4151 0.2762 0.3053 -0.0109 0.0697  -0.0111 110 SER   A C   
898  O O   . SER   A 109 ? 0.4039 0.2866 0.3341 -0.0489 0.0627  -0.0139 110 SER   A O   
899  C CB  . SER   A 109 ? 0.4970 0.3302 0.3267 -0.0030 0.0817  0.0285  110 SER   A CB  
900  O OG  . SER   A 109 ? 0.5447 0.3715 0.3481 -0.0237 0.0189  0.0305  110 SER   A OG  
901  N N   . LEU   A 110 ? 0.3299 0.2080 0.2556 -0.0151 0.0138  -0.0044 111 LEU   A N   
902  C CA  . LEU   A 110 ? 0.3472 0.1997 0.2238 -0.0027 -0.0148 0.0148  111 LEU   A CA  
903  C C   . LEU   A 110 ? 0.3748 0.2146 0.2231 0.0032  -0.0193 0.0130  111 LEU   A C   
904  O O   . LEU   A 110 ? 0.3326 0.2365 0.2496 -0.0015 -0.0263 0.0131  111 LEU   A O   
905  C CB  . LEU   A 110 ? 0.3272 0.2134 0.2271 0.0012  -0.0130 0.0338  111 LEU   A CB  
906  C CG  . LEU   A 110 ? 0.2971 0.2272 0.2533 0.0132  -0.0320 0.0422  111 LEU   A CG  
907  C CD1 . LEU   A 110 ? 0.3288 0.2387 0.2636 -0.0141 -0.0078 0.0328  111 LEU   A CD1 
908  C CD2 . LEU   A 110 ? 0.3413 0.2842 0.2713 0.0301  -0.0303 0.0253  111 LEU   A CD2 
909  N N   . THR   A 111 ? 0.4136 0.2012 0.2052 -0.0021 -0.0176 0.0394  112 THR   A N   
910  C CA  . THR   A 111 ? 0.3810 0.2160 0.1971 0.0105  -0.0139 0.0634  112 THR   A CA  
911  C C   . THR   A 111 ? 0.3598 0.2021 0.1853 0.0048  -0.0292 0.0492  112 THR   A C   
912  O O   . THR   A 111 ? 0.3109 0.2016 0.1783 -0.0250 -0.0318 0.0460  112 THR   A O   
913  C CB  . THR   A 111 ? 0.3707 0.2521 0.2032 -0.0040 0.0101  0.0402  112 THR   A CB  
914  O OG1 . THR   A 111 ? 0.3527 0.2600 0.2039 0.0313  0.0064  0.0529  112 THR   A OG1 
915  C CG2 . THR   A 111 ? 0.4024 0.2889 0.2245 -0.0236 0.0389  0.0450  112 THR   A CG2 
916  N N   . GLU   A 112 ? 0.3259 0.1836 0.1980 0.0166  -0.0168 0.0658  113 GLU   A N   
917  C CA  . GLU   A 112 ? 0.3078 0.1987 0.2056 0.0229  -0.0106 0.0413  113 GLU   A CA  
918  C C   . GLU   A 112 ? 0.2741 0.2100 0.1961 0.0037  -0.0038 0.0544  113 GLU   A C   
919  O O   . GLU   A 112 ? 0.3163 0.2330 0.1894 0.0081  0.0077  0.0666  113 GLU   A O   
920  C CB  . GLU   A 112 ? 0.2833 0.1803 0.2283 0.0010  -0.0359 0.0486  113 GLU   A CB  
921  C CG  . GLU   A 112 ? 0.3246 0.2046 0.2286 -0.0059 -0.0083 0.0522  113 GLU   A CG  
922  C CD  . GLU   A 112 ? 0.2872 0.2308 0.2048 0.0158  0.0010  0.0497  113 GLU   A CD  
923  O OE1 . GLU   A 112 ? 0.3081 0.2112 0.1875 -0.0114 0.0214  0.0426  113 GLU   A OE1 
924  O OE2 . GLU   A 112 ? 0.3146 0.2667 0.2356 0.0167  -0.0039 0.0375  113 GLU   A OE2 
925  N N   . GLU   A 113 ? 0.2914 0.2111 0.1961 0.0004  -0.0050 0.0554  114 GLU   A N   
926  C CA  . GLU   A 113 ? 0.2985 0.2233 0.2152 -0.0265 -0.0021 0.0697  114 GLU   A CA  
927  C C   . GLU   A 113 ? 0.2938 0.2278 0.1880 -0.0024 -0.0094 0.0701  114 GLU   A C   
928  O O   . GLU   A 113 ? 0.3132 0.2429 0.1762 -0.0291 -0.0258 0.0686  114 GLU   A O   
929  C CB  . GLU   A 113 ? 0.3261 0.2889 0.2633 -0.0402 0.0082  0.1050  114 GLU   A CB  
930  C CG  . GLU   A 113 ? 0.3646 0.3634 0.3209 -0.0218 -0.0155 0.0958  114 GLU   A CG  
931  C CD  . GLU   A 113 ? 0.4280 0.4882 0.3891 0.0164  -0.0548 0.0661  114 GLU   A CD  
932  O OE1 . GLU   A 113 ? 0.4771 0.5463 0.4293 0.0205  -0.0762 0.0541  114 GLU   A OE1 
933  O OE2 . GLU   A 113 ? 0.4201 0.5313 0.4390 0.0451  -0.0718 0.0520  114 GLU   A OE2 
934  N N   . GLU   A 114 ? 0.2357 0.2006 0.2000 -0.0108 -0.0104 0.0603  115 GLU   A N   
935  C CA  . GLU   A 114 ? 0.2764 0.2220 0.2093 -0.0120 0.0203  0.0549  115 GLU   A CA  
936  C C   . GLU   A 114 ? 0.2809 0.2010 0.1857 -0.0099 -0.0099 0.0693  115 GLU   A C   
937  O O   . GLU   A 114 ? 0.2843 0.2401 0.1870 -0.0092 -0.0330 0.0683  115 GLU   A O   
938  C CB  . GLU   A 114 ? 0.2977 0.2402 0.2484 -0.0035 0.0678  0.0422  115 GLU   A CB  
939  C CG  . GLU   A 114 ? 0.3636 0.3010 0.3021 -0.0128 0.1050  0.0449  115 GLU   A CG  
940  C CD  . GLU   A 114 ? 0.4478 0.3439 0.3518 -0.0037 0.1127  0.0577  115 GLU   A CD  
941  O OE1 . GLU   A 114 ? 0.3800 0.3000 0.3432 0.0077  0.1191  0.0721  115 GLU   A OE1 
942  O OE2 . GLU   A 114 ? 0.4748 0.3947 0.3770 -0.0087 0.1451  0.0381  115 GLU   A OE2 
943  N N   . ALA   A 115 ? 0.2855 0.1707 0.1965 -0.0300 -0.0048 0.0608  116 ALA   A N   
944  C CA  . ALA   A 115 ? 0.2787 0.1953 0.1841 -0.0301 -0.0125 0.0427  116 ALA   A CA  
945  C C   . ALA   A 115 ? 0.2555 0.2038 0.1808 -0.0188 0.0092  0.0622  116 ALA   A C   
946  O O   . ALA   A 115 ? 0.2754 0.2559 0.1845 -0.0493 -0.0129 0.0777  116 ALA   A O   
947  C CB  . ALA   A 115 ? 0.2830 0.2099 0.2050 -0.0280 -0.0275 0.0400  116 ALA   A CB  
948  N N   . THR   A 116 ? 0.2658 0.2185 0.1940 -0.0262 -0.0059 0.0710  117 THR   A N   
949  C CA  A THR   A 116 ? 0.2630 0.2248 0.1929 -0.0058 0.0098  0.0704  117 THR   A CA  
950  C CA  B THR   A 116 ? 0.2482 0.2134 0.1921 -0.0211 0.0135  0.0725  117 THR   A CA  
951  C C   . THR   A 116 ? 0.2769 0.2263 0.1869 -0.0387 0.0076  0.0709  117 THR   A C   
952  O O   . THR   A 116 ? 0.3216 0.2181 0.1693 -0.0271 0.0184  0.0484  117 THR   A O   
953  C CB  A THR   A 116 ? 0.2752 0.2427 0.1994 -0.0120 0.0145  0.0546  117 THR   A CB  
954  C CB  B THR   A 116 ? 0.2349 0.2179 0.1942 -0.0382 0.0184  0.0633  117 THR   A CB  
955  O OG1 A THR   A 116 ? 0.2847 0.2627 0.2259 -0.0010 0.0350  0.0540  117 THR   A OG1 
956  O OG1 B THR   A 116 ? 0.2423 0.2349 0.2300 -0.0498 -0.0197 0.0591  117 THR   A OG1 
957  C CG2 A THR   A 116 ? 0.2624 0.2479 0.1893 -0.0264 0.0381  0.0501  117 THR   A CG2 
958  C CG2 B THR   A 116 ? 0.2701 0.2318 0.1977 -0.0022 0.0752  0.0582  117 THR   A CG2 
959  N N   . GLU   A 117 ? 0.2556 0.2103 0.1792 -0.0522 -0.0210 0.0563  118 GLU   A N   
960  C CA  . GLU   A 117 ? 0.2517 0.2684 0.2156 -0.0387 -0.0275 0.0620  118 GLU   A CA  
961  C C   . GLU   A 117 ? 0.2915 0.2560 0.1994 -0.0068 -0.0185 0.0493  118 GLU   A C   
962  O O   . GLU   A 117 ? 0.2976 0.2497 0.1929 -0.0329 -0.0267 0.0376  118 GLU   A O   
963  C CB  . GLU   A 117 ? 0.2814 0.3754 0.2913 -0.0858 -0.0232 0.0667  118 GLU   A CB  
964  C CG  . GLU   A 117 ? 0.3876 0.4861 0.3845 -0.1151 -0.0107 0.0354  118 GLU   A CG  
965  C CD  . GLU   A 117 ? 0.5316 0.6104 0.4773 -0.1156 -0.0033 0.0105  118 GLU   A CD  
966  O OE1 . GLU   A 117 ? 0.5884 0.6327 0.5200 -0.1057 0.0220  -0.0009 118 GLU   A OE1 
967  O OE2 . GLU   A 117 ? 0.5613 0.6602 0.5041 -0.1200 -0.0136 0.0099  118 GLU   A OE2 
968  N N   . PHE   A 118 ? 0.2332 0.2222 0.1753 -0.0049 0.0248  0.0493  119 PHE   A N   
969  C CA  . PHE   A 118 ? 0.2625 0.2318 0.1685 -0.0057 0.0219  0.0438  119 PHE   A CA  
970  C C   . PHE   A 118 ? 0.2417 0.2237 0.1613 0.0202  -0.0176 0.0593  119 PHE   A C   
971  O O   . PHE   A 118 ? 0.2600 0.2239 0.1515 0.0016  0.0028  0.0586  119 PHE   A O   
972  C CB  . PHE   A 118 ? 0.2593 0.2411 0.1818 -0.0280 0.0091  0.0327  119 PHE   A CB  
973  C CG  . PHE   A 118 ? 0.2245 0.2794 0.1834 -0.0367 0.0032  0.0518  119 PHE   A CG  
974  C CD1 . PHE   A 118 ? 0.2536 0.2928 0.2013 0.0159  -0.0314 0.0506  119 PHE   A CD1 
975  C CD2 . PHE   A 118 ? 0.2485 0.3115 0.1794 0.0220  0.0297  0.0367  119 PHE   A CD2 
976  C CE1 . PHE   A 118 ? 0.2927 0.3323 0.1864 0.0155  -0.0119 0.0218  119 PHE   A CE1 
977  C CE2 . PHE   A 118 ? 0.2620 0.3411 0.1949 0.0234  0.0208  0.0516  119 PHE   A CE2 
978  C CZ  . PHE   A 118 ? 0.2976 0.3227 0.1911 -0.0053 0.0042  0.0445  119 PHE   A CZ  
979  N N   . LEU   A 119 ? 0.2265 0.2059 0.1737 -0.0030 -0.0041 0.0571  120 LEU   A N   
980  C CA  A LEU   A 119 ? 0.2344 0.2287 0.1730 -0.0067 -0.0188 0.0732  120 LEU   A CA  
981  C CA  B LEU   A 119 ? 0.2510 0.2410 0.1789 -0.0051 -0.0222 0.0567  120 LEU   A CA  
982  C C   . LEU   A 119 ? 0.2321 0.2368 0.1671 -0.0152 -0.0121 0.0686  120 LEU   A C   
983  O O   . LEU   A 119 ? 0.2362 0.2876 0.1786 -0.0136 0.0018  0.0961  120 LEU   A O   
984  C CB  A LEU   A 119 ? 0.2383 0.2151 0.1821 0.0006  -0.0406 0.0917  120 LEU   A CB  
985  C CB  B LEU   A 119 ? 0.2889 0.2545 0.2003 0.0045  -0.0472 0.0463  120 LEU   A CB  
986  C CG  A LEU   A 119 ? 0.2357 0.2103 0.1744 -0.0271 -0.0261 0.0919  120 LEU   A CG  
987  C CG  B LEU   A 119 ? 0.3126 0.2586 0.2115 -0.0279 -0.0331 0.0457  120 LEU   A CG  
988  C CD1 A LEU   A 119 ? 0.2740 0.2375 0.1615 -0.0297 -0.0454 0.0895  120 LEU   A CD1 
989  C CD1 B LEU   A 119 ? 0.2993 0.2474 0.2089 -0.0472 -0.0093 0.0635  120 LEU   A CD1 
990  C CD2 A LEU   A 119 ? 0.2308 0.1864 0.1970 -0.0316 0.0005  0.0868  120 LEU   A CD2 
991  C CD2 B LEU   A 119 ? 0.3029 0.2530 0.2060 -0.0284 -0.0342 0.0339  120 LEU   A CD2 
992  N N   . LYS   A 120 ? 0.2359 0.2309 0.1600 -0.0042 -0.0007 0.0354  121 LYS   A N   
993  C CA  . LYS   A 120 ? 0.2426 0.2196 0.1663 0.0280  0.0165  0.0478  121 LYS   A CA  
994  C C   . LYS   A 120 ? 0.2223 0.2097 0.1673 0.0075  0.0182  0.0485  121 LYS   A C   
995  O O   . LYS   A 120 ? 0.2529 0.2045 0.1608 0.0053  0.0316  0.0312  121 LYS   A O   
996  C CB  . LYS   A 120 ? 0.3300 0.2408 0.2442 0.0234  0.0360  0.0641  121 LYS   A CB  
997  C CG  . LYS   A 120 ? 0.4732 0.3536 0.3891 0.0429  0.0965  0.0617  121 LYS   A CG  
998  C CD  . LYS   A 120 ? 0.5736 0.4367 0.5234 0.0394  0.1373  0.0649  121 LYS   A CD  
999  C CE  . LYS   A 120 ? 0.6287 0.4886 0.6190 0.0325  0.1924  0.0647  121 LYS   A CE  
1000 N NZ  . LYS   A 120 ? 0.6762 0.5215 0.6499 0.0312  0.2011  0.0557  121 LYS   A NZ  
1001 N N   . GLN   A 121 ? 0.2148 0.1868 0.1888 0.0178  0.0069  0.0412  122 GLN   A N   
1002 C CA  . GLN   A 121 ? 0.2199 0.1760 0.1741 0.0162  0.0157  0.0468  122 GLN   A CA  
1003 C C   . GLN   A 121 ? 0.2470 0.1664 0.1478 0.0038  -0.0056 0.0312  122 GLN   A C   
1004 O O   . GLN   A 121 ? 0.2359 0.1867 0.1352 0.0010  -0.0022 0.0181  122 GLN   A O   
1005 C CB  . GLN   A 121 ? 0.1988 0.1914 0.1753 -0.0235 0.0259  0.0372  122 GLN   A CB  
1006 C CG  . GLN   A 121 ? 0.2308 0.2158 0.1856 -0.0094 0.0019  0.0479  122 GLN   A CG  
1007 C CD  . GLN   A 121 ? 0.2463 0.2207 0.1862 -0.0120 0.0240  0.0374  122 GLN   A CD  
1008 O OE1 . GLN   A 121 ? 0.2253 0.2356 0.2021 -0.0205 -0.0160 0.0495  122 GLN   A OE1 
1009 N NE2 . GLN   A 121 ? 0.2852 0.2427 0.1772 -0.0235 0.0146  0.0514  122 GLN   A NE2 
1010 N N   . ILE   A 122 ? 0.2289 0.1407 0.1456 -0.0077 -0.0066 0.0071  123 ILE   A N   
1011 C CA  . ILE   A 122 ? 0.2450 0.1401 0.1180 0.0058  0.0154  0.0050  123 ILE   A CA  
1012 C C   . ILE   A 122 ? 0.2137 0.1273 0.1223 0.0077  0.0021  0.0178  123 ILE   A C   
1013 O O   . ILE   A 122 ? 0.2241 0.1619 0.1128 -0.0218 -0.0023 0.0053  123 ILE   A O   
1014 C CB  . ILE   A 122 ? 0.2476 0.1562 0.1446 -0.0119 0.0179  -0.0065 123 ILE   A CB  
1015 C CG1 . ILE   A 122 ? 0.2704 0.1812 0.1388 0.0416  0.0183  -0.0225 123 ILE   A CG1 
1016 C CG2 . ILE   A 122 ? 0.2844 0.1674 0.1684 -0.0345 0.0041  -0.0004 123 ILE   A CG2 
1017 C CD1 . ILE   A 122 ? 0.3013 0.2341 0.1424 0.0599  -0.0043 -0.0368 123 ILE   A CD1 
1018 N N   . LEU   A 123 ? 0.1975 0.1446 0.1247 0.0082  -0.0137 -0.0045 124 LEU   A N   
1019 C CA  . LEU   A 123 ? 0.2195 0.1394 0.1142 0.0276  0.0006  0.0023  124 LEU   A CA  
1020 C C   . LEU   A 123 ? 0.1940 0.1367 0.1188 0.0062  -0.0200 -0.0079 124 LEU   A C   
1021 O O   . LEU   A 123 ? 0.1876 0.1672 0.1283 0.0081  0.0023  -0.0043 124 LEU   A O   
1022 C CB  . LEU   A 123 ? 0.2129 0.1460 0.1131 0.0244  -0.0020 0.0047  124 LEU   A CB  
1023 C CG  . LEU   A 123 ? 0.2409 0.1678 0.1278 -0.0314 -0.0027 0.0050  124 LEU   A CG  
1024 C CD1 . LEU   A 123 ? 0.3000 0.1604 0.1483 -0.0330 -0.0501 0.0383  124 LEU   A CD1 
1025 C CD2 . LEU   A 123 ? 0.2542 0.1910 0.1568 -0.0554 -0.0229 0.0009  124 LEU   A CD2 
1026 N N   . ASN   A 124 ? 0.2100 0.1372 0.1223 -0.0057 -0.0230 -0.0185 125 ASN   A N   
1027 C CA  . ASN   A 124 ? 0.1988 0.1392 0.1432 -0.0116 -0.0137 -0.0239 125 ASN   A CA  
1028 C C   . ASN   A 124 ? 0.2059 0.1491 0.1346 0.0069  -0.0075 0.0048  125 ASN   A C   
1029 O O   . ASN   A 124 ? 0.2138 0.1657 0.1249 -0.0134 -0.0104 -0.0032 125 ASN   A O   
1030 C CB  . ASN   A 124 ? 0.2027 0.1620 0.1788 -0.0228 -0.0115 0.0030  125 ASN   A CB  
1031 C CG  . ASN   A 124 ? 0.2182 0.1947 0.2295 -0.0047 -0.0090 -0.0028 125 ASN   A CG  
1032 O OD1 . ASN   A 124 ? 0.2624 0.1880 0.2724 -0.0169 -0.0060 -0.0065 125 ASN   A OD1 
1033 N ND2 . ASN   A 124 ? 0.2668 0.2392 0.2369 -0.0254 0.0034  -0.0143 125 ASN   A ND2 
1034 N N   . GLY   A 125 ? 0.1910 0.1506 0.1443 -0.0069 -0.0111 0.0058  126 GLY   A N   
1035 C CA  . GLY   A 125 ? 0.1784 0.1584 0.1322 -0.0031 -0.0143 0.0152  126 GLY   A CA  
1036 C C   . GLY   A 125 ? 0.1697 0.1481 0.1194 -0.0104 -0.0081 0.0171  126 GLY   A C   
1037 O O   . GLY   A 125 ? 0.2035 0.1545 0.1130 -0.0027 -0.0213 0.0125  126 GLY   A O   
1038 N N   . VAL   A 126 ? 0.1720 0.1530 0.1280 -0.0254 -0.0279 -0.0077 127 VAL   A N   
1039 C CA  . VAL   A 126 ? 0.1907 0.1425 0.1129 -0.0023 -0.0235 -0.0126 127 VAL   A CA  
1040 C C   . VAL   A 126 ? 0.2022 0.1299 0.1130 -0.0184 -0.0098 -0.0071 127 VAL   A C   
1041 O O   . VAL   A 126 ? 0.1949 0.1385 0.1068 -0.0199 0.0029  0.0083  127 VAL   A O   
1042 C CB  . VAL   A 126 ? 0.1741 0.1506 0.1201 0.0055  -0.0245 -0.0282 127 VAL   A CB  
1043 C CG1 . VAL   A 126 ? 0.1749 0.2022 0.1454 -0.0116 -0.0316 -0.0246 127 VAL   A CG1 
1044 C CG2 . VAL   A 126 ? 0.2113 0.1331 0.1230 0.0068  -0.0110 -0.0119 127 VAL   A CG2 
1045 N N   . TYR   A 127 ? 0.2016 0.1237 0.1221 0.0169  -0.0087 -0.0143 128 TYR   A N   
1046 C CA  . TYR   A 127 ? 0.2334 0.1170 0.1003 -0.0036 -0.0005 0.0118  128 TYR   A CA  
1047 C C   . TYR   A 127 ? 0.1696 0.1568 0.1165 -0.0163 -0.0023 0.0004  128 TYR   A C   
1048 O O   . TYR   A 127 ? 0.1962 0.1436 0.1141 -0.0022 0.0048  0.0021  128 TYR   A O   
1049 C CB  . TYR   A 127 ? 0.2458 0.1443 0.1314 0.0134  -0.0079 0.0044  128 TYR   A CB  
1050 C CG  . TYR   A 127 ? 0.1902 0.1648 0.1444 0.0009  -0.0022 -0.0304 128 TYR   A CG  
1051 C CD1 . TYR   A 127 ? 0.2360 0.2138 0.1936 0.0284  -0.0242 -0.0756 128 TYR   A CD1 
1052 C CD2 . TYR   A 127 ? 0.2329 0.1898 0.1707 0.0171  -0.0242 -0.0492 128 TYR   A CD2 
1053 C CE1 . TYR   A 127 ? 0.2309 0.2068 0.2291 0.0088  -0.0352 -0.0807 128 TYR   A CE1 
1054 C CE2 . TYR   A 127 ? 0.2291 0.1986 0.2196 0.0146  -0.0014 -0.0542 128 TYR   A CE2 
1055 C CZ  . TYR   A 127 ? 0.2308 0.1841 0.2221 0.0213  0.0044  -0.0885 128 TYR   A CZ  
1056 O OH  . TYR   A 127 ? 0.2932 0.2048 0.2646 0.0242  0.0318  -0.0877 128 TYR   A OH  
1057 N N   . TYR   A 128 ? 0.1803 0.1487 0.1115 -0.0038 -0.0279 0.0097  129 TYR   A N   
1058 C CA  . TYR   A 128 ? 0.1912 0.1548 0.1167 0.0019  -0.0209 0.0223  129 TYR   A CA  
1059 C C   . TYR   A 128 ? 0.2211 0.1466 0.1074 -0.0076 -0.0180 0.0109  129 TYR   A C   
1060 O O   . TYR   A 128 ? 0.2441 0.1615 0.1062 -0.0100 -0.0034 -0.0034 129 TYR   A O   
1061 C CB  . TYR   A 128 ? 0.1820 0.1564 0.1381 0.0107  -0.0303 0.0165  129 TYR   A CB  
1062 C CG  . TYR   A 128 ? 0.1849 0.1643 0.1554 -0.0316 -0.0480 0.0184  129 TYR   A CG  
1063 C CD1 . TYR   A 128 ? 0.2112 0.1969 0.1544 -0.0117 -0.0434 -0.0127 129 TYR   A CD1 
1064 C CD2 . TYR   A 128 ? 0.2535 0.1812 0.1711 -0.0090 -0.0668 0.0173  129 TYR   A CD2 
1065 C CE1 . TYR   A 128 ? 0.1682 0.2317 0.1437 0.0104  -0.0293 -0.0036 129 TYR   A CE1 
1066 C CE2 . TYR   A 128 ? 0.2979 0.2084 0.1542 -0.0226 -0.0607 0.0391  129 TYR   A CE2 
1067 C CZ  . TYR   A 128 ? 0.2507 0.2265 0.1371 -0.0011 -0.0481 0.0173  129 TYR   A CZ  
1068 O OH  . TYR   A 128 ? 0.3006 0.2649 0.1486 -0.0111 -0.0486 0.0410  129 TYR   A OH  
1069 N N   . LEU   A 129 ? 0.1901 0.1307 0.1246 -0.0180 -0.0182 0.0020  130 LEU   A N   
1070 C CA  . LEU   A 129 ? 0.2058 0.1248 0.1269 -0.0217 -0.0096 -0.0049 130 LEU   A CA  
1071 C C   . LEU   A 129 ? 0.2013 0.1512 0.1134 -0.0431 -0.0021 -0.0145 130 LEU   A C   
1072 O O   . LEU   A 129 ? 0.2138 0.1517 0.1246 -0.0292 0.0082  -0.0276 130 LEU   A O   
1073 C CB  . LEU   A 129 ? 0.2365 0.1378 0.1350 -0.0070 -0.0085 -0.0082 130 LEU   A CB  
1074 C CG  . LEU   A 129 ? 0.2359 0.1485 0.1298 -0.0006 -0.0142 0.0122  130 LEU   A CG  
1075 C CD1 . LEU   A 129 ? 0.3086 0.1864 0.1406 0.0242  -0.0167 -0.0017 130 LEU   A CD1 
1076 C CD2 . LEU   A 129 ? 0.2542 0.1741 0.1790 -0.0008 -0.0398 0.0239  130 LEU   A CD2 
1077 N N   . HIS   A 130 ? 0.1751 0.1555 0.1278 -0.0035 -0.0291 -0.0143 131 HIS   A N   
1078 C CA  . HIS   A 130 ? 0.2026 0.1651 0.1239 -0.0211 -0.0117 -0.0225 131 HIS   A CA  
1079 C C   . HIS   A 130 ? 0.2051 0.1629 0.1125 -0.0282 0.0042  -0.0085 131 HIS   A C   
1080 O O   . HIS   A 130 ? 0.2048 0.1801 0.1322 -0.0221 0.0131  -0.0111 131 HIS   A O   
1081 C CB  . HIS   A 130 ? 0.1922 0.1437 0.1115 0.0009  -0.0234 -0.0066 131 HIS   A CB  
1082 C CG  . HIS   A 130 ? 0.1898 0.1294 0.1239 -0.0126 -0.0161 -0.0224 131 HIS   A CG  
1083 N ND1 . HIS   A 130 ? 0.1904 0.1456 0.1349 -0.0020 -0.0151 -0.0028 131 HIS   A ND1 
1084 C CD2 . HIS   A 130 ? 0.2019 0.1266 0.1212 -0.0247 -0.0044 -0.0123 131 HIS   A CD2 
1085 C CE1 . HIS   A 130 ? 0.2173 0.1214 0.1257 0.0082  -0.0213 0.0063  131 HIS   A CE1 
1086 N NE2 . HIS   A 130 ? 0.2009 0.1404 0.1071 -0.0288 -0.0144 0.0032  131 HIS   A NE2 
1087 N N   . SER   A 131 ? 0.2146 0.1343 0.1294 -0.0137 -0.0092 -0.0159 132 SER   A N   
1088 C CA  . SER   A 131 ? 0.2612 0.1436 0.1506 -0.0167 -0.0001 -0.0205 132 SER   A CA  
1089 C C   . SER   A 131 ? 0.2760 0.1506 0.1463 -0.0333 0.0112  -0.0345 132 SER   A C   
1090 O O   . SER   A 131 ? 0.3197 0.1854 0.1616 -0.0247 0.0550  -0.0376 132 SER   A O   
1091 C CB  . SER   A 131 ? 0.3080 0.1381 0.1558 -0.0278 0.0248  -0.0152 132 SER   A CB  
1092 O OG  . SER   A 131 ? 0.3191 0.1643 0.1856 -0.0092 0.0618  -0.0226 132 SER   A OG  
1093 N N   . LEU   A 132 ? 0.2852 0.1702 0.1262 -0.0435 0.0084  -0.0057 133 LEU   A N   
1094 C CA  . LEU   A 132 ? 0.2936 0.1913 0.1381 -0.0435 -0.0167 -0.0024 133 LEU   A CA  
1095 C C   . LEU   A 132 ? 0.2883 0.1839 0.1310 -0.0499 0.0181  -0.0022 133 LEU   A C   
1096 O O   . LEU   A 132 ? 0.3382 0.2179 0.1468 -0.0686 0.0189  0.0107  133 LEU   A O   
1097 C CB  . LEU   A 132 ? 0.2996 0.2194 0.1431 -0.0657 -0.0463 0.0058  133 LEU   A CB  
1098 C CG  . LEU   A 132 ? 0.3157 0.2547 0.1729 -0.0500 -0.0378 0.0160  133 LEU   A CG  
1099 C CD1 . LEU   A 132 ? 0.3144 0.2868 0.2201 -0.0434 -0.0709 0.0306  133 LEU   A CD1 
1100 C CD2 . LEU   A 132 ? 0.3785 0.2465 0.1672 -0.0455 -0.0241 -0.0180 133 LEU   A CD2 
1101 N N   . GLN   A 133 ? 0.2672 0.1931 0.1412 -0.0478 0.0023  -0.0375 134 GLN   A N   
1102 C CA  . GLN   A 133 ? 0.2340 0.1906 0.1583 -0.0260 0.0317  -0.0020 134 GLN   A CA  
1103 C C   . GLN   A 133 ? 0.2506 0.1891 0.1536 -0.0239 0.0169  0.0309  134 GLN   A C   
1104 O O   . GLN   A 133 ? 0.2754 0.2074 0.2044 -0.0387 0.0432  0.0284  134 GLN   A O   
1105 C CB  . GLN   A 133 ? 0.2719 0.2412 0.2350 -0.0291 0.0624  -0.0105 134 GLN   A CB  
1106 C CG  . GLN   A 133 ? 0.3223 0.2633 0.3000 0.0006  0.0786  -0.0244 134 GLN   A CG  
1107 C CD  . GLN   A 133 ? 0.4450 0.3379 0.3892 0.0208  0.0861  -0.0073 134 GLN   A CD  
1108 O OE1 . GLN   A 133 ? 0.4921 0.3746 0.4151 0.0407  0.0750  -0.0062 134 GLN   A OE1 
1109 N NE2 . GLN   A 133 ? 0.5082 0.3441 0.4126 0.0382  0.0717  -0.0056 134 GLN   A NE2 
1110 N N   . ILE   A 134 ? 0.2299 0.1656 0.1234 -0.0242 0.0045  0.0061  135 ILE   A N   
1111 C CA  . ILE   A 134 ? 0.2304 0.1567 0.1231 -0.0004 -0.0130 -0.0096 135 ILE   A CA  
1112 C C   . ILE   A 134 ? 0.2298 0.1486 0.1108 -0.0259 -0.0046 0.0065  135 ILE   A C   
1113 O O   . ILE   A 134 ? 0.2370 0.1636 0.1260 -0.0285 -0.0059 0.0272  135 ILE   A O   
1114 C CB  . ILE   A 134 ? 0.2627 0.1668 0.1420 -0.0166 -0.0221 0.0132  135 ILE   A CB  
1115 C CG1 . ILE   A 134 ? 0.2981 0.2069 0.1455 -0.0180 -0.0713 0.0306  135 ILE   A CG1 
1116 C CG2 . ILE   A 134 ? 0.2550 0.1795 0.1639 -0.0030 -0.0152 0.0070  135 ILE   A CG2 
1117 C CD1 . ILE   A 134 ? 0.3155 0.2205 0.1844 0.0051  -0.0844 -0.0007 135 ILE   A CD1 
1118 N N   . ALA   A 135 ? 0.2129 0.1513 0.1169 -0.0251 -0.0306 -0.0055 136 ALA   A N   
1119 C CA  . ALA   A 135 ? 0.2038 0.1579 0.1270 -0.0078 -0.0195 -0.0234 136 ALA   A CA  
1120 C C   . ALA   A 135 ? 0.2234 0.1347 0.1226 -0.0157 0.0048  0.0049  136 ALA   A C   
1121 O O   . ALA   A 135 ? 0.2448 0.1560 0.1432 0.0090  0.0039  0.0460  136 ALA   A O   
1122 C CB  . ALA   A 135 ? 0.2495 0.1679 0.1367 -0.0224 -0.0223 -0.0276 136 ALA   A CB  
1123 N N   . HIS   A 136 ? 0.2065 0.1575 0.1135 -0.0173 0.0027  -0.0045 137 HIS   A N   
1124 C CA  . HIS   A 136 ? 0.2142 0.1673 0.1167 -0.0173 -0.0059 0.0054  137 HIS   A CA  
1125 C C   . HIS   A 136 ? 0.2259 0.1544 0.1253 0.0049  -0.0036 0.0121  137 HIS   A C   
1126 O O   . HIS   A 136 ? 0.2331 0.1745 0.1327 -0.0198 -0.0081 0.0164  137 HIS   A O   
1127 C CB  . HIS   A 136 ? 0.1988 0.1848 0.1377 -0.0264 0.0144  0.0191  137 HIS   A CB  
1128 C CG  . HIS   A 136 ? 0.1884 0.1708 0.1336 -0.0169 -0.0181 0.0121  137 HIS   A CG  
1129 N ND1 . HIS   A 136 ? 0.2075 0.1772 0.1393 -0.0119 -0.0146 0.0245  137 HIS   A ND1 
1130 C CD2 . HIS   A 136 ? 0.2187 0.1856 0.1704 -0.0230 -0.0228 0.0285  137 HIS   A CD2 
1131 C CE1 . HIS   A 136 ? 0.2108 0.1968 0.1630 0.0198  0.0015  0.0172  137 HIS   A CE1 
1132 N NE2 . HIS   A 136 ? 0.2590 0.1912 0.1847 -0.0075 -0.0060 0.0315  137 HIS   A NE2 
1133 N N   . PHE   A 137 ? 0.2162 0.1369 0.1283 -0.0157 -0.0123 -0.0041 138 PHE   A N   
1134 C CA  . PHE   A 137 ? 0.2384 0.1399 0.1463 -0.0182 0.0229  0.0078  138 PHE   A CA  
1135 C C   . PHE   A 137 ? 0.2419 0.1430 0.1486 -0.0312 -0.0001 -0.0165 138 PHE   A C   
1136 O O   . PHE   A 137 ? 0.3031 0.1757 0.2258 -0.0443 0.0424  -0.0451 138 PHE   A O   
1137 C CB  . PHE   A 137 ? 0.2366 0.1477 0.1601 -0.0209 0.0258  0.0189  138 PHE   A CB  
1138 C CG  . PHE   A 137 ? 0.2119 0.1607 0.1586 -0.0311 -0.0057 0.0096  138 PHE   A CG  
1139 C CD1 . PHE   A 137 ? 0.2171 0.2007 0.1745 -0.0130 0.0032  0.0045  138 PHE   A CD1 
1140 C CD2 . PHE   A 137 ? 0.2194 0.1682 0.1608 -0.0331 0.0004  -0.0028 138 PHE   A CD2 
1141 C CE1 . PHE   A 137 ? 0.2304 0.2090 0.1755 -0.0219 0.0038  0.0333  138 PHE   A CE1 
1142 C CE2 . PHE   A 137 ? 0.2352 0.1770 0.1655 -0.0205 -0.0158 -0.0103 138 PHE   A CE2 
1143 C CZ  . PHE   A 137 ? 0.2266 0.1719 0.1618 -0.0383 -0.0108 0.0169  138 PHE   A CZ  
1144 N N   . ASP   A 138 ? 0.2244 0.1531 0.1288 -0.0008 0.0139  0.0066  139 ASP   A N   
1145 C CA  . ASP   A 138 ? 0.2716 0.1734 0.1690 0.0103  0.0272  0.0435  139 ASP   A CA  
1146 C C   . ASP   A 138 ? 0.2295 0.1566 0.1433 0.0387  -0.0198 0.0092  139 ASP   A C   
1147 O O   . ASP   A 138 ? 0.2422 0.1873 0.1794 0.0624  -0.0035 0.0241  139 ASP   A O   
1148 C CB  . ASP   A 138 ? 0.3985 0.2011 0.2206 0.0211  0.0181  0.0514  139 ASP   A CB  
1149 C CG  . ASP   A 138 ? 0.4719 0.2640 0.2768 -0.0051 0.0137  0.0220  139 ASP   A CG  
1150 O OD1 . ASP   A 138 ? 0.4767 0.2675 0.2552 -0.0392 0.0767  -0.0556 139 ASP   A OD1 
1151 O OD2 . ASP   A 138 ? 0.4906 0.3018 0.3127 -0.0095 -0.0443 0.0440  139 ASP   A OD2 
1152 N N   . LEU   A 139 ? 0.2130 0.1631 0.1218 0.0167  -0.0075 0.0013  140 LEU   A N   
1153 C CA  . LEU   A 139 ? 0.2099 0.1626 0.1198 0.0085  -0.0073 0.0056  140 LEU   A CA  
1154 C C   . LEU   A 139 ? 0.2150 0.1791 0.1129 0.0135  -0.0079 -0.0073 140 LEU   A C   
1155 O O   . LEU   A 139 ? 0.2387 0.2066 0.1319 0.0074  -0.0226 -0.0127 140 LEU   A O   
1156 C CB  . LEU   A 139 ? 0.2315 0.1509 0.1270 0.0184  -0.0066 0.0004  140 LEU   A CB  
1157 C CG  . LEU   A 139 ? 0.2050 0.1354 0.1364 0.0049  -0.0127 -0.0022 140 LEU   A CG  
1158 C CD1 . LEU   A 139 ? 0.2615 0.1474 0.1640 0.0012  -0.0273 0.0080  140 LEU   A CD1 
1159 C CD2 . LEU   A 139 ? 0.2430 0.1688 0.1487 -0.0231 -0.0213 0.0183  140 LEU   A CD2 
1160 N N   . LYS   A 140 ? 0.2238 0.1987 0.1238 0.0383  0.0073  -0.0198 141 LYS   A N   
1161 C CA  . LYS   A 140 ? 0.2657 0.1821 0.1397 0.0335  -0.0021 -0.0159 141 LYS   A CA  
1162 C C   . LYS   A 140 ? 0.2469 0.2015 0.1458 0.0317  0.0109  -0.0109 141 LYS   A C   
1163 O O   . LYS   A 140 ? 0.2334 0.2083 0.1408 0.0089  0.0107  -0.0166 141 LYS   A O   
1164 C CB  . LYS   A 140 ? 0.2827 0.1560 0.1756 0.0149  -0.0056 0.0051  141 LYS   A CB  
1165 C CG  . LYS   A 140 ? 0.3119 0.1422 0.2114 0.0320  -0.0117 -0.0203 141 LYS   A CG  
1166 C CD  . LYS   A 140 ? 0.3786 0.1483 0.2714 0.0469  -0.0371 -0.0209 141 LYS   A CD  
1167 C CE  . LYS   A 140 ? 0.4096 0.1335 0.2992 0.0498  -0.0488 -0.0283 141 LYS   A CE  
1168 N NZ  . LYS   A 140 ? 0.4502 0.1650 0.3491 0.0434  -0.0223 -0.0212 141 LYS   A NZ  
1169 N N   . PRO   A 141 ? 0.2566 0.2147 0.1474 0.0273  -0.0006 -0.0104 142 PRO   A N   
1170 C CA  . PRO   A 141 ? 0.2826 0.2466 0.1536 0.0338  0.0145  0.0008  142 PRO   A CA  
1171 C C   . PRO   A 141 ? 0.2437 0.2484 0.1533 0.0019  0.0306  -0.0156 142 PRO   A C   
1172 O O   . PRO   A 141 ? 0.2839 0.2600 0.1796 0.0031  0.0057  -0.0172 142 PRO   A O   
1173 C CB  . PRO   A 141 ? 0.2968 0.2840 0.1427 0.0596  -0.0004 0.0056  142 PRO   A CB  
1174 C CG  . PRO   A 141 ? 0.3173 0.2924 0.1641 0.0351  0.0232  0.0002  142 PRO   A CG  
1175 C CD  . PRO   A 141 ? 0.3040 0.2616 0.1356 0.0334  -0.0036 0.0075  142 PRO   A CD  
1176 N N   . GLU   A 142 ? 0.2558 0.2159 0.1384 0.0365  0.0262  -0.0308 143 GLU   A N   
1177 C CA  . GLU   A 142 ? 0.2725 0.2314 0.1766 0.0412  -0.0126 -0.0334 143 GLU   A CA  
1178 C C   . GLU   A 142 ? 0.2505 0.2254 0.1740 0.0436  0.0161  -0.0239 143 GLU   A C   
1179 O O   . GLU   A 142 ? 0.2649 0.2608 0.1911 0.0591  0.0161  -0.0298 143 GLU   A O   
1180 C CB  . GLU   A 142 ? 0.3718 0.2620 0.2248 0.0757  -0.0195 -0.0759 143 GLU   A CB  
1181 C CG  . GLU   A 142 ? 0.4453 0.3286 0.2480 0.0284  0.0033  -0.0997 143 GLU   A CG  
1182 C CD  . GLU   A 142 ? 0.5221 0.3858 0.2593 -0.0091 0.0182  -0.1584 143 GLU   A CD  
1183 O OE1 . GLU   A 142 ? 0.4661 0.3966 0.2638 -0.0514 0.0601  -0.1736 143 GLU   A OE1 
1184 O OE2 . GLU   A 142 ? 0.6355 0.4606 0.3073 -0.0217 -0.0145 -0.1298 143 GLU   A OE2 
1185 N N   . ASN   A 143 ? 0.2260 0.2034 0.1702 0.0068  0.0364  -0.0358 144 ASN   A N   
1186 C CA  . ASN   A 143 ? 0.2240 0.2128 0.1590 0.0161  0.0281  -0.0286 144 ASN   A CA  
1187 C C   . ASN   A 143 ? 0.2612 0.2214 0.1920 -0.0212 0.0174  -0.0569 144 ASN   A C   
1188 O O   . ASN   A 143 ? 0.2801 0.2298 0.2006 -0.0047 0.0370  -0.0615 144 ASN   A O   
1189 C CB  . ASN   A 143 ? 0.2135 0.2002 0.1905 -0.0056 0.0154  -0.0185 144 ASN   A CB  
1190 C CG  . ASN   A 143 ? 0.2119 0.2141 0.2067 0.0469  0.0171  0.0030  144 ASN   A CG  
1191 O OD1 . ASN   A 143 ? 0.2234 0.2738 0.2623 0.0428  0.0040  -0.0003 144 ASN   A OD1 
1192 N ND2 . ASN   A 143 ? 0.2256 0.2105 0.2098 0.0267  -0.0075 -0.0034 144 ASN   A ND2 
1206 N N   . MET   A 145 ? 0.2102 0.2339 0.2027 0.0004  0.0443  0.0358  146 MET   A N   
1207 C CA  A MET   A 145 ? 0.2212 0.2289 0.1945 0.0013  0.0217  0.0273  146 MET   A CA  
1208 C CA  B MET   A 145 ? 0.2204 0.2278 0.2048 -0.0057 0.0381  0.0292  146 MET   A CA  
1209 C C   . MET   A 145 ? 0.2365 0.2122 0.1858 0.0143  0.0161  0.0217  146 MET   A C   
1210 O O   . MET   A 145 ? 0.2394 0.2165 0.1941 0.0096  0.0407  0.0122  146 MET   A O   
1211 C CB  A MET   A 145 ? 0.2936 0.2650 0.2570 -0.0012 -0.0193 0.0368  146 MET   A CB  
1212 C CB  B MET   A 145 ? 0.2925 0.2569 0.2728 -0.0133 0.0221  0.0443  146 MET   A CB  
1213 C CG  A MET   A 145 ? 0.3468 0.3022 0.2906 0.0077  -0.0094 0.0188  146 MET   A CG  
1214 C CG  B MET   A 145 ? 0.3233 0.2786 0.3096 0.0006  0.0327  0.0406  146 MET   A CG  
1215 S SD  A MET   A 145 ? 0.3496 0.3229 0.2975 0.0266  0.0005  0.0209  146 MET   A SD  
1216 S SD  B MET   A 145 ? 0.3392 0.2949 0.3231 0.0418  0.0540  0.0628  146 MET   A SD  
1217 C CE  A MET   A 145 ? 0.3774 0.3308 0.3122 0.0157  0.0226  0.0136  146 MET   A CE  
1218 C CE  B MET   A 145 ? 0.3276 0.3023 0.3335 0.0196  0.0807  0.0527  146 MET   A CE  
1219 N N   . LEU   A 146 ? 0.2312 0.2354 0.1771 0.0113  0.0240  0.0121  147 LEU   A N   
1220 C CA  . LEU   A 146 ? 0.2584 0.2679 0.1889 0.0153  0.0238  0.0331  147 LEU   A CA  
1221 C C   . LEU   A 146 ? 0.2396 0.2990 0.1948 0.0221  0.0031  0.0343  147 LEU   A C   
1222 O O   . LEU   A 146 ? 0.2569 0.3179 0.2102 0.0364  0.0030  0.0218  147 LEU   A O   
1223 C CB  . LEU   A 146 ? 0.2576 0.2873 0.1958 0.0046  0.0410  0.0790  147 LEU   A CB  
1224 C CG  . LEU   A 146 ? 0.2784 0.3326 0.2224 -0.0047 0.0133  0.0650  147 LEU   A CG  
1225 C CD1 . LEU   A 146 ? 0.3191 0.3438 0.2347 -0.0270 0.0010  0.0841  147 LEU   A CD1 
1226 C CD2 . LEU   A 146 ? 0.2907 0.3606 0.2268 0.0114  0.0075  0.0538  147 LEU   A CD2 
1227 N N   . LEU   A 147 ? 0.2296 0.3337 0.2133 0.0083  -0.0171 0.0232  148 LEU   A N   
1228 C CA  . LEU   A 147 ? 0.2396 0.3790 0.2442 0.0074  -0.0275 0.0348  148 LEU   A CA  
1229 C C   . LEU   A 147 ? 0.2264 0.4254 0.2746 0.0197  -0.0029 0.0832  148 LEU   A C   
1230 O O   . LEU   A 147 ? 0.2803 0.4426 0.2981 0.0139  -0.0143 0.0803  148 LEU   A O   
1231 C CB  . LEU   A 147 ? 0.2869 0.3851 0.2687 -0.0074 -0.0192 0.0051  148 LEU   A CB  
1232 C CG  . LEU   A 147 ? 0.3041 0.3790 0.2685 -0.0177 -0.0572 -0.0342 148 LEU   A CG  
1233 C CD1 . LEU   A 147 ? 0.3058 0.3786 0.2958 0.0132  -0.0260 -0.0077 148 LEU   A CD1 
1234 C CD2 . LEU   A 147 ? 0.3752 0.3858 0.2921 -0.0229 -0.0803 -0.0688 148 LEU   A CD2 
1235 N N   . ASP   A 148 ? 0.2135 0.4695 0.2898 0.0237  0.0066  0.0996  149 ASP   A N   
1236 C CA  . ASP   A 148 ? 0.1961 0.5368 0.3240 0.0005  0.0171  0.1016  149 ASP   A CA  
1237 C C   . ASP   A 148 ? 0.2106 0.5466 0.3325 0.0300  0.0399  0.1050  149 ASP   A C   
1238 O O   . ASP   A 148 ? 0.2610 0.5326 0.3205 0.0363  0.0309  0.1084  149 ASP   A O   
1239 C CB  . ASP   A 148 ? 0.2279 0.6056 0.3532 0.0036  0.0180  0.0931  149 ASP   A CB  
1240 C CG  . ASP   A 148 ? 0.2437 0.6694 0.3822 -0.0153 0.0252  0.0648  149 ASP   A CG  
1241 O OD1 . ASP   A 148 ? 0.2733 0.6929 0.4001 -0.0052 0.0388  0.0564  149 ASP   A OD1 
1242 O OD2 . ASP   A 148 ? 0.2789 0.6894 0.3996 -0.0450 0.0357  0.0635  149 ASP   A OD2 
1243 N N   . ARG   A 149 ? 0.2696 0.5787 0.3495 0.0313  0.0594  0.1142  150 ARG   A N   
1244 C CA  . ARG   A 149 ? 0.3627 0.6108 0.3704 0.0482  0.0991  0.1231  150 ARG   A CA  
1245 C C   . ARG   A 149 ? 0.4055 0.6364 0.3929 0.0292  0.1179  0.1422  150 ARG   A C   
1246 O O   . ARG   A 149 ? 0.4600 0.6410 0.3674 0.0173  0.0666  0.1634  150 ARG   A O   
1247 C CB  . ARG   A 149 ? 0.3713 0.6254 0.3912 0.0880  0.1152  0.0976  150 ARG   A CB  
1248 C CG  . ARG   A 149 ? 0.4216 0.6607 0.4295 0.0951  0.1024  0.0572  150 ARG   A CG  
1249 C CD  . ARG   A 149 ? 0.5159 0.6988 0.4643 0.0845  0.0771  0.0287  150 ARG   A CD  
1250 N NE  . ARG   A 149 ? 0.6143 0.7382 0.4948 0.0518  0.0553  0.0005  150 ARG   A NE  
1251 C CZ  . ARG   A 149 ? 0.7063 0.7699 0.5209 0.0188  0.0295  -0.0177 150 ARG   A CZ  
1252 N NH1 . ARG   A 149 ? 0.7387 0.7795 0.5262 -0.0027 0.0254  -0.0238 150 ARG   A NH1 
1253 N NH2 . ARG   A 149 ? 0.7355 0.7795 0.5344 0.0140  0.0207  -0.0227 150 ARG   A NH2 
1254 N N   . ASN   A 150 ? 0.3708 0.6354 0.4285 0.0413  0.1611  0.1530  151 ASN   A N   
1255 C CA  . ASN   A 150 ? 0.3728 0.6406 0.4678 0.0476  0.2050  0.1609  151 ASN   A CA  
1256 C C   . ASN   A 150 ? 0.4140 0.6292 0.4906 0.0120  0.1901  0.1612  151 ASN   A C   
1257 O O   . ASN   A 150 ? 0.4653 0.6562 0.5200 0.0026  0.2167  0.1547  151 ASN   A O   
1258 C CB  . ASN   A 150 ? 0.4048 0.6644 0.4861 0.0763  0.2235  0.1678  151 ASN   A CB  
1259 C CG  . ASN   A 150 ? 0.4750 0.6932 0.5192 0.0965  0.1962  0.1703  151 ASN   A CG  
1260 O OD1 . ASN   A 150 ? 0.4967 0.7121 0.5303 0.1140  0.1902  0.1565  151 ASN   A OD1 
1261 N ND2 . ASN   A 150 ? 0.5140 0.6934 0.5324 0.0958  0.1961  0.1775  151 ASN   A ND2 
1262 N N   . VAL   A 151 ? 0.3698 0.5919 0.4881 -0.0055 0.1482  0.1563  152 VAL   A N   
1263 C CA  . VAL   A 151 ? 0.3263 0.5557 0.4739 -0.0470 0.1145  0.1586  152 VAL   A CA  
1264 C C   . VAL   A 151 ? 0.3972 0.5449 0.4639 -0.0674 0.1250  0.1621  152 VAL   A C   
1265 O O   . VAL   A 151 ? 0.4162 0.5531 0.4603 -0.0514 0.1192  0.1608  152 VAL   A O   
1266 C CB  . VAL   A 151 ? 0.2413 0.5429 0.4752 -0.0267 0.0851  0.1291  152 VAL   A CB  
1267 C CG1 . VAL   A 151 ? 0.2450 0.5529 0.4857 -0.0420 0.0589  0.1154  152 VAL   A CG1 
1268 C CG2 . VAL   A 151 ? 0.2777 0.5268 0.4744 -0.0550 0.0939  0.1338  152 VAL   A CG2 
1269 N N   . PRO   A 152 ? 0.4461 0.5271 0.4585 -0.0963 0.1203  0.1592  153 PRO   A N   
1270 C CA  . PRO   A 152 ? 0.4654 0.5233 0.4390 -0.0879 0.1146  0.1588  153 PRO   A CA  
1271 C C   . PRO   A 152 ? 0.4735 0.5220 0.4064 -0.0678 0.1152  0.1566  153 PRO   A C   
1272 O O   . PRO   A 152 ? 0.5101 0.5481 0.4011 -0.0487 0.1116  0.1462  153 PRO   A O   
1273 C CB  . PRO   A 152 ? 0.4965 0.5279 0.4628 -0.0958 0.1008  0.1516  153 PRO   A CB  
1274 C CG  . PRO   A 152 ? 0.5207 0.5257 0.4718 -0.1056 0.0897  0.1526  153 PRO   A CG  
1275 C CD  . PRO   A 152 ? 0.4835 0.5094 0.4651 -0.1243 0.1102  0.1705  153 PRO   A CD  
1276 N N   . LYS   A 153 ? 0.4441 0.4764 0.3760 -0.0828 0.1021  0.1803  154 LYS   A N   
1277 C CA  . LYS   A 153 ? 0.4186 0.4470 0.3655 -0.0860 0.0747  0.1676  154 LYS   A CA  
1278 C C   . LYS   A 153 ? 0.3756 0.3839 0.3090 -0.0688 0.0353  0.1341  154 LYS   A C   
1279 O O   . LYS   A 153 ? 0.3857 0.3528 0.3207 -0.0812 0.0418  0.0915  154 LYS   A O   
1280 C CB  . LYS   A 153 ? 0.4647 0.4846 0.4179 -0.0713 0.0699  0.1780  154 LYS   A CB  
1281 C CG  . LYS   A 153 ? 0.5089 0.5451 0.4842 -0.0656 0.0611  0.1631  154 LYS   A CG  
1282 C CD  . LYS   A 153 ? 0.5642 0.6101 0.5478 -0.0347 0.0568  0.1294  154 LYS   A CD  
1283 C CE  . LYS   A 153 ? 0.6175 0.6635 0.5920 -0.0012 0.0470  0.1019  154 LYS   A CE  
1284 N NZ  . LYS   A 153 ? 0.6601 0.6914 0.6048 0.0277  0.0377  0.0880  154 LYS   A NZ  
1285 N N   . PRO   A 154 ? 0.3138 0.3702 0.2448 -0.0594 0.0077  0.0901  155 PRO   A N   
1286 C CA  . PRO   A 154 ? 0.3012 0.3505 0.2459 -0.0427 0.0277  0.0909  155 PRO   A CA  
1287 C C   . PRO   A 154 ? 0.2632 0.3247 0.2567 -0.0506 0.0141  0.0788  155 PRO   A C   
1288 O O   . PRO   A 154 ? 0.2921 0.3077 0.2331 -0.0303 0.0174  0.0688  155 PRO   A O   
1289 C CB  . PRO   A 154 ? 0.3240 0.3490 0.2382 -0.0295 0.0459  0.0808  155 PRO   A CB  
1290 C CG  . PRO   A 154 ? 0.3645 0.3670 0.2429 -0.0428 0.0595  0.0936  155 PRO   A CG  
1291 C CD  . PRO   A 154 ? 0.3669 0.3762 0.2483 -0.0355 0.0298  0.0883  155 PRO   A CD  
1292 N N   . ARG   A 155 ? 0.2413 0.2991 0.2539 -0.0276 0.0294  0.0541  156 ARG   A N   
1293 C CA  . ARG   A 155 ? 0.2392 0.2684 0.2526 -0.0473 0.0132  0.0366  156 ARG   A CA  
1294 C C   . ARG   A 155 ? 0.2247 0.2209 0.2335 0.0036  0.0108  0.0381  156 ARG   A C   
1295 O O   . ARG   A 155 ? 0.2200 0.2686 0.2396 -0.0076 -0.0083 0.0158  156 ARG   A O   
1296 C CB  . ARG   A 155 ? 0.2556 0.2904 0.2824 -0.0639 -0.0276 0.0419  156 ARG   A CB  
1297 C CG  . ARG   A 155 ? 0.2979 0.3190 0.3434 -0.0690 -0.0140 0.0427  156 ARG   A CG  
1298 C CD  . ARG   A 155 ? 0.3689 0.3497 0.3882 -0.0339 0.0138  0.0503  156 ARG   A CD  
1299 N NE  . ARG   A 155 ? 0.4093 0.3660 0.4362 -0.0245 0.0747  0.0531  156 ARG   A NE  
1300 C CZ  . ARG   A 155 ? 0.4620 0.3753 0.4709 -0.0433 0.0831  0.0593  156 ARG   A CZ  
1301 N NH1 . ARG   A 155 ? 0.4496 0.3782 0.4805 -0.0330 0.1071  0.0426  156 ARG   A NH1 
1302 N NH2 . ARG   A 155 ? 0.4925 0.3644 0.4915 -0.0603 0.0798  0.0722  156 ARG   A NH2 
1303 N N   . ILE   A 156 ? 0.2129 0.1987 0.1830 -0.0181 0.0067  0.0486  157 ILE   A N   
1304 C CA  . ILE   A 156 ? 0.2185 0.2172 0.1542 -0.0226 0.0049  0.0471  157 ILE   A CA  
1305 C C   . ILE   A 156 ? 0.2114 0.1961 0.1608 0.0001  0.0044  0.0230  157 ILE   A C   
1306 O O   . ILE   A 156 ? 0.2306 0.1853 0.1895 -0.0073 0.0233  -0.0056 157 ILE   A O   
1307 C CB  . ILE   A 156 ? 0.2220 0.2532 0.1730 -0.0111 -0.0055 0.0504  157 ILE   A CB  
1308 C CG1 . ILE   A 156 ? 0.2242 0.2540 0.2052 0.0091  0.0055  0.0224  157 ILE   A CG1 
1309 C CG2 . ILE   A 156 ? 0.2993 0.2933 0.1726 -0.0483 -0.0254 0.0630  157 ILE   A CG2 
1310 C CD1 . ILE   A 156 ? 0.2548 0.2458 0.1900 -0.0216 -0.0102 0.0143  157 ILE   A CD1 
1311 N N   . LYS   A 157 ? 0.2097 0.1961 0.1415 -0.0101 0.0146  0.0241  158 LYS   A N   
1312 C CA  . LYS   A 157 ? 0.2337 0.2065 0.1338 -0.0334 -0.0012 0.0378  158 LYS   A CA  
1313 C C   . LYS   A 157 ? 0.2411 0.1796 0.1198 -0.0322 0.0019  0.0133  158 LYS   A C   
1314 O O   . LYS   A 157 ? 0.2399 0.1897 0.1374 -0.0160 0.0178  0.0074  158 LYS   A O   
1315 C CB  . LYS   A 157 ? 0.2536 0.2207 0.1702 -0.0557 -0.0419 0.0520  158 LYS   A CB  
1316 C CG  . LYS   A 157 ? 0.2995 0.2382 0.2078 -0.0474 -0.0560 0.0383  158 LYS   A CG  
1317 C CD  . LYS   A 157 ? 0.3002 0.2383 0.2270 -0.0066 -0.0761 0.0253  158 LYS   A CD  
1318 C CE  . LYS   A 157 ? 0.2883 0.2683 0.2736 -0.0272 -0.0784 0.0323  158 LYS   A CE  
1319 N NZ  . LYS   A 157 ? 0.3396 0.2700 0.3125 0.0128  -0.0852 0.0043  158 LYS   A NZ  
1320 N N   . ILE   A 158 ? 0.1935 0.1793 0.1347 -0.0205 -0.0059 0.0267  159 ILE   A N   
1321 C CA  . ILE   A 158 ? 0.2119 0.1919 0.1171 -0.0274 0.0148  0.0143  159 ILE   A CA  
1322 C C   . ILE   A 158 ? 0.2517 0.2093 0.1699 -0.0209 0.0441  0.0251  159 ILE   A C   
1323 O O   . ILE   A 158 ? 0.2323 0.2059 0.1448 0.0023  0.0094  0.0307  159 ILE   A O   
1324 C CB  . ILE   A 158 ? 0.2009 0.2274 0.1479 -0.0360 0.0193  -0.0024 159 ILE   A CB  
1325 C CG1 . ILE   A 158 ? 0.2238 0.2459 0.1622 0.0363  0.0069  0.0088  159 ILE   A CG1 
1326 C CG2 . ILE   A 158 ? 0.2159 0.2831 0.1859 -0.0637 0.0300  -0.0176 159 ILE   A CG2 
1327 C CD1 . ILE   A 158 ? 0.2487 0.2917 0.1748 0.0506  0.0017  -0.0244 159 ILE   A CD1 
1344 N N   A ASP   A 160 ? 0.4849 0.4706 0.4376 0.1446  0.0099  0.0922  161 ASP   A N   
1345 N N   B ASP   A 160 ? 0.2076 0.2203 0.1267 0.0762  -0.0009 0.0173  161 ASP   A N   
1346 C CA  A ASP   A 160 ? 0.4441 0.4162 0.3684 0.1335  0.0145  0.0953  161 ASP   A CA  
1347 C CA  B ASP   A 160 ? 0.3055 0.2728 0.1732 0.1055  0.0541  0.0451  161 ASP   A CA  
1348 C C   A ASP   A 160 ? 0.3616 0.3274 0.2849 0.1160  -0.0002 0.0790  161 ASP   A C   
1349 C C   B ASP   A 160 ? 0.2861 0.3044 0.1759 0.1563  0.0195  0.0578  161 ASP   A C   
1350 O O   A ASP   A 160 ? 0.4141 0.3267 0.2929 0.0730  0.0138  0.0682  161 ASP   A O   
1351 O O   B ASP   A 160 ? 0.3501 0.3851 0.1661 0.2146  0.0426  0.0538  161 ASP   A O   
1352 C CB  A ASP   A 160 ? 0.4669 0.4252 0.3809 0.1710  0.0247  0.1181  161 ASP   A CB  
1353 C CB  B ASP   A 160 ? 0.3857 0.2668 0.2302 0.1344  0.1093  0.0553  161 ASP   A CB  
1354 C CG  A ASP   A 160 ? 0.5010 0.4361 0.3824 0.1822  0.0055  0.1499  161 ASP   A CG  
1355 C CG  B ASP   A 160 ? 0.4692 0.3038 0.2923 0.1407  0.1472  0.0475  161 ASP   A CG  
1356 O OD1 A ASP   A 160 ? 0.4773 0.4358 0.3832 0.2074  0.0023  0.1572  161 ASP   A OD1 
1357 O OD1 B ASP   A 160 ? 0.4997 0.3121 0.3271 0.1578  0.1838  0.0327  161 ASP   A OD1 
1358 O OD2 A ASP   A 160 ? 0.5293 0.4479 0.3791 0.1897  -0.0100 0.1532  161 ASP   A OD2 
1359 O OD2 B ASP   A 160 ? 0.5120 0.3273 0.3026 0.1426  0.1483  0.0303  161 ASP   A OD2 
1360 N N   . PHE   A 161 ? 0.2743 0.2416 0.1798 0.0569  0.0156  0.0495  162 PHE   A N   
1361 C CA  . PHE   A 161 ? 0.2363 0.2019 0.1665 0.0374  0.0169  0.0325  162 PHE   A CA  
1362 C C   . PHE   A 161 ? 0.2738 0.1881 0.1797 0.0264  -0.0144 0.0268  162 PHE   A C   
1363 O O   . PHE   A 161 ? 0.2581 0.2206 0.1657 0.0154  -0.0011 0.0317  162 PHE   A O   
1364 C CB  . PHE   A 161 ? 0.2458 0.1942 0.1666 -0.0014 -0.0289 0.0147  162 PHE   A CB  
1365 C CG  . PHE   A 161 ? 0.2547 0.1728 0.1423 0.0110  0.0123  0.0138  162 PHE   A CG  
1366 C CD1 . PHE   A 161 ? 0.3302 0.1852 0.1729 0.0358  0.0158  0.0333  162 PHE   A CD1 
1367 C CD2 . PHE   A 161 ? 0.2777 0.1780 0.1378 0.0374  -0.0128 -0.0162 162 PHE   A CD2 
1368 C CE1 . PHE   A 161 ? 0.3716 0.1983 0.1662 0.0391  0.0362  0.0198  162 PHE   A CE1 
1369 C CE2 . PHE   A 161 ? 0.3040 0.2086 0.1552 0.0391  -0.0079 -0.0053 162 PHE   A CE2 
1370 C CZ  . PHE   A 161 ? 0.3412 0.2102 0.1484 0.0399  0.0094  0.0074  162 PHE   A CZ  
1371 N N   . GLY   A 162 ? 0.2820 0.1764 0.1883 0.0378  -0.0221 0.0243  163 GLY   A N   
1372 C CA  . GLY   A 162 ? 0.2756 0.1828 0.2082 0.0573  -0.0086 0.0299  163 GLY   A CA  
1373 C C   . GLY   A 162 ? 0.2891 0.1703 0.1931 0.0325  -0.0092 0.0175  163 GLY   A C   
1374 O O   . GLY   A 162 ? 0.3457 0.1734 0.2291 0.0130  -0.0311 0.0651  163 GLY   A O   
1375 N N   . LEU   A 163 ? 0.2587 0.1802 0.1570 0.0340  -0.0163 0.0047  164 LEU   A N   
1376 C CA  . LEU   A 163 ? 0.2881 0.1648 0.1580 0.0031  -0.0164 0.0166  164 LEU   A CA  
1377 C C   . LEU   A 163 ? 0.2551 0.1593 0.1611 -0.0037 -0.0171 0.0260  164 LEU   A C   
1378 O O   . LEU   A 163 ? 0.2473 0.1847 0.1710 0.0070  -0.0039 0.0141  164 LEU   A O   
1379 C CB  . LEU   A 163 ? 0.4014 0.1820 0.1587 0.0199  -0.0288 0.0102  164 LEU   A CB  
1380 C CG  . LEU   A 163 ? 0.5132 0.2476 0.1894 -0.0385 -0.0378 0.0320  164 LEU   A CG  
1381 C CD1 . LEU   A 163 ? 0.5487 0.2772 0.1627 -0.0896 -0.0606 0.0177  164 LEU   A CD1 
1382 C CD2 . LEU   A 163 ? 0.5776 0.2589 0.2241 -0.0514 -0.0633 0.0387  164 LEU   A CD2 
1383 N N   . ALA   A 164 ? 0.2648 0.1502 0.1155 -0.0055 -0.0008 0.0152  165 ALA   A N   
1384 C CA  . ALA   A 164 ? 0.2138 0.1541 0.1355 -0.0121 0.0197  0.0136  165 ALA   A CA  
1385 C C   . ALA   A 164 ? 0.2137 0.1627 0.1341 0.0002  0.0182  0.0395  165 ALA   A C   
1386 O O   . ALA   A 164 ? 0.2479 0.1827 0.1449 0.0231  0.0030  0.0391  165 ALA   A O   
1387 C CB  . ALA   A 164 ? 0.2089 0.1762 0.1519 -0.0158 0.0087  0.0185  165 ALA   A CB  
1388 N N   . HIS   A 165 ? 0.2121 0.1617 0.1319 -0.0037 0.0142  0.0261  166 HIS   A N   
1389 C CA  . HIS   A 165 ? 0.1995 0.1850 0.1417 -0.0065 0.0097  0.0260  166 HIS   A CA  
1390 C C   . HIS   A 165 ? 0.2238 0.1835 0.1367 -0.0011 0.0271  0.0631  166 HIS   A C   
1391 O O   . HIS   A 165 ? 0.2497 0.1563 0.1352 0.0101  0.0226  0.0397  166 HIS   A O   
1392 C CB  . HIS   A 165 ? 0.2094 0.1989 0.1773 0.0045  -0.0083 0.0386  166 HIS   A CB  
1393 C CG  . HIS   A 165 ? 0.2395 0.1998 0.1943 0.0163  -0.0258 0.0230  166 HIS   A CG  
1394 N ND1 . HIS   A 165 ? 0.2496 0.1734 0.2024 0.0055  -0.0424 0.0201  166 HIS   A ND1 
1395 C CD2 . HIS   A 165 ? 0.2549 0.2125 0.2085 0.0028  -0.0242 0.0496  166 HIS   A CD2 
1396 C CE1 . HIS   A 165 ? 0.2612 0.2073 0.2113 -0.0150 -0.0283 0.0356  166 HIS   A CE1 
1397 N NE2 . HIS   A 165 ? 0.2754 0.2302 0.2261 -0.0233 -0.0344 0.0386  166 HIS   A NE2 
1398 N N   . LYS   A 166 ? 0.2608 0.2093 0.1512 0.0234  0.0270  0.0604  167 LYS   A N   
1399 C CA  . LYS   A 166 ? 0.2695 0.2422 0.1904 0.0523  0.0186  0.0616  167 LYS   A CA  
1400 C C   . LYS   A 166 ? 0.2379 0.2488 0.2493 0.0142  0.0743  0.0461  167 LYS   A C   
1401 O O   . LYS   A 166 ? 0.2874 0.2737 0.3530 -0.0323 0.0835  0.0612  167 LYS   A O   
1402 C CB  . LYS   A 166 ? 0.4180 0.3349 0.2267 0.0327  -0.0109 0.0435  167 LYS   A CB  
1403 C CG  . LYS   A 166 ? 0.5276 0.4125 0.2773 0.0258  -0.0453 0.0587  167 LYS   A CG  
1404 C CD  . LYS   A 166 ? 0.6098 0.4478 0.3110 0.0046  -0.0515 0.0664  167 LYS   A CD  
1405 C CE  . LYS   A 166 ? 0.6041 0.5007 0.3553 0.0239  -0.0540 0.0878  167 LYS   A CE  
1406 N NZ  . LYS   A 166 ? 0.6264 0.5171 0.3888 0.0307  -0.0147 0.0980  167 LYS   A NZ  
1407 N N   . ILE   A 167 ? 0.1960 0.2415 0.2132 0.0058  0.0383  -0.0201 168 ILE   A N   
1408 C CA  . ILE   A 167 ? 0.2142 0.2878 0.2500 0.0175  0.0588  -0.0496 168 ILE   A CA  
1409 C C   . ILE   A 167 ? 0.2926 0.3217 0.2931 0.0442  0.0540  -0.0629 168 ILE   A C   
1410 O O   . ILE   A 167 ? 0.4135 0.3319 0.3188 0.0875  0.0505  -0.0609 168 ILE   A O   
1411 C CB  . ILE   A 167 ? 0.1926 0.3221 0.2546 0.0141  0.0117  -0.0651 168 ILE   A CB  
1412 C CG1 . ILE   A 167 ? 0.2774 0.3059 0.2900 0.0096  0.0480  -0.0727 168 ILE   A CG1 
1413 C CG2 . ILE   A 167 ? 0.2103 0.3454 0.2876 0.0020  0.0040  -0.0398 168 ILE   A CG2 
1414 C CD1 . ILE   A 167 ? 0.2909 0.3244 0.3055 -0.0089 0.0544  -0.0838 168 ILE   A CD1 
1415 N N   . ASP   A 168 ? 0.2744 0.3597 0.2561 0.0301  0.0234  -0.0739 169 ASP   A N   
1416 C CA  . ASP   A 168 ? 0.2828 0.4191 0.2394 0.0238  0.0135  -0.0675 169 ASP   A CA  
1417 C C   . ASP   A 168 ? 0.2427 0.3604 0.2130 -0.0036 0.0444  -0.0783 169 ASP   A C   
1418 O O   . ASP   A 168 ? 0.2413 0.3618 0.2026 -0.0013 0.0493  -0.0365 169 ASP   A O   
1419 C CB  . ASP   A 168 ? 0.3925 0.5242 0.2778 0.0251  -0.0313 -0.0529 169 ASP   A CB  
1420 C CG  . ASP   A 168 ? 0.5137 0.6034 0.3160 0.0163  -0.0348 -0.0195 169 ASP   A CG  
1421 O OD1 . ASP   A 168 ? 0.4996 0.6244 0.3274 -0.0053 -0.0432 -0.0224 169 ASP   A OD1 
1422 O OD2 . ASP   A 168 ? 0.5858 0.6295 0.3301 0.0256  -0.0195 0.0049  169 ASP   A OD2 
1423 N N   . PHE   A 169 ? 0.2479 0.3287 0.2151 -0.0419 0.0417  -0.0578 170 PHE   A N   
1424 C CA  . PHE   A 169 ? 0.2882 0.3215 0.2333 -0.0254 0.0509  -0.0982 170 PHE   A CA  
1425 C C   . PHE   A 169 ? 0.2555 0.3390 0.2299 -0.0283 0.0211  -0.1027 170 PHE   A C   
1426 O O   . PHE   A 169 ? 0.2742 0.4538 0.2503 -0.0206 0.0330  -0.0945 170 PHE   A O   
1427 C CB  . PHE   A 169 ? 0.4350 0.3130 0.2358 -0.0486 0.0723  -0.1068 170 PHE   A CB  
1428 C CG  . PHE   A 169 ? 0.6602 0.3171 0.2624 -0.0768 0.1042  -0.0766 170 PHE   A CG  
1429 C CD1 . PHE   A 169 ? 0.6939 0.2800 0.2718 -0.1086 0.1158  -0.0862 170 PHE   A CD1 
1430 C CD2 . PHE   A 169 ? 0.7811 0.3392 0.2781 -0.0706 0.1160  -0.0507 170 PHE   A CD2 
1431 C CE1 . PHE   A 169 ? 0.8017 0.3080 0.2793 -0.1037 0.1318  -0.0552 170 PHE   A CE1 
1432 C CE2 . PHE   A 169 ? 0.8508 0.3367 0.2796 -0.0641 0.1307  -0.0467 170 PHE   A CE2 
1433 C CZ  . PHE   A 169 ? 0.8469 0.3240 0.2752 -0.0905 0.1517  -0.0400 170 PHE   A CZ  
1434 N N   . GLY   A 170 ? 0.3263 0.2593 0.2109 -0.0073 -0.0036 -0.0975 171 GLY   A N   
1435 C CA  . GLY   A 170 ? 0.3939 0.2226 0.2162 0.0183  0.0061  -0.0847 171 GLY   A CA  
1436 C C   . GLY   A 170 ? 0.3535 0.1977 0.2001 -0.0060 0.0173  -0.0402 171 GLY   A C   
1437 O O   . GLY   A 170 ? 0.3434 0.2014 0.2122 -0.0135 0.0236  -0.0322 171 GLY   A O   
1438 N N   . ASN   A 171 ? 0.3460 0.1652 0.1812 0.0029  0.0314  -0.0364 172 ASN   A N   
1439 C CA  . ASN   A 171 ? 0.2794 0.1711 0.1679 -0.0199 0.0157  -0.0227 172 ASN   A CA  
1440 C C   . ASN   A 171 ? 0.2968 0.1758 0.1588 -0.0371 0.0143  0.0027  172 ASN   A C   
1441 O O   . ASN   A 171 ? 0.3462 0.2149 0.1472 -0.0463 0.0151  -0.0071 172 ASN   A O   
1442 C CB  . ASN   A 171 ? 0.2564 0.2065 0.1781 -0.0313 0.0262  -0.0131 172 ASN   A CB  
1443 C CG  . ASN   A 171 ? 0.3080 0.2224 0.2093 -0.0023 0.0522  -0.0063 172 ASN   A CG  
1444 O OD1 . ASN   A 171 ? 0.3274 0.2287 0.2217 0.0060  0.0526  0.0110  172 ASN   A OD1 
1445 N ND2 . ASN   A 171 ? 0.3185 0.2588 0.2493 0.0252  0.0503  0.0082  172 ASN   A ND2 
1446 N N   . GLU   A 172 ? 0.2572 0.1757 0.1951 -0.0113 -0.0024 -0.0200 173 GLU   A N   
1447 C CA  . GLU   A 172 ? 0.2333 0.2008 0.2544 -0.0329 -0.0272 0.0146  173 GLU   A CA  
1448 C C   . GLU   A 172 ? 0.2577 0.1680 0.2461 -0.0415 0.0120  0.0104  173 GLU   A C   
1449 O O   . GLU   A 172 ? 0.3090 0.1902 0.2227 -0.0469 0.0055  0.0147  173 GLU   A O   
1450 C CB  . GLU   A 172 ? 0.3053 0.2834 0.3542 -0.0686 -0.0839 0.0113  173 GLU   A CB  
1451 C CG  . GLU   A 172 ? 0.4393 0.3486 0.4295 -0.0884 -0.1059 0.0243  173 GLU   A CG  
1452 C CD  . GLU   A 172 ? 0.5724 0.3927 0.4914 -0.1040 -0.1032 0.0467  173 GLU   A CD  
1453 O OE1 . GLU   A 172 ? 0.5634 0.3467 0.5173 -0.0841 -0.0943 0.0757  173 GLU   A OE1 
1454 O OE2 . GLU   A 172 ? 0.6647 0.4278 0.5125 -0.1461 -0.1183 0.0394  173 GLU   A OE2 
1455 N N   . PHE   A 173 ? 0.2818 0.1534 0.2721 -0.0260 0.0422  -0.0073 174 PHE   A N   
1456 C CA  . PHE   A 173 ? 0.3193 0.1693 0.2871 -0.0146 0.1075  -0.0469 174 PHE   A CA  
1457 C C   . PHE   A 173 ? 0.4132 0.2049 0.3156 0.0086  0.1346  -0.0037 174 PHE   A C   
1458 O O   . PHE   A 173 ? 0.4756 0.2216 0.3536 -0.0327 0.1639  0.0296  174 PHE   A O   
1459 C CB  . PHE   A 173 ? 0.2948 0.2152 0.2692 -0.0343 0.1075  -0.0727 174 PHE   A CB  
1460 C CG  . PHE   A 173 ? 0.3764 0.2378 0.2441 -0.0946 0.1129  -0.0611 174 PHE   A CG  
1461 C CD1 . PHE   A 173 ? 0.4379 0.2625 0.2355 -0.0812 0.1184  -0.0625 174 PHE   A CD1 
1462 C CD2 . PHE   A 173 ? 0.4545 0.2721 0.2528 -0.1177 0.0858  -0.0358 174 PHE   A CD2 
1463 C CE1 . PHE   A 173 ? 0.4874 0.2762 0.2478 -0.1173 0.1324  -0.0474 174 PHE   A CE1 
1464 C CE2 . PHE   A 173 ? 0.5339 0.3091 0.2422 -0.1326 0.0908  -0.0432 174 PHE   A CE2 
1465 C CZ  . PHE   A 173 ? 0.5466 0.3017 0.2453 -0.1340 0.1099  -0.0503 174 PHE   A CZ  
1466 N N   . LYS   A 174 ? 0.3991 0.2116 0.3105 0.0396  0.1186  -0.0180 175 LYS   A N   
1467 C CA  . LYS   A 174 ? 0.4246 0.2280 0.3333 0.0175  0.0966  -0.0084 175 LYS   A CA  
1468 C C   . LYS   A 174 ? 0.4615 0.2352 0.3342 0.0063  0.1553  -0.0011 175 LYS   A C   
1469 O O   . LYS   A 174 ? 0.4675 0.2697 0.3554 0.0332  0.1358  0.0148  175 LYS   A O   
1470 C CB  . LYS   A 174 ? 0.4112 0.2351 0.3421 0.0117  0.0331  -0.0063 175 LYS   A CB  
1471 C CG  . LYS   A 174 ? 0.3851 0.2570 0.3470 -0.0080 0.0118  0.0353  175 LYS   A CG  
1472 C CD  . LYS   A 174 ? 0.3771 0.2730 0.3659 0.0208  -0.0623 0.0708  175 LYS   A CD  
1473 C CE  . LYS   A 174 ? 0.4162 0.2934 0.4024 -0.0008 -0.0898 0.0662  175 LYS   A CE  
1474 N NZ  . LYS   A 174 ? 0.4112 0.2930 0.4083 -0.0345 -0.1337 0.0917  175 LYS   A NZ  
1475 N N   . ASN   A 175 ? 0.4993 0.2500 0.3502 -0.0129 0.1870  0.0022  176 ASN   A N   
1476 C CA  . ASN   A 175 ? 0.6082 0.2982 0.3682 -0.0346 0.2012  -0.0018 176 ASN   A CA  
1477 C C   . ASN   A 175 ? 0.5514 0.3104 0.3222 -0.0446 0.1437  0.0047  176 ASN   A C   
1478 O O   . ASN   A 175 ? 0.5869 0.3340 0.3575 0.0013  0.0962  0.0347  176 ASN   A O   
1479 C CB  . ASN   A 175 ? 0.7932 0.3729 0.4317 -0.0136 0.2170  -0.0178 176 ASN   A CB  
1480 C CG  . ASN   A 175 ? 0.9528 0.4517 0.4932 0.0077  0.2109  -0.0442 176 ASN   A CG  
1481 O OD1 . ASN   A 175 ? 1.0070 0.4802 0.5162 0.0220  0.2134  -0.0539 176 ASN   A OD1 
1482 N ND2 . ASN   A 175 ? 1.0052 0.4718 0.5115 0.0141  0.2048  -0.0536 176 ASN   A ND2 
1483 N N   . ILE   A 176 ? 0.4697 0.2607 0.2236 -0.0692 0.1196  -0.0103 177 ILE   A N   
1484 C CA  . ILE   A 176 ? 0.3896 0.2352 0.1923 -0.0334 0.0524  -0.0226 177 ILE   A CA  
1485 C C   . ILE   A 176 ? 0.3301 0.2190 0.1909 -0.0124 0.0098  -0.0280 177 ILE   A C   
1486 O O   . ILE   A 176 ? 0.2952 0.2485 0.2010 -0.0404 0.0253  -0.0345 177 ILE   A O   
1487 C CB  . ILE   A 176 ? 0.3063 0.2106 0.1584 -0.0386 0.0112  -0.0095 177 ILE   A CB  
1488 C CG1 . ILE   A 176 ? 0.3165 0.2191 0.1521 -0.0254 0.0083  -0.0284 177 ILE   A CG1 
1489 C CG2 . ILE   A 176 ? 0.2885 0.2468 0.2052 -0.0353 0.0282  -0.0245 177 ILE   A CG2 
1490 C CD1 . ILE   A 176 ? 0.3498 0.2240 0.1726 -0.0068 -0.0034 -0.0370 177 ILE   A CD1 
1491 N N   . PHE   A 177 ? 0.3171 0.1819 0.1541 -0.0180 -0.0027 -0.0160 178 PHE   A N   
1492 C CA  . PHE   A 177 ? 0.3145 0.1962 0.1469 -0.0335 -0.0162 -0.0050 178 PHE   A CA  
1493 C C   . PHE   A 177 ? 0.3038 0.2348 0.1861 -0.0231 -0.0111 0.0461  178 PHE   A C   
1494 O O   . PHE   A 177 ? 0.3432 0.2865 0.2439 0.0138  0.0041  0.0556  178 PHE   A O   
1495 C CB  . PHE   A 177 ? 0.3311 0.2054 0.1584 -0.0496 -0.0126 -0.0135 178 PHE   A CB  
1496 C CG  . PHE   A 177 ? 0.2885 0.1847 0.1716 -0.0316 0.0144  -0.0248 178 PHE   A CG  
1497 C CD1 . PHE   A 177 ? 0.3097 0.1893 0.1769 -0.0275 0.0298  -0.0344 178 PHE   A CD1 
1498 C CD2 . PHE   A 177 ? 0.2991 0.1759 0.1986 -0.0313 0.0175  -0.0251 178 PHE   A CD2 
1499 C CE1 . PHE   A 177 ? 0.2958 0.2216 0.2008 -0.0452 0.0066  -0.0126 178 PHE   A CE1 
1500 C CE2 . PHE   A 177 ? 0.2972 0.1843 0.1968 -0.0227 0.0261  -0.0158 178 PHE   A CE2 
1501 C CZ  . PHE   A 177 ? 0.2913 0.2025 0.2086 -0.0456 0.0097  -0.0175 178 PHE   A CZ  
1502 N N   . GLY   A 178 ? 0.3266 0.2471 0.1872 -0.0398 0.0073  0.0483  179 GLY   A N   
1503 C CA  . GLY   A 178 ? 0.3044 0.3012 0.1986 -0.0319 0.0138  0.0537  179 GLY   A CA  
1504 C C   . GLY   A 178 ? 0.3291 0.3074 0.2143 -0.0150 0.0184  0.0749  179 GLY   A C   
1505 O O   . GLY   A 178 ? 0.3374 0.3191 0.2269 -0.0433 0.0459  0.0408  179 GLY   A O   
1506 N N   . THR   A 179 ? 0.2863 0.2939 0.2149 -0.0026 0.0129  0.0963  180 THR   A N   
1507 C CA  . THR   A 179 ? 0.2702 0.2862 0.2485 0.0238  0.0475  0.0828  180 THR   A CA  
1508 C C   . THR   A 179 ? 0.2725 0.1957 0.2083 0.0165  0.0371  0.0463  180 THR   A C   
1509 O O   . THR   A 179 ? 0.2811 0.1850 0.1660 0.0138  0.0305  0.0177  180 THR   A O   
1510 C CB  . THR   A 179 ? 0.2691 0.3553 0.3016 0.0624  0.0437  0.1323  180 THR   A CB  
1511 O OG1 . THR   A 179 ? 0.3089 0.4208 0.3553 0.0712  -0.0137 0.1483  180 THR   A OG1 
1512 C CG2 . THR   A 179 ? 0.3117 0.3759 0.3167 0.0691  0.1050  0.1132  180 THR   A CG2 
1513 N N   . PRO   A 180 ? 0.2984 0.1581 0.2371 0.0460  0.0556  0.0494  181 PRO   A N   
1514 C CA  . PRO   A 180 ? 0.2997 0.1327 0.2139 0.0145  0.0429  0.0125  181 PRO   A CA  
1515 C C   . PRO   A 180 ? 0.2761 0.1453 0.1701 0.0182  0.0269  0.0044  181 PRO   A C   
1516 O O   . PRO   A 180 ? 0.2715 0.1443 0.1723 -0.0233 0.0020  -0.0028 181 PRO   A O   
1517 C CB  . PRO   A 180 ? 0.3618 0.1216 0.2485 0.0078  0.0571  -0.0031 181 PRO   A CB  
1518 C CG  . PRO   A 180 ? 0.3799 0.1608 0.2640 0.0452  0.0505  0.0276  181 PRO   A CG  
1519 C CD  . PRO   A 180 ? 0.3720 0.1686 0.2691 0.0619  0.0366  0.0469  181 PRO   A CD  
1520 N N   . GLU   A 181 ? 0.2800 0.1449 0.1414 0.0206  0.0154  -0.0065 182 GLU   A N   
1521 C CA  . GLU   A 181 ? 0.2793 0.1487 0.1422 0.0209  0.0306  -0.0198 182 GLU   A CA  
1522 C C   . GLU   A 181 ? 0.2344 0.1275 0.1385 -0.0020 0.0275  -0.0132 182 GLU   A C   
1523 O O   . GLU   A 181 ? 0.2200 0.1444 0.1393 0.0015  0.0033  -0.0071 182 GLU   A O   
1524 C CB  . GLU   A 181 ? 0.3437 0.2154 0.1723 0.0516  0.0630  -0.0415 182 GLU   A CB  
1525 C CG  . GLU   A 181 ? 0.3783 0.3138 0.2593 0.0840  0.0476  0.0140  182 GLU   A CG  
1526 C CD  . GLU   A 181 ? 0.3596 0.4490 0.3110 0.1132  0.0444  0.0738  182 GLU   A CD  
1527 O OE1 . GLU   A 181 ? 0.3389 0.4832 0.3365 0.0767  0.0487  0.1248  182 GLU   A OE1 
1528 O OE2 . GLU   A 181 ? 0.3980 0.4969 0.3405 0.1242  0.0103  0.0851  182 GLU   A OE2 
1529 N N   . PHE   A 182 ? 0.2030 0.1451 0.1248 -0.0058 0.0148  -0.0266 183 PHE   A N   
1530 C CA  . PHE   A 182 ? 0.2169 0.1537 0.1303 -0.0265 0.0059  -0.0055 183 PHE   A CA  
1531 C C   . PHE   A 182 ? 0.2412 0.1235 0.1276 -0.0035 0.0253  -0.0162 183 PHE   A C   
1532 O O   . PHE   A 182 ? 0.2853 0.1401 0.1713 -0.0306 0.0152  -0.0324 183 PHE   A O   
1533 C CB  . PHE   A 182 ? 0.2046 0.2171 0.1394 -0.0289 -0.0088 0.0022  183 PHE   A CB  
1534 C CG  . PHE   A 182 ? 0.2259 0.2394 0.1580 -0.0290 -0.0010 0.0096  183 PHE   A CG  
1535 C CD1 . PHE   A 182 ? 0.2320 0.2630 0.1908 -0.0232 -0.0194 0.0598  183 PHE   A CD1 
1536 C CD2 . PHE   A 182 ? 0.2178 0.2635 0.1589 -0.0098 0.0190  -0.0589 183 PHE   A CD2 
1537 C CE1 . PHE   A 182 ? 0.2366 0.3004 0.1991 -0.0166 -0.0093 0.0446  183 PHE   A CE1 
1538 C CE2 . PHE   A 182 ? 0.2357 0.2974 0.2092 -0.0527 0.0202  -0.0255 183 PHE   A CE2 
1539 C CZ  . PHE   A 182 ? 0.2679 0.3143 0.2081 -0.0103 0.0377  0.0224  183 PHE   A CZ  
1540 N N   . VAL   A 183 ? 0.2133 0.1381 0.1221 -0.0217 0.0182  0.0107  184 VAL   A N   
1541 C CA  . VAL   A 183 ? 0.2007 0.1411 0.1286 -0.0125 0.0312  0.0146  184 VAL   A CA  
1542 C C   . VAL   A 183 ? 0.2084 0.1324 0.1329 -0.0076 -0.0009 -0.0089 184 VAL   A C   
1543 O O   . VAL   A 183 ? 0.2217 0.1619 0.1378 -0.0176 0.0062  -0.0238 184 VAL   A O   
1544 C CB  . VAL   A 183 ? 0.2254 0.1430 0.1622 0.0100  0.0309  0.0091  184 VAL   A CB  
1545 C CG1 . VAL   A 183 ? 0.2563 0.1882 0.1882 0.0660  0.0319  0.0229  184 VAL   A CG1 
1546 C CG2 . VAL   A 183 ? 0.2710 0.1473 0.1708 0.0081  0.0454  -0.0123 184 VAL   A CG2 
1547 N N   . ALA   A 184 ? 0.2075 0.1341 0.1486 -0.0044 0.0407  -0.0070 185 ALA   A N   
1548 C CA  . ALA   A 184 ? 0.1918 0.1362 0.1492 -0.0127 0.0173  -0.0248 185 ALA   A CA  
1549 C C   . ALA   A 184 ? 0.2035 0.1360 0.1281 -0.0005 0.0200  -0.0109 185 ALA   A C   
1550 O O   . ALA   A 184 ? 0.1975 0.1356 0.1487 -0.0165 0.0322  0.0003  185 ALA   A O   
1551 C CB  . ALA   A 184 ? 0.2231 0.1381 0.1605 -0.0086 0.0303  -0.0488 185 ALA   A CB  
1552 N N   . PRO   A 185 ? 0.1988 0.1403 0.1348 -0.0246 0.0015  -0.0133 186 PRO   A N   
1553 C CA  . PRO   A 185 ? 0.2067 0.1591 0.1405 -0.0383 -0.0052 -0.0063 186 PRO   A CA  
1554 C C   . PRO   A 185 ? 0.2128 0.1606 0.1355 -0.0417 0.0223  -0.0231 186 PRO   A C   
1555 O O   . PRO   A 185 ? 0.2499 0.1509 0.1485 -0.0512 0.0091  -0.0154 186 PRO   A O   
1556 C CB  . PRO   A 185 ? 0.2216 0.1781 0.1576 -0.0226 -0.0051 -0.0072 186 PRO   A CB  
1557 C CG  . PRO   A 185 ? 0.2243 0.1866 0.1600 -0.0316 -0.0055 -0.0051 186 PRO   A CG  
1558 C CD  . PRO   A 185 ? 0.2298 0.1442 0.1474 -0.0087 0.0009  -0.0010 186 PRO   A CD  
1559 N N   . GLU   A 186 ? 0.2136 0.1612 0.1318 -0.0308 0.0229  -0.0222 187 GLU   A N   
1560 C CA  . GLU   A 186 ? 0.2247 0.1579 0.1326 -0.0252 0.0315  -0.0188 187 GLU   A CA  
1561 C C   . GLU   A 186 ? 0.1977 0.1459 0.1239 -0.0370 0.0280  -0.0079 187 GLU   A C   
1562 O O   . GLU   A 186 ? 0.2435 0.1583 0.1503 -0.0515 0.0562  -0.0049 187 GLU   A O   
1563 C CB  . GLU   A 186 ? 0.2345 0.1270 0.1527 -0.0518 0.0440  -0.0526 187 GLU   A CB  
1564 C CG  . GLU   A 186 ? 0.2592 0.1419 0.1615 -0.0331 0.0187  -0.0229 187 GLU   A CG  
1565 C CD  . GLU   A 186 ? 0.2426 0.1394 0.1385 -0.0358 0.0178  -0.0426 187 GLU   A CD  
1566 O OE1 . GLU   A 186 ? 0.2379 0.1541 0.1469 -0.0223 0.0202  -0.0191 187 GLU   A OE1 
1567 O OE2 . GLU   A 186 ? 0.2555 0.1454 0.1437 -0.0274 0.0116  -0.0131 187 GLU   A OE2 
1568 N N   . ILE   A 187 ? 0.2181 0.1355 0.1258 -0.0315 0.0162  -0.0099 188 ILE   A N   
1569 C CA  . ILE   A 187 ? 0.2114 0.1375 0.1480 -0.0434 0.0032  -0.0116 188 ILE   A CA  
1570 C C   . ILE   A 187 ? 0.2290 0.1462 0.1475 -0.0330 0.0334  -0.0113 188 ILE   A C   
1571 O O   . ILE   A 187 ? 0.2415 0.1546 0.1481 -0.0245 0.0310  -0.0138 188 ILE   A O   
1572 C CB  . ILE   A 187 ? 0.2248 0.1191 0.1625 -0.0430 0.0191  -0.0246 188 ILE   A CB  
1573 C CG1 . ILE   A 187 ? 0.2190 0.1781 0.1705 -0.0497 0.0388  -0.0495 188 ILE   A CG1 
1574 C CG2 . ILE   A 187 ? 0.2715 0.1390 0.1685 0.0125  0.0117  -0.0039 188 ILE   A CG2 
1575 C CD1 . ILE   A 187 ? 0.2444 0.1795 0.1938 -0.0521 0.0351  -0.0189 188 ILE   A CD1 
1576 N N   . VAL   A 188 ? 0.2281 0.1534 0.1304 -0.0348 0.0332  -0.0367 189 VAL   A N   
1577 C CA  . VAL   A 188 ? 0.2401 0.1532 0.1274 -0.0428 0.0279  -0.0246 189 VAL   A CA  
1578 C C   . VAL   A 188 ? 0.2343 0.1441 0.1481 -0.0304 0.0256  -0.0310 189 VAL   A C   
1579 O O   . VAL   A 188 ? 0.2684 0.1455 0.1505 -0.0426 0.0287  -0.0365 189 VAL   A O   
1580 C CB  . VAL   A 188 ? 0.2686 0.1555 0.1299 -0.0270 0.0424  -0.0139 189 VAL   A CB  
1581 C CG1 . VAL   A 188 ? 0.2837 0.1551 0.1492 -0.0411 0.0016  -0.0458 189 VAL   A CG1 
1582 C CG2 . VAL   A 188 ? 0.2607 0.2039 0.1408 -0.0384 0.0723  -0.0056 189 VAL   A CG2 
1583 N N   . ASN   A 189 ? 0.2242 0.1561 0.1438 -0.0332 0.0320  -0.0265 190 ASN   A N   
1584 C CA  . ASN   A 189 ? 0.2445 0.1702 0.1526 -0.0345 0.0202  -0.0160 190 ASN   A CA  
1585 C C   . ASN   A 189 ? 0.2527 0.1747 0.1517 -0.0511 0.0281  -0.0243 190 ASN   A C   
1586 O O   . ASN   A 189 ? 0.2495 0.2038 0.1694 -0.0594 0.0371  -0.0167 190 ASN   A O   
1587 C CB  . ASN   A 189 ? 0.2456 0.1837 0.1440 -0.0070 -0.0005 -0.0089 190 ASN   A CB  
1588 C CG  . ASN   A 189 ? 0.2765 0.1733 0.1516 -0.0516 -0.0031 -0.0048 190 ASN   A CG  
1589 O OD1 . ASN   A 189 ? 0.3000 0.2023 0.2107 -0.0788 -0.0036 -0.0316 190 ASN   A OD1 
1590 N ND2 . ASN   A 189 ? 0.2958 0.1937 0.1672 -0.0478 -0.0054 0.0007  190 ASN   A ND2 
1591 N N   . TYR   A 190 ? 0.2536 0.1516 0.1368 -0.0363 0.0205  -0.0261 191 TYR   A N   
1592 C CA  . TYR   A 190 ? 0.2797 0.1319 0.1389 -0.0497 0.0324  -0.0077 191 TYR   A CA  
1593 C C   . TYR   A 190 ? 0.2361 0.1562 0.1414 -0.0521 0.0363  -0.0316 191 TYR   A C   
1594 O O   . TYR   A 190 ? 0.2927 0.2016 0.1599 -0.0612 0.0766  -0.0247 191 TYR   A O   
1595 C CB  . TYR   A 190 ? 0.2796 0.1348 0.1578 -0.0157 0.0375  -0.0117 191 TYR   A CB  
1596 C CG  . TYR   A 190 ? 0.2709 0.1325 0.1586 -0.0392 0.0265  -0.0161 191 TYR   A CG  
1597 C CD1 . TYR   A 190 ? 0.2799 0.1674 0.1829 -0.0113 0.0032  -0.0231 191 TYR   A CD1 
1598 C CD2 . TYR   A 190 ? 0.2734 0.1485 0.1648 -0.0408 0.0324  -0.0359 191 TYR   A CD2 
1599 C CE1 . TYR   A 190 ? 0.2792 0.1787 0.1917 -0.0137 0.0038  -0.0331 191 TYR   A CE1 
1600 C CE2 . TYR   A 190 ? 0.2774 0.1465 0.1923 -0.0216 0.0218  -0.0270 191 TYR   A CE2 
1601 C CZ  . TYR   A 190 ? 0.2627 0.1724 0.1956 0.0016  0.0174  -0.0315 191 TYR   A CZ  
1602 O OH  . TYR   A 190 ? 0.2833 0.2128 0.2310 -0.0057 0.0101  -0.0489 191 TYR   A OH  
1603 N N   . GLU   A 191 ? 0.2226 0.1536 0.1619 -0.0364 0.0172  -0.0341 192 GLU   A N   
1604 C CA  . GLU   A 191 ? 0.2243 0.1755 0.1832 -0.0278 0.0239  -0.0551 192 GLU   A CA  
1605 C C   . GLU   A 191 ? 0.2174 0.1889 0.1927 -0.0469 0.0340  -0.0606 192 GLU   A C   
1606 O O   . GLU   A 191 ? 0.2238 0.1971 0.1947 -0.0371 0.0398  -0.0491 192 GLU   A O   
1607 C CB  . GLU   A 191 ? 0.2427 0.1969 0.2162 -0.0373 0.0034  -0.0496 192 GLU   A CB  
1608 C CG  . GLU   A 191 ? 0.3053 0.2738 0.2667 -0.0321 -0.0244 -0.0437 192 GLU   A CG  
1609 C CD  . GLU   A 191 ? 0.4163 0.3397 0.3236 -0.0454 -0.0200 -0.0115 192 GLU   A CD  
1610 O OE1 . GLU   A 191 ? 0.4273 0.3441 0.3516 -0.0451 -0.0082 0.0144  192 GLU   A OE1 
1611 O OE2 . GLU   A 191 ? 0.4476 0.3831 0.3517 -0.0675 -0.0482 0.0231  192 GLU   A OE2 
1612 N N   . PRO   A 192 ? 0.2217 0.2212 0.1861 -0.0517 0.0395  -0.0704 193 PRO   A N   
1613 C CA  . PRO   A 192 ? 0.2126 0.2250 0.1846 -0.0531 0.0513  -0.0790 193 PRO   A CA  
1614 C C   . PRO   A 192 ? 0.2454 0.1892 0.1631 -0.0344 0.0327  -0.0455 193 PRO   A C   
1615 O O   . PRO   A 192 ? 0.2603 0.2109 0.1843 -0.0397 -0.0128 -0.0413 193 PRO   A O   
1616 C CB  . PRO   A 192 ? 0.2066 0.2763 0.2262 -0.0308 0.0515  -0.0900 193 PRO   A CB  
1617 C CG  . PRO   A 192 ? 0.2293 0.2787 0.2100 -0.0585 0.0452  -0.1071 193 PRO   A CG  
1618 C CD  . PRO   A 192 ? 0.2190 0.2712 0.1973 -0.0441 0.0356  -0.0785 193 PRO   A CD  
1619 N N   . LEU   A 193 ? 0.2248 0.1627 0.1581 -0.0245 0.0152  -0.0573 194 LEU   A N   
1620 C CA  . LEU   A 193 ? 0.2180 0.1438 0.1633 -0.0405 0.0268  -0.0279 194 LEU   A CA  
1621 C C   . LEU   A 193 ? 0.2248 0.1503 0.1459 -0.0336 0.0227  -0.0223 194 LEU   A C   
1622 O O   . LEU   A 193 ? 0.2781 0.1714 0.1356 -0.0411 0.0258  -0.0175 194 LEU   A O   
1623 C CB  . LEU   A 193 ? 0.2051 0.1589 0.1748 -0.0158 0.0146  -0.0312 194 LEU   A CB  
1624 C CG  . LEU   A 193 ? 0.2299 0.1545 0.1639 -0.0179 -0.0085 -0.0253 194 LEU   A CG  
1625 C CD1 . LEU   A 193 ? 0.2309 0.1715 0.1916 0.0247  0.0097  -0.0221 194 LEU   A CD1 
1626 C CD2 . LEU   A 193 ? 0.2456 0.1872 0.1580 -0.0185 0.0094  -0.0195 194 LEU   A CD2 
1627 N N   . GLY   A 194 ? 0.2760 0.1470 0.1696 -0.0598 0.0179  -0.0250 195 GLY   A N   
1628 C CA  . GLY   A 194 ? 0.3005 0.1565 0.1558 -0.1063 0.0228  -0.0375 195 GLY   A CA  
1629 C C   . GLY   A 194 ? 0.2725 0.1429 0.1227 -0.0333 0.0095  -0.0383 195 GLY   A C   
1630 O O   . GLY   A 194 ? 0.2804 0.1514 0.1503 -0.0121 -0.0051 -0.0277 195 GLY   A O   
1631 N N   . LEU   A 195 ? 0.2461 0.1419 0.1272 -0.0260 0.0006  -0.0154 196 LEU   A N   
1632 C CA  . LEU   A 195 ? 0.2455 0.1444 0.1212 -0.0277 0.0219  -0.0219 196 LEU   A CA  
1633 C C   . LEU   A 195 ? 0.2113 0.1269 0.1304 -0.0184 0.0144  -0.0211 196 LEU   A C   
1634 O O   . LEU   A 195 ? 0.1984 0.1501 0.1491 -0.0275 0.0139  -0.0256 196 LEU   A O   
1635 C CB  . LEU   A 195 ? 0.2518 0.1420 0.1226 -0.0243 0.0103  -0.0476 196 LEU   A CB  
1636 C CG  . LEU   A 195 ? 0.2463 0.1795 0.1372 -0.0296 0.0049  -0.0439 196 LEU   A CG  
1637 C CD1 . LEU   A 195 ? 0.2802 0.1759 0.1689 -0.0524 0.0035  -0.0730 196 LEU   A CD1 
1638 C CD2 . LEU   A 195 ? 0.2699 0.1970 0.1580 -0.0086 0.0028  -0.0144 196 LEU   A CD2 
1639 N N   . GLU   A 196 ? 0.2247 0.1639 0.1397 -0.0011 -0.0053 -0.0204 197 GLU   A N   
1640 C CA  . GLU   A 196 ? 0.1855 0.1494 0.1605 0.0198  0.0147  -0.0033 197 GLU   A CA  
1641 C C   . GLU   A 196 ? 0.1950 0.1287 0.1459 -0.0226 0.0214  -0.0161 197 GLU   A C   
1642 O O   . GLU   A 196 ? 0.2088 0.1413 0.1291 -0.0261 0.0058  0.0019  197 GLU   A O   
1643 C CB  . GLU   A 196 ? 0.1776 0.1684 0.2010 0.0120  0.0118  -0.0124 197 GLU   A CB  
1644 C CG  . GLU   A 196 ? 0.2068 0.2135 0.2121 0.0230  0.0350  -0.0123 197 GLU   A CG  
1645 C CD  . GLU   A 196 ? 0.2607 0.3293 0.3121 0.0632  0.0882  0.0461  197 GLU   A CD  
1646 O OE1 . GLU   A 196 ? 0.2440 0.3728 0.3415 0.0308  0.0916  0.0776  197 GLU   A OE1 
1647 O OE2 . GLU   A 196 ? 0.4028 0.3991 0.3557 0.1005  0.1283  0.0460  197 GLU   A OE2 
1648 N N   . ALA   A 197 ? 0.2043 0.1228 0.1417 -0.0087 -0.0073 -0.0136 198 ALA   A N   
1649 C CA  . ALA   A 197 ? 0.2022 0.1147 0.1323 0.0031  -0.0004 -0.0093 198 ALA   A CA  
1650 C C   . ALA   A 197 ? 0.1851 0.1306 0.1162 -0.0083 0.0009  -0.0052 198 ALA   A C   
1651 O O   . ALA   A 197 ? 0.2198 0.1317 0.1103 -0.0121 0.0070  -0.0119 198 ALA   A O   
1652 C CB  . ALA   A 197 ? 0.2572 0.1250 0.1495 -0.0049 0.0163  0.0217  198 ALA   A CB  
1653 N N   . ASP   A 198 ? 0.1959 0.1221 0.1192 -0.0155 -0.0235 -0.0031 199 ASP   A N   
1654 C CA  . ASP   A 198 ? 0.1981 0.1186 0.1122 -0.0210 -0.0208 0.0022  199 ASP   A CA  
1655 C C   . ASP   A 198 ? 0.1949 0.1048 0.1181 -0.0016 -0.0047 -0.0158 199 ASP   A C   
1656 O O   . ASP   A 198 ? 0.1996 0.1345 0.1092 -0.0024 0.0008  -0.0066 199 ASP   A O   
1657 C CB  . ASP   A 198 ? 0.2064 0.1350 0.1102 0.0038  -0.0325 0.0054  199 ASP   A CB  
1658 C CG  . ASP   A 198 ? 0.1927 0.1526 0.1252 0.0019  -0.0160 -0.0003 199 ASP   A CG  
1659 O OD1 . ASP   A 198 ? 0.2353 0.1483 0.1126 0.0098  -0.0089 -0.0009 199 ASP   A OD1 
1660 O OD2 . ASP   A 198 ? 0.2244 0.1555 0.1225 -0.0082 -0.0171 0.0148  199 ASP   A OD2 
1661 N N   . MET   A 199 ? 0.1972 0.0912 0.1145 0.0012  -0.0088 0.0032  200 MET   A N   
1662 C CA  . MET   A 199 ? 0.1907 0.0871 0.1181 -0.0050 -0.0113 -0.0217 200 MET   A CA  
1663 C C   . MET   A 199 ? 0.1927 0.1036 0.1070 0.0051  -0.0138 -0.0212 200 MET   A C   
1664 O O   . MET   A 199 ? 0.1997 0.1235 0.1143 -0.0105 -0.0033 0.0013  200 MET   A O   
1665 C CB  . MET   A 199 ? 0.2087 0.1315 0.1291 0.0267  -0.0070 -0.0283 200 MET   A CB  
1666 C CG  . MET   A 199 ? 0.2044 0.1356 0.1302 0.0031  -0.0045 -0.0264 200 MET   A CG  
1667 S SD  . MET   A 199 ? 0.2199 0.1329 0.1271 -0.0029 -0.0196 -0.0120 200 MET   A SD  
1668 C CE  . MET   A 199 ? 0.2532 0.1305 0.1209 -0.0235 -0.0038 -0.0140 200 MET   A CE  
1669 N N   . TRP   A 200 ? 0.1862 0.1016 0.1306 -0.0038 -0.0226 -0.0336 201 TRP   A N   
1670 C CA  . TRP   A 200 ? 0.1998 0.1159 0.1277 -0.0257 -0.0077 -0.0243 201 TRP   A CA  
1671 C C   . TRP   A 200 ? 0.1821 0.0996 0.1133 0.0034  -0.0001 -0.0050 201 TRP   A C   
1672 O O   . TRP   A 200 ? 0.1918 0.1295 0.1000 -0.0121 -0.0015 -0.0076 201 TRP   A O   
1673 C CB  . TRP   A 200 ? 0.2189 0.1191 0.1289 -0.0327 -0.0257 -0.0184 201 TRP   A CB  
1674 C CG  . TRP   A 200 ? 0.1978 0.1234 0.1329 -0.0174 0.0131  -0.0151 201 TRP   A CG  
1675 C CD1 . TRP   A 200 ? 0.1923 0.1348 0.1479 -0.0270 0.0014  -0.0194 201 TRP   A CD1 
1676 C CD2 . TRP   A 200 ? 0.2022 0.1232 0.1240 -0.0074 0.0106  -0.0183 201 TRP   A CD2 
1677 N NE1 . TRP   A 200 ? 0.2150 0.1296 0.1491 -0.0386 0.0172  -0.0092 201 TRP   A NE1 
1678 C CE2 . TRP   A 200 ? 0.2080 0.1476 0.1328 -0.0298 -0.0001 -0.0064 201 TRP   A CE2 
1679 C CE3 . TRP   A 200 ? 0.2196 0.1269 0.1348 -0.0402 -0.0049 -0.0082 201 TRP   A CE3 
1680 C CZ2 . TRP   A 200 ? 0.2345 0.1686 0.1222 -0.0517 -0.0160 0.0119  201 TRP   A CZ2 
1681 C CZ3 . TRP   A 200 ? 0.2589 0.1308 0.1398 -0.0556 -0.0279 -0.0105 201 TRP   A CZ3 
1682 C CH2 . TRP   A 200 ? 0.2409 0.1648 0.1376 -0.0525 -0.0149 -0.0017 201 TRP   A CH2 
1683 N N   . SER   A 201 ? 0.1856 0.0943 0.1351 0.0017  -0.0201 0.0028  202 SER   A N   
1684 C CA  . SER   A 201 ? 0.1859 0.1025 0.1346 0.0041  -0.0140 0.0180  202 SER   A CA  
1685 C C   . SER   A 201 ? 0.1868 0.1145 0.1099 -0.0024 -0.0083 -0.0086 202 SER   A C   
1686 O O   . SER   A 201 ? 0.1992 0.1517 0.0979 -0.0015 -0.0009 0.0008  202 SER   A O   
1687 C CB  . SER   A 201 ? 0.2295 0.1047 0.1568 -0.0183 0.0039  0.0417  202 SER   A CB  
1688 O OG  . SER   A 201 ? 0.2458 0.1315 0.1561 0.0155  0.0130  0.0139  202 SER   A OG  
1689 N N   . ILE   A 202 ? 0.1948 0.1037 0.1130 -0.0163 -0.0191 0.0080  203 ILE   A N   
1690 C CA  . ILE   A 202 ? 0.2041 0.1131 0.1247 -0.0138 -0.0123 -0.0076 203 ILE   A CA  
1691 C C   . ILE   A 202 ? 0.2048 0.1161 0.1307 0.0028  -0.0169 -0.0088 203 ILE   A C   
1692 O O   . ILE   A 202 ? 0.2241 0.1310 0.1365 -0.0199 0.0017  0.0036  203 ILE   A O   
1693 C CB  . ILE   A 202 ? 0.2400 0.1174 0.1265 -0.0260 -0.0135 -0.0195 203 ILE   A CB  
1694 C CG1 . ILE   A 202 ? 0.2266 0.1512 0.1159 0.0004  -0.0202 -0.0074 203 ILE   A CG1 
1695 C CG2 . ILE   A 202 ? 0.2679 0.1264 0.1392 -0.0501 -0.0080 -0.0140 203 ILE   A CG2 
1696 C CD1 . ILE   A 202 ? 0.2501 0.2071 0.1350 -0.0028 -0.0058 -0.0128 203 ILE   A CD1 
1697 N N   . GLY   A 203 ? 0.2056 0.1106 0.1215 0.0098  -0.0303 -0.0001 204 GLY   A N   
1698 C CA  . GLY   A 203 ? 0.2249 0.1246 0.1087 0.0159  -0.0131 0.0046  204 GLY   A CA  
1699 C C   . GLY   A 203 ? 0.1914 0.1305 0.1079 -0.0072 -0.0096 0.0037  204 GLY   A C   
1700 O O   . GLY   A 203 ? 0.1961 0.1336 0.1232 -0.0037 -0.0037 0.0098  204 GLY   A O   
1701 N N   . VAL   A 204 ? 0.1899 0.1161 0.1130 0.0039  -0.0055 -0.0067 205 VAL   A N   
1702 C CA  . VAL   A 204 ? 0.1896 0.1253 0.1146 0.0050  0.0061  0.0134  205 VAL   A CA  
1703 C C   . VAL   A 204 ? 0.1841 0.1144 0.1125 0.0051  0.0114  0.0136  205 VAL   A C   
1704 O O   . VAL   A 204 ? 0.2185 0.1276 0.1195 -0.0024 0.0192  0.0088  205 VAL   A O   
1705 C CB  . VAL   A 204 ? 0.1802 0.1107 0.1289 -0.0071 0.0102  0.0059  205 VAL   A CB  
1706 C CG1 . VAL   A 204 ? 0.2437 0.1177 0.1145 0.0085  0.0115  0.0051  205 VAL   A CG1 
1707 C CG2 . VAL   A 204 ? 0.1991 0.1417 0.1490 -0.0027 0.0075  0.0112  205 VAL   A CG2 
1708 N N   . ILE   A 205 ? 0.1938 0.1205 0.1134 0.0042  -0.0154 0.0166  206 ILE   A N   
1709 C CA  . ILE   A 205 ? 0.2049 0.1417 0.1091 -0.0074 -0.0121 0.0158  206 ILE   A CA  
1710 C C   . ILE   A 205 ? 0.1957 0.1317 0.1278 -0.0062 -0.0070 0.0151  206 ILE   A C   
1711 O O   . ILE   A 205 ? 0.2004 0.1547 0.1298 -0.0058 0.0089  0.0210  206 ILE   A O   
1712 C CB  . ILE   A 205 ? 0.1921 0.1473 0.1342 -0.0074 -0.0125 0.0217  206 ILE   A CB  
1713 C CG1 . ILE   A 205 ? 0.2350 0.1627 0.1250 0.0338  -0.0031 0.0299  206 ILE   A CG1 
1714 C CG2 . ILE   A 205 ? 0.1960 0.1966 0.1545 -0.0315 -0.0124 0.0169  206 ILE   A CG2 
1715 C CD1 . ILE   A 205 ? 0.2765 0.2125 0.1374 0.0345  -0.0029 0.0267  206 ILE   A CD1 
1716 N N   . THR   A 206 ? 0.2005 0.1216 0.1157 -0.0118 -0.0223 0.0324  207 THR   A N   
1717 C CA  . THR   A 206 ? 0.2317 0.1200 0.1269 0.0042  -0.0131 0.0169  207 THR   A CA  
1718 C C   . THR   A 206 ? 0.2079 0.1366 0.1173 0.0054  -0.0033 0.0334  207 THR   A C   
1719 O O   . THR   A 206 ? 0.2216 0.1364 0.1374 -0.0018 0.0032  0.0435  207 THR   A O   
1720 C CB  . THR   A 206 ? 0.2293 0.1221 0.1390 0.0044  0.0033  0.0204  207 THR   A CB  
1721 O OG1 . THR   A 206 ? 0.2364 0.1417 0.1472 -0.0026 -0.0064 0.0017  207 THR   A OG1 
1722 C CG2 . THR   A 206 ? 0.2587 0.1076 0.1804 -0.0091 0.0041  0.0445  207 THR   A CG2 
1723 N N   . TYR   A 207 ? 0.1929 0.1306 0.1258 -0.0030 -0.0271 0.0211  208 TYR   A N   
1724 C CA  . TYR   A 207 ? 0.2013 0.1332 0.1363 0.0088  -0.0108 0.0173  208 TYR   A CA  
1725 C C   . TYR   A 207 ? 0.2064 0.1398 0.1289 0.0021  0.0130  0.0068  208 TYR   A C   
1726 O O   . TYR   A 207 ? 0.2167 0.1759 0.1297 -0.0056 0.0150  0.0030  208 TYR   A O   
1727 C CB  . TYR   A 207 ? 0.2083 0.1314 0.1245 -0.0441 -0.0306 0.0067  208 TYR   A CB  
1728 C CG  . TYR   A 207 ? 0.2279 0.1354 0.1348 -0.0252 -0.0237 0.0196  208 TYR   A CG  
1729 C CD1 . TYR   A 207 ? 0.2570 0.1440 0.1410 -0.0295 0.0225  0.0142  208 TYR   A CD1 
1730 C CD2 . TYR   A 207 ? 0.2259 0.1586 0.1189 -0.0171 -0.0141 0.0306  208 TYR   A CD2 
1731 C CE1 . TYR   A 207 ? 0.2522 0.1878 0.1448 -0.0157 0.0111  0.0056  208 TYR   A CE1 
1732 C CE2 . TYR   A 207 ? 0.2473 0.1795 0.1276 -0.0234 -0.0067 0.0224  208 TYR   A CE2 
1733 C CZ  . TYR   A 207 ? 0.2695 0.1909 0.1311 -0.0176 -0.0057 -0.0073 208 TYR   A CZ  
1734 O OH  . TYR   A 207 ? 0.3102 0.2345 0.1506 -0.0446 -0.0009 -0.0290 208 TYR   A OH  
1735 N N   . ILE   A 208 ? 0.2078 0.1154 0.1465 0.0372  0.0123  0.0059  209 ILE   A N   
1736 C CA  . ILE   A 208 ? 0.2226 0.1291 0.1448 -0.0001 0.0244  0.0165  209 ILE   A CA  
1737 C C   . ILE   A 208 ? 0.2439 0.1743 0.1388 0.0058  -0.0029 0.0279  209 ILE   A C   
1738 O O   . ILE   A 208 ? 0.2385 0.2043 0.1438 0.0038  0.0159  0.0277  209 ILE   A O   
1739 C CB  . ILE   A 208 ? 0.2220 0.1339 0.1926 0.0092  0.0466  0.0173  209 ILE   A CB  
1740 C CG1 . ILE   A 208 ? 0.2774 0.1404 0.1748 -0.0214 0.0094  0.0198  209 ILE   A CG1 
1741 C CG2 . ILE   A 208 ? 0.2656 0.2047 0.2356 0.0371  0.0581  0.0273  209 ILE   A CG2 
1742 C CD1 . ILE   A 208 ? 0.2884 0.1568 0.1993 0.0101  0.0219  0.0434  209 ILE   A CD1 
1743 N N   . LEU   A 209 ? 0.2091 0.1760 0.1478 -0.0093 -0.0149 0.0366  210 LEU   A N   
1744 C CA  . LEU   A 209 ? 0.2098 0.1962 0.1703 -0.0354 -0.0131 0.0538  210 LEU   A CA  
1745 C C   . LEU   A 209 ? 0.2060 0.2148 0.1844 -0.0286 -0.0152 0.0635  210 LEU   A C   
1746 O O   . LEU   A 209 ? 0.2080 0.2576 0.2002 -0.0022 0.0053  0.0808  210 LEU   A O   
1747 C CB  . LEU   A 209 ? 0.2311 0.2503 0.1788 -0.0557 -0.0300 0.0447  210 LEU   A CB  
1748 C CG  . LEU   A 209 ? 0.2487 0.2856 0.1868 -0.0501 -0.0271 0.0601  210 LEU   A CG  
1749 C CD1 . LEU   A 209 ? 0.3424 0.2972 0.2101 -0.0831 -0.0245 0.0209  210 LEU   A CD1 
1750 C CD2 . LEU   A 209 ? 0.3070 0.3502 0.1941 -0.0104 -0.0359 0.1063  210 LEU   A CD2 
1751 N N   . LEU   A 210 ? 0.2182 0.1745 0.1701 -0.0074 -0.0005 0.0599  211 LEU   A N   
1752 C CA  . LEU   A 210 ? 0.2396 0.1670 0.1719 0.0268  -0.0077 0.0491  211 LEU   A CA  
1753 C C   . LEU   A 210 ? 0.2786 0.1876 0.1699 -0.0012 0.0075  0.0501  211 LEU   A C   
1754 O O   . LEU   A 210 ? 0.2975 0.2122 0.1827 -0.0251 0.0084  0.0567  211 LEU   A O   
1755 C CB  . LEU   A 210 ? 0.2509 0.1550 0.2004 -0.0026 -0.0042 0.0195  211 LEU   A CB  
1756 C CG  . LEU   A 210 ? 0.2645 0.1556 0.2014 -0.0052 -0.0058 0.0385  211 LEU   A CG  
1757 C CD1 . LEU   A 210 ? 0.2943 0.1786 0.2157 0.0258  0.0095  0.0277  211 LEU   A CD1 
1758 C CD2 . LEU   A 210 ? 0.2984 0.1889 0.2218 -0.0405 -0.0185 0.0358  211 LEU   A CD2 
1759 N N   . SER   A 211 ? 0.3062 0.1767 0.1719 -0.0234 0.0217  0.0371  212 SER   A N   
1760 C CA  . SER   A 211 ? 0.3047 0.2261 0.1586 -0.0252 0.0068  0.0233  212 SER   A CA  
1761 C C   . SER   A 211 ? 0.2857 0.2280 0.1492 -0.0297 0.0248  0.0202  212 SER   A C   
1762 O O   . SER   A 211 ? 0.3322 0.2366 0.1585 -0.0205 0.0480  0.0128  212 SER   A O   
1763 C CB  . SER   A 211 ? 0.2976 0.2255 0.1529 -0.0352 0.0095  0.0273  212 SER   A CB  
1764 O OG  . SER   A 211 ? 0.2600 0.2154 0.1578 -0.0168 0.0255  0.0204  212 SER   A OG  
1765 N N   . GLY   A 212 ? 0.2299 0.2133 0.1740 -0.0193 0.0235  0.0294  213 GLY   A N   
1766 C CA  . GLY   A 212 ? 0.2494 0.2349 0.2206 -0.0245 0.0154  0.0034  213 GLY   A CA  
1767 C C   . GLY   A 212 ? 0.2555 0.2200 0.2177 -0.0181 0.0120  -0.0267 213 GLY   A C   
1768 O O   . GLY   A 212 ? 0.3077 0.2514 0.2854 0.0079  0.0030  -0.0375 213 GLY   A O   
1769 N N   . ALA   A 213 ? 0.2511 0.2008 0.1870 -0.0263 0.0281  -0.0191 214 ALA   A N   
1770 C CA  . ALA   A 213 ? 0.2780 0.2225 0.1511 -0.0414 0.0254  -0.0026 214 ALA   A CA  
1771 C C   . ALA   A 213 ? 0.2755 0.1969 0.1529 -0.0289 0.0287  0.0065  214 ALA   A C   
1772 O O   . ALA   A 213 ? 0.3012 0.1851 0.1659 0.0006  0.0297  -0.0078 214 ALA   A O   
1773 C CB  . ALA   A 213 ? 0.3124 0.2682 0.1612 -0.0385 0.0064  0.0156  214 ALA   A CB  
1774 N N   . SER   A 214 ? 0.2672 0.2157 0.1730 -0.0569 0.0405  -0.0103 215 SER   A N   
1775 C CA  . SER   A 214 ? 0.2523 0.2332 0.1587 -0.0416 0.0449  0.0050  215 SER   A CA  
1776 C C   . SER   A 214 ? 0.2643 0.2531 0.1472 -0.0471 0.0312  -0.0136 215 SER   A C   
1777 O O   . SER   A 214 ? 0.2804 0.3002 0.1905 -0.0519 0.0105  -0.0728 215 SER   A O   
1778 C CB  . SER   A 214 ? 0.2690 0.2723 0.1839 -0.0190 0.0575  0.0190  215 SER   A CB  
1779 O OG  . SER   A 214 ? 0.2699 0.2989 0.2114 -0.0237 0.0539  0.0265  215 SER   A OG  
1780 N N   . PRO   A 215 ? 0.2515 0.1995 0.1341 -0.0328 0.0194  0.0043  216 PRO   A N   
1781 C CA  . PRO   A 215 ? 0.2592 0.1809 0.1408 -0.0385 0.0106  -0.0146 216 PRO   A CA  
1782 C C   . PRO   A 215 ? 0.2339 0.1510 0.1197 -0.0304 0.0153  -0.0148 216 PRO   A C   
1783 O O   . PRO   A 215 ? 0.2764 0.1678 0.1187 -0.0300 -0.0085 -0.0076 216 PRO   A O   
1784 C CB  . PRO   A 215 ? 0.2943 0.1519 0.1390 -0.0371 -0.0151 -0.0108 216 PRO   A CB  
1785 C CG  . PRO   A 215 ? 0.2834 0.1715 0.1468 -0.0332 0.0077  -0.0329 216 PRO   A CG  
1786 C CD  . PRO   A 215 ? 0.2552 0.1930 0.1197 -0.0504 0.0208  -0.0253 216 PRO   A CD  
1787 N N   . PHE   A 216 ? 0.2442 0.1284 0.1408 -0.0252 0.0275  0.0016  217 PHE   A N   
1788 C CA  . PHE   A 216 ? 0.2469 0.1322 0.1195 -0.0258 0.0216  -0.0138 217 PHE   A CA  
1789 C C   . PHE   A 216 ? 0.2487 0.1171 0.1362 -0.0126 0.0280  -0.0136 217 PHE   A C   
1790 O O   . PHE   A 216 ? 0.2412 0.1391 0.1618 -0.0355 0.0119  -0.0247 217 PHE   A O   
1791 C CB  . PHE   A 216 ? 0.2683 0.1504 0.1364 -0.0170 0.0388  -0.0276 217 PHE   A CB  
1792 C CG  . PHE   A 216 ? 0.2362 0.1272 0.1267 0.0015  0.0245  -0.0134 217 PHE   A CG  
1793 C CD1 . PHE   A 216 ? 0.2512 0.1557 0.1356 -0.0082 0.0139  -0.0170 217 PHE   A CD1 
1794 C CD2 . PHE   A 216 ? 0.2602 0.1403 0.1329 -0.0279 0.0356  -0.0228 217 PHE   A CD2 
1795 C CE1 . PHE   A 216 ? 0.2748 0.1565 0.1360 -0.0265 0.0049  -0.0150 217 PHE   A CE1 
1796 C CE2 . PHE   A 216 ? 0.2389 0.1717 0.1334 -0.0214 0.0192  -0.0118 217 PHE   A CE2 
1797 C CZ  . PHE   A 216 ? 0.2400 0.1647 0.1275 -0.0246 0.0105  -0.0046 217 PHE   A CZ  
1798 N N   . LEU   A 217 ? 0.2407 0.1560 0.1560 0.0164  0.0331  -0.0021 218 LEU   A N   
1799 C CA  . LEU   A 217 ? 0.2480 0.1491 0.2051 0.0149  0.0334  -0.0047 218 LEU   A CA  
1800 C C   . LEU   A 217 ? 0.2975 0.1480 0.1737 0.0122  0.0506  0.0080  218 LEU   A C   
1801 O O   . LEU   A 217 ? 0.3820 0.1640 0.1628 0.0336  0.0558  0.0113  218 LEU   A O   
1802 C CB  . LEU   A 217 ? 0.2207 0.1650 0.2863 0.0176  0.0668  0.0109  218 LEU   A CB  
1803 C CG  . LEU   A 217 ? 0.2324 0.1958 0.3605 0.0104  0.0754  0.0452  218 LEU   A CG  
1804 C CD1 . LEU   A 217 ? 0.2658 0.2253 0.3900 0.0078  0.0452  0.0553  218 LEU   A CD1 
1805 C CD2 . LEU   A 217 ? 0.2622 0.2321 0.4071 -0.0071 0.0669  0.0324  218 LEU   A CD2 
1806 N N   . GLY   A 218 ? 0.2927 0.1459 0.1779 0.0186  0.0318  -0.0303 219 GLY   A N   
1807 C CA  . GLY   A 218 ? 0.3673 0.1552 0.1950 0.0021  0.0228  -0.0670 219 GLY   A CA  
1808 C C   . GLY   A 218 ? 0.3950 0.1784 0.2079 -0.0105 0.0655  -0.0579 219 GLY   A C   
1809 O O   . GLY   A 218 ? 0.3874 0.2012 0.2530 -0.0079 0.0660  -0.0469 219 GLY   A O   
1810 N N   . ASP   A 219 ? 0.4534 0.2019 0.2170 0.0183  0.0949  -0.0524 220 ASP   A N   
1811 C CA  . ASP   A 219 ? 0.4928 0.2405 0.2305 0.0301  0.1012  -0.0683 220 ASP   A CA  
1812 C C   . ASP   A 219 ? 0.4247 0.1962 0.2556 0.0130  0.0955  -0.0416 220 ASP   A C   
1813 O O   . ASP   A 219 ? 0.4344 0.2106 0.3059 0.0220  0.1219  -0.0367 220 ASP   A O   
1814 C CB  . ASP   A 219 ? 0.6266 0.3618 0.2538 0.0181  0.0950  -0.0733 220 ASP   A CB  
1815 C CG  . ASP   A 219 ? 0.7399 0.5136 0.3084 -0.0116 0.0755  -0.0481 220 ASP   A CG  
1816 O OD1 . ASP   A 219 ? 0.7834 0.5972 0.3086 -0.0209 0.0920  -0.0421 220 ASP   A OD1 
1817 O OD2 . ASP   A 219 ? 0.7991 0.5802 0.3770 -0.0316 0.0500  -0.0330 220 ASP   A OD2 
1818 N N   . THR   A 220 ? 0.3338 0.1771 0.2192 -0.0237 0.0754  -0.0325 221 THR   A N   
1819 C CA  . THR   A 220 ? 0.3051 0.1456 0.2210 -0.0438 0.0665  -0.0275 221 THR   A CA  
1820 C C   . THR   A 220 ? 0.2811 0.1457 0.2118 -0.0272 0.0428  -0.0130 221 THR   A C   
1821 O O   . THR   A 220 ? 0.2840 0.1374 0.2102 -0.0123 0.0300  -0.0058 221 THR   A O   
1822 C CB  . THR   A 220 ? 0.2785 0.1593 0.2484 -0.0059 0.0372  -0.0347 221 THR   A CB  
1823 O OG1 . THR   A 220 ? 0.2978 0.1713 0.2527 -0.0335 0.0292  -0.0471 221 THR   A OG1 
1824 C CG2 . THR   A 220 ? 0.3674 0.1932 0.2691 -0.0159 0.0518  -0.0604 221 THR   A CG2 
1825 N N   . LYS   A 221 ? 0.3001 0.1689 0.2004 -0.0313 0.0276  -0.0079 222 LYS   A N   
1826 C CA  . LYS   A 221 ? 0.2812 0.1695 0.1927 -0.0123 -0.0022 0.0021  222 LYS   A CA  
1827 C C   . LYS   A 221 ? 0.2760 0.1631 0.1810 -0.0262 0.0275  -0.0104 222 LYS   A C   
1828 O O   . LYS   A 221 ? 0.2757 0.1673 0.1668 -0.0125 0.0257  -0.0104 222 LYS   A O   
1829 C CB  . LYS   A 221 ? 0.3270 0.2419 0.2358 0.0121  -0.0185 0.0387  222 LYS   A CB  
1830 C CG  . LYS   A 221 ? 0.3899 0.3076 0.2807 0.0423  -0.0278 0.0361  222 LYS   A CG  
1831 C CD  . LYS   A 221 ? 0.4434 0.3674 0.3102 0.0532  -0.0468 0.0459  222 LYS   A CD  
1832 C CE  . LYS   A 221 ? 0.5079 0.4295 0.3509 0.0497  -0.0536 0.0592  222 LYS   A CE  
1833 N NZ  . LYS   A 221 ? 0.5565 0.4678 0.3779 0.0577  -0.0433 0.0519  222 LYS   A NZ  
1834 N N   . GLN   A 222 ? 0.2809 0.1621 0.1844 -0.0501 0.0192  -0.0020 223 GLN   A N   
1835 C CA  . GLN   A 222 ? 0.2644 0.1756 0.2089 -0.0192 0.0073  -0.0071 223 GLN   A CA  
1836 C C   . GLN   A 222 ? 0.2657 0.1664 0.2086 -0.0306 0.0233  -0.0227 223 GLN   A C   
1837 O O   . GLN   A 222 ? 0.2658 0.1695 0.2259 -0.0500 0.0183  -0.0151 223 GLN   A O   
1838 C CB  . GLN   A 222 ? 0.3077 0.2062 0.2243 -0.0444 -0.0080 -0.0194 223 GLN   A CB  
1839 C CG  . GLN   A 222 ? 0.2935 0.2129 0.2499 -0.0114 -0.0153 -0.0453 223 GLN   A CG  
1840 C CD  . GLN   A 222 ? 0.3081 0.2090 0.2451 -0.0292 -0.0228 -0.0291 223 GLN   A CD  
1841 O OE1 . GLN   A 222 ? 0.3291 0.1878 0.2388 -0.0424 -0.0138 -0.0078 223 GLN   A OE1 
1842 N NE2 . GLN   A 222 ? 0.2922 0.2248 0.2492 -0.0306 -0.0132 -0.0319 223 GLN   A NE2 
1843 N N   . GLU   A 223 ? 0.2793 0.1494 0.1933 -0.0560 0.0165  -0.0197 224 GLU   A N   
1844 C CA  A GLU   A 223 ? 0.2703 0.1621 0.1915 -0.0352 0.0203  -0.0278 224 GLU   A CA  
1845 C CA  B GLU   A 223 ? 0.2483 0.1715 0.1815 -0.0351 0.0249  -0.0437 224 GLU   A CA  
1846 C C   . GLU   A 223 ? 0.2596 0.1633 0.1745 -0.0257 0.0123  -0.0390 224 GLU   A C   
1847 O O   . GLU   A 223 ? 0.2644 0.1605 0.1652 -0.0180 -0.0049 -0.0334 224 GLU   A O   
1848 C CB  A GLU   A 223 ? 0.3404 0.1989 0.2132 -0.0624 0.0099  -0.0343 224 GLU   A CB  
1849 C CB  B GLU   A 223 ? 0.2751 0.2265 0.1819 -0.0586 0.0224  -0.0778 224 GLU   A CB  
1850 C CG  A GLU   A 223 ? 0.4453 0.2249 0.2632 -0.0678 -0.0005 -0.0248 224 GLU   A CG  
1851 C CG  B GLU   A 223 ? 0.3352 0.2743 0.2172 -0.0590 0.0083  -0.0706 224 GLU   A CG  
1852 C CD  A GLU   A 223 ? 0.5033 0.2326 0.2826 -0.1309 -0.0232 -0.0469 224 GLU   A CD  
1853 C CD  B GLU   A 223 ? 0.4315 0.3470 0.2519 -0.0673 -0.0104 -0.0526 224 GLU   A CD  
1854 O OE1 A GLU   A 223 ? 0.4876 0.2304 0.2950 -0.1689 0.0184  -0.0328 224 GLU   A OE1 
1855 O OE1 B GLU   A 223 ? 0.4768 0.3865 0.2642 -0.0625 -0.0266 -0.0477 224 GLU   A OE1 
1856 O OE2 A GLU   A 223 ? 0.5664 0.2454 0.2968 -0.1395 -0.0572 -0.0550 224 GLU   A OE2 
1857 O OE2 B GLU   A 223 ? 0.5067 0.3585 0.2860 -0.0590 0.0189  -0.0530 224 GLU   A OE2 
1858 N N   . THR   A 224 ? 0.2329 0.1451 0.1646 -0.0408 0.0169  -0.0314 225 THR   A N   
1859 C CA  . THR   A 224 ? 0.2273 0.1509 0.1529 -0.0294 0.0225  -0.0198 225 THR   A CA  
1860 C C   . THR   A 224 ? 0.2145 0.1534 0.1567 -0.0192 0.0104  -0.0189 225 THR   A C   
1861 O O   . THR   A 224 ? 0.2493 0.1548 0.1438 -0.0172 -0.0071 -0.0311 225 THR   A O   
1862 C CB  . THR   A 224 ? 0.2114 0.1467 0.1682 -0.0150 0.0327  -0.0333 225 THR   A CB  
1863 O OG1 . THR   A 224 ? 0.2510 0.1601 0.1576 -0.0066 0.0259  -0.0096 225 THR   A OG1 
1864 C CG2 . THR   A 224 ? 0.2492 0.1620 0.1778 -0.0190 0.0102  -0.0329 225 THR   A CG2 
1865 N N   . LEU   A 225 ? 0.2459 0.1505 0.1315 -0.0467 0.0255  -0.0162 226 LEU   A N   
1866 C CA  . LEU   A 225 ? 0.2336 0.1668 0.1467 -0.0365 0.0349  -0.0133 226 LEU   A CA  
1867 C C   . LEU   A 225 ? 0.2217 0.1764 0.1578 -0.0577 0.0164  -0.0403 226 LEU   A C   
1868 O O   . LEU   A 225 ? 0.2476 0.1667 0.1707 -0.0249 0.0331  -0.0205 226 LEU   A O   
1869 C CB  . LEU   A 225 ? 0.2628 0.1598 0.1629 -0.0425 0.0277  0.0015  226 LEU   A CB  
1870 C CG  . LEU   A 225 ? 0.2650 0.1793 0.1564 -0.0357 0.0204  -0.0110 226 LEU   A CG  
1871 C CD1 . LEU   A 225 ? 0.2946 0.1956 0.1833 -0.0215 0.0214  0.0105  226 LEU   A CD1 
1872 C CD2 . LEU   A 225 ? 0.3009 0.2062 0.1741 -0.0194 -0.0025 -0.0313 226 LEU   A CD2 
1873 N N   . ALA   A 226 ? 0.2214 0.1806 0.1689 -0.0577 0.0086  -0.0206 227 ALA   A N   
1874 C CA  . ALA   A 226 ? 0.2234 0.1937 0.1952 -0.0623 -0.0030 -0.0449 227 ALA   A CA  
1875 C C   . ALA   A 226 ? 0.2375 0.1790 0.1677 -0.0376 -0.0065 -0.0516 227 ALA   A C   
1876 O O   . ALA   A 226 ? 0.2316 0.2216 0.1991 -0.0086 -0.0076 -0.0589 227 ALA   A O   
1877 C CB  . ALA   A 226 ? 0.2513 0.2243 0.2311 -0.0339 -0.0095 -0.0616 227 ALA   A CB  
1878 N N   . ASN   A 227 ? 0.2295 0.1767 0.1350 -0.0442 0.0108  -0.0343 228 ASN   A N   
1879 C CA  . ASN   A 227 ? 0.2440 0.1704 0.1312 -0.0092 0.0050  -0.0288 228 ASN   A CA  
1880 C C   . ASN   A 227 ? 0.2425 0.1517 0.1466 -0.0135 -0.0034 -0.0401 228 ASN   A C   
1881 O O   . ASN   A 227 ? 0.2471 0.1739 0.1438 -0.0105 -0.0094 -0.0487 228 ASN   A O   
1882 C CB  . ASN   A 227 ? 0.2177 0.1728 0.1424 -0.0229 0.0219  -0.0501 228 ASN   A CB  
1883 C CG  . ASN   A 227 ? 0.2358 0.1981 0.1566 -0.0241 0.0052  -0.0730 228 ASN   A CG  
1884 O OD1 . ASN   A 227 ? 0.2550 0.2607 0.1784 0.0070  -0.0306 -0.0832 228 ASN   A OD1 
1885 N ND2 . ASN   A 227 ? 0.2602 0.2008 0.1672 -0.0264 0.0402  -0.0800 228 ASN   A ND2 
1886 N N   . VAL   A 228 ? 0.2316 0.1452 0.1277 -0.0270 0.0032  -0.0241 229 VAL   A N   
1887 C CA  . VAL   A 228 ? 0.2195 0.1507 0.1380 -0.0175 -0.0012 -0.0344 229 VAL   A CA  
1888 C C   . VAL   A 228 ? 0.2285 0.1639 0.1455 -0.0176 0.0108  -0.0291 229 VAL   A C   
1889 O O   . VAL   A 228 ? 0.2493 0.1807 0.1400 -0.0027 0.0007  -0.0252 229 VAL   A O   
1890 C CB  . VAL   A 228 ? 0.2280 0.1559 0.1306 -0.0089 -0.0069 -0.0184 229 VAL   A CB  
1891 C CG1 . VAL   A 228 ? 0.2615 0.1587 0.1225 -0.0332 -0.0115 -0.0392 229 VAL   A CG1 
1892 C CG2 . VAL   A 228 ? 0.2026 0.1768 0.1352 -0.0109 -0.0043 -0.0101 229 VAL   A CG2 
1893 N N   . SER   A 229 ? 0.2006 0.1767 0.1576 -0.0446 0.0122  -0.0431 230 SER   A N   
1894 C CA  . SER   A 229 ? 0.2304 0.1899 0.1747 -0.0392 0.0082  -0.0351 230 SER   A CA  
1895 C C   . SER   A 229 ? 0.2370 0.1910 0.1861 -0.0089 0.0258  -0.0516 230 SER   A C   
1896 O O   . SER   A 229 ? 0.2556 0.2061 0.2111 -0.0038 0.0374  -0.0621 230 SER   A O   
1897 C CB  . SER   A 229 ? 0.2223 0.2165 0.1995 -0.0429 0.0396  -0.0268 230 SER   A CB  
1898 O OG  . SER   A 229 ? 0.2348 0.2846 0.1762 -0.0346 0.0179  -0.0069 230 SER   A OG  
1899 N N   . ALA   A 230 ? 0.2293 0.2120 0.1700 -0.0285 -0.0152 -0.0494 231 ALA   A N   
1900 C CA  . ALA   A 230 ? 0.2545 0.2227 0.1787 -0.0045 -0.0249 -0.0445 231 ALA   A CA  
1901 C C   . ALA   A 230 ? 0.2428 0.2248 0.2000 0.0272  -0.0211 -0.0234 231 ALA   A C   
1902 O O   . ALA   A 230 ? 0.2806 0.2694 0.2263 0.0047  -0.0451 -0.0174 231 ALA   A O   
1903 C CB  . ALA   A 230 ? 0.3246 0.2463 0.1801 -0.0275 -0.0523 -0.0736 231 ALA   A CB  
1904 N N   . VAL   A 231 ? 0.2123 0.2189 0.1769 -0.0106 -0.0137 -0.0474 232 VAL   A N   
1905 C CA  . VAL   A 231 ? 0.2623 0.1946 0.1716 -0.0042 -0.0001 -0.0444 232 VAL   A CA  
1906 C C   . VAL   A 231 ? 0.2867 0.2017 0.1565 0.0115  -0.0114 -0.0130 232 VAL   A C   
1907 O O   . VAL   A 231 ? 0.2939 0.2280 0.1655 0.0452  -0.0063 -0.0327 232 VAL   A O   
1908 C CB  . VAL   A 231 ? 0.2914 0.2041 0.1869 0.0007  0.0110  -0.0614 232 VAL   A CB  
1909 C CG1 . VAL   A 231 ? 0.3143 0.1820 0.2103 -0.0121 0.0187  -0.0447 232 VAL   A CG1 
1910 C CG2 . VAL   A 231 ? 0.2846 0.2348 0.1983 -0.0024 0.0453  -0.0619 232 VAL   A CG2 
1911 N N   . ASN   A 232 ? 0.2601 0.2058 0.1407 0.0088  -0.0030 -0.0149 233 ASN   A N   
1912 C CA  . ASN   A 232 ? 0.2719 0.2021 0.1461 -0.0170 0.0074  -0.0258 233 ASN   A CA  
1913 C C   . ASN   A 232 ? 0.2687 0.1885 0.1480 -0.0301 -0.0191 -0.0295 233 ASN   A C   
1914 O O   . ASN   A 232 ? 0.2907 0.2019 0.1598 0.0070  -0.0373 -0.0381 233 ASN   A O   
1915 C CB  . ASN   A 232 ? 0.3169 0.2019 0.1420 -0.0185 -0.0010 -0.0323 233 ASN   A CB  
1916 C CG  . ASN   A 232 ? 0.2894 0.2486 0.1494 -0.0260 -0.0044 -0.0404 233 ASN   A CG  
1917 O OD1 . ASN   A 232 ? 0.3455 0.3223 0.1410 -0.0252 -0.0251 -0.0218 233 ASN   A OD1 
1918 N ND2 . ASN   A 232 ? 0.2868 0.2548 0.1589 -0.0081 -0.0051 -0.0112 233 ASN   A ND2 
1919 N N   . TYR   A 233 ? 0.2418 0.1727 0.1609 -0.0081 0.0009  -0.0232 234 TYR   A N   
1920 C CA  . TYR   A 233 ? 0.2545 0.1819 0.1672 -0.0072 -0.0006 -0.0239 234 TYR   A CA  
1921 C C   . TYR   A 233 ? 0.2842 0.1775 0.1838 -0.0040 -0.0133 -0.0159 234 TYR   A C   
1922 O O   . TYR   A 233 ? 0.2835 0.2001 0.1855 0.0041  -0.0325 -0.0178 234 TYR   A O   
1923 C CB  . TYR   A 233 ? 0.2738 0.1757 0.1631 -0.0294 0.0086  -0.0351 234 TYR   A CB  
1924 C CG  . TYR   A 233 ? 0.2693 0.1744 0.1387 -0.0306 0.0051  -0.0175 234 TYR   A CG  
1925 C CD1 . TYR   A 233 ? 0.2850 0.1716 0.1229 -0.0024 -0.0320 -0.0242 234 TYR   A CD1 
1926 C CD2 . TYR   A 233 ? 0.2915 0.1894 0.1513 -0.0352 -0.0114 -0.0233 234 TYR   A CD2 
1927 C CE1 . TYR   A 233 ? 0.2919 0.1842 0.1361 -0.0248 -0.0313 -0.0140 234 TYR   A CE1 
1928 C CE2 . TYR   A 233 ? 0.3288 0.2004 0.1502 -0.0277 -0.0090 -0.0235 234 TYR   A CE2 
1929 C CZ  . TYR   A 233 ? 0.3011 0.1561 0.1456 -0.0344 -0.0189 -0.0179 234 TYR   A CZ  
1930 O OH  . TYR   A 233 ? 0.3888 0.1801 0.1956 -0.0545 -0.0045 -0.0157 234 TYR   A OH  
1931 N N   . GLU   A 234 ? 0.2889 0.1620 0.1621 -0.0372 -0.0097 -0.0179 235 GLU   A N   
1932 C CA  . GLU   A 234 ? 0.3242 0.2278 0.1643 -0.0462 -0.0485 0.0172  235 GLU   A CA  
1933 C C   . GLU   A 234 ? 0.2678 0.2016 0.1580 -0.0295 -0.0092 0.0236  235 GLU   A C   
1934 O O   . GLU   A 234 ? 0.3025 0.1902 0.1629 -0.0044 -0.0334 -0.0001 235 GLU   A O   
1935 C CB  . GLU   A 234 ? 0.3858 0.3639 0.2081 -0.0863 -0.0413 0.0501  235 GLU   A CB  
1936 C CG  . GLU   A 234 ? 0.4456 0.4795 0.2217 -0.0484 0.0114  0.0220  235 GLU   A CG  
1937 C CD  . GLU   A 234 ? 0.5268 0.5754 0.2150 -0.0453 0.0489  -0.0049 235 GLU   A CD  
1938 O OE1 . GLU   A 234 ? 0.5631 0.6271 0.2855 -0.0466 0.0170  -0.0299 235 GLU   A OE1 
1939 O OE2 . GLU   A 234 ? 0.5423 0.6466 0.1973 -0.0264 0.1092  -0.0265 235 GLU   A OE2 
1940 N N   . PHE   A 235 ? 0.2775 0.2045 0.1493 -0.0356 -0.0250 -0.0009 236 PHE   A N   
1941 C CA  . PHE   A 235 ? 0.2589 0.2048 0.1556 -0.0080 -0.0154 0.0064  236 PHE   A CA  
1942 C C   . PHE   A 235 ? 0.3128 0.2327 0.1596 0.0012  -0.0126 0.0191  236 PHE   A C   
1943 O O   . PHE   A 235 ? 0.3731 0.2530 0.1725 0.0276  -0.0140 0.0326  236 PHE   A O   
1944 C CB  . PHE   A 235 ? 0.2735 0.2032 0.1583 0.0120  -0.0235 -0.0008 236 PHE   A CB  
1945 C CG  . PHE   A 235 ? 0.2847 0.1558 0.1476 0.0153  -0.0159 0.0133  236 PHE   A CG  
1946 C CD1 . PHE   A 235 ? 0.2908 0.1461 0.1727 -0.0067 -0.0295 0.0134  236 PHE   A CD1 
1947 C CD2 . PHE   A 235 ? 0.3156 0.1903 0.1641 0.0211  -0.0027 -0.0206 236 PHE   A CD2 
1948 C CE1 . PHE   A 235 ? 0.2932 0.1621 0.1712 0.0059  -0.0062 0.0061  236 PHE   A CE1 
1949 C CE2 . PHE   A 235 ? 0.3370 0.1934 0.1715 0.0440  -0.0360 -0.0155 236 PHE   A CE2 
1950 C CZ  . PHE   A 235 ? 0.3260 0.1643 0.1724 0.0091  -0.0357 0.0055  236 PHE   A CZ  
1951 N N   . GLU   A 236 ? 0.3143 0.2012 0.1639 -0.0221 0.0017  0.0011  237 GLU   A N   
1952 C CA  . GLU   A 236 ? 0.3045 0.1943 0.1628 -0.0253 0.0078  -0.0153 237 GLU   A CA  
1953 C C   . GLU   A 236 ? 0.2967 0.2060 0.1463 -0.0205 -0.0122 -0.0026 237 GLU   A C   
1954 O O   . GLU   A 236 ? 0.3161 0.2155 0.1415 -0.0329 0.0050  -0.0125 237 GLU   A O   
1955 C CB  . GLU   A 236 ? 0.3637 0.1878 0.2227 -0.0459 -0.0002 0.0067  237 GLU   A CB  
1956 C CG  . GLU   A 236 ? 0.4250 0.2208 0.1914 -0.0560 0.0237  0.0033  237 GLU   A CG  
1957 C CD  . GLU   A 236 ? 0.4470 0.2319 0.1752 -0.1092 0.0232  0.0001  237 GLU   A CD  
1958 O OE1 . GLU   A 236 ? 0.5141 0.2431 0.1753 -0.1081 0.0232  -0.0163 237 GLU   A OE1 
1959 O OE2 . GLU   A 236 ? 0.4532 0.2745 0.1864 -0.1003 0.0282  -0.0072 237 GLU   A OE2 
1960 N N   . ASP   A 237 ? 0.3186 0.2240 0.1685 -0.0116 -0.0082 0.0073  238 ASP   A N   
1961 C CA  . ASP   A 237 ? 0.3247 0.2233 0.1750 -0.0220 -0.0361 0.0296  238 ASP   A CA  
1962 C C   . ASP   A 237 ? 0.3114 0.2034 0.1782 -0.0464 0.0022  0.0156  238 ASP   A C   
1963 O O   . ASP   A 237 ? 0.3729 0.1991 0.1965 -0.0460 0.0173  0.0116  238 ASP   A O   
1964 C CB  . ASP   A 237 ? 0.3939 0.2775 0.2021 0.0234  -0.0451 0.0596  238 ASP   A CB  
1965 C CG  . ASP   A 237 ? 0.5085 0.3591 0.2794 0.0549  -0.0471 0.0408  238 ASP   A CG  
1966 O OD1 . ASP   A 237 ? 0.5302 0.4133 0.3409 0.0631  -0.0621 0.0339  238 ASP   A OD1 
1967 O OD2 . ASP   A 237 ? 0.5632 0.3872 0.3061 0.0920  -0.0321 0.0246  238 ASP   A OD2 
1968 N N   . GLU   A 238 ? 0.2684 0.2020 0.1664 -0.0227 0.0001  0.0033  239 GLU   A N   
1969 C CA  . GLU   A 238 ? 0.3117 0.2171 0.1939 -0.0502 0.0335  -0.0430 239 GLU   A CA  
1970 C C   . GLU   A 238 ? 0.3130 0.2436 0.1825 -0.0567 0.0192  -0.0485 239 GLU   A C   
1971 O O   . GLU   A 238 ? 0.3442 0.2808 0.2003 -0.0625 0.0181  -0.0642 239 GLU   A O   
1972 C CB  . GLU   A 238 ? 0.3243 0.2067 0.2265 -0.0311 0.0372  -0.0650 239 GLU   A CB  
1973 C CG  . GLU   A 238 ? 0.3513 0.2177 0.2790 -0.0089 0.0437  -0.0620 239 GLU   A CG  
1974 C CD  . GLU   A 238 ? 0.3687 0.2306 0.3083 -0.0238 0.0255  -0.0670 239 GLU   A CD  
1975 O OE1 . GLU   A 238 ? 0.3864 0.1981 0.2819 -0.0059 0.0132  -0.0518 239 GLU   A OE1 
1976 O OE2 . GLU   A 238 ? 0.3784 0.2885 0.3613 0.0160  0.0205  -0.0807 239 GLU   A OE2 
1977 N N   . TYR   A 239 ? 0.3193 0.2026 0.1712 -0.0337 0.0090  -0.0450 240 TYR   A N   
1978 C CA  . TYR   A 239 ? 0.3386 0.2000 0.1658 -0.0245 -0.0141 -0.0066 240 TYR   A CA  
1979 C C   . TYR   A 239 ? 0.3071 0.2036 0.1703 -0.0272 -0.0054 -0.0270 240 TYR   A C   
1980 O O   . TYR   A 239 ? 0.3265 0.2440 0.2175 -0.0262 0.0174  -0.0325 240 TYR   A O   
1981 C CB  . TYR   A 239 ? 0.4020 0.1873 0.2107 -0.0130 -0.0566 0.0452  240 TYR   A CB  
1982 C CG  . TYR   A 239 ? 0.4887 0.1970 0.2647 -0.0092 -0.1085 0.0570  240 TYR   A CG  
1983 C CD1 . TYR   A 239 ? 0.5974 0.2177 0.3164 -0.0044 -0.0956 0.0324  240 TYR   A CD1 
1984 C CD2 . TYR   A 239 ? 0.5264 0.2132 0.2891 -0.0091 -0.1667 0.0562  240 TYR   A CD2 
1985 C CE1 . TYR   A 239 ? 0.6585 0.2199 0.3393 -0.0134 -0.1077 0.0419  240 TYR   A CE1 
1986 C CE2 . TYR   A 239 ? 0.6158 0.2110 0.3058 -0.0185 -0.1581 0.0433  240 TYR   A CE2 
1987 C CZ  . TYR   A 239 ? 0.6675 0.1984 0.3402 -0.0334 -0.1240 0.0323  240 TYR   A CZ  
1988 O OH  . TYR   A 239 ? 0.7114 0.2168 0.3578 -0.0454 -0.1077 0.0001  240 TYR   A OH  
1989 N N   . PHE   A 240 ? 0.3135 0.1873 0.1643 -0.0335 0.0193  -0.0080 241 PHE   A N   
1990 C CA  . PHE   A 240 ? 0.3583 0.1660 0.1580 -0.0161 0.0381  0.0029  241 PHE   A CA  
1991 C C   . PHE   A 240 ? 0.4164 0.1910 0.1560 -0.0124 0.0464  0.0159  241 PHE   A C   
1992 O O   . PHE   A 240 ? 0.4319 0.1913 0.1814 0.0022  0.0183  0.0143  241 PHE   A O   
1993 C CB  . PHE   A 240 ? 0.3121 0.1819 0.1409 -0.0076 0.0172  0.0252  241 PHE   A CB  
1994 C CG  . PHE   A 240 ? 0.2842 0.1836 0.1367 -0.0094 0.0228  0.0084  241 PHE   A CG  
1995 C CD1 . PHE   A 240 ? 0.3251 0.2153 0.1392 -0.0293 0.0176  0.0060  241 PHE   A CD1 
1996 C CD2 . PHE   A 240 ? 0.2756 0.1889 0.1450 -0.0223 0.0207  0.0374  241 PHE   A CD2 
1997 C CE1 . PHE   A 240 ? 0.3213 0.2297 0.1575 -0.0435 -0.0010 0.0343  241 PHE   A CE1 
1998 C CE2 . PHE   A 240 ? 0.2846 0.2309 0.1549 -0.0391 0.0182  0.0238  241 PHE   A CE2 
1999 C CZ  . PHE   A 240 ? 0.2972 0.2294 0.1609 -0.0433 0.0020  0.0121  241 PHE   A CZ  
2000 N N   . SER   A 241 ? 0.4910 0.1967 0.1599 -0.0003 0.0439  0.0165  242 SER   A N   
2001 C CA  . SER   A 241 ? 0.5572 0.2103 0.1857 -0.0063 0.0095  0.0151  242 SER   A CA  
2002 C C   . SER   A 241 ? 0.5694 0.2123 0.2088 -0.0014 0.0164  0.0434  242 SER   A C   
2003 O O   . SER   A 241 ? 0.5987 0.2348 0.2369 0.0249  0.0069  0.0497  242 SER   A O   
2004 C CB  . SER   A 241 ? 0.5999 0.2546 0.1985 -0.0229 0.0254  -0.0139 242 SER   A CB  
2005 O OG  . SER   A 241 ? 0.6343 0.2783 0.2152 -0.0480 0.0888  -0.0235 242 SER   A OG  
2006 N N   . ASN   A 242 ? 0.5416 0.2231 0.2011 -0.0347 0.0954  0.0241  243 ASN   A N   
2007 C CA  . ASN   A 242 ? 0.5601 0.2742 0.2364 -0.0507 0.1301  0.0370  243 ASN   A CA  
2008 C C   . ASN   A 242 ? 0.4876 0.2381 0.2256 -0.0482 0.0855  0.0106  243 ASN   A C   
2009 O O   . ASN   A 242 ? 0.4727 0.2599 0.2649 -0.0816 0.0741  0.0010  243 ASN   A O   
2010 C CB  . ASN   A 242 ? 0.6173 0.3646 0.2938 -0.0812 0.1701  0.0442  243 ASN   A CB  
2011 C CG  . ASN   A 242 ? 0.7115 0.4466 0.3425 -0.0681 0.1647  0.0576  243 ASN   A CG  
2012 O OD1 . ASN   A 242 ? 0.7727 0.4820 0.3508 -0.0482 0.1323  0.0678  243 ASN   A OD1 
2013 N ND2 . ASN   A 242 ? 0.7222 0.4904 0.3778 -0.0743 0.1823  0.0474  243 ASN   A ND2 
2014 N N   . THR   A 243 ? 0.4104 0.2123 0.2138 -0.0131 0.1035  0.0002  244 THR   A N   
2015 C CA  . THR   A 243 ? 0.3670 0.1764 0.1912 0.0123  0.0540  0.0082  244 THR   A CA  
2016 C C   . THR   A 243 ? 0.3346 0.1602 0.1778 0.0015  0.0432  -0.0122 244 THR   A C   
2017 O O   . THR   A 243 ? 0.3719 0.1990 0.1873 0.0014  0.0206  -0.0084 244 THR   A O   
2018 C CB  . THR   A 243 ? 0.3728 0.1702 0.1868 0.0308  0.0586  0.0095  244 THR   A CB  
2019 O OG1 . THR   A 243 ? 0.4265 0.1938 0.2270 0.0301  0.0370  -0.0028 244 THR   A OG1 
2020 C CG2 . THR   A 243 ? 0.3861 0.1748 0.1767 0.0008  0.0224  0.0188  244 THR   A CG2 
2021 N N   . SER   A 244 ? 0.2953 0.1466 0.1822 -0.0040 0.0545  0.0111  245 SER   A N   
2022 C CA  . SER   A 244 ? 0.3038 0.1395 0.1788 0.0009  0.0388  0.0196  245 SER   A CA  
2023 C C   . SER   A 244 ? 0.2656 0.1275 0.1515 0.0170  0.0147  0.0357  245 SER   A C   
2024 O O   . SER   A 244 ? 0.2678 0.1217 0.1554 0.0102  0.0239  0.0113  245 SER   A O   
2025 C CB  . SER   A 244 ? 0.3357 0.1359 0.1671 0.0024  0.0090  0.0153  245 SER   A CB  
2026 O OG  . SER   A 244 ? 0.3248 0.1660 0.1763 -0.0206 0.0001  0.0075  245 SER   A OG  
2027 N N   . ALA   A 245 ? 0.2751 0.1438 0.1505 0.0237  0.0135  0.0375  246 ALA   A N   
2028 C CA  . ALA   A 245 ? 0.2903 0.1675 0.1459 0.0429  0.0034  0.0509  246 ALA   A CA  
2029 C C   . ALA   A 245 ? 0.2891 0.1401 0.1504 0.0169  0.0078  0.0201  246 ALA   A C   
2030 O O   . ALA   A 245 ? 0.2811 0.1386 0.1622 -0.0179 -0.0054 0.0191  246 ALA   A O   
2031 C CB  . ALA   A 245 ? 0.3178 0.2020 0.1695 0.0760  -0.0005 0.0584  246 ALA   A CB  
2032 N N   . LEU   A 246 ? 0.2911 0.1541 0.1404 0.0134  0.0151  0.0094  247 LEU   A N   
2033 C CA  . LEU   A 246 ? 0.2842 0.1371 0.1587 -0.0194 0.0158  -0.0086 247 LEU   A CA  
2034 C C   . LEU   A 246 ? 0.2693 0.1278 0.1407 -0.0250 0.0132  -0.0104 247 LEU   A C   
2035 O O   . LEU   A 246 ? 0.2864 0.1649 0.1280 -0.0449 0.0066  0.0090  247 LEU   A O   
2036 C CB  . LEU   A 246 ? 0.3275 0.1689 0.2250 -0.0381 0.0224  -0.0357 247 LEU   A CB  
2037 C CG  . LEU   A 246 ? 0.3128 0.1665 0.2700 -0.0027 0.0317  -0.0480 247 LEU   A CG  
2038 C CD1 . LEU   A 246 ? 0.3279 0.1539 0.2780 -0.0573 0.0278  -0.0546 247 LEU   A CD1 
2039 C CD2 . LEU   A 246 ? 0.3116 0.1469 0.2412 0.0128  0.0483  -0.0247 247 LEU   A CD2 
2040 N N   . ALA   A 247 ? 0.2284 0.1296 0.1600 0.0051  -0.0089 -0.0045 248 ALA   A N   
2041 C CA  . ALA   A 247 ? 0.2351 0.1448 0.1649 0.0039  -0.0085 0.0140  248 ALA   A CA  
2042 C C   . ALA   A 247 ? 0.2648 0.1244 0.1426 -0.0067 -0.0127 0.0119  248 ALA   A C   
2043 O O   . ALA   A 247 ? 0.2586 0.1504 0.1425 -0.0151 -0.0164 0.0297  248 ALA   A O   
2044 C CB  . ALA   A 247 ? 0.2487 0.1466 0.1769 0.0134  -0.0030 0.0165  248 ALA   A CB  
2045 N N   . LYS   A 248 ? 0.2529 0.1509 0.1354 -0.0230 -0.0310 0.0087  249 LYS   A N   
2046 C CA  . LYS   A 248 ? 0.2619 0.1635 0.1232 -0.0152 -0.0215 0.0011  249 LYS   A CA  
2047 C C   . LYS   A 248 ? 0.2625 0.1390 0.1245 -0.0067 -0.0103 0.0165  249 LYS   A C   
2048 O O   . LYS   A 248 ? 0.2787 0.1481 0.1407 -0.0261 -0.0228 0.0331  249 LYS   A O   
2049 C CB  . LYS   A 248 ? 0.2970 0.1802 0.1118 0.0104  -0.0269 -0.0187 249 LYS   A CB  
2050 C CG  . LYS   A 248 ? 0.3477 0.2124 0.1146 0.0096  -0.0097 -0.0478 249 LYS   A CG  
2051 C CD  . LYS   A 248 ? 0.4452 0.3010 0.1420 0.0060  0.0001  -0.0383 249 LYS   A CD  
2052 C CE  . LYS   A 248 ? 0.5065 0.3351 0.1964 0.0354  -0.0127 -0.0094 249 LYS   A CE  
2053 N NZ  . LYS   A 248 ? 0.5754 0.3778 0.2221 0.0573  -0.0264 0.0208  249 LYS   A NZ  
2054 N N   . ASP   A 249 ? 0.2419 0.1485 0.1363 0.0051  -0.0108 0.0184  250 ASP   A N   
2055 C CA  . ASP   A 249 ? 0.2576 0.1324 0.1196 0.0002  -0.0142 0.0368  250 ASP   A CA  
2056 C C   . ASP   A 249 ? 0.2328 0.1372 0.1183 -0.0064 -0.0077 0.0251  250 ASP   A C   
2057 O O   . ASP   A 249 ? 0.2542 0.1310 0.1247 -0.0065 0.0033  0.0172  250 ASP   A O   
2058 C CB  . ASP   A 249 ? 0.2788 0.1409 0.1377 0.0064  0.0180  0.0219  250 ASP   A CB  
2059 C CG  . ASP   A 249 ? 0.2535 0.1880 0.1725 0.0341  -0.0116 0.0527  250 ASP   A CG  
2060 O OD1 . ASP   A 249 ? 0.2461 0.1661 0.1693 0.0186  -0.0050 0.0168  250 ASP   A OD1 
2061 O OD2 . ASP   A 249 ? 0.2884 0.2261 0.1914 0.0397  -0.0053 0.0461  250 ASP   A OD2 
2062 N N   . PHE   A 250 ? 0.2244 0.1392 0.1280 0.0092  -0.0201 0.0244  251 PHE   A N   
2063 C CA  . PHE   A 250 ? 0.2299 0.1222 0.1291 -0.0164 -0.0269 0.0212  251 PHE   A CA  
2064 C C   . PHE   A 250 ? 0.2204 0.1216 0.1225 -0.0210 -0.0106 0.0245  251 PHE   A C   
2065 O O   . PHE   A 250 ? 0.2411 0.1257 0.1256 -0.0241 -0.0120 0.0158  251 PHE   A O   
2066 C CB  . PHE   A 250 ? 0.2356 0.1356 0.1400 -0.0097 -0.0407 0.0220  251 PHE   A CB  
2067 C CG  . PHE   A 250 ? 0.2370 0.1306 0.1456 -0.0353 -0.0185 0.0095  251 PHE   A CG  
2068 C CD1 . PHE   A 250 ? 0.2238 0.1852 0.1264 -0.0354 -0.0105 0.0109  251 PHE   A CD1 
2069 C CD2 . PHE   A 250 ? 0.2495 0.1272 0.1577 -0.0203 -0.0453 0.0272  251 PHE   A CD2 
2070 C CE1 . PHE   A 250 ? 0.2668 0.1676 0.1319 -0.0339 -0.0311 0.0233  251 PHE   A CE1 
2071 C CE2 . PHE   A 250 ? 0.2500 0.1510 0.1674 -0.0454 -0.0542 0.0259  251 PHE   A CE2 
2072 C CZ  . PHE   A 250 ? 0.2506 0.1698 0.1456 -0.0363 -0.0400 0.0130  251 PHE   A CZ  
2073 N N   . ILE   A 251 ? 0.2420 0.1188 0.1281 -0.0054 -0.0133 -0.0036 252 ILE   A N   
2074 C CA  . ILE   A 251 ? 0.2312 0.1201 0.1305 -0.0126 -0.0040 0.0113  252 ILE   A CA  
2075 C C   . ILE   A 251 ? 0.2264 0.1316 0.1261 0.0047  -0.0237 0.0075  252 ILE   A C   
2076 O O   . ILE   A 251 ? 0.2331 0.1159 0.1418 -0.0140 -0.0129 0.0082  252 ILE   A O   
2077 C CB  . ILE   A 251 ? 0.2389 0.1221 0.1421 0.0102  -0.0087 0.0070  252 ILE   A CB  
2078 C CG1 . ILE   A 251 ? 0.2108 0.1726 0.1464 -0.0021 -0.0135 -0.0019 252 ILE   A CG1 
2079 C CG2 . ILE   A 251 ? 0.2646 0.1374 0.1476 -0.0115 0.0080  -0.0072 252 ILE   A CG2 
2080 C CD1 . ILE   A 251 ? 0.2439 0.1725 0.1626 0.0052  0.0024  -0.0129 252 ILE   A CD1 
2081 N N   . ARG   A 252 ? 0.2393 0.1479 0.1261 -0.0131 -0.0525 -0.0083 253 ARG   A N   
2082 C CA  . ARG   A 252 ? 0.2410 0.1795 0.1583 -0.0123 -0.0624 -0.0038 253 ARG   A CA  
2083 C C   . ARG   A 252 ? 0.2261 0.1640 0.1583 0.0029  -0.0183 0.0038  253 ARG   A C   
2084 O O   . ARG   A 252 ? 0.2334 0.2147 0.1781 -0.0372 -0.0058 -0.0013 253 ARG   A O   
2085 C CB  . ARG   A 252 ? 0.2637 0.2020 0.1847 0.0038  -0.0573 0.0378  253 ARG   A CB  
2086 C CG  . ARG   A 252 ? 0.4097 0.2982 0.2769 0.0537  -0.0849 0.0584  253 ARG   A CG  
2087 C CD  . ARG   A 252 ? 0.4471 0.3857 0.3317 0.0946  -0.1096 0.0639  253 ARG   A CD  
2088 N NE  . ARG   A 252 ? 0.4825 0.4725 0.3873 0.1062  -0.1010 0.0542  253 ARG   A NE  
2089 C CZ  . ARG   A 252 ? 0.5294 0.5205 0.4357 0.1118  -0.0984 0.0069  253 ARG   A CZ  
2090 N NH1 . ARG   A 252 ? 0.5792 0.5447 0.4683 0.1207  -0.0785 0.0134  253 ARG   A NH1 
2091 N NH2 . ARG   A 252 ? 0.5375 0.5278 0.4512 0.1169  -0.0957 0.0068  253 ARG   A NH2 
2092 N N   . ARG   A 253 ? 0.2317 0.1456 0.1287 0.0238  -0.0185 0.0252  254 ARG   A N   
2093 C CA  . ARG   A 253 ? 0.2451 0.1470 0.1380 0.0292  -0.0051 0.0081  254 ARG   A CA  
2094 C C   . ARG   A 253 ? 0.2014 0.1474 0.1328 0.0171  -0.0072 0.0096  254 ARG   A C   
2095 O O   . ARG   A 253 ? 0.2158 0.1733 0.1480 0.0289  -0.0039 0.0034  254 ARG   A O   
2096 C CB  . ARG   A 253 ? 0.2799 0.1382 0.1755 0.0170  -0.0020 -0.0019 254 ARG   A CB  
2097 C CG  . ARG   A 253 ? 0.2907 0.1245 0.2069 0.0219  -0.0073 0.0133  254 ARG   A CG  
2098 C CD  . ARG   A 253 ? 0.3253 0.1407 0.2237 0.0298  0.0212  0.0213  254 ARG   A CD  
2099 N NE  . ARG   A 253 ? 0.3313 0.1542 0.2175 0.0415  0.0563  0.0254  254 ARG   A NE  
2100 C CZ  . ARG   A 253 ? 0.3610 0.1501 0.2347 0.0801  0.0814  0.0425  254 ARG   A CZ  
2101 N NH1 . ARG   A 253 ? 0.3499 0.2136 0.2788 0.0536  0.0897  0.0314  254 ARG   A NH1 
2102 N NH2 . ARG   A 253 ? 0.3921 0.1523 0.2402 0.0872  0.0397  0.0574  254 ARG   A NH2 
2103 N N   . LEU   A 254 ? 0.2173 0.1260 0.1375 0.0221  -0.0332 0.0023  255 LEU   A N   
2104 C CA  . LEU   A 254 ? 0.1931 0.1199 0.1472 0.0100  -0.0272 0.0045  255 LEU   A CA  
2105 C C   . LEU   A 254 ? 0.1975 0.1241 0.1354 -0.0123 -0.0094 -0.0155 255 LEU   A C   
2106 O O   . LEU   A 254 ? 0.2307 0.1299 0.1385 -0.0130 0.0044  0.0023  255 LEU   A O   
2107 C CB  . LEU   A 254 ? 0.2101 0.1193 0.1209 -0.0054 -0.0168 -0.0005 255 LEU   A CB  
2108 C CG  . LEU   A 254 ? 0.2240 0.1244 0.1253 -0.0021 -0.0219 -0.0114 255 LEU   A CG  
2109 C CD1 . LEU   A 254 ? 0.2065 0.1786 0.1692 -0.0073 -0.0001 -0.0238 255 LEU   A CD1 
2110 C CD2 . LEU   A 254 ? 0.2775 0.1475 0.1170 0.0068  -0.0408 -0.0158 255 LEU   A CD2 
2111 N N   . LEU   A 255 ? 0.2276 0.1284 0.1355 0.0018  -0.0252 -0.0257 256 LEU   A N   
2112 C CA  . LEU   A 255 ? 0.1890 0.1410 0.1309 0.0004  -0.0056 -0.0456 256 LEU   A CA  
2113 C C   . LEU   A 255 ? 0.2014 0.1835 0.1457 0.0025  -0.0261 -0.0177 256 LEU   A C   
2114 O O   . LEU   A 255 ? 0.2190 0.2177 0.1517 -0.0045 -0.0274 -0.0227 256 LEU   A O   
2115 C CB  . LEU   A 255 ? 0.2065 0.1558 0.1400 -0.0009 -0.0138 -0.0146 256 LEU   A CB  
2116 C CG  . LEU   A 255 ? 0.2072 0.1579 0.1280 -0.0013 -0.0023 0.0096  256 LEU   A CG  
2117 C CD1 . LEU   A 255 ? 0.2702 0.1745 0.1368 -0.0231 0.0007  -0.0064 256 LEU   A CD1 
2118 C CD2 . LEU   A 255 ? 0.2378 0.1754 0.1328 0.0087  -0.0054 0.0310  256 LEU   A CD2 
2119 N N   . VAL   A 256 ? 0.1949 0.1725 0.1573 0.0086  0.0042  -0.0093 257 VAL   A N   
2120 C CA  . VAL   A 256 ? 0.2184 0.1824 0.1741 -0.0085 -0.0003 -0.0035 257 VAL   A CA  
2121 C C   . VAL   A 256 ? 0.1960 0.1881 0.1677 -0.0143 -0.0046 -0.0060 257 VAL   A C   
2122 O O   . VAL   A 256 ? 0.2171 0.2094 0.1694 0.0077  -0.0107 0.0126  257 VAL   A O   
2123 C CB  . VAL   A 256 ? 0.2463 0.1636 0.2252 0.0312  0.0172  0.0332  257 VAL   A CB  
2124 C CG1 . VAL   A 256 ? 0.3095 0.1845 0.2736 0.0473  0.0637  -0.0011 257 VAL   A CG1 
2125 C CG2 . VAL   A 256 ? 0.2763 0.1771 0.2362 0.0335  -0.0040 0.0362  257 VAL   A CG2 
2126 N N   . LYS   A 257 ? 0.2046 0.1690 0.1875 -0.0064 0.0167  -0.0164 258 LYS   A N   
2127 C CA  A LYS   A 257 ? 0.2363 0.1790 0.1926 -0.0155 0.0090  -0.0156 258 LYS   A CA  
2128 C CA  B LYS   A 257 ? 0.2153 0.1776 0.1887 -0.0318 0.0122  -0.0298 258 LYS   A CA  
2129 C C   . LYS   A 257 ? 0.2313 0.1874 0.1836 0.0067  0.0135  -0.0177 258 LYS   A C   
2130 O O   . LYS   A 257 ? 0.2375 0.2171 0.1919 -0.0131 0.0106  0.0011  258 LYS   A O   
2131 C CB  A LYS   A 257 ? 0.2982 0.2039 0.2292 -0.0406 -0.0011 -0.0181 258 LYS   A CB  
2132 C CB  B LYS   A 257 ? 0.2417 0.1969 0.2197 -0.0878 0.0104  -0.0578 258 LYS   A CB  
2133 C CG  A LYS   A 257 ? 0.3460 0.2309 0.2551 -0.0461 0.0013  -0.0207 258 LYS   A CG  
2134 C CG  B LYS   A 257 ? 0.2687 0.2155 0.2420 -0.1125 0.0296  -0.0666 258 LYS   A CG  
2135 C CD  A LYS   A 257 ? 0.4069 0.2585 0.2762 -0.0364 0.0083  -0.0261 258 LYS   A CD  
2136 C CD  B LYS   A 257 ? 0.3036 0.2383 0.2623 -0.1159 0.0529  -0.0653 258 LYS   A CD  
2137 C CE  A LYS   A 257 ? 0.4006 0.2857 0.2871 -0.0049 0.0173  -0.0195 258 LYS   A CE  
2138 C CE  B LYS   A 257 ? 0.2701 0.2695 0.2668 -0.1111 0.0702  -0.0722 258 LYS   A CE  
2139 N NZ  A LYS   A 257 ? 0.3745 0.2995 0.2814 0.0292  0.0300  -0.0166 258 LYS   A NZ  
2140 N NZ  B LYS   A 257 ? 0.2671 0.3012 0.2736 -0.1029 0.0625  -0.0866 258 LYS   A NZ  
2141 N N   . ASP   A 258 ? 0.2035 0.2144 0.1861 -0.0033 0.0045  -0.0561 259 ASP   A N   
2142 C CA  . ASP   A 258 ? 0.2095 0.2482 0.2106 -0.0083 -0.0018 -0.0583 259 ASP   A CA  
2143 C C   . ASP   A 258 ? 0.2084 0.2279 0.2021 -0.0096 0.0139  -0.0372 259 ASP   A C   
2144 O O   . ASP   A 258 ? 0.2390 0.2205 0.1985 -0.0297 0.0086  -0.0507 259 ASP   A O   
2145 C CB  . ASP   A 258 ? 0.2320 0.2912 0.2415 0.0095  0.0163  -0.0766 259 ASP   A CB  
2146 C CG  . ASP   A 258 ? 0.2465 0.3641 0.2717 0.0086  0.0195  -0.0666 259 ASP   A CG  
2147 O OD1 . ASP   A 258 ? 0.2817 0.3585 0.2766 -0.0465 0.0527  -0.0652 259 ASP   A OD1 
2148 O OD2 . ASP   A 258 ? 0.2966 0.4238 0.3009 0.0385  0.0179  -0.0528 259 ASP   A OD2 
2149 N N   . PRO   A 259 ? 0.2296 0.2018 0.1920 -0.0394 -0.0071 0.0008  260 PRO   A N   
2150 C CA  . PRO   A 259 ? 0.2619 0.1996 0.1998 -0.0469 -0.0204 -0.0006 260 PRO   A CA  
2151 C C   . PRO   A 259 ? 0.2456 0.2015 0.2104 -0.0467 -0.0053 -0.0069 260 PRO   A C   
2152 O O   . PRO   A 259 ? 0.2784 0.2117 0.2369 -0.0621 -0.0340 -0.0073 260 PRO   A O   
2153 C CB  . PRO   A 259 ? 0.2880 0.2035 0.2197 -0.0564 -0.0359 0.0142  260 PRO   A CB  
2154 C CG  . PRO   A 259 ? 0.2782 0.2342 0.2545 -0.0619 -0.0435 0.0251  260 PRO   A CG  
2155 C CD  . PRO   A 259 ? 0.2852 0.2063 0.1989 -0.0747 -0.0261 0.0165  260 PRO   A CD  
2156 N N   . LYS   A 260 ? 0.2793 0.2251 0.1977 -0.0506 0.0297  -0.0393 261 LYS   A N   
2157 C CA  . LYS   A 260 ? 0.3366 0.2421 0.2374 -0.0444 0.0512  -0.0554 261 LYS   A CA  
2158 C C   . LYS   A 260 ? 0.3114 0.2320 0.2320 -0.0289 0.0221  -0.0329 261 LYS   A C   
2159 O O   . LYS   A 260 ? 0.3970 0.2432 0.2545 0.0021  0.0322  -0.0297 261 LYS   A O   
2160 C CB  . LYS   A 260 ? 0.4040 0.3167 0.2808 -0.0431 0.1134  -0.0447 261 LYS   A CB  
2161 C CG  . LYS   A 260 ? 0.5127 0.3842 0.3452 -0.0519 0.0873  -0.0138 261 LYS   A CG  
2162 C CD  . LYS   A 260 ? 0.6211 0.4412 0.4014 -0.0397 0.0750  -0.0088 261 LYS   A CD  
2163 C CE  . LYS   A 260 ? 0.6705 0.4829 0.4152 -0.0256 0.0799  0.0010  261 LYS   A CE  
2164 N NZ  . LYS   A 260 ? 0.7102 0.5079 0.4180 -0.0253 0.0792  0.0146  261 LYS   A NZ  
2165 N N   . LYS   A 261 ? 0.2301 0.2336 0.2067 0.0004  0.0018  -0.0125 262 LYS   A N   
2166 C CA  . LYS   A 261 ? 0.1902 0.2420 0.2340 -0.0104 -0.0128 0.0011  262 LYS   A CA  
2167 C C   . LYS   A 261 ? 0.1941 0.2011 0.2212 0.0320  -0.0101 0.0050  262 LYS   A C   
2168 O O   . LYS   A 261 ? 0.2316 0.2155 0.2503 0.0365  0.0203  0.0176  262 LYS   A O   
2169 C CB  . LYS   A 261 ? 0.2103 0.3433 0.2905 -0.0504 -0.0035 0.0137  262 LYS   A CB  
2170 C CG  . LYS   A 261 ? 0.2756 0.4483 0.3512 -0.0875 -0.0190 0.0285  262 LYS   A CG  
2171 C CD  . LYS   A 261 ? 0.3443 0.5265 0.3965 -0.1032 -0.0002 0.0318  262 LYS   A CD  
2172 C CE  . LYS   A 261 ? 0.3598 0.5735 0.4344 -0.1152 0.0045  0.0260  262 LYS   A CE  
2173 N NZ  . LYS   A 261 ? 0.3964 0.5967 0.4649 -0.1136 0.0172  0.0292  262 LYS   A NZ  
2174 N N   . ARG   A 262 ? 0.1982 0.1815 0.2022 0.0268  -0.0225 -0.0335 263 ARG   A N   
2175 C CA  . ARG   A 262 ? 0.2018 0.1971 0.1965 0.0382  -0.0359 -0.0023 263 ARG   A CA  
2176 C C   . ARG   A 262 ? 0.1851 0.1979 0.1803 0.0290  0.0000  -0.0045 263 ARG   A C   
2177 O O   . ARG   A 262 ? 0.2103 0.2258 0.1692 0.0200  0.0073  -0.0258 263 ARG   A O   
2178 C CB  . ARG   A 262 ? 0.2697 0.2086 0.2015 0.0829  -0.0111 0.0260  263 ARG   A CB  
2179 C CG  . ARG   A 262 ? 0.3290 0.1923 0.1956 0.0691  0.0294  -0.0013 263 ARG   A CG  
2180 C CD  . ARG   A 262 ? 0.2930 0.1534 0.1651 0.0350  -0.0228 -0.0109 263 ARG   A CD  
2181 N NE  . ARG   A 262 ? 0.2059 0.1641 0.1420 0.0148  0.0144  0.0177  263 ARG   A NE  
2182 C CZ  . ARG   A 262 ? 0.2199 0.1563 0.1331 0.0098  -0.0002 -0.0064 263 ARG   A CZ  
2183 N NH1 . ARG   A 262 ? 0.2332 0.1497 0.1218 0.0104  0.0041  0.0038  263 ARG   A NH1 
2184 N NH2 . ARG   A 262 ? 0.2143 0.1940 0.1477 0.0082  0.0041  -0.0080 263 ARG   A NH2 
2185 N N   . MET   A 263 ? 0.2156 0.1800 0.1717 0.0163  -0.0225 0.0031  264 MET   A N   
2186 C CA  . MET   A 263 ? 0.2500 0.1693 0.1889 0.0187  0.0049  0.0357  264 MET   A CA  
2187 C C   . MET   A 263 ? 0.2047 0.1601 0.1782 0.0016  -0.0372 0.0172  264 MET   A C   
2188 O O   . MET   A 263 ? 0.2192 0.1682 0.1510 0.0003  -0.0120 0.0300  264 MET   A O   
2189 C CB  . MET   A 263 ? 0.3263 0.2222 0.2163 -0.0074 0.0200  0.0680  264 MET   A CB  
2190 C CG  . MET   A 263 ? 0.3413 0.2349 0.2164 -0.0023 0.0306  0.0517  264 MET   A CG  
2191 S SD  . MET   A 263 ? 0.2833 0.1738 0.1893 -0.0021 0.0172  -0.0061 264 MET   A SD  
2192 C CE  . MET   A 263 ? 0.2804 0.1587 0.1933 0.0302  0.0026  0.0032  264 MET   A CE  
2193 N N   . THR   A 264 ? 0.2039 0.1648 0.1805 -0.0073 -0.0408 -0.0023 265 THR   A N   
2194 C CA  . THR   A 264 ? 0.1892 0.1474 0.1716 0.0116  -0.0278 -0.0113 265 THR   A CA  
2195 C C   . THR   A 264 ? 0.1925 0.1436 0.1671 0.0221  -0.0414 -0.0026 265 THR   A C   
2196 O O   . THR   A 264 ? 0.2234 0.1487 0.1455 -0.0030 -0.0311 0.0060  265 THR   A O   
2197 C CB  . THR   A 264 ? 0.1954 0.1512 0.2180 0.0279  0.0070  0.0044  265 THR   A CB  
2198 O OG1 . THR   A 264 ? 0.2320 0.1455 0.2314 0.0132  -0.0046 0.0089  265 THR   A OG1 
2199 C CG2 . THR   A 264 ? 0.1675 0.2083 0.2561 0.0060  0.0077  -0.0052 265 THR   A CG2 
2200 N N   . ILE   A 265 ? 0.1726 0.1399 0.1522 0.0025  -0.0218 -0.0095 266 ILE   A N   
2201 C CA  . ILE   A 265 ? 0.1786 0.1340 0.1522 0.0062  -0.0022 -0.0076 266 ILE   A CA  
2202 C C   . ILE   A 265 ? 0.2059 0.1235 0.1497 0.0118  -0.0152 -0.0042 266 ILE   A C   
2203 O O   . ILE   A 265 ? 0.2286 0.1300 0.1372 -0.0061 -0.0143 0.0021  266 ILE   A O   
2204 C CB  . ILE   A 265 ? 0.1835 0.1593 0.1269 0.0086  -0.0191 0.0119  266 ILE   A CB  
2205 C CG1 . ILE   A 265 ? 0.2021 0.1703 0.1367 0.0089  -0.0041 0.0002  266 ILE   A CG1 
2206 C CG2 . ILE   A 265 ? 0.2663 0.1459 0.1171 -0.0050 -0.0162 -0.0092 266 ILE   A CG2 
2207 C CD1 . ILE   A 265 ? 0.2251 0.2049 0.1355 0.0148  -0.0057 0.0080  266 ILE   A CD1 
2208 N N   . GLN   A 266 ? 0.2325 0.1185 0.1494 0.0119  -0.0244 -0.0122 267 GLN   A N   
2209 C CA  . GLN   A 266 ? 0.2462 0.1208 0.1559 0.0123  -0.0061 -0.0015 267 GLN   A CA  
2210 C C   . GLN   A 266 ? 0.2613 0.1301 0.1629 0.0260  -0.0170 0.0102  267 GLN   A C   
2211 O O   . GLN   A 266 ? 0.2786 0.1515 0.1895 -0.0133 -0.0178 0.0218  267 GLN   A O   
2212 C CB  . GLN   A 266 ? 0.2737 0.1946 0.1621 0.0562  -0.0077 -0.0159 267 GLN   A CB  
2213 C CG  . GLN   A 266 ? 0.3770 0.2413 0.1911 0.0829  0.0206  -0.0147 267 GLN   A CG  
2214 C CD  . GLN   A 266 ? 0.5540 0.3015 0.2720 0.1192  0.0857  0.0095  267 GLN   A CD  
2215 O OE1 . GLN   A 266 ? 0.6603 0.3256 0.3033 0.1263  0.0973  0.0033  267 GLN   A OE1 
2216 N NE2 . GLN   A 266 ? 0.5761 0.3685 0.3087 0.1180  0.1055  0.0361  267 GLN   A NE2 
2217 N N   . ASP   A 267 ? 0.2356 0.1566 0.1523 0.0056  -0.0203 -0.0078 268 ASP   A N   
2218 C CA  . ASP   A 267 ? 0.2717 0.1732 0.1574 0.0264  -0.0264 0.0139  268 ASP   A CA  
2219 C C   . ASP   A 267 ? 0.2422 0.1572 0.1697 0.0193  -0.0221 0.0299  268 ASP   A C   
2220 O O   . ASP   A 267 ? 0.2584 0.1734 0.1713 0.0265  -0.0249 0.0274  268 ASP   A O   
2221 C CB  . ASP   A 267 ? 0.2570 0.2063 0.1686 0.0055  -0.0210 0.0204  268 ASP   A CB  
2222 C CG  . ASP   A 267 ? 0.3109 0.2076 0.2281 0.0297  -0.0173 0.0017  268 ASP   A CG  
2223 O OD1 . ASP   A 267 ? 0.3433 0.2097 0.2734 0.0813  -0.0264 -0.0336 268 ASP   A OD1 
2224 O OD2 . ASP   A 267 ? 0.2732 0.2115 0.2509 0.0312  -0.0265 0.0138  268 ASP   A OD2 
2225 N N   . SER   A 268 ? 0.2252 0.1445 0.1543 0.0213  -0.0215 0.0204  269 SER   A N   
2226 C CA  A SER   A 268 ? 0.2279 0.1432 0.1435 0.0036  -0.0052 0.0279  269 SER   A CA  
2227 C CA  B SER   A 268 ? 0.2451 0.1562 0.1658 0.0053  -0.0070 0.0273  269 SER   A CA  
2228 C C   . SER   A 268 ? 0.2421 0.1556 0.1534 -0.0061 -0.0082 0.0218  269 SER   A C   
2229 O O   . SER   A 268 ? 0.2519 0.1758 0.1546 -0.0160 -0.0032 0.0317  269 SER   A O   
2230 C CB  A SER   A 268 ? 0.2292 0.1290 0.1300 0.0233  0.0008  0.0258  269 SER   A CB  
2231 C CB  B SER   A 268 ? 0.2837 0.1735 0.1936 0.0231  -0.0081 0.0290  269 SER   A CB  
2232 O OG  A SER   A 268 ? 0.1971 0.1167 0.1192 0.0189  0.0048  0.0182  269 SER   A OG  
2233 O OG  B SER   A 268 ? 0.3016 0.1931 0.2235 0.0213  -0.0090 0.0327  269 SER   A OG  
2234 N N   . LEU   A 269 ? 0.2422 0.1686 0.1583 -0.0020 -0.0337 0.0013  270 LEU   A N   
2235 C CA  . LEU   A 269 ? 0.2788 0.1725 0.1571 -0.0257 -0.0386 0.0063  270 LEU   A CA  
2236 C C   . LEU   A 269 ? 0.3177 0.1808 0.1756 -0.0419 -0.0454 0.0293  270 LEU   A C   
2237 O O   . LEU   A 269 ? 0.3339 0.2117 0.2316 -0.0481 -0.0484 0.0580  270 LEU   A O   
2238 C CB  . LEU   A 269 ? 0.3048 0.2051 0.1849 0.0007  -0.0416 0.0230  270 LEU   A CB  
2239 C CG  . LEU   A 269 ? 0.2946 0.2307 0.2454 -0.0149 -0.0658 0.0362  270 LEU   A CG  
2240 C CD1 . LEU   A 269 ? 0.3541 0.2906 0.2656 -0.0258 -0.0521 0.0592  270 LEU   A CD1 
2241 C CD2 . LEU   A 269 ? 0.3005 0.2308 0.2531 0.0218  -0.0804 0.0166  270 LEU   A CD2 
2242 N N   . GLN   A 270 ? 0.3197 0.1537 0.1619 -0.0209 -0.0368 0.0163  271 GLN   A N   
2243 C CA  . GLN   A 270 ? 0.3686 0.1634 0.1938 -0.0221 -0.0348 0.0319  271 GLN   A CA  
2244 C C   . GLN   A 270 ? 0.3655 0.1425 0.1939 -0.0605 -0.0495 0.0287  271 GLN   A C   
2245 O O   . GLN   A 270 ? 0.3894 0.1626 0.2099 -0.0252 -0.0641 0.0211  271 GLN   A O   
2246 C CB  . GLN   A 270 ? 0.4180 0.1809 0.2130 0.0426  -0.0379 0.0093  271 GLN   A CB  
2247 C CG  . GLN   A 270 ? 0.4279 0.2050 0.2343 0.0248  -0.0690 0.0021  271 GLN   A CG  
2248 C CD  . GLN   A 270 ? 0.4972 0.2229 0.2653 -0.0125 -0.0722 -0.0113 271 GLN   A CD  
2249 O OE1 . GLN   A 270 ? 0.5385 0.2332 0.3084 -0.0193 -0.0743 -0.0274 271 GLN   A OE1 
2250 N NE2 . GLN   A 270 ? 0.5338 0.2496 0.2611 -0.0240 -0.0761 -0.0185 271 GLN   A NE2 
2251 N N   . HIS   A 271 ? 0.3720 0.1386 0.1565 -0.0389 -0.0432 0.0175  272 HIS   A N   
2252 C CA  . HIS   A 271 ? 0.3477 0.1270 0.1543 -0.0397 -0.0430 0.0328  272 HIS   A CA  
2253 C C   . HIS   A 271 ? 0.2985 0.1332 0.1869 -0.0255 -0.0642 0.0335  272 HIS   A C   
2254 O O   . HIS   A 271 ? 0.3156 0.1653 0.2072 -0.0379 -0.0667 0.0440  272 HIS   A O   
2255 C CB  . HIS   A 271 ? 0.3325 0.1348 0.1507 -0.0321 -0.0331 0.0334  272 HIS   A CB  
2256 C CG  . HIS   A 271 ? 0.2703 0.1386 0.1350 0.0167  -0.0255 0.0309  272 HIS   A CG  
2257 N ND1 . HIS   A 271 ? 0.2659 0.1433 0.1506 -0.0104 -0.0155 0.0340  272 HIS   A ND1 
2258 C CD2 . HIS   A 271 ? 0.2608 0.1557 0.1492 0.0323  -0.0144 0.0169  272 HIS   A CD2 
2259 C CE1 . HIS   A 271 ? 0.2222 0.1494 0.1748 -0.0051 -0.0299 0.0100  272 HIS   A CE1 
2260 N NE2 . HIS   A 271 ? 0.2544 0.1484 0.1462 0.0115  -0.0136 0.0106  272 HIS   A NE2 
2261 N N   . PRO   A 272 ? 0.3047 0.1449 0.2096 -0.0016 -0.0480 0.0421  273 PRO   A N   
2262 C CA  . PRO   A 272 ? 0.3397 0.1577 0.2186 -0.0126 -0.0321 0.0864  273 PRO   A CA  
2263 C C   . PRO   A 272 ? 0.3202 0.1693 0.2359 -0.0496 -0.0334 0.0658  273 PRO   A C   
2264 O O   . PRO   A 272 ? 0.3584 0.1964 0.2731 -0.0502 -0.0470 0.0503  273 PRO   A O   
2265 C CB  . PRO   A 272 ? 0.3655 0.1735 0.2351 0.0076  -0.0356 0.0933  273 PRO   A CB  
2266 C CG  . PRO   A 272 ? 0.3913 0.1967 0.2621 -0.0027 -0.0440 0.0922  273 PRO   A CG  
2267 C CD  . PRO   A 272 ? 0.3331 0.1624 0.2340 0.0168  -0.0515 0.0695  273 PRO   A CD  
2268 N N   . TRP   A 273 ? 0.2744 0.1783 0.2302 -0.0295 -0.0198 0.0528  274 TRP   A N   
2269 C CA  . TRP   A 273 ? 0.2639 0.2109 0.2306 -0.0426 -0.0055 0.0533  274 TRP   A CA  
2270 C C   . TRP   A 273 ? 0.2892 0.2300 0.2614 -0.0592 -0.0259 0.0548  274 TRP   A C   
2271 O O   . TRP   A 273 ? 0.3333 0.2573 0.2894 -0.0692 -0.0528 0.0280  274 TRP   A O   
2272 C CB  . TRP   A 273 ? 0.2616 0.1865 0.2129 -0.0213 -0.0035 0.0672  274 TRP   A CB  
2273 C CG  . TRP   A 273 ? 0.2718 0.1592 0.1780 -0.0188 -0.0254 0.0673  274 TRP   A CG  
2274 C CD1 . TRP   A 273 ? 0.3023 0.1785 0.1984 -0.0150 -0.0101 0.0559  274 TRP   A CD1 
2275 C CD2 . TRP   A 273 ? 0.2815 0.1639 0.1708 -0.0244 -0.0399 0.0514  274 TRP   A CD2 
2276 N NE1 . TRP   A 273 ? 0.3124 0.1668 0.1928 -0.0202 -0.0115 0.0389  274 TRP   A NE1 
2277 C CE2 . TRP   A 273 ? 0.2943 0.1489 0.1774 -0.0157 -0.0289 0.0344  274 TRP   A CE2 
2278 C CE3 . TRP   A 273 ? 0.2961 0.1637 0.1429 -0.0215 -0.0201 0.0400  274 TRP   A CE3 
2279 C CZ2 . TRP   A 273 ? 0.3149 0.1549 0.1624 -0.0340 -0.0258 0.0470  274 TRP   A CZ2 
2280 C CZ3 . TRP   A 273 ? 0.3156 0.1762 0.1660 -0.0140 0.0026  0.0386  274 TRP   A CZ3 
2281 C CH2 . TRP   A 273 ? 0.3231 0.1681 0.1742 -0.0283 -0.0063 0.0352  274 TRP   A CH2 
2282 N N   . ILE   A 274 ? 0.2928 0.2457 0.2627 -0.0616 -0.0659 0.0917  275 ILE   A N   
2283 C CA  . ILE   A 274 ? 0.2988 0.2717 0.2642 -0.0669 -0.0752 0.0764  275 ILE   A CA  
2284 C C   . ILE   A 274 ? 0.3710 0.3111 0.3411 -0.0885 -0.1037 0.0687  275 ILE   A C   
2285 O O   . ILE   A 274 ? 0.3668 0.3462 0.3667 -0.0959 -0.1131 0.0511  275 ILE   A O   
2286 C CB  . ILE   A 274 ? 0.2905 0.2744 0.2219 -0.0625 -0.0663 0.0737  275 ILE   A CB  
2287 C CG1 . ILE   A 274 ? 0.2631 0.2960 0.2123 -0.0716 -0.0424 0.0445  275 ILE   A CG1 
2288 C CG2 . ILE   A 274 ? 0.3026 0.2864 0.2232 -0.0401 -0.0705 0.0653  275 ILE   A CG2 
2289 C CD1 . ILE   A 274 ? 0.2954 0.3333 0.2138 -0.0403 0.0022  0.0307  275 ILE   A CD1 
2290 N N   . LYS   A 275 ? 0.4383 0.2941 0.3867 -0.1295 -0.1244 0.0589  276 LYS   A N   
2291 C CA  . LYS   A 275 ? 0.5473 0.3259 0.4694 -0.1695 -0.1251 0.0220  276 LYS   A CA  
2292 C C   . LYS   A 275 ? 0.6496 0.3921 0.5317 -0.2315 -0.1552 0.0223  276 LYS   A C   
2293 O O   . LYS   A 275 ? 0.6997 0.3963 0.5328 -0.2242 -0.1229 0.0476  276 LYS   A O   
2294 C CB  . LYS   A 275 ? 0.5525 0.3047 0.4897 -0.1468 -0.1073 -0.0281 276 LYS   A CB  
2295 C CG  . LYS   A 275 ? 0.5659 0.3032 0.5217 -0.1227 -0.0928 -0.0735 276 LYS   A CG  
2296 C CD  . LYS   A 275 ? 0.5891 0.3238 0.5532 -0.0605 -0.0804 -0.1063 276 LYS   A CD  
2297 C CE  . LYS   A 275 ? 0.6112 0.3544 0.5834 -0.0161 -0.0545 -0.1100 276 LYS   A CE  
2298 N NZ  . LYS   A 275 ? 0.6124 0.3924 0.5963 0.0191  -0.0449 -0.1056 276 LYS   A NZ  
2299 N N   . PRO   A 276 ? 0.7319 0.4712 0.5927 -0.2507 -0.1950 0.0075  277 PRO   A N   
2300 C CA  . PRO   A 276 ? 0.7910 0.5118 0.6223 -0.2433 -0.2062 0.0049  277 PRO   A CA  
2301 C C   . PRO   A 276 ? 0.8381 0.5234 0.6366 -0.2264 -0.2048 0.0135  277 PRO   A C   
2302 O O   . PRO   A 276 ? 0.8609 0.5289 0.6437 -0.2244 -0.1975 0.0243  277 PRO   A O   
2303 C CB  . PRO   A 276 ? 0.7981 0.5330 0.6265 -0.2305 -0.2170 0.0039  277 PRO   A CB  
2304 C CG  . PRO   A 276 ? 0.7718 0.5271 0.6241 -0.2466 -0.2207 -0.0011 277 PRO   A CG  
2305 C CD  . PRO   A 276 ? 0.7458 0.4963 0.6109 -0.2597 -0.2148 -0.0013 277 PRO   A CD  
2306 N N   . PRO   A 290 ? 0.9012 0.8421 0.6662 0.0884  -0.0942 -0.1928 291 PRO   A N   
2307 C CA  . PRO   A 290 ? 0.8727 0.8235 0.6670 0.0765  -0.0864 -0.1969 291 PRO   A CA  
2308 C C   . PRO   A 290 ? 0.8049 0.7582 0.6643 0.0526  -0.0630 -0.2140 291 PRO   A C   
2309 O O   . PRO   A 290 ? 0.8113 0.7748 0.6671 0.0475  -0.0589 -0.2225 291 PRO   A O   
2310 C CB  . PRO   A 290 ? 0.9046 0.8525 0.6710 0.0858  -0.0950 -0.1860 291 PRO   A CB  
2311 C CG  . PRO   A 290 ? 0.9190 0.8612 0.6681 0.0889  -0.1008 -0.1867 291 PRO   A CG  
2312 C CD  . PRO   A 290 ? 0.9202 0.8546 0.6667 0.0909  -0.1006 -0.1899 291 PRO   A CD  
2313 N N   . GLN   A 291 ? 0.7074 0.6544 0.6566 0.0364  -0.0442 -0.2277 292 GLN   A N   
2314 C CA  . GLN   A 291 ? 0.6144 0.5382 0.6487 0.0173  -0.0177 -0.2359 292 GLN   A CA  
2315 C C   . GLN   A 291 ? 0.5541 0.4726 0.6311 -0.0115 -0.0041 -0.2475 292 GLN   A C   
2316 O O   . GLN   A 291 ? 0.5047 0.4167 0.6278 -0.0142 0.0357  -0.2465 292 GLN   A O   
2317 C CB  . GLN   A 291 ? 0.5620 0.4800 0.6564 0.0273  -0.0086 -0.2267 292 GLN   A CB  
2318 C CG  . GLN   A 291 ? 0.4765 0.4194 0.6687 0.0233  0.0043  -0.2018 292 GLN   A CG  
2319 C CD  . GLN   A 291 ? 0.4022 0.3771 0.6739 0.0183  0.0149  -0.1756 292 GLN   A CD  
2320 O OE1 . GLN   A 291 ? 0.3974 0.3992 0.6700 0.0245  0.0044  -0.1603 292 GLN   A OE1 
2321 N NE2 . GLN   A 291 ? 0.3535 0.3389 0.6729 0.0239  0.0265  -0.1498 292 GLN   A NE2 
2322 N N   . PHE   A 292 ? 0.5453 0.4815 0.6201 -0.0109 -0.0223 -0.2370 293 PHE   A N   
2323 C CA  . PHE   A 292 ? 0.5569 0.4907 0.6181 0.0193  -0.0144 -0.2100 293 PHE   A CA  
2324 C C   . PHE   A 292 ? 0.6668 0.5538 0.6634 0.0243  -0.0173 -0.2177 293 PHE   A C   
2325 O O   . PHE   A 292 ? 0.6506 0.5633 0.6694 0.0351  -0.0231 -0.2111 293 PHE   A O   
2326 C CB  . PHE   A 292 ? 0.4929 0.4590 0.5777 0.0647  -0.0073 -0.1446 293 PHE   A CB  
2327 C CG  . PHE   A 292 ? 0.4245 0.4162 0.5402 0.0358  -0.0085 -0.0714 293 PHE   A CG  
2328 C CD1 . PHE   A 292 ? 0.3988 0.3931 0.5217 -0.0140 -0.0232 -0.0359 293 PHE   A CD1 
2329 C CD2 . PHE   A 292 ? 0.4058 0.4172 0.5260 0.0175  -0.0313 -0.0394 293 PHE   A CD2 
2330 C CE1 . PHE   A 292 ? 0.4145 0.3835 0.5078 -0.0121 -0.0120 -0.0130 293 PHE   A CE1 
2331 C CE2 . PHE   A 292 ? 0.3946 0.4035 0.5120 0.0049  -0.0241 -0.0237 293 PHE   A CE2 
2332 C CZ  . PHE   A 292 ? 0.4094 0.3860 0.5138 -0.0017 -0.0171 -0.0082 293 PHE   A CZ  
2333 N N   . GLU   A 293 ? 0.7480 0.5799 0.6932 0.0383  -0.0109 -0.2413 294 GLU   A N   
2334 C CA  . GLU   A 293 ? 0.8312 0.6059 0.7240 0.0404  -0.0170 -0.2519 294 GLU   A CA  
2335 C C   . GLU   A 293 ? 0.8772 0.6071 0.7372 0.0354  -0.0213 -0.2475 294 GLU   A C   
2336 O O   . GLU   A 293 ? 0.8936 0.5962 0.7376 0.0285  -0.0351 -0.2562 294 GLU   A O   
2337 C CB  . GLU   A 293 ? 0.8509 0.6282 0.7402 0.0622  -0.0186 -0.2587 294 GLU   A CB  
2338 C CG  . GLU   A 293 ? 0.8625 0.6420 0.7571 0.0869  -0.0325 -0.2622 294 GLU   A CG  
2339 C CD  . GLU   A 293 ? 0.8614 0.6464 0.7712 0.1214  -0.0462 -0.2674 294 GLU   A CD  
2340 O OE1 . GLU   A 293 ? 0.8832 0.6698 0.7882 0.1345  -0.0347 -0.2559 294 GLU   A OE1 
2341 O OE2 . GLU   A 293 ? 0.8341 0.6130 0.7599 0.1439  -0.0686 -0.2785 294 GLU   A OE2 
2347 C C2  . A1BVM C .   ? 0.3508 0.3013 0.3293 0.0576  -0.1094 -0.0312 302 A1BVM A C2  
2348 C C3  . A1BVM C .   ? 0.3774 0.3244 0.3665 0.0739  -0.1200 -0.0481 302 A1BVM A C3  
2349 C C4  . A1BVM C .   ? 0.4717 0.3683 0.4379 0.0773  -0.1693 -0.1017 302 A1BVM A C4  
2350 C C5  . A1BVM C .   ? 0.5250 0.3847 0.4604 0.0714  -0.1918 -0.1092 302 A1BVM A C5  
2351 C C6  . A1BVM C .   ? 0.7343 0.4691 0.5204 0.0723  -0.1994 -0.1025 302 A1BVM A C6  
2352 C C7  . A1BVM C .   ? 0.8100 0.4992 0.5394 0.0485  -0.1950 -0.1104 302 A1BVM A C7  
2353 C C8  . A1BVM C .   ? 0.8595 0.5309 0.5519 0.0271  -0.1865 -0.1153 302 A1BVM A C8  
2354 C C10 . A1BVM C .   ? 0.7998 0.5038 0.5387 0.0595  -0.1950 -0.1141 302 A1BVM A C10 
2355 C C17 . A1BVM C .   ? 0.3373 0.2771 0.2419 0.0230  -0.0601 0.0247  302 A1BVM A C17 
2356 C C16 . A1BVM C .   ? 0.3536 0.2678 0.2304 -0.0045 -0.0403 0.0149  302 A1BVM A C16 
2357 C C15 . A1BVM C .   ? 0.3383 0.2634 0.2491 0.0147  -0.0677 0.0176  302 A1BVM A C15 
2358 C C14 . A1BVM C .   ? 0.3577 0.2892 0.2591 0.0362  -0.0869 0.0329  302 A1BVM A C14 
2359 C C13 . A1BVM C .   ? 0.4082 0.3162 0.3235 0.0456  -0.0530 -0.0019 302 A1BVM A C13 
2360 C C12 . A1BVM C .   ? 0.4868 0.3686 0.4343 0.0689  -0.1786 -0.0920 302 A1BVM A C12 
2361 C C11 . A1BVM C .   ? 0.5196 0.3822 0.4545 0.0708  -0.1994 -0.1003 302 A1BVM A C11 
2362 C C1  . A1BVM C .   ? 0.3414 0.2886 0.2953 0.0582  -0.0780 0.0035  302 A1BVM A C1  
2363 N N   . A1BVM C .   ? 0.4384 0.3495 0.4139 0.0836  -0.1592 -0.0766 302 A1BVM A N   
2364 C C   . A1BVM C .   ? 0.3216 0.2537 0.2527 0.0409  -0.0691 0.0152  302 A1BVM A C   
2365 C C9  . A1BVM C .   ? 0.8485 0.5344 0.5465 0.0429  -0.1910 -0.1205 302 A1BVM A C9  
2366 N N1  . A1BVM C .   ? 0.5764 0.4002 0.4781 0.0857  -0.1984 -0.1031 302 A1BVM A N1  
2367 N N2  . A1BVM C .   ? 0.8806 0.5377 0.5530 0.0243  -0.1802 -0.1281 302 A1BVM A N2  
2368 N N3  . A1BVM C .   ? 0.3905 0.3254 0.3553 0.0836  -0.0743 -0.0330 302 A1BVM A N3  
2369 N N4  . A1BVM C .   ? 0.4138 0.3208 0.3361 0.0499  -0.0473 -0.0185 302 A1BVM A N4  
2370 N N5  . A1BVM C .   ? 0.3483 0.2638 0.2359 -0.0064 -0.0538 0.0219  302 A1BVM A N5  
2371 O O   . HOH   D .   ? 0.7546 0.4615 0.2319 -0.1598 -0.1022 0.0466  401 HOH   A O   
2374 O O   . HOH   D .   ? 0.6546 0.2006 0.2211 0.0467  -0.1242 -0.0239 403 HOH   A O   
2375 O O   . HOH   D .   ? 0.7867 0.2137 0.4296 -0.0272 0.1564  -0.0177 404 HOH   A O   
2376 O O   . HOH   D .   ? 0.8300 0.3699 0.2708 0.1630  0.0275  0.0783  405 HOH   A O   
2378 O O   . HOH   D .   ? 0.9211 0.6114 0.5639 -0.0506 -0.1121 0.3251  407 HOH   A O   
2379 O O   . HOH   D .   ? 0.5086 1.0074 0.3195 -0.3015 -0.0460 0.1339  408 HOH   A O   
2381 O O   . HOH   D .   ? 0.7245 0.6064 0.3448 0.2905  -0.1679 -0.1230 410 HOH   A O   
2383 O O   . HOH   D .   ? 0.4193 0.3950 0.2041 -0.0521 -0.0016 -0.1088 412 HOH   A O   
2384 O O   . HOH   D .   ? 0.4125 0.2948 0.1793 -0.0404 0.0020  -0.0467 413 HOH   A O   
2387 O O   . HOH   D .   ? 0.6059 0.6366 0.4437 0.2505  0.2412  0.2235  416 HOH   A O   
2388 O O   . HOH   D .   ? 0.3784 0.3496 0.2523 0.1332  -0.0610 -0.0075 417 HOH   A O   
2389 O O   . HOH   D .   ? 1.0768 0.4859 0.8008 -0.3264 0.1307  0.0758  418 HOH   A O   
2390 O O   . HOH   D .   ? 0.6778 0.4326 0.4779 -0.2067 0.2579  -0.2023 419 HOH   A O   
2391 O O   . HOH   D .   ? 0.2949 0.3651 0.6445 -0.0515 0.0970  -0.0251 420 HOH   A O   
2392 O O   . HOH   D .   ? 0.3971 0.2782 0.3337 -0.0384 -0.0414 0.0905  421 HOH   A O   
2393 O O   . HOH   D .   ? 0.4194 1.1524 0.5008 0.2306  -0.1222 -0.1650 422 HOH   A O   
2394 O O   . HOH   D .   ? 0.7544 0.3331 0.4050 0.1009  -0.2888 -0.0813 423 HOH   A O   
2395 O O   . HOH   D .   ? 0.3229 0.2139 0.2320 0.0406  -0.0605 -0.0161 424 HOH   A O   
2396 O O   . HOH   D .   ? 0.5468 0.3706 0.3013 -0.0958 0.0887  0.0880  425 HOH   A O   
2397 O O   . HOH   D .   ? 0.5993 0.8381 0.3297 0.3890  0.0268  -0.0281 426 HOH   A O   
2398 O O   . HOH   D .   ? 0.3301 0.2302 0.5757 -0.0210 -0.0825 0.0890  427 HOH   A O   
2399 O O   . HOH   D .   ? 0.5732 0.5071 0.4716 -0.1564 0.2447  -0.0897 428 HOH   A O   
2400 O O   . HOH   D .   ? 0.2299 0.2121 0.2853 -0.0045 -0.0112 0.0434  429 HOH   A O   
2401 O O   . HOH   D .   ? 0.3395 0.2314 0.2394 0.0110  -0.0148 0.0076  430 HOH   A O   
2402 O O   . HOH   D .   ? 0.8911 0.6287 0.3293 0.0570  0.0639  -0.1314 431 HOH   A O   
2403 O O   . HOH   D .   ? 0.3461 0.3836 0.9680 0.0121  0.1269  -0.1880 432 HOH   A O   
2405 O O   . HOH   D .   ? 0.4426 0.7101 0.4177 -0.2037 0.0210  0.0381  434 HOH   A O   
2406 O O   . HOH   D .   ? 0.2418 0.1871 0.2419 0.0002  -0.0203 -0.0239 435 HOH   A O   
2407 O O   . HOH   D .   ? 0.3686 0.4665 0.4417 -0.1231 -0.1258 0.0281  436 HOH   A O   
2409 O O   A HOH   D .   ? 0.3020 0.2033 0.1448 0.0370  0.0001  0.0184  438 HOH   A O   
2410 O O   B HOH   D .   ? 0.5605 0.2459 0.1667 0.0557  0.0834  0.0275  438 HOH   A O   
2411 O O   . HOH   D .   ? 0.4836 0.7629 0.4770 0.2911  0.1959  0.2934  439 HOH   A O   
2412 O O   . HOH   D .   ? 0.5960 0.6212 0.5405 0.2986  -0.2387 -0.2629 440 HOH   A O   
2413 O O   . HOH   D .   ? 0.4823 0.5846 0.5447 0.2188  -0.0486 -0.1189 441 HOH   A O   
2414 O O   . HOH   D .   ? 0.6655 0.3345 1.1408 0.0663  0.0264  -0.1551 442 HOH   A O   
2415 O O   . HOH   D .   ? 0.3198 0.3051 0.2443 -0.0312 0.0314  -0.0429 443 HOH   A O   
2416 O O   . HOH   D .   ? 0.4073 0.3751 0.2274 0.0379  0.0156  0.0379  444 HOH   A O   
2418 O O   . HOH   D .   ? 0.6751 0.5360 0.5165 -0.1913 0.2104  -0.2222 446 HOH   A O   
2419 O O   . HOH   D .   ? 0.7274 0.8560 0.3674 -0.1325 -0.0942 0.0497  447 HOH   A O   
2420 O O   . HOH   D .   ? 0.6633 0.5263 0.6412 0.2186  0.1567  -0.0152 448 HOH   A O   
2421 O O   . HOH   D .   ? 0.4434 0.2451 0.2853 0.0494  0.0442  -0.0340 449 HOH   A O   
2422 O O   . HOH   D .   ? 0.5460 0.7916 0.3838 0.3619  -0.0359 0.0419  450 HOH   A O   
2423 O O   . HOH   D .   ? 0.5431 0.2309 0.2741 0.0559  0.0022  -0.0584 451 HOH   A O   
2424 O O   . HOH   D .   ? 0.3767 0.3209 0.2579 0.0174  -0.0817 0.0051  452 HOH   A O   
2426 O O   . HOH   D .   ? 0.8292 0.3163 0.3791 -0.0431 -0.2333 0.0069  454 HOH   A O   
2427 O O   . HOH   D .   ? 0.6411 0.7655 0.3537 0.2066  -0.0694 0.1261  455 HOH   A O   
2428 O O   . HOH   D .   ? 0.2784 0.2156 0.1840 -0.0253 0.0268  -0.0512 456 HOH   A O   
2429 O O   . HOH   D .   ? 0.2727 0.2278 0.2273 0.0528  0.0349  0.0362  457 HOH   A O   
2430 O O   . HOH   D .   ? 0.3491 0.4181 0.3739 0.0785  -0.1178 -0.1541 458 HOH   A O   
2431 O O   . HOH   D .   ? 0.4317 0.1920 0.1418 -0.0928 -0.0115 0.0098  459 HOH   A O   
2432 O O   . HOH   D .   ? 0.3665 0.3601 0.2878 -0.1027 0.0230  0.0187  460 HOH   A O   
2433 O O   . HOH   D .   ? 0.7613 0.5393 0.2793 -0.0290 -0.1114 -0.1385 461 HOH   A O   
2434 O O   . HOH   D .   ? 0.6502 0.3501 0.4915 -0.0785 0.2047  -0.0733 462 HOH   A O   
2435 O O   . HOH   D .   ? 0.2821 0.2603 0.3868 0.0159  0.0276  0.1261  463 HOH   A O   
2437 O O   . HOH   D .   ? 0.5686 0.9033 0.2940 -0.3052 -0.0249 0.1004  465 HOH   A O   
2438 O O   . HOH   D .   ? 0.2682 0.2209 0.1640 0.0168  -0.0076 0.0413  466 HOH   A O   
2439 O O   . HOH   D .   ? 0.4265 0.3208 0.5833 -0.0314 0.2082  -0.1819 467 HOH   A O   
2440 O O   . HOH   D .   ? 0.4757 0.4649 0.3163 0.1578  0.0424  0.1261  468 HOH   A O   
2441 O O   . HOH   D .   ? 0.8538 0.7153 0.5081 0.1055  0.0528  0.1663  469 HOH   A O   
2442 O O   . HOH   D .   ? 0.3472 0.3400 0.3698 -0.0154 -0.0159 -0.0858 470 HOH   A O   
2444 O O   . HOH   D .   ? 0.3684 0.3605 0.2018 0.0204  0.0357  0.0241  472 HOH   A O   
2445 O O   . HOH   D .   ? 0.4240 0.3063 0.3135 -0.0191 -0.0458 0.0760  473 HOH   A O   
2446 O O   . HOH   D .   ? 0.2619 0.1718 0.1253 -0.0007 -0.0072 0.0036  474 HOH   A O   
2448 O O   . HOH   D .   ? 0.3176 0.2002 0.2346 -0.0147 0.0144  0.0150  476 HOH   A O   
2449 O O   . HOH   D .   ? 0.2388 0.1338 0.1419 -0.0032 0.0016  -0.0117 477 HOH   A O   
2450 O O   . HOH   D .   ? 0.2753 0.1664 0.1539 -0.0182 0.0303  -0.0140 478 HOH   A O   
2451 O O   . HOH   D .   ? 0.5285 0.7588 0.5415 0.0383  -0.0720 -0.3400 479 HOH   A O   
2452 O O   . HOH   D .   ? 0.5909 0.5274 0.3619 -0.1330 0.0852  0.0007  480 HOH   A O   
2453 O O   . HOH   D .   ? 0.4235 0.4011 0.2530 0.0609  0.0515  0.0041  481 HOH   A O   
2454 O O   . HOH   D .   ? 0.3006 0.6177 0.2012 -0.0180 0.0080  0.0213  482 HOH   A O   
2455 O O   . HOH   D .   ? 0.3801 0.2891 0.3629 0.0545  -0.0603 -0.1229 483 HOH   A O   
2456 O O   . HOH   D .   ? 0.7513 0.4109 0.2624 -0.0538 0.1257  0.0766  484 HOH   A O   
2457 O O   . HOH   D .   ? 0.8743 0.5640 0.6363 -0.2639 -0.4079 0.1852  485 HOH   A O   
2458 O O   . HOH   D .   ? 0.4246 0.9094 0.5584 0.1666  -0.0157 -0.2184 486 HOH   A O   
2459 O O   . HOH   D .   ? 0.4398 0.3534 0.3136 0.1595  0.0477  0.1130  487 HOH   A O   
2460 O O   . HOH   D .   ? 0.3402 0.2766 0.1827 -0.0449 -0.0259 0.0405  488 HOH   A O   
2461 O O   . HOH   D .   ? 0.2414 0.1792 0.1790 -0.0164 -0.0175 0.0117  489 HOH   A O   
2462 O O   . HOH   D .   ? 0.2547 0.3987 0.2836 0.0193  0.0000  0.0765  490 HOH   A O   
2463 O O   . HOH   D .   ? 0.6366 0.2532 0.5521 0.0544  0.3280  0.0171  491 HOH   A O   
2464 O O   . HOH   D .   ? 0.4937 0.2401 0.2968 0.0086  0.1642  0.0436  492 HOH   A O   
2466 O O   . HOH   D .   ? 0.8658 0.4448 0.3939 0.1393  -0.2434 -0.1350 494 HOH   A O   
2467 O O   . HOH   D .   ? 0.4017 0.5353 0.3022 0.1077  0.0108  0.0708  495 HOH   A O   
2468 O O   . HOH   D .   ? 0.4542 0.6621 0.4412 -0.1190 0.0672  0.2563  496 HOH   A O   
2469 O O   . HOH   D .   ? 0.4046 0.4286 0.3251 -0.0547 0.0360  -0.0130 497 HOH   A O   
2470 O O   . HOH   D .   ? 0.2812 0.6123 0.4769 -0.1119 0.0772  -0.2285 498 HOH   A O   
2471 O O   . HOH   D .   ? 0.2232 0.1565 0.1464 0.0210  -0.0164 0.0177  499 HOH   A O   
2472 O O   . HOH   D .   ? 0.3471 0.5872 0.3430 -0.0672 -0.0793 0.1286  500 HOH   A O   
2473 O O   . HOH   D .   ? 0.2616 0.5935 0.3254 -0.0814 0.0520  -0.2332 501 HOH   A O   
2474 O O   . HOH   D .   ? 0.3359 0.2506 0.2145 -0.0212 0.0283  0.0465  502 HOH   A O   
2475 O O   . HOH   D .   ? 0.3309 0.3049 0.2397 0.0112  -0.0239 0.0023  503 HOH   A O   
2476 O O   . HOH   D .   ? 0.8026 0.4384 0.3086 0.2219  -0.1165 0.0051  504 HOH   A O   
2477 O O   . HOH   D .   ? 0.2354 0.1627 0.1472 -0.0136 -0.0135 -0.0026 505 HOH   A O   
2478 O O   . HOH   D .   ? 0.5445 0.3586 0.2828 0.1604  0.1230  0.1380  506 HOH   A O   
2479 O O   . HOH   D .   ? 0.3424 0.2524 0.5087 -0.0034 0.0619  0.0494  507 HOH   A O   
2480 O O   . HOH   D .   ? 1.0040 0.4467 0.4201 0.0094  0.1333  -0.1593 508 HOH   A O   
2481 O O   . HOH   D .   ? 0.5563 0.4941 0.4980 0.0720  -0.0700 -0.2231 509 HOH   A O   
2482 O O   . HOH   D .   ? 0.5607 0.6580 0.4306 -0.2673 -0.0712 0.1035  510 HOH   A O   
2483 O O   . HOH   D .   ? 0.4472 0.2320 0.2887 -0.0432 -0.0425 -0.0175 511 HOH   A O   
2484 O O   . HOH   D .   ? 0.5158 0.2607 0.5942 0.0117  0.1995  -0.1099 512 HOH   A O   
2485 O O   . HOH   D .   ? 0.5679 0.7951 0.3717 -0.3024 -0.1323 0.2023  513 HOH   A O   
2486 O O   . HOH   D .   ? 0.4195 0.4696 0.6148 -0.1516 -0.1957 0.2130  514 HOH   A O   
2487 O O   . HOH   D .   ? 0.2574 0.4536 0.4495 -0.0171 -0.0445 0.2576  515 HOH   A O   
2488 O O   . HOH   D .   ? 0.2494 0.2545 0.2247 0.0242  -0.0147 0.1190  516 HOH   A O   
2489 O O   . HOH   D .   ? 0.4085 0.4258 0.7403 0.0762  -0.1284 -0.3035 517 HOH   A O   
2490 O O   . HOH   D .   ? 0.3029 0.3960 0.2579 0.0040  -0.0760 -0.0002 518 HOH   A O   
2491 O O   . HOH   D .   ? 0.6098 0.5687 0.5899 -0.1682 -0.1556 0.3218  519 HOH   A O   
2492 O O   . HOH   D .   ? 0.4879 0.7339 0.3243 -0.2616 0.0020  0.0640  520 HOH   A O   
2493 O O   . HOH   D .   ? 0.3668 0.3012 0.3179 -0.0649 0.0738  -0.1062 521 HOH   A O   
2494 O O   . HOH   D .   ? 0.2999 0.2908 0.4018 -0.0709 0.1152  -0.1757 522 HOH   A O   
2495 O O   . HOH   D .   ? 0.3672 0.2218 0.1897 0.0523  0.0332  0.0118  523 HOH   A O   
2496 O O   . HOH   D .   ? 0.5851 0.3681 0.2438 0.1592  -0.0403 0.0039  524 HOH   A O   
2498 O O   A HOH   D .   ? 0.3368 0.2367 0.4400 0.0436  -0.0824 0.1089  526 HOH   A O   
2499 O O   B HOH   D .   ? 0.5540 0.1669 0.2811 -0.0124 0.1505  0.0233  526 HOH   A O   
2500 O O   . HOH   D .   ? 0.3229 0.3332 0.4536 0.0878  0.0681  -0.0696 527 HOH   A O   
2501 O O   . HOH   D .   ? 0.7036 0.3258 0.4222 -0.1664 0.1316  0.0738  528 HOH   A O   
2502 O O   . HOH   D .   ? 0.3420 0.4030 0.3155 0.0501  0.0585  -0.0164 529 HOH   A O   
2503 O O   . HOH   D .   ? 0.4089 0.2969 0.2799 -0.0792 0.0285  -0.0008 530 HOH   A O   
2504 O O   . HOH   D .   ? 0.5511 0.2496 0.2351 -0.0482 -0.0177 0.0698  531 HOH   A O   
2505 O O   . HOH   D .   ? 0.3665 0.2713 0.2179 -0.0562 -0.0150 -0.0340 532 HOH   A O   
2506 O O   . HOH   D .   ? 0.4498 0.2711 0.5561 -0.0113 -0.2408 0.0185  533 HOH   A O   
2507 O O   . HOH   D .   ? 0.5134 1.1353 0.5334 0.0919  0.2229  0.1399  534 HOH   A O   
2508 O O   . HOH   D .   ? 0.3126 0.3796 0.2536 0.0608  -0.0487 -0.0031 535 HOH   A O   
2509 O O   . HOH   D .   ? 0.3811 0.6494 0.8930 0.0722  -0.1634 -0.2232 536 HOH   A O   
2510 O O   . HOH   D .   ? 0.5120 0.6752 0.4390 0.2664  -0.0694 -0.1432 537 HOH   A O   
2511 O O   . HOH   D .   ? 0.3257 0.4878 0.4000 -0.0173 -0.0267 -0.0226 538 HOH   A O   
2512 O O   . HOH   D .   ? 0.7949 0.4566 0.2496 -0.2367 0.0159  -0.0565 539 HOH   A O   
2513 O O   . HOH   D .   ? 1.2450 0.5288 0.3902 -0.3892 -0.0826 0.0440  540 HOH   A O   
2514 O O   . HOH   D .   ? 0.3548 0.2686 0.2058 -0.0480 0.0075  0.0073  541 HOH   A O   
2515 O O   . HOH   D .   ? 0.5022 0.1791 0.3069 0.0872  -0.0207 0.0564  542 HOH   A O   
2516 O O   . HOH   D .   ? 0.5684 0.7894 0.4864 0.0983  -0.0703 0.3157  543 HOH   A O   
2517 O O   . HOH   D .   ? 0.8445 0.3852 0.2672 0.1316  -0.1104 -0.0764 544 HOH   A O   
2518 O O   . HOH   D .   ? 0.3716 0.3557 0.3856 0.1455  0.0112  0.1457  545 HOH   A O   
2519 O O   . HOH   D .   ? 0.2529 0.1588 0.2179 -0.0012 -0.0258 -0.0390 546 HOH   A O   
2520 O O   . HOH   D .   ? 0.4135 0.6225 0.3217 -0.1351 0.0649  0.0413  547 HOH   A O   
2521 O O   . HOH   D .   ? 0.3316 0.2380 0.2832 -0.0243 0.1063  -0.0841 548 HOH   A O   
2522 O O   . HOH   D .   ? 0.3391 1.1545 0.3545 -0.1574 -0.0411 0.1448  549 HOH   A O   
2523 O O   . HOH   D .   ? 0.6691 0.2680 0.3207 -0.1156 0.0019  0.0899  550 HOH   A O   
2524 O O   . HOH   D .   ? 0.2649 0.7443 0.6539 0.0899  0.0614  0.2221  551 HOH   A O   
2525 O O   . HOH   D .   ? 0.3076 1.0688 0.3948 0.0208  0.0134  0.1359  552 HOH   A O   
2526 O O   . HOH   D .   ? 0.7616 0.4030 0.8083 0.0446  -0.1768 0.2526  553 HOH   A O   
2527 O O   . HOH   D .   ? 0.2751 0.3128 0.5262 -0.0416 -0.0374 0.0609  554 HOH   A O   
2529 O O   . HOH   D .   ? 0.5773 0.5379 0.4214 -0.0323 -0.1339 -0.0167 556 HOH   A O   
2530 O O   . HOH   D .   ? 0.3985 0.3317 0.2136 -0.0184 -0.0285 0.0402  557 HOH   A O   
2531 O O   . HOH   D .   ? 0.3410 0.2993 0.2102 -0.0226 -0.0130 -0.0216 558 HOH   A O   
2532 O O   . HOH   D .   ? 0.5216 1.0637 0.4796 -0.2793 0.0782  0.1024  559 HOH   A O   
2533 O O   . HOH   D .   ? 0.8250 0.3041 0.9510 -0.0059 -0.0640 -0.1839 560 HOH   A O   
2534 O O   . HOH   D .   ? 0.3897 0.5071 0.6119 0.1821  -0.1574 -0.2907 561 HOH   A O   
2535 O O   . HOH   D .   ? 0.3089 0.4755 0.3387 0.0235  -0.0434 0.1132  562 HOH   A O   
2536 O O   . HOH   D .   ? 0.4318 0.2368 0.2883 0.0672  0.0737  0.0079  563 HOH   A O   
2537 O O   . HOH   D .   ? 0.8975 0.3730 0.6351 -0.1297 0.2050  0.0117  564 HOH   A O   
2538 O O   . HOH   D .   ? 0.6041 0.7271 0.2856 0.1623  0.0361  0.0340  565 HOH   A O   
2540 O O   . HOH   D .   ? 0.4447 0.2100 0.2555 -0.0225 0.0470  0.0242  567 HOH   A O   
2541 O O   . HOH   D .   ? 0.5362 0.2407 0.3185 -0.0275 0.1049  -0.0577 568 HOH   A O   
2543 O O   . HOH   D .   ? 0.3337 0.2880 0.2800 -0.0159 0.0305  0.0695  570 HOH   A O   
2544 O O   . HOH   D .   ? 0.2661 0.4994 0.7814 0.0201  -0.0231 -0.3559 571 HOH   A O   
2545 O O   . HOH   D .   ? 0.5737 0.5116 0.6700 -0.1585 0.1381  -0.2439 572 HOH   A O   
2546 O O   . HOH   D .   ? 0.4124 0.4153 0.3351 -0.1192 -0.1066 0.0290  573 HOH   A O   
2547 O O   . HOH   D .   ? 0.4728 0.6956 1.3455 -0.1425 -0.1224 0.1950  574 HOH   A O   
2548 O O   A HOH   D .   ? 0.2798 0.3054 0.5445 -0.1063 -0.1726 0.1269  575 HOH   A O   
2549 O O   B HOH   D .   ? 0.1874 0.2942 0.3745 0.0312  0.0442  0.1946  575 HOH   A O   
2550 O O   . HOH   D .   ? 0.2608 0.9135 0.5194 -0.0411 0.0012  -0.2396 576 HOH   A O   
2551 O O   . HOH   D .   ? 0.3410 0.3669 0.2843 0.0121  0.0160  -0.0361 577 HOH   A O   
2552 O O   . HOH   D .   ? 0.3534 0.7992 0.5303 -0.0813 0.0154  -0.3070 578 HOH   A O   
2553 O O   . HOH   D .   ? 0.5634 0.9207 0.4271 -0.1965 -0.0564 0.2474  579 HOH   A O   
2556 O O   . HOH   D .   ? 0.6906 0.9237 0.2871 0.1928  0.0588  -0.0824 582 HOH   A O   
2557 O O   . HOH   D .   ? 0.4193 0.3896 0.4700 0.0272  -0.1062 -0.1196 583 HOH   A O   
2558 O O   . HOH   D .   ? 0.3648 0.1823 0.2037 -0.0004 0.0745  0.0109  584 HOH   A O   
2559 O O   . HOH   D .   ? 0.4472 0.6549 0.9333 -0.0443 -0.1618 -0.1484 585 HOH   A O   
2560 O O   . HOH   D .   ? 0.4489 0.7435 0.4415 0.2565  0.1143  0.2298  586 HOH   A O   
2561 O O   . HOH   D .   ? 0.8572 0.7917 0.7881 0.0427  -0.4793 -0.1116 587 HOH   A O   
2562 O O   . HOH   D .   ? 0.8923 0.8815 0.3359 -0.2683 -0.0546 0.0150  588 HOH   A O   
2563 O O   . HOH   D .   ? 0.3483 0.2048 0.3031 0.0482  -0.0070 0.0219  589 HOH   A O   
2564 O O   . HOH   D .   ? 0.7797 0.8372 0.5485 0.1962  0.2419  0.3254  590 HOH   A O   
2566 O O   . HOH   D .   ? 0.5649 0.5371 0.4798 0.1949  0.1916  0.1953  592 HOH   A O   
2567 O O   . HOH   D .   ? 0.3901 0.8249 0.4404 -0.1155 -0.0553 0.3207  593 HOH   A O   
2568 O O   . HOH   D .   ? 0.5430 0.4908 0.7605 0.1346  0.3224  0.2707  594 HOH   A O   
2569 O O   . HOH   D .   ? 0.5808 0.4052 1.0537 0.1019  -0.0962 -0.2034 595 HOH   A O   
2570 O O   . HOH   D .   ? 0.3774 0.5002 0.3597 -0.0293 0.1547  -0.1237 596 HOH   A O   
2571 O O   . HOH   D .   ? 1.2951 0.4584 0.5478 0.0964  0.1913  0.0062  597 HOH   A O   
2573 O O   . HOH   D .   ? 0.7878 0.6932 0.6633 0.1601  -0.0478 -0.3466 599 HOH   A O   
2574 O O   . HOH   D .   ? 0.2364 0.1636 0.1851 -0.0154 0.0119  -0.0174 600 HOH   A O   
2575 O O   . HOH   D .   ? 0.3718 0.3666 0.4236 0.0258  -0.0844 -0.1169 601 HOH   A O   
2576 O O   . HOH   D .   ? 0.9081 0.4576 0.8904 0.0848  -0.2163 0.2622  602 HOH   A O   
2577 O O   . HOH   D .   ? 0.6436 0.3579 1.0069 0.0289  -0.1281 0.0384  603 HOH   A O   
2578 O O   . HOH   D .   ? 0.6810 0.5638 1.0021 -0.0224 -0.3427 -0.2701 604 HOH   A O   
2579 O O   . HOH   D .   ? 0.5471 0.4870 0.2992 0.1704  0.0448  -0.0216 605 HOH   A O   
2581 O O   . HOH   D .   ? 0.4671 0.1970 0.3118 -0.0225 0.0499  -0.0972 607 HOH   A O   
2582 O O   . HOH   D .   ? 0.4069 0.7319 0.3276 -0.0931 0.0961  -0.1914 608 HOH   A O   
2583 O O   . HOH   D .   ? 0.5119 0.4545 0.2292 0.0128  -0.0763 0.0234  609 HOH   A O   
2584 O O   . HOH   D .   ? 0.6175 0.5047 0.3771 -0.0872 0.0087  -0.1852 610 HOH   A O   
2585 O O   . HOH   D .   ? 0.6382 0.6684 0.5764 0.3517  -0.0627 0.0516  611 HOH   A O   
2586 O O   . HOH   D .   ? 0.5562 0.7936 0.6798 -0.3549 0.0350  -0.1941 612 HOH   A O   
2587 O O   . HOH   D .   ? 0.3098 0.2460 0.3010 -0.0736 0.0579  -0.0633 613 HOH   A O   
2588 O O   . HOH   D .   ? 0.8405 0.8186 0.3920 -0.2787 0.0209  -0.0723 614 HOH   A O   
2589 O O   . HOH   D .   ? 0.6056 0.5009 0.9191 -0.0197 -0.3859 -0.1176 615 HOH   A O   
2590 O O   . HOH   D .   ? 0.3516 0.4651 0.5955 -0.0470 -0.0319 0.0481  616 HOH   A O   
2591 O O   . HOH   D .   ? 0.5465 0.4547 0.6461 0.0933  0.0969  0.1386  617 HOH   A O   
2592 O O   . HOH   D .   ? 0.4473 0.9651 0.6129 0.2470  -0.1354 -0.2431 618 HOH   A O   
2593 O O   . HOH   D .   ? 0.4768 1.1639 0.4960 0.1059  0.1532  0.1504  619 HOH   A O   
2594 O O   . HOH   D .   ? 0.8855 0.3427 0.8429 -0.0099 0.4720  -0.0376 620 HOH   A O   
2595 O O   . HOH   D .   ? 0.5140 0.2941 0.3465 0.1247  -0.1630 -0.0603 621 HOH   A O   
2596 O O   . HOH   D .   ? 0.3339 0.2096 0.2546 0.0088  0.0506  -0.0667 622 HOH   A O   
2597 O O   . HOH   D .   ? 0.7105 0.4165 0.3395 0.1607  0.1036  0.0229  623 HOH   A O   
2598 O O   . HOH   D .   ? 0.3099 0.2877 0.2456 0.0937  0.0673  0.0652  624 HOH   A O   
2599 O O   . HOH   D .   ? 0.3459 0.6795 0.9851 -0.0411 0.0451  0.1605  625 HOH   A O   
2600 O O   . HOH   D .   ? 0.5627 0.5452 0.6073 -0.0688 -0.2629 0.0250  626 HOH   A O   
2602 O O   . HOH   D .   ? 0.8787 0.4531 0.5033 -0.1630 -0.1710 0.1575  628 HOH   A O   
2603 O O   . HOH   D .   ? 0.9486 0.5894 0.6372 0.2706  -0.2314 -0.1468 629 HOH   A O   
2604 O O   . HOH   D .   ? 0.3769 0.9303 0.3676 0.1068  0.0793  -0.0039 630 HOH   A O   
2605 O O   . HOH   D .   ? 0.6319 0.6204 0.6161 -0.2320 -0.0832 0.1692  631 HOH   A O   
2606 O O   . HOH   D .   ? 0.4292 0.4816 0.2661 0.1240  -0.0231 0.1085  632 HOH   A O   
# 
