data_9N1S
# 
_entry.id   9N1S 
# 
_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   9N1S         pdb_00009n1s 10.2210/pdb9n1s/pdb 
WWPDB D_1000291319 ?            ?                   
# 
_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       2025-04-30 
_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                        9N1S 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9BWA 
_pdbx_database_related.content_type   unspecified 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 swlovell@ku.edu       Scott Lovell           ? 'principal investigator/group leader' 0000-0002-3215-4472 
3 lina.gonzalez@chp.edu Lina  Ghaloul-Gonzalez ? 'principal investigator/group leader' 0000-0001-7697-2672 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lovell, S.'           1 0000-0002-3215-4472 
'Cooper, A.'           2 0000-0002-1893-4149 
'Powers, A.'           3 0009-0003-3653-6165 
'Battaile, K.P.'       4 0000-0003-0833-3259 
'Moshen, A.W.'         5 0000-0002-0096-5959 
'Ghaloul-Gonzalez, L.' 6 0000-0001-7697-2672 
# 
_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 the Transport and Golgi Organization protein 2 Homolog (TANGO2)' 
_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 'Lovell, S.'           1 0000-0002-3215-4472 
primary 'Ghaloul-Gonzalez, L.' 2 0000-0001-7697-2672 
# 
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 'Transport and Golgi organization protein 2 homolog' 31844.932 1  ? ? ? ? 
2 non-polymer syn 'PHOSPHATE ION'                                      94.971    1  ? ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                       35.453    1  ? ? ? ? 
4 water       nat water                                                18.015    56 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;M(OCS)IIFFKFDPRPVSKNAYRLILAANRDEFYSRPSKLADFWGNNNEILSGLDMEEGKEGGTWLGISTRGKLAALTNY
LQPQLDWQARGRGELVTHFLTTDVDSLSYLKKVSMEGHLYNGFNLIAADLSTAKGDVICYYGNRGEPDPIVLTPGTYGLS
NALLETPWRKLCFGKQLFLEAVERSQALPKDVLIASLLDVLNNEEAQLPDPAIEDQGGEYVQPMLSKYAAVCVRCPGYGT
RTNTIILVDADGHVTFTERSMMDKDLSHWETRTYEFTLQSHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MCIIFFKFDPRPVSKNAYRLILAANRDEFYSRPSKLADFWGNNNEILSGLDMEEGKEGGTWLGISTRGKLAALTNYLQPQ
LDWQARGRGELVTHFLTTDVDSLSYLKKVSMEGHLYNGFNLIAADLSTAKGDVICYYGNRGEPDPIVLTPGTYGLSNALL
ETPWRKLCFGKQLFLEAVERSQALPKDVLIASLLDVLNNEEAQLPDPAIEDQGGEYVQPMLSKYAAVCVRCPGYGTRTNT
IILVDADGHVTFTERSMMDKDLSHWETRTYEFTLQSHHHHHH
;
_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 'PHOSPHATE ION' PO4 
3 'CHLORIDE ION'  CL  
4 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   OCS n 
1 3   ILE n 
1 4   ILE n 
1 5   PHE n 
1 6   PHE n 
1 7   LYS n 
1 8   PHE n 
1 9   ASP n 
1 10  PRO n 
1 11  ARG n 
1 12  PRO n 
1 13  VAL n 
1 14  SER n 
1 15  LYS n 
1 16  ASN n 
1 17  ALA n 
1 18  TYR n 
1 19  ARG n 
1 20  LEU n 
1 21  ILE n 
1 22  LEU n 
1 23  ALA n 
1 24  ALA n 
1 25  ASN n 
1 26  ARG n 
1 27  ASP n 
1 28  GLU n 
1 29  PHE n 
1 30  TYR n 
1 31  SER n 
1 32  ARG n 
1 33  PRO n 
1 34  SER n 
1 35  LYS n 
1 36  LEU n 
1 37  ALA n 
1 38  ASP n 
1 39  PHE n 
1 40  TRP n 
1 41  GLY n 
1 42  ASN n 
1 43  ASN n 
1 44  ASN n 
1 45  GLU n 
1 46  ILE n 
1 47  LEU n 
1 48  SER n 
1 49  GLY n 
1 50  LEU n 
1 51  ASP n 
1 52  MET n 
1 53  GLU n 
1 54  GLU n 
1 55  GLY n 
1 56  LYS n 
1 57  GLU n 
1 58  GLY n 
1 59  GLY n 
1 60  THR n 
1 61  TRP n 
1 62  LEU n 
1 63  GLY n 
1 64  ILE n 
1 65  SER n 
1 66  THR n 
1 67  ARG n 
1 68  GLY n 
1 69  LYS n 
1 70  LEU n 
1 71  ALA n 
1 72  ALA n 
1 73  LEU n 
1 74  THR n 
1 75  ASN n 
1 76  TYR n 
1 77  LEU n 
1 78  GLN n 
1 79  PRO n 
1 80  GLN n 
1 81  LEU n 
1 82  ASP n 
1 83  TRP n 
1 84  GLN n 
1 85  ALA n 
1 86  ARG n 
1 87  GLY n 
1 88  ARG n 
1 89  GLY n 
1 90  GLU n 
1 91  LEU n 
1 92  VAL n 
1 93  THR n 
1 94  HIS n 
1 95  PHE n 
1 96  LEU n 
1 97  THR n 
1 98  THR n 
1 99  ASP n 
1 100 VAL n 
1 101 ASP n 
1 102 SER n 
1 103 LEU n 
1 104 SER n 
1 105 TYR n 
1 106 LEU n 
1 107 LYS n 
1 108 LYS n 
1 109 VAL n 
1 110 SER n 
1 111 MET n 
1 112 GLU n 
1 113 GLY n 
1 114 HIS n 
1 115 LEU n 
1 116 TYR n 
1 117 ASN n 
1 118 GLY n 
1 119 PHE n 
1 120 ASN n 
1 121 LEU n 
1 122 ILE n 
1 123 ALA n 
1 124 ALA n 
1 125 ASP n 
1 126 LEU n 
1 127 SER n 
1 128 THR n 
1 129 ALA n 
1 130 LYS n 
1 131 GLY n 
1 132 ASP n 
1 133 VAL n 
1 134 ILE n 
1 135 CYS n 
1 136 TYR n 
1 137 TYR n 
1 138 GLY n 
1 139 ASN n 
1 140 ARG n 
1 141 GLY n 
1 142 GLU n 
1 143 PRO n 
1 144 ASP n 
1 145 PRO n 
1 146 ILE n 
1 147 VAL n 
1 148 LEU n 
1 149 THR n 
1 150 PRO n 
1 151 GLY n 
1 152 THR n 
1 153 TYR n 
1 154 GLY n 
1 155 LEU n 
1 156 SER n 
1 157 ASN n 
1 158 ALA n 
1 159 LEU n 
1 160 LEU n 
1 161 GLU n 
1 162 THR n 
1 163 PRO n 
1 164 TRP n 
1 165 ARG n 
1 166 LYS n 
1 167 LEU n 
1 168 CYS n 
1 169 PHE n 
1 170 GLY n 
1 171 LYS n 
1 172 GLN n 
1 173 LEU n 
1 174 PHE n 
1 175 LEU n 
1 176 GLU n 
1 177 ALA n 
1 178 VAL n 
1 179 GLU n 
1 180 ARG n 
1 181 SER n 
1 182 GLN n 
1 183 ALA n 
1 184 LEU n 
1 185 PRO n 
1 186 LYS n 
1 187 ASP n 
1 188 VAL n 
1 189 LEU n 
1 190 ILE n 
1 191 ALA n 
1 192 SER n 
1 193 LEU n 
1 194 LEU n 
1 195 ASP n 
1 196 VAL n 
1 197 LEU n 
1 198 ASN n 
1 199 ASN n 
1 200 GLU n 
1 201 GLU n 
1 202 ALA n 
1 203 GLN n 
1 204 LEU n 
1 205 PRO n 
1 206 ASP n 
1 207 PRO n 
1 208 ALA n 
1 209 ILE n 
1 210 GLU n 
1 211 ASP n 
1 212 GLN n 
1 213 GLY n 
1 214 GLY n 
1 215 GLU n 
1 216 TYR n 
1 217 VAL n 
1 218 GLN n 
1 219 PRO n 
1 220 MET n 
1 221 LEU n 
1 222 SER n 
1 223 LYS n 
1 224 TYR n 
1 225 ALA n 
1 226 ALA n 
1 227 VAL n 
1 228 CYS n 
1 229 VAL n 
1 230 ARG n 
1 231 CYS n 
1 232 PRO n 
1 233 GLY n 
1 234 TYR n 
1 235 GLY n 
1 236 THR n 
1 237 ARG n 
1 238 THR n 
1 239 ASN n 
1 240 THR n 
1 241 ILE n 
1 242 ILE n 
1 243 LEU n 
1 244 VAL n 
1 245 ASP n 
1 246 ALA n 
1 247 ASP n 
1 248 GLY n 
1 249 HIS n 
1 250 VAL n 
1 251 THR n 
1 252 PHE n 
1 253 THR n 
1 254 GLU n 
1 255 ARG n 
1 256 SER n 
1 257 MET n 
1 258 MET n 
1 259 ASP n 
1 260 LYS n 
1 261 ASP n 
1 262 LEU n 
1 263 SER n 
1 264 HIS n 
1 265 TRP n 
1 266 GLU n 
1 267 THR n 
1 268 ARG n 
1 269 THR n 
1 270 TYR n 
1 271 GLU n 
1 272 PHE n 
1 273 THR n 
1 274 LEU n 
1 275 GLN n 
1 276 SER n 
1 277 HIS n 
1 278 HIS n 
1 279 HIS n 
1 280 HIS n 
1 281 HIS n 
1 282 HIS 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                   282 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TANGO2, C22orf25' 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_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                       'pET-27b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                 ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE              ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'         ? 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'          ? 'Cl -1'          35.453  
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 
OCS 'L-peptide linking' n 'CYSTEINESULFONIC ACID' ? 'C3 H7 N O5 S'   169.156 
PHE 'L-peptide linking' y PHENYLALANINE           ? 'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION'         ? 'O4 P -3'        94.971  
PRO 'L-peptide linking' y PROLINE                 ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                  ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE               ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN              ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                  ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   OCS 2   2   2   OCS OCS A . n 
A 1 3   ILE 3   3   3   ILE ILE A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   PHE 5   5   5   PHE PHE A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   ASP 9   9   9   ASP ASP A . n 
A 1 10  PRO 10  10  10  PRO PRO A . n 
A 1 11  ARG 11  11  11  ARG ARG A . n 
A 1 12  PRO 12  12  12  PRO PRO A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  TYR 18  18  18  TYR TYR A . n 
A 1 19  ARG 19  19  19  ARG ARG A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  ASN 25  25  25  ASN ASN A . n 
A 1 26  ARG 26  26  26  ARG ARG A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  PHE 29  29  29  PHE PHE A . n 
A 1 30  TYR 30  30  30  TYR TYR A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  ARG 32  32  32  ARG ARG A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  TRP 40  40  40  TRP TRP A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  ASN 42  42  42  ASN ASN A . n 
A 1 43  ASN 43  43  43  ASN ASN A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  MET 52  52  52  MET MET A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  GLY 58  58  58  GLY GLY A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  TRP 61  61  61  TRP TRP A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  GLN 78  78  78  GLN GLN A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  GLN 80  80  80  GLN GLN A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  TRP 83  83  83  TRP TRP A . n 
A 1 84  GLN 84  84  84  GLN GLN A . n 
A 1 85  ALA 85  85  85  ALA ALA A . n 
A 1 86  ARG 86  86  86  ARG ARG A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 SER 110 110 110 SER SER A . n 
A 1 111 MET 111 111 111 MET MET A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 HIS 114 114 114 HIS HIS A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 ASN 120 120 120 ASN ASN A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 LYS 130 130 130 LYS LYS A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 CYS 135 135 135 CYS CYS A . n 
A 1 136 TYR 136 136 136 TYR TYR A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ARG 140 140 140 ARG ARG A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 GLU 142 142 142 GLU GLU A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 PRO 145 145 145 PRO PRO A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 PRO 150 150 150 PRO PRO A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 TYR 153 153 153 TYR TYR A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 ASN 157 157 157 ASN ASN A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 PRO 163 163 163 PRO PRO A . n 
A 1 164 TRP 164 164 164 TRP TRP A . n 
A 1 165 ARG 165 165 165 ARG ARG A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 CYS 168 168 168 CYS CYS A . n 
A 1 169 PHE 169 169 169 PHE PHE A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 GLN 172 172 172 GLN GLN A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 PHE 174 174 174 PHE PHE A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 GLU 176 176 176 GLU GLU A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 GLU 179 179 179 GLU GLU A . n 
A 1 180 ARG 180 180 180 ARG ARG A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 GLN 182 182 182 GLN GLN A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 LYS 186 186 186 LYS LYS A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 LEU 194 194 194 LEU LEU A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 VAL 196 196 196 VAL VAL A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 ASN 198 198 198 ASN ASN A . n 
A 1 199 ASN 199 199 199 ASN ASN A . n 
A 1 200 GLU 200 200 200 GLU GLU A . n 
A 1 201 GLU 201 201 201 GLU GLU A . n 
A 1 202 ALA 202 202 202 ALA ALA A . n 
A 1 203 GLN 203 203 203 GLN GLN A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 ASP 206 206 206 ASP ASP A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 ASP 211 211 211 ASP ASP A . n 
A 1 212 GLN 212 212 212 GLN GLN A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 TYR 216 216 216 TYR TYR A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 PRO 219 219 219 PRO PRO A . n 
A 1 220 MET 220 220 220 MET MET A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 LYS 223 223 223 LYS LYS A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 VAL 227 227 227 VAL VAL A . n 
A 1 228 CYS 228 228 228 CYS CYS A . n 
A 1 229 VAL 229 229 229 VAL VAL A . n 
A 1 230 ARG 230 230 230 ARG ARG A . n 
A 1 231 CYS 231 231 231 CYS CYS A . n 
A 1 232 PRO 232 232 232 PRO PRO A . n 
A 1 233 GLY 233 233 233 GLY GLY A . n 
A 1 234 TYR 234 234 234 TYR TYR A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 THR 236 236 236 THR THR A . n 
A 1 237 ARG 237 237 237 ARG ARG A . n 
A 1 238 THR 238 238 238 THR THR A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 THR 240 240 240 THR THR A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 ILE 242 242 242 ILE ILE A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ASP 247 247 247 ASP ASP A . n 
A 1 248 GLY 248 248 248 GLY GLY A . n 
A 1 249 HIS 249 249 249 HIS HIS A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 THR 251 251 251 THR THR A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 THR 253 253 253 THR THR A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 MET 257 257 257 MET MET A . n 
A 1 258 MET 258 258 258 MET MET A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 HIS 264 264 264 HIS HIS A . n 
A 1 265 TRP 265 265 265 TRP TRP A . n 
A 1 266 GLU 266 266 266 GLU GLU A . n 
A 1 267 THR 267 267 267 THR THR A . n 
A 1 268 ARG 268 268 268 ARG ARG A . n 
A 1 269 THR 269 269 269 THR THR A . n 
A 1 270 TYR 270 270 270 TYR TYR A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 PHE 272 272 272 PHE PHE A . n 
A 1 273 THR 273 273 273 THR THR A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 GLN 275 275 275 GLN GLN A . n 
A 1 276 SER 276 276 ?   ?   ?   A . n 
A 1 277 HIS 277 277 ?   ?   ?   A . n 
A 1 278 HIS 278 278 ?   ?   ?   A . n 
A 1 279 HIS 279 279 ?   ?   ?   A . n 
A 1 280 HIS 280 280 ?   ?   ?   A . n 
A 1 281 HIS 281 281 ?   ?   ?   A . n 
A 1 282 HIS 282 282 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 PO4 ? ? PO4 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 OCS ? ? OCS ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 PO4 1  301 1  PO4 PO4 A . 
C 3 CL  1  302 1  CL  CL  A . 
D 4 HOH 1  401 52 HOH HOH A . 
D 4 HOH 2  402 35 HOH HOH A . 
D 4 HOH 3  403 10 HOH HOH A . 
D 4 HOH 4  404 9  HOH HOH A . 
D 4 HOH 5  405 22 HOH HOH A . 
D 4 HOH 6  406 4  HOH HOH A . 
D 4 HOH 7  407 32 HOH HOH A . 
D 4 HOH 8  408 54 HOH HOH A . 
D 4 HOH 9  409 23 HOH HOH A . 
D 4 HOH 10 410 42 HOH HOH A . 
D 4 HOH 11 411 50 HOH HOH A . 
D 4 HOH 12 412 25 HOH HOH A . 
D 4 HOH 13 413 7  HOH HOH A . 
D 4 HOH 14 414 20 HOH HOH A . 
D 4 HOH 15 415 3  HOH HOH A . 
D 4 HOH 16 416 15 HOH HOH A . 
D 4 HOH 17 417 30 HOH HOH A . 
D 4 HOH 18 418 26 HOH HOH A . 
D 4 HOH 19 419 13 HOH HOH A . 
D 4 HOH 20 420 28 HOH HOH A . 
D 4 HOH 21 421 44 HOH HOH A . 
D 4 HOH 22 422 21 HOH HOH A . 
D 4 HOH 23 423 5  HOH HOH A . 
D 4 HOH 24 424 2  HOH HOH A . 
D 4 HOH 25 425 18 HOH HOH A . 
D 4 HOH 26 426 19 HOH HOH A . 
D 4 HOH 27 427 46 HOH HOH A . 
D 4 HOH 28 428 17 HOH HOH A . 
D 4 HOH 29 429 40 HOH HOH A . 
D 4 HOH 30 430 16 HOH HOH A . 
D 4 HOH 31 431 36 HOH HOH A . 
D 4 HOH 32 432 14 HOH HOH A . 
D 4 HOH 33 433 31 HOH HOH A . 
D 4 HOH 34 434 48 HOH HOH A . 
D 4 HOH 35 435 38 HOH HOH A . 
D 4 HOH 36 436 43 HOH HOH A . 
D 4 HOH 37 437 6  HOH HOH A . 
D 4 HOH 38 438 27 HOH HOH A . 
D 4 HOH 39 439 39 HOH HOH A . 
D 4 HOH 40 440 24 HOH HOH A . 
D 4 HOH 41 441 49 HOH HOH A . 
D 4 HOH 42 442 1  HOH HOH A . 
D 4 HOH 43 443 12 HOH HOH A . 
D 4 HOH 44 444 33 HOH HOH A . 
D 4 HOH 45 445 11 HOH HOH A . 
D 4 HOH 46 446 37 HOH HOH A . 
D 4 HOH 47 447 47 HOH HOH A . 
D 4 HOH 48 448 41 HOH HOH A . 
D 4 HOH 49 449 8  HOH HOH A . 
D 4 HOH 50 450 53 HOH HOH A . 
D 4 HOH 51 451 45 HOH HOH A . 
D 4 HOH 52 452 29 HOH HOH A . 
D 4 HOH 53 453 56 HOH HOH A . 
D 4 HOH 54 454 34 HOH HOH A . 
D 4 HOH 55 455 51 HOH HOH A . 
D 4 HOH 56 456 55 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 15  ? CG  ? A LYS 15  CG  
2  1 Y 1 A LYS 15  ? CD  ? A LYS 15  CD  
3  1 Y 1 A LYS 15  ? CE  ? A LYS 15  CE  
4  1 Y 1 A LYS 15  ? NZ  ? A LYS 15  NZ  
5  1 Y 1 A GLU 54  ? CG  ? A GLU 54  CG  
6  1 Y 1 A GLU 54  ? CD  ? A GLU 54  CD  
7  1 Y 1 A GLU 54  ? OE1 ? A GLU 54  OE1 
8  1 Y 1 A GLU 54  ? OE2 ? A GLU 54  OE2 
9  1 Y 1 A GLN 84  ? CG  ? A GLN 84  CG  
10 1 Y 1 A GLN 84  ? CD  ? A GLN 84  CD  
11 1 Y 1 A GLN 84  ? OE1 ? A GLN 84  OE1 
12 1 Y 1 A GLN 84  ? NE2 ? A GLN 84  NE2 
13 1 Y 1 A LYS 130 ? CG  ? A LYS 130 CG  
14 1 Y 1 A LYS 130 ? CD  ? A LYS 130 CD  
15 1 Y 1 A LYS 130 ? CE  ? A LYS 130 CE  
16 1 Y 1 A LYS 130 ? NZ  ? A LYS 130 NZ  
17 1 Y 1 A GLU 179 ? CG  ? A GLU 179 CG  
18 1 Y 1 A GLU 179 ? CD  ? A GLU 179 CD  
19 1 Y 1 A GLU 179 ? OE1 ? A GLU 179 OE1 
20 1 Y 1 A GLU 179 ? OE2 ? A GLU 179 OE2 
21 1 Y 1 A ASP 259 ? CG  ? A ASP 259 CG  
22 1 Y 1 A ASP 259 ? OD1 ? A ASP 259 OD1 
23 1 Y 1 A ASP 259 ? OD2 ? A ASP 259 OD2 
# 
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  ? ? ? '(dev_5533: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9N1S 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.895 
_cell.length_a_esd                 ? 
_cell.length_b                     49.895 
_cell.length_b_esd                 ? 
_cell.length_c                     241.716 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9N1S 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9N1S 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.93 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Berkeley Screen B8: 20% (w/v) PEG 3350, 70 mM Bis-Tris Propane, 30 mM Citric Acid pH 7.6 , TANGO2 at 5.5 mg/mL. Plate 19608 well B8 drop 1, Puck: PSL-2010, Cryo: 80% (v/v) crystallant and 20% (v/v) PEG 200
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 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         2024-12-14 
_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                    'Double Crystal 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   0.9786 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 19-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9786 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9N1S 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.30 
_reflns.d_resolution_low                               46.12 
_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                                     14036 
_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                           96.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.99 
_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                                0.113 
_reflns.pdbx_Rpim_I_all                                0.046 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       82398 
_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                              0.103 
_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                                    2.30 
_reflns_shell.d_res_low                                     2.38 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           8441 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1399 
_reflns_shell.percent_possible_obs                          99.9 
_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                               6.0 
_reflns_shell.pdbx_chi_squared                              1.05 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.8 
_reflns_shell.pdbx_Rrim_I_all                               1.167 
_reflns_shell.pdbx_Rpim_I_all                               0.468 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.781 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.066 
_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                                 9N1S 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.30 
_refine.ls_d_res_low                             46.12 
_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                     13964 
_refine.ls_number_reflns_R_free                  690 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.11 
_refine.ls_percent_reflns_R_free                 4.94 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2072 
_refine.ls_R_factor_R_free                       0.2449 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2051 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.20 
_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                            0.28 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.30 
_refine_hist.d_res_low                        46.12 
_refine_hist.number_atoms_solvent             56 
_refine_hist.number_atoms_total               2205 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2143 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         6 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  ? 2196 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.575  ? 2988 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.624 ? 795  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.045  ? 331  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 386  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.30 2.48  . . 145 2652 100.00 . . . . 0.2910 . . . . . . . . . . . 0.3360 
'X-RAY DIFFRACTION' 2.48 2.73  . . 134 2419 90.00  . . . . 0.2679 . . . . . . . . . . . 0.3442 
'X-RAY DIFFRACTION' 2.73 3.12  . . 140 2721 100.00 . . . . 0.2388 . . . . . . . . . . . 0.2750 
'X-RAY DIFFRACTION' 3.12 3.93  . . 121 2542 92.00  . . . . 0.1964 . . . . . . . . . . . 0.2547 
'X-RAY DIFFRACTION' 3.93 46.12 . . 150 2940 99.00  . . . . 0.1770 . . . . . . . . . . . 0.2032 
# 
_struct.entry_id                     9N1S 
_struct.title                        
'Crystal structure of the Transport and Golgi Organization protein 2 Homolog (TANGO2) tetragonal form' 
_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        9N1S 
_struct_keywords.text            'TANGO2, TANGO2-related disease, LIPID TRANSPORT' 
_struct_keywords.pdbx_keywords   'LIPID TRANSPORT' 
# 
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                    TNG2_HUMAN 
_struct_ref.pdbx_db_accession          Q6ICL3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MCIIFFKFDPRPVSKNAYRLILAANRDEFYSRPSKLADFWGNNNEILSGLDMEEGKEGGTWLGISTRGKLAALTNYLQPQ
LDWQARGRGELVTHFLTTDVDSLSYLKKVSMEGHLYNGFNLIAADLSTAKGDVICYYGNRGEPDPIVLTPGTYGLSNALL
ETPWRKLCFGKQLFLEAVERSQALPKDVLIASLLDVLNNEEAQLPDPAIEDQGGEYVQPMLSKYAAVCVRCPGYGTRTNT
IILVDADGHVTFTERSMMDKDLSHWETRTYEFTLQS
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9N1S 
_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                 276 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q6ICL3 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  276 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       276 
# 
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 9N1S HIS A 277 ? UNP Q6ICL3 ? ? 'expression tag' 277 1 
1 9N1S HIS A 278 ? UNP Q6ICL3 ? ? 'expression tag' 278 2 
1 9N1S HIS A 279 ? UNP Q6ICL3 ? ? 'expression tag' 279 3 
1 9N1S HIS A 280 ? UNP Q6ICL3 ? ? 'expression tag' 280 4 
1 9N1S HIS A 281 ? UNP Q6ICL3 ? ? 'expression tag' 281 5 
1 9N1S HIS A 282 ? UNP Q6ICL3 ? ? 'expression tag' 282 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 89  ? THR A 97  ? GLY A 89  THR A 97  1 ? 9  
HELX_P HELX_P2 AA2 ASP A 101 ? GLU A 112 ? ASP A 101 GLU A 112 1 ? 12 
HELX_P HELX_P3 AA3 GLY A 113 ? TYR A 116 ? GLY A 113 TYR A 116 5 ? 4  
HELX_P HELX_P4 AA4 TRP A 164 ? GLN A 182 ? TRP A 164 GLN A 182 1 ? 19 
HELX_P HELX_P5 AA5 PRO A 185 ? ASN A 198 ? PRO A 185 ASN A 198 1 ? 14 
HELX_P HELX_P6 AA6 ASP A 206 ? GLN A 218 ? ASP A 206 GLN A 218 1 ? 13 
HELX_P HELX_P7 AA7 MET A 220 ? ALA A 225 ? MET A 220 ALA A 225 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        both 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           OCS 
_struct_conn.ptnr1_label_seq_id            2 
_struct_conn.ptnr1_label_atom_id           C 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           A 
_struct_conn.ptnr2_label_comp_id           ILE 
_struct_conn.ptnr2_label_seq_id            3 
_struct_conn.ptnr2_label_atom_id           N 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            OCS 
_struct_conn.ptnr1_auth_seq_id             2 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            ILE 
_struct_conn.ptnr2_auth_seq_id             3 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.327 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 OCS A 2 ? . . . . OCS A 2 ? 1_555 . . . . . . . CYS 1 OCS Oxidation     'Named protein modification' 
2 OCS A 2 ? . . . . OCS A 2 ? 1_555 . . . . . . . CYS 2 OCS Hydroxylation 'Named protein modification' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LEU 
_struct_mon_prot_cis.label_seq_id           204 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           LEU 
_struct_mon_prot_cis.auth_seq_id            204 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    205 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     205 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -2.33 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 6 ? 
AA3 ? 7 ? 
# 
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 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? 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 GLY A 151 ? LEU A 155 ? GLY A 151 LEU A 155 
AA1 2 ILE A 3   ? PHE A 8   ? ILE A 3   PHE A 8   
AA1 3 TYR A 18  ? PHE A 29  ? TYR A 18  PHE A 29  
AA1 4 TYR A 234 ? ASP A 245 ? TYR A 234 ASP A 245 
AA1 5 ARG A 230 ? CYS A 231 ? ARG A 230 CYS A 231 
AA2 1 GLY A 151 ? LEU A 155 ? GLY A 151 LEU A 155 
AA2 2 ILE A 3   ? PHE A 8   ? ILE A 3   PHE A 8   
AA2 3 TYR A 18  ? PHE A 29  ? TYR A 18  PHE A 29  
AA2 4 TYR A 234 ? ASP A 245 ? TYR A 234 ASP A 245 
AA2 5 HIS A 249 ? MET A 257 ? HIS A 249 MET A 257 
AA2 6 TRP A 265 ? THR A 273 ? TRP A 265 THR A 273 
AA3 1 SER A 34  ? TRP A 40  ? SER A 34  TRP A 40  
AA3 2 ILE A 46  ? ASP A 51  ? ILE A 46  ASP A 51  
AA3 3 LEU A 62  ? SER A 65  ? LEU A 62  SER A 65  
AA3 4 LYS A 69  ? ASN A 75  ? LYS A 69  ASN A 75  
AA3 5 PHE A 119 ? ASP A 125 ? PHE A 119 ASP A 125 
AA3 6 VAL A 133 ? GLY A 138 ? VAL A 133 GLY A 138 
AA3 7 ILE A 146 ? VAL A 147 ? ILE A 146 VAL A 147 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 155 ? O LEU A 155 N ILE A 4   ? N ILE A 4   
AA1 2 3 N ILE A 3   ? N ILE A 3   O ASN A 25  ? O ASN A 25  
AA1 3 4 N ARG A 26  ? N ARG A 26  O ARG A 237 ? O ARG A 237 
AA1 4 5 O TYR A 234 ? O TYR A 234 N CYS A 231 ? N CYS A 231 
AA2 1 2 O LEU A 155 ? O LEU A 155 N ILE A 4   ? N ILE A 4   
AA2 2 3 N ILE A 3   ? N ILE A 3   O ASN A 25  ? O ASN A 25  
AA2 3 4 N ARG A 26  ? N ARG A 26  O ARG A 237 ? O ARG A 237 
AA2 4 5 N ILE A 241 ? N ILE A 241 O THR A 253 ? O THR A 253 
AA2 5 6 N SER A 256 ? N SER A 256 O GLU A 266 ? O GLU A 266 
AA3 1 2 N TRP A 40  ? N TRP A 40  O ILE A 46  ? O ILE A 46  
AA3 2 3 N LEU A 47  ? N LEU A 47  O ILE A 64  ? O ILE A 64  
AA3 3 4 N SER A 65  ? N SER A 65  O LYS A 69  ? O LYS A 69  
AA3 4 5 N LEU A 70  ? N LEU A 70  O ALA A 124 ? O ALA A 124 
AA3 5 6 N ALA A 123 ? N ALA A 123 O CYS A 135 ? O CYS A 135 
AA3 6 7 N TYR A 136 ? N TYR A 136 O ILE A 146 ? O ILE A 146 
# 
_pdbx_entry_details.entry_id                   9N1S 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 ARG A 11  ? ? -113.65 70.82   
2 1 THR A 98  ? ? -127.35 -169.89 
3 1 SER A 156 ? ? -138.19 -155.15 
4 1 ALA A 158 ? ? -92.17  -156.33 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    OCS 
_pdbx_struct_mod_residue.label_seq_id     2 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     OCS 
_pdbx_struct_mod_residue.auth_seq_id      2 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   CYS 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -25.5513 -7.9330  -11.1408 0.4257 ? -0.1514 ? 0.0021  ? 0.4516 ? -0.0511 ? 0.4139 ? 3.5735 ? 
-2.6174 ? -1.1344 ? 3.5913 ? 0.7865  ? 4.0990 ? -0.0350 ? -0.2613 ? 0.0710  ? 0.2650  ? 0.0078  ? 0.2222  ? 0.0764  ? -0.1736 ? 
-0.0090 ? 
2 'X-RAY DIFFRACTION' ? refined -8.3795  1.0020   -8.9489  0.4702 ? -0.1846 ? 0.0385  ? 0.5894 ? -0.0539 ? 0.4427 ? 4.4498 ? 
-0.6627 ? -0.1259 ? 3.0472 ? 1.6045  ? 6.1083 ? -0.0485 ? -0.4545 ? 0.5672  ? -0.3380 ? 0.3285  ? -0.5118 ? -0.5716 ? 1.0310  ? 
-0.2879 ? 
3 'X-RAY DIFFRACTION' ? refined -12.3456 1.4593   -14.8076 0.3861 ? -0.0879 ? 0.0481  ? 0.4822 ? -0.0368 ? 0.4623 ? 4.2124 ? 
0.8499  ? 0.6031  ? 1.8103 ? -0.6194 ? 3.4875 ? 0.2860  ? -0.3604 ? 0.2239  ? -0.2467 ? -0.1756 ? -0.3795 ? -0.6450 ? 0.7405  ? 
-0.1115 ? 
4 'X-RAY DIFFRACTION' ? refined -13.5902 3.3784   -24.4685 0.5454 ? -0.0865 ? 0.0039  ? 0.5528 ? 0.0774  ? 0.6272 ? 2.7323 ? 
1.0904  ? 1.4515  ? 3.4295 ? -0.2233 ? 1.3340 ? 0.2377  ? 0.3270  ? 0.3755  ? -0.4972 ? -0.3434 ? -0.7997 ? -0.2998 ? 0.1952  ? 
0.0070  ? 
5 'X-RAY DIFFRACTION' ? refined -24.9283 0.7256   -23.1402 0.3941 ? -0.0685 ? 0.0158  ? 0.3402 ? -0.0357 ? 0.3891 ? 3.5443 ? 
-0.1575 ? -0.3359 ? 2.7731 ? 0.0292  ? 2.6079 ? -0.0076 ? 0.1893  ? 0.3049  ? -0.0980 ? -0.0213 ? -0.0250 ? -0.1584 ? -0.0301 ? 
0.0144  ? 
6 'X-RAY DIFFRACTION' ? refined -26.2942 -19.6260 -15.4998 0.4550 ? -0.1651 ? 0.0496  ? 0.4812 ? -0.0170 ? 0.5111 ? 6.0675 ? 
-2.8743 ? -3.8004 ? 5.1653 ? 1.7160  ? 2.3826 ? -0.1430 ? -0.4538 ? -0.9399 ? 0.1959  ? -0.5859 ? 1.1281  ? 0.7758  ? -0.1272 ? 
0.6060  ? 
7 'X-RAY DIFFRACTION' ? refined -22.6319 -16.7697 -3.9516  0.3919 ? -0.0846 ? -0.0202 ? 0.6447 ? 0.0481  ? 0.4166 ? 5.1048 ? 
0.4836  ? -3.7121 ? 3.9451 ? 0.5612  ? 2.9286 ? -0.3515 ? -0.4111 ? -0.2406 ? 0.2711  ? -0.3439 ? 0.1649  ? -0.1292 ? 0.1284  ? 
0.7240  ? 
8 'X-RAY DIFFRACTION' ? refined -12.7607 -18.7478 -26.6447 0.4339 ? -0.0452 ? -0.0043 ? 0.5262 ? -0.0295 ? 0.4471 ? 2.2542 ? 
-0.3008 ? -0.5656 ? 2.2132 ? 0.7896  ? 2.6724 ? 0.2011  ? 0.1160  ? -0.4016 ? 0.1326  ? 0.0304  ? -0.1243 ? -0.0303 ? -0.0473 ? 
-0.1857 ? 
9 'X-RAY DIFFRACTION' ? refined -14.0215 -8.3852  -5.0045  0.4985 ? -0.1946 ? 0.0079  ? 0.6367 ? -0.0492 ? 0.3411 ? 4.2782 ? 
-0.0828 ? 1.6840  ? 2.7794 ? -1.1346 ? 2.6149 ? 0.1943  ? -0.4096 ? -0.2492 ? 0.0644  ? -0.2384 ? 0.0886  ? -0.0711 ? 0.1278  ? 
-0.0269 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 3 through 29 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 30 through 48 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 49 through 75 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 76 through 101 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 102 through 164 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 165 through 181 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 182 through 197 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 198 through 237 )
;
9 'X-RAY DIFFRACTION' 9 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 238 through 275 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1   ? A MET 1   
2 1 Y 1 A SER 276 ? A SER 276 
3 1 Y 1 A HIS 277 ? A HIS 277 
4 1 Y 1 A HIS 278 ? A HIS 278 
5 1 Y 1 A HIS 279 ? A HIS 279 
6 1 Y 1 A HIS 280 ? A HIS 280 
7 1 Y 1 A HIS 281 ? A HIS 281 
8 1 Y 1 A HIS 282 ? A HIS 282 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
OCS N    N  N N 251 
OCS CA   C  N R 252 
OCS CB   C  N N 253 
OCS SG   S  N N 254 
OCS C    C  N N 255 
OCS O    O  N N 256 
OCS OXT  O  N N 257 
OCS OD1  O  N N 258 
OCS OD2  O  N N 259 
OCS OD3  O  N N 260 
OCS H    H  N N 261 
OCS H2   H  N N 262 
OCS HA   H  N N 263 
OCS HB2  H  N N 264 
OCS HB3  H  N N 265 
OCS HXT  H  N N 266 
OCS HD2  H  N N 267 
PHE N    N  N N 268 
PHE CA   C  N S 269 
PHE C    C  N N 270 
PHE O    O  N N 271 
PHE CB   C  N N 272 
PHE CG   C  Y N 273 
PHE CD1  C  Y N 274 
PHE CD2  C  Y N 275 
PHE CE1  C  Y N 276 
PHE CE2  C  Y N 277 
PHE CZ   C  Y N 278 
PHE OXT  O  N N 279 
PHE H    H  N N 280 
PHE H2   H  N N 281 
PHE HA   H  N N 282 
PHE HB2  H  N N 283 
PHE HB3  H  N N 284 
PHE HD1  H  N N 285 
PHE HD2  H  N N 286 
PHE HE1  H  N N 287 
PHE HE2  H  N N 288 
PHE HZ   H  N N 289 
PHE HXT  H  N N 290 
PO4 P    P  N N 291 
PO4 O1   O  N N 292 
PO4 O2   O  N N 293 
PO4 O3   O  N N 294 
PO4 O4   O  N N 295 
PRO N    N  N N 296 
PRO CA   C  N S 297 
PRO C    C  N N 298 
PRO O    O  N N 299 
PRO CB   C  N N 300 
PRO CG   C  N N 301 
PRO CD   C  N N 302 
PRO OXT  O  N N 303 
PRO H    H  N N 304 
PRO HA   H  N N 305 
PRO HB2  H  N N 306 
PRO HB3  H  N N 307 
PRO HG2  H  N N 308 
PRO HG3  H  N N 309 
PRO HD2  H  N N 310 
PRO HD3  H  N N 311 
PRO HXT  H  N N 312 
SER N    N  N N 313 
SER CA   C  N S 314 
SER C    C  N N 315 
SER O    O  N N 316 
SER CB   C  N N 317 
SER OG   O  N N 318 
SER OXT  O  N N 319 
SER H    H  N N 320 
SER H2   H  N N 321 
SER HA   H  N N 322 
SER HB2  H  N N 323 
SER HB3  H  N N 324 
SER HG   H  N N 325 
SER HXT  H  N N 326 
THR N    N  N N 327 
THR CA   C  N S 328 
THR C    C  N N 329 
THR O    O  N N 330 
THR CB   C  N R 331 
THR OG1  O  N N 332 
THR CG2  C  N N 333 
THR OXT  O  N N 334 
THR H    H  N N 335 
THR H2   H  N N 336 
THR HA   H  N N 337 
THR HB   H  N N 338 
THR HG1  H  N N 339 
THR HG21 H  N N 340 
THR HG22 H  N N 341 
THR HG23 H  N N 342 
THR HXT  H  N N 343 
TRP N    N  N N 344 
TRP CA   C  N S 345 
TRP C    C  N N 346 
TRP O    O  N N 347 
TRP CB   C  N N 348 
TRP CG   C  Y N 349 
TRP CD1  C  Y N 350 
TRP CD2  C  Y N 351 
TRP NE1  N  Y N 352 
TRP CE2  C  Y N 353 
TRP CE3  C  Y N 354 
TRP CZ2  C  Y N 355 
TRP CZ3  C  Y N 356 
TRP CH2  C  Y N 357 
TRP OXT  O  N N 358 
TRP H    H  N N 359 
TRP H2   H  N N 360 
TRP HA   H  N N 361 
TRP HB2  H  N N 362 
TRP HB3  H  N N 363 
TRP HD1  H  N N 364 
TRP HE1  H  N N 365 
TRP HE3  H  N N 366 
TRP HZ2  H  N N 367 
TRP HZ3  H  N N 368 
TRP HH2  H  N N 369 
TRP HXT  H  N N 370 
TYR N    N  N N 371 
TYR CA   C  N S 372 
TYR C    C  N N 373 
TYR O    O  N N 374 
TYR CB   C  N N 375 
TYR CG   C  Y N 376 
TYR CD1  C  Y N 377 
TYR CD2  C  Y N 378 
TYR CE1  C  Y N 379 
TYR CE2  C  Y N 380 
TYR CZ   C  Y N 381 
TYR OH   O  N N 382 
TYR OXT  O  N N 383 
TYR H    H  N N 384 
TYR H2   H  N N 385 
TYR HA   H  N N 386 
TYR HB2  H  N N 387 
TYR HB3  H  N N 388 
TYR HD1  H  N N 389 
TYR HD2  H  N N 390 
TYR HE1  H  N N 391 
TYR HE2  H  N N 392 
TYR HH   H  N N 393 
TYR HXT  H  N N 394 
VAL N    N  N N 395 
VAL CA   C  N S 396 
VAL C    C  N N 397 
VAL O    O  N N 398 
VAL CB   C  N N 399 
VAL CG1  C  N N 400 
VAL CG2  C  N N 401 
VAL OXT  O  N N 402 
VAL H    H  N N 403 
VAL H2   H  N N 404 
VAL HA   H  N N 405 
VAL HB   H  N N 406 
VAL HG11 H  N N 407 
VAL HG12 H  N N 408 
VAL HG13 H  N N 409 
VAL HG21 H  N N 410 
VAL HG22 H  N N 411 
VAL HG23 H  N N 412 
VAL HXT  H  N N 413 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
OCS N   CA   sing N N 237 
OCS N   H    sing N N 238 
OCS N   H2   sing N N 239 
OCS CA  CB   sing N N 240 
OCS CA  C    sing N N 241 
OCS CA  HA   sing N N 242 
OCS CB  SG   sing N N 243 
OCS CB  HB2  sing N N 244 
OCS CB  HB3  sing N N 245 
OCS SG  OD1  doub N N 246 
OCS SG  OD2  sing N N 247 
OCS SG  OD3  doub N N 248 
OCS C   O    doub N N 249 
OCS C   OXT  sing N N 250 
OCS OXT HXT  sing N N 251 
OCS OD2 HD2  sing N N 252 
PHE N   CA   sing N N 253 
PHE N   H    sing N N 254 
PHE N   H2   sing N N 255 
PHE CA  C    sing N N 256 
PHE CA  CB   sing N N 257 
PHE CA  HA   sing N N 258 
PHE C   O    doub N N 259 
PHE C   OXT  sing N N 260 
PHE CB  CG   sing N N 261 
PHE CB  HB2  sing N N 262 
PHE CB  HB3  sing N N 263 
PHE CG  CD1  doub Y N 264 
PHE CG  CD2  sing Y N 265 
PHE CD1 CE1  sing Y N 266 
PHE CD1 HD1  sing N N 267 
PHE CD2 CE2  doub Y N 268 
PHE CD2 HD2  sing N N 269 
PHE CE1 CZ   doub Y N 270 
PHE CE1 HE1  sing N N 271 
PHE CE2 CZ   sing Y N 272 
PHE CE2 HE2  sing N N 273 
PHE CZ  HZ   sing N N 274 
PHE OXT HXT  sing N N 275 
PO4 P   O1   doub N N 276 
PO4 P   O2   sing N N 277 
PO4 P   O3   sing N N 278 
PO4 P   O4   sing N N 279 
PRO N   CA   sing N N 280 
PRO N   CD   sing N N 281 
PRO N   H    sing N N 282 
PRO CA  C    sing N N 283 
PRO CA  CB   sing N N 284 
PRO CA  HA   sing N N 285 
PRO C   O    doub N N 286 
PRO C   OXT  sing N N 287 
PRO CB  CG   sing N N 288 
PRO CB  HB2  sing N N 289 
PRO CB  HB3  sing N N 290 
PRO CG  CD   sing N N 291 
PRO CG  HG2  sing N N 292 
PRO CG  HG3  sing N N 293 
PRO CD  HD2  sing N N 294 
PRO CD  HD3  sing N N 295 
PRO OXT HXT  sing N N 296 
SER N   CA   sing N N 297 
SER N   H    sing N N 298 
SER N   H2   sing N N 299 
SER CA  C    sing N N 300 
SER CA  CB   sing N N 301 
SER CA  HA   sing N N 302 
SER C   O    doub N N 303 
SER C   OXT  sing N N 304 
SER CB  OG   sing N N 305 
SER CB  HB2  sing N N 306 
SER CB  HB3  sing N N 307 
SER OG  HG   sing N N 308 
SER OXT HXT  sing N N 309 
THR N   CA   sing N N 310 
THR N   H    sing N N 311 
THR N   H2   sing N N 312 
THR CA  C    sing N N 313 
THR CA  CB   sing N N 314 
THR CA  HA   sing N N 315 
THR C   O    doub N N 316 
THR C   OXT  sing N N 317 
THR CB  OG1  sing N N 318 
THR CB  CG2  sing N N 319 
THR CB  HB   sing N N 320 
THR OG1 HG1  sing N N 321 
THR CG2 HG21 sing N N 322 
THR CG2 HG22 sing N N 323 
THR CG2 HG23 sing N N 324 
THR OXT HXT  sing N N 325 
TRP N   CA   sing N N 326 
TRP N   H    sing N N 327 
TRP N   H2   sing N N 328 
TRP CA  C    sing N N 329 
TRP CA  CB   sing N N 330 
TRP CA  HA   sing N N 331 
TRP C   O    doub N N 332 
TRP C   OXT  sing N N 333 
TRP CB  CG   sing N N 334 
TRP CB  HB2  sing N N 335 
TRP CB  HB3  sing N N 336 
TRP CG  CD1  doub Y N 337 
TRP CG  CD2  sing Y N 338 
TRP CD1 NE1  sing Y N 339 
TRP CD1 HD1  sing N N 340 
TRP CD2 CE2  doub Y N 341 
TRP CD2 CE3  sing Y N 342 
TRP NE1 CE2  sing Y N 343 
TRP NE1 HE1  sing N N 344 
TRP CE2 CZ2  sing Y N 345 
TRP CE3 CZ3  doub Y N 346 
TRP CE3 HE3  sing N N 347 
TRP CZ2 CH2  doub Y N 348 
TRP CZ2 HZ2  sing N N 349 
TRP CZ3 CH2  sing Y N 350 
TRP CZ3 HZ3  sing N N 351 
TRP CH2 HH2  sing N N 352 
TRP OXT HXT  sing N N 353 
TYR N   CA   sing N N 354 
TYR N   H    sing N N 355 
TYR N   H2   sing N N 356 
TYR CA  C    sing N N 357 
TYR CA  CB   sing N N 358 
TYR CA  HA   sing N N 359 
TYR C   O    doub N N 360 
TYR C   OXT  sing N N 361 
TYR CB  CG   sing N N 362 
TYR CB  HB2  sing N N 363 
TYR CB  HB3  sing N N 364 
TYR CG  CD1  doub Y N 365 
TYR CG  CD2  sing Y N 366 
TYR CD1 CE1  sing Y N 367 
TYR CD1 HD1  sing N N 368 
TYR CD2 CE2  doub Y N 369 
TYR CD2 HD2  sing N N 370 
TYR CE1 CZ   doub Y N 371 
TYR CE1 HE1  sing N N 372 
TYR CE2 CZ   sing Y N 373 
TYR CE2 HE2  sing N N 374 
TYR CZ  OH   sing N N 375 
TYR OH  HH   sing N N 376 
TYR OXT HXT  sing N N 377 
VAL N   CA   sing N N 378 
VAL N   H    sing N N 379 
VAL N   H2   sing N N 380 
VAL CA  C    sing N N 381 
VAL CA  CB   sing N N 382 
VAL CA  HA   sing N N 383 
VAL C   O    doub N N 384 
VAL C   OXT  sing N N 385 
VAL CB  CG1  sing N N 386 
VAL CB  CG2  sing N N 387 
VAL CB  HB   sing N N 388 
VAL CG1 HG11 sing N N 389 
VAL CG1 HG12 sing N N 390 
VAL CG1 HG13 sing N N 391 
VAL CG2 HG21 sing N N 392 
VAL CG2 HG22 sing N N 393 
VAL CG2 HG23 sing N N 394 
VAL OXT HXT  sing N N 395 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/Office of the Director' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           S10OD030394 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9BWA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9N1S 
_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]   0.020042 
_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]   0.020042 
_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]   0.004137 
_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  
CL 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
HETATM 1    N  N   . OCS A 1 2   ? -14.260 -10.976 -22.534 1.00 43.61  ? 2   OCS A N   1 
HETATM 2    C  CA  . OCS A 1 2   ? -14.905 -10.616 -21.249 1.00 46.36  ? 2   OCS A CA  1 
HETATM 3    C  CB  . OCS A 1 2   ? -15.047 -9.107  -21.055 1.00 52.85  ? 2   OCS A CB  1 
HETATM 4    S  SG  . OCS A 1 2   ? -13.549 -8.173  -21.255 1.00 69.44  ? 2   OCS A SG  1 
HETATM 5    C  C   . OCS A 1 2   ? -16.291 -11.279 -21.167 1.00 46.10  ? 2   OCS A C   1 
HETATM 6    O  O   . OCS A 1 2   ? -16.728 -11.851 -22.187 1.00 51.45  ? 2   OCS A O   1 
HETATM 7    O  OD1 . OCS A 1 2   ? -12.457 -9.092  -21.147 1.00 60.30  ? 2   OCS A OD1 1 
HETATM 8    O  OD2 . OCS A 1 2   ? -13.619 -7.645  -22.726 1.00 48.35  ? 2   OCS A OD2 1 
HETATM 9    O  OD3 . OCS A 1 2   ? -13.621 -7.088  -20.317 1.00 62.40  ? 2   OCS A OD3 1 
ATOM   10   N  N   . ILE A 1 3   ? -16.951 -11.232 -20.017 1.00 50.28  ? 3   ILE A N   1 
ATOM   11   C  CA  . ILE A 1 3   ? -18.340 -11.675 -19.927 1.00 44.60  ? 3   ILE A CA  1 
ATOM   12   C  C   . ILE A 1 3   ? -18.939 -11.239 -18.588 1.00 42.22  ? 3   ILE A C   1 
ATOM   13   O  O   . ILE A 1 3   ? -18.324 -11.384 -17.532 1.00 41.50  ? 3   ILE A O   1 
ATOM   14   C  CB  . ILE A 1 3   ? -18.461 -13.201 -20.142 1.00 42.33  ? 3   ILE A CB  1 
ATOM   15   C  CG1 . ILE A 1 3   ? -19.939 -13.600 -20.217 1.00 41.26  ? 3   ILE A CG1 1 
ATOM   16   C  CG2 . ILE A 1 3   ? -17.733 -13.968 -19.048 1.00 43.29  ? 3   ILE A CG2 1 
ATOM   17   C  CD1 . ILE A 1 3   ? -20.169 -15.035 -20.640 1.00 48.82  ? 3   ILE A CD1 1 
ATOM   18   N  N   . ILE A 1 4   ? -20.157 -10.709 -18.653 1.00 41.91  ? 4   ILE A N   1 
ATOM   19   C  CA  . ILE A 1 4   ? -20.825 -10.118 -17.504 1.00 45.96  ? 4   ILE A CA  1 
ATOM   20   C  C   . ILE A 1 4   ? -22.248 -10.651 -17.427 1.00 45.26  ? 4   ILE A C   1 
ATOM   21   O  O   . ILE A 1 4   ? -22.938 -10.742 -18.444 1.00 41.31  ? 4   ILE A O   1 
ATOM   22   C  CB  . ILE A 1 4   ? -20.831 -8.578  -17.601 1.00 45.40  ? 4   ILE A CB  1 
ATOM   23   C  CG1 . ILE A 1 4   ? -19.402 -8.050  -17.736 1.00 41.37  ? 4   ILE A CG1 1 
ATOM   24   C  CG2 . ILE A 1 4   ? -21.534 -7.972  -16.382 1.00 41.82  ? 4   ILE A CG2 1 
ATOM   25   C  CD1 . ILE A 1 4   ? -19.325 -6.571  -18.028 1.00 43.66  ? 4   ILE A CD1 1 
ATOM   26   N  N   . PHE A 1 5   ? -22.679 -10.999 -16.221 1.00 45.08  ? 5   PHE A N   1 
ATOM   27   C  CA  . PHE A 1 5   ? -24.065 -11.348 -15.935 1.00 46.18  ? 5   PHE A CA  1 
ATOM   28   C  C   . PHE A 1 5   ? -24.557 -10.434 -14.823 1.00 41.41  ? 5   PHE A C   1 
ATOM   29   O  O   . PHE A 1 5   ? -23.807 -10.134 -13.890 1.00 42.42  ? 5   PHE A O   1 
ATOM   30   C  CB  . PHE A 1 5   ? -24.197 -12.802 -15.504 1.00 46.00  ? 5   PHE A CB  1 
ATOM   31   C  CG  . PHE A 1 5   ? -23.582 -13.770 -16.468 1.00 45.78  ? 5   PHE A CG  1 
ATOM   32   C  CD1 . PHE A 1 5   ? -24.236 -14.110 -17.631 1.00 42.17  ? 5   PHE A CD1 1 
ATOM   33   C  CD2 . PHE A 1 5   ? -22.345 -14.337 -16.206 1.00 48.39  ? 5   PHE A CD2 1 
ATOM   34   C  CE1 . PHE A 1 5   ? -23.672 -14.996 -18.520 1.00 47.58  ? 5   PHE A CE1 1 
ATOM   35   C  CE2 . PHE A 1 5   ? -21.774 -15.224 -17.094 1.00 44.99  ? 5   PHE A CE2 1 
ATOM   36   C  CZ  . PHE A 1 5   ? -22.440 -15.555 -18.248 1.00 49.76  ? 5   PHE A CZ  1 
ATOM   37   N  N   . PHE A 1 6   ? -25.797 -9.965  -14.924 1.00 39.74  ? 6   PHE A N   1 
ATOM   38   C  CA  . PHE A 1 6   ? -26.320 -9.117  -13.859 1.00 43.83  ? 6   PHE A CA  1 
ATOM   39   C  C   . PHE A 1 6   ? -27.838 -9.134  -13.856 1.00 47.67  ? 6   PHE A C   1 
ATOM   40   O  O   . PHE A 1 6   ? -28.474 -8.958  -14.900 1.00 47.06  ? 6   PHE A O   1 
ATOM   41   C  CB  . PHE A 1 6   ? -25.780 -7.675  -13.981 1.00 36.02  ? 6   PHE A CB  1 
ATOM   42   C  CG  . PHE A 1 6   ? -26.288 -6.907  -15.169 1.00 41.41  ? 6   PHE A CG  1 
ATOM   43   C  CD1 . PHE A 1 6   ? -27.492 -6.226  -15.112 1.00 45.32  ? 6   PHE A CD1 1 
ATOM   44   C  CD2 . PHE A 1 6   ? -25.533 -6.822  -16.330 1.00 39.44  ? 6   PHE A CD2 1 
ATOM   45   C  CE1 . PHE A 1 6   ? -27.951 -5.505  -16.207 1.00 48.10  ? 6   PHE A CE1 1 
ATOM   46   C  CE2 . PHE A 1 6   ? -25.986 -6.101  -17.420 1.00 43.87  ? 6   PHE A CE2 1 
ATOM   47   C  CZ  . PHE A 1 6   ? -27.194 -5.441  -17.360 1.00 46.91  ? 6   PHE A CZ  1 
ATOM   48   N  N   . LYS A 1 7   ? -28.407 -9.360  -12.670 1.00 48.73  ? 7   LYS A N   1 
ATOM   49   C  CA  . LYS A 1 7   ? -29.837 -9.228  -12.432 1.00 44.87  ? 7   LYS A CA  1 
ATOM   50   C  C   . LYS A 1 7   ? -30.096 -7.871  -11.795 1.00 43.16  ? 7   LYS A C   1 
ATOM   51   O  O   . LYS A 1 7   ? -29.329 -7.420  -10.944 1.00 45.66  ? 7   LYS A O   1 
ATOM   52   C  CB  . LYS A 1 7   ? -30.363 -10.337 -11.528 1.00 46.20  ? 7   LYS A CB  1 
ATOM   53   C  CG  . LYS A 1 7   ? -31.849 -10.223 -11.226 1.00 44.92  ? 7   LYS A CG  1 
ATOM   54   C  CD  . LYS A 1 7   ? -32.294 -11.240 -10.171 1.00 55.01  ? 7   LYS A CD  1 
ATOM   55   C  CE  . LYS A 1 7   ? -32.257 -12.661 -10.709 1.00 62.76  ? 7   LYS A CE  1 
ATOM   56   N  NZ  . LYS A 1 7   ? -33.574 -13.350 -10.545 1.00 75.83  ? 7   LYS A NZ  1 
ATOM   57   N  N   . PHE A 1 8   ? -31.190 -7.233  -12.198 1.00 45.67  ? 8   PHE A N   1 
ATOM   58   C  CA  . PHE A 1 8   ? -31.431 -5.817  -11.922 1.00 48.85  ? 8   PHE A CA  1 
ATOM   59   C  C   . PHE A 1 8   ? -32.901 -5.652  -11.578 1.00 51.24  ? 8   PHE A C   1 
ATOM   60   O  O   . PHE A 1 8   ? -33.771 -5.914  -12.409 1.00 54.53  ? 8   PHE A O   1 
ATOM   61   C  CB  . PHE A 1 8   ? -30.989 -4.971  -13.138 1.00 55.35  ? 8   PHE A CB  1 
ATOM   62   C  CG  . PHE A 1 8   ? -31.776 -3.715  -13.348 1.00 49.46  ? 8   PHE A CG  1 
ATOM   63   C  CD1 . PHE A 1 8   ? -31.866 -2.759  -12.364 1.00 54.42  ? 8   PHE A CD1 1 
ATOM   64   C  CD2 . PHE A 1 8   ? -32.388 -3.474  -14.568 1.00 58.67  ? 8   PHE A CD2 1 
ATOM   65   C  CE1 . PHE A 1 8   ? -32.591 -1.595  -12.571 1.00 57.15  ? 8   PHE A CE1 1 
ATOM   66   C  CE2 . PHE A 1 8   ? -33.112 -2.315  -14.782 1.00 58.24  ? 8   PHE A CE2 1 
ATOM   67   C  CZ  . PHE A 1 8   ? -33.210 -1.374  -13.780 1.00 55.22  ? 8   PHE A CZ  1 
ATOM   68   N  N   . ASP A 1 9   ? -33.170 -5.246  -10.335 1.00 56.44  ? 9   ASP A N   1 
ATOM   69   C  CA  . ASP A 1 9   ? -34.528 -5.149  -9.801  1.00 56.62  ? 9   ASP A CA  1 
ATOM   70   C  C   . ASP A 1 9   ? -34.636 -3.845  -9.021  1.00 61.20  ? 9   ASP A C   1 
ATOM   71   O  O   . ASP A 1 9   ? -34.305 -3.787  -7.832  1.00 59.41  ? 9   ASP A O   1 
ATOM   72   C  CB  . ASP A 1 9   ? -34.856 -6.347  -8.906  1.00 55.68  ? 9   ASP A CB  1 
ATOM   73   C  CG  . ASP A 1 9   ? -36.322 -6.416  -8.530  1.00 64.20  ? 9   ASP A CG  1 
ATOM   74   O  OD1 . ASP A 1 9   ? -37.142 -5.730  -9.179  1.00 62.75  ? 9   ASP A OD1 1 
ATOM   75   O  OD2 . ASP A 1 9   ? -36.654 -7.156  -7.581  1.00 73.06  ? 9   ASP A OD2 1 
ATOM   76   N  N   . PRO A 1 10  ? -35.097 -2.770  -9.671  1.00 63.07  ? 10  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 10  ? -35.097 -1.463  -8.985  1.00 64.74  ? 10  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 10  ? -36.149 -1.341  -7.899  1.00 65.48  ? 10  PRO A C   1 
ATOM   79   O  O   . PRO A 1 10  ? -35.960 -0.547  -6.970  1.00 67.46  ? 10  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 10  ? -35.352 -0.469  -10.130 1.00 64.76  ? 10  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 10  ? -36.137 -1.260  -11.129 1.00 60.78  ? 10  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 10  ? -35.626 -2.680  -11.043 1.00 58.31  ? 10  PRO A CD  1 
ATOM   83   N  N   . ARG A 1 11  ? -37.248 -2.089  -7.988  1.00 67.99  ? 11  ARG A N   1 
ATOM   84   C  CA  . ARG A 1 11  ? -38.306 -2.051  -6.985  1.00 75.17  ? 11  ARG A CA  1 
ATOM   85   C  C   . ARG A 1 11  ? -38.363 -3.395  -6.272  1.00 72.25  ? 11  ARG A C   1 
ATOM   86   O  O   . ARG A 1 11  ? -39.308 -4.168  -6.475  1.00 72.08  ? 11  ARG A O   1 
ATOM   87   C  CB  . ARG A 1 11  ? -39.656 -1.728  -7.628  1.00 78.56  ? 11  ARG A CB  1 
ATOM   88   C  CG  . ARG A 1 11  ? -39.722 -0.350  -8.284  1.00 81.66  ? 11  ARG A CG  1 
ATOM   89   C  CD  . ARG A 1 11  ? -40.406 0.685   -7.384  1.00 87.70  ? 11  ARG A CD  1 
ATOM   90   N  NE  . ARG A 1 11  ? -41.863 0.600   -7.443  1.00 99.44  ? 11  ARG A NE  1 
ATOM   91   C  CZ  . ARG A 1 11  ? -42.629 0.005   -6.531  1.00 90.63  ? 11  ARG A CZ  1 
ATOM   92   N  NH1 . ARG A 1 11  ? -42.112 -0.560  -5.453  1.00 85.23  ? 11  ARG A NH1 1 
ATOM   93   N  NH2 . ARG A 1 11  ? -43.947 -0.020  -6.709  1.00 85.84  ? 11  ARG A NH2 1 
ATOM   94   N  N   . PRO A 1 12  ? -37.371 -3.715  -5.442  1.00 74.16  ? 12  PRO A N   1 
ATOM   95   C  CA  . PRO A 1 12  ? -37.374 -5.019  -4.764  1.00 76.37  ? 12  PRO A CA  1 
ATOM   96   C  C   . PRO A 1 12  ? -38.616 -5.199  -3.904  1.00 80.80  ? 12  PRO A C   1 
ATOM   97   O  O   . PRO A 1 12  ? -39.047 -4.288  -3.190  1.00 68.27  ? 12  PRO A O   1 
ATOM   98   C  CB  . PRO A 1 12  ? -36.094 -4.988  -3.917  1.00 73.67  ? 12  PRO A CB  1 
ATOM   99   C  CG  . PRO A 1 12  ? -35.734 -3.537  -3.805  1.00 72.99  ? 12  PRO A CG  1 
ATOM   100  C  CD  . PRO A 1 12  ? -36.202 -2.895  -5.076  1.00 68.08  ? 12  PRO A CD  1 
ATOM   101  N  N   . VAL A 1 13  ? -39.182 -6.406  -3.969  1.00 88.74  ? 13  VAL A N   1 
ATOM   102  C  CA  . VAL A 1 13  ? -40.438 -6.677  -3.284  1.00 87.56  ? 13  VAL A CA  1 
ATOM   103  C  C   . VAL A 1 13  ? -40.251 -6.866  -1.783  1.00 88.19  ? 13  VAL A C   1 
ATOM   104  O  O   . VAL A 1 13  ? -41.206 -6.682  -1.019  1.00 86.68  ? 13  VAL A O   1 
ATOM   105  C  CB  . VAL A 1 13  ? -41.123 -7.922  -3.879  1.00 92.61  ? 13  VAL A CB  1 
ATOM   106  C  CG1 . VAL A 1 13  ? -41.171 -7.835  -5.405  1.00 87.93  ? 13  VAL A CG1 1 
ATOM   107  C  CG2 . VAL A 1 13  ? -40.411 -9.200  -3.428  1.00 92.54  ? 13  VAL A CG2 1 
ATOM   108  N  N   . SER A 1 14  ? -39.047 -7.227  -1.342  1.00 86.00  ? 14  SER A N   1 
ATOM   109  C  CA  . SER A 1 14  ? -38.803 -7.512  0.064   1.00 84.24  ? 14  SER A CA  1 
ATOM   110  C  C   . SER A 1 14  ? -37.632 -6.693  0.598   1.00 89.65  ? 14  SER A C   1 
ATOM   111  O  O   . SER A 1 14  ? -37.083 -5.843  -0.113  1.00 82.58  ? 14  SER A O   1 
ATOM   112  C  CB  . SER A 1 14  ? -38.537 -9.008  0.261   1.00 89.66  ? 14  SER A CB  1 
ATOM   113  O  OG  . SER A 1 14  ? -37.406 -9.423  -0.489  1.00 85.08  ? 14  SER A OG  1 
ATOM   114  N  N   . LYS A 1 15  ? -37.245 -6.964  1.853   1.00 88.98  ? 15  LYS A N   1 
ATOM   115  C  CA  . LYS A 1 15  ? -36.232 -6.154  2.523   1.00 83.95  ? 15  LYS A CA  1 
ATOM   116  C  C   . LYS A 1 15  ? -34.818 -6.616  2.186   1.00 82.52  ? 15  LYS A C   1 
ATOM   117  O  O   . LYS A 1 15  ? -33.920 -5.786  2.019   1.00 89.08  ? 15  LYS A O   1 
ATOM   118  C  CB  . LYS A 1 15  ? -36.454 -6.200  4.037   1.00 86.25  ? 15  LYS A CB  1 
ATOM   119  N  N   . ASN A 1 16  ? -34.589 -7.927  2.100   1.00 84.34  ? 16  ASN A N   1 
ATOM   120  C  CA  . ASN A 1 16  ? -33.255 -8.461  1.860   1.00 81.28  ? 16  ASN A CA  1 
ATOM   121  C  C   . ASN A 1 16  ? -33.051 -8.912  0.421   1.00 78.44  ? 16  ASN A C   1 
ATOM   122  O  O   . ASN A 1 16  ? -32.065 -9.602  0.131   1.00 71.70  ? 16  ASN A O   1 
ATOM   123  C  CB  . ASN A 1 16  ? -32.965 -9.624  2.815   1.00 94.45  ? 16  ASN A CB  1 
ATOM   124  C  CG  . ASN A 1 16  ? -33.842 -10.829 2.552   1.00 96.76  ? 16  ASN A CG  1 
ATOM   125  O  OD1 . ASN A 1 16  ? -34.728 -10.797 1.695   1.00 92.76  ? 16  ASN A OD1 1 
ATOM   126  N  ND2 . ASN A 1 16  ? -33.587 -11.911 3.279   1.00 99.59  ? 16  ASN A ND2 1 
ATOM   127  N  N   . ALA A 1 17  ? -33.958 -8.549  -0.482  1.00 72.49  ? 17  ALA A N   1 
ATOM   128  C  CA  . ALA A 1 17  ? -33.739 -8.788  -1.901  1.00 66.39  ? 17  ALA A CA  1 
ATOM   129  C  C   . ALA A 1 17  ? -32.608 -7.893  -2.408  1.00 53.35  ? 17  ALA A C   1 
ATOM   130  O  O   . ALA A 1 17  ? -32.188 -6.938  -1.752  1.00 58.90  ? 17  ALA A O   1 
ATOM   131  C  CB  . ALA A 1 17  ? -35.017 -8.529  -2.696  1.00 64.14  ? 17  ALA A CB  1 
ATOM   132  N  N   . TYR A 1 18  ? -32.110 -8.212  -3.591  1.00 52.33  ? 18  TYR A N   1 
ATOM   133  C  CA  . TYR A 1 18  ? -31.002 -7.481  -4.191  1.00 57.64  ? 18  TYR A CA  1 
ATOM   134  C  C   . TYR A 1 18  ? -31.507 -6.612  -5.335  1.00 54.75  ? 18  TYR A C   1 
ATOM   135  O  O   . TYR A 1 18  ? -32.235 -7.088  -6.215  1.00 54.05  ? 18  TYR A O   1 
ATOM   136  C  CB  . TYR A 1 18  ? -29.923 -8.443  -4.700  1.00 52.38  ? 18  TYR A CB  1 
ATOM   137  C  CG  . TYR A 1 18  ? -29.207 -9.199  -3.601  1.00 50.84  ? 18  TYR A CG  1 
ATOM   138  C  CD1 . TYR A 1 18  ? -28.210 -8.594  -2.855  1.00 47.78  ? 18  TYR A CD1 1 
ATOM   139  C  CD2 . TYR A 1 18  ? -29.519 -10.524 -3.324  1.00 53.89  ? 18  TYR A CD2 1 
ATOM   140  C  CE1 . TYR A 1 18  ? -27.543 -9.282  -1.857  1.00 54.31  ? 18  TYR A CE1 1 
ATOM   141  C  CE2 . TYR A 1 18  ? -28.863 -11.221 -2.335  1.00 48.97  ? 18  TYR A CE2 1 
ATOM   142  C  CZ  . TYR A 1 18  ? -27.873 -10.596 -1.601  1.00 59.44  ? 18  TYR A CZ  1 
ATOM   143  O  OH  . TYR A 1 18  ? -27.214 -11.288 -0.606  1.00 57.48  ? 18  TYR A OH  1 
ATOM   144  N  N   . ARG A 1 19  ? -31.129 -5.332  -5.307  1.00 51.60  ? 19  ARG A N   1 
ATOM   145  C  CA  . ARG A 1 19  ? -31.337 -4.478  -6.471  1.00 49.49  ? 19  ARG A CA  1 
ATOM   146  C  C   . ARG A 1 19  ? -30.372 -4.829  -7.598  1.00 49.89  ? 19  ARG A C   1 
ATOM   147  O  O   . ARG A 1 19  ? -30.677 -4.582  -8.770  1.00 50.73  ? 19  ARG A O   1 
ATOM   148  C  CB  . ARG A 1 19  ? -31.176 -3.011  -6.080  1.00 50.69  ? 19  ARG A CB  1 
ATOM   149  C  CG  . ARG A 1 19  ? -32.282 -2.498  -5.173  1.00 58.21  ? 19  ARG A CG  1 
ATOM   150  C  CD  . ARG A 1 19  ? -31.746 -1.499  -4.165  1.00 61.81  ? 19  ARG A CD  1 
ATOM   151  N  NE  . ARG A 1 19  ? -31.294 -0.264  -4.794  1.00 56.15  ? 19  ARG A NE  1 
ATOM   152  C  CZ  . ARG A 1 19  ? -30.721 0.737   -4.141  1.00 60.54  ? 19  ARG A CZ  1 
ATOM   153  N  NH1 . ARG A 1 19  ? -30.502 0.676   -2.833  1.00 66.66  ? 19  ARG A NH1 1 
ATOM   154  N  NH2 . ARG A 1 19  ? -30.356 1.824   -4.817  1.00 54.47  ? 19  ARG A NH2 1 
ATOM   155  N  N   . LEU A 1 20  ? -29.213 -5.401  -7.269  1.00 45.50  ? 20  LEU A N   1 
ATOM   156  C  CA  . LEU A 1 20  ? -28.218 -5.755  -8.273  1.00 37.07  ? 20  LEU A CA  1 
ATOM   157  C  C   . LEU A 1 20  ? -27.415 -6.958  -7.808  1.00 49.86  ? 20  LEU A C   1 
ATOM   158  O  O   . LEU A 1 20  ? -26.928 -6.988  -6.669  1.00 50.59  ? 20  LEU A O   1 
ATOM   159  C  CB  . LEU A 1 20  ? -27.274 -4.578  -8.549  1.00 44.13  ? 20  LEU A CB  1 
ATOM   160  C  CG  . LEU A 1 20  ? -26.271 -4.772  -9.693  1.00 51.15  ? 20  LEU A CG  1 
ATOM   161  C  CD1 . LEU A 1 20  ? -26.974 -5.065  -11.019 1.00 38.82  ? 20  LEU A CD1 1 
ATOM   162  C  CD2 . LEU A 1 20  ? -25.370 -3.552  -9.833  1.00 52.95  ? 20  LEU A CD2 1 
ATOM   163  N  N   . ILE A 1 21  ? -27.293 -7.950  -8.689  1.00 41.88  ? 21  ILE A N   1 
ATOM   164  C  CA  . ILE A 1 21  ? -26.364 -9.063  -8.533  1.00 42.54  ? 21  ILE A CA  1 
ATOM   165  C  C   . ILE A 1 21  ? -25.550 -9.121  -9.816  1.00 44.04  ? 21  ILE A C   1 
ATOM   166  O  O   . ILE A 1 21  ? -26.110 -9.379  -10.891 1.00 47.96  ? 21  ILE A O   1 
ATOM   167  C  CB  . ILE A 1 21  ? -27.079 -10.400 -8.291  1.00 40.85  ? 21  ILE A CB  1 
ATOM   168  C  CG1 . ILE A 1 21  ? -27.981 -10.313 -7.067  1.00 48.57  ? 21  ILE A CG1 1 
ATOM   169  C  CG2 . ILE A 1 21  ? -26.067 -11.523 -8.130  1.00 45.47  ? 21  ILE A CG2 1 
ATOM   170  C  CD1 . ILE A 1 21  ? -28.852 -11.546 -6.858  1.00 53.87  ? 21  ILE A CD1 1 
ATOM   171  N  N   . LEU A 1 22  ? -24.244 -8.893  -9.715  1.00 41.06  ? 22  LEU A N   1 
ATOM   172  C  CA  . LEU A 1 22  ? -23.382 -8.798  -10.885 1.00 40.66  ? 22  LEU A CA  1 
ATOM   173  C  C   . LEU A 1 22  ? -22.187 -9.724  -10.733 1.00 44.04  ? 22  LEU A C   1 
ATOM   174  O  O   . LEU A 1 22  ? -21.622 -9.850  -9.644  1.00 49.09  ? 22  LEU A O   1 
ATOM   175  C  CB  . LEU A 1 22  ? -22.914 -7.361  -11.101 1.00 41.23  ? 22  LEU A CB  1 
ATOM   176  C  CG  . LEU A 1 22  ? -22.107 -7.101  -12.375 1.00 44.04  ? 22  LEU A CG  1 
ATOM   177  C  CD1 . LEU A 1 22  ? -22.435 -5.717  -12.917 1.00 44.44  ? 22  LEU A CD1 1 
ATOM   178  C  CD2 . LEU A 1 22  ? -20.613 -7.224  -12.139 1.00 38.25  ? 22  LEU A CD2 1 
ATOM   179  N  N   . ALA A 1 23  ? -21.812 -10.366 -11.835 1.00 43.57  ? 23  ALA A N   1 
ATOM   180  C  CA  . ALA A 1 23  ? -20.694 -11.303 -11.881 1.00 43.65  ? 23  ALA A CA  1 
ATOM   181  C  C   . ALA A 1 23  ? -19.992 -11.125 -13.220 1.00 47.86  ? 23  ALA A C   1 
ATOM   182  O  O   . ALA A 1 23  ? -20.599 -11.350 -14.270 1.00 39.65  ? 23  ALA A O   1 
ATOM   183  C  CB  . ALA A 1 23  ? -21.181 -12.745 -11.717 1.00 45.08  ? 23  ALA A CB  1 
ATOM   184  N  N   . ALA A 1 24  ? -18.726 -10.723 -13.184 1.00 46.12  ? 24  ALA A N   1 
ATOM   185  C  CA  . ALA A 1 24  ? -18.017 -10.334 -14.389 1.00 37.82  ? 24  ALA A CA  1 
ATOM   186  C  C   . ALA A 1 24  ? -16.627 -10.944 -14.417 1.00 43.42  ? 24  ALA A C   1 
ATOM   187  O  O   . ALA A 1 24  ? -15.948 -11.014 -13.388 1.00 49.72  ? 24  ALA A O   1 
ATOM   188  C  CB  . ALA A 1 24  ? -17.903 -8.802  -14.484 1.00 40.77  ? 24  ALA A CB  1 
ATOM   189  N  N   . ASN A 1 25  ? -16.213 -11.374 -15.605 1.00 37.86  ? 25  ASN A N   1 
ATOM   190  C  CA  . ASN A 1 25  ? -14.848 -11.802 -15.863 1.00 38.63  ? 25  ASN A CA  1 
ATOM   191  C  C   . ASN A 1 25  ? -14.178 -10.791 -16.780 1.00 44.43  ? 25  ASN A C   1 
ATOM   192  O  O   . ASN A 1 25  ? -14.781 -10.333 -17.760 1.00 49.76  ? 25  ASN A O   1 
ATOM   193  C  CB  . ASN A 1 25  ? -14.812 -13.184 -16.525 1.00 44.70  ? 25  ASN A CB  1 
ATOM   194  C  CG  . ASN A 1 25  ? -15.119 -14.298 -15.563 1.00 45.68  ? 25  ASN A CG  1 
ATOM   195  O  OD1 . ASN A 1 25  ? -15.016 -14.126 -14.349 1.00 40.16  ? 25  ASN A OD1 1 
ATOM   196  N  ND2 . ASN A 1 25  ? -15.492 -15.454 -16.096 1.00 45.11  ? 25  ASN A ND2 1 
ATOM   197  N  N   . ARG A 1 26  ? -12.937 -10.448 -16.468 1.00 43.20  ? 26  ARG A N   1 
ATOM   198  C  CA  . ARG A 1 26  ? -12.122 -9.594  -17.326 1.00 48.31  ? 26  ARG A CA  1 
ATOM   199  C  C   . ARG A 1 26  ? -11.075 -10.489 -17.979 1.00 52.23  ? 26  ARG A C   1 
ATOM   200  O  O   . ARG A 1 26  ? -10.180 -11.007 -17.301 1.00 52.86  ? 26  ARG A O   1 
ATOM   201  C  CB  . ARG A 1 26  ? -11.470 -8.459  -16.543 1.00 55.45  ? 26  ARG A CB  1 
ATOM   202  C  CG  . ARG A 1 26  ? -10.871 -7.364  -17.428 1.00 62.30  ? 26  ARG A CG  1 
ATOM   203  C  CD  . ARG A 1 26  ? -9.341  -7.336  -17.370 1.00 63.74  ? 26  ARG A CD  1 
ATOM   204  N  NE  . ARG A 1 26  ? -8.836  -7.266  -16.000 1.00 73.45  ? 26  ARG A NE  1 
ATOM   205  C  CZ  . ARG A 1 26  ? -7.549  -7.220  -15.671 1.00 67.46  ? 26  ARG A CZ  1 
ATOM   206  N  NH1 . ARG A 1 26  ? -6.601  -7.201  -16.592 1.00 69.68  ? 26  ARG A NH1 1 
ATOM   207  N  NH2 . ARG A 1 26  ? -7.207  -7.184  -14.388 1.00 62.62  ? 26  ARG A NH2 1 
ATOM   208  N  N   . ASP A 1 27  ? -11.203 -10.685 -19.285 1.00 47.16  ? 27  ASP A N   1 
ATOM   209  C  CA  . ASP A 1 27  ? -10.241 -11.443 -20.072 1.00 48.77  ? 27  ASP A CA  1 
ATOM   210  C  C   . ASP A 1 27  ? -9.271  -10.463 -20.717 1.00 52.18  ? 27  ASP A C   1 
ATOM   211  O  O   . ASP A 1 27  ? -9.692  -9.478  -21.334 1.00 45.67  ? 27  ASP A O   1 
ATOM   212  C  CB  . ASP A 1 27  ? -10.959 -12.275 -21.133 1.00 44.64  ? 27  ASP A CB  1 
ATOM   213  C  CG  . ASP A 1 27  ? -12.035 -13.169 -20.540 1.00 46.22  ? 27  ASP A CG  1 
ATOM   214  O  OD1 . ASP A 1 27  ? -12.052 -13.345 -19.300 1.00 47.64  ? 27  ASP A OD1 1 
ATOM   215  O  OD2 . ASP A 1 27  ? -12.877 -13.685 -21.304 1.00 48.44  ? 27  ASP A OD2 1 
ATOM   216  N  N   . GLU A 1 28  ? -7.977  -10.722 -20.557 1.00 47.62  ? 28  GLU A N   1 
ATOM   217  C  CA  . GLU A 1 28  ? -6.950  -9.826  -21.071 1.00 47.97  ? 28  GLU A CA  1 
ATOM   218  C  C   . GLU A 1 28  ? -5.654  -10.613 -21.187 1.00 46.87  ? 28  GLU A C   1 
ATOM   219  O  O   . GLU A 1 28  ? -5.505  -11.690 -20.603 1.00 48.95  ? 28  GLU A O   1 
ATOM   220  C  CB  . GLU A 1 28  ? -6.786  -8.599  -20.162 1.00 57.13  ? 28  GLU A CB  1 
ATOM   221  C  CG  . GLU A 1 28  ? -5.782  -7.558  -20.647 1.00 62.66  ? 28  GLU A CG  1 
ATOM   222  C  CD  . GLU A 1 28  ? -6.174  -6.923  -21.973 1.00 63.89  ? 28  GLU A CD  1 
ATOM   223  O  OE1 . GLU A 1 28  ? -7.208  -6.221  -22.025 1.00 66.81  ? 28  GLU A OE1 1 
ATOM   224  O  OE2 . GLU A 1 28  ? -5.444  -7.135  -22.963 1.00 59.21  ? 28  GLU A OE2 1 
ATOM   225  N  N   . PHE A 1 29  ? -4.725  -10.079 -21.971 1.00 52.17  ? 29  PHE A N   1 
ATOM   226  C  CA  . PHE A 1 29  ? -3.388  -10.653 -22.019 1.00 58.17  ? 29  PHE A CA  1 
ATOM   227  C  C   . PHE A 1 29  ? -2.739  -10.522 -20.644 1.00 59.28  ? 29  PHE A C   1 
ATOM   228  O  O   . PHE A 1 29  ? -2.811  -9.468  -20.007 1.00 53.65  ? 29  PHE A O   1 
ATOM   229  C  CB  . PHE A 1 29  ? -2.538  -9.964  -23.090 1.00 59.48  ? 29  PHE A CB  1 
ATOM   230  C  CG  . PHE A 1 29  ? -3.018  -10.208 -24.503 1.00 59.64  ? 29  PHE A CG  1 
ATOM   231  C  CD1 . PHE A 1 29  ? -2.766  -11.420 -25.142 1.00 62.73  ? 29  PHE A CD1 1 
ATOM   232  C  CD2 . PHE A 1 29  ? -3.710  -9.224  -25.195 1.00 57.41  ? 29  PHE A CD2 1 
ATOM   233  C  CE1 . PHE A 1 29  ? -3.209  -11.651 -26.443 1.00 59.75  ? 29  PHE A CE1 1 
ATOM   234  C  CE2 . PHE A 1 29  ? -4.148  -9.441  -26.499 1.00 59.75  ? 29  PHE A CE2 1 
ATOM   235  C  CZ  . PHE A 1 29  ? -3.900  -10.656 -27.121 1.00 54.65  ? 29  PHE A CZ  1 
ATOM   236  N  N   . TYR A 1 30  ? -2.108  -11.605 -20.185 1.00 57.19  ? 30  TYR A N   1 
ATOM   237  C  CA  . TYR A 1 30  ? -1.506  -11.619 -18.857 1.00 60.73  ? 30  TYR A CA  1 
ATOM   238  C  C   . TYR A 1 30  ? -0.351  -10.632 -18.727 1.00 62.53  ? 30  TYR A C   1 
ATOM   239  O  O   . TYR A 1 30  ? 0.043   -10.301 -17.603 1.00 62.61  ? 30  TYR A O   1 
ATOM   240  C  CB  . TYR A 1 30  ? -1.029  -13.040 -18.534 1.00 58.70  ? 30  TYR A CB  1 
ATOM   241  C  CG  . TYR A 1 30  ? -2.134  -14.077 -18.557 1.00 57.50  ? 30  TYR A CG  1 
ATOM   242  C  CD1 . TYR A 1 30  ? -3.420  -13.763 -18.131 1.00 57.35  ? 30  TYR A CD1 1 
ATOM   243  C  CD2 . TYR A 1 30  ? -1.894  -15.368 -19.014 1.00 59.43  ? 30  TYR A CD2 1 
ATOM   244  C  CE1 . TYR A 1 30  ? -4.437  -14.708 -18.154 1.00 50.38  ? 30  TYR A CE1 1 
ATOM   245  C  CE2 . TYR A 1 30  ? -2.904  -16.320 -19.037 1.00 57.26  ? 30  TYR A CE2 1 
ATOM   246  C  CZ  . TYR A 1 30  ? -4.172  -15.982 -18.605 1.00 53.15  ? 30  TYR A CZ  1 
ATOM   247  O  OH  . TYR A 1 30  ? -5.179  -16.923 -18.637 1.00 52.74  ? 30  TYR A OH  1 
ATOM   248  N  N   . SER A 1 31  ? 0.193   -10.146 -19.843 1.00 60.82  ? 31  SER A N   1 
ATOM   249  C  CA  . SER A 1 31  ? 1.311   -9.211  -19.783 1.00 67.90  ? 31  SER A CA  1 
ATOM   250  C  C   . SER A 1 31  ? 0.891   -7.808  -19.351 1.00 69.12  ? 31  SER A C   1 
ATOM   251  O  O   . SER A 1 31  ? 1.735   -7.046  -18.866 1.00 71.22  ? 31  SER A O   1 
ATOM   252  C  CB  . SER A 1 31  ? 1.997   -9.134  -21.149 1.00 70.71  ? 31  SER A CB  1 
ATOM   253  O  OG  . SER A 1 31  ? 1.099   -8.669  -22.156 1.00 62.40  ? 31  SER A OG  1 
ATOM   254  N  N   . ARG A 1 32  ? -0.378  -7.454  -19.504 1.00 63.39  ? 32  ARG A N   1 
ATOM   255  C  CA  . ARG A 1 32  ? -0.809  -6.072  -19.298 1.00 63.95  ? 32  ARG A CA  1 
ATOM   256  C  C   . ARG A 1 32  ? -0.824  -5.735  -17.813 1.00 61.36  ? 32  ARG A C   1 
ATOM   257  O  O   . ARG A 1 32  ? -1.558  -6.373  -17.055 1.00 50.41  ? 32  ARG A O   1 
ATOM   258  C  CB  . ARG A 1 32  ? -2.198  -5.883  -19.908 1.00 61.22  ? 32  ARG A CB  1 
ATOM   259  C  CG  . ARG A 1 32  ? -2.650  -4.437  -20.049 1.00 65.32  ? 32  ARG A CG  1 
ATOM   260  C  CD  . ARG A 1 32  ? -3.815  -4.334  -21.026 1.00 64.33  ? 32  ARG A CD  1 
ATOM   261  N  NE  . ARG A 1 32  ? -4.331  -2.977  -21.150 1.00 65.64  ? 32  ARG A NE  1 
ATOM   262  C  CZ  . ARG A 1 32  ? -5.112  -2.562  -22.139 1.00 76.55  ? 32  ARG A CZ  1 
ATOM   263  N  NH1 . ARG A 1 32  ? -5.481  -3.375  -23.120 1.00 73.74  ? 32  ARG A NH1 1 
ATOM   264  N  NH2 . ARG A 1 32  ? -5.527  -1.298  -22.149 1.00 77.62  ? 32  ARG A NH2 1 
ATOM   265  N  N   . PRO A 1 33  ? -0.047  -4.753  -17.354 1.00 57.63  ? 33  PRO A N   1 
ATOM   266  C  CA  . PRO A 1 33  ? -0.051  -4.432  -15.924 1.00 59.43  ? 33  PRO A CA  1 
ATOM   267  C  C   . PRO A 1 33  ? -1.400  -3.898  -15.459 1.00 58.50  ? 33  PRO A C   1 
ATOM   268  O  O   . PRO A 1 33  ? -2.107  -3.195  -16.181 1.00 61.80  ? 33  PRO A O   1 
ATOM   269  C  CB  . PRO A 1 33  ? 1.050   -3.368  -15.794 1.00 66.69  ? 33  PRO A CB  1 
ATOM   270  C  CG  . PRO A 1 33  ? 1.201   -2.789  -17.161 1.00 63.49  ? 33  PRO A CG  1 
ATOM   271  C  CD  . PRO A 1 33  ? 0.902   -3.912  -18.114 1.00 64.68  ? 33  PRO A CD  1 
ATOM   272  N  N   . SER A 1 34  ? -1.754  -4.249  -14.221 1.00 59.20  ? 34  SER A N   1 
ATOM   273  C  CA  . SER A 1 34  ? -3.014  -3.817  -13.634 1.00 54.47  ? 34  SER A CA  1 
ATOM   274  C  C   . SER A 1 34  ? -2.828  -3.636  -12.138 1.00 59.76  ? 34  SER A C   1 
ATOM   275  O  O   . SER A 1 34  ? -1.885  -4.162  -11.542 1.00 70.38  ? 34  SER A O   1 
ATOM   276  C  CB  . SER A 1 34  ? -4.140  -4.826  -13.894 1.00 55.57  ? 34  SER A CB  1 
ATOM   277  O  OG  . SER A 1 34  ? -4.083  -5.311  -15.224 1.00 70.77  ? 34  SER A OG  1 
ATOM   278  N  N   . LYS A 1 35  ? -3.743  -2.887  -11.531 1.00 61.17  ? 35  LYS A N   1 
ATOM   279  C  CA  . LYS A 1 35  ? -3.779  -2.710  -10.087 1.00 60.77  ? 35  LYS A CA  1 
ATOM   280  C  C   . LYS A 1 35  ? -5.079  -3.291  -9.545  1.00 54.25  ? 35  LYS A C   1 
ATOM   281  O  O   . LYS A 1 35  ? -6.143  -3.143  -10.159 1.00 55.22  ? 35  LYS A O   1 
ATOM   282  C  CB  . LYS A 1 35  ? -3.659  -1.233  -9.682  1.00 59.28  ? 35  LYS A CB  1 
ATOM   283  C  CG  . LYS A 1 35  ? -2.219  -0.727  -9.550  1.00 76.49  ? 35  LYS A CG  1 
ATOM   284  C  CD  . LYS A 1 35  ? -1.377  -1.615  -8.628  1.00 84.96  ? 35  LYS A CD  1 
ATOM   285  C  CE  . LYS A 1 35  ? 0.000   -1.027  -8.366  1.00 84.73  ? 35  LYS A CE  1 
ATOM   286  N  NZ  . LYS A 1 35  ? 0.572   -1.556  -7.089  1.00 95.60  ? 35  LYS A NZ  1 
ATOM   287  N  N   . LEU A 1 36  ? -4.981  -3.955  -8.395  1.00 46.98  ? 36  LEU A N   1 
ATOM   288  C  CA  . LEU A 1 36  ? -6.130  -4.585  -7.775  1.00 48.52  ? 36  LEU A CA  1 
ATOM   289  C  C   . LEU A 1 36  ? -7.096  -3.530  -7.247  1.00 47.42  ? 36  LEU A C   1 
ATOM   290  O  O   . LEU A 1 36  ? -6.725  -2.389  -6.955  1.00 47.30  ? 36  LEU A O   1 
ATOM   291  C  CB  . LEU A 1 36  ? -5.682  -5.506  -6.646  1.00 50.40  ? 36  LEU A CB  1 
ATOM   292  C  CG  . LEU A 1 36  ? -5.400  -6.956  -7.041  1.00 54.03  ? 36  LEU A CG  1 
ATOM   293  C  CD1 . LEU A 1 36  ? -4.400  -7.042  -8.184  1.00 49.89  ? 36  LEU A CD1 1 
ATOM   294  C  CD2 . LEU A 1 36  ? -4.900  -7.743  -5.824  1.00 45.39  ? 36  LEU A CD2 1 
ATOM   295  N  N   . ALA A 1 37  ? -8.359  -3.939  -7.119  1.00 43.89  ? 37  ALA A N   1 
ATOM   296  C  CA  . ALA A 1 37  ? -9.413  -3.002  -6.747  1.00 50.86  ? 37  ALA A CA  1 
ATOM   297  C  C   . ALA A 1 37  ? -9.094  -2.333  -5.418  1.00 47.47  ? 37  ALA A C   1 
ATOM   298  O  O   . ALA A 1 37  ? -8.606  -2.969  -4.477  1.00 44.06  ? 37  ALA A O   1 
ATOM   299  C  CB  . ALA A 1 37  ? -10.761 -3.722  -6.660  1.00 44.39  ? 37  ALA A CB  1 
ATOM   300  N  N   . ASP A 1 38  ? -9.363  -1.033  -5.350  1.00 50.05  ? 38  ASP A N   1 
ATOM   301  C  CA  . ASP A 1 38  ? -9.218  -0.263  -4.118  1.00 48.32  ? 38  ASP A CA  1 
ATOM   302  C  C   . ASP A 1 38  ? -9.873  1.089   -4.370  1.00 47.35  ? 38  ASP A C   1 
ATOM   303  O  O   . ASP A 1 38  ? -10.193 1.443   -5.509  1.00 51.06  ? 38  ASP A O   1 
ATOM   304  C  CB  . ASP A 1 38  ? -7.753  -0.113  -3.702  1.00 45.09  ? 38  ASP A CB  1 
ATOM   305  C  CG  . ASP A 1 38  ? -7.584  0.038   -2.191  1.00 50.79  ? 38  ASP A CG  1 
ATOM   306  O  OD1 . ASP A 1 38  ? -8.568  0.356   -1.494  1.00 42.89  ? 38  ASP A OD1 1 
ATOM   307  O  OD2 . ASP A 1 38  ? -6.456  -0.158  -1.693  1.00 56.91  ? 38  ASP A OD2 1 
ATOM   308  N  N   . PHE A 1 39  ? -10.075 1.834   -3.297  1.00 49.97  ? 39  PHE A N   1 
ATOM   309  C  CA  . PHE A 1 39  ? -10.734 3.127   -3.399  1.00 53.05  ? 39  PHE A CA  1 
ATOM   310  C  C   . PHE A 1 39  ? -9.765  4.185   -3.906  1.00 53.81  ? 39  PHE A C   1 
ATOM   311  O  O   . PHE A 1 39  ? -8.600  4.235   -3.501  1.00 53.01  ? 39  PHE A O   1 
ATOM   312  C  CB  . PHE A 1 39  ? -11.305 3.537   -2.042  1.00 54.22  ? 39  PHE A CB  1 
ATOM   313  C  CG  . PHE A 1 39  ? -12.431 2.664   -1.577  1.00 51.36  ? 39  PHE A CG  1 
ATOM   314  C  CD1 . PHE A 1 39  ? -13.721 2.869   -2.043  1.00 50.73  ? 39  PHE A CD1 1 
ATOM   315  C  CD2 . PHE A 1 39  ? -12.204 1.637   -0.678  1.00 49.02  ? 39  PHE A CD2 1 
ATOM   316  C  CE1 . PHE A 1 39  ? -14.763 2.068   -1.614  1.00 52.00  ? 39  PHE A CE1 1 
ATOM   317  C  CE2 . PHE A 1 39  ? -13.242 0.831   -0.247  1.00 46.37  ? 39  PHE A CE2 1 
ATOM   318  C  CZ  . PHE A 1 39  ? -14.521 1.047   -0.713  1.00 49.06  ? 39  PHE A CZ  1 
ATOM   319  N  N   . TRP A 1 40  ? -10.263 5.030   -4.801  1.00 52.87  ? 40  TRP A N   1 
ATOM   320  C  CA  . TRP A 1 40  ? -9.496  6.132   -5.364  1.00 60.80  ? 40  TRP A CA  1 
ATOM   321  C  C   . TRP A 1 40  ? -10.470 7.264   -5.665  1.00 59.65  ? 40  TRP A C   1 
ATOM   322  O  O   . TRP A 1 40  ? -11.646 7.209   -5.291  1.00 59.68  ? 40  TRP A O   1 
ATOM   323  C  CB  . TRP A 1 40  ? -8.723  5.684   -6.612  1.00 50.46  ? 40  TRP A CB  1 
ATOM   324  C  CG  . TRP A 1 40  ? -9.581  5.071   -7.680  1.00 53.16  ? 40  TRP A CG  1 
ATOM   325  C  CD1 . TRP A 1 40  ? -10.031 3.783   -7.729  1.00 52.52  ? 40  TRP A CD1 1 
ATOM   326  C  CD2 . TRP A 1 40  ? -10.087 5.715   -8.854  1.00 55.85  ? 40  TRP A CD2 1 
ATOM   327  N  NE1 . TRP A 1 40  ? -10.787 3.587   -8.858  1.00 54.79  ? 40  TRP A NE1 1 
ATOM   328  C  CE2 . TRP A 1 40  ? -10.837 4.757   -9.566  1.00 53.36  ? 40  TRP A CE2 1 
ATOM   329  C  CE3 . TRP A 1 40  ? -9.979  7.009   -9.373  1.00 57.47  ? 40  TRP A CE3 1 
ATOM   330  C  CZ2 . TRP A 1 40  ? -11.475 5.050   -10.772 1.00 56.54  ? 40  TRP A CZ2 1 
ATOM   331  C  CZ3 . TRP A 1 40  ? -10.618 7.299   -10.573 1.00 59.34  ? 40  TRP A CZ3 1 
ATOM   332  C  CH2 . TRP A 1 40  ? -11.355 6.325   -11.256 1.00 54.33  ? 40  TRP A CH2 1 
ATOM   333  N  N   . GLY A 1 41  ? -9.989  8.287   -6.347  1.00 62.71  ? 41  GLY A N   1 
ATOM   334  C  CA  . GLY A 1 41  ? -10.797 9.453   -6.642  1.00 66.74  ? 41  GLY A CA  1 
ATOM   335  C  C   . GLY A 1 41  ? -10.586 10.557  -5.620  1.00 78.06  ? 41  GLY A C   1 
ATOM   336  O  O   . GLY A 1 41  ? -9.801  10.444  -4.675  1.00 83.67  ? 41  GLY A O   1 
ATOM   337  N  N   . ASN A 1 42  ? -11.329 11.641  -5.830  1.00 92.78  ? 42  ASN A N   1 
ATOM   338  C  CA  . ASN A 1 42  ? -11.152 12.822  -4.996  1.00 97.07  ? 42  ASN A CA  1 
ATOM   339  C  C   . ASN A 1 42  ? -11.433 12.511  -3.531  1.00 100.71 ? 42  ASN A C   1 
ATOM   340  O  O   . ASN A 1 42  ? -10.650 12.878  -2.645  1.00 102.34 ? 42  ASN A O   1 
ATOM   341  C  CB  . ASN A 1 42  ? -12.062 13.948  -5.489  1.00 100.31 ? 42  ASN A CB  1 
ATOM   342  C  CG  . ASN A 1 42  ? -11.467 14.709  -6.656  1.00 103.43 ? 42  ASN A CG  1 
ATOM   343  O  OD1 . ASN A 1 42  ? -10.261 14.660  -6.896  1.00 103.97 ? 42  ASN A OD1 1 
ATOM   344  N  ND2 . ASN A 1 42  ? -12.311 15.432  -7.380  1.00 105.99 ? 42  ASN A ND2 1 
ATOM   345  N  N   . ASN A 1 43  ? -12.540 11.822  -3.255  1.00 84.78  ? 43  ASN A N   1 
ATOM   346  C  CA  . ASN A 1 43  ? -12.978 11.560  -1.889  1.00 75.18  ? 43  ASN A CA  1 
ATOM   347  C  C   . ASN A 1 43  ? -12.913 10.073  -1.555  1.00 72.48  ? 43  ASN A C   1 
ATOM   348  O  O   . ASN A 1 43  ? -13.697 9.579   -0.742  1.00 65.02  ? 43  ASN A O   1 
ATOM   349  C  CB  . ASN A 1 43  ? -14.398 12.086  -1.672  1.00 87.05  ? 43  ASN A CB  1 
ATOM   350  C  CG  . ASN A 1 43  ? -14.638 13.437  -2.335  1.00 94.82  ? 43  ASN A CG  1 
ATOM   351  O  OD1 . ASN A 1 43  ? -14.274 13.654  -3.490  1.00 99.72  ? 43  ASN A OD1 1 
ATOM   352  N  ND2 . ASN A 1 43  ? -15.263 14.348  -1.604  1.00 80.89  ? 43  ASN A ND2 1 
ATOM   353  N  N   . ASN A 1 44  ? -11.983 9.347   -2.183  1.00 76.77  ? 44  ASN A N   1 
ATOM   354  C  CA  . ASN A 1 44  ? -11.923 7.888   -2.069  1.00 74.29  ? 44  ASN A CA  1 
ATOM   355  C  C   . ASN A 1 44  ? -13.274 7.260   -2.409  1.00 61.30  ? 44  ASN A C   1 
ATOM   356  O  O   . ASN A 1 44  ? -13.605 6.168   -1.946  1.00 62.65  ? 44  ASN A O   1 
ATOM   357  C  CB  . ASN A 1 44  ? -11.466 7.449   -0.674  1.00 67.01  ? 44  ASN A CB  1 
ATOM   358  C  CG  . ASN A 1 44  ? -9.952  7.404   -0.537  1.00 64.53  ? 44  ASN A CG  1 
ATOM   359  O  OD1 . ASN A 1 44  ? -9.218  7.519   -1.521  1.00 67.55  ? 44  ASN A OD1 1 
ATOM   360  N  ND2 . ASN A 1 44  ? -9.480  7.218   0.686   1.00 82.91  ? 44  ASN A ND2 1 
ATOM   361  N  N   . GLU A 1 45  ? -14.059 7.946   -3.234  1.00 63.96  ? 45  GLU A N   1 
ATOM   362  C  CA  . GLU A 1 45  ? -15.449 7.583   -3.461  1.00 64.48  ? 45  GLU A CA  1 
ATOM   363  C  C   . GLU A 1 45  ? -15.642 6.610   -4.619  1.00 58.49  ? 45  GLU A C   1 
ATOM   364  O  O   . GLU A 1 45  ? -16.776 6.192   -4.857  1.00 59.28  ? 45  GLU A O   1 
ATOM   365  C  CB  . GLU A 1 45  ? -16.289 8.860   -3.683  1.00 66.45  ? 45  GLU A CB  1 
ATOM   366  C  CG  . GLU A 1 45  ? -16.524 9.300   -5.137  1.00 66.04  ? 45  GLU A CG  1 
ATOM   367  C  CD  . GLU A 1 45  ? -15.321 9.992   -5.763  1.00 81.59  ? 45  GLU A CD  1 
ATOM   368  O  OE1 . GLU A 1 45  ? -14.240 9.998   -5.143  1.00 80.71  ? 45  GLU A OE1 1 
ATOM   369  O  OE2 . GLU A 1 45  ? -15.462 10.529  -6.894  1.00 83.17  ? 45  GLU A OE2 1 
ATOM   370  N  N   . ILE A 1 46  ? -14.580 6.225   -5.328  1.00 59.50  ? 46  ILE A N   1 
ATOM   371  C  CA  . ILE A 1 46  ? -14.680 5.313   -6.461  1.00 57.22  ? 46  ILE A CA  1 
ATOM   372  C  C   . ILE A 1 46  ? -13.934 4.027   -6.131  1.00 53.92  ? 46  ILE A C   1 
ATOM   373  O  O   . ILE A 1 46  ? -12.844 4.065   -5.552  1.00 51.47  ? 46  ILE A O   1 
ATOM   374  C  CB  . ILE A 1 46  ? -14.127 5.937   -7.762  1.00 61.22  ? 46  ILE A CB  1 
ATOM   375  C  CG1 . ILE A 1 46  ? -14.799 7.283   -8.024  1.00 59.33  ? 46  ILE A CG1 1 
ATOM   376  C  CG2 . ILE A 1 46  ? -14.333 4.979   -8.942  1.00 50.59  ? 46  ILE A CG2 1 
ATOM   377  C  CD1 . ILE A 1 46  ? -14.324 7.969   -9.287  1.00 66.77  ? 46  ILE A CD1 1 
ATOM   378  N  N   . LEU A 1 47  ? -14.522 2.891   -6.510  1.00 49.56  ? 47  LEU A N   1 
ATOM   379  C  CA  . LEU A 1 47  ? -13.937 1.578   -6.266  1.00 47.85  ? 47  LEU A CA  1 
ATOM   380  C  C   . LEU A 1 47  ? -13.839 0.815   -7.580  1.00 50.16  ? 47  LEU A C   1 
ATOM   381  O  O   . LEU A 1 47  ? -14.854 0.601   -8.259  1.00 47.45  ? 47  LEU A O   1 
ATOM   382  C  CB  . LEU A 1 47  ? -14.775 0.797   -5.253  1.00 44.50  ? 47  LEU A CB  1 
ATOM   383  C  CG  . LEU A 1 47  ? -14.308 -0.627  -4.960  1.00 44.27  ? 47  LEU A CG  1 
ATOM   384  C  CD1 . LEU A 1 47  ? -12.893 -0.633  -4.409  1.00 43.62  ? 47  LEU A CD1 1 
ATOM   385  C  CD2 . LEU A 1 47  ? -15.271 -1.309  -4.006  1.00 45.62  ? 47  LEU A CD2 1 
ATOM   386  N  N   . SER A 1 48  ? -12.625 0.400   -7.935  1.00 47.84  ? 48  SER A N   1 
ATOM   387  C  CA  . SER A 1 48  ? -12.408 -0.357  -9.163  1.00 48.72  ? 48  SER A CA  1 
ATOM   388  C  C   . SER A 1 48  ? -10.940 -0.761  -9.237  1.00 45.18  ? 48  SER A C   1 
ATOM   389  O  O   . SER A 1 48  ? -10.089 -0.246  -8.509  1.00 40.23  ? 48  SER A O   1 
ATOM   390  C  CB  . SER A 1 48  ? -12.783 0.448   -10.407 1.00 48.15  ? 48  SER A CB  1 
ATOM   391  O  OG  . SER A 1 48  ? -11.887 1.540   -10.591 1.00 48.62  ? 48  SER A OG  1 
ATOM   392  N  N   . GLY A 1 49  ? -10.655 -1.703  -10.135 1.00 42.98  ? 49  GLY A N   1 
ATOM   393  C  CA  . GLY A 1 49  ? -9.301  -1.920  -10.571 1.00 40.92  ? 49  GLY A CA  1 
ATOM   394  C  C   . GLY A 1 49  ? -8.876  -0.822  -11.517 1.00 39.73  ? 49  GLY A C   1 
ATOM   395  O  O   . GLY A 1 49  ? -9.677  0.026   -11.912 1.00 43.38  ? 49  GLY A O   1 
ATOM   396  N  N   . LEU A 1 50  ? -7.599  -0.836  -11.883 1.00 40.64  ? 50  LEU A N   1 
ATOM   397  C  CA  . LEU A 1 50  ? -7.076  0.175   -12.795 1.00 55.44  ? 50  LEU A CA  1 
ATOM   398  C  C   . LEU A 1 50  ? -6.067  -0.430  -13.760 1.00 51.13  ? 50  LEU A C   1 
ATOM   399  O  O   . LEU A 1 50  ? -5.111  -1.088  -13.342 1.00 49.40  ? 50  LEU A O   1 
ATOM   400  C  CB  . LEU A 1 50  ? -6.435  1.330   -12.011 1.00 46.68  ? 50  LEU A CB  1 
ATOM   401  C  CG  . LEU A 1 50  ? -7.431  2.167   -11.203 1.00 51.44  ? 50  LEU A CG  1 
ATOM   402  C  CD1 . LEU A 1 50  ? -6.717  3.076   -10.208 1.00 44.81  ? 50  LEU A CD1 1 
ATOM   403  C  CD2 . LEU A 1 50  ? -8.310  2.989   -12.138 1.00 50.81  ? 50  LEU A CD2 1 
ATOM   404  N  N   . ASP A 1 51  ? -6.283  -0.191  -15.051 1.00 53.06  ? 51  ASP A N   1 
ATOM   405  C  CA  . ASP A 1 51  ? -5.264  -0.494  -16.047 1.00 50.85  ? 51  ASP A CA  1 
ATOM   406  C  C   . ASP A 1 51  ? -4.021  0.346   -15.772 1.00 57.45  ? 51  ASP A C   1 
ATOM   407  O  O   . ASP A 1 51  ? -4.111  1.486   -15.305 1.00 57.37  ? 51  ASP A O   1 
ATOM   408  C  CB  . ASP A 1 51  ? -5.803  -0.211  -17.449 1.00 58.17  ? 51  ASP A CB  1 
ATOM   409  C  CG  . ASP A 1 51  ? -4.814  -0.574  -18.544 1.00 67.53  ? 51  ASP A CG  1 
ATOM   410  O  OD1 . ASP A 1 51  ? -3.952  -1.450  -18.318 1.00 65.05  ? 51  ASP A OD1 1 
ATOM   411  O  OD2 . ASP A 1 51  ? -4.891  0.029   -19.637 1.00 69.74  ? 51  ASP A OD2 1 
ATOM   412  N  N   . MET A 1 52  ? -2.848  -0.235  -16.042 1.00 56.52  ? 52  MET A N   1 
ATOM   413  C  CA  . MET A 1 52  ? -1.578  0.455   -15.851 1.00 57.37  ? 52  MET A CA  1 
ATOM   414  C  C   . MET A 1 52  ? -0.712  0.403   -17.106 1.00 62.25  ? 52  MET A C   1 
ATOM   415  O  O   . MET A 1 52  ? 0.502   0.613   -17.024 1.00 61.04  ? 52  MET A O   1 
ATOM   416  C  CB  . MET A 1 52  ? -0.820  -0.136  -14.660 1.00 54.84  ? 52  MET A CB  1 
ATOM   417  C  CG  . MET A 1 52  ? -1.539  0.049   -13.333 1.00 68.61  ? 52  MET A CG  1 
ATOM   418  S  SD  . MET A 1 52  ? -1.740  1.784   -12.861 1.00 76.00  ? 52  MET A SD  1 
ATOM   419  C  CE  . MET A 1 52  ? -0.333  1.999   -11.769 1.00 68.55  ? 52  MET A CE  1 
ATOM   420  N  N   . GLU A 1 53  ? -1.311  0.126   -18.263 1.00 61.38  ? 53  GLU A N   1 
ATOM   421  C  CA  . GLU A 1 53  ? -0.575  0.179   -19.520 1.00 72.81  ? 53  GLU A CA  1 
ATOM   422  C  C   . GLU A 1 53  ? -0.015  1.579   -19.733 1.00 67.18  ? 53  GLU A C   1 
ATOM   423  O  O   . GLU A 1 53  ? -0.679  2.576   -19.444 1.00 71.76  ? 53  GLU A O   1 
ATOM   424  C  CB  . GLU A 1 53  ? -1.495  -0.206  -20.680 1.00 73.13  ? 53  GLU A CB  1 
ATOM   425  C  CG  . GLU A 1 53  ? -0.787  -0.494  -21.992 1.00 80.15  ? 53  GLU A CG  1 
ATOM   426  C  CD  . GLU A 1 53  ? -0.169  -1.883  -22.036 1.00 84.17  ? 53  GLU A CD  1 
ATOM   427  O  OE1 . GLU A 1 53  ? 0.702   -2.184  -21.190 1.00 79.42  ? 53  GLU A OE1 1 
ATOM   428  O  OE2 . GLU A 1 53  ? -0.561  -2.678  -22.918 1.00 86.71  ? 53  GLU A OE2 1 
ATOM   429  N  N   . GLU A 1 54  ? 1.219   1.654   -20.221 1.00 69.81  ? 54  GLU A N   1 
ATOM   430  C  CA  . GLU A 1 54  ? 1.835   2.952   -20.476 1.00 74.38  ? 54  GLU A CA  1 
ATOM   431  C  C   . GLU A 1 54  ? 0.988   3.745   -21.465 1.00 76.12  ? 54  GLU A C   1 
ATOM   432  O  O   . GLU A 1 54  ? 0.602   3.235   -22.522 1.00 74.99  ? 54  GLU A O   1 
ATOM   433  C  CB  . GLU A 1 54  ? 3.253   2.773   -21.015 1.00 68.81  ? 54  GLU A CB  1 
ATOM   434  N  N   . GLY A 1 55  ? 0.700   4.999   -21.119 1.00 79.69  ? 55  GLY A N   1 
ATOM   435  C  CA  . GLY A 1 55  ? -0.166  5.837   -21.921 1.00 77.75  ? 55  GLY A CA  1 
ATOM   436  C  C   . GLY A 1 55  ? -1.647  5.649   -21.679 1.00 80.26  ? 55  GLY A C   1 
ATOM   437  O  O   . GLY A 1 55  ? -2.453  6.369   -22.287 1.00 74.07  ? 55  GLY A O   1 
ATOM   438  N  N   . LYS A 1 56  ? -2.031  4.705   -20.812 1.00 80.40  ? 56  LYS A N   1 
ATOM   439  C  CA  . LYS A 1 56  ? -3.429  4.399   -20.539 1.00 72.66  ? 56  LYS A CA  1 
ATOM   440  C  C   . LYS A 1 56  ? -3.703  4.297   -19.041 1.00 71.80  ? 56  LYS A C   1 
ATOM   441  O  O   . LYS A 1 56  ? -4.774  3.810   -18.650 1.00 55.29  ? 56  LYS A O   1 
ATOM   442  C  CB  . LYS A 1 56  ? -3.843  3.080   -21.210 1.00 69.97  ? 56  LYS A CB  1 
ATOM   443  C  CG  . LYS A 1 56  ? -3.477  2.952   -22.681 1.00 71.79  ? 56  LYS A CG  1 
ATOM   444  C  CD  . LYS A 1 56  ? -4.533  3.570   -23.591 1.00 76.92  ? 56  LYS A CD  1 
ATOM   445  C  CE  . LYS A 1 56  ? -5.071  2.550   -24.600 1.00 78.29  ? 56  LYS A CE  1 
ATOM   446  N  NZ  . LYS A 1 56  ? -3.991  1.820   -25.326 1.00 75.18  ? 56  LYS A NZ  1 
ATOM   447  N  N   . GLU A 1 57  ? -2.762  4.719   -18.197 1.00 70.82  ? 57  GLU A N   1 
ATOM   448  C  CA  . GLU A 1 57  ? -2.925  4.535   -16.760 1.00 71.12  ? 57  GLU A CA  1 
ATOM   449  C  C   . GLU A 1 57  ? -4.204  5.210   -16.277 1.00 64.01  ? 57  GLU A C   1 
ATOM   450  O  O   . GLU A 1 57  ? -4.568  6.297   -16.734 1.00 67.12  ? 57  GLU A O   1 
ATOM   451  C  CB  . GLU A 1 57  ? -1.713  5.096   -16.013 1.00 70.95  ? 57  GLU A CB  1 
ATOM   452  C  CG  . GLU A 1 57  ? -0.423  4.298   -16.211 1.00 73.78  ? 57  GLU A CG  1 
ATOM   453  C  CD  . GLU A 1 57  ? 0.531   4.927   -17.223 1.00 85.55  ? 57  GLU A CD  1 
ATOM   454  O  OE1 . GLU A 1 57  ? 0.067   5.666   -18.120 1.00 86.06  ? 57  GLU A OE1 1 
ATOM   455  O  OE2 . GLU A 1 57  ? 1.754   4.676   -17.125 1.00 81.61  ? 57  GLU A OE2 1 
ATOM   456  N  N   . GLY A 1 58  ? -4.899  4.544   -15.354 1.00 63.71  ? 58  GLY A N   1 
ATOM   457  C  CA  . GLY A 1 58  ? -6.115  5.071   -14.778 1.00 58.10  ? 58  GLY A CA  1 
ATOM   458  C  C   . GLY A 1 58  ? -7.396  4.618   -15.438 1.00 54.35  ? 58  GLY A C   1 
ATOM   459  O  O   . GLY A 1 58  ? -8.475  4.939   -14.930 1.00 55.97  ? 58  GLY A O   1 
ATOM   460  N  N   . GLY A 1 59  ? -7.320  3.902   -16.561 1.00 52.68  ? 59  GLY A N   1 
ATOM   461  C  CA  . GLY A 1 59  ? -8.507  3.350   -17.171 1.00 46.79  ? 59  GLY A CA  1 
ATOM   462  C  C   . GLY A 1 59  ? -9.048  2.177   -16.374 1.00 51.14  ? 59  GLY A C   1 
ATOM   463  O  O   . GLY A 1 59  ? -8.394  1.624   -15.490 1.00 54.66  ? 59  GLY A O   1 
ATOM   464  N  N   . THR A 1 60  ? -10.281 1.792   -16.682 1.00 44.25  ? 60  THR A N   1 
ATOM   465  C  CA  . THR A 1 60  ? -10.870 0.656   -15.990 1.00 50.81  ? 60  THR A CA  1 
ATOM   466  C  C   . THR A 1 60  ? -12.000 0.065   -16.823 1.00 49.14  ? 60  THR A C   1 
ATOM   467  O  O   . THR A 1 60  ? -12.533 0.703   -17.732 1.00 47.81  ? 60  THR A O   1 
ATOM   468  C  CB  . THR A 1 60  ? -11.378 1.050   -14.597 1.00 51.80  ? 60  THR A CB  1 
ATOM   469  O  OG1 . THR A 1 60  ? -11.924 -0.103  -13.938 1.00 51.13  ? 60  THR A OG1 1 
ATOM   470  C  CG2 . THR A 1 60  ? -12.448 2.130   -14.699 1.00 53.31  ? 60  THR A CG2 1 
ATOM   471  N  N   . TRP A 1 61  ? -12.346 -1.177  -16.488 1.00 49.22  ? 61  TRP A N   1 
ATOM   472  C  CA  . TRP A 1 61  ? -13.381 -1.947  -17.163 1.00 54.04  ? 61  TRP A CA  1 
ATOM   473  C  C   . TRP A 1 61  ? -14.638 -2.109  -16.316 1.00 51.44  ? 61  TRP A C   1 
ATOM   474  O  O   . TRP A 1 61  ? -15.664 -2.557  -16.835 1.00 44.24  ? 61  TRP A O   1 
ATOM   475  C  CB  . TRP A 1 61  ? -12.837 -3.344  -17.514 1.00 48.31  ? 61  TRP A CB  1 
ATOM   476  C  CG  . TRP A 1 61  ? -12.324 -4.074  -16.287 1.00 55.50  ? 61  TRP A CG  1 
ATOM   477  C  CD1 . TRP A 1 61  ? -12.987 -5.025  -15.552 1.00 55.51  ? 61  TRP A CD1 1 
ATOM   478  C  CD2 . TRP A 1 61  ? -11.054 -3.885  -15.641 1.00 57.57  ? 61  TRP A CD2 1 
ATOM   479  N  NE1 . TRP A 1 61  ? -12.204 -5.442  -14.499 1.00 55.13  ? 61  TRP A NE1 1 
ATOM   480  C  CE2 . TRP A 1 61  ? -11.015 -4.755  -14.527 1.00 55.55  ? 61  TRP A CE2 1 
ATOM   481  C  CE3 . TRP A 1 61  ? -9.944  -3.066  -15.899 1.00 61.19  ? 61  TRP A CE3 1 
ATOM   482  C  CZ2 . TRP A 1 61  ? -9.908  -4.835  -13.676 1.00 50.35  ? 61  TRP A CZ2 1 
ATOM   483  C  CZ3 . TRP A 1 61  ? -8.846  -3.140  -15.044 1.00 63.37  ? 61  TRP A CZ3 1 
ATOM   484  C  CH2 . TRP A 1 61  ? -8.840  -4.020  -13.944 1.00 54.12  ? 61  TRP A CH2 1 
ATOM   485  N  N   . LEU A 1 62  ? -14.579 -1.774  -15.030 1.00 50.44  ? 62  LEU A N   1 
ATOM   486  C  CA  . LEU A 1 62  ? -15.680 -2.024  -14.104 1.00 43.85  ? 62  LEU A CA  1 
ATOM   487  C  C   . LEU A 1 62  ? -15.430 -1.259  -12.814 1.00 42.49  ? 62  LEU A C   1 
ATOM   488  O  O   . LEU A 1 62  ? -14.346 -1.361  -12.229 1.00 43.70  ? 62  LEU A O   1 
ATOM   489  C  CB  . LEU A 1 62  ? -15.809 -3.521  -13.832 1.00 47.45  ? 62  LEU A CB  1 
ATOM   490  C  CG  . LEU A 1 62  ? -16.863 -3.982  -12.834 1.00 49.00  ? 62  LEU A CG  1 
ATOM   491  C  CD1 . LEU A 1 62  ? -18.241 -3.476  -13.241 1.00 47.20  ? 62  LEU A CD1 1 
ATOM   492  C  CD2 . LEU A 1 62  ? -16.852 -5.501  -12.718 1.00 44.77  ? 62  LEU A CD2 1 
ATOM   493  N  N   . GLY A 1 63  ? -16.416 -0.493  -12.364 1.00 37.46  ? 63  GLY A N   1 
ATOM   494  C  CA  . GLY A 1 63  ? -16.250 0.303   -11.167 1.00 49.26  ? 63  GLY A CA  1 
ATOM   495  C  C   . GLY A 1 63  ? -17.577 0.763   -10.611 1.00 51.12  ? 63  GLY A C   1 
ATOM   496  O  O   . GLY A 1 63  ? -18.595 0.781   -11.308 1.00 45.09  ? 63  GLY A O   1 
ATOM   497  N  N   . ILE A 1 64  ? -17.549 1.133   -9.330  1.00 49.92  ? 64  ILE A N   1 
ATOM   498  C  CA  . ILE A 1 64  ? -18.723 1.637   -8.628  1.00 48.05  ? 64  ILE A CA  1 
ATOM   499  C  C   . ILE A 1 64  ? -18.271 2.744   -7.688  1.00 52.73  ? 64  ILE A C   1 
ATOM   500  O  O   . ILE A 1 64  ? -17.236 2.620   -7.027  1.00 49.68  ? 64  ILE A O   1 
ATOM   501  C  CB  . ILE A 1 64  ? -19.437 0.512   -7.855  1.00 47.58  ? 64  ILE A CB  1 
ATOM   502  C  CG1 . ILE A 1 64  ? -20.767 1.015   -7.290  1.00 55.68  ? 64  ILE A CG1 1 
ATOM   503  C  CG2 . ILE A 1 64  ? -18.560 -0.010  -6.720  1.00 48.30  ? 64  ILE A CG2 1 
ATOM   504  C  CD1 . ILE A 1 64  ? -21.582 -0.062  -6.574  1.00 56.86  ? 64  ILE A CD1 1 
ATOM   505  N  N   . SER A 1 65  ? -19.045 3.824   -7.625  1.00 50.55  ? 65  SER A N   1 
ATOM   506  C  CA  . SER A 1 65  ? -18.787 4.905   -6.678  1.00 56.72  ? 65  SER A CA  1 
ATOM   507  C  C   . SER A 1 65  ? -19.836 4.896   -5.570  1.00 53.40  ? 65  SER A C   1 
ATOM   508  O  O   . SER A 1 65  ? -20.972 4.451   -5.768  1.00 47.18  ? 65  SER A O   1 
ATOM   509  C  CB  . SER A 1 65  ? -18.791 6.268   -7.372  1.00 57.17  ? 65  SER A CB  1 
ATOM   510  O  OG  . SER A 1 65  ? -20.109 6.780   -7.477  1.00 65.44  ? 65  SER A OG  1 
ATOM   511  N  N   . THR A 1 66  ? -19.434 5.388   -4.391  1.00 55.02  ? 66  THR A N   1 
ATOM   512  C  CA  . THR A 1 66  ? -20.366 5.489   -3.271  1.00 58.59  ? 66  THR A CA  1 
ATOM   513  C  C   . THR A 1 66  ? -21.436 6.546   -3.514  1.00 62.45  ? 66  THR A C   1 
ATOM   514  O  O   . THR A 1 66  ? -22.479 6.521   -2.853  1.00 66.24  ? 66  THR A O   1 
ATOM   515  C  CB  . THR A 1 66  ? -19.616 5.808   -1.979  1.00 59.60  ? 66  THR A CB  1 
ATOM   516  O  OG1 . THR A 1 66  ? -19.093 7.139   -2.045  1.00 62.89  ? 66  THR A OG1 1 
ATOM   517  C  CG2 . THR A 1 66  ? -18.473 4.825   -1.765  1.00 55.23  ? 66  THR A CG2 1 
ATOM   518  N  N   . ARG A 1 67  ? -21.199 7.473   -4.442  1.00 66.12  ? 67  ARG A N   1 
ATOM   519  C  CA  . ARG A 1 67  ? -22.234 8.406   -4.865  1.00 64.94  ? 67  ARG A CA  1 
ATOM   520  C  C   . ARG A 1 67  ? -23.364 7.724   -5.629  1.00 62.22  ? 67  ARG A C   1 
ATOM   521  O  O   . ARG A 1 67  ? -24.311 8.407   -6.029  1.00 68.42  ? 67  ARG A O   1 
ATOM   522  C  CB  . ARG A 1 67  ? -21.633 9.512   -5.740  1.00 70.44  ? 67  ARG A CB  1 
ATOM   523  C  CG  . ARG A 1 67  ? -20.821 10.562  -4.987  1.00 82.49  ? 67  ARG A CG  1 
ATOM   524  C  CD  . ARG A 1 67  ? -21.430 11.956  -5.134  1.00 92.36  ? 67  ARG A CD  1 
ATOM   525  N  NE  . ARG A 1 67  ? -22.564 12.168  -4.240  1.00 97.17  ? 67  ARG A NE  1 
ATOM   526  C  CZ  . ARG A 1 67  ? -22.478 12.707  -3.031  1.00 104.36 ? 67  ARG A CZ  1 
ATOM   527  N  NH1 . ARG A 1 67  ? -21.319 13.112  -2.535  1.00 105.60 ? 67  ARG A NH1 1 
ATOM   528  N  NH2 . ARG A 1 67  ? -23.583 12.846  -2.301  1.00 101.08 ? 67  ARG A NH2 1 
ATOM   529  N  N   . GLY A 1 68  ? -23.285 6.413   -5.850  1.00 55.87  ? 68  GLY A N   1 
ATOM   530  C  CA  . GLY A 1 68  ? -24.340 5.699   -6.538  1.00 61.18  ? 68  GLY A CA  1 
ATOM   531  C  C   . GLY A 1 68  ? -24.180 5.673   -8.043  1.00 62.39  ? 68  GLY A C   1 
ATOM   532  O  O   . GLY A 1 68  ? -25.112 6.023   -8.776  1.00 61.92  ? 68  GLY A O   1 
ATOM   533  N  N   . LYS A 1 69  ? -23.004 5.270   -8.520  1.00 54.51  ? 69  LYS A N   1 
ATOM   534  C  CA  . LYS A 1 69  ? -22.736 5.153   -9.947  1.00 52.49  ? 69  LYS A CA  1 
ATOM   535  C  C   . LYS A 1 69  ? -22.025 3.836   -10.220 1.00 55.53  ? 69  LYS A C   1 
ATOM   536  O  O   . LYS A 1 69  ? -21.191 3.399   -9.422  1.00 55.13  ? 69  LYS A O   1 
ATOM   537  C  CB  . LYS A 1 69  ? -21.873 6.311   -10.460 1.00 56.13  ? 69  LYS A CB  1 
ATOM   538  C  CG  . LYS A 1 69  ? -22.596 7.646   -10.518 1.00 57.41  ? 69  LYS A CG  1 
ATOM   539  C  CD  . LYS A 1 69  ? -21.793 8.671   -11.302 1.00 63.81  ? 69  LYS A CD  1 
ATOM   540  C  CE  . LYS A 1 69  ? -22.688 9.456   -12.251 1.00 68.15  ? 69  LYS A CE  1 
ATOM   541  N  NZ  . LYS A 1 69  ? -21.892 10.317  -13.171 1.00 76.58  ? 69  LYS A NZ  1 
ATOM   542  N  N   . LEU A 1 70  ? -22.361 3.201   -11.344 1.00 48.84  ? 70  LEU A N   1 
ATOM   543  C  CA  . LEU A 1 70  ? -21.711 1.957   -11.736 1.00 49.98  ? 70  LEU A CA  1 
ATOM   544  C  C   . LEU A 1 70  ? -21.647 1.896   -13.255 1.00 49.59  ? 70  LEU A C   1 
ATOM   545  O  O   . LEU A 1 70  ? -22.587 2.306   -13.940 1.00 42.65  ? 70  LEU A O   1 
ATOM   546  C  CB  . LEU A 1 70  ? -22.454 0.736   -11.180 1.00 41.19  ? 70  LEU A CB  1 
ATOM   547  C  CG  . LEU A 1 70  ? -21.980 -0.635  -11.660 1.00 47.57  ? 70  LEU A CG  1 
ATOM   548  C  CD1 . LEU A 1 70  ? -22.158 -1.687  -10.586 1.00 53.16  ? 70  LEU A CD1 1 
ATOM   549  C  CD2 . LEU A 1 70  ? -22.729 -1.065  -12.925 1.00 45.39  ? 70  LEU A CD2 1 
ATOM   550  N  N   . ALA A 1 71  ? -20.540 1.376   -13.776 1.00 41.15  ? 71  ALA A N   1 
ATOM   551  C  CA  . ALA A 1 71  ? -20.419 1.191   -15.214 1.00 43.80  ? 71  ALA A CA  1 
ATOM   552  C  C   . ALA A 1 71  ? -19.466 0.039   -15.485 1.00 48.40  ? 71  ALA A C   1 
ATOM   553  O  O   . ALA A 1 71  ? -18.618 -0.304  -14.651 1.00 46.30  ? 71  ALA A O   1 
ATOM   554  C  CB  . ALA A 1 71  ? -19.938 2.465   -15.913 1.00 42.28  ? 71  ALA A CB  1 
ATOM   555  N  N   . ALA A 1 72  ? -19.628 -0.557  -16.665 1.00 39.00  ? 72  ALA A N   1 
ATOM   556  C  CA  . ALA A 1 72  ? -18.813 -1.683  -17.092 1.00 45.10  ? 72  ALA A CA  1 
ATOM   557  C  C   . ALA A 1 72  ? -18.668 -1.631  -18.606 1.00 44.88  ? 72  ALA A C   1 
ATOM   558  O  O   . ALA A 1 72  ? -19.541 -1.113  -19.308 1.00 40.20  ? 72  ALA A O   1 
ATOM   559  C  CB  . ALA A 1 72  ? -19.421 -3.025  -16.674 1.00 37.52  ? 72  ALA A CB  1 
ATOM   560  N  N   . LEU A 1 73  ? -17.561 -2.178  -19.103 1.00 40.49  ? 73  LEU A N   1 
ATOM   561  C  CA  . LEU A 1 73  ? -17.277 -2.173  -20.529 1.00 47.33  ? 73  LEU A CA  1 
ATOM   562  C  C   . LEU A 1 73  ? -16.765 -3.536  -20.952 1.00 43.56  ? 73  LEU A C   1 
ATOM   563  O  O   . LEU A 1 73  ? -16.096 -4.233  -20.186 1.00 51.68  ? 73  LEU A O   1 
ATOM   564  C  CB  . LEU A 1 73  ? -16.256 -1.085  -20.879 1.00 53.21  ? 73  LEU A CB  1 
ATOM   565  C  CG  . LEU A 1 73  ? -15.929 -0.921  -22.354 1.00 47.30  ? 73  LEU A CG  1 
ATOM   566  C  CD1 . LEU A 1 73  ? -15.875 0.553   -22.720 1.00 56.02  ? 73  LEU A CD1 1 
ATOM   567  C  CD2 . LEU A 1 73  ? -14.612 -1.599  -22.679 1.00 52.27  ? 73  LEU A CD2 1 
ATOM   568  N  N   . THR A 1 74  ? -17.105 -3.914  -22.185 1.00 47.55  ? 74  THR A N   1 
ATOM   569  C  CA  . THR A 1 74  ? -16.561 -5.101  -22.827 1.00 47.01  ? 74  THR A CA  1 
ATOM   570  C  C   . THR A 1 74  ? -16.086 -4.723  -24.223 1.00 49.73  ? 74  THR A C   1 
ATOM   571  O  O   . THR A 1 74  ? -16.643 -3.827  -24.867 1.00 45.20  ? 74  THR A O   1 
ATOM   572  C  CB  . THR A 1 74  ? -17.586 -6.244  -22.930 1.00 43.81  ? 74  THR A CB  1 
ATOM   573  O  OG1 . THR A 1 74  ? -18.668 -5.848  -23.777 1.00 43.98  ? 74  THR A OG1 1 
ATOM   574  C  CG2 . THR A 1 74  ? -18.125 -6.627  -21.556 1.00 44.23  ? 74  THR A CG2 1 
ATOM   575  N  N   . ASN A 1 75  ? -15.047 -5.407  -24.688 1.00 49.08  ? 75  ASN A N   1 
ATOM   576  C  CA  . ASN A 1 75  ? -14.549 -5.172  -26.029 1.00 48.98  ? 75  ASN A CA  1 
ATOM   577  C  C   . ASN A 1 75  ? -15.371 -5.956  -27.046 1.00 48.01  ? 75  ASN A C   1 
ATOM   578  O  O   . ASN A 1 75  ? -15.870 -7.049  -26.769 1.00 47.82  ? 75  ASN A O   1 
ATOM   579  C  CB  . ASN A 1 75  ? -13.078 -5.570  -26.140 1.00 56.78  ? 75  ASN A CB  1 
ATOM   580  C  CG  . ASN A 1 75  ? -12.184 -4.736  -25.254 1.00 60.04  ? 75  ASN A CG  1 
ATOM   581  O  OD1 . ASN A 1 75  ? -12.630 -3.761  -24.647 1.00 59.96  ? 75  ASN A OD1 1 
ATOM   582  N  ND2 . ASN A 1 75  ? -10.911 -5.106  -25.180 1.00 67.75  ? 75  ASN A ND2 1 
ATOM   583  N  N   . TYR A 1 76  ? -15.513 -5.383  -28.232 1.00 50.11  ? 76  TYR A N   1 
ATOM   584  C  CA  . TYR A 1 76  ? -16.141 -6.076  -29.351 1.00 50.36  ? 76  TYR A CA  1 
ATOM   585  C  C   . TYR A 1 76  ? -15.061 -6.883  -30.055 1.00 46.74  ? 76  TYR A C   1 
ATOM   586  O  O   . TYR A 1 76  ? -14.066 -6.318  -30.516 1.00 51.21  ? 76  TYR A O   1 
ATOM   587  C  CB  . TYR A 1 76  ? -16.804 -5.076  -30.290 1.00 48.97  ? 76  TYR A CB  1 
ATOM   588  C  CG  . TYR A 1 76  ? -17.719 -5.675  -31.336 1.00 52.18  ? 76  TYR A CG  1 
ATOM   589  C  CD1 . TYR A 1 76  ? -18.997 -6.108  -31.008 1.00 47.41  ? 76  TYR A CD1 1 
ATOM   590  C  CD2 . TYR A 1 76  ? -17.314 -5.775  -32.669 1.00 50.83  ? 76  TYR A CD2 1 
ATOM   591  C  CE1 . TYR A 1 76  ? -19.847 -6.642  -31.975 1.00 44.79  ? 76  TYR A CE1 1 
ATOM   592  C  CE2 . TYR A 1 76  ? -18.151 -6.302  -33.635 1.00 48.75  ? 76  TYR A CE2 1 
ATOM   593  C  CZ  . TYR A 1 76  ? -19.416 -6.737  -33.283 1.00 52.44  ? 76  TYR A CZ  1 
ATOM   594  O  OH  . TYR A 1 76  ? -20.254 -7.261  -34.254 1.00 49.59  ? 76  TYR A OH  1 
ATOM   595  N  N   . LEU A 1 77  ? -15.233 -8.201  -30.088 1.00 46.70  ? 77  LEU A N   1 
ATOM   596  C  CA  . LEU A 1 77  ? -14.298 -9.068  -30.790 1.00 48.89  ? 77  LEU A CA  1 
ATOM   597  C  C   . LEU A 1 77  ? -14.210 -8.653  -32.254 1.00 53.12  ? 77  LEU A C   1 
ATOM   598  O  O   . LEU A 1 77  ? -15.196 -8.729  -32.988 1.00 51.05  ? 77  LEU A O   1 
ATOM   599  C  CB  . LEU A 1 77  ? -14.756 -10.521 -30.678 1.00 48.53  ? 77  LEU A CB  1 
ATOM   600  C  CG  . LEU A 1 77  ? -13.958 -11.567 -31.462 1.00 51.02  ? 77  LEU A CG  1 
ATOM   601  C  CD1 . LEU A 1 77  ? -12.571 -11.765 -30.853 1.00 52.08  ? 77  LEU A CD1 1 
ATOM   602  C  CD2 . LEU A 1 77  ? -14.723 -12.884 -31.512 1.00 50.64  ? 77  LEU A CD2 1 
ATOM   603  N  N   . GLN A 1 78  ? -13.025 -8.217  -32.672 1.00 57.34  ? 78  GLN A N   1 
ATOM   604  C  CA  . GLN A 1 78  ? -12.779 -7.799  -34.045 1.00 62.25  ? 78  GLN A CA  1 
ATOM   605  C  C   . GLN A 1 78  ? -11.605 -8.569  -34.619 1.00 61.99  ? 78  GLN A C   1 
ATOM   606  O  O   . GLN A 1 78  ? -10.628 -8.844  -33.911 1.00 64.05  ? 78  GLN A O   1 
ATOM   607  C  CB  . GLN A 1 78  ? -12.482 -6.293  -34.105 1.00 66.81  ? 78  GLN A CB  1 
ATOM   608  C  CG  . GLN A 1 78  ? -13.702 -5.404  -33.962 1.00 65.46  ? 78  GLN A CG  1 
ATOM   609  C  CD  . GLN A 1 78  ? -13.365 -3.922  -33.829 1.00 74.98  ? 78  GLN A CD  1 
ATOM   610  O  OE1 . GLN A 1 78  ? -14.227 -3.115  -33.485 1.00 70.69  ? 78  GLN A OE1 1 
ATOM   611  N  NE2 . GLN A 1 78  ? -12.113 -3.562  -34.104 1.00 75.11  ? 78  GLN A NE2 1 
ATOM   612  N  N   . PRO A 1 79  ? -11.661 -8.935  -35.905 1.00 64.46  ? 79  PRO A N   1 
ATOM   613  C  CA  . PRO A 1 79  ? -10.480 -9.552  -36.530 1.00 64.50  ? 79  PRO A CA  1 
ATOM   614  C  C   . PRO A 1 79  ? -9.276  -8.627  -36.573 1.00 69.00  ? 79  PRO A C   1 
ATOM   615  O  O   . PRO A 1 79  ? -8.144  -9.112  -36.694 1.00 68.78  ? 79  PRO A O   1 
ATOM   616  C  CB  . PRO A 1 79  ? -10.965 -9.904  -37.946 1.00 69.03  ? 79  PRO A CB  1 
ATOM   617  C  CG  . PRO A 1 79  ? -12.457 -9.923  -37.859 1.00 67.33  ? 79  PRO A CG  1 
ATOM   618  C  CD  . PRO A 1 79  ? -12.823 -8.913  -36.810 1.00 63.38  ? 79  PRO A CD  1 
ATOM   619  N  N   . GLN A 1 80  ? -9.484  -7.314  -36.486 1.00 79.94  ? 80  GLN A N   1 
ATOM   620  C  CA  . GLN A 1 80  ? -8.420  -6.340  -36.689 1.00 86.06  ? 80  GLN A CA  1 
ATOM   621  C  C   . GLN A 1 80  ? -8.660  -5.167  -35.752 1.00 81.32  ? 80  GLN A C   1 
ATOM   622  O  O   . GLN A 1 80  ? -9.787  -4.910  -35.322 1.00 73.98  ? 80  GLN A O   1 
ATOM   623  C  CB  . GLN A 1 80  ? -8.366  -5.889  -38.156 1.00 93.24  ? 80  GLN A CB  1 
ATOM   624  C  CG  . GLN A 1 80  ? -7.203  -4.981  -38.515 1.00 102.69 ? 80  GLN A CG  1 
ATOM   625  C  CD  . GLN A 1 80  ? -5.848  -5.596  -38.207 1.00 103.65 ? 80  GLN A CD  1 
ATOM   626  O  OE1 . GLN A 1 80  ? -5.554  -6.733  -38.595 1.00 90.69  ? 80  GLN A OE1 1 
ATOM   627  N  NE2 . GLN A 1 80  ? -5.011  -4.840  -37.497 1.00 98.38  ? 80  GLN A NE2 1 
ATOM   628  N  N   . LEU A 1 81  ? -7.583  -4.456  -35.430 1.00 77.95  ? 81  LEU A N   1 
ATOM   629  C  CA  . LEU A 1 81  ? -7.642  -3.354  -34.481 1.00 72.93  ? 81  LEU A CA  1 
ATOM   630  C  C   . LEU A 1 81  ? -7.064  -2.093  -35.106 1.00 75.34  ? 81  LEU A C   1 
ATOM   631  O  O   . LEU A 1 81  ? -6.014  -2.133  -35.755 1.00 71.95  ? 81  LEU A O   1 
ATOM   632  C  CB  . LEU A 1 81  ? -6.874  -3.696  -33.195 1.00 79.05  ? 81  LEU A CB  1 
ATOM   633  C  CG  . LEU A 1 81  ? -7.448  -3.168  -31.881 1.00 82.27  ? 81  LEU A CG  1 
ATOM   634  C  CD1 . LEU A 1 81  ? -8.746  -3.883  -31.528 1.00 74.12  ? 81  LEU A CD1 1 
ATOM   635  C  CD2 . LEU A 1 81  ? -6.430  -3.316  -30.758 1.00 74.65  ? 81  LEU A CD2 1 
ATOM   636  N  N   . ASP A 1 82  ? -7.762  -0.976  -34.909 1.00 73.93  ? 82  ASP A N   1 
ATOM   637  C  CA  . ASP A 1 82  ? -7.231  0.343   -35.244 1.00 70.67  ? 82  ASP A CA  1 
ATOM   638  C  C   . ASP A 1 82  ? -6.396  0.820   -34.060 1.00 84.20  ? 82  ASP A C   1 
ATOM   639  O  O   . ASP A 1 82  ? -6.933  1.079   -32.977 1.00 77.95  ? 82  ASP A O   1 
ATOM   640  C  CB  . ASP A 1 82  ? -8.358  1.320   -35.555 1.00 66.18  ? 82  ASP A CB  1 
ATOM   641  C  CG  . ASP A 1 82  ? -7.855  2.730   -35.830 1.00 73.82  ? 82  ASP A CG  1 
ATOM   642  O  OD1 . ASP A 1 82  ? -6.628  2.924   -35.950 1.00 76.22  ? 82  ASP A OD1 1 
ATOM   643  O  OD2 . ASP A 1 82  ? -8.692  3.651   -35.927 1.00 76.55  ? 82  ASP A OD2 1 
ATOM   644  N  N   . TRP A 1 83  ? -5.088  0.933   -34.251 1.00 89.28  ? 83  TRP A N   1 
ATOM   645  C  CA  . TRP A 1 83  ? -4.176  1.249   -33.162 1.00 87.88  ? 83  TRP A CA  1 
ATOM   646  C  C   . TRP A 1 83  ? -4.048  2.745   -32.897 1.00 85.88  ? 83  TRP A C   1 
ATOM   647  O  O   . TRP A 1 83  ? -3.361  3.134   -31.950 1.00 85.31  ? 83  TRP A O   1 
ATOM   648  C  CB  . TRP A 1 83  ? -2.792  0.644   -33.450 1.00 88.04  ? 83  TRP A CB  1 
ATOM   649  C  CG  . TRP A 1 83  ? -2.791  -0.861  -33.417 1.00 87.91  ? 83  TRP A CG  1 
ATOM   650  C  CD1 . TRP A 1 83  ? -3.207  -1.704  -34.409 1.00 95.10  ? 83  TRP A CD1 1 
ATOM   651  C  CD2 . TRP A 1 83  ? -2.357  -1.699  -32.336 1.00 86.74  ? 83  TRP A CD2 1 
ATOM   652  N  NE1 . TRP A 1 83  ? -3.059  -3.014  -34.011 1.00 93.78  ? 83  TRP A NE1 1 
ATOM   653  C  CE2 . TRP A 1 83  ? -2.539  -3.037  -32.744 1.00 85.55  ? 83  TRP A CE2 1 
ATOM   654  C  CE3 . TRP A 1 83  ? -1.829  -1.447  -31.067 1.00 87.88  ? 83  TRP A CE3 1 
ATOM   655  C  CZ2 . TRP A 1 83  ? -2.213  -4.118  -31.927 1.00 79.48  ? 83  TRP A CZ2 1 
ATOM   656  C  CZ3 . TRP A 1 83  ? -1.506  -2.523  -30.254 1.00 86.85  ? 83  TRP A CZ3 1 
ATOM   657  C  CH2 . TRP A 1 83  ? -1.700  -3.841  -30.689 1.00 87.54  ? 83  TRP A CH2 1 
ATOM   658  N  N   . GLN A 1 84  ? -4.699  3.590   -33.697 1.00 80.65  ? 84  GLN A N   1 
ATOM   659  C  CA  . GLN A 1 84  ? -4.644  5.035   -33.517 1.00 79.53  ? 84  GLN A CA  1 
ATOM   660  C  C   . GLN A 1 84  ? -5.846  5.592   -32.762 1.00 79.28  ? 84  GLN A C   1 
ATOM   661  O  O   . GLN A 1 84  ? -5.900  6.804   -32.521 1.00 70.64  ? 84  GLN A O   1 
ATOM   662  C  CB  . GLN A 1 84  ? -4.531  5.728   -34.884 1.00 74.89  ? 84  GLN A CB  1 
ATOM   663  N  N   . ALA A 1 85  ? -6.799  4.745   -32.376 1.00 64.41  ? 85  ALA A N   1 
ATOM   664  C  CA  . ALA A 1 85  ? -8.034  5.218   -31.775 1.00 65.85  ? 85  ALA A CA  1 
ATOM   665  C  C   . ALA A 1 85  ? -7.868  5.427   -30.269 1.00 69.42  ? 85  ALA A C   1 
ATOM   666  O  O   . ALA A 1 85  ? -6.905  4.968   -29.646 1.00 61.49  ? 85  ALA A O   1 
ATOM   667  C  CB  . ALA A 1 85  ? -9.170  4.232   -32.047 1.00 69.19  ? 85  ALA A CB  1 
ATOM   668  N  N   . ARG A 1 86  ? -8.838  6.129   -29.683 1.00 69.11  ? 86  ARG A N   1 
ATOM   669  C  CA  . ARG A 1 86  ? -8.816  6.389   -28.253 1.00 64.02  ? 86  ARG A CA  1 
ATOM   670  C  C   . ARG A 1 86  ? -8.908  5.084   -27.468 1.00 68.16  ? 86  ARG A C   1 
ATOM   671  O  O   . ARG A 1 86  ? -9.549  4.116   -27.894 1.00 61.96  ? 86  ARG A O   1 
ATOM   672  C  CB  . ARG A 1 86  ? -9.983  7.286   -27.846 1.00 63.99  ? 86  ARG A CB  1 
ATOM   673  C  CG  . ARG A 1 86  ? -9.973  8.693   -28.394 1.00 60.42  ? 86  ARG A CG  1 
ATOM   674  C  CD  . ARG A 1 86  ? -11.271 9.393   -27.982 1.00 68.21  ? 86  ARG A CD  1 
ATOM   675  N  NE  . ARG A 1 86  ? -11.411 10.733  -28.537 1.00 83.00  ? 86  ARG A NE  1 
ATOM   676  C  CZ  . ARG A 1 86  ? -12.468 11.516  -28.355 1.00 85.63  ? 86  ARG A CZ  1 
ATOM   677  N  NH1 . ARG A 1 86  ? -13.508 11.119  -27.634 1.00 81.41  ? 86  ARG A NH1 1 
ATOM   678  N  NH2 . ARG A 1 86  ? -12.491 12.720  -28.922 1.00 88.96  ? 86  ARG A NH2 1 
ATOM   679  N  N   . GLY A 1 87  ? -8.269  5.063   -26.303 1.00 66.02  ? 87  GLY A N   1 
ATOM   680  C  CA  . GLY A 1 87  ? -8.426  3.941   -25.400 1.00 60.90  ? 87  GLY A CA  1 
ATOM   681  C  C   . GLY A 1 87  ? -9.851  3.857   -24.891 1.00 63.60  ? 87  GLY A C   1 
ATOM   682  O  O   . GLY A 1 87  ? -10.518 4.866   -24.658 1.00 67.60  ? 87  GLY A O   1 
ATOM   683  N  N   . ARG A 1 88  ? -10.333 2.625   -24.724 1.00 62.98  ? 88  ARG A N   1 
ATOM   684  C  CA  . ARG A 1 88  ? -11.669 2.394   -24.194 1.00 62.70  ? 88  ARG A CA  1 
ATOM   685  C  C   . ARG A 1 88  ? -11.718 2.440   -22.673 1.00 62.28  ? 88  ARG A C   1 
ATOM   686  O  O   . ARG A 1 88  ? -12.818 2.505   -22.105 1.00 53.49  ? 88  ARG A O   1 
ATOM   687  C  CB  . ARG A 1 88  ? -12.191 1.043   -24.693 1.00 60.70  ? 88  ARG A CB  1 
ATOM   688  C  CG  . ARG A 1 88  ? -12.498 1.022   -26.189 1.00 52.06  ? 88  ARG A CG  1 
ATOM   689  C  CD  . ARG A 1 88  ? -12.563 -0.395  -26.747 1.00 57.49  ? 88  ARG A CD  1 
ATOM   690  N  NE  . ARG A 1 88  ? -11.247 -1.022  -26.802 1.00 62.69  ? 88  ARG A NE  1 
ATOM   691  C  CZ  . ARG A 1 88  ? -10.975 -2.146  -27.454 1.00 63.16  ? 88  ARG A CZ  1 
ATOM   692  N  NH1 . ARG A 1 88  ? -11.903 -2.782  -28.155 1.00 55.99  ? 88  ARG A NH1 1 
ATOM   693  N  NH2 . ARG A 1 88  ? -9.742  -2.642  -27.403 1.00 63.40  ? 88  ARG A NH2 1 
ATOM   694  N  N   . GLY A 1 89  ? -10.563 2.424   -22.004 1.00 66.98  ? 89  GLY A N   1 
ATOM   695  C  CA  . GLY A 1 89  ? -10.545 2.454   -20.554 1.00 61.49  ? 89  GLY A CA  1 
ATOM   696  C  C   . GLY A 1 89  ? -11.132 3.715   -19.956 1.00 59.88  ? 89  GLY A C   1 
ATOM   697  O  O   . GLY A 1 89  ? -11.574 3.696   -18.798 1.00 58.60  ? 89  GLY A O   1 
ATOM   698  N  N   . GLU A 1 90  ? -11.151 4.813   -20.715 1.00 54.09  ? 90  GLU A N   1 
ATOM   699  C  CA  . GLU A 1 90  ? -11.658 6.077   -20.202 1.00 58.74  ? 90  GLU A CA  1 
ATOM   700  C  C   . GLU A 1 90  ? -13.181 6.142   -20.182 1.00 60.80  ? 90  GLU A C   1 
ATOM   701  O  O   . GLU A 1 90  ? -13.742 7.011   -19.506 1.00 57.66  ? 90  GLU A O   1 
ATOM   702  C  CB  . GLU A 1 90  ? -11.121 7.244   -21.039 1.00 51.40  ? 90  GLU A CB  1 
ATOM   703  C  CG  . GLU A 1 90  ? -11.660 7.276   -22.461 1.00 55.94  ? 90  GLU A CG  1 
ATOM   704  C  CD  . GLU A 1 90  ? -10.975 8.321   -23.324 1.00 67.14  ? 90  GLU A CD  1 
ATOM   705  O  OE1 . GLU A 1 90  ? -10.223 9.159   -22.772 1.00 69.92  ? 90  GLU A OE1 1 
ATOM   706  O  OE2 . GLU A 1 90  ? -11.181 8.300   -24.555 1.00 65.55  ? 90  GLU A OE2 1 
ATOM   707  N  N   . LEU A 1 91  ? -13.863 5.255   -20.908 1.00 55.28  ? 91  LEU A N   1 
ATOM   708  C  CA  . LEU A 1 91  ? -15.319 5.332   -20.983 1.00 55.80  ? 91  LEU A CA  1 
ATOM   709  C  C   . LEU A 1 91  ? -15.953 5.086   -19.616 1.00 54.09  ? 91  LEU A C   1 
ATOM   710  O  O   . LEU A 1 91  ? -16.870 5.807   -19.206 1.00 51.70  ? 91  LEU A O   1 
ATOM   711  C  CB  . LEU A 1 91  ? -15.835 4.337   -22.025 1.00 51.15  ? 91  LEU A CB  1 
ATOM   712  C  CG  . LEU A 1 91  ? -15.372 4.650   -23.449 1.00 54.25  ? 91  LEU A CG  1 
ATOM   713  C  CD1 . LEU A 1 91  ? -15.581 3.480   -24.386 1.00 52.51  ? 91  LEU A CD1 1 
ATOM   714  C  CD2 . LEU A 1 91  ? -16.103 5.887   -23.973 1.00 59.47  ? 91  LEU A CD2 1 
ATOM   715  N  N   . VAL A 1 92  ? -15.484 4.066   -18.897 1.00 50.19  ? 92  VAL A N   1 
ATOM   716  C  CA  . VAL A 1 92  ? -16.004 3.817   -17.554 1.00 56.13  ? 92  VAL A CA  1 
ATOM   717  C  C   . VAL A 1 92  ? -15.514 4.884   -16.575 1.00 53.74  ? 92  VAL A C   1 
ATOM   718  O  O   . VAL A 1 92  ? -16.290 5.410   -15.772 1.00 55.88  ? 92  VAL A O   1 
ATOM   719  C  CB  . VAL A 1 92  ? -15.622 2.401   -17.091 1.00 55.27  ? 92  VAL A CB  1 
ATOM   720  C  CG1 . VAL A 1 92  ? -15.841 2.239   -15.590 1.00 53.40  ? 92  VAL A CG1 1 
ATOM   721  C  CG2 . VAL A 1 92  ? -16.433 1.361   -17.863 1.00 51.12  ? 92  VAL A CG2 1 
ATOM   722  N  N   . THR A 1 93  ? -14.228 5.229   -16.634 1.00 54.76  ? 93  THR A N   1 
ATOM   723  C  CA  . THR A 1 93  ? -13.667 6.158   -15.655 1.00 59.29  ? 93  THR A CA  1 
ATOM   724  C  C   . THR A 1 93  ? -14.373 7.507   -15.696 1.00 60.65  ? 93  THR A C   1 
ATOM   725  O  O   . THR A 1 93  ? -14.751 8.055   -14.653 1.00 61.03  ? 93  THR A O   1 
ATOM   726  C  CB  . THR A 1 93  ? -12.169 6.339   -15.903 1.00 56.01  ? 93  THR A CB  1 
ATOM   727  O  OG1 . THR A 1 93  ? -11.495 5.098   -15.657 1.00 61.92  ? 93  THR A OG1 1 
ATOM   728  C  CG2 . THR A 1 93  ? -11.596 7.411   -14.995 1.00 63.06  ? 93  THR A CG2 1 
ATOM   729  N  N   . HIS A 1 94  ? -14.549 8.066   -16.893 1.00 58.60  ? 94  HIS A N   1 
ATOM   730  C  CA  . HIS A 1 94  ? -15.131 9.400   -16.999 1.00 62.38  ? 94  HIS A CA  1 
ATOM   731  C  C   . HIS A 1 94  ? -16.574 9.434   -16.512 1.00 60.14  ? 94  HIS A C   1 
ATOM   732  O  O   . HIS A 1 94  ? -17.060 10.503  -16.130 1.00 61.38  ? 94  HIS A O   1 
ATOM   733  C  CB  . HIS A 1 94  ? -15.044 9.900   -18.443 1.00 61.43  ? 94  HIS A CB  1 
ATOM   734  C  CG  . HIS A 1 94  ? -13.660 10.295  -18.865 1.00 62.08  ? 94  HIS A CG  1 
ATOM   735  N  ND1 . HIS A 1 94  ? -13.333 10.578  -20.177 1.00 70.43  ? 94  HIS A ND1 1 
ATOM   736  C  CD2 . HIS A 1 94  ? -12.521 10.459  -18.151 1.00 63.47  ? 94  HIS A CD2 1 
ATOM   737  C  CE1 . HIS A 1 94  ? -12.052 10.898  -20.252 1.00 65.14  ? 94  HIS A CE1 1 
ATOM   738  N  NE2 . HIS A 1 94  ? -11.536 10.832  -19.037 1.00 69.44  ? 94  HIS A NE2 1 
ATOM   739  N  N   . PHE A 1 95  ? -17.273 8.296   -16.519 1.00 56.22  ? 95  PHE A N   1 
ATOM   740  C  CA  . PHE A 1 95  ? -18.612 8.275   -15.940 1.00 57.92  ? 95  PHE A CA  1 
ATOM   741  C  C   . PHE A 1 95  ? -18.556 8.298   -14.415 1.00 59.86  ? 95  PHE A C   1 
ATOM   742  O  O   . PHE A 1 95  ? -19.322 9.021   -13.770 1.00 60.45  ? 95  PHE A O   1 
ATOM   743  C  CB  . PHE A 1 95  ? -19.381 7.049   -16.418 1.00 56.75  ? 95  PHE A CB  1 
ATOM   744  C  CG  . PHE A 1 95  ? -20.775 6.963   -15.868 1.00 53.53  ? 95  PHE A CG  1 
ATOM   745  C  CD1 . PHE A 1 95  ? -21.737 7.881   -16.246 1.00 53.81  ? 95  PHE A CD1 1 
ATOM   746  C  CD2 . PHE A 1 95  ? -21.122 5.964   -14.974 1.00 53.19  ? 95  PHE A CD2 1 
ATOM   747  C  CE1 . PHE A 1 95  ? -23.018 7.808   -15.747 1.00 52.55  ? 95  PHE A CE1 1 
ATOM   748  C  CE2 . PHE A 1 95  ? -22.405 5.886   -14.469 1.00 54.88  ? 95  PHE A CE2 1 
ATOM   749  C  CZ  . PHE A 1 95  ? -23.354 6.810   -14.859 1.00 57.85  ? 95  PHE A CZ  1 
ATOM   750  N  N   . LEU A 1 96  ? -17.651 7.518   -13.822 1.00 56.81  ? 96  LEU A N   1 
ATOM   751  C  CA  . LEU A 1 96  ? -17.578 7.444   -12.369 1.00 59.08  ? 96  LEU A CA  1 
ATOM   752  C  C   . LEU A 1 96  ? -17.061 8.732   -11.744 1.00 60.11  ? 96  LEU A C   1 
ATOM   753  O  O   . LEU A 1 96  ? -17.316 8.973   -10.560 1.00 61.83  ? 96  LEU A O   1 
ATOM   754  C  CB  . LEU A 1 96  ? -16.691 6.273   -11.945 1.00 57.35  ? 96  LEU A CB  1 
ATOM   755  C  CG  . LEU A 1 96  ? -17.149 4.883   -12.397 1.00 56.49  ? 96  LEU A CG  1 
ATOM   756  C  CD1 . LEU A 1 96  ? -16.115 3.824   -12.012 1.00 42.83  ? 96  LEU A CD1 1 
ATOM   757  C  CD2 . LEU A 1 96  ? -18.514 4.529   -11.821 1.00 50.61  ? 96  LEU A CD2 1 
ATOM   758  N  N   . THR A 1 97  ? -16.354 9.567   -12.508 1.00 64.25  ? 97  THR A N   1 
ATOM   759  C  CA  . THR A 1 97  ? -15.740 10.775  -11.975 1.00 60.44  ? 97  THR A CA  1 
ATOM   760  C  C   . THR A 1 97  ? -16.534 12.040  -12.289 1.00 68.65  ? 97  THR A C   1 
ATOM   761  O  O   . THR A 1 97  ? -16.015 13.144  -12.099 1.00 72.10  ? 97  THR A O   1 
ATOM   762  C  CB  . THR A 1 97  ? -14.309 10.927  -12.505 1.00 63.00  ? 97  THR A CB  1 
ATOM   763  O  OG1 . THR A 1 97  ? -14.317 10.996  -13.940 1.00 63.48  ? 97  THR A OG1 1 
ATOM   764  C  CG2 . THR A 1 97  ? -13.442 9.756   -12.053 1.00 65.61  ? 97  THR A CG2 1 
ATOM   765  N  N   . THR A 1 98  ? -17.771 11.909  -12.769 1.00 72.74  ? 98  THR A N   1 
ATOM   766  C  CA  . THR A 1 98  ? -18.597 13.081  -13.040 1.00 79.05  ? 98  THR A CA  1 
ATOM   767  C  C   . THR A 1 98  ? -19.948 12.950  -12.346 1.00 82.99  ? 98  THR A C   1 
ATOM   768  O  O   . THR A 1 98  ? -20.141 12.053  -11.518 1.00 82.86  ? 98  THR A O   1 
ATOM   769  C  CB  . THR A 1 98  ? -18.792 13.278  -14.543 1.00 81.53  ? 98  THR A CB  1 
ATOM   770  O  OG1 . THR A 1 98  ? -19.552 12.186  -15.080 1.00 81.91  ? 98  THR A OG1 1 
ATOM   771  C  CG2 . THR A 1 98  ? -17.439 13.364  -15.244 1.00 76.94  ? 98  THR A CG2 1 
ATOM   772  N  N   . ASP A 1 99  ? -20.886 13.846  -12.670 1.00 85.24  ? 99  ASP A N   1 
ATOM   773  C  CA  . ASP A 1 99  ? -22.207 13.848  -12.052 1.00 86.73  ? 99  ASP A CA  1 
ATOM   774  C  C   . ASP A 1 99  ? -23.325 13.713  -13.081 1.00 83.67  ? 99  ASP A C   1 
ATOM   775  O  O   . ASP A 1 99  ? -24.477 14.052  -12.791 1.00 86.32  ? 99  ASP A O   1 
ATOM   776  C  CB  . ASP A 1 99  ? -22.406 15.121  -11.225 1.00 88.01  ? 99  ASP A CB  1 
ATOM   777  C  CG  . ASP A 1 99  ? -22.371 16.381  -12.074 1.00 94.93  ? 99  ASP A CG  1 
ATOM   778  O  OD1 . ASP A 1 99  ? -21.522 16.471  -12.989 1.00 92.61  ? 99  ASP A OD1 1 
ATOM   779  O  OD2 . ASP A 1 99  ? -23.198 17.284  -11.826 1.00 97.51  ? 99  ASP A OD2 1 
ATOM   780  N  N   . VAL A 1 100 ? -23.014 13.213  -14.271 1.00 71.16  ? 100 VAL A N   1 
ATOM   781  C  CA  . VAL A 1 100 ? -24.008 13.069  -15.327 1.00 68.77  ? 100 VAL A CA  1 
ATOM   782  C  C   . VAL A 1 100 ? -24.826 11.807  -15.086 1.00 66.45  ? 100 VAL A C   1 
ATOM   783  O  O   . VAL A 1 100 ? -24.302 10.784  -14.630 1.00 65.45  ? 100 VAL A O   1 
ATOM   784  C  CB  . VAL A 1 100 ? -23.322 13.025  -16.707 1.00 67.97  ? 100 VAL A CB  1 
ATOM   785  C  CG1 . VAL A 1 100 ? -24.359 13.108  -17.814 1.00 67.37  ? 100 VAL A CG1 1 
ATOM   786  C  CG2 . VAL A 1 100 ? -22.296 14.144  -16.839 1.00 73.11  ? 100 VAL A CG2 1 
ATOM   787  N  N   . ASP A 1 101 ? -26.120 11.869  -15.394 1.00 63.08  ? 101 ASP A N   1 
ATOM   788  C  CA  . ASP A 1 101 ? -26.944 10.670  -15.312 1.00 64.61  ? 101 ASP A CA  1 
ATOM   789  C  C   . ASP A 1 101 ? -26.567 9.698   -16.432 1.00 61.13  ? 101 ASP A C   1 
ATOM   790  O  O   . ASP A 1 101 ? -26.059 10.085  -17.490 1.00 60.66  ? 101 ASP A O   1 
ATOM   791  C  CB  . ASP A 1 101 ? -28.434 11.015  -15.379 1.00 61.98  ? 101 ASP A CB  1 
ATOM   792  C  CG  . ASP A 1 101 ? -28.841 11.632  -16.704 1.00 64.73  ? 101 ASP A CG  1 
ATOM   793  O  OD1 . ASP A 1 101 ? -28.461 12.794  -16.957 1.00 71.78  ? 101 ASP A OD1 1 
ATOM   794  O  OD2 . ASP A 1 101 ? -29.538 10.955  -17.495 1.00 62.81  ? 101 ASP A OD2 1 
ATOM   795  N  N   . SER A 1 102 ? -26.838 8.413   -16.191 1.00 55.59  ? 102 SER A N   1 
ATOM   796  C  CA  . SER A 1 102 ? -26.314 7.372   -17.068 1.00 57.65  ? 102 SER A CA  1 
ATOM   797  C  C   . SER A 1 102 ? -26.790 7.548   -18.507 1.00 53.65  ? 102 SER A C   1 
ATOM   798  O  O   . SER A 1 102 ? -26.006 7.393   -19.447 1.00 53.97  ? 102 SER A O   1 
ATOM   799  C  CB  . SER A 1 102 ? -26.718 5.996   -16.537 1.00 55.38  ? 102 SER A CB  1 
ATOM   800  O  OG  . SER A 1 102 ? -28.126 5.894   -16.421 1.00 52.96  ? 102 SER A OG  1 
ATOM   801  N  N   . LEU A 1 103 ? -28.072 7.857   -18.706 1.00 55.03  ? 103 LEU A N   1 
ATOM   802  C  CA  . LEU A 1 103 ? -28.577 8.004   -20.066 1.00 55.92  ? 103 LEU A CA  1 
ATOM   803  C  C   . LEU A 1 103 ? -27.923 9.185   -20.773 1.00 55.51  ? 103 LEU A C   1 
ATOM   804  O  O   . LEU A 1 103 ? -27.562 9.088   -21.950 1.00 55.45  ? 103 LEU A O   1 
ATOM   805  C  CB  . LEU A 1 103 ? -30.096 8.164   -20.058 1.00 56.54  ? 103 LEU A CB  1 
ATOM   806  C  CG  . LEU A 1 103 ? -30.720 8.289   -21.452 1.00 58.99  ? 103 LEU A CG  1 
ATOM   807  C  CD1 . LEU A 1 103 ? -30.472 7.028   -22.277 1.00 52.67  ? 103 LEU A CD1 1 
ATOM   808  C  CD2 . LEU A 1 103 ? -32.207 8.583   -21.356 1.00 61.97  ? 103 LEU A CD2 1 
ATOM   809  N  N   . SER A 1 104 ? -27.765 10.311  -20.071 1.00 57.04  ? 104 SER A N   1 
ATOM   810  C  CA  . SER A 1 104 ? -27.137 11.477  -20.686 1.00 63.42  ? 104 SER A CA  1 
ATOM   811  C  C   . SER A 1 104 ? -25.681 11.199  -21.043 1.00 61.12  ? 104 SER A C   1 
ATOM   812  O  O   . SER A 1 104 ? -25.191 11.652  -22.086 1.00 57.83  ? 104 SER A O   1 
ATOM   813  C  CB  . SER A 1 104 ? -27.243 12.687  -19.754 1.00 65.45  ? 104 SER A CB  1 
ATOM   814  O  OG  . SER A 1 104 ? -28.548 13.244  -19.777 1.00 61.26  ? 104 SER A OG  1 
ATOM   815  N  N   . TYR A 1 105 ? -24.968 10.462  -20.186 1.00 60.80  ? 105 TYR A N   1 
ATOM   816  C  CA  . TYR A 1 105 ? -23.580 10.133  -20.488 1.00 58.93  ? 105 TYR A CA  1 
ATOM   817  C  C   . TYR A 1 105 ? -23.483 9.276   -21.747 1.00 58.88  ? 105 TYR A C   1 
ATOM   818  O  O   . TYR A 1 105 ? -22.655 9.534   -22.628 1.00 55.52  ? 105 TYR A O   1 
ATOM   819  C  CB  . TYR A 1 105 ? -22.932 9.419   -19.301 1.00 56.92  ? 105 TYR A CB  1 
ATOM   820  C  CG  . TYR A 1 105 ? -21.469 9.094   -19.519 1.00 54.95  ? 105 TYR A CG  1 
ATOM   821  C  CD1 . TYR A 1 105 ? -20.493 10.080  -19.414 1.00 53.15  ? 105 TYR A CD1 1 
ATOM   822  C  CD2 . TYR A 1 105 ? -21.064 7.805   -19.835 1.00 52.23  ? 105 TYR A CD2 1 
ATOM   823  C  CE1 . TYR A 1 105 ? -19.155 9.789   -19.617 1.00 49.21  ? 105 TYR A CE1 1 
ATOM   824  C  CE2 . TYR A 1 105 ? -19.727 7.504   -20.041 1.00 53.48  ? 105 TYR A CE2 1 
ATOM   825  C  CZ  . TYR A 1 105 ? -18.779 8.496   -19.932 1.00 50.68  ? 105 TYR A CZ  1 
ATOM   826  O  OH  . TYR A 1 105 ? -17.451 8.189   -20.137 1.00 50.57  ? 105 TYR A OH  1 
ATOM   827  N  N   . LEU A 1 106 ? -24.335 8.254   -21.855 1.00 54.43  ? 106 LEU A N   1 
ATOM   828  C  CA  . LEU A 1 106 ? -24.249 7.366   -23.009 1.00 55.60  ? 106 LEU A CA  1 
ATOM   829  C  C   . LEU A 1 106 ? -24.610 8.086   -24.304 1.00 52.89  ? 106 LEU A C   1 
ATOM   830  O  O   . LEU A 1 106 ? -24.104 7.724   -25.370 1.00 56.88  ? 106 LEU A O   1 
ATOM   831  C  CB  . LEU A 1 106 ? -25.150 6.150   -22.813 1.00 52.81  ? 106 LEU A CB  1 
ATOM   832  C  CG  . LEU A 1 106 ? -24.736 5.152   -21.731 1.00 48.85  ? 106 LEU A CG  1 
ATOM   833  C  CD1 . LEU A 1 106 ? -25.561 3.871   -21.876 1.00 41.89  ? 106 LEU A CD1 1 
ATOM   834  C  CD2 . LEU A 1 106 ? -23.245 4.846   -21.761 1.00 40.97  ? 106 LEU A CD2 1 
ATOM   835  N  N   . LYS A 1 107 ? -25.482 9.094   -24.238 1.00 55.44  ? 107 LYS A N   1 
ATOM   836  C  CA  . LYS A 1 107 ? -25.782 9.881   -25.431 1.00 54.26  ? 107 LYS A CA  1 
ATOM   837  C  C   . LYS A 1 107 ? -24.559 10.658  -25.897 1.00 55.51  ? 107 LYS A C   1 
ATOM   838  O  O   . LYS A 1 107 ? -24.321 10.788  -27.104 1.00 59.55  ? 107 LYS A O   1 
ATOM   839  C  CB  . LYS A 1 107 ? -26.950 10.823  -25.157 1.00 57.92  ? 107 LYS A CB  1 
ATOM   840  C  CG  . LYS A 1 107 ? -28.315 10.189  -25.384 1.00 57.56  ? 107 LYS A CG  1 
ATOM   841  C  CD  . LYS A 1 107 ? -29.276 10.551  -24.265 1.00 67.49  ? 107 LYS A CD  1 
ATOM   842  C  CE  . LYS A 1 107 ? -30.729 10.433  -24.705 1.00 65.98  ? 107 LYS A CE  1 
ATOM   843  N  NZ  . LYS A 1 107 ? -31.559 11.534  -24.130 1.00 67.77  ? 107 LYS A NZ  1 
ATOM   844  N  N   . LYS A 1 108 ? -23.776 11.198  -24.960 1.00 63.94  ? 108 LYS A N   1 
ATOM   845  C  CA  . LYS A 1 108 ? -22.519 11.827  -25.345 1.00 62.71  ? 108 LYS A CA  1 
ATOM   846  C  C   . LYS A 1 108 ? -21.575 10.807  -25.967 1.00 60.20  ? 108 LYS A C   1 
ATOM   847  O  O   . LYS A 1 108 ? -20.902 11.096  -26.962 1.00 66.23  ? 108 LYS A O   1 
ATOM   848  C  CB  . LYS A 1 108 ? -21.854 12.495  -24.140 1.00 65.12  ? 108 LYS A CB  1 
ATOM   849  C  CG  . LYS A 1 108 ? -20.420 12.963  -24.427 1.00 75.22  ? 108 LYS A CG  1 
ATOM   850  C  CD  . LYS A 1 108 ? -19.942 14.027  -23.440 1.00 85.36  ? 108 LYS A CD  1 
ATOM   851  C  CE  . LYS A 1 108 ? -19.089 13.435  -22.324 1.00 89.43  ? 108 LYS A CE  1 
ATOM   852  N  NZ  . LYS A 1 108 ? -19.393 14.066  -21.002 1.00 93.04  ? 108 LYS A NZ  1 
ATOM   853  N  N   . VAL A 1 109 ? -21.516 9.605   -25.394 1.00 56.44  ? 109 VAL A N   1 
ATOM   854  C  CA  . VAL A 1 109 ? -20.585 8.597   -25.887 1.00 57.23  ? 109 VAL A CA  1 
ATOM   855  C  C   . VAL A 1 109 ? -20.973 8.150   -27.288 1.00 53.34  ? 109 VAL A C   1 
ATOM   856  O  O   . VAL A 1 109 ? -20.108 7.880   -28.127 1.00 61.34  ? 109 VAL A O   1 
ATOM   857  C  CB  . VAL A 1 109 ? -20.519 7.414   -24.902 1.00 53.23  ? 109 VAL A CB  1 
ATOM   858  C  CG1 . VAL A 1 109 ? -19.659 6.287   -25.454 1.00 48.09  ? 109 VAL A CG1 1 
ATOM   859  C  CG2 . VAL A 1 109 ? -19.979 7.889   -23.557 1.00 51.14  ? 109 VAL A CG2 1 
ATOM   860  N  N   . SER A 1 110 ? -22.274 8.066   -27.569 1.00 55.22  ? 110 SER A N   1 
ATOM   861  C  CA  . SER A 1 110 ? -22.701 7.625   -28.896 1.00 57.82  ? 110 SER A CA  1 
ATOM   862  C  C   . SER A 1 110 ? -22.350 8.654   -29.967 1.00 62.51  ? 110 SER A C   1 
ATOM   863  O  O   . SER A 1 110 ? -22.099 8.287   -31.121 1.00 64.12  ? 110 SER A O   1 
ATOM   864  C  CB  . SER A 1 110 ? -24.200 7.328   -28.895 1.00 49.94  ? 110 SER A CB  1 
ATOM   865  O  OG  . SER A 1 110 ? -24.959 8.488   -28.608 1.00 53.51  ? 110 SER A OG  1 
ATOM   866  N  N   . MET A 1 111 ? -22.324 9.939   -29.613 1.00 61.39  ? 111 MET A N   1 
ATOM   867  C  CA  . MET A 1 111 ? -21.852 10.945  -30.557 1.00 65.84  ? 111 MET A CA  1 
ATOM   868  C  C   . MET A 1 111 ? -20.371 10.758  -30.874 1.00 67.73  ? 111 MET A C   1 
ATOM   869  O  O   . MET A 1 111 ? -19.922 11.121  -31.969 1.00 71.80  ? 111 MET A O   1 
ATOM   870  C  CB  . MET A 1 111 ? -22.097 12.350  -30.002 1.00 68.75  ? 111 MET A CB  1 
ATOM   871  C  CG  . MET A 1 111 ? -23.562 12.702  -29.776 1.00 74.29  ? 111 MET A CG  1 
ATOM   872  S  SD  . MET A 1 111 ? -24.598 12.442  -31.231 1.00 92.14  ? 111 MET A SD  1 
ATOM   873  C  CE  . MET A 1 111 ? -26.085 13.324  -30.759 1.00 114.44 ? 111 MET A CE  1 
ATOM   874  N  N   . GLU A 1 112 ? -19.601 10.207  -29.935 1.00 63.51  ? 112 GLU A N   1 
ATOM   875  C  CA  . GLU A 1 112 ? -18.175 9.980   -30.130 1.00 72.19  ? 112 GLU A CA  1 
ATOM   876  C  C   . GLU A 1 112 ? -17.832 8.503   -30.289 1.00 69.83  ? 112 GLU A C   1 
ATOM   877  O  O   . GLU A 1 112 ? -16.654 8.139   -30.216 1.00 72.57  ? 112 GLU A O   1 
ATOM   878  C  CB  . GLU A 1 112 ? -17.372 10.554  -28.957 1.00 78.63  ? 112 GLU A CB  1 
ATOM   879  C  CG  . GLU A 1 112 ? -18.009 11.750  -28.271 1.00 80.84  ? 112 GLU A CG  1 
ATOM   880  C  CD  . GLU A 1 112 ? -17.010 12.558  -27.462 1.00 85.22  ? 112 GLU A CD  1 
ATOM   881  O  OE1 . GLU A 1 112 ? -16.625 12.111  -26.361 1.00 76.28  ? 112 GLU A OE1 1 
ATOM   882  O  OE2 . GLU A 1 112 ? -16.598 13.639  -27.942 1.00 95.71  ? 112 GLU A OE2 1 
ATOM   883  N  N   . GLY A 1 113 ? -18.828 7.643   -30.500 1.00 68.43  ? 113 GLY A N   1 
ATOM   884  C  CA  . GLY A 1 113 ? -18.561 6.216   -30.530 1.00 65.51  ? 113 GLY A CA  1 
ATOM   885  C  C   . GLY A 1 113 ? -17.557 5.821   -31.591 1.00 62.91  ? 113 GLY A C   1 
ATOM   886  O  O   . GLY A 1 113 ? -16.795 4.870   -31.406 1.00 57.92  ? 113 GLY A O   1 
ATOM   887  N  N   . HIS A 1 114 ? -17.527 6.551   -32.705 1.00 66.89  ? 114 HIS A N   1 
ATOM   888  C  CA  . HIS A 1 114 ? -16.683 6.177   -33.834 1.00 71.64  ? 114 HIS A CA  1 
ATOM   889  C  C   . HIS A 1 114 ? -15.194 6.438   -33.595 1.00 72.65  ? 114 HIS A C   1 
ATOM   890  O  O   . HIS A 1 114 ? -14.382 6.077   -34.457 1.00 67.67  ? 114 HIS A O   1 
ATOM   891  C  CB  . HIS A 1 114 ? -17.153 6.909   -35.096 1.00 76.36  ? 114 HIS A CB  1 
ATOM   892  C  CG  . HIS A 1 114 ? -17.304 8.392   -34.929 1.00 85.28  ? 114 HIS A CG  1 
ATOM   893  N  ND1 . HIS A 1 114 ? -16.237 9.255   -34.967 1.00 83.74  ? 114 HIS A ND1 1 
ATOM   894  C  CD2 . HIS A 1 114 ? -18.405 9.163   -34.751 1.00 84.79  ? 114 HIS A CD2 1 
ATOM   895  C  CE1 . HIS A 1 114 ? -16.662 10.495  -34.799 1.00 89.99  ? 114 HIS A CE1 1 
ATOM   896  N  NE2 . HIS A 1 114 ? -17.971 10.469  -34.667 1.00 94.63  ? 114 HIS A NE2 1 
ATOM   897  N  N   . LEU A 1 115 ? -14.810 7.032   -32.463 1.00 68.61  ? 115 LEU A N   1 
ATOM   898  C  CA  . LEU A 1 115 ? -13.408 7.291   -32.158 1.00 65.42  ? 115 LEU A CA  1 
ATOM   899  C  C   . LEU A 1 115 ? -12.744 6.175   -31.362 1.00 65.23  ? 115 LEU A C   1 
ATOM   900  O  O   . LEU A 1 115 ? -11.560 6.293   -31.027 1.00 59.99  ? 115 LEU A O   1 
ATOM   901  C  CB  . LEU A 1 115 ? -13.279 8.604   -31.379 1.00 72.68  ? 115 LEU A CB  1 
ATOM   902  C  CG  . LEU A 1 115 ? -14.100 9.752   -31.958 1.00 77.71  ? 115 LEU A CG  1 
ATOM   903  C  CD1 . LEU A 1 115 ? -13.730 11.073  -31.320 1.00 78.17  ? 115 LEU A CD1 1 
ATOM   904  C  CD2 . LEU A 1 115 ? -13.907 9.829   -33.461 1.00 77.93  ? 115 LEU A CD2 1 
ATOM   905  N  N   . TYR A 1 116 ? -13.470 5.106   -31.048 1.00 62.62  ? 116 TYR A N   1 
ATOM   906  C  CA  . TYR A 1 116 ? -12.937 3.982   -30.302 1.00 58.18  ? 116 TYR A CA  1 
ATOM   907  C  C   . TYR A 1 116 ? -13.033 2.717   -31.144 1.00 55.77  ? 116 TYR A C   1 
ATOM   908  O  O   . TYR A 1 116 ? -13.791 2.650   -32.115 1.00 58.56  ? 116 TYR A O   1 
ATOM   909  C  CB  . TYR A 1 116 ? -13.699 3.773   -28.981 1.00 49.37  ? 116 TYR A CB  1 
ATOM   910  C  CG  . TYR A 1 116 ? -13.757 4.994   -28.092 1.00 55.60  ? 116 TYR A CG  1 
ATOM   911  C  CD1 . TYR A 1 116 ? -14.730 5.962   -28.277 1.00 57.02  ? 116 TYR A CD1 1 
ATOM   912  C  CD2 . TYR A 1 116 ? -12.845 5.172   -27.057 1.00 60.09  ? 116 TYR A CD2 1 
ATOM   913  C  CE1 . TYR A 1 116 ? -14.792 7.077   -27.471 1.00 56.80  ? 116 TYR A CE1 1 
ATOM   914  C  CE2 . TYR A 1 116 ? -12.898 6.286   -26.241 1.00 60.08  ? 116 TYR A CE2 1 
ATOM   915  C  CZ  . TYR A 1 116 ? -13.875 7.237   -26.453 1.00 61.62  ? 116 TYR A CZ  1 
ATOM   916  O  OH  . TYR A 1 116 ? -13.941 8.353   -25.645 1.00 52.09  ? 116 TYR A OH  1 
ATOM   917  N  N   . ASN A 1 117 ? -12.248 1.712   -30.769 1.00 59.57  ? 117 ASN A N   1 
ATOM   918  C  CA  . ASN A 1 117 ? -12.515 0.363   -31.245 1.00 55.20  ? 117 ASN A CA  1 
ATOM   919  C  C   . ASN A 1 117 ? -13.827 -0.132  -30.639 1.00 52.01  ? 117 ASN A C   1 
ATOM   920  O  O   . ASN A 1 117 ? -14.416 0.505   -29.762 1.00 52.64  ? 117 ASN A O   1 
ATOM   921  C  CB  . ASN A 1 117 ? -11.360 -0.574  -30.901 1.00 57.86  ? 117 ASN A CB  1 
ATOM   922  C  CG  . ASN A 1 117 ? -10.104 -0.272  -31.705 1.00 64.90  ? 117 ASN A CG  1 
ATOM   923  O  OD1 . ASN A 1 117 ? -9.877  -0.849  -32.770 1.00 66.47  ? 117 ASN A OD1 1 
ATOM   924  N  ND2 . ASN A 1 117 ? -9.283  0.639   -31.196 1.00 67.18  ? 117 ASN A ND2 1 
ATOM   925  N  N   . GLY A 1 118 ? -14.281 -1.288  -31.112 1.00 52.12  ? 118 GLY A N   1 
ATOM   926  C  CA  . GLY A 1 118 ? -15.594 -1.771  -30.717 1.00 50.27  ? 118 GLY A CA  1 
ATOM   927  C  C   . GLY A 1 118 ? -15.701 -1.932  -29.210 1.00 47.32  ? 118 GLY A C   1 
ATOM   928  O  O   . GLY A 1 118 ? -14.786 -2.425  -28.551 1.00 41.07  ? 118 GLY A O   1 
ATOM   929  N  N   . PHE A 1 119 ? -16.835 -1.509  -28.664 1.00 46.93  ? 119 PHE A N   1 
ATOM   930  C  CA  . PHE A 1 119 ? -17.045 -1.611  -27.230 1.00 47.36  ? 119 PHE A CA  1 
ATOM   931  C  C   . PHE A 1 119 ? -18.536 -1.623  -26.929 1.00 47.08  ? 119 PHE A C   1 
ATOM   932  O  O   . PHE A 1 119 ? -19.346 -1.084  -27.689 1.00 48.78  ? 119 PHE A O   1 
ATOM   933  C  CB  . PHE A 1 119 ? -16.352 -0.457  -26.483 1.00 50.84  ? 119 PHE A CB  1 
ATOM   934  C  CG  . PHE A 1 119 ? -16.999 0.889   -26.683 1.00 44.99  ? 119 PHE A CG  1 
ATOM   935  C  CD1 . PHE A 1 119 ? -18.072 1.283   -25.903 1.00 41.56  ? 119 PHE A CD1 1 
ATOM   936  C  CD2 . PHE A 1 119 ? -16.511 1.774   -27.635 1.00 51.61  ? 119 PHE A CD2 1 
ATOM   937  C  CE1 . PHE A 1 119 ? -18.663 2.523   -26.074 1.00 42.36  ? 119 PHE A CE1 1 
ATOM   938  C  CE2 . PHE A 1 119 ? -17.100 3.018   -27.814 1.00 51.24  ? 119 PHE A CE2 1 
ATOM   939  C  CZ  . PHE A 1 119 ? -18.177 3.391   -27.031 1.00 50.70  ? 119 PHE A CZ  1 
ATOM   940  N  N   . ASN A 1 120 ? -18.876 -2.262  -25.815 1.00 42.91  ? 120 ASN A N   1 
ATOM   941  C  CA  . ASN A 1 120 ? -20.194 -2.190  -25.200 1.00 43.83  ? 120 ASN A CA  1 
ATOM   942  C  C   . ASN A 1 120 ? -20.047 -1.509  -23.844 1.00 52.59  ? 120 ASN A C   1 
ATOM   943  O  O   . ASN A 1 120 ? -19.050 -1.715  -23.142 1.00 48.54  ? 120 ASN A O   1 
ATOM   944  C  CB  . ASN A 1 120 ? -20.795 -3.575  -25.023 1.00 43.91  ? 120 ASN A CB  1 
ATOM   945  C  CG  . ASN A 1 120 ? -20.775 -4.376  -26.298 1.00 45.47  ? 120 ASN A CG  1 
ATOM   946  O  OD1 . ASN A 1 120 ? -21.716 -4.314  -27.087 1.00 40.98  ? 120 ASN A OD1 1 
ATOM   947  N  ND2 . ASN A 1 120 ? -19.704 -5.135  -26.510 1.00 42.07  ? 120 ASN A ND2 1 
ATOM   948  N  N   . LEU A 1 121 ? -21.043 -0.709  -23.467 1.00 47.36  ? 121 LEU A N   1 
ATOM   949  C  CA  . LEU A 1 121 ? -20.936 0.129   -22.280 1.00 46.56  ? 121 LEU A CA  1 
ATOM   950  C  C   . LEU A 1 121 ? -22.236 0.092   -21.494 1.00 40.40  ? 121 LEU A C   1 
ATOM   951  O  O   . LEU A 1 121 ? -23.301 0.415   -22.027 1.00 46.15  ? 121 LEU A O   1 
ATOM   952  C  CB  . LEU A 1 121 ? -20.580 1.567   -22.679 1.00 45.18  ? 121 LEU A CB  1 
ATOM   953  C  CG  . LEU A 1 121 ? -20.330 2.575   -21.557 1.00 48.26  ? 121 LEU A CG  1 
ATOM   954  C  CD1 . LEU A 1 121 ? -19.203 2.112   -20.640 1.00 49.60  ? 121 LEU A CD1 1 
ATOM   955  C  CD2 . LEU A 1 121 ? -20.016 3.953   -22.151 1.00 44.81  ? 121 LEU A CD2 1 
ATOM   956  N  N   . ILE A 1 122 ? -22.138 -0.295  -20.225 1.00 44.93  ? 122 ILE A N   1 
ATOM   957  C  CA  . ILE A 1 122 ? -23.241 -0.220  -19.273 1.00 46.45  ? 122 ILE A CA  1 
ATOM   958  C  C   . ILE A 1 122 ? -22.974 0.951   -18.333 1.00 47.78  ? 122 ILE A C   1 
ATOM   959  O  O   . ILE A 1 122 ? -21.873 1.073   -17.783 1.00 43.45  ? 122 ILE A O   1 
ATOM   960  C  CB  . ILE A 1 122 ? -23.380 -1.530  -18.476 1.00 48.94  ? 122 ILE A CB  1 
ATOM   961  C  CG1 . ILE A 1 122 ? -23.755 -2.696  -19.391 1.00 47.20  ? 122 ILE A CG1 1 
ATOM   962  C  CG2 . ILE A 1 122 ? -24.396 -1.364  -17.346 1.00 53.81  ? 122 ILE A CG2 1 
ATOM   963  C  CD1 . ILE A 1 122 ? -25.143 -2.605  -19.982 1.00 49.02  ? 122 ILE A CD1 1 
ATOM   964  N  N   . ALA A 1 123 ? -23.976 1.808   -18.144 1.00 47.88  ? 123 ALA A N   1 
ATOM   965  C  CA  . ALA A 1 123 ? -23.903 2.898   -17.175 1.00 42.93  ? 123 ALA A CA  1 
ATOM   966  C  C   . ALA A 1 123 ? -25.169 2.879   -16.333 1.00 48.88  ? 123 ALA A C   1 
ATOM   967  O  O   . ALA A 1 123 ? -26.275 2.759   -16.875 1.00 46.93  ? 123 ALA A O   1 
ATOM   968  C  CB  . ALA A 1 123 ? -23.735 4.253   -17.858 1.00 46.87  ? 123 ALA A CB  1 
ATOM   969  N  N   . ALA A 1 124 ? -25.014 3.013   -15.020 1.00 46.40  ? 124 ALA A N   1 
ATOM   970  C  CA  . ALA A 1 124 ? -26.118 2.819   -14.098 1.00 49.13  ? 124 ALA A CA  1 
ATOM   971  C  C   . ALA A 1 124 ? -26.101 3.883   -13.013 1.00 55.43  ? 124 ALA A C   1 
ATOM   972  O  O   . ALA A 1 124 ? -25.046 4.209   -12.460 1.00 53.04  ? 124 ALA A O   1 
ATOM   973  C  CB  . ALA A 1 124 ? -26.040 1.422   -13.466 1.00 47.05  ? 124 ALA A CB  1 
ATOM   974  N  N   . ASP A 1 125 ? -27.285 4.428   -12.723 1.00 58.52  ? 125 ASP A N   1 
ATOM   975  C  CA  . ASP A 1 125 ? -27.493 5.303   -11.576 1.00 56.68  ? 125 ASP A CA  1 
ATOM   976  C  C   . ASP A 1 125 ? -28.129 4.480   -10.461 1.00 53.89  ? 125 ASP A C   1 
ATOM   977  O  O   . ASP A 1 125 ? -29.200 3.898   -10.653 1.00 51.66  ? 125 ASP A O   1 
ATOM   978  C  CB  . ASP A 1 125 ? -28.391 6.485   -11.929 1.00 55.50  ? 125 ASP A CB  1 
ATOM   979  C  CG  . ASP A 1 125 ? -27.898 7.252   -13.133 1.00 61.00  ? 125 ASP A CG  1 
ATOM   980  O  OD1 . ASP A 1 125 ? -26.668 7.430   -13.261 1.00 58.26  ? 125 ASP A OD1 1 
ATOM   981  O  OD2 . ASP A 1 125 ? -28.746 7.676   -13.945 1.00 58.05  ? 125 ASP A OD2 1 
ATOM   982  N  N   . LEU A 1 126 ? -27.476 4.435   -9.306  1.00 58.16  ? 126 LEU A N   1 
ATOM   983  C  CA  . LEU A 1 126 ? -27.985 3.714   -8.144  1.00 58.41  ? 126 LEU A CA  1 
ATOM   984  C  C   . LEU A 1 126 ? -28.458 4.734   -7.122  1.00 59.51  ? 126 LEU A C   1 
ATOM   985  O  O   . LEU A 1 126 ? -27.667 5.550   -6.637  1.00 57.87  ? 126 LEU A O   1 
ATOM   986  C  CB  . LEU A 1 126 ? -26.911 2.805   -7.555  1.00 57.85  ? 126 LEU A CB  1 
ATOM   987  C  CG  . LEU A 1 126 ? -26.308 1.825   -8.559  1.00 57.44  ? 126 LEU A CG  1 
ATOM   988  C  CD1 . LEU A 1 126 ? -25.113 1.104   -7.960  1.00 58.20  ? 126 LEU A CD1 1 
ATOM   989  C  CD2 . LEU A 1 126 ? -27.354 0.828   -9.036  1.00 55.88  ? 126 LEU A CD2 1 
ATOM   990  N  N   . SER A 1 127 ? -29.744 4.696   -6.801  1.00 65.10  ? 127 SER A N   1 
ATOM   991  C  CA  . SER A 1 127 ? -30.350 5.667   -5.899  1.00 69.30  ? 127 SER A CA  1 
ATOM   992  C  C   . SER A 1 127 ? -31.408 4.951   -5.080  1.00 69.36  ? 127 SER A C   1 
ATOM   993  O  O   . SER A 1 127 ? -32.425 4.510   -5.624  1.00 68.84  ? 127 SER A O   1 
ATOM   994  C  CB  . SER A 1 127 ? -30.952 6.839   -6.676  1.00 67.10  ? 127 SER A CB  1 
ATOM   995  O  OG  . SER A 1 127 ? -31.325 7.890   -5.807  1.00 75.78  ? 127 SER A OG  1 
ATOM   996  N  N   . THR A 1 128 ? -31.160 4.817   -3.777  1.00 72.21  ? 128 THR A N   1 
ATOM   997  C  CA  . THR A 1 128 ? -32.155 4.210   -2.898  1.00 81.87  ? 128 THR A CA  1 
ATOM   998  C  C   . THR A 1 128 ? -33.455 5.007   -2.929  1.00 83.56  ? 128 THR A C   1 
ATOM   999  O  O   . THR A 1 128 ? -34.548 4.435   -2.866  1.00 78.64  ? 128 THR A O   1 
ATOM   1000 C  CB  . THR A 1 128 ? -31.604 4.120   -1.473  1.00 83.37  ? 128 THR A CB  1 
ATOM   1001 O  OG1 . THR A 1 128 ? -30.195 3.861   -1.525  1.00 82.33  ? 128 THR A OG1 1 
ATOM   1002 C  CG2 . THR A 1 128 ? -32.281 2.996   -0.698  1.00 77.50  ? 128 THR A CG2 1 
ATOM   1003 N  N   . ALA A 1 129 ? -33.353 6.331   -3.049  1.00 97.35  ? 129 ALA A N   1 
ATOM   1004 C  CA  . ALA A 1 129 ? -34.516 7.208   -3.053  1.00 87.67  ? 129 ALA A CA  1 
ATOM   1005 C  C   . ALA A 1 129 ? -35.106 7.385   -4.448  1.00 95.77  ? 129 ALA A C   1 
ATOM   1006 O  O   . ALA A 1 129 ? -36.308 7.182   -4.642  1.00 98.11  ? 129 ALA A O   1 
ATOM   1007 C  CB  . ALA A 1 129 ? -34.136 8.573   -2.471  1.00 92.72  ? 129 ALA A CB  1 
ATOM   1008 N  N   . LYS A 1 130 ? -34.274 7.762   -5.426  1.00 85.21  ? 130 LYS A N   1 
ATOM   1009 C  CA  . LYS A 1 130 ? -34.782 8.146   -6.737  1.00 76.43  ? 130 LYS A CA  1 
ATOM   1010 C  C   . LYS A 1 130 ? -35.125 6.946   -7.615  1.00 77.13  ? 130 LYS A C   1 
ATOM   1011 O  O   . LYS A 1 130 ? -35.990 7.056   -8.490  1.00 81.36  ? 130 LYS A O   1 
ATOM   1012 C  CB  . LYS A 1 130 ? -33.760 9.035   -7.448  1.00 68.62  ? 130 LYS A CB  1 
ATOM   1013 N  N   . GLY A 1 131 ? -34.465 5.817   -7.417  1.00 73.97  ? 131 GLY A N   1 
ATOM   1014 C  CA  . GLY A 1 131 ? -34.748 4.630   -8.207  1.00 63.03  ? 131 GLY A CA  1 
ATOM   1015 C  C   . GLY A 1 131 ? -33.633 4.351   -9.201  1.00 63.70  ? 131 GLY A C   1 
ATOM   1016 O  O   . GLY A 1 131 ? -33.111 5.258   -9.867  1.00 62.47  ? 131 GLY A O   1 
ATOM   1017 N  N   . ASP A 1 132 ? -33.271 3.077   -9.319  1.00 63.46  ? 132 ASP A N   1 
ATOM   1018 C  CA  . ASP A 1 132 ? -32.136 2.679   -10.143 1.00 62.04  ? 132 ASP A CA  1 
ATOM   1019 C  C   . ASP A 1 132 ? -32.466 2.735   -11.628 1.00 57.27  ? 132 ASP A C   1 
ATOM   1020 O  O   . ASP A 1 132 ? -33.589 2.424   -12.042 1.00 63.65  ? 132 ASP A O   1 
ATOM   1021 C  CB  . ASP A 1 132 ? -31.679 1.267   -9.774  1.00 56.55  ? 132 ASP A CB  1 
ATOM   1022 C  CG  . ASP A 1 132 ? -31.349 1.125   -8.303  1.00 60.36  ? 132 ASP A CG  1 
ATOM   1023 O  OD1 . ASP A 1 132 ? -30.698 2.027   -7.744  1.00 58.51  ? 132 ASP A OD1 1 
ATOM   1024 O  OD2 . ASP A 1 132 ? -31.750 0.109   -7.705  1.00 70.58  ? 132 ASP A OD2 1 
ATOM   1025 N  N   . VAL A 1 133 ? -31.476 3.121   -12.423 1.00 53.14  ? 133 VAL A N   1 
ATOM   1026 C  CA  . VAL A 1 133 ? -31.571 3.139   -13.877 1.00 53.13  ? 133 VAL A CA  1 
ATOM   1027 C  C   . VAL A 1 133 ? -30.317 2.487   -14.439 1.00 46.42  ? 133 VAL A C   1 
ATOM   1028 O  O   . VAL A 1 133 ? -29.202 2.856   -14.059 1.00 49.23  ? 133 VAL A O   1 
ATOM   1029 C  CB  . VAL A 1 133 ? -31.717 4.573   -14.419 1.00 49.61  ? 133 VAL A CB  1 
ATOM   1030 C  CG1 . VAL A 1 133 ? -31.764 4.566   -15.944 1.00 48.35  ? 133 VAL A CG1 1 
ATOM   1031 C  CG2 . VAL A 1 133 ? -32.952 5.235   -13.839 1.00 42.66  ? 133 VAL A CG2 1 
ATOM   1032 N  N   . ILE A 1 134 ? -30.493 1.519   -15.335 1.00 44.19  ? 134 ILE A N   1 
ATOM   1033 C  CA  . ILE A 1 134 ? -29.383 0.904   -16.053 1.00 43.85  ? 134 ILE A CA  1 
ATOM   1034 C  C   . ILE A 1 134 ? -29.622 1.107   -17.541 1.00 45.94  ? 134 ILE A C   1 
ATOM   1035 O  O   . ILE A 1 134 ? -30.693 0.762   -18.052 1.00 46.89  ? 134 ILE A O   1 
ATOM   1036 C  CB  . ILE A 1 134 ? -29.235 -0.590  -15.719 1.00 48.57  ? 134 ILE A CB  1 
ATOM   1037 C  CG1 . ILE A 1 134 ? -29.106 -0.777  -14.206 1.00 49.03  ? 134 ILE A CG1 1 
ATOM   1038 C  CG2 . ILE A 1 134 ? -28.018 -1.177  -16.424 1.00 42.82  ? 134 ILE A CG2 1 
ATOM   1039 C  CD1 . ILE A 1 134 ? -28.785 -2.193  -13.778 1.00 52.55  ? 134 ILE A CD1 1 
ATOM   1040 N  N   . CYS A 1 135 ? -28.630 1.672   -18.226 1.00 48.72  ? 135 CYS A N   1 
ATOM   1041 C  CA  . CYS A 1 135 ? -28.689 1.921   -19.656 1.00 47.68  ? 135 CYS A CA  1 
ATOM   1042 C  C   . CYS A 1 135 ? -27.529 1.216   -20.344 1.00 50.75  ? 135 CYS A C   1 
ATOM   1043 O  O   . CYS A 1 135 ? -26.551 0.817   -19.700 1.00 43.04  ? 135 CYS A O   1 
ATOM   1044 C  CB  . CYS A 1 135 ? -28.632 3.421   -19.967 1.00 50.69  ? 135 CYS A CB  1 
ATOM   1045 S  SG  . CYS A 1 135 ? -29.840 4.405   -19.076 1.00 51.14  ? 135 CYS A SG  1 
ATOM   1046 N  N   . TYR A 1 136 ? -27.651 1.077   -21.670 1.00 47.78  ? 136 TYR A N   1 
ATOM   1047 C  CA  . TYR A 1 136 ? -26.692 0.330   -22.465 1.00 41.24  ? 136 TYR A CA  1 
ATOM   1048 C  C   . TYR A 1 136 ? -26.481 1.002   -23.808 1.00 41.91  ? 136 TYR A C   1 
ATOM   1049 O  O   . TYR A 1 136 ? -27.439 1.472   -24.430 1.00 47.53  ? 136 TYR A O   1 
ATOM   1050 C  CB  . TYR A 1 136 ? -27.161 -1.110  -22.689 1.00 38.68  ? 136 TYR A CB  1 
ATOM   1051 C  CG  . TYR A 1 136 ? -26.463 -1.788  -23.842 1.00 48.20  ? 136 TYR A CG  1 
ATOM   1052 C  CD1 . TYR A 1 136 ? -25.132 -2.173  -23.741 1.00 45.55  ? 136 TYR A CD1 1 
ATOM   1053 C  CD2 . TYR A 1 136 ? -27.134 -2.043  -25.037 1.00 48.20  ? 136 TYR A CD2 1 
ATOM   1054 C  CE1 . TYR A 1 136 ? -24.490 -2.792  -24.787 1.00 47.16  ? 136 TYR A CE1 1 
ATOM   1055 C  CE2 . TYR A 1 136 ? -26.501 -2.667  -26.092 1.00 38.42  ? 136 TYR A CE2 1 
ATOM   1056 C  CZ  . TYR A 1 136 ? -25.177 -3.036  -25.962 1.00 48.61  ? 136 TYR A CZ  1 
ATOM   1057 O  OH  . TYR A 1 136 ? -24.522 -3.651  -27.010 1.00 40.75  ? 136 TYR A OH  1 
ATOM   1058 N  N   . TYR A 1 137 ? -25.221 1.046   -24.248 1.00 41.65  ? 137 TYR A N   1 
ATOM   1059 C  CA  . TYR A 1 137 ? -24.877 1.533   -25.574 1.00 47.17  ? 137 TYR A CA  1 
ATOM   1060 C  C   . TYR A 1 137 ? -23.612 0.832   -26.044 1.00 50.23  ? 137 TYR A C   1 
ATOM   1061 O  O   . TYR A 1 137 ? -22.675 0.649   -25.258 1.00 44.34  ? 137 TYR A O   1 
ATOM   1062 C  CB  . TYR A 1 137 ? -24.650 3.048   -25.607 1.00 49.56  ? 137 TYR A CB  1 
ATOM   1063 C  CG  . TYR A 1 137 ? -23.938 3.491   -26.868 1.00 43.85  ? 137 TYR A CG  1 
ATOM   1064 C  CD1 . TYR A 1 137 ? -24.623 3.605   -28.069 1.00 51.63  ? 137 TYR A CD1 1 
ATOM   1065 C  CD2 . TYR A 1 137 ? -22.575 3.763   -26.861 1.00 46.01  ? 137 TYR A CD2 1 
ATOM   1066 C  CE1 . TYR A 1 137 ? -23.971 3.989   -29.236 1.00 49.87  ? 137 TYR A CE1 1 
ATOM   1067 C  CE2 . TYR A 1 137 ? -21.915 4.149   -28.012 1.00 51.61  ? 137 TYR A CE2 1 
ATOM   1068 C  CZ  . TYR A 1 137 ? -22.614 4.251   -29.200 1.00 52.25  ? 137 TYR A CZ  1 
ATOM   1069 O  OH  . TYR A 1 137 ? -21.955 4.642   -30.348 1.00 52.78  ? 137 TYR A OH  1 
ATOM   1070 N  N   . GLY A 1 138 ? -23.595 0.449   -27.326 1.00 42.47  ? 138 GLY A N   1 
ATOM   1071 C  CA  . GLY A 1 138 ? -22.410 -0.104  -27.951 1.00 46.91  ? 138 GLY A CA  1 
ATOM   1072 C  C   . GLY A 1 138 ? -22.187 0.470   -29.338 1.00 47.04  ? 138 GLY A C   1 
ATOM   1073 O  O   . GLY A 1 138 ? -23.131 0.559   -30.129 1.00 47.70  ? 138 GLY A O   1 
ATOM   1074 N  N   . ASN A 1 139 ? -20.950 0.858   -29.650 1.00 40.39  ? 139 ASN A N   1 
ATOM   1075 C  CA  . ASN A 1 139 ? -20.644 1.535   -30.905 1.00 42.79  ? 139 ASN A CA  1 
ATOM   1076 C  C   . ASN A 1 139 ? -20.558 0.580   -32.095 1.00 47.96  ? 139 ASN A C   1 
ATOM   1077 O  O   . ASN A 1 139 ? -20.107 0.988   -33.170 1.00 44.55  ? 139 ASN A O   1 
ATOM   1078 C  CB  . ASN A 1 139 ? -19.327 2.309   -30.779 1.00 47.23  ? 139 ASN A CB  1 
ATOM   1079 C  CG  . ASN A 1 139 ? -18.122 1.396   -30.725 1.00 48.10  ? 139 ASN A CG  1 
ATOM   1080 O  OD1 . ASN A 1 139 ? -18.247 0.217   -30.412 1.00 52.70  ? 139 ASN A OD1 1 
ATOM   1081 N  ND2 . ASN A 1 139 ? -16.948 1.936   -31.030 1.00 49.38  ? 139 ASN A ND2 1 
ATOM   1082 N  N   . ARG A 1 140 ? -20.952 -0.678  -31.919 1.00 46.26  ? 140 ARG A N   1 
ATOM   1083 C  CA  . ARG A 1 140 ? -21.085 -1.617  -33.019 1.00 45.39  ? 140 ARG A CA  1 
ATOM   1084 C  C   . ARG A 1 140 ? -22.519 -2.094  -33.195 1.00 43.02  ? 140 ARG A C   1 
ATOM   1085 O  O   . ARG A 1 140 ? -22.769 -2.950  -34.050 1.00 45.34  ? 140 ARG A O   1 
ATOM   1086 C  CB  . ARG A 1 140 ? -20.158 -2.824  -32.805 1.00 46.84  ? 140 ARG A CB  1 
ATOM   1087 C  CG  . ARG A 1 140 ? -18.668 -2.490  -32.898 1.00 47.42  ? 140 ARG A CG  1 
ATOM   1088 C  CD  . ARG A 1 140 ? -18.224 -2.306  -34.362 1.00 51.50  ? 140 ARG A CD  1 
ATOM   1089 N  NE  . ARG A 1 140 ? -16.805 -1.984  -34.478 1.00 53.28  ? 140 ARG A NE  1 
ATOM   1090 C  CZ  . ARG A 1 140 ? -16.306 -0.757  -34.404 1.00 51.47  ? 140 ARG A CZ  1 
ATOM   1091 N  NH1 . ARG A 1 140 ? -17.086 0.297   -34.224 1.00 56.71  ? 140 ARG A NH1 1 
ATOM   1092 N  NH2 . ARG A 1 140 ? -14.991 -0.585  -34.508 1.00 51.84  ? 140 ARG A NH2 1 
ATOM   1093 N  N   . GLY A 1 141 ? -23.459 -1.581  -32.401 1.00 43.34  ? 141 GLY A N   1 
ATOM   1094 C  CA  . GLY A 1 141 ? -24.864 -1.915  -32.538 1.00 40.68  ? 141 GLY A CA  1 
ATOM   1095 C  C   . GLY A 1 141 ? -25.694 -0.697  -32.892 1.00 44.85  ? 141 GLY A C   1 
ATOM   1096 O  O   . GLY A 1 141 ? -25.299 0.102   -33.745 1.00 45.47  ? 141 GLY A O   1 
ATOM   1097 N  N   . GLU A 1 142 ? -26.845 -0.541  -32.247 1.00 45.58  ? 142 GLU A N   1 
ATOM   1098 C  CA  . GLU A 1 142 ? -27.732 0.563   -32.582 1.00 51.62  ? 142 GLU A CA  1 
ATOM   1099 C  C   . GLU A 1 142 ? -27.158 1.888   -32.076 1.00 51.87  ? 142 GLU A C   1 
ATOM   1100 O  O   . GLU A 1 142 ? -26.511 1.937   -31.028 1.00 48.92  ? 142 GLU A O   1 
ATOM   1101 C  CB  . GLU A 1 142 ? -29.117 0.328   -31.990 1.00 50.08  ? 142 GLU A CB  1 
ATOM   1102 C  CG  . GLU A 1 142 ? -29.844 -0.880  -32.576 1.00 51.47  ? 142 GLU A CG  1 
ATOM   1103 C  CD  . GLU A 1 142 ? -30.097 -0.762  -34.075 1.00 64.82  ? 142 GLU A CD  1 
ATOM   1104 O  OE1 . GLU A 1 142 ? -30.449 -1.779  -34.713 1.00 60.09  ? 142 GLU A OE1 1 
ATOM   1105 O  OE2 . GLU A 1 142 ? -29.942 0.355   -34.624 1.00 66.62  ? 142 GLU A OE2 1 
ATOM   1106 N  N   . PRO A 1 143 ? -27.386 2.983   -32.810 1.00 56.27  ? 143 PRO A N   1 
ATOM   1107 C  CA  . PRO A 1 143 ? -26.754 4.257   -32.428 1.00 53.63  ? 143 PRO A CA  1 
ATOM   1108 C  C   . PRO A 1 143 ? -27.280 4.848   -31.129 1.00 59.84  ? 143 PRO A C   1 
ATOM   1109 O  O   . PRO A 1 143 ? -26.533 5.555   -30.439 1.00 52.76  ? 143 PRO A O   1 
ATOM   1110 C  CB  . PRO A 1 143 ? -27.061 5.174   -33.623 1.00 51.34  ? 143 PRO A CB  1 
ATOM   1111 C  CG  . PRO A 1 143 ? -28.321 4.623   -34.197 1.00 56.22  ? 143 PRO A CG  1 
ATOM   1112 C  CD  . PRO A 1 143 ? -28.253 3.121   -33.995 1.00 53.88  ? 143 PRO A CD  1 
ATOM   1113 N  N   . ASP A 1 144 ? -28.533 4.578   -30.771 1.00 57.26  ? 144 ASP A N   1 
ATOM   1114 C  CA  . ASP A 1 144 ? -29.143 5.257   -29.633 1.00 56.64  ? 144 ASP A CA  1 
ATOM   1115 C  C   . ASP A 1 144 ? -29.039 4.412   -28.381 1.00 50.53  ? 144 ASP A C   1 
ATOM   1116 O  O   . ASP A 1 144 ? -29.358 3.217   -28.424 1.00 52.58  ? 144 ASP A O   1 
ATOM   1117 C  CB  . ASP A 1 144 ? -30.612 5.562   -29.927 1.00 58.78  ? 144 ASP A CB  1 
ATOM   1118 C  CG  . ASP A 1 144 ? -30.783 6.575   -31.043 1.00 61.67  ? 144 ASP A CG  1 
ATOM   1119 O  OD1 . ASP A 1 144 ? -30.049 7.588   -31.053 1.00 63.98  ? 144 ASP A OD1 1 
ATOM   1120 O  OD2 . ASP A 1 144 ? -31.647 6.358   -31.914 1.00 68.08  ? 144 ASP A OD2 1 
ATOM   1121 N  N   . PRO A 1 145 ? -28.601 4.983   -27.255 1.00 51.40  ? 145 PRO A N   1 
ATOM   1122 C  CA  . PRO A 1 145 ? -28.633 4.235   -25.993 1.00 49.45  ? 145 PRO A CA  1 
ATOM   1123 C  C   . PRO A 1 145 ? -30.055 3.848   -25.620 1.00 43.57  ? 145 PRO A C   1 
ATOM   1124 O  O   . PRO A 1 145 ? -31.029 4.472   -26.045 1.00 44.87  ? 145 PRO A O   1 
ATOM   1125 C  CB  . PRO A 1 145 ? -28.042 5.213   -24.971 1.00 53.74  ? 145 PRO A CB  1 
ATOM   1126 C  CG  . PRO A 1 145 ? -27.254 6.198   -25.773 1.00 44.81  ? 145 PRO A CG  1 
ATOM   1127 C  CD  . PRO A 1 145 ? -27.950 6.301   -27.104 1.00 55.90  ? 145 PRO A CD  1 
ATOM   1128 N  N   . ILE A 1 146 ? -30.166 2.784   -24.824 1.00 41.59  ? 146 ILE A N   1 
ATOM   1129 C  CA  . ILE A 1 146 ? -31.459 2.250   -24.414 1.00 41.40  ? 146 ILE A CA  1 
ATOM   1130 C  C   . ILE A 1 146 ? -31.499 2.147   -22.894 1.00 45.52  ? 146 ILE A C   1 
ATOM   1131 O  O   . ILE A 1 146 ? -30.481 1.910   -22.234 1.00 37.51  ? 146 ILE A O   1 
ATOM   1132 C  CB  . ILE A 1 146 ? -31.759 0.872   -25.059 1.00 41.87  ? 146 ILE A CB  1 
ATOM   1133 C  CG1 . ILE A 1 146 ? -30.658 -0.137  -24.718 1.00 39.02  ? 146 ILE A CG1 1 
ATOM   1134 C  CG2 . ILE A 1 146 ? -31.906 1.009   -26.572 1.00 40.91  ? 146 ILE A CG2 1 
ATOM   1135 C  CD1 . ILE A 1 146 ? -31.012 -1.567  -25.094 1.00 41.16  ? 146 ILE A CD1 1 
ATOM   1136 N  N   . VAL A 1 147 ? -32.690 2.348   -22.344 1.00 43.41  ? 147 VAL A N   1 
ATOM   1137 C  CA  . VAL A 1 147 ? -32.947 2.138   -20.926 1.00 51.38  ? 147 VAL A CA  1 
ATOM   1138 C  C   . VAL A 1 147 ? -33.451 0.711   -20.757 1.00 50.07  ? 147 VAL A C   1 
ATOM   1139 O  O   . VAL A 1 147 ? -34.444 0.318   -21.384 1.00 47.81  ? 147 VAL A O   1 
ATOM   1140 C  CB  . VAL A 1 147 ? -33.965 3.155   -20.386 1.00 49.81  ? 147 VAL A CB  1 
ATOM   1141 C  CG1 . VAL A 1 147 ? -34.121 2.995   -18.884 1.00 38.64  ? 147 VAL A CG1 1 
ATOM   1142 C  CG2 . VAL A 1 147 ? -33.541 4.580   -20.759 1.00 46.31  ? 147 VAL A CG2 1 
ATOM   1143 N  N   . LEU A 1 148 ? -32.766 -0.065  -19.918 1.00 45.13  ? 148 LEU A N   1 
ATOM   1144 C  CA  . LEU A 1 148 ? -33.083 -1.477  -19.765 1.00 47.06  ? 148 LEU A CA  1 
ATOM   1145 C  C   . LEU A 1 148 ? -34.223 -1.670  -18.776 1.00 46.91  ? 148 LEU A C   1 
ATOM   1146 O  O   . LEU A 1 148 ? -34.288 -1.004  -17.737 1.00 44.84  ? 148 LEU A O   1 
ATOM   1147 C  CB  . LEU A 1 148 ? -31.856 -2.257  -19.287 1.00 48.57  ? 148 LEU A CB  1 
ATOM   1148 C  CG  . LEU A 1 148 ? -30.594 -2.195  -20.149 1.00 44.11  ? 148 LEU A CG  1 
ATOM   1149 C  CD1 . LEU A 1 148 ? -29.503 -3.059  -19.524 1.00 47.30  ? 148 LEU A CD1 1 
ATOM   1150 C  CD2 . LEU A 1 148 ? -30.878 -2.628  -21.576 1.00 50.26  ? 148 LEU A CD2 1 
ATOM   1151 N  N   . THR A 1 149 ? -35.120 -2.589  -19.104 1.00 45.17  ? 149 THR A N   1 
ATOM   1152 C  CA  . THR A 1 149 ? -36.132 -3.022  -18.157 1.00 49.55  ? 149 THR A CA  1 
ATOM   1153 C  C   . THR A 1 149 ? -35.521 -3.997  -17.156 1.00 51.22  ? 149 THR A C   1 
ATOM   1154 O  O   . THR A 1 149 ? -34.498 -4.629  -17.431 1.00 47.32  ? 149 THR A O   1 
ATOM   1155 C  CB  . THR A 1 149 ? -37.293 -3.683  -18.890 1.00 45.94  ? 149 THR A CB  1 
ATOM   1156 O  OG1 . THR A 1 149 ? -36.820 -4.831  -19.600 1.00 50.69  ? 149 THR A OG1 1 
ATOM   1157 C  CG2 . THR A 1 149 ? -37.929 -2.712  -19.862 1.00 44.61  ? 149 THR A CG2 1 
ATOM   1158 N  N   . PRO A 1 150 ? -36.134 -4.143  -15.984 1.00 54.69  ? 150 PRO A N   1 
ATOM   1159 C  CA  . PRO A 1 150 ? -35.596 -5.084  -14.991 1.00 52.90  ? 150 PRO A CA  1 
ATOM   1160 C  C   . PRO A 1 150 ? -35.522 -6.502  -15.540 1.00 49.82  ? 150 PRO A C   1 
ATOM   1161 O  O   . PRO A 1 150 ? -36.376 -6.931  -16.316 1.00 49.34  ? 150 PRO A O   1 
ATOM   1162 C  CB  . PRO A 1 150 ? -36.594 -4.981  -13.828 1.00 54.72  ? 150 PRO A CB  1 
ATOM   1163 C  CG  . PRO A 1 150 ? -37.210 -3.621  -13.977 1.00 46.75  ? 150 PRO A CG  1 
ATOM   1164 C  CD  . PRO A 1 150 ? -37.262 -3.350  -15.455 1.00 50.13  ? 150 PRO A CD  1 
ATOM   1165 N  N   . GLY A 1 151 ? -34.483 -7.224  -15.134 1.00 46.68  ? 151 GLY A N   1 
ATOM   1166 C  CA  . GLY A 1 151 ? -34.307 -8.595  -15.560 1.00 44.65  ? 151 GLY A CA  1 
ATOM   1167 C  C   . GLY A 1 151 ? -32.855 -9.021  -15.434 1.00 43.04  ? 151 GLY A C   1 
ATOM   1168 O  O   . GLY A 1 151 ? -32.011 -8.287  -14.919 1.00 41.97  ? 151 GLY A O   1 
ATOM   1169 N  N   . THR A 1 152 ? -32.594 -10.234 -15.917 1.00 45.43  ? 152 THR A N   1 
ATOM   1170 C  CA  . THR A 1 152 ? -31.258 -10.817 -15.919 1.00 43.21  ? 152 THR A CA  1 
ATOM   1171 C  C   . THR A 1 152 ? -30.664 -10.699 -17.316 1.00 45.51  ? 152 THR A C   1 
ATOM   1172 O  O   . THR A 1 152 ? -31.264 -11.154 -18.295 1.00 49.01  ? 152 THR A O   1 
ATOM   1173 C  CB  . THR A 1 152 ? -31.291 -12.281 -15.485 1.00 50.06  ? 152 THR A CB  1 
ATOM   1174 O  OG1 . THR A 1 152 ? -31.828 -12.370 -14.157 1.00 56.05  ? 152 THR A OG1 1 
ATOM   1175 C  CG2 . THR A 1 152 ? -29.888 -12.888 -15.508 1.00 53.09  ? 152 THR A CG2 1 
ATOM   1176 N  N   . TYR A 1 153 ? -29.487 -10.096 -17.400 1.00 47.34  ? 153 TYR A N   1 
ATOM   1177 C  CA  . TYR A 1 153 ? -28.844 -9.802  -18.665 1.00 47.77  ? 153 TYR A CA  1 
ATOM   1178 C  C   . TYR A 1 153 ? -27.483 -10.479 -18.739 1.00 47.54  ? 153 TYR A C   1 
ATOM   1179 O  O   . TYR A 1 153 ? -26.854 -10.792 -17.717 1.00 38.41  ? 153 TYR A O   1 
ATOM   1180 C  CB  . TYR A 1 153 ? -28.676 -8.288  -18.864 1.00 45.73  ? 153 TYR A CB  1 
ATOM   1181 C  CG  . TYR A 1 153 ? -29.966 -7.570  -19.173 1.00 48.58  ? 153 TYR A CG  1 
ATOM   1182 C  CD1 . TYR A 1 153 ? -30.801 -7.132  -18.152 1.00 45.79  ? 153 TYR A CD1 1 
ATOM   1183 C  CD2 . TYR A 1 153 ? -30.351 -7.328  -20.486 1.00 42.64  ? 153 TYR A CD2 1 
ATOM   1184 C  CE1 . TYR A 1 153 ? -31.987 -6.475  -18.430 1.00 48.09  ? 153 TYR A CE1 1 
ATOM   1185 C  CE2 . TYR A 1 153 ? -31.528 -6.669  -20.775 1.00 45.06  ? 153 TYR A CE2 1 
ATOM   1186 C  CZ  . TYR A 1 153 ? -32.347 -6.248  -19.744 1.00 48.68  ? 153 TYR A CZ  1 
ATOM   1187 O  OH  . TYR A 1 153 ? -33.527 -5.595  -20.021 1.00 46.49  ? 153 TYR A OH  1 
ATOM   1188 N  N   . GLY A 1 154 ? -27.053 -10.706 -19.971 1.00 45.56  ? 154 GLY A N   1 
ATOM   1189 C  CA  . GLY A 1 154 ? -25.713 -11.207 -20.235 1.00 40.35  ? 154 GLY A CA  1 
ATOM   1190 C  C   . GLY A 1 154 ? -25.057 -10.406 -21.343 1.00 40.38  ? 154 GLY A C   1 
ATOM   1191 O  O   . GLY A 1 154 ? -25.694 -10.066 -22.335 1.00 46.10  ? 154 GLY A O   1 
ATOM   1192 N  N   . LEU A 1 155 ? -23.776 -10.102 -21.148 1.00 36.06  ? 155 LEU A N   1 
ATOM   1193 C  CA  . LEU A 1 155 ? -23.007 -9.292  -22.084 1.00 37.30  ? 155 LEU A CA  1 
ATOM   1194 C  C   . LEU A 1 155 ? -21.612 -9.881  -22.209 1.00 44.18  ? 155 LEU A C   1 
ATOM   1195 O  O   . LEU A 1 155 ? -20.960 -10.200 -21.216 1.00 36.65  ? 155 LEU A O   1 
ATOM   1196 C  CB  . LEU A 1 155 ? -22.922 -7.830  -21.628 1.00 37.77  ? 155 LEU A CB  1 
ATOM   1197 C  CG  . LEU A 1 155 ? -21.938 -6.921  -22.361 1.00 40.00  ? 155 LEU A CG  1 
ATOM   1198 C  CD1 . LEU A 1 155 ? -22.298 -6.769  -23.832 1.00 43.20  ? 155 LEU A CD1 1 
ATOM   1199 C  CD2 . LEU A 1 155 ? -21.889 -5.554  -21.697 1.00 36.81  ? 155 LEU A CD2 1 
ATOM   1200 N  N   . SER A 1 156 ? -21.138 -9.983  -23.448 1.00 32.97  ? 156 SER A N   1 
ATOM   1201 C  CA  . SER A 1 156 ? -19.861 -10.607 -23.758 1.00 34.70  ? 156 SER A CA  1 
ATOM   1202 C  C   . SER A 1 156 ? -19.217 -9.711  -24.808 1.00 38.91  ? 156 SER A C   1 
ATOM   1203 O  O   . SER A 1 156 ? -19.469 -8.500  -24.839 1.00 36.59  ? 156 SER A O   1 
ATOM   1204 C  CB  . SER A 1 156 ? -20.053 -12.067 -24.186 1.00 41.50  ? 156 SER A CB  1 
ATOM   1205 O  OG  . SER A 1 156 ? -18.808 -12.754 -24.204 1.00 39.03  ? 156 SER A OG  1 
ATOM   1206 N  N   . ASN A 1 157 ? -18.322 -10.277 -25.621 1.00 41.45  ? 157 ASN A N   1 
ATOM   1207 C  CA  . ASN A 1 157 ? -17.609 -9.516  -26.643 1.00 43.55  ? 157 ASN A CA  1 
ATOM   1208 C  C   . ASN A 1 157 ? -18.381 -9.388  -27.964 1.00 49.39  ? 157 ASN A C   1 
ATOM   1209 O  O   . ASN A 1 157 ? -17.822 -8.905  -28.963 1.00 45.70  ? 157 ASN A O   1 
ATOM   1210 C  CB  . ASN A 1 157 ? -16.240 -10.161 -26.859 1.00 41.99  ? 157 ASN A CB  1 
ATOM   1211 C  CG  . ASN A 1 157 ? -15.465 -10.303 -25.561 1.00 43.22  ? 157 ASN A CG  1 
ATOM   1212 O  OD1 . ASN A 1 157 ? -15.205 -11.409 -25.092 1.00 45.61  ? 157 ASN A OD1 1 
ATOM   1213 N  ND2 . ASN A 1 157 ? -15.121 -9.176  -24.961 1.00 41.21  ? 157 ASN A ND2 1 
ATOM   1214 N  N   . ALA A 1 158 ? -19.628 -9.835  -27.999 1.00 46.60  ? 158 ALA A N   1 
ATOM   1215 C  CA  . ALA A 1 158 ? -20.612 -9.433  -28.997 1.00 38.32  ? 158 ALA A CA  1 
ATOM   1216 C  C   . ALA A 1 158 ? -21.387 -8.233  -28.438 1.00 39.57  ? 158 ALA A C   1 
ATOM   1217 O  O   . ALA A 1 158 ? -20.869 -7.476  -27.613 1.00 57.77  ? 158 ALA A O   1 
ATOM   1218 C  CB  . ALA A 1 158 ? -21.516 -10.612 -29.361 1.00 34.92  ? 158 ALA A CB  1 
ATOM   1219 N  N   . LEU A 1 159 ? -22.600 -8.001  -28.918 1.00 36.63  ? 159 LEU A N   1 
ATOM   1220 C  CA  . LEU A 1 159 ? -23.472 -7.005  -28.310 1.00 43.53  ? 159 LEU A CA  1 
ATOM   1221 C  C   . LEU A 1 159 ? -24.193 -7.587  -27.088 1.00 44.24  ? 159 LEU A C   1 
ATOM   1222 O  O   . LEU A 1 159 ? -24.030 -8.755  -26.721 1.00 37.27  ? 159 LEU A O   1 
ATOM   1223 C  CB  . LEU A 1 159 ? -24.496 -6.491  -29.324 1.00 39.33  ? 159 LEU A CB  1 
ATOM   1224 C  CG  . LEU A 1 159 ? -23.910 -6.055  -30.673 1.00 41.50  ? 159 LEU A CG  1 
ATOM   1225 C  CD1 . LEU A 1 159 ? -25.036 -5.569  -31.585 1.00 46.81  ? 159 LEU A CD1 1 
ATOM   1226 C  CD2 . LEU A 1 159 ? -22.849 -4.986  -30.460 1.00 34.71  ? 159 LEU A CD2 1 
ATOM   1227 N  N   . LEU A 1 160 ? -25.008 -6.751  -26.448 1.00 39.65  ? 160 LEU A N   1 
ATOM   1228 C  CA  . LEU A 1 160 ? -25.812 -7.202  -25.325 1.00 45.88  ? 160 LEU A CA  1 
ATOM   1229 C  C   . LEU A 1 160 ? -26.772 -8.295  -25.768 1.00 38.12  ? 160 LEU A C   1 
ATOM   1230 O  O   . LEU A 1 160 ? -27.497 -8.139  -26.745 1.00 40.23  ? 160 LEU A O   1 
ATOM   1231 C  CB  . LEU A 1 160 ? -26.588 -6.023  -24.731 1.00 44.23  ? 160 LEU A CB  1 
ATOM   1232 C  CG  . LEU A 1 160 ? -27.468 -6.317  -23.513 1.00 44.55  ? 160 LEU A CG  1 
ATOM   1233 C  CD1 . LEU A 1 160 ? -26.605 -6.585  -22.286 1.00 45.03  ? 160 LEU A CD1 1 
ATOM   1234 C  CD2 . LEU A 1 160 ? -28.431 -5.166  -23.252 1.00 47.31  ? 160 LEU A CD2 1 
ATOM   1235 N  N   . GLU A 1 161 ? -26.800 -9.400  -25.024 1.00 43.50  ? 161 GLU A N   1 
ATOM   1236 C  CA  . GLU A 1 161 ? -27.707 -10.517 -25.242 1.00 40.72  ? 161 GLU A CA  1 
ATOM   1237 C  C   . GLU A 1 161 ? -27.470 -11.234 -26.565 1.00 42.23  ? 161 GLU A C   1 
ATOM   1238 O  O   . GLU A 1 161 ? -28.335 -12.014 -27.002 1.00 43.68  ? 161 GLU A O   1 
ATOM   1239 C  CB  . GLU A 1 161 ? -29.169 -10.057 -25.168 1.00 45.97  ? 161 GLU A CB  1 
ATOM   1240 C  CG  . GLU A 1 161 ? -29.622 -9.714  -23.756 1.00 46.66  ? 161 GLU A CG  1 
ATOM   1241 C  CD  . GLU A 1 161 ? -29.758 -10.943 -22.892 1.00 42.36  ? 161 GLU A CD  1 
ATOM   1242 O  OE1 . GLU A 1 161 ? -30.238 -11.974 -23.390 1.00 37.92  ? 161 GLU A OE1 1 
ATOM   1243 O  OE2 . GLU A 1 161 ? -29.381 -10.883 -21.707 1.00 51.54  ? 161 GLU A OE2 1 
ATOM   1244 N  N   . THR A 1 162 ? -26.338 -11.012 -27.215 1.00 42.22  ? 162 THR A N   1 
ATOM   1245 C  CA  . THR A 1 162 ? -26.007 -11.803 -28.391 1.00 39.38  ? 162 THR A CA  1 
ATOM   1246 C  C   . THR A 1 162 ? -25.913 -13.268 -27.971 1.00 43.47  ? 162 THR A C   1 
ATOM   1247 O  O   . THR A 1 162 ? -25.186 -13.584 -27.020 1.00 46.71  ? 162 THR A O   1 
ATOM   1248 C  CB  . THR A 1 162 ? -24.690 -11.345 -29.007 1.00 36.88  ? 162 THR A CB  1 
ATOM   1249 O  OG1 . THR A 1 162 ? -24.704 -9.923  -29.153 1.00 38.62  ? 162 THR A OG1 1 
ATOM   1250 C  CG2 . THR A 1 162 ? -24.482 -12.009 -30.390 1.00 38.07  ? 162 THR A CG2 1 
ATOM   1251 N  N   . PRO A 1 163 ? -26.628 -14.183 -28.634 1.00 42.03  ? 163 PRO A N   1 
ATOM   1252 C  CA  . PRO A 1 163 ? -26.738 -15.566 -28.138 1.00 41.50  ? 163 PRO A CA  1 
ATOM   1253 C  C   . PRO A 1 163 ? -25.527 -16.452 -28.435 1.00 42.22  ? 163 PRO A C   1 
ATOM   1254 O  O   . PRO A 1 163 ? -25.652 -17.548 -28.986 1.00 41.56  ? 163 PRO A O   1 
ATOM   1255 C  CB  . PRO A 1 163 ? -27.999 -16.075 -28.846 1.00 48.05  ? 163 PRO A CB  1 
ATOM   1256 C  CG  . PRO A 1 163 ? -28.009 -15.326 -30.154 1.00 49.07  ? 163 PRO A CG  1 
ATOM   1257 C  CD  . PRO A 1 163 ? -27.439 -13.959 -29.850 1.00 51.71  ? 163 PRO A CD  1 
ATOM   1258 N  N   . TRP A 1 164 ? -24.344 -15.979 -28.049 1.00 40.86  ? 164 TRP A N   1 
ATOM   1259 C  CA  . TRP A 1 164 ? -23.194 -16.872 -27.966 1.00 42.73  ? 164 TRP A CA  1 
ATOM   1260 C  C   . TRP A 1 164 ? -23.524 -18.015 -27.007 1.00 46.21  ? 164 TRP A C   1 
ATOM   1261 O  O   . TRP A 1 164 ? -24.218 -17.820 -26.003 1.00 44.16  ? 164 TRP A O   1 
ATOM   1262 C  CB  . TRP A 1 164 ? -21.960 -16.117 -27.478 1.00 44.15  ? 164 TRP A CB  1 
ATOM   1263 C  CG  . TRP A 1 164 ? -21.330 -15.229 -28.508 1.00 47.86  ? 164 TRP A CG  1 
ATOM   1264 C  CD1 . TRP A 1 164 ? -21.815 -14.934 -29.757 1.00 44.79  ? 164 TRP A CD1 1 
ATOM   1265 C  CD2 . TRP A 1 164 ? -20.089 -14.523 -28.383 1.00 49.00  ? 164 TRP A CD2 1 
ATOM   1266 N  NE1 . TRP A 1 164 ? -20.955 -14.082 -30.406 1.00 43.32  ? 164 TRP A NE1 1 
ATOM   1267 C  CE2 . TRP A 1 164 ? -19.885 -13.820 -29.589 1.00 44.35  ? 164 TRP A CE2 1 
ATOM   1268 C  CE3 . TRP A 1 164 ? -19.132 -14.413 -27.365 1.00 43.28  ? 164 TRP A CE3 1 
ATOM   1269 C  CZ2 . TRP A 1 164 ? -18.762 -13.019 -29.805 1.00 46.73  ? 164 TRP A CZ2 1 
ATOM   1270 C  CZ3 . TRP A 1 164 ? -18.016 -13.626 -27.587 1.00 46.59  ? 164 TRP A CZ3 1 
ATOM   1271 C  CH2 . TRP A 1 164 ? -17.840 -12.936 -28.796 1.00 45.33  ? 164 TRP A CH2 1 
ATOM   1272 N  N   . ARG A 1 165 ? -23.036 -19.214 -27.325 1.00 40.10  ? 165 ARG A N   1 
ATOM   1273 C  CA  . ARG A 1 165 ? -23.326 -20.370 -26.491 1.00 43.29  ? 165 ARG A CA  1 
ATOM   1274 C  C   . ARG A 1 165 ? -22.679 -20.247 -25.121 1.00 43.90  ? 165 ARG A C   1 
ATOM   1275 O  O   . ARG A 1 165 ? -23.242 -20.729 -24.136 1.00 41.44  ? 165 ARG A O   1 
ATOM   1276 C  CB  . ARG A 1 165 ? -22.861 -21.653 -27.172 1.00 46.28  ? 165 ARG A CB  1 
ATOM   1277 C  CG  . ARG A 1 165 ? -23.691 -22.019 -28.373 1.00 59.87  ? 165 ARG A CG  1 
ATOM   1278 C  CD  . ARG A 1 165 ? -23.355 -23.412 -28.874 1.00 62.28  ? 165 ARG A CD  1 
ATOM   1279 N  NE  . ARG A 1 165 ? -23.686 -24.441 -27.896 1.00 62.08  ? 165 ARG A NE  1 
ATOM   1280 C  CZ  . ARG A 1 165 ? -23.692 -25.742 -28.157 1.00 61.61  ? 165 ARG A CZ  1 
ATOM   1281 N  NH1 . ARG A 1 165 ? -23.381 -26.207 -29.356 1.00 57.82  ? 165 ARG A NH1 1 
ATOM   1282 N  NH2 . ARG A 1 165 ? -24.016 -26.597 -27.190 1.00 57.27  ? 165 ARG A NH2 1 
ATOM   1283 N  N   . LYS A 1 166 ? -21.497 -19.632 -25.041 1.00 47.44  ? 166 LYS A N   1 
ATOM   1284 C  CA  . LYS A 1 166 ? -20.895 -19.377 -23.737 1.00 45.58  ? 166 LYS A CA  1 
ATOM   1285 C  C   . LYS A 1 166 ? -21.747 -18.413 -22.928 1.00 48.79  ? 166 LYS A C   1 
ATOM   1286 O  O   . LYS A 1 166 ? -21.813 -18.518 -21.698 1.00 45.37  ? 166 LYS A O   1 
ATOM   1287 C  CB  . LYS A 1 166 ? -19.479 -18.814 -23.892 1.00 42.65  ? 166 LYS A CB  1 
ATOM   1288 C  CG  . LYS A 1 166 ? -19.425 -17.412 -24.495 1.00 45.89  ? 166 LYS A CG  1 
ATOM   1289 C  CD  . LYS A 1 166 ? -17.996 -16.886 -24.559 1.00 43.20  ? 166 LYS A CD  1 
ATOM   1290 C  CE  . LYS A 1 166 ? -17.492 -16.469 -23.199 1.00 41.08  ? 166 LYS A CE  1 
ATOM   1291 N  NZ  . LYS A 1 166 ? -16.046 -16.100 -23.253 1.00 49.06  ? 166 LYS A NZ  1 
ATOM   1292 N  N   . LEU A 1 167 ? -22.392 -17.454 -23.596 1.00 47.02  ? 167 LEU A N   1 
ATOM   1293 C  CA  . LEU A 1 167 ? -23.220 -16.497 -22.866 1.00 44.77  ? 167 LEU A CA  1 
ATOM   1294 C  C   . LEU A 1 167 ? -24.505 -17.153 -22.381 1.00 44.45  ? 167 LEU A C   1 
ATOM   1295 O  O   . LEU A 1 167 ? -24.911 -16.965 -21.228 1.00 47.72  ? 167 LEU A O   1 
ATOM   1296 C  CB  . LEU A 1 167 ? -23.524 -15.287 -23.746 1.00 39.54  ? 167 LEU A CB  1 
ATOM   1297 C  CG  . LEU A 1 167 ? -24.394 -14.214 -23.102 1.00 36.64  ? 167 LEU A CG  1 
ATOM   1298 C  CD1 . LEU A 1 167 ? -23.869 -13.918 -21.708 1.00 48.54  ? 167 LEU A CD1 1 
ATOM   1299 C  CD2 . LEU A 1 167 ? -24.430 -12.935 -23.910 1.00 40.01  ? 167 LEU A CD2 1 
ATOM   1300 N  N   . CYS A 1 168 ? -25.151 -17.933 -23.246 1.00 43.10  ? 168 CYS A N   1 
ATOM   1301 C  CA  . CYS A 1 168 ? -26.365 -18.639 -22.851 1.00 50.14  ? 168 CYS A CA  1 
ATOM   1302 C  C   . CYS A 1 168 ? -26.088 -19.606 -21.704 1.00 54.50  ? 168 CYS A C   1 
ATOM   1303 O  O   . CYS A 1 168 ? -26.816 -19.635 -20.702 1.00 51.26  ? 168 CYS A O   1 
ATOM   1304 C  CB  . CYS A 1 168 ? -26.935 -19.378 -24.060 1.00 56.65  ? 168 CYS A CB  1 
ATOM   1305 S  SG  . CYS A 1 168 ? -27.766 -18.301 -25.259 1.00 64.82  ? 168 CYS A SG  1 
ATOM   1306 N  N   . PHE A 1 169 ? -25.020 -20.394 -21.831 1.00 43.72  ? 169 PHE A N   1 
ATOM   1307 C  CA  . PHE A 1 169 ? -24.703 -21.415 -20.842 1.00 46.54  ? 169 PHE A CA  1 
ATOM   1308 C  C   . PHE A 1 169 ? -24.307 -20.794 -19.508 1.00 56.54  ? 169 PHE A C   1 
ATOM   1309 O  O   . PHE A 1 169 ? -24.742 -21.261 -18.444 1.00 45.76  ? 169 PHE A O   1 
ATOM   1310 C  CB  . PHE A 1 169 ? -23.591 -22.302 -21.405 1.00 44.15  ? 169 PHE A CB  1 
ATOM   1311 C  CG  . PHE A 1 169 ? -23.020 -23.270 -20.419 1.00 48.49  ? 169 PHE A CG  1 
ATOM   1312 C  CD1 . PHE A 1 169 ? -23.629 -24.498 -20.201 1.00 44.76  ? 169 PHE A CD1 1 
ATOM   1313 C  CD2 . PHE A 1 169 ? -21.856 -22.965 -19.731 1.00 44.38  ? 169 PHE A CD2 1 
ATOM   1314 C  CE1 . PHE A 1 169 ? -23.094 -25.395 -19.296 1.00 51.17  ? 169 PHE A CE1 1 
ATOM   1315 C  CE2 . PHE A 1 169 ? -21.315 -23.859 -18.828 1.00 48.52  ? 169 PHE A CE2 1 
ATOM   1316 C  CZ  . PHE A 1 169 ? -21.935 -25.075 -18.606 1.00 49.07  ? 169 PHE A CZ  1 
ATOM   1317 N  N   . GLY A 1 170 ? -23.485 -19.740 -19.543 1.00 47.80  ? 170 GLY A N   1 
ATOM   1318 C  CA  . GLY A 1 170 ? -23.091 -19.086 -18.310 1.00 48.68  ? 170 GLY A CA  1 
ATOM   1319 C  C   . GLY A 1 170 ? -24.251 -18.394 -17.622 1.00 51.96  ? 170 GLY A C   1 
ATOM   1320 O  O   . GLY A 1 170 ? -24.335 -18.371 -16.389 1.00 48.33  ? 170 GLY A O   1 
ATOM   1321 N  N   . LYS A 1 171 ? -25.155 -17.811 -18.407 1.00 47.67  ? 171 LYS A N   1 
ATOM   1322 C  CA  . LYS A 1 171 ? -26.347 -17.192 -17.839 1.00 48.81  ? 171 LYS A CA  1 
ATOM   1323 C  C   . LYS A 1 171 ? -27.221 -18.229 -17.140 1.00 53.79  ? 171 LYS A C   1 
ATOM   1324 O  O   . LYS A 1 171 ? -27.859 -17.939 -16.123 1.00 50.27  ? 171 LYS A O   1 
ATOM   1325 C  CB  . LYS A 1 171 ? -27.121 -16.476 -18.941 1.00 52.62  ? 171 LYS A CB  1 
ATOM   1326 C  CG  . LYS A 1 171 ? -28.307 -15.665 -18.473 1.00 57.09  ? 171 LYS A CG  1 
ATOM   1327 C  CD  . LYS A 1 171 ? -28.690 -14.659 -19.553 1.00 57.27  ? 171 LYS A CD  1 
ATOM   1328 C  CE  . LYS A 1 171 ? -30.089 -14.121 -19.344 1.00 56.66  ? 171 LYS A CE  1 
ATOM   1329 N  NZ  . LYS A 1 171 ? -30.419 -13.123 -20.387 1.00 51.98  ? 171 LYS A NZ  1 
ATOM   1330 N  N   . GLN A 1 172 ? -27.276 -19.447 -17.683 1.00 53.65  ? 172 GLN A N   1 
ATOM   1331 C  CA  . GLN A 1 172 ? -28.001 -20.520 -17.007 1.00 59.51  ? 172 GLN A CA  1 
ATOM   1332 C  C   . GLN A 1 172 ? -27.377 -20.828 -15.647 1.00 58.06  ? 172 GLN A C   1 
ATOM   1333 O  O   . GLN A 1 172 ? -28.090 -20.988 -14.650 1.00 52.34  ? 172 GLN A O   1 
ATOM   1334 C  CB  . GLN A 1 172 ? -28.018 -21.765 -17.894 1.00 56.59  ? 172 GLN A CB  1 
ATOM   1335 C  CG  . GLN A 1 172 ? -28.798 -22.932 -17.330 1.00 74.83  ? 172 GLN A CG  1 
ATOM   1336 C  CD  . GLN A 1 172 ? -28.208 -24.275 -17.742 1.00 93.32  ? 172 GLN A CD  1 
ATOM   1337 O  OE1 . GLN A 1 172 ? -28.294 -24.680 -18.904 1.00 92.98  ? 172 GLN A OE1 1 
ATOM   1338 N  NE2 . GLN A 1 172 ? -27.590 -24.967 -16.784 1.00 89.48  ? 172 GLN A NE2 1 
ATOM   1339 N  N   . LEU A 1 173 ? -26.045 -20.907 -15.585 1.00 60.07  ? 173 LEU A N   1 
ATOM   1340 C  CA  . LEU A 1 173 ? -25.375 -21.152 -14.310 1.00 54.51  ? 173 LEU A CA  1 
ATOM   1341 C  C   . LEU A 1 173 ? -25.589 -19.991 -13.345 1.00 50.65  ? 173 LEU A C   1 
ATOM   1342 O  O   . LEU A 1 173 ? -25.755 -20.201 -12.136 1.00 57.37  ? 173 LEU A O   1 
ATOM   1343 C  CB  . LEU A 1 173 ? -23.880 -21.379 -14.534 1.00 48.03  ? 173 LEU A CB  1 
ATOM   1344 C  CG  . LEU A 1 173 ? -23.483 -22.516 -15.482 1.00 52.37  ? 173 LEU A CG  1 
ATOM   1345 C  CD1 . LEU A 1 173 ? -21.968 -22.572 -15.624 1.00 45.86  ? 173 LEU A CD1 1 
ATOM   1346 C  CD2 . LEU A 1 173 ? -24.029 -23.857 -15.006 1.00 51.21  ? 173 LEU A CD2 1 
ATOM   1347 N  N   . PHE A 1 174 ? -25.563 -18.764 -13.861 1.00 49.42  ? 174 PHE A N   1 
ATOM   1348 C  CA  . PHE A 1 174 ? -25.745 -17.588 -13.018 1.00 46.65  ? 174 PHE A CA  1 
ATOM   1349 C  C   . PHE A 1 174 ? -27.121 -17.591 -12.369 1.00 51.04  ? 174 PHE A C   1 
ATOM   1350 O  O   . PHE A 1 174 ? -27.253 -17.345 -11.165 1.00 52.31  ? 174 PHE A O   1 
ATOM   1351 C  CB  . PHE A 1 174 ? -25.536 -16.327 -13.858 1.00 46.15  ? 174 PHE A CB  1 
ATOM   1352 C  CG  . PHE A 1 174 ? -25.808 -15.050 -13.127 1.00 48.03  ? 174 PHE A CG  1 
ATOM   1353 C  CD1 . PHE A 1 174 ? -24.810 -14.431 -12.393 1.00 45.68  ? 174 PHE A CD1 1 
ATOM   1354 C  CD2 . PHE A 1 174 ? -27.063 -14.460 -13.182 1.00 45.42  ? 174 PHE A CD2 1 
ATOM   1355 C  CE1 . PHE A 1 174 ? -25.055 -13.250 -11.720 1.00 42.67  ? 174 PHE A CE1 1 
ATOM   1356 C  CE2 . PHE A 1 174 ? -27.315 -13.276 -12.510 1.00 49.42  ? 174 PHE A CE2 1 
ATOM   1357 C  CZ  . PHE A 1 174 ? -26.306 -12.669 -11.777 1.00 46.33  ? 174 PHE A CZ  1 
ATOM   1358 N  N   . LEU A 1 175 ? -28.162 -17.883 -13.152 1.00 49.78  ? 175 LEU A N   1 
ATOM   1359 C  CA  . LEU A 1 175 ? -29.508 -17.941 -12.593 1.00 55.64  ? 175 LEU A CA  1 
ATOM   1360 C  C   . LEU A 1 175 ? -29.642 -19.080 -11.589 1.00 51.89  ? 175 LEU A C   1 
ATOM   1361 O  O   . LEU A 1 175 ? -30.306 -18.927 -10.560 1.00 54.04  ? 175 LEU A O   1 
ATOM   1362 C  CB  . LEU A 1 175 ? -30.536 -18.087 -13.713 1.00 50.80  ? 175 LEU A CB  1 
ATOM   1363 C  CG  . LEU A 1 175 ? -30.791 -16.826 -14.540 1.00 60.28  ? 175 LEU A CG  1 
ATOM   1364 C  CD1 . LEU A 1 175 ? -31.546 -17.163 -15.825 1.00 61.40  ? 175 LEU A CD1 1 
ATOM   1365 C  CD2 . LEU A 1 175 ? -31.555 -15.799 -13.728 1.00 53.44  ? 175 LEU A CD2 1 
ATOM   1366 N  N   . GLU A 1 176 ? -29.030 -20.232 -11.877 1.00 57.38  ? 176 GLU A N   1 
ATOM   1367 C  CA  . GLU A 1 176 ? -29.103 -21.363 -10.958 1.00 62.22  ? 176 GLU A CA  1 
ATOM   1368 C  C   . GLU A 1 176 ? -28.442 -21.029 -9.628  1.00 58.63  ? 176 GLU A C   1 
ATOM   1369 O  O   . GLU A 1 176 ? -28.945 -21.407 -8.566  1.00 62.24  ? 176 GLU A O   1 
ATOM   1370 C  CB  . GLU A 1 176 ? -28.454 -22.599 -11.587 1.00 56.75  ? 176 GLU A CB  1 
ATOM   1371 C  CG  . GLU A 1 176 ? -29.268 -23.224 -12.714 1.00 69.21  ? 176 GLU A CG  1 
ATOM   1372 C  CD  . GLU A 1 176 ? -28.553 -24.387 -13.392 1.00 80.76  ? 176 GLU A CD  1 
ATOM   1373 O  OE1 . GLU A 1 176 ? -27.394 -24.681 -13.017 1.00 77.13  ? 176 GLU A OE1 1 
ATOM   1374 O  OE2 . GLU A 1 176 ? -29.154 -25.010 -14.299 1.00 78.25  ? 176 GLU A OE2 1 
ATOM   1375 N  N   . ALA A 1 177 ? -27.309 -20.324 -9.670  1.00 59.28  ? 177 ALA A N   1 
ATOM   1376 C  CA  . ALA A 1 177 ? -26.624 -19.940 -8.441  1.00 58.54  ? 177 ALA A CA  1 
ATOM   1377 C  C   . ALA A 1 177 ? -27.447 -18.943 -7.639  1.00 59.59  ? 177 ALA A C   1 
ATOM   1378 O  O   . ALA A 1 177 ? -27.511 -19.033 -6.409  1.00 57.10  ? 177 ALA A O   1 
ATOM   1379 C  CB  . ALA A 1 177 ? -25.247 -19.359 -8.772  1.00 51.99  ? 177 ALA A CB  1 
ATOM   1380 N  N   . VAL A 1 178 ? -28.080 -17.984 -8.315  1.00 55.45  ? 178 VAL A N   1 
ATOM   1381 C  CA  . VAL A 1 178 ? -28.886 -16.988 -7.618  1.00 59.39  ? 178 VAL A CA  1 
ATOM   1382 C  C   . VAL A 1 178 ? -30.109 -17.642 -6.983  1.00 64.67  ? 178 VAL A C   1 
ATOM   1383 O  O   . VAL A 1 178 ? -30.398 -17.432 -5.801  1.00 70.19  ? 178 VAL A O   1 
ATOM   1384 C  CB  . VAL A 1 178 ? -29.284 -15.855 -8.581  1.00 59.47  ? 178 VAL A CB  1 
ATOM   1385 C  CG1 . VAL A 1 178 ? -30.356 -14.966 -7.974  1.00 61.14  ? 178 VAL A CG1 1 
ATOM   1386 C  CG2 . VAL A 1 178 ? -28.061 -15.028 -8.955  1.00 61.85  ? 178 VAL A CG2 1 
ATOM   1387 N  N   . GLU A 1 179 ? -30.843 -18.450 -7.754  1.00 63.09  ? 179 GLU A N   1 
ATOM   1388 C  CA  . GLU A 1 179 ? -32.001 -19.137 -7.192  1.00 65.43  ? 179 GLU A CA  1 
ATOM   1389 C  C   . GLU A 1 179 ? -31.589 -20.110 -6.096  1.00 66.81  ? 179 GLU A C   1 
ATOM   1390 O  O   . GLU A 1 179 ? -32.356 -20.355 -5.158  1.00 69.83  ? 179 GLU A O   1 
ATOM   1391 C  CB  . GLU A 1 179 ? -32.763 -19.874 -8.294  1.00 54.90  ? 179 GLU A CB  1 
ATOM   1392 N  N   . ARG A 1 180 ? -30.387 -20.671 -6.192  1.00 68.70  ? 180 ARG A N   1 
ATOM   1393 C  CA  . ARG A 1 180 ? -29.958 -21.693 -5.246  1.00 69.81  ? 180 ARG A CA  1 
ATOM   1394 C  C   . ARG A 1 180 ? -29.591 -21.099 -3.891  1.00 75.39  ? 180 ARG A C   1 
ATOM   1395 O  O   . ARG A 1 180 ? -29.837 -21.727 -2.856  1.00 85.39  ? 180 ARG A O   1 
ATOM   1396 C  CB  . ARG A 1 180 ? -28.771 -22.468 -5.837  1.00 78.18  ? 180 ARG A CB  1 
ATOM   1397 C  CG  . ARG A 1 180 ? -28.000 -23.329 -4.842  1.00 83.62  ? 180 ARG A CG  1 
ATOM   1398 C  CD  . ARG A 1 180 ? -26.948 -24.216 -5.539  1.00 85.26  ? 180 ARG A CD  1 
ATOM   1399 N  NE  . ARG A 1 180 ? -25.880 -23.458 -6.183  1.00 86.02  ? 180 ARG A NE  1 
ATOM   1400 C  CZ  . ARG A 1 180 ? -25.653 -23.423 -7.495  1.00 91.26  ? 180 ARG A CZ  1 
ATOM   1401 N  NH1 . ARG A 1 180 ? -26.400 -24.107 -8.350  1.00 86.15  ? 180 ARG A NH1 1 
ATOM   1402 N  NH2 . ARG A 1 180 ? -24.644 -22.691 -7.961  1.00 81.45  ? 180 ARG A NH2 1 
ATOM   1403 N  N   . SER A 1 181 ? -29.013 -19.892 -3.869  1.00 85.87  ? 181 SER A N   1 
ATOM   1404 C  CA  . SER A 1 181 ? -28.402 -19.393 -2.648  1.00 90.25  ? 181 SER A CA  1 
ATOM   1405 C  C   . SER A 1 181 ? -28.621 -17.917 -2.353  1.00 90.98  ? 181 SER A C   1 
ATOM   1406 O  O   . SER A 1 181 ? -28.049 -17.419 -1.375  1.00 91.54  ? 181 SER A O   1 
ATOM   1407 C  CB  . SER A 1 181 ? -26.883 -19.657 -2.686  1.00 82.76  ? 181 SER A CB  1 
ATOM   1408 O  OG  . SER A 1 181 ? -26.244 -18.740 -3.545  1.00 76.05  ? 181 SER A OG  1 
ATOM   1409 N  N   . GLN A 1 182 ? -29.424 -17.199 -3.140  1.00 85.77  ? 182 GLN A N   1 
ATOM   1410 C  CA  . GLN A 1 182 ? -29.580 -15.771 -2.884  1.00 86.75  ? 182 GLN A CA  1 
ATOM   1411 C  C   . GLN A 1 182 ? -30.273 -15.490 -1.554  1.00 87.91  ? 182 GLN A C   1 
ATOM   1412 O  O   . GLN A 1 182 ? -30.090 -14.402 -0.997  1.00 83.61  ? 182 GLN A O   1 
ATOM   1413 C  CB  . GLN A 1 182 ? -30.352 -15.096 -4.023  1.00 81.89  ? 182 GLN A CB  1 
ATOM   1414 C  CG  . GLN A 1 182 ? -31.828 -15.442 -4.103  1.00 82.21  ? 182 GLN A CG  1 
ATOM   1415 C  CD  . GLN A 1 182 ? -32.574 -14.525 -5.055  1.00 88.52  ? 182 GLN A CD  1 
ATOM   1416 O  OE1 . GLN A 1 182 ? -32.278 -13.331 -5.139  1.00 83.57  ? 182 GLN A OE1 1 
ATOM   1417 N  NE2 . GLN A 1 182 ? -33.537 -15.079 -5.787  1.00 90.55  ? 182 GLN A NE2 1 
ATOM   1418 N  N   . ALA A 1 183 ? -31.067 -16.435 -1.042  1.00 83.47  ? 183 ALA A N   1 
ATOM   1419 C  CA  . ALA A 1 183 ? -31.736 -16.274 0.245   1.00 75.05  ? 183 ALA A CA  1 
ATOM   1420 C  C   . ALA A 1 183 ? -30.877 -16.715 1.424   1.00 77.00  ? 183 ALA A C   1 
ATOM   1421 O  O   . ALA A 1 183 ? -31.295 -16.544 2.574   1.00 80.86  ? 183 ALA A O   1 
ATOM   1422 C  CB  . ALA A 1 183 ? -33.047 -17.064 0.255   1.00 67.77  ? 183 ALA A CB  1 
ATOM   1423 N  N   . LEU A 1 184 ? -29.703 -17.283 1.166   1.00 82.05  ? 184 LEU A N   1 
ATOM   1424 C  CA  . LEU A 1 184 ? -28.738 -17.685 2.182   1.00 71.71  ? 184 LEU A CA  1 
ATOM   1425 C  C   . LEU A 1 184 ? -27.824 -16.498 2.463   1.00 65.55  ? 184 LEU A C   1 
ATOM   1426 O  O   . LEU A 1 184 ? -28.001 -15.437 1.853   1.00 69.13  ? 184 LEU A O   1 
ATOM   1427 C  CB  . LEU A 1 184 ? -27.959 -18.905 1.702   1.00 69.46  ? 184 LEU A CB  1 
ATOM   1428 C  CG  . LEU A 1 184 ? -28.826 -20.060 1.174   1.00 73.34  ? 184 LEU A CG  1 
ATOM   1429 C  CD1 . LEU A 1 184 ? -27.957 -21.158 0.577   1.00 70.18  ? 184 LEU A CD1 1 
ATOM   1430 C  CD2 . LEU A 1 184 ? -29.714 -20.613 2.282   1.00 65.92  ? 184 LEU A CD2 1 
ATOM   1431 N  N   . PRO A 1 185 ? -26.858 -16.609 3.377   1.00 55.57  ? 185 PRO A N   1 
ATOM   1432 C  CA  . PRO A 1 185 ? -25.994 -15.454 3.653   1.00 62.17  ? 185 PRO A CA  1 
ATOM   1433 C  C   . PRO A 1 185 ? -25.254 -15.030 2.396   1.00 53.73  ? 185 PRO A C   1 
ATOM   1434 O  O   . PRO A 1 185 ? -24.877 -15.856 1.567   1.00 57.61  ? 185 PRO A O   1 
ATOM   1435 C  CB  . PRO A 1 185 ? -25.028 -15.968 4.731   1.00 64.16  ? 185 PRO A CB  1 
ATOM   1436 C  CG  . PRO A 1 185 ? -25.712 -17.146 5.339   1.00 60.99  ? 185 PRO A CG  1 
ATOM   1437 C  CD  . PRO A 1 185 ? -26.503 -17.769 4.215   1.00 62.64  ? 185 PRO A CD  1 
ATOM   1438 N  N   . LYS A 1 186 ? -25.027 -13.723 2.265   1.00 45.34  ? 186 LYS A N   1 
ATOM   1439 C  CA  . LYS A 1 186 ? -24.479 -13.204 1.019   1.00 57.97  ? 186 LYS A CA  1 
ATOM   1440 C  C   . LYS A 1 186 ? -23.133 -13.832 0.680   1.00 59.62  ? 186 LYS A C   1 
ATOM   1441 O  O   . LYS A 1 186 ? -22.738 -13.835 -0.493  1.00 47.47  ? 186 LYS A O   1 
ATOM   1442 C  CB  . LYS A 1 186 ? -24.351 -11.682 1.091   1.00 50.84  ? 186 LYS A CB  1 
ATOM   1443 C  CG  . LYS A 1 186 ? -23.096 -11.181 1.762   1.00 53.35  ? 186 LYS A CG  1 
ATOM   1444 C  CD  . LYS A 1 186 ? -23.146 -9.664  1.923   1.00 59.89  ? 186 LYS A CD  1 
ATOM   1445 C  CE  . LYS A 1 186 ? -21.946 -9.140  2.705   1.00 64.93  ? 186 LYS A CE  1 
ATOM   1446 N  NZ  . LYS A 1 186 ? -22.123 -7.707  3.080   1.00 61.74  ? 186 LYS A NZ  1 
ATOM   1447 N  N   . ASP A 1 187 ? -22.431 -14.383 1.672   1.00 49.91  ? 187 ASP A N   1 
ATOM   1448 C  CA  . ASP A 1 187 ? -21.125 -14.977 1.399   1.00 56.39  ? 187 ASP A CA  1 
ATOM   1449 C  C   . ASP A 1 187 ? -21.242 -16.241 0.551   1.00 55.93  ? 187 ASP A C   1 
ATOM   1450 O  O   . ASP A 1 187 ? -20.389 -16.492 -0.312  1.00 49.62  ? 187 ASP A O   1 
ATOM   1451 C  CB  . ASP A 1 187 ? -20.406 -15.262 2.712   1.00 58.81  ? 187 ASP A CB  1 
ATOM   1452 C  CG  . ASP A 1 187 ? -19.903 -13.995 3.376   1.00 79.58  ? 187 ASP A CG  1 
ATOM   1453 O  OD1 . ASP A 1 187 ? -18.764 -13.588 3.080   1.00 85.91  ? 187 ASP A OD1 1 
ATOM   1454 O  OD2 . ASP A 1 187 ? -20.663 -13.392 4.168   1.00 71.72  ? 187 ASP A OD2 1 
ATOM   1455 N  N   . VAL A 1 188 ? -22.278 -17.053 0.780   1.00 48.31  ? 188 VAL A N   1 
ATOM   1456 C  CA  . VAL A 1 188 ? -22.425 -18.260 -0.026  1.00 54.21  ? 188 VAL A CA  1 
ATOM   1457 C  C   . VAL A 1 188 ? -22.870 -17.906 -1.441  1.00 54.60  ? 188 VAL A C   1 
ATOM   1458 O  O   . VAL A 1 188 ? -22.514 -18.600 -2.398  1.00 49.33  ? 188 VAL A O   1 
ATOM   1459 C  CB  . VAL A 1 188 ? -23.390 -19.259 0.638   1.00 66.90  ? 188 VAL A CB  1 
ATOM   1460 C  CG1 . VAL A 1 188 ? -24.824 -18.780 0.559   1.00 70.05  ? 188 VAL A CG1 1 
ATOM   1461 C  CG2 . VAL A 1 188 ? -23.266 -20.628 -0.024  1.00 59.70  ? 188 VAL A CG2 1 
ATOM   1462 N  N   . LEU A 1 189 ? -23.664 -16.844 -1.602  1.00 53.92  ? 189 LEU A N   1 
ATOM   1463 C  CA  . LEU A 1 189 ? -24.002 -16.388 -2.946  1.00 44.54  ? 189 LEU A CA  1 
ATOM   1464 C  C   . LEU A 1 189 ? -22.751 -15.966 -3.705  1.00 48.79  ? 189 LEU A C   1 
ATOM   1465 O  O   . LEU A 1 189 ? -22.600 -16.276 -4.895  1.00 46.09  ? 189 LEU A O   1 
ATOM   1466 C  CB  . LEU A 1 189 ? -24.999 -15.234 -2.879  1.00 44.62  ? 189 LEU A CB  1 
ATOM   1467 C  CG  . LEU A 1 189 ? -25.306 -14.525 -4.197  1.00 50.38  ? 189 LEU A CG  1 
ATOM   1468 C  CD1 . LEU A 1 189 ? -25.864 -15.506 -5.229  1.00 55.43  ? 189 LEU A CD1 1 
ATOM   1469 C  CD2 . LEU A 1 189 ? -26.271 -13.371 -3.977  1.00 48.63  ? 189 LEU A CD2 1 
ATOM   1470 N  N   . ILE A 1 190 ? -21.842 -15.256 -3.032  1.00 43.16  ? 190 ILE A N   1 
ATOM   1471 C  CA  . ILE A 1 190 ? -20.599 -14.830 -3.667  1.00 44.40  ? 190 ILE A CA  1 
ATOM   1472 C  C   . ILE A 1 190 ? -19.769 -16.036 -4.079  1.00 46.42  ? 190 ILE A C   1 
ATOM   1473 O  O   . ILE A 1 190 ? -19.199 -16.069 -5.174  1.00 41.47  ? 190 ILE A O   1 
ATOM   1474 C  CB  . ILE A 1 190 ? -19.815 -13.895 -2.727  1.00 46.45  ? 190 ILE A CB  1 
ATOM   1475 C  CG1 . ILE A 1 190 ? -20.457 -12.506 -2.731  1.00 48.92  ? 190 ILE A CG1 1 
ATOM   1476 C  CG2 . ILE A 1 190 ? -18.348 -13.812 -3.119  1.00 43.29  ? 190 ILE A CG2 1 
ATOM   1477 C  CD1 . ILE A 1 190 ? -19.977 -11.607 -1.601  1.00 53.19  ? 190 ILE A CD1 1 
ATOM   1478 N  N   . ALA A 1 191 ? -19.668 -17.037 -3.205  1.00 45.49  ? 191 ALA A N   1 
ATOM   1479 C  CA  . ALA A 1 191 ? -18.900 -18.230 -3.552  1.00 52.91  ? 191 ALA A CA  1 
ATOM   1480 C  C   . ALA A 1 191 ? -19.534 -18.981 -4.722  1.00 44.76  ? 191 ALA A C   1 
ATOM   1481 O  O   . ALA A 1 191 ? -18.826 -19.520 -5.578  1.00 48.67  ? 191 ALA A O   1 
ATOM   1482 C  CB  . ALA A 1 191 ? -18.772 -19.143 -2.336  1.00 48.49  ? 191 ALA A CB  1 
ATOM   1483 N  N   . SER A 1 192 ? -20.869 -19.038 -4.767  1.00 43.17  ? 192 SER A N   1 
ATOM   1484 C  CA  . SER A 1 192 ? -21.543 -19.716 -5.868  1.00 50.88  ? 192 SER A CA  1 
ATOM   1485 C  C   . SER A 1 192 ? -21.239 -19.033 -7.195  1.00 49.99  ? 192 SER A C   1 
ATOM   1486 O  O   . SER A 1 192 ? -21.057 -19.700 -8.218  1.00 55.39  ? 192 SER A O   1 
ATOM   1487 C  CB  . SER A 1 192 ? -23.055 -19.745 -5.629  1.00 45.00  ? 192 SER A CB  1 
ATOM   1488 O  OG  . SER A 1 192 ? -23.387 -20.567 -4.529  1.00 61.56  ? 192 SER A OG  1 
ATOM   1489 N  N   . LEU A 1 193 ? -21.198 -17.701 -7.194  1.00 44.18  ? 193 LEU A N   1 
ATOM   1490 C  CA  . LEU A 1 193 ? -20.976 -16.946 -8.419  1.00 49.70  ? 193 LEU A CA  1 
ATOM   1491 C  C   . LEU A 1 193 ? -19.521 -16.990 -8.867  1.00 50.17  ? 193 LEU A C   1 
ATOM   1492 O  O   . LEU A 1 193 ? -19.253 -16.984 -10.073 1.00 42.99  ? 193 LEU A O   1 
ATOM   1493 C  CB  . LEU A 1 193 ? -21.440 -15.507 -8.215  1.00 44.34  ? 193 LEU A CB  1 
ATOM   1494 C  CG  . LEU A 1 193 ? -22.954 -15.325 -8.074  1.00 48.36  ? 193 LEU A CG  1 
ATOM   1495 C  CD1 . LEU A 1 193 ? -23.289 -13.903 -7.649  1.00 42.28  ? 193 LEU A CD1 1 
ATOM   1496 C  CD2 . LEU A 1 193 ? -23.662 -15.683 -9.383  1.00 52.15  ? 193 LEU A CD2 1 
ATOM   1497 N  N   . LEU A 1 194 ? -18.576 -17.035 -7.926  1.00 43.41  ? 194 LEU A N   1 
ATOM   1498 C  CA  . LEU A 1 194 ? -17.183 -17.261 -8.297  1.00 43.12  ? 194 LEU A CA  1 
ATOM   1499 C  C   . LEU A 1 194 ? -17.010 -18.637 -8.927  1.00 48.92  ? 194 LEU A C   1 
ATOM   1500 O  O   . LEU A 1 194 ? -16.214 -18.810 -9.857  1.00 51.76  ? 194 LEU A O   1 
ATOM   1501 C  CB  . LEU A 1 194 ? -16.278 -17.124 -7.074  1.00 49.53  ? 194 LEU A CB  1 
ATOM   1502 C  CG  . LEU A 1 194 ? -16.193 -15.737 -6.433  1.00 49.62  ? 194 LEU A CG  1 
ATOM   1503 C  CD1 . LEU A 1 194 ? -15.484 -15.811 -5.088  1.00 51.34  ? 194 LEU A CD1 1 
ATOM   1504 C  CD2 . LEU A 1 194 ? -15.480 -14.769 -7.362  1.00 49.94  ? 194 LEU A CD2 1 
ATOM   1505 N  N   . ASP A 1 195 ? -17.742 -19.631 -8.424  1.00 45.75  ? 195 ASP A N   1 
ATOM   1506 C  CA  . ASP A 1 195 ? -17.708 -20.959 -9.030  1.00 51.92  ? 195 ASP A CA  1 
ATOM   1507 C  C   . ASP A 1 195 ? -18.231 -20.921 -10.461 1.00 51.05  ? 195 ASP A C   1 
ATOM   1508 O  O   . ASP A 1 195 ? -17.669 -21.575 -11.348 1.00 51.02  ? 195 ASP A O   1 
ATOM   1509 C  CB  . ASP A 1 195 ? -18.506 -21.933 -8.158  1.00 52.50  ? 195 ASP A CB  1 
ATOM   1510 C  CG  . ASP A 1 195 ? -18.978 -23.166 -8.914  1.00 64.14  ? 195 ASP A CG  1 
ATOM   1511 O  OD1 . ASP A 1 195 ? -20.212 -23.403 -8.951  1.00 67.96  ? 195 ASP A OD1 1 
ATOM   1512 O  OD2 . ASP A 1 195 ? -18.126 -23.893 -9.469  1.00 65.00  ? 195 ASP A OD2 1 
ATOM   1513 N  N   . VAL A 1 196 ? -19.300 -20.153 -10.705 1.00 44.72  ? 196 VAL A N   1 
ATOM   1514 C  CA  . VAL A 1 196 ? -19.799 -19.982 -12.065 1.00 48.66  ? 196 VAL A CA  1 
ATOM   1515 C  C   . VAL A 1 196 ? -18.756 -19.297 -12.933 1.00 49.96  ? 196 VAL A C   1 
ATOM   1516 O  O   . VAL A 1 196 ? -18.515 -19.697 -14.083 1.00 45.22  ? 196 VAL A O   1 
ATOM   1517 C  CB  . VAL A 1 196 ? -21.118 -19.183 -12.050 1.00 47.98  ? 196 VAL A CB  1 
ATOM   1518 C  CG1 . VAL A 1 196 ? -21.520 -18.804 -13.471 1.00 43.66  ? 196 VAL A CG1 1 
ATOM   1519 C  CG2 . VAL A 1 196 ? -22.223 -19.977 -11.366 1.00 38.47  ? 196 VAL A CG2 1 
ATOM   1520 N  N   . LEU A 1 197 ? -18.131 -18.242 -12.411 1.00 43.39  ? 197 LEU A N   1 
ATOM   1521 C  CA  . LEU A 1 197 ? -17.199 -17.464 -13.214 1.00 47.76  ? 197 LEU A CA  1 
ATOM   1522 C  C   . LEU A 1 197 ? -15.938 -18.244 -13.570 1.00 47.69  ? 197 LEU A C   1 
ATOM   1523 O  O   . LEU A 1 197 ? -15.224 -17.850 -14.500 1.00 48.17  ? 197 LEU A O   1 
ATOM   1524 C  CB  . LEU A 1 197 ? -16.831 -16.176 -12.474 1.00 44.93  ? 197 LEU A CB  1 
ATOM   1525 C  CG  . LEU A 1 197 ? -17.918 -15.100 -12.456 1.00 43.40  ? 197 LEU A CG  1 
ATOM   1526 C  CD1 . LEU A 1 197 ? -17.443 -13.907 -11.637 1.00 38.62  ? 197 LEU A CD1 1 
ATOM   1527 C  CD2 . LEU A 1 197 ? -18.304 -14.663 -13.874 1.00 42.90  ? 197 LEU A CD2 1 
ATOM   1528 N  N   . ASN A 1 198 ? -15.646 -19.331 -12.860 1.00 44.45  ? 198 ASN A N   1 
ATOM   1529 C  CA  . ASN A 1 198 ? -14.485 -20.157 -13.148 1.00 47.05  ? 198 ASN A CA  1 
ATOM   1530 C  C   . ASN A 1 198 ? -14.851 -21.450 -13.866 1.00 47.02  ? 198 ASN A C   1 
ATOM   1531 O  O   . ASN A 1 198 ? -14.011 -22.350 -13.964 1.00 49.91  ? 198 ASN A O   1 
ATOM   1532 C  CB  . ASN A 1 198 ? -13.728 -20.455 -11.856 1.00 45.96  ? 198 ASN A CB  1 
ATOM   1533 C  CG  . ASN A 1 198 ? -12.864 -19.286 -11.414 1.00 56.67  ? 198 ASN A CG  1 
ATOM   1534 O  OD1 . ASN A 1 198 ? -13.237 -18.511 -10.523 1.00 58.34  ? 198 ASN A OD1 1 
ATOM   1535 N  ND2 . ASN A 1 198 ? -11.705 -19.141 -12.050 1.00 62.61  ? 198 ASN A ND2 1 
ATOM   1536 N  N   . ASN A 1 199 ? -16.080 -21.558 -14.376 1.00 44.20  ? 199 ASN A N   1 
ATOM   1537 C  CA  . ASN A 1 199 ? -16.472 -22.709 -15.185 1.00 47.38  ? 199 ASN A CA  1 
ATOM   1538 C  C   . ASN A 1 199 ? -15.754 -22.650 -16.530 1.00 47.01  ? 199 ASN A C   1 
ATOM   1539 O  O   . ASN A 1 199 ? -15.889 -21.672 -17.276 1.00 43.90  ? 199 ASN A O   1 
ATOM   1540 C  CB  . ASN A 1 199 ? -17.989 -22.719 -15.381 1.00 44.56  ? 199 ASN A CB  1 
ATOM   1541 C  CG  . ASN A 1 199 ? -18.466 -23.913 -16.187 1.00 52.16  ? 199 ASN A CG  1 
ATOM   1542 O  OD1 . ASN A 1 199 ? -18.261 -23.983 -17.410 1.00 48.78  ? 199 ASN A OD1 1 
ATOM   1543 N  ND2 . ASN A 1 199 ? -19.124 -24.856 -15.513 1.00 46.74  ? 199 ASN A ND2 1 
ATOM   1544 N  N   . GLU A 1 200 ? -15.003 -23.705 -16.854 1.00 50.99  ? 200 GLU A N   1 
ATOM   1545 C  CA  . GLU A 1 200 ? -14.158 -23.724 -18.042 1.00 44.75  ? 200 GLU A CA  1 
ATOM   1546 C  C   . GLU A 1 200 ? -14.691 -24.646 -19.137 1.00 44.79  ? 200 GLU A C   1 
ATOM   1547 O  O   . GLU A 1 200 ? -13.959 -24.980 -20.075 1.00 42.80  ? 200 GLU A O   1 
ATOM   1548 C  CB  . GLU A 1 200 ? -12.735 -24.132 -17.652 1.00 46.58  ? 200 GLU A CB  1 
ATOM   1549 C  CG  . GLU A 1 200 ? -12.103 -23.207 -16.612 1.00 53.36  ? 200 GLU A CG  1 
ATOM   1550 C  CD  . GLU A 1 200 ? -10.726 -23.669 -16.162 1.00 52.48  ? 200 GLU A CD  1 
ATOM   1551 O  OE1 . GLU A 1 200 ? -10.062 -24.412 -16.915 1.00 47.05  ? 200 GLU A OE1 1 
ATOM   1552 O  OE2 . GLU A 1 200 ? -10.311 -23.292 -15.045 1.00 64.19  ? 200 GLU A OE2 1 
ATOM   1553 N  N   . GLU A 1 201 ? -15.951 -25.062 -19.034 1.00 43.86  ? 201 GLU A N   1 
ATOM   1554 C  CA  . GLU A 1 201 ? -16.536 -25.952 -20.031 1.00 48.79  ? 201 GLU A CA  1 
ATOM   1555 C  C   . GLU A 1 201 ? -16.817 -25.161 -21.298 1.00 46.41  ? 201 GLU A C   1 
ATOM   1556 O  O   . GLU A 1 201 ? -17.713 -24.308 -21.320 1.00 46.27  ? 201 GLU A O   1 
ATOM   1557 C  CB  . GLU A 1 201 ? -17.819 -26.583 -19.493 1.00 52.89  ? 201 GLU A CB  1 
ATOM   1558 C  CG  . GLU A 1 201 ? -17.686 -27.195 -18.102 1.00 51.83  ? 201 GLU A CG  1 
ATOM   1559 C  CD  . GLU A 1 201 ? -18.954 -27.907 -17.653 1.00 57.51  ? 201 GLU A CD  1 
ATOM   1560 O  OE1 . GLU A 1 201 ? -19.566 -28.627 -18.477 1.00 58.21  ? 201 GLU A OE1 1 
ATOM   1561 O  OE2 . GLU A 1 201 ? -19.341 -27.742 -16.476 1.00 56.66  ? 201 GLU A OE2 1 
ATOM   1562 N  N   . ALA A 1 202 ? -16.046 -25.418 -22.350 1.00 48.98  ? 202 ALA A N   1 
ATOM   1563 C  CA  . ALA A 1 202 ? -16.264 -24.731 -23.617 1.00 48.17  ? 202 ALA A CA  1 
ATOM   1564 C  C   . ALA A 1 202 ? -17.588 -25.162 -24.236 1.00 47.02  ? 202 ALA A C   1 
ATOM   1565 O  O   . ALA A 1 202 ? -17.937 -26.346 -24.233 1.00 45.49  ? 202 ALA A O   1 
ATOM   1566 C  CB  . ALA A 1 202 ? -15.118 -25.021 -24.586 1.00 47.31  ? 202 ALA A CB  1 
ATOM   1567 N  N   . GLN A 1 203 ? -18.327 -24.184 -24.768 1.00 45.34  ? 203 GLN A N   1 
ATOM   1568 C  CA  . GLN A 1 203 ? -19.627 -24.407 -25.396 1.00 47.83  ? 203 GLN A CA  1 
ATOM   1569 C  C   . GLN A 1 203 ? -19.458 -24.290 -26.910 1.00 49.29  ? 203 GLN A C   1 
ATOM   1570 O  O   . GLN A 1 203 ? -19.434 -23.182 -27.457 1.00 44.00  ? 203 GLN A O   1 
ATOM   1571 C  CB  . GLN A 1 203 ? -20.645 -23.406 -24.862 1.00 49.57  ? 203 GLN A CB  1 
ATOM   1572 C  CG  . GLN A 1 203 ? -20.844 -23.505 -23.358 1.00 44.64  ? 203 GLN A CG  1 
ATOM   1573 C  CD  . GLN A 1 203 ? -21.330 -24.879 -22.929 1.00 48.38  ? 203 GLN A CD  1 
ATOM   1574 O  OE1 . GLN A 1 203 ? -22.363 -25.366 -23.400 1.00 47.03  ? 203 GLN A OE1 1 
ATOM   1575 N  NE2 . GLN A 1 203 ? -20.582 -25.517 -22.027 1.00 49.47  ? 203 GLN A NE2 1 
ATOM   1576 N  N   . LEU A 1 204 ? -19.349 -25.429 -27.578 1.00 50.54  ? 204 LEU A N   1 
ATOM   1577 C  CA  . LEU A 1 204 ? -18.997 -25.489 -28.989 1.00 44.84  ? 204 LEU A CA  1 
ATOM   1578 C  C   . LEU A 1 204 ? -19.857 -26.523 -29.689 1.00 48.02  ? 204 LEU A C   1 
ATOM   1579 O  O   . LEU A 1 204 ? -20.378 -27.445 -29.054 1.00 47.66  ? 204 LEU A O   1 
ATOM   1580 C  CB  . LEU A 1 204 ? -17.516 -25.841 -29.183 1.00 45.02  ? 204 LEU A CB  1 
ATOM   1581 C  CG  . LEU A 1 204 ? -16.506 -24.745 -28.855 1.00 44.48  ? 204 LEU A CG  1 
ATOM   1582 C  CD1 . LEU A 1 204 ? -15.109 -25.326 -28.760 1.00 50.15  ? 204 LEU A CD1 1 
ATOM   1583 C  CD2 . LEU A 1 204 ? -16.556 -23.644 -29.895 1.00 42.34  ? 204 LEU A CD2 1 
ATOM   1584 N  N   . PRO A 1 205 ? -20.026 -26.399 -31.018 1.00 59.43  ? 205 PRO A N   1 
ATOM   1585 C  CA  . PRO A 1 205 ? -19.502 -25.328 -31.890 1.00 48.27  ? 205 PRO A CA  1 
ATOM   1586 C  C   . PRO A 1 205 ? -20.300 -24.033 -31.729 1.00 45.98  ? 205 PRO A C   1 
ATOM   1587 O  O   . PRO A 1 205 ? -21.456 -24.066 -31.320 1.00 52.62  ? 205 PRO A O   1 
ATOM   1588 C  CB  . PRO A 1 205 ? -19.633 -25.933 -33.292 1.00 59.32  ? 205 PRO A CB  1 
ATOM   1589 C  CG  . PRO A 1 205 ? -20.819 -26.855 -33.183 1.00 62.27  ? 205 PRO A CG  1 
ATOM   1590 C  CD  . PRO A 1 205 ? -20.738 -27.436 -31.788 1.00 52.27  ? 205 PRO A CD  1 
ATOM   1591 N  N   . ASP A 1 206 ? -19.694 -22.881 -32.021 1.00 47.71  ? 206 ASP A N   1 
ATOM   1592 C  CA  . ASP A 1 206 ? -20.361 -21.581 -31.949 1.00 50.43  ? 206 ASP A CA  1 
ATOM   1593 C  C   . ASP A 1 206 ? -20.121 -20.859 -33.269 1.00 47.23  ? 206 ASP A C   1 
ATOM   1594 O  O   . ASP A 1 206 ? -19.105 -20.167 -33.439 1.00 44.65  ? 206 ASP A O   1 
ATOM   1595 C  CB  . ASP A 1 206 ? -19.851 -20.757 -30.765 1.00 45.09  ? 206 ASP A CB  1 
ATOM   1596 C  CG  . ASP A 1 206 ? -20.746 -19.564 -30.454 1.00 52.38  ? 206 ASP A CG  1 
ATOM   1597 O  OD1 . ASP A 1 206 ? -21.339 -18.984 -31.399 1.00 42.82  ? 206 ASP A OD1 1 
ATOM   1598 O  OD2 . ASP A 1 206 ? -20.856 -19.207 -29.259 1.00 40.45  ? 206 ASP A OD2 1 
ATOM   1599 N  N   . PRO A 1 207 ? -21.026 -21.013 -34.237 1.00 52.87  ? 207 PRO A N   1 
ATOM   1600 C  CA  . PRO A 1 207 ? -20.849 -20.290 -35.515 1.00 53.50  ? 207 PRO A CA  1 
ATOM   1601 C  C   . PRO A 1 207 ? -20.803 -18.779 -35.351 1.00 50.20  ? 207 PRO A C   1 
ATOM   1602 O  O   . PRO A 1 207 ? -20.140 -18.098 -36.147 1.00 45.90  ? 207 PRO A O   1 
ATOM   1603 C  CB  . PRO A 1 207 ? -22.068 -20.721 -36.344 1.00 47.34  ? 207 PRO A CB  1 
ATOM   1604 C  CG  . PRO A 1 207 ? -22.534 -22.003 -35.729 1.00 59.46  ? 207 PRO A CG  1 
ATOM   1605 C  CD  . PRO A 1 207 ? -22.186 -21.926 -34.258 1.00 46.42  ? 207 PRO A CD  1 
ATOM   1606 N  N   . ALA A 1 208 ? -21.508 -18.234 -34.351 1.00 47.61  ? 208 ALA A N   1 
ATOM   1607 C  CA  . ALA A 1 208 ? -21.526 -16.787 -34.154 1.00 44.20  ? 208 ALA A CA  1 
ATOM   1608 C  C   . ALA A 1 208 ? -20.151 -16.258 -33.765 1.00 42.71  ? 208 ALA A C   1 
ATOM   1609 O  O   . ALA A 1 208 ? -19.742 -15.186 -34.224 1.00 50.16  ? 208 ALA A O   1 
ATOM   1610 C  CB  . ALA A 1 208 ? -22.561 -16.416 -33.096 1.00 45.05  ? 208 ALA A CB  1 
ATOM   1611 N  N   . ILE A 1 209 ? -19.430 -16.979 -32.906 1.00 49.69  ? 209 ILE A N   1 
ATOM   1612 C  CA  . ILE A 1 209 ? -18.089 -16.542 -32.530 1.00 52.64  ? 209 ILE A CA  1 
ATOM   1613 C  C   . ILE A 1 209 ? -17.146 -16.628 -33.720 1.00 41.26  ? 209 ILE A C   1 
ATOM   1614 O  O   . ILE A 1 209 ? -16.354 -15.713 -33.969 1.00 40.32  ? 209 ILE A O   1 
ATOM   1615 C  CB  . ILE A 1 209 ? -17.562 -17.363 -31.337 1.00 47.57  ? 209 ILE A CB  1 
ATOM   1616 C  CG1 . ILE A 1 209 ? -18.341 -17.003 -30.079 1.00 41.94  ? 209 ILE A CG1 1 
ATOM   1617 C  CG2 . ILE A 1 209 ? -16.067 -17.131 -31.155 1.00 40.80  ? 209 ILE A CG2 1 
ATOM   1618 C  CD1 . ILE A 1 209 ? -18.020 -17.883 -28.875 1.00 44.33  ? 209 ILE A CD1 1 
ATOM   1619 N  N   . GLU A 1 210 ? -17.205 -17.732 -34.468 1.00 50.78  ? 210 GLU A N   1 
ATOM   1620 C  CA  . GLU A 1 210 ? -16.309 -17.898 -35.608 1.00 49.52  ? 210 GLU A CA  1 
ATOM   1621 C  C   . GLU A 1 210 ? -16.527 -16.807 -36.646 1.00 50.45  ? 210 GLU A C   1 
ATOM   1622 O  O   . GLU A 1 210 ? -15.563 -16.284 -37.226 1.00 48.02  ? 210 GLU A O   1 
ATOM   1623 C  CB  . GLU A 1 210 ? -16.513 -19.272 -36.243 1.00 47.01  ? 210 GLU A CB  1 
ATOM   1624 C  CG  . GLU A 1 210 ? -15.857 -20.406 -35.487 1.00 57.00  ? 210 GLU A CG  1 
ATOM   1625 C  CD  . GLU A 1 210 ? -16.126 -21.749 -36.132 1.00 55.92  ? 210 GLU A CD  1 
ATOM   1626 O  OE1 . GLU A 1 210 ? -17.280 -22.220 -36.059 1.00 65.50  ? 210 GLU A OE1 1 
ATOM   1627 O  OE2 . GLU A 1 210 ? -15.191 -22.324 -36.729 1.00 64.09  ? 210 GLU A OE2 1 
ATOM   1628 N  N   . ASP A 1 211 ? -17.789 -16.465 -36.914 1.00 48.51  ? 211 ASP A N   1 
ATOM   1629 C  CA  . ASP A 1 211 ? -18.080 -15.462 -37.931 1.00 43.90  ? 211 ASP A CA  1 
ATOM   1630 C  C   . ASP A 1 211 ? -17.587 -14.082 -37.511 1.00 42.87  ? 211 ASP A C   1 
ATOM   1631 O  O   . ASP A 1 211 ? -17.001 -13.357 -38.319 1.00 53.62  ? 211 ASP A O   1 
ATOM   1632 C  CB  . ASP A 1 211 ? -19.583 -15.432 -38.209 1.00 54.41  ? 211 ASP A CB  1 
ATOM   1633 C  CG  . ASP A 1 211 ? -19.953 -14.482 -39.331 1.00 65.25  ? 211 ASP A CG  1 
ATOM   1634 O  OD1 . ASP A 1 211 ? -19.793 -14.865 -40.512 1.00 65.20  ? 211 ASP A OD1 1 
ATOM   1635 O  OD2 . ASP A 1 211 ? -20.405 -13.357 -39.032 1.00 64.06  ? 211 ASP A OD2 1 
ATOM   1636 N  N   . GLN A 1 212 ? -17.822 -13.696 -36.257 1.00 46.84  ? 212 GLN A N   1 
ATOM   1637 C  CA  . GLN A 1 212 ? -17.472 -12.342 -35.838 1.00 46.69  ? 212 GLN A CA  1 
ATOM   1638 C  C   . GLN A 1 212 ? -15.965 -12.182 -35.650 1.00 46.78  ? 212 GLN A C   1 
ATOM   1639 O  O   . GLN A 1 212 ? -15.390 -11.162 -36.046 1.00 46.60  ? 212 GLN A O   1 
ATOM   1640 C  CB  . GLN A 1 212 ? -18.207 -11.988 -34.544 1.00 51.08  ? 212 GLN A CB  1 
ATOM   1641 C  CG  . GLN A 1 212 ? -18.061 -10.530 -34.170 1.00 51.24  ? 212 GLN A CG  1 
ATOM   1642 C  CD  . GLN A 1 212 ? -18.599 -10.212 -32.806 1.00 44.11  ? 212 GLN A CD  1 
ATOM   1643 O  OE1 . GLN A 1 212 ? -19.563 -10.819 -32.340 1.00 46.19  ? 212 GLN A OE1 1 
ATOM   1644 N  NE2 . GLN A 1 212 ? -17.979 -9.250  -32.151 1.00 46.61  ? 212 GLN A NE2 1 
ATOM   1645 N  N   . GLY A 1 213 ? -15.312 -13.166 -35.022 1.00 46.83  ? 213 GLY A N   1 
ATOM   1646 C  CA  . GLY A 1 213 ? -13.879 -13.084 -34.793 1.00 45.02  ? 213 GLY A CA  1 
ATOM   1647 C  C   . GLY A 1 213 ? -13.033 -13.400 -36.004 1.00 53.31  ? 213 GLY A C   1 
ATOM   1648 O  O   . GLY A 1 213 ? -11.871 -12.980 -36.063 1.00 54.66  ? 213 GLY A O   1 
ATOM   1649 N  N   . GLY A 1 214 ? -13.587 -14.128 -36.970 1.00 48.27  ? 214 GLY A N   1 
ATOM   1650 C  CA  . GLY A 1 214 ? -12.845 -14.414 -38.185 1.00 55.55  ? 214 GLY A CA  1 
ATOM   1651 C  C   . GLY A 1 214 ? -11.578 -15.193 -37.906 1.00 49.41  ? 214 GLY A C   1 
ATOM   1652 O  O   . GLY A 1 214 ? -11.565 -16.160 -37.138 1.00 46.86  ? 214 GLY A O   1 
ATOM   1653 N  N   . GLU A 1 215 ? -10.489 -14.766 -38.550 1.00 47.64  ? 215 GLU A N   1 
ATOM   1654 C  CA  . GLU A 1 215 ? -9.234  -15.502 -38.460 1.00 47.35  ? 215 GLU A CA  1 
ATOM   1655 C  C   . GLU A 1 215 ? -8.590  -15.361 -37.087 1.00 49.17  ? 215 GLU A C   1 
ATOM   1656 O  O   . GLU A 1 215 ? -7.907  -16.286 -36.630 1.00 45.31  ? 215 GLU A O   1 
ATOM   1657 C  CB  . GLU A 1 215 ? -8.269  -15.017 -39.550 1.00 45.58  ? 215 GLU A CB  1 
ATOM   1658 C  CG  . GLU A 1 215 ? -8.768  -15.208 -40.978 1.00 48.43  ? 215 GLU A CG  1 
ATOM   1659 C  CD  . GLU A 1 215 ? -9.492  -13.985 -41.546 1.00 51.98  ? 215 GLU A CD  1 
ATOM   1660 O  OE1 . GLU A 1 215 ? -9.860  -13.075 -40.774 1.00 46.34  ? 215 GLU A OE1 1 
ATOM   1661 O  OE2 . GLU A 1 215 ? -9.697  -13.937 -42.786 1.00 48.45  ? 215 GLU A OE2 1 
ATOM   1662 N  N   . TYR A 1 216 ? -8.802  -14.224 -36.417 1.00 45.51  ? 216 TYR A N   1 
ATOM   1663 C  CA  . TYR A 1 216 ? -8.118  -13.949 -35.158 1.00 43.29  ? 216 TYR A CA  1 
ATOM   1664 C  C   . TYR A 1 216 ? -8.534  -14.928 -34.071 1.00 48.85  ? 216 TYR A C   1 
ATOM   1665 O  O   . TYR A 1 216 ? -7.713  -15.323 -33.233 1.00 53.16  ? 216 TYR A O   1 
ATOM   1666 C  CB  . TYR A 1 216 ? -8.404  -12.507 -34.729 1.00 47.63  ? 216 TYR A CB  1 
ATOM   1667 C  CG  . TYR A 1 216 ? -7.932  -12.150 -33.340 1.00 51.74  ? 216 TYR A CG  1 
ATOM   1668 C  CD1 . TYR A 1 216 ? -6.583  -12.193 -33.013 1.00 54.68  ? 216 TYR A CD1 1 
ATOM   1669 C  CD2 . TYR A 1 216 ? -8.833  -11.756 -32.358 1.00 51.58  ? 216 TYR A CD2 1 
ATOM   1670 C  CE1 . TYR A 1 216 ? -6.144  -11.862 -31.745 1.00 52.71  ? 216 TYR A CE1 1 
ATOM   1671 C  CE2 . TYR A 1 216 ? -8.405  -11.424 -31.089 1.00 48.96  ? 216 TYR A CE2 1 
ATOM   1672 C  CZ  . TYR A 1 216 ? -7.057  -11.477 -30.788 1.00 55.65  ? 216 TYR A CZ  1 
ATOM   1673 O  OH  . TYR A 1 216 ? -6.619  -11.145 -29.525 1.00 57.77  ? 216 TYR A OH  1 
ATOM   1674 N  N   . VAL A 1 217 ? -9.810  -15.324 -34.054 1.00 50.19  ? 217 VAL A N   1 
ATOM   1675 C  CA  . VAL A 1 217 ? -10.316 -16.188 -32.991 1.00 51.38  ? 217 VAL A CA  1 
ATOM   1676 C  C   . VAL A 1 217 ? -10.131 -17.669 -33.290 1.00 48.09  ? 217 VAL A C   1 
ATOM   1677 O  O   . VAL A 1 217 ? -10.337 -18.500 -32.390 1.00 48.04  ? 217 VAL A O   1 
ATOM   1678 C  CB  . VAL A 1 217 ? -11.807 -15.870 -32.721 1.00 52.26  ? 217 VAL A CB  1 
ATOM   1679 C  CG1 . VAL A 1 217 ? -12.707 -16.434 -33.822 1.00 41.58  ? 217 VAL A CG1 1 
ATOM   1680 C  CG2 . VAL A 1 217 ? -12.228 -16.380 -31.341 1.00 49.71  ? 217 VAL A CG2 1 
ATOM   1681 N  N   . GLN A 1 218 ? -9.732  -18.029 -34.511 1.00 46.65  ? 218 GLN A N   1 
ATOM   1682 C  CA  . GLN A 1 218 ? -9.613  -19.447 -34.853 1.00 53.93  ? 218 GLN A CA  1 
ATOM   1683 C  C   . GLN A 1 218 ? -8.666  -20.198 -33.923 1.00 52.27  ? 218 GLN A C   1 
ATOM   1684 O  O   . GLN A 1 218 ? -9.054  -21.265 -33.409 1.00 49.94  ? 218 GLN A O   1 
ATOM   1685 C  CB  . GLN A 1 218 ? -9.166  -19.594 -36.311 1.00 53.00  ? 218 GLN A CB  1 
ATOM   1686 C  CG  . GLN A 1 218 ? -10.260 -19.342 -37.345 1.00 56.98  ? 218 GLN A CG  1 
ATOM   1687 C  CD  . GLN A 1 218 ? -11.309 -20.439 -37.370 1.00 54.63  ? 218 GLN A CD  1 
ATOM   1688 O  OE1 . GLN A 1 218 ? -10.988 -21.628 -37.495 1.00 55.35  ? 218 GLN A OE1 1 
ATOM   1689 N  NE2 . GLN A 1 218 ? -12.571 -20.046 -37.260 1.00 50.57  ? 218 GLN A NE2 1 
ATOM   1690 N  N   . PRO A 1 219 ? -7.439  -19.739 -33.669 1.00 47.68  ? 219 PRO A N   1 
ATOM   1691 C  CA  . PRO A 1 219 ? -6.562  -20.470 -32.738 1.00 52.57  ? 219 PRO A CA  1 
ATOM   1692 C  C   . PRO A 1 219 ? -6.964  -20.348 -31.270 1.00 52.53  ? 219 PRO A C   1 
ATOM   1693 O  O   . PRO A 1 219 ? -6.422  -21.096 -30.441 1.00 50.48  ? 219 PRO A O   1 
ATOM   1694 C  CB  . PRO A 1 219 ? -5.177  -19.856 -32.995 1.00 49.67  ? 219 PRO A CB  1 
ATOM   1695 C  CG  . PRO A 1 219 ? -5.444  -18.537 -33.655 1.00 49.72  ? 219 PRO A CG  1 
ATOM   1696 C  CD  . PRO A 1 219 ? -6.715  -18.699 -34.431 1.00 45.33  ? 219 PRO A CD  1 
ATOM   1697 N  N   . MET A 1 220 ? -7.870  -19.433 -30.918 1.00 51.26  ? 220 MET A N   1 
ATOM   1698 C  CA  . MET A 1 220 ? -8.351  -19.318 -29.548 1.00 50.44  ? 220 MET A CA  1 
ATOM   1699 C  C   . MET A 1 220 ? -9.634  -20.105 -29.300 1.00 50.42  ? 220 MET A C   1 
ATOM   1700 O  O   . MET A 1 220 ? -10.031 -20.263 -28.145 1.00 42.70  ? 220 MET A O   1 
ATOM   1701 C  CB  . MET A 1 220 ? -8.615  -17.847 -29.192 1.00 53.28  ? 220 MET A CB  1 
ATOM   1702 C  CG  . MET A 1 220 ? -7.631  -16.854 -29.782 1.00 64.44  ? 220 MET A CG  1 
ATOM   1703 S  SD  . MET A 1 220 ? -7.655  -15.258 -28.925 1.00 76.81  ? 220 MET A SD  1 
ATOM   1704 C  CE  . MET A 1 220 ? -9.371  -14.779 -29.117 1.00 57.05  ? 220 MET A CE  1 
ATOM   1705 N  N   . LEU A 1 221 ? -10.266 -20.628 -30.355 1.00 52.22  ? 221 LEU A N   1 
ATOM   1706 C  CA  . LEU A 1 221 ? -11.675 -21.006 -30.271 1.00 49.60  ? 221 LEU A CA  1 
ATOM   1707 C  C   . LEU A 1 221 ? -11.923 -22.060 -29.200 1.00 45.75  ? 221 LEU A C   1 
ATOM   1708 O  O   . LEU A 1 221 ? -12.886 -21.955 -28.435 1.00 43.77  ? 221 LEU A O   1 
ATOM   1709 C  CB  . LEU A 1 221 ? -12.150 -21.512 -31.631 1.00 44.21  ? 221 LEU A CB  1 
ATOM   1710 C  CG  . LEU A 1 221 ? -13.655 -21.696 -31.811 1.00 48.24  ? 221 LEU A CG  1 
ATOM   1711 C  CD1 . LEU A 1 221 ? -14.395 -20.378 -31.685 1.00 43.86  ? 221 LEU A CD1 1 
ATOM   1712 C  CD2 . LEU A 1 221 ? -13.919 -22.347 -33.161 1.00 43.76  ? 221 LEU A CD2 1 
ATOM   1713 N  N   . SER A 1 222 ? -11.072 -23.089 -29.133 1.00 47.88  ? 222 SER A N   1 
ATOM   1714 C  CA  . SER A 1 222 ? -11.333 -24.197 -28.214 1.00 51.42  ? 222 SER A CA  1 
ATOM   1715 C  C   . SER A 1 222 ? -11.514 -23.712 -26.782 1.00 47.80  ? 222 SER A C   1 
ATOM   1716 O  O   . SER A 1 222 ? -12.301 -24.294 -26.026 1.00 50.81  ? 222 SER A O   1 
ATOM   1717 C  CB  . SER A 1 222 ? -10.188 -25.211 -28.280 1.00 46.37  ? 222 SER A CB  1 
ATOM   1718 O  OG  . SER A 1 222 ? -8.993  -24.642 -27.754 1.00 50.27  ? 222 SER A OG  1 
ATOM   1719 N  N   . LYS A 1 223 ? -10.806 -22.650 -26.396 1.00 46.79  ? 223 LYS A N   1 
ATOM   1720 C  CA  . LYS A 1 223 ? -10.862 -22.126 -25.040 1.00 46.93  ? 223 LYS A CA  1 
ATOM   1721 C  C   . LYS A 1 223 ? -11.677 -20.846 -24.916 1.00 50.50  ? 223 LYS A C   1 
ATOM   1722 O  O   . LYS A 1 223 ? -12.112 -20.514 -23.801 1.00 47.15  ? 223 LYS A O   1 
ATOM   1723 C  CB  . LYS A 1 223 ? -9.446  -21.852 -24.530 1.00 49.46  ? 223 LYS A CB  1 
ATOM   1724 C  CG  . LYS A 1 223 ? -8.564  -23.086 -24.486 1.00 55.06  ? 223 LYS A CG  1 
ATOM   1725 C  CD  . LYS A 1 223 ? -9.086  -24.095 -23.474 1.00 53.19  ? 223 LYS A CD  1 
ATOM   1726 C  CE  . LYS A 1 223 ? -8.135  -25.266 -23.329 1.00 54.65  ? 223 LYS A CE  1 
ATOM   1727 N  NZ  . LYS A 1 223 ? -6.788  -24.808 -22.888 1.00 53.67  ? 223 LYS A NZ  1 
ATOM   1728 N  N   . TYR A 1 224 ? -11.880 -20.126 -26.021 1.00 46.08  ? 224 TYR A N   1 
ATOM   1729 C  CA  . TYR A 1 224 ? -12.539 -18.823 -25.969 1.00 45.22  ? 224 TYR A CA  1 
ATOM   1730 C  C   . TYR A 1 224 ? -14.023 -18.957 -25.670 1.00 42.40  ? 224 TYR A C   1 
ATOM   1731 O  O   . TYR A 1 224 ? -14.628 -18.034 -25.114 1.00 45.06  ? 224 TYR A O   1 
ATOM   1732 C  CB  . TYR A 1 224 ? -12.308 -18.101 -27.307 1.00 47.70  ? 224 TYR A CB  1 
ATOM   1733 C  CG  . TYR A 1 224 ? -12.842 -16.690 -27.394 1.00 44.79  ? 224 TYR A CG  1 
ATOM   1734 C  CD1 . TYR A 1 224 ? -12.061 -15.606 -27.009 1.00 42.11  ? 224 TYR A CD1 1 
ATOM   1735 C  CD2 . TYR A 1 224 ? -14.116 -16.440 -27.889 1.00 43.12  ? 224 TYR A CD2 1 
ATOM   1736 C  CE1 . TYR A 1 224 ? -12.540 -14.316 -27.102 1.00 41.17  ? 224 TYR A CE1 1 
ATOM   1737 C  CE2 . TYR A 1 224 ? -14.608 -15.152 -27.984 1.00 38.91  ? 224 TYR A CE2 1 
ATOM   1738 C  CZ  . TYR A 1 224 ? -13.816 -14.094 -27.591 1.00 48.09  ? 224 TYR A CZ  1 
ATOM   1739 O  OH  . TYR A 1 224 ? -14.309 -12.811 -27.681 1.00 50.86  ? 224 TYR A OH  1 
ATOM   1740 N  N   . ALA A 1 225 ? -14.618 -20.099 -26.011 1.00 42.05  ? 225 ALA A N   1 
ATOM   1741 C  CA  . ALA A 1 225 ? -16.053 -20.313 -25.913 1.00 53.20  ? 225 ALA A CA  1 
ATOM   1742 C  C   . ALA A 1 225 ? -16.496 -20.795 -24.528 1.00 46.34  ? 225 ALA A C   1 
ATOM   1743 O  O   . ALA A 1 225 ? -17.587 -21.361 -24.399 1.00 51.81  ? 225 ALA A O   1 
ATOM   1744 C  CB  . ALA A 1 225 ? -16.507 -21.313 -26.987 1.00 44.96  ? 225 ALA A CB  1 
ATOM   1745 N  N   . ALA A 1 226 ? -15.688 -20.581 -23.502 1.00 41.45  ? 226 ALA A N   1 
ATOM   1746 C  CA  . ALA A 1 226 ? -16.059 -20.876 -22.127 1.00 48.59  ? 226 ALA A CA  1 
ATOM   1747 C  C   . ALA A 1 226 ? -16.246 -19.585 -21.341 1.00 39.38  ? 226 ALA A C   1 
ATOM   1748 O  O   . ALA A 1 226 ? -15.725 -18.528 -21.703 1.00 40.53  ? 226 ALA A O   1 
ATOM   1749 C  CB  . ALA A 1 226 ? -14.993 -21.747 -21.441 1.00 42.56  ? 226 ALA A CB  1 
ATOM   1750 N  N   . VAL A 1 227 ? -17.008 -19.684 -20.251 1.00 41.36  ? 227 VAL A N   1 
ATOM   1751 C  CA  . VAL A 1 227 ? -17.144 -18.547 -19.343 1.00 39.12  ? 227 VAL A CA  1 
ATOM   1752 C  C   . VAL A 1 227 ? -15.768 -18.116 -18.856 1.00 39.24  ? 227 VAL A C   1 
ATOM   1753 O  O   . VAL A 1 227 ? -15.427 -16.928 -18.849 1.00 39.62  ? 227 VAL A O   1 
ATOM   1754 C  CB  . VAL A 1 227 ? -18.069 -18.911 -18.165 1.00 46.87  ? 227 VAL A CB  1 
ATOM   1755 C  CG1 . VAL A 1 227 ? -18.156 -17.761 -17.159 1.00 40.75  ? 227 VAL A CG1 1 
ATOM   1756 C  CG2 . VAL A 1 227 ? -19.455 -19.284 -18.677 1.00 48.26  ? 227 VAL A CG2 1 
ATOM   1757 N  N   . CYS A 1 228 ? -14.959 -19.080 -18.435 1.00 44.22  ? 228 CYS A N   1 
ATOM   1758 C  CA  . CYS A 1 228 ? -13.609 -18.830 -17.958 1.00 48.19  ? 228 CYS A CA  1 
ATOM   1759 C  C   . CYS A 1 228 ? -12.640 -19.244 -19.056 1.00 40.76  ? 228 CYS A C   1 
ATOM   1760 O  O   . CYS A 1 228 ? -12.578 -20.428 -19.418 1.00 42.39  ? 228 CYS A O   1 
ATOM   1761 C  CB  . CYS A 1 228 ? -13.346 -19.598 -16.662 1.00 41.85  ? 228 CYS A CB  1 
ATOM   1762 S  SG  . CYS A 1 228 ? -11.716 -19.337 -15.954 1.00 50.22  ? 228 CYS A SG  1 
ATOM   1763 N  N   . VAL A 1 229 ? -11.915 -18.269 -19.598 1.00 42.99  ? 229 VAL A N   1 
ATOM   1764 C  CA  . VAL A 1 229 ? -11.076 -18.460 -20.776 1.00 41.20  ? 229 VAL A CA  1 
ATOM   1765 C  C   . VAL A 1 229 ? -9.651  -18.726 -20.327 1.00 39.33  ? 229 VAL A C   1 
ATOM   1766 O  O   . VAL A 1 229 ? -9.073  -17.938 -19.566 1.00 43.89  ? 229 VAL A O   1 
ATOM   1767 C  CB  . VAL A 1 229 ? -11.143 -17.233 -21.703 1.00 44.84  ? 229 VAL A CB  1 
ATOM   1768 C  CG1 . VAL A 1 229 ? -10.236 -17.418 -22.912 1.00 44.43  ? 229 VAL A CG1 1 
ATOM   1769 C  CG2 . VAL A 1 229 ? -12.581 -16.986 -22.137 1.00 44.99  ? 229 VAL A CG2 1 
ATOM   1770 N  N   . ARG A 1 230 ? -9.082  -19.842 -20.788 1.00 39.82  ? 230 ARG A N   1 
ATOM   1771 C  CA  . ARG A 1 230 ? -7.700  -20.216 -20.478 1.00 42.47  ? 230 ARG A CA  1 
ATOM   1772 C  C   . ARG A 1 230 ? -6.974  -20.461 -21.799 1.00 49.10  ? 230 ARG A C   1 
ATOM   1773 O  O   . ARG A 1 230 ? -6.861  -21.600 -22.266 1.00 45.51  ? 230 ARG A O   1 
ATOM   1774 C  CB  . ARG A 1 230 ? -7.658  -21.446 -19.564 1.00 44.15  ? 230 ARG A CB  1 
ATOM   1775 C  CG  . ARG A 1 230 ? -8.169  -21.190 -18.156 1.00 46.88  ? 230 ARG A CG  1 
ATOM   1776 C  CD  . ARG A 1 230 ? -7.094  -20.551 -17.301 1.00 52.36  ? 230 ARG A CD  1 
ATOM   1777 N  NE  . ARG A 1 230 ? -7.597  -20.153 -15.994 1.00 51.81  ? 230 ARG A NE  1 
ATOM   1778 C  CZ  . ARG A 1 230 ? -8.022  -18.935 -15.691 1.00 45.55  ? 230 ARG A CZ  1 
ATOM   1779 N  NH1 . ARG A 1 230 ? -8.032  -17.963 -16.585 1.00 48.38  ? 230 ARG A NH1 1 
ATOM   1780 N  NH2 . ARG A 1 230 ? -8.448  -18.684 -14.455 1.00 53.93  ? 230 ARG A NH2 1 
ATOM   1781 N  N   . CYS A 1 231 ? -6.477  -19.387 -22.394 1.00 45.24  ? 231 CYS A N   1 
ATOM   1782 C  CA  . CYS A 1 231 ? -5.680  -19.430 -23.608 1.00 44.90  ? 231 CYS A CA  1 
ATOM   1783 C  C   . CYS A 1 231 ? -4.215  -19.226 -23.274 1.00 49.33  ? 231 CYS A C   1 
ATOM   1784 O  O   . CYS A 1 231 ? -3.858  -18.899 -22.137 1.00 50.26  ? 231 CYS A O   1 
ATOM   1785 C  CB  . CYS A 1 231 ? -6.153  -18.351 -24.585 1.00 41.69  ? 231 CYS A CB  1 
ATOM   1786 S  SG  . CYS A 1 231 ? -7.776  -18.653 -25.324 1.00 47.05  ? 231 CYS A SG  1 
ATOM   1787 N  N   . PRO A 1 232 ? -3.320  -19.425 -24.245 1.00 51.32  ? 232 PRO A N   1 
ATOM   1788 C  CA  . PRO A 1 232 ? -1.902  -19.116 -24.003 1.00 45.98  ? 232 PRO A CA  1 
ATOM   1789 C  C   . PRO A 1 232 ? -1.659  -17.621 -23.864 1.00 52.00  ? 232 PRO A C   1 
ATOM   1790 O  O   . PRO A 1 232 ? -1.754  -16.880 -24.848 1.00 56.39  ? 232 PRO A O   1 
ATOM   1791 C  CB  . PRO A 1 232 ? -1.194  -19.684 -25.238 1.00 48.89  ? 232 PRO A CB  1 
ATOM   1792 C  CG  . PRO A 1 232 ? -2.144  -20.720 -25.785 1.00 53.13  ? 232 PRO A CG  1 
ATOM   1793 C  CD  . PRO A 1 232 ? -3.523  -20.206 -25.483 1.00 51.95  ? 232 PRO A CD  1 
ATOM   1794 N  N   . GLY A 1 233 ? -1.347  -17.172 -22.646 1.00 47.86  ? 233 GLY A N   1 
ATOM   1795 C  CA  . GLY A 1 233 ? -1.040  -15.776 -22.405 1.00 50.11  ? 233 GLY A CA  1 
ATOM   1796 C  C   . GLY A 1 233 ? -2.226  -14.836 -22.429 1.00 55.55  ? 233 GLY A C   1 
ATOM   1797 O  O   . GLY A 1 233 ? -2.029  -13.614 -22.407 1.00 45.42  ? 233 GLY A O   1 
ATOM   1798 N  N   . TYR A 1 234 ? -3.449  -15.365 -22.467 1.00 52.39  ? 234 TYR A N   1 
ATOM   1799 C  CA  . TYR A 1 234 ? -4.660  -14.559 -22.530 1.00 56.74  ? 234 TYR A CA  1 
ATOM   1800 C  C   . TYR A 1 234 ? -5.775  -15.328 -21.833 1.00 49.19  ? 234 TYR A C   1 
ATOM   1801 O  O   . TYR A 1 234 ? -5.863  -16.549 -21.974 1.00 45.90  ? 234 TYR A O   1 
ATOM   1802 C  CB  . TYR A 1 234 ? -5.029  -14.248 -23.995 1.00 45.76  ? 234 TYR A CB  1 
ATOM   1803 C  CG  . TYR A 1 234 ? -6.344  -13.517 -24.172 1.00 42.75  ? 234 TYR A CG  1 
ATOM   1804 C  CD1 . TYR A 1 234 ? -6.397  -12.132 -24.186 1.00 45.31  ? 234 TYR A CD1 1 
ATOM   1805 C  CD2 . TYR A 1 234 ? -7.534  -14.218 -24.328 1.00 52.06  ? 234 TYR A CD2 1 
ATOM   1806 C  CE1 . TYR A 1 234 ? -7.599  -11.460 -24.347 1.00 47.72  ? 234 TYR A CE1 1 
ATOM   1807 C  CE2 . TYR A 1 234 ? -8.742  -13.557 -24.487 1.00 53.37  ? 234 TYR A CE2 1 
ATOM   1808 C  CZ  . TYR A 1 234 ? -8.767  -12.177 -24.498 1.00 51.44  ? 234 TYR A CZ  1 
ATOM   1809 O  OH  . TYR A 1 234 ? -9.967  -11.514 -24.659 1.00 48.56  ? 234 TYR A OH  1 
ATOM   1810 N  N   . GLY A 1 235 ? -6.609  -14.619 -21.080 1.00 46.01  ? 235 GLY A N   1 
ATOM   1811 C  CA  . GLY A 1 235 ? -7.765  -15.254 -20.480 1.00 49.89  ? 235 GLY A CA  1 
ATOM   1812 C  C   . GLY A 1 235 ? -8.239  -14.522 -19.233 1.00 45.17  ? 235 GLY A C   1 
ATOM   1813 O  O   . GLY A 1 235 ? -7.820  -13.398 -18.947 1.00 45.07  ? 235 GLY A O   1 
ATOM   1814 N  N   . THR A 1 236 ? -9.115  -15.205 -18.504 1.00 39.72  ? 236 THR A N   1 
ATOM   1815 C  CA  . THR A 1 236 ? -9.786  -14.624 -17.339 1.00 43.86  ? 236 THR A CA  1 
ATOM   1816 C  C   . THR A 1 236 ? -8.771  -14.339 -16.240 1.00 47.60  ? 236 THR A C   1 
ATOM   1817 O  O   . THR A 1 236 ? -8.210  -15.263 -15.641 1.00 48.89  ? 236 THR A O   1 
ATOM   1818 C  CB  . THR A 1 236 ? -10.875 -15.573 -16.838 1.00 42.20  ? 236 THR A CB  1 
ATOM   1819 O  OG1 . THR A 1 236 ? -11.803 -15.838 -17.909 1.00 41.19  ? 236 THR A OG1 1 
ATOM   1820 C  CG2 . THR A 1 236 ? -11.639 -14.967 -15.666 1.00 40.53  ? 236 THR A CG2 1 
ATOM   1821 N  N   . ARG A 1 237 ? -8.540  -13.055 -15.969 1.00 46.77  ? 237 ARG A N   1 
ATOM   1822 C  CA  . ARG A 1 237 ? -7.642  -12.630 -14.907 1.00 42.72  ? 237 ARG A CA  1 
ATOM   1823 C  C   . ARG A 1 237 ? -8.372  -12.125 -13.677 1.00 44.96  ? 237 ARG A C   1 
ATOM   1824 O  O   . ARG A 1 237 ? -7.826  -12.206 -12.576 1.00 50.36  ? 237 ARG A O   1 
ATOM   1825 C  CB  . ARG A 1 237 ? -6.719  -11.515 -15.405 1.00 45.93  ? 237 ARG A CB  1 
ATOM   1826 C  CG  . ARG A 1 237 ? -5.780  -11.949 -16.504 1.00 59.66  ? 237 ARG A CG  1 
ATOM   1827 C  CD  . ARG A 1 237 ? -5.020  -10.762 -17.061 1.00 58.16  ? 237 ARG A CD  1 
ATOM   1828 N  NE  . ARG A 1 237 ? -4.321  -10.033 -16.006 1.00 69.07  ? 237 ARG A NE  1 
ATOM   1829 C  CZ  . ARG A 1 237 ? -3.574  -8.960  -16.221 1.00 68.14  ? 237 ARG A CZ  1 
ATOM   1830 N  NH1 . ARG A 1 237 ? -3.405  -8.470  -17.437 1.00 64.87  ? 237 ARG A NH1 1 
ATOM   1831 N  NH2 . ARG A 1 237 ? -2.983  -8.362  -15.191 1.00 68.45  ? 237 ARG A NH2 1 
ATOM   1832 N  N   . THR A 1 238 ? -9.591  -11.614 -13.830 1.00 51.28  ? 238 THR A N   1 
ATOM   1833 C  CA  . THR A 1 238 ? -10.317 -10.986 -12.732 1.00 47.07  ? 238 THR A CA  1 
ATOM   1834 C  C   . THR A 1 238 ? -11.755 -11.481 -12.702 1.00 43.11  ? 238 THR A C   1 
ATOM   1835 O  O   . THR A 1 238 ? -12.455 -11.425 -13.714 1.00 44.25  ? 238 THR A O   1 
ATOM   1836 C  CB  . THR A 1 238 ? -10.290 -9.461  -12.884 1.00 50.62  ? 238 THR A CB  1 
ATOM   1837 O  OG1 . THR A 1 238 ? -8.961  -9.042  -13.224 1.00 59.33  ? 238 THR A OG1 1 
ATOM   1838 C  CG2 . THR A 1 238 ? -10.709 -8.774  -11.593 1.00 48.89  ? 238 THR A CG2 1 
ATOM   1839 N  N   . ASN A 1 239 ? -12.182 -11.971 -11.539 1.00 47.76  ? 239 ASN A N   1 
ATOM   1840 C  CA  . ASN A 1 239 ? -13.584 -12.266 -11.263 1.00 43.37  ? 239 ASN A CA  1 
ATOM   1841 C  C   . ASN A 1 239 ? -14.099 -11.200 -10.308 1.00 47.31  ? 239 ASN A C   1 
ATOM   1842 O  O   . ASN A 1 239 ? -13.495 -10.973 -9.256  1.00 45.48  ? 239 ASN A O   1 
ATOM   1843 C  CB  . ASN A 1 239 ? -13.759 -13.649 -10.636 1.00 43.72  ? 239 ASN A CB  1 
ATOM   1844 C  CG  . ASN A 1 239 ? -12.808 -14.686 -11.219 1.00 54.19  ? 239 ASN A CG  1 
ATOM   1845 O  OD1 . ASN A 1 239 ? -12.062 -15.339 -10.482 1.00 44.64  ? 239 ASN A OD1 1 
ATOM   1846 N  ND2 . ASN A 1 239 ? -12.839 -14.854 -12.544 1.00 43.38  ? 239 ASN A ND2 1 
ATOM   1847 N  N   . THR A 1 240 ? -15.198 -10.540 -10.670 1.00 50.10  ? 240 THR A N   1 
ATOM   1848 C  CA  . THR A 1 240 ? -15.729 -9.446  -9.861  1.00 45.75  ? 240 THR A CA  1 
ATOM   1849 C  C   . THR A 1 240 ? -17.214 -9.662  -9.608  1.00 47.48  ? 240 THR A C   1 
ATOM   1850 O  O   . THR A 1 240 ? -17.994 -9.825  -10.554 1.00 51.87  ? 240 THR A O   1 
ATOM   1851 C  CB  . THR A 1 240 ? -15.504 -8.089  -10.547 1.00 48.88  ? 240 THR A CB  1 
ATOM   1852 O  OG1 . THR A 1 240 ? -14.120 -7.946  -10.894 1.00 49.74  ? 240 THR A OG1 1 
ATOM   1853 C  CG2 . THR A 1 240 ? -15.900 -6.945  -9.616  1.00 51.36  ? 240 THR A CG2 1 
ATOM   1854 N  N   . ILE A 1 241 ? -17.593 -9.639  -8.332  1.00 43.61  ? 241 ILE A N   1 
ATOM   1855 C  CA  . ILE A 1 241 ? -18.978 -9.781  -7.891  1.00 49.89  ? 241 ILE A CA  1 
ATOM   1856 C  C   . ILE A 1 241 ? -19.385 -8.468  -7.231  1.00 45.19  ? 241 ILE A C   1 
ATOM   1857 O  O   . ILE A 1 241 ? -18.690 -7.980  -6.336  1.00 47.38  ? 241 ILE A O   1 
ATOM   1858 C  CB  . ILE A 1 241 ? -19.145 -10.945 -6.894  1.00 45.45  ? 241 ILE A CB  1 
ATOM   1859 C  CG1 . ILE A 1 241 ? -18.533 -12.235 -7.447  1.00 48.92  ? 241 ILE A CG1 1 
ATOM   1860 C  CG2 . ILE A 1 241 ? -20.611 -11.140 -6.537  1.00 40.66  ? 241 ILE A CG2 1 
ATOM   1861 C  CD1 . ILE A 1 241 ? -19.403 -12.979 -8.407  1.00 53.55  ? 241 ILE A CD1 1 
ATOM   1862 N  N   . ILE A 1 242 ? -20.499 -7.897  -7.666  1.00 46.63  ? 242 ILE A N   1 
ATOM   1863 C  CA  . ILE A 1 242 ? -21.042 -6.697  -7.044  1.00 44.85  ? 242 ILE A CA  1 
ATOM   1864 C  C   . ILE A 1 242 ? -22.477 -6.986  -6.640  1.00 47.07  ? 242 ILE A C   1 
ATOM   1865 O  O   . ILE A 1 242 ? -23.284 -7.435  -7.462  1.00 45.39  ? 242 ILE A O   1 
ATOM   1866 C  CB  . ILE A 1 242 ? -20.967 -5.476  -7.976  1.00 47.99  ? 242 ILE A CB  1 
ATOM   1867 C  CG1 . ILE A 1 242 ? -19.527 -5.281  -8.466  1.00 47.96  ? 242 ILE A CG1 1 
ATOM   1868 C  CG2 . ILE A 1 242 ? -21.445 -4.233  -7.239  1.00 47.38  ? 242 ILE A CG2 1 
ATOM   1869 C  CD1 . ILE A 1 242 ? -19.331 -4.082  -9.368  1.00 44.89  ? 242 ILE A CD1 1 
ATOM   1870 N  N   . LEU A 1 243 ? -22.782 -6.744  -5.372  1.00 48.39  ? 243 LEU A N   1 
ATOM   1871 C  CA  . LEU A 1 243 ? -24.119 -6.892  -4.820  1.00 53.39  ? 243 LEU A CA  1 
ATOM   1872 C  C   . LEU A 1 243 ? -24.573 -5.550  -4.260  1.00 48.42  ? 243 LEU A C   1 
ATOM   1873 O  O   . LEU A 1 243 ? -23.775 -4.813  -3.673  1.00 48.44  ? 243 LEU A O   1 
ATOM   1874 C  CB  . LEU A 1 243 ? -24.153 -7.950  -3.705  1.00 48.71  ? 243 LEU A CB  1 
ATOM   1875 C  CG  . LEU A 1 243 ? -23.544 -9.319  -4.019  1.00 52.73  ? 243 LEU A CG  1 
ATOM   1876 C  CD1 . LEU A 1 243 ? -23.640 -10.220 -2.780  1.00 48.54  ? 243 LEU A CD1 1 
ATOM   1877 C  CD2 . LEU A 1 243 ? -24.210 -9.975  -5.219  1.00 43.25  ? 243 LEU A CD2 1 
ATOM   1878 N  N   . VAL A 1 244 ? -25.845 -5.228  -4.469  1.00 50.10  ? 244 VAL A N   1 
ATOM   1879 C  CA  . VAL A 1 244 ? -26.496 -4.074  -3.856  1.00 52.29  ? 244 VAL A CA  1 
ATOM   1880 C  C   . VAL A 1 244 ? -27.842 -4.570  -3.344  1.00 52.68  ? 244 VAL A C   1 
ATOM   1881 O  O   . VAL A 1 244 ? -28.711 -4.933  -4.145  1.00 49.45  ? 244 VAL A O   1 
ATOM   1882 C  CB  . VAL A 1 244 ? -26.682 -2.910  -4.839  1.00 50.88  ? 244 VAL A CB  1 
ATOM   1883 C  CG1 . VAL A 1 244 ? -27.318 -1.718  -4.134  1.00 53.44  ? 244 VAL A CG1 1 
ATOM   1884 C  CG2 . VAL A 1 244 ? -25.352 -2.527  -5.481  1.00 45.92  ? 244 VAL A CG2 1 
ATOM   1885 N  N   . ASP A 1 245 ? -28.018 -4.598  -2.024  1.00 51.80  ? 245 ASP A N   1 
ATOM   1886 C  CA  . ASP A 1 245 ? -29.282 -5.059  -1.468  1.00 52.91  ? 245 ASP A CA  1 
ATOM   1887 C  C   . ASP A 1 245 ? -30.276 -3.899  -1.427  1.00 54.12  ? 245 ASP A C   1 
ATOM   1888 O  O   . ASP A 1 245 ? -29.975 -2.776  -1.837  1.00 56.14  ? 245 ASP A O   1 
ATOM   1889 C  CB  . ASP A 1 245 ? -29.071 -5.701  -0.096  1.00 64.57  ? 245 ASP A CB  1 
ATOM   1890 C  CG  . ASP A 1 245 ? -28.520 -4.743  0.934   1.00 63.69  ? 245 ASP A CG  1 
ATOM   1891 O  OD1 . ASP A 1 245 ? -28.677 -3.515  0.767   1.00 62.88  ? 245 ASP A OD1 1 
ATOM   1892 O  OD2 . ASP A 1 245 ? -27.926 -5.225  1.923   1.00 71.57  ? 245 ASP A OD2 1 
ATOM   1893 N  N   . ALA A 1 246 ? -31.482 -4.175  -0.929  1.00 56.55  ? 246 ALA A N   1 
ATOM   1894 C  CA  . ALA A 1 246 ? -32.553 -3.187  -0.994  1.00 60.76  ? 246 ALA A CA  1 
ATOM   1895 C  C   . ALA A 1 246 ? -32.180 -1.904  -0.260  1.00 62.65  ? 246 ALA A C   1 
ATOM   1896 O  O   . ALA A 1 246 ? -32.526 -0.804  -0.708  1.00 64.99  ? 246 ALA A O   1 
ATOM   1897 C  CB  . ALA A 1 246 ? -33.844 -3.776  -0.418  1.00 63.07  ? 246 ALA A CB  1 
ATOM   1898 N  N   . ASP A 1 247 ? -31.476 -2.021  0.869   1.00 64.43  ? 247 ASP A N   1 
ATOM   1899 C  CA  . ASP A 1 247 ? -31.156 -0.861  1.692   1.00 67.11  ? 247 ASP A CA  1 
ATOM   1900 C  C   . ASP A 1 247 ? -29.903 -0.117  1.239   1.00 62.94  ? 247 ASP A C   1 
ATOM   1901 O  O   . ASP A 1 247 ? -29.623 0.963   1.771   1.00 63.27  ? 247 ASP A O   1 
ATOM   1902 C  CB  . ASP A 1 247 ? -30.990 -1.289  3.153   1.00 69.35  ? 247 ASP A CB  1 
ATOM   1903 C  CG  . ASP A 1 247 ? -32.281 -1.790  3.762   1.00 71.65  ? 247 ASP A CG  1 
ATOM   1904 O  OD1 . ASP A 1 247 ? -33.362 -1.308  3.358   1.00 71.91  ? 247 ASP A OD1 1 
ATOM   1905 O  OD2 . ASP A 1 247 ? -32.217 -2.664  4.648   1.00 76.24  ? 247 ASP A OD2 1 
ATOM   1906 N  N   . GLY A 1 248 ? -29.149 -0.652  0.282   1.00 62.66  ? 248 GLY A N   1 
ATOM   1907 C  CA  . GLY A 1 248 ? -28.001 0.042   -0.254  1.00 61.20  ? 248 GLY A CA  1 
ATOM   1908 C  C   . GLY A 1 248 ? -26.649 -0.442  0.214   1.00 61.88  ? 248 GLY A C   1 
ATOM   1909 O  O   . GLY A 1 248 ? -25.645 0.234   -0.052  1.00 59.30  ? 248 GLY A O   1 
ATOM   1910 N  N   . HIS A 1 249 ? -26.589 -1.580  0.904   1.00 59.42  ? 249 HIS A N   1 
ATOM   1911 C  CA  . HIS A 1 249 ? -25.305 -2.152  1.289   1.00 61.84  ? 249 HIS A CA  1 
ATOM   1912 C  C   . HIS A 1 249 ? -24.651 -2.783  0.062   1.00 59.60  ? 249 HIS A C   1 
ATOM   1913 O  O   . HIS A 1 249 ? -25.241 -3.656  -0.586  1.00 51.24  ? 249 HIS A O   1 
ATOM   1914 C  CB  . HIS A 1 249 ? -25.489 -3.198  2.386   1.00 59.77  ? 249 HIS A CB  1 
ATOM   1915 C  CG  . HIS A 1 249 ? -26.396 -2.767  3.494   1.00 67.57  ? 249 HIS A CG  1 
ATOM   1916 N  ND1 . HIS A 1 249 ? -26.848 -1.472  3.633   1.00 74.01  ? 249 HIS A ND1 1 
ATOM   1917 C  CD2 . HIS A 1 249 ? -26.938 -3.464  4.521   1.00 78.99  ? 249 HIS A CD2 1 
ATOM   1918 C  CE1 . HIS A 1 249 ? -27.633 -1.391  4.692   1.00 72.27  ? 249 HIS A CE1 1 
ATOM   1919 N  NE2 . HIS A 1 249 ? -27.702 -2.585  5.251   1.00 77.76  ? 249 HIS A NE2 1 
ATOM   1920 N  N   . VAL A 1 250 ? -23.436 -2.341  -0.252  1.00 58.63  ? 250 VAL A N   1 
ATOM   1921 C  CA  . VAL A 1 250 ? -22.688 -2.821  -1.410  1.00 57.35  ? 250 VAL A CA  1 
ATOM   1922 C  C   . VAL A 1 250 ? -21.672 -3.859  -0.948  1.00 56.59  ? 250 VAL A C   1 
ATOM   1923 O  O   . VAL A 1 250 ? -21.063 -3.722  0.119   1.00 55.57  ? 250 VAL A O   1 
ATOM   1924 C  CB  . VAL A 1 250 ? -21.986 -1.655  -2.139  1.00 52.56  ? 250 VAL A CB  1 
ATOM   1925 C  CG1 . VAL A 1 250 ? -21.168 -2.171  -3.315  1.00 57.64  ? 250 VAL A CG1 1 
ATOM   1926 C  CG2 . VAL A 1 250 ? -23.004 -0.625  -2.601  1.00 54.18  ? 250 VAL A CG2 1 
ATOM   1927 N  N   . THR A 1 251 ? -21.493 -4.902  -1.757  1.00 58.48  ? 251 THR A N   1 
ATOM   1928 C  CA  . THR A 1 251 ? -20.438 -5.887  -1.557  1.00 51.94  ? 251 THR A CA  1 
ATOM   1929 C  C   . THR A 1 251 ? -19.695 -6.042  -2.876  1.00 52.38  ? 251 THR A C   1 
ATOM   1930 O  O   . THR A 1 251 ? -20.293 -6.432  -3.884  1.00 50.51  ? 251 THR A O   1 
ATOM   1931 C  CB  . THR A 1 251 ? -21.003 -7.229  -1.088  1.00 57.01  ? 251 THR A CB  1 
ATOM   1932 O  OG1 . THR A 1 251 ? -21.881 -7.023  0.033   1.00 50.58  ? 251 THR A OG1 1 
ATOM   1933 C  CG2 . THR A 1 251 ? -19.862 -8.156  -0.676  1.00 48.52  ? 251 THR A CG2 1 
ATOM   1934 N  N   . PHE A 1 252 ? -18.397 -5.745  -2.863  1.00 53.87  ? 252 PHE A N   1 
ATOM   1935 C  CA  . PHE A 1 252 ? -17.560 -5.724  -4.061  1.00 52.59  ? 252 PHE A CA  1 
ATOM   1936 C  C   . PHE A 1 252 ? -16.421 -6.713  -3.856  1.00 47.40  ? 252 PHE A C   1 
ATOM   1937 O  O   . PHE A 1 252 ? -15.517 -6.461  -3.060  1.00 47.56  ? 252 PHE A O   1 
ATOM   1938 C  CB  . PHE A 1 252 ? -17.034 -4.307  -4.308  1.00 51.00  ? 252 PHE A CB  1 
ATOM   1939 C  CG  . PHE A 1 252 ? -16.284 -4.142  -5.594  1.00 47.72  ? 252 PHE A CG  1 
ATOM   1940 C  CD1 . PHE A 1 252 ? -14.967 -4.541  -5.697  1.00 51.02  ? 252 PHE A CD1 1 
ATOM   1941 C  CD2 . PHE A 1 252 ? -16.891 -3.566  -6.694  1.00 49.87  ? 252 PHE A CD2 1 
ATOM   1942 C  CE1 . PHE A 1 252 ? -14.269 -4.381  -6.885  1.00 47.05  ? 252 PHE A CE1 1 
ATOM   1943 C  CE2 . PHE A 1 252 ? -16.199 -3.398  -7.876  1.00 55.89  ? 252 PHE A CE2 1 
ATOM   1944 C  CZ  . PHE A 1 252 ? -14.881 -3.804  -7.968  1.00 47.46  ? 252 PHE A CZ  1 
ATOM   1945 N  N   . THR A 1 253 ? -16.464 -7.832  -4.577  1.00 51.16  ? 253 THR A N   1 
ATOM   1946 C  CA  . THR A 1 253 ? -15.443 -8.871  -4.497  1.00 50.49  ? 253 THR A CA  1 
ATOM   1947 C  C   . THR A 1 253 ? -14.662 -8.909  -5.802  1.00 47.25  ? 253 THR A C   1 
ATOM   1948 O  O   . THR A 1 253 ? -15.239 -8.738  -6.877  1.00 48.45  ? 253 THR A O   1 
ATOM   1949 C  CB  . THR A 1 253 ? -16.074 -10.242 -4.237  1.00 44.15  ? 253 THR A CB  1 
ATOM   1950 O  OG1 . THR A 1 253 ? -16.853 -10.191 -3.042  1.00 56.38  ? 253 THR A OG1 1 
ATOM   1951 C  CG2 . THR A 1 253 ? -15.011 -11.308 -4.096  1.00 50.48  ? 253 THR A CG2 1 
ATOM   1952 N  N   . GLU A 1 254 ? -13.349 -9.132  -5.706  1.00 49.19  ? 254 GLU A N   1 
ATOM   1953 C  CA  . GLU A 1 254 ? -12.495 -9.185  -6.893  1.00 41.90  ? 254 GLU A CA  1 
ATOM   1954 C  C   . GLU A 1 254 ? -11.376 -10.191 -6.646  1.00 40.36  ? 254 GLU A C   1 
ATOM   1955 O  O   . GLU A 1 254 ? -10.473 -9.932  -5.848  1.00 41.76  ? 254 GLU A O   1 
ATOM   1956 C  CB  . GLU A 1 254 ? -11.919 -7.804  -7.220  1.00 41.36  ? 254 GLU A CB  1 
ATOM   1957 C  CG  . GLU A 1 254 ? -11.201 -7.745  -8.563  1.00 40.52  ? 254 GLU A CG  1 
ATOM   1958 C  CD  . GLU A 1 254 ? -10.157 -6.634  -8.635  1.00 48.51  ? 254 GLU A CD  1 
ATOM   1959 O  OE1 . GLU A 1 254 ? -9.261  -6.605  -7.766  1.00 49.60  ? 254 GLU A OE1 1 
ATOM   1960 O  OE2 . GLU A 1 254 ? -10.228 -5.798  -9.561  1.00 51.01  ? 254 GLU A OE2 1 
ATOM   1961 N  N   . ARG A 1 255 ? -11.433 -11.328 -7.343  1.00 39.77  ? 255 ARG A N   1 
ATOM   1962 C  CA  . ARG A 1 255 ? -10.371 -12.332 -7.317  1.00 46.43  ? 255 ARG A CA  1 
ATOM   1963 C  C   . ARG A 1 255 ? -9.480  -12.135 -8.536  1.00 43.16  ? 255 ARG A C   1 
ATOM   1964 O  O   . ARG A 1 255 ? -9.978  -12.062 -9.660  1.00 41.81  ? 255 ARG A O   1 
ATOM   1965 C  CB  . ARG A 1 255 ? -10.967 -13.740 -7.299  1.00 46.14  ? 255 ARG A CB  1 
ATOM   1966 C  CG  . ARG A 1 255 ? -9.962  -14.889 -7.290  1.00 47.20  ? 255 ARG A CG  1 
ATOM   1967 C  CD  . ARG A 1 255 ? -10.642 -16.166 -6.826  1.00 48.51  ? 255 ARG A CD  1 
ATOM   1968 N  NE  . ARG A 1 255 ? -9.889  -17.374 -7.137  1.00 61.45  ? 255 ARG A NE  1 
ATOM   1969 C  CZ  . ARG A 1 255 ? -9.888  -17.977 -8.321  1.00 67.85  ? 255 ARG A CZ  1 
ATOM   1970 N  NH1 . ARG A 1 255 ? -10.536 -17.468 -9.363  1.00 61.74  ? 255 ARG A NH1 1 
ATOM   1971 N  NH2 . ARG A 1 255 ? -9.213  -19.115 -8.469  1.00 74.31  ? 255 ARG A NH2 1 
ATOM   1972 N  N   . SER A 1 256 ? -8.169  -12.049 -8.305  1.00 45.07  ? 256 SER A N   1 
ATOM   1973 C  CA  . SER A 1 256 ? -7.211  -11.685 -9.338  1.00 54.26  ? 256 SER A CA  1 
ATOM   1974 C  C   . SER A 1 256 ? -6.078  -12.698 -9.409  1.00 54.65  ? 256 SER A C   1 
ATOM   1975 O  O   . SER A 1 256 ? -5.561  -13.135 -8.379  1.00 48.75  ? 256 SER A O   1 
ATOM   1976 C  CB  . SER A 1 256 ? -6.618  -10.279 -9.070  1.00 53.72  ? 256 SER A CB  1 
ATOM   1977 O  OG  . SER A 1 256 ? -7.629  -9.286  -9.001  1.00 46.58  ? 256 SER A OG  1 
ATOM   1978 N  N   . MET A 1 257 ? -5.701  -13.059 -10.636 1.00 50.82  ? 257 MET A N   1 
ATOM   1979 C  CA  . MET A 1 257 ? -4.507  -13.862 -10.877 1.00 54.51  ? 257 MET A CA  1 
ATOM   1980 C  C   . MET A 1 257 ? -3.259  -13.028 -10.610 1.00 54.98  ? 257 MET A C   1 
ATOM   1981 O  O   . MET A 1 257 ? -3.164  -11.876 -11.025 1.00 57.16  ? 257 MET A O   1 
ATOM   1982 C  CB  . MET A 1 257 ? -4.523  -14.361 -12.322 1.00 55.08  ? 257 MET A CB  1 
ATOM   1983 C  CG  . MET A 1 257 ? -3.303  -15.132 -12.769 1.00 67.87  ? 257 MET A CG  1 
ATOM   1984 S  SD  . MET A 1 257 ? -3.338  -15.418 -14.563 1.00 72.96  ? 257 MET A SD  1 
ATOM   1985 C  CE  . MET A 1 257 ? -4.526  -16.755 -14.694 1.00 67.04  ? 257 MET A CE  1 
ATOM   1986 N  N   . MET A 1 258 ? -2.295  -13.618 -9.901  1.00 63.60  ? 258 MET A N   1 
ATOM   1987 C  CA  . MET A 1 258 ? -1.135  -12.868 -9.428  1.00 66.34  ? 258 MET A CA  1 
ATOM   1988 C  C   . MET A 1 258 ? 0.183   -13.352 -10.013 1.00 62.85  ? 258 MET A C   1 
ATOM   1989 O  O   . MET A 1 258 ? 0.944   -12.544 -10.557 1.00 79.40  ? 258 MET A O   1 
ATOM   1990 C  CB  . MET A 1 258 ? -1.062  -12.920 -7.882  1.00 55.67  ? 258 MET A CB  1 
ATOM   1991 C  CG  . MET A 1 258 ? -2.233  -12.259 -7.168  1.00 54.23  ? 258 MET A CG  1 
ATOM   1992 S  SD  . MET A 1 258 ? -2.715  -10.641 -7.822  1.00 53.98  ? 258 MET A SD  1 
ATOM   1993 C  CE  . MET A 1 258 ? -1.520  -9.542  -7.078  1.00 48.62  ? 258 MET A CE  1 
ATOM   1994 N  N   . ASP A 1 259 ? 0.490   -14.643 -9.907  1.00 93.65  ? 259 ASP A N   1 
ATOM   1995 C  CA  . ASP A 1 259 ? 1.771   -15.158 -10.373 1.00 104.19 ? 259 ASP A CA  1 
ATOM   1996 C  C   . ASP A 1 259 ? 1.759   -15.556 -11.841 1.00 109.84 ? 259 ASP A C   1 
ATOM   1997 O  O   . ASP A 1 259 ? 2.824   -15.847 -12.397 1.00 114.52 ? 259 ASP A O   1 
ATOM   1998 C  CB  . ASP A 1 259 ? 2.196   -16.368 -9.531  1.00 108.03 ? 259 ASP A CB  1 
ATOM   1999 N  N   . LYS A 1 260 ? 0.592   -15.572 -12.478 1.00 102.14 ? 260 LYS A N   1 
ATOM   2000 C  CA  . LYS A 1 260 ? 0.415   -16.040 -13.847 1.00 109.63 ? 260 LYS A CA  1 
ATOM   2001 C  C   . LYS A 1 260 ? 0.743   -17.521 -13.997 1.00 110.61 ? 260 LYS A C   1 
ATOM   2002 O  O   . LYS A 1 260 ? 0.878   -18.013 -15.125 1.00 110.47 ? 260 LYS A O   1 
ATOM   2003 C  CB  . LYS A 1 260 ? 1.248   -15.207 -14.832 1.00 112.03 ? 260 LYS A CB  1 
ATOM   2004 C  CG  . LYS A 1 260 ? 1.051   -13.689 -14.695 1.00 106.19 ? 260 LYS A CG  1 
ATOM   2005 C  CD  . LYS A 1 260 ? -0.399  -13.333 -14.352 1.00 98.90  ? 260 LYS A CD  1 
ATOM   2006 C  CE  . LYS A 1 260 ? -0.728  -11.869 -14.635 1.00 90.40  ? 260 LYS A CE  1 
ATOM   2007 N  NZ  . LYS A 1 260 ? -0.329  -10.954 -13.522 1.00 86.33  ? 260 LYS A NZ  1 
ATOM   2008 N  N   . ASP A 1 261 ? 0.884   -18.240 -12.884 1.00 107.34 ? 261 ASP A N   1 
ATOM   2009 C  CA  . ASP A 1 261 ? 0.970   -19.693 -12.882 1.00 103.63 ? 261 ASP A CA  1 
ATOM   2010 C  C   . ASP A 1 261 ? -0.365  -20.351 -12.551 1.00 101.78 ? 261 ASP A C   1 
ATOM   2011 O  O   . ASP A 1 261 ? -0.436  -21.584 -12.486 1.00 97.05  ? 261 ASP A O   1 
ATOM   2012 C  CB  . ASP A 1 261 ? 2.045   -20.161 -11.889 1.00 106.32 ? 261 ASP A CB  1 
ATOM   2013 C  CG  . ASP A 1 261 ? 1.768   -19.721 -10.461 1.00 96.19  ? 261 ASP A CG  1 
ATOM   2014 O  OD1 . ASP A 1 261 ? 0.766   -19.011 -10.226 1.00 96.91  ? 261 ASP A OD1 1 
ATOM   2015 O  OD2 . ASP A 1 261 ? 2.560   -20.088 -9.571  1.00 93.73  ? 261 ASP A OD2 1 
ATOM   2016 N  N   . LEU A 1 262 ? -1.422  -19.565 -12.345 1.00 96.07  ? 262 LEU A N   1 
ATOM   2017 C  CA  . LEU A 1 262 ? -2.781  -20.040 -12.103 1.00 90.01  ? 262 LEU A CA  1 
ATOM   2018 C  C   . LEU A 1 262 ? -2.916  -20.768 -10.772 1.00 87.69  ? 262 LEU A C   1 
ATOM   2019 O  O   . LEU A 1 262 ? -3.931  -21.448 -10.541 1.00 86.38  ? 262 LEU A O   1 
ATOM   2020 C  CB  . LEU A 1 262 ? -3.251  -20.940 -13.253 1.00 93.91  ? 262 LEU A CB  1 
ATOM   2021 C  CG  . LEU A 1 262 ? -3.119  -20.275 -14.628 1.00 86.10  ? 262 LEU A CG  1 
ATOM   2022 C  CD1 . LEU A 1 262 ? -1.970  -20.874 -15.433 1.00 98.61  ? 262 LEU A CD1 1 
ATOM   2023 C  CD2 . LEU A 1 262 ? -4.428  -20.365 -15.398 1.00 82.49  ? 262 LEU A CD2 1 
ATOM   2024 N  N   . SER A 1 263 ? -1.936  -20.640 -9.881  1.00 84.25  ? 263 SER A N   1 
ATOM   2025 C  CA  . SER A 1 263 ? -2.018  -21.170 -8.531  1.00 80.68  ? 263 SER A CA  1 
ATOM   2026 C  C   . SER A 1 263 ? -1.953  -20.090 -7.462  1.00 72.49  ? 263 SER A C   1 
ATOM   2027 O  O   . SER A 1 263 ? -2.213  -20.386 -6.291  1.00 73.82  ? 263 SER A O   1 
ATOM   2028 C  CB  . SER A 1 263 ? -0.891  -22.186 -8.289  1.00 81.68  ? 263 SER A CB  1 
ATOM   2029 O  OG  . SER A 1 263 ? 0.335   -21.732 -8.840  1.00 91.18  ? 263 SER A OG  1 
ATOM   2030 N  N   . HIS A 1 264 ? -1.614  -18.857 -7.825  1.00 72.05  ? 264 HIS A N   1 
ATOM   2031 C  CA  . HIS A 1 264 ? -1.534  -17.737 -6.897  1.00 70.69  ? 264 HIS A CA  1 
ATOM   2032 C  C   . HIS A 1 264 ? -2.653  -16.756 -7.225  1.00 59.74  ? 264 HIS A C   1 
ATOM   2033 O  O   . HIS A 1 264 ? -2.667  -16.161 -8.306  1.00 58.98  ? 264 HIS A O   1 
ATOM   2034 C  CB  . HIS A 1 264 ? -0.167  -17.056 -6.980  1.00 75.44  ? 264 HIS A CB  1 
ATOM   2035 C  CG  . HIS A 1 264 ? 0.949   -17.869 -6.398  1.00 82.88  ? 264 HIS A CG  1 
ATOM   2036 N  ND1 . HIS A 1 264 ? 1.903   -17.332 -5.560  1.00 91.28  ? 264 HIS A ND1 1 
ATOM   2037 C  CD2 . HIS A 1 264 ? 1.256   -19.181 -6.525  1.00 84.50  ? 264 HIS A CD2 1 
ATOM   2038 C  CE1 . HIS A 1 264 ? 2.754   -18.278 -5.201  1.00 80.87  ? 264 HIS A CE1 1 
ATOM   2039 N  NE2 . HIS A 1 264 ? 2.382   -19.410 -5.772  1.00 83.98  ? 264 HIS A NE2 1 
ATOM   2040 N  N   . TRP A 1 265 ? -3.581  -16.586 -6.288  1.00 62.92  ? 265 TRP A N   1 
ATOM   2041 C  CA  . TRP A 1 265 ? -4.720  -15.697 -6.449  1.00 54.26  ? 265 TRP A CA  1 
ATOM   2042 C  C   . TRP A 1 265 ? -4.874  -14.839 -5.200  1.00 58.94  ? 265 TRP A C   1 
ATOM   2043 O  O   . TRP A 1 265 ? -4.581  -15.277 -4.080  1.00 54.36  ? 265 TRP A O   1 
ATOM   2044 C  CB  . TRP A 1 265 ? -6.016  -16.492 -6.704  1.00 52.70  ? 265 TRP A CB  1 
ATOM   2045 C  CG  . TRP A 1 265 ? -6.031  -17.245 -8.006  1.00 59.93  ? 265 TRP A CG  1 
ATOM   2046 C  CD1 . TRP A 1 265 ? -5.471  -18.466 -8.258  1.00 57.89  ? 265 TRP A CD1 1 
ATOM   2047 C  CD2 . TRP A 1 265 ? -6.641  -16.823 -9.233  1.00 58.56  ? 265 TRP A CD2 1 
ATOM   2048 N  NE1 . TRP A 1 265 ? -5.693  -18.827 -9.565  1.00 67.40  ? 265 TRP A NE1 1 
ATOM   2049 C  CE2 . TRP A 1 265 ? -6.408  -17.835 -10.185 1.00 58.84  ? 265 TRP A CE2 1 
ATOM   2050 C  CE3 . TRP A 1 265 ? -7.363  -15.686 -9.617  1.00 56.42  ? 265 TRP A CE3 1 
ATOM   2051 C  CZ2 . TRP A 1 265 ? -6.869  -17.746 -11.495 1.00 55.70  ? 265 TRP A CZ2 1 
ATOM   2052 C  CZ3 . TRP A 1 265 ? -7.819  -15.598 -10.917 1.00 55.59  ? 265 TRP A CZ3 1 
ATOM   2053 C  CH2 . TRP A 1 265 ? -7.572  -16.622 -11.842 1.00 63.82  ? 265 TRP A CH2 1 
ATOM   2054 N  N   . GLU A 1 266 ? -5.333  -13.605 -5.403  1.00 48.22  ? 266 GLU A N   1 
ATOM   2055 C  CA  . GLU A 1 266 ? -5.617  -12.680 -4.312  1.00 52.07  ? 266 GLU A CA  1 
ATOM   2056 C  C   . GLU A 1 266 ? -7.029  -12.145 -4.499  1.00 50.85  ? 266 GLU A C   1 
ATOM   2057 O  O   . GLU A 1 266 ? -7.398  -11.730 -5.601  1.00 47.50  ? 266 GLU A O   1 
ATOM   2058 C  CB  . GLU A 1 266 ? -4.601  -11.529 -4.272  1.00 51.62  ? 266 GLU A CB  1 
ATOM   2059 C  CG  . GLU A 1 266 ? -4.796  -10.585 -3.092  1.00 47.05  ? 266 GLU A CG  1 
ATOM   2060 C  CD  . GLU A 1 266 ? -3.696  -9.538  -2.977  1.00 58.07  ? 266 GLU A CD  1 
ATOM   2061 O  OE1 . GLU A 1 266 ? -2.519  -9.843  -3.303  1.00 49.99  ? 266 GLU A OE1 1 
ATOM   2062 O  OE2 . GLU A 1 266 ? -4.014  -8.406  -2.544  1.00 55.40  ? 266 GLU A OE2 1 
ATOM   2063 N  N   . THR A 1 267 ? -7.823  -12.169 -3.430  1.00 44.76  ? 267 THR A N   1 
ATOM   2064 C  CA  . THR A 1 267 ? -9.218  -11.744 -3.485  1.00 52.15  ? 267 THR A CA  1 
ATOM   2065 C  C   . THR A 1 267 ? -9.454  -10.629 -2.479  1.00 43.67  ? 267 THR A C   1 
ATOM   2066 O  O   . THR A 1 267 ? -9.066  -10.747 -1.318  1.00 47.90  ? 267 THR A O   1 
ATOM   2067 C  CB  . THR A 1 267 ? -10.160 -12.915 -3.204  1.00 47.49  ? 267 THR A CB  1 
ATOM   2068 O  OG1 . THR A 1 267 ? -9.785  -14.026 -4.027  1.00 45.23  ? 267 THR A OG1 1 
ATOM   2069 C  CG2 . THR A 1 267 ? -11.604 -12.523 -3.486  1.00 41.38  ? 267 THR A CG2 1 
ATOM   2070 N  N   . ARG A 1 268 ? -10.080 -9.544  -2.937  1.00 44.59  ? 268 ARG A N   1 
ATOM   2071 C  CA  . ARG A 1 268 ? -10.399 -8.399  -2.093  1.00 49.89  ? 268 ARG A CA  1 
ATOM   2072 C  C   . ARG A 1 268 ? -11.904 -8.179  -2.099  1.00 49.75  ? 268 ARG A C   1 
ATOM   2073 O  O   . ARG A 1 268 ? -12.521 -8.115  -3.168  1.00 46.22  ? 268 ARG A O   1 
ATOM   2074 C  CB  . ARG A 1 268 ? -9.676  -7.138  -2.581  1.00 49.07  ? 268 ARG A CB  1 
ATOM   2075 C  CG  . ARG A 1 268 ? -8.159  -7.246  -2.534  1.00 52.04  ? 268 ARG A CG  1 
ATOM   2076 C  CD  . ARG A 1 268 ? -7.483  -5.931  -2.930  1.00 59.19  ? 268 ARG A CD  1 
ATOM   2077 N  NE  . ARG A 1 268 ? -6.027  -6.044  -2.916  1.00 54.96  ? 268 ARG A NE  1 
ATOM   2078 C  CZ  . ARG A 1 268 ? -5.201  -5.109  -3.359  1.00 55.43  ? 268 ARG A CZ  1 
ATOM   2079 N  NH1 . ARG A 1 268 ? -5.655  -3.975  -3.870  1.00 58.08  ? 268 ARG A NH1 1 
ATOM   2080 N  NH2 . ARG A 1 268 ? -3.883  -5.323  -3.292  1.00 48.60  ? 268 ARG A NH2 1 
ATOM   2081 N  N   . THR A 1 269 ? -12.488 -8.065  -0.912  1.00 48.60  ? 269 THR A N   1 
ATOM   2082 C  CA  . THR A 1 269 ? -13.909 -7.776  -0.764  1.00 55.34  ? 269 THR A CA  1 
ATOM   2083 C  C   . THR A 1 269 ? -14.075 -6.505  0.052   1.00 54.96  ? 269 THR A C   1 
ATOM   2084 O  O   . THR A 1 269 ? -13.436 -6.351  1.103   1.00 52.72  ? 269 THR A O   1 
ATOM   2085 C  CB  . THR A 1 269 ? -14.653 -8.933  -0.081  1.00 51.77  ? 269 THR A CB  1 
ATOM   2086 O  OG1 . THR A 1 269 ? -14.531 -10.120 -0.880  1.00 46.12  ? 269 THR A OG1 1 
ATOM   2087 C  CG2 . THR A 1 269 ? -16.123 -8.582  0.091   1.00 50.94  ? 269 THR A CG2 1 
ATOM   2088 N  N   . TYR A 1 270 ? -14.943 -5.615  -0.419  1.00 51.48  ? 270 TYR A N   1 
ATOM   2089 C  CA  . TYR A 1 270 ? -15.252 -4.374  0.285   1.00 56.52  ? 270 TYR A CA  1 
ATOM   2090 C  C   . TYR A 1 270 ? -16.751 -4.315  0.538   1.00 61.87  ? 270 TYR A C   1 
ATOM   2091 O  O   . TYR A 1 270 ? -17.546 -4.403  -0.407  1.00 59.00  ? 270 TYR A O   1 
ATOM   2092 C  CB  . TYR A 1 270 ? -14.800 -3.165  -0.527  1.00 55.99  ? 270 TYR A CB  1 
ATOM   2093 C  CG  . TYR A 1 270 ? -13.320 -3.147  -0.829  1.00 55.25  ? 270 TYR A CG  1 
ATOM   2094 C  CD1 . TYR A 1 270 ? -12.416 -2.579  0.066   1.00 54.46  ? 270 TYR A CD1 1 
ATOM   2095 C  CD2 . TYR A 1 270 ? -12.828 -3.683  -2.005  1.00 46.55  ? 270 TYR A CD2 1 
ATOM   2096 C  CE1 . TYR A 1 270 ? -11.061 -2.555  -0.211  1.00 53.25  ? 270 TYR A CE1 1 
ATOM   2097 C  CE2 . TYR A 1 270 ? -11.477 -3.666  -2.294  1.00 46.93  ? 270 TYR A CE2 1 
ATOM   2098 C  CZ  . TYR A 1 270 ? -10.600 -3.101  -1.399  1.00 53.24  ? 270 TYR A CZ  1 
ATOM   2099 O  OH  . TYR A 1 270 ? -9.254  -3.085  -1.691  1.00 47.87  ? 270 TYR A OH  1 
ATOM   2100 N  N   . GLU A 1 271 ? -17.128 -4.177  1.804   1.00 62.37  ? 271 GLU A N   1 
ATOM   2101 C  CA  . GLU A 1 271 ? -18.516 -4.026  2.221   1.00 60.68  ? 271 GLU A CA  1 
ATOM   2102 C  C   . GLU A 1 271 ? -18.687 -2.609  2.748   1.00 57.42  ? 271 GLU A C   1 
ATOM   2103 O  O   . GLU A 1 271 ? -17.978 -2.199  3.677   1.00 67.76  ? 271 GLU A O   1 
ATOM   2104 C  CB  . GLU A 1 271 ? -18.878 -5.049  3.300   1.00 66.58  ? 271 GLU A CB  1 
ATOM   2105 C  CG  . GLU A 1 271 ? -18.366 -6.459  3.019   1.00 63.03  ? 271 GLU A CG  1 
ATOM   2106 C  CD  . GLU A 1 271 ? -18.773 -7.452  4.090   1.00 66.96  ? 271 GLU A CD  1 
ATOM   2107 O  OE1 . GLU A 1 271 ? -19.704 -7.148  4.868   1.00 72.49  ? 271 GLU A OE1 1 
ATOM   2108 O  OE2 . GLU A 1 271 ? -18.154 -8.535  4.162   1.00 67.19  ? 271 GLU A OE2 1 
ATOM   2109 N  N   . PHE A 1 272 ? -19.620 -1.866  2.159   1.00 57.37  ? 272 PHE A N   1 
ATOM   2110 C  CA  . PHE A 1 272 ? -19.868 -0.480  2.549   1.00 66.33  ? 272 PHE A CA  1 
ATOM   2111 C  C   . PHE A 1 272 ? -21.316 -0.150  2.199   1.00 69.13  ? 272 PHE A C   1 
ATOM   2112 O  O   . PHE A 1 272 ? -22.124 -1.043  1.936   1.00 69.04  ? 272 PHE A O   1 
ATOM   2113 C  CB  . PHE A 1 272 ? -18.862 0.464   1.873   1.00 62.47  ? 272 PHE A CB  1 
ATOM   2114 C  CG  . PHE A 1 272 ? -18.973 0.495   0.376   1.00 60.19  ? 272 PHE A CG  1 
ATOM   2115 C  CD1 . PHE A 1 272 ? -18.250 -0.390  -0.402  1.00 59.11  ? 272 PHE A CD1 1 
ATOM   2116 C  CD2 . PHE A 1 272 ? -19.795 1.419   -0.251  1.00 67.89  ? 272 PHE A CD2 1 
ATOM   2117 C  CE1 . PHE A 1 272 ? -18.348 -0.360  -1.788  1.00 64.15  ? 272 PHE A CE1 1 
ATOM   2118 C  CE2 . PHE A 1 272 ? -19.900 1.452   -1.633  1.00 62.39  ? 272 PHE A CE2 1 
ATOM   2119 C  CZ  . PHE A 1 272 ? -19.174 0.562   -2.400  1.00 61.45  ? 272 PHE A CZ  1 
ATOM   2120 N  N   . THR A 1 273 ? -21.648 1.143   2.203   1.00 72.34  ? 273 THR A N   1 
ATOM   2121 C  CA  . THR A 1 273 ? -23.018 1.591   1.989   1.00 70.02  ? 273 THR A CA  1 
ATOM   2122 C  C   . THR A 1 273 ? -23.031 2.828   1.105   1.00 66.13  ? 273 THR A C   1 
ATOM   2123 O  O   . THR A 1 273 ? -22.119 3.657   1.154   1.00 68.17  ? 273 THR A O   1 
ATOM   2124 C  CB  . THR A 1 273 ? -23.709 1.880   3.330   1.00 71.42  ? 273 THR A CB  1 
ATOM   2125 O  OG1 . THR A 1 273 ? -23.836 0.657   4.071   1.00 70.99  ? 273 THR A OG1 1 
ATOM   2126 C  CG2 . THR A 1 273 ? -25.088 2.500   3.128   1.00 72.74  ? 273 THR A CG2 1 
ATOM   2127 N  N   . LEU A 1 274 ? -24.085 2.943   0.299   1.00 68.54  ? 274 LEU A N   1 
ATOM   2128 C  CA  . LEU A 1 274 ? -24.255 4.096   -0.569  1.00 74.26  ? 274 LEU A CA  1 
ATOM   2129 C  C   . LEU A 1 274 ? -24.655 5.323   0.243   1.00 66.87  ? 274 LEU A C   1 
ATOM   2130 O  O   . LEU A 1 274 ? -25.117 5.225   1.376   1.00 81.68  ? 274 LEU A O   1 
ATOM   2131 C  CB  . LEU A 1 274 ? -25.320 3.823   -1.634  1.00 72.48  ? 274 LEU A CB  1 
ATOM   2132 C  CG  . LEU A 1 274 ? -25.115 2.629   -2.560  1.00 66.55  ? 274 LEU A CG  1 
ATOM   2133 C  CD1 . LEU A 1 274 ? -26.320 2.466   -3.480  1.00 67.43  ? 274 LEU A CD1 1 
ATOM   2134 C  CD2 . LEU A 1 274 ? -23.843 2.778   -3.372  1.00 66.42  ? 274 LEU A CD2 1 
ATOM   2135 N  N   . GLN A 1 275 ? -24.487 6.491   -0.366  1.00 78.90  ? 275 GLN A N   1 
ATOM   2136 C  CA  . GLN A 1 275 ? -24.817 7.751   0.285   1.00 88.55  ? 275 GLN A CA  1 
ATOM   2137 C  C   . GLN A 1 275 ? -26.172 8.273   -0.189  1.00 91.18  ? 275 GLN A C   1 
ATOM   2138 O  O   . GLN A 1 275 ? -27.208 7.990   0.416   1.00 92.60  ? 275 GLN A O   1 
ATOM   2139 C  CB  . GLN A 1 275 ? -23.724 8.787   0.012   1.00 97.36  ? 275 GLN A CB  1 
ATOM   2140 C  CG  . GLN A 1 275 ? -22.318 8.314   0.363   1.00 87.72  ? 275 GLN A CG  1 
ATOM   2141 C  CD  . GLN A 1 275 ? -21.268 9.393   0.157   1.00 94.52  ? 275 GLN A CD  1 
ATOM   2142 O  OE1 . GLN A 1 275 ? -21.008 9.820   -0.971  1.00 95.91  ? 275 GLN A OE1 1 
ATOM   2143 N  NE2 . GLN A 1 275 ? -20.658 9.843   1.250   1.00 94.68  ? 275 GLN A NE2 1 
HETATM 2144 P  P   . PO4 B 2 .   ? -7.680  -0.210  -25.224 1.00 73.28  ? 301 PO4 A P   1 
HETATM 2145 O  O1  . PO4 B 2 .   ? -6.273  0.102   -25.833 1.00 74.76  ? 301 PO4 A O1  1 
HETATM 2146 O  O2  . PO4 B 2 .   ? -8.793  0.405   -26.138 1.00 58.09  ? 301 PO4 A O2  1 
HETATM 2147 O  O3  . PO4 B 2 .   ? -7.870  -1.765  -25.106 1.00 67.91  ? 301 PO4 A O3  1 
HETATM 2148 O  O4  . PO4 B 2 .   ? -7.782  0.423   -23.788 1.00 77.54  ? 301 PO4 A O4  1 
HETATM 2149 CL CL  . CL  C 3 .   ? 1.215   -7.687  -1.672  1.00 88.08  ? 302 CL  A CL  1 
HETATM 2150 O  O   . HOH D 4 .   ? -31.080 -3.816  -33.471 1.00 44.70  ? 401 HOH A O   1 
HETATM 2151 O  O   . HOH D 4 .   ? -7.460  2.404   -22.284 1.00 58.39  ? 402 HOH A O   1 
HETATM 2152 O  O   . HOH D 4 .   ? -13.918 1.477   -19.701 1.00 50.80  ? 403 HOH A O   1 
HETATM 2153 O  O   . HOH D 4 .   ? -12.584 -10.967 -27.160 1.00 44.19  ? 404 HOH A O   1 
HETATM 2154 O  O   . HOH D 4 .   ? -9.674  1.545   -28.278 1.00 58.96  ? 405 HOH A O   1 
HETATM 2155 O  O   . HOH D 4 .   ? -18.180 -22.369 -19.673 1.00 45.91  ? 406 HOH A O   1 
HETATM 2156 O  O   . HOH D 4 .   ? 0.223   -12.341 -22.398 1.00 47.22  ? 407 HOH A O   1 
HETATM 2157 O  O   . HOH D 4 .   ? -1.217  -7.611  -3.132  1.00 52.09  ? 408 HOH A O   1 
HETATM 2158 O  O   . HOH D 4 .   ? -12.949 -23.527 -37.255 1.00 43.37  ? 409 HOH A O   1 
HETATM 2159 O  O   . HOH D 4 .   ? -20.647 -28.153 -20.797 1.00 49.10  ? 410 HOH A O   1 
HETATM 2160 O  O   . HOH D 4 .   ? -21.384 -12.537 -33.081 1.00 51.50  ? 411 HOH A O   1 
HETATM 2161 O  O   . HOH D 4 .   ? -11.919 -24.322 -21.581 1.00 50.24  ? 412 HOH A O   1 
HETATM 2162 O  O   . HOH D 4 .   ? -15.029 -15.145 -20.897 1.00 39.45  ? 413 HOH A O   1 
HETATM 2163 O  O   . HOH D 4 .   ? -26.118 0.308   -28.988 1.00 39.51  ? 414 HOH A O   1 
HETATM 2164 O  O   . HOH D 4 .   ? -13.735 -8.821  -13.357 1.00 44.92  ? 415 HOH A O   1 
HETATM 2165 O  O   . HOH D 4 .   ? -15.249 -14.058 -24.992 1.00 42.12  ? 416 HOH A O   1 
HETATM 2166 O  O   . HOH D 4 .   ? -4.758  -19.568 -19.734 1.00 47.84  ? 417 HOH A O   1 
HETATM 2167 O  O   . HOH D 4 .   ? -28.350 0.982   -27.391 1.00 44.15  ? 418 HOH A O   1 
HETATM 2168 O  O   . HOH D 4 .   ? -19.751 -20.345 -27.119 1.00 41.20  ? 419 HOH A O   1 
HETATM 2169 O  O   . HOH D 4 .   ? -33.352 1.029   -16.275 1.00 50.97  ? 420 HOH A O   1 
HETATM 2170 O  O   . HOH D 4 .   ? -7.314  -0.022  -8.097  1.00 48.03  ? 421 HOH A O   1 
HETATM 2171 O  O   . HOH D 4 .   ? -10.623 -16.995 -13.312 1.00 43.01  ? 422 HOH A O   1 
HETATM 2172 O  O   . HOH D 4 .   ? -8.085  -8.698  -6.250  1.00 44.84  ? 423 HOH A O   1 
HETATM 2173 O  O   . HOH D 4 .   ? -28.846 -8.665  -29.059 1.00 44.10  ? 424 HOH A O   1 
HETATM 2174 O  O   . HOH D 4 .   ? -7.787  -5.258  -10.715 1.00 49.21  ? 425 HOH A O   1 
HETATM 2175 O  O   . HOH D 4 .   ? -11.293 -21.780 -21.437 1.00 38.35  ? 426 HOH A O   1 
HETATM 2176 O  O   . HOH D 4 .   ? -9.965  -23.947 -36.394 1.00 55.05  ? 427 HOH A O   1 
HETATM 2177 O  O   . HOH D 4 .   ? -22.045 -28.065 -15.911 1.00 48.02  ? 428 HOH A O   1 
HETATM 2178 O  O   . HOH D 4 .   ? -24.605 -24.364 -24.729 1.00 56.05  ? 429 HOH A O   1 
HETATM 2179 O  O   . HOH D 4 .   ? -6.984  1.874   -19.800 1.00 54.50  ? 430 HOH A O   1 
HETATM 2180 O  O   . HOH D 4 .   ? -31.351 1.935   -29.924 1.00 51.37  ? 431 HOH A O   1 
HETATM 2181 O  O   . HOH D 4 .   ? -12.482 -5.585  -11.242 1.00 43.54  ? 432 HOH A O   1 
HETATM 2182 O  O   . HOH D 4 .   ? -26.649 -9.711  -31.188 1.00 44.17  ? 433 HOH A O   1 
HETATM 2183 O  O   . HOH D 4 .   ? -22.294 -23.214 -10.853 1.00 54.06  ? 434 HOH A O   1 
HETATM 2184 O  O   . HOH D 4 .   ? -8.828  -4.124  -23.011 1.00 64.61  ? 435 HOH A O   1 
HETATM 2185 O  O   . HOH D 4 .   ? -34.529 -11.686 -13.641 1.00 57.77  ? 436 HOH A O   1 
HETATM 2186 O  O   . HOH D 4 .   ? -20.936 -2.676  -29.446 1.00 37.33  ? 437 HOH A O   1 
HETATM 2187 O  O   . HOH D 4 .   ? -9.814  -20.998 -13.186 1.00 52.79  ? 438 HOH A O   1 
HETATM 2188 O  O   . HOH D 4 .   ? -11.326 -21.065 -8.176  1.00 59.98  ? 439 HOH A O   1 
HETATM 2189 O  O   . HOH D 4 .   ? -9.217  -23.438 -31.455 1.00 42.47  ? 440 HOH A O   1 
HETATM 2190 O  O   . HOH D 4 .   ? -35.080 2.535   -24.069 1.00 47.02  ? 441 HOH A O   1 
HETATM 2191 O  O   . HOH D 4 .   ? -22.443 -12.543 -26.598 1.00 39.12  ? 442 HOH A O   1 
HETATM 2192 O  O   . HOH D 4 .   ? -17.053 -23.411 -33.258 1.00 51.08  ? 443 HOH A O   1 
HETATM 2193 O  O   . HOH D 4 .   ? -10.850 -8.367  -30.661 1.00 46.52  ? 444 HOH A O   1 
HETATM 2194 O  O   . HOH D 4 .   ? -27.963 -2.599  -30.348 1.00 48.91  ? 445 HOH A O   1 
HETATM 2195 O  O   . HOH D 4 .   ? -22.159 -4.706  2.785   1.00 57.23  ? 446 HOH A O   1 
HETATM 2196 O  O   . HOH D 4 .   ? -14.468 -26.232 -15.292 1.00 45.64  ? 447 HOH A O   1 
HETATM 2197 O  O   . HOH D 4 .   ? -7.478  -27.081 -26.637 1.00 52.93  ? 448 HOH A O   1 
HETATM 2198 O  O   . HOH D 4 .   ? -6.734  -24.206 -30.465 1.00 44.52  ? 449 HOH A O   1 
HETATM 2199 O  O   . HOH D 4 .   ? -0.247  -14.550 -26.484 1.00 47.68  ? 450 HOH A O   1 
HETATM 2200 O  O   . HOH D 4 .   ? -9.347  10.855  -25.681 1.00 62.79  ? 451 HOH A O   1 
HETATM 2201 O  O   . HOH D 4 .   ? -9.679  -5.290  -19.852 1.00 65.66  ? 452 HOH A O   1 
HETATM 2202 O  O   . HOH D 4 .   ? -4.797  -14.070 -29.149 1.00 57.56  ? 453 HOH A O   1 
HETATM 2203 O  O   . HOH D 4 .   ? -4.315  -23.498 -32.134 1.00 40.91  ? 454 HOH A O   1 
HETATM 2204 O  O   . HOH D 4 .   ? -11.489 -8.805  -28.119 1.00 49.26  ? 455 HOH A O   1 
HETATM 2205 O  O   . HOH D 4 .   ? -3.707  -18.078 -28.812 1.00 45.06  ? 456 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 
10   N N   . ILE A 3   ? 0.6520 0.6578 0.6005 -0.0867 -0.0114 -0.0011 3   ILE A N   
11   C CA  . ILE A 3   ? 0.5884 0.5807 0.5256 -0.0910 -0.0197 -0.0091 3   ILE A CA  
12   C C   . ILE A 3   ? 0.5522 0.5486 0.5033 -0.1070 -0.0210 -0.0150 3   ILE A C   
13   O O   . ILE A 3   ? 0.5398 0.5423 0.4947 -0.1120 -0.0212 -0.0161 3   ILE A O   
14   C CB  . ILE A 3   ? 0.5725 0.5488 0.4869 -0.0851 -0.0272 -0.0134 3   ILE A CB  
15   C CG1 . ILE A 3   ? 0.5630 0.5292 0.4756 -0.0925 -0.0347 -0.0241 3   ILE A CG1 
16   C CG2 . ILE A 3   ? 0.5869 0.5610 0.4968 -0.0877 -0.0273 -0.0122 3   ILE A CG2 
17   C CD1 . ILE A 3   ? 0.6718 0.6171 0.5659 -0.0887 -0.0415 -0.0316 3   ILE A CD1 
18   N N   . ILE A 4   ? 0.5469 0.5421 0.5035 -0.1115 -0.0221 -0.0195 4   ILE A N   
19   C CA  . ILE A 4   ? 0.5926 0.5924 0.5613 -0.1233 -0.0210 -0.0246 4   ILE A CA  
20   C C   . ILE A 4   ? 0.5847 0.5822 0.5528 -0.1281 -0.0251 -0.0314 4   ILE A C   
21   O O   . ILE A 4   ? 0.5347 0.5332 0.5017 -0.1219 -0.0297 -0.0346 4   ILE A O   
22   C CB  . ILE A 4   ? 0.5789 0.5833 0.5627 -0.1236 -0.0146 -0.0231 4   ILE A CB  
23   C CG1 . ILE A 4   ? 0.5232 0.5317 0.5171 -0.1229 -0.0082 -0.0177 4   ILE A CG1 
24   C CG2 . ILE A 4   ? 0.5295 0.5372 0.5223 -0.1331 -0.0139 -0.0304 4   ILE A CG2 
25   C CD1 . ILE A 4   ? 0.5482 0.5526 0.5580 -0.1239 0.0022  -0.0145 4   ILE A CD1 
26   N N   . PHE A 5   ? 0.5821 0.5789 0.5520 -0.1380 -0.0228 -0.0341 5   PHE A N   
27   C CA  . PHE A 5   ? 0.5922 0.5916 0.5708 -0.1461 -0.0221 -0.0400 5   PHE A CA  
28   C C   . PHE A 5   ? 0.5257 0.5346 0.5130 -0.1505 -0.0158 -0.0413 5   PHE A C   
29   O O   . PHE A 5   ? 0.5416 0.5487 0.5215 -0.1502 -0.0130 -0.0393 5   PHE A O   
30   C CB  . PHE A 5   ? 0.5979 0.5819 0.5680 -0.1530 -0.0196 -0.0396 5   PHE A CB  
31   C CG  . PHE A 5   ? 0.6047 0.5736 0.5612 -0.1467 -0.0256 -0.0397 5   PHE A CG  
32   C CD1 . PHE A 5   ? 0.5566 0.5266 0.5189 -0.1454 -0.0338 -0.0489 5   PHE A CD1 
33   C CD2 . PHE A 5   ? 0.6486 0.6045 0.5853 -0.1393 -0.0242 -0.0323 5   PHE A CD2 
34   C CE1 . PHE A 5   ? 0.6361 0.5900 0.5818 -0.1371 -0.0398 -0.0511 5   PHE A CE1 
35   C CE2 . PHE A 5   ? 0.6156 0.5565 0.5373 -0.1306 -0.0287 -0.0325 5   PHE A CE2 
36   C CZ  . PHE A 5   ? 0.6761 0.6137 0.6009 -0.1298 -0.0361 -0.0420 5   PHE A CZ  
37   N N   . PHE A 6   ? 0.4952 0.5168 0.4981 -0.1524 -0.0148 -0.0466 6   PHE A N   
38   C CA  . PHE A 6   ? 0.5423 0.5720 0.5509 -0.1539 -0.0077 -0.0483 6   PHE A CA  
39   C C   . PHE A 6   ? 0.5785 0.6260 0.6068 -0.1573 -0.0047 -0.0538 6   PHE A C   
40   O O   . PHE A 6   ? 0.5624 0.6225 0.6031 -0.1524 -0.0118 -0.0588 6   PHE A O   
41   C CB  . PHE A 6   ? 0.4439 0.4723 0.4523 -0.1461 -0.0082 -0.0486 6   PHE A CB  
42   C CG  . PHE A 6   ? 0.5081 0.5411 0.5241 -0.1363 -0.0110 -0.0488 6   PHE A CG  
43   C CD1 . PHE A 6   ? 0.5498 0.5956 0.5765 -0.1309 -0.0089 -0.0532 6   PHE A CD1 
44   C CD2 . PHE A 6   ? 0.4880 0.5129 0.4974 -0.1285 -0.0141 -0.0434 6   PHE A CD2 
45   C CE1 . PHE A 6   ? 0.5831 0.6329 0.6114 -0.1161 -0.0119 -0.0524 6   PHE A CE1 
46   C CE2 . PHE A 6   ? 0.5439 0.5704 0.5528 -0.1141 -0.0150 -0.0413 6   PHE A CE2 
47   C CZ  . PHE A 6   ? 0.5757 0.6141 0.5927 -0.1069 -0.0147 -0.0459 6   PHE A CZ  
48   N N   . LYS A 7   ? 0.5898 0.6411 0.6206 -0.1636 0.0061  -0.0529 7   LYS A N   
49   C CA  . LYS A 7   ? 0.5254 0.5995 0.5798 -0.1669 0.0129  -0.0576 7   LYS A CA  
50   C C   . LYS A 7   ? 0.5023 0.5839 0.5538 -0.1563 0.0173  -0.0593 7   LYS A C   
51   O O   . LYS A 7   ? 0.5456 0.6128 0.5765 -0.1525 0.0202  -0.0573 7   LYS A O   
52   C CB  . LYS A 7   ? 0.5411 0.6132 0.6010 -0.1796 0.0275  -0.0534 7   LYS A CB  
53   C CG  . LYS A 7   ? 0.5046 0.6060 0.5963 -0.1847 0.0380  -0.0578 7   LYS A CG  
54   C CD  . LYS A 7   ? 0.6332 0.7281 0.7287 -0.1972 0.0595  -0.0494 7   LYS A CD  
55   C CE  . LYS A 7   ? 0.7328 0.8120 0.8397 -0.2138 0.0601  -0.0496 7   LYS A CE  
56   N NZ  . LYS A 7   ? 0.8773 0.9763 1.0275 -0.2321 0.0758  -0.0530 7   LYS A NZ  
57   N N   . PHE A 8   ? 0.5194 0.6244 0.5916 -0.1501 0.0167  -0.0651 8   PHE A N   
58   C CA  . PHE A 8   ? 0.5604 0.6676 0.6281 -0.1357 0.0189  -0.0677 8   PHE A CA  
59   C C   . PHE A 8   ? 0.5719 0.7112 0.6638 -0.1324 0.0270  -0.0721 8   PHE A C   
60   O O   . PHE A 8   ? 0.5958 0.7624 0.7137 -0.1318 0.0211  -0.0775 8   PHE A O   
61   C CB  . PHE A 8   ? 0.6477 0.7454 0.7099 -0.1232 0.0083  -0.0677 8   PHE A CB  
62   C CG  . PHE A 8   ? 0.5689 0.6752 0.6354 -0.1054 0.0100  -0.0708 8   PHE A CG  
63   C CD1 . PHE A 8   ? 0.6377 0.7346 0.6955 -0.0990 0.0190  -0.0729 8   PHE A CD1 
64   C CD2 . PHE A 8   ? 0.6774 0.7995 0.7525 -0.0912 0.0018  -0.0722 8   PHE A CD2 
65   C CE1 . PHE A 8   ? 0.6709 0.7708 0.7296 -0.0798 0.0217  -0.0753 8   PHE A CE1 
66   C CE2 . PHE A 8   ? 0.6698 0.7982 0.7447 -0.0699 0.0038  -0.0735 8   PHE A CE2 
67   C CZ  . PHE A 8   ? 0.6385 0.7538 0.7056 -0.0646 0.0147  -0.0743 8   PHE A CZ  
68   N N   . ASP A 9   ? 0.6404 0.7798 0.7241 -0.1289 0.0402  -0.0713 9   ASP A N   
69   C CA  . ASP A 9   ? 0.6242 0.7961 0.7308 -0.1255 0.0527  -0.0737 9   ASP A CA  
70   C C   . ASP A 9   ? 0.6910 0.8556 0.7788 -0.1072 0.0590  -0.0765 9   ASP A C   
71   O O   . ASP A 9   ? 0.6808 0.8311 0.7454 -0.1057 0.0690  -0.0748 9   ASP A O   
72   C CB  . ASP A 9   ? 0.6075 0.7860 0.7224 -0.1411 0.0694  -0.0672 9   ASP A CB  
73   C CG  . ASP A 9   ? 0.6899 0.9092 0.8403 -0.1415 0.0849  -0.0690 9   ASP A CG  
74   O OD1 . ASP A 9   ? 0.6532 0.9030 0.8279 -0.1307 0.0780  -0.0775 9   ASP A OD1 
75   O OD2 . ASP A 9   ? 0.8001 1.0220 0.9539 -0.1507 0.1056  -0.0609 9   ASP A OD2 
76   N N   . PRO A 10  ? 0.7105 0.8822 0.8038 -0.0901 0.0531  -0.0816 10  PRO A N   
77   C CA  . PRO A 10  ? 0.7444 0.8991 0.8162 -0.0718 0.0587  -0.0858 10  PRO A CA  
78   C C   . PRO A 10  ? 0.7435 0.9232 0.8211 -0.0631 0.0754  -0.0874 10  PRO A C   
79   O O   . PRO A 10  ? 0.7840 0.9440 0.8353 -0.0510 0.0818  -0.0918 10  PRO A O   
80   C CB  . PRO A 10  ? 0.7443 0.8965 0.8196 -0.0539 0.0498  -0.0878 10  PRO A CB  
81   C CG  . PRO A 10  ? 0.6699 0.8620 0.7773 -0.0571 0.0425  -0.0876 10  PRO A CG  
82   C CD  . PRO A 10  ? 0.6359 0.8287 0.7509 -0.0832 0.0409  -0.0844 10  PRO A CD  
83   N N   . ARG A 11  ? 0.7489 0.9724 0.8619 -0.0689 0.0832  -0.0855 11  ARG A N   
84   C CA  . ARG A 11  ? 0.8260 1.0793 0.9506 -0.0612 0.1034  -0.0848 11  ARG A CA  
85   C C   . ARG A 11  ? 0.7831 1.0447 0.9172 -0.0822 0.1192  -0.0758 11  ARG A C   
86   O O   . ARG A 11  ? 0.7532 1.0545 0.9311 -0.0943 0.1285  -0.0741 11  ARG A O   
87   C CB  . ARG A 11  ? 0.8384 1.1423 1.0043 -0.0491 0.1034  -0.0902 11  ARG A CB  
88   C CG  . ARG A 11  ? 0.8861 1.1791 1.0375 -0.0217 0.0917  -0.0963 11  ARG A CG  
89   C CD  . ARG A 11  ? 0.9652 1.2633 1.1037 0.0043  0.1063  -0.0995 11  ARG A CD  
90   N NE  . ARG A 11  ? 1.0782 1.4399 1.2603 0.0148  0.1153  -0.1021 11  ARG A NE  
91   C CZ  . ARG A 11  ? 0.9464 1.3449 1.1524 0.0080  0.1366  -0.0989 11  ARG A CZ  
92   N NH1 . ARG A 11  ? 0.8935 1.2681 1.0769 -0.0057 0.1520  -0.0915 11  ARG A NH1 
93   N NH2 . ARG A 11  ? 0.8483 1.3109 1.1023 0.0171  0.1438  -0.1029 11  ARG A NH2 
94   N N   . PRO A 12  ? 0.8325 1.0575 0.9278 -0.0864 0.1231  -0.0701 12  PRO A N   
95   C CA  . PRO A 12  ? 0.8599 1.0849 0.9568 -0.1026 0.1407  -0.0580 12  PRO A CA  
96   C C   . PRO A 12  ? 0.8978 1.1569 1.0152 -0.0983 0.1694  -0.0517 12  PRO A C   
97   O O   . PRO A 12  ? 0.7419 1.0085 0.8434 -0.0763 0.1785  -0.0548 12  PRO A O   
98   C CB  . PRO A 12  ? 0.8584 1.0403 0.9005 -0.0964 0.1376  -0.0554 12  PRO A CB  
99   C CG  . PRO A 12  ? 0.8628 1.0301 0.8803 -0.0764 0.1249  -0.0686 12  PRO A CG  
100  C CD  . PRO A 12  ? 0.7848 0.9676 0.8343 -0.0755 0.1117  -0.0756 12  PRO A CD  
101  N N   . VAL A 13  ? 0.9798 1.2580 1.1340 -0.1198 0.1854  -0.0429 13  VAL A N   
102  C CA  . VAL A 13  ? 0.9411 1.2578 1.1281 -0.1204 0.2163  -0.0358 13  VAL A CA  
103  C C   . VAL A 13  ? 0.9717 1.2660 1.1131 -0.1078 0.2444  -0.0201 13  VAL A C   
104  O O   . VAL A 13  ? 0.9392 1.2620 1.0922 -0.0971 0.2716  -0.0141 13  VAL A O   
105  C CB  . VAL A 13  ? 0.9753 1.3190 1.2245 -0.1516 0.2259  -0.0334 13  VAL A CB  
106  C CG1 . VAL A 13  ? 0.8975 1.2604 1.1831 -0.1612 0.1937  -0.0511 13  VAL A CG1 
107  C CG2 . VAL A 13  ? 0.9960 1.2971 1.2232 -0.1694 0.2404  -0.0174 13  VAL A CG2 
108  N N   . SER A 14  ? 0.9777 1.2242 1.0658 -0.1056 0.2389  -0.0135 14  SER A N   
109  C CA  . SER A 14  ? 0.9797 1.2036 1.0174 -0.0896 0.2638  0.0017  14  SER A CA  
110  C C   . SER A 14  ? 1.0818 1.2713 1.0533 -0.0654 0.2427  -0.0080 14  SER A C   
111  O O   . SER A 14  ? 0.9947 1.1777 0.9654 -0.0636 0.2125  -0.0255 14  SER A O   
112  C CB  . SER A 14  ? 1.0566 1.2571 1.0930 -0.1085 0.2831  0.0214  14  SER A CB  
113  O OG  . SER A 14  ? 1.0131 1.1827 1.0369 -0.1201 0.2557  0.0166  14  SER A OG  
114  N N   . LYS A 15  ? 1.0990 1.2663 1.0154 -0.0463 0.2594  0.0030  15  LYS A N   
115  C CA  . LYS A 15  ? 1.0642 1.2061 0.9194 -0.0208 0.2394  -0.0107 15  LYS A CA  
116  C C   . LYS A 15  ? 1.0641 1.1751 0.8960 -0.0286 0.2141  -0.0138 15  LYS A C   
117  O O   . LYS A 15  ? 1.1574 1.2562 0.9712 -0.0219 0.1848  -0.0336 15  LYS A O   
118  C CB  . LYS A 15  ? 1.1132 1.2494 0.9145 0.0092  0.2661  -0.0002 15  LYS A CB  
119  N N   . ASN A 16  ? 1.0912 1.1886 0.9246 -0.0424 0.2261  0.0051  16  ASN A N   
120  C CA  . ASN A 16  ? 1.0702 1.1400 0.8783 -0.0455 0.2049  0.0042  16  ASN A CA  
121  C C   . ASN A 16  ? 1.0181 1.0883 0.8740 -0.0752 0.1887  0.0019  16  ASN A C   
122  O O   . ASN A 16  ? 0.9448 0.9934 0.7860 -0.0801 0.1767  0.0054  16  ASN A O   
123  C CB  . ASN A 16  ? 1.2599 1.3056 1.0231 -0.0330 0.2284  0.0274  16  ASN A CB  
124  C CG  . ASN A 16  ? 1.2780 1.3215 1.0770 -0.0550 0.2612  0.0512  16  ASN A CG  
125  O OD1 . ASN A 16  ? 1.1988 1.2660 1.0596 -0.0797 0.2648  0.0476  16  ASN A OD1 
126  N ND2 . ASN A 16  ? 1.3362 1.3505 1.0970 -0.0455 0.2852  0.0747  16  ASN A ND2 
127  N N   . ALA A 17  ? 0.9162 1.0121 0.8260 -0.0916 0.1877  -0.0045 17  ALA A N   
128  C CA  . ALA A 17  ? 0.8251 0.9234 0.7742 -0.1141 0.1678  -0.0110 17  ALA A CA  
129  C C   . ALA A 17  ? 0.6689 0.7559 0.6021 -0.1079 0.1357  -0.0276 17  ALA A C   
130  O O   . ALA A 17  ? 0.7507 0.8329 0.6542 -0.0898 0.1277  -0.0383 17  ALA A O   
131  C CB  . ALA A 17  ? 0.7653 0.8993 0.7723 -0.1271 0.1723  -0.0163 17  ALA A CB  
132  N N   . TYR A 18  ? 0.6506 0.7326 0.6051 -0.1233 0.1184  -0.0306 18  TYR A N   
133  C CA  . TYR A 18  ? 0.7243 0.7955 0.6701 -0.1207 0.0922  -0.0431 18  TYR A CA  
134  C C   . TYR A 18  ? 0.6712 0.7577 0.6515 -0.1252 0.0812  -0.0529 18  TYR A C   
135  O O   . TYR A 18  ? 0.6458 0.7479 0.6599 -0.1370 0.0828  -0.0504 18  TYR A O   
136  C CB  . TYR A 18  ? 0.6668 0.7193 0.6042 -0.1293 0.0820  -0.0376 18  TYR A CB  
137  C CG  . TYR A 18  ? 0.6674 0.7018 0.5626 -0.1182 0.0891  -0.0284 18  TYR A CG  
138  C CD1 . TYR A 18  ? 0.6415 0.6708 0.5031 -0.1016 0.0763  -0.0381 18  TYR A CD1 
139  C CD2 . TYR A 18  ? 0.7121 0.7340 0.6015 -0.1233 0.1085  -0.0109 18  TYR A CD2 
140  C CE1 . TYR A 18  ? 0.7427 0.7593 0.5616 -0.0860 0.0803  -0.0307 18  TYR A CE1 
141  C CE2 . TYR A 18  ? 0.6714 0.6732 0.5159 -0.1080 0.1165  0.0002  18  TYR A CE2 
142  C CZ  . TYR A 18  ? 0.8166 0.8182 0.6238 -0.0871 0.1012  -0.0097 18  TYR A CZ  
143  O OH  . TYR A 18  ? 0.8134 0.7989 0.5716 -0.0664 0.1069  0.0004  18  TYR A OH  
144  N N   . ARG A 19  ? 0.6363 0.7171 0.6070 -0.1144 0.0701  -0.0651 19  ARG A N   
145  C CA  . ARG A 19  ? 0.6001 0.6856 0.5945 -0.1149 0.0593  -0.0718 19  ARG A CA  
146  C C   . ARG A 19  ? 0.6073 0.6806 0.6076 -0.1250 0.0445  -0.0701 19  ARG A C   
147  O O   . ARG A 19  ? 0.6091 0.6889 0.6296 -0.1260 0.0381  -0.0704 19  ARG A O   
148  C CB  . ARG A 19  ? 0.6237 0.6975 0.6046 -0.1006 0.0555  -0.0842 19  ARG A CB  
149  C CG  . ARG A 19  ? 0.7160 0.8037 0.6922 -0.0862 0.0700  -0.0871 19  ARG A CG  
150  C CD  . ARG A 19  ? 0.7787 0.8460 0.7236 -0.0723 0.0671  -0.1010 19  ARG A CD  
151  N NE  . ARG A 19  ? 0.7127 0.7587 0.6619 -0.0695 0.0558  -0.1125 19  ARG A NE  
152  C CZ  . ARG A 19  ? 0.7827 0.8055 0.7121 -0.0614 0.0502  -0.1292 19  ARG A CZ  
153  N NH1 . ARG A 19  ? 0.8705 0.8918 0.7703 -0.0520 0.0513  -0.1386 19  ARG A NH1 
154  N NH2 . ARG A 19  ? 0.7110 0.7095 0.6492 -0.0617 0.0440  -0.1374 19  ARG A NH2 
155  N N   . LEU A 20  ? 0.5634 0.6213 0.5443 -0.1290 0.0390  -0.0681 20  LEU A N   
156  C CA  . LEU A 20  ? 0.4583 0.5065 0.4437 -0.1364 0.0269  -0.0659 20  LEU A CA  
157  C C   . LEU A 20  ? 0.6293 0.6690 0.5963 -0.1399 0.0267  -0.0591 20  LEU A C   
158  O O   . LEU A 20  ? 0.6482 0.6833 0.5906 -0.1324 0.0282  -0.0611 20  LEU A O   
159  C CB  . LEU A 20  ? 0.5523 0.5880 0.5363 -0.1331 0.0170  -0.0749 20  LEU A CB  
160  C CG  . LEU A 20  ? 0.6411 0.6693 0.6330 -0.1390 0.0081  -0.0711 20  LEU A CG  
161  C CD1 . LEU A 20  ? 0.4777 0.5122 0.4851 -0.1396 0.0079  -0.0642 20  LEU A CD1 
162  C CD2 . LEU A 20  ? 0.6667 0.6820 0.6631 -0.1385 0.0036  -0.0794 20  LEU A CD2 
163  N N   . ILE A 21  ? 0.5262 0.5631 0.5020 -0.1482 0.0244  -0.0520 21  ILE A N   
164  C CA  . ILE A 21  ? 0.5449 0.5687 0.5026 -0.1492 0.0226  -0.0451 21  ILE A CA  
165  C C   . ILE A 21  ? 0.5621 0.5822 0.5291 -0.1521 0.0103  -0.0456 21  ILE A C   
166  O O   . ILE A 21  ? 0.6051 0.6280 0.5890 -0.1572 0.0086  -0.0449 21  ILE A O   
167  C CB  . ILE A 21  ? 0.5262 0.5433 0.4826 -0.1556 0.0363  -0.0347 21  ILE A CB  
168  C CG1 . ILE A 21  ? 0.6247 0.6472 0.5738 -0.1518 0.0537  -0.0311 21  ILE A CG1 
169  C CG2 . ILE A 21  ? 0.5996 0.5966 0.5316 -0.1524 0.0353  -0.0264 21  ILE A CG2 
170  C CD1 . ILE A 21  ? 0.6914 0.7071 0.6483 -0.1618 0.0731  -0.0197 21  ILE A CD1 
171  N N   . LEU A 22  ? 0.5289 0.5457 0.4857 -0.1474 0.0017  -0.0481 22  LEU A N   
172  C CA  . LEU A 22  ? 0.5210 0.5366 0.4874 -0.1483 -0.0066 -0.0475 22  LEU A CA  
173  C C   . LEU A 22  ? 0.5704 0.5818 0.5212 -0.1438 -0.0111 -0.0433 22  LEU A C   
174  O O   . LEU A 22  ? 0.6389 0.6530 0.5734 -0.1373 -0.0128 -0.0456 22  LEU A O   
175  C CB  . LEU A 22  ? 0.5222 0.5420 0.5025 -0.1480 -0.0102 -0.0552 22  LEU A CB  
176  C CG  . LEU A 22  ? 0.5543 0.5723 0.5468 -0.1482 -0.0131 -0.0516 22  LEU A CG  
177  C CD1 . LEU A 22  ? 0.5559 0.5693 0.5633 -0.1479 -0.0090 -0.0540 22  LEU A CD1 
178  C CD2 . LEU A 22  ? 0.4786 0.5026 0.4721 -0.1479 -0.0184 -0.0538 22  LEU A CD2 
179  N N   . ALA A 23  ? 0.5654 0.5714 0.5187 -0.1438 -0.0138 -0.0379 23  ALA A N   
180  C CA  . ALA A 23  ? 0.5727 0.5743 0.5113 -0.1365 -0.0176 -0.0331 23  ALA A CA  
181  C C   . ALA A 23  ? 0.6210 0.6261 0.5713 -0.1347 -0.0215 -0.0314 23  ALA A C   
182  O O   . ALA A 23  ? 0.5185 0.5161 0.4720 -0.1360 -0.0208 -0.0293 23  ALA A O   
183  C CB  . ALA A 23  ? 0.6040 0.5852 0.5235 -0.1356 -0.0116 -0.0253 23  ALA A CB  
184  N N   . ALA A 24  ? 0.5920 0.6109 0.5493 -0.1305 -0.0255 -0.0332 24  ALA A N   
185  C CA  . ALA A 24  ? 0.4801 0.5049 0.4521 -0.1286 -0.0245 -0.0299 24  ALA A CA  
186  C C   . ALA A 24  ? 0.5478 0.5846 0.5174 -0.1194 -0.0278 -0.0275 24  ALA A C   
187  O O   . ALA A 24  ? 0.6230 0.6745 0.5916 -0.1162 -0.0334 -0.0333 24  ALA A O   
188  C CB  . ALA A 24  ? 0.5059 0.5393 0.5037 -0.1363 -0.0209 -0.0349 24  ALA A CB  
189  N N   . ASN A 25  ? 0.4793 0.5126 0.4465 -0.1120 -0.0249 -0.0200 25  ASN A N   
190  C CA  . ASN A 25  ? 0.4828 0.5322 0.4530 -0.1013 -0.0255 -0.0167 25  ASN A CA  
191  C C   . ASN A 25  ? 0.5416 0.6063 0.5404 -0.1041 -0.0169 -0.0134 25  ASN A C   
192  O O   . ASN A 25  ? 0.6140 0.6648 0.6120 -0.1046 -0.0096 -0.0077 25  ASN A O   
193  C CB  . ASN A 25  ? 0.5755 0.6060 0.5169 -0.0871 -0.0260 -0.0097 25  ASN A CB  
194  C CG  . ASN A 25  ? 0.6028 0.6159 0.5170 -0.0824 -0.0302 -0.0101 25  ASN A CG  
195  O OD1 . ASN A 25  ? 0.5297 0.5525 0.4436 -0.0838 -0.0335 -0.0141 25  ASN A OD1 
196  N ND2 . ASN A 25  ? 0.6134 0.5979 0.5027 -0.0753 -0.0292 -0.0062 25  ASN A ND2 
197  N N   . ARG A 26  ? 0.5076 0.6017 0.5322 -0.1047 -0.0167 -0.0170 26  ARG A N   
198  C CA  . ARG A 26  ? 0.5562 0.6662 0.6133 -0.1082 -0.0039 -0.0118 26  ARG A CA  
199  C C   . ARG A 26  ? 0.6022 0.7277 0.6547 -0.0912 -0.0008 -0.0036 26  ARG A C   
200  O O   . ARG A 26  ? 0.5990 0.7510 0.6583 -0.0848 -0.0091 -0.0097 26  ARG A O   
201  C CB  . ARG A 26  ? 0.6235 0.7592 0.7242 -0.1250 -0.0041 -0.0247 26  ARG A CB  
202  C CG  . ARG A 26  ? 0.6951 0.8373 0.8346 -0.1346 0.0152  -0.0180 26  ARG A CG  
203  C CD  . ARG A 26  ? 0.6846 0.8706 0.8664 -0.1367 0.0182  -0.0224 26  ARG A CD  
204  N NE  . ARG A 26  ? 0.7901 1.0077 0.9931 -0.1442 -0.0005 -0.0450 26  ARG A NE  
205  C CZ  . ARG A 26  ? 0.6842 0.9495 0.9293 -0.1467 -0.0044 -0.0562 26  ARG A CZ  
206  N NH1 . ARG A 26  ? 0.6946 0.9825 0.9704 -0.1450 0.0123  -0.0454 26  ARG A NH1 
207  N NH2 . ARG A 26  ? 0.6093 0.9035 0.8664 -0.1493 -0.0255 -0.0795 26  ARG A NH2 
208  N N   . ASP A 27  ? 0.5482 0.6581 0.5855 -0.0803 0.0103  0.0095  27  ASP A N   
209  C CA  . ASP A 27  ? 0.5667 0.6890 0.5973 -0.0612 0.0165  0.0184  27  ASP A CA  
210  C C   . ASP A 27  ? 0.5875 0.7356 0.6596 -0.0657 0.0360  0.0264  27  ASP A C   
211  O O   . ASP A 27  ? 0.5069 0.6402 0.5880 -0.0733 0.0502  0.0339  27  ASP A O   
212  C CB  . ASP A 27  ? 0.5405 0.6295 0.5261 -0.0438 0.0169  0.0259  27  ASP A CB  
213  C CG  . ASP A 27  ? 0.5809 0.6414 0.5339 -0.0449 0.0011  0.0174  27  ASP A CG  
214  O OD1 . ASP A 27  ? 0.5954 0.6617 0.5530 -0.0532 -0.0082 0.0096  27  ASP A OD1 
215  O OD2 . ASP A 27  ? 0.6281 0.6609 0.5516 -0.0372 -0.0014 0.0178  27  ASP A OD2 
216  N N   . GLU A 28  ? 0.5079 0.6948 0.6066 -0.0603 0.0384  0.0255  28  GLU A N   
217  C CA  . GLU A 28  ? 0.4853 0.7032 0.6343 -0.0679 0.0595  0.0322  28  GLU A CA  
218  C C   . GLU A 28  ? 0.4532 0.7122 0.6156 -0.0506 0.0610  0.0339  28  GLU A C   
219  O O   . GLU A 28  ? 0.4858 0.7510 0.6231 -0.0354 0.0428  0.0268  28  GLU A O   
220  C CB  . GLU A 28  ? 0.5776 0.8138 0.7794 -0.0973 0.0586  0.0178  28  GLU A CB  
221  C CG  . GLU A 28  ? 0.6177 0.8818 0.8813 -0.1120 0.0837  0.0232  28  GLU A CG  
222  C CD  . GLU A 28  ? 0.6490 0.8782 0.9005 -0.1080 0.1128  0.0468  28  GLU A CD  
223  O OE1 . GLU A 28  ? 0.7047 0.8944 0.9393 -0.1160 0.1150  0.0488  28  GLU A OE1 
224  O OE2 . GLU A 28  ? 0.5838 0.8260 0.8399 -0.0933 0.1341  0.0641  28  GLU A OE2 
225  N N   . PHE A 29  ? 0.4984 0.7843 0.6996 -0.0510 0.0853  0.0452  29  PHE A N   
226  C CA  . PHE A 29  ? 0.5485 0.8853 0.7762 -0.0366 0.0887  0.0454  29  PHE A CA  
227  C C   . PHE A 29  ? 0.5316 0.9165 0.8045 -0.0506 0.0683  0.0220  29  PHE A C   
228  O O   . PHE A 29  ? 0.4426 0.8373 0.7587 -0.0791 0.0664  0.0086  29  PHE A O   
229  C CB  . PHE A 29  ? 0.5437 0.9032 0.8131 -0.0379 0.1233  0.0628  29  PHE A CB  
230  C CG  . PHE A 29  ? 0.5769 0.8949 0.7944 -0.0145 0.1432  0.0865  29  PHE A CG  
231  C CD1 . PHE A 29  ? 0.6323 0.9476 0.8036 0.0201  0.1415  0.0941  29  PHE A CD1 
232  C CD2 . PHE A 29  ? 0.5630 0.8440 0.7745 -0.0238 0.1632  0.1000  29  PHE A CD2 
233  C CE1 . PHE A 29  ? 0.6240 0.9023 0.7438 0.0445  0.1570  0.1121  29  PHE A CE1 
234  C CE2 . PHE A 29  ? 0.6218 0.8677 0.7807 0.0027  0.1794  0.1203  29  PHE A CE2 
235  C CZ  . PHE A 29  ? 0.5724 0.8184 0.6857 0.0366  0.1752  0.1250  29  PHE A CZ  
236  N N   . TYR A 30  ? 0.6744 0.9245 0.5740 0.0385  0.1292  -0.1033 30  TYR A N   
237  C CA  . TYR A 30  ? 0.6909 0.9857 0.6307 0.0519  0.1183  -0.1043 30  TYR A CA  
238  C C   . TYR A 30  ? 0.6711 1.0550 0.6497 0.0307  0.1357  -0.1164 30  TYR A C   
239  O O   . TYR A 30  ? 0.6475 1.0722 0.6591 0.0307  0.1261  -0.1169 30  TYR A O   
240  C CB  . TYR A 30  ? 0.6614 0.9593 0.6095 0.1027  0.1061  -0.1164 30  TYR A CB  
241  C CG  . TYR A 30  ? 0.6891 0.8941 0.6014 0.1202  0.0894  -0.1053 30  TYR A CG  
242  C CD1 . TYR A 30  ? 0.7144 0.8579 0.6069 0.0970  0.0776  -0.0824 30  TYR A CD1 
243  C CD2 . TYR A 30  ? 0.7262 0.9059 0.6261 0.1588  0.0863  -0.1200 30  TYR A CD2 
244  C CE1 . TYR A 30  ? 0.6619 0.7262 0.5261 0.1072  0.0642  -0.0740 30  TYR A CE1 
245  C CE2 . TYR A 30  ? 0.7389 0.8293 0.6072 0.1694  0.0721  -0.1116 30  TYR A CE2 
246  C CZ  . TYR A 30  ? 0.7106 0.7462 0.5626 0.1411  0.0617  -0.0883 30  TYR A CZ  
247  O OH  . TYR A 30  ? 0.7421 0.6948 0.5669 0.1461  0.0495  -0.0818 30  TYR A OH  
248  N N   . SER A 31  ? 0.6401 1.0566 0.6143 0.0103  0.1616  -0.1267 31  SER A N   
249  C CA  . SER A 31  ? 0.6879 1.1908 0.7010 -0.0165 0.1820  -0.1395 31  SER A CA  
250  C C   . SER A 31  ? 0.7094 1.1941 0.7229 -0.0638 0.1846  -0.1232 31  SER A C   
251  O O   . SER A 31  ? 0.7003 1.2519 0.7538 -0.0867 0.1940  -0.1342 31  SER A O   
252  C CB  . SER A 31  ? 0.7138 1.2552 0.7177 -0.0269 0.2129  -0.1536 31  SER A CB  
253  O OG  . SER A 31  ? 0.6502 1.1211 0.5998 -0.0523 0.2225  -0.1354 31  SER A OG  
254  N N   . ARG A 32  ? 0.6794 1.0778 0.6515 -0.0780 0.1759  -0.1000 32  ARG A N   
255  C CA  . ARG A 32  ? 0.6978 1.0691 0.6629 -0.1208 0.1807  -0.0851 32  ARG A CA  
256  C C   . ARG A 32  ? 0.6478 1.0367 0.6467 -0.1215 0.1620  -0.0864 32  ARG A C   
257  O O   . ARG A 32  ? 0.5225 0.8777 0.5152 -0.0957 0.1382  -0.0783 32  ARG A O   
258  C CB  . ARG A 32  ? 0.7121 0.9907 0.6234 -0.1271 0.1737  -0.0621 32  ARG A CB  
259  C CG  . ARG A 32  ? 0.7832 1.0229 0.6756 -0.1675 0.1823  -0.0456 32  ARG A CG  
260  C CD  . ARG A 32  ? 0.8155 0.9782 0.6506 -0.1683 0.1791  -0.0260 32  ARG A CD  
261  N NE  . ARG A 32  ? 0.8559 0.9709 0.6673 -0.1997 0.1841  -0.0078 32  ARG A NE  
262  C CZ  . ARG A 32  ? 1.0311 1.0873 0.7902 -0.2059 0.1865  0.0104  32  ARG A CZ  
263  N NH1 . ARG A 32  ? 1.0116 1.0537 0.7366 -0.1863 0.1847  0.0109  32  ARG A NH1 
264  N NH2 . ARG A 32  ? 1.0672 1.0764 0.8055 -0.2307 0.1898  0.0274  32  ARG A NH2 
265  N N   . PRO A 33  ? 0.5718 1.0129 0.6050 -0.1521 0.1726  -0.0971 33  PRO A N   
266  C CA  . PRO A 33  ? 0.5778 1.0397 0.6407 -0.1516 0.1533  -0.1020 33  PRO A CA  
267  C C   . PRO A 33  ? 0.6035 0.9833 0.6358 -0.1601 0.1380  -0.0813 33  PRO A C   
268  O O   . PRO A 33  ? 0.6775 0.9951 0.6755 -0.1830 0.1470  -0.0659 33  PRO A O   
269  C CB  . PRO A 33  ? 0.6334 1.1640 0.7363 -0.1917 0.1721  -0.1210 33  PRO A CB  
270  C CG  . PRO A 33  ? 0.6080 1.1177 0.6865 -0.2245 0.2026  -0.1141 33  PRO A CG  
271  C CD  . PRO A 33  ? 0.6416 1.1281 0.6880 -0.1906 0.2038  -0.1070 33  PRO A CD  
272  N N   . SER A 34  ? 0.6075 0.9907 0.6511 -0.1387 0.1144  -0.0811 34  SER A N   
273  C CA  . SER A 34  ? 0.5769 0.8956 0.5970 -0.1428 0.0996  -0.0649 34  SER A CA  
274  C C   . SER A 34  ? 0.6218 0.9799 0.6689 -0.1368 0.0827  -0.0751 34  SER A C   
275  O O   . SER A 34  ? 0.7229 1.1507 0.8006 -0.1185 0.0767  -0.0904 34  SER A O   
276  C CB  . SER A 34  ? 0.6224 0.8809 0.6082 -0.1150 0.0870  -0.0465 34  SER A CB  
277  O OG  . SER A 34  ? 0.8282 1.0680 0.7926 -0.1114 0.0997  -0.0436 34  SER A OG  
278  N N   . LYS A 35  ? 0.6581 0.9739 0.6922 -0.1492 0.0741  -0.0678 35  LYS A N   
279  C CA  . LYS A 35  ? 0.6377 0.9830 0.6882 -0.1419 0.0570  -0.0764 35  LYS A CA  
280  C C   . LYS A 35  ? 0.5810 0.8767 0.6034 -0.1188 0.0411  -0.0569 35  LYS A C   
281  O O   . LYS A 35  ? 0.6240 0.8555 0.6186 -0.1243 0.0434  -0.0412 35  LYS A O   
282  C CB  . LYS A 35  ? 0.6138 0.9610 0.6774 -0.1783 0.0618  -0.0911 35  LYS A CB  
283  C CG  . LYS A 35  ? 0.7919 1.2166 0.8978 -0.2008 0.0714  -0.1185 35  LYS A CG  
284  C CD  . LYS A 35  ? 0.8607 1.3709 0.9963 -0.1700 0.0558  -0.1333 35  LYS A CD  
285  C CE  . LYS A 35  ? 0.8118 1.4115 0.9960 -0.1937 0.0621  -0.1657 35  LYS A CE  
286  N NZ  . LYS A 35  ? 0.9150 1.5938 1.1237 -0.1640 0.0390  -0.1823 35  LYS A NZ  
287  N N   . LEU A 36  ? 0.4756 0.8047 0.5047 -0.0932 0.0251  -0.0578 36  LEU A N   
288  C CA  . LEU A 36  ? 0.5168 0.8066 0.5203 -0.0736 0.0127  -0.0388 36  LEU A CA  
289  C C   . LEU A 36  ? 0.5152 0.7768 0.5100 -0.0919 0.0101  -0.0390 36  LEU A C   
290  O O   . LEU A 36  ? 0.5021 0.7827 0.5124 -0.1138 0.0128  -0.0570 36  LEU A O   
291  C CB  . LEU A 36  ? 0.5249 0.8576 0.5325 -0.0419 -0.0021 -0.0376 36  LEU A CB  
292  C CG  . LEU A 36  ? 0.5771 0.9009 0.5750 -0.0103 -0.0045 -0.0253 36  LEU A CG  
293  C CD1 . LEU A 36  ? 0.5105 0.8581 0.5269 -0.0131 0.0079  -0.0387 36  LEU A CD1 
294  C CD2 . LEU A 36  ? 0.4544 0.8183 0.4519 0.0236  -0.0207 -0.0224 36  LEU A CD2 
295  N N   . ALA A 37  ? 0.4935 0.7098 0.4644 -0.0826 0.0050  -0.0208 37  ALA A N   
296  C CA  . ALA A 37  ? 0.5940 0.7822 0.5561 -0.0952 0.0031  -0.0213 37  ALA A CA  
297  C C   . ALA A 37  ? 0.5325 0.7641 0.5072 -0.0969 -0.0044 -0.0387 37  ALA A C   
298  O O   . ALA A 37  ? 0.4733 0.7491 0.4517 -0.0789 -0.0132 -0.0401 37  ALA A O   
299  C CB  . ALA A 37  ? 0.5315 0.6828 0.4723 -0.0829 -0.0015 -0.0013 37  ALA A CB  
300  N N   . ASP A 38  ? 0.5691 0.7852 0.5473 -0.1170 -0.0017 -0.0529 38  ASP A N   
301  C CA  . ASP A 38  ? 0.5329 0.7828 0.5202 -0.1207 -0.0091 -0.0741 38  ASP A CA  
302  C C   . ASP A 38  ? 0.5376 0.7410 0.5204 -0.1400 -0.0046 -0.0843 38  ASP A C   
303  O O   . ASP A 38  ? 0.6047 0.7568 0.5785 -0.1510 0.0040  -0.0746 38  ASP A O   
304  C CB  . ASP A 38  ? 0.4619 0.7757 0.4758 -0.1276 -0.0113 -0.0966 38  ASP A CB  
305  C CG  . ASP A 38  ? 0.5151 0.8821 0.5328 -0.1172 -0.0251 -0.1142 38  ASP A CG  
306  O OD1 . ASP A 38  ? 0.4264 0.7762 0.4272 -0.1115 -0.0294 -0.1138 38  ASP A OD1 
307  O OD2 . ASP A 38  ? 0.5643 0.9963 0.6018 -0.1132 -0.0319 -0.1301 38  ASP A OD2 
308  N N   . PHE A 39  ? 0.5646 0.7841 0.5500 -0.1412 -0.0113 -0.1043 39  PHE A N   
309  C CA  . PHE A 39  ? 0.6217 0.7928 0.6011 -0.1541 -0.0089 -0.1166 39  PHE A CA  
310  C C   . PHE A 39  ? 0.6316 0.7877 0.6254 -0.1855 -0.0004 -0.1355 39  PHE A C   
311  O O   . PHE A 39  ? 0.5966 0.8045 0.6131 -0.1986 -0.0008 -0.1548 39  PHE A O   
312  C CB  . PHE A 39  ? 0.6299 0.8242 0.6058 -0.1427 -0.0183 -0.1349 39  PHE A CB  
313  C CG  . PHE A 39  ? 0.5965 0.7989 0.5560 -0.1171 -0.0224 -0.1154 39  PHE A CG  
314  C CD1 . PHE A 39  ? 0.6076 0.7651 0.5549 -0.1098 -0.0202 -0.1040 39  PHE A CD1 
315  C CD2 . PHE A 39  ? 0.5502 0.8063 0.5059 -0.1008 -0.0282 -0.1080 39  PHE A CD2 
316  C CE1 . PHE A 39  ? 0.6223 0.7941 0.5593 -0.0915 -0.0217 -0.0880 39  PHE A CE1 
317  C CE2 . PHE A 39  ? 0.5210 0.7809 0.4599 -0.0826 -0.0286 -0.0881 39  PHE A CE2 
318  C CZ  . PHE A 39  ? 0.5704 0.7911 0.5026 -0.0805 -0.0243 -0.0793 39  PHE A CZ  
319  N N   . TRP A 40  ? 0.6480 0.7333 0.6276 -0.1979 0.0074  -0.1295 40  TRP A N   
320  C CA  . TRP A 40  ? 0.7574 0.8097 0.7430 -0.2316 0.0189  -0.1428 40  TRP A CA  
321  C C   . TRP A 40  ? 0.7785 0.7477 0.7405 -0.2324 0.0195  -0.1420 40  TRP A C   
322  O O   . TRP A 40  ? 0.7883 0.7424 0.7367 -0.2059 0.0097  -0.1375 40  TRP A O   
323  C CB  . TRP A 40  ? 0.6266 0.6770 0.6138 -0.2468 0.0331  -0.1252 40  TRP A CB  
324  C CG  . TRP A 40  ? 0.6842 0.6916 0.6442 -0.2290 0.0352  -0.0932 40  TRP A CG  
325  C CD1 . TRP A 40  ? 0.6691 0.7016 0.6248 -0.2024 0.0284  -0.0759 40  TRP A CD1 
326  C CD2 . TRP A 40  ? 0.7534 0.6842 0.6845 -0.2369 0.0436  -0.0758 40  TRP A CD2 
327  N NE1 . TRP A 40  ? 0.7232 0.7053 0.6531 -0.1950 0.0313  -0.0526 40  TRP A NE1 
328  C CE2 . TRP A 40  ? 0.7309 0.6526 0.6438 -0.2136 0.0398  -0.0513 40  TRP A CE2 
329  C CE3 . TRP A 40  ? 0.8009 0.6662 0.7165 -0.2612 0.0537  -0.0779 40  TRP A CE3 
330  C CZ2 . TRP A 40  ? 0.8031 0.6617 0.6835 -0.2115 0.0437  -0.0304 40  TRP A CZ2 
331  C CZ3 . TRP A 40  ? 0.8602 0.6552 0.7391 -0.2573 0.0586  -0.0528 40  TRP A CZ3 
332  C CH2 . TRP A 40  ? 0.8019 0.5985 0.6638 -0.2315 0.0525  -0.0302 40  TRP A CH2 
333  N N   . GLY A 41  ? 0.8371 0.7521 0.7935 -0.2621 0.0316  -0.1460 41  GLY A N   
334  C CA  . GLY A 41  ? 0.9264 0.7527 0.8569 -0.2617 0.0318  -0.1455 41  GLY A CA  
335  C C   . GLY A 41  ? 1.0696 0.8853 1.0112 -0.2759 0.0280  -0.1824 41  GLY A C   
336  O O   . GLY A 41  ? 1.1089 0.9914 1.0789 -0.2880 0.0245  -0.2100 41  GLY A O   
337  N N   . ASN A 42  ? 1.2934 1.0218 1.2100 -0.2715 0.0271  -0.1840 42  ASN A N   
338  C CA  . ASN A 42  ? 1.3557 1.0544 1.2780 -0.2866 0.0247  -0.2210 42  ASN A CA  
339  C C   . ASN A 42  ? 1.3709 1.1435 1.3123 -0.2647 0.0093  -0.2508 42  ASN A C   
340  O O   . ASN A 42  ? 1.3713 1.1823 1.3347 -0.2858 0.0072  -0.2865 42  ASN A O   
341  C CB  . ASN A 42  ? 1.4464 1.0317 1.3332 -0.2748 0.0241  -0.2147 42  ASN A CB  
342  C CG  . ASN A 42  ? 1.5221 1.0207 1.3871 -0.3102 0.0420  -0.1968 42  ASN A CG  
343  O OD1 . ASN A 42  ? 1.5144 1.0385 1.3975 -0.3524 0.0568  -0.2006 42  ASN A OD1 
344  N ND2 . ASN A 42  ? 1.6018 0.9989 1.4264 -0.2925 0.0410  -0.1770 42  ASN A ND2 
345  N N   . ASN A 43  ? 1.1637 0.9613 1.0962 -0.2239 -0.0011 -0.2374 43  ASN A N   
346  C CA  . ASN A 43  ? 1.0175 0.8794 0.9598 -0.2006 -0.0134 -0.2617 43  ASN A CA  
347  C C   . ASN A 43  ? 0.9500 0.9010 0.9031 -0.1853 -0.0170 -0.2435 43  ASN A C   
348  O O   . ASN A 43  ? 0.8422 0.8359 0.7922 -0.1574 -0.0247 -0.2454 43  ASN A O   
349  C CB  . ASN A 43  ? 1.1882 1.0078 1.1117 -0.1658 -0.0207 -0.2656 43  ASN A CB  
350  C CG  . ASN A 43  ? 1.3298 1.0396 1.2332 -0.1721 -0.0175 -0.2708 43  ASN A CG  
351  O OD1 . ASN A 43  ? 1.4160 1.0661 1.3068 -0.1911 -0.0083 -0.2470 43  ASN A OD1 
352  N ND2 . ASN A 43  ? 1.1655 0.8455 1.0623 -0.1544 -0.0247 -0.3017 43  ASN A ND2 
353  N N   . ASN A 44  ? 0.9917 0.9693 0.9558 -0.2032 -0.0102 -0.2256 44  ASN A N   
354  C CA  . ASN A 44  ? 0.9363 0.9806 0.9058 -0.1866 -0.0130 -0.2035 44  ASN A CA  
355  C C   . ASN A 44  ? 0.7837 0.8103 0.7353 -0.1569 -0.0155 -0.1759 44  ASN A C   
356  O O   . ASN A 44  ? 0.7841 0.8605 0.7359 -0.1385 -0.0195 -0.1627 44  ASN A O   
357  C CB  . ASN A 44  ? 0.8118 0.9400 0.7942 -0.1790 -0.0227 -0.2253 44  ASN A CB  
358  C CG  . ASN A 44  ? 0.7557 0.9334 0.7628 -0.2043 -0.0220 -0.2424 44  ASN A CG  
359  O OD1 . ASN A 44  ? 0.7974 0.9545 0.8147 -0.2282 -0.0115 -0.2347 44  ASN A OD1 
360  N ND2 . ASN A 44  ? 0.9612 1.2110 0.9780 -0.1981 -0.0330 -0.2663 44  ASN A ND2 
361  N N   . GLU A 45  ? 0.8466 0.8014 0.7821 -0.1527 -0.0133 -0.1667 45  GLU A N   
362  C CA  . GLU A 45  ? 0.8614 0.8042 0.7844 -0.1241 -0.0180 -0.1491 45  GLU A CA  
363  C C   . GLU A 45  ? 0.7906 0.7253 0.7066 -0.1213 -0.0147 -0.1149 45  GLU A C   
364  O O   . GLU A 45  ? 0.8033 0.7363 0.7128 -0.1004 -0.0192 -0.1011 45  GLU A O   
365  C CB  . GLU A 45  ? 0.9141 0.7881 0.8227 -0.1131 -0.0211 -0.1602 45  GLU A CB  
366  C CG  . GLU A 45  ? 0.9418 0.7378 0.8295 -0.1153 -0.0180 -0.1374 45  GLU A CG  
367  C CD  . GLU A 45  ? 1.1567 0.9047 1.0387 -0.1499 -0.0072 -0.1385 45  GLU A CD  
368  O OE1 . GLU A 45  ? 1.1268 0.9121 1.0278 -0.1741 -0.0026 -0.1574 45  GLU A OE1 
369  O OE2 . GLU A 45  ? 1.2092 0.8845 1.0666 -0.1533 -0.0031 -0.1201 45  GLU A OE2 
370  N N   . ILE A 46  ? 0.8023 0.7374 0.7211 -0.1417 -0.0070 -0.1040 46  ILE A N   
371  C CA  . ILE A 46  ? 0.7792 0.7057 0.6891 -0.1392 -0.0036 -0.0756 46  ILE A CA  
372  C C   . ILE A 46  ? 0.7122 0.7000 0.6365 -0.1402 -0.0022 -0.0697 46  ILE A C   
373  O O   . ILE A 46  ? 0.6635 0.6884 0.6036 -0.1528 -0.0001 -0.0847 46  ILE A O   
374  C CB  . ILE A 46  ? 0.8544 0.7230 0.7488 -0.1587 0.0062  -0.0654 46  ILE A CB  
375  C CG1 . ILE A 46  ? 0.8607 0.6580 0.7354 -0.1554 0.0039  -0.0700 46  ILE A CG1 
376  C CG2 . ILE A 46  ? 0.7264 0.5886 0.6074 -0.1527 0.0085  -0.0387 46  ILE A CG2 
377  C CD1 . ILE A 46  ? 0.9855 0.7157 0.8359 -0.1747 0.0149  -0.0556 46  ILE A CD1 
378  N N   . LEU A 47  ? 0.6557 0.6530 0.5745 -0.1260 -0.0044 -0.0490 47  LEU A N   
379  C CA  . LEU A 47  ? 0.6164 0.6586 0.5432 -0.1218 -0.0039 -0.0401 47  LEU A CA  
380  C C   . LEU A 47  ? 0.6563 0.6760 0.5735 -0.1229 0.0008  -0.0208 47  LEU A C   
381  O O   . LEU A 47  ? 0.6360 0.6266 0.5402 -0.1151 -0.0020 -0.0081 47  LEU A O   
382  C CB  . LEU A 47  ? 0.5631 0.6378 0.4901 -0.1040 -0.0103 -0.0352 47  LEU A CB  
383  C CG  . LEU A 47  ? 0.5488 0.6565 0.4767 -0.0959 -0.0106 -0.0215 47  LEU A CG  
384  C CD1 . LEU A 47  ? 0.5232 0.6710 0.4630 -0.0996 -0.0110 -0.0340 47  LEU A CD1 
385  C CD2 . LEU A 47  ? 0.5607 0.6898 0.4828 -0.0826 -0.0137 -0.0128 47  LEU A CD2 
386  N N   . SER A 48  ? 0.6180 0.6568 0.5427 -0.1314 0.0074  -0.0213 48  SER A N   
387  C CA  . SER A 48  ? 0.6379 0.6605 0.5527 -0.1311 0.0131  -0.0070 48  SER A CA  
388  C C   . SER A 48  ? 0.5750 0.6363 0.5054 -0.1373 0.0204  -0.0141 48  SER A C   
389  O O   . SER A 48  ? 0.4941 0.5909 0.4435 -0.1465 0.0214  -0.0308 48  SER A O   
390  C CB  . SER A 48  ? 0.6553 0.6244 0.5497 -0.1413 0.0184  -0.0003 48  SER A CB  
391  O OG  . SER A 48  ? 0.6634 0.6232 0.5609 -0.1632 0.0286  -0.0106 48  SER A OG  
392  N N   . GLY A 49  ? 0.3755 0.6966 0.5609 -0.1079 -0.0064 -0.0127 49  GLY A N   
393  C CA  . GLY A 49  ? 0.3305 0.6826 0.5416 -0.1114 -0.0012 -0.0071 49  GLY A CA  
394  C C   . GLY A 49  ? 0.3320 0.6527 0.5248 -0.1219 0.0178  -0.0179 49  GLY A C   
395  O O   . GLY A 49  ? 0.4061 0.6751 0.5669 -0.1230 0.0255  -0.0281 49  GLY A O   
396  N N   . LEU A 50  ? 0.3248 0.6793 0.5398 -0.1297 0.0250  -0.0139 50  LEU A N   
397  C CA  . LEU A 50  ? 0.5248 0.8565 0.7249 -0.1431 0.0430  -0.0205 50  LEU A CA  
398  C C   . LEU A 50  ? 0.4525 0.8129 0.6774 -0.1319 0.0526  -0.0123 50  LEU A C   
399  O O   . LEU A 50  ? 0.3986 0.8178 0.6607 -0.1319 0.0474  -0.0042 50  LEU A O   
400  C CB  . LEU A 50  ? 0.4100 0.7579 0.6059 -0.1797 0.0451  -0.0290 50  LEU A CB  
401  C CG  . LEU A 50  ? 0.4928 0.8035 0.6582 -0.1913 0.0404  -0.0432 50  LEU A CG  
402  C CD1 . LEU A 50  ? 0.4002 0.7369 0.5656 -0.2278 0.0385  -0.0537 50  LEU A CD1 
403  C CD2 . LEU A 50  ? 0.5208 0.7579 0.6518 -0.1843 0.0519  -0.0505 50  LEU A CD2 
404  N N   . ASP A 51  ? 0.4968 0.8181 0.7013 -0.1219 0.0667  -0.0144 51  ASP A N   
405  C CA  . ASP A 51  ? 0.4536 0.8031 0.6755 -0.1160 0.0807  -0.0101 51  ASP A CA  
406  C C   . ASP A 51  ? 0.5182 0.9096 0.7551 -0.1481 0.0889  -0.0086 51  ASP A C   
407  O O   . ASP A 51  ? 0.5302 0.9017 0.7479 -0.1764 0.0893  -0.0138 51  ASP A O   
408  C CB  . ASP A 51  ? 0.5740 0.8731 0.7630 -0.1048 0.0944  -0.0126 51  ASP A CB  
409  C CG  . ASP A 51  ? 0.6772 1.0081 0.8804 -0.0969 0.1108  -0.0100 51  ASP A CG  
410  O OD1 . ASP A 51  ? 0.6144 1.0004 0.8570 -0.0863 0.1093  -0.0071 51  ASP A OD1 
411  O OD2 . ASP A 51  ? 0.7237 1.0268 0.8992 -0.1010 0.1256  -0.0101 51  ASP A OD2 
412  N N   . MET A 52  ? 0.4744 0.9254 0.7477 -0.1436 0.0950  -0.0021 52  MET A N   
413  C CA  . MET A 52  ? 0.4617 0.9632 0.7550 -0.1742 0.1028  0.0015  52  MET A CA  
414  C C   . MET A 52  ? 0.5115 1.0387 0.8149 -0.1695 0.1236  0.0053  52  MET A C   
415  O O   . MET A 52  ? 0.4659 1.0541 0.7991 -0.1877 0.1304  0.0112  52  MET A O   
416  C CB  . MET A 52  ? 0.3919 0.9629 0.7289 -0.1790 0.0877  0.0082  52  MET A CB  
417  C CG  . MET A 52  ? 0.5750 1.1319 0.9001 -0.1909 0.0683  0.0047  52  MET A CG  
418  S SD  . MET A 52  ? 0.6942 1.2127 0.9808 -0.2356 0.0712  -0.0080 52  MET A SD  
419  C CE  . MET A 52  ? 0.5614 1.1605 0.8829 -0.2680 0.0619  -0.0026 52  MET A CE  
420  N N   . GLU A 53  ? 0.5222 1.0088 0.8012 -0.1464 0.1340  0.0022  53  GLU A N   
421  C CA  . GLU A 53  ? 0.6590 1.1681 0.9394 -0.1440 0.1558  0.0044  53  GLU A CA  
422  C C   . GLU A 53  ? 0.5926 1.1021 0.8579 -0.1850 0.1677  0.0097  53  GLU A C   
423  O O   . GLU A 53  ? 0.6794 1.1345 0.9125 -0.2064 0.1626  0.0083  53  GLU A O   
424  C CB  . GLU A 53  ? 0.6920 1.1487 0.9380 -0.1171 0.1628  -0.0012 53  GLU A CB  
425  C CG  . GLU A 53  ? 0.7698 1.2573 1.0184 -0.1060 0.1850  -0.0017 53  GLU A CG  
426  C CD  . GLU A 53  ? 0.7888 1.3288 1.0805 -0.0728 0.1857  -0.0069 53  GLU A CD  
427  O OE1 . GLU A 53  ? 0.6937 1.2922 1.0315 -0.0763 0.1798  -0.0021 53  GLU A OE1 
428  O OE2 . GLU A 53  ? 0.8309 1.3528 1.1108 -0.0427 0.1914  -0.0162 53  GLU A OE2 
429  N N   . GLU A 54  ? 0.5966 1.1685 0.8874 -0.1962 0.1834  0.0161  54  GLU A N   
430  C CA  . GLU A 54  ? 0.6568 1.2332 0.9360 -0.2383 0.1948  0.0240  54  GLU A CA  
431  C C   . GLU A 54  ? 0.7211 1.2234 0.9477 -0.2438 0.2037  0.0257  54  GLU A C   
432  O O   . GLU A 54  ? 0.7177 1.2052 0.9265 -0.2179 0.2139  0.0245  54  GLU A O   
433  C CB  . GLU A 54  ? 0.5457 1.2073 0.8615 -0.2454 0.2126  0.0320  54  GLU A CB  
434  N N   . GLY A 55  ? 0.7903 1.2455 0.9921 -0.2776 0.1992  0.0284  55  GLY A N   
435  C CA  . GLY A 55  ? 0.8068 1.1863 0.9610 -0.2834 0.2041  0.0327  55  GLY A CA  
436  C C   . GLY A 55  ? 0.8720 1.1800 0.9977 -0.2583 0.1901  0.0236  55  GLY A C   
437  O O   . GLY A 55  ? 0.8277 1.0708 0.9156 -0.2613 0.1919  0.0282  55  GLY A O   
438  N N   . LYS A 56  ? 0.8632 1.1839 1.0077 -0.2343 0.1756  0.0132  56  LYS A N   
439  C CA  . LYS A 56  ? 0.7917 1.0551 0.9139 -0.2099 0.1621  0.0055  56  LYS A CA  
440  C C   . LYS A 56  ? 0.7743 1.0421 0.9118 -0.2137 0.1440  -0.0037 56  LYS A C   
441  O O   . LYS A 56  ? 0.5785 0.8159 0.7062 -0.1914 0.1318  -0.0098 56  LYS A O   
442  C CB  . LYS A 56  ? 0.7541 1.0257 0.8786 -0.1698 0.1626  0.0031  56  LYS A CB  
443  C CG  . LYS A 56  ? 0.7784 1.0599 0.8895 -0.1627 0.1813  0.0090  56  LYS A CG  
444  C CD  . LYS A 56  ? 0.8820 1.0952 0.9456 -0.1603 0.1836  0.0137  56  LYS A CD  
445  C CE  . LYS A 56  ? 0.9062 1.1136 0.9548 -0.1267 0.1866  0.0096  56  LYS A CE  
446  N NZ  . LYS A 56  ? 0.8395 1.1092 0.9079 -0.1178 0.2031  0.0074  56  LYS A NZ  
447  N N   . GLU A 57  ? 0.7403 1.0497 0.9010 -0.2426 0.1416  -0.0043 57  GLU A N   
448  C CA  . GLU A 57  ? 0.7341 1.0591 0.9092 -0.2474 0.1243  -0.0128 57  GLU A CA  
449  C C   . GLU A 57  ? 0.6789 0.9334 0.8199 -0.2479 0.1157  -0.0233 57  GLU A C   
450  O O   . GLU A 57  ? 0.7466 0.9451 0.8586 -0.2622 0.1223  -0.0244 57  GLU A O   
451  C CB  . GLU A 57  ? 0.7065 1.0834 0.9057 -0.2847 0.1232  -0.0121 57  GLU A CB  
452  C CG  . GLU A 57  ? 0.6992 1.1614 0.9426 -0.2815 0.1287  -0.0018 57  GLU A CG  
453  C CD  . GLU A 57  ? 0.8409 1.3228 1.0868 -0.3028 0.1479  0.0077  57  GLU A CD  
454  O OE1 . GLU A 57  ? 0.8778 1.3031 1.0891 -0.3084 0.1586  0.0097  57  GLU A OE1 
455  O OE2 . GLU A 57  ? 0.7529 1.3109 1.0370 -0.3143 0.1520  0.0150  57  GLU A OE2 
456  N N   . GLY A 58  ? 0.6720 0.9307 0.8181 -0.2312 0.1009  -0.0298 58  GLY A N   
457  C CA  . GLY A 58  ? 0.6284 0.8321 0.7469 -0.2288 0.0930  -0.0412 58  GLY A CA  
458  C C   . GLY A 58  ? 0.6033 0.7604 0.7013 -0.1958 0.0919  -0.0393 58  GLY A C   
459  O O   . GLY A 58  ? 0.6428 0.7614 0.7222 -0.1897 0.0850  -0.0481 58  GLY A O   
460  N N   . GLY A 59  ? 0.5799 0.7414 0.6805 -0.1748 0.0986  -0.0293 59  GLY A N   
461  C CA  . GLY A 59  ? 0.5238 0.6474 0.6065 -0.1447 0.0952  -0.0276 59  GLY A CA  
462  C C   . GLY A 59  ? 0.5654 0.7125 0.6652 -0.1240 0.0797  -0.0288 59  GLY A C   
463  O O   . GLY A 59  ? 0.5835 0.7815 0.7117 -0.1293 0.0721  -0.0281 59  GLY A O   
464  N N   . THR A 60  ? 0.4958 0.6067 0.5786 -0.1013 0.0735  -0.0285 60  THR A N   
465  C CA  . THR A 60  ? 0.5674 0.6976 0.6656 -0.0832 0.0581  -0.0269 60  THR A CA  
466  C C   . THR A 60  ? 0.5640 0.6579 0.6453 -0.0574 0.0542  -0.0236 60  THR A C   
467  O O   . THR A 60  ? 0.5705 0.6214 0.6246 -0.0545 0.0616  -0.0235 60  THR A O   
468  C CB  . THR A 60  ? 0.5784 0.7140 0.6760 -0.0948 0.0480  -0.0337 60  THR A CB  
469  O OG1 . THR A 60  ? 0.5568 0.7159 0.6700 -0.0793 0.0325  -0.0281 60  THR A OG1 
470  C CG2 . THR A 60  ? 0.6265 0.7066 0.6924 -0.0962 0.0515  -0.0417 60  THR A CG2 
471  N N   . TRP A 61  ? 0.5529 0.6657 0.6516 -0.0402 0.0409  -0.0193 61  TRP A N   
472  C CA  . TRP A 61  ? 0.6269 0.7119 0.7143 -0.0174 0.0336  -0.0162 61  TRP A CA  
473  C C   . TRP A 61  ? 0.5985 0.6741 0.6819 -0.0127 0.0192  -0.0146 61  TRP A C   
474  O O   . TRP A 61  ? 0.5199 0.5698 0.5911 0.0027  0.0124  -0.0116 61  TRP A O   
475  C CB  . TRP A 61  ? 0.5380 0.6478 0.6499 -0.0007 0.0287  -0.0124 61  TRP A CB  
476  C CG  . TRP A 61  ? 0.6018 0.7577 0.7494 -0.0036 0.0163  -0.0067 61  TRP A CG  
477  C CD1 . TRP A 61  ? 0.5945 0.7584 0.7563 0.0054  -0.0021 0.0009  61  TRP A CD1 
478  C CD2 . TRP A 61  ? 0.6037 0.8065 0.7771 -0.0185 0.0200  -0.0054 61  TRP A CD2 
479  N NE1 . TRP A 61  ? 0.5630 0.7749 0.7569 -0.0022 -0.0102 0.0081  61  TRP A NE1 
480  C CE2 . TRP A 61  ? 0.5570 0.7948 0.7589 -0.0164 0.0028  0.0039  61  TRP A CE2 
481  C CE3 . TRP A 61  ? 0.6425 0.8638 0.8184 -0.0350 0.0354  -0.0092 61  TRP A CE3 
482  C CZ2 . TRP A 61  ? 0.4630 0.7546 0.6956 -0.0290 -0.0002 0.0093  61  TRP A CZ2 
483  C CZ3 . TRP A 61  ? 0.6417 0.9172 0.8491 -0.0485 0.0328  -0.0052 61  TRP A CZ3 
484  C CH2 . TRP A 61  ? 0.5034 0.8142 0.7387 -0.0447 0.0148  0.0039  61  TRP A CH2 
485  N N   . LEU A 62  ? 0.5744 0.6746 0.6676 -0.0268 0.0142  -0.0167 62  LEU A N   
486  C CA  . LEU A 62  ? 0.4897 0.5940 0.5824 -0.0235 0.0012  -0.0147 62  LEU A CA  
487  C C   . LEU A 62  ? 0.4635 0.5928 0.5583 -0.0439 0.0019  -0.0223 62  LEU A C   
488  O O   . LEU A 62  ? 0.4597 0.6276 0.5731 -0.0578 0.0013  -0.0216 62  LEU A O   
489  C CB  . LEU A 62  ? 0.5190 0.6486 0.6354 -0.0112 -0.0149 -0.0024 62  LEU A CB  
490  C CG  . LEU A 62  ? 0.5325 0.6765 0.6527 -0.0100 -0.0300 0.0044  62  LEU A CG  
491  C CD1 . LEU A 62  ? 0.5304 0.6376 0.6255 -0.0016 -0.0287 0.0009  62  LEU A CD1 
492  C CD2 . LEU A 62  ? 0.4642 0.6271 0.6097 0.0006  -0.0467 0.0195  62  LEU A CD2 
493  N N   . GLY A 63  ? 0.4123 0.5223 0.4886 -0.0455 0.0029  -0.0306 63  GLY A N   
494  C CA  . GLY A 63  ? 0.5562 0.6858 0.6296 -0.0646 0.0048  -0.0428 63  GLY A CA  
495  C C   . GLY A 63  ? 0.5894 0.7055 0.6473 -0.0586 0.0035  -0.0509 63  GLY A C   
496  O O   . GLY A 63  ? 0.5277 0.6106 0.5748 -0.0409 0.0039  -0.0478 63  GLY A O   
497  N N   . ILE A 64  ? 0.5642 0.7110 0.6216 -0.0737 0.0021  -0.0617 64  ILE A N   
498  C CA  . ILE A 64  ? 0.5462 0.6896 0.5900 -0.0692 0.0032  -0.0735 64  ILE A CA  
499  C C   . ILE A 64  ? 0.6072 0.7568 0.6396 -0.0905 0.0111  -0.0969 64  ILE A C   
500  O O   . ILE A 64  ? 0.5531 0.7404 0.5940 -0.1113 0.0077  -0.0980 64  ILE A O   
501  C CB  . ILE A 64  ? 0.5205 0.7104 0.5768 -0.0634 -0.0110 -0.0597 64  ILE A CB  
502  C CG1 . ILE A 64  ? 0.6279 0.8166 0.6710 -0.0552 -0.0077 -0.0710 64  ILE A CG1 
503  C CG2 . ILE A 64  ? 0.5050 0.7545 0.5755 -0.0834 -0.0199 -0.0550 64  ILE A CG2 
504  C CD1 . ILE A 64  ? 0.6231 0.8597 0.6778 -0.0510 -0.0211 -0.0548 64  ILE A CD1 
505  N N   . SER A 65  ? 0.5981 0.7108 0.6119 -0.0852 0.0209  -0.1161 65  SER A N   
506  C CA  . SER A 65  ? 0.6807 0.7935 0.6809 -0.1039 0.0285  -0.1433 65  SER A CA  
507  C C   . SER A 65  ? 0.6305 0.7743 0.6242 -0.0983 0.0275  -0.1558 65  SER A C   
508  O O   . SER A 65  ? 0.5502 0.6953 0.5470 -0.0763 0.0250  -0.1464 65  SER A O   
509  C CB  . SER A 65  ? 0.7150 0.7579 0.6992 -0.1031 0.0417  -0.1596 65  SER A CB  
510  O OG  . SER A 65  ? 0.8338 0.8443 0.8085 -0.0804 0.0470  -0.1688 65  SER A OG  
511  N N   . THR A 66  ? 0.6443 0.8175 0.6287 -0.1198 0.0295  -0.1776 66  THR A N   
512  C CA  . THR A 66  ? 0.6812 0.8887 0.6561 -0.1167 0.0312  -0.1938 66  THR A CA  
513  C C   . THR A 66  ? 0.7519 0.9076 0.7133 -0.0962 0.0448  -0.2165 66  THR A C   
514  O O   . THR A 66  ? 0.7925 0.9742 0.7501 -0.0841 0.0478  -0.2260 66  THR A O   
515  C CB  . THR A 66  ? 0.6828 0.9346 0.6470 -0.1467 0.0303  -0.2141 66  THR A CB  
516  O OG1 . THR A 66  ? 0.7466 0.9484 0.6946 -0.1600 0.0414  -0.2438 66  THR A OG1 
517  C CG2 . THR A 66  ? 0.6046 0.9080 0.5859 -0.1665 0.0159  -0.1896 66  THR A CG2 
518  N N   . ARG A 67  ? 0.8238 0.9090 0.7795 -0.0919 0.0531  -0.2239 67  ARG A N   
519  C CA  . ARG A 67  ? 0.8298 0.8596 0.7780 -0.0678 0.0639  -0.2389 67  ARG A CA  
520  C C   . ARG A 67  ? 0.7915 0.8206 0.7518 -0.0376 0.0597  -0.2144 67  ARG A C   
521  O O   . ARG A 67  ? 0.8840 0.8732 0.8422 -0.0143 0.0670  -0.2222 67  ARG A O   
522  C CB  . ARG A 67  ? 0.9275 0.8808 0.8681 -0.0730 0.0713  -0.2464 67  ARG A CB  
523  C CG  . ARG A 67  ? 1.0909 1.0268 1.0164 -0.1001 0.0779  -0.2790 67  ARG A CG  
524  C CD  . ARG A 67  ? 1.2440 1.1071 1.1581 -0.0869 0.0900  -0.3060 67  ARG A CD  
525  N NE  . ARG A 67  ? 1.2999 1.1826 1.2096 -0.0679 0.0966  -0.3306 67  ARG A NE  
526  C CZ  . ARG A 67  ? 1.3899 1.2904 1.2849 -0.0820 0.1026  -0.3676 67  ARG A CZ  
527  N NH1 . ARG A 67  ? 1.4097 1.3096 1.2929 -0.1172 0.1013  -0.3843 67  ARG A NH1 
528  N NH2 . ARG A 67  ? 1.3418 1.2649 1.2339 -0.0612 0.1103  -0.3889 67  ARG A NH2 
529  N N   . GLY A 68  ? 0.6927 0.7633 0.6667 -0.0375 0.0472  -0.1851 68  GLY A N   
530  C CA  . GLY A 68  ? 0.7557 0.8285 0.7405 -0.0128 0.0411  -0.1623 68  GLY A CA  
531  C C   . GLY A 68  ? 0.7877 0.8085 0.7744 -0.0021 0.0392  -0.1432 68  GLY A C   
532  O O   . GLY A 68  ? 0.7933 0.7801 0.7794 0.0203  0.0415  -0.1388 68  GLY A O   
533  N N   . LYS A 69  ? 0.6880 0.7059 0.6772 -0.0178 0.0351  -0.1316 69  LYS A N   
534  C CA  . LYS A 69  ? 0.6764 0.6530 0.6651 -0.0103 0.0340  -0.1136 69  LYS A CA  
535  C C   . LYS A 69  ? 0.6992 0.7099 0.7008 -0.0172 0.0231  -0.0927 69  LYS A C   
536  O O   . LYS A 69  ? 0.6777 0.7295 0.6874 -0.0351 0.0193  -0.0942 69  LYS A O   
537  C CB  . LYS A 69  ? 0.7435 0.6687 0.7203 -0.0225 0.0446  -0.1243 69  LYS A CB  
538  C CG  . LYS A 69  ? 0.7808 0.6542 0.7463 -0.0112 0.0544  -0.1414 69  LYS A CG  
539  C CD  . LYS A 69  ? 0.8849 0.6999 0.8397 -0.0229 0.0622  -0.1433 69  LYS A CD  
540  C CE  . LYS A 69  ? 0.9620 0.7174 0.9102 -0.0005 0.0657  -0.1370 69  LYS A CE  
541  N NZ  . LYS A 69  ? 1.0905 0.7908 1.0285 -0.0133 0.0713  -0.1308 69  LYS A NZ  
542  N N   . LEU A 70  ? 0.6193 0.6134 0.6231 -0.0025 0.0175  -0.0737 70  LEU A N   
543  C CA  . LEU A 70  ? 0.6217 0.6395 0.6380 -0.0054 0.0080  -0.0563 70  LEU A CA  
544  C C   . LEU A 70  ? 0.6329 0.6102 0.6410 0.0052  0.0097  -0.0452 70  LEU A C   
545  O O   . LEU A 70  ? 0.5595 0.5044 0.5568 0.0203  0.0107  -0.0422 70  LEU A O   
546  C CB  . LEU A 70  ? 0.4914 0.5515 0.5219 0.0013  -0.0064 -0.0434 70  LEU A CB  
547  C CG  . LEU A 70  ? 0.5622 0.6380 0.6073 0.0028  -0.0183 -0.0251 70  LEU A CG  
548  C CD1 . LEU A 70  ? 0.6096 0.7374 0.6728 -0.0028 -0.0321 -0.0145 70  LEU A CD1 
549  C CD2 . LEU A 70  ? 0.5473 0.5911 0.5863 0.0205  -0.0231 -0.0139 70  LEU A CD2 
550  N N   . ALA A 71  ? 0.5221 0.5054 0.5359 -0.0023 0.0099  -0.0389 71  ALA A N   
551  C CA  . ALA A 71  ? 0.5689 0.5218 0.5733 0.0068  0.0120  -0.0293 71  ALA A CA  
552  C C   . ALA A 71  ? 0.6134 0.5929 0.6328 0.0045  0.0074  -0.0219 71  ALA A C   
553  O O   . ALA A 71  ? 0.5687 0.5847 0.6058 -0.0074 0.0057  -0.0239 71  ALA A O   
554  C CB  . ALA A 71  ? 0.5691 0.4813 0.5561 -0.0005 0.0260  -0.0344 71  ALA A CB  
555  N N   . ALA A 72  ? 0.5024 0.4645 0.5149 0.0168  0.0051  -0.0137 72  ALA A N   
556  C CA  . ALA A 72  ? 0.5689 0.5498 0.5950 0.0195  0.0017  -0.0092 72  ALA A CA  
557  C C   . ALA A 72  ? 0.5824 0.5338 0.5891 0.0270  0.0090  -0.0074 72  ALA A C   
558  O O   . ALA A 72  ? 0.5411 0.4603 0.5259 0.0337  0.0096  -0.0045 72  ALA A O   
559  C CB  . ALA A 72  ? 0.4606 0.4616 0.5034 0.0292  -0.0158 -0.0014 72  ALA A CB  
560  N N   . LEU A 73  ? 0.5188 0.4852 0.5344 0.0262  0.0146  -0.0087 73  LEU A N   
561  C CA  . LEU A 73  ? 0.6186 0.5653 0.6147 0.0317  0.0237  -0.0087 73  LEU A CA  
562  C C   . LEU A 73  ? 0.5601 0.5245 0.5706 0.0432  0.0195  -0.0110 73  LEU A C   
563  O O   . LEU A 73  ? 0.6425 0.6386 0.6827 0.0429  0.0150  -0.0117 73  LEU A O   
564  C CB  . LEU A 73  ? 0.6961 0.6416 0.6842 0.0162  0.0417  -0.0105 73  LEU A CB  
565  C CG  . LEU A 73  ? 0.6343 0.5640 0.5987 0.0184  0.0533  -0.0085 73  LEU A CG  
566  C CD1 . LEU A 73  ? 0.7610 0.6638 0.7037 0.0037  0.0648  -0.0032 73  LEU A CD1 
567  C CD2 . LEU A 73  ? 0.6800 0.6448 0.6614 0.0182  0.0627  -0.0134 73  LEU A CD2 
568  N N   . THR A 74  ? 0.6249 0.5679 0.6141 0.0540  0.0201  -0.0124 74  THR A N   
569  C CA  . THR A 74  ? 0.6120 0.5648 0.6093 0.0662  0.0196  -0.0193 74  THR A CA  
570  C C   . THR A 74  ? 0.6589 0.6022 0.6286 0.0665  0.0359  -0.0240 74  THR A C   
571  O O   . THR A 74  ? 0.6198 0.5387 0.5588 0.0611  0.0402  -0.0185 74  THR A O   
572  C CB  . THR A 74  ? 0.5767 0.5138 0.5741 0.0796  0.0003  -0.0192 74  THR A CB  
573  O OG1 . THR A 74  ? 0.6006 0.5067 0.5639 0.0814  -0.0031 -0.0164 74  THR A OG1 
574  C CG2 . THR A 74  ? 0.5691 0.5192 0.5923 0.0773  -0.0162 -0.0112 74  THR A CG2 
575  N N   . ASN A 75  ? 0.6394 0.6046 0.6210 0.0733  0.0451  -0.0334 75  ASN A N   
576  C CA  . ASN A 75  ? 0.6473 0.6113 0.6024 0.0739  0.0619  -0.0392 75  ASN A CA  
577  C C   . ASN A 75  ? 0.6524 0.5909 0.5808 0.0877  0.0536  -0.0468 75  ASN A C   
578  O O   . ASN A 75  ? 0.6484 0.5786 0.5900 0.1000  0.0375  -0.0524 75  ASN A O   
579  C CB  . ASN A 75  ? 0.7245 0.7287 0.7043 0.0769  0.0774  -0.0481 75  ASN A CB  
580  C CG  . ASN A 75  ? 0.7480 0.7817 0.7518 0.0595  0.0860  -0.0405 75  ASN A CG  
581  O OD1 . ASN A 75  ? 0.7540 0.7733 0.7509 0.0443  0.0824  -0.0307 75  ASN A OD1 
582  N ND2 . ASN A 75  ? 0.8218 0.8979 0.8546 0.0618  0.0973  -0.0459 75  ASN A ND2 
583  N N   . TYR A 76  ? 0.6460 0.6661 0.5918 -0.0059 -0.0121 0.0197  76  TYR A N   
584  C CA  . TYR A 76  ? 0.6703 0.6742 0.5689 0.0104  -0.0107 0.0123  76  TYR A CA  
585  C C   . TYR A 76  ? 0.6181 0.6261 0.5316 0.0211  0.0084  0.0058  76  TYR A C   
586  O O   . TYR A 76  ? 0.6678 0.6811 0.5969 0.0221  0.0364  0.0122  76  TYR A O   
587  C CB  . TYR A 76  ? 0.6755 0.6597 0.5254 0.0163  0.0012  0.0201  76  TYR A CB  
588  C CG  . TYR A 76  ? 0.7419 0.7052 0.5356 0.0303  -0.0047 0.0138  76  TYR A CG  
589  C CD1 . TYR A 76  ? 0.6900 0.6475 0.4640 0.0304  -0.0332 0.0085  76  TYR A CD1 
590  C CD2 . TYR A 76  ? 0.7412 0.6904 0.4996 0.0423  0.0186  0.0134  76  TYR A CD2 
591  C CE1 . TYR A 76  ? 0.6807 0.6171 0.4040 0.0424  -0.0414 0.0038  76  TYR A CE1 
592  C CE2 . TYR A 76  ? 0.7411 0.6678 0.4434 0.0538  0.0113  0.0075  76  TYR A CE2 
593  C CZ  . TYR A 76  ? 0.7957 0.7151 0.4818 0.0540  -0.0202 0.0030  76  TYR A CZ  
594  O OH  . TYR A 76  ? 0.7859 0.6810 0.4172 0.0648  -0.0303 -0.0020 76  TYR A OH  
595  N N   . LEU A 77  ? 0.6180 0.6250 0.5314 0.0285  -0.0072 -0.0072 77  LEU A N   
596  C CA  . LEU A 77  ? 0.6402 0.6496 0.5679 0.0413  0.0097  -0.0178 77  LEU A CA  
597  C C   . LEU A 77  ? 0.7151 0.7094 0.5938 0.0546  0.0411  -0.0181 77  LEU A C   
598  O O   . LEU A 77  ? 0.7159 0.6884 0.5355 0.0622  0.0348  -0.0210 77  LEU A O   
599  C CB  . LEU A 77  ? 0.6382 0.6420 0.5639 0.0482  -0.0170 -0.0325 77  LEU A CB  
600  C CG  . LEU A 77  ? 0.6664 0.6686 0.6035 0.0648  -0.0032 -0.0486 77  LEU A CG  
601  C CD1 . LEU A 77  ? 0.6466 0.6727 0.6594 0.0604  0.0056  -0.0485 77  LEU A CD1 
602  C CD2 . LEU A 77  ? 0.6723 0.6602 0.5917 0.0724  -0.0335 -0.0626 77  LEU A CD2 
603  N N   . GLN A 78  ? 0.7563 0.7626 0.6597 0.0559  0.0740  -0.0141 78  GLN A N   
604  C CA  . GLN A 78  ? 0.8372 0.8326 0.6955 0.0655  0.1079  -0.0129 78  GLN A CA  
605  C C   . GLN A 78  ? 0.8201 0.8288 0.7062 0.0772  0.1351  -0.0265 78  GLN A C   
606  O O   . GLN A 78  ? 0.8149 0.8473 0.7713 0.0734  0.1372  -0.0280 78  GLN A O   
607  C CB  . GLN A 78  ? 0.8938 0.8923 0.7524 0.0538  0.1272  0.0083  78  GLN A CB  
608  C CG  . GLN A 78  ? 0.8968 0.8762 0.7143 0.0467  0.1076  0.0200  78  GLN A CG  
609  C CD  . GLN A 78  ? 1.0125 0.9946 0.8419 0.0340  0.1211  0.0406  78  GLN A CD  
610  O OE1 . GLN A 78  ? 0.9675 0.9377 0.7807 0.0272  0.1038  0.0495  78  GLN A OE1 
611  N NE2 . GLN A 78  ? 0.9983 0.9963 0.8593 0.0310  0.1517  0.0478  78  GLN A NE2 
612  N N   . PRO A 79  ? 0.8740 0.8680 0.7072 0.0913  0.1563  -0.0376 79  PRO A N   
613  C CA  . PRO A 79  ? 0.8605 0.8698 0.7205 0.1031  0.1892  -0.0523 79  PRO A CA  
614  C C   . PRO A 79  ? 0.8947 0.9295 0.7976 0.0948  0.2252  -0.0379 79  PRO A C   
615  O O   . PRO A 79  ? 0.8671 0.9248 0.8216 0.1016  0.2490  -0.0483 79  PRO A O   
616  C CB  . PRO A 79  ? 0.9539 0.9376 0.7314 0.1171  0.2050  -0.0652 79  PRO A CB  
617  C CG  . PRO A 79  ? 0.9608 0.9154 0.6820 0.1150  0.1678  -0.0617 79  PRO A CG  
618  C CD  . PRO A 79  ? 0.8992 0.8614 0.6473 0.0975  0.1486  -0.0394 79  PRO A CD  
619  N N   . GLN A 80  ? 1.0396 1.0714 0.9264 0.0804  0.2293  -0.0143 80  GLN A N   
620  C CA  . GLN A 80  ? 1.1000 1.1522 1.0178 0.0711  0.2641  0.0024  80  GLN A CA  
621  C C   . GLN A 80  ? 1.0325 1.0852 0.9720 0.0525  0.2452  0.0256  80  GLN A C   
622  O O   . GLN A 80  ? 0.9567 0.9895 0.8645 0.0482  0.2141  0.0295  80  GLN A O   
623  C CB  . GLN A 80  ? 1.2172 1.2583 1.0672 0.0749  0.3011  0.0063  80  GLN A CB  
624  C CG  . GLN A 80  ? 1.3190 1.3837 1.1991 0.0652  0.3416  0.0235  80  GLN A CG  
625  C CD  . GLN A 80  ? 1.2906 1.3920 1.2557 0.0702  0.3634  0.0123  80  GLN A CD  
626  O OE1 . GLN A 80  ? 1.1224 1.2297 1.0938 0.0868  0.3739  -0.0128 80  GLN A OE1 
627  N NE2 . GLN A 80  ? 1.1929 1.3181 1.2270 0.0559  0.3685  0.0307  80  GLN A NE2 
628  N N   . LEU A 81  ? 0.9630 1.0390 0.9595 0.0416  0.2643  0.0399  81  LEU A N   
629  C CA  . LEU A 81  ? 0.8895 0.9666 0.9148 0.0237  0.2471  0.0601  81  LEU A CA  
630  C C   . LEU A 81  ? 0.9207 1.0013 0.9405 0.0133  0.2775  0.0827  81  LEU A C   
631  O O   . LEU A 81  ? 0.8637 0.9645 0.9057 0.0151  0.3139  0.0846  81  LEU A O   
632  C CB  . LEU A 81  ? 0.9305 1.0312 1.0418 0.0163  0.2305  0.0581  81  LEU A CB  
633  C CG  . LEU A 81  ? 0.9681 1.0618 1.0959 0.0015  0.1931  0.0661  81  LEU A CG  
634  C CD1 . LEU A 81  ? 0.8847 0.9600 0.9714 0.0072  0.1596  0.0522  81  LEU A CD1 
635  C CD2 . LEU A 81  ? 0.8357 0.9529 1.0480 -0.0094 0.1829  0.0689  81  LEU A CD2 
636  N N   . ASP A 82  ? 0.9185 0.9797 0.9107 0.0021  0.2622  0.0997  82  ASP A N   
637  C CA  . ASP A 82  ? 0.8749 0.9376 0.8726 -0.0118 0.2822  0.1248  82  ASP A CA  
638  C C   . ASP A 82  ? 1.0125 1.0952 1.0916 -0.0257 0.2729  0.1341  82  ASP A C   
639  O O   . ASP A 82  ? 0.9310 1.0052 1.0254 -0.0325 0.2395  0.1334  82  ASP A O   
640  C CB  . ASP A 82  ? 0.8495 0.8797 0.7856 -0.0168 0.2663  0.1382  82  ASP A CB  
641  C CG  . ASP A 82  ? 0.9441 0.9723 0.8884 -0.0328 0.2813  0.1660  82  ASP A CG  
642  O OD1 . ASP A 82  ? 0.9510 1.0040 0.9411 -0.0397 0.3089  0.1757  82  ASP A OD1 
643  O OD2 . ASP A 82  ? 0.9997 1.0014 0.9076 -0.0386 0.2644  0.1787  82  ASP A OD2 
644  N N   . TRP A 83  ? 1.0503 1.1600 1.1819 -0.0306 0.3022  0.1424  83  TRP A N   
645  C CA  . TRP A 83  ? 0.9981 1.1282 1.2126 -0.0436 0.2930  0.1506  83  TRP A CA  
646  C C   . TRP A 83  ? 0.9724 1.0935 1.1970 -0.0621 0.2889  0.1762  83  TRP A C   
647  O O   . TRP A 83  ? 0.9397 1.0730 1.2289 -0.0749 0.2772  0.1843  83  TRP A O   
648  C CB  . TRP A 83  ? 0.9673 1.1332 1.2445 -0.0399 0.3248  0.1475  83  TRP A CB  
649  C CG  . TRP A 83  ? 0.9589 1.1345 1.2468 -0.0225 0.3215  0.1205  83  TRP A CG  
650  C CD1 . TRP A 83  ? 1.0700 1.2390 1.3043 -0.0047 0.3378  0.1026  83  TRP A CD1 
651  C CD2 . TRP A 83  ? 0.9164 1.1071 1.2724 -0.0219 0.2976  0.1088  83  TRP A CD2 
652  N NE1 . TRP A 83  ? 1.0387 1.2178 1.3066 0.0079  0.3255  0.0797  83  TRP A NE1 
653  C CE2 . TRP A 83  ? 0.9048 1.0975 1.2481 -0.0028 0.3003  0.0841  83  TRP A CE2 
654  C CE3 . TRP A 83  ? 0.9044 1.1051 1.3297 -0.0367 0.2722  0.1174  83  TRP A CE3 
655  C CZ2 . TRP A 83  ? 0.8050 1.0095 1.2053 0.0018  0.2777  0.0691  83  TRP A CZ2 
656  C CZ3 . TRP A 83  ? 0.8697 1.0821 1.3480 -0.0332 0.2498  0.1032  83  TRP A CZ3 
657  C CH2 . TRP A 83  ? 0.8815 1.0959 1.3486 -0.0141 0.2523  0.0799  83  TRP A CH2 
658  N N   . GLN A 84  ? 0.9345 1.0323 1.0976 -0.0645 0.2953  0.1894  84  GLN A N   
659  C CA  . GLN A 84  ? 0.9222 1.0071 1.0926 -0.0815 0.2890  0.2139  84  GLN A CA  
660  C C   . GLN A 84  ? 0.9378 0.9926 1.0817 -0.0840 0.2496  0.2107  84  GLN A C   
661  O O   . GLN A 84  ? 0.8309 0.8711 0.9820 -0.0970 0.2395  0.2281  84  GLN A O   
662  C CB  . GLN A 84  ? 0.8812 0.9587 1.0054 -0.0854 0.3199  0.2341  84  GLN A CB  
663  N N   . ALA A 85  ? 0.7615 0.8076 0.8783 -0.0722 0.2274  0.1887  85  ALA A N   
664  C CA  . ALA A 85  ? 0.7980 0.8182 0.8860 -0.0728 0.1941  0.1837  85  ALA A CA  
665  C C   . ALA A 85  ? 0.8235 0.8495 0.9645 -0.0835 0.1673  0.1783  85  ALA A C   
666  O O   . ALA A 85  ? 0.6970 0.7457 0.8936 -0.0889 0.1694  0.1759  85  ALA A O   
667  C CB  . ALA A 85  ? 0.8614 0.8710 0.8965 -0.0569 0.1823  0.1639  85  ALA A CB  
668  N N   . ARG A 86  ? 0.8329 0.8371 0.9559 -0.0869 0.1412  0.1756  86  ARG A N   
669  C CA  . ARG A 86  ? 0.7548 0.7609 0.9169 -0.0978 0.1152  0.1682  86  ARG A CA  
670  C C   . ARG A 86  ? 0.7973 0.8199 0.9725 -0.0939 0.1015  0.1481  86  ARG A C   
671  O O   . ARG A 86  ? 0.7301 0.7535 0.8707 -0.0807 0.1017  0.1357  86  ARG A O   
672  C CB  . ARG A 86  ? 0.7721 0.7524 0.9070 -0.0990 0.0920  0.1642  86  ARG A CB  
673  C CG  . ARG A 86  ? 0.7361 0.6952 0.8645 -0.1049 0.0964  0.1839  86  ARG A CG  
674  C CD  . ARG A 86  ? 0.8514 0.7858 0.9546 -0.1021 0.0715  0.1744  86  ARG A CD  
675  N NE  . ARG A 86  ? 1.0495 0.9590 1.1452 -0.1063 0.0709  0.1925  86  ARG A NE  
676  C CZ  . ARG A 86  ? 1.0963 0.9816 1.1755 -0.1031 0.0508  0.1871  86  ARG A CZ  
677  N NH1 . ARG A 86  ? 1.0468 0.9321 1.1144 -0.0956 0.0322  0.1636  86  ARG A NH1 
678  N NH2 . ARG A 86  ? 1.1474 1.0089 1.2238 -0.1077 0.0491  0.2062  86  ARG A NH2 
679  N N   . GLY A 87  ? 0.7499 0.7838 0.9747 -0.1070 0.0869  0.1460  87  GLY A N   
680  C CA  . GLY A 87  ? 0.6771 0.7231 0.9136 -0.1074 0.0675  0.1292  87  GLY A CA  
681  C C   . GLY A 87  ? 0.7302 0.7625 0.9237 -0.1042 0.0447  0.1136  87  GLY A C   
682  O O   . GLY A 87  ? 0.7924 0.8076 0.9684 -0.1077 0.0359  0.1139  87  GLY A O   
683  N N   . ARG A 88  ? 0.7244 0.7651 0.9036 -0.0973 0.0349  0.0995  88  ARG A N   
684  C CA  . ARG A 88  ? 0.7354 0.7685 0.8785 -0.0954 0.0135  0.0849  88  ARG A CA  
685  C C   . ARG A 88  ? 0.7210 0.7593 0.8859 -0.1126 -0.0114 0.0770  88  ARG A C   
686  O O   . ARG A 88  ? 0.6203 0.6536 0.7583 -0.1142 -0.0273 0.0651  88  ARG A O   
687  C CB  . ARG A 88  ? 0.7167 0.7555 0.8339 -0.0820 0.0121  0.0747  88  ARG A CB  
688  C CG  . ARG A 88  ? 0.6240 0.6520 0.7020 -0.0648 0.0330  0.0788  88  ARG A CG  
689  C CD  . ARG A 88  ? 0.6951 0.7300 0.7593 -0.0521 0.0352  0.0693  88  ARG A CD  
690  N NE  . ARG A 88  ? 0.7403 0.7925 0.8492 -0.0528 0.0479  0.0714  88  ARG A NE  
691  C CZ  . ARG A 88  ? 0.7448 0.8033 0.8515 -0.0404 0.0567  0.0637  88  ARG A CZ  
692  N NH1 . ARG A 88  ? 0.6743 0.7211 0.7318 -0.0268 0.0538  0.0543  88  ARG A NH1 
693  N NH2 . ARG A 88  ? 0.7251 0.8014 0.8825 -0.0412 0.0676  0.0648  88  ARG A NH2 
694  N N   . GLY A 89  ? 0.7613 0.8098 0.9738 -0.1265 -0.0152 0.0833  89  GLY A N   
695  C CA  . GLY A 89  ? 0.6854 0.7366 0.9142 -0.1454 -0.0403 0.0767  89  GLY A CA  
696  C C   . GLY A 89  ? 0.6752 0.7107 0.8892 -0.1535 -0.0481 0.0722  89  GLY A C   
697  O O   . GLY A 89  ? 0.6611 0.6971 0.8685 -0.1666 -0.0684 0.0607  89  GLY A O   
698  N N   . GLU A 90  ? 0.6086 0.6297 0.8168 -0.1466 -0.0329 0.0807  90  GLU A N   
699  C CA  . GLU A 90  ? 0.6761 0.6796 0.8760 -0.1527 -0.0410 0.0757  90  GLU A CA  
700  C C   . GLU A 90  ? 0.7189 0.7155 0.8757 -0.1430 -0.0473 0.0596  90  GLU A C   
701  O O   . GLU A 90  ? 0.6847 0.6702 0.8359 -0.1484 -0.0573 0.0489  90  GLU A O   
702  C CB  . GLU A 90  ? 0.5838 0.5725 0.7966 -0.1499 -0.0253 0.0928  90  GLU A CB  
703  C CG  . GLU A 90  ? 0.6543 0.6360 0.8352 -0.1314 -0.0071 0.1000  90  GLU A CG  
704  C CD  . GLU A 90  ? 0.7957 0.7651 0.9903 -0.1320 0.0091  0.1211  90  GLU A CD  
705  O OE1 . GLU A 90  ? 0.8210 0.7850 1.0504 -0.1459 0.0040  0.1288  90  GLU A OE1 
706  O OE2 . GLU A 90  ? 0.7857 0.7503 0.9548 -0.1200 0.0259  0.1309  90  GLU A OE2 
707  N N   . LEU A 91  ? 0.6562 0.6591 0.7849 -0.1286 -0.0421 0.0566  91  LEU A N   
708  C CA  . LEU A 91  ? 0.6767 0.6741 0.7694 -0.1187 -0.0481 0.0432  91  LEU A CA  
709  C C   . LEU A 91  ? 0.6530 0.6604 0.7416 -0.1309 -0.0667 0.0247  91  LEU A C   
710  O O   . LEU A 91  ? 0.6291 0.6297 0.7055 -0.1301 -0.0722 0.0119  91  LEU A O   
711  C CB  . LEU A 91  ? 0.6257 0.6273 0.6904 -0.1025 -0.0412 0.0449  91  LEU A CB  
712  C CG  . LEU A 91  ? 0.6714 0.6612 0.7288 -0.0906 -0.0211 0.0616  91  LEU A CG  
713  C CD1 . LEU A 91  ? 0.6560 0.6510 0.6883 -0.0772 -0.0141 0.0620  91  LEU A CD1 
714  C CD2 . LEU A 91  ? 0.7505 0.7184 0.7905 -0.0838 -0.0197 0.0650  91  LEU A CD2 
715  N N   . VAL A 92  ? 0.5945 0.6184 0.6939 -0.1428 -0.0765 0.0230  92  VAL A N   
716  C CA  . VAL A 92  ? 0.6689 0.7028 0.7610 -0.1585 -0.0941 0.0076  92  VAL A CA  
717  C C   . VAL A 92  ? 0.6360 0.6607 0.7452 -0.1749 -0.1005 0.0033  92  VAL A C   
718  O O   . VAL A 92  ? 0.6685 0.6916 0.7629 -0.1810 -0.1073 -0.0136 92  VAL A O   
719  C CB  . VAL A 92  ? 0.6501 0.7018 0.7483 -0.1684 -0.1062 0.0098  92  VAL A CB  
720  C CG1 . VAL A 92  ? 0.6250 0.6856 0.7183 -0.1912 -0.1254 -0.0016 92  VAL A CG1 
721  C CG2 . VAL A 92  ? 0.6029 0.6621 0.6773 -0.1532 -0.1046 0.0083  92  VAL A CG2 
722  N N   . THR A 93  ? 0.6403 0.6587 0.7818 -0.1821 -0.0981 0.0174  93  THR A N   
723  C CA  . THR A 93  ? 0.6953 0.7031 0.8543 -0.1998 -0.1079 0.0142  93  THR A CA  
724  C C   . THR A 93  ? 0.7225 0.7117 0.8704 -0.1932 -0.1039 0.0035  93  THR A C   
725  O O   . THR A 93  ? 0.7318 0.7157 0.8714 -0.2046 -0.1145 -0.0136 93  THR A O   
726  C CB  . THR A 93  ? 0.6408 0.6453 0.8418 -0.2066 -0.1049 0.0343  93  THR A CB  
727  O OG1 . THR A 93  ? 0.7043 0.7261 0.9224 -0.2145 -0.1127 0.0413  93  THR A OG1 
728  C CG2 . THR A 93  ? 0.7292 0.7183 0.9486 -0.2242 -0.1165 0.0323  93  THR A CG2 
729  N N   . HIS A 94  ? 0.7004 0.6781 0.8479 -0.1753 -0.0894 0.0131  94  HIS A N   
730  C CA  . HIS A 94  ? 0.7565 0.7132 0.9005 -0.1688 -0.0883 0.0056  94  HIS A CA  
731  C C   . HIS A 94  ? 0.7359 0.6966 0.8528 -0.1630 -0.0933 -0.0189 94  HIS A C   
732  O O   . HIS A 94  ? 0.7560 0.7018 0.8744 -0.1620 -0.0970 -0.0329 94  HIS A O   
733  C CB  . HIS A 94  ? 0.7481 0.6914 0.8945 -0.1525 -0.0737 0.0241  94  HIS A CB  
734  C CG  . HIS A 94  ? 0.7480 0.6848 0.9261 -0.1596 -0.0668 0.0470  94  HIS A CG  
735  N ND1 . HIS A 94  ? 0.8557 0.7849 1.0357 -0.1492 -0.0511 0.0679  94  HIS A ND1 
736  C CD2 . HIS A 94  ? 0.7547 0.6924 0.9645 -0.1773 -0.0736 0.0533  94  HIS A CD2 
737  C CE1 . HIS A 94  ? 0.7776 0.7060 0.9914 -0.1600 -0.0463 0.0858  94  HIS A CE1 
738  N NE2 . HIS A 94  ? 0.8235 0.7567 1.0583 -0.1766 -0.0607 0.0775  94  HIS A NE2 
739  N N   . PHE A 95  ? 0.6866 0.6676 0.7818 -0.1590 -0.0936 -0.0248 95  PHE A N   
740  C CA  . PHE A 95  ? 0.7123 0.7022 0.7862 -0.1562 -0.0977 -0.0480 95  PHE A CA  
741  C C   . PHE A 95  ? 0.7352 0.7332 0.8059 -0.1776 -0.1086 -0.0662 95  PHE A C   
742  O O   . PHE A 95  ? 0.7459 0.7409 0.8099 -0.1783 -0.1099 -0.0881 95  PHE A O   
743  C CB  . PHE A 95  ? 0.6982 0.7072 0.7510 -0.1470 -0.0962 -0.0470 95  PHE A CB  
744  C CG  . PHE A 95  ? 0.6587 0.6813 0.6938 -0.1446 -0.0994 -0.0689 95  PHE A CG  
745  C CD1 . PHE A 95  ? 0.6655 0.6778 0.7012 -0.1292 -0.0954 -0.0794 95  PHE A CD1 
746  C CD2 . PHE A 95  ? 0.6512 0.6978 0.6720 -0.1585 -0.1068 -0.0780 95  PHE A CD2 
747  C CE1 . PHE A 95  ? 0.6475 0.6756 0.6735 -0.1263 -0.0965 -0.1002 95  PHE A CE1 
748  C CE2 . PHE A 95  ? 0.6718 0.7347 0.6785 -0.1575 -0.1072 -0.0975 95  PHE A CE2 
749  C CZ  . PHE A 95  ? 0.7107 0.7656 0.7218 -0.1407 -0.1010 -0.1094 95  PHE A CZ  
750  N N   . LEU A 96  ? 0.6919 0.6995 0.7674 -0.1957 -0.1170 -0.0579 96  LEU A N   
751  C CA  . LEU A 96  ? 0.7215 0.7357 0.7875 -0.2192 -0.1297 -0.0730 96  LEU A CA  
752  C C   . LEU A 96  ? 0.7378 0.7298 0.8165 -0.2287 -0.1341 -0.0814 96  LEU A C   
753  O O   . LEU A 96  ? 0.7643 0.7575 0.8274 -0.2450 -0.1421 -0.1012 96  LEU A O   
754  C CB  . LEU A 96  ? 0.6937 0.7207 0.7648 -0.2369 -0.1416 -0.0588 96  LEU A CB  
755  C CG  . LEU A 96  ? 0.6798 0.7277 0.7388 -0.2307 -0.1417 -0.0519 96  LEU A CG  
756  C CD1 . LEU A 96  ? 0.4992 0.5554 0.5726 -0.2476 -0.1561 -0.0366 96  LEU A CD1 
757  C CD2 . LEU A 96  ? 0.6100 0.6754 0.6375 -0.2331 -0.1430 -0.0711 96  LEU A CD2 
758  N N   . THR A 97  ? 0.7884 0.7597 0.8932 -0.2200 -0.1294 -0.0669 97  THR A N   
759  C CA  . THR A 97  ? 0.7426 0.6899 0.8639 -0.2299 -0.1364 -0.0717 97  THR A CA  
760  C C   . THR A 97  ? 0.8526 0.7806 0.9752 -0.2140 -0.1306 -0.0864 97  THR A C   
761  O O   . THR A 97  ? 0.8983 0.8018 1.0392 -0.2183 -0.1364 -0.0875 97  THR A O   
762  C CB  . THR A 97  ? 0.7671 0.7037 0.9231 -0.2346 -0.1378 -0.0439 97  THR A CB  
763  O OG1 . THR A 97  ? 0.7703 0.7046 0.9370 -0.2140 -0.1224 -0.0255 97  THR A OG1 
764  C CG2 . THR A 97  ? 0.7919 0.7457 0.9551 -0.2516 -0.1471 -0.0313 97  THR A CG2 
765  N N   . THR A 98  ? 0.9065 0.8438 1.0136 -0.1959 -0.1215 -0.0972 98  THR A N   
766  C CA  . THR A 98  ? 0.9904 0.9098 1.1035 -0.1800 -0.1184 -0.1124 98  THR A CA  
767  C C   . THR A 98  ? 1.0415 0.9778 1.1340 -0.1763 -0.1157 -0.1436 98  THR A C   
768  O O   . THR A 98  ? 1.0392 0.9991 1.1100 -0.1903 -0.1172 -0.1532 98  THR A O   
769  C CB  . THR A 98  ? 1.0216 0.9315 1.1446 -0.1585 -0.1102 -0.0918 98  THR A CB  
770  O OG1 . THR A 98  ? 1.0254 0.9582 1.1287 -0.1481 -0.1034 -0.0888 98  THR A OG1 
771  C CG2 . THR A 98  ? 0.9609 0.8587 1.1039 -0.1634 -0.1090 -0.0606 98  THR A CG2 
772  N N   . ASP A 99  ? 1.0707 0.9958 1.1721 -0.1584 -0.1123 -0.1589 99  ASP A N   
773  C CA  . ASP A 99  ? 1.0876 1.0304 1.1775 -0.1528 -0.1074 -0.1903 99  ASP A CA  
774  C C   . ASP A 99  ? 1.0446 0.9948 1.1395 -0.1289 -0.1012 -0.1873 99  ASP A C   
775  O O   . ASP A 99  ? 1.0739 1.0332 1.1728 -0.1187 -0.0972 -0.2128 99  ASP A O   
776  C CB  . ASP A 99  ? 1.1065 1.0301 1.2075 -0.1542 -0.1107 -0.2202 99  ASP A CB  
777  C CG  . ASP A 99  ? 1.1951 1.0846 1.3273 -0.1365 -0.1151 -0.2140 99  ASP A CG  
778  O OD1 . ASP A 99  ? 1.1675 1.0400 1.3114 -0.1350 -0.1187 -0.1822 99  ASP A OD1 
779  O OD2 . ASP A 99  ? 1.2261 1.1062 1.3726 -0.1246 -0.1150 -0.2408 99  ASP A OD2 
780  N N   . VAL A 100 ? 0.8872 0.8341 0.9822 -0.1201 -0.1003 -0.1575 100 VAL A N   
781  C CA  . VAL A 100 ? 0.8556 0.8053 0.9520 -0.0988 -0.0975 -0.1515 100 VAL A CA  
782  C C   . VAL A 100 ? 0.8216 0.8062 0.8972 -0.1002 -0.0937 -0.1582 100 VAL A C   
783  O O   . VAL A 100 ? 0.8087 0.8112 0.8668 -0.1160 -0.0939 -0.1517 100 VAL A O   
784  C CB  . VAL A 100 ? 0.8512 0.7820 0.9494 -0.0908 -0.0976 -0.1171 100 VAL A CB  
785  C CG1 . VAL A 100 ? 0.8452 0.7708 0.9437 -0.0694 -0.0984 -0.1112 100 VAL A CG1 
786  C CG2 . VAL A 100 ? 0.9199 0.8195 1.0384 -0.0954 -0.1015 -0.1061 100 VAL A CG2 
787  N N   . ASP A 101 ? 0.7739 0.7681 0.8548 -0.0842 -0.0922 -0.1701 101 ASP A N   
788  C CA  . ASP A 101 ? 0.7880 0.8147 0.8522 -0.0848 -0.0899 -0.1728 101 ASP A CA  
789  C C   . ASP A 101 ? 0.7498 0.7742 0.7986 -0.0802 -0.0926 -0.1426 101 ASP A C   
790  O O   . ASP A 101 ? 0.7511 0.7500 0.8036 -0.0705 -0.0940 -0.1220 101 ASP A O   
791  C CB  . ASP A 101 ? 0.7455 0.7840 0.8255 -0.0686 -0.0882 -0.1926 101 ASP A CB  
792  C CG  . ASP A 101 ? 0.7831 0.7964 0.8797 -0.0461 -0.0944 -0.1784 101 ASP A CG  
793  O OD1 . ASP A 101 ? 0.8763 0.8595 0.9915 -0.0399 -0.0978 -0.1775 101 ASP A OD1 
794  O OD2 . ASP A 101 ? 0.7582 0.7800 0.8484 -0.0357 -0.0978 -0.1671 101 ASP A OD2 
795  N N   . SER A 102 ? 0.7427 0.5917 0.7779 -0.0525 0.0191  -0.1045 102 SER A N   
796  C CA  . SER A 102 ? 0.7645 0.6300 0.7960 -0.0578 0.0161  -0.0895 102 SER A CA  
797  C C   . SER A 102 ? 0.7105 0.5757 0.7521 -0.0531 0.0166  -0.0719 102 SER A C   
798  O O   . SER A 102 ? 0.7136 0.5806 0.7563 -0.0591 0.0147  -0.0599 102 SER A O   
799  C CB  . SER A 102 ? 0.7337 0.6203 0.7502 -0.0565 0.0175  -0.0911 102 SER A CB  
800  O OG  . SER A 102 ? 0.7001 0.5933 0.7189 -0.0470 0.0231  -0.0920 102 SER A OG  
801  N N   . LEU A 103 ? 0.7255 0.5911 0.7741 -0.0417 0.0192  -0.0698 103 LEU A N   
802  C CA  . LEU A 103 ? 0.7334 0.6021 0.7892 -0.0362 0.0171  -0.0522 103 LEU A CA  
803  C C   . LEU A 103 ? 0.7329 0.5783 0.7978 -0.0381 0.0164  -0.0417 103 LEU A C   
804  O O   . LEU A 103 ? 0.7321 0.5807 0.7943 -0.0406 0.0146  -0.0251 103 LEU A O   
805  C CB  . LEU A 103 ? 0.7349 0.6121 0.8011 -0.0225 0.0185  -0.0523 103 LEU A CB  
806  C CG  . LEU A 103 ? 0.7613 0.6463 0.8339 -0.0154 0.0134  -0.0339 103 LEU A CG  
807  C CD1 . LEU A 103 ? 0.6787 0.5851 0.7374 -0.0229 0.0094  -0.0267 103 LEU A CD1 
808  C CD2 . LEU A 103 ? 0.7898 0.6858 0.8792 -0.0007 0.0136  -0.0347 103 LEU A CD2 
809  N N   . SER A 104 ? 0.7572 0.5778 0.8322 -0.0374 0.0186  -0.0515 104 SER A N   
810  C CA  . SER A 104 ? 0.8431 0.6370 0.9297 -0.0409 0.0190  -0.0410 104 SER A CA  
811  C C   . SER A 104 ? 0.8143 0.6109 0.8971 -0.0572 0.0183  -0.0358 104 SER A C   
812  O O   . SER A 104 ? 0.7739 0.5621 0.8613 -0.0611 0.0198  -0.0176 104 SER A O   
813  C CB  . SER A 104 ? 0.8745 0.6384 0.9739 -0.0383 0.0218  -0.0568 104 SER A CB  
814  O OG  . SER A 104 ? 0.8202 0.5770 0.9302 -0.0206 0.0240  -0.0558 104 SER A OG  
815  N N   . TYR A 105 ? 0.8084 0.6184 0.8834 -0.0662 0.0166  -0.0503 105 TYR A N   
816  C CA  . TYR A 105 ? 0.7817 0.5999 0.8576 -0.0802 0.0159  -0.0460 105 TYR A CA  
817  C C   . TYR A 105 ? 0.7775 0.6150 0.8447 -0.0793 0.0175  -0.0279 105 TYR A C   
818  O O   . TYR A 105 ? 0.7338 0.5700 0.8059 -0.0866 0.0208  -0.0144 105 TYR A O   
819  C CB  . TYR A 105 ? 0.7538 0.5862 0.8229 -0.0868 0.0118  -0.0639 105 TYR A CB  
820  C CG  . TYR A 105 ? 0.7226 0.5672 0.7981 -0.0999 0.0102  -0.0607 105 TYR A CG  
821  C CD1 . TYR A 105 ? 0.6981 0.5293 0.7920 -0.1125 0.0095  -0.0636 105 TYR A CD1 
822  C CD2 . TYR A 105 ? 0.6827 0.5527 0.7493 -0.0998 0.0099  -0.0553 105 TYR A CD2 
823  C CE1 . TYR A 105 ? 0.6390 0.4865 0.7442 -0.1246 0.0085  -0.0606 105 TYR A CE1 
824  C CE2 . TYR A 105 ? 0.6904 0.5746 0.7669 -0.1096 0.0094  -0.0526 105 TYR A CE2 
825  C CZ  . TYR A 105 ? 0.6512 0.5265 0.7478 -0.1220 0.0087  -0.0548 105 TYR A CZ  
826  O OH  . TYR A 105 ? 0.6386 0.5332 0.7498 -0.1320 0.0087  -0.0520 105 TYR A OH  
827  N N   . LEU A 106 ? 0.7195 0.5751 0.7736 -0.0710 0.0162  -0.0281 106 LEU A N   
828  C CA  . LEU A 106 ? 0.7319 0.6054 0.7753 -0.0706 0.0171  -0.0153 106 LEU A CA  
829  C C   . LEU A 106 ? 0.7001 0.5660 0.7436 -0.0662 0.0184  0.0041  106 LEU A C   
830  O O   . LEU A 106 ? 0.7503 0.6260 0.7848 -0.0694 0.0211  0.0163  106 LEU A O   
831  C CB  . LEU A 106 ? 0.6942 0.5862 0.7261 -0.0644 0.0148  -0.0215 106 LEU A CB  
832  C CG  . LEU A 106 ? 0.6425 0.5445 0.6693 -0.0683 0.0141  -0.0353 106 LEU A CG  
833  C CD1 . LEU A 106 ? 0.5523 0.4704 0.5689 -0.0642 0.0136  -0.0367 106 LEU A CD1 
834  C CD2 . LEU A 106 ? 0.5403 0.4472 0.5690 -0.0773 0.0150  -0.0349 106 LEU A CD2 
835  N N   . LYS A 107 ? 0.7352 0.5839 0.7874 -0.0576 0.0170  0.0077  107 LYS A N   
836  C CA  . LYS A 107 ? 0.7236 0.5624 0.7758 -0.0522 0.0174  0.0293  107 LYS A CA  
837  C C   . LYS A 107 ? 0.7428 0.5652 0.8012 -0.0634 0.0236  0.0413  107 LYS A C   
838  O O   . LYS A 107 ? 0.7963 0.6210 0.8455 -0.0640 0.0265  0.0617  107 LYS A O   
839  C CB  . LYS A 107 ? 0.7711 0.5936 0.8359 -0.0386 0.0146  0.0305  107 LYS A CB  
840  C CG  . LYS A 107 ? 0.7607 0.6054 0.8210 -0.0257 0.0084  0.0303  107 LYS A CG  
841  C CD  . LYS A 107 ? 0.8831 0.7224 0.9588 -0.0159 0.0085  0.0148  107 LYS A CD  
842  C CE  . LYS A 107 ? 0.8558 0.7133 0.9376 -0.0005 0.0026  0.0210  107 LYS A CE  
843  N NZ  . LYS A 107 ? 0.8771 0.7170 0.9808 0.0139  0.0043  0.0177  107 LYS A NZ  
844  N N   . LYS A 108 ? 0.8496 0.6563 0.9234 -0.0733 0.0259  0.0290  108 LYS A N   
845  C CA  . LYS A 108 ? 0.8343 0.6297 0.9187 -0.0874 0.0323  0.0387  108 LYS A CA  
846  C C   . LYS A 108 ? 0.7965 0.6199 0.8708 -0.0955 0.0364  0.0432  108 LYS A C   
847  O O   . LYS A 108 ? 0.8729 0.6966 0.9467 -0.1018 0.0440  0.0615  108 LYS A O   
848  C CB  . LYS A 108 ? 0.8641 0.6419 0.9685 -0.0981 0.0316  0.0202  108 LYS A CB  
849  C CG  . LYS A 108 ? 0.9879 0.7617 1.1085 -0.1164 0.0377  0.0270  108 LYS A CG  
850  C CD  . LYS A 108 ? 1.1174 0.8645 1.2615 -0.1275 0.0361  0.0116  108 LYS A CD  
851  C CE  . LYS A 108 ? 1.1605 0.9276 1.3100 -0.1381 0.0300  -0.0123 108 LYS A CE  
852  N NZ  . LYS A 108 ? 1.2109 0.9576 1.3667 -0.1386 0.0233  -0.0374 108 LYS A NZ  
853  N N   . VAL A 109 ? 0.7439 0.5903 0.8102 -0.0946 0.0327  0.0274  109 VAL A N   
854  C CA  . VAL A 109 ? 0.7478 0.6192 0.8076 -0.1004 0.0372  0.0290  109 VAL A CA  
855  C C   . VAL A 109 ? 0.7016 0.5845 0.7406 -0.0941 0.0409  0.0452  109 VAL A C   
856  O O   . VAL A 109 ? 0.8002 0.6955 0.8348 -0.0997 0.0492  0.0546  109 VAL A O   
857  C CB  . VAL A 109 ? 0.6925 0.5814 0.7487 -0.0989 0.0318  0.0095  109 VAL A CB  
858  C CG1 . VAL A 109 ? 0.6212 0.5344 0.6717 -0.1014 0.0366  0.0108  109 VAL A CG1 
859  C CG2 . VAL A 109 ? 0.6631 0.5439 0.7362 -0.1062 0.0273  -0.0060 109 VAL A CG2 
860  N N   . SER A 110 ? 0.7304 0.6116 0.7562 -0.0823 0.0348  0.0480  110 SER A N   
861  C CA  . SER A 110 ? 0.7664 0.6608 0.7695 -0.0763 0.0354  0.0615  110 SER A CA  
862  C C   . SER A 110 ? 0.8309 0.7139 0.8305 -0.0785 0.0422  0.0862  110 SER A C   
863  O O   . SER A 110 ? 0.8534 0.7503 0.8325 -0.0784 0.0473  0.0982  110 SER A O   
864  C CB  . SER A 110 ? 0.6680 0.5671 0.6624 -0.0641 0.0252  0.0581  110 SER A CB  
865  O OG  . SER A 110 ? 0.7157 0.5947 0.7228 -0.0571 0.0212  0.0649  110 SER A OG  
866  N N   . MET A 111 ? 0.8195 0.6757 0.8375 -0.0804 0.0432  0.0941  111 MET A N   
867  C CA  . MET A 111 ? 0.8808 0.7222 0.8984 -0.0847 0.0516  0.1198  111 MET A CA  
868  C C   . MET A 111 ? 0.8995 0.7519 0.9220 -0.0998 0.0648  0.1232  111 MET A C   
869  O O   . MET A 111 ? 0.9543 0.8074 0.9662 -0.1034 0.0748  0.1457  111 MET A O   
870  C CB  . MET A 111 ? 0.9220 0.7273 0.9627 -0.0845 0.0506  0.1253  111 MET A CB  
871  C CG  . MET A 111 ? 0.9961 0.7902 1.0363 -0.0672 0.0397  0.1249  111 MET A CG  
872  S SD  . MET A 111 ? 1.2266 1.0374 1.2368 -0.0516 0.0333  0.1484  111 MET A SD  
873  C CE  . MET A 111 ? 1.5103 1.3009 1.5369 -0.0326 0.0224  0.1501  111 MET A CE  
874  N N   . GLU A 112 ? 0.8369 0.7000 0.8761 -0.1083 0.0651  0.1023  112 GLU A N   
875  C CA  . GLU A 112 ? 0.9377 0.8166 0.9885 -0.1218 0.0768  0.1033  112 GLU A CA  
876  C C   . GLU A 112 ? 0.9016 0.8125 0.9390 -0.1185 0.0783  0.0906  112 GLU A C   
877  O O   . GLU A 112 ? 0.9256 0.8541 0.9778 -0.1273 0.0864  0.0862  112 GLU A O   
878  C CB  . GLU A 112 ? 1.0112 0.8800 1.0965 -0.1348 0.0754  0.0901  112 GLU A CB  
879  C CG  . GLU A 112 ? 1.0463 0.8799 1.1454 -0.1345 0.0687  0.0886  112 GLU A CG  
880  C CD  . GLU A 112 ? 1.0947 0.9158 1.2275 -0.1518 0.0702  0.0800  112 GLU A CD  
881  O OE1 . GLU A 112 ? 0.9737 0.8065 1.1181 -0.1558 0.0626  0.0569  112 GLU A OE1 
882  O OE2 . GLU A 112 ? 1.2296 1.0296 1.3774 -0.1620 0.0787  0.0970  112 GLU A OE2 
883  N N   . GLY A 113 ? 0.8894 0.8084 0.9024 -0.1061 0.0707  0.0841  113 GLY A N   
884  C CA  . GLY A 113 ? 0.8477 0.7909 0.8504 -0.1029 0.0715  0.0695  113 GLY A CA  
885  C C   . GLY A 113 ? 0.8110 0.7739 0.8055 -0.1068 0.0865  0.0777  113 GLY A C   
886  O O   . GLY A 113 ? 0.7394 0.7209 0.7402 -0.1074 0.0912  0.0653  113 GLY A O   
887  N N   . HIS A 114 ? 0.8674 0.8265 0.8477 -0.1084 0.0952  0.0996  114 HIS A N   
888  C CA  . HIS A 114 ? 0.9254 0.9049 0.8915 -0.1109 0.1118  0.1084  114 HIS A CA  
889  C C   . HIS A 114 ? 0.9238 0.9145 0.9221 -0.1237 0.1260  0.1101  114 HIS A C   
890  O O   . HIS A 114 ? 0.8561 0.8677 0.8473 -0.1257 0.1425  0.1158  114 HIS A O   
891  C CB  . HIS A 114 ? 0.9972 0.9699 0.9343 -0.1085 0.1168  0.1340  114 HIS A CB  
892  C CG  . HIS A 114 ? 1.1140 1.0593 1.0670 -0.1141 0.1159  0.1544  114 HIS A CG  
893  N ND1 . HIS A 114 ? 1.0882 1.0278 1.0657 -0.1280 0.1302  0.1686  114 HIS A ND1 
894  C CD2 . HIS A 114 ? 1.1168 1.0379 1.0668 -0.1073 0.1031  0.1631  114 HIS A CD2 
895  C CE1 . HIS A 114 ? 1.1740 1.0831 1.1621 -0.1303 0.1262  0.1846  114 HIS A CE1 
896  N NE2 . HIS A 114 ? 1.2422 1.1396 1.2139 -0.1166 0.1100  0.1816  114 HIS A NE2 
897  N N   . LEU A 115 ? 0.8644 0.8444 0.8981 -0.1323 0.1203  0.1042  115 LEU A N   
898  C CA  . LEU A 115 ? 0.8072 0.8015 0.8769 -0.1458 0.1309  0.1040  115 LEU A CA  
899  C C   . LEU A 115 ? 0.7908 0.8090 0.8785 -0.1432 0.1271  0.0818  115 LEU A C   
900  O O   . LEU A 115 ? 0.7072 0.7431 0.8290 -0.1533 0.1335  0.0796  115 LEU A O   
901  C CB  . LEU A 115 ? 0.8971 0.8672 0.9971 -0.1585 0.1256  0.1084  115 LEU A CB  
902  C CG  . LEU A 115 ? 0.9764 0.9150 1.0614 -0.1582 0.1261  0.1300  115 LEU A CG  
903  C CD1 . LEU A 115 ? 0.9793 0.8924 1.0986 -0.1731 0.1253  0.1346  115 LEU A CD1 
904  C CD2 . LEU A 115 ? 0.9844 0.9321 1.0445 -0.1577 0.1433  0.1545  115 LEU A CD2 
905  N N   . TYR A 116 ? 0.7638 0.7834 0.8319 -0.1301 0.1167  0.0663  116 TYR A N   
906  C CA  . TYR A 116 ? 0.6968 0.7349 0.7789 -0.1252 0.1124  0.0477  116 TYR A CA  
907  C C   . TYR A 116 ? 0.6699 0.7225 0.7267 -0.1134 0.1202  0.0420  116 TYR A C   
908  O O   . TYR A 116 ? 0.7185 0.7645 0.7419 -0.1084 0.1234  0.0483  116 TYR A O   
909  C CB  . TYR A 116 ? 0.5897 0.6127 0.6734 -0.1209 0.0931  0.0330  116 TYR A CB  
910  C CG  . TYR A 116 ? 0.6679 0.6731 0.7717 -0.1310 0.0844  0.0340  116 TYR A CG  
911  C CD1 . TYR A 116 ? 0.6990 0.6776 0.7901 -0.1316 0.0810  0.0430  116 TYR A CD1 
912  C CD2 . TYR A 116 ? 0.7107 0.7258 0.8465 -0.1392 0.0786  0.0247  116 TYR A CD2 
913  C CE1 . TYR A 116 ? 0.6967 0.6553 0.8064 -0.1400 0.0741  0.0415  116 TYR A CE1 
914  C CE2 . TYR A 116 ? 0.7110 0.7083 0.8634 -0.1494 0.0703  0.0220  116 TYR A CE2 
915  C CZ  . TYR A 116 ? 0.7450 0.7121 0.8842 -0.1496 0.0689  0.0297  116 TYR A CZ  
916  O OH  . TYR A 116 ? 0.6259 0.5713 0.7819 -0.1589 0.0617  0.0247  116 TYR A OH  
917  N N   . ASN A 117 ? 0.7061 0.7783 0.7791 -0.1085 0.1224  0.0293  117 ASN A N   
918  C CA  . ASN A 117 ? 0.6563 0.7343 0.7069 -0.0956 0.1256  0.0178  117 ASN A CA  
919  C C   . ASN A 117 ? 0.6297 0.6863 0.6603 -0.0890 0.1086  0.0080  117 ASN A C   
920  O O   . ASN A 117 ? 0.6408 0.6819 0.6773 -0.0929 0.0955  0.0090  117 ASN A O   
921  C CB  . ASN A 117 ? 0.6733 0.7746 0.7506 -0.0899 0.1317  0.0075  117 ASN A CB  
922  C CG  . ASN A 117 ? 0.7471 0.8755 0.8433 -0.0947 0.1523  0.0160  117 ASN A CG  
923  O OD1 . ASN A 117 ? 0.7689 0.9089 0.8478 -0.0882 0.1685  0.0145  117 ASN A OD1 
924  N ND2 . ASN A 117 ? 0.7601 0.8997 0.8926 -0.1069 0.1525  0.0238  117 ASN A ND2 
925  N N   . GLY A 118 ? 0.6387 0.6948 0.6469 -0.0794 0.1099  -0.0027 118 GLY A N   
926  C CA  . GLY A 118 ? 0.6276 0.6654 0.6170 -0.0751 0.0959  -0.0109 118 GLY A CA  
927  C C   . GLY A 118 ? 0.5861 0.6160 0.5956 -0.0749 0.0829  -0.0171 118 GLY A C   
928  O O   . GLY A 118 ? 0.4964 0.5363 0.5279 -0.0724 0.0838  -0.0219 118 GLY A O   
929  N N   . PHE A 119 ? 0.5893 0.6031 0.5906 -0.0766 0.0710  -0.0165 119 PHE A N   
930  C CA  . PHE A 119 ? 0.5930 0.5992 0.6073 -0.0764 0.0597  -0.0222 119 PHE A CA  
931  C C   . PHE A 119 ? 0.5998 0.5909 0.5982 -0.0750 0.0503  -0.0250 119 PHE A C   
932  O O   . PHE A 119 ? 0.6276 0.6143 0.6116 -0.0759 0.0497  -0.0195 119 PHE A O   
933  C CB  . PHE A 119 ? 0.6287 0.6371 0.6659 -0.0841 0.0567  -0.0168 119 PHE A CB  
934  C CG  . PHE A 119 ? 0.5604 0.5556 0.5937 -0.0901 0.0545  -0.0081 119 PHE A CG  
935  C CD1 . PHE A 119 ? 0.5238 0.5034 0.5519 -0.0892 0.0445  -0.0114 119 PHE A CD1 
936  C CD2 . PHE A 119 ? 0.6422 0.6402 0.6784 -0.0961 0.0638  0.0044  119 PHE A CD2 
937  C CE1 . PHE A 119 ? 0.5388 0.5045 0.5663 -0.0924 0.0428  -0.0036 119 PHE A CE1 
938  C CE2 . PHE A 119 ? 0.6437 0.6256 0.6776 -0.1003 0.0619  0.0145  119 PHE A CE2 
939  C CZ  . PHE A 119 ? 0.6436 0.6088 0.6741 -0.0976 0.0509  0.0099  119 PHE A CZ  
940  N N   . ASN A 120 ? 0.5478 0.5330 0.5495 -0.0724 0.0432  -0.0324 120 ASN A N   
941  C CA  . ASN A 120 ? 0.5658 0.5398 0.5596 -0.0722 0.0353  -0.0350 120 ASN A CA  
942  C C   . ASN A 120 ? 0.6743 0.6442 0.6799 -0.0745 0.0291  -0.0357 120 ASN A C   
943  O O   . ASN A 120 ? 0.6170 0.5931 0.6342 -0.0747 0.0279  -0.0375 120 ASN A O   
944  C CB  . ASN A 120 ? 0.5711 0.5408 0.5564 -0.0684 0.0343  -0.0430 120 ASN A CB  
945  C CG  . ASN A 120 ? 0.5938 0.5667 0.5673 -0.0664 0.0403  -0.0469 120 ASN A CG  
946  O OD1 . ASN A 120 ? 0.5414 0.5140 0.5016 -0.0677 0.0384  -0.0478 120 ASN A OD1 
947  N ND2 . ASN A 120 ? 0.5474 0.5249 0.5262 -0.0626 0.0471  -0.0501 120 ASN A ND2 
948  N N   . LEU A 121 ? 0.6119 0.5730 0.6146 -0.0756 0.0247  -0.0353 121 LEU A N   
949  C CA  . LEU A 121 ? 0.6007 0.5564 0.6118 -0.0781 0.0197  -0.0383 121 LEU A CA  
950  C C   . LEU A 121 ? 0.5277 0.4761 0.5312 -0.0751 0.0164  -0.0432 121 LEU A C   
951  O O   . LEU A 121 ? 0.6029 0.5481 0.6027 -0.0729 0.0167  -0.0409 121 LEU A O   
952  C CB  . LEU A 121 ? 0.5817 0.5320 0.6028 -0.0831 0.0209  -0.0326 121 LEU A CB  
953  C CG  . LEU A 121 ? 0.6200 0.5622 0.6515 -0.0875 0.0159  -0.0386 121 LEU A CG  
954  C CD1 . LEU A 121 ? 0.6306 0.5840 0.6701 -0.0904 0.0116  -0.0450 121 LEU A CD1 
955  C CD2 . LEU A 121 ? 0.5758 0.5079 0.6191 -0.0935 0.0186  -0.0315 121 LEU A CD2 
956  N N   . ILE A 122 ? 0.5857 0.5341 0.5872 -0.0744 0.0133  -0.0491 122 ILE A N   
957  C CA  . ILE A 122 ? 0.6088 0.5524 0.6035 -0.0722 0.0123  -0.0542 122 ILE A CA  
958  C C   . ILE A 122 ? 0.6266 0.5644 0.6247 -0.0742 0.0089  -0.0605 122 ILE A C   
959  O O   . ILE A 122 ? 0.5693 0.5106 0.5709 -0.0776 0.0045  -0.0634 122 ILE A O   
960  C CB  . ILE A 122 ? 0.6426 0.5890 0.6280 -0.0701 0.0127  -0.0553 122 ILE A CB  
961  C CG1 . ILE A 122 ? 0.6208 0.5684 0.6042 -0.0692 0.0164  -0.0519 122 ILE A CG1 
962  C CG2 . ILE A 122 ? 0.7078 0.6515 0.6852 -0.0687 0.0139  -0.0599 122 ILE A CG2 
963  C CD1 . ILE A 122 ? 0.6438 0.5917 0.6271 -0.0695 0.0183  -0.0524 122 ILE A CD1 
964  N N   . ALA A 123 ? 0.6302 0.5601 0.6289 -0.0719 0.0104  -0.0641 123 ALA A N   
965  C CA  . ALA A 123 ? 0.5700 0.4909 0.5701 -0.0730 0.0082  -0.0739 123 ALA A CA  
966  C C   . ALA A 123 ? 0.6486 0.5685 0.6402 -0.0672 0.0122  -0.0807 123 ALA A C   
967  O O   . ALA A 123 ? 0.6219 0.5440 0.6171 -0.0625 0.0163  -0.0766 123 ALA A O   
968  C CB  . ALA A 123 ? 0.6196 0.5275 0.6337 -0.0751 0.0083  -0.0720 123 ALA A CB  
969  N N   . ALA A 124 ? 0.6211 0.5403 0.6017 -0.0676 0.0108  -0.0914 124 ALA A N   
970  C CA  . ALA A 124 ? 0.6585 0.5804 0.6276 -0.0624 0.0171  -0.0976 124 ALA A CA  
971  C C   . ALA A 124 ? 0.7436 0.6566 0.7060 -0.0616 0.0168  -0.1138 124 ALA A C   
972  O O   . ALA A 124 ? 0.7160 0.6265 0.6730 -0.0669 0.0092  -0.1212 124 ALA A O   
973  C CB  . ALA A 124 ? 0.6339 0.5670 0.5868 -0.0631 0.0180  -0.0925 124 ALA A CB  
974  N N   . ASP A 125 ? 0.7832 0.6928 0.7475 -0.0546 0.0250  -0.1206 125 ASP A N   
975  C CA  . ASP A 125 ? 0.7660 0.6675 0.7201 -0.0517 0.0280  -0.1390 125 ASP A CA  
976  C C   . ASP A 125 ? 0.7335 0.6491 0.6649 -0.0487 0.0357  -0.1419 125 ASP A C   
977  O O   . ASP A 125 ? 0.7002 0.6263 0.6364 -0.0443 0.0450  -0.1344 125 ASP A O   
978  C CB  . ASP A 125 ? 0.7494 0.6374 0.7219 -0.0437 0.0342  -0.1453 125 ASP A CB  
979  C CG  . ASP A 125 ? 0.8167 0.6897 0.8111 -0.0460 0.0283  -0.1372 125 ASP A CG  
980  O OD1 . ASP A 125 ? 0.7841 0.6507 0.7787 -0.0555 0.0200  -0.1372 125 ASP A OD1 
981  O OD2 . ASP A 125 ? 0.7748 0.6442 0.7868 -0.0382 0.0321  -0.1298 125 ASP A OD2 
982  N N   . LEU A 126 ? 0.7953 0.7124 0.7022 -0.0517 0.0316  -0.1521 126 LEU A N   
983  C CA  . LEU A 126 ? 0.8034 0.7330 0.6828 -0.0490 0.0395  -0.1536 126 LEU A CA  
984  C C   . LEU A 126 ? 0.8240 0.7476 0.6894 -0.0440 0.0464  -0.1761 126 LEU A C   
985  O O   . LEU A 126 ? 0.8096 0.7229 0.6664 -0.0473 0.0374  -0.1925 126 LEU A O   
986  C CB  . LEU A 126 ? 0.8011 0.7391 0.6579 -0.0543 0.0292  -0.1466 126 LEU A CB  
987  C CG  . LEU A 126 ? 0.7896 0.7313 0.6615 -0.0580 0.0227  -0.1271 126 LEU A CG  
988  C CD1 . LEU A 126 ? 0.8026 0.7519 0.6568 -0.0609 0.0107  -0.1215 126 LEU A CD1 
989  C CD2 . LEU A 126 ? 0.7657 0.7133 0.6443 -0.0558 0.0342  -0.1125 126 LEU A CD2 
990  N N   . SER A 127 ? 0.8926 0.8234 0.7576 -0.0364 0.0627  -0.1783 127 SER A N   
991  C CA  . SER A 127 ? 0.9511 0.8768 0.8053 -0.0291 0.0729  -0.2009 127 SER A CA  
992  C C   . SER A 127 ? 0.9512 0.8964 0.7878 -0.0241 0.0909  -0.1979 127 SER A C   
993  O O   . SER A 127 ? 0.9333 0.8902 0.7919 -0.0207 0.1018  -0.1858 127 SER A O   
994  C CB  . SER A 127 ? 0.9170 0.8275 0.8050 -0.0215 0.0768  -0.2089 127 SER A CB  
995  O OG  . SER A 127 ? 1.0336 0.9334 0.9122 -0.0141 0.0852  -0.2343 127 SER A OG  
996  N N   . THR A 128 ? 0.9989 0.9495 0.7954 -0.0247 0.0937  -0.2082 128 THR A N   
997  C CA  . THR A 128 ? 1.1217 1.0911 0.8978 -0.0204 0.1135  -0.2053 128 THR A CA  
998  C C   . THR A 128 ? 1.1347 1.1071 0.9329 -0.0093 0.1326  -0.2187 128 THR A C   
999  O O   . THR A 128 ? 1.0628 1.0545 0.8705 -0.0062 0.1503  -0.2088 128 THR A O   
1000 C CB  . THR A 128 ? 1.1566 1.1302 0.8808 -0.0217 0.1124  -0.2162 128 THR A CB  
1001 O OG1 . THR A 128 ? 1.1498 1.1171 0.8614 -0.0299 0.0891  -0.2113 128 THR A OG1 
1002 C CG2 . THR A 128 ? 1.0842 1.0783 0.7822 -0.0216 0.1293  -0.1999 128 THR A CG2 
1003 N N   . ALA A 129 ? 1.3116 1.2651 1.1221 -0.0032 0.1294  -0.2407 129 ALA A N   
1004 C CA  . ALA A 129 ? 1.1813 1.1349 1.0149 0.0103  0.1466  -0.2554 129 ALA A CA  
1005 C C   . ALA A 129 ? 1.2670 1.2199 1.1519 0.0148  0.1446  -0.2413 129 ALA A C   
1006 O O   . ALA A 129 ? 1.2822 1.2548 1.1909 0.0226  0.1598  -0.2352 129 ALA A O   
1007 C CB  . ALA A 129 ? 1.2571 1.1864 1.0792 0.0157  0.1446  -0.2872 129 ALA A CB  
1008 N N   . LYS A 130 ? 1.1342 1.0669 1.0364 0.0099  0.1259  -0.2356 130 LYS A N   
1009 C CA  . LYS A 130 ? 1.0097 0.9385 0.9557 0.0158  0.1227  -0.2241 130 LYS A CA  
1010 C C   . LYS A 130 ? 1.0060 0.9567 0.9679 0.0099  0.1201  -0.1978 130 LYS A C   
1011 O O   . LYS A 130 ? 1.0450 1.0053 1.0412 0.0169  0.1223  -0.1887 130 LYS A O   
1012 C CB  . LYS A 130 ? 0.9175 0.8159 0.8739 0.0121  0.1057  -0.2268 130 LYS A CB  
1013 N N   . GLY A 131 ? 0.9712 0.9295 0.9099 -0.0023 0.1144  -0.1860 131 GLY A N   
1014 C CA  . GLY A 131 ? 0.8225 0.7976 0.7748 -0.0090 0.1123  -0.1637 131 GLY A CA  
1015 C C   . GLY A 131 ? 0.8344 0.7966 0.7895 -0.0177 0.0936  -0.1517 131 GLY A C   
1016 O O   . GLY A 131 ? 0.8205 0.7650 0.7881 -0.0159 0.0837  -0.1551 131 GLY A O   
1017 N N   . ASP A 132 ? 0.8320 0.8026 0.7767 -0.0271 0.0902  -0.1369 132 ASP A N   
1018 C CA  . ASP A 132 ? 0.8173 0.7780 0.7618 -0.0348 0.0747  -0.1267 132 ASP A CA  
1019 C C   . ASP A 132 ? 0.7465 0.7085 0.7208 -0.0341 0.0690  -0.1167 132 ASP A C   
1020 O O   . ASP A 132 ? 0.8159 0.7933 0.8091 -0.0315 0.0755  -0.1116 132 ASP A O   
1021 C CB  . ASP A 132 ? 0.7522 0.7194 0.6772 -0.0428 0.0739  -0.1145 132 ASP A CB  
1022 C CG  . ASP A 132 ? 0.8114 0.7797 0.7023 -0.0430 0.0782  -0.1209 132 ASP A CG  
1023 O OD1 . ASP A 132 ? 0.7957 0.7546 0.6730 -0.0411 0.0725  -0.1353 132 ASP A OD1 
1024 O OD2 . ASP A 132 ? 0.9420 0.9205 0.8192 -0.0455 0.0872  -0.1114 132 ASP A OD2 
1025 N N   . VAL A 133 ? 0.6977 0.6458 0.6757 -0.0370 0.0568  -0.1137 133 VAL A N   
1026 C CA  . VAL A 133 ? 0.6904 0.6390 0.6890 -0.0371 0.0502  -0.1028 133 VAL A CA  
1027 C C   . VAL A 133 ? 0.6102 0.5535 0.6001 -0.0456 0.0407  -0.0945 133 VAL A C   
1028 O O   . VAL A 133 ? 0.6527 0.5853 0.6325 -0.0489 0.0354  -0.0990 133 VAL A O   
1029 C CB  . VAL A 133 ? 0.6447 0.5800 0.6603 -0.0294 0.0476  -0.1065 133 VAL A CB  
1030 C CG1 . VAL A 133 ? 0.6229 0.5600 0.6541 -0.0292 0.0400  -0.0925 133 VAL A CG1 
1031 C CG2 . VAL A 133 ? 0.5510 0.4917 0.5783 -0.0182 0.0579  -0.1159 133 VAL A CG2 
1032 N N   . ILE A 134 ? 0.5770 0.5293 0.5725 -0.0492 0.0387  -0.0839 134 ILE A N   
1033 C CA  . ILE A 134 ? 0.5757 0.5240 0.5663 -0.0552 0.0315  -0.0767 134 ILE A CA  
1034 C C   . ILE A 134 ? 0.5970 0.5475 0.6010 -0.0542 0.0271  -0.0694 134 ILE A C   
1035 O O   . ILE A 134 ? 0.6019 0.5641 0.6156 -0.0527 0.0284  -0.0668 134 ILE A O   
1036 C CB  . ILE A 134 ? 0.6373 0.5911 0.6172 -0.0602 0.0337  -0.0720 134 ILE A CB  
1037 C CG1 . ILE A 134 ? 0.6490 0.6022 0.6116 -0.0600 0.0381  -0.0764 134 ILE A CG1 
1038 C CG2 . ILE A 134 ? 0.5669 0.5162 0.5438 -0.0640 0.0273  -0.0663 134 ILE A CG2 
1039 C CD1 . ILE A 134 ? 0.6974 0.6516 0.6477 -0.0639 0.0397  -0.0686 134 ILE A CD1 
1040 N N   . CYS A 135 ? 0.6351 0.5764 0.6397 -0.0557 0.0219  -0.0659 135 CYS A N   
1041 C CA  . CYS A 135 ? 0.6192 0.5619 0.6307 -0.0547 0.0180  -0.0571 135 CYS A CA  
1042 C C   . CYS A 135 ? 0.6605 0.6032 0.6644 -0.0606 0.0159  -0.0523 135 CYS A C   
1043 O O   . CYS A 135 ? 0.5658 0.5058 0.5638 -0.0642 0.0161  -0.0552 135 CYS A O   
1044 C CB  . CYS A 135 ? 0.6584 0.5886 0.6792 -0.0502 0.0165  -0.0547 135 CYS A CB  
1045 S SG  . CYS A 135 ? 0.6614 0.5878 0.6937 -0.0405 0.0206  -0.0630 135 CYS A SG  
1046 N N   . TYR A 136 ? 0.6213 0.5691 0.6251 -0.0604 0.0136  -0.0451 136 TYR A N   
1047 C CA  . TYR A 136 ? 0.5402 0.4904 0.5363 -0.0645 0.0137  -0.0419 136 TYR A CA  
1048 C C   . TYR A 136 ? 0.5491 0.4996 0.5435 -0.0635 0.0124  -0.0324 136 TYR A C   
1049 O O   . TYR A 136 ? 0.6185 0.5728 0.6146 -0.0592 0.0089  -0.0275 136 TYR A O   
1050 C CB  . TYR A 136 ? 0.5069 0.4652 0.4975 -0.0666 0.0142  -0.0456 136 TYR A CB  
1051 C CG  . TYR A 136 ? 0.6294 0.5904 0.6116 -0.0686 0.0147  -0.0440 136 TYR A CG  
1052 C CD1 . TYR A 136 ? 0.5976 0.5554 0.5778 -0.0700 0.0182  -0.0442 136 TYR A CD1 
1053 C CD2 . TYR A 136 ? 0.6286 0.5979 0.6050 -0.0686 0.0116  -0.0432 136 TYR A CD2 
1054 C CE1 . TYR A 136 ? 0.6191 0.5804 0.5923 -0.0704 0.0210  -0.0442 136 TYR A CE1 
1055 C CE2 . TYR A 136 ? 0.5077 0.4796 0.4726 -0.0701 0.0133  -0.0442 136 TYR A CE2 
1056 C CZ  . TYR A 136 ? 0.6387 0.6058 0.6022 -0.0706 0.0193  -0.0449 136 TYR A CZ  
1057 O OH  . TYR A 136 ? 0.5417 0.5122 0.4945 -0.0706 0.0234  -0.0472 136 TYR A OH  
1058 N N   . TYR A 137 ? 0.5474 0.4959 0.5391 -0.0671 0.0153  -0.0286 137 TYR A N   
1059 C CA  . TYR A 137 ? 0.6187 0.5688 0.6047 -0.0672 0.0167  -0.0179 137 TYR A CA  
1060 C C   . TYR A 137 ? 0.6572 0.6131 0.6383 -0.0711 0.0225  -0.0183 137 TYR A C   
1061 O O   . TYR A 137 ? 0.5800 0.5349 0.5698 -0.0740 0.0246  -0.0227 137 TYR A O   
1062 C CB  . TYR A 137 ? 0.6501 0.5878 0.6452 -0.0671 0.0173  -0.0085 137 TYR A CB  
1063 C CG  . TYR A 137 ? 0.5796 0.5183 0.5683 -0.0694 0.0217  0.0051  137 TYR A CG  
1064 C CD1 . TYR A 137 ? 0.6809 0.6251 0.6558 -0.0648 0.0194  0.0156  137 TYR A CD1 
1065 C CD2 . TYR A 137 ? 0.6050 0.5420 0.6010 -0.0765 0.0284  0.0080  137 TYR A CD2 
1066 C CE1 . TYR A 137 ? 0.6617 0.6075 0.6257 -0.0667 0.0250  0.0298  137 TYR A CE1 
1067 C CE2 . TYR A 137 ? 0.6770 0.6167 0.6672 -0.0794 0.0354  0.0217  137 TYR A CE2 
1068 C CZ  . TYR A 137 ? 0.6901 0.6333 0.6619 -0.0743 0.0343  0.0331  137 TYR A CZ  
1069 O OH  . TYR A 137 ? 0.6991 0.6455 0.6607 -0.0770 0.0426  0.0484  137 TYR A OH  
1070 N N   . GLY A 138 ? 0.5609 0.5248 0.5281 -0.0704 0.0247  -0.0141 138 GLY A N   
1071 C CA  . GLY A 138 ? 0.6163 0.5872 0.5787 -0.0725 0.0328  -0.0142 138 GLY A CA  
1072 C C   . GLY A 138 ? 0.6209 0.5967 0.5697 -0.0727 0.0376  -0.0021 138 GLY A C   
1073 O O   . GLY A 138 ? 0.6334 0.6122 0.5667 -0.0696 0.0326  0.0019  138 GLY A O   
1074 N N   . ASN A 139 ? 0.5336 0.5127 0.4881 -0.0764 0.0473  0.0048  139 ASN A N   
1075 C CA  . ASN A 139 ? 0.5671 0.5502 0.5084 -0.0776 0.0545  0.0199  139 ASN A CA  
1076 C C   . ASN A 139 ? 0.6365 0.6333 0.5523 -0.0747 0.0602  0.0157  139 ASN A C   
1077 O O   . ASN A 139 ? 0.5961 0.5997 0.4971 -0.0757 0.0692  0.0276  139 ASN A O   
1078 C CB  . ASN A 139 ? 0.6169 0.6003 0.5773 -0.0847 0.0647  0.0290  139 ASN A CB  
1079 C CG  . ASN A 139 ? 0.6198 0.6184 0.5892 -0.0860 0.0742  0.0199  139 ASN A CG  
1080 O OD1 . ASN A 139 ? 0.6778 0.6806 0.6440 -0.0811 0.0716  0.0055  139 ASN A OD1 
1081 N ND2 . ASN A 139 ? 0.6285 0.6356 0.6121 -0.0923 0.0860  0.0290  139 ASN A ND2 
1082 N N   . ARG A 140 ? 0.6160 0.6158 0.5258 -0.0716 0.0563  -0.0013 140 ARG A N   
1083 C CA  . ARG A 140 ? 0.6105 0.6198 0.4942 -0.0689 0.0596  -0.0099 140 ARG A CA  
1084 C C   . ARG A 140 ? 0.5853 0.5940 0.4552 -0.0671 0.0459  -0.0182 140 ARG A C   
1085 O O   . ARG A 140 ? 0.6196 0.6353 0.4676 -0.0661 0.0458  -0.0293 140 ARG A O   
1086 C CB  . ARG A 140 ? 0.6254 0.6380 0.5163 -0.0673 0.0688  -0.0251 140 ARG A CB  
1087 C CG  . ARG A 140 ? 0.6251 0.6468 0.5300 -0.0684 0.0838  -0.0181 140 ARG A CG  
1088 C CD  . ARG A 140 ? 0.6807 0.7154 0.5606 -0.0679 0.0967  -0.0116 140 ARG A CD  
1089 N NE  . ARG A 140 ? 0.6933 0.7404 0.5905 -0.0700 0.1132  -0.0043 140 ARG A NE  
1090 C CZ  . ARG A 140 ? 0.6651 0.7137 0.5769 -0.0768 0.1177  0.0142  140 ARG A CZ  
1091 N NH1 . ARG A 140 ? 0.7365 0.7719 0.6463 -0.0805 0.1075  0.0276  140 ARG A NH1 
1092 N NH2 . ARG A 140 ? 0.6581 0.7217 0.5900 -0.0799 0.1333  0.0189  140 ARG A NH2 
1093 N N   . GLY A 141 ? 0.5869 0.5889 0.4707 -0.0671 0.0348  -0.0148 141 GLY A N   
1094 C CA  . GLY A 141 ? 0.5542 0.5602 0.4314 -0.0660 0.0217  -0.0211 141 GLY A CA  
1095 C C   . GLY A 141 ? 0.6068 0.6156 0.4816 -0.0625 0.0129  -0.0046 141 GLY A C   
1096 O O   . GLY A 141 ? 0.6187 0.6295 0.4793 -0.0607 0.0166  0.0110  141 GLY A O   
1097 N N   . GLU A 142 ? 0.6111 0.6201 0.5007 -0.0607 0.0022  -0.0067 142 GLU A N   
1098 C CA  . GLU A 142 ? 0.6860 0.6985 0.5768 -0.0546 -0.0072 0.0085  142 GLU A CA  
1099 C C   . GLU A 142 ? 0.6900 0.6859 0.5951 -0.0525 -0.0011 0.0242  142 GLU A C   
1100 O O   . GLU A 142 ? 0.6508 0.6348 0.5733 -0.0560 0.0058  0.0188  142 GLU A O   
1101 C CB  . GLU A 142 ? 0.6580 0.6787 0.5660 -0.0526 -0.0187 0.0005  142 GLU A CB  
1102 C CG  . GLU A 142 ? 0.6734 0.7114 0.5706 -0.0567 -0.0271 -0.0147 142 GLU A CG  
1103 C CD  . GLU A 142 ? 0.8467 0.9007 0.7155 -0.0539 -0.0356 -0.0082 142 GLU A CD  
1104 O OE1 . GLU A 142 ? 0.7874 0.8542 0.6414 -0.0588 -0.0416 -0.0233 142 GLU A OE1 
1105 O OE2 . GLU A 142 ? 0.8730 0.9257 0.7326 -0.0472 -0.0364 0.0120  142 GLU A OE2 
1106 N N   . PRO A 143 ? 0.7486 0.7427 0.6466 -0.0469 -0.0042 0.0440  143 PRO A N   
1107 C CA  . PRO A 143 ? 0.7172 0.6912 0.6292 -0.0466 0.0029  0.0590  143 PRO A CA  
1108 C C   . PRO A 143 ? 0.7909 0.7512 0.7317 -0.0436 0.0000  0.0540  143 PRO A C   
1109 O O   . PRO A 143 ? 0.7022 0.6443 0.6580 -0.0474 0.0073  0.0560  143 PRO A O   
1110 C CB  . PRO A 143 ? 0.6937 0.6683 0.5887 -0.0400 -0.0008 0.0831  143 PRO A CB  
1111 C CG  . PRO A 143 ? 0.7524 0.7484 0.6353 -0.0333 -0.0159 0.0790  143 PRO A CG  
1112 C CD  . PRO A 143 ? 0.7201 0.7298 0.5975 -0.0405 -0.0154 0.0541  143 PRO A CD  
1113 N N   . ASP A 144 ? 0.7519 0.7221 0.7015 -0.0376 -0.0099 0.0462  144 ASP A N   
1114 C CA  . ASP A 144 ? 0.7393 0.6982 0.7145 -0.0325 -0.0113 0.0424  144 ASP A CA  
1115 C C   . ASP A 144 ? 0.6582 0.6180 0.6437 -0.0384 -0.0073 0.0220  144 ASP A C   
1116 O O   . ASP A 144 ? 0.6810 0.6565 0.6603 -0.0420 -0.0097 0.0108  144 ASP A O   
1117 C CB  . ASP A 144 ? 0.7593 0.7314 0.7427 -0.0209 -0.0229 0.0475  144 ASP A CB  
1118 C CG  . ASP A 144 ? 0.8001 0.7685 0.7747 -0.0120 -0.0282 0.0715  144 ASP A CG  
1119 O OD1 . ASP A 144 ? 0.8366 0.7807 0.8135 -0.0120 -0.0210 0.0846  144 ASP A OD1 
1120 O OD2 . ASP A 144 ? 0.8771 0.8670 0.8427 -0.0056 -0.0400 0.0777  144 ASP A OD2 
1121 N N   . PRO A 145 ? 0.6701 0.6127 0.6701 -0.0400 -0.0016 0.0167  145 PRO A N   
1122 C CA  . PRO A 145 ? 0.6425 0.5872 0.6493 -0.0439 0.0011  -0.0007 145 PRO A CA  
1123 C C   . PRO A 145 ? 0.5601 0.5192 0.5762 -0.0382 -0.0034 -0.0075 145 PRO A C   
1124 O O   . PRO A 145 ? 0.5717 0.5365 0.5965 -0.0292 -0.0090 -0.0003 145 PRO A O   
1125 C CB  . PRO A 145 ? 0.6998 0.6236 0.7184 -0.0450 0.0059  -0.0039 145 PRO A CB  
1126 C CG  . PRO A 145 ? 0.5916 0.5014 0.6094 -0.0466 0.0079  0.0109  145 PRO A CG  
1127 C CD  . PRO A 145 ? 0.7320 0.6513 0.7406 -0.0398 0.0028  0.0261  145 PRO A CD  
1128 N N   . ILE A 146 ? 0.5326 0.4990 0.5487 -0.0434 -0.0007 -0.0203 146 ILE A N   
1129 C CA  . ILE A 146 ? 0.5211 0.5038 0.5482 -0.0411 -0.0026 -0.0273 146 ILE A CA  
1130 C C   . ILE A 146 ? 0.5732 0.5499 0.6066 -0.0423 0.0050  -0.0378 146 ILE A C   
1131 O O   . ILE A 146 ? 0.4786 0.4436 0.5031 -0.0477 0.0094  -0.0420 146 ILE A O   
1132 C CB  . ILE A 146 ? 0.5241 0.5232 0.5435 -0.0480 -0.0062 -0.0316 146 ILE A CB  
1133 C CG1 . ILE A 146 ? 0.4954 0.4852 0.5019 -0.0566 -0.0004 -0.0379 146 ILE A CG1 
1134 C CG2 . ILE A 146 ? 0.5120 0.5210 0.5216 -0.0458 -0.0150 -0.0229 146 ILE A CG2 
1135 C CD1 . ILE A 146 ? 0.5205 0.5205 0.5228 -0.0637 -0.0019 -0.0454 146 ILE A CD1 
1136 N N   . VAL A 147 ? 0.5376 0.5250 0.5867 -0.0366 0.0064  -0.0417 147 VAL A N   
1137 C CA  . VAL A 147 ? 0.6377 0.6244 0.6902 -0.0374 0.0151  -0.0518 147 VAL A CA  
1138 C C   . VAL A 147 ? 0.6159 0.6183 0.6681 -0.0455 0.0173  -0.0555 147 VAL A C   
1139 O O   . VAL A 147 ? 0.5766 0.5984 0.6415 -0.0459 0.0132  -0.0543 147 VAL A O   
1140 C CB  . VAL A 147 ? 0.6103 0.6007 0.6815 -0.0260 0.0187  -0.0547 147 VAL A CB  
1141 C CG1 . VAL A 147 ? 0.4701 0.4592 0.5389 -0.0268 0.0297  -0.0661 147 VAL A CG1 
1142 C CG2 . VAL A 147 ? 0.5716 0.5422 0.6460 -0.0177 0.0156  -0.0494 147 VAL A CG2 
1143 N N   . LEU A 148 ? 0.5606 0.5545 0.5996 -0.0524 0.0230  -0.0595 148 LEU A N   
1144 C CA  . LEU A 148 ? 0.5828 0.5848 0.6205 -0.0611 0.0260  -0.0611 148 LEU A CA  
1145 C C   . LEU A 148 ? 0.5724 0.5876 0.6224 -0.0612 0.0350  -0.0648 148 LEU A C   
1146 O O   . LEU A 148 ? 0.5479 0.5597 0.5960 -0.0558 0.0421  -0.0683 148 LEU A O   
1147 C CB  . LEU A 148 ? 0.6132 0.5997 0.6324 -0.0666 0.0283  -0.0610 148 LEU A CB  
1148 C CG  . LEU A 148 ? 0.5637 0.5396 0.5725 -0.0671 0.0224  -0.0580 148 LEU A CG  
1149 C CD1 . LEU A 148 ? 0.6120 0.5769 0.6081 -0.0706 0.0250  -0.0578 148 LEU A CD1 
1150 C CD2 . LEU A 148 ? 0.6384 0.6220 0.6492 -0.0695 0.0165  -0.0565 148 LEU A CD2 
1151 N N   . THR A 149 ? 0.5406 0.5718 0.6037 -0.0681 0.0355  -0.0650 149 THR A N   
1152 C CA  . THR A 149 ? 0.5871 0.6325 0.6630 -0.0715 0.0467  -0.0670 149 THR A CA  
1153 C C   . THR A 149 ? 0.6194 0.6500 0.6767 -0.0788 0.0556  -0.0650 149 THR A C   
1154 O O   . THR A 149 ? 0.5811 0.5946 0.6223 -0.0827 0.0513  -0.0626 149 THR A O   
1155 C CB  . THR A 149 ? 0.5253 0.5944 0.6259 -0.0787 0.0433  -0.0679 149 THR A CB  
1156 O OG1 . THR A 149 ? 0.5914 0.6512 0.6834 -0.0897 0.0377  -0.0680 149 THR A OG1 
1157 C CG2 . THR A 149 ? 0.4966 0.5834 0.6151 -0.0694 0.0324  -0.0677 149 THR A CG2 
1158 N N   . PRO A 150 ? 0.6603 0.6982 0.7193 -0.0798 0.0689  -0.0649 150 PRO A N   
1159 C CA  . PRO A 150 ? 0.6491 0.6731 0.6877 -0.0860 0.0774  -0.0597 150 PRO A CA  
1160 C C   . PRO A 150 ? 0.6113 0.6281 0.6534 -0.0980 0.0756  -0.0549 150 PRO A C   
1161 O O   . PRO A 150 ? 0.5933 0.6235 0.6580 -0.1053 0.0733  -0.0573 150 PRO A O   
1162 C CB  . PRO A 150 ? 0.6652 0.7048 0.7091 -0.0858 0.0936  -0.0597 150 PRO A CB  
1163 C CG  . PRO A 150 ? 0.5540 0.6086 0.6137 -0.0743 0.0929  -0.0680 150 PRO A CG  
1164 C CD  . PRO A 150 ? 0.5896 0.6483 0.6669 -0.0731 0.0776  -0.0690 150 PRO A CD  
1165 N N   . GLY A 151 ? 0.5860 0.5811 0.6065 -0.0996 0.0758  -0.0491 151 GLY A N   
1166 C CA  . GLY A 151 ? 0.5640 0.5459 0.5867 -0.1094 0.0754  -0.0451 151 GLY A CA  
1167 C C   . GLY A 151 ? 0.5588 0.5171 0.5595 -0.1050 0.0706  -0.0403 151 GLY A C   
1168 O O   . GLY A 151 ? 0.5518 0.5070 0.5360 -0.0961 0.0674  -0.0396 151 GLY A O   
1169 N N   . THR A 152 ? 0.5933 0.5358 0.5968 -0.1114 0.0701  -0.0380 152 THR A N   
1170 C CA  . THR A 152 ? 0.5775 0.4984 0.5660 -0.1062 0.0660  -0.0334 152 THR A CA  
1171 C C   . THR A 152 ? 0.6057 0.5249 0.5987 -0.1040 0.0560  -0.0430 152 THR A C   
1172 O O   . THR A 152 ? 0.6451 0.5661 0.6510 -0.1115 0.0541  -0.0507 152 THR A O   
1173 C CB  . THR A 152 ? 0.6713 0.5713 0.6595 -0.1128 0.0738  -0.0240 152 THR A CB  
1174 O OG1 . THR A 152 ? 0.7489 0.6517 0.7292 -0.1149 0.0847  -0.0125 152 THR A OG1 
1175 C CG2 . THR A 152 ? 0.7207 0.5994 0.6970 -0.1043 0.0691  -0.0188 152 THR A CG2 
1176 N N   . TYR A 153 ? 0.6331 0.5503 0.6152 -0.0945 0.0498  -0.0429 153 TYR A N   
1177 C CA  . TYR A 153 ? 0.6375 0.5561 0.6214 -0.0914 0.0426  -0.0504 153 TYR A CA  
1178 C C   . TYR A 153 ? 0.6418 0.5453 0.6192 -0.0853 0.0415  -0.0476 153 TYR A C   
1179 O O   . TYR A 153 ? 0.5312 0.4269 0.5013 -0.0805 0.0430  -0.0387 153 TYR A O   
1180 C CB  . TYR A 153 ? 0.6073 0.5404 0.5897 -0.0861 0.0372  -0.0527 153 TYR A CB  
1181 C CG  . TYR A 153 ? 0.6346 0.5837 0.6276 -0.0892 0.0366  -0.0566 153 TYR A CG  
1182 C CD1 . TYR A 153 ? 0.5955 0.5528 0.5917 -0.0893 0.0419  -0.0546 153 TYR A CD1 
1183 C CD2 . TYR A 153 ? 0.5543 0.5123 0.5537 -0.0907 0.0306  -0.0621 153 TYR A CD2 
1184 C CE1 . TYR A 153 ? 0.6141 0.5886 0.6246 -0.0901 0.0417  -0.0582 153 TYR A CE1 
1185 C CE2 . TYR A 153 ? 0.5751 0.5504 0.5866 -0.0916 0.0282  -0.0642 153 TYR A CE2 
1186 C CZ  . TYR A 153 ? 0.6153 0.5992 0.6350 -0.0908 0.0339  -0.0623 153 TYR A CZ  
1187 O OH  . TYR A 153 ? 0.5755 0.5790 0.6118 -0.0897 0.0319  -0.0643 153 TYR A OH  
1188 N N   . GLY A 154 ? 0.6165 0.5180 0.5963 -0.0846 0.0390  -0.0553 154 GLY A N   
1189 C CA  . GLY A 154 ? 0.5545 0.4464 0.5320 -0.0768 0.0390  -0.0547 154 GLY A CA  
1190 C C   . GLY A 154 ? 0.5512 0.4552 0.5278 -0.0734 0.0357  -0.0607 154 GLY A C   
1191 O O   . GLY A 154 ? 0.6214 0.5332 0.5971 -0.0779 0.0339  -0.0677 154 GLY A O   
1192 N N   . LEU A 155 ? 0.4953 0.4026 0.4724 -0.0656 0.0347  -0.0566 155 LEU A N   
1193 C CA  . LEU A 155 ? 0.5066 0.4264 0.4844 -0.0629 0.0338  -0.0595 155 LEU A CA  
1194 C C   . LEU A 155 ? 0.5921 0.5104 0.5761 -0.0545 0.0368  -0.0588 155 LEU A C   
1195 O O   . LEU A 155 ? 0.4960 0.4119 0.4848 -0.0489 0.0350  -0.0519 155 LEU A O   
1196 C CB  . LEU A 155 ? 0.5080 0.4404 0.4867 -0.0638 0.0294  -0.0547 155 LEU A CB  
1197 C CG  . LEU A 155 ? 0.5311 0.4749 0.5137 -0.0622 0.0295  -0.0539 155 LEU A CG  
1198 C CD1 . LEU A 155 ? 0.5725 0.5202 0.5488 -0.0644 0.0322  -0.0580 155 LEU A CD1 
1199 C CD2 . LEU A 155 ? 0.4875 0.4377 0.4733 -0.0643 0.0249  -0.0500 155 LEU A CD2 
1200 N N   . SER A 156 ? 0.4490 0.3714 0.4324 -0.0527 0.0414  -0.0656 156 SER A N   
1201 C CA  . SER A 156 ? 0.4677 0.3910 0.4597 -0.0435 0.0468  -0.0672 156 SER A CA  
1202 C C   . SER A 156 ? 0.5151 0.4566 0.5069 -0.0438 0.0507  -0.0688 156 SER A C   
1203 O O   . SER A 156 ? 0.4830 0.4349 0.4723 -0.0496 0.0470  -0.0639 156 SER A O   
1204 C CB  . SER A 156 ? 0.5611 0.4644 0.5514 -0.0403 0.0525  -0.0762 156 SER A CB  
1205 O OG  . SER A 156 ? 0.5261 0.4283 0.5287 -0.0282 0.0579  -0.0763 156 SER A OG  
1206 N N   . ASN A 157 ? 0.5447 0.4896 0.5405 -0.0369 0.0594  -0.0747 157 ASN A N   
1207 C CA  . ASN A 157 ? 0.5652 0.5289 0.5605 -0.0371 0.0663  -0.0748 157 ASN A CA  
1208 C C   . ASN A 157 ? 0.6468 0.6100 0.6196 -0.0423 0.0697  -0.0825 157 ASN A C   
1209 O O   . ASN A 157 ? 0.5974 0.5747 0.5644 -0.0420 0.0777  -0.0823 157 ASN A O   
1210 C CB  . ASN A 157 ? 0.5372 0.5094 0.5490 -0.0260 0.0758  -0.0774 157 ASN A CB  
1211 C CG  . ASN A 157 ? 0.5438 0.5203 0.5782 -0.0197 0.0696  -0.0688 157 ASN A CG  
1212 O OD1 . ASN A 157 ? 0.5753 0.5400 0.6178 -0.0100 0.0699  -0.0703 157 ASN A OD1 
1213 N ND2 . ASN A 157 ? 0.5098 0.5020 0.5539 -0.0251 0.0630  -0.0597 157 ASN A ND2 
1214 N N   . ALA A 158 ? 0.6204 0.5697 0.5806 -0.0475 0.0639  -0.0888 158 ALA A N   
1215 C CA  . ALA A 158 ? 0.5211 0.4741 0.4609 -0.0542 0.0608  -0.0930 158 ALA A CA  
1216 C C   . ALA A 158 ? 0.5344 0.4930 0.4762 -0.0602 0.0513  -0.0812 158 ALA A C   
1217 O O   . ALA A 158 ? 0.7591 0.7218 0.7141 -0.0595 0.0500  -0.0709 158 ALA A O   
1218 C CB  . ALA A 158 ? 0.4863 0.4244 0.4163 -0.0573 0.0589  -0.1083 158 ALA A CB  
1219 N N   . LEU A 159 ? 0.5007 0.4607 0.4304 -0.0657 0.0444  -0.0835 159 LEU A N   
1220 C CA  . LEU A 159 ? 0.5852 0.5485 0.5201 -0.0693 0.0359  -0.0741 159 LEU A CA  
1221 C C   . LEU A 159 ? 0.5938 0.5468 0.5404 -0.0718 0.0319  -0.0762 159 LEU A C   
1222 O O   . LEU A 159 ? 0.5082 0.4494 0.4586 -0.0713 0.0351  -0.0828 159 LEU A O   
1223 C CB  . LEU A 159 ? 0.5335 0.5067 0.4540 -0.0723 0.0292  -0.0740 159 LEU A CB  
1224 C CG  . LEU A 159 ? 0.5638 0.5473 0.4656 -0.0702 0.0338  -0.0712 159 LEU A CG  
1225 C CD1 . LEU A 159 ? 0.6328 0.6271 0.5188 -0.0721 0.0240  -0.0691 159 LEU A CD1 
1226 C CD2 . LEU A 159 ? 0.4742 0.4607 0.3841 -0.0679 0.0402  -0.0570 159 LEU A CD2 
1227 N N   . LEU A 160 ? 0.5325 0.4891 0.4851 -0.0739 0.0261  -0.0696 160 LEU A N   
1228 C CA  . LEU A 160 ? 0.6104 0.5607 0.5721 -0.0768 0.0243  -0.0706 160 LEU A CA  
1229 C C   . LEU A 160 ? 0.5135 0.4608 0.4740 -0.0828 0.0227  -0.0807 160 LEU A C   
1230 O O   . LEU A 160 ? 0.5388 0.4964 0.4936 -0.0859 0.0175  -0.0854 160 LEU A O   
1231 C CB  . LEU A 160 ? 0.5850 0.5425 0.5531 -0.0770 0.0199  -0.0639 160 LEU A CB  
1232 C CG  . LEU A 160 ? 0.5871 0.5419 0.5638 -0.0796 0.0204  -0.0640 160 LEU A CG  
1233 C CD1 . LEU A 160 ? 0.5963 0.5413 0.5734 -0.0770 0.0242  -0.0603 160 LEU A CD1 
1234 C CD2 . LEU A 160 ? 0.6163 0.5812 0.5999 -0.0784 0.0169  -0.0606 160 LEU A CD2 
1235 N N   . GLU A 161 ? 0.5843 0.5175 0.5508 -0.0850 0.0266  -0.0835 161 GLU A N   
1236 C CA  . GLU A 161 ? 0.5503 0.4765 0.5205 -0.0932 0.0262  -0.0931 161 GLU A CA  
1237 C C   . GLU A 161 ? 0.5740 0.4966 0.5339 -0.0947 0.0261  -0.1070 161 GLU A C   
1238 O O   . GLU A 161 ? 0.5925 0.5123 0.5548 -0.1036 0.0232  -0.1185 161 GLU A O   
1239 C CB  . GLU A 161 ? 0.6087 0.5503 0.5875 -0.1003 0.0202  -0.0931 161 GLU A CB  
1240 C CG  . GLU A 161 ? 0.6136 0.5560 0.6032 -0.1004 0.0235  -0.0833 161 GLU A CG  
1241 C CD  . GLU A 161 ? 0.5629 0.4879 0.5588 -0.1059 0.0304  -0.0826 161 GLU A CD  
1242 O OE1 . GLU A 161 ? 0.5075 0.4248 0.5084 -0.1143 0.0307  -0.0916 161 GLU A OE1 
1243 O OE2 . GLU A 161 ? 0.6818 0.5998 0.6766 -0.1020 0.0353  -0.0728 161 GLU A OE2 
1244 N N   . THR A 162 ? 0.5772 0.5007 0.5264 -0.0870 0.0297  -0.1076 162 THR A N   
1245 C CA  . THR A 162 ? 0.5470 0.4653 0.4840 -0.0870 0.0324  -0.1228 162 THR A CA  
1246 C C   . THR A 162 ? 0.6045 0.4972 0.5500 -0.0887 0.0380  -0.1317 162 THR A C   
1247 O O   . THR A 162 ? 0.6465 0.5264 0.6019 -0.0823 0.0436  -0.1229 162 THR A O   
1248 C CB  . THR A 162 ? 0.5165 0.4411 0.4435 -0.0775 0.0391  -0.1202 162 THR A CB  
1249 O OG1 . THR A 162 ? 0.5338 0.4770 0.4568 -0.0762 0.0352  -0.1075 162 THR A OG1 
1250 C CG2 . THR A 162 ? 0.5380 0.4618 0.4466 -0.0772 0.0426  -0.1377 162 THR A CG2 
1251 N N   . PRO A 163 ? 0.5901 0.4741 0.5328 -0.0973 0.0359  -0.1487 163 PRO A N   
1252 C CA  . PRO A 163 ? 0.5891 0.4440 0.5437 -0.1014 0.0411  -0.1559 163 PRO A CA  
1253 C C   . PRO A 163 ? 0.6064 0.4396 0.5583 -0.0907 0.0512  -0.1642 163 PRO A C   
1254 O O   . PRO A 163 ? 0.6053 0.4177 0.5562 -0.0945 0.0543  -0.1825 163 PRO A O   
1255 C CB  . PRO A 163 ? 0.6716 0.5281 0.6261 -0.1166 0.0336  -0.1732 163 PRO A CB  
1256 C CG  . PRO A 163 ? 0.6834 0.5646 0.6163 -0.1150 0.0269  -0.1818 163 PRO A CG  
1257 C CD  . PRO A 163 ? 0.7117 0.6124 0.6405 -0.1048 0.0272  -0.1617 163 PRO A CD  
1258 N N   . TRP A 164 ? 0.5869 0.4254 0.5402 -0.0773 0.0565  -0.1516 164 TRP A N   
1259 C CA  . TRP A 164 ? 0.6151 0.4336 0.5749 -0.0648 0.0664  -0.1548 164 TRP A CA  
1260 C C   . TRP A 164 ? 0.6646 0.4514 0.6397 -0.0672 0.0686  -0.1511 164 TRP A C   
1261 O O   . TRP A 164 ? 0.6363 0.4229 0.6186 -0.0741 0.0642  -0.1370 164 TRP A O   
1262 C CB  . TRP A 164 ? 0.6258 0.4604 0.5914 -0.0515 0.0694  -0.1389 164 TRP A CB  
1263 C CG  . TRP A 164 ? 0.6684 0.5284 0.6218 -0.0475 0.0721  -0.1425 164 TRP A CG  
1264 C CD1 . TRP A 164 ? 0.6324 0.5037 0.5658 -0.0537 0.0710  -0.1555 164 TRP A CD1 
1265 C CD2 . TRP A 164 ? 0.6742 0.5528 0.6348 -0.0371 0.0767  -0.1317 164 TRP A CD2 
1266 N NE1 . TRP A 164 ? 0.6089 0.5026 0.5343 -0.0476 0.0763  -0.1514 164 TRP A NE1 
1267 C CE2 . TRP A 164 ? 0.6141 0.5127 0.5584 -0.0382 0.0804  -0.1374 164 TRP A CE2 
1268 C CE3 . TRP A 164 ? 0.5943 0.4763 0.5738 -0.0277 0.0774  -0.1174 164 TRP A CE3 
1269 C CZ2 . TRP A 164 ? 0.6352 0.5558 0.5845 -0.0315 0.0868  -0.1288 164 TRP A CZ2 
1270 C CZ3 . TRP A 164 ? 0.6259 0.5320 0.6124 -0.0212 0.0817  -0.1111 164 TRP A CZ3 
1271 C CH2 . TRP A 164 ? 0.6084 0.5329 0.5811 -0.0238 0.0874  -0.1166 164 TRP A CH2 
1272 N N   . ARG A 165 ? 0.6184 0.4865 0.4188 0.0783  -0.1349 -0.1038 165 ARG A N   
1273 C CA  . ARG A 165 ? 0.6437 0.5098 0.4914 0.0393  -0.1220 -0.1119 165 ARG A CA  
1274 C C   . ARG A 165 ? 0.6468 0.5138 0.5075 0.0144  -0.0940 -0.0718 165 ARG A C   
1275 O O   . ARG A 165 ? 0.5968 0.4770 0.5007 -0.0165 -0.0813 -0.0753 165 ARG A O   
1276 C CB  . ARG A 165 ? 0.6996 0.5255 0.5332 0.0431  -0.1177 -0.1204 165 ARG A CB  
1277 C CG  . ARG A 165 ? 0.8691 0.7039 0.7020 0.0608  -0.1473 -0.1734 165 ARG A CG  
1278 C CD  . ARG A 165 ? 0.9115 0.7085 0.7465 0.0552  -0.1379 -0.1897 165 ARG A CD  
1279 N NE  . ARG A 165 ? 0.8891 0.6795 0.7901 0.0130  -0.1113 -0.1933 165 ARG A NE  
1280 C CZ  . ARG A 165 ? 0.8836 0.6450 0.8123 -0.0006 -0.0964 -0.2158 165 ARG A CZ  
1281 N NH1 . ARG A 165 ? 0.8540 0.5936 0.7494 0.0222  -0.1093 -0.2407 165 ARG A NH1 
1282 N NH2 . ARG A 165 ? 0.8111 0.5627 0.8023 -0.0364 -0.0638 -0.2129 165 ARG A NH2 
1283 N N   . LYS A 166 ? 0.7076 0.5621 0.5329 0.0293  -0.0826 -0.0354 166 LYS A N   
1284 C CA  . LYS A 166 ? 0.6750 0.5443 0.5127 0.0098  -0.0623 -0.0042 166 LYS A CA  
1285 C C   . LYS A 166 ? 0.6907 0.6041 0.5591 -0.0063 -0.0651 -0.0151 166 LYS A C   
1286 O O   . LYS A 166 ? 0.6337 0.5669 0.5234 -0.0306 -0.0509 -0.0038 166 LYS A O   
1287 C CB  . LYS A 166 ? 0.6530 0.5084 0.4590 0.0295  -0.0517 0.0273  166 LYS A CB  
1288 C CG  . LYS A 166 ? 0.6958 0.5594 0.4884 0.0529  -0.0564 0.0242  166 LYS A CG  
1289 C CD  . LYS A 166 ? 0.6717 0.5207 0.4488 0.0682  -0.0383 0.0525  166 LYS A CD  
1290 C CE  . LYS A 166 ? 0.6225 0.5087 0.4296 0.0451  -0.0262 0.0653  166 LYS A CE  
1291 N NZ  . LYS A 166 ? 0.7274 0.6048 0.5320 0.0580  -0.0095 0.0864  166 LYS A NZ  
1292 N N   . LEU A 167 ? 0.6633 0.5921 0.5312 0.0102  -0.0812 -0.0351 167 LEU A N   
1293 C CA  . LEU A 167 ? 0.6105 0.5795 0.5111 -0.0042 -0.0814 -0.0457 167 LEU A CA  
1294 C C   . LEU A 167 ? 0.5851 0.5729 0.5309 -0.0307 -0.0860 -0.0729 167 LEU A C   
1295 O O   . LEU A 167 ? 0.6088 0.6202 0.5841 -0.0566 -0.0725 -0.0704 167 LEU A O   
1296 C CB  . LEU A 167 ? 0.5456 0.5230 0.4339 0.0261  -0.0929 -0.0548 167 LEU A CB  
1297 C CG  . LEU A 167 ? 0.4835 0.5001 0.4084 0.0146  -0.0909 -0.0660 167 LEU A CG  
1298 C CD1 . LEU A 167 ? 0.6227 0.6561 0.5654 -0.0147 -0.0681 -0.0488 167 LEU A CD1 
1299 C CD2 . LEU A 167 ? 0.5311 0.5488 0.4404 0.0499  -0.0919 -0.0637 167 LEU A CD2 
1300 N N   . CYS A 168 ? 0.5681 0.5465 0.5230 -0.0243 -0.1029 -0.1021 168 CYS A N   
1301 C CA  . CYS A 168 ? 0.6329 0.6277 0.6447 -0.0510 -0.1033 -0.1340 168 CYS A CA  
1302 C C   . CYS A 168 ? 0.6879 0.6653 0.7175 -0.0811 -0.0715 -0.1128 168 CYS A C   
1303 O O   . CYS A 168 ? 0.6275 0.6228 0.6976 -0.1069 -0.0552 -0.1168 168 CYS A O   
1304 C CB  . CYS A 168 ? 0.7139 0.7034 0.7352 -0.0375 -0.1273 -0.1750 168 CYS A CB  
1305 S SG  . CYS A 168 ? 0.8080 0.8349 0.8197 0.0006  -0.1680 -0.2089 168 CYS A SG  
1306 N N   . PHE A 169 ? 0.5744 0.5152 0.5715 -0.0746 -0.0592 -0.0871 169 PHE A N   
1307 C CA  . PHE A 169 ? 0.6134 0.5336 0.6212 -0.0947 -0.0266 -0.0622 169 PHE A CA  
1308 C C   . PHE A 169 ? 0.7370 0.6793 0.7321 -0.1036 -0.0096 -0.0289 169 PHE A C   
1309 O O   . PHE A 169 ? 0.5918 0.5369 0.6099 -0.1235 0.0159  -0.0199 169 PHE A O   
1310 C CB  . PHE A 169 ? 0.6086 0.4864 0.5824 -0.0796 -0.0194 -0.0413 169 PHE A CB  
1311 C CG  . PHE A 169 ? 0.6715 0.5263 0.6446 -0.0901 0.0157  -0.0045 169 PHE A CG  
1312 C CD1 . PHE A 169 ? 0.6188 0.4478 0.6342 -0.1078 0.0424  -0.0144 169 PHE A CD1 
1313 C CD2 . PHE A 169 ? 0.6309 0.4912 0.5643 -0.0794 0.0242  0.0391  169 PHE A CD2 
1314 C CE1 . PHE A 169 ? 0.7101 0.5136 0.7204 -0.1109 0.0805  0.0261  169 PHE A CE1 
1315 C CE2 . PHE A 169 ? 0.6911 0.5349 0.6176 -0.0813 0.0549  0.0761  169 PHE A CE2 
1316 C CZ  . PHE A 169 ? 0.6970 0.5094 0.6579 -0.0951 0.0849  0.0734  169 PHE A CZ  
1317 N N   . GLY A 170 ? 0.6324 0.5910 0.5928 -0.0880 -0.0206 -0.0126 170 GLY A N   
1318 C CA  . GLY A 170 ? 0.6366 0.6249 0.5881 -0.0961 -0.0082 0.0095  170 GLY A CA  
1319 C C   . GLY A 170 ? 0.6555 0.6772 0.6414 -0.1154 -0.0058 -0.0111 170 GLY A C   
1320 O O   . GLY A 170 ? 0.6029 0.6429 0.5904 -0.1296 0.0131  0.0022  170 GLY A O   
1321 N N   . LYS A 171 ? 0.5895 0.6212 0.6007 -0.1129 -0.0245 -0.0433 171 LYS A N   
1322 C CA  . LYS A 171 ? 0.5799 0.6427 0.6319 -0.1308 -0.0218 -0.0653 171 LYS A CA  
1323 C C   . LYS A 171 ? 0.6330 0.6873 0.7233 -0.1551 0.0004  -0.0723 171 LYS A C   
1324 O O   . LYS A 171 ? 0.5743 0.6484 0.6872 -0.1737 0.0183  -0.0736 171 LYS A O   
1325 C CB  . LYS A 171 ? 0.6172 0.6932 0.6890 -0.1164 -0.0482 -0.0971 171 LYS A CB  
1326 C CG  . LYS A 171 ? 0.6471 0.7582 0.7638 -0.1303 -0.0475 -0.1197 171 LYS A CG  
1327 C CD  . LYS A 171 ? 0.6435 0.7705 0.7621 -0.1038 -0.0729 -0.1383 171 LYS A CD  
1328 C CE  . LYS A 171 ? 0.6054 0.7671 0.7804 -0.1143 -0.0772 -0.1677 171 LYS A CE  
1329 N NZ  . LYS A 171 ? 0.5419 0.7202 0.7130 -0.0810 -0.1005 -0.1800 171 LYS A NZ  
1330 N N   . GLN A 172 ? 0.6381 0.6603 0.7400 -0.1553 0.0041  -0.0782 172 GLN A N   
1331 C CA  . GLN A 172 ? 0.7037 0.7091 0.8483 -0.1779 0.0358  -0.0818 172 GLN A CA  
1332 C C   . GLN A 172 ? 0.6987 0.6961 0.8112 -0.1823 0.0706  -0.0373 172 GLN A C   
1333 O O   . GLN A 172 ? 0.6165 0.6178 0.7543 -0.1996 0.1000  -0.0345 172 GLN A O   
1334 C CB  . GLN A 172 ? 0.6717 0.6414 0.8369 -0.1761 0.0371  -0.0977 172 GLN A CB  
1335 C CG  . GLN A 172 ? 0.8913 0.8370 1.1151 -0.1999 0.0769  -0.1063 172 GLN A CG  
1336 C CD  . GLN A 172 ? 1.1421 1.0398 1.3640 -0.1959 0.0965  -0.0961 172 GLN A CD  
1337 O OE1 . GLN A 172 ? 1.1348 1.0236 1.3742 -0.1906 0.0753  -0.1302 172 GLN A OE1 
1338 N NE2 . GLN A 172 ? 1.1115 0.9791 1.3093 -0.1952 0.1380  -0.0485 172 GLN A NE2 
1339 N N   . LEU A 173 ? 0.7460 0.7345 0.8017 -0.1638 0.0682  -0.0023 173 LEU A N   
1340 C CA  . LEU A 173 ? 0.6873 0.6787 0.7051 -0.1603 0.0949  0.0393  173 LEU A CA  
1341 C C   . LEU A 173 ? 0.6266 0.6633 0.6346 -0.1671 0.0934  0.0376  173 LEU A C   
1342 O O   . LEU A 173 ? 0.7135 0.7572 0.7091 -0.1717 0.1218  0.0573  173 LEU A O   
1343 C CB  . LEU A 173 ? 0.6253 0.6078 0.5917 -0.1367 0.0862  0.0711  173 LEU A CB  
1344 C CG  . LEU A 173 ? 0.6951 0.6304 0.6644 -0.1276 0.0897  0.0760  173 LEU A CG  
1345 C CD1 . LEU A 173 ? 0.6298 0.5623 0.5505 -0.1035 0.0811  0.1084  173 LEU A CD1 
1346 C CD2 . LEU A 173 ? 0.6841 0.5812 0.6806 -0.1375 0.1317  0.0879  173 LEU A CD2 
1347 N N   . PHE A 174 ? 0.6002 0.6661 0.6113 -0.1651 0.0643  0.0152  174 PHE A N   
1348 C CA  . PHE A 174 ? 0.5519 0.6604 0.5603 -0.1729 0.0644  0.0082  174 PHE A CA  
1349 C C   . PHE A 174 ? 0.5919 0.7059 0.6415 -0.1949 0.0855  -0.0086 174 PHE A C   
1350 O O   . PHE A 174 ? 0.6061 0.7401 0.6414 -0.2021 0.1062  0.0015  174 PHE A O   
1351 C CB  . PHE A 174 ? 0.5366 0.6652 0.5515 -0.1653 0.0363  -0.0131 174 PHE A CB  
1352 C CG  . PHE A 174 ? 0.5435 0.7133 0.5682 -0.1753 0.0391  -0.0269 174 PHE A CG  
1353 C CD1 . PHE A 174 ? 0.5132 0.7136 0.5087 -0.1709 0.0405  -0.0170 174 PHE A CD1 
1354 C CD2 . PHE A 174 ? 0.4918 0.6731 0.5607 -0.1892 0.0404  -0.0538 174 PHE A CD2 
1355 C CE1 . PHE A 174 ? 0.4576 0.6966 0.4671 -0.1820 0.0455  -0.0356 174 PHE A CE1 
1356 C CE2 . PHE A 174 ? 0.5269 0.7432 0.6076 -0.1990 0.0468  -0.0671 174 PHE A CE2 
1357 C CZ  . PHE A 174 ? 0.4887 0.7324 0.5393 -0.1964 0.0504  -0.0590 174 PHE A CZ  
1358 N N   . LEU A 175 ? 0.5634 0.6622 0.6658 -0.2045 0.0808  -0.0369 175 LEU A N   
1359 C CA  . LEU A 175 ? 0.6186 0.7220 0.7734 -0.2266 0.1030  -0.0564 175 LEU A CA  
1360 C C   . LEU A 175 ? 0.5819 0.6569 0.7328 -0.2340 0.1478  -0.0302 175 LEU A C   
1361 O O   . LEU A 175 ? 0.6026 0.6857 0.7650 -0.2470 0.1772  -0.0277 175 LEU A O   
1362 C CB  . LEU A 175 ? 0.5369 0.6372 0.7563 -0.2325 0.0847  -0.0975 175 LEU A CB  
1363 C CG  . LEU A 175 ? 0.6424 0.7750 0.8728 -0.2226 0.0482  -0.1238 175 LEU A CG  
1364 C CD1 . LEU A 175 ? 0.6411 0.7731 0.9186 -0.2169 0.0219  -0.1618 175 LEU A CD1 
1365 C CD2 . LEU A 175 ? 0.5375 0.7013 0.7918 -0.2352 0.0589  -0.1335 175 LEU A CD2 
1366 N N   . GLU A 176 ? 0.6691 0.7072 0.8037 -0.2238 0.1583  -0.0086 176 GLU A N   
1367 C CA  . GLU A 176 ? 0.7437 0.7476 0.8729 -0.2251 0.2080  0.0228  176 GLU A CA  
1368 C C   . GLU A 176 ? 0.7144 0.7386 0.7748 -0.2117 0.2248  0.0616  176 GLU A C   
1369 O O   . GLU A 176 ? 0.7649 0.7776 0.8225 -0.2152 0.2681  0.0798  176 GLU A O   
1370 C CB  . GLU A 176 ? 0.6909 0.6508 0.8145 -0.2134 0.2163  0.0402  176 GLU A CB  
1371 C CG  . GLU A 176 ? 0.8314 0.7679 1.0305 -0.2286 0.2117  -0.0022 176 GLU A CG  
1372 C CD  . GLU A 176 ? 0.9943 0.8874 1.1869 -0.2173 0.2194  0.0111  176 GLU A CD  
1373 O OE1 . GLU A 176 ? 0.9735 0.8546 1.1023 -0.1959 0.2269  0.0571  176 GLU A OE1 
1374 O OE2 . GLU A 176 ? 0.9481 0.8225 1.2027 -0.2293 0.2176  -0.0274 176 GLU A OE2 
1375 N N   . ALA A 177 ? 0.7302 0.7862 0.7360 -0.1946 0.1922  0.0722  177 ALA A N   
1376 C CA  . ALA A 177 ? 0.7311 0.8197 0.6734 -0.1799 0.2002  0.0997  177 ALA A CA  
1377 C C   . ALA A 177 ? 0.7294 0.8521 0.6828 -0.1962 0.2076  0.0784  177 ALA A C   
1378 O O   . ALA A 177 ? 0.7071 0.8401 0.6225 -0.1897 0.2364  0.0993  177 ALA A O   
1379 C CB  . ALA A 177 ? 0.6515 0.7722 0.5518 -0.1613 0.1619  0.1049  177 ALA A CB  
1380 N N   . VAL A 178 ? 0.6548 0.7952 0.6566 -0.2142 0.1836  0.0381  178 VAL A N   
1381 C CA  . VAL A 178 ? 0.6886 0.8600 0.7080 -0.2307 0.1919  0.0158  178 VAL A CA  
1382 C C   . VAL A 178 ? 0.7532 0.8967 0.8074 -0.2457 0.2370  0.0179  178 VAL A C   
1383 O O   . VAL A 178 ? 0.8274 0.9831 0.8565 -0.2473 0.2660  0.0277  178 VAL A O   
1384 C CB  . VAL A 178 ? 0.6666 0.8592 0.7337 -0.2416 0.1589  -0.0237 178 VAL A CB  
1385 C CG1 . VAL A 178 ? 0.6682 0.8840 0.7708 -0.2612 0.1734  -0.0484 178 VAL A CG1 
1386 C CG2 . VAL A 178 ? 0.6987 0.9196 0.7317 -0.2269 0.1266  -0.0243 178 VAL A CG2 
1387 N N   . GLU A 179 ? 0.7251 0.8315 0.8404 -0.2565 0.2460  0.0058  179 GLU A N   
1388 C CA  . GLU A 179 ? 0.7504 0.8257 0.9102 -0.2656 0.2873  0.0053  179 GLU A CA  
1389 C C   . GLU A 179 ? 0.7956 0.8419 0.9009 -0.2471 0.3319  0.0537  179 GLU A C   
1390 O O   . GLU A 179 ? 0.8367 0.8685 0.9482 -0.2444 0.3645  0.0623  179 GLU A O   
1391 C CB  . GLU A 179 ? 0.6010 0.6471 0.8379 -0.2738 0.2793  -0.0232 179 GLU A CB  
1392 N N   . ARG A 180 ? 0.8417 0.8788 0.8898 -0.2290 0.3321  0.0875  180 ARG A N   
1393 C CA  . ARG A 180 ? 0.8826 0.8926 0.8774 -0.2002 0.3666  0.1369  180 ARG A CA  
1394 C C   . ARG A 180 ? 0.9655 1.0150 0.8841 -0.1810 0.3724  0.1594  180 ARG A C   
1395 O O   . ARG A 180 ? 1.1072 1.1397 0.9977 -0.1632 0.4044  0.1870  180 ARG A O   
1396 C CB  . ARG A 180 ? 1.0063 0.9973 0.9668 -0.1803 0.3569  0.1650  180 ARG A CB  
1397 C CG  . ARG A 180 ? 1.1023 1.0833 0.9916 -0.1426 0.3751  0.2157  180 ARG A CG  
1398 C CD  . ARG A 180 ? 1.1369 1.0927 1.0099 -0.1234 0.3640  0.2383  180 ARG A CD  
1399 N NE  . ARG A 180 ? 1.1449 1.1377 0.9859 -0.1190 0.3216  0.2343  180 ARG A NE  
1400 C CZ  . ARG A 180 ? 1.2032 1.1832 1.0809 -0.1310 0.2967  0.2134  180 ARG A CZ  
1401 N NH1 . ARG A 180 ? 1.1309 1.0648 1.0774 -0.1506 0.3116  0.1927  180 ARG A NH1 
1402 N NH2 . ARG A 180 ? 1.0753 1.0945 0.9248 -0.1211 0.2479  0.2051  180 ARG A NH2 
1403 N N   . SER A 181 ? 1.0918 1.1948 0.9761 -0.1848 0.3405  0.1419  181 SER A N   
1404 C CA  . SER A 181 ? 1.1586 1.3064 0.9640 -0.1600 0.3393  0.1597  181 SER A CA  
1405 C C   . SER A 181 ? 1.1493 1.3484 0.9591 -0.1761 0.3144  0.1183  181 SER A C   
1406 O O   . SER A 181 ? 1.1645 1.4008 0.9130 -0.1542 0.3065  0.1218  181 SER A O   
1407 C CB  . SER A 181 ? 1.0814 1.2453 0.8180 -0.1287 0.3140  0.1844  181 SER A CB  
1408 O OG  . SER A 181 ? 0.9754 1.1842 0.7298 -0.1417 0.2620  0.1531  181 SER A OG  
1409 N N   . GLN A 182 ? 0.9621 1.2191 1.0777 -0.0714 0.0294  -0.0801 182 GLN A N   
1410 C CA  . GLN A 182 ? 0.9820 1.2306 1.0835 -0.0675 0.0065  -0.0838 182 GLN A CA  
1411 C C   . GLN A 182 ? 1.0019 1.2387 1.0997 -0.0686 0.0221  -0.0960 182 GLN A C   
1412 O O   . GLN A 182 ? 0.9589 1.1823 1.0357 -0.0699 0.0111  -0.0954 182 GLN A O   
1413 C CB  . GLN A 182 ? 0.9078 1.1700 1.0334 -0.0592 -0.0142 -0.0995 182 GLN A CB  
1414 C CG  . GLN A 182 ? 0.8911 1.1730 1.0594 -0.0555 -0.0032 -0.1290 182 GLN A CG  
1415 C CD  . GLN A 182 ? 0.9575 1.2584 1.1474 -0.0429 -0.0291 -0.1391 182 GLN A CD  
1416 O OE1 . GLN A 182 ? 0.9053 1.1910 1.0788 -0.0347 -0.0475 -0.1269 182 GLN A OE1 
1417 N NE2 . GLN A 182 ? 0.9586 1.2949 1.1869 -0.0411 -0.0292 -0.1612 182 GLN A NE2 
1418 N N   . ALA A 183 ? 0.9382 1.1771 1.0562 -0.0699 0.0512  -0.1092 183 ALA A N   
1419 C CA  . ALA A 183 ? 0.8384 1.0629 0.9501 -0.0721 0.0716  -0.1209 183 ALA A CA  
1420 C C   . ALA A 183 ? 0.8817 1.0943 0.9496 -0.0772 0.0865  -0.0973 183 ALA A C   
1421 O O   . ALA A 183 ? 0.9409 1.1404 0.9910 -0.0805 0.1033  -0.1045 183 ALA A O   
1422 C CB  . ALA A 183 ? 0.7290 0.9604 0.8855 -0.0713 0.0996  -0.1476 183 ALA A CB  
1423 N N   . LEU A 184 ? 0.9492 1.1686 0.9998 -0.0771 0.0814  -0.0689 184 LEU A N   
1424 C CA  . LEU A 184 ? 0.8318 1.0506 0.8421 -0.0785 0.0891  -0.0398 184 LEU A CA  
1425 C C   . LEU A 184 ? 0.7642 0.9877 0.7387 -0.0851 0.0580  -0.0317 184 LEU A C   
1426 O O   . LEU A 184 ? 0.8079 1.0272 0.7915 -0.0873 0.0369  -0.0479 184 LEU A O   
1427 C CB  . LEU A 184 ? 0.7973 1.0238 0.8180 -0.0734 0.1018  -0.0128 184 LEU A CB  
1428 C CG  . LEU A 184 ? 0.8336 1.0548 0.8980 -0.0710 0.1353  -0.0272 184 LEU A CG  
1429 C CD1 . LEU A 184 ? 0.7880 1.0129 0.8657 -0.0677 0.1500  -0.0019 184 LEU A CD1 
1430 C CD2 . LEU A 184 ? 0.7450 0.9512 0.8084 -0.0696 0.1723  -0.0352 184 LEU A CD2 
1431 N N   . PRO A 185 ? 0.6474 0.8816 0.5826 -0.0884 0.0552  -0.0076 185 PRO A N   
1432 C CA  . PRO A 185 ? 0.7378 0.9813 0.6429 -0.0992 0.0269  -0.0066 185 PRO A CA  
1433 C C   . PRO A 185 ? 0.6230 0.8710 0.5473 -0.0989 0.0029  -0.0009 185 PRO A C   
1434 O O   . PRO A 185 ? 0.6630 0.9168 0.6090 -0.0913 0.0058  0.0158  185 PRO A O   
1435 C CB  . PRO A 185 ? 0.7682 1.0356 0.6339 -0.1006 0.0279  0.0227  185 PRO A CB  
1436 C CG  . PRO A 185 ? 0.7309 0.9899 0.5966 -0.0902 0.0622  0.0323  185 PRO A CG  
1437 C CD  . PRO A 185 ? 0.7403 0.9819 0.6576 -0.0820 0.0784  0.0205  185 PRO A CD  
1438 N N   . LYS A 186 ? 0.5216 0.7637 0.4373 -0.1083 -0.0168 -0.0154 186 LYS A N   
1439 C CA  . LYS A 186 ? 0.6770 0.9155 0.6102 -0.1071 -0.0354 -0.0121 186 LYS A CA  
1440 C C   . LYS A 186 ? 0.6916 0.9510 0.6228 -0.1070 -0.0439 0.0175  186 LYS A C   
1441 O O   . LYS A 186 ? 0.5330 0.7881 0.4827 -0.1035 -0.0518 0.0242  186 LYS A O   
1442 C CB  . LYS A 186 ? 0.5948 0.8193 0.5176 -0.1179 -0.0486 -0.0302 186 LYS A CB  
1443 C CG  . LYS A 186 ? 0.6301 0.8723 0.5248 -0.1343 -0.0610 -0.0236 186 LYS A CG  
1444 C CD  . LYS A 186 ? 0.7219 0.9439 0.6099 -0.1481 -0.0645 -0.0488 186 LYS A CD  
1445 C CE  . LYS A 186 ? 0.7867 1.0325 0.6478 -0.1702 -0.0750 -0.0505 186 LYS A CE  
1446 N NZ  . LYS A 186 ? 0.7563 0.9792 0.6104 -0.1879 -0.0692 -0.0820 186 LYS A NZ  
1447 N N   . ASP A 187 ? 0.5676 0.8514 0.4775 -0.1097 -0.0415 0.0370  187 ASP A N   
1448 C CA  . ASP A 187 ? 0.6396 0.9480 0.5549 -0.1074 -0.0489 0.0679  187 ASP A CA  
1449 C C   . ASP A 187 ? 0.6256 0.9278 0.5717 -0.0936 -0.0302 0.0845  187 ASP A C   
1450 O O   . ASP A 187 ? 0.5379 0.8452 0.5021 -0.0920 -0.0349 0.1002  187 ASP A O   
1451 C CB  . ASP A 187 ? 0.6684 1.0120 0.5544 -0.1104 -0.0523 0.0876  187 ASP A CB  
1452 C CG  . ASP A 187 ? 0.9354 1.2947 0.7936 -0.1302 -0.0738 0.0700  187 ASP A CG  
1453 O OD1 . ASP A 187 ? 1.0063 1.3874 0.8705 -0.1384 -0.0923 0.0777  187 ASP A OD1 
1454 O OD2 . ASP A 187 ? 0.8478 1.1960 0.6812 -0.1394 -0.0690 0.0452  187 ASP A OD2 
1455 N N   . VAL A 188 ? 0.5303 0.8203 0.4848 -0.0855 -0.0053 0.0789  188 VAL A N   
1456 C CA  . VAL A 188 ? 0.5967 0.8796 0.5834 -0.0764 0.0179  0.0886  188 VAL A CA  
1457 C C   . VAL A 188 ? 0.5991 0.8671 0.6085 -0.0792 0.0107  0.0665  188 VAL A C   
1458 O O   . VAL A 188 ? 0.5255 0.7920 0.5569 -0.0775 0.0202  0.0746  188 VAL A O   
1459 C CB  . VAL A 188 ? 0.7584 1.0321 0.7513 -0.0691 0.0519  0.0865  188 VAL A CB  
1460 C CG1 . VAL A 188 ? 0.8017 1.0582 0.8019 -0.0729 0.0557  0.0486  188 VAL A CG1 
1461 C CG2 . VAL A 188 ? 0.6577 0.9260 0.6847 -0.0617 0.0826  0.1012  188 VAL A CG2 
1462 N N   . LEU A 189 ? 0.5957 0.8531 0.5997 -0.0829 -0.0043 0.0395  189 LEU A N   
1463 C CA  . LEU A 189 ? 0.4747 0.7234 0.4943 -0.0826 -0.0160 0.0242  189 LEU A CA  
1464 C C   . LEU A 189 ? 0.5304 0.7797 0.5436 -0.0862 -0.0329 0.0410  189 LEU A C   
1465 O O   . LEU A 189 ? 0.4931 0.7391 0.5192 -0.0855 -0.0319 0.0419  189 LEU A O   
1466 C CB  . LEU A 189 ? 0.4799 0.7186 0.4969 -0.0818 -0.0287 -0.0011 189 LEU A CB  
1467 C CG  . LEU A 189 ? 0.5515 0.7843 0.5785 -0.0775 -0.0455 -0.0110 189 LEU A CG  
1468 C CD1 . LEU A 189 ? 0.6037 0.8474 0.6552 -0.0744 -0.0358 -0.0190 189 LEU A CD1 
1469 C CD2 . LEU A 189 ? 0.5319 0.7547 0.5612 -0.0728 -0.0544 -0.0305 189 LEU A CD2 
1470 N N   . ILE A 190 ? 0.4639 0.7189 0.4573 -0.0923 -0.0468 0.0519  190 ILE A N   
1471 C CA  . ILE A 190 ? 0.4796 0.7361 0.4714 -0.0975 -0.0602 0.0663  190 ILE A CA  
1472 C C   . ILE A 190 ? 0.4955 0.7632 0.5051 -0.0945 -0.0462 0.0906  190 ILE A C   
1473 O O   . ILE A 190 ? 0.4322 0.6921 0.4515 -0.0962 -0.0469 0.0962  190 ILE A O   
1474 C CB  . ILE A 190 ? 0.5084 0.7761 0.4803 -0.1080 -0.0755 0.0683  190 ILE A CB  
1475 C CG1 . ILE A 190 ? 0.5508 0.7964 0.5114 -0.1128 -0.0852 0.0431  190 ILE A CG1 
1476 C CG2 . ILE A 190 ? 0.4621 0.7426 0.4403 -0.1143 -0.0840 0.0873  190 ILE A CG2 
1477 C CD1 . ILE A 190 ? 0.6084 0.8640 0.5486 -0.1275 -0.0936 0.0344  190 ILE A CD1 
1478 N N   . ALA A 191 ? 0.4768 0.7607 0.4910 -0.0893 -0.0300 0.1070  191 ALA A N   
1479 C CA  . ALA A 191 ? 0.5602 0.8521 0.5980 -0.0839 -0.0104 0.1329  191 ALA A CA  
1480 C C   . ALA A 191 ? 0.4562 0.7287 0.5157 -0.0830 0.0108  0.1200  191 ALA A C   
1481 O O   . ALA A 191 ? 0.5008 0.7698 0.5785 -0.0844 0.0222  0.1316  191 ALA A O   
1482 C CB  . ALA A 191 ? 0.4979 0.8086 0.5357 -0.0746 0.0063  0.1566  191 ALA A CB  
1483 N N   . SER A 192 ? 0.4393 0.7020 0.4991 -0.0824 0.0177  0.0939  192 SER A N   
1484 C CA  . SER A 192 ? 0.5331 0.7866 0.6135 -0.0851 0.0355  0.0753  192 SER A CA  
1485 C C   . SER A 192 ? 0.5265 0.7731 0.5997 -0.0909 0.0170  0.0671  192 SER A C   
1486 O O   . SER A 192 ? 0.5920 0.8343 0.6784 -0.0960 0.0324  0.0642  192 SER A O   
1487 C CB  . SER A 192 ? 0.4571 0.7098 0.5427 -0.0842 0.0414  0.0456  192 SER A CB  
1488 O OG  . SER A 192 ? 0.6641 0.9174 0.7575 -0.0795 0.0677  0.0526  192 SER A OG  
1489 N N   . LEU A 193 ? 0.4615 0.7044 0.5126 -0.0907 -0.0125 0.0630  193 LEU A N   
1490 C CA  . LEU A 193 ? 0.5388 0.7710 0.5783 -0.0933 -0.0287 0.0582  193 LEU A CA  
1491 C C   . LEU A 193 ? 0.5467 0.7734 0.5862 -0.0985 -0.0266 0.0807  193 LEU A C   
1492 O O   . LEU A 193 ? 0.4606 0.6767 0.4961 -0.1024 -0.0249 0.0790  193 LEU A O   
1493 C CB  . LEU A 193 ? 0.4799 0.7045 0.5005 -0.0895 -0.0538 0.0484  193 LEU A CB  
1494 C CG  . LEU A 193 ? 0.5272 0.7571 0.5533 -0.0828 -0.0572 0.0246  193 LEU A CG  
1495 C CD1 . LEU A 193 ? 0.4583 0.6769 0.4713 -0.0779 -0.0757 0.0190  193 LEU A CD1 
1496 C CD2 . LEU A 193 ? 0.5703 0.8080 0.6033 -0.0811 -0.0573 0.0099  193 LEU A CD2 
1497 N N   . LEU A 194 ? 0.4561 0.6930 0.5001 -0.0990 -0.0266 0.1013  194 LEU A N   
1498 C CA  . LEU A 194 ? 0.4482 0.6865 0.5037 -0.1032 -0.0210 0.1234  194 LEU A CA  
1499 C C   . LEU A 194 ? 0.5141 0.7500 0.5946 -0.1033 0.0101  0.1305  194 LEU A C   
1500 O O   . LEU A 194 ? 0.5509 0.7765 0.6392 -0.1088 0.0195  0.1378  194 LEU A O   
1501 C CB  . LEU A 194 ? 0.5198 0.7823 0.5800 -0.1026 -0.0290 0.1438  194 LEU A CB  
1502 C CG  . LEU A 194 ? 0.5270 0.7931 0.5652 -0.1084 -0.0555 0.1341  194 LEU A CG  
1503 C CD1 . LEU A 194 ? 0.5363 0.8378 0.5764 -0.1095 -0.0630 0.1501  194 LEU A CD1 
1504 C CD2 . LEU A 194 ? 0.5386 0.7865 0.5723 -0.1166 -0.0652 0.1313  194 LEU A CD2 
1505 N N   . ASP A 195 ? 0.4673 0.7091 0.5619 -0.0985 0.0311  0.1272  195 ASP A N   
1506 C CA  . ASP A 195 ? 0.5388 0.7735 0.6605 -0.1007 0.0679  0.1286  195 ASP A CA  
1507 C C   . ASP A 195 ? 0.5353 0.7561 0.6484 -0.1115 0.0708  0.1015  195 ASP A C   
1508 O O   . ASP A 195 ? 0.5338 0.7442 0.6604 -0.1192 0.0942  0.1036  195 ASP A O   
1509 C CB  . ASP A 195 ? 0.5390 0.7788 0.6771 -0.0940 0.0930  0.1272  195 ASP A CB  
1510 C CG  . ASP A 195 ? 0.6816 0.9093 0.8462 -0.1009 0.1338  0.1116  195 ASP A CG  
1511 O OD1 . ASP A 195 ? 0.7294 0.9573 0.8955 -0.1048 0.1416  0.0824  195 ASP A OD1 
1512 O OD2 . ASP A 195 ? 0.6878 0.9068 0.8752 -0.1041 0.1603  0.1258  195 ASP A OD2 
1513 N N   . VAL A 196 ? 0.4620 0.6847 0.5525 -0.1118 0.0478  0.0765  196 VAL A N   
1514 C CA  . VAL A 196 ? 0.5182 0.7367 0.5939 -0.1198 0.0433  0.0535  196 VAL A CA  
1515 C C   . VAL A 196 ? 0.5464 0.7493 0.6025 -0.1236 0.0325  0.0669  196 VAL A C   
1516 O O   . VAL A 196 ? 0.4908 0.6853 0.5419 -0.1337 0.0467  0.0597  196 VAL A O   
1517 C CB  . VAL A 196 ? 0.5112 0.7411 0.5706 -0.1143 0.0170  0.0304  196 VAL A CB  
1518 C CG1 . VAL A 196 ? 0.4630 0.6955 0.5003 -0.1188 0.0042  0.0136  196 VAL A CG1 
1519 C CG2 . VAL A 196 ? 0.3779 0.6224 0.4614 -0.1136 0.0337  0.0114  196 VAL A CG2 
1520 N N   . LEU A 197 ? 0.4689 0.6668 0.5128 -0.1178 0.0100  0.0838  197 LEU A N   
1521 C CA  . LEU A 197 ? 0.5362 0.7159 0.5624 -0.1217 0.0014  0.0946  197 LEU A CA  
1522 C C   . LEU A 197 ? 0.5305 0.7029 0.5787 -0.1295 0.0276  0.1117  197 LEU A C   
1523 O O   . LEU A 197 ? 0.5472 0.7009 0.5823 -0.1358 0.0296  0.1164  197 LEU A O   
1524 C CB  . LEU A 197 ? 0.5052 0.6815 0.5203 -0.1166 -0.0234 0.1042  197 LEU A CB  
1525 C CG  . LEU A 197 ? 0.4953 0.6675 0.4863 -0.1086 -0.0469 0.0894  197 LEU A CG  
1526 C CD1 . LEU A 197 ? 0.4388 0.6042 0.4244 -0.1076 -0.0627 0.0964  197 LEU A CD1 
1527 C CD2 . LEU A 197 ? 0.5029 0.6604 0.4668 -0.1067 -0.0527 0.0825  197 LEU A CD2 
1528 N N   . ASN A 198 ? 0.6334 0.6027 0.4529 -0.0774 -0.0039 0.0860  198 ASN A N   
1529 C CA  . ASN A 198 ? 0.6626 0.6280 0.4973 -0.0733 -0.0219 0.0842  198 ASN A CA  
1530 C C   . ASN A 198 ? 0.6544 0.6159 0.5164 -0.0745 -0.0238 0.0883  198 ASN A C   
1531 O O   . ASN A 198 ? 0.6899 0.6434 0.5632 -0.0702 -0.0379 0.0895  198 ASN A O   
1532 C CB  . ASN A 198 ? 0.6625 0.6139 0.4698 -0.0706 -0.0342 0.0933  198 ASN A CB  
1533 C CG  . ASN A 198 ? 0.8014 0.7605 0.5914 -0.0687 -0.0393 0.0824  198 ASN A CG  
1534 O OD1 . ASN A 198 ? 0.8338 0.7893 0.5934 -0.0714 -0.0316 0.0842  198 ASN A OD1 
1535 N ND2 . ASN A 198 ? 0.8660 0.8364 0.6765 -0.0650 -0.0513 0.0695  198 ASN A ND2 
1536 N N   . ASN A 199 ? 0.6122 0.5803 0.4867 -0.0800 -0.0103 0.0891  199 ASN A N   
1537 C CA  . ASN A 199 ? 0.6433 0.6101 0.5467 -0.0830 -0.0114 0.0890  199 ASN A CA  
1538 C C   . ASN A 199 ? 0.6251 0.6055 0.5556 -0.0776 -0.0193 0.0729  199 ASN A C   
1539 O O   . ASN A 199 ? 0.5782 0.5763 0.5134 -0.0756 -0.0135 0.0621  199 ASN A O   
1540 C CB  . ASN A 199 ? 0.6017 0.5783 0.5132 -0.0910 0.0049  0.0913  199 ASN A CB  
1541 C CG  . ASN A 199 ? 0.6880 0.6640 0.6301 -0.0966 0.0041  0.0891  199 ASN A CG  
1542 O OD1 . ASN A 199 ? 0.6324 0.6218 0.5993 -0.0936 -0.0008 0.0754  199 ASN A OD1 
1543 N ND2 . ASN A 199 ? 0.6256 0.5853 0.5652 -0.1057 0.0099  0.1020  199 ASN A ND2 
1544 N N   . GLU A 200 ? 0.6732 0.6438 0.6204 -0.0745 -0.0316 0.0716  200 GLU A N   
1545 C CA  . GLU A 200 ? 0.5821 0.5649 0.5533 -0.0686 -0.0394 0.0559  200 GLU A CA  
1546 C C   . GLU A 200 ? 0.5721 0.5578 0.5719 -0.0714 -0.0381 0.0489  200 GLU A C   
1547 O O   . GLU A 200 ? 0.5381 0.5297 0.5583 -0.0662 -0.0453 0.0366  200 GLU A O   
1548 C CB  . GLU A 200 ? 0.6081 0.5822 0.5794 -0.0605 -0.0553 0.0558  200 GLU A CB  
1549 C CG  . GLU A 200 ? 0.7026 0.6776 0.6472 -0.0582 -0.0589 0.0593  200 GLU A CG  
1550 C CD  . GLU A 200 ? 0.6922 0.6629 0.6388 -0.0493 -0.0768 0.0589  200 GLU A CD  
1551 O OE1 . GLU A 200 ? 0.6139 0.5869 0.5869 -0.0434 -0.0852 0.0512  200 GLU A OE1 
1552 O OE2 . GLU A 200 ? 0.8501 0.8167 0.7720 -0.0475 -0.0829 0.0655  200 GLU A OE2 
1553 N N   . GLU A 201 ? 0.5602 0.5434 0.5628 -0.0801 -0.0286 0.0549  201 GLU A N   
1554 C CA  . GLU A 201 ? 0.6121 0.5993 0.6425 -0.0848 -0.0276 0.0464  201 GLU A CA  
1555 C C   . GLU A 201 ? 0.5684 0.5841 0.6108 -0.0821 -0.0238 0.0306  201 GLU A C   
1556 O O   . GLU A 201 ? 0.5637 0.5957 0.5988 -0.0841 -0.0140 0.0313  201 GLU A O   
1557 C CB  . GLU A 201 ? 0.6664 0.6454 0.6979 -0.0969 -0.0177 0.0567  201 GLU A CB  
1558 C CG  . GLU A 201 ? 0.6700 0.6186 0.6806 -0.0999 -0.0180 0.0762  201 GLU A CG  
1559 C CD  . GLU A 201 ? 0.7439 0.6832 0.7581 -0.1143 -0.0055 0.0860  201 GLU A CD  
1560 O OE1 . GLU A 201 ? 0.7418 0.6860 0.7839 -0.1222 -0.0030 0.0766  201 GLU A OE1 
1561 O OE2 . GLU A 201 ? 0.7451 0.6732 0.7343 -0.1185 0.0026  0.1020  201 GLU A OE2 
1562 N N   . ALA A 202 ? 0.5934 0.6151 0.6524 -0.0764 -0.0313 0.0167  202 ALA A N   
1563 C CA  . ALA A 202 ? 0.5722 0.6190 0.6390 -0.0730 -0.0279 0.0025  202 ALA A CA  
1564 C C   . ALA A 202 ? 0.5479 0.6082 0.6305 -0.0799 -0.0230 -0.0028 202 ALA A C   
1565 O O   . ALA A 202 ? 0.5264 0.5762 0.6257 -0.0872 -0.0254 -0.0038 202 ALA A O   
1566 C CB  . ALA A 202 ? 0.5558 0.6055 0.6362 -0.0659 -0.0359 -0.0116 202 ALA A CB  
1567 N N   . GLN A 203 ? 0.5205 0.6041 0.5981 -0.0774 -0.0162 -0.0066 203 GLN A N   
1568 C CA  . GLN A 203 ? 0.5397 0.6445 0.6331 -0.0823 -0.0126 -0.0132 203 GLN A CA  
1569 C C   . GLN A 203 ? 0.5486 0.6729 0.6513 -0.0755 -0.0172 -0.0303 203 GLN A C   
1570 O O   . GLN A 203 ? 0.4813 0.6202 0.5703 -0.0662 -0.0141 -0.0324 203 GLN A O   
1571 C CB  . GLN A 203 ? 0.5612 0.6802 0.6419 -0.0817 -0.0023 -0.0047 203 GLN A CB  
1572 C CG  . GLN A 203 ? 0.5092 0.6096 0.5772 -0.0887 0.0038  0.0117  203 GLN A CG  
1573 C CD  . GLN A 203 ? 0.5550 0.6431 0.6403 -0.1020 0.0038  0.0152  203 GLN A CD  
1574 O OE1 . GLN A 203 ? 0.5248 0.6303 0.6319 -0.1098 0.0067  0.0082  203 GLN A OE1 
1575 N NE2 . GLN A 203 ? 0.5822 0.6398 0.6578 -0.1048 0.0005  0.0259  203 GLN A NE2 
1576 N N   . LEU A 204 ? 0.5580 0.6805 0.6817 -0.0798 -0.0239 -0.0423 204 LEU A N   
1577 C CA  . LEU A 204 ? 0.4785 0.6160 0.6091 -0.0734 -0.0291 -0.0599 204 LEU A CA  
1578 C C   . LEU A 204 ? 0.5066 0.6560 0.6618 -0.0817 -0.0330 -0.0740 204 LEU A C   
1579 O O   . LEU A 204 ? 0.5012 0.6384 0.6714 -0.0938 -0.0325 -0.0706 204 LEU A O   
1580 C CB  . LEU A 204 ? 0.4867 0.6067 0.6172 -0.0680 -0.0344 -0.0646 204 LEU A CB  
1581 C CG  . LEU A 204 ? 0.4883 0.6038 0.5979 -0.0597 -0.0313 -0.0571 204 LEU A CG  
1582 C CD1 . LEU A 204 ? 0.5632 0.6624 0.6798 -0.0564 -0.0374 -0.0609 204 LEU A CD1 
1583 C CD2 . LEU A 204 ? 0.4588 0.5950 0.5549 -0.0515 -0.0266 -0.0636 204 LEU A CD2 
1584 N N   . PRO A 205 ? 0.6421 0.8151 0.8009 -0.0763 -0.0368 -0.0906 205 PRO A N   
1585 C CA  . PRO A 205 ? 0.5029 0.6897 0.6416 -0.0625 -0.0359 -0.0943 205 PRO A CA  
1586 C C   . PRO A 205 ? 0.4737 0.6782 0.5950 -0.0559 -0.0297 -0.0839 205 PRO A C   
1587 O O   . PRO A 205 ? 0.5504 0.7680 0.6807 -0.0612 -0.0279 -0.0802 205 PRO A O   
1588 C CB  . PRO A 205 ? 0.6331 0.8377 0.7830 -0.0611 -0.0427 -0.1161 205 PRO A CB  
1589 C CG  . PRO A 205 ? 0.6589 0.8734 0.8336 -0.0739 -0.0460 -0.1230 205 PRO A CG  
1590 C CD  . PRO A 205 ? 0.5391 0.7247 0.7221 -0.0846 -0.0424 -0.1084 205 PRO A CD  
1591 N N   . ASP A 206 ? 0.5040 0.7079 0.6010 -0.0445 -0.0251 -0.0790 206 ASP A N   
1592 C CA  . ASP A 206 ? 0.5409 0.7567 0.6185 -0.0356 -0.0186 -0.0693 206 ASP A CA  
1593 C C   . ASP A 206 ? 0.5020 0.7308 0.5617 -0.0226 -0.0185 -0.0763 206 ASP A C   
1594 O O   . ASP A 206 ? 0.4805 0.6950 0.5211 -0.0172 -0.0130 -0.0728 206 ASP A O   
1595 C CB  . ASP A 206 ? 0.4864 0.6802 0.5467 -0.0353 -0.0105 -0.0529 206 ASP A CB  
1596 C CG  . ASP A 206 ? 0.5810 0.7840 0.6253 -0.0275 -0.0028 -0.0427 206 ASP A CG  
1597 O OD1 . ASP A 206 ? 0.4559 0.6786 0.4927 -0.0167 -0.0030 -0.0466 206 ASP A OD1 
1598 O OD2 . ASP A 206 ? 0.4363 0.6263 0.4742 -0.0310 0.0032  -0.0309 206 ASP A OD2 
1599 N N   . PRO A 207 ? 0.5625 0.8189 0.6274 -0.0179 -0.0243 -0.0867 207 PRO A N   
1600 C CA  . PRO A 207 ? 0.5743 0.8422 0.6163 -0.0038 -0.0242 -0.0917 207 PRO A CA  
1601 C C   . PRO A 207 ? 0.5456 0.8046 0.5573 0.0085  -0.0142 -0.0760 207 PRO A C   
1602 O O   . PRO A 207 ? 0.5014 0.7540 0.4887 0.0177  -0.0095 -0.0755 207 PRO A O   
1603 C CB  . PRO A 207 ? 0.4805 0.7833 0.5350 -0.0009 -0.0342 -0.1043 207 PRO A CB  
1604 C CG  . PRO A 207 ? 0.6213 0.9271 0.7107 -0.0177 -0.0397 -0.1120 207 PRO A CG  
1605 C CD  . PRO A 207 ? 0.4644 0.7429 0.5565 -0.0261 -0.0316 -0.0959 207 PRO A CD  
1606 N N   . ALA A 208 ? 0.5132 0.7705 0.5252 0.0088  -0.0096 -0.0636 208 ALA A N   
1607 C CA  . ALA A 208 ? 0.4835 0.7291 0.4669 0.0210  0.0006  -0.0495 208 ALA A CA  
1608 C C   . ALA A 208 ? 0.4810 0.6944 0.4475 0.0173  0.0098  -0.0432 208 ALA A C   
1609 O O   . ALA A 208 ? 0.5884 0.7896 0.5277 0.0269  0.0182  -0.0372 208 ALA A O   
1610 C CB  . ALA A 208 ? 0.4903 0.7412 0.4802 0.0214  0.0042  -0.0398 208 ALA A CB  
1611 N N   . ILE A 209 ? 0.5690 0.7680 0.5512 0.0036  0.0086  -0.0442 209 ILE A N   
1612 C CA  . ILE A 209 ? 0.6184 0.7924 0.5892 -0.0005 0.0155  -0.0407 209 ILE A CA  
1613 C C   . ILE A 209 ? 0.4760 0.6509 0.4407 0.0022  0.0162  -0.0503 209 ILE A C   
1614 O O   . ILE A 209 ? 0.4756 0.6363 0.4200 0.0050  0.0261  -0.0466 209 ILE A O   
1615 C CB  . ILE A 209 ? 0.5522 0.7139 0.5415 -0.0136 0.0116  -0.0396 209 ILE A CB  
1616 C CG1 . ILE A 209 ? 0.4836 0.6399 0.4702 -0.0159 0.0150  -0.0280 209 ILE A CG1 
1617 C CG2 . ILE A 209 ? 0.4740 0.6179 0.4582 -0.0176 0.0151  -0.0408 209 ILE A CG2 
1618 C CD1 . ILE A 209 ? 0.5129 0.6574 0.5140 -0.0277 0.0105  -0.0250 209 ILE A CD1 
1619 N N   . GLU A 210 ? 0.5855 0.7762 0.5676 0.0003  0.0070  -0.0637 210 GLU A N   
1620 C CA  . GLU A 210 ? 0.5706 0.7637 0.5471 0.0029  0.0084  -0.0746 210 GLU A CA  
1621 C C   . GLU A 210 ? 0.5918 0.7884 0.5366 0.0157  0.0160  -0.0707 210 GLU A C   
1622 O O   . GLU A 210 ? 0.5699 0.7566 0.4980 0.0174  0.0255  -0.0714 210 GLU A O   
1623 C CB  . GLU A 210 ? 0.5258 0.7354 0.5251 -0.0004 -0.0030 -0.0912 210 GLU A CB  
1624 C CG  . GLU A 210 ? 0.6465 0.8455 0.6736 -0.0115 -0.0086 -0.0964 210 GLU A CG  
1625 C CD  . GLU A 210 ? 0.6214 0.8325 0.6705 -0.0148 -0.0188 -0.1136 210 GLU A CD  
1626 O OE1 . GLU A 210 ? 0.7349 0.9584 0.7955 -0.0177 -0.0255 -0.1158 210 GLU A OE1 
1627 O OE2 . GLU A 210 ? 0.7234 0.9325 0.7794 -0.0149 -0.0194 -0.1262 210 GLU A OE2 
1628 N N   . ASP A 211 ? 0.5651 0.7766 0.5015 0.0254  0.0123  -0.0666 211 ASP A N   
1629 C CA  . ASP A 211 ? 0.5167 0.7310 0.4203 0.0407  0.0179  -0.0615 211 ASP A CA  
1630 C C   . ASP A 211 ? 0.5219 0.7080 0.3990 0.0441  0.0333  -0.0459 211 ASP A C   
1631 O O   . ASP A 211 ? 0.6711 0.8455 0.5207 0.0501  0.0434  -0.0427 211 ASP A O   
1632 C CB  . ASP A 211 ? 0.6410 0.8808 0.5454 0.0519  0.0084  -0.0609 211 ASP A CB  
1633 C CG  . ASP A 211 ? 0.7886 1.0332 0.6574 0.0709  0.0113  -0.0553 211 ASP A CG  
1634 O OD1 . ASP A 211 ? 0.7865 1.0448 0.6457 0.0756  0.0066  -0.0658 211 ASP A OD1 
1635 O OD2 . ASP A 211 ? 0.7840 1.0171 0.6327 0.0821  0.0183  -0.0402 211 ASP A OD2 
1636 N N   . GLN A 212 ? 0.5744 0.7477 0.4576 0.0396  0.0363  -0.0364 212 GLN A N   
1637 C CA  . GLN A 212 ? 0.5903 0.7358 0.4480 0.0429  0.0509  -0.0231 212 GLN A CA  
1638 C C   . GLN A 212 ? 0.5988 0.7234 0.4552 0.0304  0.0605  -0.0256 212 GLN A C   
1639 O O   . GLN A 212 ? 0.6118 0.7162 0.4425 0.0330  0.0744  -0.0195 212 GLN A O   
1640 C CB  . GLN A 212 ? 0.6458 0.7854 0.5097 0.0420  0.0514  -0.0143 212 GLN A CB  
1641 C CG  . GLN A 212 ? 0.6670 0.7773 0.5025 0.0477  0.0663  -0.0018 212 GLN A CG  
1642 C CD  . GLN A 212 ? 0.5774 0.6798 0.4188 0.0451  0.0682  0.0045  212 GLN A CD  
1643 O OE1 . GLN A 212 ? 0.5906 0.7137 0.4508 0.0459  0.0595  0.0034  212 GLN A OE1 
1644 N NE2 . GLN A 212 ? 0.6245 0.6970 0.4495 0.0409  0.0805  0.0103  212 GLN A NE2 
1645 N N   . GLY A 213 ? 0.5885 0.7176 0.4733 0.0169  0.0537  -0.0342 213 GLY A N   
1646 C CA  . GLY A 213 ? 0.5685 0.6841 0.4578 0.0057  0.0608  -0.0384 213 GLY A CA  
1647 C C   . GLY A 213 ? 0.6716 0.7947 0.5593 0.0057  0.0645  -0.0487 213 GLY A C   
1648 O O   . GLY A 213 ? 0.6932 0.8054 0.5782 -0.0015 0.0752  -0.0509 213 GLY A O   
1649 N N   . GLY A 214 ? 0.6003 0.7433 0.4903 0.0130  0.0563  -0.0563 214 GLY A N   
1650 C CA  . GLY A 214 ? 0.6918 0.8425 0.5764 0.0142  0.0607  -0.0669 214 GLY A CA  
1651 C C   . GLY A 214 ? 0.6040 0.7570 0.5162 0.0026  0.0601  -0.0790 214 GLY A C   
1652 O O   . GLY A 214 ? 0.5603 0.7187 0.5016 -0.0032 0.0481  -0.0844 214 GLY A O   
1653 N N   . GLU A 215 ? 0.5862 0.7349 0.4891 -0.0003 0.0738  -0.0830 215 GLU A N   
1654 C CA  . GLU A 215 ? 0.5707 0.7268 0.5015 -0.0091 0.0738  -0.0967 215 GLU A CA  
1655 C C   . GLU A 215 ? 0.5903 0.7369 0.5412 -0.0194 0.0722  -0.0933 215 GLU A C   
1656 O O   . GLU A 215 ? 0.5283 0.6836 0.5099 -0.0240 0.0635  -0.1031 215 GLU A O   
1657 C CB  . GLU A 215 ? 0.5531 0.7101 0.4687 -0.0101 0.0914  -0.1023 215 GLU A CB  
1658 C CG  . GLU A 215 ? 0.5934 0.7610 0.4857 0.0006  0.0931  -0.1072 215 GLU A CG  
1659 C CD  . GLU A 215 ? 0.6580 0.8113 0.5058 0.0096  0.1034  -0.0913 215 GLU A CD  
1660 O OE1 . GLU A 215 ? 0.5963 0.7310 0.4334 0.0089  0.1069  -0.0764 215 GLU A OE1 
1661 O OE2 . GLU A 215 ? 0.6198 0.7797 0.4415 0.0186  0.1079  -0.0938 215 GLU A OE2 
1662 N N   . TYR A 216 ? 0.5559 0.6844 0.4889 -0.0219 0.0799  -0.0799 216 TYR A N   
1663 C CA  . TYR A 216 ? 0.5258 0.6458 0.4734 -0.0323 0.0794  -0.0780 216 TYR A CA  
1664 C C   . TYR A 216 ? 0.5870 0.7116 0.5576 -0.0329 0.0610  -0.0779 216 TYR A C   
1665 O O   . TYR A 216 ? 0.6334 0.7603 0.6260 -0.0396 0.0548  -0.0824 216 TYR A O   
1666 C CB  . TYR A 216 ? 0.5977 0.6945 0.5176 -0.0342 0.0919  -0.0648 216 TYR A CB  
1667 C CG  . TYR A 216 ? 0.6495 0.7367 0.5797 -0.0443 0.0899  -0.0630 216 TYR A CG  
1668 C CD1 . TYR A 216 ? 0.6777 0.7711 0.6286 -0.0556 0.0922  -0.0730 216 TYR A CD1 
1669 C CD2 . TYR A 216 ? 0.6554 0.7297 0.5747 -0.0424 0.0856  -0.0523 216 TYR A CD2 
1670 C CE1 . TYR A 216 ? 0.6521 0.7393 0.6112 -0.0646 0.0885  -0.0727 216 TYR A CE1 
1671 C CE2 . TYR A 216 ? 0.6231 0.6888 0.5482 -0.0514 0.0835  -0.0517 216 TYR A CE2 
1672 C CZ  . TYR A 216 ? 0.6994 0.7716 0.6436 -0.0625 0.0842  -0.0620 216 TYR A CZ  
1673 O OH  . TYR A 216 ? 0.7266 0.7929 0.6756 -0.0713 0.0802  -0.0628 216 TYR A OH  
1674 N N   . VAL A 217 ? 0.6049 0.7315 0.5706 -0.0259 0.0523  -0.0724 217 VAL A N   
1675 C CA  . VAL A 217 ? 0.6136 0.7411 0.5975 -0.0278 0.0377  -0.0699 217 VAL A CA  
1676 C C   . VAL A 217 ? 0.5587 0.6990 0.5696 -0.0271 0.0255  -0.0816 217 VAL A C   
1677 O O   . VAL A 217 ? 0.5534 0.6910 0.5811 -0.0297 0.0141  -0.0796 217 VAL A O   
1678 C CB  . VAL A 217 ? 0.6308 0.7553 0.5996 -0.0224 0.0360  -0.0588 217 VAL A CB  
1679 C CG1 . VAL A 217 ? 0.4905 0.6307 0.4589 -0.0145 0.0313  -0.0640 217 VAL A CG1 
1680 C CG2 . VAL A 217 ? 0.5961 0.7156 0.5772 -0.0272 0.0265  -0.0525 217 VAL A CG2 
1681 N N   . GLN A 218 ? 0.5356 0.6873 0.5496 -0.0236 0.0284  -0.0935 218 GLN A N   
1682 C CA  . GLN A 218 ? 0.6162 0.7776 0.6551 -0.0222 0.0174  -0.1064 218 GLN A CA  
1683 C C   . GLN A 218 ? 0.5875 0.7451 0.6533 -0.0262 0.0091  -0.1097 218 GLN A C   
1684 O O   . GLN A 218 ? 0.5537 0.7074 0.6363 -0.0262 -0.0030 -0.1100 218 GLN A O   
1685 C CB  . GLN A 218 ? 0.6014 0.7757 0.6367 -0.0177 0.0240  -0.1204 218 GLN A CB  
1686 C CG  . GLN A 218 ? 0.6570 0.8387 0.6692 -0.0109 0.0258  -0.1203 218 GLN A CG  
1687 C CD  . GLN A 218 ? 0.6201 0.8091 0.6465 -0.0097 0.0116  -0.1258 218 GLN A CD  
1688 O OE1 . GLN A 218 ? 0.6201 0.8124 0.6705 -0.0112 0.0037  -0.1391 218 GLN A OE1 
1689 N NE2 . GLN A 218 ? 0.5722 0.7637 0.5853 -0.0071 0.0088  -0.1166 218 GLN A NE2 
1690 N N   . PRO A 219 ? 0.5270 0.6859 0.5988 -0.0293 0.0146  -0.1123 219 PRO A N   
1691 C CA  . PRO A 219 ? 0.5805 0.7386 0.6783 -0.0305 0.0040  -0.1152 219 PRO A CA  
1692 C C   . PRO A 219 ? 0.5860 0.7304 0.6796 -0.0340 -0.0042 -0.1008 219 PRO A C   
1693 O O   . PRO A 219 ? 0.5549 0.6965 0.6667 -0.0331 -0.0157 -0.1009 219 PRO A O   
1694 C CB  . PRO A 219 ? 0.5375 0.7067 0.6429 -0.0335 0.0136  -0.1237 219 PRO A CB  
1695 C CG  . PRO A 219 ? 0.5486 0.7152 0.6253 -0.0368 0.0306  -0.1191 219 PRO A CG  
1696 C CD  . PRO A 219 ? 0.5000 0.6639 0.5583 -0.0311 0.0308  -0.1159 219 PRO A CD  
1697 N N   . MET A 220 ? 0.5810 0.7165 0.6500 -0.0367 0.0016  -0.0885 220 MET A N   
1698 C CA  . MET A 220 ? 0.5772 0.7001 0.6393 -0.0399 -0.0046 -0.0754 220 MET A CA  
1699 C C   . MET A 220 ? 0.5789 0.6960 0.6409 -0.0386 -0.0115 -0.0685 220 MET A C   
1700 O O   . MET A 220 ? 0.4859 0.5922 0.5443 -0.0412 -0.0169 -0.0578 220 MET A O   
1701 C CB  . MET A 220 ? 0.6244 0.7397 0.6605 -0.0436 0.0068  -0.0667 220 MET A CB  
1702 C CG  . MET A 220 ? 0.7660 0.8853 0.7970 -0.0468 0.0193  -0.0736 220 MET A CG  
1703 S SD  . MET A 220 ? 0.9365 1.0400 0.9417 -0.0537 0.0301  -0.0646 220 MET A SD  
1704 C CE  . MET A 220 ? 0.6986 0.7916 0.6774 -0.0471 0.0357  -0.0519 220 MET A CE  
1705 N N   . LEU A 221 ? 0.5976 0.7225 0.6641 -0.0354 -0.0112 -0.0754 221 LEU A N   
1706 C CA  . LEU A 221 ? 0.5658 0.6897 0.6293 -0.0360 -0.0138 -0.0696 221 LEU A CA  
1707 C C   . LEU A 221 ? 0.5166 0.6282 0.5934 -0.0399 -0.0238 -0.0633 221 LEU A C   
1708 O O   . LEU A 221 ? 0.4961 0.6021 0.5648 -0.0434 -0.0232 -0.0520 221 LEU A O   
1709 C CB  . LEU A 221 ? 0.4909 0.6284 0.5604 -0.0324 -0.0141 -0.0818 221 LEU A CB  
1710 C CG  . LEU A 221 ? 0.5405 0.6850 0.6074 -0.0330 -0.0157 -0.0791 221 LEU A CG  
1711 C CD1 . LEU A 221 ? 0.4921 0.6397 0.5349 -0.0299 -0.0071 -0.0682 221 LEU A CD1 
1712 C CD2 . LEU A 221 ? 0.4760 0.6355 0.5512 -0.0299 -0.0187 -0.0950 221 LEU A CD2 
1713 N N   . SER A 222 ? 0.5387 0.6452 0.6354 -0.0386 -0.0323 -0.0699 222 SER A N   
1714 C CA  . SER A 222 ? 0.5854 0.6756 0.6928 -0.0412 -0.0414 -0.0629 222 SER A CA  
1715 C C   . SER A 222 ? 0.5489 0.6271 0.6401 -0.0447 -0.0416 -0.0460 222 SER A C   
1716 O O   . SER A 222 ? 0.5917 0.6573 0.6814 -0.0491 -0.0438 -0.0358 222 SER A O   
1717 C CB  . SER A 222 ? 0.5163 0.6005 0.6450 -0.0361 -0.0505 -0.0714 222 SER A CB  
1718 O OG  . SER A 222 ? 0.5654 0.6523 0.6923 -0.0327 -0.0523 -0.0701 222 SER A OG  
1719 N N   . LYS A 223 ? 0.5394 0.6209 0.6175 -0.0437 -0.0383 -0.0436 223 LYS A N   
1720 C CA  . LYS A 223 ? 0.5506 0.6215 0.6110 -0.0466 -0.0388 -0.0301 223 LYS A CA  
1721 C C   . LYS A 223 ? 0.6023 0.6764 0.6399 -0.0494 -0.0271 -0.0242 223 LYS A C   
1722 O O   . LYS A 223 ? 0.5686 0.6331 0.5898 -0.0525 -0.0258 -0.0127 223 LYS A O   
1723 C CB  . LYS A 223 ? 0.5814 0.6536 0.6441 -0.0442 -0.0450 -0.0331 223 LYS A CB  
1724 C CG  . LYS A 223 ? 0.6460 0.7149 0.7313 -0.0384 -0.0579 -0.0378 223 LYS A CG  
1725 C CD  . LYS A 223 ? 0.6303 0.6784 0.7123 -0.0384 -0.0662 -0.0242 223 LYS A CD  
1726 C CE  . LYS A 223 ? 0.6447 0.6853 0.7465 -0.0299 -0.0797 -0.0271 223 LYS A CE  
1727 N NZ  . LYS A 223 ? 0.6272 0.6796 0.7326 -0.0245 -0.0875 -0.0315 223 LYS A NZ  
1728 N N   . TYR A 224 ? 0.5436 0.6293 0.5778 -0.0473 -0.0184 -0.0314 224 TYR A N   
1729 C CA  . TYR A 224 ? 0.5401 0.6263 0.5519 -0.0473 -0.0070 -0.0259 224 TYR A CA  
1730 C C   . TYR A 224 ? 0.5058 0.5928 0.5126 -0.0480 -0.0042 -0.0175 224 TYR A C   
1731 O O   . TYR A 224 ? 0.5469 0.6302 0.5351 -0.0478 0.0037  -0.0099 224 TYR A O   
1732 C CB  . TYR A 224 ? 0.5693 0.6655 0.5774 -0.0431 0.0013  -0.0347 224 TYR A CB  
1733 C CG  . TYR A 224 ? 0.5419 0.6345 0.5254 -0.0407 0.0138  -0.0291 224 TYR A CG  
1734 C CD1 . TYR A 224 ? 0.5160 0.5987 0.4854 -0.0435 0.0211  -0.0286 224 TYR A CD1 
1735 C CD2 . TYR A 224 ? 0.5211 0.6204 0.4969 -0.0353 0.0182  -0.0254 224 TYR A CD2 
1736 C CE1 . TYR A 224 ? 0.5146 0.5889 0.4607 -0.0407 0.0335  -0.0235 224 TYR A CE1 
1737 C CE2 . TYR A 224 ? 0.4771 0.5711 0.4302 -0.0303 0.0294  -0.0198 224 TYR A CE2 
1738 C CZ  . TYR A 224 ? 0.6038 0.6826 0.5410 -0.0329 0.0376  -0.0184 224 TYR A CZ  
1739 O OH  . TYR A 224 ? 0.6502 0.7187 0.5637 -0.0274 0.0497  -0.0126 224 TYR A OH  
1740 N N   . ALA A 225 ? 0.4938 0.5856 0.5182 -0.0494 -0.0098 -0.0199 225 ALA A N   
1741 C CA  . ALA A 225 ? 0.6322 0.7307 0.6583 -0.0515 -0.0067 -0.0150 225 ALA A CA  
1742 C C   . ALA A 225 ? 0.5506 0.6361 0.5738 -0.0582 -0.0074 -0.0027 225 ALA A C   
1743 O O   . ALA A 225 ? 0.6153 0.7058 0.6475 -0.0629 -0.0057 0.0003  225 ALA A O   
1744 C CB  . ALA A 225 ? 0.5164 0.6275 0.5643 -0.0520 -0.0118 -0.0257 225 ALA A CB  
1745 N N   . ALA A 226 ? 0.4981 0.5683 0.5086 -0.0592 -0.0096 0.0040  226 ALA A N   
1746 C CA  . ALA A 226 ? 0.5966 0.6531 0.5963 -0.0644 -0.0092 0.0171  226 ALA A CA  
1747 C C   . ALA A 226 ? 0.4895 0.5436 0.4632 -0.0633 -0.0004 0.0232  226 ALA A C   
1748 O O   . ALA A 226 ? 0.5063 0.5633 0.4703 -0.0591 0.0031  0.0177  226 ALA A O   
1749 C CB  . ALA A 226 ? 0.5250 0.5646 0.5273 -0.0651 -0.0207 0.0205  226 ALA A CB  
1750 N N   . VAL A 227 ? 0.5209 0.5680 0.4825 -0.0678 0.0045  0.0344  227 VAL A N   
1751 C CA  . VAL A 227 ? 0.5032 0.5451 0.4381 -0.0668 0.0127  0.0396  227 VAL A CA  
1752 C C   . VAL A 227 ? 0.5127 0.5438 0.4344 -0.0657 0.0055  0.0370  227 VAL A C   
1753 O O   . VAL A 227 ? 0.5224 0.5531 0.4298 -0.0634 0.0108  0.0323  227 VAL A O   
1754 C CB  . VAL A 227 ? 0.6074 0.6427 0.5307 -0.0725 0.0190  0.0520  227 VAL A CB  
1755 C CG1 . VAL A 227 ? 0.5421 0.5709 0.4355 -0.0711 0.0276  0.0558  227 VAL A CG1 
1756 C CG2 . VAL A 227 ? 0.6137 0.6651 0.5550 -0.0750 0.0271  0.0523  227 VAL A CG2 
1757 N N   . CYS A 228 ? 0.5769 0.5991 0.5042 -0.0671 -0.0069 0.0397  228 CYS A N   
1758 C CA  . CYS A 228 ? 0.6313 0.6484 0.5512 -0.0655 -0.0168 0.0361  228 CYS A CA  
1759 C C   . CYS A 228 ? 0.5258 0.5516 0.4712 -0.0621 -0.0251 0.0246  228 CYS A C   
1760 O O   . CYS A 228 ? 0.5407 0.5648 0.5051 -0.0608 -0.0325 0.0252  228 CYS A O   
1761 C CB  . CYS A 228 ? 0.5605 0.5629 0.4667 -0.0665 -0.0261 0.0476  228 CYS A CB  
1762 S SG  . CYS A 228 ? 0.6698 0.6711 0.5674 -0.0633 -0.0414 0.0426  228 CYS A SG  
1763 N N   . VAL A 229 ? 0.5512 0.5852 0.4969 -0.0612 -0.0221 0.0139  229 VAL A N   
1764 C CA  . VAL A 229 ? 0.5172 0.5624 0.4858 -0.0585 -0.0255 0.0017  229 VAL A CA  
1765 C C   . VAL A 229 ? 0.4900 0.5376 0.4668 -0.0573 -0.0383 -0.0036 229 VAL A C   
1766 O O   . VAL A 229 ? 0.5527 0.5995 0.5155 -0.0601 -0.0394 -0.0052 229 VAL A O   
1767 C CB  . VAL A 229 ? 0.5628 0.6148 0.5263 -0.0586 -0.0124 -0.0061 229 VAL A CB  
1768 C CG1 . VAL A 229 ? 0.5466 0.6105 0.5311 -0.0566 -0.0139 -0.0186 229 VAL A CG1 
1769 C CG2 . VAL A 229 ? 0.5668 0.6197 0.5231 -0.0568 -0.0019 -0.0007 229 VAL A CG2 
1770 N N   . ARG A 230 ? 0.4871 0.5384 0.4876 -0.0528 -0.0485 -0.0076 230 ARG A N   
1771 C CA  . ARG A 230 ? 0.5138 0.5718 0.5282 -0.0489 -0.0621 -0.0139 230 ARG A CA  
1772 C C   . ARG A 230 ? 0.5833 0.6566 0.6255 -0.0457 -0.0612 -0.0287 230 ARG A C   
1773 O O   . ARG A 230 ? 0.5316 0.6040 0.5935 -0.0399 -0.0679 -0.0308 230 ARG A O   
1774 C CB  . ARG A 230 ? 0.5395 0.5840 0.5539 -0.0434 -0.0765 -0.0027 230 ARG A CB  
1775 C CG  . ARG A 230 ? 0.5892 0.6195 0.5727 -0.0463 -0.0779 0.0116  230 ARG A CG  
1776 C CD  . ARG A 230 ? 0.6589 0.6974 0.6330 -0.0456 -0.0874 0.0072  230 ARG A CD  
1777 N NE  . ARG A 230 ? 0.6674 0.6935 0.6076 -0.0487 -0.0871 0.0188  230 ARG A NE  
1778 C CZ  . ARG A 230 ? 0.5951 0.6214 0.5141 -0.0559 -0.0755 0.0166  230 ARG A CZ  
1779 N NH1 . ARG A 230 ? 0.6253 0.6609 0.5519 -0.0607 -0.0630 0.0052  230 ARG A NH1 
1780 N NH2 . ARG A 230 ? 0.7157 0.7305 0.6030 -0.0578 -0.0757 0.0265  230 ARG A NH2 
1781 N N   . CYS A 231 ? 0.5302 0.6159 0.5729 -0.0499 -0.0516 -0.0391 231 CYS A N   
1782 C CA  . CYS A 231 ? 0.5128 0.6147 0.5785 -0.0482 -0.0478 -0.0537 231 CYS A CA  
1783 C C   . CYS A 231 ? 0.5581 0.6761 0.6400 -0.0486 -0.0552 -0.0643 231 CYS A C   
1784 O O   . CYS A 231 ? 0.5735 0.6904 0.6458 -0.0507 -0.0632 -0.0610 231 CYS A O   
1785 C CB  . CYS A 231 ? 0.4755 0.5791 0.5292 -0.0531 -0.0297 -0.0572 231 CYS A CB  
1786 S SG  . CYS A 231 ? 0.5499 0.6450 0.5929 -0.0503 -0.0223 -0.0496 231 CYS A SG  
1787 N N   . PRO A 232 ? 0.5688 0.7047 0.6763 -0.0464 -0.0531 -0.0785 232 PRO A N   
1788 C CA  . PRO A 232 ? 0.4876 0.6448 0.6148 -0.0481 -0.0581 -0.0910 232 PRO A CA  
1789 C C   . PRO A 232 ? 0.5675 0.7277 0.6805 -0.0610 -0.0454 -0.0953 232 PRO A C   
1790 O O   . PRO A 232 ? 0.6243 0.7851 0.7331 -0.0671 -0.0277 -0.1002 232 PRO A O   
1791 C CB  . PRO A 232 ? 0.5084 0.6836 0.6655 -0.0431 -0.0545 -0.1053 232 PRO A CB  
1792 C CG  . PRO A 232 ? 0.5677 0.7280 0.7230 -0.0354 -0.0560 -0.0992 232 PRO A CG  
1793 C CD  . PRO A 232 ? 0.5705 0.7097 0.6935 -0.0408 -0.0492 -0.0846 232 PRO A CD  
1794 N N   . GLY A 233 ? 0.5183 0.6784 0.6218 -0.0651 -0.0541 -0.0934 233 GLY A N   
1795 C CA  . GLY A 233 ? 0.5504 0.7115 0.6419 -0.0785 -0.0430 -0.0996 233 GLY A CA  
1796 C C   . GLY A 233 ? 0.6395 0.7750 0.6962 -0.0842 -0.0272 -0.0894 233 GLY A C   
1797 O O   . GLY A 233 ? 0.5164 0.6475 0.5619 -0.0953 -0.0144 -0.0948 233 GLY A O   
1798 N N   . TYR A 234 ? 0.6102 0.7290 0.6513 -0.0769 -0.0274 -0.0755 234 TYR A N   
1799 C CA  . TYR A 234 ? 0.6822 0.7801 0.6934 -0.0793 -0.0132 -0.0657 234 TYR A CA  
1800 C C   . TYR A 234 ? 0.5953 0.6807 0.5930 -0.0725 -0.0215 -0.0510 234 TYR A C   
1801 O O   . TYR A 234 ? 0.5474 0.6366 0.5602 -0.0653 -0.0320 -0.0479 234 TYR A O   
1802 C CB  . TYR A 234 ? 0.5434 0.6402 0.5551 -0.0783 0.0030  -0.0676 234 TYR A CB  
1803 C CG  . TYR A 234 ? 0.5211 0.5988 0.5043 -0.0768 0.0159  -0.0569 234 TYR A CG  
1804 C CD1 . TYR A 234 ? 0.5648 0.6289 0.5277 -0.0832 0.0312  -0.0576 234 TYR A CD1 
1805 C CD2 . TYR A 234 ? 0.6420 0.7156 0.6204 -0.0688 0.0129  -0.0470 234 TYR A CD2 
1806 C CE1 . TYR A 234 ? 0.6096 0.6564 0.5472 -0.0789 0.0425  -0.0477 234 TYR A CE1 
1807 C CE2 . TYR A 234 ? 0.6702 0.7314 0.6261 -0.0659 0.0237  -0.0382 234 TYR A CE2 
1808 C CZ  . TYR A 234 ? 0.6571 0.7049 0.5923 -0.0696 0.0381  -0.0382 234 TYR A CZ  
1809 O OH  . TYR A 234 ? 0.6320 0.6674 0.5456 -0.0638 0.0484  -0.0294 234 TYR A OH  
1810 N N   . GLY A 235 ? 0.5695 0.6391 0.5395 -0.0752 -0.0156 -0.0427 235 GLY A N   
1811 C CA  . GLY A 235 ? 0.6266 0.6853 0.5835 -0.0703 -0.0193 -0.0287 235 GLY A CA  
1812 C C   . GLY A 235 ? 0.5810 0.6265 0.5088 -0.0740 -0.0167 -0.0225 235 GLY A C   
1813 O O   . GLY A 235 ? 0.5849 0.6269 0.5008 -0.0804 -0.0102 -0.0295 235 GLY A O   
1814 N N   . THR A 236 ? 0.5184 0.5558 0.4352 -0.0707 -0.0210 -0.0099 236 THR A N   
1815 C CA  . THR A 236 ? 0.5849 0.6096 0.4719 -0.0731 -0.0165 -0.0027 236 THR A CA  
1816 C C   . THR A 236 ? 0.6356 0.6612 0.5120 -0.0770 -0.0274 -0.0080 236 THR A C   
1817 O O   . THR A 236 ? 0.6487 0.6785 0.5303 -0.0739 -0.0438 -0.0048 236 THR A O   
1818 C CB  . THR A 236 ? 0.5683 0.5863 0.4487 -0.0698 -0.0181 0.0121  236 THR A CB  
1819 O OG1 . THR A 236 ? 0.5498 0.5716 0.4437 -0.0670 -0.0093 0.0143  236 THR A OG1 
1820 C CG2 . THR A 236 ? 0.5617 0.5680 0.4104 -0.0720 -0.0108 0.0193  236 THR A CG2 
1821 N N   . ARG A 237 ? 0.6317 0.6527 0.4926 -0.0833 -0.0188 -0.0167 237 ARG A N   
1822 C CA  . ARG A 237 ? 0.5835 0.6069 0.4326 -0.0886 -0.0285 -0.0248 237 ARG A CA  
1823 C C   . ARG A 237 ? 0.6289 0.6374 0.4419 -0.0900 -0.0243 -0.0191 237 ARG A C   
1824 O O   . ARG A 237 ? 0.7013 0.7121 0.4999 -0.0916 -0.0369 -0.0212 237 ARG A O   
1825 C CB  . ARG A 237 ? 0.6195 0.6478 0.4777 -0.0976 -0.0218 -0.0420 237 ARG A CB  
1826 C CG  . ARG A 237 ? 0.7755 0.8220 0.6691 -0.0975 -0.0258 -0.0503 237 ARG A CG  
1827 C CD  . ARG A 237 ? 0.7536 0.8019 0.6541 -0.1085 -0.0139 -0.0660 237 ARG A CD  
1828 N NE  . ARG A 237 ? 0.8950 0.9450 0.7843 -0.1180 -0.0194 -0.0776 237 ARG A NE  
1829 C CZ  . ARG A 237 ? 0.8814 0.9319 0.7756 -0.1308 -0.0101 -0.0932 237 ARG A CZ  
1830 N NH1 . ARG A 237 ? 0.8365 0.8842 0.7443 -0.1352 0.0062  -0.0974 237 ARG A NH1 
1831 N NH2 . ARG A 237 ? 0.8878 0.9410 0.7719 -0.1401 -0.0168 -0.1053 237 ARG A NH2 
1832 N N   . THR A 238 ? 0.6684 0.7913 0.4888 -0.0847 0.0128  -0.0793 238 THR A N   
1833 C CA  . THR A 238 ? 0.6148 0.7311 0.4424 -0.1056 0.0085  -0.0716 238 THR A CA  
1834 C C   . THR A 238 ? 0.5734 0.6615 0.4031 -0.1070 -0.0030 -0.0818 238 THR A C   
1835 O O   . THR A 238 ? 0.5978 0.6704 0.4130 -0.0999 -0.0075 -0.0933 238 THR A O   
1836 C CB  . THR A 238 ? 0.6612 0.7866 0.4757 -0.1180 0.0142  -0.0649 238 THR A CB  
1837 O OG1 . THR A 238 ? 0.7626 0.9157 0.5761 -0.1158 0.0238  -0.0541 238 THR A OG1 
1838 C CG2 . THR A 238 ? 0.6373 0.7609 0.4596 -0.1371 0.0117  -0.0584 238 THR A CG2 
1839 N N   . ASN A 239 ? 0.6272 0.7118 0.4756 -0.1170 -0.0084 -0.0753 239 ASN A N   
1840 C CA  . ASN A 239 ? 0.5751 0.6415 0.4315 -0.1234 -0.0179 -0.0789 239 ASN A CA  
1841 C C   . ASN A 239 ? 0.6216 0.6983 0.4777 -0.1401 -0.0125 -0.0718 239 ASN A C   
1842 O O   . ASN A 239 ? 0.5914 0.6850 0.4515 -0.1494 -0.0074 -0.0614 239 ASN A O   
1843 C CB  . ASN A 239 ? 0.5744 0.6324 0.4543 -0.1230 -0.0282 -0.0740 239 ASN A CB  
1844 C CG  . ASN A 239 ? 0.7075 0.7597 0.5920 -0.1053 -0.0319 -0.0794 239 ASN A CG  
1845 O OD1 . ASN A 239 ? 0.5778 0.6388 0.4797 -0.1053 -0.0330 -0.0686 239 ASN A OD1 
1846 N ND2 . ASN A 239 ? 0.5807 0.6185 0.4490 -0.0890 -0.0346 -0.0967 239 ASN A ND2 
1847 N N   . THR A 240 ? 0.6619 0.7286 0.5129 -0.1428 -0.0144 -0.0785 240 THR A N   
1848 C CA  . THR A 240 ? 0.6044 0.6792 0.4547 -0.1545 -0.0088 -0.0761 240 THR A CA  
1849 C C   . THR A 240 ? 0.6235 0.6924 0.4882 -0.1578 -0.0138 -0.0782 240 THR A C   
1850 O O   . THR A 240 ? 0.6834 0.7374 0.5500 -0.1518 -0.0219 -0.0852 240 THR A O   
1851 C CB  . THR A 240 ? 0.6505 0.7229 0.4838 -0.1541 -0.0051 -0.0802 240 THR A CB  
1852 O OG1 . THR A 240 ? 0.6612 0.7437 0.4849 -0.1516 -0.0005 -0.0751 240 THR A OG1 
1853 C CG2 . THR A 240 ? 0.6804 0.7576 0.5135 -0.1643 -0.0007 -0.0805 240 THR A CG2 
1854 N N   . ILE A 241 ? 0.5660 0.6501 0.4407 -0.1675 -0.0091 -0.0713 241 ILE A N   
1855 C CA  . ILE A 241 ? 0.6381 0.7271 0.5304 -0.1717 -0.0103 -0.0697 241 ILE A CA  
1856 C C   . ILE A 241 ? 0.5771 0.6775 0.4622 -0.1752 0.0000  -0.0751 241 ILE A C   
1857 O O   . ILE A 241 ? 0.6050 0.7173 0.4778 -0.1805 0.0075  -0.0737 241 ILE A O   
1858 C CB  . ILE A 241 ? 0.5710 0.6739 0.4821 -0.1794 -0.0122 -0.0551 241 ILE A CB  
1859 C CG1 . ILE A 241 ? 0.6174 0.7049 0.5365 -0.1746 -0.0241 -0.0511 241 ILE A CG1 
1860 C CG2 . ILE A 241 ? 0.4992 0.6126 0.4330 -0.1844 -0.0131 -0.0500 241 ILE A CG2 
1861 C CD1 . ILE A 241 ? 0.6780 0.7445 0.6121 -0.1697 -0.0386 -0.0558 241 ILE A CD1 
1862 N N   . ILE A 242 ? 0.5941 0.6898 0.4877 -0.1714 -0.0013 -0.0820 242 ILE A N   
1863 C CA  . ILE A 242 ? 0.5693 0.6740 0.4608 -0.1714 0.0076  -0.0896 242 ILE A CA  
1864 C C   . ILE A 242 ? 0.5834 0.7046 0.5004 -0.1713 0.0100  -0.0867 242 ILE A C   
1865 O O   . ILE A 242 ? 0.5586 0.6721 0.4939 -0.1685 0.0003  -0.0847 242 ILE A O   
1866 C CB  . ILE A 242 ? 0.6194 0.7040 0.5002 -0.1652 0.0041  -0.1001 242 ILE A CB  
1867 C CG1 . ILE A 242 ? 0.6295 0.7035 0.4891 -0.1667 0.0020  -0.0983 242 ILE A CG1 
1868 C CG2 . ILE A 242 ? 0.6102 0.6998 0.4903 -0.1636 0.0117  -0.1102 242 ILE A CG2 
1869 C CD1 . ILE A 242 ? 0.5997 0.6565 0.4494 -0.1636 -0.0024 -0.1032 242 ILE A CD1 
1870 N N   . LEU A 243 ? 0.5912 0.7379 0.5093 -0.1745 0.0223  -0.0858 243 LEU A N   
1871 C CA  . LEU A 243 ? 0.6376 0.8104 0.5808 -0.1740 0.0291  -0.0816 243 LEU A CA  
1872 C C   . LEU A 243 ? 0.5736 0.7557 0.5103 -0.1658 0.0411  -0.0976 243 LEU A C   
1873 O O   . LEU A 243 ? 0.5840 0.7623 0.4943 -0.1658 0.0466  -0.1078 243 LEU A O   
1874 C CB  . LEU A 243 ? 0.5655 0.7685 0.5166 -0.1844 0.0350  -0.0637 243 LEU A CB  
1875 C CG  . LEU A 243 ? 0.6179 0.8100 0.5756 -0.1924 0.0221  -0.0478 243 LEU A CG  
1876 C CD1 . LEU A 243 ? 0.5508 0.7754 0.5182 -0.2040 0.0277  -0.0269 243 LEU A CD1 
1877 C CD2 . LEU A 243 ? 0.4964 0.6686 0.4784 -0.1902 0.0061  -0.0453 243 LEU A CD2 
1878 N N   . VAL A 244 ? 0.5826 0.7755 0.5454 -0.1582 0.0434  -0.1006 244 VAL A N   
1879 C CA  . VAL A 244 ? 0.6053 0.8119 0.5696 -0.1470 0.0560  -0.1164 244 VAL A CA  
1880 C C   . VAL A 244 ? 0.5850 0.8330 0.5836 -0.1452 0.0660  -0.1060 244 VAL A C   
1881 O O   . VAL A 244 ? 0.5333 0.7813 0.5642 -0.1442 0.0568  -0.0975 244 VAL A O   
1882 C CB  . VAL A 244 ? 0.5969 0.7723 0.5638 -0.1359 0.0470  -0.1313 244 VAL A CB  
1883 C CG1 . VAL A 244 ? 0.6246 0.8110 0.5949 -0.1219 0.0591  -0.1502 244 VAL A CG1 
1884 C CG2 . VAL A 244 ? 0.5562 0.6949 0.4938 -0.1404 0.0361  -0.1351 244 VAL A CG2 
1885 N N   . ASP A 245 ? 0.5634 0.8493 0.5554 -0.1455 0.0842  -0.1054 245 ASP A N   
1886 C CA  . ASP A 245 ? 0.5500 0.8841 0.5762 -0.1443 0.0965  -0.0923 245 ASP A CA  
1887 C C   . ASP A 245 ? 0.5556 0.9021 0.5986 -0.1247 0.1072  -0.1113 245 ASP A C   
1888 O O   . ASP A 245 ? 0.5973 0.9103 0.6255 -0.1131 0.1025  -0.1339 245 ASP A O   
1889 C CB  . ASP A 245 ? 0.6885 1.0643 0.7005 -0.1539 0.1119  -0.0789 245 ASP A CB  
1890 C CG  . ASP A 245 ? 0.6889 1.0713 0.6595 -0.1457 0.1267  -0.1013 245 ASP A CG  
1891 O OD1 . ASP A 245 ? 0.6870 1.0520 0.6502 -0.1295 0.1294  -0.1280 245 ASP A OD1 
1892 O OD2 . ASP A 245 ? 0.7902 1.1936 0.7357 -0.1560 0.1336  -0.0920 245 ASP A OD2 
1893 N N   . ALA A 246 ? 0.5582 0.9545 0.6360 -0.1207 0.1210  -0.1005 246 ALA A N   
1894 C CA  . ALA A 246 ? 0.5973 1.0094 0.7017 -0.0999 0.1304  -0.1162 246 ALA A CA  
1895 C C   . ALA A 246 ? 0.6352 1.0400 0.7051 -0.0825 0.1439  -0.1487 246 ALA A C   
1896 O O   . ALA A 246 ? 0.6690 1.0520 0.7482 -0.0646 0.1407  -0.1699 246 ALA A O   
1897 C CB  . ALA A 246 ? 0.5900 1.0679 0.7385 -0.0993 0.1465  -0.0962 246 ALA A CB  
1898 N N   . ASP A 247 ? 0.6657 1.0865 0.6958 -0.0875 0.1567  -0.1530 247 ASP A N   
1899 C CA  . ASP A 247 ? 0.7133 1.1291 0.7077 -0.0713 0.1686  -0.1857 247 ASP A CA  
1900 C C   . ASP A 247 ? 0.6936 1.0459 0.6518 -0.0741 0.1500  -0.2044 247 ASP A C   
1901 O O   . ASP A 247 ? 0.7119 1.0488 0.6433 -0.0609 0.1539  -0.2340 247 ASP A O   
1902 C CB  . ASP A 247 ? 0.7353 1.2001 0.6996 -0.0758 0.1897  -0.1822 247 ASP A CB  
1903 C CG  . ASP A 247 ? 0.7292 1.2654 0.7280 -0.0700 0.2126  -0.1660 247 ASP A CG  
1904 O OD1 . ASP A 247 ? 0.7142 1.2642 0.7537 -0.0525 0.2182  -0.1727 247 ASP A OD1 
1905 O OD2 . ASP A 247 ? 0.7760 1.3572 0.7637 -0.0834 0.2247  -0.1443 247 ASP A OD2 
1906 N N   . GLY A 248 ? 0.7024 1.0187 0.6597 -0.0905 0.1298  -0.1882 248 GLY A N   
1907 C CA  . GLY A 248 ? 0.7113 0.9732 0.6409 -0.0940 0.1125  -0.2010 248 GLY A CA  
1908 C C   . GLY A 248 ? 0.7355 0.9887 0.6268 -0.1114 0.1080  -0.1942 248 GLY A C   
1909 O O   . GLY A 248 ? 0.7239 0.9377 0.5917 -0.1146 0.0954  -0.2054 248 GLY A O   
1910 N N   . HIS A 249 ? 0.6935 0.9831 0.5811 -0.1235 0.1166  -0.1739 249 HIS A N   
1911 C CA  . HIS A 249 ? 0.7368 1.0192 0.5937 -0.1403 0.1102  -0.1634 249 HIS A CA  
1912 C C   . HIS A 249 ? 0.7152 0.9654 0.5839 -0.1509 0.0917  -0.1467 249 HIS A C   
1913 O O   . HIS A 249 ? 0.5970 0.8543 0.4957 -0.1540 0.0880  -0.1287 249 HIS A O   
1914 C CB  . HIS A 249 ? 0.6955 1.0274 0.5482 -0.1500 0.1233  -0.1435 249 HIS A CB  
1915 C CG  . HIS A 249 ? 0.7814 1.1576 0.6284 -0.1379 0.1453  -0.1557 249 HIS A CG  
1916 N ND1 . HIS A 249 ? 0.8682 1.2355 0.7083 -0.1179 0.1522  -0.1879 249 HIS A ND1 
1917 C CD2 . HIS A 249 ? 0.9073 1.3393 0.7545 -0.1420 0.1626  -0.1395 249 HIS A CD2 
1918 C CE1 . HIS A 249 ? 0.8313 1.2483 0.6664 -0.1079 0.1744  -0.1939 249 HIS A CE1 
1919 N NE2 . HIS A 249 ? 0.8855 1.3450 0.7239 -0.1231 0.1818  -0.1634 249 HIS A NE2 
1920 N N   . VAL A 250 ? 0.7220 0.9383 0.5672 -0.1562 0.0797  -0.1530 250 VAL A N   
1921 C CA  . VAL A 250 ? 0.7132 0.9014 0.5643 -0.1636 0.0644  -0.1401 250 VAL A CA  
1922 C C   . VAL A 250 ? 0.7045 0.9031 0.5426 -0.1777 0.0619  -0.1223 250 VAL A C   
1923 O O   . VAL A 250 ? 0.6955 0.9070 0.5088 -0.1834 0.0661  -0.1248 250 VAL A O   
1924 C CB  . VAL A 250 ? 0.6697 0.8184 0.5089 -0.1607 0.0530  -0.1542 250 VAL A CB  
1925 C CG1 . VAL A 250 ? 0.7401 0.8677 0.5824 -0.1673 0.0403  -0.1400 250 VAL A CG1 
1926 C CG2 . VAL A 250 ? 0.6890 0.8250 0.5447 -0.1462 0.0531  -0.1701 250 VAL A CG2 
1927 N N   . THR A 251 ? 0.7251 0.9171 0.5799 -0.1824 0.0535  -0.1049 251 THR A N   
1928 C CA  . THR A 251 ? 0.6436 0.8385 0.4916 -0.1931 0.0478  -0.0883 251 THR A CA  
1929 C C   . THR A 251 ? 0.6580 0.8230 0.5093 -0.1914 0.0356  -0.0865 251 THR A C   
1930 O O   . THR A 251 ? 0.6320 0.7854 0.5017 -0.1863 0.0300  -0.0845 251 THR A O   
1931 C CB  . THR A 251 ? 0.6924 0.9134 0.5602 -0.1995 0.0500  -0.0673 251 THR A CB  
1932 O OG1 . THR A 251 ? 0.5998 0.8554 0.4666 -0.1995 0.0642  -0.0678 251 THR A OG1 
1933 C CG2 . THR A 251 ? 0.5861 0.8107 0.4468 -0.2097 0.0436  -0.0503 251 THR A CG2 
1934 N N   . PHE A 252 ? 0.6861 0.8415 0.5193 -0.1957 0.0312  -0.0867 252 PHE A N   
1935 C CA  . PHE A 252 ? 0.6773 0.8109 0.5102 -0.1933 0.0227  -0.0852 252 PHE A CA  
1936 C C   . PHE A 252 ? 0.6091 0.7507 0.4414 -0.1988 0.0190  -0.0704 252 PHE A C   
1937 O O   . PHE A 252 ? 0.6123 0.7634 0.4315 -0.2064 0.0191  -0.0673 252 PHE A O   
1938 C CB  . PHE A 252 ? 0.6675 0.7849 0.4854 -0.1932 0.0205  -0.0969 252 PHE A CB  
1939 C CG  . PHE A 252 ? 0.6315 0.7322 0.4494 -0.1909 0.0137  -0.0931 252 PHE A CG  
1940 C CD1 . PHE A 252 ? 0.6729 0.7792 0.4864 -0.1954 0.0111  -0.0824 252 PHE A CD1 
1941 C CD2 . PHE A 252 ? 0.6631 0.7461 0.4857 -0.1838 0.0101  -0.0989 252 PHE A CD2 
1942 C CE1 . PHE A 252 ? 0.6254 0.7235 0.4386 -0.1921 0.0077  -0.0779 252 PHE A CE1 
1943 C CE2 . PHE A 252 ? 0.7440 0.8167 0.5630 -0.1820 0.0050  -0.0935 252 PHE A CE2 
1944 C CZ  . PHE A 252 ? 0.6359 0.7178 0.4495 -0.1858 0.0051  -0.0832 252 PHE A CZ  
1945 N N   . THR A 253 ? 0.6532 0.7897 0.5010 -0.1944 0.0139  -0.0622 253 THR A N   
1946 C CA  . THR A 253 ? 0.6413 0.7829 0.4944 -0.1960 0.0093  -0.0491 253 THR A CA  
1947 C C   . THR A 253 ? 0.6056 0.7322 0.4575 -0.1868 0.0053  -0.0523 253 THR A C   
1948 O O   . THR A 253 ? 0.6259 0.7368 0.4783 -0.1788 0.0033  -0.0610 253 THR A O   
1949 C CB  . THR A 253 ? 0.5524 0.6987 0.4263 -0.1969 0.0048  -0.0374 253 THR A CB  
1950 O OG1 . THR A 253 ? 0.6999 0.8673 0.5749 -0.2057 0.0107  -0.0315 253 THR A OG1 
1951 C CG2 . THR A 253 ? 0.6288 0.7778 0.5115 -0.1970 -0.0018 -0.0239 253 THR A CG2 
1952 N N   . GLU A 254 ? 0.6279 0.7628 0.4782 -0.1876 0.0044  -0.0443 254 GLU A N   
1953 C CA  . GLU A 254 ? 0.5380 0.6670 0.3871 -0.1776 0.0036  -0.0458 254 GLU A CA  
1954 C C   . GLU A 254 ? 0.5104 0.6516 0.3716 -0.1745 0.0012  -0.0341 254 GLU A C   
1955 O O   . GLU A 254 ? 0.5225 0.6808 0.3833 -0.1830 0.0017  -0.0244 254 GLU A O   
1956 C CB  . GLU A 254 ? 0.5352 0.6658 0.3705 -0.1816 0.0070  -0.0486 254 GLU A CB  
1957 C CG  . GLU A 254 ? 0.5257 0.6557 0.3583 -0.1714 0.0086  -0.0484 254 GLU A CG  
1958 C CD  . GLU A 254 ? 0.6249 0.7665 0.4519 -0.1793 0.0106  -0.0411 254 GLU A CD  
1959 O OE1 . GLU A 254 ? 0.6316 0.7892 0.4639 -0.1881 0.0096  -0.0315 254 GLU A OE1 
1960 O OE2 . GLU A 254 ? 0.6613 0.7966 0.4801 -0.1780 0.0115  -0.0430 254 GLU A OE2 
1961 N N   . ARG A 255 ? 0.5022 0.6334 0.3752 -0.1617 -0.0032 -0.0359 255 ARG A N   
1962 C CA  . ARG A 255 ? 0.5789 0.7182 0.4671 -0.1536 -0.0062 -0.0275 255 ARG A CA  
1963 C C   . ARG A 255 ? 0.5380 0.6814 0.4204 -0.1389 -0.0006 -0.0338 255 ARG A C   
1964 O O   . ARG A 255 ? 0.5295 0.6583 0.4009 -0.1285 0.0002  -0.0470 255 ARG A O   
1965 C CB  . ARG A 255 ? 0.5744 0.6975 0.4812 -0.1472 -0.0166 -0.0268 255 ARG A CB  
1966 C CG  . ARG A 255 ? 0.5800 0.7060 0.5072 -0.1358 -0.0224 -0.0196 255 ARG A CG  
1967 C CD  . ARG A 255 ? 0.5947 0.7042 0.5443 -0.1372 -0.0362 -0.0126 255 ARG A CD  
1968 N NE  . ARG A 255 ? 0.7544 0.8547 0.7258 -0.1209 -0.0453 -0.0117 255 ARG A NE  
1969 C CZ  . ARG A 255 ? 0.8427 0.9205 0.8149 -0.1003 -0.0497 -0.0302 255 ARG A CZ  
1970 N NH1 . ARG A 255 ? 0.7770 0.8416 0.7272 -0.0945 -0.0461 -0.0492 255 ARG A NH1 
1971 N NH2 . ARG A 255 ? 0.9201 0.9882 0.9150 -0.0842 -0.0591 -0.0303 255 ARG A NH2 
1972 N N   . SER A 256 ? 0.5520 0.7186 0.4420 -0.1385 0.0032  -0.0229 256 SER A N   
1973 C CA  . SER A 256 ? 0.6647 0.8464 0.5506 -0.1270 0.0117  -0.0242 256 SER A CA  
1974 C C   . SER A 256 ? 0.6568 0.8551 0.5645 -0.1119 0.0123  -0.0180 256 SER A C   
1975 O O   . SER A 256 ? 0.5721 0.7816 0.4985 -0.1186 0.0068  -0.0042 256 SER A O   
1976 C CB  . SER A 256 ? 0.6540 0.8548 0.5322 -0.1429 0.0166  -0.0143 256 SER A CB  
1977 O OG  . SER A 256 ? 0.5752 0.7589 0.4357 -0.1546 0.0153  -0.0215 256 SER A OG  
1978 N N   . MET A 257 ? 0.6085 0.8096 0.5129 -0.0904 0.0188  -0.0284 257 MET A N   
1979 C CA  . MET A 257 ? 0.6411 0.8636 0.5664 -0.0716 0.0229  -0.0246 257 MET A CA  
1980 C C   . MET A 257 ? 0.6300 0.8935 0.5656 -0.0804 0.0316  -0.0053 257 MET A C   
1981 O O   . MET A 257 ? 0.6585 0.9344 0.5788 -0.0903 0.0389  -0.0013 257 MET A O   
1982 C CB  . MET A 257 ? 0.6547 0.8708 0.5672 -0.0447 0.0293  -0.0446 257 MET A CB  
1983 C CG  . MET A 257 ? 0.8020 1.0431 0.7337 -0.0194 0.0369  -0.0454 257 MET A CG  
1984 S SD  . MET A 257 ? 0.8763 1.1159 0.7799 0.0120  0.0480  -0.0719 257 MET A SD  
1985 C CE  . MET A 257 ? 0.8216 1.0033 0.7224 0.0246  0.0277  -0.0976 257 MET A CE  
1986 N N   . MET A 258 ? 0.7224 1.0067 0.6874 -0.0780 0.0285  0.0089  258 MET A N   
1987 C CA  . MET A 258 ? 0.7389 1.0624 0.7193 -0.0908 0.0322  0.0305  258 MET A CA  
1988 C C   . MET A 258 ? 0.6731 1.0350 0.6799 -0.0691 0.0425  0.0375  258 MET A C   
1989 O O   . MET A 258 ? 0.8708 1.2671 0.8792 -0.0710 0.0540  0.0477  258 MET A O   
1990 C CB  . MET A 258 ? 0.5996 0.9226 0.5929 -0.1122 0.0180  0.0465  258 MET A CB  
1991 C CG  . MET A 258 ? 0.5991 0.8947 0.5666 -0.1346 0.0106  0.0416  258 MET A CG  
1992 S SD  . MET A 258 ? 0.6078 0.8978 0.5453 -0.1475 0.0179  0.0341  258 MET A SD  
1993 C CE  . MET A 258 ? 0.5256 0.8478 0.4741 -0.1700 0.0138  0.0559  258 MET A CE  
1994 N N   . ASP A 259 ? 1.0564 1.4150 1.0870 -0.0483 0.0383  0.0338  259 ASP A N   
1995 C CA  . ASP A 259 ? 1.1666 1.5645 1.2276 -0.0246 0.0484  0.0399  259 ASP A CA  
1996 C C   . ASP A 259 ? 1.2423 1.6418 1.2893 0.0073  0.0636  0.0170  259 ASP A C   
1997 O O   . ASP A 259 ? 1.2814 1.7204 1.3496 0.0299  0.0769  0.0199  259 ASP A O   
1998 C CB  . ASP A 259 ? 1.2041 1.5984 1.3020 -0.0151 0.0350  0.0474  259 ASP A CB  
1999 N N   . LYS A 260 ? 1.1695 1.5300 1.1813 0.0102  0.0620  -0.0056 260 LYS A N   
2000 C CA  . LYS A 260 ? 1.2734 1.6276 1.2643 0.0402  0.0724  -0.0314 260 LYS A CA  
2001 C C   . LYS A 260 ? 1.2823 1.6242 1.2963 0.0729  0.0676  -0.0478 260 LYS A C   
2002 O O   . LYS A 260 ? 1.2844 1.6281 1.2849 0.1038  0.0775  -0.0709 260 LYS A O   
2003 C CB  . LYS A 260 ? 1.2901 1.6953 1.2714 0.0476  0.0951  -0.0243 260 LYS A CB  
2004 C CG  . LYS A 260 ? 1.2176 1.6351 1.1821 0.0147  0.0976  -0.0049 260 LYS A CG  
2005 C CD  . LYS A 260 ? 1.1518 1.5172 1.0887 -0.0062 0.0825  -0.0148 260 LYS A CD  
2006 C CE  . LYS A 260 ? 1.0498 1.4214 0.9635 -0.0299 0.0862  -0.0038 260 LYS A CE  
2007 N NZ  . LYS A 260 ? 0.9878 1.3725 0.9196 -0.0601 0.0795  0.0208  260 LYS A NZ  
2008 N N   . ASP A 261 ? 1.2339 1.5628 1.2818 0.0675  0.0515  -0.0363 261 ASP A N   
2009 C CA  . ASP A 261 ? 1.1872 1.4905 1.2599 0.0947  0.0399  -0.0511 261 ASP A CA  
2010 C C   . ASP A 261 ? 1.1877 1.4294 1.2503 0.0857  0.0175  -0.0636 261 ASP A C   
2011 O O   . ASP A 261 ? 1.1304 1.3416 1.2152 0.1046  0.0026  -0.0747 261 ASP A O   
2012 C CB  . ASP A 261 ? 1.1955 1.5258 1.3185 0.0955  0.0342  -0.0264 261 ASP A CB  
2013 C CG  . ASP A 261 ? 1.0654 1.3919 1.1973 0.0572  0.0193  0.0019  261 ASP A CG  
2014 O OD1 . ASP A 261 ? 1.0923 1.3974 1.1926 0.0313  0.0157  0.0016  261 ASP A OD1 
2015 O OD2 . ASP A 261 ? 1.0150 1.3613 1.1851 0.0541  0.0111  0.0241  261 ASP A OD2 
2016 N N   . LEU A 262 ? 1.1312 1.3545 1.1646 0.0578  0.0139  -0.0611 262 LEU A N   
2017 C CA  . LEU A 262 ? 1.0750 1.2468 1.0983 0.0467  -0.0052 -0.0706 262 LEU A CA  
2018 C C   . LEU A 262 ? 1.0393 1.1959 1.0966 0.0320  -0.0247 -0.0504 262 LEU A C   
2019 O O   . LEU A 262 ? 1.0356 1.1510 1.0955 0.0261  -0.0428 -0.0554 262 LEU A O   
2020 C CB  . LEU A 262 ? 1.1409 1.2763 1.1511 0.0756  -0.0114 -0.1042 262 LEU A CB  
2021 C CG  . LEU A 262 ? 1.0489 1.2021 1.0205 0.0917  0.0078  -0.1242 262 LEU A CG  
2022 C CD1 . LEU A 262 ? 1.1963 1.3735 1.1769 0.1300  0.0206  -0.1394 262 LEU A CD1 
2023 C CD2 . LEU A 262 ? 1.0290 1.1389 0.9664 0.0914  -0.0030 -0.1483 262 LEU A CD2 
2024 N N   . SER A 263 ? 0.9755 1.1660 1.0595 0.0242  -0.0228 -0.0251 263 SER A N   
2025 C CA  . SER A 263 ? 0.9234 1.1068 1.0351 0.0060  -0.0407 -0.0005 263 SER A CA  
2026 C C   . SER A 263 ? 0.8135 1.0251 0.9157 -0.0272 -0.0372 0.0245  263 SER A C   
2027 O O   . SER A 263 ? 0.8276 1.0347 0.9424 -0.0466 -0.0513 0.0450  263 SER A O   
2028 C CB  . SER A 263 ? 0.9174 1.1123 1.0739 0.0275  -0.0478 0.0086  263 SER A CB  
2029 O OG  . SER A 263 ? 1.0207 1.2599 1.1839 0.0447  -0.0290 0.0080  263 SER A OG  
2030 N N   . HIS A 264 ? 0.8060 1.0459 0.8857 -0.0343 -0.0203 0.0235  264 HIS A N   
2031 C CA  . HIS A 264 ? 0.7851 1.0476 0.8530 -0.0645 -0.0185 0.0425  264 HIS A CA  
2032 C C   . HIS A 264 ? 0.6651 0.9104 0.6942 -0.0790 -0.0124 0.0293  264 HIS A C   
2033 O O   . HIS A 264 ? 0.6608 0.9094 0.6710 -0.0696 0.0002  0.0148  264 HIS A O   
2034 C CB  . HIS A 264 ? 0.8257 1.1344 0.9062 -0.0634 -0.0078 0.0556  264 HIS A CB  
2035 C CG  . HIS A 264 ? 0.8981 1.2298 1.0209 -0.0543 -0.0157 0.0743  264 HIS A CG  
2036 N ND1 . HIS A 264 ? 0.9868 1.3556 1.1258 -0.0710 -0.0188 0.0992  264 HIS A ND1 
2037 C CD2 . HIS A 264 ? 0.9116 1.2330 1.0661 -0.0300 -0.0235 0.0720  264 HIS A CD2 
2038 C CE1 . HIS A 264 ? 0.8365 1.2199 1.0163 -0.0575 -0.0273 0.1131  264 HIS A CE1 
2039 N NE2 . HIS A 264 ? 0.8819 1.2362 1.0726 -0.0318 -0.0300 0.0967  264 HIS A NE2 
2040 N N   . TRP A 265 ? 0.7141 0.9442 0.7323 -0.1012 -0.0212 0.0357  265 TRP A N   
2041 C CA  . TRP A 265 ? 0.6203 0.8345 0.6069 -0.1146 -0.0168 0.0243  265 TRP A CA  
2042 C C   . TRP A 265 ? 0.6792 0.9063 0.6541 -0.1417 -0.0191 0.0383  265 TRP A C   
2043 O O   . TRP A 265 ? 0.6132 0.8507 0.6014 -0.1523 -0.0285 0.0562  265 TRP A O   
2044 C CB  . TRP A 265 ? 0.6133 0.7912 0.5978 -0.1100 -0.0251 0.0121  265 TRP A CB  
2045 C CG  . TRP A 265 ? 0.7103 0.8686 0.6982 -0.0835 -0.0251 -0.0078 265 TRP A CG  
2046 C CD1 . TRP A 265 ? 0.6786 0.8287 0.6921 -0.0627 -0.0328 -0.0101 265 TRP A CD1 
2047 C CD2 . TRP A 265 ? 0.7064 0.8496 0.6692 -0.0738 -0.0185 -0.0297 265 TRP A CD2 
2048 N NE1 . TRP A 265 ? 0.8093 0.9395 0.8121 -0.0398 -0.0308 -0.0350 265 TRP A NE1 
2049 C CE2 . TRP A 265 ? 0.7128 0.8398 0.6832 -0.0471 -0.0222 -0.0463 265 TRP A CE2 
2050 C CE3 . TRP A 265 ? 0.6893 0.8305 0.6241 -0.0845 -0.0113 -0.0369 265 TRP A CE3 
2051 C CZ2 . TRP A 265 ? 0.6864 0.7973 0.6327 -0.0319 -0.0188 -0.0699 265 TRP A CZ2 
2052 C CZ3 . TRP A 265 ? 0.6905 0.8162 0.6053 -0.0705 -0.0084 -0.0570 265 TRP A CZ3 
2053 C CH2 . TRP A 265 ? 0.7982 0.9099 0.7166 -0.0449 -0.0121 -0.0734 265 TRP A CH2 
2054 N N   . GLU A 266 ? 0.5526 0.7783 0.5014 -0.1523 -0.0116 0.0295  266 GLU A N   
2055 C CA  . GLU A 266 ? 0.6046 0.8371 0.5366 -0.1754 -0.0136 0.0356  266 GLU A CA  
2056 C C   . GLU A 266 ? 0.6038 0.8141 0.5140 -0.1799 -0.0102 0.0202  266 GLU A C   
2057 O O   . GLU A 266 ? 0.5688 0.7665 0.4696 -0.1708 -0.0040 0.0061  266 GLU A O   
2058 C CB  . GLU A 266 ? 0.5934 0.8477 0.5201 -0.1847 -0.0104 0.0412  266 GLU A CB  
2059 C CG  . GLU A 266 ? 0.5407 0.7989 0.4483 -0.2075 -0.0156 0.0444  266 GLU A CG  
2060 C CD  . GLU A 266 ? 0.6739 0.9513 0.5813 -0.2190 -0.0178 0.0521  266 GLU A CD  
2061 O OE1 . GLU A 266 ? 0.5560 0.8563 0.4870 -0.2130 -0.0180 0.0652  266 GLU A OE1 
2062 O OE2 . GLU A 266 ? 0.6497 0.9195 0.5357 -0.2337 -0.0204 0.0450  266 GLU A OE2 
2063 N N   . THR A 267 ? 0.5297 0.7383 0.4325 -0.1934 -0.0139 0.0241  267 THR A N   
2064 C CA  . THR A 267 ? 0.6336 0.8263 0.5214 -0.1967 -0.0102 0.0113  267 THR A CA  
2065 C C   . THR A 267 ? 0.5304 0.7325 0.3964 -0.2129 -0.0079 0.0094  267 THR A C   
2066 O O   . THR A 267 ? 0.5793 0.7984 0.4422 -0.2244 -0.0122 0.0216  267 THR A O   
2067 C CB  . THR A 267 ? 0.5728 0.7567 0.4751 -0.1954 -0.0157 0.0167  267 THR A CB  
2068 O OG1 . THR A 267 ? 0.5411 0.7129 0.4645 -0.1798 -0.0216 0.0173  267 THR A OG1 
2069 C CG2 . THR A 267 ? 0.5029 0.6730 0.3963 -0.1963 -0.0116 0.0039  267 THR A CG2 
2070 N N   . ARG A 268 ? 0.5513 0.7414 0.4016 -0.2128 -0.0023 -0.0065 268 ARG A N   
2071 C CA  . ARG A 268 ? 0.6245 0.8175 0.4535 -0.2244 -0.0006 -0.0142 268 ARG A CA  
2072 C C   . ARG A 268 ? 0.6281 0.8108 0.4515 -0.2215 0.0051  -0.0267 268 ARG A C   
2073 O O   . ARG A 268 ? 0.5868 0.7532 0.4163 -0.2118 0.0072  -0.0354 268 ARG A O   
2074 C CB  . ARG A 268 ? 0.6191 0.8064 0.4388 -0.2273 -0.0016 -0.0210 268 ARG A CB  
2075 C CG  . ARG A 268 ? 0.6482 0.8518 0.4773 -0.2318 -0.0072 -0.0064 268 ARG A CG  
2076 C CD  . ARG A 268 ? 0.7419 0.9419 0.5650 -0.2386 -0.0101 -0.0094 268 ARG A CD  
2077 N NE  . ARG A 268 ? 0.6764 0.8976 0.5141 -0.2435 -0.0153 0.0075  268 ARG A NE  
2078 C CZ  . ARG A 268 ? 0.6796 0.9049 0.5213 -0.2504 -0.0188 0.0124  268 ARG A CZ  
2079 N NH1 . ARG A 268 ? 0.7232 0.9290 0.5544 -0.2534 -0.0191 0.0019  268 ARG A NH1 
2080 N NH2 . ARG A 268 ? 0.5784 0.8292 0.4388 -0.2549 -0.0232 0.0306  268 ARG A NH2 
2081 N N   . THR A 269 ? 0.6129 0.8085 0.4250 -0.2295 0.0078  -0.0269 269 THR A N   
2082 C CA  . THR A 269 ? 0.7000 0.8938 0.5090 -0.2265 0.0152  -0.0378 269 THR A CA  
2083 C C   . THR A 269 ? 0.7025 0.8993 0.4864 -0.2312 0.0189  -0.0533 269 THR A C   
2084 O O   . THR A 269 ? 0.6752 0.8863 0.4418 -0.2408 0.0161  -0.0498 269 THR A O   
2085 C CB  . THR A 269 ? 0.6445 0.8567 0.4659 -0.2297 0.0172  -0.0230 269 THR A CB  
2086 O OG1 . THR A 269 ? 0.5677 0.7703 0.4143 -0.2244 0.0104  -0.0114 269 THR A OG1 
2087 C CG2 . THR A 269 ? 0.6319 0.8496 0.4542 -0.2265 0.0265  -0.0326 269 THR A CG2 
2088 N N   . TYR A 270 ? 0.6639 0.8460 0.4459 -0.2237 0.0235  -0.0710 270 TYR A N   
2089 C CA  . TYR A 270 ? 0.7358 0.9154 0.4963 -0.2242 0.0264  -0.0904 270 TYR A CA  
2090 C C   . TYR A 270 ? 0.7986 0.9879 0.5642 -0.2157 0.0378  -0.0997 270 TYR A C   
2091 O O   . TYR A 270 ? 0.7590 0.9379 0.5449 -0.2071 0.0394  -0.1014 270 TYR A O   
2092 C CB  . TYR A 270 ? 0.7396 0.8906 0.4971 -0.2221 0.0192  -0.1031 270 TYR A CB  
2093 C CG  . TYR A 270 ? 0.7317 0.8787 0.4888 -0.2309 0.0089  -0.0915 270 TYR A CG  
2094 C CD1 . TYR A 270 ? 0.7267 0.8770 0.4656 -0.2423 0.0010  -0.0936 270 TYR A CD1 
2095 C CD2 . TYR A 270 ? 0.6172 0.7593 0.3921 -0.2274 0.0068  -0.0789 270 TYR A CD2 
2096 C CE1 . TYR A 270 ? 0.7093 0.8605 0.4535 -0.2512 -0.0089 -0.0803 270 TYR A CE1 
2097 C CE2 . TYR A 270 ? 0.6199 0.7652 0.3980 -0.2339 -0.0001 -0.0670 270 TYR A CE2 
2098 C CZ  . TYR A 270 ? 0.7021 0.8530 0.4677 -0.2464 -0.0080 -0.0662 270 TYR A CZ  
2099 O OH  . TYR A 270 ? 0.6286 0.7872 0.4030 -0.2536 -0.0154 -0.0516 270 TYR A OH  
2100 N N   . GLU A 271 ? 0.8033 1.0158 0.5506 -0.2179 0.0456  -0.1051 271 GLU A N   
2101 C CA  . GLU A 271 ? 0.7745 1.0052 0.5258 -0.2090 0.0593  -0.1143 271 GLU A CA  
2102 C C   . GLU A 271 ? 0.7445 0.9653 0.4717 -0.2018 0.0620  -0.1435 271 GLU A C   
2103 O O   . GLU A 271 ? 0.8846 1.1089 0.5812 -0.2082 0.0585  -0.1514 271 GLU A O   
2104 C CB  . GLU A 271 ? 0.8363 1.1082 0.5852 -0.2159 0.0683  -0.0961 271 GLU A CB  
2105 C CG  . GLU A 271 ? 0.7830 1.0602 0.5517 -0.2258 0.0603  -0.0665 271 GLU A CG  
2106 C CD  . GLU A 271 ? 0.8189 1.1367 0.5887 -0.2345 0.0672  -0.0441 271 GLU A CD  
2107 O OE1 . GLU A 271 ? 0.8821 1.2289 0.6431 -0.2311 0.0816  -0.0500 271 GLU A OE1 
2108 O OE2 . GLU A 271 ? 0.8166 1.1389 0.5973 -0.2443 0.0582  -0.0196 271 GLU A OE2 
2109 N N   . PHE A 272 ? 0.7438 0.9506 0.4853 -0.1881 0.0659  -0.1599 272 PHE A N   
2110 C CA  . PHE A 272 ? 0.8684 1.0594 0.5924 -0.1778 0.0667  -0.1902 272 PHE A CA  
2111 C C   . PHE A 272 ? 0.8938 1.0907 0.6421 -0.1605 0.0778  -0.2011 272 PHE A C   
2112 O O   . PHE A 272 ? 0.8760 1.0973 0.6499 -0.1591 0.0862  -0.1842 272 PHE A O   
2113 C CB  . PHE A 272 ? 0.8359 0.9833 0.5543 -0.1822 0.0485  -0.1987 272 PHE A CB  
2114 C CG  . PHE A 272 ? 0.8054 0.9285 0.5529 -0.1794 0.0412  -0.1893 272 PHE A CG  
2115 C CD1 . PHE A 272 ? 0.7884 0.9109 0.5468 -0.1888 0.0352  -0.1658 272 PHE A CD1 
2116 C CD2 . PHE A 272 ? 0.9050 1.0066 0.6679 -0.1661 0.0398  -0.2046 272 PHE A CD2 
2117 C CE1 . PHE A 272 ? 0.8519 0.9544 0.6310 -0.1854 0.0289  -0.1585 272 PHE A CE1 
2118 C CE2 . PHE A 272 ? 0.8344 0.9156 0.6204 -0.1645 0.0318  -0.1942 272 PHE A CE2 
2119 C CZ  . PHE A 272 ? 0.8203 0.9028 0.6118 -0.1743 0.0268  -0.1717 272 PHE A CZ  
2120 N N   . THR A 273 ? 0.9437 1.1176 0.6872 -0.1474 0.0759  -0.2288 273 THR A N   
2121 C CA  . THR A 273 ? 0.9037 1.0850 0.6716 -0.1282 0.0864  -0.2418 273 THR A CA  
2122 C C   . THR A 273 ? 0.8662 1.0006 0.6459 -0.1190 0.0722  -0.2588 273 THR A C   
2123 O O   . THR A 273 ? 0.9100 1.0103 0.6699 -0.1240 0.0578  -0.2711 273 THR A O   
2124 C CB  . THR A 273 ? 0.9162 1.1323 0.6651 -0.1156 0.1051  -0.2621 273 THR A CB  
2125 O OG1 . THR A 273 ? 0.8963 1.1614 0.6398 -0.1255 0.1187  -0.2396 273 THR A OG1 
2126 C CG2 . THR A 273 ? 0.9208 1.1450 0.6981 -0.0924 0.1163  -0.2787 273 THR A CG2 
2127 N N   . LEU A 274 ? 0.8853 1.0189 0.7001 -0.1066 0.0743  -0.2571 274 LEU A N   
2128 C CA  . LEU A 274 ? 0.9663 1.0579 0.7973 -0.0969 0.0602  -0.2698 274 LEU A CA  
2129 C C   . LEU A 274 ? 0.8798 0.9602 0.7008 -0.0786 0.0633  -0.3048 274 LEU A C   
2130 O O   . LEU A 274 ? 1.0612 1.1747 0.8676 -0.0690 0.0808  -0.3197 274 LEU A O   
2131 C CB  . LEU A 274 ? 0.9284 1.0252 0.8004 -0.0888 0.0602  -0.2568 274 LEU A CB  
2132 C CG  . LEU A 274 ? 0.8468 0.9509 0.7309 -0.1032 0.0553  -0.2265 274 LEU A CG  
2133 C CD1 . LEU A 274 ? 0.8428 0.9530 0.7662 -0.0937 0.0537  -0.2180 274 LEU A CD1 
2134 C CD2 . LEU A 274 ? 0.8619 0.9309 0.7308 -0.1173 0.0378  -0.2165 274 LEU A CD2 
2135 N N   . GLN A 275 ? 1.0451 1.0785 0.8744 -0.0731 0.0455  -0.3176 275 GLN A N   
2136 C CA  . GLN A 275 ? 1.1768 1.1883 0.9996 -0.0541 0.0434  -0.3536 275 GLN A CA  
2137 C C   . GLN A 275 ? 1.1963 1.2086 1.0597 -0.0298 0.0478  -0.3631 275 GLN A C   
2138 O O   . GLN A 275 ? 1.1966 1.2509 1.0707 -0.0127 0.0694  -0.3722 275 GLN A O   
2139 C CB  . GLN A 275 ? 1.3118 1.2665 1.1210 -0.0644 0.0169  -0.3619 275 GLN A CB  
2140 C CG  . GLN A 275 ? 1.2012 1.1551 0.9769 -0.0896 0.0096  -0.3491 275 GLN A CG  
2141 C CD  . GLN A 275 ? 1.3078 1.2089 1.0746 -0.1009 -0.0176 -0.3561 275 GLN A CD  
2142 O OE1 . GLN A 275 ? 1.3277 1.1986 1.1176 -0.1078 -0.0343 -0.3395 275 GLN A OE1 
2143 N NE2 . GLN A 275 ? 1.3246 1.2153 1.0574 -0.1041 -0.0235 -0.3793 275 GLN A NE2 
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