data_8XT5
# 
_entry.id   8XT5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8XT5         pdb_00008xt5 10.2210/pdb8xt5/pdb 
WWPDB D_1300043731 ?            ?                   
# 
_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       2025-01-22 
# 
_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                        8XT5 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              54503624@qq.com 
_pdbx_contact_author.name_first         Qin 
_pdbx_contact_author.name_last          Wang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2852-619X 
# 
_audit_author.name               'Wang, Q.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_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                     'Structure of the E3 ubiquitin ligase RGLG5 VWA domain' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Wang, Q.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   ? 
# 
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 'E3 ubiquitin-protein ligase RGLG5' 31997.697 1   2.3.2.27 ? 'VWA domain' ? 
2 non-polymer syn 'CHLORIDE ION'                      35.453    2   ?        ? ?            ? 
3 water       nat water                               18.015    229 ?        ? ?            ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'RING domain ligase 5' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GTSSMADIGSRKYSRIADNYRSIDEVTAALSHAGLESSNLIVGIDVTKSNEWTGARSFGRKSLHFIGTTPNPYQQAISII
GKTLSVFDEDNLIPCYGFGDATTHDQDVFSFNPNDTYCNGFEEVLMCYREIVPQLRLSGPTSFAPIIERAMTIVEESGGQ
YHVLLIIADGQVTRSVDTDNGGFSPQEQQTIDAIVRASEYPLSIVLVGVGDGPWDTMRQFDDNIPARAFDNFQFVNFTDI
MSKNIDPARKEAEFALSALMEIPSQYKATLELGLLGQRTGHCPDRIALPPP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GTSSMADIGSRKYSRIADNYRSIDEVTAALSHAGLESSNLIVGIDVTKSNEWTGARSFGRKSLHFIGTTPNPYQQAISII
GKTLSVFDEDNLIPCYGFGDATTHDQDVFSFNPNDTYCNGFEEVLMCYREIVPQLRLSGPTSFAPIIERAMTIVEESGGQ
YHVLLIIADGQVTRSVDTDNGGFSPQEQQTIDAIVRASEYPLSIVLVGVGDGPWDTMRQFDDNIPARAFDNFQFVNFTDI
MSKNIDPARKEAEFALSALMEIPSQYKATLELGLLGQRTGHCPDRIALPPP
;
_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 'CHLORIDE ION' CL  
3 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   THR n 
1 3   SER n 
1 4   SER n 
1 5   MET n 
1 6   ALA n 
1 7   ASP n 
1 8   ILE n 
1 9   GLY n 
1 10  SER n 
1 11  ARG n 
1 12  LYS n 
1 13  TYR n 
1 14  SER n 
1 15  ARG n 
1 16  ILE n 
1 17  ALA n 
1 18  ASP n 
1 19  ASN n 
1 20  TYR n 
1 21  ARG n 
1 22  SER n 
1 23  ILE n 
1 24  ASP n 
1 25  GLU n 
1 26  VAL n 
1 27  THR n 
1 28  ALA n 
1 29  ALA n 
1 30  LEU n 
1 31  SER n 
1 32  HIS n 
1 33  ALA n 
1 34  GLY n 
1 35  LEU n 
1 36  GLU n 
1 37  SER n 
1 38  SER n 
1 39  ASN n 
1 40  LEU n 
1 41  ILE n 
1 42  VAL n 
1 43  GLY n 
1 44  ILE n 
1 45  ASP n 
1 46  VAL n 
1 47  THR n 
1 48  LYS n 
1 49  SER n 
1 50  ASN n 
1 51  GLU n 
1 52  TRP n 
1 53  THR n 
1 54  GLY n 
1 55  ALA n 
1 56  ARG n 
1 57  SER n 
1 58  PHE n 
1 59  GLY n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  LEU n 
1 64  HIS n 
1 65  PHE n 
1 66  ILE n 
1 67  GLY n 
1 68  THR n 
1 69  THR n 
1 70  PRO n 
1 71  ASN n 
1 72  PRO n 
1 73  TYR n 
1 74  GLN n 
1 75  GLN n 
1 76  ALA n 
1 77  ILE n 
1 78  SER n 
1 79  ILE n 
1 80  ILE n 
1 81  GLY n 
1 82  LYS n 
1 83  THR n 
1 84  LEU n 
1 85  SER n 
1 86  VAL n 
1 87  PHE n 
1 88  ASP n 
1 89  GLU n 
1 90  ASP n 
1 91  ASN n 
1 92  LEU n 
1 93  ILE n 
1 94  PRO n 
1 95  CYS n 
1 96  TYR n 
1 97  GLY n 
1 98  PHE n 
1 99  GLY n 
1 100 ASP n 
1 101 ALA n 
1 102 THR n 
1 103 THR n 
1 104 HIS n 
1 105 ASP n 
1 106 GLN n 
1 107 ASP n 
1 108 VAL n 
1 109 PHE n 
1 110 SER n 
1 111 PHE n 
1 112 ASN n 
1 113 PRO n 
1 114 ASN n 
1 115 ASP n 
1 116 THR n 
1 117 TYR n 
1 118 CYS n 
1 119 ASN n 
1 120 GLY n 
1 121 PHE n 
1 122 GLU n 
1 123 GLU n 
1 124 VAL n 
1 125 LEU n 
1 126 MET n 
1 127 CYS n 
1 128 TYR n 
1 129 ARG n 
1 130 GLU n 
1 131 ILE n 
1 132 VAL n 
1 133 PRO n 
1 134 GLN n 
1 135 LEU n 
1 136 ARG n 
1 137 LEU n 
1 138 SER n 
1 139 GLY n 
1 140 PRO n 
1 141 THR n 
1 142 SER n 
1 143 PHE n 
1 144 ALA n 
1 145 PRO n 
1 146 ILE n 
1 147 ILE n 
1 148 GLU n 
1 149 ARG n 
1 150 ALA n 
1 151 MET n 
1 152 THR n 
1 153 ILE n 
1 154 VAL n 
1 155 GLU n 
1 156 GLU n 
1 157 SER n 
1 158 GLY n 
1 159 GLY n 
1 160 GLN n 
1 161 TYR n 
1 162 HIS n 
1 163 VAL n 
1 164 LEU n 
1 165 LEU n 
1 166 ILE n 
1 167 ILE n 
1 168 ALA n 
1 169 ASP n 
1 170 GLY n 
1 171 GLN n 
1 172 VAL n 
1 173 THR n 
1 174 ARG n 
1 175 SER n 
1 176 VAL n 
1 177 ASP n 
1 178 THR n 
1 179 ASP n 
1 180 ASN n 
1 181 GLY n 
1 182 GLY n 
1 183 PHE n 
1 184 SER n 
1 185 PRO n 
1 186 GLN n 
1 187 GLU n 
1 188 GLN n 
1 189 GLN n 
1 190 THR n 
1 191 ILE n 
1 192 ASP n 
1 193 ALA n 
1 194 ILE n 
1 195 VAL n 
1 196 ARG n 
1 197 ALA n 
1 198 SER n 
1 199 GLU n 
1 200 TYR n 
1 201 PRO n 
1 202 LEU n 
1 203 SER n 
1 204 ILE n 
1 205 VAL n 
1 206 LEU n 
1 207 VAL n 
1 208 GLY n 
1 209 VAL n 
1 210 GLY n 
1 211 ASP n 
1 212 GLY n 
1 213 PRO n 
1 214 TRP n 
1 215 ASP n 
1 216 THR n 
1 217 MET n 
1 218 ARG n 
1 219 GLN n 
1 220 PHE n 
1 221 ASP n 
1 222 ASP n 
1 223 ASN n 
1 224 ILE n 
1 225 PRO n 
1 226 ALA n 
1 227 ARG n 
1 228 ALA n 
1 229 PHE n 
1 230 ASP n 
1 231 ASN n 
1 232 PHE n 
1 233 GLN n 
1 234 PHE n 
1 235 VAL n 
1 236 ASN n 
1 237 PHE n 
1 238 THR n 
1 239 ASP n 
1 240 ILE n 
1 241 MET n 
1 242 SER n 
1 243 LYS n 
1 244 ASN n 
1 245 ILE n 
1 246 ASP n 
1 247 PRO n 
1 248 ALA n 
1 249 ARG n 
1 250 LYS n 
1 251 GLU n 
1 252 ALA n 
1 253 GLU n 
1 254 PHE n 
1 255 ALA n 
1 256 LEU n 
1 257 SER n 
1 258 ALA n 
1 259 LEU n 
1 260 MET n 
1 261 GLU n 
1 262 ILE n 
1 263 PRO n 
1 264 SER n 
1 265 GLN n 
1 266 TYR n 
1 267 LYS n 
1 268 ALA n 
1 269 THR n 
1 270 LEU n 
1 271 GLU n 
1 272 LEU n 
1 273 GLY n 
1 274 LEU n 
1 275 LEU n 
1 276 GLY n 
1 277 GLN n 
1 278 ARG n 
1 279 THR n 
1 280 GLY n 
1 281 HIS n 
1 282 CYS n 
1 283 PRO n 
1 284 ASP n 
1 285 ARG n 
1 286 ILE n 
1 287 ALA n 
1 288 LEU n 
1 289 PRO n 
1 290 PRO n 
1 291 PRO 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                   291 
_entity_src_gen.gene_src_common_name               'Mouse-ear cress' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'RGLG5, At1g67800' 
_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      'Arabidopsis thaliana' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3702 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
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 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   55  ?   ?   ?   A . n 
A 1 2   THR 2   56  ?   ?   ?   A . n 
A 1 3   SER 3   57  ?   ?   ?   A . n 
A 1 4   SER 4   58  ?   ?   ?   A . n 
A 1 5   MET 5   59  ?   ?   ?   A . n 
A 1 6   ALA 6   60  ?   ?   ?   A . n 
A 1 7   ASP 7   61  ?   ?   ?   A . n 
A 1 8   ILE 8   62  ?   ?   ?   A . n 
A 1 9   GLY 9   63  ?   ?   ?   A . n 
A 1 10  SER 10  64  ?   ?   ?   A . n 
A 1 11  ARG 11  65  ?   ?   ?   A . n 
A 1 12  LYS 12  66  ?   ?   ?   A . n 
A 1 13  TYR 13  67  ?   ?   ?   A . n 
A 1 14  SER 14  68  ?   ?   ?   A . n 
A 1 15  ARG 15  69  ?   ?   ?   A . n 
A 1 16  ILE 16  70  ?   ?   ?   A . n 
A 1 17  ALA 17  71  ?   ?   ?   A . n 
A 1 18  ASP 18  72  ?   ?   ?   A . n 
A 1 19  ASN 19  73  ?   ?   ?   A . n 
A 1 20  TYR 20  74  74  TYR TYR A . n 
A 1 21  ARG 21  75  75  ARG ARG A . n 
A 1 22  SER 22  76  76  SER SER A . n 
A 1 23  ILE 23  77  77  ILE ILE A . n 
A 1 24  ASP 24  78  78  ASP ASP A . n 
A 1 25  GLU 25  79  79  GLU GLU A . n 
A 1 26  VAL 26  80  80  VAL VAL A . n 
A 1 27  THR 27  81  81  THR THR A . n 
A 1 28  ALA 28  82  82  ALA ALA A . n 
A 1 29  ALA 29  83  83  ALA ALA A . n 
A 1 30  LEU 30  84  84  LEU LEU A . n 
A 1 31  SER 31  85  85  SER SER A . n 
A 1 32  HIS 32  86  86  HIS HIS A . n 
A 1 33  ALA 33  87  87  ALA ALA A . n 
A 1 34  GLY 34  88  88  GLY GLY A . n 
A 1 35  LEU 35  89  89  LEU LEU A . n 
A 1 36  GLU 36  90  90  GLU GLU A . n 
A 1 37  SER 37  91  91  SER SER A . n 
A 1 38  SER 38  92  92  SER SER A . n 
A 1 39  ASN 39  93  93  ASN ASN A . n 
A 1 40  LEU 40  94  94  LEU LEU A . n 
A 1 41  ILE 41  95  95  ILE ILE A . n 
A 1 42  VAL 42  96  96  VAL VAL A . n 
A 1 43  GLY 43  97  97  GLY GLY A . n 
A 1 44  ILE 44  98  98  ILE ILE A . n 
A 1 45  ASP 45  99  99  ASP ASP A . n 
A 1 46  VAL 46  100 100 VAL VAL A . n 
A 1 47  THR 47  101 101 THR THR A . n 
A 1 48  LYS 48  102 102 LYS LYS A . n 
A 1 49  SER 49  103 103 SER SER A . n 
A 1 50  ASN 50  104 104 ASN ASN A . n 
A 1 51  GLU 51  105 105 GLU GLU A . n 
A 1 52  TRP 52  106 106 TRP TRP A . n 
A 1 53  THR 53  107 107 THR THR A . n 
A 1 54  GLY 54  108 108 GLY GLY A . n 
A 1 55  ALA 55  109 109 ALA ALA A . n 
A 1 56  ARG 56  110 110 ARG ARG A . n 
A 1 57  SER 57  111 111 SER SER A . n 
A 1 58  PHE 58  112 112 PHE PHE A . n 
A 1 59  GLY 59  113 113 GLY GLY A . n 
A 1 60  ARG 60  114 114 ARG ARG A . n 
A 1 61  LYS 61  115 115 LYS LYS A . n 
A 1 62  SER 62  116 116 SER SER A . n 
A 1 63  LEU 63  117 117 LEU LEU A . n 
A 1 64  HIS 64  118 118 HIS HIS A . n 
A 1 65  PHE 65  119 119 PHE PHE A . n 
A 1 66  ILE 66  120 120 ILE ILE A . n 
A 1 67  GLY 67  121 121 GLY GLY A . n 
A 1 68  THR 68  122 122 THR THR A . n 
A 1 69  THR 69  123 123 THR THR A . n 
A 1 70  PRO 70  124 124 PRO PRO A . n 
A 1 71  ASN 71  125 125 ASN ASN A . n 
A 1 72  PRO 72  126 126 PRO PRO A . n 
A 1 73  TYR 73  127 127 TYR TYR A . n 
A 1 74  GLN 74  128 128 GLN GLN A . n 
A 1 75  GLN 75  129 129 GLN GLN A . n 
A 1 76  ALA 76  130 130 ALA ALA A . n 
A 1 77  ILE 77  131 131 ILE ILE A . n 
A 1 78  SER 78  132 132 SER SER A . n 
A 1 79  ILE 79  133 133 ILE ILE A . n 
A 1 80  ILE 80  134 134 ILE ILE A . n 
A 1 81  GLY 81  135 135 GLY GLY A . n 
A 1 82  LYS 82  136 136 LYS LYS A . n 
A 1 83  THR 83  137 137 THR THR A . n 
A 1 84  LEU 84  138 138 LEU LEU A . n 
A 1 85  SER 85  139 139 SER SER A . n 
A 1 86  VAL 86  140 140 VAL VAL A . n 
A 1 87  PHE 87  141 141 PHE PHE A . n 
A 1 88  ASP 88  142 142 ASP ASP A . n 
A 1 89  GLU 89  143 143 GLU GLU A . n 
A 1 90  ASP 90  144 144 ASP ASP A . n 
A 1 91  ASN 91  145 145 ASN ASN A . n 
A 1 92  LEU 92  146 146 LEU LEU A . n 
A 1 93  ILE 93  147 147 ILE ILE A . n 
A 1 94  PRO 94  148 148 PRO PRO A . n 
A 1 95  CYS 95  149 149 CYS CYS A . n 
A 1 96  TYR 96  150 150 TYR TYR A . n 
A 1 97  GLY 97  151 151 GLY GLY A . n 
A 1 98  PHE 98  152 152 PHE PHE A . n 
A 1 99  GLY 99  153 153 GLY GLY A . n 
A 1 100 ASP 100 154 154 ASP ASP A . n 
A 1 101 ALA 101 155 155 ALA ALA A . n 
A 1 102 THR 102 156 156 THR THR A . n 
A 1 103 THR 103 157 157 THR THR A . n 
A 1 104 HIS 104 158 158 HIS HIS A . n 
A 1 105 ASP 105 159 159 ASP ASP A . n 
A 1 106 GLN 106 160 160 GLN GLN A . n 
A 1 107 ASP 107 161 161 ASP ASP A . n 
A 1 108 VAL 108 162 162 VAL VAL A . n 
A 1 109 PHE 109 163 163 PHE PHE A . n 
A 1 110 SER 110 164 164 SER SER A . n 
A 1 111 PHE 111 165 165 PHE PHE A . n 
A 1 112 ASN 112 166 166 ASN ASN A . n 
A 1 113 PRO 113 167 167 PRO PRO A . n 
A 1 114 ASN 114 168 168 ASN ASN A . n 
A 1 115 ASP 115 169 169 ASP ASP A . n 
A 1 116 THR 116 170 170 THR THR A . n 
A 1 117 TYR 117 171 171 TYR TYR A . n 
A 1 118 CYS 118 172 172 CYS CYS A . n 
A 1 119 ASN 119 173 173 ASN ASN A . n 
A 1 120 GLY 120 174 174 GLY GLY A . n 
A 1 121 PHE 121 175 175 PHE PHE A . n 
A 1 122 GLU 122 176 176 GLU GLU A . n 
A 1 123 GLU 123 177 177 GLU GLU A . n 
A 1 124 VAL 124 178 178 VAL VAL A . n 
A 1 125 LEU 125 179 179 LEU LEU A . n 
A 1 126 MET 126 180 180 MET MET A . n 
A 1 127 CYS 127 181 181 CYS CYS A . n 
A 1 128 TYR 128 182 182 TYR TYR A . n 
A 1 129 ARG 129 183 183 ARG ARG A . n 
A 1 130 GLU 130 184 184 GLU GLU A . n 
A 1 131 ILE 131 185 185 ILE ILE A . n 
A 1 132 VAL 132 186 186 VAL VAL A . n 
A 1 133 PRO 133 187 187 PRO PRO A . n 
A 1 134 GLN 134 188 188 GLN GLN A . n 
A 1 135 LEU 135 189 189 LEU LEU A . n 
A 1 136 ARG 136 190 190 ARG ARG A . n 
A 1 137 LEU 137 191 191 LEU LEU A . n 
A 1 138 SER 138 192 192 SER SER A . n 
A 1 139 GLY 139 193 193 GLY GLY A . n 
A 1 140 PRO 140 194 194 PRO PRO A . n 
A 1 141 THR 141 195 195 THR THR A . n 
A 1 142 SER 142 196 196 SER SER A . n 
A 1 143 PHE 143 197 197 PHE PHE A . n 
A 1 144 ALA 144 198 198 ALA ALA A . n 
A 1 145 PRO 145 199 199 PRO PRO A . n 
A 1 146 ILE 146 200 200 ILE ILE A . n 
A 1 147 ILE 147 201 201 ILE ILE A . n 
A 1 148 GLU 148 202 202 GLU GLU A . n 
A 1 149 ARG 149 203 203 ARG ARG A . n 
A 1 150 ALA 150 204 204 ALA ALA A . n 
A 1 151 MET 151 205 205 MET MET A . n 
A 1 152 THR 152 206 206 THR THR A . n 
A 1 153 ILE 153 207 207 ILE ILE A . n 
A 1 154 VAL 154 208 208 VAL VAL A . n 
A 1 155 GLU 155 209 209 GLU GLU A . n 
A 1 156 GLU 156 210 210 GLU GLU A . n 
A 1 157 SER 157 211 211 SER SER A . n 
A 1 158 GLY 158 212 212 GLY GLY A . n 
A 1 159 GLY 159 213 213 GLY GLY A . n 
A 1 160 GLN 160 214 214 GLN GLN A . n 
A 1 161 TYR 161 215 215 TYR TYR A . n 
A 1 162 HIS 162 216 216 HIS HIS A . n 
A 1 163 VAL 163 217 217 VAL VAL A . n 
A 1 164 LEU 164 218 218 LEU LEU A . n 
A 1 165 LEU 165 219 219 LEU LEU A . n 
A 1 166 ILE 166 220 220 ILE ILE A . n 
A 1 167 ILE 167 221 221 ILE ILE A . n 
A 1 168 ALA 168 222 222 ALA ALA A . n 
A 1 169 ASP 169 223 223 ASP ASP A . n 
A 1 170 GLY 170 224 224 GLY GLY A . n 
A 1 171 GLN 171 225 225 GLN GLN A . n 
A 1 172 VAL 172 226 226 VAL VAL A . n 
A 1 173 THR 173 227 227 THR THR A . n 
A 1 174 ARG 174 228 228 ARG ARG A . n 
A 1 175 SER 175 229 229 SER SER A . n 
A 1 176 VAL 176 230 230 VAL VAL A . n 
A 1 177 ASP 177 231 231 ASP ASP A . n 
A 1 178 THR 178 232 232 THR THR A . n 
A 1 179 ASP 179 233 233 ASP ASP A . n 
A 1 180 ASN 180 234 234 ASN ASN A . n 
A 1 181 GLY 181 235 235 GLY GLY A . n 
A 1 182 GLY 182 236 236 GLY GLY A . n 
A 1 183 PHE 183 237 237 PHE PHE A . n 
A 1 184 SER 184 238 238 SER SER A . n 
A 1 185 PRO 185 239 239 PRO PRO A . n 
A 1 186 GLN 186 240 240 GLN GLN A . n 
A 1 187 GLU 187 241 241 GLU GLU A . n 
A 1 188 GLN 188 242 242 GLN GLN A . n 
A 1 189 GLN 189 243 243 GLN GLN A . n 
A 1 190 THR 190 244 244 THR THR A . n 
A 1 191 ILE 191 245 245 ILE ILE A . n 
A 1 192 ASP 192 246 246 ASP ASP A . n 
A 1 193 ALA 193 247 247 ALA ALA A . n 
A 1 194 ILE 194 248 248 ILE ILE A . n 
A 1 195 VAL 195 249 249 VAL VAL A . n 
A 1 196 ARG 196 250 250 ARG ARG A . n 
A 1 197 ALA 197 251 251 ALA ALA A . n 
A 1 198 SER 198 252 252 SER SER A . n 
A 1 199 GLU 199 253 253 GLU GLU A . n 
A 1 200 TYR 200 254 254 TYR TYR A . n 
A 1 201 PRO 201 255 255 PRO PRO A . n 
A 1 202 LEU 202 256 256 LEU LEU A . n 
A 1 203 SER 203 257 257 SER SER A . n 
A 1 204 ILE 204 258 258 ILE ILE A . n 
A 1 205 VAL 205 259 259 VAL VAL A . n 
A 1 206 LEU 206 260 260 LEU LEU A . n 
A 1 207 VAL 207 261 261 VAL VAL A . n 
A 1 208 GLY 208 262 262 GLY GLY A . n 
A 1 209 VAL 209 263 263 VAL VAL A . n 
A 1 210 GLY 210 264 264 GLY GLY A . n 
A 1 211 ASP 211 265 265 ASP ASP A . n 
A 1 212 GLY 212 266 266 GLY GLY A . n 
A 1 213 PRO 213 267 267 PRO PRO A . n 
A 1 214 TRP 214 268 268 TRP TRP A . n 
A 1 215 ASP 215 269 269 ASP ASP A . n 
A 1 216 THR 216 270 270 THR THR A . n 
A 1 217 MET 217 271 271 MET MET A . n 
A 1 218 ARG 218 272 272 ARG ARG A . n 
A 1 219 GLN 219 273 273 GLN GLN A . n 
A 1 220 PHE 220 274 274 PHE PHE A . n 
A 1 221 ASP 221 275 275 ASP ASP A . n 
A 1 222 ASP 222 276 276 ASP ASP A . n 
A 1 223 ASN 223 277 277 ASN ASN A . n 
A 1 224 ILE 224 278 278 ILE ILE A . n 
A 1 225 PRO 225 279 279 PRO PRO A . n 
A 1 226 ALA 226 280 280 ALA ALA A . n 
A 1 227 ARG 227 281 281 ARG ARG A . n 
A 1 228 ALA 228 282 282 ALA ALA A . n 
A 1 229 PHE 229 283 283 PHE PHE A . n 
A 1 230 ASP 230 284 284 ASP ASP A . n 
A 1 231 ASN 231 285 285 ASN ASN A . n 
A 1 232 PHE 232 286 286 PHE PHE A . n 
A 1 233 GLN 233 287 287 GLN GLN A . n 
A 1 234 PHE 234 288 288 PHE PHE A . n 
A 1 235 VAL 235 289 289 VAL VAL A . n 
A 1 236 ASN 236 290 290 ASN ASN A . n 
A 1 237 PHE 237 291 291 PHE PHE A . n 
A 1 238 THR 238 292 292 THR THR A . n 
A 1 239 ASP 239 293 293 ASP ASP A . n 
A 1 240 ILE 240 294 294 ILE ILE A . n 
A 1 241 MET 241 295 295 MET MET A . n 
A 1 242 SER 242 296 296 SER SER A . n 
A 1 243 LYS 243 297 297 LYS LYS A . n 
A 1 244 ASN 244 298 298 ASN ASN A . n 
A 1 245 ILE 245 299 299 ILE ILE A . n 
A 1 246 ASP 246 300 300 ASP ASP A . n 
A 1 247 PRO 247 301 301 PRO PRO A . n 
A 1 248 ALA 248 302 302 ALA ALA A . n 
A 1 249 ARG 249 303 303 ARG ARG A . n 
A 1 250 LYS 250 304 304 LYS LYS A . n 
A 1 251 GLU 251 305 305 GLU GLU A . n 
A 1 252 ALA 252 306 306 ALA ALA A . n 
A 1 253 GLU 253 307 307 GLU GLU A . n 
A 1 254 PHE 254 308 308 PHE PHE A . n 
A 1 255 ALA 255 309 309 ALA ALA A . n 
A 1 256 LEU 256 310 310 LEU LEU A . n 
A 1 257 SER 257 311 311 SER SER A . n 
A 1 258 ALA 258 312 312 ALA ALA A . n 
A 1 259 LEU 259 313 313 LEU LEU A . n 
A 1 260 MET 260 314 314 MET MET A . n 
A 1 261 GLU 261 315 315 GLU GLU A . n 
A 1 262 ILE 262 316 316 ILE ILE A . n 
A 1 263 PRO 263 317 317 PRO PRO A . n 
A 1 264 SER 264 318 318 SER SER A . n 
A 1 265 GLN 265 319 319 GLN GLN A . n 
A 1 266 TYR 266 320 320 TYR TYR A . n 
A 1 267 LYS 267 321 321 LYS LYS A . n 
A 1 268 ALA 268 322 322 ALA ALA A . n 
A 1 269 THR 269 323 323 THR THR A . n 
A 1 270 LEU 270 324 324 LEU LEU A . n 
A 1 271 GLU 271 325 325 GLU GLU A . n 
A 1 272 LEU 272 326 326 LEU LEU A . n 
A 1 273 GLY 273 327 327 GLY GLY A . n 
A 1 274 LEU 274 328 328 LEU LEU A . n 
A 1 275 LEU 275 329 329 LEU LEU A . n 
A 1 276 GLY 276 330 330 GLY GLY A . n 
A 1 277 GLN 277 331 331 GLN GLN A . n 
A 1 278 ARG 278 332 332 ARG ARG A . n 
A 1 279 THR 279 333 333 THR THR A . n 
A 1 280 GLY 280 334 334 GLY GLY A . n 
A 1 281 HIS 281 335 335 HIS HIS A . n 
A 1 282 CYS 282 336 336 CYS CYS A . n 
A 1 283 PRO 283 337 337 PRO PRO A . n 
A 1 284 ASP 284 338 338 ASP ASP A . n 
A 1 285 ARG 285 339 339 ARG ARG A . n 
A 1 286 ILE 286 340 340 ILE ILE A . n 
A 1 287 ALA 287 341 341 ALA ALA A . n 
A 1 288 LEU 288 342 342 LEU LEU A . n 
A 1 289 PRO 289 343 343 PRO PRO A . n 
A 1 290 PRO 290 344 344 PRO PRO A . n 
A 1 291 PRO 291 345 345 PRO PRO A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CL  1   401 1   CL  CL  A . 
C 2 CL  1   402 2   CL  CL  A . 
D 3 HOH 1   501 193 HOH HOH A . 
D 3 HOH 2   502 162 HOH HOH A . 
D 3 HOH 3   503 3   HOH HOH A . 
D 3 HOH 4   504 178 HOH HOH A . 
D 3 HOH 5   505 151 HOH HOH A . 
D 3 HOH 6   506 207 HOH HOH A . 
D 3 HOH 7   507 133 HOH HOH A . 
D 3 HOH 8   508 218 HOH HOH A . 
D 3 HOH 9   509 90  HOH HOH A . 
D 3 HOH 10  510 88  HOH HOH A . 
D 3 HOH 11  511 58  HOH HOH A . 
D 3 HOH 12  512 174 HOH HOH A . 
D 3 HOH 13  513 197 HOH HOH A . 
D 3 HOH 14  514 52  HOH HOH A . 
D 3 HOH 15  515 110 HOH HOH A . 
D 3 HOH 16  516 220 HOH HOH A . 
D 3 HOH 17  517 12  HOH HOH A . 
D 3 HOH 18  518 18  HOH HOH A . 
D 3 HOH 19  519 138 HOH HOH A . 
D 3 HOH 20  520 208 HOH HOH A . 
D 3 HOH 21  521 108 HOH HOH A . 
D 3 HOH 22  522 27  HOH HOH A . 
D 3 HOH 23  523 22  HOH HOH A . 
D 3 HOH 24  524 49  HOH HOH A . 
D 3 HOH 25  525 63  HOH HOH A . 
D 3 HOH 26  526 78  HOH HOH A . 
D 3 HOH 27  527 156 HOH HOH A . 
D 3 HOH 28  528 131 HOH HOH A . 
D 3 HOH 29  529 91  HOH HOH A . 
D 3 HOH 30  530 87  HOH HOH A . 
D 3 HOH 31  531 32  HOH HOH A . 
D 3 HOH 32  532 219 HOH HOH A . 
D 3 HOH 33  533 204 HOH HOH A . 
D 3 HOH 34  534 185 HOH HOH A . 
D 3 HOH 35  535 68  HOH HOH A . 
D 3 HOH 36  536 29  HOH HOH A . 
D 3 HOH 37  537 129 HOH HOH A . 
D 3 HOH 38  538 106 HOH HOH A . 
D 3 HOH 39  539 26  HOH HOH A . 
D 3 HOH 40  540 62  HOH HOH A . 
D 3 HOH 41  541 97  HOH HOH A . 
D 3 HOH 42  542 48  HOH HOH A . 
D 3 HOH 43  543 46  HOH HOH A . 
D 3 HOH 44  544 69  HOH HOH A . 
D 3 HOH 45  545 210 HOH HOH A . 
D 3 HOH 46  546 31  HOH HOH A . 
D 3 HOH 47  547 179 HOH HOH A . 
D 3 HOH 48  548 122 HOH HOH A . 
D 3 HOH 49  549 100 HOH HOH A . 
D 3 HOH 50  550 126 HOH HOH A . 
D 3 HOH 51  551 200 HOH HOH A . 
D 3 HOH 52  552 19  HOH HOH A . 
D 3 HOH 53  553 64  HOH HOH A . 
D 3 HOH 54  554 37  HOH HOH A . 
D 3 HOH 55  555 123 HOH HOH A . 
D 3 HOH 56  556 172 HOH HOH A . 
D 3 HOH 57  557 59  HOH HOH A . 
D 3 HOH 58  558 60  HOH HOH A . 
D 3 HOH 59  559 195 HOH HOH A . 
D 3 HOH 60  560 134 HOH HOH A . 
D 3 HOH 61  561 5   HOH HOH A . 
D 3 HOH 62  562 41  HOH HOH A . 
D 3 HOH 63  563 67  HOH HOH A . 
D 3 HOH 64  564 30  HOH HOH A . 
D 3 HOH 65  565 13  HOH HOH A . 
D 3 HOH 66  566 16  HOH HOH A . 
D 3 HOH 67  567 9   HOH HOH A . 
D 3 HOH 68  568 216 HOH HOH A . 
D 3 HOH 69  569 14  HOH HOH A . 
D 3 HOH 70  570 4   HOH HOH A . 
D 3 HOH 71  571 6   HOH HOH A . 
D 3 HOH 72  572 203 HOH HOH A . 
D 3 HOH 73  573 86  HOH HOH A . 
D 3 HOH 74  574 77  HOH HOH A . 
D 3 HOH 75  575 10  HOH HOH A . 
D 3 HOH 76  576 33  HOH HOH A . 
D 3 HOH 77  577 42  HOH HOH A . 
D 3 HOH 78  578 2   HOH HOH A . 
D 3 HOH 79  579 7   HOH HOH A . 
D 3 HOH 80  580 40  HOH HOH A . 
D 3 HOH 81  581 25  HOH HOH A . 
D 3 HOH 82  582 167 HOH HOH A . 
D 3 HOH 83  583 136 HOH HOH A . 
D 3 HOH 84  584 190 HOH HOH A . 
D 3 HOH 85  585 89  HOH HOH A . 
D 3 HOH 86  586 113 HOH HOH A . 
D 3 HOH 87  587 45  HOH HOH A . 
D 3 HOH 88  588 173 HOH HOH A . 
D 3 HOH 89  589 130 HOH HOH A . 
D 3 HOH 90  590 35  HOH HOH A . 
D 3 HOH 91  591 120 HOH HOH A . 
D 3 HOH 92  592 177 HOH HOH A . 
D 3 HOH 93  593 43  HOH HOH A . 
D 3 HOH 94  594 79  HOH HOH A . 
D 3 HOH 95  595 115 HOH HOH A . 
D 3 HOH 96  596 47  HOH HOH A . 
D 3 HOH 97  597 81  HOH HOH A . 
D 3 HOH 98  598 34  HOH HOH A . 
D 3 HOH 99  599 44  HOH HOH A . 
D 3 HOH 100 600 184 HOH HOH A . 
D 3 HOH 101 601 199 HOH HOH A . 
D 3 HOH 102 602 84  HOH HOH A . 
D 3 HOH 103 603 20  HOH HOH A . 
D 3 HOH 104 604 125 HOH HOH A . 
D 3 HOH 105 605 36  HOH HOH A . 
D 3 HOH 106 606 8   HOH HOH A . 
D 3 HOH 107 607 17  HOH HOH A . 
D 3 HOH 108 608 213 HOH HOH A . 
D 3 HOH 109 609 180 HOH HOH A . 
D 3 HOH 110 610 66  HOH HOH A . 
D 3 HOH 111 611 74  HOH HOH A . 
D 3 HOH 112 612 82  HOH HOH A . 
D 3 HOH 113 613 103 HOH HOH A . 
D 3 HOH 114 614 205 HOH HOH A . 
D 3 HOH 115 615 24  HOH HOH A . 
D 3 HOH 116 616 71  HOH HOH A . 
D 3 HOH 117 617 191 HOH HOH A . 
D 3 HOH 118 618 209 HOH HOH A . 
D 3 HOH 119 619 56  HOH HOH A . 
D 3 HOH 120 620 65  HOH HOH A . 
D 3 HOH 121 621 145 HOH HOH A . 
D 3 HOH 122 622 201 HOH HOH A . 
D 3 HOH 123 623 211 HOH HOH A . 
D 3 HOH 124 624 117 HOH HOH A . 
D 3 HOH 125 625 188 HOH HOH A . 
D 3 HOH 126 626 228 HOH HOH A . 
D 3 HOH 127 627 157 HOH HOH A . 
D 3 HOH 128 628 154 HOH HOH A . 
D 3 HOH 129 629 21  HOH HOH A . 
D 3 HOH 130 630 28  HOH HOH A . 
D 3 HOH 131 631 83  HOH HOH A . 
D 3 HOH 132 632 104 HOH HOH A . 
D 3 HOH 133 633 132 HOH HOH A . 
D 3 HOH 134 634 39  HOH HOH A . 
D 3 HOH 135 635 214 HOH HOH A . 
D 3 HOH 136 636 23  HOH HOH A . 
D 3 HOH 137 637 128 HOH HOH A . 
D 3 HOH 138 638 94  HOH HOH A . 
D 3 HOH 139 639 1   HOH HOH A . 
D 3 HOH 140 640 175 HOH HOH A . 
D 3 HOH 141 641 111 HOH HOH A . 
D 3 HOH 142 642 155 HOH HOH A . 
D 3 HOH 143 643 72  HOH HOH A . 
D 3 HOH 144 644 11  HOH HOH A . 
D 3 HOH 145 645 85  HOH HOH A . 
D 3 HOH 146 646 187 HOH HOH A . 
D 3 HOH 147 647 95  HOH HOH A . 
D 3 HOH 148 648 73  HOH HOH A . 
D 3 HOH 149 649 15  HOH HOH A . 
D 3 HOH 150 650 141 HOH HOH A . 
D 3 HOH 151 651 51  HOH HOH A . 
D 3 HOH 152 652 142 HOH HOH A . 
D 3 HOH 153 653 50  HOH HOH A . 
D 3 HOH 154 654 137 HOH HOH A . 
D 3 HOH 155 655 140 HOH HOH A . 
D 3 HOH 156 656 102 HOH HOH A . 
D 3 HOH 157 657 135 HOH HOH A . 
D 3 HOH 158 658 121 HOH HOH A . 
D 3 HOH 159 659 109 HOH HOH A . 
D 3 HOH 160 660 152 HOH HOH A . 
D 3 HOH 161 661 171 HOH HOH A . 
D 3 HOH 162 662 226 HOH HOH A . 
D 3 HOH 163 663 159 HOH HOH A . 
D 3 HOH 164 664 114 HOH HOH A . 
D 3 HOH 165 665 107 HOH HOH A . 
D 3 HOH 166 666 170 HOH HOH A . 
D 3 HOH 167 667 55  HOH HOH A . 
D 3 HOH 168 668 153 HOH HOH A . 
D 3 HOH 169 669 161 HOH HOH A . 
D 3 HOH 170 670 182 HOH HOH A . 
D 3 HOH 171 671 105 HOH HOH A . 
D 3 HOH 172 672 99  HOH HOH A . 
D 3 HOH 173 673 75  HOH HOH A . 
D 3 HOH 174 674 198 HOH HOH A . 
D 3 HOH 175 675 54  HOH HOH A . 
D 3 HOH 176 676 164 HOH HOH A . 
D 3 HOH 177 677 53  HOH HOH A . 
D 3 HOH 178 678 38  HOH HOH A . 
D 3 HOH 179 679 143 HOH HOH A . 
D 3 HOH 180 680 101 HOH HOH A . 
D 3 HOH 181 681 93  HOH HOH A . 
D 3 HOH 182 682 124 HOH HOH A . 
D 3 HOH 183 683 70  HOH HOH A . 
D 3 HOH 184 684 181 HOH HOH A . 
D 3 HOH 185 685 80  HOH HOH A . 
D 3 HOH 186 686 176 HOH HOH A . 
D 3 HOH 187 687 57  HOH HOH A . 
D 3 HOH 188 688 194 HOH HOH A . 
D 3 HOH 189 689 212 HOH HOH A . 
D 3 HOH 190 690 196 HOH HOH A . 
D 3 HOH 191 691 192 HOH HOH A . 
D 3 HOH 192 692 202 HOH HOH A . 
D 3 HOH 193 693 168 HOH HOH A . 
D 3 HOH 194 694 61  HOH HOH A . 
D 3 HOH 195 695 221 HOH HOH A . 
D 3 HOH 196 696 183 HOH HOH A . 
D 3 HOH 197 697 112 HOH HOH A . 
D 3 HOH 198 698 116 HOH HOH A . 
D 3 HOH 199 699 139 HOH HOH A . 
D 3 HOH 200 700 206 HOH HOH A . 
D 3 HOH 201 701 224 HOH HOH A . 
D 3 HOH 202 702 76  HOH HOH A . 
D 3 HOH 203 703 225 HOH HOH A . 
D 3 HOH 204 704 215 HOH HOH A . 
D 3 HOH 205 705 146 HOH HOH A . 
D 3 HOH 206 706 169 HOH HOH A . 
D 3 HOH 207 707 227 HOH HOH A . 
D 3 HOH 208 708 147 HOH HOH A . 
D 3 HOH 209 709 92  HOH HOH A . 
D 3 HOH 210 710 217 HOH HOH A . 
D 3 HOH 211 711 229 HOH HOH A . 
D 3 HOH 212 712 98  HOH HOH A . 
D 3 HOH 213 713 165 HOH HOH A . 
D 3 HOH 214 714 96  HOH HOH A . 
D 3 HOH 215 715 223 HOH HOH A . 
D 3 HOH 216 716 149 HOH HOH A . 
D 3 HOH 217 717 189 HOH HOH A . 
D 3 HOH 218 718 150 HOH HOH A . 
D 3 HOH 219 719 144 HOH HOH A . 
D 3 HOH 220 720 148 HOH HOH A . 
D 3 HOH 221 721 186 HOH HOH A . 
D 3 HOH 222 722 158 HOH HOH A . 
D 3 HOH 223 723 166 HOH HOH A . 
D 3 HOH 224 724 118 HOH HOH A . 
D 3 HOH 225 725 163 HOH HOH A . 
D 3 HOH 226 726 222 HOH HOH A . 
D 3 HOH 227 727 119 HOH HOH A . 
D 3 HOH 228 728 127 HOH HOH A . 
D 3 HOH 229 729 160 HOH HOH A . 
# 
_software.citation_id            ? 
_software.classification         refinement 
_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                   PHENIX 
_software.os                     ? 
_software.os_version             ? 
_software.type                   ? 
_software.version                1.9_1692 
_software.pdbx_ordinal           1 
# 
_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                     8XT5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     44.998 
_cell.length_a_esd                 ? 
_cell.length_b                     66.945 
_cell.length_b_esd                 ? 
_cell.length_c                     84.884 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8XT5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8XT5 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.00 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.43 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '30% polyethylene glycol 8K, 0.5 M KCl, 0.1 M MES pH 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-04-06 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9789 
_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                        'AichiSR BEAMLINE BL2S1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9789 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL2S1 
_diffrn_source.pdbx_synchrotron_site       AichiSR 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XT5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.39 
_reflns.d_resolution_low                               26.857 
_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                                     51982 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.56 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          1.36 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.065 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.39 
_reflns_shell.d_res_low                                     1.42 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3108 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.593 
_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                                  ? 
_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                                 8XT5 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.391 
_refine.ls_d_res_low                             26.857 
_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                     51982 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.56 
_refine.ls_percent_reflns_R_free                 3.85 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1565 
_refine.ls_R_factor_R_free                       0.1839 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1554 
_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                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 16.80 
_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                            0.16 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2109 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_refine_hist.number_atoms_solvent             229 
_refine_hist.number_atoms_total               2340 
_refine_hist.d_res_high                       1.391 
_refine_hist.d_res_low                        26.857 
# 
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' ? 0.012  ? 2157 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.369  ? 2936 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.159 ? 787  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 327  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 392  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.3911 1.4259 . . 135 3352 95.00  . . . . 0.2924 . . . . . . . . . . . 0.3466 
'X-RAY DIFFRACTION' 1.4259 1.4644 . . 142 3543 100.00 . . . . 0.2242 . . . . . . . . . . . 0.2689 
'X-RAY DIFFRACTION' 1.4644 1.5075 . . 141 3520 100.00 . . . . 0.1716 . . . . . . . . . . . 0.2274 
'X-RAY DIFFRACTION' 1.5075 1.5562 . . 142 3555 100.00 . . . . 0.1462 . . . . . . . . . . . 0.1917 
'X-RAY DIFFRACTION' 1.5562 1.6118 . . 141 3532 100.00 . . . . 0.1339 . . . . . . . . . . . 0.1745 
'X-RAY DIFFRACTION' 1.6118 1.6763 . . 142 3559 100.00 . . . . 0.1309 . . . . . . . . . . . 0.1627 
'X-RAY DIFFRACTION' 1.6763 1.7526 . . 142 3554 100.00 . . . . 0.1394 . . . . . . . . . . . 0.1811 
'X-RAY DIFFRACTION' 1.7526 1.8449 . . 142 3550 100.00 . . . . 0.1382 . . . . . . . . . . . 0.1942 
'X-RAY DIFFRACTION' 1.8449 1.9605 . . 144 3585 100.00 . . . . 0.1352 . . . . . . . . . . . 0.1864 
'X-RAY DIFFRACTION' 1.9605 2.1118 . . 142 3562 100.00 . . . . 0.1430 . . . . . . . . . . . 0.1899 
'X-RAY DIFFRACTION' 2.1118 2.3242 . . 144 3589 100.00 . . . . 0.1430 . . . . . . . . . . . 0.1471 
'X-RAY DIFFRACTION' 2.3242 2.6603 . . 145 3640 100.00 . . . . 0.1568 . . . . . . . . . . . 0.2109 
'X-RAY DIFFRACTION' 2.6603 3.3507 . . 146 3652 100.00 . . . . 0.1663 . . . . . . . . . . . 0.1756 
'X-RAY DIFFRACTION' 3.3507 26.857 . . 152 3789 99.00  . . . . 0.1587 . . . . . . . . . . . 0.1771 
# 
_struct.entry_id                     8XT5 
_struct.title                        'The closed state of RGLG5-VWA' 
_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        8XT5 
_struct_keywords.text            'ligase, VWA domain, PLANT PROTEIN' 
_struct_keywords.pdbx_keywords   'PLANT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RGLG5_ARATH 
_struct_ref.pdbx_db_accession          Q8LB88 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;RKYSRIADNYRSIDEVTAALSHAGLESSNLIVGIDVTKSNEWTGARSFGRKSLHFIGTTPNPYQQAISIIGKTLSVFDED
NLIPCYGFGDATTHDQDVFSFNPNDTYCNGFEEVLMCYREIVPQLRLSGPTSFAPIIERAMTIVEESGGQYHVLLIIADG
QVTRSVDTDNGGFSPQEQQTIDAIVRASEYPLSIVLVGVGDGPWDTMRQFDDNIPARAFDNFQFVNFTDIMSKNIDPARK
EAEFALSALMEIPSQYKATLELGLLGQRTGHCPDRIALPPP
;
_struct_ref.pdbx_align_begin           65 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8XT5 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 11 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 291 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q8LB88 
_struct_ref_seq.db_align_beg                  65 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  345 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       65 
_struct_ref_seq.pdbx_auth_seq_align_end       345 
# 
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 8XT5 GLY A 1  ? UNP Q8LB88 ? ? 'expression tag' 55 1  
1 8XT5 THR A 2  ? UNP Q8LB88 ? ? 'expression tag' 56 2  
1 8XT5 SER A 3  ? UNP Q8LB88 ? ? 'expression tag' 57 3  
1 8XT5 SER A 4  ? UNP Q8LB88 ? ? 'expression tag' 58 4  
1 8XT5 MET A 5  ? UNP Q8LB88 ? ? 'expression tag' 59 5  
1 8XT5 ALA A 6  ? UNP Q8LB88 ? ? 'expression tag' 60 6  
1 8XT5 ASP A 7  ? UNP Q8LB88 ? ? 'expression tag' 61 7  
1 8XT5 ILE A 8  ? UNP Q8LB88 ? ? 'expression tag' 62 8  
1 8XT5 GLY A 9  ? UNP Q8LB88 ? ? 'expression tag' 63 9  
1 8XT5 SER A 10 ? UNP Q8LB88 ? ? 'expression tag' 64 10 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 300   ? 
1 MORE         -20   ? 
1 'SSA (A^2)'  12190 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 22  ? ALA A 33  ? SER A 76  ALA A 87  1 ? 12 
HELX_P HELX_P2  AA2 THR A 47  ? TRP A 52  ? THR A 101 TRP A 106 5 ? 6  
HELX_P HELX_P3  AA3 ASN A 71  ? SER A 85  ? ASN A 125 SER A 139 1 ? 15 
HELX_P HELX_P4  AA4 VAL A 86  ? ASP A 88  ? VAL A 140 ASP A 142 5 ? 3  
HELX_P HELX_P5  AA5 GLY A 120 ? VAL A 132 ? GLY A 174 VAL A 186 1 ? 13 
HELX_P HELX_P6  AA6 PRO A 133 ? LEU A 135 ? PRO A 187 LEU A 189 5 ? 3  
HELX_P HELX_P7  AA7 PHE A 143 ? SER A 157 ? PHE A 197 SER A 211 1 ? 15 
HELX_P HELX_P8  AA8 SER A 184 ? SER A 198 ? SER A 238 SER A 252 1 ? 15 
HELX_P HELX_P9  AA9 THR A 216 ? ASN A 223 ? THR A 270 ASN A 277 1 ? 8  
HELX_P HELX_P10 AB1 PHE A 237 ? SER A 242 ? PHE A 291 SER A 296 1 ? 6  
HELX_P HELX_P11 AB2 ASP A 246 ? MET A 260 ? ASP A 300 MET A 314 1 ? 15 
HELX_P HELX_P12 AB3 GLU A 261 ? LEU A 272 ? GLU A 315 LEU A 326 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 139 A . ? GLY 193 A PRO 140 A ? PRO 194 A 1 -8.25 
2 GLY 212 A . ? GLY 266 A PRO 213 A ? PRO 267 A 1 13.76 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 109 ? SER A 110 ? PHE A 163 SER A 164 
AA1 2 CYS A 95  ? PHE A 98  ? CYS A 149 PHE A 152 
AA1 3 ASN A 39  ? ASP A 45  ? ASN A 93  ASP A 99  
AA1 4 HIS A 162 ? ALA A 168 ? HIS A 216 ALA A 222 
AA1 5 LEU A 202 ? GLY A 208 ? LEU A 256 GLY A 262 
AA1 6 PHE A 232 ? ASN A 236 ? PHE A 286 ASN A 290 
AA2 1 LEU A 92  ? ILE A 93  ? LEU A 146 ILE A 147 
AA2 2 CYS A 118 ? ASN A 119 ? CYS A 172 ASN A 173 
# 
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 PHE A 109 ? O PHE A 163 N GLY A 97  ? N GLY A 151 
AA1 2 3 O TYR A 96  ? O TYR A 150 N ILE A 44  ? N ILE A 98  
AA1 3 4 N GLY A 43  ? N GLY A 97  O LEU A 165 ? O LEU A 219 
AA1 4 5 N ILE A 166 ? N ILE A 220 O VAL A 207 ? O VAL A 261 
AA1 5 6 N GLY A 208 ? N GLY A 262 O VAL A 235 ? O VAL A 289 
AA2 1 2 N ILE A 93  ? N ILE A 147 O CYS A 118 ? O CYS A 172 
# 
_pdbx_entry_details.entry_id                   8XT5 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 640 ? ? O A HOH 696 ? ? 1.40 
2 1 O   A HOH 506 ? ? O A HOH 572 ? ? 1.81 
3 1 O   A HOH 518 ? ? O A HOH 588 ? ? 1.87 
4 1 O   A HOH 692 ? ? O A HOH 711 ? ? 1.98 
5 1 O   A HOH 725 ? ? O A HOH 727 ? ? 2.02 
6 1 NZ  A LYS 321 ? ? O A HOH 501 ? ? 2.11 
7 1 OE1 A GLU 79  ? ? O A HOH 502 ? ? 2.17 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 NH2 A ARG 110 ? ? 1_555 OD2 A ASP 276 ? ? 4_555 1.16 
2 1 NH1 A ARG 110 ? ? 1_555 OE1 A GLN 273 ? ? 4_555 1.78 
3 1 CZ  A ARG 110 ? ? 1_555 OD2 A ASP 276 ? ? 4_555 1.84 
4 1 CZ  A ARG 110 ? ? 1_555 OE1 A GLN 273 ? ? 4_555 1.96 
5 1 NH2 A ARG 110 ? ? 1_555 OE1 A GLN 273 ? ? 4_555 2.13 
6 1 OD1 A ASN 168 ? ? 1_555 NH2 A ARG 228 ? ? 3_644 2.16 
7 1 O   A HOH 545 ? ? 1_555 O   A HOH 684 ? ? 3_644 2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_1             267 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            N 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_2             267 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.559 
_pdbx_validate_rmsd_bond.bond_target_value         1.474 
_pdbx_validate_rmsd_bond.bond_deviation            0.085 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.014 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C A ASP 233 ? ? N A ASN 234 ? ? CA A ASN 234 ? ? 136.90 121.70 15.20  2.50 Y 
2 1 O A ASN 234 ? ? C A ASN 234 ? ? N  A GLY 235 ? ? 105.72 123.20 -17.48 1.70 Y 
3 1 C A GLY 266 ? ? N A PRO 267 ? ? CD A PRO 267 ? ? 137.67 120.60 17.07  2.20 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 GLU A 90  ? ? -120.41 -142.68 
2 1 PHE A 112 ? ? -149.30 38.07   
3 1 HIS A 158 ? ? 46.46   -128.74 
4 1 SER A 192 ? ? -143.95 -140.92 
5 1 HIS A 335 ? ? -146.38 55.77   
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             ASN 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              234 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   25.77 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 55 ? A GLY 1  
2  1 Y 1 A THR 56 ? A THR 2  
3  1 Y 1 A SER 57 ? A SER 3  
4  1 Y 1 A SER 58 ? A SER 4  
5  1 Y 1 A MET 59 ? A MET 5  
6  1 Y 1 A ALA 60 ? A ALA 6  
7  1 Y 1 A ASP 61 ? A ASP 7  
8  1 Y 1 A ILE 62 ? A ILE 8  
9  1 Y 1 A GLY 63 ? A GLY 9  
10 1 Y 1 A SER 64 ? A SER 10 
11 1 Y 1 A ARG 65 ? A ARG 11 
12 1 Y 1 A LYS 66 ? A LYS 12 
13 1 Y 1 A TYR 67 ? A TYR 13 
14 1 Y 1 A SER 68 ? A SER 14 
15 1 Y 1 A ARG 69 ? A ARG 15 
16 1 Y 1 A ILE 70 ? A ILE 16 
17 1 Y 1 A ALA 71 ? A ALA 17 
18 1 Y 1 A ASP 72 ? A ASP 18 
19 1 Y 1 A ASN 73 ? A ASN 19 
# 
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 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
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 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_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   6K89 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8XT5 
_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]   0.022223 
_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]   0.014938 
_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]   0.011781 
_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  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . TYR A 1 20  ? 28.403 -5.950  9.681   1.00 35.97  ? 74  TYR A N   1 
ATOM   2    C  CA  . TYR A 1 20  ? 29.066 -7.072  9.024   1.00 32.59  ? 74  TYR A CA  1 
ATOM   3    C  C   . TYR A 1 20  ? 30.466 -6.688  8.562   1.00 32.98  ? 74  TYR A C   1 
ATOM   4    O  O   . TYR A 1 20  ? 30.709 -5.552  8.153   1.00 35.25  ? 74  TYR A O   1 
ATOM   5    C  CB  . TYR A 1 20  ? 28.234 -7.564  7.838   1.00 30.89  ? 74  TYR A CB  1 
ATOM   6    C  CG  . TYR A 1 20  ? 26.864 -8.047  8.235   1.00 30.71  ? 74  TYR A CG  1 
ATOM   7    C  CD1 . TYR A 1 20  ? 26.678 -9.318  8.768   1.00 31.05  ? 74  TYR A CD1 1 
ATOM   8    C  CD2 . TYR A 1 20  ? 25.753 -7.232  8.087   1.00 32.20  ? 74  TYR A CD2 1 
ATOM   9    C  CE1 . TYR A 1 20  ? 25.420 -9.762  9.136   1.00 31.45  ? 74  TYR A CE1 1 
ATOM   10   C  CE2 . TYR A 1 20  ? 24.490 -7.669  8.450   1.00 32.81  ? 74  TYR A CE2 1 
ATOM   11   C  CZ  . TYR A 1 20  ? 24.329 -8.931  8.976   1.00 33.02  ? 74  TYR A CZ  1 
ATOM   12   O  OH  . TYR A 1 20  ? 23.070 -9.356  9.339   1.00 35.06  ? 74  TYR A OH  1 
ATOM   13   N  N   . ARG A 1 21  ? 31.389 -7.642  8.619   1.00 33.39  ? 75  ARG A N   1 
ATOM   14   C  CA  . ARG A 1 21  ? 32.800 -7.420  8.329   1.00 33.93  ? 75  ARG A CA  1 
ATOM   15   C  C   . ARG A 1 21  ? 33.126 -7.443  6.837   1.00 30.75  ? 75  ARG A C   1 
ATOM   16   O  O   . ARG A 1 21  ? 34.150 -6.908  6.412   1.00 31.27  ? 75  ARG A O   1 
ATOM   17   C  CB  . ARG A 1 21  ? 33.652 -8.459  9.059   1.00 39.50  ? 75  ARG A CB  1 
ATOM   18   C  CG  . ARG A 1 21  ? 34.784 -7.849  9.864   1.00 47.79  ? 75  ARG A CG  1 
ATOM   19   C  CD  . ARG A 1 21  ? 35.351 -8.837  10.862  1.00 55.03  ? 75  ARG A CD  1 
ATOM   20   N  NE  . ARG A 1 21  ? 36.363 -8.227  11.723  1.00 60.17  ? 75  ARG A NE  1 
ATOM   21   C  CZ  . ARG A 1 21  ? 37.673 -8.294  11.501  1.00 65.74  ? 75  ARG A CZ  1 
ATOM   22   N  NH1 . ARG A 1 21  ? 38.137 -8.947  10.442  1.00 66.61  ? 75  ARG A NH1 1 
ATOM   23   N  NH2 . ARG A 1 21  ? 38.519 -7.706  12.336  1.00 67.55  ? 75  ARG A NH2 1 
ATOM   24   N  N   . SER A 1 22  ? 32.297 -8.152  6.077   1.00 27.08  ? 76  SER A N   1 
ATOM   25   C  CA  . SER A 1 22  ? 32.558 -8.344  4.654   1.00 23.82  ? 76  SER A CA  1 
ATOM   26   C  C   . SER A 1 22  ? 31.262 -8.565  3.899   1.00 21.44  ? 76  SER A C   1 
ATOM   27   O  O   . SER A 1 22  ? 30.227 -8.901  4.490   1.00 20.97  ? 76  SER A O   1 
ATOM   28   C  CB  . SER A 1 22  ? 33.472 -9.545  4.422   1.00 27.11  ? 76  SER A CB  1 
ATOM   29   O  OG  . SER A 1 22  ? 32.783 -10.737 4.748   1.00 29.51  ? 76  SER A OG  1 
ATOM   30   N  N   . ILE A 1 23  ? 31.318 -8.439  2.580   1.00 20.74  ? 77  ILE A N   1 
ATOM   31   C  CA  . ILE A 1 23  ? 30.121 -8.737  1.826   1.00 20.67  ? 77  ILE A CA  1 
ATOM   32   C  C   . ILE A 1 23  ? 29.777 -10.225 1.885   1.00 18.37  ? 77  ILE A C   1 
ATOM   33   O  O   . ILE A 1 23  ? 28.612 -10.564 1.744   1.00 18.86  ? 77  ILE A O   1 
ATOM   34   C  CB  . ILE A 1 23  ? 30.204 -8.289  0.370   1.00 25.02  ? 77  ILE A CB  1 
ATOM   35   C  CG1 . ILE A 1 23  ? 31.402 -8.891  -0.344  1.00 25.22  ? 77  ILE A CG1 1 
ATOM   36   C  CG2 . ILE A 1 23  ? 30.222 -6.763  0.288   1.00 25.83  ? 77  ILE A CG2 1 
ATOM   37   C  CD1 . ILE A 1 23  ? 31.382 -8.559  -1.825  1.00 28.52  ? 77  ILE A CD1 1 
ATOM   38   N  N   . ASP A 1 24  ? 30.751 -11.103 2.143   1.00 19.22  ? 78  ASP A N   1 
ATOM   39   C  CA  . ASP A 1 24  ? 30.421 -12.524 2.268   1.00 19.13  ? 78  ASP A CA  1 
ATOM   40   C  C   . ASP A 1 24  ? 29.487 -12.743 3.459   1.00 19.63  ? 78  ASP A C   1 
ATOM   41   O  O   . ASP A 1 24  ? 28.549 -13.534 3.377   1.00 20.21  ? 78  ASP A O   1 
ATOM   42   C  CB  . ASP A 1 24  ? 31.683 -13.380 2.409   1.00 19.24  ? 78  ASP A CB  1 
ATOM   43   C  CG  . ASP A 1 24  ? 32.444 -13.533 1.094   1.00 21.82  ? 78  ASP A CG  1 
ATOM   44   O  OD1 . ASP A 1 24  ? 31.985 -13.010 0.058   1.00 23.62  ? 78  ASP A OD1 1 
ATOM   45   O  OD2 . ASP A 1 24  ? 33.508 -14.191 1.098   1.00 22.57  ? 78  ASP A OD2 1 
ATOM   46   N  N   . GLU A 1 25  ? 29.714 -12.019 4.551   1.00 19.49  ? 79  GLU A N   1 
ATOM   47   C  CA  . GLU A 1 25  ? 28.784 -12.088 5.675   1.00 20.29  ? 79  GLU A CA  1 
ATOM   48   C  C   . GLU A 1 25  ? 27.395 -11.535 5.324   1.00 19.89  ? 79  GLU A C   1 
ATOM   49   O  O   . GLU A 1 25  ? 26.380 -12.026 5.822   1.00 20.81  ? 79  GLU A O   1 
ATOM   50   C  CB  . GLU A 1 25  ? 29.365 -11.362 6.886   1.00 23.38  ? 79  GLU A CB  1 
ATOM   51   C  CG  . GLU A 1 25  ? 30.504 -12.146 7.535   1.00 29.52  ? 79  GLU A CG  1 
ATOM   52   C  CD  . GLU A 1 25  ? 30.978 -11.522 8.832   1.00 38.20  ? 79  GLU A CD  1 
ATOM   53   O  OE1 . GLU A 1 25  ? 30.325 -10.569 9.308   1.00 41.07  ? 79  GLU A OE1 1 
ATOM   54   O  OE2 . GLU A 1 25  ? 32.001 -11.993 9.378   1.00 43.59  ? 79  GLU A OE2 1 
ATOM   55   N  N   . VAL A 1 26  ? 27.334 -10.530 4.452   1.00 18.79  ? 80  VAL A N   1 
ATOM   56   C  CA  . VAL A 1 26  ? 26.042 -9.999  4.026   1.00 17.96  ? 80  VAL A CA  1 
ATOM   57   C  C   . VAL A 1 26  ? 25.299 -11.032 3.173   1.00 18.65  ? 80  VAL A C   1 
ATOM   58   O  O   . VAL A 1 26  ? 24.105 -11.259 3.360   1.00 19.51  ? 80  VAL A O   1 
ATOM   59   C  CB  . VAL A 1 26  ? 26.209 -8.675  3.258   1.00 17.88  ? 80  VAL A CB  1 
ATOM   60   C  CG1 . VAL A 1 26  ? 24.848 -8.178  2.742   1.00 18.46  ? 80  VAL A CG1 1 
ATOM   61   C  CG2 . VAL A 1 26  ? 26.891 -7.638  4.161   1.00 19.79  ? 80  VAL A CG2 1 
ATOM   62   N  N   . THR A 1 27  ? 26.014 -11.677 2.253   1.00 17.62  ? 81  THR A N   1 
ATOM   63   C  CA  . THR A 1 27  ? 25.441 -12.771 1.463   1.00 16.69  ? 81  THR A CA  1 
ATOM   64   C  C   . THR A 1 27  ? 24.794 -13.814 2.366   1.00 16.67  ? 81  THR A C   1 
ATOM   65   O  O   . THR A 1 27  ? 23.630 -14.206 2.184   1.00 17.17  ? 81  THR A O   1 
ATOM   66   C  CB  . THR A 1 27  ? 26.515 -13.445 0.597   1.00 16.56  ? 81  THR A CB  1 
ATOM   67   O  OG1 . THR A 1 27  ? 27.012 -12.489 -0.351  1.00 17.42  ? 81  THR A OG1 1 
ATOM   68   C  CG2 . THR A 1 27  ? 25.937 -14.631 -0.137  1.00 16.65  ? 81  THR A CG2 1 
ATOM   69   N  N   . ALA A 1 28  ? 25.554 -14.259 3.355   1.00 17.20  ? 82  ALA A N   1 
ATOM   70   C  CA  . ALA A 1 28  ? 25.058 -15.274 4.268   1.00 18.95  ? 82  ALA A CA  1 
ATOM   71   C  C   . ALA A 1 28  ? 23.854 -14.787 5.071   1.00 19.36  ? 82  ALA A C   1 
ATOM   72   O  O   . ALA A 1 28  ? 22.914 -15.548 5.302   1.00 20.78  ? 82  ALA A O   1 
ATOM   73   C  CB  . ALA A 1 28  ? 26.165 -15.726 5.195   1.00 20.35  ? 82  ALA A CB  1 
ATOM   74   N  N   . ALA A 1 29  ? 23.881 -13.521 5.480   1.00 19.62  ? 83  ALA A N   1 
ATOM   75   C  CA  . ALA A 1 29  ? 22.765 -12.950 6.229   1.00 20.24  ? 83  ALA A CA  1 
ATOM   76   C  C   . ALA A 1 29  ? 21.498 -12.884 5.367   1.00 22.02  ? 83  ALA A C   1 
ATOM   77   O  O   . ALA A 1 29  ? 20.397 -13.128 5.851   1.00 22.67  ? 83  ALA A O   1 
ATOM   78   C  CB  . ALA A 1 29  ? 23.134 -11.577 6.761   1.00 20.80  ? 83  ALA A CB  1 
ATOM   79   N  N   . LEU A 1 30  ? 21.642 -12.574 4.082   1.00 20.57  ? 84  LEU A N   1 
ATOM   80   C  CA  . LEU A 1 30  ? 20.482 -12.561 3.196   1.00 19.22  ? 84  LEU A CA  1 
ATOM   81   C  C   . LEU A 1 30  ? 19.873 -13.952 3.038   1.00 19.39  ? 84  LEU A C   1 
ATOM   82   O  O   . LEU A 1 30  ? 18.645 -14.117 3.033   1.00 20.74  ? 84  LEU A O   1 
ATOM   83   C  CB  . LEU A 1 30  ? 20.864 -12.000 1.828   1.00 20.42  ? 84  LEU A CB  1 
ATOM   84   C  CG  . LEU A 1 30  ? 21.225 -10.517 1.773   1.00 20.21  ? 84  LEU A CG  1 
ATOM   85   C  CD1 . LEU A 1 30  ? 21.865 -10.217 0.430   1.00 19.81  ? 84  LEU A CD1 1 
ATOM   86   C  CD2 . LEU A 1 30  ? 19.985 -9.627  1.995   1.00 22.13  ? 84  LEU A CD2 1 
ATOM   87   N  N   . SER A 1 31  ? 20.729 -14.961 2.910   1.00 19.27  ? 85  SER A N   1 
ATOM   88   C  CA  . SER A 1 31  ? 20.250 -16.333 2.852   1.00 20.27  ? 85  SER A CA  1 
ATOM   89   C  C   . SER A 1 31  ? 19.543 -16.722 4.146   1.00 21.28  ? 85  SER A C   1 
ATOM   90   O  O   . SER A 1 31  ? 18.456 -17.294 4.120   1.00 22.01  ? 85  SER A O   1 
ATOM   91   C  CB  . SER A 1 31  ? 21.409 -17.287 2.577   1.00 21.13  ? 85  SER A CB  1 
ATOM   92   O  OG  . SER A 1 31  ? 20.951 -18.626 2.556   1.00 22.58  ? 85  SER A OG  1 
ATOM   93   N  N   . HIS A 1 32  ? 20.160 -16.381 5.273   1.00 20.73  ? 86  HIS A N   1 
ATOM   94   C  CA  . HIS A 1 32  ? 19.608 -16.693 6.585   1.00 22.62  ? 86  HIS A CA  1 
ATOM   95   C  C   . HIS A 1 32  ? 18.248 -16.003 6.769   1.00 23.48  ? 86  HIS A C   1 
ATOM   96   O  O   . HIS A 1 32  ? 17.354 -16.549 7.414   1.00 25.46  ? 86  HIS A O   1 
ATOM   97   C  CB  . HIS A 1 32  ? 20.596 -16.275 7.680   1.00 24.47  ? 86  HIS A CB  1 
ATOM   98   C  CG  . HIS A 1 32  ? 20.091 -16.493 9.075   1.00 30.65  ? 86  HIS A CG  1 
ATOM   99   N  ND1 . HIS A 1 32  ? 20.167 -17.712 9.712   1.00 33.98  ? 86  HIS A ND1 1 
ATOM   100  C  CD2 . HIS A 1 32  ? 19.534 -15.637 9.964   1.00 34.08  ? 86  HIS A CD2 1 
ATOM   101  C  CE1 . HIS A 1 32  ? 19.652 -17.608 10.923  1.00 36.14  ? 86  HIS A CE1 1 
ATOM   102  N  NE2 . HIS A 1 32  ? 19.264 -16.359 11.105  1.00 36.99  ? 86  HIS A NE2 1 
ATOM   103  N  N   . ALA A 1 33  ? 18.068 -14.832 6.185   1.00 24.67  ? 87  ALA A N   1 
ATOM   104  C  CA  . ALA A 1 33  ? 16.793 -14.121 6.196   1.00 25.16  ? 87  ALA A CA  1 
ATOM   105  C  C   . ALA A 1 33  ? 15.742 -14.640 5.227   1.00 27.90  ? 87  ALA A C   1 
ATOM   106  O  O   . ALA A 1 33  ? 14.640 -14.155 5.191   1.00 29.74  ? 87  ALA A O   1 
ATOM   107  C  CB  . ALA A 1 33  ? 17.038 -12.656 5.976   1.00 27.36  ? 87  ALA A CB  1 
ATOM   108  N  N   . GLY A 1 34  ? 16.096 -15.617 4.429   1.00 26.29  ? 88  GLY A N   1 
ATOM   109  C  CA  . GLY A 1 34  ? 15.138 -16.288 3.609   1.00 26.99  ? 88  GLY A CA  1 
ATOM   110  C  C   . GLY A 1 34  ? 15.210 -16.105 2.106   1.00 27.49  ? 88  GLY A C   1 
ATOM   111  O  O   . GLY A 1 34  ? 14.400 -16.619 1.388   1.00 29.21  ? 88  GLY A O   1 
ATOM   112  N  N   . LEU A 1 35  ? 16.228 -15.406 1.653   1.00 24.99  ? 89  LEU A N   1 
ATOM   113  C  CA  . LEU A 1 35  ? 16.426 -15.271 0.216   1.00 24.42  ? 89  LEU A CA  1 
ATOM   114  C  C   . LEU A 1 35  ? 16.798 -16.616 -0.386  1.00 24.93  ? 89  LEU A C   1 
ATOM   115  O  O   . LEU A 1 35  ? 17.599 -17.333 0.131   1.00 26.31  ? 89  LEU A O   1 
ATOM   116  C  CB  . LEU A 1 35  ? 17.454 -14.194 -0.086  1.00 23.93  ? 89  LEU A CB  1 
ATOM   117  C  CG  . LEU A 1 35  ? 17.480 -13.728 -1.540  1.00 23.88  ? 89  LEU A CG  1 
ATOM   118  C  CD1 . LEU A 1 35  ? 16.194 -13.049 -1.985  1.00 23.33  ? 89  LEU A CD1 1 
ATOM   119  C  CD2 . LEU A 1 35  ? 18.622 -12.787 -1.748  1.00 24.98  ? 89  LEU A CD2 1 
ATOM   120  N  N   . GLU A 1 36  ? 16.156 -16.946 -1.482  1.00 26.18  ? 90  GLU A N   1 
ATOM   121  C  CA  . GLU A 1 36  ? 16.381 -18.164 -2.187  1.00 28.70  ? 90  GLU A CA  1 
ATOM   122  C  C   . GLU A 1 36  ? 16.836 -17.878 -3.614  1.00 28.74  ? 90  GLU A C   1 
ATOM   123  O  O   . GLU A 1 36  ? 17.547 -16.964 -3.834  1.00 32.28  ? 90  GLU A O   1 
ATOM   124  C  CB  . GLU A 1 36  ? 15.108 -19.013 -2.162  1.00 34.08  ? 90  GLU A CB  1 
ATOM   125  C  CG  . GLU A 1 36  ? 14.568 -19.292 -0.767  1.00 41.19  ? 90  GLU A CG  1 
ATOM   126  C  CD  . GLU A 1 36  ? 15.394 -20.330 -0.032  1.00 47.64  ? 90  GLU A CD  1 
ATOM   127  O  OE1 . GLU A 1 36  ? 15.884 -21.236 -0.699  1.00 49.89  ? 90  GLU A OE1 1 
ATOM   128  O  OE2 . GLU A 1 36  ? 15.537 -20.221 1.198   1.00 50.23  ? 90  GLU A OE2 1 
ATOM   129  N  N   . SER A 1 37  ? 16.417 -18.652 -4.581  1.00 28.33  ? 91  SER A N   1 
ATOM   130  C  CA  . SER A 1 37  ? 16.779 -18.393 -5.971  1.00 26.33  ? 91  SER A CA  1 
ATOM   131  C  C   . SER A 1 37  ? 16.406 -16.962 -6.347  1.00 24.06  ? 91  SER A C   1 
ATOM   132  O  O   . SER A 1 37  ? 15.260 -16.553 -6.180  1.00 25.40  ? 91  SER A O   1 
ATOM   133  C  CB  . SER A 1 37  ? 16.095 -19.392 -6.906  1.00 30.12  ? 91  SER A CB  1 
ATOM   134  O  OG  . SER A 1 37  ? 16.569 -19.256 -8.236  1.00 32.98  ? 91  SER A OG  1 
ATOM   135  N  N   . SER A 1 38  ? 17.387 -16.203 -6.832  1.00 21.71  ? 92  SER A N   1 
ATOM   136  C  CA  . SER A 1 38  ? 17.214 -14.775 -7.080  1.00 21.57  ? 92  SER A CA  1 
ATOM   137  C  C   . SER A 1 38  ? 18.062 -14.345 -8.271  1.00 20.44  ? 92  SER A C   1 
ATOM   138  O  O   . SER A 1 38  ? 19.231 -14.704 -8.370  1.00 23.12  ? 92  SER A O   1 
ATOM   139  C  CB  . SER A 1 38  ? 17.585 -13.975 -5.832  1.00 23.74  ? 92  SER A CB  1 
ATOM   140  O  OG  . SER A 1 38  ? 17.187 -12.624 -5.972  1.00 26.13  ? 92  SER A OG  1 
ATOM   141  N  N   . ASN A 1 39  ? 17.496 -13.556 -9.163  1.00 18.79  ? 93  ASN A N   1 
ATOM   142  C  CA  . ASN A 1 39  ? 18.091 -13.176 -10.416 1.00 17.65  ? 93  ASN A CA  1 
ATOM   143  C  C   . ASN A 1 39  ? 18.388 -11.692 -10.390 1.00 16.60  ? 93  ASN A C   1 
ATOM   144  O  O   . ASN A 1 39  ? 17.833 -10.992 -9.615  1.00 19.38  ? 93  ASN A O   1 
ATOM   145  C  CB  . ASN A 1 39  ? 17.124 -13.536 -11.514 1.00 16.94  ? 93  ASN A CB  1 
ATOM   146  C  CG  . ASN A 1 39  ? 16.847 -15.029 -11.542 1.00 19.24  ? 93  ASN A CG  1 
ATOM   147  O  OD1 . ASN A 1 39  ? 17.677 -15.779 -11.905 1.00 23.90  ? 93  ASN A OD1 1 
ATOM   148  N  ND2 . ASN A 1 39  ? 15.706 -15.427 -11.086 1.00 23.18  ? 93  ASN A ND2 1 
ATOM   149  N  N   . LEU A 1 40  ? 19.336 -11.260 -11.175 1.00 16.28  ? 94  LEU A N   1 
ATOM   150  C  CA  . LEU A 1 40  ? 19.795 -9.883  -11.167 1.00 15.50  ? 94  LEU A CA  1 
ATOM   151  C  C   . LEU A 1 40  ? 19.754 -9.306  -12.582 1.00 14.74  ? 94  LEU A C   1 
ATOM   152  O  O   . LEU A 1 40  ? 20.184 -9.949  -13.554 1.00 16.03  ? 94  LEU A O   1 
ATOM   153  C  CB  . LEU A 1 40  ? 21.210 -9.809  -10.594 1.00 15.22  ? 94  LEU A CB  1 
ATOM   154  C  CG  . LEU A 1 40  ? 21.920 -8.452  -10.568 1.00 15.76  ? 94  LEU A CG  1 
ATOM   155  C  CD1 . LEU A 1 40  ? 21.218 -7.473  -9.625  1.00 17.77  ? 94  LEU A CD1 1 
ATOM   156  C  CD2 . LEU A 1 40  ? 23.391 -8.611  -10.171 1.00 17.88  ? 94  LEU A CD2 1 
ATOM   157  N  N   . ILE A 1 41  ? 19.246 -8.080  -12.681 1.00 13.84  ? 95  ILE A N   1 
ATOM   158  C  CA  . ILE A 1 41  ? 19.262 -7.278  -13.908 1.00 13.36  ? 95  ILE A CA  1 
ATOM   159  C  C   . ILE A 1 41  ? 19.966 -5.977  -13.562 1.00 13.99  ? 95  ILE A C   1 
ATOM   160  O  O   . ILE A 1 41  ? 19.678 -5.396  -12.516 1.00 14.41  ? 95  ILE A O   1 
ATOM   161  C  CB  . ILE A 1 41  ? 17.844 -6.973  -14.406 1.00 13.75  ? 95  ILE A CB  1 
ATOM   162  C  CG1 . ILE A 1 41  ? 17.031 -8.252  -14.619 1.00 15.39  ? 95  ILE A CG1 1 
ATOM   163  C  CG2 . ILE A 1 41  ? 17.868 -6.083  -15.672 1.00 15.92  ? 95  ILE A CG2 1 
ATOM   164  C  CD1 . ILE A 1 41  ? 15.535 -7.983  -14.686 1.00 16.90  ? 95  ILE A CD1 1 
ATOM   165  N  N   . VAL A 1 42  ? 20.891 -5.527  -14.409 1.00 13.75  ? 96  VAL A N   1 
ATOM   166  C  CA  . VAL A 1 42  ? 21.629 -4.283  -14.160 1.00 14.41  ? 96  VAL A CA  1 
ATOM   167  C  C   . VAL A 1 42  ? 21.258 -3.222  -15.193 1.00 14.15  ? 96  VAL A C   1 
ATOM   168  O  O   . VAL A 1 42  ? 21.291 -3.477  -16.390 1.00 16.03  ? 96  VAL A O   1 
ATOM   169  C  CB  . VAL A 1 42  ? 23.140 -4.547  -14.177 1.00 16.14  ? 96  VAL A CB  1 
ATOM   170  C  CG1 . VAL A 1 42  ? 23.938 -3.257  -13.971 1.00 18.07  ? 96  VAL A CG1 1 
ATOM   171  C  CG2 . VAL A 1 42  ? 23.503 -5.559  -13.086 1.00 17.05  ? 96  VAL A CG2 1 
ATOM   172  N  N   . GLY A 1 43  ? 20.873 -2.043  -14.714 1.00 13.63  ? 97  GLY A N   1 
ATOM   173  C  CA  . GLY A 1 43  ? 20.635 -0.896  -15.577 1.00 13.85  ? 97  GLY A CA  1 
ATOM   174  C  C   . GLY A 1 43  ? 21.584 0.239   -15.237 1.00 13.55  ? 97  GLY A C   1 
ATOM   175  O  O   . GLY A 1 43  ? 21.703 0.622   -14.075 1.00 15.27  ? 97  GLY A O   1 
ATOM   176  N  N   . ILE A 1 44  ? 22.251 0.775   -16.253 1.00 14.09  ? 98  ILE A N   1 
ATOM   177  C  CA  . ILE A 1 44  ? 23.303 1.767   -16.091 1.00 14.51  ? 98  ILE A CA  1 
ATOM   178  C  C   . ILE A 1 44  ? 22.944 3.079   -16.780 1.00 13.82  ? 98  ILE A C   1 
ATOM   179  O  O   . ILE A 1 44  ? 22.739 3.118   -17.997 1.00 14.93  ? 98  ILE A O   1 
ATOM   180  C  CB  . ILE A 1 44  ? 24.636 1.235   -16.653 1.00 15.12  ? 98  ILE A CB  1 
ATOM   181  C  CG1 . ILE A 1 44  ? 24.989 -0.109  -15.993 1.00 15.99  ? 98  ILE A CG1 1 
ATOM   182  C  CG2 . ILE A 1 44  ? 25.779 2.286   -16.516 1.00 16.23  ? 98  ILE A CG2 1 
ATOM   183  C  CD1 . ILE A 1 44  ? 26.207 -0.783  -16.564 1.00 18.64  ? 98  ILE A CD1 1 
ATOM   184  N  N   . ASP A 1 45  ? 22.871 4.138   -15.982 1.00 13.89  ? 99  ASP A N   1 
ATOM   185  C  CA  . ASP A 1 45  ? 22.670 5.505   -16.441 1.00 15.13  ? 99  ASP A CA  1 
ATOM   186  C  C   . ASP A 1 45  ? 23.876 5.973   -17.232 1.00 15.07  ? 99  ASP A C   1 
ATOM   187  O  O   . ASP A 1 45  ? 24.963 6.101   -16.664 1.00 16.45  ? 99  ASP A O   1 
ATOM   188  C  CB  . ASP A 1 45  ? 22.452 6.379   -15.184 1.00 16.79  ? 99  ASP A CB  1 
ATOM   189  C  CG  . ASP A 1 45  ? 22.275 7.857   -15.468 1.00 19.38  ? 99  ASP A CG  1 
ATOM   190  O  OD1 . ASP A 1 45  ? 22.778 8.390   -16.470 1.00 20.75  ? 99  ASP A OD1 1 
ATOM   191  O  OD2 . ASP A 1 45  ? 21.675 8.517   -14.599 1.00 25.39  ? 99  ASP A OD2 1 
ATOM   192  N  N   . VAL A 1 46  ? 23.696 6.264   -18.521 1.00 15.53  ? 100 VAL A N   1 
ATOM   193  C  CA  . VAL A 1 46  ? 24.787 6.816   -19.318 1.00 14.57  ? 100 VAL A CA  1 
ATOM   194  C  C   . VAL A 1 46  ? 24.397 8.180   -19.923 1.00 16.40  ? 100 VAL A C   1 
ATOM   195  O  O   . VAL A 1 46  ? 24.658 8.485   -21.096 1.00 18.34  ? 100 VAL A O   1 
ATOM   196  C  CB  . VAL A 1 46  ? 25.264 5.808   -20.402 1.00 15.79  ? 100 VAL A CB  1 
ATOM   197  C  CG1 . VAL A 1 46  ? 26.044 4.661   -19.725 1.00 17.96  ? 100 VAL A CG1 1 
ATOM   198  C  CG2 . VAL A 1 46  ? 24.103 5.235   -21.229 1.00 17.98  ? 100 VAL A CG2 1 
ATOM   199  N  N   . THR A 1 47  ? 23.793 9.013   -19.079 1.00 17.06  ? 101 THR A N   1 
ATOM   200  C  CA  . THR A 1 47  ? 23.481 10.398  -19.433 1.00 19.05  ? 101 THR A CA  1 
ATOM   201  C  C   . THR A 1 47  ? 24.683 11.322  -19.244 1.00 19.17  ? 101 THR A C   1 
ATOM   202  O  O   . THR A 1 47  ? 25.667 10.987  -18.575 1.00 19.08  ? 101 THR A O   1 
ATOM   203  C  CB  . THR A 1 47  ? 22.301 10.957  -18.602 1.00 19.10  ? 101 THR A CB  1 
ATOM   204  O  OG1 . THR A 1 47  ? 22.632 10.927  -17.206 1.00 20.00  ? 101 THR A OG1 1 
ATOM   205  C  CG2 . THR A 1 47  ? 21.046 10.145  -18.841 1.00 18.56  ? 101 THR A CG2 1 
ATOM   206  N  N   . LYS A 1 48  ? 24.586 12.509  -19.824 1.00 20.44  ? 102 LYS A N   1 
ATOM   207  C  CA  . LYS A 1 48  ? 25.705 13.433  -19.906 1.00 22.97  ? 102 LYS A CA  1 
ATOM   208  C  C   . LYS A 1 48  ? 26.220 13.931  -18.563 1.00 23.67  ? 102 LYS A C   1 
ATOM   209  O  O   . LYS A 1 48  ? 27.415 14.210  -18.424 1.00 23.36  ? 102 LYS A O   1 
ATOM   210  C  CB  . LYS A 1 48  ? 25.299 14.628  -20.761 1.00 25.47  ? 102 LYS A CB  1 
ATOM   211  C  CG  . LYS A 1 48  ? 26.439 15.579  -21.072 1.00 27.80  ? 102 LYS A CG  1 
ATOM   212  C  CD  . LYS A 1 48  ? 27.415 14.951  -22.034 1.00 30.34  ? 102 LYS A CD  1 
ATOM   213  C  CE  . LYS A 1 48  ? 28.286 16.018  -22.703 1.00 32.39  ? 102 LYS A CE  1 
ATOM   214  N  NZ  . LYS A 1 48  ? 29.247 15.400  -23.661 1.00 35.16  ? 102 LYS A NZ  1 
ATOM   215  N  N   . SER A 1 49  ? 25.337 14.043  -17.576 1.00 23.51  ? 103 SER A N   1 
ATOM   216  C  CA  . SER A 1 49  ? 25.743 14.654  -16.309 1.00 24.77  ? 103 SER A CA  1 
ATOM   217  C  C   . SER A 1 49  ? 26.805 13.835  -15.592 1.00 23.18  ? 103 SER A C   1 
ATOM   218  O  O   . SER A 1 49  ? 27.483 14.360  -14.706 1.00 23.03  ? 103 SER A O   1 
ATOM   219  C  CB  . SER A 1 49  ? 24.545 14.867  -15.387 1.00 28.98  ? 103 SER A CB  1 
ATOM   220  O  OG  . SER A 1 49  ? 23.947 13.644  -15.031 1.00 30.58  ? 103 SER A OG  1 
ATOM   221  N  N   . ASN A 1 50  ? 26.964 12.569  -15.979 1.00 22.01  ? 104 ASN A N   1 
ATOM   222  C  CA  . ASN A 1 50  ? 28.065 11.765  -15.449 1.00 20.41  ? 104 ASN A CA  1 
ATOM   223  C  C   . ASN A 1 50  ? 29.436 12.403  -15.657 1.00 21.07  ? 104 ASN A C   1 
ATOM   224  O  O   . ASN A 1 50  ? 30.379 12.136  -14.906 1.00 22.18  ? 104 ASN A O   1 
ATOM   225  C  CB  . ASN A 1 50  ? 28.045 10.371  -16.074 1.00 19.63  ? 104 ASN A CB  1 
ATOM   226  C  CG  . ASN A 1 50  ? 26.965 9.508   -15.497 1.00 20.44  ? 104 ASN A CG  1 
ATOM   227  O  OD1 . ASN A 1 50  ? 27.032 9.115   -14.328 1.00 20.49  ? 104 ASN A OD1 1 
ATOM   228  N  ND2 . ASN A 1 50  ? 25.945 9.205   -16.305 1.00 18.89  ? 104 ASN A ND2 1 
ATOM   229  N  N   . GLU A 1 51  ? 29.554 13.269  -16.656 1.00 22.88  ? 105 GLU A N   1 
ATOM   230  C  CA  . GLU A 1 51  ? 30.820 13.942  -16.909 1.00 24.00  ? 105 GLU A CA  1 
ATOM   231  C  C   . GLU A 1 51  ? 31.200 14.932  -15.812 1.00 26.59  ? 105 GLU A C   1 
ATOM   232  O  O   . GLU A 1 51  ? 32.385 15.203  -15.614 1.00 29.51  ? 105 GLU A O   1 
ATOM   233  C  CB  . GLU A 1 51  ? 30.789 14.649  -18.269 1.00 25.81  ? 105 GLU A CB  1 
ATOM   234  C  CG  . GLU A 1 51  ? 30.817 13.666  -19.436 1.00 29.10  ? 105 GLU A CG  1 
ATOM   235  C  CD  . GLU A 1 51  ? 30.787 14.353  -20.789 1.00 34.43  ? 105 GLU A CD  1 
ATOM   236  O  OE1 . GLU A 1 51  ? 30.792 15.602  -20.826 1.00 35.88  ? 105 GLU A OE1 1 
ATOM   237  O  OE2 . GLU A 1 51  ? 30.767 13.643  -21.817 1.00 36.93  ? 105 GLU A OE2 1 
ATOM   238  N  N   . TRP A 1 52  ? 30.226 15.459  -15.077 1.00 26.71  ? 106 TRP A N   1 
ATOM   239  C  CA  . TRP A 1 52  ? 30.573 16.490  -14.095 1.00 28.90  ? 106 TRP A CA  1 
ATOM   240  C  C   . TRP A 1 52  ? 30.098 16.212  -12.661 1.00 28.32  ? 106 TRP A C   1 
ATOM   241  O  O   . TRP A 1 52  ? 30.424 16.975  -11.749 1.00 30.31  ? 106 TRP A O   1 
ATOM   242  C  CB  . TRP A 1 52  ? 30.052 17.861  -14.564 1.00 30.49  ? 106 TRP A CB  1 
ATOM   243  C  CG  . TRP A 1 52  ? 28.563 17.947  -14.740 1.00 31.07  ? 106 TRP A CG  1 
ATOM   244  C  CD1 . TRP A 1 52  ? 27.626 18.006  -13.752 1.00 31.75  ? 106 TRP A CD1 1 
ATOM   245  C  CD2 . TRP A 1 52  ? 27.841 18.012  -15.983 1.00 31.39  ? 106 TRP A CD2 1 
ATOM   246  N  NE1 . TRP A 1 52  ? 26.367 18.084  -14.296 1.00 32.42  ? 106 TRP A NE1 1 
ATOM   247  C  CE2 . TRP A 1 52  ? 26.470 18.090  -15.658 1.00 30.65  ? 106 TRP A CE2 1 
ATOM   248  C  CE3 . TRP A 1 52  ? 28.221 17.995  -17.326 1.00 31.91  ? 106 TRP A CE3 1 
ATOM   249  C  CZ2 . TRP A 1 52  ? 25.476 18.158  -16.639 1.00 30.60  ? 106 TRP A CZ2 1 
ATOM   250  C  CZ3 . TRP A 1 52  ? 27.233 18.067  -18.296 1.00 32.53  ? 106 TRP A CZ3 1 
ATOM   251  C  CH2 . TRP A 1 52  ? 25.878 18.149  -17.948 1.00 30.95  ? 106 TRP A CH2 1 
ATOM   252  N  N   . THR A 1 53  ? 29.385 15.110  -12.431 1.00 26.47  ? 107 THR A N   1 
ATOM   253  C  CA  . THR A 1 53  ? 28.904 14.818  -11.081 1.00 26.49  ? 107 THR A CA  1 
ATOM   254  C  C   . THR A 1 53  ? 29.924 14.043  -10.229 1.00 27.48  ? 107 THR A C   1 
ATOM   255  O  O   . THR A 1 53  ? 29.619 13.621  -9.116  1.00 28.94  ? 107 THR A O   1 
ATOM   256  C  CB  . THR A 1 53  ? 27.574 14.048  -11.108 1.00 26.85  ? 107 THR A CB  1 
ATOM   257  O  OG1 . THR A 1 53  ? 27.678 12.947  -12.016 1.00 27.44  ? 107 THR A OG1 1 
ATOM   258  C  CG2 . THR A 1 53  ? 26.448 14.964  -11.558 1.00 26.93  ? 107 THR A CG2 1 
ATOM   259  N  N   . GLY A 1 54  ? 31.139 13.885  -10.747 1.00 26.19  ? 108 GLY A N   1 
ATOM   260  C  CA  . GLY A 1 54  ? 32.250 13.383  -9.957  1.00 27.46  ? 108 GLY A CA  1 
ATOM   261  C  C   . GLY A 1 54  ? 33.190 14.482  -9.497  1.00 28.84  ? 108 GLY A C   1 
ATOM   262  O  O   . GLY A 1 54  ? 34.324 14.211  -9.106  1.00 30.22  ? 108 GLY A O   1 
ATOM   263  N  N   . ALA A 1 55  ? 32.726 15.727  -9.548  1.00 30.14  ? 109 ALA A N   1 
ATOM   264  C  CA  . ALA A 1 55  ? 33.552 16.871  -9.171  1.00 33.38  ? 109 ALA A CA  1 
ATOM   265  C  C   . ALA A 1 55  ? 34.083 16.732  -7.749  1.00 34.66  ? 109 ALA A C   1 
ATOM   266  O  O   . ALA A 1 55  ? 35.261 16.955  -7.474  1.00 34.95  ? 109 ALA A O   1 
ATOM   267  C  CB  . ALA A 1 55  ? 32.757 18.155  -9.311  1.00 34.00  ? 109 ALA A CB  1 
ATOM   268  N  N   . ARG A 1 56  ? 33.198 16.350  -6.844  1.00 35.85  ? 110 ARG A N   1 
ATOM   269  C  CA  . ARG A 1 56  ? 33.553 16.263  -5.442  1.00 39.43  ? 110 ARG A CA  1 
ATOM   270  C  C   . ARG A 1 56  ? 33.857 14.821  -5.036  1.00 35.70  ? 110 ARG A C   1 
ATOM   271  O  O   . ARG A 1 56  ? 34.776 14.561  -4.261  1.00 37.50  ? 110 ARG A O   1 
ATOM   272  C  CB  . ARG A 1 56  ? 32.415 16.840  -4.611  1.00 46.69  ? 110 ARG A CB  1 
ATOM   273  C  CG  . ARG A 1 56  ? 32.547 18.343  -4.376  1.00 54.72  ? 110 ARG A CG  1 
ATOM   274  C  CD  . ARG A 1 56  ? 32.527 18.597  -2.902  1.00 60.79  ? 110 ARG A CD  1 
ATOM   275  N  NE  . ARG A 1 56  ? 31.196 19.078  -2.571  1.00 66.96  ? 110 ARG A NE  1 
ATOM   276  C  CZ  . ARG A 1 56  ? 30.809 19.446  -1.359  1.00 71.98  ? 110 ARG A CZ  1 
ATOM   277  N  NH1 . ARG A 1 56  ? 31.656 19.441  -0.339  1.00 72.96  ? 110 ARG A NH1 1 
ATOM   278  N  NH2 . ARG A 1 56  ? 29.568 19.833  -1.181  1.00 73.56  ? 110 ARG A NH2 1 
ATOM   279  N  N   . SER A 1 57  ? 33.094 13.886  -5.593  1.00 31.98  ? 111 SER A N   1 
ATOM   280  C  CA  . SER A 1 57  ? 33.109 12.490  -5.148  1.00 31.27  ? 111 SER A CA  1 
ATOM   281  C  C   . SER A 1 57  ? 34.019 11.571  -5.952  1.00 31.25  ? 111 SER A C   1 
ATOM   282  O  O   . SER A 1 57  ? 34.160 10.394  -5.615  1.00 31.97  ? 111 SER A O   1 
ATOM   283  C  CB  . SER A 1 57  ? 31.700 11.908  -5.204  1.00 29.99  ? 111 SER A CB  1 
ATOM   284  O  OG  . SER A 1 57  ? 31.223 11.947  -6.536  1.00 29.99  ? 111 SER A OG  1 
ATOM   285  N  N   . PHE A 1 58  ? 34.601 12.076  -7.034  1.00 28.51  ? 112 PHE A N   1 
ATOM   286  C  CA  . PHE A 1 58  ? 35.428 11.220  -7.874  1.00 28.59  ? 112 PHE A CA  1 
ATOM   287  C  C   . PHE A 1 58  ? 36.551 12.010  -8.547  1.00 28.94  ? 112 PHE A C   1 
ATOM   288  O  O   . PHE A 1 58  ? 36.897 11.759  -9.696  1.00 29.27  ? 112 PHE A O   1 
ATOM   289  C  CB  . PHE A 1 58  ? 34.558 10.495  -8.914  1.00 28.64  ? 112 PHE A CB  1 
ATOM   290  C  CG  . PHE A 1 58  ? 35.223 9.293   -9.536  1.00 27.51  ? 112 PHE A CG  1 
ATOM   291  C  CD1 . PHE A 1 58  ? 35.805 8.316   -8.741  1.00 28.07  ? 112 PHE A CD1 1 
ATOM   292  C  CD2 . PHE A 1 58  ? 35.244 9.128   -10.915 1.00 26.44  ? 112 PHE A CD2 1 
ATOM   293  C  CE1 . PHE A 1 58  ? 36.420 7.210   -9.313  1.00 27.56  ? 112 PHE A CE1 1 
ATOM   294  C  CE2 . PHE A 1 58  ? 35.851 8.032   -11.494 1.00 27.18  ? 112 PHE A CE2 1 
ATOM   295  C  CZ  . PHE A 1 58  ? 36.447 7.068   -10.692 1.00 27.11  ? 112 PHE A CZ  1 
ATOM   296  N  N   . GLY A 1 59  ? 37.119 12.961  -7.808  1.00 30.06  ? 113 GLY A N   1 
ATOM   297  C  CA  . GLY A 1 59  ? 38.316 13.667  -8.231  1.00 32.03  ? 113 GLY A CA  1 
ATOM   298  C  C   . GLY A 1 59  ? 38.226 14.395  -9.560  1.00 33.94  ? 113 GLY A C   1 
ATOM   299  O  O   . GLY A 1 59  ? 39.215 14.474  -10.295 1.00 34.06  ? 113 GLY A O   1 
ATOM   300  N  N   . ARG A 1 60  ? 37.046 14.939  -9.853  1.00 33.96  ? 114 ARG A N   1 
ATOM   301  C  CA  . ARG A 1 60  ? 36.776 15.681  -11.090 1.00 36.35  ? 114 ARG A CA  1 
ATOM   302  C  C   . ARG A 1 60  ? 36.918 14.814  -12.340 1.00 35.22  ? 114 ARG A C   1 
ATOM   303  O  O   . ARG A 1 60  ? 37.124 15.319  -13.437 1.00 38.37  ? 114 ARG A O   1 
ATOM   304  C  CB  . ARG A 1 60  ? 37.685 16.914  -11.205 1.00 40.67  ? 114 ARG A CB  1 
ATOM   305  C  CG  . ARG A 1 60  ? 37.661 17.806  -9.979  1.00 45.29  ? 114 ARG A CG  1 
ATOM   306  C  CD  . ARG A 1 60  ? 38.292 19.166  -10.266 1.00 50.42  ? 114 ARG A CD  1 
ATOM   307  N  NE  . ARG A 1 60  ? 37.319 20.108  -10.809 1.00 57.72  ? 114 ARG A NE  1 
ATOM   308  C  CZ  . ARG A 1 60  ? 37.104 20.307  -12.106 1.00 63.36  ? 114 ARG A CZ  1 
ATOM   309  N  NH1 . ARG A 1 60  ? 37.801 19.631  -13.010 1.00 65.74  ? 114 ARG A NH1 1 
ATOM   310  N  NH2 . ARG A 1 60  ? 36.193 21.187  -12.502 1.00 65.45  ? 114 ARG A NH2 1 
ATOM   311  N  N   . LYS A 1 61  ? 36.793 13.502  -12.175 1.00 31.02  ? 115 LYS A N   1 
ATOM   312  C  CA  . LYS A 1 61  ? 36.742 12.604  -13.324 1.00 29.53  ? 115 LYS A CA  1 
ATOM   313  C  C   . LYS A 1 61  ? 35.290 12.311  -13.667 1.00 26.44  ? 115 LYS A C   1 
ATOM   314  O  O   . LYS A 1 61  ? 34.417 12.385  -12.802 1.00 27.24  ? 115 LYS A O   1 
ATOM   315  C  CB  . LYS A 1 61  ? 37.485 11.295  -13.038 1.00 29.57  ? 115 LYS A CB  1 
ATOM   316  C  CG  . LYS A 1 61  ? 38.958 11.491  -12.668 1.00 32.00  ? 115 LYS A CG  1 
ATOM   317  C  CD  . LYS A 1 61  ? 39.586 10.192  -12.159 1.00 36.04  ? 115 LYS A CD  1 
ATOM   318  C  CE  . LYS A 1 61  ? 39.213 9.914   -10.700 1.00 38.35  ? 115 LYS A CE  1 
ATOM   319  N  NZ  . LYS A 1 61  ? 39.797 8.646   -10.184 1.00 41.50  ? 115 LYS A NZ  1 
ATOM   320  N  N   . SER A 1 62  ? 35.029 11.994  -14.931 1.00 25.05  ? 116 SER A N   1 
ATOM   321  C  CA  . SER A 1 62  ? 33.729 11.439  -15.304 1.00 23.68  ? 116 SER A CA  1 
ATOM   322  C  C   . SER A 1 62  ? 33.430 10.211  -14.462 1.00 20.76  ? 116 SER A C   1 
ATOM   323  O  O   . SER A 1 62  ? 34.314 9.398   -14.209 1.00 22.13  ? 116 SER A O   1 
ATOM   324  C  CB  . SER A 1 62  ? 33.689 11.068  -16.787 1.00 23.69  ? 116 SER A CB  1 
ATOM   325  O  OG  . SER A 1 62  ? 32.490 10.370  -17.095 1.00 23.17  ? 116 SER A OG  1 
ATOM   326  N  N   . LEU A 1 63  ? 32.177 10.051  -14.050 1.00 19.73  ? 117 LEU A N   1 
ATOM   327  C  CA  . LEU A 1 63  ? 31.806 8.848   -13.313 1.00 18.85  ? 117 LEU A CA  1 
ATOM   328  C  C   . LEU A 1 63  ? 31.929 7.595   -14.178 1.00 18.87  ? 117 LEU A C   1 
ATOM   329  O  O   . LEU A 1 63  ? 31.957 6.484   -13.650 1.00 19.79  ? 117 LEU A O   1 
ATOM   330  C  CB  . LEU A 1 63  ? 30.386 8.948   -12.762 1.00 19.71  ? 117 LEU A CB  1 
ATOM   331  C  CG  . LEU A 1 63  ? 30.126 10.088  -11.771 1.00 19.63  ? 117 LEU A CG  1 
ATOM   332  C  CD1 . LEU A 1 63  ? 28.714 9.998   -11.225 1.00 21.39  ? 117 LEU A CD1 1 
ATOM   333  C  CD2 . LEU A 1 63  ? 31.153 10.108  -10.628 1.00 20.81  ? 117 LEU A CD2 1 
ATOM   334  N  N   . HIS A 1 64  ? 32.004 7.767   -15.497 1.00 19.36  ? 118 HIS A N   1 
ATOM   335  C  CA  . HIS A 1 64  ? 32.196 6.631   -16.394 1.00 18.78  ? 118 HIS A CA  1 
ATOM   336  C  C   . HIS A 1 64  ? 33.633 6.534   -16.889 1.00 19.62  ? 118 HIS A C   1 
ATOM   337  O  O   . HIS A 1 64  ? 33.930 5.771   -17.804 1.00 21.72  ? 118 HIS A O   1 
ATOM   338  C  CB  . HIS A 1 64  ? 31.230 6.705   -17.579 1.00 17.76  ? 118 HIS A CB  1 
ATOM   339  C  CG  . HIS A 1 64  ? 29.831 6.333   -17.216 1.00 17.05  ? 118 HIS A CG  1 
ATOM   340  N  ND1 . HIS A 1 64  ? 29.504 5.092   -16.708 1.00 16.61  ? 118 HIS A ND1 1 
ATOM   341  C  CD2 . HIS A 1 64  ? 28.669 7.029   -17.278 1.00 17.88  ? 118 HIS A CD2 1 
ATOM   342  C  CE1 . HIS A 1 64  ? 28.208 5.037   -16.479 1.00 16.65  ? 118 HIS A CE1 1 
ATOM   343  N  NE2 . HIS A 1 64  ? 27.676 6.209   -16.805 1.00 17.91  ? 118 HIS A NE2 1 
ATOM   344  N  N   . PHE A 1 65  ? 34.530 7.297   -16.273 1.00 21.01  ? 119 PHE A N   1 
ATOM   345  C  CA  . PHE A 1 65  ? 35.939 7.236   -16.652 1.00 22.34  ? 119 PHE A CA  1 
ATOM   346  C  C   . PHE A 1 65  ? 36.503 5.832   -16.454 1.00 22.63  ? 119 PHE A C   1 
ATOM   347  O  O   . PHE A 1 65  ? 36.327 5.222   -15.391 1.00 22.16  ? 119 PHE A O   1 
ATOM   348  C  CB  . PHE A 1 65  ? 36.756 8.250   -15.849 1.00 25.18  ? 119 PHE A CB  1 
ATOM   349  C  CG  . PHE A 1 65  ? 38.212 8.282   -16.216 1.00 28.85  ? 119 PHE A CG  1 
ATOM   350  C  CD1 . PHE A 1 65  ? 38.628 8.942   -17.358 1.00 31.17  ? 119 PHE A CD1 1 
ATOM   351  C  CD2 . PHE A 1 65  ? 39.166 7.678   -15.410 1.00 29.44  ? 119 PHE A CD2 1 
ATOM   352  C  CE1 . PHE A 1 65  ? 39.964 8.983   -17.704 1.00 33.24  ? 119 PHE A CE1 1 
ATOM   353  C  CE2 . PHE A 1 65  ? 40.515 7.721   -15.753 1.00 30.98  ? 119 PHE A CE2 1 
ATOM   354  C  CZ  . PHE A 1 65  ? 40.906 8.371   -16.897 1.00 32.00  ? 119 PHE A CZ  1 
ATOM   355  N  N   . ILE A 1 66  ? 37.157 5.313   -17.490 1.00 23.75  ? 120 ILE A N   1 
ATOM   356  C  CA  . ILE A 1 66  ? 37.806 4.010   -17.409 1.00 24.54  ? 120 ILE A CA  1 
ATOM   357  C  C   . ILE A 1 66  ? 39.288 4.230   -17.161 1.00 26.33  ? 120 ILE A C   1 
ATOM   358  O  O   . ILE A 1 66  ? 40.026 4.663   -18.044 1.00 27.63  ? 120 ILE A O   1 
ATOM   359  C  CB  . ILE A 1 66  ? 37.592 3.173   -18.683 1.00 26.31  ? 120 ILE A CB  1 
ATOM   360  C  CG1 . ILE A 1 66  ? 36.094 2.929   -18.919 1.00 26.84  ? 120 ILE A CG1 1 
ATOM   361  C  CG2 . ILE A 1 66  ? 38.352 1.857   -18.585 1.00 26.95  ? 120 ILE A CG2 1 
ATOM   362  C  CD1 . ILE A 1 66  ? 35.392 2.240   -17.767 1.00 27.14  ? 120 ILE A CD1 1 
ATOM   363  N  N   . GLY A 1 67  ? 39.708 3.938   -15.938 1.00 27.00  ? 121 GLY A N   1 
ATOM   364  C  CA  . GLY A 1 67  ? 41.071 4.207   -15.521 1.00 27.28  ? 121 GLY A CA  1 
ATOM   365  C  C   . GLY A 1 67  ? 41.659 3.063   -14.724 1.00 27.42  ? 121 GLY A C   1 
ATOM   366  O  O   . GLY A 1 67  ? 41.274 1.909   -14.901 1.00 29.87  ? 121 GLY A O   1 
ATOM   367  N  N   . THR A 1 68  ? 42.586 3.391   -13.832 1.00 27.68  ? 122 THR A N   1 
ATOM   368  C  CA  . THR A 1 68  ? 43.333 2.373   -13.102 1.00 27.99  ? 122 THR A CA  1 
ATOM   369  C  C   . THR A 1 68  ? 42.647 1.920   -11.817 1.00 26.04  ? 122 THR A C   1 
ATOM   370  O  O   . THR A 1 68  ? 43.017 0.900   -11.241 1.00 28.32  ? 122 THR A O   1 
ATOM   371  C  CB  . THR A 1 68  ? 44.745 2.879   -12.758 1.00 30.09  ? 122 THR A CB  1 
ATOM   372  O  OG1 . THR A 1 68  ? 44.649 4.002   -11.871 1.00 32.62  ? 122 THR A OG1 1 
ATOM   373  C  CG2 . THR A 1 68  ? 45.465 3.308   -14.021 1.00 31.79  ? 122 THR A CG2 1 
ATOM   374  N  N   . THR A 1 69  ? 41.668 2.691   -11.358 1.00 25.88  ? 123 THR A N   1 
ATOM   375  C  CA  . THR A 1 69  ? 40.867 2.316   -10.195 1.00 27.09  ? 123 THR A CA  1 
ATOM   376  C  C   . THR A 1 69  ? 39.404 2.302   -10.627 1.00 24.89  ? 123 THR A C   1 
ATOM   377  O  O   . THR A 1 69  ? 39.034 3.016   -11.553 1.00 25.06  ? 123 THR A O   1 
ATOM   378  C  CB  . THR A 1 69  ? 41.075 3.279   -8.998  1.00 31.30  ? 123 THR A CB  1 
ATOM   379  O  OG1 . THR A 1 69  ? 40.647 4.599   -9.351  1.00 33.24  ? 123 THR A OG1 1 
ATOM   380  C  CG2 . THR A 1 69  ? 42.541 3.316   -8.582  1.00 32.31  ? 123 THR A CG2 1 
ATOM   381  N  N   . PRO A 1 70  ? 38.571 1.480   -9.975  1.00 25.05  ? 124 PRO A N   1 
ATOM   382  C  CA  . PRO A 1 70  ? 37.191 1.365   -10.458 1.00 22.75  ? 124 PRO A CA  1 
ATOM   383  C  C   . PRO A 1 70  ? 36.375 2.628   -10.226 1.00 20.96  ? 124 PRO A C   1 
ATOM   384  O  O   . PRO A 1 70  ? 36.468 3.267   -9.168  1.00 22.92  ? 124 PRO A O   1 
ATOM   385  C  CB  . PRO A 1 70  ? 36.624 0.201   -9.636  1.00 23.70  ? 124 PRO A CB  1 
ATOM   386  C  CG  . PRO A 1 70  ? 37.487 0.133   -8.414  1.00 26.95  ? 124 PRO A CG  1 
ATOM   387  C  CD  . PRO A 1 70  ? 38.851 0.560   -8.855  1.00 26.72  ? 124 PRO A CD  1 
ATOM   388  N  N   . ASN A 1 71  ? 35.562 2.986   -11.213 1.00 18.36  ? 125 ASN A N   1 
ATOM   389  C  CA  . ASN A 1 71  ? 34.671 4.120   -11.047 1.00 17.76  ? 125 ASN A CA  1 
ATOM   390  C  C   . ASN A 1 71  ? 33.435 3.668   -10.244 1.00 16.86  ? 125 ASN A C   1 
ATOM   391  O  O   . ASN A 1 71  ? 33.304 2.486   -9.924  1.00 17.61  ? 125 ASN A O   1 
ATOM   392  C  CB  . ASN A 1 71  ? 34.336 4.741   -12.418 1.00 17.71  ? 125 ASN A CB  1 
ATOM   393  C  CG  . ASN A 1 71  ? 33.452 3.871   -13.293 1.00 17.33  ? 125 ASN A CG  1 
ATOM   394  O  OD1 . ASN A 1 71  ? 32.528 3.206   -12.825 1.00 16.94  ? 125 ASN A OD1 1 
ATOM   395  N  ND2 . ASN A 1 71  ? 33.711 3.906   -14.591 1.00 17.83  ? 125 ASN A ND2 1 
ATOM   396  N  N   . PRO A 1 72  ? 32.564 4.602   -9.844  1.00 16.27  ? 126 PRO A N   1 
ATOM   397  C  CA  . PRO A 1 72  ? 31.475 4.184   -8.957  1.00 16.72  ? 126 PRO A CA  1 
ATOM   398  C  C   . PRO A 1 72  ? 30.526 3.165   -9.586  1.00 15.91  ? 126 PRO A C   1 
ATOM   399  O  O   . PRO A 1 72  ? 29.991 2.321   -8.861  1.00 16.02  ? 126 PRO A O   1 
ATOM   400  C  CB  . PRO A 1 72  ? 30.758 5.500   -8.645  1.00 18.19  ? 126 PRO A CB  1 
ATOM   401  C  CG  . PRO A 1 72  ? 31.837 6.532   -8.756  1.00 18.74  ? 126 PRO A CG  1 
ATOM   402  C  CD  . PRO A 1 72  ? 32.709 6.070   -9.888  1.00 18.66  ? 126 PRO A CD  1 
ATOM   403  N  N   . TYR A 1 73  ? 30.344 3.199   -10.902 1.00 15.53  ? 127 TYR A N   1 
ATOM   404  C  CA  . TYR A 1 73  ? 29.508 2.188   -11.546 1.00 15.99  ? 127 TYR A CA  1 
ATOM   405  C  C   . TYR A 1 73  ? 30.144 0.818   -11.431 1.00 16.36  ? 127 TYR A C   1 
ATOM   406  O  O   . TYR A 1 73  ? 29.476 -0.144  -11.029 1.00 15.98  ? 127 TYR A O   1 
ATOM   407  C  CB  . TYR A 1 73  ? 29.254 2.548   -13.018 1.00 16.35  ? 127 TYR A CB  1 
ATOM   408  C  CG  . TYR A 1 73  ? 28.321 3.733   -13.154 1.00 15.33  ? 127 TYR A CG  1 
ATOM   409  C  CD1 . TYR A 1 73  ? 26.948 3.550   -13.211 1.00 15.58  ? 127 TYR A CD1 1 
ATOM   410  C  CD2 . TYR A 1 73  ? 28.811 5.031   -13.199 1.00 16.30  ? 127 TYR A CD2 1 
ATOM   411  C  CE1 . TYR A 1 73  ? 26.082 4.626   -13.311 1.00 15.94  ? 127 TYR A CE1 1 
ATOM   412  C  CE2 . TYR A 1 73  ? 27.954 6.103   -13.295 1.00 16.75  ? 127 TYR A CE2 1 
ATOM   413  C  CZ  . TYR A 1 73  ? 26.589 5.890   -13.358 1.00 15.77  ? 127 TYR A CZ  1 
ATOM   414  O  OH  . TYR A 1 73  ? 25.705 6.954   -13.456 1.00 17.60  ? 127 TYR A OH  1 
ATOM   415  N  N   . GLN A 1 74  ? 31.432 0.731   -11.751 1.00 16.08  ? 128 GLN A N   1 
ATOM   416  C  CA  . GLN A 1 74  ? 32.162 -0.535  -11.652 1.00 16.03  ? 128 GLN A CA  1 
ATOM   417  C  C   . GLN A 1 74  ? 32.147 -1.059  -10.222 1.00 15.41  ? 128 GLN A C   1 
ATOM   418  O  O   . GLN A 1 74  ? 31.922 -2.251  -9.999  1.00 17.42  ? 128 GLN A O   1 
ATOM   419  C  CB  . GLN A 1 74  ? 33.597 -0.352  -12.148 1.00 15.89  ? 128 GLN A CB  1 
ATOM   420  C  CG  . GLN A 1 74  ? 33.679 0.005   -13.633 1.00 18.14  ? 128 GLN A CG  1 
ATOM   421  C  CD  . GLN A 1 74  ? 35.076 0.399   -14.054 1.00 18.42  ? 128 GLN A CD  1 
ATOM   422  O  OE1 . GLN A 1 74  ? 35.688 1.296   -13.469 1.00 19.76  ? 128 GLN A OE1 1 
ATOM   423  N  NE2 . GLN A 1 74  ? 35.594 -0.270  -15.076 1.00 20.48  ? 128 GLN A NE2 1 
ATOM   424  N  N   . GLN A 1 75  ? 32.377 -0.201  -9.260  1.00 16.74  ? 129 GLN A N   1 
ATOM   425  C  CA  . GLN A 1 75  ? 32.353 -0.611  -7.881  1.00 17.04  ? 129 GLN A CA  1 
ATOM   426  C  C   . GLN A 1 75  ? 30.987 -1.119  -7.429  1.00 15.42  ? 129 GLN A C   1 
ATOM   427  O  O   . GLN A 1 75  ? 30.900 -2.108  -6.789  1.00 17.27  ? 129 GLN A O   1 
ATOM   428  C  CB  . GLN A 1 75  ? 32.737 0.548   -6.981  1.00 19.48  ? 129 GLN A CB  1 
ATOM   429  C  CG  . GLN A 1 75  ? 34.176 0.995   -7.027  1.00 22.84  ? 129 GLN A CG  1 
ATOM   430  C  CD  . GLN A 1 75  ? 34.427 2.220   -6.162  1.00 27.47  ? 129 GLN A CD  1 
ATOM   431  O  OE1 . GLN A 1 75  ? 34.412 2.118   -5.005  1.00 29.18  ? 129 GLN A OE1 1 
ATOM   432  N  NE2 . GLN A 1 75  ? 34.659 3.373   -6.780  1.00 31.19  ? 129 GLN A NE2 1 
ATOM   433  N  N   . ALA A 1 76  ? 29.923 -0.399  -7.744  1.00 16.19  ? 130 ALA A N   1 
ATOM   434  C  CA  . ALA A 1 76  ? 28.591 -0.819  -7.329  1.00 16.16  ? 130 ALA A CA  1 
ATOM   435  C  C   . ALA A 1 76  ? 28.198 -2.151  -7.949  1.00 15.94  ? 130 ALA A C   1 
ATOM   436  O  O   . ALA A 1 76  ? 27.636 -3.011  -7.276  1.00 17.20  ? 130 ALA A O   1 
ATOM   437  C  CB  . ALA A 1 76  ? 27.569 0.255   -7.684  1.00 18.69  ? 130 ALA A CB  1 
ATOM   438  N  N   . ILE A 1 77  ? 28.480 -2.336  -9.218  1.00 16.49  ? 131 ILE A N   1 
ATOM   439  C  CA  . ILE A 1 77  ? 28.248 -3.602  -9.886  1.00 16.77  ? 131 ILE A CA  1 
ATOM   440  C  C   . ILE A 1 77  ? 29.023 -4.769  -9.263  1.00 16.28  ? 131 ILE A C   1 
ATOM   441  O  O   . ILE A 1 77  ? 28.492 -5.779  -9.011  1.00 17.07  ? 131 ILE A O   1 
ATOM   442  C  CB  . ILE A 1 77  ? 28.557 -3.489  -11.398 1.00 17.41  ? 131 ILE A CB  1 
ATOM   443  C  CG1 . ILE A 1 77  ? 27.547 -2.547  -12.086 1.00 19.16  ? 131 ILE A CG1 1 
ATOM   444  C  CG2 . ILE A 1 77  ? 28.539 -4.859  -12.072 1.00 18.65  ? 131 ILE A CG2 1 
ATOM   445  C  CD1 . ILE A 1 77  ? 27.948 -2.169  -13.495 1.00 21.28  ? 131 ILE A CD1 1 
ATOM   446  N  N   . SER A 1 78  ? 30.294 -4.548  -9.007  1.00 15.96  ? 132 SER A N   1 
ATOM   447  C  CA  . SER A 1 78  ? 31.134 -5.555  -8.393  1.00 16.07  ? 132 SER A CA  1 
ATOM   448  C  C   . SER A 1 78  ? 30.615 -5.950  -7.042  1.00 17.01  ? 132 SER A C   1 
ATOM   449  O  O   . SER A 1 78  ? 30.562 -7.082  -6.724  1.00 17.41  ? 132 SER A O   1 
ATOM   450  C  CB  . SER A 1 78  ? 32.536 -5.026  -8.161  1.00 19.11  ? 132 SER A CB  1 
ATOM   451  O  OG  . SER A 1 78  ? 33.252 -4.981  -9.321  1.00 27.00  ? 132 SER A OG  1 
ATOM   452  N  N   . ILE A 1 79  ? 30.263 -4.975  -6.248  1.00 15.70  ? 133 ILE A N   1 
ATOM   453  C  CA  . ILE A 1 79  ? 29.837 -5.282  -4.891  1.00 15.74  ? 133 ILE A CA  1 
ATOM   454  C  C   . ILE A 1 79  ? 28.481 -5.989  -4.858  1.00 14.60  ? 133 ILE A C   1 
ATOM   455  O  O   . ILE A 1 79  ? 28.346 -7.045  -4.218  1.00 15.55  ? 133 ILE A O   1 
ATOM   456  C  CB  . ILE A 1 79  ? 29.774 -3.999  -4.034  1.00 15.72  ? 133 ILE A CB  1 
ATOM   457  C  CG1 . ILE A 1 79  ? 31.178 -3.429  -3.817  1.00 17.26  ? 133 ILE A CG1 1 
ATOM   458  C  CG2 . ILE A 1 79  ? 29.105 -4.279  -2.675  1.00 17.13  ? 133 ILE A CG2 1 
ATOM   459  C  CD1 . ILE A 1 79  ? 31.167 -1.997  -3.326  1.00 19.00  ? 133 ILE A CD1 1 
ATOM   460  N  N   . ILE A 1 80  ? 27.481 -5.454  -5.556  1.00 15.22  ? 134 ILE A N   1 
ATOM   461  C  CA  . ILE A 1 80  ? 26.162 -6.083  -5.547  1.00 15.68  ? 134 ILE A CA  1 
ATOM   462  C  C   . ILE A 1 80  ? 26.193 -7.406  -6.312  1.00 15.46  ? 134 ILE A C   1 
ATOM   463  O  O   . ILE A 1 80  ? 25.585 -8.399  -5.879  1.00 16.01  ? 134 ILE A O   1 
ATOM   464  C  CB  . ILE A 1 80  ? 25.082 -5.156  -6.144  1.00 15.52  ? 134 ILE A CB  1 
ATOM   465  C  CG1 . ILE A 1 80  ? 24.988 -3.856  -5.345  1.00 17.51  ? 134 ILE A CG1 1 
ATOM   466  C  CG2 . ILE A 1 80  ? 23.738 -5.885  -6.235  1.00 17.07  ? 134 ILE A CG2 1 
ATOM   467  C  CD1 . ILE A 1 80  ? 24.662 -4.057  -3.896  1.00 19.46  ? 134 ILE A CD1 1 
ATOM   468  N  N   . GLY A 1 81  ? 26.918 -7.435  -7.429  1.00 15.40  ? 135 GLY A N   1 
ATOM   469  C  CA  . GLY A 1 81  ? 27.038 -8.654  -8.210  1.00 16.33  ? 135 GLY A CA  1 
ATOM   470  C  C   . GLY A 1 81  ? 27.642 -9.773  -7.387  1.00 16.34  ? 135 GLY A C   1 
ATOM   471  O  O   . GLY A 1 81  ? 27.140 -10.900 -7.396  1.00 18.29  ? 135 GLY A O   1 
ATOM   472  N  N   . LYS A 1 82  ? 28.722 -9.482  -6.667  1.00 15.67  ? 136 LYS A N   1 
ATOM   473  C  CA  . LYS A 1 82  ? 29.325 -10.516 -5.843  1.00 16.67  ? 136 LYS A CA  1 
ATOM   474  C  C   . LYS A 1 82  ? 28.379 -10.949 -4.722  1.00 16.87  ? 136 LYS A C   1 
ATOM   475  O  O   . LYS A 1 82  ? 28.216 -12.149 -4.465  1.00 18.19  ? 136 LYS A O   1 
ATOM   476  C  CB  . LYS A 1 82  ? 30.664 -10.057 -5.250  1.00 18.98  ? 136 LYS A CB  1 
ATOM   477  C  CG  . LYS A 1 82  ? 31.301 -11.100 -4.337  1.00 23.46  ? 136 LYS A CG  1 
ATOM   478  C  CD  . LYS A 1 82  ? 32.790 -10.840 -4.093  1.00 30.51  ? 136 LYS A CD  1 
ATOM   479  C  CE  . LYS A 1 82  ? 33.404 -11.863 -3.121  1.00 34.77  ? 136 LYS A CE  1 
ATOM   480  N  NZ  . LYS A 1 82  ? 33.680 -11.328 -1.744  1.00 37.51  ? 136 LYS A NZ  1 
ATOM   481  N  N   . THR A 1 83  ? 27.732 -9.986  -4.079  1.00 15.81  ? 137 THR A N   1 
ATOM   482  C  CA  . THR A 1 83  ? 26.885 -10.295 -2.936  1.00 15.37  ? 137 THR A CA  1 
ATOM   483  C  C   . THR A 1 83  ? 25.737 -11.235 -3.327  1.00 16.86  ? 137 THR A C   1 
ATOM   484  O  O   . THR A 1 83  ? 25.397 -12.167 -2.588  1.00 17.00  ? 137 THR A O   1 
ATOM   485  C  CB  . THR A 1 83  ? 26.307 -9.014  -2.307  1.00 15.85  ? 137 THR A CB  1 
ATOM   486  O  OG1 . THR A 1 83  ? 27.372 -8.131  -1.906  1.00 17.87  ? 137 THR A OG1 1 
ATOM   487  C  CG2 . THR A 1 83  ? 25.464 -9.350  -1.088  1.00 17.27  ? 137 THR A CG2 1 
ATOM   488  N  N   . LEU A 1 84  ? 25.178 -11.031 -4.513  1.00 15.86  ? 138 LEU A N   1 
ATOM   489  C  CA  . LEU A 1 84  ? 24.002 -11.788 -4.930  1.00 15.63  ? 138 LEU A CA  1 
ATOM   490  C  C   . LEU A 1 84  ? 24.325 -13.011 -5.772  1.00 15.78  ? 138 LEU A C   1 
ATOM   491  O  O   . LEU A 1 84  ? 23.418 -13.783 -6.089  1.00 17.78  ? 138 LEU A O   1 
ATOM   492  C  CB  . LEU A 1 84  ? 23.048 -10.880 -5.704  1.00 16.05  ? 138 LEU A CB  1 
ATOM   493  C  CG  . LEU A 1 84  ? 22.322 -9.827  -4.869  1.00 16.86  ? 138 LEU A CG  1 
ATOM   494  C  CD1 . LEU A 1 84  ? 21.586 -8.850  -5.771  1.00 17.61  ? 138 LEU A CD1 1 
ATOM   495  C  CD2 . LEU A 1 84  ? 21.360 -10.496 -3.890  1.00 17.65  ? 138 LEU A CD2 1 
ATOM   496  N  N   . SER A 1 85  ? 25.594 -13.213 -6.114  1.00 16.19  ? 139 SER A N   1 
ATOM   497  C  CA  . SER A 1 85  ? 25.956 -14.264 -7.075  1.00 18.64  ? 139 SER A CA  1 
ATOM   498  C  C   . SER A 1 85  ? 25.509 -15.674 -6.675  1.00 19.90  ? 139 SER A C   1 
ATOM   499  O  O   . SER A 1 85  ? 25.059 -16.432 -7.535  1.00 20.78  ? 139 SER A O   1 
ATOM   500  C  CB  . SER A 1 85  ? 27.465 -14.261 -7.327  1.00 21.20  ? 139 SER A CB  1 
ATOM   501  O  OG  . SER A 1 85  ? 28.220 -14.493 -6.153  1.00 26.33  ? 139 SER A OG  1 
ATOM   502  N  N   . VAL A 1 86  ? 25.604 -16.045 -5.398  1.00 19.68  ? 140 VAL A N   1 
ATOM   503  C  CA  . VAL A 1 86  ? 25.304 -17.442 -5.037  1.00 19.63  ? 140 VAL A CA  1 
ATOM   504  C  C   . VAL A 1 86  ? 23.828 -17.795 -5.156  1.00 19.37  ? 140 VAL A C   1 
ATOM   505  O  O   . VAL A 1 86  ? 23.485 -18.982 -5.189  1.00 22.35  ? 140 VAL A O   1 
ATOM   506  C  CB  . VAL A 1 86  ? 25.761 -17.803 -3.601  1.00 20.88  ? 140 VAL A CB  1 
ATOM   507  C  CG1 . VAL A 1 86  ? 27.277 -17.647 -3.442  1.00 24.16  ? 140 VAL A CG1 1 
ATOM   508  C  CG2 . VAL A 1 86  ? 24.998 -17.000 -2.561  1.00 21.87  ? 140 VAL A CG2 1 
ATOM   509  N  N   . PHE A 1 87  ? 22.955 -16.795 -5.211  1.00 18.58  ? 141 PHE A N   1 
ATOM   510  C  CA  . PHE A 1 87  ? 21.518 -17.035 -5.319  1.00 18.98  ? 141 PHE A CA  1 
ATOM   511  C  C   . PHE A 1 87  ? 21.079 -17.237 -6.767  1.00 20.88  ? 141 PHE A C   1 
ATOM   512  O  O   . PHE A 1 87  ? 19.943 -17.619 -7.021  1.00 20.87  ? 141 PHE A O   1 
ATOM   513  C  CB  . PHE A 1 87  ? 20.728 -15.869 -4.709  1.00 19.64  ? 141 PHE A CB  1 
ATOM   514  C  CG  . PHE A 1 87  ? 21.111 -15.558 -3.296  1.00 19.34  ? 141 PHE A CG  1 
ATOM   515  C  CD1 . PHE A 1 87  ? 20.602 -16.313 -2.253  1.00 21.00  ? 141 PHE A CD1 1 
ATOM   516  C  CD2 . PHE A 1 87  ? 21.965 -14.504 -3.001  1.00 20.00  ? 141 PHE A CD2 1 
ATOM   517  C  CE1 . PHE A 1 87  ? 20.959 -16.043 -0.947  1.00 21.85  ? 141 PHE A CE1 1 
ATOM   518  C  CE2 . PHE A 1 87  ? 22.319 -14.228 -1.681  1.00 19.22  ? 141 PHE A CE2 1 
ATOM   519  C  CZ  . PHE A 1 87  ? 21.811 -15.003 -0.658  1.00 21.06  ? 141 PHE A CZ  1 
ATOM   520  N  N   . ASP A 1 88  ? 21.975 -16.982 -7.697  1.00 22.11  ? 142 ASP A N   1 
ATOM   521  C  CA  . ASP A 1 88  ? 21.679 -16.990 -9.129  1.00 22.60  ? 142 ASP A CA  1 
ATOM   522  C  C   . ASP A 1 88  ? 22.028 -18.315 -9.780  1.00 24.90  ? 142 ASP A C   1 
ATOM   523  O  O   . ASP A 1 88  ? 23.140 -18.561 -10.070 1.00 26.63  ? 142 ASP A O   1 
ATOM   524  C  CB  . ASP A 1 88  ? 22.513 -15.896 -9.779  1.00 23.84  ? 142 ASP A CB  1 
ATOM   525  C  CG  . ASP A 1 88  ? 21.996 -15.446 -11.131 1.00 28.11  ? 142 ASP A CG  1 
ATOM   526  O  OD1 . ASP A 1 88  ? 21.279 -16.170 -11.803 1.00 28.25  ? 142 ASP A OD1 1 
ATOM   527  O  OD2 . ASP A 1 88  ? 22.356 -14.334 -11.524 1.00 31.23  ? 142 ASP A OD2 1 
ATOM   528  N  N   . GLU A 1 89  ? 21.014 -19.098 -10.039 1.00 27.46  ? 143 GLU A N   1 
ATOM   529  C  CA  . GLU A 1 89  ? 21.190 -20.444 -10.566 1.00 30.95  ? 143 GLU A CA  1 
ATOM   530  C  C   . GLU A 1 89  ? 21.811 -20.427 -11.960 1.00 26.80  ? 143 GLU A C   1 
ATOM   531  O  O   . GLU A 1 89  ? 22.839 -21.075 -12.204 1.00 27.87  ? 143 GLU A O   1 
ATOM   532  C  CB  . GLU A 1 89  ? 19.848 -21.176 -10.595 1.00 41.15  ? 143 GLU A CB  1 
ATOM   533  C  CG  . GLU A 1 89  ? 19.464 -21.775 -9.260  1.00 53.27  ? 143 GLU A CG  1 
ATOM   534  C  CD  . GLU A 1 89  ? 18.374 -22.827 -9.360  1.00 63.03  ? 143 GLU A CD  1 
ATOM   535  O  OE1 . GLU A 1 89  ? 17.908 -23.097 -10.484 1.00 66.43  ? 143 GLU A OE1 1 
ATOM   536  O  OE2 . GLU A 1 89  ? 17.977 -23.377 -8.311  1.00 67.89  ? 143 GLU A OE2 1 
ATOM   537  N  N   . ASP A 1 90  ? 21.206 -19.675 -12.873 1.00 23.85  ? 144 ASP A N   1 
ATOM   538  C  CA  . ASP A 1 90  ? 21.690 -19.713 -14.240 1.00 22.14  ? 144 ASP A CA  1 
ATOM   539  C  C   . ASP A 1 90  ? 22.870 -18.770 -14.471 1.00 19.15  ? 144 ASP A C   1 
ATOM   540  O  O   . ASP A 1 90  ? 23.535 -18.859 -15.491 1.00 19.30  ? 144 ASP A O   1 
ATOM   541  C  CB  . ASP A 1 90  ? 20.534 -19.453 -15.229 1.00 22.43  ? 144 ASP A CB  1 
ATOM   542  C  CG  . ASP A 1 90  ? 19.974 -18.034 -15.193 1.00 23.63  ? 144 ASP A CG  1 
ATOM   543  O  OD1 . ASP A 1 90  ? 20.532 -17.121 -14.546 1.00 22.80  ? 144 ASP A OD1 1 
ATOM   544  O  OD2 . ASP A 1 90  ? 18.920 -17.827 -15.841 1.00 27.14  ? 144 ASP A OD2 1 
ATOM   545  N  N   . ASN A 1 91  ? 23.141 -17.902 -13.493 1.00 18.57  ? 145 ASN A N   1 
ATOM   546  C  CA  . ASN A 1 91  ? 24.228 -16.907 -13.544 1.00 18.72  ? 145 ASN A CA  1 
ATOM   547  C  C   . ASN A 1 91  ? 24.171 -15.968 -14.750 1.00 19.12  ? 145 ASN A C   1 
ATOM   548  O  O   . ASN A 1 91  ? 25.179 -15.380 -15.141 1.00 21.27  ? 145 ASN A O   1 
ATOM   549  C  CB  . ASN A 1 91  ? 25.597 -17.594 -13.503 1.00 21.33  ? 145 ASN A CB  1 
ATOM   550  C  CG  . ASN A 1 91  ? 26.666 -16.715 -12.880 1.00 23.84  ? 145 ASN A CG  1 
ATOM   551  O  OD1 . ASN A 1 91  ? 26.376 -15.912 -11.991 1.00 27.33  ? 145 ASN A OD1 1 
ATOM   552  N  ND2 . ASN A 1 91  ? 27.897 -16.833 -13.367 1.00 24.27  ? 145 ASN A ND2 1 
ATOM   553  N  N   . LEU A 1 92  ? 22.986 -15.803 -15.318 1.00 17.77  ? 146 LEU A N   1 
ATOM   554  C  CA  . LEU A 1 92  ? 22.803 -14.903 -16.446 1.00 19.65  ? 146 LEU A CA  1 
ATOM   555  C  C   . LEU A 1 92  ? 22.351 -13.563 -15.934 1.00 17.65  ? 146 LEU A C   1 
ATOM   556  O  O   . LEU A 1 92  ? 21.368 -13.487 -15.186 1.00 19.86  ? 146 LEU A O   1 
ATOM   557  C  CB  . LEU A 1 92  ? 21.774 -15.456 -17.415 1.00 20.03  ? 146 LEU A CB  1 
ATOM   558  C  CG  . LEU A 1 92  ? 22.143 -16.833 -17.959 1.00 22.80  ? 146 LEU A CG  1 
ATOM   559  C  CD1 . LEU A 1 92  ? 21.064 -17.335 -18.879 1.00 24.55  ? 146 LEU A CD1 1 
ATOM   560  C  CD2 . LEU A 1 92  ? 23.472 -16.790 -18.680 1.00 24.50  ? 146 LEU A CD2 1 
ATOM   561  N  N   . ILE A 1 93  ? 23.066 -12.512 -16.327 1.00 15.30  ? 147 ILE A N   1 
ATOM   562  C  CA  . ILE A 1 93  ? 22.743 -11.173 -15.864 1.00 15.89  ? 147 ILE A CA  1 
ATOM   563  C  C   . ILE A 1 93  ? 22.459 -10.236 -17.030 1.00 15.69  ? 147 ILE A C   1 
ATOM   564  O  O   . ILE A 1 93  ? 23.396 -9.702  -17.645 1.00 16.05  ? 147 ILE A O   1 
ATOM   565  C  CB  . ILE A 1 93  ? 23.875 -10.576 -15.024 1.00 16.86  ? 147 ILE A CB  1 
ATOM   566  C  CG1 . ILE A 1 93  ? 24.239 -11.507 -13.873 1.00 19.65  ? 147 ILE A CG1 1 
ATOM   567  C  CG2 . ILE A 1 93  ? 23.480 -9.205  -14.494 1.00 17.25  ? 147 ILE A CG2 1 
ATOM   568  C  CD1 . ILE A 1 93  ? 25.402 -11.021 -13.064 1.00 21.89  ? 147 ILE A CD1 1 
ATOM   569  N  N   . PRO A 1 94  ? 21.172 -10.014 -17.326 1.00 16.07  ? 148 PRO A N   1 
ATOM   570  C  CA  . PRO A 1 94  ? 20.845 -8.999  -18.334 1.00 15.26  ? 148 PRO A CA  1 
ATOM   571  C  C   . PRO A 1 94  ? 21.361 -7.646  -17.872 1.00 14.41  ? 148 PRO A C   1 
ATOM   572  O  O   . PRO A 1 94  ? 21.231 -7.302  -16.698 1.00 15.77  ? 148 PRO A O   1 
ATOM   573  C  CB  . PRO A 1 94  ? 19.315 -9.034  -18.392 1.00 16.08  ? 148 PRO A CB  1 
ATOM   574  C  CG  . PRO A 1 94  ? 18.944 -10.410 -17.856 1.00 17.01  ? 148 PRO A CG  1 
ATOM   575  C  CD  . PRO A 1 94  ? 19.962 -10.656 -16.780 1.00 16.13  ? 148 PRO A CD  1 
ATOM   576  N  N   . CYS A 1 95  ? 21.975 -6.907  -18.784 1.00 15.24  ? 149 CYS A N   1 
ATOM   577  C  CA  . CYS A 1 95  ? 22.588 -5.624  -18.445 1.00 15.63  ? 149 CYS A CA  1 
ATOM   578  C  C   . CYS A 1 95  ? 22.347 -4.622  -19.562 1.00 13.97  ? 149 CYS A C   1 
ATOM   579  O  O   . CYS A 1 95  ? 22.599 -4.912  -20.749 1.00 15.87  ? 149 CYS A O   1 
ATOM   580  C  CB  . CYS A 1 95  ? 24.089 -5.791  -18.190 1.00 18.39  ? 149 CYS A CB  1 
ATOM   581  S  SG  . CYS A 1 95  ? 24.950 -4.240  -17.821 1.00 21.97  ? 149 CYS A SG  1 
ATOM   582  N  N   . TYR A 1 96  ? 21.881 -3.445  -19.164 1.00 14.20  ? 150 TYR A N   1 
ATOM   583  C  CA  . TYR A 1 96  ? 21.411 -2.426  -20.110 1.00 13.73  ? 150 TYR A CA  1 
ATOM   584  C  C   . TYR A 1 96  ? 21.890 -1.051  -19.755 1.00 13.61  ? 150 TYR A C   1 
ATOM   585  O  O   . TYR A 1 96  ? 22.105 -0.756  -18.580 1.00 16.76  ? 150 TYR A O   1 
ATOM   586  C  CB  . TYR A 1 96  ? 19.874 -2.411  -20.167 1.00 15.16  ? 150 TYR A CB  1 
ATOM   587  C  CG  . TYR A 1 96  ? 19.308 -3.761  -20.502 1.00 14.74  ? 150 TYR A CG  1 
ATOM   588  C  CD1 . TYR A 1 96  ? 19.239 -4.189  -21.819 1.00 16.14  ? 150 TYR A CD1 1 
ATOM   589  C  CD2 . TYR A 1 96  ? 18.889 -4.625  -19.499 1.00 15.36  ? 150 TYR A CD2 1 
ATOM   590  C  CE1 . TYR A 1 96  ? 18.766 -5.440  -22.135 1.00 16.27  ? 150 TYR A CE1 1 
ATOM   591  C  CE2 . TYR A 1 96  ? 18.388 -5.881  -19.811 1.00 17.16  ? 150 TYR A CE2 1 
ATOM   592  C  CZ  . TYR A 1 96  ? 18.333 -6.274  -21.131 1.00 17.14  ? 150 TYR A CZ  1 
ATOM   593  O  OH  . TYR A 1 96  ? 17.848 -7.524  -21.477 1.00 18.36  ? 150 TYR A OH  1 
ATOM   594  N  N   . GLY A 1 97  ? 22.035 -0.215  -20.777 1.00 14.32  ? 151 GLY A N   1 
ATOM   595  C  CA  . GLY A 1 97  ? 22.284 1.198   -20.574 1.00 14.39  ? 151 GLY A CA  1 
ATOM   596  C  C   . GLY A 1 97  ? 21.088 2.012   -21.021 1.00 15.58  ? 151 GLY A C   1 
ATOM   597  O  O   . GLY A 1 97  ? 20.283 1.565   -21.848 1.00 16.10  ? 151 GLY A O   1 
ATOM   598  N  N   . PHE A 1 98  ? 20.982 3.226   -20.486 1.00 14.73  ? 152 PHE A N   1 
ATOM   599  C  CA  . PHE A 1 98  ? 19.926 4.138   -20.887 1.00 14.61  ? 152 PHE A CA  1 
ATOM   600  C  C   . PHE A 1 98  ? 20.446 5.571   -20.787 1.00 14.52  ? 152 PHE A C   1 
ATOM   601  O  O   . PHE A 1 98  ? 21.213 5.898   -19.896 1.00 15.57  ? 152 PHE A O   1 
ATOM   602  C  CB  . PHE A 1 98  ? 18.649 3.948   -20.039 1.00 15.38  ? 152 PHE A CB  1 
ATOM   603  C  CG  . PHE A 1 98  ? 18.862 4.106   -18.559 1.00 15.26  ? 152 PHE A CG  1 
ATOM   604  C  CD1 . PHE A 1 98  ? 19.200 3.012   -17.769 1.00 16.00  ? 152 PHE A CD1 1 
ATOM   605  C  CD2 . PHE A 1 98  ? 18.721 5.350   -17.958 1.00 16.43  ? 152 PHE A CD2 1 
ATOM   606  C  CE1 . PHE A 1 98  ? 19.397 3.159   -16.420 1.00 16.87  ? 152 PHE A CE1 1 
ATOM   607  C  CE2 . PHE A 1 98  ? 18.917 5.504   -16.601 1.00 17.76  ? 152 PHE A CE2 1 
ATOM   608  C  CZ  . PHE A 1 98  ? 19.265 4.400   -15.825 1.00 17.48  ? 152 PHE A CZ  1 
ATOM   609  N  N   . GLY A 1 99  ? 20.024 6.420   -21.716 1.00 14.98  ? 153 GLY A N   1 
ATOM   610  C  CA  . GLY A 1 99  ? 20.361 7.829   -21.651 1.00 15.46  ? 153 GLY A CA  1 
ATOM   611  C  C   . GLY A 1 99  ? 21.484 8.289   -22.556 1.00 16.03  ? 153 GLY A C   1 
ATOM   612  O  O   . GLY A 1 99  ? 21.872 9.455   -22.499 1.00 16.86  ? 153 GLY A O   1 
ATOM   613  N  N   . ASP A 1 100 ? 22.025 7.391   -23.371 1.00 16.58  ? 154 ASP A N   1 
ATOM   614  C  CA  . ASP A 1 100 ? 22.958 7.779   -24.420 1.00 16.98  ? 154 ASP A CA  1 
ATOM   615  C  C   . ASP A 1 100 ? 22.212 8.263   -25.653 1.00 15.93  ? 154 ASP A C   1 
ATOM   616  O  O   . ASP A 1 100 ? 20.984 8.281   -25.671 1.00 17.15  ? 154 ASP A O   1 
ATOM   617  C  CB  . ASP A 1 100 ? 23.855 6.610   -24.808 1.00 17.92  ? 154 ASP A CB  1 
ATOM   618  C  CG  . ASP A 1 100 ? 23.108 5.568   -25.613 1.00 17.65  ? 154 ASP A CG  1 
ATOM   619  O  OD1 . ASP A 1 100 ? 22.055 5.114   -25.128 1.00 18.77  ? 154 ASP A OD1 1 
ATOM   620  O  OD2 . ASP A 1 100 ? 23.542 5.233   -26.732 1.00 19.52  ? 154 ASP A OD2 1 
ATOM   621  N  N   . ALA A 1 101 ? 22.954 8.624   -26.694 1.00 17.81  ? 155 ALA A N   1 
ATOM   622  C  CA  . ALA A 1 101 ? 22.353 9.186   -27.888 1.00 19.52  ? 155 ALA A CA  1 
ATOM   623  C  C   . ALA A 1 101 ? 21.419 8.214   -28.613 1.00 18.47  ? 155 ALA A C   1 
ATOM   624  O  O   . ALA A 1 101 ? 20.506 8.646   -29.328 1.00 21.20  ? 155 ALA A O   1 
ATOM   625  C  CB  . ALA A 1 101 ? 23.443 9.671   -28.832 1.00 19.78  ? 155 ALA A CB  1 
ATOM   626  N  N   . THR A 1 102 ? 21.617 6.912   -28.423 1.00 17.85  ? 156 THR A N   1 
ATOM   627  C  CA  . THR A 1 102 ? 20.785 5.942   -29.139 1.00 18.39  ? 156 THR A CA  1 
ATOM   628  C  C   . THR A 1 102 ? 19.488 5.637   -28.404 1.00 18.55  ? 156 THR A C   1 
ATOM   629  O  O   . THR A 1 102 ? 18.574 5.066   -28.996 1.00 21.25  ? 156 THR A O   1 
ATOM   630  C  CB  . THR A 1 102 ? 21.523 4.600   -29.405 1.00 19.84  ? 156 THR A CB  1 
ATOM   631  O  OG1 . THR A 1 102 ? 21.701 3.863   -28.187 1.00 20.02  ? 156 THR A OG1 1 
ATOM   632  C  CG2 . THR A 1 102 ? 22.867 4.838   -30.096 1.00 21.92  ? 156 THR A CG2 1 
ATOM   633  N  N   . THR A 1 103 ? 19.396 6.001   -27.123 1.00 17.90  ? 157 THR A N   1 
ATOM   634  C  CA  . THR A 1 103 ? 18.217 5.641   -26.344 1.00 16.59  ? 157 THR A CA  1 
ATOM   635  C  C   . THR A 1 103 ? 17.456 6.803   -25.723 1.00 17.25  ? 157 THR A C   1 
ATOM   636  O  O   . THR A 1 103 ? 16.251 6.676   -25.490 1.00 18.73  ? 157 THR A O   1 
ATOM   637  C  CB  . THR A 1 103 ? 18.579 4.673   -25.200 1.00 17.46  ? 157 THR A CB  1 
ATOM   638  O  OG1 . THR A 1 103 ? 19.586 5.258   -24.360 1.00 17.97  ? 157 THR A OG1 1 
ATOM   639  C  CG2 . THR A 1 103 ? 19.077 3.328   -25.743 1.00 18.21  ? 157 THR A CG2 1 
ATOM   640  N  N   . HIS A 1 104 ? 18.151 7.905   -25.442 1.00 17.80  ? 158 HIS A N   1 
ATOM   641  C  CA  . HIS A 1 104 ? 17.547 9.064   -24.772 1.00 18.37  ? 158 HIS A CA  1 
ATOM   642  C  C   . HIS A 1 104 ? 16.727 8.586   -23.571 1.00 17.26  ? 158 HIS A C   1 
ATOM   643  O  O   . HIS A 1 104 ? 17.251 7.839   -22.758 1.00 18.15  ? 158 HIS A O   1 
ATOM   644  C  CB  . HIS A 1 104 ? 16.729 9.890   -25.783 1.00 18.74  ? 158 HIS A CB  1 
ATOM   645  C  CG  . HIS A 1 104 ? 17.572 10.432  -26.898 1.00 21.25  ? 158 HIS A CG  1 
ATOM   646  N  ND1 . HIS A 1 104 ? 18.484 11.450  -26.707 1.00 24.17  ? 158 HIS A ND1 1 
ATOM   647  C  CD2 . HIS A 1 104 ? 17.676 10.068  -28.197 1.00 25.10  ? 158 HIS A CD2 1 
ATOM   648  C  CE1 . HIS A 1 104 ? 19.095 11.708  -27.852 1.00 24.51  ? 158 HIS A CE1 1 
ATOM   649  N  NE2 . HIS A 1 104 ? 18.631 10.879  -28.768 1.00 26.05  ? 158 HIS A NE2 1 
ATOM   650  N  N   . ASP A 1 105 ? 15.471 9.008   -23.460 1.00 17.59  ? 159 ASP A N   1 
ATOM   651  C  CA  . ASP A 1 105 ? 14.593 8.568   -22.374 1.00 17.87  ? 159 ASP A CA  1 
ATOM   652  C  C   . ASP A 1 105 ? 13.511 7.603   -22.878 1.00 18.84  ? 159 ASP A C   1 
ATOM   653  O  O   . ASP A 1 105 ? 12.492 7.402   -22.218 1.00 19.45  ? 159 ASP A O   1 
ATOM   654  C  CB  . ASP A 1 105 ? 13.948 9.787   -21.697 1.00 20.15  ? 159 ASP A CB  1 
ATOM   655  C  CG  . ASP A 1 105 ? 13.077 10.596  -22.649 1.00 21.16  ? 159 ASP A CG  1 
ATOM   656  O  OD1 . ASP A 1 105 ? 13.243 10.478  -23.877 1.00 20.95  ? 159 ASP A OD1 1 
ATOM   657  O  OD2 . ASP A 1 105 ? 12.233 11.382  -22.163 1.00 23.70  ? 159 ASP A OD2 1 
ATOM   658  N  N   . GLN A 1 106 ? 13.775 6.993   -24.031 1.00 18.76  ? 160 GLN A N   1 
ATOM   659  C  CA  . GLN A 1 106 ? 12.784 6.203   -24.764 1.00 19.95  ? 160 GLN A CA  1 
ATOM   660  C  C   . GLN A 1 106 ? 13.060 4.705   -24.783 1.00 19.92  ? 160 GLN A C   1 
ATOM   661  O  O   . GLN A 1 106 ? 12.155 3.897   -25.015 1.00 21.31  ? 160 GLN A O   1 
ATOM   662  C  CB  . GLN A 1 106 ? 12.712 6.684   -26.212 1.00 24.56  ? 160 GLN A CB  1 
ATOM   663  C  CG  . GLN A 1 106 ? 12.271 8.124   -26.380 1.00 26.96  ? 160 GLN A CG  1 
ATOM   664  C  CD  . GLN A 1 106 ? 10.873 8.347   -25.864 1.00 29.35  ? 160 GLN A CD  1 
ATOM   665  O  OE1 . GLN A 1 106 ? 9.918  7.740   -26.350 1.00 33.02  ? 160 GLN A OE1 1 
ATOM   666  N  NE2 . GLN A 1 106 ? 10.739 9.216   -24.868 1.00 30.97  ? 160 GLN A NE2 1 
ATOM   667  N  N   . ASP A 1 107 ? 14.318 4.338   -24.576 1.00 16.91  ? 161 ASP A N   1 
ATOM   668  C  CA  . ASP A 1 107 ? 14.755 2.966   -24.814 1.00 16.96  ? 161 ASP A CA  1 
ATOM   669  C  C   . ASP A 1 107 ? 15.876 2.548   -23.882 1.00 15.16  ? 161 ASP A C   1 
ATOM   670  O  O   . ASP A 1 107 ? 16.417 3.362   -23.139 1.00 16.37  ? 161 ASP A O   1 
ATOM   671  C  CB  . ASP A 1 107 ? 15.225 2.809   -26.267 1.00 19.10  ? 161 ASP A CB  1 
ATOM   672  C  CG  . ASP A 1 107 ? 14.073 2.690   -27.240 1.00 21.93  ? 161 ASP A CG  1 
ATOM   673  O  OD1 . ASP A 1 107 ? 13.357 1.667   -27.182 1.00 23.94  ? 161 ASP A OD1 1 
ATOM   674  O  OD2 . ASP A 1 107 ? 13.891 3.605   -28.072 1.00 26.15  ? 161 ASP A OD2 1 
ATOM   675  N  N   . VAL A 1 108 ? 16.207 1.261   -23.924 1.00 16.50  ? 162 VAL A N   1 
ATOM   676  C  CA  . VAL A 1 108 ? 17.446 0.784   -23.340 1.00 15.54  ? 162 VAL A CA  1 
ATOM   677  C  C   . VAL A 1 108 ? 18.236 0.046   -24.404 1.00 15.65  ? 162 VAL A C   1 
ATOM   678  O  O   . VAL A 1 108 ? 17.671 -0.397  -25.410 1.00 16.75  ? 162 VAL A O   1 
ATOM   679  C  CB  . VAL A 1 108 ? 17.210 -0.149  -22.126 1.00 15.91  ? 162 VAL A CB  1 
ATOM   680  C  CG1 . VAL A 1 108 ? 16.386 0.565   -21.045 1.00 17.19  ? 162 VAL A CG1 1 
ATOM   681  C  CG2 . VAL A 1 108 ? 16.532 -1.468  -22.539 1.00 17.72  ? 162 VAL A CG2 1 
ATOM   682  N  N   . PHE A 1 109 ? 19.548 -0.034  -24.223 1.00 15.43  ? 163 PHE A N   1 
ATOM   683  C  CA  . PHE A 1 109 ? 20.378 -0.866  -25.101 1.00 15.39  ? 163 PHE A CA  1 
ATOM   684  C  C   . PHE A 1 109 ? 21.067 -1.931  -24.255 1.00 14.74  ? 163 PHE A C   1 
ATOM   685  O  O   . PHE A 1 109 ? 21.353 -1.713  -23.078 1.00 15.53  ? 163 PHE A O   1 
ATOM   686  C  CB  . PHE A 1 109 ? 21.415 -0.034  -25.886 1.00 15.47  ? 163 PHE A CB  1 
ATOM   687  C  CG  . PHE A 1 109 ? 22.517 0.570   -25.032 1.00 15.53  ? 163 PHE A CG  1 
ATOM   688  C  CD1 . PHE A 1 109 ? 23.631 -0.183  -24.671 1.00 17.57  ? 163 PHE A CD1 1 
ATOM   689  C  CD2 . PHE A 1 109 ? 22.458 1.902   -24.627 1.00 17.12  ? 163 PHE A CD2 1 
ATOM   690  C  CE1 . PHE A 1 109 ? 24.640 0.359   -23.885 1.00 18.51  ? 163 PHE A CE1 1 
ATOM   691  C  CE2 . PHE A 1 109 ? 23.478 2.454   -23.842 1.00 18.50  ? 163 PHE A CE2 1 
ATOM   692  C  CZ  . PHE A 1 109 ? 24.569 1.679   -23.478 1.00 18.06  ? 163 PHE A CZ  1 
ATOM   693  N  N   . SER A 1 110 ? 21.321 -3.091  -24.855 1.00 16.07  ? 164 SER A N   1 
ATOM   694  C  CA  . SER A 1 110 ? 22.050 -4.145  -24.167 1.00 16.16  ? 164 SER A CA  1 
ATOM   695  C  C   . SER A 1 110 ? 23.540 -3.864  -24.185 1.00 16.23  ? 164 SER A C   1 
ATOM   696  O  O   . SER A 1 110 ? 24.093 -3.465  -25.214 1.00 18.18  ? 164 SER A O   1 
ATOM   697  C  CB  . SER A 1 110 ? 21.784 -5.499  -24.815 1.00 18.21  ? 164 SER A CB  1 
ATOM   698  O  OG  . SER A 1 110 ? 22.556 -6.489  -24.156 1.00 20.10  ? 164 SER A OG  1 
ATOM   699  N  N   . PHE A 1 111 ? 24.212 -4.109  -23.067 1.00 16.01  ? 165 PHE A N   1 
ATOM   700  C  CA  . PHE A 1 111 ? 25.669 -3.999  -23.034 1.00 17.43  ? 165 PHE A CA  1 
ATOM   701  C  C   . PHE A 1 111 ? 26.378 -5.215  -23.622 1.00 19.85  ? 165 PHE A C   1 
ATOM   702  O  O   . PHE A 1 111 ? 27.579 -5.177  -23.854 1.00 20.95  ? 165 PHE A O   1 
ATOM   703  C  CB  . PHE A 1 111 ? 26.161 -3.781  -21.608 1.00 17.62  ? 165 PHE A CB  1 
ATOM   704  C  CG  . PHE A 1 111 ? 26.320 -2.342  -21.250 1.00 16.75  ? 165 PHE A CG  1 
ATOM   705  C  CD1 . PHE A 1 111 ? 27.463 -1.648  -21.622 1.00 18.64  ? 165 PHE A CD1 1 
ATOM   706  C  CD2 . PHE A 1 111 ? 25.324 -1.671  -20.569 1.00 18.04  ? 165 PHE A CD2 1 
ATOM   707  C  CE1 . PHE A 1 111 ? 27.614 -0.315  -21.312 1.00 19.87  ? 165 PHE A CE1 1 
ATOM   708  C  CE2 . PHE A 1 111 ? 25.474 -0.334  -20.248 1.00 19.22  ? 165 PHE A CE2 1 
ATOM   709  C  CZ  . PHE A 1 111 ? 26.628 0.345   -20.620 1.00 18.74  ? 165 PHE A CZ  1 
ATOM   710  N  N   . ASN A 1 112 ? 25.649 -6.302  -23.843 1.00 18.77  ? 166 ASN A N   1 
ATOM   711  C  CA  . ASN A 1 112 ? 26.254 -7.473  -24.444 1.00 20.87  ? 166 ASN A CA  1 
ATOM   712  C  C   . ASN A 1 112 ? 26.210 -7.348  -25.958 1.00 23.36  ? 166 ASN A C   1 
ATOM   713  O  O   . ASN A 1 112 ? 25.138 -7.171  -26.533 1.00 24.77  ? 166 ASN A O   1 
ATOM   714  C  CB  . ASN A 1 112 ? 25.536 -8.733  -23.985 1.00 20.60  ? 166 ASN A CB  1 
ATOM   715  C  CG  . ASN A 1 112 ? 26.272 -9.985  -24.390 1.00 22.78  ? 166 ASN A CG  1 
ATOM   716  O  OD1 . ASN A 1 112 ? 26.298 -10.338 -25.565 1.00 26.19  ? 166 ASN A OD1 1 
ATOM   717  N  ND2 . ASN A 1 112 ? 26.882 -10.663 -23.422 1.00 22.34  ? 166 ASN A ND2 1 
ATOM   718  N  N   . PRO A 1 113 ? 27.378 -7.417  -26.609 1.00 23.99  ? 167 PRO A N   1 
ATOM   719  C  CA  . PRO A 1 113 ? 27.435 -7.201  -28.062 1.00 26.05  ? 167 PRO A CA  1 
ATOM   720  C  C   . PRO A 1 113 ? 27.100 -8.439  -28.889 1.00 26.30  ? 167 PRO A C   1 
ATOM   721  O  O   . PRO A 1 113 ? 27.124 -8.363  -30.120 1.00 27.29  ? 167 PRO A O   1 
ATOM   722  C  CB  . PRO A 1 113 ? 28.891 -6.793  -28.288 1.00 25.92  ? 167 PRO A CB  1 
ATOM   723  C  CG  . PRO A 1 113 ? 29.639 -7.540  -27.219 1.00 28.02  ? 167 PRO A CG  1 
ATOM   724  C  CD  . PRO A 1 113 ? 28.719 -7.545  -26.009 1.00 25.16  ? 167 PRO A CD  1 
ATOM   725  N  N   . ASN A 1 114 ? 26.794 -9.553  -28.232 1.00 24.87  ? 168 ASN A N   1 
ATOM   726  C  CA  . ASN A 1 114 ? 26.570 -10.818 -28.928 1.00 27.01  ? 168 ASN A CA  1 
ATOM   727  C  C   . ASN A 1 114 ? 25.139 -11.353 -28.814 1.00 26.77  ? 168 ASN A C   1 
ATOM   728  O  O   . ASN A 1 114 ? 24.903 -12.558 -28.940 1.00 27.79  ? 168 ASN A O   1 
ATOM   729  C  CB  . ASN A 1 114 ? 27.561 -11.859 -28.412 1.00 27.46  ? 168 ASN A CB  1 
ATOM   730  C  CG  . ASN A 1 114 ? 29.000 -11.496 -28.736 1.00 28.82  ? 168 ASN A CG  1 
ATOM   731  O  OD1 . ASN A 1 114 ? 29.285 -10.933 -29.796 1.00 30.63  ? 168 ASN A OD1 1 
ATOM   732  N  ND2 . ASN A 1 114 ? 29.906 -11.779 -27.814 1.00 27.02  ? 168 ASN A ND2 1 
ATOM   733  N  N   . ASP A 1 115 ? 24.192 -10.442 -28.602 1.00 25.54  ? 169 ASP A N   1 
ATOM   734  C  CA  . ASP A 1 115 ? 22.764 -10.757 -28.548 1.00 26.61  ? 169 ASP A CA  1 
ATOM   735  C  C   . ASP A 1 115 ? 22.452 -11.868 -27.555 1.00 26.18  ? 169 ASP A C   1 
ATOM   736  O  O   . ASP A 1 115 ? 21.672 -12.773 -27.829 1.00 27.82  ? 169 ASP A O   1 
ATOM   737  C  CB  . ASP A 1 115 ? 22.242 -11.141 -29.937 1.00 29.54  ? 169 ASP A CB  1 
ATOM   738  C  CG  . ASP A 1 115 ? 20.729 -11.033 -30.039 1.00 35.28  ? 169 ASP A CG  1 
ATOM   739  O  OD1 . ASP A 1 115 ? 20.135 -10.260 -29.258 1.00 37.96  ? 169 ASP A OD1 1 
ATOM   740  O  OD2 . ASP A 1 115 ? 20.133 -11.712 -30.901 1.00 39.36  ? 169 ASP A OD2 1 
ATOM   741  N  N   . THR A 1 116 ? 23.075 -11.793 -26.390 1.00 24.29  ? 170 THR A N   1 
ATOM   742  C  CA  . THR A 1 116 ? 22.876 -12.802 -25.372 1.00 23.10  ? 170 THR A CA  1 
ATOM   743  C  C   . THR A 1 116 ? 23.041 -12.164 -23.997 1.00 20.54  ? 170 THR A C   1 
ATOM   744  O  O   . THR A 1 116 ? 23.305 -10.969 -23.896 1.00 22.12  ? 170 THR A O   1 
ATOM   745  C  CB  . THR A 1 116 ? 23.856 -13.986 -25.575 1.00 27.04  ? 170 THR A CB  1 
ATOM   746  O  OG1 . THR A 1 116 ? 23.453 -15.093 -24.762 1.00 29.45  ? 170 THR A OG1 1 
ATOM   747  C  CG2 . THR A 1 116 ? 25.295 -13.590 -25.260 1.00 27.31  ? 170 THR A CG2 1 
ATOM   748  N  N   . TYR A 1 117 ? 22.848 -12.943 -22.940 1.00 20.60  ? 171 TYR A N   1 
ATOM   749  C  CA  . TYR A 1 117 ? 23.031 -12.437 -21.588 1.00 19.63  ? 171 TYR A CA  1 
ATOM   750  C  C   . TYR A 1 117 ? 24.419 -12.795 -21.077 1.00 19.79  ? 171 TYR A C   1 
ATOM   751  O  O   . TYR A 1 117 ? 24.919 -13.907 -21.296 1.00 23.02  ? 171 TYR A O   1 
ATOM   752  C  CB  . TYR A 1 117 ? 21.971 -12.996 -20.633 1.00 19.09  ? 171 TYR A CB  1 
ATOM   753  C  CG  . TYR A 1 117 ? 20.549 -12.548 -20.883 1.00 18.78  ? 171 TYR A CG  1 
ATOM   754  C  CD1 . TYR A 1 117 ? 20.267 -11.274 -21.354 1.00 20.29  ? 171 TYR A CD1 1 
ATOM   755  C  CD2 . TYR A 1 117 ? 19.484 -13.400 -20.622 1.00 20.18  ? 171 TYR A CD2 1 
ATOM   756  C  CE1 . TYR A 1 117 ? 18.955 -10.867 -21.566 1.00 19.08  ? 171 TYR A CE1 1 
ATOM   757  C  CE2 . TYR A 1 117 ? 18.177 -13.003 -20.824 1.00 20.65  ? 171 TYR A CE2 1 
ATOM   758  C  CZ  . TYR A 1 117 ? 17.919 -11.740 -21.298 1.00 19.47  ? 171 TYR A CZ  1 
ATOM   759  O  OH  . TYR A 1 117 ? 16.617 -11.353 -21.498 1.00 22.80  ? 171 TYR A OH  1 
ATOM   760  N  N   . CYS A 1 118 ? 25.026 -11.844 -20.376 1.00 19.86  ? 172 CYS A N   1 
ATOM   761  C  CA  . CYS A 1 118 ? 26.329 -12.064 -19.751 1.00 18.77  ? 172 CYS A CA  1 
ATOM   762  C  C   . CYS A 1 118 ? 26.299 -13.200 -18.751 1.00 17.63  ? 172 CYS A C   1 
ATOM   763  O  O   . CYS A 1 118 ? 25.349 -13.345 -17.980 1.00 19.05  ? 172 CYS A O   1 
ATOM   764  C  CB  . CYS A 1 118 ? 26.803 -10.804 -19.038 1.00 20.06  ? 172 CYS A CB  1 
ATOM   765  S  SG  . CYS A 1 118 ? 27.239 -9.482  -20.142 1.00 22.23  ? 172 CYS A SG  1 
ATOM   766  N  N   . ASN A 1 119 ? 27.356 -13.996 -18.770 1.00 18.95  ? 173 ASN A N   1 
ATOM   767  C  CA  . ASN A 1 119 ? 27.555 -15.057 -17.794 1.00 19.56  ? 173 ASN A CA  1 
ATOM   768  C  C   . ASN A 1 119 ? 28.330 -14.536 -16.580 1.00 20.88  ? 173 ASN A C   1 
ATOM   769  O  O   . ASN A 1 119 ? 29.568 -14.524 -16.584 1.00 21.46  ? 173 ASN A O   1 
ATOM   770  C  CB  . ASN A 1 119 ? 28.293 -16.244 -18.431 1.00 21.69  ? 173 ASN A CB  1 
ATOM   771  C  CG  . ASN A 1 119 ? 27.596 -16.772 -19.682 1.00 23.35  ? 173 ASN A CG  1 
ATOM   772  O  OD1 . ASN A 1 119 ? 26.588 -17.470 -19.586 1.00 25.56  ? 173 ASN A OD1 1 
ATOM   773  N  ND2 . ASN A 1 119 ? 28.159 -16.480 -20.854 1.00 26.44  ? 173 ASN A ND2 1 
ATOM   774  N  N   . GLY A 1 120 ? 27.603 -14.081 -15.567 1.00 18.34  ? 174 GLY A N   1 
ATOM   775  C  CA  . GLY A 1 120 ? 28.192 -13.599 -14.330 1.00 17.39  ? 174 GLY A CA  1 
ATOM   776  C  C   . GLY A 1 120 ? 28.519 -12.118 -14.329 1.00 16.53  ? 174 GLY A C   1 
ATOM   777  O  O   . GLY A 1 120 ? 28.639 -11.489 -15.387 1.00 18.07  ? 174 GLY A O   1 
ATOM   778  N  N   . PHE A 1 121 ? 28.678 -11.556 -13.134 1.00 17.55  ? 175 PHE A N   1 
ATOM   779  C  CA  . PHE A 1 121 ? 28.876 -10.115 -13.025 1.00 17.23  ? 175 PHE A CA  1 
ATOM   780  C  C   . PHE A 1 121 ? 30.248 -9.712  -13.581 1.00 17.82  ? 175 PHE A C   1 
ATOM   781  O  O   . PHE A 1 121 ? 30.418 -8.569  -14.026 1.00 17.74  ? 175 PHE A O   1 
ATOM   782  C  CB  . PHE A 1 121 ? 28.691 -9.647  -11.567 1.00 18.11  ? 175 PHE A CB  1 
ATOM   783  C  CG  . PHE A 1 121 ? 29.851 -9.953  -10.663 1.00 19.89  ? 175 PHE A CG  1 
ATOM   784  C  CD1 . PHE A 1 121 ? 30.887 -9.049  -10.513 1.00 21.56  ? 175 PHE A CD1 1 
ATOM   785  C  CD2 . PHE A 1 121 ? 29.884 -11.127 -9.928  1.00 20.53  ? 175 PHE A CD2 1 
ATOM   786  C  CE1 . PHE A 1 121 ? 31.958 -9.326  -9.669  1.00 22.77  ? 175 PHE A CE1 1 
ATOM   787  C  CE2 . PHE A 1 121 ? 30.958 -11.410 -9.082  1.00 23.31  ? 175 PHE A CE2 1 
ATOM   788  C  CZ  . PHE A 1 121 ? 31.989 -10.506 -8.962  1.00 22.94  ? 175 PHE A CZ  1 
ATOM   789  N  N   . GLU A 1 122 ? 31.211 -10.624 -13.564 1.00 18.46  ? 176 GLU A N   1 
ATOM   790  C  CA  . GLU A 1 122 ? 32.517 -10.314 -14.136 1.00 19.24  ? 176 GLU A CA  1 
ATOM   791  C  C   . GLU A 1 122 ? 32.407 -10.011 -15.632 1.00 18.12  ? 176 GLU A C   1 
ATOM   792  O  O   . GLU A 1 122 ? 33.059 -9.098  -16.147 1.00 19.04  ? 176 GLU A O   1 
ATOM   793  C  CB  . GLU A 1 122 ? 33.494 -11.466 -13.887 1.00 22.98  ? 176 GLU A CB  1 
ATOM   794  C  CG  . GLU A 1 122 ? 33.612 -11.873 -12.412 1.00 27.63  ? 176 GLU A CG  1 
ATOM   795  C  CD  . GLU A 1 122 ? 32.741 -13.073 -12.004 1.00 30.69  ? 176 GLU A CD  1 
ATOM   796  O  OE1 . GLU A 1 122 ? 31.623 -13.273 -12.546 1.00 26.07  ? 176 GLU A OE1 1 
ATOM   797  O  OE2 . GLU A 1 122 ? 33.198 -13.831 -11.119 1.00 36.85  ? 176 GLU A OE2 1 
ATOM   798  N  N   . GLU A 1 123 ? 31.560 -10.751 -16.339 1.00 18.56  ? 177 GLU A N   1 
ATOM   799  C  CA  . GLU A 1 123 ? 31.376 -10.508 -17.763 1.00 19.35  ? 177 GLU A CA  1 
ATOM   800  C  C   . GLU A 1 123 ? 30.589 -9.213  -18.002 1.00 17.71  ? 177 GLU A C   1 
ATOM   801  O  O   . GLU A 1 123 ? 30.842 -8.501  -18.978 1.00 19.54  ? 177 GLU A O   1 
ATOM   802  C  CB  . GLU A 1 123 ? 30.677 -11.696 -18.433 1.00 22.49  ? 177 GLU A CB  1 
ATOM   803  C  CG  . GLU A 1 123 ? 30.655 -11.576 -19.953 1.00 26.65  ? 177 GLU A CG  1 
ATOM   804  C  CD  . GLU A 1 123 ? 30.393 -12.898 -20.644 1.00 30.60  ? 177 GLU A CD  1 
ATOM   805  O  OE1 . GLU A 1 123 ? 31.338 -13.453 -21.245 1.00 33.81  ? 177 GLU A OE1 1 
ATOM   806  O  OE2 . GLU A 1 123 ? 29.241 -13.375 -20.600 1.00 32.83  ? 177 GLU A OE2 1 
ATOM   807  N  N   . VAL A 1 124 ? 29.635 -8.911  -17.122 1.00 18.47  ? 178 VAL A N   1 
ATOM   808  C  CA  . VAL A 1 124 ? 28.956 -7.622  -17.155 1.00 17.88  ? 178 VAL A CA  1 
ATOM   809  C  C   . VAL A 1 124 ? 29.988 -6.489  -17.111 1.00 16.12  ? 178 VAL A C   1 
ATOM   810  O  O   . VAL A 1 124 ? 29.935 -5.541  -17.912 1.00 17.53  ? 178 VAL A O   1 
ATOM   811  C  CB  . VAL A 1 124 ? 27.972 -7.463  -15.978 1.00 17.27  ? 178 VAL A CB  1 
ATOM   812  C  CG1 . VAL A 1 124 ? 27.446 -6.020  -15.920 1.00 18.08  ? 178 VAL A CG1 1 
ATOM   813  C  CG2 . VAL A 1 124 ? 26.810 -8.469  -16.089 1.00 18.71  ? 178 VAL A CG2 1 
ATOM   814  N  N   . LEU A 1 125 ? 30.940 -6.590  -16.184 1.00 15.97  ? 179 LEU A N   1 
ATOM   815  C  CA  . LEU A 1 125 ? 31.975 -5.564  -16.045 1.00 16.70  ? 179 LEU A CA  1 
ATOM   816  C  C   . LEU A 1 125 ? 32.839 -5.471  -17.300 1.00 17.40  ? 179 LEU A C   1 
ATOM   817  O  O   . LEU A 1 125 ? 33.225 -4.381  -17.700 1.00 18.94  ? 179 LEU A O   1 
ATOM   818  C  CB  . LEU A 1 125 ? 32.848 -5.842  -14.818 1.00 18.53  ? 179 LEU A CB  1 
ATOM   819  C  CG  . LEU A 1 125 ? 32.179 -5.606  -13.461 1.00 21.25  ? 179 LEU A CG  1 
ATOM   820  C  CD1 . LEU A 1 125 ? 33.011 -6.239  -12.368 1.00 23.14  ? 179 LEU A CD1 1 
ATOM   821  C  CD2 . LEU A 1 125 ? 31.998 -4.115  -13.183 1.00 22.43  ? 179 LEU A CD2 1 
ATOM   822  N  N   . MET A 1 126 ? 33.143 -6.606  -17.926 1.00 19.35  ? 180 MET A N   1 
ATOM   823  C  CA  . MET A 1 126 ? 33.905 -6.601  -19.173 1.00 24.29  ? 180 MET A CA  1 
ATOM   824  C  C   . MET A 1 126 ? 33.152 -5.875  -20.283 1.00 21.17  ? 180 MET A C   1 
ATOM   825  O  O   . MET A 1 126 ? 33.737 -5.069  -21.011 1.00 22.32  ? 180 MET A O   1 
ATOM   826  C  CB  . MET A 1 126 ? 34.233 -8.031  -19.620 1.00 41.90  ? 180 MET A CB  1 
ATOM   827  C  CG  . MET A 1 126 ? 35.195 -8.785  -18.717 1.00 62.13  ? 180 MET A CG  1 
ATOM   828  S  SD  . MET A 1 126 ? 35.570 -10.418 -19.392 1.00 79.75  ? 180 MET A SD  1 
ATOM   829  C  CE  . MET A 1 126 ? 34.073 -11.318 -19.001 1.00 83.70  ? 180 MET A CE  1 
ATOM   830  N  N   . CYS A 1 127 ? 31.852 -6.147  -20.410 1.00 18.81  ? 181 CYS A N   1 
ATOM   831  C  CA  . CYS A 1 127 ? 31.060 -5.511  -21.454 1.00 18.60  ? 181 CYS A CA  1 
ATOM   832  C  C   . CYS A 1 127 ? 30.985 -4.005  -21.215 1.00 18.80  ? 181 CYS A C   1 
ATOM   833  O  O   . CYS A 1 127 ? 31.121 -3.209  -22.146 1.00 20.27  ? 181 CYS A O   1 
ATOM   834  C  CB  . CYS A 1 127 ? 29.654 -6.107  -21.523 1.00 19.48  ? 181 CYS A CB  1 
ATOM   835  S  SG  . CYS A 1 127 ? 29.612 -7.783  -22.189 1.00 21.50  ? 181 CYS A SG  1 
ATOM   836  N  N   . TYR A 1 128 ? 30.781 -3.628  -19.960 1.00 17.77  ? 182 TYR A N   1 
ATOM   837  C  CA  . TYR A 1 128 ? 30.699 -2.226  -19.583 1.00 18.81  ? 182 TYR A CA  1 
ATOM   838  C  C   . TYR A 1 128 ? 31.985 -1.507  -19.992 1.00 18.99  ? 182 TYR A C   1 
ATOM   839  O  O   . TYR A 1 128 ? 31.939 -0.455  -20.627 1.00 19.55  ? 182 TYR A O   1 
ATOM   840  C  CB  . TYR A 1 128 ? 30.448 -2.083  -18.078 1.00 19.45  ? 182 TYR A CB  1 
ATOM   841  C  CG  . TYR A 1 128 ? 30.658 -0.669  -17.574 1.00 17.46  ? 182 TYR A CG  1 
ATOM   842  C  CD1 . TYR A 1 128 ? 29.660 0.285   -17.680 1.00 17.41  ? 182 TYR A CD1 1 
ATOM   843  C  CD2 . TYR A 1 128 ? 31.863 -0.295  -16.988 1.00 18.73  ? 182 TYR A CD2 1 
ATOM   844  C  CE1 . TYR A 1 128 ? 29.871 1.591   -17.218 1.00 17.01  ? 182 TYR A CE1 1 
ATOM   845  C  CE2 . TYR A 1 128 ? 32.073 0.988   -16.531 1.00 18.70  ? 182 TYR A CE2 1 
ATOM   846  C  CZ  . TYR A 1 128 ? 31.078 1.917   -16.636 1.00 17.36  ? 182 TYR A CZ  1 
ATOM   847  O  OH  . TYR A 1 128 ? 31.332 3.186   -16.178 1.00 17.49  ? 182 TYR A OH  1 
ATOM   848  N  N   . ARG A 1 129 ? 33.133 -2.086  -19.654 1.00 20.59  ? 183 ARG A N   1 
ATOM   849  C  CA  . ARG A 1 129 ? 34.415 -1.464  -19.946 1.00 25.12  ? 183 ARG A CA  1 
ATOM   850  C  C   . ARG A 1 129 ? 34.621 -1.321  -21.440 1.00 26.96  ? 183 ARG A C   1 
ATOM   851  O  O   . ARG A 1 129 ? 35.237 -0.360  -21.912 1.00 28.94  ? 183 ARG A O   1 
ATOM   852  C  CB  . ARG A 1 129 ? 35.564 -2.287  -19.358 1.00 30.50  ? 183 ARG A CB  1 
ATOM   853  C  CG  . ARG A 1 129 ? 36.747 -1.428  -18.954 1.00 39.66  ? 183 ARG A CG  1 
ATOM   854  C  CD  . ARG A 1 129 ? 37.922 -2.228  -18.411 1.00 46.53  ? 183 ARG A CD  1 
ATOM   855  N  NE  . ARG A 1 129 ? 39.005 -1.323  -18.026 1.00 53.34  ? 183 ARG A NE  1 
ATOM   856  C  CZ  . ARG A 1 129 ? 40.293 -1.563  -18.240 1.00 60.13  ? 183 ARG A CZ  1 
ATOM   857  N  NH1 . ARG A 1 129 ? 40.664 -2.668  -18.873 1.00 62.60  ? 183 ARG A NH1 1 
ATOM   858  N  NH2 . ARG A 1 129 ? 41.209 -0.684  -17.840 1.00 62.70  ? 183 ARG A NH2 1 
ATOM   859  N  N   . GLU A 1 130 ? 34.105 -2.289  -22.181 1.00 29.39  ? 184 GLU A N   1 
ATOM   860  C  CA  . GLU A 1 130 ? 34.323 -2.332  -23.609 1.00 35.39  ? 184 GLU A CA  1 
ATOM   861  C  C   . GLU A 1 130 ? 33.514 -1.280  -24.353 1.00 28.94  ? 184 GLU A C   1 
ATOM   862  O  O   . GLU A 1 130 ? 33.971 -0.674  -25.322 1.00 30.27  ? 184 GLU A O   1 
ATOM   863  C  CB  . GLU A 1 130 ? 33.960 -3.713  -24.125 1.00 51.01  ? 184 GLU A CB  1 
ATOM   864  C  CG  . GLU A 1 130 ? 33.985 -3.837  -25.605 1.00 69.01  ? 184 GLU A CG  1 
ATOM   865  C  CD  . GLU A 1 130 ? 35.123 -4.689  -26.074 1.00 85.06  ? 184 GLU A CD  1 
ATOM   866  O  OE1 . GLU A 1 130 ? 35.540 -5.575  -25.298 1.00 91.60  ? 184 GLU A OE1 1 
ATOM   867  O  OE2 . GLU A 1 130 ? 35.615 -4.442  -27.216 1.00 92.54  ? 184 GLU A OE2 1 
ATOM   868  N  N   . ILE A 1 131 ? 32.283 -1.105  -23.908 1.00 24.15  ? 185 ILE A N   1 
ATOM   869  C  CA  . ILE A 1 131 ? 31.310 -0.293  -24.619 1.00 21.52  ? 185 ILE A CA  1 
ATOM   870  C  C   . ILE A 1 131 ? 31.241 1.160   -24.149 1.00 21.91  ? 185 ILE A C   1 
ATOM   871  O  O   . ILE A 1 131 ? 31.048 2.056   -24.962 1.00 22.28  ? 185 ILE A O   1 
ATOM   872  C  CB  . ILE A 1 131 ? 29.926 -0.940  -24.496 1.00 24.18  ? 185 ILE A CB  1 
ATOM   873  C  CG1 . ILE A 1 131 ? 29.926 -2.229  -25.313 1.00 28.94  ? 185 ILE A CG1 1 
ATOM   874  C  CG2 . ILE A 1 131 ? 28.806 0.005   -24.942 1.00 23.94  ? 185 ILE A CG2 1 
ATOM   875  C  CD1 . ILE A 1 131 ? 28.624 -2.885  -25.360 1.00 33.67  ? 185 ILE A CD1 1 
ATOM   876  N  N   . VAL A 1 132 ? 31.435 1.420   -22.860 1.00 21.67  ? 186 VAL A N   1 
ATOM   877  C  CA  . VAL A 1 132 ? 31.131 2.765   -22.370 1.00 22.71  ? 186 VAL A CA  1 
ATOM   878  C  C   . VAL A 1 132 ? 32.001 3.897   -23.000 1.00 24.89  ? 186 VAL A C   1 
ATOM   879  O  O   . VAL A 1 132 ? 31.476 4.982   -23.253 1.00 24.76  ? 186 VAL A O   1 
ATOM   880  C  CB  . VAL A 1 132 ? 31.164 2.816   -20.798 1.00 21.92  ? 186 VAL A CB  1 
ATOM   881  C  CG1 . VAL A 1 132 ? 32.558 2.778   -20.225 1.00 24.49  ? 186 VAL A CG1 1 
ATOM   882  C  CG2 . VAL A 1 132 ? 30.394 4.040   -20.295 1.00 23.62  ? 186 VAL A CG2 1 
ATOM   883  N  N   . PRO A 1 133 ? 33.286 3.637   -23.343 1.00 27.80  ? 187 PRO A N   1 
ATOM   884  C  CA  . PRO A 1 133 ? 34.032 4.729   -23.991 1.00 28.66  ? 187 PRO A CA  1 
ATOM   885  C  C   . PRO A 1 133 ? 33.538 5.043   -25.416 1.00 29.71  ? 187 PRO A C   1 
ATOM   886  O  O   . PRO A 1 133 ? 33.888 6.099   -25.964 1.00 31.88  ? 187 PRO A O   1 
ATOM   887  C  CB  . PRO A 1 133 ? 35.472 4.191   -24.035 1.00 30.39  ? 187 PRO A CB  1 
ATOM   888  C  CG  . PRO A 1 133 ? 35.510 3.094   -23.038 1.00 29.94  ? 187 PRO A CG  1 
ATOM   889  C  CD  . PRO A 1 133 ? 34.160 2.469   -23.136 1.00 28.29  ? 187 PRO A CD  1 
ATOM   890  N  N   . GLN A 1 134 ? 32.808 4.101   -26.015 1.00 29.40  ? 188 GLN A N   1 
ATOM   891  C  CA  . GLN A 1 134 ? 32.178 4.368   -27.320 1.00 30.55  ? 188 GLN A CA  1 
ATOM   892  C  C   . GLN A 1 134 ? 30.820 5.084   -27.278 1.00 26.16  ? 188 GLN A C   1 
ATOM   893  O  O   . GLN A 1 134 ? 30.337 5.580   -28.301 1.00 28.54  ? 188 GLN A O   1 
ATOM   894  C  CB  . GLN A 1 134 ? 32.012 3.034   -28.076 1.00 37.53  ? 188 GLN A CB  1 
ATOM   895  C  CG  . GLN A 1 134 ? 33.181 2.023   -28.169 1.00 44.43  ? 188 GLN A CG  1 
ATOM   896  C  CD  . GLN A 1 134 ? 32.668 0.617   -28.509 1.00 52.84  ? 188 GLN A CD  1 
ATOM   897  O  OE1 . GLN A 1 134 ? 31.969 0.429   -29.514 1.00 56.97  ? 188 GLN A OE1 1 
ATOM   898  N  NE2 . GLN A 1 134 ? 33.273 -0.390  -27.852 1.00 54.29  ? 188 GLN A NE2 1 
ATOM   899  N  N   . LEU A 1 135 ? 30.277 5.352   -26.098 1.00 22.52  ? 189 LEU A N   1 
ATOM   900  C  CA  . LEU A 1 135 ? 28.951 5.989   -26.026 1.00 21.39  ? 189 LEU A CA  1 
ATOM   901  C  C   . LEU A 1 135 ? 29.002 7.500   -26.180 1.00 21.49  ? 189 LEU A C   1 
ATOM   902  O  O   . LEU A 1 135 ? 29.993 8.134   -25.825 1.00 23.92  ? 189 LEU A O   1 
ATOM   903  C  CB  . LEU A 1 135 ? 28.261 5.662   -24.699 1.00 22.36  ? 189 LEU A CB  1 
ATOM   904  C  CG  . LEU A 1 135 ? 28.127 4.176   -24.379 1.00 21.79  ? 189 LEU A CG  1 
ATOM   905  C  CD1 . LEU A 1 135 ? 27.534 3.979   -22.983 1.00 22.50  ? 189 LEU A CD1 1 
ATOM   906  C  CD2 . LEU A 1 135 ? 27.292 3.472   -25.436 1.00 22.36  ? 189 LEU A CD2 1 
ATOM   907  N  N   . ARG A 1 136 ? 27.924 8.066   -26.716 1.00 21.39  ? 190 ARG A N   1 
ATOM   908  C  CA  . ARG A 1 136 ? 27.722 9.503   -26.646 1.00 23.55  ? 190 ARG A CA  1 
ATOM   909  C  C   . ARG A 1 136 ? 26.686 9.746   -25.559 1.00 19.38  ? 190 ARG A C   1 
ATOM   910  O  O   . ARG A 1 136 ? 25.504 9.410   -25.709 1.00 19.51  ? 190 ARG A O   1 
ATOM   911  C  CB  . ARG A 1 136 ? 27.270 10.070  -27.985 1.00 30.41  ? 190 ARG A CB  1 
ATOM   912  C  CG  . ARG A 1 136 ? 27.389 11.580  -28.079 1.00 41.42  ? 190 ARG A CG  1 
ATOM   913  C  CD  . ARG A 1 136 ? 28.071 11.994  -29.371 1.00 52.69  ? 190 ARG A CD  1 
ATOM   914  N  NE  . ARG A 1 136 ? 29.518 11.800  -29.325 1.00 61.15  ? 190 ARG A NE  1 
ATOM   915  C  CZ  . ARG A 1 136 ? 30.296 11.733  -30.401 1.00 68.47  ? 190 ARG A CZ  1 
ATOM   916  N  NH1 . ARG A 1 136 ? 29.762 11.814  -31.613 1.00 70.30  ? 190 ARG A NH1 1 
ATOM   917  N  NH2 . ARG A 1 136 ? 31.604 11.564  -30.265 1.00 70.11  ? 190 ARG A NH2 1 
ATOM   918  N  N   . LEU A 1 137 ? 27.113 10.277  -24.443 1.00 19.61  ? 191 LEU A N   1 
ATOM   919  C  CA  . LEU A 1 137 ? 26.251 10.466  -23.312 1.00 19.04  ? 191 LEU A CA  1 
ATOM   920  C  C   . LEU A 1 137 ? 25.226 11.547  -23.623 1.00 17.33  ? 191 LEU A C   1 
ATOM   921  O  O   . LEU A 1 137 ? 25.578 12.512  -24.239 1.00 20.89  ? 191 LEU A O   1 
ATOM   922  C  CB  . LEU A 1 137 ? 27.059 10.825  -22.087 1.00 20.14  ? 191 LEU A CB  1 
ATOM   923  C  CG  . LEU A 1 137 ? 28.228 9.916   -21.735 1.00 20.92  ? 191 LEU A CG  1 
ATOM   924  C  CD1 . LEU A 1 137 ? 28.854 10.413  -20.475 1.00 25.02  ? 191 LEU A CD1 1 
ATOM   925  C  CD2 . LEU A 1 137 ? 27.842 8.462   -21.574 1.00 22.08  ? 191 LEU A CD2 1 
ATOM   926  N  N   . SER A 1 138 ? 23.984 11.356  -23.208 1.00 16.63  ? 192 SER A N   1 
ATOM   927  C  CA  . SER A 1 138 ? 22.900 12.200  -23.650 1.00 17.37  ? 192 SER A CA  1 
ATOM   928  C  C   . SER A 1 138 ? 21.866 12.449  -22.555 1.00 17.66  ? 192 SER A C   1 
ATOM   929  O  O   . SER A 1 138 ? 22.190 12.645  -21.437 1.00 18.29  ? 192 SER A O   1 
ATOM   930  C  CB  . SER A 1 138 ? 22.293 11.563  -24.907 1.00 19.01  ? 192 SER A CB  1 
ATOM   931  O  OG  . SER A 1 138 ? 21.311 12.328  -25.545 1.00 19.20  ? 192 SER A OG  1 
ATOM   932  N  N   . GLY A 1 139 ? 20.610 12.457  -22.956 1.00 17.68  ? 193 GLY A N   1 
ATOM   933  C  CA  . GLY A 1 139 ? 19.501 12.641  -22.055 1.00 18.85  ? 193 GLY A CA  1 
ATOM   934  C  C   . GLY A 1 139 ? 18.182 12.577  -22.805 1.00 18.91  ? 193 GLY A C   1 
ATOM   935  O  O   . GLY A 1 139 ? 18.194 12.228  -23.907 1.00 18.98  ? 193 GLY A O   1 
ATOM   936  N  N   . PRO A 1 140 ? 17.069 12.888  -22.159 1.00 19.21  ? 194 PRO A N   1 
ATOM   937  C  CA  . PRO A 1 140 ? 16.973 13.130  -20.720 1.00 20.39  ? 194 PRO A CA  1 
ATOM   938  C  C   . PRO A 1 140 ? 17.036 11.829  -19.923 1.00 19.39  ? 194 PRO A C   1 
ATOM   939  O  O   . PRO A 1 140 ? 17.287 10.751  -20.483 1.00 19.90  ? 194 PRO A O   1 
ATOM   940  C  CB  . PRO A 1 140 ? 15.606 13.804  -20.562 1.00 22.94  ? 194 PRO A CB  1 
ATOM   941  C  CG  . PRO A 1 140 ? 14.833 13.392  -21.718 1.00 24.76  ? 194 PRO A CG  1 
ATOM   942  C  CD  . PRO A 1 140 ? 15.795 13.139  -22.853 1.00 21.77  ? 194 PRO A CD  1 
ATOM   943  N  N   . THR A 1 141 ? 16.834 11.943  -18.611 1.00 19.51  ? 195 THR A N   1 
ATOM   944  C  CA  . THR A 1 141 ? 16.925 10.817  -17.696 1.00 17.85  ? 195 THR A CA  1 
ATOM   945  C  C   . THR A 1 141 ? 15.548 10.311  -17.307 1.00 16.90  ? 195 THR A C   1 
ATOM   946  O  O   . THR A 1 141 ? 14.738 11.075  -16.765 1.00 18.16  ? 195 THR A O   1 
ATOM   947  C  CB  . THR A 1 141 ? 17.673 11.194  -16.403 1.00 19.73  ? 195 THR A CB  1 
ATOM   948  O  OG1 . THR A 1 141 ? 18.980 11.699  -16.725 1.00 22.50  ? 195 THR A OG1 1 
ATOM   949  C  CG2 . THR A 1 141 ? 17.789 9.991   -15.491 1.00 21.89  ? 195 THR A CG2 1 
ATOM   950  N  N   . SER A 1 142 ? 15.277 9.045   -17.608 1.00 16.73  ? 196 SER A N   1 
ATOM   951  C  CA  . SER A 1 142 ? 14.050 8.393   -17.156 1.00 16.43  ? 196 SER A CA  1 
ATOM   952  C  C   . SER A 1 142 ? 14.374 6.967   -16.779 1.00 15.90  ? 196 SER A C   1 
ATOM   953  O  O   . SER A 1 142 ? 15.209 6.352   -17.421 1.00 18.48  ? 196 SER A O   1 
ATOM   954  C  CB  . SER A 1 142 ? 12.975 8.399   -18.237 1.00 16.97  ? 196 SER A CB  1 
ATOM   955  O  OG  . SER A 1 142 ? 11.838 7.681   -17.773 1.00 17.20  ? 196 SER A OG  1 
ATOM   956  N  N   . PHE A 1 143 ? 13.711 6.435   -15.760 1.00 14.98  ? 197 PHE A N   1 
ATOM   957  C  CA  . PHE A 1 143 ? 13.915 5.022   -15.433 1.00 15.80  ? 197 PHE A CA  1 
ATOM   958  C  C   . PHE A 1 143 ? 12.762 4.168   -15.961 1.00 15.22  ? 197 PHE A C   1 
ATOM   959  O  O   . PHE A 1 143 ? 12.733 2.961   -15.721 1.00 15.53  ? 197 PHE A O   1 
ATOM   960  C  CB  . PHE A 1 143 ? 14.062 4.804   -13.916 1.00 16.22  ? 197 PHE A CB  1 
ATOM   961  C  CG  . PHE A 1 143 ? 15.132 5.641   -13.280 1.00 16.03  ? 197 PHE A CG  1 
ATOM   962  C  CD1 . PHE A 1 143 ? 16.328 5.882   -13.934 1.00 17.23  ? 197 PHE A CD1 1 
ATOM   963  C  CD2 . PHE A 1 143 ? 14.926 6.224   -12.036 1.00 17.99  ? 197 PHE A CD2 1 
ATOM   964  C  CE1 . PHE A 1 143 ? 17.305 6.670   -13.349 1.00 18.18  ? 197 PHE A CE1 1 
ATOM   965  C  CE2 . PHE A 1 143 ? 15.905 7.028   -11.446 1.00 19.16  ? 197 PHE A CE2 1 
ATOM   966  C  CZ  . PHE A 1 143 ? 17.093 7.254   -12.114 1.00 18.30  ? 197 PHE A CZ  1 
ATOM   967  N  N   . ALA A 1 144 ? 11.815 4.760   -16.679 1.00 14.70  ? 198 ALA A N   1 
ATOM   968  C  CA  . ALA A 1 144 ? 10.698 3.955   -17.179 1.00 14.95  ? 198 ALA A CA  1 
ATOM   969  C  C   . ALA A 1 144 ? 11.152 2.864   -18.158 1.00 16.00  ? 198 ALA A C   1 
ATOM   970  O  O   . ALA A 1 144 ? 10.731 1.726   -18.011 1.00 16.47  ? 198 ALA A O   1 
ATOM   971  C  CB  . ALA A 1 144 ? 9.625  4.844   -17.814 1.00 16.74  ? 198 ALA A CB  1 
ATOM   972  N  N   . PRO A 1 145 ? 12.029 3.180   -19.137 1.00 14.88  ? 199 PRO A N   1 
ATOM   973  C  CA  . PRO A 1 145 ? 12.432 2.103   -20.051 1.00 16.00  ? 199 PRO A CA  1 
ATOM   974  C  C   . PRO A 1 145 ? 13.158 0.949   -19.355 1.00 14.37  ? 199 PRO A C   1 
ATOM   975  O  O   . PRO A 1 145 ? 12.820 -0.204  -19.641 1.00 14.58  ? 199 PRO A O   1 
ATOM   976  C  CB  . PRO A 1 145 ? 13.344 2.827   -21.046 1.00 17.25  ? 199 PRO A CB  1 
ATOM   977  C  CG  . PRO A 1 145 ? 12.826 4.250   -21.051 1.00 18.28  ? 199 PRO A CG  1 
ATOM   978  C  CD  . PRO A 1 145 ? 12.491 4.498   -19.616 1.00 17.40  ? 199 PRO A CD  1 
ATOM   979  N  N   . ILE A 1 146 ? 14.060 1.222   -18.417 1.00 14.54  ? 200 ILE A N   1 
ATOM   980  C  CA  . ILE A 1 146 ? 14.770 0.107   -17.788 1.00 14.79  ? 200 ILE A CA  1 
ATOM   981  C  C   . ILE A 1 146 ? 13.821 -0.717  -16.898 1.00 14.34  ? 200 ILE A C   1 
ATOM   982  O  O   . ILE A 1 146 ? 13.898 -1.945  -16.879 1.00 14.77  ? 200 ILE A O   1 
ATOM   983  C  CB  . ILE A 1 146 ? 16.037 0.568   -16.977 1.00 15.04  ? 200 ILE A CB  1 
ATOM   984  C  CG1 . ILE A 1 146 ? 16.798 -0.636  -16.410 1.00 15.53  ? 200 ILE A CG1 1 
ATOM   985  C  CG2 . ILE A 1 146 ? 15.696 1.572   -15.853 1.00 16.56  ? 200 ILE A CG2 1 
ATOM   986  C  CD1 . ILE A 1 146 ? 17.349 -1.579  -17.464 1.00 17.28  ? 200 ILE A CD1 1 
ATOM   987  N  N   . ILE A 1 147 ? 12.893 -0.063  -16.209 1.00 13.13  ? 201 ILE A N   1 
ATOM   988  C  CA  . ILE A 1 147 ? 11.941 -0.797  -15.375 1.00 14.68  ? 201 ILE A CA  1 
ATOM   989  C  C   . ILE A 1 147 ? 11.004 -1.641  -16.255 1.00 15.16  ? 201 ILE A C   1 
ATOM   990  O  O   . ILE A 1 147 ? 10.706 -2.794  -15.927 1.00 15.39  ? 201 ILE A O   1 
ATOM   991  C  CB  . ILE A 1 147 ? 11.148 0.164   -14.463 1.00 13.81  ? 201 ILE A CB  1 
ATOM   992  C  CG1 . ILE A 1 147 ? 12.090 0.774   -13.424 1.00 14.77  ? 201 ILE A CG1 1 
ATOM   993  C  CG2 . ILE A 1 147 ? 9.979  -0.565  -13.774 1.00 15.97  ? 201 ILE A CG2 1 
ATOM   994  C  CD1 . ILE A 1 147 ? 11.501 1.951   -12.674 1.00 15.99  ? 201 ILE A CD1 1 
ATOM   995  N  N   . GLU A 1 148 ? 10.599 -1.106  -17.404 1.00 14.90  ? 202 GLU A N   1 
ATOM   996  C  CA  . GLU A 1 148 ? 9.765  -1.867  -18.335 1.00 15.71  ? 202 GLU A CA  1 
ATOM   997  C  C   . GLU A 1 148 ? 10.504 -3.057  -18.937 1.00 14.49  ? 202 GLU A C   1 
ATOM   998  O  O   . GLU A 1 148 ? 9.913  -4.131  -19.121 1.00 15.64  ? 202 GLU A O   1 
ATOM   999  C  CB  . GLU A 1 148 ? 9.245  -0.961  -19.454 1.00 17.11  ? 202 GLU A CB  1 
ATOM   1000 C  CG  . GLU A 1 148 ? 8.123  -0.026  -19.005 1.00 19.74  ? 202 GLU A CG  1 
ATOM   1001 C  CD  . GLU A 1 148 ? 7.722  0.951   -20.086 1.00 26.80  ? 202 GLU A CD  1 
ATOM   1002 O  OE1 . GLU A 1 148 ? 8.289  0.876   -21.197 1.00 28.70  ? 202 GLU A OE1 1 
ATOM   1003 O  OE2 . GLU A 1 148 ? 6.840  1.795   -19.822 1.00 32.10  ? 202 GLU A OE2 1 
ATOM   1004 N  N   . ARG A 1 149 ? 11.783 -2.890  -19.255 1.00 15.37  ? 203 ARG A N   1 
ATOM   1005 C  CA  . ARG A 1 149 ? 12.570 -4.029  -19.734 1.00 14.91  ? 203 ARG A CA  1 
ATOM   1006 C  C   . ARG A 1 149 ? 12.654 -5.109  -18.652 1.00 14.44  ? 203 ARG A C   1 
ATOM   1007 O  O   . ARG A 1 149 ? 12.513 -6.304  -18.944 1.00 15.29  ? 203 ARG A O   1 
ATOM   1008 C  CB  . ARG A 1 149 ? 13.966 -3.571  -20.170 1.00 14.70  ? 203 ARG A CB  1 
ATOM   1009 C  CG  . ARG A 1 149 ? 14.892 -4.671  -20.691 1.00 16.19  ? 203 ARG A CG  1 
ATOM   1010 C  CD  . ARG A 1 149 ? 14.298 -5.452  -21.877 1.00 19.44  ? 203 ARG A CD  1 
ATOM   1011 N  NE  . ARG A 1 149 ? 14.988 -6.735  -22.029 1.00 20.48  ? 203 ARG A NE  1 
ATOM   1012 C  CZ  . ARG A 1 149 ? 14.474 -7.786  -22.649 1.00 21.50  ? 203 ARG A CZ  1 
ATOM   1013 N  NH1 . ARG A 1 149 ? 13.268 -7.703  -23.192 1.00 23.97  ? 203 ARG A NH1 1 
ATOM   1014 N  NH2 . ARG A 1 149 ? 15.166 -8.920  -22.719 1.00 23.20  ? 203 ARG A NH2 1 
ATOM   1015 N  N   . ALA A 1 150 ? 12.857 -4.690  -17.404 1.00 14.14  ? 204 ALA A N   1 
ATOM   1016 C  CA  . ALA A 1 150 ? 12.903 -5.639  -16.279 1.00 14.75  ? 204 ALA A CA  1 
ATOM   1017 C  C   . ALA A 1 150 ? 11.578 -6.397  -16.160 1.00 15.09  ? 204 ALA A C   1 
ATOM   1018 O  O   . ALA A 1 150 ? 11.573 -7.601  -15.962 1.00 16.00  ? 204 ALA A O   1 
ATOM   1019 C  CB  . ALA A 1 150 ? 13.237 -4.918  -14.973 1.00 14.92  ? 204 ALA A CB  1 
ATOM   1020 N  N   . MET A 1 151 ? 10.455 -5.705  -16.294 1.00 14.67  ? 205 MET A N   1 
ATOM   1021 C  CA  . MET A 1 151 ? 9.152  -6.372  -16.220 1.00 15.98  ? 205 MET A CA  1 
ATOM   1022 C  C   . MET A 1 151 ? 9.016  -7.420  -17.312 1.00 16.40  ? 205 MET A C   1 
ATOM   1023 O  O   . MET A 1 151 ? 8.489  -8.500  -17.082 1.00 17.88  ? 205 MET A O   1 
ATOM   1024 C  CB  . MET A 1 151 ? 8.028  -5.339  -16.331 1.00 17.75  ? 205 MET A CB  1 
ATOM   1025 C  CG  . MET A 1 151 ? 7.994  -4.415  -15.124 1.00 20.99  ? 205 MET A CG  1 
ATOM   1026 S  SD  . MET A 1 151 ? 7.198  -2.851  -15.501 1.00 30.04  ? 205 MET A SD  1 
ATOM   1027 C  CE  . MET A 1 151 ? 5.589  -3.463  -15.801 1.00 22.82  ? 205 MET A CE  1 
ATOM   1028 N  N   . THR A 1 152 ? 9.480  -7.091  -18.509 1.00 15.51  ? 206 THR A N   1 
ATOM   1029 C  CA  . THR A 1 152 ? 9.421  -8.002  -19.634 1.00 16.77  ? 206 THR A CA  1 
ATOM   1030 C  C   . THR A 1 152 ? 10.278 -9.233  -19.350 1.00 15.50  ? 206 THR A C   1 
ATOM   1031 O  O   . THR A 1 152 ? 9.847  -10.361 -19.602 1.00 17.02  ? 206 THR A O   1 
ATOM   1032 C  CB  . THR A 1 152 ? 9.885  -7.301  -20.922 1.00 17.39  ? 206 THR A CB  1 
ATOM   1033 O  OG1 . THR A 1 152 ? 9.049  -6.156  -21.158 1.00 19.79  ? 206 THR A OG1 1 
ATOM   1034 C  CG2 . THR A 1 152 ? 9.813  -8.243  -22.118 1.00 19.18  ? 206 THR A CG2 1 
ATOM   1035 N  N   . ILE A 1 153 ? 11.472 -9.032  -18.802 1.00 14.99  ? 207 ILE A N   1 
ATOM   1036 C  CA  . ILE A 1 153 ? 12.349 -10.152 -18.451 1.00 15.06  ? 207 ILE A CA  1 
ATOM   1037 C  C   . ILE A 1 153 ? 11.704 -11.052 -17.388 1.00 15.21  ? 207 ILE A C   1 
ATOM   1038 O  O   . ILE A 1 153 ? 11.716 -12.284 -17.511 1.00 17.16  ? 207 ILE A O   1 
ATOM   1039 C  CB  . ILE A 1 153 ? 13.721 -9.637  -17.966 1.00 15.39  ? 207 ILE A CB  1 
ATOM   1040 C  CG1 . ILE A 1 153 ? 14.495 -9.012  -19.137 1.00 16.42  ? 207 ILE A CG1 1 
ATOM   1041 C  CG2 . ILE A 1 153 ? 14.540 -10.762 -17.316 1.00 16.99  ? 207 ILE A CG2 1 
ATOM   1042 C  CD1 . ILE A 1 153 ? 15.663 -8.141  -18.701 1.00 17.26  ? 207 ILE A CD1 1 
ATOM   1043 N  N   . VAL A 1 154 ? 11.091 -10.446 -16.381 1.00 15.42  ? 208 VAL A N   1 
ATOM   1044 C  CA  . VAL A 1 154 ? 10.449 -11.226 -15.330 1.00 15.78  ? 208 VAL A CA  1 
ATOM   1045 C  C   . VAL A 1 154 ? 9.311  -12.060 -15.916 1.00 16.12  ? 208 VAL A C   1 
ATOM   1046 O  O   . VAL A 1 154 ? 9.192  -13.263 -15.637 1.00 17.50  ? 208 VAL A O   1 
ATOM   1047 C  CB  . VAL A 1 154 ? 9.922  -10.310 -14.201 1.00 16.05  ? 208 VAL A CB  1 
ATOM   1048 C  CG1 . VAL A 1 154 ? 9.095  -11.105 -13.203 1.00 17.05  ? 208 VAL A CG1 1 
ATOM   1049 C  CG2 . VAL A 1 154 ? 11.097 -9.650  -13.473 1.00 17.42  ? 208 VAL A CG2 1 
ATOM   1050 N  N   . GLU A 1 155 ? 8.485  -11.442 -16.752 1.00 16.65  ? 209 GLU A N   1 
ATOM   1051 C  CA  . GLU A 1 155 ? 7.395  -12.160 -17.412 1.00 18.27  ? 209 GLU A CA  1 
ATOM   1052 C  C   . GLU A 1 155 ? 7.924  -13.313 -18.276 1.00 19.02  ? 209 GLU A C   1 
ATOM   1053 O  O   . GLU A 1 155 ? 7.403  -14.430 -18.215 1.00 19.78  ? 209 GLU A O   1 
ATOM   1054 C  CB  . GLU A 1 155 ? 6.565  -11.191 -18.255 1.00 20.29  ? 209 GLU A CB  1 
ATOM   1055 C  CG  . GLU A 1 155 ? 5.357  -11.813 -18.936 1.00 21.35  ? 209 GLU A CG  1 
ATOM   1056 C  CD  . GLU A 1 155 ? 4.125  -11.936 -18.041 1.00 24.37  ? 209 GLU A CD  1 
ATOM   1057 O  OE1 . GLU A 1 155 ? 4.216  -11.737 -16.807 1.00 24.73  ? 209 GLU A OE1 1 
ATOM   1058 O  OE2 . GLU A 1 155 ? 3.042  -12.240 -18.593 1.00 26.13  ? 209 GLU A OE2 1 
ATOM   1059 N  N   . GLU A 1 156 ? 8.980  -13.062 -19.047 1.00 19.29  ? 210 GLU A N   1 
ATOM   1060 C  CA  . GLU A 1 156 ? 9.569  -14.097 -19.912 1.00 20.73  ? 210 GLU A CA  1 
ATOM   1061 C  C   . GLU A 1 156 ? 10.100 -15.283 -19.108 1.00 20.19  ? 210 GLU A C   1 
ATOM   1062 O  O   . GLU A 1 156 ? 10.100 -16.423 -19.583 1.00 23.59  ? 210 GLU A O   1 
ATOM   1063 C  CB  . GLU A 1 156 ? 10.693 -13.507 -20.774 1.00 24.12  ? 210 GLU A CB  1 
ATOM   1064 C  CG  . GLU A 1 156 ? 10.187 -12.551 -21.849 1.00 26.66  ? 210 GLU A CG  1 
ATOM   1065 C  CD  . GLU A 1 156 ? 11.295 -11.981 -22.717 1.00 30.12  ? 210 GLU A CD  1 
ATOM   1066 O  OE1 . GLU A 1 156 ? 12.474 -12.034 -22.306 1.00 32.96  ? 210 GLU A OE1 1 
ATOM   1067 O  OE2 . GLU A 1 156 ? 10.981 -11.471 -23.814 1.00 33.27  ? 210 GLU A OE2 1 
ATOM   1068 N  N   . SER A 1 157 ? 10.541 -15.011 -17.885 1.00 19.94  ? 211 SER A N   1 
ATOM   1069 C  CA  . SER A 1 157 ? 11.071 -16.047 -17.007 1.00 19.82  ? 211 SER A CA  1 
ATOM   1070 C  C   . SER A 1 157 ? 9.979  -16.878 -16.351 1.00 20.25  ? 211 SER A C   1 
ATOM   1071 O  O   . SER A 1 157 ? 10.272 -17.854 -15.656 1.00 21.92  ? 211 SER A O   1 
ATOM   1072 C  CB  . SER A 1 157 ? 11.950 -15.433 -15.923 1.00 18.49  ? 211 SER A CB  1 
ATOM   1073 O  OG  . SER A 1 157 ? 11.169 -14.899 -14.853 1.00 17.98  ? 211 SER A OG  1 
ATOM   1074 N  N   . GLY A 1 158 ? 8.723  -16.507 -16.579 1.00 19.36  ? 212 GLY A N   1 
ATOM   1075 C  CA  . GLY A 1 158 ? 7.612  -17.165 -15.915 1.00 20.35  ? 212 GLY A CA  1 
ATOM   1076 C  C   . GLY A 1 158 ? 7.470  -16.733 -14.463 1.00 20.12  ? 212 GLY A C   1 
ATOM   1077 O  O   . GLY A 1 158 ? 7.063  -17.515 -13.607 1.00 22.80  ? 212 GLY A O   1 
ATOM   1078 N  N   . GLY A 1 159 ? 7.802  -15.482 -14.174 1.00 18.54  ? 213 GLY A N   1 
ATOM   1079 C  CA  . GLY A 1 159 ? 7.621  -14.959 -12.837 1.00 18.19  ? 213 GLY A CA  1 
ATOM   1080 C  C   . GLY A 1 159 ? 8.669  -15.363 -11.820 1.00 17.86  ? 213 GLY A C   1 
ATOM   1081 O  O   . GLY A 1 159 ? 8.392  -15.372 -10.620 1.00 18.58  ? 213 GLY A O   1 
ATOM   1082 N  N   . GLN A 1 160 ? 9.884  -15.658 -12.265 1.00 17.54  ? 214 GLN A N   1 
ATOM   1083 C  CA  . GLN A 1 160 ? 10.967 -15.867 -11.305 1.00 17.70  ? 214 GLN A CA  1 
ATOM   1084 C  C   . GLN A 1 160 ? 11.329 -14.536 -10.649 1.00 16.21  ? 214 GLN A C   1 
ATOM   1085 O  O   . GLN A 1 160 ? 11.191 -13.457 -11.252 1.00 16.15  ? 214 GLN A O   1 
ATOM   1086 C  CB  . GLN A 1 160 ? 12.185 -16.490 -11.984 1.00 20.05  ? 214 GLN A CB  1 
ATOM   1087 C  CG  . GLN A 1 160 ? 11.853 -17.802 -12.658 1.00 22.56  ? 214 GLN A CG  1 
ATOM   1088 C  CD  . GLN A 1 160 ? 13.057 -18.458 -13.293 1.00 28.62  ? 214 GLN A CD  1 
ATOM   1089 O  OE1 . GLN A 1 160 ? 14.166 -18.401 -12.762 1.00 34.36  ? 214 GLN A OE1 1 
ATOM   1090 N  NE2 . GLN A 1 160 ? 12.848 -19.074 -14.451 1.00 31.54  ? 214 GLN A NE2 1 
ATOM   1091 N  N   . TYR A 1 161 ? 11.797 -14.607 -9.411  1.00 15.95  ? 215 TYR A N   1 
ATOM   1092 C  CA  . TYR A 1 161 ? 12.126 -13.401 -8.668  1.00 15.72  ? 215 TYR A CA  1 
ATOM   1093 C  C   . TYR A 1 161 ? 13.378 -12.727 -9.206  1.00 15.14  ? 215 TYR A C   1 
ATOM   1094 O  O   . TYR A 1 161 ? 14.431 -13.360 -9.370  1.00 16.34  ? 215 TYR A O   1 
ATOM   1095 C  CB  . TYR A 1 161 ? 12.301 -13.721 -7.181  1.00 15.96  ? 215 TYR A CB  1 
ATOM   1096 C  CG  . TYR A 1 161 ? 12.657 -12.504 -6.369  1.00 16.02  ? 215 TYR A CG  1 
ATOM   1097 C  CD1 . TYR A 1 161 ? 11.728 -11.494 -6.161  1.00 17.78  ? 215 TYR A CD1 1 
ATOM   1098 C  CD2 . TYR A 1 161 ? 13.920 -12.365 -5.808  1.00 16.85  ? 215 TYR A CD2 1 
ATOM   1099 C  CE1 . TYR A 1 161 ? 12.053 -10.371 -5.423  1.00 17.65  ? 215 TYR A CE1 1 
ATOM   1100 C  CE2 . TYR A 1 161 ? 14.247 -11.251 -5.067  1.00 18.41  ? 215 TYR A CE2 1 
ATOM   1101 C  CZ  . TYR A 1 161 ? 13.315 -10.267 -4.875  1.00 17.40  ? 215 TYR A CZ  1 
ATOM   1102 O  OH  . TYR A 1 161 ? 13.678 -9.160  -4.138  1.00 19.82  ? 215 TYR A OH  1 
ATOM   1103 N  N   . HIS A 1 162 ? 13.273 -11.424 -9.450  1.00 15.41  ? 216 HIS A N   1 
ATOM   1104 C  CA  . HIS A 1 162 ? 14.394 -10.631 -9.955  1.00 16.14  ? 216 HIS A CA  1 
ATOM   1105 C  C   . HIS A 1 162 ? 14.643 -9.406  -9.099  1.00 13.98  ? 216 HIS A C   1 
ATOM   1106 O  O   . HIS A 1 162 ? 13.703 -8.807  -8.582  1.00 15.32  ? 216 HIS A O   1 
ATOM   1107 C  CB  . HIS A 1 162 ? 14.142 -10.160 -11.393 1.00 15.84  ? 216 HIS A CB  1 
ATOM   1108 C  CG  . HIS A 1 162 ? 14.245 -11.241 -12.424 1.00 14.44  ? 216 HIS A CG  1 
ATOM   1109 N  ND1 . HIS A 1 162 ? 13.335 -12.272 -12.528 1.00 16.20  ? 216 HIS A ND1 1 
ATOM   1110 C  CD2 . HIS A 1 162 ? 15.142 -11.426 -13.424 1.00 16.48  ? 216 HIS A CD2 1 
ATOM   1111 C  CE1 . HIS A 1 162 ? 13.673 -13.052 -13.543 1.00 16.83  ? 216 HIS A CE1 1 
ATOM   1112 N  NE2 . HIS A 1 162 ? 14.766 -12.560 -14.101 1.00 16.99  ? 216 HIS A NE2 1 
ATOM   1113 N  N   . VAL A 1 163 ? 15.914 -9.029  -8.989  1.00 14.38  ? 217 VAL A N   1 
ATOM   1114 C  CA  . VAL A 1 163 ? 16.313 -7.734  -8.463  1.00 14.09  ? 217 VAL A CA  1 
ATOM   1115 C  C   . VAL A 1 163 ? 16.815 -6.894  -9.632  1.00 13.49  ? 217 VAL A C   1 
ATOM   1116 O  O   . VAL A 1 163 ? 17.701 -7.323  -10.373 1.00 15.31  ? 217 VAL A O   1 
ATOM   1117 C  CB  . VAL A 1 163 ? 17.427 -7.870  -7.385  1.00 15.48  ? 217 VAL A CB  1 
ATOM   1118 C  CG1 . VAL A 1 163 ? 17.928 -6.476  -6.944  1.00 17.91  ? 217 VAL A CG1 1 
ATOM   1119 C  CG2 . VAL A 1 163 ? 16.940 -8.726  -6.189  1.00 17.25  ? 217 VAL A CG2 1 
ATOM   1120 N  N   . LEU A 1 164 ? 16.216 -5.724  -9.819  1.00 13.79  ? 218 LEU A N   1 
ATOM   1121 C  CA  . LEU A 1 164 ? 16.705 -4.755  -10.801 1.00 13.47  ? 218 LEU A CA  1 
ATOM   1122 C  C   . LEU A 1 164 ? 17.568 -3.742  -10.084 1.00 13.63  ? 218 LEU A C   1 
ATOM   1123 O  O   . LEU A 1 164 ? 17.078 -3.012  -9.232  1.00 14.88  ? 218 LEU A O   1 
ATOM   1124 C  CB  . LEU A 1 164 ? 15.550 -4.041  -11.521 1.00 13.62  ? 218 LEU A CB  1 
ATOM   1125 C  CG  . LEU A 1 164 ? 15.978 -2.839  -12.373 1.00 13.58  ? 218 LEU A CG  1 
ATOM   1126 C  CD1 . LEU A 1 164 ? 16.960 -3.228  -13.505 1.00 15.16  ? 218 LEU A CD1 1 
ATOM   1127 C  CD2 . LEU A 1 164 ? 14.760 -2.092  -12.927 1.00 15.81  ? 218 LEU A CD2 1 
ATOM   1128 N  N   . LEU A 1 165 ? 18.851 -3.728  -10.422 1.00 13.50  ? 219 LEU A N   1 
ATOM   1129 C  CA  . LEU A 1 165 ? 19.795 -2.756  -9.898  1.00 13.80  ? 219 LEU A CA  1 
ATOM   1130 C  C   . LEU A 1 165 ? 19.936 -1.619  -10.904 1.00 14.47  ? 219 LEU A C   1 
ATOM   1131 O  O   . LEU A 1 165 ? 20.489 -1.825  -11.977 1.00 16.64  ? 219 LEU A O   1 
ATOM   1132 C  CB  . LEU A 1 165 ? 21.146 -3.430  -9.644  1.00 15.42  ? 219 LEU A CB  1 
ATOM   1133 C  CG  . LEU A 1 165 ? 22.231 -2.580  -9.000  1.00 17.42  ? 219 LEU A CG  1 
ATOM   1134 C  CD1 . LEU A 1 165 ? 21.844 -2.322  -7.559  1.00 21.59  ? 219 LEU A CD1 1 
ATOM   1135 C  CD2 . LEU A 1 165 ? 23.613 -3.245  -9.105  1.00 18.09  ? 219 LEU A CD2 1 
ATOM   1136 N  N   . ILE A 1 166 ? 19.412 -0.452  -10.562 1.00 13.55  ? 220 ILE A N   1 
ATOM   1137 C  CA  . ILE A 1 166 ? 19.599 0.741   -11.379 1.00 14.08  ? 220 ILE A CA  1 
ATOM   1138 C  C   . ILE A 1 166 ? 20.691 1.583   -10.743 1.00 14.24  ? 220 ILE A C   1 
ATOM   1139 O  O   . ILE A 1 166 ? 20.585 1.932   -9.573  1.00 17.12  ? 220 ILE A O   1 
ATOM   1140 C  CB  . ILE A 1 166 ? 18.328 1.592   -11.487 1.00 14.74  ? 220 ILE A CB  1 
ATOM   1141 C  CG1 . ILE A 1 166 ? 17.145 0.774   -12.028 1.00 14.25  ? 220 ILE A CG1 1 
ATOM   1142 C  CG2 . ILE A 1 166 ? 18.589 2.803   -12.392 1.00 16.69  ? 220 ILE A CG2 1 
ATOM   1143 C  CD1 . ILE A 1 166 ? 15.845 1.530   -11.914 1.00 17.33  ? 220 ILE A CD1 1 
ATOM   1144 N  N   . ILE A 1 167 ? 21.734 1.902   -11.498 1.00 15.29  ? 221 ILE A N   1 
ATOM   1145 C  CA  . ILE A 1 167 ? 22.784 2.779   -10.986 1.00 14.74  ? 221 ILE A CA  1 
ATOM   1146 C  C   . ILE A 1 167 ? 22.705 4.081   -11.759 1.00 13.54  ? 221 ILE A C   1 
ATOM   1147 O  O   . ILE A 1 167 ? 22.726 4.055   -12.989 1.00 15.85  ? 221 ILE A O   1 
ATOM   1148 C  CB  . ILE A 1 167 ? 24.177 2.150   -11.126 1.00 16.24  ? 221 ILE A CB  1 
ATOM   1149 C  CG1 . ILE A 1 167 ? 24.156 0.704   -10.633 1.00 17.91  ? 221 ILE A CG1 1 
ATOM   1150 C  CG2 . ILE A 1 167 ? 25.179 2.953   -10.318 1.00 17.22  ? 221 ILE A CG2 1 
ATOM   1151 C  CD1 . ILE A 1 167 ? 25.362 -0.079  -11.050 1.00 21.39  ? 221 ILE A CD1 1 
ATOM   1152 N  N   . ALA A 1 168 ? 22.617 5.197   -11.043 1.00 15.28  ? 222 ALA A N   1 
ATOM   1153 C  CA  . ALA A 1 168 ? 22.401 6.489   -11.682 1.00 16.19  ? 222 ALA A CA  1 
ATOM   1154 C  C   . ALA A 1 168 ? 23.057 7.614   -10.903 1.00 17.03  ? 222 ALA A C   1 
ATOM   1155 O  O   . ALA A 1 168 ? 23.296 7.478   -9.709  1.00 18.42  ? 222 ALA A O   1 
ATOM   1156 C  CB  . ALA A 1 168 ? 20.904 6.764   -11.836 1.00 18.69  ? 222 ALA A CB  1 
ATOM   1157 N  N   . ASP A 1 169 ? 23.311 8.732   -11.586 1.00 20.13  ? 223 ASP A N   1 
ATOM   1158 C  CA  . ASP A 1 169 ? 24.020 9.874   -10.992 1.00 21.80  ? 223 ASP A CA  1 
ATOM   1159 C  C   . ASP A 1 169 ? 23.102 11.055  -10.814 1.00 23.82  ? 223 ASP A C   1 
ATOM   1160 O  O   . ASP A 1 169 ? 23.533 12.158  -10.486 1.00 25.80  ? 223 ASP A O   1 
ATOM   1161 C  CB  . ASP A 1 169 ? 25.209 10.297  -11.859 1.00 23.05  ? 223 ASP A CB  1 
ATOM   1162 C  CG  . ASP A 1 169 ? 24.788 11.113  -13.074 1.00 25.58  ? 223 ASP A CG  1 
ATOM   1163 O  OD1 . ASP A 1 169 ? 23.798 10.734  -13.732 1.00 28.36  ? 223 ASP A OD1 1 
ATOM   1164 O  OD2 . ASP A 1 169 ? 25.443 12.133  -13.380 1.00 25.42  ? 223 ASP A OD2 1 
ATOM   1165 N  N   . GLY A 1 170 ? 21.827 10.845  -11.056 1.00 24.36  ? 224 GLY A N   1 
ATOM   1166 C  CA  . GLY A 1 170 ? 20.914 11.951  -10.943 1.00 25.97  ? 224 GLY A CA  1 
ATOM   1167 C  C   . GLY A 1 170 ? 19.516 11.420  -10.849 1.00 25.09  ? 224 GLY A C   1 
ATOM   1168 O  O   . GLY A 1 170 ? 19.222 10.283  -11.223 1.00 26.43  ? 224 GLY A O   1 
ATOM   1169 N  N   . GLN A 1 171 ? 18.611 12.169  -10.244 1.00 25.52  ? 225 GLN A N   1 
ATOM   1170 C  CA  . GLN A 1 171 ? 17.210 11.862  -10.329 1.00 28.72  ? 225 GLN A CA  1 
ATOM   1171 C  C   . GLN A 1 171 ? 16.727 12.059  -11.769 1.00 24.18  ? 225 GLN A C   1 
ATOM   1172 O  O   . GLN A 1 171 ? 17.343 12.656  -12.551 1.00 24.50  ? 225 GLN A O   1 
ATOM   1173 C  CB  . GLN A 1 171 ? 16.399 12.783  -9.428  1.00 37.13  ? 225 GLN A CB  1 
ATOM   1174 C  CG  . GLN A 1 171 ? 14.943 12.411  -9.383  1.00 48.21  ? 225 GLN A CG  1 
ATOM   1175 C  CD  . GLN A 1 171 ? 14.770 10.949  -9.086  1.00 57.09  ? 225 GLN A CD  1 
ATOM   1176 O  OE1 . GLN A 1 171 ? 15.545 10.397  -8.319  1.00 63.87  ? 225 GLN A OE1 1 
ATOM   1177 N  NE2 . GLN A 1 171 ? 13.818 10.313  -9.711  1.00 57.00  ? 225 GLN A NE2 1 
ATOM   1178 N  N   . VAL A 1 172 ? 15.572 11.526  -12.045 1.00 23.35  ? 226 VAL A N   1 
ATOM   1179 C  CA  . VAL A 1 172 ? 14.840 11.668  -13.284 1.00 23.73  ? 226 VAL A CA  1 
ATOM   1180 C  C   . VAL A 1 172 ? 14.674 13.153  -13.659 1.00 24.36  ? 226 VAL A C   1 
ATOM   1181 O  O   . VAL A 1 172 ? 14.518 14.003  -12.780 1.00 26.25  ? 226 VAL A O   1 
ATOM   1182 C  CB  . VAL A 1 172 ? 13.484 10.964  -13.123 1.00 26.55  ? 226 VAL A CB  1 
ATOM   1183 C  CG1 . VAL A 1 172 ? 12.563 11.298  -14.199 1.00 30.41  ? 226 VAL A CG1 1 
ATOM   1184 C  CG2 . VAL A 1 172 ? 13.689 9.450   -13.022 1.00 27.61  ? 226 VAL A CG2 1 
ATOM   1185 N  N   . THR A 1 173 ? 14.757 13.462  -14.954 1.00 23.04  ? 227 THR A N   1 
ATOM   1186 C  CA  . THR A 1 173 ? 14.710 14.836  -15.445 1.00 22.65  ? 227 THR A CA  1 
ATOM   1187 C  C   . THR A 1 173 ? 13.487 15.594  -14.941 1.00 22.26  ? 227 THR A C   1 
ATOM   1188 O  O   . THR A 1 173 ? 12.369 15.071  -14.950 1.00 22.14  ? 227 THR A O   1 
ATOM   1189 C  CB  . THR A 1 173 ? 14.736 14.854  -16.986 1.00 21.41  ? 227 THR A CB  1 
ATOM   1190 O  OG1 . THR A 1 173 ? 15.996 14.323  -17.422 1.00 23.59  ? 227 THR A OG1 1 
ATOM   1191 C  CG2 . THR A 1 173 ? 14.570 16.260  -17.533 1.00 24.43  ? 227 THR A CG2 1 
ATOM   1192 N  N   . ARG A 1 174 ? 13.726 16.823  -14.483 1.00 24.39  ? 228 ARG A N   1 
ATOM   1193 C  CA  . ARG A 1 174 ? 12.683 17.696  -13.957 1.00 28.29  ? 228 ARG A CA  1 
ATOM   1194 C  C   . ARG A 1 174 ? 12.197 18.677  -15.015 1.00 27.01  ? 228 ARG A C   1 
ATOM   1195 O  O   . ARG A 1 174 ? 12.868 18.906  -16.020 1.00 27.06  ? 228 ARG A O   1 
ATOM   1196 C  CB  . ARG A 1 174 ? 13.199 18.464  -12.734 1.00 35.76  ? 228 ARG A CB  1 
ATOM   1197 C  CG  . ARG A 1 174 ? 13.300 17.617  -11.473 1.00 44.98  ? 228 ARG A CG  1 
ATOM   1198 C  CD  . ARG A 1 174 ? 14.017 18.335  -10.331 1.00 52.70  ? 228 ARG A CD  1 
ATOM   1199 N  NE  . ARG A 1 174 ? 14.168 19.770  -10.555 1.00 59.38  ? 228 ARG A NE  1 
ATOM   1200 C  CZ  . ARG A 1 174 ? 15.317 20.428  -10.445 1.00 63.85  ? 228 ARG A CZ  1 
ATOM   1201 N  NH1 . ARG A 1 174 ? 16.425 19.782  -10.109 1.00 64.65  ? 228 ARG A NH1 1 
ATOM   1202 N  NH2 . ARG A 1 174 ? 15.361 21.733  -10.674 1.00 66.01  ? 228 ARG A NH2 1 
ATOM   1203 N  N   . SER A 1 175 ? 11.030 19.263  -14.773 1.00 27.17  ? 229 SER A N   1 
ATOM   1204 C  CA  . SER A 1 175 ? 10.479 20.274  -15.660 1.00 30.00  ? 229 SER A CA  1 
ATOM   1205 C  C   . SER A 1 175 ? 11.346 21.523  -15.601 1.00 30.91  ? 229 SER A C   1 
ATOM   1206 O  O   . SER A 1 175 ? 11.935 21.816  -14.562 1.00 30.70  ? 229 SER A O   1 
ATOM   1207 C  CB  . SER A 1 175 ? 9.037  20.596  -15.264 1.00 33.44  ? 229 SER A CB  1 
ATOM   1208 O  OG  . SER A 1 175 ? 8.601  21.799  -15.865 1.00 37.71  ? 229 SER A OG  1 
ATOM   1209 N  N   . VAL A 1 176 ? 11.437 22.262  -16.701 1.00 33.44  ? 230 VAL A N   1 
ATOM   1210 C  CA  . VAL A 1 176 ? 12.224 23.489  -16.686 1.00 37.41  ? 230 VAL A CA  1 
ATOM   1211 C  C   . VAL A 1 176 ? 11.372 24.654  -16.196 1.00 42.38  ? 230 VAL A C   1 
ATOM   1212 O  O   . VAL A 1 176 ? 11.889 25.732  -15.895 1.00 43.36  ? 230 VAL A O   1 
ATOM   1213 C  CB  . VAL A 1 176 ? 12.821 23.823  -18.071 1.00 37.88  ? 230 VAL A CB  1 
ATOM   1214 C  CG1 . VAL A 1 176 ? 13.909 22.812  -18.447 1.00 37.41  ? 230 VAL A CG1 1 
ATOM   1215 C  CG2 . VAL A 1 176 ? 11.737 23.908  -19.133 1.00 38.74  ? 230 VAL A CG2 1 
ATOM   1216 N  N   . ASP A 1 177 ? 10.063 24.427  -16.117 1.00 46.40  ? 231 ASP A N   1 
ATOM   1217 C  CA  . ASP A 1 177 ? 9.150  25.390  -15.504 1.00 51.63  ? 231 ASP A CA  1 
ATOM   1218 C  C   . ASP A 1 177 ? 9.188  25.221  -13.991 1.00 55.01  ? 231 ASP A C   1 
ATOM   1219 O  O   . ASP A 1 177 ? 8.340  24.547  -13.402 1.00 55.01  ? 231 ASP A O   1 
ATOM   1220 C  CB  . ASP A 1 177 ? 7.724  25.221  -16.050 1.00 54.27  ? 231 ASP A CB  1 
ATOM   1221 C  CG  . ASP A 1 177 ? 6.708  26.163  -15.391 1.00 58.02  ? 231 ASP A CG  1 
ATOM   1222 O  OD1 . ASP A 1 177 ? 7.090  27.029  -14.576 1.00 59.11  ? 231 ASP A OD1 1 
ATOM   1223 O  OD2 . ASP A 1 177 ? 5.506  26.042  -15.716 1.00 59.51  ? 231 ASP A OD2 1 
ATOM   1224 N  N   . THR A 1 178 ? 10.175 25.849  -13.362 1.00 58.23  ? 232 THR A N   1 
ATOM   1225 C  CA  . THR A 1 178 ? 10.404 25.652  -11.938 1.00 61.26  ? 232 THR A CA  1 
ATOM   1226 C  C   . THR A 1 178 ? 9.397  26.396  -11.057 1.00 62.60  ? 232 THR A C   1 
ATOM   1227 O  O   . THR A 1 178 ? 9.434  26.257  -9.839  1.00 62.64  ? 232 THR A O   1 
ATOM   1228 C  CB  . THR A 1 178 ? 11.833 26.086  -11.530 1.00 62.74  ? 232 THR A CB  1 
ATOM   1229 O  OG1 . THR A 1 178 ? 12.075 27.429  -11.967 1.00 63.05  ? 232 THR A OG1 1 
ATOM   1230 C  CG2 . THR A 1 178 ? 12.878 25.156  -12.144 1.00 63.38  ? 232 THR A CG2 1 
ATOM   1231 N  N   . ASP A 1 179 ? 8.497  27.173  -11.656 1.00 64.17  ? 233 ASP A N   1 
ATOM   1232 C  CA  . ASP A 1 179 ? 7.500  27.884  -10.856 1.00 66.78  ? 233 ASP A CA  1 
ATOM   1233 C  C   . ASP A 1 179 ? 6.188  27.098  -10.705 1.00 69.74  ? 233 ASP A C   1 
ATOM   1234 O  O   . ASP A 1 179 ? 5.685  26.980  -9.583  1.00 70.18  ? 233 ASP A O   1 
ATOM   1235 C  CB  . ASP A 1 179 ? 7.227  29.280  -11.425 1.00 66.19  ? 233 ASP A CB  1 
ATOM   1236 C  CG  . ASP A 1 179 ? 6.586  30.198  -10.406 1.00 65.90  ? 233 ASP A CG  1 
ATOM   1237 O  OD1 . ASP A 1 179 ? 6.656  29.886  -9.197  1.00 65.61  ? 233 ASP A OD1 1 
ATOM   1238 O  OD2 . ASP A 1 179 ? 6.039  31.241  -10.811 1.00 66.02  ? 233 ASP A OD2 1 
ATOM   1239 N  N   . ASN A 1 180 ? 5.631  26.574  -11.801 1.00 71.62  ? 234 ASN A N   1 
ATOM   1240 C  CA  . ASN A 1 180 ? 4.341  25.985  -12.168 1.00 73.64  ? 234 ASN A CA  1 
ATOM   1241 C  C   . ASN A 1 180 ? 4.411  24.582  -12.770 1.00 73.32  ? 234 ASN A C   1 
ATOM   1242 O  O   . ASN A 1 180 ? 3.512  24.193  -13.532 1.00 73.29  ? 234 ASN A O   1 
ATOM   1243 C  CB  . ASN A 1 180 ? 3.573  26.920  -13.113 1.00 74.99  ? 234 ASN A CB  1 
ATOM   1244 C  CG  . ASN A 1 180 ? 3.260  28.282  -12.490 1.00 76.18  ? 234 ASN A CG  1 
ATOM   1245 O  OD1 . ASN A 1 180 ? 2.361  28.421  -11.657 1.00 77.06  ? 234 ASN A OD1 1 
ATOM   1246 N  ND2 . ASN A 1 180 ? 3.999  29.305  -12.922 1.00 76.34  ? 234 ASN A ND2 1 
ATOM   1247 N  N   . GLY A 1 181 ? 5.557  24.174  -13.324 1.00 72.58  ? 235 GLY A N   1 
ATOM   1248 C  CA  . GLY A 1 181 ? 5.585  22.948  -14.106 1.00 71.19  ? 235 GLY A CA  1 
ATOM   1249 C  C   . GLY A 1 181 ? 5.615  21.802  -13.115 1.00 69.86  ? 235 GLY A C   1 
ATOM   1250 O  O   . GLY A 1 181 ? 6.531  21.718  -12.300 1.00 71.97  ? 235 GLY A O   1 
ATOM   1251 N  N   . GLY A 1 182 ? 4.591  20.956  -13.143 1.00 65.32  ? 236 GLY A N   1 
ATOM   1252 C  CA  . GLY A 1 182 ? 4.464  19.873  -12.183 1.00 60.92  ? 236 GLY A CA  1 
ATOM   1253 C  C   . GLY A 1 182 ? 5.443  18.745  -12.447 1.00 56.04  ? 236 GLY A C   1 
ATOM   1254 O  O   . GLY A 1 182 ? 6.645  18.979  -12.570 1.00 56.13  ? 236 GLY A O   1 
ATOM   1255 N  N   . PHE A 1 183 ? 4.932  17.517  -12.529 1.00 51.26  ? 237 PHE A N   1 
ATOM   1256 C  CA  . PHE A 1 183 ? 5.759  16.379  -12.926 1.00 46.03  ? 237 PHE A CA  1 
ATOM   1257 C  C   . PHE A 1 183 ? 6.123  16.466  -14.398 1.00 39.02  ? 237 PHE A C   1 
ATOM   1258 O  O   . PHE A 1 183 ? 5.266  16.704  -15.249 1.00 39.75  ? 237 PHE A O   1 
ATOM   1259 C  CB  . PHE A 1 183 ? 5.056  15.040  -12.678 1.00 48.05  ? 237 PHE A CB  1 
ATOM   1260 C  CG  . PHE A 1 183 ? 4.883  14.685  -11.227 1.00 50.82  ? 237 PHE A CG  1 
ATOM   1261 C  CD1 . PHE A 1 183 ? 5.665  15.265  -10.244 1.00 52.25  ? 237 PHE A CD1 1 
ATOM   1262 C  CD2 . PHE A 1 183 ? 3.937  13.744  -10.855 1.00 51.63  ? 237 PHE A CD2 1 
ATOM   1263 C  CE1 . PHE A 1 183 ? 5.492  14.922  -8.910  1.00 52.94  ? 237 PHE A CE1 1 
ATOM   1264 C  CE2 . PHE A 1 183 ? 3.761  13.395  -9.531  1.00 52.10  ? 237 PHE A CE2 1 
ATOM   1265 C  CZ  . PHE A 1 183 ? 4.538  13.985  -8.556  1.00 52.53  ? 237 PHE A CZ  1 
ATOM   1266 N  N   . SER A 1 184 ? 7.399  16.256  -14.693 1.00 32.72  ? 238 SER A N   1 
ATOM   1267 C  CA  . SER A 1 184 ? 7.847  16.116  -16.066 1.00 27.50  ? 238 SER A CA  1 
ATOM   1268 C  C   . SER A 1 184 ? 7.321  14.794  -16.626 1.00 25.05  ? 238 SER A C   1 
ATOM   1269 O  O   . SER A 1 184 ? 6.893  13.921  -15.862 1.00 23.83  ? 238 SER A O   1 
ATOM   1270 C  CB  . SER A 1 184 ? 9.370  16.142  -16.138 1.00 26.61  ? 238 SER A CB  1 
ATOM   1271 O  OG  . SER A 1 184 ? 9.893  14.992  -15.481 1.00 24.97  ? 238 SER A OG  1 
ATOM   1272 N  N   . PRO A 1 185 ? 7.361  14.636  -17.958 1.00 25.63  ? 239 PRO A N   1 
ATOM   1273 C  CA  . PRO A 1 185 ? 7.019  13.345  -18.550 1.00 24.61  ? 239 PRO A CA  1 
ATOM   1274 C  C   . PRO A 1 185 ? 7.899  12.244  -17.990 1.00 22.78  ? 239 PRO A C   1 
ATOM   1275 O  O   . PRO A 1 185 ? 7.427  11.136  -17.765 1.00 23.37  ? 239 PRO A O   1 
ATOM   1276 C  CB  . PRO A 1 185 ? 7.276  13.564  -20.044 1.00 25.38  ? 239 PRO A CB  1 
ATOM   1277 C  CG  . PRO A 1 185 ? 7.047  15.024  -20.243 1.00 27.05  ? 239 PRO A CG  1 
ATOM   1278 C  CD  . PRO A 1 185 ? 7.541  15.679  -18.980 1.00 25.94  ? 239 PRO A CD  1 
ATOM   1279 N  N   . GLN A 1 186 ? 9.166  12.551  -17.732 1.00 22.09  ? 240 GLN A N   1 
ATOM   1280 C  CA  . GLN A 1 186 ? 10.089 11.542  -17.224 1.00 20.08  ? 240 GLN A CA  1 
ATOM   1281 C  C   . GLN A 1 186 ? 9.707  11.116  -15.816 1.00 20.21  ? 240 GLN A C   1 
ATOM   1282 O  O   . GLN A 1 186 ? 9.767  9.929   -15.478 1.00 19.41  ? 240 GLN A O   1 
ATOM   1283 C  CB  . GLN A 1 186 ? 11.530 12.059  -17.246 1.00 20.13  ? 240 GLN A CB  1 
ATOM   1284 C  CG  . GLN A 1 186 ? 12.094 12.284  -18.640 1.00 20.84  ? 240 GLN A CG  1 
ATOM   1285 C  CD  . GLN A 1 186 ? 11.632 13.590  -19.256 1.00 21.45  ? 240 GLN A CD  1 
ATOM   1286 O  OE1 . GLN A 1 186 ? 11.180 14.502  -18.561 1.00 22.85  ? 240 GLN A OE1 1 
ATOM   1287 N  NE2 . GLN A 1 186 ? 11.710 13.669  -20.573 1.00 23.42  ? 240 GLN A NE2 1 
ATOM   1288 N  N   . GLU A 1 187 ? 9.339  12.079  -14.985 1.00 21.57  ? 241 GLU A N   1 
ATOM   1289 C  CA  . GLU A 1 187 ? 8.914  11.792  -13.622 1.00 22.57  ? 241 GLU A CA  1 
ATOM   1290 C  C   . GLU A 1 187 ? 7.630  10.971  -13.597 1.00 22.31  ? 241 GLU A C   1 
ATOM   1291 O  O   . GLU A 1 187 ? 7.554  9.945   -12.919 1.00 21.62  ? 241 GLU A O   1 
ATOM   1292 C  CB  . GLU A 1 187 ? 8.729  13.102  -12.848 1.00 24.06  ? 241 GLU A CB  1 
ATOM   1293 C  CG  . GLU A 1 187 ? 10.043 13.750  -12.452 1.00 27.26  ? 241 GLU A CG  1 
ATOM   1294 C  CD  . GLU A 1 187 ? 9.889  15.195  -11.975 1.00 30.13  ? 241 GLU A CD  1 
ATOM   1295 O  OE1 . GLU A 1 187 ? 8.870  15.852  -12.294 1.00 31.91  ? 241 GLU A OE1 1 
ATOM   1296 O  OE2 . GLU A 1 187 ? 10.797 15.665  -11.260 1.00 32.62  ? 241 GLU A OE2 1 
ATOM   1297 N  N   . GLN A 1 188 ? 6.626  11.414  -14.350 1.00 23.07  ? 242 GLN A N   1 
ATOM   1298 C  CA  . GLN A 1 188 ? 5.353  10.697  -14.400 1.00 23.38  ? 242 GLN A CA  1 
ATOM   1299 C  C   . GLN A 1 188 ? 5.528  9.279   -14.959 1.00 22.53  ? 242 GLN A C   1 
ATOM   1300 O  O   . GLN A 1 188 ? 5.011  8.314   -14.392 1.00 22.95  ? 242 GLN A O   1 
ATOM   1301 C  CB  . GLN A 1 188 ? 4.330  11.472  -15.236 1.00 26.26  ? 242 GLN A CB  1 
ATOM   1302 C  CG  . GLN A 1 188 ? 2.943  10.853  -15.209 1.00 29.64  ? 242 GLN A CG  1 
ATOM   1303 C  CD  . GLN A 1 188 ? 2.322  10.894  -13.824 1.00 34.45  ? 242 GLN A CD  1 
ATOM   1304 O  OE1 . GLN A 1 188 ? 2.048  11.968  -13.288 1.00 38.68  ? 242 GLN A OE1 1 
ATOM   1305 N  NE2 . GLN A 1 188 ? 2.101  9.723   -13.236 1.00 34.60  ? 242 GLN A NE2 1 
ATOM   1306 N  N   . GLN A 1 189 ? 6.271  9.136   -16.050 1.00 21.90  ? 243 GLN A N   1 
ATOM   1307 C  CA  . GLN A 1 189 ? 6.445  7.808   -16.641 1.00 22.96  ? 243 GLN A CA  1 
ATOM   1308 C  C   . GLN A 1 189 ? 7.235  6.891   -15.719 1.00 19.65  ? 243 GLN A C   1 
ATOM   1309 O  O   . GLN A 1 189 ? 6.953  5.696   -15.624 1.00 19.88  ? 243 GLN A O   1 
ATOM   1310 C  CB  . GLN A 1 189 ? 7.125  7.901   -18.002 1.00 26.18  ? 243 GLN A CB  1 
ATOM   1311 C  CG  . GLN A 1 189 ? 6.181  8.428   -19.083 1.00 30.95  ? 243 GLN A CG  1 
ATOM   1312 C  CD  . GLN A 1 189 ? 6.900  8.866   -20.332 1.00 37.80  ? 243 GLN A CD  1 
ATOM   1313 O  OE1 . GLN A 1 189 ? 8.115  8.717   -20.449 1.00 42.19  ? 243 GLN A OE1 1 
ATOM   1314 N  NE2 . GLN A 1 189 ? 6.151  9.413   -21.282 1.00 41.11  ? 243 GLN A NE2 1 
ATOM   1315 N  N   . THR A 1 190 ? 8.211  7.443   -15.016 1.00 19.42  ? 244 THR A N   1 
ATOM   1316 C  CA  . THR A 1 190 ? 8.990  6.627   -14.092 1.00 18.42  ? 244 THR A CA  1 
ATOM   1317 C  C   . THR A 1 190 ? 8.144  6.172   -12.896 1.00 18.53  ? 244 THR A C   1 
ATOM   1318 O  O   . THR A 1 190 ? 8.200  5.003   -12.502 1.00 18.76  ? 244 THR A O   1 
ATOM   1319 C  CB  . THR A 1 190 ? 10.234 7.386   -13.604 1.00 17.00  ? 244 THR A CB  1 
ATOM   1320 O  OG1 . THR A 1 190 ? 11.132 7.563   -14.711 1.00 17.52  ? 244 THR A OG1 1 
ATOM   1321 C  CG2 . THR A 1 190 ? 10.938 6.620   -12.517 1.00 19.28  ? 244 THR A CG2 1 
ATOM   1322 N  N   . ILE A 1 191 ? 7.362  7.080   -12.329 1.00 18.89  ? 245 ILE A N   1 
ATOM   1323 C  CA  . ILE A 1 191 ? 6.468  6.730   -11.231 1.00 19.70  ? 245 ILE A CA  1 
ATOM   1324 C  C   . ILE A 1 191 ? 5.479  5.659   -11.682 1.00 19.58  ? 245 ILE A C   1 
ATOM   1325 O  O   . ILE A 1 191 ? 5.276  4.662   -10.981 1.00 20.02  ? 245 ILE A O   1 
ATOM   1326 C  CB  . ILE A 1 191 ? 5.719  7.979   -10.713 1.00 21.58  ? 245 ILE A CB  1 
ATOM   1327 C  CG1 . ILE A 1 191 ? 6.708  8.913   -10.008 1.00 23.69  ? 245 ILE A CG1 1 
ATOM   1328 C  CG2 . ILE A 1 191 ? 4.595  7.595   -9.757  1.00 22.47  ? 245 ILE A CG2 1 
ATOM   1329 C  CD1 . ILE A 1 191 ? 6.133  10.279  -9.671  1.00 25.62  ? 245 ILE A CD1 1 
ATOM   1330 N  N   . ASP A 1 192 ? 4.891  5.848   -12.858 1.00 19.32  ? 246 ASP A N   1 
ATOM   1331 C  CA  . ASP A 1 192 ? 3.939  4.881   -13.399 1.00 20.67  ? 246 ASP A CA  1 
ATOM   1332 C  C   . ASP A 1 192 ? 4.586  3.507   -13.556 1.00 19.67  ? 246 ASP A C   1 
ATOM   1333 O  O   . ASP A 1 192 ? 3.964  2.484   -13.258 1.00 19.56  ? 246 ASP A O   1 
ATOM   1334 C  CB  . ASP A 1 192 ? 3.389  5.341   -14.756 1.00 23.91  ? 246 ASP A CB  1 
ATOM   1335 C  CG  . ASP A 1 192 ? 2.493  6.572   -14.654 1.00 30.29  ? 246 ASP A CG  1 
ATOM   1336 O  OD1 . ASP A 1 192 ? 2.140  6.975   -13.529 1.00 31.36  ? 246 ASP A OD1 1 
ATOM   1337 O  OD2 . ASP A 1 192 ? 2.132  7.126   -15.717 1.00 34.05  ? 246 ASP A OD2 1 
ATOM   1338 N  N   . ALA A 1 193 ? 5.832  3.482   -14.018 1.00 18.46  ? 247 ALA A N   1 
ATOM   1339 C  CA  . ALA A 1 193 ? 6.526  2.219   -14.227 1.00 17.79  ? 247 ALA A CA  1 
ATOM   1340 C  C   . ALA A 1 193 ? 6.782  1.526   -12.902 1.00 17.71  ? 247 ALA A C   1 
ATOM   1341 O  O   . ALA A 1 193 ? 6.662  0.315   -12.811 1.00 17.18  ? 247 ALA A O   1 
ATOM   1342 C  CB  . ALA A 1 193 ? 7.842  2.439   -14.976 1.00 17.82  ? 247 ALA A CB  1 
ATOM   1343 N  N   . ILE A 1 194 ? 7.136  2.267   -11.880 1.00 17.35  ? 248 ILE A N   1 
ATOM   1344 C  CA  . ILE A 1 194 ? 7.290  1.690   -10.555 1.00 17.04  ? 248 ILE A CA  1 
ATOM   1345 C  C   . ILE A 1 194 ? 6.011  1.059   -10.042 1.00 17.03  ? 248 ILE A C   1 
ATOM   1346 O  O   . ILE A 1 194 ? 6.025  -0.004  -9.536  1.00 17.29  ? 248 ILE A O   1 
ATOM   1347 C  CB  . ILE A 1 194 ? 7.845  2.698   -9.547  1.00 17.26  ? 248 ILE A CB  1 
ATOM   1348 C  CG1 . ILE A 1 194 ? 9.290  3.109   -9.923  1.00 17.50  ? 248 ILE A CG1 1 
ATOM   1349 C  CG2 . ILE A 1 194 ? 7.846  2.128   -8.142  1.00 19.59  ? 248 ILE A CG2 1 
ATOM   1350 C  CD1 . ILE A 1 194 ? 9.819  4.308   -9.172  1.00 18.55  ? 248 ILE A CD1 1 
ATOM   1351 N  N   . VAL A 1 195 ? 4.906  1.738   -10.220 1.00 17.42  ? 249 VAL A N   1 
ATOM   1352 C  CA  . VAL A 1 195 ? 3.620  1.178   -9.844  1.00 18.85  ? 249 VAL A CA  1 
ATOM   1353 C  C   . VAL A 1 195 ? 3.267  -0.087  -10.630 1.00 18.15  ? 249 VAL A C   1 
ATOM   1354 O  O   . VAL A 1 195 ? 2.963  -1.089  -10.070 1.00 18.22  ? 249 VAL A O   1 
ATOM   1355 C  CB  . VAL A 1 195 ? 2.533  2.232   -9.974  1.00 18.79  ? 249 VAL A CB  1 
ATOM   1356 C  CG1 . VAL A 1 195 ? 1.216  1.616   -9.606  1.00 19.02  ? 249 VAL A CG1 1 
ATOM   1357 C  CG2 . VAL A 1 195 ? 2.804  3.381   -9.048  1.00 20.36  ? 249 VAL A CG2 1 
ATOM   1358 N  N   . ARG A 1 196 ? 3.370  -0.031  -11.931 1.00 17.85  ? 250 ARG A N   1 
ATOM   1359 C  CA  . ARG A 1 196 ? 3.090  -1.179  -12.749 1.00 19.14  ? 250 ARG A CA  1 
ATOM   1360 C  C   . ARG A 1 196 ? 4.011  -2.348  -12.406 1.00 18.52  ? 250 ARG A C   1 
ATOM   1361 O  O   . ARG A 1 196 ? 3.599  -3.442  -12.388 1.00 18.85  ? 250 ARG A O   1 
ATOM   1362 C  CB  . ARG A 1 196 ? 3.248  -0.872  -14.221 1.00 23.56  ? 250 ARG A CB  1 
ATOM   1363 C  CG  . ARG A 1 196 ? 2.189  -0.118  -14.962 1.00 30.55  ? 250 ARG A CG  1 
ATOM   1364 C  CD  . ARG A 1 196 ? 2.515  -0.164  -16.468 1.00 38.77  ? 250 ARG A CD  1 
ATOM   1365 N  NE  . ARG A 1 196 ? 2.517  -1.517  -17.071 1.00 46.89  ? 250 ARG A NE  1 
ATOM   1366 C  CZ  . ARG A 1 196 ? 2.812  -1.808  -18.355 1.00 48.76  ? 250 ARG A CZ  1 
ATOM   1367 N  NH1 . ARG A 1 196 ? 3.223  -0.888  -19.209 1.00 49.79  ? 250 ARG A NH1 1 
ATOM   1368 N  NH2 . ARG A 1 196 ? 2.728  -3.029  -18.791 1.00 48.96  ? 250 ARG A NH2 1 
ATOM   1369 N  N   . ALA A 1 197 ? 5.264  -2.050  -12.133 1.00 17.13  ? 251 ALA A N   1 
ATOM   1370 C  CA  . ALA A 1 197 ? 6.232  -3.088  -11.816 1.00 17.87  ? 251 ALA A CA  1 
ATOM   1371 C  C   . ALA A 1 197 ? 5.809  -3.886  -10.594 1.00 17.72  ? 251 ALA A C   1 
ATOM   1372 O  O   . ALA A 1 197 ? 6.220  -5.038  -10.445 1.00 17.72  ? 251 ALA A O   1 
ATOM   1373 C  CB  . ALA A 1 197 ? 7.598  -2.480  -11.590 1.00 17.31  ? 251 ALA A CB  1 
ATOM   1374 N  N   . SER A 1 198 ? 4.986  -3.299  -9.723  1.00 17.31  ? 252 SER A N   1 
ATOM   1375 C  CA  . SER A 1 198 ? 4.634  -3.981  -8.479  1.00 18.89  ? 252 SER A CA  1 
ATOM   1376 C  C   . SER A 1 198 ? 3.648  -5.137  -8.704  1.00 19.45  ? 252 SER A C   1 
ATOM   1377 O  O   . SER A 1 198 ? 3.296  -5.839  -7.758  1.00 21.15  ? 252 SER A O   1 
ATOM   1378 C  CB  . SER A 1 198 ? 4.079  -2.991  -7.441  1.00 20.15  ? 252 SER A CB  1 
ATOM   1379 O  OG  . SER A 1 198 ? 2.804  -2.482  -7.799  1.00 20.69  ? 252 SER A OG  1 
ATOM   1380 N  N   . GLU A 1 199 ? 3.225  -5.346  -9.948  1.00 18.80  ? 253 GLU A N   1 
ATOM   1381 C  CA  . GLU A 1 199 ? 2.448  -6.538  -10.305 1.00 20.07  ? 253 GLU A CA  1 
ATOM   1382 C  C   . GLU A 1 199 ? 3.344  -7.737  -10.630 1.00 19.64  ? 253 GLU A C   1 
ATOM   1383 O  O   . GLU A 1 199 ? 2.842  -8.818  -10.957 1.00 21.78  ? 253 GLU A O   1 
ATOM   1384 C  CB  . GLU A 1 199 ? 1.539  -6.247  -11.500 1.00 23.45  ? 253 GLU A CB  1 
ATOM   1385 C  CG  . GLU A 1 199 ? 0.433  -5.250  -11.210 1.00 30.06  ? 253 GLU A CG  1 
ATOM   1386 C  CD  . GLU A 1 199 ? -0.471 -5.020  -12.411 1.00 38.78  ? 253 GLU A CD  1 
ATOM   1387 O  OE1 . GLU A 1 199 ? -0.298 -5.718  -13.437 1.00 39.40  ? 253 GLU A OE1 1 
ATOM   1388 O  OE2 . GLU A 1 199 ? -1.349 -4.134  -12.331 1.00 44.60  ? 253 GLU A OE2 1 
ATOM   1389 N  N   . TYR A 1 200 ? 4.658  -7.545  -10.517 1.00 17.99  ? 254 TYR A N   1 
ATOM   1390 C  CA  . TYR A 1 200 ? 5.662  -8.553  -10.872 1.00 17.81  ? 254 TYR A CA  1 
ATOM   1391 C  C   . TYR A 1 200 ? 6.529  -8.874  -9.677  1.00 16.37  ? 254 TYR A C   1 
ATOM   1392 O  O   . TYR A 1 200 ? 6.732  -8.009  -8.829  1.00 17.48  ? 254 TYR A O   1 
ATOM   1393 C  CB  . TYR A 1 200 ? 6.543  -8.055  -12.031 1.00 16.73  ? 254 TYR A CB  1 
ATOM   1394 C  CG  . TYR A 1 200 ? 5.729  -7.793  -13.272 1.00 18.34  ? 254 TYR A CG  1 
ATOM   1395 C  CD1 . TYR A 1 200 ? 5.041  -6.592  -13.430 1.00 18.10  ? 254 TYR A CD1 1 
ATOM   1396 C  CD2 . TYR A 1 200 ? 5.609  -8.755  -14.271 1.00 19.48  ? 254 TYR A CD2 1 
ATOM   1397 C  CE1 . TYR A 1 200 ? 4.262  -6.360  -14.544 1.00 18.05  ? 254 TYR A CE1 1 
ATOM   1398 C  CE2 . TYR A 1 200 ? 4.844  -8.526  -15.392 1.00 20.44  ? 254 TYR A CE2 1 
ATOM   1399 C  CZ  . TYR A 1 200 ? 4.169  -7.328  -15.524 1.00 20.36  ? 254 TYR A CZ  1 
ATOM   1400 O  OH  . TYR A 1 200 ? 3.386  -7.096  -16.633 1.00 24.00  ? 254 TYR A OH  1 
ATOM   1401 N  N   . PRO A 1 201 ? 7.051  -10.112 -9.601  1.00 16.48  ? 255 PRO A N   1 
ATOM   1402 C  CA  . PRO A 1 201 ? 7.973  -10.488 -8.514  1.00 16.09  ? 255 PRO A CA  1 
ATOM   1403 C  C   . PRO A 1 201 ? 9.338  -9.862  -8.765  1.00 16.19  ? 255 PRO A C   1 
ATOM   1404 O  O   . PRO A 1 201 ? 10.276 -10.526 -9.205  1.00 16.13  ? 255 PRO A O   1 
ATOM   1405 C  CB  . PRO A 1 201 ? 8.007  -12.022 -8.589  1.00 16.95  ? 255 PRO A CB  1 
ATOM   1406 C  CG  . PRO A 1 201 ? 7.691  -12.321 -10.033 1.00 17.46  ? 255 PRO A CG  1 
ATOM   1407 C  CD  . PRO A 1 201 ? 6.687  -11.268 -10.444 1.00 17.59  ? 255 PRO A CD  1 
ATOM   1408 N  N   . LEU A 1 202 ? 9.418  -8.570  -8.477  1.00 16.32  ? 256 LEU A N   1 
ATOM   1409 C  CA  . LEU A 1 202 ? 10.544 -7.747  -8.894  1.00 16.36  ? 256 LEU A CA  1 
ATOM   1410 C  C   . LEU A 1 202 ? 10.834 -6.710  -7.829  1.00 15.75  ? 256 LEU A C   1 
ATOM   1411 O  O   . LEU A 1 202 ? 9.927  -5.985  -7.423  1.00 17.40  ? 256 LEU A O   1 
ATOM   1412 C  CB  . LEU A 1 202 ? 10.224 -7.073  -10.232 1.00 16.51  ? 256 LEU A CB  1 
ATOM   1413 C  CG  . LEU A 1 202 ? 11.188 -6.007  -10.761 1.00 16.96  ? 256 LEU A CG  1 
ATOM   1414 C  CD1 . LEU A 1 202 ? 12.526 -6.633  -11.131 1.00 16.92  ? 256 LEU A CD1 1 
ATOM   1415 C  CD2 . LEU A 1 202 ? 10.588 -5.276  -11.979 1.00 20.32  ? 256 LEU A CD2 1 
ATOM   1416 N  N   . SER A 1 203 ? 12.081 -6.651  -7.369  1.00 15.82  ? 257 SER A N   1 
ATOM   1417 C  CA  . SER A 1 203 ? 12.534 -5.583  -6.479  1.00 16.10  ? 257 SER A CA  1 
ATOM   1418 C  C   . SER A 1 203 ? 13.403 -4.615  -7.247  1.00 14.36  ? 257 SER A C   1 
ATOM   1419 O  O   . SER A 1 203 ? 14.300 -5.028  -7.976  1.00 17.03  ? 257 SER A O   1 
ATOM   1420 C  CB  . SER A 1 203 ? 13.323 -6.146  -5.308  1.00 16.63  ? 257 SER A CB  1 
ATOM   1421 O  OG  . SER A 1 203 ? 12.468 -6.831  -4.407  1.00 19.30  ? 257 SER A OG  1 
ATOM   1422 N  N   . ILE A 1 204 ? 13.146 -3.343  -7.091  1.00 14.69  ? 258 ILE A N   1 
ATOM   1423 C  CA  . ILE A 1 204 ? 13.933 -2.312  -7.742  1.00 15.56  ? 258 ILE A CA  1 
ATOM   1424 C  C   . ILE A 1 204 ? 14.826 -1.622  -6.727  1.00 15.50  ? 258 ILE A C   1 
ATOM   1425 O  O   . ILE A 1 204 ? 14.363 -1.114  -5.762  1.00 16.56  ? 258 ILE A O   1 
ATOM   1426 C  CB  . ILE A 1 204 ? 13.023 -1.270  -8.418  1.00 15.48  ? 258 ILE A CB  1 
ATOM   1427 C  CG1 . ILE A 1 204 ? 12.077 -1.938  -9.399  1.00 16.69  ? 258 ILE A CG1 1 
ATOM   1428 C  CG2 . ILE A 1 204 ? 13.839 -0.190  -9.114  1.00 17.58  ? 258 ILE A CG2 1 
ATOM   1429 C  CD1 . ILE A 1 204 ? 10.895 -1.081  -9.808  1.00 17.43  ? 258 ILE A CD1 1 
ATOM   1430 N  N   . VAL A 1 205 ? 16.113 -1.627  -6.992  1.00 14.72  ? 259 VAL A N   1 
ATOM   1431 C  CA  . VAL A 1 205 ? 17.086 -0.949  -6.154  1.00 16.04  ? 259 VAL A CA  1 
ATOM   1432 C  C   . VAL A 1 205 ? 17.785 0.151   -6.936  1.00 15.11  ? 259 VAL A C   1 
ATOM   1433 O  O   . VAL A 1 205 ? 18.473 -0.102  -7.861  1.00 16.37  ? 259 VAL A O   1 
ATOM   1434 C  CB  . VAL A 1 205 ? 18.146 -1.931  -5.659  1.00 16.16  ? 259 VAL A CB  1 
ATOM   1435 C  CG1 . VAL A 1 205 ? 19.144 -1.214  -4.786  1.00 18.51  ? 259 VAL A CG1 1 
ATOM   1436 C  CG2 . VAL A 1 205 ? 17.522 -3.064  -4.861  1.00 18.48  ? 259 VAL A CG2 1 
ATOM   1437 N  N   . LEU A 1 206 ? 17.550 1.385   -6.526  1.00 16.06  ? 260 LEU A N   1 
ATOM   1438 C  CA  . LEU A 1 206 ? 18.195 2.524   -7.174  1.00 16.16  ? 260 LEU A CA  1 
ATOM   1439 C  C   . LEU A 1 206 ? 19.425 2.929   -6.380  1.00 16.01  ? 260 LEU A C   1 
ATOM   1440 O  O   . LEU A 1 206 ? 19.312 3.297   -5.211  1.00 16.97  ? 260 LEU A O   1 
ATOM   1441 C  CB  . LEU A 1 206 ? 17.221 3.691   -7.298  1.00 17.97  ? 260 LEU A CB  1 
ATOM   1442 C  CG  . LEU A 1 206 ? 17.788 4.992   -7.868  1.00 19.03  ? 260 LEU A CG  1 
ATOM   1443 C  CD1 . LEU A 1 206 ? 18.254 4.774   -9.302  1.00 19.50  ? 260 LEU A CD1 1 
ATOM   1444 C  CD2 . LEU A 1 206 ? 16.756 6.104   -7.819  1.00 19.54  ? 260 LEU A CD2 1 
ATOM   1445 N  N   . VAL A 1 207 ? 20.586 2.838   -7.016  1.00 16.37  ? 261 VAL A N   1 
ATOM   1446 C  CA  . VAL A 1 207 ? 21.850 3.215   -6.400  1.00 16.97  ? 261 VAL A CA  1 
ATOM   1447 C  C   . VAL A 1 207 ? 22.276 4.581   -6.915  1.00 16.10  ? 261 VAL A C   1 
ATOM   1448 O  O   . VAL A 1 207 ? 22.484 4.774   -8.117  1.00 17.12  ? 261 VAL A O   1 
ATOM   1449 C  CB  . VAL A 1 207 ? 22.959 2.194   -6.704  1.00 17.30  ? 261 VAL A CB  1 
ATOM   1450 C  CG1 . VAL A 1 207 ? 24.273 2.649   -6.104  1.00 18.18  ? 261 VAL A CG1 1 
ATOM   1451 C  CG2 . VAL A 1 207 ? 22.594 0.808   -6.180  1.00 17.63  ? 261 VAL A CG2 1 
ATOM   1452 N  N   . GLY A 1 208 ? 22.393 5.533   -6.001  1.00 16.93  ? 262 GLY A N   1 
ATOM   1453 C  CA  . GLY A 1 208 ? 22.848 6.864   -6.349  1.00 17.29  ? 262 GLY A CA  1 
ATOM   1454 C  C   . GLY A 1 208 ? 24.351 6.980   -6.229  1.00 17.48  ? 262 GLY A C   1 
ATOM   1455 O  O   . GLY A 1 208 ? 24.913 6.764   -5.157  1.00 19.01  ? 262 GLY A O   1 
ATOM   1456 N  N   . VAL A 1 209 ? 25.003 7.321   -7.335  1.00 17.13  ? 263 VAL A N   1 
ATOM   1457 C  CA  . VAL A 1 209 ? 26.438 7.563   -7.339  1.00 17.36  ? 263 VAL A CA  1 
ATOM   1458 C  C   . VAL A 1 209 ? 26.704 9.038   -7.660  1.00 19.40  ? 263 VAL A C   1 
ATOM   1459 O  O   . VAL A 1 209 ? 25.788 9.771   -8.032  1.00 20.32  ? 263 VAL A O   1 
ATOM   1460 C  CB  . VAL A 1 209 ? 27.169 6.645   -8.354  1.00 17.67  ? 263 VAL A CB  1 
ATOM   1461 C  CG1 . VAL A 1 209 ? 27.032 5.169   -7.951  1.00 18.09  ? 263 VAL A CG1 1 
ATOM   1462 C  CG2 . VAL A 1 209 ? 26.638 6.862   -9.782  1.00 17.77  ? 263 VAL A CG2 1 
ATOM   1463 N  N   . GLY A 1 210 ? 27.948 9.482   -7.489  1.00 18.88  ? 264 GLY A N   1 
ATOM   1464 C  CA  . GLY A 1 210 ? 28.295 10.870  -7.752  1.00 20.84  ? 264 GLY A CA  1 
ATOM   1465 C  C   . GLY A 1 210 ? 27.808 11.838  -6.684  1.00 23.19  ? 264 GLY A C   1 
ATOM   1466 O  O   . GLY A 1 210 ? 27.387 11.417  -5.596  1.00 23.98  ? 264 GLY A O   1 
ATOM   1467 N  N   . ASP A 1 211 ? 27.868 13.122  -7.001  1.00 24.31  ? 265 ASP A N   1 
ATOM   1468 C  CA  . ASP A 1 211 ? 27.581 14.173  -6.049  1.00 27.50  ? 265 ASP A CA  1 
ATOM   1469 C  C   . ASP A 1 211 ? 26.120 14.452  -5.827  1.00 31.36  ? 265 ASP A C   1 
ATOM   1470 O  O   . ASP A 1 211 ? 25.769 15.050  -4.870  1.00 32.79  ? 265 ASP A O   1 
ATOM   1471 C  CB  . ASP A 1 211 ? 28.224 15.484  -6.499  1.00 29.63  ? 265 ASP A CB  1 
ATOM   1472 C  CG  . ASP A 1 211 ? 29.716 15.427  -6.605  1.00 30.91  ? 265 ASP A CG  1 
ATOM   1473 O  OD1 . ASP A 1 211 ? 30.365 14.544  -6.079  1.00 31.01  ? 265 ASP A OD1 1 
ATOM   1474 O  OD2 . ASP A 1 211 ? 30.246 16.319  -7.246  1.00 30.96  ? 265 ASP A OD2 1 
ATOM   1475 N  N   . GLY A 1 212 ? 25.268 14.011  -6.732  1.00 30.80  ? 266 GLY A N   1 
ATOM   1476 C  CA  . GLY A 1 212 ? 23.856 14.228  -6.585  1.00 32.34  ? 266 GLY A CA  1 
ATOM   1477 C  C   . GLY A 1 212 ? 23.436 15.536  -7.221  1.00 35.51  ? 266 GLY A C   1 
ATOM   1478 O  O   . GLY A 1 212 ? 23.962 15.834  -8.246  1.00 36.43  ? 266 GLY A O   1 
ATOM   1479 N  N   . PRO A 1 213 ? 22.443 16.339  -6.632  1.00 37.13  ? 267 PRO A N   1 
ATOM   1480 C  CA  . PRO A 1 213 ? 22.079 16.010  -5.253  1.00 37.60  ? 267 PRO A CA  1 
ATOM   1481 C  C   . PRO A 1 213 ? 21.106 14.881  -5.070  1.00 39.83  ? 267 PRO A C   1 
ATOM   1482 O  O   . PRO A 1 213 ? 20.421 14.553  -6.009  1.00 39.97  ? 267 PRO A O   1 
ATOM   1483 C  CB  . PRO A 1 213 ? 21.438 17.297  -4.739  1.00 37.99  ? 267 PRO A CB  1 
ATOM   1484 C  CG  . PRO A 1 213 ? 20.677 17.772  -5.878  1.00 38.19  ? 267 PRO A CG  1 
ATOM   1485 C  CD  . PRO A 1 213 ? 21.599 17.593  -7.013  1.00 37.89  ? 267 PRO A CD  1 
ATOM   1486 N  N   . TRP A 1 214 ? 21.100 14.301  -3.867  1.00 41.74  ? 268 TRP A N   1 
ATOM   1487 C  CA  . TRP A 1 214 ? 20.261 13.154  -3.542  1.00 42.66  ? 268 TRP A CA  1 
ATOM   1488 C  C   . TRP A 1 214 ? 19.376 13.444  -2.336  1.00 47.79  ? 268 TRP A C   1 
ATOM   1489 O  O   . TRP A 1 214 ? 18.977 12.529  -1.618  1.00 48.43  ? 268 TRP A O   1 
ATOM   1490 C  CB  . TRP A 1 214 ? 21.121 11.920  -3.258  1.00 38.98  ? 268 TRP A CB  1 
ATOM   1491 C  CG  . TRP A 1 214 ? 21.897 11.419  -4.435  1.00 35.00  ? 268 TRP A CG  1 
ATOM   1492 C  CD1 . TRP A 1 214 ? 23.251 11.428  -4.583  1.00 33.62  ? 268 TRP A CD1 1 
ATOM   1493 C  CD2 . TRP A 1 214 ? 21.366 10.824  -5.621  1.00 32.78  ? 268 TRP A CD2 1 
ATOM   1494 N  NE1 . TRP A 1 214 ? 23.598 10.882  -5.792  1.00 32.57  ? 268 TRP A NE1 1 
ATOM   1495 C  CE2 . TRP A 1 214 ? 22.459 10.498  -6.449  1.00 30.80  ? 268 TRP A CE2 1 
ATOM   1496 C  CE3 . TRP A 1 214 ? 20.073 10.536  -6.067  1.00 32.22  ? 268 TRP A CE3 1 
ATOM   1497 C  CZ2 . TRP A 1 214 ? 22.298 9.910   -7.697  1.00 30.83  ? 268 TRP A CZ2 1 
ATOM   1498 C  CZ3 . TRP A 1 214 ? 19.915 9.940   -7.303  1.00 33.17  ? 268 TRP A CZ3 1 
ATOM   1499 C  CH2 . TRP A 1 214 ? 21.023 9.628   -8.103  1.00 30.49  ? 268 TRP A CH2 1 
ATOM   1500 N  N   . ASP A 1 215 ? 19.079 14.700  -2.071  1.00 52.40  ? 269 ASP A N   1 
ATOM   1501 C  CA  . ASP A 1 215 ? 18.311 15.018  -0.900  1.00 57.33  ? 269 ASP A CA  1 
ATOM   1502 C  C   . ASP A 1 215 ? 16.839 15.214  -1.201  1.00 58.98  ? 269 ASP A C   1 
ATOM   1503 O  O   . ASP A 1 215 ? 16.091 15.594  -0.324  1.00 59.41  ? 269 ASP A O   1 
ATOM   1504 C  CB  . ASP A 1 215 ? 18.876 16.261  -0.244  1.00 60.27  ? 269 ASP A CB  1 
ATOM   1505 C  CG  . ASP A 1 215 ? 18.932 17.420  -1.181  1.00 62.58  ? 269 ASP A CG  1 
ATOM   1506 O  OD1 . ASP A 1 215 ? 18.606 17.260  -2.365  1.00 63.25  ? 269 ASP A OD1 1 
ATOM   1507 O  OD2 . ASP A 1 215 ? 19.297 18.506  -0.725  1.00 63.41  ? 269 ASP A OD2 1 
ATOM   1508 N  N   . THR A 1 216 ? 16.459 14.925  -2.439  1.00 59.71  ? 270 THR A N   1 
ATOM   1509 C  CA  . THR A 1 216 ? 15.088 14.937  -2.953  1.00 59.78  ? 270 THR A CA  1 
ATOM   1510 C  C   . THR A 1 216 ? 14.441 13.529  -3.114  1.00 58.30  ? 270 THR A C   1 
ATOM   1511 O  O   . THR A 1 216 ? 13.341 13.410  -3.584  1.00 57.71  ? 270 THR A O   1 
ATOM   1512 C  CB  . THR A 1 216 ? 15.111 15.665  -4.294  1.00 60.91  ? 270 THR A CB  1 
ATOM   1513 O  OG1 . THR A 1 216 ? 15.465 17.024  -4.067  1.00 61.79  ? 270 THR A OG1 1 
ATOM   1514 C  CG2 . THR A 1 216 ? 13.827 15.654  -4.987  1.00 61.00  ? 270 THR A CG2 1 
ATOM   1515 N  N   . MET A 1 217 ? 15.114 12.472  -2.680  1.00 57.83  ? 271 MET A N   1 
ATOM   1516 C  CA  . MET A 1 217 ? 14.623 11.119  -2.955  1.00 58.02  ? 271 MET A CA  1 
ATOM   1517 C  C   . MET A 1 217 ? 13.502 10.750  -2.064  1.00 58.93  ? 271 MET A C   1 
ATOM   1518 O  O   . MET A 1 217 ? 12.588 10.017  -2.414  1.00 56.75  ? 271 MET A O   1 
ATOM   1519 C  CB  . MET A 1 217 ? 15.722 10.125  -2.724  1.00 57.82  ? 271 MET A CB  1 
ATOM   1520 C  CG  . MET A 1 217 ? 16.653 10.065  -3.887  1.00 56.90  ? 271 MET A CG  1 
ATOM   1521 S  SD  . MET A 1 217 ? 15.736 9.931   -5.402  1.00 58.32  ? 271 MET A SD  1 
ATOM   1522 C  CE  . MET A 1 217 ? 14.926 8.369   -5.245  1.00 60.17  ? 271 MET A CE  1 
ATOM   1523 N  N   . ARG A 1 218 ? 13.580 11.275  -0.858  1.00 60.38  ? 272 ARG A N   1 
ATOM   1524 C  CA  . ARG A 1 218 ? 12.516 10.998  0.041   1.00 61.55  ? 272 ARG A CA  1 
ATOM   1525 C  C   . ARG A 1 218 ? 11.324 11.700  -0.498  1.00 59.84  ? 272 ARG A C   1 
ATOM   1526 O  O   . ARG A 1 218 ? 10.252 11.210  -0.308  1.00 59.20  ? 272 ARG A O   1 
ATOM   1527 C  CB  . ARG A 1 218 ? 12.831 11.491  1.441   1.00 64.34  ? 272 ARG A CB  1 
ATOM   1528 C  CG  . ARG A 1 218 ? 13.328 10.417  2.363   1.00 66.97  ? 272 ARG A CG  1 
ATOM   1529 C  CD  . ARG A 1 218 ? 13.419 10.970  3.760   1.00 69.46  ? 272 ARG A CD  1 
ATOM   1530 N  NE  . ARG A 1 218 ? 13.658 12.416  3.757   1.00 71.36  ? 272 ARG A NE  1 
ATOM   1531 C  CZ  . ARG A 1 218 ? 14.822 12.973  4.059   1.00 72.94  ? 272 ARG A CZ  1 
ATOM   1532 N  NH1 . ARG A 1 218 ? 15.861 12.206  4.398   1.00 73.25  ? 272 ARG A NH1 1 
ATOM   1533 N  NH2 . ARG A 1 218 ? 14.945 14.297  4.027   1.00 73.42  ? 272 ARG A NH2 1 
ATOM   1534 N  N   . GLN A 1 219 ? 11.461 12.711  -1.366  1.00 59.37  ? 273 GLN A N   1 
ATOM   1535 C  CA  . GLN A 1 219 ? 10.122 13.174  -1.743  1.00 58.71  ? 273 GLN A CA  1 
ATOM   1536 C  C   . GLN A 1 219 ? 9.592  12.420  -2.945  1.00 54.03  ? 273 GLN A C   1 
ATOM   1537 O  O   . GLN A 1 219 ? 8.407  12.090  -3.019  1.00 52.49  ? 273 GLN A O   1 
ATOM   1538 C  CB  . GLN A 1 219 ? 10.114 14.676  -2.042  1.00 62.77  ? 273 GLN A CB  1 
ATOM   1539 C  CG  . GLN A 1 219 ? 8.739  15.226  -2.444  1.00 66.68  ? 273 GLN A CG  1 
ATOM   1540 C  CD  . GLN A 1 219 ? 7.636  14.910  -1.441  1.00 70.69  ? 273 GLN A CD  1 
ATOM   1541 O  OE1 . GLN A 1 219 ? 7.818  15.054  -0.231  1.00 73.30  ? 273 GLN A OE1 1 
ATOM   1542 N  NE2 . GLN A 1 219 ? 6.483  14.474  -1.945  1.00 71.06  ? 273 GLN A NE2 1 
ATOM   1543 N  N   . PHE A 1 220 ? 10.461 11.956  -3.831  1.00 50.80  ? 274 PHE A N   1 
ATOM   1544 C  CA  . PHE A 1 220 ? 10.061 11.101  -4.928  1.00 48.64  ? 274 PHE A CA  1 
ATOM   1545 C  C   . PHE A 1 220 ? 9.309  9.874   -4.430  1.00 47.39  ? 274 PHE A C   1 
ATOM   1546 O  O   . PHE A 1 220 ? 8.330  9.442   -5.044  1.00 45.41  ? 274 PHE A O   1 
ATOM   1547 C  CB  . PHE A 1 220 ? 11.291 10.689  -5.721  1.00 48.22  ? 274 PHE A CB  1 
ATOM   1548 C  CG  . PHE A 1 220 ? 10.996 9.773   -6.869  1.00 48.49  ? 274 PHE A CG  1 
ATOM   1549 C  CD1 . PHE A 1 220 ? 10.545 10.277  -8.075  1.00 48.97  ? 274 PHE A CD1 1 
ATOM   1550 C  CD2 . PHE A 1 220 ? 11.183 8.407   -6.746  1.00 48.25  ? 274 PHE A CD2 1 
ATOM   1551 C  CE1 . PHE A 1 220 ? 10.280 9.441   -9.134  1.00 48.82  ? 274 PHE A CE1 1 
ATOM   1552 C  CE2 . PHE A 1 220 ? 10.920 7.565   -7.802  1.00 48.04  ? 274 PHE A CE2 1 
ATOM   1553 C  CZ  . PHE A 1 220 ? 10.467 8.081   -8.997  1.00 48.42  ? 274 PHE A CZ  1 
ATOM   1554 N  N   . ASP A 1 221 ? 9.769  9.323   -3.312  1.00 48.05  ? 275 ASP A N   1 
ATOM   1555 C  CA  . ASP A 1 221 ? 9.125  8.164   -2.718  1.00 49.29  ? 275 ASP A CA  1 
ATOM   1556 C  C   . ASP A 1 221 ? 7.698  8.502   -2.286  1.00 49.35  ? 275 ASP A C   1 
ATOM   1557 O  O   . ASP A 1 221 ? 6.778  7.720   -2.522  1.00 49.04  ? 275 ASP A O   1 
ATOM   1558 C  CB  . ASP A 1 221 ? 9.940  7.644   -1.533  1.00 50.40  ? 275 ASP A CB  1 
ATOM   1559 C  CG  . ASP A 1 221 ? 9.418  6.322   -1.006  1.00 52.05  ? 275 ASP A CG  1 
ATOM   1560 O  OD1 . ASP A 1 221 ? 9.505  5.315   -1.742  1.00 52.23  ? 275 ASP A OD1 1 
ATOM   1561 O  OD2 . ASP A 1 221 ? 8.931  6.285   0.144   1.00 53.26  ? 275 ASP A OD2 1 
ATOM   1562 N  N   . ASP A 1 222 ? 7.517  9.670   -1.668  1.00 50.38  ? 276 ASP A N   1 
ATOM   1563 C  CA  . ASP A 1 222 ? 6.148  10.032  -1.297  1.00 51.61  ? 276 ASP A CA  1 
ATOM   1564 C  C   . ASP A 1 222 ? 5.256  10.166  -2.516  1.00 50.04  ? 276 ASP A C   1 
ATOM   1565 O  O   . ASP A 1 222 ? 4.092  9.770   -2.501  1.00 51.65  ? 276 ASP A O   1 
ATOM   1566 C  CB  . ASP A 1 222 ? 6.101  11.364  -0.542  1.00 55.26  ? 276 ASP A CB  1 
ATOM   1567 C  CG  . ASP A 1 222 ? 6.977  11.383  0.689   1.00 59.49  ? 276 ASP A CG  1 
ATOM   1568 O  OD1 . ASP A 1 222 ? 7.329  10.297  1.193   1.00 60.44  ? 276 ASP A OD1 1 
ATOM   1569 O  OD2 . ASP A 1 222 ? 7.304  12.501  1.150   1.00 62.36  ? 276 ASP A OD2 1 
ATOM   1570 N  N   . ASN A 1 223 ? 5.809  10.548  -3.660  1.00 46.07  ? 277 ASN A N   1 
ATOM   1571 C  CA  . ASN A 1 223 ? 5.020  10.806  -4.854  1.00 42.42  ? 277 ASN A CA  1 
ATOM   1572 C  C   . ASN A 1 223 ? 4.623  9.541   -5.597  1.00 37.76  ? 277 ASN A C   1 
ATOM   1573 O  O   . ASN A 1 223 ? 3.895  9.611   -6.585  1.00 37.81  ? 277 ASN A O   1 
ATOM   1574 C  CB  . ASN A 1 223 ? 5.786  11.738  -5.795  1.00 44.49  ? 277 ASN A CB  1 
ATOM   1575 C  CG  . ASN A 1 223 ? 5.896  13.150  -5.252  1.00 46.88  ? 277 ASN A CG  1 
ATOM   1576 O  OD1 . ASN A 1 223 ? 5.083  13.579  -4.432  1.00 47.50  ? 277 ASN A OD1 1 
ATOM   1577 N  ND2 . ASN A 1 223 ? 6.902  13.880  -5.710  1.00 47.51  ? 277 ASN A ND2 1 
ATOM   1578 N  N   . ILE A 1 224 ? 5.110  8.392   -5.134  1.00 34.04  ? 278 ILE A N   1 
ATOM   1579 C  CA  . ILE A 1 224 ? 4.703  7.122   -5.719  1.00 30.96  ? 278 ILE A CA  1 
ATOM   1580 C  C   . ILE A 1 224 ? 3.423  6.624   -5.053  1.00 30.24  ? 278 ILE A C   1 
ATOM   1581 O  O   . ILE A 1 224 ? 3.378  6.481   -3.829  1.00 32.77  ? 278 ILE A O   1 
ATOM   1582 C  CB  . ILE A 1 224 ? 5.784  6.040   -5.575  1.00 29.42  ? 278 ILE A CB  1 
ATOM   1583 C  CG1 . ILE A 1 224 ? 7.155  6.550   -6.034  1.00 29.86  ? 278 ILE A CG1 1 
ATOM   1584 C  CG2 . ILE A 1 224 ? 5.393  4.798   -6.366  1.00 27.72  ? 278 ILE A CG2 1 
ATOM   1585 C  CD1 . ILE A 1 224 ? 8.312  5.644   -5.611  1.00 30.64  ? 278 ILE A CD1 1 
ATOM   1586 N  N   . PRO A 1 225 ? 2.380  6.354   -5.855  1.00 27.57  ? 279 PRO A N   1 
ATOM   1587 C  CA  . PRO A 1 225 ? 1.112  5.845   -5.317  1.00 27.34  ? 279 PRO A CA  1 
ATOM   1588 C  C   . PRO A 1 225 ? 1.303  4.564   -4.519  1.00 27.95  ? 279 PRO A C   1 
ATOM   1589 O  O   . PRO A 1 225 ? 2.272  3.839   -4.750  1.00 27.45  ? 279 PRO A O   1 
ATOM   1590 C  CB  . PRO A 1 225 ? 0.276  5.584   -6.576  1.00 27.84  ? 279 PRO A CB  1 
ATOM   1591 C  CG  . PRO A 1 225 ? 0.824  6.532   -7.589  1.00 27.05  ? 279 PRO A CG  1 
ATOM   1592 C  CD  . PRO A 1 225 ? 2.302  6.582   -7.308  1.00 27.49  ? 279 PRO A CD  1 
ATOM   1593 N  N   . ALA A 1 226 ? 0.391  4.302   -3.590  1.00 29.78  ? 280 ALA A N   1 
ATOM   1594 C  CA  . ALA A 1 226 ? 0.454  3.089   -2.784  1.00 31.31  ? 280 ALA A CA  1 
ATOM   1595 C  C   . ALA A 1 226 ? 0.441  1.849   -3.671  1.00 32.61  ? 280 ALA A C   1 
ATOM   1596 O  O   . ALA A 1 226 ? -0.263 1.800   -4.678  1.00 33.64  ? 280 ALA A O   1 
ATOM   1597 C  CB  . ALA A 1 226 ? -0.699 3.046   -1.791  1.00 33.60  ? 280 ALA A CB  1 
ATOM   1598 N  N   . ARG A 1 227 ? 1.243  0.861   -3.290  1.00 31.16  ? 281 ARG A N   1 
ATOM   1599 C  CA  . ARG A 1 227 ? 1.364  -0.387  -4.033  1.00 29.61  ? 281 ARG A CA  1 
ATOM   1600 C  C   . ARG A 1 227 ? 1.095  -1.558  -3.105  1.00 30.65  ? 281 ARG A C   1 
ATOM   1601 O  O   . ARG A 1 227 ? 1.057  -1.385  -1.891  1.00 30.45  ? 281 ARG A O   1 
ATOM   1602 C  CB  . ARG A 1 227 ? 2.755  -0.522  -4.647  1.00 26.32  ? 281 ARG A CB  1 
ATOM   1603 C  CG  . ARG A 1 227 ? 3.040  0.437   -5.773  1.00 23.48  ? 281 ARG A CG  1 
ATOM   1604 C  CD  . ARG A 1 227 ? 4.474  0.885   -5.693  1.00 23.80  ? 281 ARG A CD  1 
ATOM   1605 N  NE  . ARG A 1 227 ? 4.634  1.887   -4.644  1.00 27.42  ? 281 ARG A NE  1 
ATOM   1606 C  CZ  . ARG A 1 227 ? 5.780  2.136   -4.022  1.00 27.70  ? 281 ARG A CZ  1 
ATOM   1607 N  NH1 . ARG A 1 227 ? 6.870  1.447   -4.334  1.00 25.23  ? 281 ARG A NH1 1 
ATOM   1608 N  NH2 . ARG A 1 227 ? 5.833  3.066   -3.078  1.00 29.73  ? 281 ARG A NH2 1 
ATOM   1609 N  N   . ALA A 1 228 ? 0.937  -2.749  -3.676  1.00 31.62  ? 282 ALA A N   1 
ATOM   1610 C  CA  . ALA A 1 228 ? 0.675  -3.944  -2.879  1.00 31.56  ? 282 ALA A CA  1 
ATOM   1611 C  C   . ALA A 1 228 ? 1.892  -4.310  -2.040  1.00 28.01  ? 282 ALA A C   1 
ATOM   1612 O  O   . ALA A 1 228 ? 1.762  -4.847  -0.945  1.00 28.77  ? 282 ALA A O   1 
ATOM   1613 C  CB  . ALA A 1 228 ? 0.275  -5.100  -3.769  1.00 33.55  ? 282 ALA A CB  1 
ATOM   1614 N  N   . PHE A 1 229 ? 3.087  -4.040  -2.555  1.00 28.92  ? 283 PHE A N   1 
ATOM   1615 C  CA  . PHE A 1 229 ? 4.271  -4.147  -1.708  1.00 29.70  ? 283 PHE A CA  1 
ATOM   1616 C  C   . PHE A 1 229 ? 5.253  -3.047  -2.056  1.00 30.27  ? 283 PHE A C   1 
ATOM   1617 O  O   . PHE A 1 229 ? 5.213  -2.490  -3.155  1.00 31.85  ? 283 PHE A O   1 
ATOM   1618 C  CB  . PHE A 1 229 ? 4.924  -5.548  -1.802  1.00 26.68  ? 283 PHE A CB  1 
ATOM   1619 C  CG  . PHE A 1 229 ? 5.689  -5.827  -3.086  1.00 26.14  ? 283 PHE A CG  1 
ATOM   1620 C  CD1 . PHE A 1 229 ? 5.027  -6.075  -4.279  1.00 23.99  ? 283 PHE A CD1 1 
ATOM   1621 C  CD2 . PHE A 1 229 ? 7.074  -5.907  -3.076  1.00 26.31  ? 283 PHE A CD2 1 
ATOM   1622 C  CE1 . PHE A 1 229 ? 5.734  -6.361  -5.445  1.00 21.81  ? 283 PHE A CE1 1 
ATOM   1623 C  CE2 . PHE A 1 229 ? 7.788  -6.197  -4.244  1.00 24.93  ? 283 PHE A CE2 1 
ATOM   1624 C  CZ  . PHE A 1 229 ? 7.110  -6.423  -5.434  1.00 22.51  ? 283 PHE A CZ  1 
ATOM   1625 N  N   . ASP A 1 230 ? 6.083  -2.679  -1.088  1.00 32.75  ? 284 ASP A N   1 
ATOM   1626 C  CA  . ASP A 1 230 ? 7.099  -1.674  -1.325  1.00 32.75  ? 284 ASP A CA  1 
ATOM   1627 C  C   . ASP A 1 230 ? 8.179  -2.337  -2.148  1.00 27.50  ? 284 ASP A C   1 
ATOM   1628 O  O   . ASP A 1 230 ? 9.011  -3.076  -1.629  1.00 32.27  ? 284 ASP A O   1 
ATOM   1629 C  CB  . ASP A 1 230 ? 7.670  -1.105  -0.025  1.00 38.41  ? 284 ASP A CB  1 
ATOM   1630 C  CG  . ASP A 1 230 ? 8.454  0.180   -0.250  1.00 43.95  ? 284 ASP A CG  1 
ATOM   1631 O  OD1 . ASP A 1 230 ? 8.786  0.486   -1.418  1.00 42.51  ? 284 ASP A OD1 1 
ATOM   1632 O  OD2 . ASP A 1 230 ? 8.742  0.884   0.740   1.00 49.06  ? 284 ASP A OD2 1 
ATOM   1633 N  N   . ASN A 1 231 ? 8.132  -2.075  -3.444  1.00 21.16  ? 285 ASN A N   1 
ATOM   1634 C  CA  . ASN A 1 231 ? 9.016  -2.703  -4.410  1.00 18.50  ? 285 ASN A CA  1 
ATOM   1635 C  C   . ASN A 1 231 ? 10.214 -1.841  -4.771  1.00 16.87  ? 285 ASN A C   1 
ATOM   1636 O  O   . ASN A 1 231 ? 10.957 -2.178  -5.689  1.00 19.03  ? 285 ASN A O   1 
ATOM   1637 C  CB  . ASN A 1 231 ? 8.240  -3.034  -5.688  1.00 18.88  ? 285 ASN A CB  1 
ATOM   1638 C  CG  . ASN A 1 231 ? 7.702  -1.794  -6.390  1.00 17.58  ? 285 ASN A CG  1 
ATOM   1639 O  OD1 . ASN A 1 231 ? 7.403  -0.778  -5.756  1.00 21.28  ? 285 ASN A OD1 1 
ATOM   1640 N  ND2 . ASN A 1 231 ? 7.561  -1.879  -7.695  1.00 18.37  ? 285 ASN A ND2 1 
ATOM   1641 N  N   . PHE A 1 232 ? 10.384 -0.717  -4.085  1.00 19.13  ? 286 PHE A N   1 
ATOM   1642 C  CA  . PHE A 1 232 ? 11.384 0.262   -4.490  1.00 20.92  ? 286 PHE A CA  1 
ATOM   1643 C  C   . PHE A 1 232 ? 12.224 0.721   -3.301  1.00 21.91  ? 286 PHE A C   1 
ATOM   1644 O  O   . PHE A 1 232 ? 11.686 1.009   -2.231  1.00 26.90  ? 286 PHE A O   1 
ATOM   1645 C  CB  . PHE A 1 232 ? 10.702 1.458   -5.160  1.00 22.93  ? 286 PHE A CB  1 
ATOM   1646 C  CG  . PHE A 1 232 ? 11.653 2.531   -5.589  1.00 22.58  ? 286 PHE A CG  1 
ATOM   1647 C  CD1 . PHE A 1 232 ? 12.333 2.432   -6.793  1.00 22.28  ? 286 PHE A CD1 1 
ATOM   1648 C  CD2 . PHE A 1 232 ? 11.866 3.645   -4.788  1.00 25.35  ? 286 PHE A CD2 1 
ATOM   1649 C  CE1 . PHE A 1 232 ? 13.217 3.424   -7.191  1.00 24.39  ? 286 PHE A CE1 1 
ATOM   1650 C  CE2 . PHE A 1 232 ? 12.747 4.637   -5.178  1.00 27.55  ? 286 PHE A CE2 1 
ATOM   1651 C  CZ  . PHE A 1 232 ? 13.425 4.523   -6.379  1.00 26.55  ? 286 PHE A CZ  1 
ATOM   1652 N  N   . GLN A 1 233 ? 13.520 0.813   -3.499  1.00 20.33  ? 287 GLN A N   1 
ATOM   1653 C  CA  . GLN A 1 233 ? 14.431 1.281   -2.475  1.00 21.40  ? 287 GLN A CA  1 
ATOM   1654 C  C   . GLN A 1 233 ? 15.538 2.095   -3.097  1.00 19.16  ? 287 GLN A C   1 
ATOM   1655 O  O   . GLN A 1 233 ? 15.946 1.815   -4.164  1.00 19.68  ? 287 GLN A O   1 
ATOM   1656 C  CB  . GLN A 1 233 ? 15.028 0.126   -1.683  1.00 24.98  ? 287 GLN A CB  1 
ATOM   1657 C  CG  . GLN A 1 233 ? 15.668 -0.986  -2.487  1.00 30.34  ? 287 GLN A CG  1 
ATOM   1658 C  CD  . GLN A 1 233 ? 15.302 -2.400  -2.033  1.00 38.69  ? 287 GLN A CD  1 
ATOM   1659 O  OE1 . GLN A 1 233 ? 15.723 -2.806  -0.987  1.00 44.97  ? 287 GLN A OE1 1 
ATOM   1660 N  NE2 . GLN A 1 233 ? 14.534 -3.139  -2.828  1.00 36.68  ? 287 GLN A NE2 1 
ATOM   1661 N  N   . PHE A 1 234 ? 16.005 3.096   -2.377  1.00 20.79  ? 288 PHE A N   1 
ATOM   1662 C  CA  . PHE A 1 234 ? 17.129 3.920   -2.789  1.00 19.31  ? 288 PHE A CA  1 
ATOM   1663 C  C   . PHE A 1 234 ? 18.281 3.783   -1.804  1.00 20.49  ? 288 PHE A C   1 
ATOM   1664 O  O   . PHE A 1 234 ? 18.068 3.721   -0.584  1.00 23.37  ? 288 PHE A O   1 
ATOM   1665 C  CB  . PHE A 1 234 ? 16.711 5.388   -2.881  1.00 19.85  ? 288 PHE A CB  1 
ATOM   1666 C  CG  . PHE A 1 234 ? 17.865 6.342   -3.085  1.00 20.78  ? 288 PHE A CG  1 
ATOM   1667 C  CD1 . PHE A 1 234 ? 18.482 6.440   -4.318  1.00 21.57  ? 288 PHE A CD1 1 
ATOM   1668 C  CD2 . PHE A 1 234 ? 18.321 7.140   -2.050  1.00 22.03  ? 288 PHE A CD2 1 
ATOM   1669 C  CE1 . PHE A 1 234 ? 19.542 7.308   -4.517  1.00 22.51  ? 288 PHE A CE1 1 
ATOM   1670 C  CE2 . PHE A 1 234 ? 19.385 8.017   -2.246  1.00 22.08  ? 288 PHE A CE2 1 
ATOM   1671 C  CZ  . PHE A 1 234 ? 19.986 8.103   -3.477  1.00 21.68  ? 288 PHE A CZ  1 
ATOM   1672 N  N   . VAL A 1 235 ? 19.503 3.753   -2.321  1.00 18.39  ? 289 VAL A N   1 
ATOM   1673 C  CA  . VAL A 1 235 ? 20.684 3.783   -1.471  1.00 18.83  ? 289 VAL A CA  1 
ATOM   1674 C  C   . VAL A 1 235 ? 21.688 4.755   -2.060  1.00 18.24  ? 289 VAL A C   1 
ATOM   1675 O  O   . VAL A 1 235 ? 21.942 4.745   -3.276  1.00 18.21  ? 289 VAL A O   1 
ATOM   1676 C  CB  . VAL A 1 235 ? 21.313 2.372   -1.298  1.00 21.61  ? 289 VAL A CB  1 
ATOM   1677 C  CG1 . VAL A 1 235 ? 21.583 1.707   -2.654  1.00 22.34  ? 289 VAL A CG1 1 
ATOM   1678 C  CG2 . VAL A 1 235 ? 22.595 2.442   -0.464  1.00 22.36  ? 289 VAL A CG2 1 
ATOM   1679 N  N   . ASN A 1 236 ? 22.234 5.612   -1.206  1.00 19.74  ? 290 ASN A N   1 
ATOM   1680 C  CA  . ASN A 1 236 ? 23.281 6.530   -1.626  1.00 20.18  ? 290 ASN A CA  1 
ATOM   1681 C  C   . ASN A 1 236 ? 24.655 5.876   -1.462  1.00 19.73  ? 290 ASN A C   1 
ATOM   1682 O  O   . ASN A 1 236 ? 25.159 5.714   -0.341  1.00 20.60  ? 290 ASN A O   1 
ATOM   1683 C  CB  . ASN A 1 236 ? 23.200 7.841   -0.829  1.00 22.20  ? 290 ASN A CB  1 
ATOM   1684 C  CG  . ASN A 1 236 ? 24.126 8.917   -1.373  1.00 24.91  ? 290 ASN A CG  1 
ATOM   1685 O  OD1 . ASN A 1 236 ? 25.277 8.654   -1.712  1.00 25.66  ? 290 ASN A OD1 1 
ATOM   1686 N  ND2 . ASN A 1 236 ? 23.620 10.143  -1.456  1.00 29.01  ? 290 ASN A ND2 1 
ATOM   1687 N  N   . PHE A 1 237 ? 25.244 5.488   -2.586  1.00 18.38  ? 291 PHE A N   1 
ATOM   1688 C  CA  . PHE A 1 237 ? 26.551 4.837   -2.619  1.00 19.12  ? 291 PHE A CA  1 
ATOM   1689 C  C   . PHE A 1 237 ? 27.632 5.799   -2.146  1.00 19.94  ? 291 PHE A C   1 
ATOM   1690 O  O   . PHE A 1 237 ? 28.493 5.425   -1.348  1.00 21.96  ? 291 PHE A O   1 
ATOM   1691 C  CB  . PHE A 1 237 ? 26.827 4.326   -4.044  1.00 19.53  ? 291 PHE A CB  1 
ATOM   1692 C  CG  . PHE A 1 237 ? 28.256 3.884   -4.311  1.00 20.39  ? 291 PHE A CG  1 
ATOM   1693 C  CD1 . PHE A 1 237 ? 29.224 4.808   -4.668  1.00 20.35  ? 291 PHE A CD1 1 
ATOM   1694 C  CD2 . PHE A 1 237 ? 28.600 2.535   -4.308  1.00 20.45  ? 291 PHE A CD2 1 
ATOM   1695 C  CE1 . PHE A 1 237 ? 30.528 4.413   -4.949  1.00 21.16  ? 291 PHE A CE1 1 
ATOM   1696 C  CE2 . PHE A 1 237 ? 29.905 2.135   -4.598  1.00 20.28  ? 291 PHE A CE2 1 
ATOM   1697 C  CZ  . PHE A 1 237 ? 30.865 3.079   -4.917  1.00 20.02  ? 291 PHE A CZ  1 
ATOM   1698 N  N   . THR A 1 238 ? 27.572 7.040   -2.625  1.00 20.66  ? 292 THR A N   1 
ATOM   1699 C  CA  . THR A 1 238 ? 28.615 8.021   -2.347  1.00 22.14  ? 292 THR A CA  1 
ATOM   1700 C  C   . THR A 1 238 ? 28.773 8.274   -0.853  1.00 23.69  ? 292 THR A C   1 
ATOM   1701 O  O   . THR A 1 238 ? 29.896 8.310   -0.340  1.00 26.12  ? 292 THR A O   1 
ATOM   1702 C  CB  . THR A 1 238 ? 28.328 9.350   -3.059  1.00 24.17  ? 292 THR A CB  1 
ATOM   1703 O  OG1 . THR A 1 238 ? 28.139 9.096   -4.454  1.00 24.22  ? 292 THR A OG1 1 
ATOM   1704 C  CG2 . THR A 1 238 ? 29.487 10.331  -2.855  1.00 25.59  ? 292 THR A CG2 1 
ATOM   1705 N  N   . ASP A 1 239 ? 27.651 8.420   -0.156  1.00 25.05  ? 293 ASP A N   1 
ATOM   1706 C  CA  . ASP A 1 239 ? 27.664 8.738   1.272   1.00 28.58  ? 293 ASP A CA  1 
ATOM   1707 C  C   . ASP A 1 239 ? 28.285 7.620   2.111   1.00 26.64  ? 293 ASP A C   1 
ATOM   1708 O  O   . ASP A 1 239 ? 28.975 7.887   3.093   1.00 29.02  ? 293 ASP A O   1 
ATOM   1709 C  CB  . ASP A 1 239 ? 26.246 9.029   1.768   1.00 32.11  ? 293 ASP A CB  1 
ATOM   1710 C  CG  . ASP A 1 239 ? 25.779 10.431  1.423   1.00 36.87  ? 293 ASP A CG  1 
ATOM   1711 O  OD1 . ASP A 1 239 ? 26.571 11.215  0.848   1.00 36.61  ? 293 ASP A OD1 1 
ATOM   1712 O  OD2 . ASP A 1 239 ? 24.610 10.750  1.733   1.00 42.64  ? 293 ASP A OD2 1 
ATOM   1713 N  N   . ILE A 1 240 ? 28.048 6.371   1.725   1.00 24.44  ? 294 ILE A N   1 
ATOM   1714 C  CA  . ILE A 1 240 ? 28.649 5.247   2.433   1.00 23.35  ? 294 ILE A CA  1 
ATOM   1715 C  C   . ILE A 1 240 ? 30.124 5.084   2.083   1.00 24.42  ? 294 ILE A C   1 
ATOM   1716 O  O   . ILE A 1 240 ? 30.963 4.916   2.974   1.00 26.08  ? 294 ILE A O   1 
ATOM   1717 C  CB  . ILE A 1 240 ? 27.909 3.938   2.117   1.00 23.88  ? 294 ILE A CB  1 
ATOM   1718 C  CG1 . ILE A 1 240 ? 26.493 4.001   2.682   1.00 26.20  ? 294 ILE A CG1 1 
ATOM   1719 C  CG2 . ILE A 1 240 ? 28.673 2.743   2.696   1.00 23.71  ? 294 ILE A CG2 1 
ATOM   1720 C  CD1 . ILE A 1 240 ? 25.570 2.933   2.127   1.00 26.02  ? 294 ILE A CD1 1 
ATOM   1721 N  N   . MET A 1 241 ? 30.450 5.161   0.798   1.00 24.66  ? 295 MET A N   1 
ATOM   1722 C  CA  . MET A 1 241 ? 31.784 4.792   0.331   1.00 26.54  ? 295 MET A CA  1 
ATOM   1723 C  C   . MET A 1 241 ? 32.828 5.880   0.585   1.00 29.21  ? 295 MET A C   1 
ATOM   1724 O  O   . MET A 1 241 ? 34.028 5.663   0.390   1.00 31.16  ? 295 MET A O   1 
ATOM   1725 C  CB  . MET A 1 241 ? 31.730 4.424   -1.157  1.00 25.72  ? 295 MET A CB  1 
ATOM   1726 C  CG  . MET A 1 241 ? 30.916 3.154   -1.435  1.00 26.32  ? 295 MET A CG  1 
ATOM   1727 S  SD  . MET A 1 241 ? 31.602 1.643   -0.682  1.00 28.59  ? 295 MET A SD  1 
ATOM   1728 C  CE  . MET A 1 241 ? 33.186 1.550   -1.522  1.00 30.88  ? 295 MET A CE  1 
ATOM   1729 N  N   . SER A 1 242 ? 32.375 7.039   1.048   1.00 29.34  ? 296 SER A N   1 
ATOM   1730 C  CA  . SER A 1 242 ? 33.284 8.121   1.398   1.00 32.46  ? 296 SER A CA  1 
ATOM   1731 C  C   . SER A 1 242 ? 33.660 8.080   2.875   1.00 35.31  ? 296 SER A C   1 
ATOM   1732 O  O   . SER A 1 242 ? 34.523 8.836   3.317   1.00 37.73  ? 296 SER A O   1 
ATOM   1733 C  CB  . SER A 1 242 ? 32.665 9.476   1.063   1.00 34.06  ? 296 SER A CB  1 
ATOM   1734 O  OG  . SER A 1 242 ? 31.523 9.729   1.866   1.00 36.23  ? 296 SER A OG  1 
ATOM   1735 N  N   . LYS A 1 243 ? 33.011 7.203   3.638   1.00 37.75  ? 297 LYS A N   1 
ATOM   1736 C  CA  . LYS A 1 243 ? 33.227 7.142   5.085   1.00 40.15  ? 297 LYS A CA  1 
ATOM   1737 C  C   . LYS A 1 243 ? 34.638 6.699   5.449   1.00 43.27  ? 297 LYS A C   1 
ATOM   1738 O  O   . LYS A 1 243 ? 35.249 5.882   4.758   1.00 43.33  ? 297 LYS A O   1 
ATOM   1739 C  CB  . LYS A 1 243 ? 32.215 6.204   5.748   1.00 40.61  ? 297 LYS A CB  1 
ATOM   1740 C  CG  . LYS A 1 243 ? 30.820 6.793   5.916   1.00 40.95  ? 297 LYS A CG  1 
ATOM   1741 C  CD  . LYS A 1 243 ? 29.856 5.789   6.532   1.00 41.94  ? 297 LYS A CD  1 
ATOM   1742 C  CE  . LYS A 1 243 ? 28.415 6.251   6.404   1.00 43.14  ? 297 LYS A CE  1 
ATOM   1743 N  NZ  . LYS A 1 243 ? 27.485 5.347   7.136   1.00 44.46  ? 297 LYS A NZ  1 
ATOM   1744 N  N   . ASN A 1 244 ? 35.147 7.264   6.540   1.00 46.29  ? 298 ASN A N   1 
ATOM   1745 C  CA  . ASN A 1 244 ? 36.434 6.876   7.101   1.00 49.39  ? 298 ASN A CA  1 
ATOM   1746 C  C   . ASN A 1 244 ? 36.297 5.529   7.804   1.00 49.71  ? 298 ASN A C   1 
ATOM   1747 O  O   . ASN A 1 244 ? 36.183 5.453   9.026   1.00 50.39  ? 298 ASN A O   1 
ATOM   1748 C  CB  . ASN A 1 244 ? 36.944 7.953   8.063   1.00 53.66  ? 298 ASN A CB  1 
ATOM   1749 C  CG  . ASN A 1 244 ? 38.304 7.623   8.648   1.00 57.78  ? 298 ASN A CG  1 
ATOM   1750 O  OD1 . ASN A 1 244 ? 39.048 6.807   8.103   1.00 59.12  ? 298 ASN A OD1 1 
ATOM   1751 N  ND2 . ASN A 1 244 ? 38.638 8.264   9.764   1.00 58.98  ? 298 ASN A ND2 1 
ATOM   1752 N  N   . ILE A 1 245 ? 36.303 4.471   7.002   1.00 46.32  ? 299 ILE A N   1 
ATOM   1753 C  CA  . ILE A 1 245 ? 35.975 3.125   7.451   1.00 46.66  ? 299 ILE A CA  1 
ATOM   1754 C  C   . ILE A 1 245 ? 36.824 2.129   6.661   1.00 44.95  ? 299 ILE A C   1 
ATOM   1755 O  O   . ILE A 1 245 ? 37.166 2.390   5.510   1.00 45.74  ? 299 ILE A O   1 
ATOM   1756 C  CB  . ILE A 1 245 ? 34.453 2.838   7.254   1.00 50.48  ? 299 ILE A CB  1 
ATOM   1757 C  CG1 . ILE A 1 245 ? 33.631 3.488   8.367   1.00 52.54  ? 299 ILE A CG1 1 
ATOM   1758 C  CG2 . ILE A 1 245 ? 34.147 1.352   7.208   1.00 51.31  ? 299 ILE A CG2 1 
ATOM   1759 C  CD1 . ILE A 1 245 ? 32.146 3.261   8.211   1.00 53.87  ? 299 ILE A CD1 1 
ATOM   1760 N  N   . ASP A 1 246 ? 37.193 1.014   7.290   1.00 42.34  ? 300 ASP A N   1 
ATOM   1761 C  CA  . ASP A 1 246 ? 37.848 -0.098  6.598   1.00 40.03  ? 300 ASP A CA  1 
ATOM   1762 C  C   . ASP A 1 246 ? 37.094 -0.481  5.320   1.00 37.47  ? 300 ASP A C   1 
ATOM   1763 O  O   . ASP A 1 246 ? 35.883 -0.660  5.363   1.00 36.50  ? 300 ASP A O   1 
ATOM   1764 C  CB  . ASP A 1 246 ? 37.945 -1.305  7.535   1.00 40.89  ? 300 ASP A CB  1 
ATOM   1765 C  CG  . ASP A 1 246 ? 38.365 -2.567  6.821   1.00 42.82  ? 300 ASP A CG  1 
ATOM   1766 O  OD1 . ASP A 1 246 ? 39.562 -2.696  6.496   1.00 43.95  ? 300 ASP A OD1 1 
ATOM   1767 O  OD2 . ASP A 1 246 ? 37.490 -3.428  6.575   1.00 44.48  ? 300 ASP A OD2 1 
ATOM   1768 N  N   . PRO A 1 247 ? 37.811 -0.601  4.186   1.00 35.24  ? 301 PRO A N   1 
ATOM   1769 C  CA  . PRO A 1 247 ? 37.199 -0.838  2.868   1.00 34.42  ? 301 PRO A CA  1 
ATOM   1770 C  C   . PRO A 1 247 ? 36.285 -2.063  2.807   1.00 31.28  ? 301 PRO A C   1 
ATOM   1771 O  O   . PRO A 1 247 ? 35.208 -1.960  2.223   1.00 29.54  ? 301 PRO A O   1 
ATOM   1772 C  CB  . PRO A 1 247 ? 38.408 -1.024  1.948   1.00 37.01  ? 301 PRO A CB  1 
ATOM   1773 C  CG  . PRO A 1 247 ? 39.495 -0.255  2.614   1.00 37.43  ? 301 PRO A CG  1 
ATOM   1774 C  CD  . PRO A 1 247 ? 39.273 -0.433  4.088   1.00 36.51  ? 301 PRO A CD  1 
ATOM   1775 N  N   . ALA A 1 248 ? 36.680 -3.192  3.386   1.00 29.93  ? 302 ALA A N   1 
ATOM   1776 C  CA  . ALA A 1 248 ? 35.808 -4.362  3.361   1.00 29.52  ? 302 ALA A CA  1 
ATOM   1777 C  C   . ALA A 1 248 ? 34.508 -4.077  4.108   1.00 27.95  ? 302 ALA A C   1 
ATOM   1778 O  O   . ALA A 1 248 ? 33.429 -4.440  3.643   1.00 27.17  ? 302 ALA A O   1 
ATOM   1779 C  CB  . ALA A 1 248 ? 36.508 -5.573  3.953   1.00 31.52  ? 302 ALA A CB  1 
ATOM   1780 N  N   . ARG A 1 249 ? 34.614 -3.420  5.259   1.00 29.73  ? 303 ARG A N   1 
ATOM   1781 C  CA  . ARG A 1 249 ? 33.445 -3.093  6.068   1.00 30.43  ? 303 ARG A CA  1 
ATOM   1782 C  C   . ARG A 1 249 ? 32.547 -2.101  5.338   1.00 27.74  ? 303 ARG A C   1 
ATOM   1783 O  O   . ARG A 1 249 ? 31.321 -2.175  5.410   1.00 25.94  ? 303 ARG A O   1 
ATOM   1784 C  CB  . ARG A 1 249 ? 33.873 -2.519  7.428   1.00 35.48  ? 303 ARG A CB  1 
ATOM   1785 C  CG  . ARG A 1 249 ? 32.719 -2.269  8.383   1.00 41.74  ? 303 ARG A CG  1 
ATOM   1786 C  CD  . ARG A 1 249 ? 33.155 -1.465  9.605   1.00 48.01  ? 303 ARG A CD  1 
ATOM   1787 N  NE  . ARG A 1 249 ? 32.014 -1.056  10.424  1.00 55.00  ? 303 ARG A NE  1 
ATOM   1788 C  CZ  . ARG A 1 249 ? 31.875 0.149   10.968  1.00 61.35  ? 303 ARG A CZ  1 
ATOM   1789 N  NH1 . ARG A 1 249 ? 32.821 1.065   10.797  1.00 63.97  ? 303 ARG A NH1 1 
ATOM   1790 N  NH2 . ARG A 1 249 ? 30.810 0.432   11.706  1.00 63.22  ? 303 ARG A NH2 1 
ATOM   1791 N  N   . LYS A 1 250 ? 33.173 -1.164  4.635   1.00 27.59  ? 304 LYS A N   1 
ATOM   1792 C  CA  . LYS A 1 250 ? 32.443 -0.141  3.912   1.00 27.65  ? 304 LYS A CA  1 
ATOM   1793 C  C   . LYS A 1 250 ? 31.659 -0.741  2.753   1.00 24.31  ? 304 LYS A C   1 
ATOM   1794 O  O   . LYS A 1 250 ? 30.502 -0.371  2.516   1.00 22.74  ? 304 LYS A O   1 
ATOM   1795 C  CB  . LYS A 1 250 ? 33.402 0.935   3.411   1.00 31.72  ? 304 LYS A CB  1 
ATOM   1796 C  CG  . LYS A 1 250 ? 32.799 2.314   3.407   1.00 34.80  ? 304 LYS A CG  1 
ATOM   1797 C  CD  . LYS A 1 250 ? 33.792 3.360   2.919   1.00 36.97  ? 304 LYS A CD  1 
ATOM   1798 C  CE  . LYS A 1 250 ? 34.736 2.814   1.867   1.00 37.98  ? 304 LYS A CE  1 
ATOM   1799 N  NZ  . LYS A 1 250 ? 35.844 3.772   1.586   1.00 39.64  ? 304 LYS A NZ  1 
ATOM   1800 N  N   . GLU A 1 251 ? 32.279 -1.648  2.021   1.00 22.16  ? 305 GLU A N   1 
ATOM   1801 C  CA  . GLU A 1 251 ? 31.608 -2.383  0.944   1.00 21.43  ? 305 GLU A CA  1 
ATOM   1802 C  C   . GLU A 1 251 ? 30.454 -3.215  1.470   1.00 19.97  ? 305 GLU A C   1 
ATOM   1803 O  O   . GLU A 1 251 ? 29.419 -3.283  0.882   1.00 20.33  ? 305 GLU A O   1 
ATOM   1804 C  CB  . GLU A 1 251 ? 32.597 -3.222  0.145   1.00 24.83  ? 305 GLU A CB  1 
ATOM   1805 C  CG  . GLU A 1 251 ? 33.655 -2.352  -0.462  1.00 27.98  ? 305 GLU A CG  1 
ATOM   1806 C  CD  . GLU A 1 251 ? 34.455 -2.963  -1.576  1.00 32.41  ? 305 GLU A CD  1 
ATOM   1807 O  OE1 . GLU A 1 251 ? 34.322 -4.164  -1.820  1.00 33.72  ? 305 GLU A OE1 1 
ATOM   1808 O  OE2 . GLU A 1 251 ? 35.219 -2.178  -2.178  1.00 34.58  ? 305 GLU A OE2 1 
ATOM   1809 N  N   . ALA A 1 252 ? 30.638 -3.797  2.629   1.00 20.01  ? 306 ALA A N   1 
ATOM   1810 C  CA  . ALA A 1 252 ? 29.593 -4.543  3.265   1.00 19.49  ? 306 ALA A CA  1 
ATOM   1811 C  C   . ALA A 1 252 ? 28.451 -3.643  3.699   1.00 19.23  ? 306 ALA A C   1 
ATOM   1812 O  O   . ALA A 1 252 ? 27.334 -4.011  3.576   1.00 20.49  ? 306 ALA A O   1 
ATOM   1813 C  CB  . ALA A 1 252 ? 30.122 -5.349  4.443   1.00 22.06  ? 306 ALA A CB  1 
ATOM   1814 N  N   . GLU A 1 253 ? 28.765 -2.454  4.181   1.00 19.57  ? 307 GLU A N   1 
ATOM   1815 C  CA  . GLU A 1 253 ? 27.727 -1.498  4.564   1.00 21.76  ? 307 GLU A CA  1 
ATOM   1816 C  C   . GLU A 1 253 ? 26.900 -1.094  3.355   1.00 20.40  ? 307 GLU A C   1 
ATOM   1817 O  O   . GLU A 1 253 ? 25.670 -1.021  3.428   1.00 20.91  ? 307 GLU A O   1 
ATOM   1818 C  CB  . GLU A 1 253 ? 28.334 -0.251  5.216   1.00 24.20  ? 307 GLU A CB  1 
ATOM   1819 C  CG  . GLU A 1 253 ? 27.292 0.778   5.626   1.00 29.17  ? 307 GLU A CG  1 
ATOM   1820 C  CD  . GLU A 1 253 ? 27.881 1.912   6.443   1.00 33.85  ? 307 GLU A CD  1 
ATOM   1821 O  OE1 . GLU A 1 253 ? 28.984 1.730   7.003   1.00 35.85  ? 307 GLU A OE1 1 
ATOM   1822 O  OE2 . GLU A 1 253 ? 27.242 2.983   6.514   1.00 37.73  ? 307 GLU A OE2 1 
ATOM   1823 N  N   . PHE A 1 254 ? 27.569 -0.856  2.234   1.00 19.31  ? 308 PHE A N   1 
ATOM   1824 C  CA  . PHE A 1 254 ? 26.846 -0.534  1.015   1.00 19.07  ? 308 PHE A CA  1 
ATOM   1825 C  C   . PHE A 1 254 ? 25.947 -1.687  0.580   1.00 17.13  ? 308 PHE A C   1 
ATOM   1826 O  O   . PHE A 1 254 ? 24.765 -1.483  0.257   1.00 17.96  ? 308 PHE A O   1 
ATOM   1827 C  CB  . PHE A 1 254 ? 27.795 -0.173  -0.131  1.00 17.85  ? 308 PHE A CB  1 
ATOM   1828 C  CG  . PHE A 1 254 ? 27.099 -0.066  -1.451  1.00 16.86  ? 308 PHE A CG  1 
ATOM   1829 C  CD1 . PHE A 1 254 ? 26.093 0.864   -1.642  1.00 18.83  ? 308 PHE A CD1 1 
ATOM   1830 C  CD2 . PHE A 1 254 ? 27.415 -0.926  -2.490  1.00 18.20  ? 308 PHE A CD2 1 
ATOM   1831 C  CE1 . PHE A 1 254 ? 25.427 0.940   -2.860  1.00 19.91  ? 308 PHE A CE1 1 
ATOM   1832 C  CE2 . PHE A 1 254 ? 26.757 -0.854  -3.700  1.00 19.70  ? 308 PHE A CE2 1 
ATOM   1833 C  CZ  . PHE A 1 254 ? 25.763 0.085   -3.884  1.00 21.21  ? 308 PHE A CZ  1 
ATOM   1834 N  N   . ALA A 1 255 ? 26.502 -2.894  0.548   1.00 16.63  ? 309 ALA A N   1 
ATOM   1835 C  CA  . ALA A 1 255 ? 25.723 -4.060  0.132   1.00 17.27  ? 309 ALA A CA  1 
ATOM   1836 C  C   . ALA A 1 255 ? 24.489 -4.242  1.011   1.00 16.39  ? 309 ALA A C   1 
ATOM   1837 O  O   . ALA A 1 255 ? 23.386 -4.475  0.507   1.00 17.17  ? 309 ALA A O   1 
ATOM   1838 C  CB  . ALA A 1 255 ? 26.593 -5.314  0.164   1.00 17.76  ? 309 ALA A CB  1 
ATOM   1839 N  N   . LEU A 1 256 ? 24.666 -4.123  2.323   1.00 18.12  ? 310 LEU A N   1 
ATOM   1840 C  CA  . LEU A 1 256 ? 23.558 -4.297  3.239   1.00 18.69  ? 310 LEU A CA  1 
ATOM   1841 C  C   . LEU A 1 256 ? 22.520 -3.184  3.083   1.00 18.09  ? 310 LEU A C   1 
ATOM   1842 O  O   . LEU A 1 256 ? 21.321 -3.444  3.087   1.00 19.40  ? 310 LEU A O   1 
ATOM   1843 C  CB  . LEU A 1 256 ? 24.078 -4.349  4.671   1.00 20.64  ? 310 LEU A CB  1 
ATOM   1844 C  CG  . LEU A 1 256 ? 23.020 -4.522  5.754   1.00 24.14  ? 310 LEU A CG  1 
ATOM   1845 C  CD1 . LEU A 1 256 ? 22.331 -5.872  5.618   1.00 28.20  ? 310 LEU A CD1 1 
ATOM   1846 C  CD2 . LEU A 1 256 ? 23.622 -4.339  7.152   1.00 25.91  ? 310 LEU A CD2 1 
ATOM   1847 N  N   . SER A 1 257 ? 22.981 -1.949  2.943   1.00 18.54  ? 311 SER A N   1 
ATOM   1848 C  CA  . SER A 1 257 ? 22.059 -0.838  2.767   1.00 19.87  ? 311 SER A CA  1 
ATOM   1849 C  C   . SER A 1 257 ? 21.262 -0.953  1.471   1.00 19.90  ? 311 SER A C   1 
ATOM   1850 O  O   . SER A 1 257 ? 20.081 -0.600  1.431   1.00 22.03  ? 311 SER A O   1 
ATOM   1851 C  CB  . SER A 1 257 ? 22.821 0.483   2.803   1.00 21.90  ? 311 SER A CB  1 
ATOM   1852 O  OG  . SER A 1 257 ? 23.426 0.670   4.070   1.00 28.07  ? 311 SER A OG  1 
ATOM   1853 N  N   . ALA A 1 258 ? 21.893 -1.454  0.418   1.00 18.14  ? 312 ALA A N   1 
ATOM   1854 C  CA  . ALA A 1 258 ? 21.207 -1.666  -0.848  1.00 18.13  ? 312 ALA A CA  1 
ATOM   1855 C  C   . ALA A 1 258 ? 20.180 -2.783  -0.777  1.00 17.30  ? 312 ALA A C   1 
ATOM   1856 O  O   . ALA A 1 258 ? 19.109 -2.691  -1.394  1.00 19.99  ? 312 ALA A O   1 
ATOM   1857 C  CB  . ALA A 1 258 ? 22.210 -1.970  -1.942  1.00 18.35  ? 312 ALA A CB  1 
ATOM   1858 N  N   . LEU A 1 259 ? 20.507 -3.849  -0.045  1.00 16.92  ? 313 LEU A N   1 
ATOM   1859 C  CA  . LEU A 1 259 ? 19.760 -5.102  -0.150  1.00 16.84  ? 313 LEU A CA  1 
ATOM   1860 C  C   . LEU A 1 259 ? 18.987 -5.523  1.092   1.00 20.06  ? 313 LEU A C   1 
ATOM   1861 O  O   . LEU A 1 259 ? 18.334 -6.568  1.076   1.00 20.18  ? 313 LEU A O   1 
ATOM   1862 C  CB  . LEU A 1 259 ? 20.713 -6.231  -0.541  1.00 16.59  ? 313 LEU A CB  1 
ATOM   1863 C  CG  . LEU A 1 259 ? 21.517 -5.998  -1.825  1.00 17.00  ? 313 LEU A CG  1 
ATOM   1864 C  CD1 . LEU A 1 259 ? 22.588 -7.081  -1.982  1.00 17.64  ? 313 LEU A CD1 1 
ATOM   1865 C  CD2 . LEU A 1 259 ? 20.607 -5.936  -3.064  1.00 19.37  ? 313 LEU A CD2 1 
ATOM   1866 N  N   . MET A 1 260 ? 19.027 -4.749  2.141   1.00 22.72  ? 314 MET A N   1 
ATOM   1867 C  CA  . MET A 1 260 ? 18.414 -5.197  3.378   1.00 29.79  ? 314 MET A CA  1 
ATOM   1868 C  C   . MET A 1 260 ? 16.914 -5.472  3.327   1.00 26.74  ? 314 MET A C   1 
ATOM   1869 O  O   . MET A 1 260 ? 16.465 -6.269  4.065   1.00 26.73  ? 314 MET A O   1 
ATOM   1870 C  CB  . MET A 1 260 ? 18.724 -4.269  4.547   1.00 46.64  ? 314 MET A CB  1 
ATOM   1871 C  CG  . MET A 1 260 ? 18.095 -2.919  4.426   1.00 64.20  ? 314 MET A CG  1 
ATOM   1872 S  SD  . MET A 1 260 ? 18.669 -1.723  5.654   1.00 80.43  ? 314 MET A SD  1 
ATOM   1873 C  CE  . MET A 1 260 ? 18.441 -0.224  4.739   1.00 87.95  ? 314 MET A CE  1 
ATOM   1874 N  N   . GLU A 1 261 ? 16.198 -4.825  2.441   1.00 23.44  ? 315 GLU A N   1 
ATOM   1875 C  CA  . GLU A 1 261 ? 14.779 -5.071  2.282   1.00 22.99  ? 315 GLU A CA  1 
ATOM   1876 C  C   . GLU A 1 261 ? 14.426 -6.204  1.334   1.00 19.63  ? 315 GLU A C   1 
ATOM   1877 O  O   . GLU A 1 261 ? 13.305 -6.577  1.242   1.00 20.61  ? 315 GLU A O   1 
ATOM   1878 C  CB  . GLU A 1 261 ? 14.074 -3.815  1.810   1.00 27.70  ? 315 GLU A CB  1 
ATOM   1879 C  CG  . GLU A 1 261 ? 14.174 -2.657  2.746   1.00 34.09  ? 315 GLU A CG  1 
ATOM   1880 C  CD  . GLU A 1 261 ? 13.503 -2.933  4.048   1.00 41.00  ? 315 GLU A CD  1 
ATOM   1881 O  OE1 . GLU A 1 261 ? 12.469 -3.562  4.082   1.00 42.64  ? 315 GLU A OE1 1 
ATOM   1882 O  OE2 . GLU A 1 261 ? 14.039 -2.534  5.055   1.00 44.89  ? 315 GLU A OE2 1 
ATOM   1883 N  N   . ILE A 1 262 ? 15.406 -6.715  0.625   1.00 17.19  ? 316 ILE A N   1 
ATOM   1884 C  CA  . ILE A 1 262 ? 15.145 -7.730  -0.386  1.00 18.10  ? 316 ILE A CA  1 
ATOM   1885 C  C   . ILE A 1 262 ? 14.484 -9.007  0.185   1.00 18.52  ? 316 ILE A C   1 
ATOM   1886 O  O   . ILE A 1 262 ? 13.519 -9.505  -0.397  1.00 18.74  ? 316 ILE A O   1 
ATOM   1887 C  CB  . ILE A 1 262 ? 16.454 -8.071  -1.141  1.00 20.40  ? 316 ILE A CB  1 
ATOM   1888 C  CG1 . ILE A 1 262 ? 16.883 -6.891  -2.016  1.00 22.02  ? 316 ILE A CG1 1 
ATOM   1889 C  CG2 . ILE A 1 262 ? 16.300 -9.335  -1.951  1.00 22.18  ? 316 ILE A CG2 1 
ATOM   1890 C  CD1 . ILE A 1 262 ? 15.822 -6.435  -2.953  1.00 22.87  ? 316 ILE A CD1 1 
ATOM   1891 N  N   . PRO A 1 263 ? 14.962 -9.530  1.338   1.00 17.89  ? 317 PRO A N   1 
ATOM   1892 C  CA  . PRO A 1 263 ? 14.258 -10.718 1.845   1.00 20.07  ? 317 PRO A CA  1 
ATOM   1893 C  C   . PRO A 1 263 ? 12.777 -10.462 2.142   1.00 20.52  ? 317 PRO A C   1 
ATOM   1894 O  O   . PRO A 1 263 ? 11.961 -11.343 1.855   1.00 19.91  ? 317 PRO A O   1 
ATOM   1895 C  CB  . PRO A 1 263 ? 15.034 -11.063 3.126   1.00 20.93  ? 317 PRO A CB  1 
ATOM   1896 C  CG  . PRO A 1 263 ? 16.408 -10.548 2.853   1.00 20.40  ? 317 PRO A CG  1 
ATOM   1897 C  CD  . PRO A 1 263 ? 16.193 -9.258  2.106   1.00 19.52  ? 317 PRO A CD  1 
ATOM   1898 N  N   . SER A 1 264 ? 12.426 -9.312  2.670   1.00 19.21  ? 318 SER A N   1 
ATOM   1899 C  CA  . SER A 1 264 ? 11.052 -8.975  2.954   1.00 22.03  ? 318 SER A CA  1 
ATOM   1900 C  C   . SER A 1 264 ? 10.198 -8.817  1.693   1.00 19.84  ? 318 SER A C   1 
ATOM   1901 O  O   . SER A 1 264 ? 9.092  -9.217  1.644   1.00 19.42  ? 318 SER A O   1 
ATOM   1902 C  CB  . SER A 1 264 ? 11.046 -7.670  3.701   1.00 29.96  ? 318 SER A CB  1 
ATOM   1903 O  OG  . SER A 1 264 ? 9.743  -7.352  3.993   1.00 38.31  ? 318 SER A OG  1 
ATOM   1904 N  N   . GLN A 1 265 ? 10.785 -8.210  0.685   1.00 17.78  ? 319 GLN A N   1 
ATOM   1905 C  CA  . GLN A 1 265 ? 10.132 -8.045  -0.584  1.00 16.76  ? 319 GLN A CA  1 
ATOM   1906 C  C   . GLN A 1 265 ? 9.928  -9.381  -1.261  1.00 17.21  ? 319 GLN A C   1 
ATOM   1907 O  O   . GLN A 1 265 ? 8.911  -9.641  -1.771  1.00 16.87  ? 319 GLN A O   1 
ATOM   1908 C  CB  . GLN A 1 265 ? 10.918 -7.058  -1.458  1.00 17.21  ? 319 GLN A CB  1 
ATOM   1909 C  CG  . GLN A 1 265 ? 10.873 -5.644  -0.918  1.00 18.68  ? 319 GLN A CG  1 
ATOM   1910 C  CD  . GLN A 1 265 ? 11.623 -4.637  -1.732  1.00 22.17  ? 319 GLN A CD  1 
ATOM   1911 O  OE1 . GLN A 1 265 ? 12.129 -4.939  -2.726  1.00 25.78  ? 319 GLN A OE1 1 
ATOM   1912 N  NE2 . GLN A 1 265 ? 11.675 -3.430  -1.261  1.00 27.72  ? 319 GLN A NE2 1 
ATOM   1913 N  N   . TYR A 1 266 ? 10.928 -10.225 -1.228  1.00 17.98  ? 320 TYR A N   1 
ATOM   1914 C  CA  . TYR A 1 266 ? 10.775 -11.580 -1.755  1.00 17.67  ? 320 TYR A CA  1 
ATOM   1915 C  C   . TYR A 1 266 ? 9.616  -12.307 -1.064  1.00 18.37  ? 320 TYR A C   1 
ATOM   1916 O  O   . TYR A 1 266 ? 8.783  -12.926 -1.725  1.00 18.10  ? 320 TYR A O   1 
ATOM   1917 C  CB  . TYR A 1 266 ? 12.073 -12.368 -1.598  1.00 17.42  ? 320 TYR A CB  1 
ATOM   1918 C  CG  . TYR A 1 266 ? 11.921 -13.816 -2.002  1.00 17.09  ? 320 TYR A CG  1 
ATOM   1919 C  CD1 . TYR A 1 266 ? 11.631 -14.155 -3.317  1.00 19.07  ? 320 TYR A CD1 1 
ATOM   1920 C  CD2 . TYR A 1 266 ? 12.038 -14.838 -1.070  1.00 18.15  ? 320 TYR A CD2 1 
ATOM   1921 C  CE1 . TYR A 1 266 ? 11.470 -15.461 -3.704  1.00 19.40  ? 320 TYR A CE1 1 
ATOM   1922 C  CE2 . TYR A 1 266 ? 11.886 -16.173 -1.451  1.00 18.89  ? 320 TYR A CE2 1 
ATOM   1923 C  CZ  . TYR A 1 266 ? 11.600 -16.470 -2.774  1.00 18.55  ? 320 TYR A CZ  1 
ATOM   1924 O  OH  . TYR A 1 266 ? 11.441 -17.782 -3.173  1.00 20.93  ? 320 TYR A OH  1 
ATOM   1925 N  N   . LYS A 1 267 ? 9.521  -12.188 0.245   1.00 19.03  ? 321 LYS A N   1 
ATOM   1926 C  CA  . LYS A 1 267 ? 8.398  -12.791 0.953   1.00 21.33  ? 321 LYS A CA  1 
ATOM   1927 C  C   . LYS A 1 267 ? 7.066  -12.246 0.526   1.00 19.58  ? 321 LYS A C   1 
ATOM   1928 O  O   . LYS A 1 267 ? 6.131  -12.960 0.425   1.00 19.94  ? 321 LYS A O   1 
ATOM   1929 C  CB  . LYS A 1 267 ? 8.578  -12.637 2.447   1.00 27.55  ? 321 LYS A CB  1 
ATOM   1930 C  CG  . LYS A 1 267 ? 9.735  -13.440 2.922   1.00 42.53  ? 321 LYS A CG  1 
ATOM   1931 C  CD  . LYS A 1 267 ? 9.859  -13.366 4.429   1.00 55.09  ? 321 LYS A CD  1 
ATOM   1932 C  CE  . LYS A 1 267 ? 10.945 -14.301 4.918   1.00 63.63  ? 321 LYS A CE  1 
ATOM   1933 N  NZ  . LYS A 1 267 ? 12.222 -13.655 4.609   1.00 67.98  ? 321 LYS A NZ  1 
ATOM   1934 N  N   . ALA A 1 268 ? 7.019  -10.961 0.269   1.00 19.32  ? 322 ALA A N   1 
ATOM   1935 C  CA  . ALA A 1 268 ? 5.777  -10.370 -0.209  1.00 19.21  ? 322 ALA A CA  1 
ATOM   1936 C  C   . ALA A 1 268 ? 5.361  -10.955 -1.567  1.00 19.35  ? 322 ALA A C   1 
ATOM   1937 O  O   . ALA A 1 268 ? 4.172  -11.107 -1.835  1.00 20.06  ? 322 ALA A O   1 
ATOM   1938 C  CB  . ALA A 1 268 ? 5.908  -8.868  -0.289  1.00 18.89  ? 322 ALA A CB  1 
ATOM   1939 N  N   . THR A 1 269 ? 6.327  -11.305 -2.417  1.00 17.85  ? 323 THR A N   1 
ATOM   1940 C  CA  . THR A 1 269 ? 5.960  -11.885 -3.711  1.00 18.04  ? 323 THR A CA  1 
ATOM   1941 C  C   . THR A 1 269 ? 5.315  -13.253 -3.528  1.00 18.11  ? 323 THR A C   1 
ATOM   1942 O  O   . THR A 1 269 ? 4.576  -13.715 -4.400  1.00 19.18  ? 323 THR A O   1 
ATOM   1943 C  CB  . THR A 1 269 ? 7.158  -12.016 -4.687  1.00 19.18  ? 323 THR A CB  1 
ATOM   1944 O  OG1 . THR A 1 269 ? 8.013  -13.097 -4.297  1.00 19.48  ? 323 THR A OG1 1 
ATOM   1945 C  CG2 . THR A 1 269 ? 7.930  -10.690 -4.818  1.00 19.35  ? 323 THR A CG2 1 
ATOM   1946 N  N   . LEU A 1 270 ? 5.572  -13.893 -2.391  1.00 18.34  ? 324 LEU A N   1 
ATOM   1947 C  CA  . LEU A 1 270 ? 4.918  -15.162 -2.074  1.00 19.41  ? 324 LEU A CA  1 
ATOM   1948 C  C   . LEU A 1 270 ? 3.514  -14.874 -1.577  1.00 19.70  ? 324 LEU A C   1 
ATOM   1949 O  O   . LEU A 1 270 ? 2.521  -15.436 -2.060  1.00 21.38  ? 324 LEU A O   1 
ATOM   1950 C  CB  . LEU A 1 270 ? 5.697  -15.948 -1.012  1.00 19.57  ? 324 LEU A CB  1 
ATOM   1951 C  CG  . LEU A 1 270 ? 7.204  -16.116 -1.239  1.00 23.30  ? 324 LEU A CG  1 
ATOM   1952 C  CD1 . LEU A 1 270 ? 7.769  -17.128 -0.249  1.00 25.86  ? 324 LEU A CD1 1 
ATOM   1953 C  CD2 . LEU A 1 270 ? 7.509  -16.536 -2.662  1.00 23.87  ? 324 LEU A CD2 1 
ATOM   1954 N  N   . GLU A 1 271 ? 3.439  -14.001 -0.580  1.00 20.11  ? 325 GLU A N   1 
ATOM   1955 C  CA  . GLU A 1 271 ? 2.168  -13.658 0.033   1.00 22.09  ? 325 GLU A CA  1 
ATOM   1956 C  C   . GLU A 1 271 ? 1.167  -13.121 -0.990  1.00 20.54  ? 325 GLU A C   1 
ATOM   1957 O  O   . GLU A 1 271 ? -0.026 -13.433 -0.922  1.00 22.81  ? 325 GLU A O   1 
ATOM   1958 C  CB  . GLU A 1 271 ? 2.369  -12.623 1.135   1.00 25.98  ? 325 GLU A CB  1 
ATOM   1959 C  CG  . GLU A 1 271 ? 1.062  -12.207 1.788   1.00 32.30  ? 325 GLU A CG  1 
ATOM   1960 C  CD  . GLU A 1 271 ? 1.257  -11.292 2.977   1.00 42.14  ? 325 GLU A CD  1 
ATOM   1961 O  OE1 . GLU A 1 271 ? 2.315  -10.631 3.052   1.00 44.87  ? 325 GLU A OE1 1 
ATOM   1962 O  OE2 . GLU A 1 271 ? 0.348  -11.235 3.835   1.00 45.10  ? 325 GLU A OE2 1 
ATOM   1963 N  N   . LEU A 1 272 ? 1.659  -12.328 -1.937  1.00 19.92  ? 326 LEU A N   1 
ATOM   1964 C  CA  . LEU A 1 272 ? 0.779  -11.705 -2.919  1.00 19.88  ? 326 LEU A CA  1 
ATOM   1965 C  C   . LEU A 1 272 ? 0.525  -12.572 -4.149  1.00 20.28  ? 326 LEU A C   1 
ATOM   1966 O  O   . LEU A 1 272 ? -0.188 -12.162 -5.057  1.00 23.73  ? 326 LEU A O   1 
ATOM   1967 C  CB  . LEU A 1 272 ? 1.347  -10.350 -3.346  1.00 20.89  ? 326 LEU A CB  1 
ATOM   1968 C  CG  . LEU A 1 272 ? 1.393  -9.273  -2.260  1.00 22.75  ? 326 LEU A CG  1 
ATOM   1969 C  CD1 . LEU A 1 272 ? 2.212  -8.073  -2.738  1.00 24.76  ? 326 LEU A CD1 1 
ATOM   1970 C  CD2 . LEU A 1 272 ? -0.015 -8.834  -1.878  1.00 25.04  ? 326 LEU A CD2 1 
ATOM   1971 N  N   . GLY A 1 273 ? 1.099  -13.771 -4.184  1.00 19.04  ? 327 GLY A N   1 
ATOM   1972 C  CA  . GLY A 1 273 ? 0.873  -14.673 -5.301  1.00 19.66  ? 327 GLY A CA  1 
ATOM   1973 C  C   . GLY A 1 273 ? 1.509  -14.208 -6.610  1.00 19.11  ? 327 GLY A C   1 
ATOM   1974 O  O   . GLY A 1 273 ? 0.952  -14.445 -7.689  1.00 23.42  ? 327 GLY A O   1 
ATOM   1975 N  N   . LEU A 1 274 ? 2.671  -13.571 -6.521  1.00 19.06  ? 328 LEU A N   1 
ATOM   1976 C  CA  . LEU A 1 274 ? 3.374  -13.070 -7.701  1.00 18.27  ? 328 LEU A CA  1 
ATOM   1977 C  C   . LEU A 1 274 ? 4.445  -14.031 -8.206  1.00 18.12  ? 328 LEU A C   1 
ATOM   1978 O  O   . LEU A 1 274 ? 4.622  -14.178 -9.420  1.00 20.62  ? 328 LEU A O   1 
ATOM   1979 C  CB  . LEU A 1 274 ? 4.018  -11.705 -7.408  1.00 18.62  ? 328 LEU A CB  1 
ATOM   1980 C  CG  . LEU A 1 274 ? 3.098  -10.606 -6.867  1.00 19.68  ? 328 LEU A CG  1 
ATOM   1981 C  CD1 . LEU A 1 274 ? 3.924  -9.349  -6.581  1.00 20.03  ? 328 LEU A CD1 1 
ATOM   1982 C  CD2 . LEU A 1 274 ? 1.948  -10.315 -7.822  1.00 23.10  ? 328 LEU A CD2 1 
ATOM   1983 N  N   . LEU A 1 275 ? 5.164  -14.675 -7.287  1.00 18.17  ? 329 LEU A N   1 
ATOM   1984 C  CA  . LEU A 1 275 ? 6.250  -15.577 -7.677  1.00 18.73  ? 329 LEU A CA  1 
ATOM   1985 C  C   . LEU A 1 275 ? 5.723  -16.731 -8.517  1.00 20.91  ? 329 LEU A C   1 
ATOM   1986 O  O   . LEU A 1 275 ? 4.764  -17.409 -8.131  1.00 22.04  ? 329 LEU A O   1 
ATOM   1987 C  CB  . LEU A 1 275 ? 6.987  -16.133 -6.455  1.00 19.86  ? 329 LEU A CB  1 
ATOM   1988 C  CG  . LEU A 1 275 ? 8.240  -16.949 -6.807  1.00 20.71  ? 329 LEU A CG  1 
ATOM   1989 C  CD1 . LEU A 1 275 ? 9.387  -16.026 -7.193  1.00 21.89  ? 329 LEU A CD1 1 
ATOM   1990 C  CD2 . LEU A 1 275 ? 8.655  -17.910 -5.682  1.00 21.73  ? 329 LEU A CD2 1 
ATOM   1991 N  N   . GLY A 1 276 ? 6.352  -16.947 -9.669  1.00 21.08  ? 330 GLY A N   1 
ATOM   1992 C  CA  . GLY A 1 276 ? 5.992  -18.039 -10.546 1.00 22.11  ? 330 GLY A CA  1 
ATOM   1993 C  C   . GLY A 1 276 ? 4.735  -17.793 -11.356 1.00 21.89  ? 330 GLY A C   1 
ATOM   1994 O  O   . GLY A 1 276 ? 4.221  -18.702 -11.999 1.00 25.63  ? 330 GLY A O   1 
ATOM   1995 N  N   . GLN A 1 277 ? 4.232  -16.563 -11.331 1.00 23.11  ? 331 GLN A N   1 
ATOM   1996 C  CA  . GLN A 1 277 ? 2.992  -16.260 -12.022 1.00 24.20  ? 331 GLN A CA  1 
ATOM   1997 C  C   . GLN A 1 277 ? 3.245  -15.216 -13.104 1.00 25.84  ? 331 GLN A C   1 
ATOM   1998 O  O   . GLN A 1 277 ? 4.137  -14.386 -12.979 1.00 28.94  ? 331 GLN A O   1 
ATOM   1999 C  CB  . GLN A 1 277 ? 1.930  -15.788 -11.015 1.00 24.16  ? 331 GLN A CB  1 
ATOM   2000 C  CG  . GLN A 1 277 ? 1.603  -16.816 -9.905  1.00 25.61  ? 331 GLN A CG  1 
ATOM   2001 C  CD  . GLN A 1 277 ? 0.899  -18.071 -10.416 1.00 27.14  ? 331 GLN A CD  1 
ATOM   2002 O  OE1 . GLN A 1 277 ? 0.176  -18.025 -11.406 1.00 30.19  ? 331 GLN A OE1 1 
ATOM   2003 N  NE2 . GLN A 1 277 ? 1.094  -19.196 -9.723  1.00 27.79  ? 331 GLN A NE2 1 
ATOM   2004 N  N   . ARG A 1 278 ? 2.482  -15.300 -14.188 1.00 25.23  ? 332 ARG A N   1 
ATOM   2005 C  CA  . ARG A 1 278 ? 2.555  -14.339 -15.281 1.00 26.16  ? 332 ARG A CA  1 
ATOM   2006 C  C   . ARG A 1 278 ? 1.337  -13.423 -15.245 1.00 26.88  ? 332 ARG A C   1 
ATOM   2007 O  O   . ARG A 1 278 ? 0.247  -13.851 -14.863 1.00 28.43  ? 332 ARG A O   1 
ATOM   2008 C  CB  . ARG A 1 278 ? 2.630  -15.056 -16.635 1.00 28.94  ? 332 ARG A CB  1 
ATOM   2009 C  CG  . ARG A 1 278 ? 3.950  -15.763 -16.929 1.00 31.97  ? 332 ARG A CG  1 
ATOM   2010 C  CD  . ARG A 1 278 ? 3.797  -16.705 -18.127 1.00 37.62  ? 332 ARG A CD  1 
ATOM   2011 N  NE  . ARG A 1 278 ? 5.016  -17.467 -18.395 1.00 42.83  ? 332 ARG A NE  1 
ATOM   2012 C  CZ  . ARG A 1 278 ? 5.913  -17.150 -19.325 1.00 45.00  ? 332 ARG A CZ  1 
ATOM   2013 N  NH1 . ARG A 1 278 ? 5.730  -16.086 -20.095 1.00 45.73  ? 332 ARG A NH1 1 
ATOM   2014 N  NH2 . ARG A 1 278 ? 6.992  -17.904 -19.491 1.00 45.99  ? 332 ARG A NH2 1 
ATOM   2015 N  N   . THR A 1 279 ? 1.512  -12.170 -15.647 1.00 27.47  ? 333 THR A N   1 
ATOM   2016 C  CA  . THR A 1 279 ? 0.394  -11.228 -15.684 1.00 27.98  ? 333 THR A CA  1 
ATOM   2017 C  C   . THR A 1 279 ? -0.418 -11.349 -16.967 1.00 28.78  ? 333 THR A C   1 
ATOM   2018 O  O   . THR A 1 279 ? -1.629 -11.116 -16.974 1.00 31.13  ? 333 THR A O   1 
ATOM   2019 C  CB  . THR A 1 279 ? 0.872  -9.776  -15.567 1.00 27.56  ? 333 THR A CB  1 
ATOM   2020 O  OG1 . THR A 1 279 ? 1.619  -9.427  -16.740 1.00 26.68  ? 333 THR A OG1 1 
ATOM   2021 C  CG2 . THR A 1 279 ? 1.733  -9.590  -14.331 1.00 28.20  ? 333 THR A CG2 1 
ATOM   2022 N  N   . GLY A 1 280 ? 0.258  -11.692 -18.058 1.00 27.89  ? 334 GLY A N   1 
ATOM   2023 C  CA  . GLY A 1 280 ? -0.379 -11.721 -19.361 1.00 28.70  ? 334 GLY A CA  1 
ATOM   2024 C  C   . GLY A 1 280 ? -0.430 -10.365 -20.043 1.00 30.42  ? 334 GLY A C   1 
ATOM   2025 O  O   . GLY A 1 280 ? -0.977 -10.251 -21.140 1.00 32.54  ? 334 GLY A O   1 
ATOM   2026 N  N   . HIS A 1 281 ? 0.132  -9.332  -19.417 1.00 29.84  ? 335 HIS A N   1 
ATOM   2027 C  CA  . HIS A 1 281 ? 0.133  -8.008  -20.044 1.00 31.37  ? 335 HIS A CA  1 
ATOM   2028 C  C   . HIS A 1 281 ? 1.378  -7.192  -19.721 1.00 30.68  ? 335 HIS A C   1 
ATOM   2029 O  O   . HIS A 1 281 ? 1.285  -6.060  -19.243 1.00 32.64  ? 335 HIS A O   1 
ATOM   2030 C  CB  . HIS A 1 281 ? -1.120 -7.213  -19.649 1.00 34.87  ? 335 HIS A CB  1 
ATOM   2031 C  CG  . HIS A 1 281 ? -1.390 -7.178  -18.177 1.00 37.24  ? 335 HIS A CG  1 
ATOM   2032 N  ND1 . HIS A 1 281 ? -2.357 -7.959  -17.580 1.00 39.02  ? 335 HIS A ND1 1 
ATOM   2033 C  CD2 . HIS A 1 281 ? -0.833 -6.446  -17.182 1.00 37.86  ? 335 HIS A CD2 1 
ATOM   2034 C  CE1 . HIS A 1 281 ? -2.381 -7.714  -16.282 1.00 39.06  ? 335 HIS A CE1 1 
ATOM   2035 N  NE2 . HIS A 1 281 ? -1.464 -6.800  -16.014 1.00 38.41  ? 335 HIS A NE2 1 
ATOM   2036 N  N   . CYS A 1 282 ? 2.543  -7.756  -20.014 1.00 27.79  ? 336 CYS A N   1 
ATOM   2037 C  CA  . CYS A 1 282 ? 3.801  -7.077  -19.723 1.00 26.72  ? 336 CYS A CA  1 
ATOM   2038 C  C   . CYS A 1 282 ? 4.147  -6.057  -20.825 1.00 28.66  ? 336 CYS A C   1 
ATOM   2039 O  O   . CYS A 1 282 ? 3.521  -6.052  -21.882 1.00 29.18  ? 336 CYS A O   1 
ATOM   2040 C  CB  . CYS A 1 282 ? 4.921  -8.113  -19.532 1.00 27.35  ? 336 CYS A CB  1 
ATOM   2041 S  SG  . CYS A 1 282 ? 5.772  -8.647  -21.029 1.00 30.60  ? 336 CYS A SG  1 
ATOM   2042 N  N   . PRO A 1 283 ? 5.122  -5.161  -20.569 1.00 27.67  ? 337 PRO A N   1 
ATOM   2043 C  CA  . PRO A 1 283 ? 5.430  -4.111  -21.551 1.00 28.13  ? 337 PRO A CA  1 
ATOM   2044 C  C   . PRO A 1 283 ? 5.909  -4.609  -22.913 1.00 29.57  ? 337 PRO A C   1 
ATOM   2045 O  O   . PRO A 1 283 ? 5.808  -3.861  -23.888 1.00 31.36  ? 337 PRO A O   1 
ATOM   2046 C  CB  . PRO A 1 283 ? 6.548  -3.319  -20.865 1.00 27.12  ? 337 PRO A CB  1 
ATOM   2047 C  CG  . PRO A 1 283 ? 6.287  -3.498  -19.422 1.00 27.61  ? 337 PRO A CG  1 
ATOM   2048 C  CD  . PRO A 1 283 ? 5.818  -4.920  -19.291 1.00 26.79  ? 337 PRO A CD  1 
ATOM   2049 N  N   . ASP A 1 284 ? 6.410  -5.838  -22.976 1.00 29.36  ? 338 ASP A N   1 
ATOM   2050 C  CA  . ASP A 1 284 ? 7.026  -6.371  -24.192 1.00 30.91  ? 338 ASP A CA  1 
ATOM   2051 C  C   . ASP A 1 284 ? 8.069  -5.407  -24.744 1.00 26.50  ? 338 ASP A C   1 
ATOM   2052 O  O   . ASP A 1 284 ? 8.111  -5.129  -25.945 1.00 28.57  ? 338 ASP A O   1 
ATOM   2053 C  CB  . ASP A 1 284 ? 5.968  -6.668  -25.260 1.00 40.46  ? 338 ASP A CB  1 
ATOM   2054 C  CG  . ASP A 1 284 ? 5.272  -7.996  -25.035 1.00 52.85  ? 338 ASP A CG  1 
ATOM   2055 O  OD1 . ASP A 1 284 ? 5.679  -8.727  -24.105 1.00 55.65  ? 338 ASP A OD1 1 
ATOM   2056 O  OD2 . ASP A 1 284 ? 4.323  -8.311  -25.786 1.00 58.89  ? 338 ASP A OD2 1 
ATOM   2057 N  N   . ARG A 1 285 ? 8.901  -4.882  -23.855 1.00 22.38  ? 339 ARG A N   1 
ATOM   2058 C  CA  . ARG A 1 285 ? 9.927  -3.939  -24.269 1.00 20.99  ? 339 ARG A CA  1 
ATOM   2059 C  C   . ARG A 1 285 ? 11.200 -4.664  -24.688 1.00 21.35  ? 339 ARG A C   1 
ATOM   2060 O  O   . ARG A 1 285 ? 11.748 -5.470  -23.926 1.00 22.57  ? 339 ARG A O   1 
ATOM   2061 C  CB  . ARG A 1 285 ? 10.247 -2.940  -23.161 1.00 21.76  ? 339 ARG A CB  1 
ATOM   2062 C  CG  . ARG A 1 285 ? 11.422 -2.050  -23.521 1.00 22.42  ? 339 ARG A CG  1 
ATOM   2063 C  CD  . ARG A 1 285 ? 11.653 -0.938  -22.519 1.00 21.49  ? 339 ARG A CD  1 
ATOM   2064 N  NE  . ARG A 1 285 ? 10.622 0.095   -22.568 1.00 22.31  ? 339 ARG A NE  1 
ATOM   2065 C  CZ  . ARG A 1 285 ? 10.621 1.095   -23.444 1.00 22.96  ? 339 ARG A CZ  1 
ATOM   2066 N  NH1 . ARG A 1 285 ? 11.571 1.172   -24.369 1.00 23.63  ? 339 ARG A NH1 1 
ATOM   2067 N  NH2 . ARG A 1 285 ? 9.660  2.004   -23.402 1.00 25.79  ? 339 ARG A NH2 1 
ATOM   2068 N  N   . ILE A 1 286 ? 11.656 -4.356  -25.898 1.00 23.37  ? 340 ILE A N   1 
ATOM   2069 C  CA  . ILE A 1 286 ? 12.842 -4.961  -26.492 1.00 24.06  ? 340 ILE A CA  1 
ATOM   2070 C  C   . ILE A 1 286 ? 14.024 -3.985  -26.458 1.00 21.06  ? 340 ILE A C   1 
ATOM   2071 O  O   . ILE A 1 286 ? 13.888 -2.812  -26.824 1.00 24.78  ? 340 ILE A O   1 
ATOM   2072 C  CB  . ILE A 1 286 ? 12.561 -5.386  -27.952 1.00 28.05  ? 340 ILE A CB  1 
ATOM   2073 C  CG1 . ILE A 1 286 ? 11.437 -6.427  -28.000 1.00 31.11  ? 340 ILE A CG1 1 
ATOM   2074 C  CG2 . ILE A 1 286 ? 13.811 -5.936  -28.616 1.00 30.95  ? 340 ILE A CG2 1 
ATOM   2075 C  CD1 . ILE A 1 286 ? 11.016 -6.797  -29.401 1.00 34.20  ? 340 ILE A CD1 1 
ATOM   2076 N  N   . ALA A 1 287 ? 15.182 -4.460  -26.012 1.00 18.70  ? 341 ALA A N   1 
ATOM   2077 C  CA  . ALA A 1 287 ? 16.382 -3.628  -25.978 1.00 18.81  ? 341 ALA A CA  1 
ATOM   2078 C  C   . ALA A 1 287 ? 17.015 -3.452  -27.354 1.00 19.28  ? 341 ALA A C   1 
ATOM   2079 O  O   . ALA A 1 287 ? 16.965 -4.352  -28.196 1.00 23.03  ? 341 ALA A O   1 
ATOM   2080 C  CB  . ALA A 1 287 ? 17.402 -4.226  -25.030 1.00 20.61  ? 341 ALA A CB  1 
ATOM   2081 N  N   . LEU A 1 288 ? 17.619 -2.289  -27.573 1.00 19.65  ? 342 LEU A N   1 
ATOM   2082 C  CA  . LEU A 1 288 ? 18.439 -2.056  -28.760 1.00 20.25  ? 342 LEU A CA  1 
ATOM   2083 C  C   . LEU A 1 288 ? 19.798 -2.736  -28.593 1.00 20.94  ? 342 LEU A C   1 
ATOM   2084 O  O   . LEU A 1 288 ? 20.215 -3.007  -27.479 1.00 19.30  ? 342 LEU A O   1 
ATOM   2085 C  CB  . LEU A 1 288 ? 18.620 -0.553  -29.002 1.00 21.65  ? 342 LEU A CB  1 
ATOM   2086 C  CG  . LEU A 1 288 ? 17.332 0.279   -29.067 1.00 23.21  ? 342 LEU A CG  1 
ATOM   2087 C  CD1 . LEU A 1 288 ? 17.671 1.749   -29.296 1.00 24.03  ? 342 LEU A CD1 1 
ATOM   2088 C  CD2 . LEU A 1 288 ? 16.363 -0.246  -30.128 1.00 28.93  ? 342 LEU A CD2 1 
ATOM   2089 N  N   . PRO A 1 289 ? 20.492 -3.030  -29.705 1.00 23.37  ? 343 PRO A N   1 
ATOM   2090 C  CA  . PRO A 1 289 ? 21.872 -3.508  -29.572 1.00 23.63  ? 343 PRO A CA  1 
ATOM   2091 C  C   . PRO A 1 289 ? 22.781 -2.395  -29.053 1.00 21.88  ? 343 PRO A C   1 
ATOM   2092 O  O   . PRO A 1 289 ? 22.385 -1.230  -29.065 1.00 23.84  ? 343 PRO A O   1 
ATOM   2093 C  CB  . PRO A 1 289 ? 22.244 -3.917  -31.004 1.00 26.77  ? 343 PRO A CB  1 
ATOM   2094 C  CG  . PRO A 1 289 ? 21.352 -3.089  -31.871 1.00 28.23  ? 343 PRO A CG  1 
ATOM   2095 C  CD  . PRO A 1 289 ? 20.062 -2.946  -31.111 1.00 26.03  ? 343 PRO A CD  1 
ATOM   2096 N  N   . PRO A 1 290 ? 23.973 -2.721  -28.616 1.00 21.47  ? 344 PRO A N   1 
ATOM   2097 C  CA  . PRO A 1 290 ? 24.840 -1.667  -28.131 1.00 23.17  ? 344 PRO A CA  1 
ATOM   2098 C  C   . PRO A 1 290 ? 25.351 -0.846  -29.260 1.00 24.74  ? 344 PRO A C   1 
ATOM   2099 O  O   . PRO A 1 290 ? 25.467 -1.314  -30.345 1.00 29.80  ? 344 PRO A O   1 
ATOM   2100 C  CB  . PRO A 1 290 ? 25.999 -2.389  -27.478 1.00 23.79  ? 344 PRO A CB  1 
ATOM   2101 C  CG  . PRO A 1 290 ? 25.931 -3.766  -27.970 1.00 22.58  ? 344 PRO A CG  1 
ATOM   2102 C  CD  . PRO A 1 290 ? 24.514 -4.054  -28.332 1.00 22.89  ? 344 PRO A CD  1 
ATOM   2103 N  N   . PRO A 1 291 ? 25.599 0.476   -28.915 1.00 26.47  ? 345 PRO A N   1 
ATOM   2104 C  CA  . PRO A 1 291 ? 26.301 1.226   -29.966 1.00 41.33  ? 345 PRO A CA  1 
ATOM   2105 C  C   . PRO A 1 291 ? 27.675 0.557   -30.212 1.00 58.43  ? 345 PRO A C   1 
ATOM   2106 O  O   . PRO A 1 291 ? 28.410 0.863   -31.157 1.00 60.30  ? 345 PRO A O   1 
ATOM   2107 C  CB  . PRO A 1 291 ? 26.498 2.594   -29.337 1.00 35.03  ? 345 PRO A CB  1 
ATOM   2108 C  CG  . PRO A 1 291 ? 25.358 2.767   -28.464 1.00 34.41  ? 345 PRO A CG  1 
ATOM   2109 C  CD  . PRO A 1 291 ? 25.282 1.472   -27.773 1.00 36.92  ? 345 PRO A CD  1 
HETATM 2110 CL CL  . CL  B 2 .   ? 18.239 -8.317  -24.263 1.00 41.21  ? 401 CL  A CL  1 
HETATM 2111 CL CL  . CL  C 2 .   ? 17.653 -11.384 -25.968 1.00 126.42 ? 402 CL  A CL  1 
HETATM 2112 O  O   . HOH D 3 .   ? 12.409 -14.028 2.539   1.00 34.05  ? 501 HOH A O   1 
HETATM 2113 O  O   . HOH D 3 .   ? 30.458 -9.664  11.274  1.00 56.39  ? 502 HOH A O   1 
HETATM 2114 O  O   . HOH D 3 .   ? 19.633 -15.469 -13.342 1.00 22.08  ? 503 HOH A O   1 
HETATM 2115 O  O   . HOH D 3 .   ? 2.313  -9.133  1.293   1.00 50.95  ? 504 HOH A O   1 
HETATM 2116 O  O   . HOH D 3 .   ? 34.937 -5.884  -0.314  1.00 41.15  ? 505 HOH A O   1 
HETATM 2117 O  O   . HOH D 3 .   ? 23.261 -16.164 -22.611 1.00 50.57  ? 506 HOH A O   1 
HETATM 2118 O  O   . HOH D 3 .   ? 39.418 -3.967  4.445   1.00 46.99  ? 507 HOH A O   1 
HETATM 2119 O  O   . HOH D 3 .   ? 35.047 -0.084  -4.213  1.00 51.72  ? 508 HOH A O   1 
HETATM 2120 O  O   . HOH D 3 .   ? 34.358 15.000  -17.073 1.00 47.46  ? 509 HOH A O   1 
HETATM 2121 O  O   . HOH D 3 .   ? 10.896 24.794  -8.406  1.00 40.19  ? 510 HOH A O   1 
HETATM 2122 O  O   . HOH D 3 .   ? 12.938 14.439  -10.643 1.00 32.37  ? 511 HOH A O   1 
HETATM 2123 O  O   . HOH D 3 .   ? 29.984 -16.185 -5.446  1.00 49.52  ? 512 HOH A O   1 
HETATM 2124 O  O   . HOH D 3 .   ? 1.767  10.480  -7.678  1.00 49.42  ? 513 HOH A O   1 
HETATM 2125 O  O   . HOH D 3 .   ? 11.771 -9.380  -25.049 1.00 31.52  ? 514 HOH A O   1 
HETATM 2126 O  O   . HOH D 3 .   ? 2.882  -14.071 -20.375 1.00 43.95  ? 515 HOH A O   1 
HETATM 2127 O  O   . HOH D 3 .   ? 1.521  14.079  -14.653 1.00 51.70  ? 516 HOH A O   1 
HETATM 2128 O  O   . HOH D 3 .   ? 25.551 12.373  -8.893  1.00 25.78  ? 517 HOH A O   1 
HETATM 2129 O  O   . HOH D 3 .   ? 21.041 11.013  -14.795 1.00 23.75  ? 518 HOH A O   1 
HETATM 2130 O  O   . HOH D 3 .   ? 8.539  2.971   -2.254  1.00 52.09  ? 519 HOH A O   1 
HETATM 2131 O  O   . HOH D 3 .   ? 36.681 -0.115  -1.619  1.00 56.51  ? 520 HOH A O   1 
HETATM 2132 O  O   . HOH D 3 .   ? 6.815  4.334   -20.345 1.00 40.98  ? 521 HOH A O   1 
HETATM 2133 O  O   . HOH D 3 .   ? 31.558 -13.596 -15.197 1.00 26.67  ? 522 HOH A O   1 
HETATM 2134 O  O   . HOH D 3 .   ? 10.478 7.709   -20.056 1.00 29.35  ? 523 HOH A O   1 
HETATM 2135 O  O   . HOH D 3 .   ? 15.576 5.382   -28.954 1.00 31.35  ? 524 HOH A O   1 
HETATM 2136 O  O   . HOH D 3 .   ? 32.648 9.943   -19.658 1.00 39.18  ? 525 HOH A O   1 
HETATM 2137 O  O   . HOH D 3 .   ? 1.339  6.143   -11.192 1.00 38.10  ? 526 HOH A O   1 
HETATM 2138 O  O   . HOH D 3 .   ? 25.080 -21.971 -11.215 1.00 48.68  ? 527 HOH A O   1 
HETATM 2139 O  O   . HOH D 3 .   ? 19.283 13.960  -13.712 1.00 48.91  ? 528 HOH A O   1 
HETATM 2140 O  O   . HOH D 3 .   ? 29.729 -3.219  7.508   1.00 34.93  ? 529 HOH A O   1 
HETATM 2141 O  O   . HOH D 3 .   ? 0.794  -3.433  -6.193  1.00 39.59  ? 530 HOH A O   1 
HETATM 2142 O  O   . HOH D 3 .   ? 23.943 -7.642  -28.810 1.00 32.66  ? 531 HOH A O   1 
HETATM 2143 O  O   . HOH D 3 .   ? 24.318 -0.494  6.251   1.00 49.84  ? 532 HOH A O   1 
HETATM 2144 O  O   . HOH D 3 .   ? 38.572 -0.246  -15.666 1.00 49.35  ? 533 HOH A O   1 
HETATM 2145 O  O   . HOH D 3 .   ? -3.210 -10.695 -14.914 1.00 52.13  ? 534 HOH A O   1 
HETATM 2146 O  O   . HOH D 3 .   ? 36.150 -5.774  7.694   1.00 38.45  ? 535 HOH A O   1 
HETATM 2147 O  O   . HOH D 3 .   ? 23.258 -12.573 -9.786  1.00 23.11  ? 536 HOH A O   1 
HETATM 2148 O  O   . HOH D 3 .   ? 37.321 16.360  -5.938  1.00 50.97  ? 537 HOH A O   1 
HETATM 2149 O  O   . HOH D 3 .   ? -1.767 -10.158 -5.727  1.00 42.80  ? 538 HOH A O   1 
HETATM 2150 O  O   . HOH D 3 .   ? 8.336  -4.432  -8.852  1.00 22.57  ? 539 HOH A O   1 
HETATM 2151 O  O   . HOH D 3 .   ? 9.957  10.560  -20.917 1.00 44.32  ? 540 HOH A O   1 
HETATM 2152 O  O   . HOH D 3 .   ? 13.153 12.254  -25.839 1.00 43.60  ? 541 HOH A O   1 
HETATM 2153 O  O   . HOH D 3 .   ? 18.184 -17.979 -9.906  1.00 30.20  ? 542 HOH A O   1 
HETATM 2154 O  O   . HOH D 3 .   ? 2.069  -4.795  -16.568 1.00 32.50  ? 543 HOH A O   1 
HETATM 2155 O  O   . HOH D 3 .   ? 38.078 2.170   -14.229 1.00 30.64  ? 544 HOH A O   1 
HETATM 2156 O  O   . HOH D 3 .   ? 16.374 -17.704 -14.064 1.00 52.98  ? 545 HOH A O   1 
HETATM 2157 O  O   . HOH D 3 .   ? 14.623 -13.052 -21.029 1.00 27.00  ? 546 HOH A O   1 
HETATM 2158 O  O   . HOH D 3 .   ? 11.671 4.334   -29.353 1.00 53.98  ? 547 HOH A O   1 
HETATM 2159 O  O   . HOH D 3 .   ? 44.484 -0.972  -12.456 1.00 46.60  ? 548 HOH A O   1 
HETATM 2160 O  O   . HOH D 3 .   ? 30.627 -15.757 -12.607 1.00 38.82  ? 549 HOH A O   1 
HETATM 2161 O  O   . HOH D 3 .   ? 36.424 0.244   -25.876 1.00 48.66  ? 550 HOH A O   1 
HETATM 2162 O  O   . HOH D 3 .   ? 1.396  -3.839  -14.322 1.00 32.03  ? 551 HOH A O   1 
HETATM 2163 O  O   . HOH D 3 .   ? 25.916 -18.074 -9.473  1.00 26.24  ? 552 HOH A O   1 
HETATM 2164 O  O   . HOH D 3 .   ? 34.197 6.155   -20.444 1.00 33.74  ? 553 HOH A O   1 
HETATM 2165 O  O   . HOH D 3 .   ? 32.933 14.619  -12.852 1.00 30.82  ? 554 HOH A O   1 
HETATM 2166 O  O   . HOH D 3 .   ? 19.615 13.899  -18.130 1.00 37.56  ? 555 HOH A O   1 
HETATM 2167 O  O   . HOH D 3 .   ? 17.345 -19.548 -17.177 1.00 26.88  ? 556 HOH A O   1 
HETATM 2168 O  O   . HOH D 3 .   ? 5.537  4.456   -17.554 1.00 31.66  ? 557 HOH A O   1 
HETATM 2169 O  O   . HOH D 3 .   ? 32.377 -14.170 -23.631 1.00 37.54  ? 558 HOH A O   1 
HETATM 2170 O  O   . HOH D 3 .   ? 4.863  0.835   -17.912 1.00 42.47  ? 559 HOH A O   1 
HETATM 2171 O  O   . HOH D 3 .   ? 30.736 18.087  -19.744 1.00 37.00  ? 560 HOH A O   1 
HETATM 2172 O  O   . HOH D 3 .   ? 23.921 -9.221  -20.273 1.00 20.39  ? 561 HOH A O   1 
HETATM 2173 O  O   . HOH D 3 .   ? 14.780 -18.197 -10.114 1.00 26.30  ? 562 HOH A O   1 
HETATM 2174 O  O   . HOH D 3 .   ? 31.402 17.022  -23.263 1.00 35.03  ? 563 HOH A O   1 
HETATM 2175 O  O   . HOH D 3 .   ? 21.894 1.418   -29.494 1.00 29.70  ? 564 HOH A O   1 
HETATM 2176 O  O   . HOH D 3 .   ? 29.945 7.952   -6.154  1.00 22.92  ? 565 HOH A O   1 
HETATM 2177 O  O   . HOH D 3 .   ? 19.209 -11.218 -7.162  1.00 23.53  ? 566 HOH A O   1 
HETATM 2178 O  O   . HOH D 3 .   ? 21.329 -13.018 -7.874  1.00 22.32  ? 567 HOH A O   1 
HETATM 2179 O  O   . HOH D 3 .   ? 41.408 -1.340  7.994   1.00 53.51  ? 568 HOH A O   1 
HETATM 2180 O  O   . HOH D 3 .   ? 3.696  -19.927 -8.244  1.00 24.33  ? 569 HOH A O   1 
HETATM 2181 O  O   . HOH D 3 .   ? 15.538 3.799   -18.361 1.00 19.21  ? 570 HOH A O   1 
HETATM 2182 O  O   . HOH D 3 .   ? 25.814 -11.722 -9.650  1.00 20.52  ? 571 HOH A O   1 
HETATM 2183 O  O   . HOH D 3 .   ? 24.814 -16.602 -21.789 1.00 34.66  ? 572 HOH A O   1 
HETATM 2184 O  O   . HOH D 3 .   ? 22.010 -11.706 10.280  1.00 36.56  ? 573 HOH A O   1 
HETATM 2185 O  O   . HOH D 3 .   ? 37.871 0.242   -22.424 1.00 36.82  ? 574 HOH A O   1 
HETATM 2186 O  O   . HOH D 3 .   ? 25.793 6.432   -27.762 1.00 22.46  ? 575 HOH A O   1 
HETATM 2187 O  O   . HOH D 3 .   ? 29.375 -13.684 -25.901 1.00 26.76  ? 576 HOH A O   1 
HETATM 2188 O  O   . HOH D 3 .   ? 14.145 -7.699  4.447   1.00 26.84  ? 577 HOH A O   1 
HETATM 2189 O  O   . HOH D 3 .   ? 14.031 -0.339  -25.422 1.00 21.39  ? 578 HOH A O   1 
HETATM 2190 O  O   . HOH D 3 .   ? 34.439 -2.719  -15.870 1.00 24.20  ? 579 HOH A O   1 
HETATM 2191 O  O   . HOH D 3 .   ? 9.392  18.637  -12.646 1.00 35.15  ? 580 HOH A O   1 
HETATM 2192 O  O   . HOH D 3 .   ? 29.661 -12.603 -1.368  1.00 27.55  ? 581 HOH A O   1 
HETATM 2193 O  O   . HOH D 3 .   ? 0.154  12.505  -11.357 1.00 48.25  ? 582 HOH A O   1 
HETATM 2194 O  O   . HOH D 3 .   ? 4.228  -21.276 -11.009 1.00 42.35  ? 583 HOH A O   1 
HETATM 2195 O  O   . HOH D 3 .   ? 18.158 -19.182 2.100   1.00 19.75  ? 584 HOH A O   1 
HETATM 2196 O  O   . HOH D 3 .   ? 24.379 2.677   5.707   1.00 43.70  ? 585 HOH A O   1 
HETATM 2197 O  O   . HOH D 3 .   ? 37.057 13.146  -4.954  1.00 42.90  ? 586 HOH A O   1 
HETATM 2198 O  O   . HOH D 3 .   ? 32.679 8.079   -5.242  1.00 31.37  ? 587 HOH A O   1 
HETATM 2199 O  O   . HOH D 3 .   ? 21.293 12.703  -15.549 1.00 47.03  ? 588 HOH A O   1 
HETATM 2200 O  O   . HOH D 3 .   ? 42.967 -0.355  -8.763  1.00 44.93  ? 589 HOH A O   1 
HETATM 2201 O  O   . HOH D 3 .   ? 0.133  -9.431  -10.869 1.00 28.36  ? 590 HOH A O   1 
HETATM 2202 O  O   . HOH D 3 .   ? 9.334  -5.074  2.453   1.00 48.11  ? 591 HOH A O   1 
HETATM 2203 O  O   . HOH D 3 .   ? 35.055 -12.723 -9.370  1.00 54.29  ? 592 HOH A O   1 
HETATM 2204 O  O   . HOH D 3 .   ? 38.037 5.107   -13.197 1.00 29.10  ? 593 HOH A O   1 
HETATM 2205 O  O   . HOH D 3 .   ? 18.554 4.498   -31.722 1.00 41.32  ? 594 HOH A O   1 
HETATM 2206 O  O   . HOH D 3 .   ? 11.269 17.109  -19.538 1.00 41.78  ? 595 HOH A O   1 
HETATM 2207 O  O   . HOH D 3 .   ? 26.060 -18.568 -17.079 1.00 27.87  ? 596 HOH A O   1 
HETATM 2208 O  O   . HOH D 3 .   ? 14.289 -11.137 -24.222 1.00 39.82  ? 597 HOH A O   1 
HETATM 2209 O  O   . HOH D 3 .   ? 15.691 -13.920 -16.352 1.00 26.45  ? 598 HOH A O   1 
HETATM 2210 O  O   . HOH D 3 .   ? 7.058  -9.182  3.551   1.00 31.84  ? 599 HOH A O   1 
HETATM 2211 O  O   . HOH D 3 .   ? 1.939  7.793   -1.832  1.00 50.77  ? 600 HOH A O   1 
HETATM 2212 O  O   . HOH D 3 .   ? -0.024 -16.750 -13.883 1.00 40.28  ? 601 HOH A O   1 
HETATM 2213 O  O   . HOH D 3 .   ? 0.679  -6.457  -6.979  1.00 36.54  ? 602 HOH A O   1 
HETATM 2214 O  O   . HOH D 3 .   ? 13.790 -13.851 -18.564 1.00 23.77  ? 603 HOH A O   1 
HETATM 2215 O  O   . HOH D 3 .   ? 31.146 -16.248 -21.084 1.00 44.23  ? 604 HOH A O   1 
HETATM 2216 O  O   . HOH D 3 .   ? 35.632 -8.343  -15.308 1.00 32.42  ? 605 HOH A O   1 
HETATM 2217 O  O   . HOH D 3 .   ? 16.019 5.651   -21.497 1.00 22.22  ? 606 HOH A O   1 
HETATM 2218 O  O   . HOH D 3 .   ? 5.514  -12.268 -14.218 1.00 25.08  ? 607 HOH A O   1 
HETATM 2219 O  O   . HOH D 3 .   ? 32.302 8.728   -27.324 1.00 54.76  ? 608 HOH A O   1 
HETATM 2220 O  O   . HOH D 3 .   ? 11.084 22.230  -11.908 1.00 51.37  ? 609 HOH A O   1 
HETATM 2221 O  O   . HOH D 3 .   ? 22.587 14.809  -10.628 1.00 37.88  ? 610 HOH A O   1 
HETATM 2222 O  O   . HOH D 3 .   ? 22.426 -8.726  -25.867 1.00 37.08  ? 611 HOH A O   1 
HETATM 2223 O  O   . HOH D 3 .   ? 38.238 4.211   -7.186  1.00 37.42  ? 612 HOH A O   1 
HETATM 2224 O  O   . HOH D 3 .   ? -0.666 -5.586  0.286   1.00 46.43  ? 613 HOH A O   1 
HETATM 2225 O  O   . HOH D 3 .   ? 18.453 -18.439 -12.457 1.00 35.08  ? 614 HOH A O   1 
HETATM 2226 O  O   . HOH D 3 .   ? 14.694 -15.538 -3.458  1.00 27.25  ? 615 HOH A O   1 
HETATM 2227 O  O   . HOH D 3 .   ? 33.842 -10.804 1.037   1.00 33.58  ? 616 HOH A O   1 
HETATM 2228 O  O   . HOH D 3 .   ? 27.114 -14.536 -3.397  1.00 25.25  ? 617 HOH A O   1 
HETATM 2229 O  O   . HOH D 3 .   ? 30.908 -0.345  -32.030 1.00 49.19  ? 618 HOH A O   1 
HETATM 2230 O  O   . HOH D 3 .   ? 19.854 -12.449 8.558   1.00 33.56  ? 619 HOH A O   1 
HETATM 2231 O  O   . HOH D 3 .   ? 37.139 12.118  -16.844 1.00 39.05  ? 620 HOH A O   1 
HETATM 2232 O  O   . HOH D 3 .   ? 34.645 -5.118  -4.490  1.00 50.60  ? 621 HOH A O   1 
HETATM 2233 O  O   . HOH D 3 .   ? 34.207 -15.064 -1.537  1.00 42.52  ? 622 HOH A O   1 
HETATM 2234 O  O   . HOH D 3 .   ? 14.703 -20.828 -15.747 1.00 48.15  ? 623 HOH A O   1 
HETATM 2235 O  O   . HOH D 3 .   ? 29.550 -0.760  8.996   1.00 51.04  ? 624 HOH A O   1 
HETATM 2236 O  O   . HOH D 3 .   ? 10.422 12.802  -23.873 1.00 52.11  ? 625 HOH A O   1 
HETATM 2237 O  O   . HOH D 3 .   ? 24.946 6.669   6.943   1.00 53.61  ? 626 HOH A O   1 
HETATM 2238 O  O   . HOH D 3 .   ? 42.628 5.396   -19.033 1.00 49.11  ? 627 HOH A O   1 
HETATM 2239 O  O   . HOH D 3 .   ? -2.440 -13.399 0.652   1.00 50.18  ? 628 HOH A O   1 
HETATM 2240 O  O   . HOH D 3 .   ? 15.727 -7.289  -25.773 1.00 25.07  ? 629 HOH A O   1 
HETATM 2241 O  O   . HOH D 3 .   ? 33.580 -6.772  1.900   1.00 29.34  ? 630 HOH A O   1 
HETATM 2242 O  O   . HOH D 3 .   ? 10.353 -2.314  -27.483 1.00 33.35  ? 631 HOH A O   1 
HETATM 2243 O  O   . HOH D 3 .   ? 18.180 -15.108 -15.158 1.00 42.49  ? 632 HOH A O   1 
HETATM 2244 O  O   . HOH D 3 .   ? 5.114  -11.247 3.493   1.00 44.74  ? 633 HOH A O   1 
HETATM 2245 O  O   . HOH D 3 .   ? 12.810 -18.178 -5.701  1.00 33.42  ? 634 HOH A O   1 
HETATM 2246 O  O   . HOH D 3 .   ? 24.934 12.818  -0.941  1.00 52.03  ? 635 HOH A O   1 
HETATM 2247 O  O   . HOH D 3 .   ? 27.477 -13.406 -11.011 1.00 24.33  ? 636 HOH A O   1 
HETATM 2248 O  O   . HOH D 3 .   ? 23.649 -17.069 -26.889 1.00 40.84  ? 637 HOH A O   1 
HETATM 2249 O  O   . HOH D 3 .   ? 2.701  -10.622 -20.989 1.00 39.89  ? 638 HOH A O   1 
HETATM 2250 O  O   . HOH D 3 .   ? 17.080 7.968   -19.630 1.00 18.14  ? 639 HOH A O   1 
HETATM 2251 O  O   . HOH D 3 .   ? 21.253 -15.117 -29.514 1.00 57.13  ? 640 HOH A O   1 
HETATM 2252 O  O   . HOH D 3 .   ? -1.369 6.580   -3.098  1.00 40.59  ? 641 HOH A O   1 
HETATM 2253 O  O   . HOH D 3 .   ? 25.959 12.200  -3.162  1.00 47.67  ? 642 HOH A O   1 
HETATM 2254 O  O   . HOH D 3 .   ? 14.409 3.853   -0.040  1.00 40.38  ? 643 HOH A O   1 
HETATM 2255 O  O   . HOH D 3 .   ? 21.962 -7.855  -21.633 1.00 22.78  ? 644 HOH A O   1 
HETATM 2256 O  O   . HOH D 3 .   ? -1.402 -13.281 -12.499 1.00 36.99  ? 645 HOH A O   1 
HETATM 2257 O  O   . HOH D 3 .   ? 27.458 -3.675  11.288  1.00 58.97  ? 646 HOH A O   1 
HETATM 2258 O  O   . HOH D 3 .   ? 12.627 -1.592  -29.187 1.00 40.94  ? 647 HOH A O   1 
HETATM 2259 O  O   . HOH D 3 .   ? 37.187 6.685   -20.098 1.00 34.34  ? 648 HOH A O   1 
HETATM 2260 O  O   . HOH D 3 .   ? 12.507 -17.270 -8.365  1.00 22.73  ? 649 HOH A O   1 
HETATM 2261 O  O   . HOH D 3 .   ? 25.229 -6.474  -31.363 1.00 47.41  ? 650 HOH A O   1 
HETATM 2262 O  O   . HOH D 3 .   ? 21.254 5.713   1.577   1.00 35.02  ? 651 HOH A O   1 
HETATM 2263 O  O   . HOH D 3 .   ? 39.466 8.207   -7.281  1.00 50.61  ? 652 HOH A O   1 
HETATM 2264 O  O   . HOH D 3 .   ? 3.061  -12.219 -11.280 1.00 36.76  ? 653 HOH A O   1 
HETATM 2265 O  O   . HOH D 3 .   ? 12.030 0.656   0.687   1.00 59.81  ? 654 HOH A O   1 
HETATM 2266 O  O   . HOH D 3 .   ? 40.246 5.959   -11.952 1.00 45.97  ? 655 HOH A O   1 
HETATM 2267 O  O   . HOH D 3 .   ? 21.327 14.828  -19.626 1.00 36.76  ? 656 HOH A O   1 
HETATM 2268 O  O   . HOH D 3 .   ? 25.229 -20.768 -6.789  1.00 48.75  ? 657 HOH A O   1 
HETATM 2269 O  O   . HOH D 3 .   ? -1.573 -8.351  -12.921 1.00 49.74  ? 658 HOH A O   1 
HETATM 2270 O  O   . HOH D 3 .   ? 1.745  -7.798  -23.506 1.00 49.07  ? 659 HOH A O   1 
HETATM 2271 O  O   . HOH D 3 .   ? 3.109  1.252   -1.003  1.00 44.79  ? 660 HOH A O   1 
HETATM 2272 O  O   . HOH D 3 .   ? 34.596 -12.484 6.338   1.00 42.83  ? 661 HOH A O   1 
HETATM 2273 O  O   . HOH D 3 .   ? 20.062 -20.436 -6.015  1.00 49.18  ? 662 HOH A O   1 
HETATM 2274 O  O   . HOH D 3 .   ? -2.497 -13.500 -6.416  1.00 51.11  ? 663 HOH A O   1 
HETATM 2275 O  O   . HOH D 3 .   ? 35.290 -7.171  -9.570  1.00 45.50  ? 664 HOH A O   1 
HETATM 2276 O  O   . HOH D 3 .   ? 23.559 5.821   2.199   1.00 41.82  ? 665 HOH A O   1 
HETATM 2277 O  O   . HOH D 3 .   ? 17.082 -0.432  1.358   1.00 47.99  ? 666 HOH A O   1 
HETATM 2278 O  O   . HOH D 3 .   ? 29.930 11.351  -24.558 1.00 33.98  ? 667 HOH A O   1 
HETATM 2279 O  O   . HOH D 3 .   ? 26.067 -4.006  -31.604 1.00 45.82  ? 668 HOH A O   1 
HETATM 2280 O  O   . HOH D 3 .   ? 18.862 -20.303 4.189   1.00 53.92  ? 669 HOH A O   1 
HETATM 2281 O  O   . HOH D 3 .   ? 16.407 -4.281  -31.181 1.00 50.68  ? 670 HOH A O   1 
HETATM 2282 O  O   . HOH D 3 .   ? 29.762 -14.789 -10.661 1.00 43.46  ? 671 HOH A O   1 
HETATM 2283 O  O   . HOH D 3 .   ? 10.539 -3.178  1.742   1.00 47.68  ? 672 HOH A O   1 
HETATM 2284 O  O   . HOH D 3 .   ? 3.198  -6.524  1.173   1.00 44.04  ? 673 HOH A O   1 
HETATM 2285 O  O   . HOH D 3 .   ? 19.416 2.518   1.889   1.00 45.47  ? 674 HOH A O   1 
HETATM 2286 O  O   . HOH D 3 .   ? 20.952 10.428  0.027   1.00 36.89  ? 675 HOH A O   1 
HETATM 2287 O  O   . HOH D 3 .   ? -1.283 -20.496 -12.498 1.00 49.15  ? 676 HOH A O   1 
HETATM 2288 O  O   . HOH D 3 .   ? 28.256 -13.431 -23.520 1.00 32.25  ? 677 HOH A O   1 
HETATM 2289 O  O   . HOH D 3 .   ? 22.162 14.373  -17.443 1.00 36.54  ? 678 HOH A O   1 
HETATM 2290 O  O   . HOH D 3 .   ? 0.056  -2.128  -10.334 1.00 50.27  ? 679 HOH A O   1 
HETATM 2291 O  O   . HOH D 3 .   ? 0.873  9.243   -10.432 1.00 40.74  ? 680 HOH A O   1 
HETATM 2292 O  O   . HOH D 3 .   ? 10.362 15.540  -22.646 1.00 44.69  ? 681 HOH A O   1 
HETATM 2293 O  O   . HOH D 3 .   ? 2.916  5.657   -18.353 1.00 47.67  ? 682 HOH A O   1 
HETATM 2294 O  O   . HOH D 3 .   ? 28.283 -18.979 -15.599 1.00 31.49  ? 683 HOH A O   1 
HETATM 2295 O  O   . HOH D 3 .   ? 29.558 16.544  -26.551 1.00 50.14  ? 684 HOH A O   1 
HETATM 2296 O  O   . HOH D 3 .   ? 16.683 17.900  -14.614 1.00 38.76  ? 685 HOH A O   1 
HETATM 2297 O  O   . HOH D 3 .   ? 0.955  -10.705 -23.590 1.00 49.98  ? 686 HOH A O   1 
HETATM 2298 O  O   . HOH D 3 .   ? 34.705 6.308   -5.620  1.00 33.76  ? 687 HOH A O   1 
HETATM 2299 O  O   . HOH D 3 .   ? 20.402 -25.026 -10.285 1.00 42.30  ? 688 HOH A O   1 
HETATM 2300 O  O   . HOH D 3 .   ? 43.314 6.471   -13.698 1.00 48.44  ? 689 HOH A O   1 
HETATM 2301 O  O   . HOH D 3 .   ? 12.298 -13.043 -26.243 1.00 58.33  ? 690 HOH A O   1 
HETATM 2302 O  O   . HOH D 3 .   ? 29.766 14.499  -2.954  1.00 40.33  ? 691 HOH A O   1 
HETATM 2303 O  O   . HOH D 3 .   ? 33.285 -7.416  -5.009  1.00 46.69  ? 692 HOH A O   1 
HETATM 2304 O  O   . HOH D 3 .   ? 13.923 2.651   -31.165 1.00 51.91  ? 693 HOH A O   1 
HETATM 2305 O  O   . HOH D 3 .   ? 41.480 -6.398  11.938  1.00 32.14  ? 694 HOH A O   1 
HETATM 2306 O  O   . HOH D 3 .   ? 10.458 -16.895 -22.809 1.00 51.96  ? 695 HOH A O   1 
HETATM 2307 O  O   . HOH D 3 .   ? 22.393 -15.753 -29.013 1.00 67.57  ? 696 HOH A O   1 
HETATM 2308 O  O   . HOH D 3 .   ? 32.449 8.067   -2.471  1.00 43.37  ? 697 HOH A O   1 
HETATM 2309 O  O   . HOH D 3 .   ? 7.463  -5.550  0.226   1.00 41.72  ? 698 HOH A O   1 
HETATM 2310 O  O   . HOH D 3 .   ? 15.993 13.111  -29.080 1.00 43.21  ? 699 HOH A O   1 
HETATM 2311 O  O   . HOH D 3 .   ? -2.706 -11.455 -1.911  1.00 53.31  ? 700 HOH A O   1 
HETATM 2312 O  O   . HOH D 3 .   ? -2.461 -13.350 3.347   1.00 50.20  ? 701 HOH A O   1 
HETATM 2313 O  O   . HOH D 3 .   ? 14.049 -9.367  -26.235 1.00 38.94  ? 702 HOH A O   1 
HETATM 2314 O  O   . HOH D 3 .   ? 36.328 -4.906  10.427  1.00 52.22  ? 703 HOH A O   1 
HETATM 2315 O  O   . HOH D 3 .   ? 39.722 -0.627  -12.862 1.00 52.36  ? 704 HOH A O   1 
HETATM 2316 O  O   . HOH D 3 .   ? 36.611 -5.962  -16.852 1.00 41.55  ? 705 HOH A O   1 
HETATM 2317 O  O   . HOH D 3 .   ? 33.998 17.323  -12.637 1.00 47.42  ? 706 HOH A O   1 
HETATM 2318 O  O   . HOH D 3 .   ? 9.534  -8.558  -25.796 1.00 49.91  ? 707 HOH A O   1 
HETATM 2319 O  O   . HOH D 3 .   ? 15.187 8.062   -28.845 1.00 46.96  ? 708 HOH A O   1 
HETATM 2320 O  O   . HOH D 3 .   ? 0.237  -12.227 -10.688 1.00 40.94  ? 709 HOH A O   1 
HETATM 2321 O  O   . HOH D 3 .   ? 8.855  5.053   -21.242 1.00 42.68  ? 710 HOH A O   1 
HETATM 2322 O  O   . HOH D 3 .   ? 34.060 -8.889  -6.087  1.00 51.80  ? 711 HOH A O   1 
HETATM 2323 O  O   . HOH D 3 .   ? 36.468 -4.109  -14.427 1.00 43.07  ? 712 HOH A O   1 
HETATM 2324 O  O   . HOH D 3 .   ? 36.653 -2.680  -12.069 1.00 45.34  ? 713 HOH A O   1 
HETATM 2325 O  O   . HOH D 3 .   ? 31.986 -16.972 -18.665 1.00 48.30  ? 714 HOH A O   1 
HETATM 2326 O  O   . HOH D 3 .   ? 35.438 -2.624  -6.881  1.00 48.59  ? 715 HOH A O   1 
HETATM 2327 O  O   . HOH D 3 .   ? 30.727 -18.479 -16.794 1.00 38.43  ? 716 HOH A O   1 
HETATM 2328 O  O   . HOH D 3 .   ? 13.563 -24.549 -1.891  1.00 52.63  ? 717 HOH A O   1 
HETATM 2329 O  O   . HOH D 3 .   ? 0.212  -15.641 -19.670 1.00 50.40  ? 718 HOH A O   1 
HETATM 2330 O  O   . HOH D 3 .   ? 15.107 4.962   -31.983 1.00 55.51  ? 719 HOH A O   1 
HETATM 2331 O  O   . HOH D 3 .   ? 32.013 -17.553 -14.547 1.00 53.31  ? 720 HOH A O   1 
HETATM 2332 O  O   . HOH D 3 .   ? 33.918 -14.673 -16.712 1.00 51.85  ? 721 HOH A O   1 
HETATM 2333 O  O   . HOH D 3 .   ? 14.060 11.063  -28.236 1.00 53.24  ? 722 HOH A O   1 
HETATM 2334 O  O   . HOH D 3 .   ? -1.109 -8.192  -8.838  1.00 49.23  ? 723 HOH A O   1 
HETATM 2335 O  O   . HOH D 3 .   ? 20.428 1.743   -32.062 1.00 45.22  ? 724 HOH A O   1 
HETATM 2336 O  O   . HOH D 3 .   ? 43.277 -3.086  9.205   1.00 51.91  ? 725 HOH A O   1 
HETATM 2337 O  O   . HOH D 3 .   ? 35.380 -9.032  -12.084 1.00 52.73  ? 726 HOH A O   1 
HETATM 2338 O  O   . HOH D 3 .   ? 42.137 -4.585  9.942   1.00 50.04  ? 727 HOH A O   1 
HETATM 2339 O  O   . HOH D 3 .   ? 9.418  17.821  -21.494 1.00 47.73  ? 728 HOH A O   1 
HETATM 2340 O  O   . HOH D 3 .   ? 19.647 8.629   1.485   1.00 47.94  ? 729 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . TYR A 20  ? 0.5670 0.4751 0.3246 0.0753  -0.0114 -0.0146 74  TYR A N   
2    C CA  . TYR A 20  ? 0.4849 0.4568 0.2965 0.1202  -0.0425 -0.0433 74  TYR A CA  
3    C C   . TYR A 20  ? 0.4870 0.4730 0.2932 0.1420  -0.0865 -0.0578 74  TYR A C   
4    O O   . TYR A 20  ? 0.5417 0.4894 0.3085 0.1631  -0.0571 -0.0703 74  TYR A O   
5    C CB  . TYR A 20  ? 0.4598 0.4224 0.2914 0.1304  -0.0208 -0.0459 74  TYR A CB  
6    C CG  . TYR A 20  ? 0.4461 0.3971 0.3236 0.1539  0.0153  -0.0287 74  TYR A CG  
7    C CD1 . TYR A 20  ? 0.4522 0.3854 0.3420 0.1374  0.0211  -0.0424 74  TYR A CD1 
8    C CD2 . TYR A 20  ? 0.4646 0.4147 0.3441 0.1454  0.0275  0.0042  74  TYR A CD2 
9    C CE1 . TYR A 20  ? 0.4516 0.3927 0.3505 0.1153  0.0060  -0.0546 74  TYR A CE1 
10   C CE2 . TYR A 20  ? 0.4646 0.4236 0.3585 0.1231  0.0253  0.0009  74  TYR A CE2 
11   C CZ  . TYR A 20  ? 0.4814 0.4040 0.3694 0.1040  0.0227  -0.0390 74  TYR A CZ  
12   O OH  . TYR A 20  ? 0.5182 0.4176 0.3962 0.1112  0.0295  -0.0125 74  TYR A OH  
13   N N   . ARG A 21  ? 0.4854 0.4892 0.2942 0.1110  -0.1103 -0.0558 75  ARG A N   
14   C CA  . ARG A 21  ? 0.4504 0.5178 0.3210 0.0874  -0.1474 -0.0205 75  ARG A CA  
15   C C   . ARG A 21  ? 0.4114 0.4519 0.3050 0.0307  -0.1336 -0.0136 75  ARG A C   
16   O O   . ARG A 21  ? 0.4201 0.4674 0.3005 0.0012  -0.1130 -0.0157 75  ARG A O   
17   C CB  . ARG A 21  ? 0.5155 0.6061 0.3792 0.0952  -0.1768 0.0095  75  ARG A CB  
18   C CG  . ARG A 21  ? 0.6441 0.6890 0.4826 0.0853  -0.1647 0.0266  75  ARG A CG  
19   C CD  . ARG A 21  ? 0.7438 0.7760 0.5712 0.0534  -0.1573 0.0238  75  ARG A CD  
20   N NE  . ARG A 21  ? 0.7936 0.8486 0.6438 0.0205  -0.1612 0.0257  75  ARG A NE  
21   C CZ  . ARG A 21  ? 0.8783 0.9167 0.7027 0.0119  -0.1552 0.0276  75  ARG A CZ  
22   N NH1 . ARG A 21  ? 0.8861 0.9282 0.7166 0.0180  -0.1400 0.0301  75  ARG A NH1 
23   N NH2 . ARG A 21  ? 0.9120 0.9345 0.7200 0.0114  -0.1470 0.0273  75  ARG A NH2 
24   N N   . SER A 22  ? 0.3975 0.3621 0.2694 0.0540  -0.1373 0.0015  76  SER A N   
25   C CA  . SER A 22  ? 0.3243 0.3154 0.2653 0.0728  -0.1215 0.0103  76  SER A CA  
26   C C   . SER A 22  ? 0.2874 0.2773 0.2498 0.0657  -0.0983 0.0109  76  SER A C   
27   O O   . SER A 22  ? 0.2757 0.2785 0.2427 0.0556  -0.0543 0.0123  76  SER A O   
28   C CB  . SER A 22  ? 0.3929 0.3230 0.3141 0.0812  -0.1001 0.0279  76  SER A CB  
29   O OG  . SER A 22  ? 0.4287 0.3307 0.3619 0.1039  -0.0951 0.0105  76  SER A OG  
30   N N   . ILE A 23  ? 0.3201 0.2295 0.2385 0.0145  -0.1035 0.0197  77  ILE A N   
31   C CA  . ILE A 23  ? 0.3287 0.2096 0.2470 -0.0242 -0.0996 0.0386  77  ILE A CA  
32   C C   . ILE A 23  ? 0.2788 0.1938 0.2254 0.0228  -0.0644 0.0368  77  ILE A C   
33   O O   . ILE A 23  ? 0.2772 0.2494 0.1900 0.0061  -0.0382 0.0298  77  ILE A O   
34   C CB  . ILE A 23  ? 0.4419 0.2484 0.2603 -0.0099 -0.0641 0.0344  77  ILE A CB  
35   C CG1 . ILE A 23  ? 0.4564 0.2507 0.2511 0.0637  -0.0538 0.0218  77  ILE A CG1 
36   C CG2 . ILE A 23  ? 0.4816 0.2169 0.2831 -0.0135 -0.0856 0.0836  77  ILE A CG2 
37   C CD1 . ILE A 23  ? 0.5072 0.3436 0.2329 0.0826  -0.0628 -0.0137 77  ILE A CD1 
38   N N   . ASP A 24  ? 0.2842 0.2165 0.2294 0.0238  -0.0392 0.0408  78  ASP A N   
39   C CA  . ASP A 24  ? 0.2614 0.2150 0.2506 0.0214  -0.0139 0.0311  78  ASP A CA  
40   C C   . ASP A 24  ? 0.2893 0.2166 0.2400 0.0456  -0.0342 0.0323  78  ASP A C   
41   O O   . ASP A 24  ? 0.2921 0.2235 0.2525 0.0413  -0.0457 0.0479  78  ASP A O   
42   C CB  . ASP A 24  ? 0.2428 0.2118 0.2764 0.0204  0.0244  0.0404  78  ASP A CB  
43   C CG  . ASP A 24  ? 0.2605 0.2674 0.3012 -0.0019 0.0011  0.0639  78  ASP A CG  
44   O OD1 . ASP A 24  ? 0.2673 0.3245 0.3054 0.0179  0.0151  0.0638  78  ASP A OD1 
45   O OD2 . ASP A 24  ? 0.2556 0.2811 0.3207 0.0166  0.0157  0.0678  78  ASP A OD2 
46   N N   . GLU A 25  ? 0.2741 0.2289 0.2374 0.0546  -0.0159 0.0329  79  GLU A N   
47   C CA  . GLU A 25  ? 0.2945 0.2662 0.2101 0.0747  -0.0865 0.0144  79  GLU A CA  
48   C C   . GLU A 25  ? 0.2977 0.2415 0.2164 0.0576  -0.0397 0.0247  79  GLU A C   
49   O O   . GLU A 25  ? 0.3156 0.2551 0.2199 0.0573  -0.0172 0.0453  79  GLU A O   
50   C CB  . GLU A 25  ? 0.3389 0.3229 0.2265 0.1189  -0.1252 -0.0160 79  GLU A CB  
51   C CG  . GLU A 25  ? 0.4281 0.3966 0.2970 0.1394  -0.1739 -0.0155 79  GLU A CG  
52   C CD  . GLU A 25  ? 0.5178 0.5360 0.3976 0.1661  -0.1995 -0.0169 79  GLU A CD  
53   O OE1 . GLU A 25  ? 0.5920 0.5603 0.4082 0.1307  -0.1561 -0.0359 79  GLU A OE1 
54   O OE2 . GLU A 25  ? 0.5837 0.6046 0.4680 0.1923  -0.2172 0.0133  79  GLU A OE2 
55   N N   . VAL A 26  ? 0.2931 0.2071 0.2137 0.0766  -0.0479 0.0260  80  VAL A N   
56   C CA  . VAL A 26  ? 0.2783 0.1815 0.2226 0.0255  -0.0342 0.0285  80  VAL A CA  
57   C C   . VAL A 26  ? 0.2786 0.2150 0.2152 0.0630  -0.0206 0.0170  80  VAL A C   
58   O O   . VAL A 26  ? 0.2803 0.2475 0.2134 0.0699  0.0130  0.0415  80  VAL A O   
59   C CB  . VAL A 26  ? 0.2530 0.2037 0.2225 0.0297  -0.0310 0.0210  80  VAL A CB  
60   C CG1 . VAL A 26  ? 0.2555 0.2052 0.2405 0.0305  -0.0386 0.0200  80  VAL A CG1 
61   C CG2 . VAL A 26  ? 0.2966 0.2083 0.2472 0.0165  -0.0524 -0.0061 80  VAL A CG2 
62   N N   . THR A 27  ? 0.2731 0.1936 0.2027 0.0423  -0.0215 0.0318  81  THR A N   
63   C CA  . THR A 27  ? 0.2331 0.1936 0.2075 0.0140  0.0079  0.0298  81  THR A CA  
64   C C   . THR A 27  ? 0.2126 0.2173 0.2036 -0.0005 -0.0219 0.0347  81  THR A C   
65   O O   . THR A 27  ? 0.2230 0.2347 0.1948 0.0187  -0.0086 0.0439  81  THR A O   
66   C CB  . THR A 27  ? 0.2295 0.1965 0.2034 -0.0068 -0.0096 0.0191  81  THR A CB  
67   O OG1 . THR A 27  ? 0.2478 0.2068 0.2075 0.0255  0.0024  0.0347  81  THR A OG1 
68   C CG2 . THR A 27  ? 0.2223 0.2193 0.1912 0.0140  -0.0412 0.0309  81  THR A CG2 
69   N N   . ALA A 28  ? 0.2324 0.2190 0.2021 0.0544  -0.0262 0.0576  82  ALA A N   
70   C CA  . ALA A 28  ? 0.2375 0.2510 0.2317 0.0730  -0.0018 0.0728  82  ALA A CA  
71   C C   . ALA A 28  ? 0.2645 0.2391 0.2321 0.0568  -0.0053 0.0585  82  ALA A C   
72   O O   . ALA A 28  ? 0.2941 0.2469 0.2485 0.0363  -0.0073 0.0685  82  ALA A O   
73   C CB  . ALA A 28  ? 0.2740 0.2649 0.2344 0.0635  -0.0162 0.0668  82  ALA A CB  
74   N N   . ALA A 29  ? 0.2646 0.2673 0.2135 0.0638  0.0131  0.0530  83  ALA A N   
75   C CA  . ALA A 29  ? 0.2911 0.2454 0.2326 0.0680  -0.0146 0.0309  83  ALA A CA  
76   C C   . ALA A 29  ? 0.3232 0.2792 0.2343 0.0680  0.0075  0.0558  83  ALA A C   
77   O O   . ALA A 29  ? 0.3022 0.2995 0.2597 0.0462  0.0288  0.0636  83  ALA A O   
78   C CB  . ALA A 29  ? 0.2928 0.2728 0.2247 0.0659  -0.0274 0.0075  83  ALA A CB  
79   N N   . LEU A 30  ? 0.3035 0.2682 0.2099 0.0603  -0.0033 0.0346  84  LEU A N   
80   C CA  . LEU A 30  ? 0.2503 0.2640 0.2157 0.0436  0.0308  0.0552  84  LEU A CA  
81   C C   . LEU A 30  ? 0.2442 0.2660 0.2265 0.0637  0.0245  0.0707  84  LEU A C   
82   O O   . LEU A 30  ? 0.2375 0.3164 0.2341 0.0668  0.0189  0.0725  84  LEU A O   
83   C CB  . LEU A 30  ? 0.2562 0.2783 0.2415 0.0363  0.0180  0.0789  84  LEU A CB  
84   C CG  . LEU A 30  ? 0.2537 0.2602 0.2540 0.0653  0.0475  0.0787  84  LEU A CG  
85   C CD1 . LEU A 30  ? 0.2414 0.2734 0.2378 0.0747  0.0222  0.0692  84  LEU A CD1 
86   C CD2 . LEU A 30  ? 0.3224 0.2416 0.2770 0.0715  0.0418  0.0628  84  LEU A CD2 
87   N N   . SER A 31  ? 0.2500 0.2359 0.2461 0.0537  -0.0013 0.0673  85  SER A N   
88   C CA  . SER A 31  ? 0.2605 0.2478 0.2619 0.0617  -0.0062 0.0525  85  SER A CA  
89   C C   . SER A 31  ? 0.2633 0.2912 0.2541 0.0442  -0.0067 0.0806  85  SER A C   
90   O O   . SER A 31  ? 0.2605 0.3271 0.2488 0.0483  -0.0052 0.0530  85  SER A O   
91   C CB  . SER A 31  ? 0.2867 0.2317 0.2843 0.0817  -0.0063 0.0514  85  SER A CB  
92   O OG  . SER A 31  ? 0.3125 0.2395 0.3057 0.0441  -0.0027 0.0419  85  SER A OG  
93   N N   . HIS A 32  ? 0.2280 0.3230 0.2365 0.0472  0.0120  0.0994  86  HIS A N   
94   C CA  . HIS A 32  ? 0.2511 0.3441 0.2641 0.0580  0.0257  0.1120  86  HIS A CA  
95   C C   . HIS A 32  ? 0.2447 0.3429 0.3047 0.0611  0.0557  0.1078  86  HIS A C   
96   O O   . HIS A 32  ? 0.2705 0.3577 0.3392 0.0567  0.0455  0.1044  86  HIS A O   
97   C CB  . HIS A 32  ? 0.2986 0.3819 0.2491 0.0428  0.0288  0.1368  86  HIS A CB  
98   C CG  . HIS A 32  ? 0.4323 0.4451 0.2872 0.0470  0.0449  0.1250  86  HIS A CG  
99   N ND1 . HIS A 32  ? 0.5005 0.4891 0.3016 0.0266  0.0493  0.1308  86  HIS A ND1 
100  C CD2 . HIS A 32  ? 0.4867 0.5016 0.3065 0.0428  0.0781  0.0996  86  HIS A CD2 
101  C CE1 . HIS A 32  ? 0.5490 0.5081 0.3159 0.0481  0.0628  0.1315  86  HIS A CE1 
102  N NE2 . HIS A 32  ? 0.5601 0.5313 0.3139 0.0435  0.0560  0.1029  86  HIS A NE2 
103  N N   . ALA A 33  ? 0.2778 0.3506 0.3088 0.1045  0.0518  0.1065  87  ALA A N   
104  C CA  . ALA A 33  ? 0.2565 0.3784 0.3212 0.1450  0.0641  0.1257  87  ALA A CA  
105  C C   . ALA A 33  ? 0.2714 0.4286 0.3601 0.1120  0.0738  0.1326  87  ALA A C   
106  O O   . ALA A 33  ? 0.2589 0.4766 0.3945 0.0706  0.0888  0.1283  87  ALA A O   
107  C CB  . ALA A 33  ? 0.3355 0.3703 0.3338 0.1634  0.0544  0.1239  87  ALA A CB  
108  N N   . GLY A 34  ? 0.2574 0.4091 0.3325 0.0727  0.0827  0.1392  88  GLY A N   
109  C CA  . GLY A 34  ? 0.2737 0.3989 0.3528 0.0781  0.0495  0.1552  88  GLY A CA  
110  C C   . GLY A 34  ? 0.2735 0.4235 0.3475 0.0170  0.0403  0.1238  88  GLY A C   
111  O O   . GLY A 34  ? 0.2876 0.4604 0.3617 0.0042  0.0173  0.1214  88  GLY A O   
112  N N   . LEU A 35  ? 0.2569 0.3815 0.3113 0.0380  0.0173  0.1260  89  LEU A N   
113  C CA  . LEU A 35  ? 0.2852 0.3407 0.3021 0.0416  0.0452  0.1113  89  LEU A CA  
114  C C   . LEU A 35  ? 0.2663 0.3406 0.3403 0.0421  0.0349  0.0995  89  LEU A C   
115  O O   . LEU A 35  ? 0.2827 0.3772 0.3397 0.0378  0.0254  0.0974  89  LEU A O   
116  C CB  . LEU A 35  ? 0.3007 0.3203 0.2881 0.0456  0.0048  0.0979  89  LEU A CB  
117  C CG  . LEU A 35  ? 0.2882 0.3297 0.2895 0.0481  -0.0105 0.0861  89  LEU A CG  
118  C CD1 . LEU A 35  ? 0.2874 0.3108 0.2883 0.0677  -0.0395 0.0579  89  LEU A CD1 
119  C CD2 . LEU A 35  ? 0.3376 0.3284 0.2830 -0.0009 -0.0076 0.1038  89  LEU A CD2 
120  N N   . GLU A 36  ? 0.2716 0.3436 0.3797 -0.0104 -0.0007 0.1017  90  GLU A N   
121  C CA  . GLU A 36  ? 0.3400 0.3613 0.3893 -0.0561 0.0026  0.1048  90  GLU A CA  
122  C C   . GLU A 36  ? 0.3706 0.3547 0.3667 -0.0991 0.0219  0.0884  90  GLU A C   
123  O O   . GLU A 36  ? 0.4351 0.4149 0.3766 -0.1037 0.0117  0.0840  90  GLU A O   
124  C CB  . GLU A 36  ? 0.4376 0.4268 0.4306 -0.0484 0.0153  0.1283  90  GLU A CB  
125  C CG  . GLU A 36  ? 0.5602 0.4957 0.5090 -0.0537 0.0110  0.1462  90  GLU A CG  
126  C CD  . GLU A 36  ? 0.6979 0.5513 0.5609 -0.0356 0.0165  0.1523  90  GLU A CD  
127  O OE1 . GLU A 36  ? 0.7354 0.5655 0.5948 -0.0215 0.0252  0.1742  90  GLU A OE1 
128  O OE2 . GLU A 36  ? 0.7346 0.5843 0.5894 -0.0450 0.0049  0.1409  90  GLU A OE2 
129  N N   . SER A 37  ? 0.3799 0.3306 0.3660 -0.0674 0.0191  0.0749  91  SER A N   
130  C CA  . SER A 37  ? 0.3601 0.2987 0.3418 -0.0433 0.0398  0.0758  91  SER A CA  
131  C C   . SER A 37  ? 0.2781 0.2966 0.3397 0.0157  0.0315  0.0837  91  SER A C   
132  O O   . SER A 37  ? 0.2654 0.3574 0.3423 0.0166  0.0520  0.0707  91  SER A O   
133  C CB  . SER A 37  ? 0.4396 0.3636 0.3412 -0.0439 0.0451  0.0569  91  SER A CB  
134  O OG  . SER A 37  ? 0.5072 0.3858 0.3600 -0.0450 0.0669  0.0577  91  SER A OG  
135  N N   . SER A 38  ? 0.2939 0.2284 0.3027 -0.0067 -0.0014 0.0708  92  SER A N   
136  C CA  . SER A 38  ? 0.2759 0.2617 0.2820 0.0078  0.0289  0.0568  92  SER A CA  
137  C C   . SER A 38  ? 0.2495 0.2528 0.2742 0.0120  0.0344  0.0508  92  SER A C   
138  O O   . SER A 38  ? 0.2449 0.3142 0.3191 0.0325  0.0236  0.0466  92  SER A O   
139  C CB  . SER A 38  ? 0.3000 0.2673 0.3348 -0.0066 -0.0531 0.0453  92  SER A CB  
140  O OG  . SER A 38  ? 0.3478 0.3109 0.3341 -0.0218 -0.0313 0.0445  92  SER A OG  
141  N N   . ASN A 39  ? 0.2813 0.2085 0.2242 0.0115  0.0331  0.0301  93  ASN A N   
142  C CA  . ASN A 39  ? 0.2478 0.1985 0.2244 -0.0194 0.0166  -0.0157 93  ASN A CA  
143  C C   . ASN A 39  ? 0.2081 0.1749 0.2479 0.0005  0.0373  -0.0133 93  ASN A C   
144  O O   . ASN A 39  ? 0.2322 0.2107 0.2936 0.0223  0.0436  -0.0189 93  ASN A O   
145  C CB  . ASN A 39  ? 0.2577 0.1745 0.2113 -0.0250 0.0447  -0.0131 93  ASN A CB  
146  C CG  . ASN A 39  ? 0.2188 0.2313 0.2809 -0.0186 0.0707  -0.0201 93  ASN A CG  
147  O OD1 . ASN A 39  ? 0.3142 0.2681 0.3259 0.0268  0.1052  -0.0480 93  ASN A OD1 
148  N ND2 . ASN A 39  ? 0.2747 0.2597 0.3465 -0.0401 0.0275  0.0212  93  ASN A ND2 
149  N N   . LEU A 40  ? 0.2221 0.1676 0.2289 -0.0031 0.0186  0.0353  94  LEU A N   
150  C CA  . LEU A 40  ? 0.1965 0.1707 0.2217 -0.0106 0.0131  0.0264  94  LEU A CA  
151  C C   . LEU A 40  ? 0.1735 0.1854 0.2010 -0.0035 0.0172  0.0194  94  LEU A C   
152  O O   . LEU A 40  ? 0.2136 0.1866 0.2088 0.0144  0.0195  0.0393  94  LEU A O   
153  C CB  . LEU A 40  ? 0.1921 0.1735 0.2128 0.0100  0.0271  0.0017  94  LEU A CB  
154  C CG  . LEU A 40  ? 0.2078 0.1847 0.2063 0.0120  -0.0005 -0.0144 94  LEU A CG  
155  C CD1 . LEU A 40  ? 0.2517 0.2212 0.2022 0.0415  -0.0149 -0.0247 94  LEU A CD1 
156  C CD2 . LEU A 40  ? 0.2022 0.2455 0.2318 0.0195  -0.0394 0.0147  94  LEU A CD2 
157  N N   . ILE A 41  ? 0.1804 0.1649 0.1805 0.0067  -0.0013 0.0166  95  ILE A N   
158  C CA  . ILE A 41  ? 0.1976 0.1556 0.1544 0.0051  -0.0042 0.0092  95  ILE A CA  
159  C C   . ILE A 41  ? 0.2047 0.1616 0.1654 -0.0198 0.0062  0.0195  95  ILE A C   
160  O O   . ILE A 41  ? 0.2067 0.1759 0.1650 0.0116  0.0078  0.0061  95  ILE A O   
161  C CB  . ILE A 41  ? 0.1816 0.1840 0.1571 -0.0097 -0.0090 0.0261  95  ILE A CB  
162  C CG1 . ILE A 41  ? 0.1788 0.2032 0.2028 -0.0232 -0.0207 -0.0001 95  ILE A CG1 
163  C CG2 . ILE A 41  ? 0.2291 0.2267 0.1491 0.0086  -0.0260 0.0433  95  ILE A CG2 
164  C CD1 . ILE A 41  ? 0.1930 0.2352 0.2139 0.0104  -0.0131 -0.0072 95  ILE A CD1 
165  N N   . VAL A 42  ? 0.1783 0.1607 0.1836 -0.0070 0.0043  0.0251  96  VAL A N   
166  C CA  . VAL A 42  ? 0.1896 0.1679 0.1901 -0.0115 -0.0236 0.0100  96  VAL A CA  
167  C C   . VAL A 42  ? 0.1898 0.1648 0.1833 -0.0134 0.0035  0.0036  96  VAL A C   
168  O O   . VAL A 42  ? 0.2688 0.1739 0.1662 -0.0185 0.0176  0.0112  96  VAL A O   
169  C CB  . VAL A 42  ? 0.2042 0.1839 0.2252 -0.0259 -0.0254 0.0465  96  VAL A CB  
170  C CG1 . VAL A 42  ? 0.2438 0.1980 0.2447 -0.0354 -0.0248 0.0441  96  VAL A CG1 
171  C CG2 . VAL A 42  ? 0.2391 0.1907 0.2181 0.0106  -0.0051 0.0566  96  VAL A CG2 
172  N N   . GLY A 43  ? 0.1765 0.1551 0.1863 0.0062  0.0000  0.0214  97  GLY A N   
173  C CA  . GLY A 43  ? 0.1503 0.1822 0.1938 -0.0218 0.0052  0.0314  97  GLY A CA  
174  C C   . GLY A 43  ? 0.1539 0.1787 0.1824 -0.0129 0.0177  0.0249  97  GLY A C   
175  O O   . GLY A 43  ? 0.2302 0.1866 0.1635 -0.0031 0.0013  -0.0012 97  GLY A O   
176  N N   . ILE A 44  ? 0.1474 0.1876 0.2003 -0.0117 -0.0058 0.0197  98  ILE A N   
177  C CA  . ILE A 44  ? 0.1475 0.1799 0.2239 -0.0108 0.0048  0.0089  98  ILE A CA  
178  C C   . ILE A 44  ? 0.1620 0.1704 0.1929 0.0070  0.0049  0.0120  98  ILE A C   
179  O O   . ILE A 44  ? 0.1973 0.1909 0.1789 -0.0151 -0.0270 0.0214  98  ILE A O   
180  C CB  . ILE A 44  ? 0.1467 0.1861 0.2416 -0.0041 -0.0015 0.0163  98  ILE A CB  
181  C CG1 . ILE A 44  ? 0.1885 0.1747 0.2445 0.0254  0.0076  0.0120  98  ILE A CG1 
182  C CG2 . ILE A 44  ? 0.1694 0.2024 0.2448 -0.0251 -0.0096 0.0329  98  ILE A CG2 
183  C CD1 . ILE A 44  ? 0.2484 0.2083 0.2516 0.0120  0.0225  0.0025  98  ILE A CD1 
184  N N   . ASP A 45  ? 0.1732 0.1534 0.2013 0.0082  -0.0053 0.0261  99  ASP A N   
185  C CA  . ASP A 45  ? 0.1870 0.1763 0.2116 -0.0014 -0.0075 0.0254  99  ASP A CA  
186  C C   . ASP A 45  ? 0.1762 0.1954 0.2012 -0.0149 -0.0150 0.0460  99  ASP A C   
187  O O   . ASP A 45  ? 0.1924 0.2146 0.2178 -0.0177 -0.0413 0.0405  99  ASP A O   
188  C CB  . ASP A 45  ? 0.2732 0.1545 0.2102 0.0179  -0.0021 -0.0192 99  ASP A CB  
189  C CG  . ASP A 45  ? 0.3093 0.1948 0.2321 0.0368  0.0362  -0.0176 99  ASP A CG  
190  O OD1 . ASP A 45  ? 0.3217 0.2314 0.2355 0.0247  -0.0033 0.0190  99  ASP A OD1 
191  O OD2 . ASP A 45  ? 0.3808 0.2726 0.3114 0.0458  0.0987  0.0188  99  ASP A OD2 
192  N N   . VAL A 46  ? 0.2089 0.1659 0.2155 -0.0178 0.0191  0.0418  100 VAL A N   
193  C CA  . VAL A 46  ? 0.1770 0.1370 0.2397 0.0090  0.0210  0.0404  100 VAL A CA  
194  C C   . VAL A 46  ? 0.2060 0.1844 0.2325 -0.0247 0.0231  0.0461  100 VAL A C   
195  O O   . VAL A 46  ? 0.2429 0.2069 0.2470 -0.0265 0.0129  0.0558  100 VAL A O   
196  C CB  . VAL A 46  ? 0.1685 0.1731 0.2585 -0.0117 -0.0015 0.0090  100 VAL A CB  
197  C CG1 . VAL A 46  ? 0.2429 0.1940 0.2453 0.0219  0.0042  0.0213  100 VAL A CG1 
198  C CG2 . VAL A 46  ? 0.2095 0.2011 0.2724 -0.0094 -0.0105 0.0004  100 VAL A CG2 
199  N N   . THR A 47  ? 0.2201 0.1817 0.2465 0.0054  0.0009  0.0173  101 THR A N   
200  C CA  . THR A 47  ? 0.2657 0.1794 0.2786 0.0045  -0.0001 0.0268  101 THR A CA  
201  C C   . THR A 47  ? 0.2454 0.1772 0.3056 -0.0199 -0.0369 0.0562  101 THR A C   
202  O O   . THR A 47  ? 0.2313 0.2110 0.2825 -0.0178 -0.0600 0.0356  101 THR A O   
203  C CB  . THR A 47  ? 0.2743 0.2155 0.2358 0.0215  -0.0134 0.0064  101 THR A CB  
204  O OG1 . THR A 47  ? 0.3038 0.2377 0.2184 0.0195  -0.0108 -0.0048 101 THR A OG1 
205  C CG2 . THR A 47  ? 0.2427 0.2157 0.2470 0.0041  -0.0085 0.0086  101 THR A CG2 
206  N N   . LYS A 48  ? 0.2764 0.1622 0.3379 -0.0420 -0.0585 0.0544  102 LYS A N   
207  C CA  . LYS A 48  ? 0.3002 0.2064 0.3663 -0.0252 -0.0932 0.0715  102 LYS A CA  
208  C C   . LYS A 48  ? 0.3222 0.2013 0.3758 -0.0036 -0.1066 0.0575  102 LYS A C   
209  O O   . LYS A 48  ? 0.2998 0.2034 0.3844 -0.0185 -0.0979 0.0423  102 LYS A O   
210  C CB  . LYS A 48  ? 0.3403 0.2463 0.3810 -0.0436 -0.1224 0.1009  102 LYS A CB  
211  C CG  . LYS A 48  ? 0.4095 0.2614 0.3855 -0.1019 -0.0876 0.0874  102 LYS A CG  
212  C CD  . LYS A 48  ? 0.3811 0.3434 0.4282 -0.0789 -0.0167 0.0896  102 LYS A CD  
213  C CE  . LYS A 48  ? 0.4062 0.3849 0.4398 -0.0735 0.0224  0.1060  102 LYS A CE  
214  N NZ  . LYS A 48  ? 0.4407 0.4331 0.4622 -0.0733 0.0451  0.1096  102 LYS A NZ  
215  N N   . SER A 49  ? 0.3510 0.2083 0.3337 -0.0034 -0.0862 0.0416  103 SER A N   
216  C CA  . SER A 49  ? 0.3579 0.2403 0.3429 0.0247  -0.0749 0.0424  103 SER A CA  
217  C C   . SER A 49  ? 0.3430 0.1935 0.3442 0.0444  -0.0717 0.0332  103 SER A C   
218  O O   . SER A 49  ? 0.3301 0.2120 0.3330 -0.0285 -0.0960 0.0374  103 SER A O   
219  C CB  . SER A 49  ? 0.4316 0.3090 0.3604 0.0378  -0.0646 0.0589  103 SER A CB  
220  O OG  . SER A 49  ? 0.4265 0.3536 0.3820 0.0390  -0.0454 0.0924  103 SER A OG  
221  N N   . ASN A 50  ? 0.3189 0.1803 0.3373 0.0319  -0.0471 0.0290  104 ASN A N   
222  C CA  . ASN A 50  ? 0.2749 0.1755 0.3251 0.0034  -0.0552 0.0257  104 ASN A CA  
223  C C   . ASN A 50  ? 0.2712 0.1847 0.3445 -0.0197 -0.0908 0.0585  104 ASN A C   
224  O O   . ASN A 50  ? 0.2660 0.2144 0.3623 -0.0192 -0.1105 0.0692  104 ASN A O   
225  C CB  . ASN A 50  ? 0.2560 0.1942 0.2956 -0.0155 -0.0374 0.0319  104 ASN A CB  
226  C CG  . ASN A 50  ? 0.2846 0.2224 0.2696 -0.0149 -0.0794 0.0243  104 ASN A CG  
227  O OD1 . ASN A 50  ? 0.3076 0.2061 0.2646 -0.0055 -0.0706 0.0041  104 ASN A OD1 
228  N ND2 . ASN A 50  ? 0.2601 0.1959 0.2619 -0.0194 -0.0583 0.0248  104 ASN A ND2 
229  N N   . GLU A 51  ? 0.3135 0.1889 0.3671 -0.0438 -0.0767 0.0613  105 GLU A N   
230  C CA  . GLU A 51  ? 0.3352 0.1996 0.3769 -0.0535 -0.1001 0.0837  105 GLU A CA  
231  C C   . GLU A 51  ? 0.3805 0.2420 0.3878 -0.0678 -0.1141 0.0691  105 GLU A C   
232  O O   . GLU A 51  ? 0.4132 0.3127 0.3953 -0.0852 -0.1286 0.0431  105 GLU A O   
233  C CB  . GLU A 51  ? 0.3493 0.2586 0.3728 -0.0937 -0.0835 0.0746  105 GLU A CB  
234  C CG  . GLU A 51  ? 0.3944 0.3014 0.4100 -0.0747 -0.0617 0.0650  105 GLU A CG  
235  C CD  . GLU A 51  ? 0.5058 0.3402 0.4622 -0.0461 -0.0560 0.0510  105 GLU A CD  
236  O OE1 . GLU A 51  ? 0.5035 0.3888 0.4710 -0.0028 -0.0430 0.0420  105 GLU A OE1 
237  O OE2 . GLU A 51  ? 0.5798 0.3592 0.4640 -0.0327 -0.0673 0.0470  105 GLU A OE2 
238  N N   . TRP A 52  ? 0.3803 0.2467 0.3877 -0.0605 -0.1464 0.0304  106 TRP A N   
239  C CA  . TRP A 52  ? 0.4555 0.2297 0.4128 -0.0680 -0.1326 0.0226  106 TRP A CA  
240  C C   . TRP A 52  ? 0.4363 0.2315 0.4083 -0.0925 -0.1236 -0.0009 106 TRP A C   
241  O O   . TRP A 52  ? 0.5007 0.2445 0.4064 -0.0631 -0.1429 0.0097  106 TRP A O   
242  C CB  . TRP A 52  ? 0.4748 0.2575 0.4261 -0.0248 -0.0915 0.0117  106 TRP A CB  
243  C CG  . TRP A 52  ? 0.4884 0.2667 0.4255 -0.0128 -0.1082 0.0267  106 TRP A CG  
244  C CD1 . TRP A 52  ? 0.5066 0.2715 0.4283 -0.0130 -0.0933 0.0360  106 TRP A CD1 
245  C CD2 . TRP A 52  ? 0.5294 0.2420 0.4213 0.0075  -0.0686 0.0378  106 TRP A CD2 
246  N NE1 . TRP A 52  ? 0.5375 0.2674 0.4270 0.0010  -0.0649 0.0335  106 TRP A NE1 
247  C CE2 . TRP A 52  ? 0.5147 0.2318 0.4181 0.0434  -0.0867 0.0288  106 TRP A CE2 
248  C CE3 . TRP A 52  ? 0.5413 0.2415 0.4296 0.0142  -0.0747 0.0199  106 TRP A CE3 
249  C CZ2 . TRP A 52  ? 0.5173 0.2223 0.4230 0.0365  -0.0772 0.0045  106 TRP A CZ2 
250  C CZ3 . TRP A 52  ? 0.5466 0.2592 0.4302 -0.0092 -0.0722 0.0051  106 TRP A CZ3 
251  C CH2 . TRP A 52  ? 0.5170 0.2391 0.4200 0.0103  -0.0943 0.0102  106 TRP A CH2 
252  N N   . THR A 53  ? 0.3687 0.2361 0.4010 -0.0745 -0.1039 0.0114  107 THR A N   
253  C CA  . THR A 53  ? 0.3505 0.2425 0.4135 -0.0626 -0.0910 0.0038  107 THR A CA  
254  C C   . THR A 53  ? 0.3669 0.2529 0.4243 -0.1031 -0.0998 0.0197  107 THR A C   
255  O O   . THR A 53  ? 0.4125 0.2556 0.4314 -0.0739 -0.0831 0.0411  107 THR A O   
256  C CB  . THR A 53  ? 0.3464 0.2557 0.4182 -0.0067 -0.0934 -0.0063 107 THR A CB  
257  O OG1 . THR A 53  ? 0.3696 0.2461 0.4270 -0.0319 -0.0842 -0.0234 107 THR A OG1 
258  C CG2 . THR A 53  ? 0.3228 0.2877 0.4126 0.0031  -0.0789 -0.0274 107 THR A CG2 
259  N N   . GLY A 54  ? 0.3234 0.2480 0.4235 -0.0587 -0.1417 0.0247  108 GLY A N   
260  C CA  . GLY A 54  ? 0.3406 0.2637 0.4392 -0.0650 -0.1416 0.0328  108 GLY A CA  
261  C C   . GLY A 54  ? 0.3970 0.2345 0.4644 -0.0804 -0.1358 0.0424  108 GLY A C   
262  O O   . GLY A 54  ? 0.3996 0.2752 0.4734 -0.0997 -0.1513 0.0457  108 GLY A O   
263  N N   . ALA A 55  ? 0.4391 0.2328 0.4735 -0.1281 -0.1169 0.0388  109 ALA A N   
264  C CA  . ALA A 55  ? 0.4917 0.2782 0.4984 -0.1236 -0.1234 0.0279  109 ALA A CA  
265  C C   . ALA A 55  ? 0.5050 0.2912 0.5209 -0.1737 -0.1383 0.0134  109 ALA A C   
266  O O   . ALA A 55  ? 0.4731 0.3337 0.5211 -0.1688 -0.1057 0.0293  109 ALA A O   
267  C CB  . ALA A 55  ? 0.5396 0.2488 0.5035 -0.1103 -0.0906 0.0036  109 ALA A CB  
268  N N   . ARG A 56  ? 0.5269 0.2914 0.5438 -0.1635 -0.1832 0.0088  110 ARG A N   
269  C CA  . ARG A 56  ? 0.5560 0.3665 0.5756 -0.1604 -0.1893 0.0068  110 ARG A CA  
270  C C   . ARG A 56  ? 0.4476 0.3747 0.5340 -0.0787 -0.2183 0.0461  110 ARG A C   
271  O O   . ARG A 56  ? 0.4749 0.4163 0.5335 -0.0530 -0.2181 0.0409  110 ARG A O   
272  C CB  . ARG A 56  ? 0.6614 0.4545 0.6581 -0.1609 -0.1594 -0.0162 110 ARG A CB  
273  C CG  . ARG A 56  ? 0.7764 0.5479 0.7549 -0.1266 -0.1238 -0.0215 110 ARG A CG  
274  C CD  . ARG A 56  ? 0.8534 0.6368 0.8195 -0.1012 -0.1002 -0.0377 110 ARG A CD  
275  N NE  . ARG A 56  ? 0.9488 0.7141 0.8811 -0.0762 -0.0793 -0.0496 110 ARG A NE  
276  C CZ  . ARG A 56  ? 1.0319 0.7698 0.9331 -0.0621 -0.0985 -0.0569 110 ARG A CZ  
277  N NH1 . ARG A 56  ? 1.0255 0.7978 0.9490 -0.0703 -0.1156 -0.0524 110 ARG A NH1 
278  N NH2 . ARG A 56  ? 1.0615 0.7877 0.9458 -0.0617 -0.1097 -0.0642 110 ARG A NH2 
279  N N   . SER A 57  ? 0.4017 0.3051 0.5083 -0.0843 -0.1746 0.0688  111 SER A N   
280  C CA  . SER A 57  ? 0.3648 0.3132 0.5099 -0.0653 -0.1445 0.0638  111 SER A CA  
281  C C   . SER A 57  ? 0.3492 0.3438 0.4942 -0.0562 -0.1203 0.0509  111 SER A C   
282  O O   . SER A 57  ? 0.3676 0.3655 0.4815 -0.0339 -0.1115 0.0528  111 SER A O   
283  C CB  . SER A 57  ? 0.3095 0.2945 0.5354 -0.0667 -0.1377 0.0629  111 SER A CB  
284  O OG  . SER A 57  ? 0.3050 0.2781 0.5565 -0.0483 -0.1178 0.0393  111 SER A OG  
285  N N   . PHE A 58  ? 0.2792 0.3256 0.4785 -0.0871 -0.1096 0.0506  112 PHE A N   
286  C CA  . PHE A 58  ? 0.3040 0.3279 0.4543 -0.1087 -0.1189 0.0423  112 PHE A CA  
287  C C   . PHE A 58  ? 0.3300 0.3165 0.4531 -0.1259 -0.1327 0.0631  112 PHE A C   
288  O O   . PHE A 58  ? 0.3679 0.3142 0.4302 -0.1243 -0.0975 0.0590  112 PHE A O   
289  C CB  . PHE A 58  ? 0.3360 0.3190 0.4330 -0.0936 -0.1267 0.0523  112 PHE A CB  
290  C CG  . PHE A 58  ? 0.3185 0.3204 0.4062 -0.0985 -0.1427 0.0685  112 PHE A CG  
291  C CD1 . PHE A 58  ? 0.3498 0.3066 0.4102 -0.1065 -0.1523 0.0698  112 PHE A CD1 
292  C CD2 . PHE A 58  ? 0.2919 0.3053 0.4074 -0.1444 -0.0935 0.0730  112 PHE A CD2 
293  C CE1 . PHE A 58  ? 0.3197 0.3264 0.4008 -0.1252 -0.1430 0.0436  112 PHE A CE1 
294  C CE2 . PHE A 58  ? 0.3123 0.3114 0.4090 -0.1361 -0.0732 0.0931  112 PHE A CE2 
295  C CZ  . PHE A 58  ? 0.3133 0.3190 0.3978 -0.1098 -0.1012 0.0767  112 PHE A CZ  
296  N N   . GLY A 59  ? 0.3151 0.3472 0.4798 -0.1166 -0.1506 0.0519  113 GLY A N   
297  C CA  . GLY A 59  ? 0.3486 0.3625 0.5059 -0.1279 -0.1642 0.0481  113 GLY A CA  
298  C C   . GLY A 59  ? 0.3890 0.3751 0.5253 -0.1349 -0.1451 0.0523  113 GLY A C   
299  O O   . GLY A 59  ? 0.3676 0.3902 0.5362 -0.1277 -0.1374 0.0409  113 GLY A O   
300  N N   . ARG A 60  ? 0.3973 0.3496 0.5433 -0.1561 -0.1504 0.0546  114 ARG A N   
301  C CA  . ARG A 60  ? 0.4510 0.3539 0.5763 -0.1912 -0.1233 0.0806  114 ARG A CA  
302  C C   . ARG A 60  ? 0.4630 0.3389 0.5362 -0.1717 -0.1123 0.0714  114 ARG A C   
303  O O   . ARG A 60  ? 0.5421 0.3741 0.5419 -0.1209 -0.0943 0.0778  114 ARG A O   
304  C CB  . ARG A 60  ? 0.4917 0.3974 0.6561 -0.2079 -0.0991 0.0913  114 ARG A CB  
305  C CG  . ARG A 60  ? 0.5596 0.4371 0.7239 -0.2514 -0.0951 0.0783  114 ARG A CG  
306  C CD  . ARG A 60  ? 0.6477 0.5000 0.7679 -0.2402 -0.0828 0.0672  114 ARG A CD  
307  N NE  . ARG A 60  ? 0.7602 0.5807 0.8520 -0.1921 -0.0781 0.0553  114 ARG A NE  
308  C CZ  . ARG A 60  ? 0.8298 0.6667 0.9109 -0.1661 -0.0901 0.0387  114 ARG A CZ  
309  N NH1 . ARG A 60  ? 0.8684 0.7044 0.9250 -0.1602 -0.0894 0.0294  114 ARG A NH1 
310  N NH2 . ARG A 60  ? 0.8548 0.6985 0.9335 -0.1589 -0.1013 0.0319  114 ARG A NH2 
311  N N   . LYS A 61  ? 0.3526 0.3298 0.4961 -0.1618 -0.1322 0.0778  115 LYS A N   
312  C CA  . LYS A 61  ? 0.3100 0.3327 0.4792 -0.1254 -0.1482 0.0826  115 LYS A CA  
313  C C   . LYS A 61  ? 0.2904 0.2839 0.4303 -0.1318 -0.1405 0.0724  115 LYS A C   
314  O O   . LYS A 61  ? 0.3248 0.2868 0.4235 -0.0939 -0.1321 0.0768  115 LYS A O   
315  C CB  . LYS A 61  ? 0.2584 0.3588 0.5064 -0.0930 -0.1607 0.1051  115 LYS A CB  
316  C CG  . LYS A 61  ? 0.2671 0.4224 0.5264 -0.1037 -0.1509 0.1020  115 LYS A CG  
317  C CD  . LYS A 61  ? 0.3338 0.4904 0.5452 -0.0382 -0.1250 0.1053  115 LYS A CD  
318  C CE  . LYS A 61  ? 0.3768 0.5104 0.5698 -0.0452 -0.0968 0.1193  115 LYS A CE  
319  N NZ  . LYS A 61  ? 0.4531 0.5355 0.5883 -0.0885 -0.0786 0.1004  115 LYS A NZ  
320  N N   . SER A 62  ? 0.3017 0.2557 0.3945 -0.1014 -0.1265 0.0560  116 SER A N   
321  C CA  . SER A 62  ? 0.2657 0.2571 0.3768 -0.1165 -0.0717 0.0567  116 SER A CA  
322  C C   . SER A 62  ? 0.2032 0.2348 0.3506 -0.0845 -0.0845 0.0630  116 SER A C   
323  O O   . SER A 62  ? 0.2390 0.2442 0.3575 -0.0643 -0.0989 0.0399  116 SER A O   
324  C CB  . SER A 62  ? 0.2649 0.2469 0.3882 -0.0868 -0.0601 0.0688  116 SER A CB  
325  O OG  . SER A 62  ? 0.2444 0.2498 0.3861 -0.0433 -0.0582 0.0883  116 SER A OG  
326  N N   . LEU A 63  ? 0.2054 0.2276 0.3167 -0.0636 -0.0636 0.0445  117 LEU A N   
327  C CA  . LEU A 63  ? 0.1998 0.1921 0.3245 -0.0352 -0.0302 0.0304  117 LEU A CA  
328  C C   . LEU A 63  ? 0.1999 0.2149 0.3021 -0.0525 -0.0259 0.0143  117 LEU A C   
329  O O   . LEU A 63  ? 0.2371 0.2250 0.2897 -0.0443 -0.0366 0.0501  117 LEU A O   
330  C CB  . LEU A 63  ? 0.2255 0.2004 0.3229 -0.0242 -0.0216 0.0191  117 LEU A CB  
331  C CG  . LEU A 63  ? 0.2270 0.2198 0.2990 -0.0044 -0.0769 0.0277  117 LEU A CG  
332  C CD1 . LEU A 63  ? 0.2690 0.2582 0.2853 -0.0118 -0.0467 0.0254  117 LEU A CD1 
333  C CD2 . LEU A 63  ? 0.2477 0.2393 0.3037 0.0209  -0.0574 -0.0034 117 LEU A CD2 
334  N N   . HIS A 64  ? 0.2072 0.2167 0.3117 -0.0375 -0.0265 0.0240  118 HIS A N   
335  C CA  . HIS A 64  ? 0.1646 0.2512 0.2980 -0.0112 -0.0591 0.0495  118 HIS A CA  
336  C C   . HIS A 64  ? 0.1761 0.2516 0.3178 -0.0552 -0.0492 0.0715  118 HIS A C   
337  O O   . HIS A 64  ? 0.2177 0.2826 0.3251 -0.0034 -0.0300 0.0545  118 HIS A O   
338  C CB  . HIS A 64  ? 0.1564 0.2243 0.2940 -0.0158 -0.0514 0.0491  118 HIS A CB  
339  C CG  . HIS A 64  ? 0.1717 0.1858 0.2905 -0.0094 -0.0465 0.0255  118 HIS A CG  
340  N ND1 . HIS A 64  ? 0.1781 0.1843 0.2687 0.0025  -0.0608 0.0060  118 HIS A ND1 
341  C CD2 . HIS A 64  ? 0.2214 0.1979 0.2599 -0.0145 -0.0621 0.0200  118 HIS A CD2 
342  C CE1 . HIS A 64  ? 0.1731 0.2012 0.2585 0.0167  -0.0796 0.0082  118 HIS A CE1 
343  N NE2 . HIS A 64  ? 0.2357 0.1704 0.2745 -0.0260 -0.0610 0.0190  118 HIS A NE2 
344  N N   . PHE A 65  ? 0.1898 0.2680 0.3404 -0.0631 -0.0238 0.0661  119 PHE A N   
345  C CA  . PHE A 65  ? 0.1661 0.3043 0.3785 -0.0541 -0.0096 0.0697  119 PHE A CA  
346  C C   . PHE A 65  ? 0.1966 0.3083 0.3549 -0.0271 0.0027  0.1052  119 PHE A C   
347  O O   . PHE A 65  ? 0.1933 0.3014 0.3474 -0.0318 -0.0103 0.0893  119 PHE A O   
348  C CB  . PHE A 65  ? 0.1814 0.3361 0.4393 -0.0899 -0.0311 0.0750  119 PHE A CB  
349  C CG  . PHE A 65  ? 0.2021 0.4038 0.4901 -0.0963 -0.0084 0.1036  119 PHE A CG  
350  C CD1 . PHE A 65  ? 0.2420 0.4461 0.4960 -0.0888 0.0265  0.1261  119 PHE A CD1 
351  C CD2 . PHE A 65  ? 0.1789 0.4315 0.5080 -0.0869 -0.0248 0.1032  119 PHE A CD2 
352  C CE1 . PHE A 65  ? 0.2661 0.4828 0.5140 -0.0998 0.0166  0.1065  119 PHE A CE1 
353  C CE2 . PHE A 65  ? 0.2191 0.4407 0.5173 -0.0864 0.0051  0.1147  119 PHE A CE2 
354  C CZ  . PHE A 65  ? 0.2323 0.4715 0.5121 -0.0995 0.0155  0.1228  119 PHE A CZ  
355  N N   . ILE A 66  ? 0.1906 0.3258 0.3861 0.0225  0.0145  0.0998  120 ILE A N   
356  C CA  . ILE A 66  ? 0.1848 0.3576 0.3902 0.0082  0.0052  0.0934  120 ILE A CA  
357  C C   . ILE A 66  ? 0.2035 0.3882 0.4089 -0.0100 -0.0068 0.1348  120 ILE A C   
358  O O   . ILE A 66  ? 0.2145 0.4087 0.4266 -0.0127 0.0205  0.1018  120 ILE A O   
359  C CB  . ILE A 66  ? 0.2219 0.3748 0.4030 0.0446  -0.0182 0.0573  120 ILE A CB  
360  C CG1 . ILE A 66  ? 0.2290 0.3733 0.4177 0.0204  0.0082  0.0548  120 ILE A CG1 
361  C CG2 . ILE A 66  ? 0.2477 0.3751 0.4013 0.0180  0.0040  0.0279  120 ILE A CG2 
362  C CD1 . ILE A 66  ? 0.2256 0.3858 0.4197 -0.0016 0.0114  0.0550  120 ILE A CD1 
363  N N   . GLY A 67  ? 0.1844 0.4186 0.4230 -0.0167 -0.0719 0.1651  121 GLY A N   
364  C CA  . GLY A 67  ? 0.1816 0.4161 0.4389 -0.0240 -0.0763 0.1759  121 GLY A CA  
365  C C   . GLY A 67  ? 0.1797 0.4037 0.4584 -0.0269 -0.0746 0.1508  121 GLY A C   
366  O O   . GLY A 67  ? 0.2484 0.4055 0.4811 -0.0534 -0.0687 0.1188  121 GLY A O   
367  N N   . THR A 68  ? 0.1761 0.4186 0.4570 -0.0350 -0.0800 0.1456  122 THR A N   
368  C CA  . THR A 68  ? 0.1816 0.4123 0.4696 -0.0164 -0.0516 0.1161  122 THR A CA  
369  C C   . THR A 68  ? 0.1750 0.3595 0.4549 -0.0193 -0.0329 0.1001  122 THR A C   
370  O O   . THR A 68  ? 0.2767 0.3549 0.4445 0.0361  -0.0245 0.1201  122 THR A O   
371  C CB  . THR A 68  ? 0.1947 0.4619 0.4865 -0.0248 -0.0362 0.1157  122 THR A CB  
372  O OG1 . THR A 68  ? 0.2635 0.4802 0.4958 -0.0418 -0.0492 0.1128  122 THR A OG1 
373  C CG2 . THR A 68  ? 0.2218 0.4981 0.4881 -0.0253 0.0045  0.1243  122 THR A CG2 
374  N N   . THR A 69  ? 0.1678 0.3716 0.4438 0.0033  -0.0189 0.0627  123 THR A N   
375  C CA  . THR A 69  ? 0.1816 0.3953 0.4526 0.0106  -0.0451 0.0360  123 THR A CA  
376  C C   . THR A 69  ? 0.1881 0.3414 0.4164 0.0250  -0.0345 0.0567  123 THR A C   
377  O O   . THR A 69  ? 0.2247 0.3290 0.3987 0.0156  -0.0247 0.0596  123 THR A O   
378  C CB  . THR A 69  ? 0.2493 0.4472 0.4929 0.0012  -0.0525 -0.0005 123 THR A CB  
379  O OG1 . THR A 69  ? 0.2639 0.4689 0.5300 -0.0297 -0.0635 -0.0199 123 THR A OG1 
380  C CG2 . THR A 69  ? 0.2772 0.4620 0.4887 -0.0112 -0.0493 -0.0131 123 THR A CG2 
381  N N   . PRO A 70  ? 0.2326 0.3170 0.4020 -0.0038 -0.0564 0.0685  124 PRO A N   
382  C CA  . PRO A 70  ? 0.2004 0.2765 0.3875 0.0073  -0.0560 0.0631  124 PRO A CA  
383  C C   . PRO A 70  ? 0.1755 0.2771 0.3438 0.0184  -0.0597 0.0632  124 PRO A C   
384  O O   . PRO A 70  ? 0.2150 0.3112 0.3446 -0.0195 -0.0464 0.0460  124 PRO A O   
385  C CB  . PRO A 70  ? 0.2176 0.2933 0.3896 0.0290  -0.0703 0.0778  124 PRO A CB  
386  C CG  . PRO A 70  ? 0.2663 0.3488 0.4089 -0.0064 -0.0691 0.0798  124 PRO A CG  
387  C CD  . PRO A 70  ? 0.2639 0.3302 0.4212 0.0044  -0.0579 0.0929  124 PRO A CD  
388  N N   . ASN A 71  ? 0.1587 0.2401 0.2988 -0.0025 -0.0415 0.0720  125 ASN A N   
389  C CA  . ASN A 71  ? 0.1809 0.2199 0.2740 0.0105  -0.0304 0.0590  125 ASN A CA  
390  C C   . ASN A 71  ? 0.1998 0.1807 0.2604 -0.0222 -0.0285 0.0299  125 ASN A C   
391  O O   . ASN A 71  ? 0.1935 0.2163 0.2593 -0.0226 -0.0238 0.0245  125 ASN A O   
392  C CB  . ASN A 71  ? 0.1664 0.2372 0.2693 -0.0090 -0.0211 0.0546  125 ASN A CB  
393  C CG  . ASN A 71  ? 0.1772 0.2317 0.2495 -0.0137 -0.0147 0.0478  125 ASN A CG  
394  O OD1 . ASN A 71  ? 0.1698 0.2140 0.2600 -0.0375 -0.0105 0.0501  125 ASN A OD1 
395  N ND2 . ASN A 71  ? 0.2092 0.2273 0.2409 -0.0029 -0.0126 0.0478  125 ASN A ND2 
396  N N   . PRO A 72  ? 0.1957 0.1764 0.2460 -0.0023 -0.0174 0.0224  126 PRO A N   
397  C CA  . PRO A 72  ? 0.2257 0.1848 0.2249 -0.0376 -0.0152 0.0077  126 PRO A CA  
398  C C   . PRO A 72  ? 0.1938 0.1943 0.2164 -0.0279 -0.0312 0.0286  126 PRO A C   
399  O O   . PRO A 72  ? 0.1989 0.1976 0.2124 -0.0117 -0.0215 0.0224  126 PRO A O   
400  C CB  . PRO A 72  ? 0.2694 0.1642 0.2576 -0.0389 -0.0258 -0.0083 126 PRO A CB  
401  C CG  . PRO A 72  ? 0.2593 0.1999 0.2530 -0.0170 -0.0189 0.0159  126 PRO A CG  
402  C CD  . PRO A 72  ? 0.2630 0.1818 0.2641 0.0162  -0.0267 0.0252  126 PRO A CD  
403  N N   . TYR A 73  ? 0.1690 0.2025 0.2185 -0.0094 -0.0316 0.0153  127 TYR A N   
404  C CA  . TYR A 73  ? 0.2009 0.2044 0.2023 -0.0102 -0.0413 0.0274  127 TYR A CA  
405  C C   . TYR A 73  ? 0.2001 0.2177 0.2039 0.0097  -0.0125 0.0290  127 TYR A C   
406  O O   . TYR A 73  ? 0.1829 0.2147 0.2096 -0.0163 -0.0160 0.0331  127 TYR A O   
407  C CB  . TYR A 73  ? 0.2182 0.1964 0.2066 -0.0019 -0.0458 0.0477  127 TYR A CB  
408  C CG  . TYR A 73  ? 0.2121 0.1627 0.2078 -0.0233 -0.0422 0.0446  127 TYR A CG  
409  C CD1 . TYR A 73  ? 0.1851 0.1929 0.2139 -0.0034 -0.0274 0.0229  127 TYR A CD1 
410  C CD2 . TYR A 73  ? 0.2124 0.1859 0.2212 -0.0262 -0.0347 0.0362  127 TYR A CD2 
411  C CE1 . TYR A 73  ? 0.2361 0.1658 0.2039 0.0112  -0.0173 0.0243  127 TYR A CE1 
412  C CE2 . TYR A 73  ? 0.2262 0.1760 0.2342 -0.0259 -0.0476 0.0255  127 TYR A CE2 
413  C CZ  . TYR A 73  ? 0.2289 0.1583 0.2119 -0.0093 -0.0442 0.0247  127 TYR A CZ  
414  O OH  . TYR A 73  ? 0.2624 0.1948 0.2113 0.0206  -0.0232 0.0263  127 TYR A OH  
415  N N   . GLN A 74  ? 0.2053 0.1941 0.2115 -0.0015 -0.0058 0.0301  128 GLN A N   
416  C CA  . GLN A 74  ? 0.1784 0.2132 0.2177 0.0020  -0.0028 0.0275  128 GLN A CA  
417  C C   . GLN A 74  ? 0.1526 0.2143 0.2187 -0.0263 -0.0065 0.0065  128 GLN A C   
418  O O   . GLN A 74  ? 0.2263 0.1848 0.2506 -0.0223 0.0060  0.0261  128 GLN A O   
419  C CB  . GLN A 74  ? 0.1844 0.2199 0.1995 -0.0003 0.0062  0.0529  128 GLN A CB  
420  C CG  . GLN A 74  ? 0.1919 0.2517 0.2455 -0.0113 -0.0100 0.0316  128 GLN A CG  
421  C CD  . GLN A 74  ? 0.1659 0.2576 0.2765 -0.0152 -0.0057 0.0141  128 GLN A CD  
422  O OE1 . GLN A 74  ? 0.1837 0.2675 0.2995 -0.0005 -0.0188 0.0285  128 GLN A OE1 
423  N NE2 . GLN A 74  ? 0.2034 0.2712 0.3036 -0.0008 0.0083  -0.0192 128 GLN A NE2 
424  N N   . GLN A 75  ? 0.1766 0.2485 0.2109 -0.0097 -0.0138 0.0123  129 GLN A N   
425  C CA  . GLN A 75  ? 0.1994 0.2211 0.2269 -0.0252 -0.0330 0.0111  129 GLN A CA  
426  C C   . GLN A 75  ? 0.2034 0.1652 0.2175 0.0110  -0.0407 0.0486  129 GLN A C   
427  O O   . GLN A 75  ? 0.2355 0.1856 0.2351 0.0130  -0.0375 0.0292  129 GLN A O   
428  C CB  . GLN A 75  ? 0.2412 0.2616 0.2372 -0.0310 -0.0498 0.0398  129 GLN A CB  
429  C CG  . GLN A 75  ? 0.2728 0.3157 0.2794 -0.0321 -0.0505 0.0225  129 GLN A CG  
430  C CD  . GLN A 75  ? 0.3088 0.4015 0.3336 -0.1085 -0.0719 0.0050  129 GLN A CD  
431  O OE1 . GLN A 75  ? 0.3323 0.4422 0.3343 -0.0946 -0.0569 -0.0095 129 GLN A OE1 
432  N NE2 . GLN A 75  ? 0.3787 0.4385 0.3680 -0.0894 -0.0877 -0.0154 129 GLN A NE2 
433  N N   . ALA A 76  ? 0.1927 0.1979 0.2245 0.0079  -0.0191 0.0410  130 ALA A N   
434  C CA  . ALA A 76  ? 0.1851 0.2025 0.2264 0.0023  -0.0107 0.0500  130 ALA A CA  
435  C C   . ALA A 76  ? 0.1900 0.1966 0.2190 -0.0059 -0.0240 0.0470  130 ALA A C   
436  O O   . ALA A 76  ? 0.2111 0.2007 0.2417 0.0091  -0.0106 0.0617  130 ALA A O   
437  C CB  . ALA A 76  ? 0.2166 0.2269 0.2667 0.0546  -0.0107 0.0545  130 ALA A CB  
438  N N   . ILE A 77  ? 0.2063 0.2193 0.2008 0.0163  -0.0266 0.0245  131 ILE A N   
439  C CA  . ILE A 77  ? 0.2257 0.2136 0.1979 -0.0076 -0.0292 0.0199  131 ILE A CA  
440  C C   . ILE A 77  ? 0.1894 0.2145 0.2145 -0.0053 -0.0297 0.0284  131 ILE A C   
441  O O   . ILE A 77  ? 0.2270 0.2117 0.2096 -0.0346 -0.0102 0.0203  131 ILE A O   
442  C CB  . ILE A 77  ? 0.2611 0.2189 0.1815 -0.0104 -0.0390 0.0221  131 ILE A CB  
443  C CG1 . ILE A 77  ? 0.2605 0.2692 0.1985 -0.0115 -0.0425 0.0492  131 ILE A CG1 
444  C CG2 . ILE A 77  ? 0.3005 0.2327 0.1757 -0.0296 -0.0499 -0.0019 131 ILE A CG2 
445  C CD1 . ILE A 77  ? 0.3352 0.2581 0.2154 -0.0121 -0.0501 0.0447  131 ILE A CD1 
446  N N   . SER A 78  ? 0.1704 0.2096 0.2265 0.0113  -0.0253 0.0259  132 SER A N   
447  C CA  . SER A 78  ? 0.1852 0.2051 0.2202 0.0078  -0.0287 0.0405  132 SER A CA  
448  C C   . SER A 78  ? 0.2277 0.2178 0.2006 0.0247  -0.0208 0.0282  132 SER A C   
449  O O   . SER A 78  ? 0.2474 0.2031 0.2109 0.0037  -0.0166 0.0281  132 SER A O   
450  C CB  . SER A 78  ? 0.1857 0.2937 0.2468 -0.0172 0.0434  0.0775  132 SER A CB  
451  O OG  . SER A 78  ? 0.3521 0.3573 0.3166 -0.0077 -0.0171 0.0490  132 SER A OG  
452  N N   . ILE A 79  ? 0.1848 0.2281 0.1836 0.0162  -0.0295 0.0129  133 ILE A N   
453  C CA  . ILE A 79  ? 0.2097 0.2029 0.1853 0.0022  -0.0352 0.0028  133 ILE A CA  
454  C C   . ILE A 79  ? 0.1811 0.1751 0.1984 -0.0081 -0.0229 0.0152  133 ILE A C   
455  O O   . ILE A 79  ? 0.2141 0.1750 0.2018 -0.0008 -0.0103 0.0152  133 ILE A O   
456  C CB  . ILE A 79  ? 0.2166 0.2080 0.1726 -0.0192 -0.0378 -0.0192 133 ILE A CB  
457  C CG1 . ILE A 79  ? 0.2195 0.2193 0.2168 -0.0339 -0.0322 -0.0173 133 ILE A CG1 
458  C CG2 . ILE A 79  ? 0.2623 0.2259 0.1627 -0.0104 -0.0447 0.0030  133 ILE A CG2 
459  C CD1 . ILE A 79  ? 0.2439 0.2392 0.2388 -0.0387 -0.0600 0.0036  133 ILE A CD1 
460  N N   . ILE A 80  ? 0.1827 0.1961 0.1996 -0.0017 -0.0375 0.0032  134 ILE A N   
461  C CA  . ILE A 80  ? 0.1943 0.1896 0.2119 -0.0106 -0.0425 0.0074  134 ILE A CA  
462  C C   . ILE A 80  ? 0.1996 0.1991 0.1888 -0.0334 -0.0134 0.0060  134 ILE A C   
463  O O   . ILE A 80  ? 0.2152 0.1821 0.2112 -0.0070 -0.0025 0.0185  134 ILE A O   
464  C CB  . ILE A 80  ? 0.1790 0.1926 0.2182 0.0118  -0.0394 0.0129  134 ILE A CB  
465  C CG1 . ILE A 80  ? 0.2235 0.2135 0.2284 0.0076  -0.0094 0.0036  134 ILE A CG1 
466  C CG2 . ILE A 80  ? 0.1838 0.2172 0.2478 -0.0251 -0.0191 0.0099  134 ILE A CG2 
467  C CD1 . ILE A 80  ? 0.2749 0.2338 0.2307 -0.0274 0.0235  -0.0147 134 ILE A CD1 
468  N N   . GLY A 81  ? 0.1995 0.1947 0.1910 0.0166  -0.0062 0.0000  135 GLY A N   
469  C CA  . GLY A 81  ? 0.2209 0.2153 0.1844 0.0216  -0.0199 0.0154  135 GLY A CA  
470  C C   . GLY A 81  ? 0.2221 0.1869 0.2117 -0.0108 -0.0257 0.0085  135 GLY A C   
471  O O   . GLY A 81  ? 0.2625 0.2093 0.2232 -0.0056 -0.0132 0.0199  135 GLY A O   
472  N N   . LYS A 82  ? 0.1970 0.1909 0.2073 0.0127  -0.0147 0.0201  136 LYS A N   
473  C CA  . LYS A 82  ? 0.2177 0.2100 0.2058 0.0346  0.0073  0.0209  136 LYS A CA  
474  C C   . LYS A 82  ? 0.2441 0.1987 0.1980 0.0250  0.0254  0.0011  136 LYS A C   
475  O O   . LYS A 82  ? 0.2653 0.2063 0.2196 0.0070  0.0170  0.0164  136 LYS A O   
476  C CB  . LYS A 82  ? 0.2469 0.2370 0.2372 -0.0300 -0.0143 0.0419  136 LYS A CB  
477  C CG  . LYS A 82  ? 0.3171 0.2827 0.2914 -0.0246 -0.0441 0.0580  136 LYS A CG  
478  C CD  . LYS A 82  ? 0.4499 0.3577 0.3516 -0.0111 -0.0448 0.0541  136 LYS A CD  
479  C CE  . LYS A 82  ? 0.4911 0.4347 0.3953 0.0217  -0.0631 0.0352  136 LYS A CE  
480  N NZ  . LYS A 82  ? 0.5260 0.4583 0.4407 -0.0097 -0.0569 0.0300  136 LYS A NZ  
481  N N   . THR A 83  ? 0.2265 0.2052 0.1691 0.0003  -0.0115 0.0132  137 THR A N   
482  C CA  . THR A 83  ? 0.2051 0.2057 0.1733 0.0004  -0.0338 0.0054  137 THR A CA  
483  C C   . THR A 83  ? 0.2424 0.2129 0.1853 0.0263  -0.0325 0.0089  137 THR A C   
484  O O   . THR A 83  ? 0.2582 0.2121 0.1755 0.0275  -0.0146 0.0190  137 THR A O   
485  C CB  . THR A 83  ? 0.2275 0.1822 0.1924 0.0026  -0.0063 0.0066  137 THR A CB  
486  O OG1 . THR A 83  ? 0.2501 0.2198 0.2092 -0.0139 -0.0002 -0.0041 137 THR A OG1 
487  C CG2 . THR A 83  ? 0.2542 0.2351 0.1669 0.0167  0.0241  0.0434  137 THR A CG2 
488  N N   . LEU A 84  ? 0.2029 0.2123 0.1875 -0.0052 -0.0014 0.0054  138 LEU A N   
489  C CA  . LEU A 84  ? 0.1922 0.2105 0.1913 0.0124  -0.0059 0.0038  138 LEU A CA  
490  C C   . LEU A 84  ? 0.2018 0.2086 0.1892 -0.0147 0.0183  0.0267  138 LEU A C   
491  O O   . LEU A 84  ? 0.2510 0.2000 0.2245 -0.0453 0.0169  0.0019  138 LEU A O   
492  C CB  . LEU A 84  ? 0.2082 0.2074 0.1942 0.0209  -0.0201 0.0007  138 LEU A CB  
493  C CG  . LEU A 84  ? 0.2515 0.1832 0.2058 0.0132  -0.0001 0.0078  138 LEU A CG  
494  C CD1 . LEU A 84  ? 0.2322 0.2188 0.2179 0.0133  -0.0388 0.0104  138 LEU A CD1 
495  C CD2 . LEU A 84  ? 0.2400 0.2115 0.2192 0.0000  0.0566  0.0292  138 LEU A CD2 
496  N N   . SER A 85  ? 0.2329 0.1918 0.1902 0.0000  -0.0080 -0.0042 139 SER A N   
497  C CA  . SER A 85  ? 0.2723 0.2190 0.2168 0.0065  0.0269  -0.0002 139 SER A CA  
498  C C   . SER A 85  ? 0.2871 0.2358 0.2333 0.0108  0.0104  -0.0011 139 SER A C   
499  O O   . SER A 85  ? 0.2920 0.2490 0.2486 -0.0297 -0.0054 -0.0100 139 SER A O   
500  C CB  . SER A 85  ? 0.2836 0.2685 0.2535 0.0156  0.0422  0.0318  139 SER A CB  
501  O OG  . SER A 85  ? 0.3567 0.3445 0.2993 0.0134  0.0181  0.0116  139 SER A OG  
502  N N   . VAL A 86  ? 0.2927 0.2148 0.2404 0.0499  0.0166  0.0352  140 VAL A N   
503  C CA  . VAL A 86  ? 0.3038 0.1946 0.2474 0.0333  0.0157  0.0326  140 VAL A CA  
504  C C   . VAL A 86  ? 0.2943 0.2006 0.2411 0.0117  0.0070  0.0119  140 VAL A C   
505  O O   . VAL A 86  ? 0.3568 0.2050 0.2874 -0.0081 -0.0065 0.0147  140 VAL A O   
506  C CB  . VAL A 86  ? 0.2729 0.2428 0.2778 0.0366  -0.0052 0.0166  140 VAL A CB  
507  C CG1 . VAL A 86  ? 0.3031 0.3028 0.3121 0.0204  -0.0057 0.0318  140 VAL A CG1 
508  C CG2 . VAL A 86  ? 0.3360 0.2521 0.2428 -0.0054 -0.0357 -0.0078 140 VAL A CG2 
509  N N   . PHE A 87  ? 0.2650 0.2211 0.2200 0.0102  -0.0021 0.0078  141 PHE A N   
510  C CA  . PHE A 87  ? 0.2635 0.2337 0.2238 0.0049  0.0067  -0.0121 141 PHE A CA  
511  C C   . PHE A 87  ? 0.3094 0.2487 0.2351 -0.0048 0.0032  0.0105  141 PHE A C   
512  O O   . PHE A 87  ? 0.2944 0.2480 0.2506 -0.0128 0.0175  0.0234  141 PHE A O   
513  C CB  . PHE A 87  ? 0.2711 0.2348 0.2405 -0.0045 0.0382  -0.0088 141 PHE A CB  
514  C CG  . PHE A 87  ? 0.2525 0.2497 0.2328 -0.0237 0.0260  0.0114  141 PHE A CG  
515  C CD1 . PHE A 87  ? 0.2962 0.2552 0.2466 -0.0270 0.0290  0.0246  141 PHE A CD1 
516  C CD2 . PHE A 87  ? 0.2774 0.2372 0.2453 0.0212  0.0493  0.0017  141 PHE A CD2 
517  C CE1 . PHE A 87  ? 0.3138 0.2690 0.2476 -0.0306 0.0186  0.0131  141 PHE A CE1 
518  C CE2 . PHE A 87  ? 0.2710 0.2069 0.2522 -0.0034 0.0329  0.0508  141 PHE A CE2 
519  C CZ  . PHE A 87  ? 0.2995 0.2244 0.2763 0.0055  0.0196  0.0191  141 PHE A CZ  
520  N N   . ASP A 88  ? 0.3506 0.2619 0.2275 0.0163  0.0066  0.0087  142 ASP A N   
521  C CA  . ASP A 88  ? 0.3340 0.2623 0.2624 -0.0153 0.0300  -0.0367 142 ASP A CA  
522  C C   . ASP A 88  ? 0.3766 0.2681 0.3015 -0.0109 0.0492  -0.0438 142 ASP A C   
523  O O   . ASP A 88  ? 0.3785 0.3093 0.3241 0.0047  0.0559  -0.0567 142 ASP A O   
524  C CB  . ASP A 88  ? 0.3897 0.2837 0.2322 -0.0580 0.0277  -0.0316 142 ASP A CB  
525  C CG  . ASP A 88  ? 0.4664 0.3372 0.2645 -0.0831 0.0185  -0.0551 142 ASP A CG  
526  O OD1 . ASP A 88  ? 0.4684 0.3321 0.2730 -0.0594 0.0252  -0.0849 142 ASP A OD1 
527  O OD2 . ASP A 88  ? 0.5269 0.3785 0.2814 -0.1408 0.0088  -0.0591 142 ASP A OD2 
528  N N   . GLU A 89  ? 0.4932 0.2431 0.3071 -0.0134 0.0510  -0.0391 143 GLU A N   
529  C CA  . GLU A 89  ? 0.5560 0.2620 0.3578 -0.0198 0.0473  -0.0337 143 GLU A CA  
530  C C   . GLU A 89  ? 0.4934 0.2065 0.3183 0.0046  0.0157  -0.0365 143 GLU A C   
531  O O   . GLU A 89  ? 0.5356 0.2296 0.2936 -0.0383 -0.0109 -0.0309 143 GLU A O   
532  C CB  . GLU A 89  ? 0.6710 0.3842 0.5084 -0.0727 0.0363  -0.0442 143 GLU A CB  
533  C CG  . GLU A 89  ? 0.8002 0.5525 0.6714 -0.0707 0.0209  -0.0359 143 GLU A CG  
534  C CD  . GLU A 89  ? 0.8954 0.7054 0.7941 -0.0647 0.0127  -0.0186 143 GLU A CD  
535  O OE1 . GLU A 89  ? 0.9481 0.7399 0.8362 -0.0756 0.0048  -0.0206 143 GLU A OE1 
536  O OE2 . GLU A 89  ? 0.9555 0.7559 0.8682 -0.0399 0.0085  -0.0122 143 GLU A OE2 
537  N N   . ASP A 90  ? 0.4114 0.1843 0.3104 -0.0383 0.0256  -0.0401 144 ASP A N   
538  C CA  . ASP A 90  ? 0.3484 0.2035 0.2894 -0.0101 0.0243  -0.0478 144 ASP A CA  
539  C C   . ASP A 90  ? 0.2894 0.1713 0.2669 -0.0154 -0.0155 -0.0339 144 ASP A C   
540  O O   . ASP A 90  ? 0.2861 0.1775 0.2698 0.0065  0.0099  -0.0294 144 ASP A O   
541  C CB  . ASP A 90  ? 0.3067 0.2387 0.3067 0.0173  0.0248  -0.0602 144 ASP A CB  
542  C CG  . ASP A 90  ? 0.2955 0.2779 0.3243 0.0336  0.0004  -0.0907 144 ASP A CG  
543  O OD1 . ASP A 90  ? 0.2756 0.2756 0.3151 -0.0231 0.0369  -0.0702 144 ASP A OD1 
544  O OD2 . ASP A 90  ? 0.3343 0.3235 0.3732 0.0411  -0.0327 -0.1175 144 ASP A OD2 
545  N N   . ASN A 91  ? 0.2889 0.1749 0.2419 -0.0397 -0.0052 -0.0319 145 ASN A N   
546  C CA  . ASN A 91  ? 0.2658 0.1962 0.2494 -0.0152 0.0245  -0.0090 145 ASN A CA  
547  C C   . ASN A 91  ? 0.2718 0.2109 0.2437 -0.0274 0.0294  -0.0054 145 ASN A C   
548  O O   . ASN A 91  ? 0.2685 0.2635 0.2762 -0.0347 0.0104  0.0455  145 ASN A O   
549  C CB  . ASN A 91  ? 0.2894 0.2401 0.2808 -0.0404 0.0114  -0.0177 145 ASN A CB  
550  C CG  . ASN A 91  ? 0.3120 0.2931 0.3007 -0.0155 -0.0030 -0.0236 145 ASN A CG  
551  O OD1 . ASN A 91  ? 0.3649 0.3687 0.3047 0.0041  -0.0396 -0.0321 145 ASN A OD1 
552  N ND2 . ASN A 91  ? 0.2768 0.2980 0.3474 0.0067  -0.0197 -0.0003 145 ASN A ND2 
553  N N   . LEU A 92  ? 0.2586 0.1870 0.2296 -0.0058 0.0127  -0.0081 146 LEU A N   
554  C CA  . LEU A 92  ? 0.2893 0.1942 0.2633 0.0007  0.0213  -0.0043 146 LEU A CA  
555  C C   . LEU A 92  ? 0.2330 0.1709 0.2667 0.0005  0.0473  -0.0177 146 LEU A C   
556  O O   . LEU A 92  ? 0.2581 0.1841 0.3124 -0.0036 0.0722  -0.0154 146 LEU A O   
557  C CB  . LEU A 92  ? 0.3038 0.1850 0.2722 -0.0120 -0.0504 -0.0307 146 LEU A CB  
558  C CG  . LEU A 92  ? 0.3750 0.2028 0.2886 -0.0195 -0.0591 -0.0349 146 LEU A CG  
559  C CD1 . LEU A 92  ? 0.4135 0.2223 0.2968 -0.0217 -0.0906 -0.0148 146 LEU A CD1 
560  C CD2 . LEU A 92  ? 0.4444 0.2181 0.2685 0.0439  -0.0229 -0.0486 146 LEU A CD2 
561  N N   . ILE A 93  ? 0.2344 0.1362 0.2106 0.0096  -0.0098 -0.0013 147 ILE A N   
562  C CA  . ILE A 93  ? 0.2198 0.1595 0.2244 -0.0031 -0.0144 0.0171  147 ILE A CA  
563  C C   . ILE A 93  ? 0.2165 0.1652 0.2143 -0.0127 0.0212  0.0083  147 ILE A C   
564  O O   . ILE A 93  ? 0.2003 0.1968 0.2125 0.0013  0.0108  0.0086  147 ILE A O   
565  C CB  . ILE A 93  ? 0.2331 0.1831 0.2246 0.0297  -0.0098 -0.0099 147 ILE A CB  
566  C CG1 . ILE A 93  ? 0.2833 0.2268 0.2366 -0.0002 -0.0426 -0.0401 147 ILE A CG1 
567  C CG2 . ILE A 93  ? 0.2490 0.1599 0.2466 0.0380  0.0247  -0.0212 147 ILE A CG2 
568  C CD1 . ILE A 93  ? 0.3074 0.2879 0.2365 -0.0055 -0.0131 -0.0302 147 ILE A CD1 
569  N N   . PRO A 94  ? 0.2365 0.1752 0.1990 -0.0035 0.0236  0.0325  148 PRO A N   
570  C CA  . PRO A 94  ? 0.1986 0.1666 0.2148 -0.0158 0.0257  0.0033  148 PRO A CA  
571  C C   . PRO A 94  ? 0.1913 0.1531 0.2032 -0.0026 0.0304  0.0056  148 PRO A C   
572  O O   . PRO A 94  ? 0.2314 0.1833 0.1844 0.0055  0.0190  0.0039  148 PRO A O   
573  C CB  . PRO A 94  ? 0.2115 0.1641 0.2352 -0.0097 -0.0035 0.0063  148 PRO A CB  
574  C CG  . PRO A 94  ? 0.2583 0.1837 0.2042 0.0120  -0.0089 0.0214  148 PRO A CG  
575  C CD  . PRO A 94  ? 0.2335 0.1884 0.1911 0.0075  0.0103  0.0361  148 PRO A CD  
576  N N   . CYS A 95  ? 0.2066 0.1514 0.2212 -0.0024 0.0312  0.0276  149 CYS A N   
577  C CA  . CYS A 95  ? 0.2087 0.1624 0.2229 0.0056  0.0006  0.0457  149 CYS A CA  
578  C C   . CYS A 95  ? 0.1769 0.1771 0.1766 -0.0042 0.0023  0.0256  149 CYS A C   
579  O O   . CYS A 95  ? 0.2196 0.2145 0.1690 0.0128  0.0168  0.0011  149 CYS A O   
580  C CB  . CYS A 95  ? 0.2297 0.1992 0.2700 0.0236  -0.0077 0.0382  149 CYS A CB  
581  S SG  . CYS A 95  ? 0.2364 0.2771 0.3212 -0.0023 -0.0215 0.0418  149 CYS A SG  
582  N N   . TYR A 96  ? 0.1990 0.1440 0.1966 0.0162  0.0162  0.0287  150 TYR A N   
583  C CA  . TYR A 96  ? 0.1643 0.1497 0.2076 -0.0020 0.0102  0.0241  150 TYR A CA  
584  C C   . TYR A 96  ? 0.1824 0.1389 0.1957 -0.0024 0.0022  0.0318  150 TYR A C   
585  O O   . TYR A 96  ? 0.2516 0.2110 0.1740 -0.0023 -0.0017 0.0096  150 TYR A O   
586  C CB  . TYR A 96  ? 0.1687 0.1948 0.2125 -0.0032 0.0104  0.0041  150 TYR A CB  
587  C CG  . TYR A 96  ? 0.1868 0.1669 0.2062 -0.0180 0.0168  0.0120  150 TYR A CG  
588  C CD1 . TYR A 96  ? 0.2225 0.1980 0.1928 -0.0164 0.0128  0.0365  150 TYR A CD1 
589  C CD2 . TYR A 96  ? 0.1697 0.1824 0.2313 -0.0220 0.0202  0.0075  150 TYR A CD2 
590  C CE1 . TYR A 96  ? 0.2124 0.1885 0.2172 -0.0289 -0.0094 0.0311  150 TYR A CE1 
591  C CE2 . TYR A 96  ? 0.1979 0.2158 0.2385 -0.0361 0.0080  0.0034  150 TYR A CE2 
592  C CZ  . TYR A 96  ? 0.2228 0.1936 0.2349 -0.0128 0.0036  0.0036  150 TYR A CZ  
593  O OH  . TYR A 96  ? 0.2444 0.2132 0.2399 -0.0288 -0.0080 -0.0018 150 TYR A OH  
594  N N   . GLY A 97  ? 0.1922 0.1524 0.1996 -0.0096 0.0138  0.0269  151 GLY A N   
595  C CA  . GLY A 97  ? 0.1639 0.1563 0.2265 0.0022  0.0132  0.0421  151 GLY A CA  
596  C C   . GLY A 97  ? 0.2026 0.1633 0.2260 -0.0214 0.0040  0.0254  151 GLY A C   
597  O O   . GLY A 97  ? 0.2084 0.1854 0.2179 -0.0246 0.0062  0.0174  151 GLY A O   
598  N N   . PHE A 98  ? 0.1844 0.1571 0.2182 -0.0096 -0.0011 0.0304  152 PHE A N   
599  C CA  . PHE A 98  ? 0.1604 0.1636 0.2311 0.0191  -0.0035 0.0254  152 PHE A CA  
600  C C   . PHE A 98  ? 0.1710 0.1609 0.2197 0.0043  -0.0185 0.0271  152 PHE A C   
601  O O   . PHE A 98  ? 0.1839 0.1827 0.2249 0.0039  -0.0204 0.0369  152 PHE A O   
602  C CB  . PHE A 98  ? 0.1498 0.2113 0.2232 0.0057  -0.0308 0.0227  152 PHE A CB  
603  C CG  . PHE A 98  ? 0.1510 0.2089 0.2199 -0.0078 -0.0300 0.0216  152 PHE A CG  
604  C CD1 . PHE A 98  ? 0.1600 0.2287 0.2193 0.0030  0.0046  0.0351  152 PHE A CD1 
605  C CD2 . PHE A 98  ? 0.1689 0.2361 0.2193 -0.0093 -0.0087 0.0208  152 PHE A CD2 
606  C CE1 . PHE A 98  ? 0.1912 0.2106 0.2392 0.0071  0.0081  0.0333  152 PHE A CE1 
607  C CE2 . PHE A 98  ? 0.2169 0.2241 0.2339 0.0004  0.0000  0.0332  152 PHE A CE2 
608  C CZ  . PHE A 98  ? 0.2004 0.2208 0.2430 0.0134  0.0276  0.0485  152 PHE A CZ  
609  N N   . GLY A 99  ? 0.1917 0.1655 0.2118 0.0191  -0.0128 0.0449  153 GLY A N   
610  C CA  . GLY A 99  ? 0.2195 0.1765 0.1915 -0.0069 0.0063  0.0404  153 GLY A CA  
611  C C   . GLY A 99  ? 0.2075 0.1987 0.2026 -0.0070 -0.0112 0.0476  153 GLY A C   
612  O O   . GLY A 99  ? 0.2125 0.1917 0.2364 -0.0174 -0.0206 0.0449  153 GLY A O   
613  N N   . ASP A 100 ? 0.2033 0.2121 0.2147 0.0044  0.0057  0.0451  154 ASP A N   
614  C CA  . ASP A 100 ? 0.2103 0.2078 0.2270 0.0166  0.0150  0.0528  154 ASP A CA  
615  C C   . ASP A 100 ? 0.1824 0.1983 0.2248 -0.0160 0.0264  0.0468  154 ASP A C   
616  O O   . ASP A 100 ? 0.1814 0.2268 0.2435 -0.0017 0.0045  0.0341  154 ASP A O   
617  C CB  . ASP A 100 ? 0.2191 0.1999 0.2620 -0.0187 0.0115  0.0425  154 ASP A CB  
618  C CG  . ASP A 100 ? 0.2210 0.1987 0.2510 -0.0054 0.0169  0.0265  154 ASP A CG  
619  O OD1 . ASP A 100 ? 0.2168 0.2336 0.2626 -0.0100 0.0217  0.0192  154 ASP A OD1 
620  O OD2 . ASP A 100 ? 0.2944 0.2251 0.2221 0.0247  0.0180  0.0393  154 ASP A OD2 
621  N N   . ALA A 101 ? 0.2304 0.2244 0.2219 -0.0207 0.0149  0.0548  155 ALA A N   
622  C CA  . ALA A 101 ? 0.2499 0.2633 0.2284 0.0012  0.0285  0.0712  155 ALA A CA  
623  C C   . ALA A 101 ? 0.2473 0.2244 0.2302 0.0354  0.0167  0.0443  155 ALA A C   
624  O O   . ALA A 101 ? 0.2640 0.2674 0.2743 0.0225  -0.0280 0.0567  155 ALA A O   
625  C CB  . ALA A 101 ? 0.2382 0.2726 0.2409 0.0129  0.0401  0.0577  155 ALA A CB  
626  N N   . THR A 102 ? 0.2710 0.2150 0.1923 -0.0200 0.0002  0.0323  156 THR A N   
627  C CA  . THR A 102 ? 0.2540 0.2400 0.2049 -0.0164 0.0137  0.0173  156 THR A CA  
628  C C   . THR A 102 ? 0.2421 0.2494 0.2135 -0.0023 0.0019  0.0342  156 THR A C   
629  O O   . THR A 102 ? 0.2588 0.3103 0.2381 -0.0088 -0.0173 0.0426  156 THR A O   
630  C CB  . THR A 102 ? 0.2799 0.2663 0.2076 -0.0195 0.0457  0.0050  156 THR A CB  
631  O OG1 . THR A 102 ? 0.2805 0.2686 0.2115 0.0051  0.0251  0.0368  156 THR A OG1 
632  C CG2 . THR A 102 ? 0.3057 0.2924 0.2347 -0.0186 0.0863  0.0002  156 THR A CG2 
633  N N   . THR A 103 ? 0.2343 0.2279 0.2179 -0.0021 0.0460  0.0322  157 THR A N   
634  C CA  . THR A 103 ? 0.2120 0.2051 0.2133 0.0114  -0.0088 0.0327  157 THR A CA  
635  C C   . THR A 103 ? 0.2178 0.1967 0.2408 -0.0147 -0.0394 0.0248  157 THR A C   
636  O O   . THR A 103 ? 0.2106 0.2426 0.2585 -0.0034 -0.0232 0.0262  157 THR A O   
637  C CB  . THR A 103 ? 0.2654 0.1999 0.1981 0.0039  -0.0461 0.0399  157 THR A CB  
638  O OG1 . THR A 103 ? 0.2492 0.2329 0.2007 -0.0192 -0.0302 0.0100  157 THR A OG1 
639  C CG2 . THR A 103 ? 0.2750 0.2099 0.2071 0.0074  -0.0223 0.0183  157 THR A CG2 
640  N N   . HIS A 104 ? 0.2362 0.1991 0.2409 0.0078  -0.0071 0.0312  158 HIS A N   
641  C CA  . HIS A 104 ? 0.2336 0.2190 0.2454 0.0504  -0.0179 0.0631  158 HIS A CA  
642  C C   . HIS A 104 ? 0.2147 0.2161 0.2248 -0.0066 -0.0141 0.0527  158 HIS A C   
643  O O   . HIS A 104 ? 0.2261 0.2427 0.2207 0.0080  -0.0111 0.0436  158 HIS A O   
644  C CB  . HIS A 104 ? 0.2190 0.2232 0.2698 0.0051  -0.0074 0.0690  158 HIS A CB  
645  C CG  . HIS A 104 ? 0.2348 0.2793 0.2933 -0.0210 0.0309  0.0990  158 HIS A CG  
646  N ND1 . HIS A 104 ? 0.2764 0.3440 0.2981 -0.0378 0.0255  0.1372  158 HIS A ND1 
647  C CD2 . HIS A 104 ? 0.3096 0.3333 0.3109 0.0047  0.0217  0.1030  158 HIS A CD2 
648  C CE1 . HIS A 104 ? 0.2900 0.3410 0.3004 0.0088  0.0251  0.1361  158 HIS A CE1 
649  N NE2 . HIS A 104 ? 0.3230 0.3548 0.3121 0.0297  0.0065  0.1073  158 HIS A NE2 
650  N N   . ASP A 105 ? 0.1901 0.2293 0.2489 -0.0061 0.0084  0.0378  159 ASP A N   
651  C CA  . ASP A 105 ? 0.2091 0.2050 0.2650 0.0151  -0.0293 0.0441  159 ASP A CA  
652  C C   . ASP A 105 ? 0.2259 0.2130 0.2769 0.0177  -0.0171 0.0542  159 ASP A C   
653  O O   . ASP A 105 ? 0.2474 0.2180 0.2737 0.0122  -0.0011 0.0531  159 ASP A O   
654  C CB  . ASP A 105 ? 0.2546 0.2082 0.3028 0.0619  -0.0260 0.0318  159 ASP A CB  
655  C CG  . ASP A 105 ? 0.2580 0.2184 0.3275 0.0397  -0.0002 0.0047  159 ASP A CG  
656  O OD1 . ASP A 105 ? 0.2226 0.2399 0.3336 0.0279  -0.0190 0.0090  159 ASP A OD1 
657  O OD2 . ASP A 105 ? 0.2756 0.2812 0.3436 0.0726  0.0006  0.0195  159 ASP A OD2 
658  N N   . GLN A 106 ? 0.2122 0.2111 0.2896 0.0183  -0.0486 0.0489  160 GLN A N   
659  C CA  . GLN A 106 ? 0.2225 0.2324 0.3031 -0.0108 -0.0635 0.0280  160 GLN A CA  
660  C C   . GLN A 106 ? 0.2233 0.2419 0.2914 0.0015  -0.0430 0.0211  160 GLN A C   
661  O O   . GLN A 106 ? 0.1948 0.2544 0.3606 -0.0047 -0.0545 0.0277  160 GLN A O   
662  C CB  . GLN A 106 ? 0.3121 0.2665 0.3545 0.0113  -0.1179 0.0348  160 GLN A CB  
663  C CG  . GLN A 106 ? 0.3313 0.2953 0.3978 0.0468  -0.1168 0.0345  160 GLN A CG  
664  C CD  . GLN A 106 ? 0.3181 0.3499 0.4472 0.0239  -0.1061 0.0191  160 GLN A CD  
665  O OE1 . GLN A 106 ? 0.3836 0.3824 0.4887 0.0456  -0.0850 0.0222  160 GLN A OE1 
666  N NE2 . GLN A 106 ? 0.3646 0.3600 0.4522 0.0212  -0.0859 0.0191  160 GLN A NE2 
667  N N   . ASP A 107 ? 0.1984 0.2125 0.2317 0.0238  -0.0351 0.0317  161 ASP A N   
668  C CA  . ASP A 107 ? 0.2134 0.2163 0.2149 0.0440  -0.0261 0.0178  161 ASP A CA  
669  C C   . ASP A 107 ? 0.1574 0.2061 0.2125 0.0254  -0.0192 0.0424  161 ASP A C   
670  O O   . ASP A 107 ? 0.1985 0.2255 0.1982 0.0015  -0.0261 0.0347  161 ASP A O   
671  C CB  . ASP A 107 ? 0.2389 0.2569 0.2298 -0.0110 -0.0286 0.0075  161 ASP A CB  
672  C CG  . ASP A 107 ? 0.2873 0.2710 0.2749 -0.0200 -0.0436 0.0489  161 ASP A CG  
673  O OD1 . ASP A 107 ? 0.3054 0.3075 0.2969 -0.0463 -0.0269 0.0212  161 ASP A OD1 
674  O OD2 . ASP A 107 ? 0.3568 0.3432 0.2938 -0.0112 -0.0746 0.0648  161 ASP A OD2 
675  N N   . VAL A 108 ? 0.1903 0.2199 0.2168 0.0448  0.0106  0.0517  162 VAL A N   
676  C CA  . VAL A 108 ? 0.1859 0.2140 0.1903 0.0341  0.0165  0.0351  162 VAL A CA  
677  C C   . VAL A 108 ? 0.1905 0.2187 0.1856 0.0139  0.0181  0.0380  162 VAL A C   
678  O O   . VAL A 108 ? 0.2163 0.2270 0.1930 0.0003  -0.0273 0.0012  162 VAL A O   
679  C CB  . VAL A 108 ? 0.2234 0.1867 0.1945 -0.0131 0.0136  0.0127  162 VAL A CB  
680  C CG1 . VAL A 108 ? 0.2165 0.2504 0.1863 0.0170  0.0351  -0.0002 162 VAL A CG1 
681  C CG2 . VAL A 108 ? 0.2541 0.2038 0.2153 -0.0328 0.0141  0.0211  162 VAL A CG2 
682  N N   . PHE A 109 ? 0.1998 0.1997 0.1868 0.0229  0.0243  0.0173  163 PHE A N   
683  C CA  . PHE A 109 ? 0.2153 0.1891 0.1805 0.0228  0.0397  0.0157  163 PHE A CA  
684  C C   . PHE A 109 ? 0.1966 0.1896 0.1739 0.0176  -0.0057 0.0020  163 PHE A C   
685  O O   . PHE A 109 ? 0.2125 0.2089 0.1685 -0.0151 -0.0076 0.0073  163 PHE A O   
686  C CB  . PHE A 109 ? 0.2013 0.1941 0.1923 -0.0171 0.0036  0.0271  163 PHE A CB  
687  C CG  . PHE A 109 ? 0.1828 0.1987 0.2084 -0.0207 -0.0121 0.0354  163 PHE A CG  
688  C CD1 . PHE A 109 ? 0.1806 0.2670 0.2199 -0.0333 -0.0109 0.0321  163 PHE A CD1 
689  C CD2 . PHE A 109 ? 0.2384 0.2013 0.2107 -0.0396 0.0007  0.0463  163 PHE A CD2 
690  C CE1 . PHE A 109 ? 0.1874 0.2692 0.2467 -0.0626 -0.0003 0.0293  163 PHE A CE1 
691  C CE2 . PHE A 109 ? 0.2396 0.2360 0.2272 -0.0111 -0.0160 0.0574  163 PHE A CE2 
692  C CZ  . PHE A 109 ? 0.2191 0.2245 0.2426 -0.0342 -0.0100 0.0530  163 PHE A CZ  
693  N N   . SER A 110 ? 0.2180 0.1952 0.1973 0.0186  0.0040  0.0052  164 SER A N   
694  C CA  . SER A 110 ? 0.2167 0.1786 0.2188 0.0234  -0.0211 -0.0004 164 SER A CA  
695  C C   . SER A 110 ? 0.2158 0.1937 0.2071 0.0083  -0.0030 0.0062  164 SER A C   
696  O O   . SER A 110 ? 0.2540 0.2242 0.2126 -0.0096 0.0090  0.0177  164 SER A O   
697  C CB  . SER A 110 ? 0.2573 0.1829 0.2519 0.0380  -0.0352 -0.0163 164 SER A CB  
698  O OG  . SER A 110 ? 0.2617 0.2204 0.2815 0.0236  0.0106  -0.0023 164 SER A OG  
699  N N   . PHE A 111 ? 0.1939 0.1987 0.2157 0.0057  -0.0058 0.0053  165 PHE A N   
700  C CA  . PHE A 111 ? 0.2270 0.2228 0.2124 0.0147  -0.0079 -0.0184 165 PHE A CA  
701  C C   . PHE A 111 ? 0.2770 0.2240 0.2532 -0.0021 -0.0008 -0.0130 165 PHE A C   
702  O O   . PHE A 111 ? 0.2628 0.2686 0.2645 -0.0028 0.0097  -0.0058 165 PHE A O   
703  C CB  . PHE A 111 ? 0.2194 0.2289 0.2214 -0.0039 -0.0151 -0.0153 165 PHE A CB  
704  C CG  . PHE A 111 ? 0.2022 0.2172 0.2172 0.0156  0.0194  0.0340  165 PHE A CG  
705  C CD1 . PHE A 111 ? 0.2386 0.2369 0.2327 0.0074  0.0104  0.0297  165 PHE A CD1 
706  C CD2 . PHE A 111 ? 0.2307 0.2484 0.2063 0.0509  -0.0029 0.0309  165 PHE A CD2 
707  C CE1 . PHE A 111 ? 0.2228 0.2621 0.2699 0.0088  0.0061  0.0428  165 PHE A CE1 
708  C CE2 . PHE A 111 ? 0.2391 0.2608 0.2305 0.0234  -0.0079 0.0183  165 PHE A CE2 
709  C CZ  . PHE A 111 ? 0.2293 0.2360 0.2466 0.0176  -0.0111 0.0142  165 PHE A CZ  
710  N N   . ASN A 112 ? 0.2740 0.1855 0.2535 0.0198  0.0087  -0.0078 166 ASN A N   
711  C CA  . ASN A 112 ? 0.3191 0.2188 0.2551 -0.0064 0.0296  0.0128  166 ASN A CA  
712  C C   . ASN A 112 ? 0.3559 0.2816 0.2502 0.0284  0.0306  -0.0191 166 ASN A C   
713  O O   . ASN A 112 ? 0.3549 0.3207 0.2656 0.0324  0.0481  -0.0186 166 ASN A O   
714  C CB  . ASN A 112 ? 0.3317 0.1844 0.2667 0.0323  0.0390  -0.0180 166 ASN A CB  
715  C CG  . ASN A 112 ? 0.3472 0.2501 0.2684 0.0753  0.0206  -0.0067 166 ASN A CG  
716  O OD1 . ASN A 112 ? 0.4208 0.3167 0.2574 0.0705  0.0058  -0.0116 166 ASN A OD1 
717  N ND2 . ASN A 112 ? 0.2814 0.2920 0.2754 0.0420  0.0474  0.0387  166 ASN A ND2 
718  N N   . PRO A 113 ? 0.3334 0.3080 0.2703 0.0431  0.0478  -0.0204 167 PRO A N   
719  C CA  . PRO A 113 ? 0.3639 0.3564 0.2696 0.0316  0.0630  -0.0157 167 PRO A CA  
720  C C   . PRO A 113 ? 0.3817 0.3501 0.2676 0.0108  0.0516  -0.0204 167 PRO A C   
721  O O   . PRO A 113 ? 0.4199 0.3760 0.2409 -0.0192 0.0427  -0.0190 167 PRO A O   
722  C CB  . PRO A 113 ? 0.3214 0.3747 0.2888 0.0344  0.0596  0.0152  167 PRO A CB  
723  C CG  . PRO A 113 ? 0.3617 0.3952 0.3077 0.0400  0.0696  -0.0028 167 PRO A CG  
724  C CD  . PRO A 113 ? 0.2951 0.3621 0.2990 0.0359  0.0883  -0.0259 167 PRO A CD  
725  N N   . ASN A 114 ? 0.3655 0.3033 0.2761 -0.0121 0.0412  -0.0237 168 ASN A N   
726  C CA  . ASN A 114 ? 0.4165 0.3207 0.2891 0.0152  0.0190  -0.0218 168 ASN A CA  
727  C C   . ASN A 114 ? 0.4202 0.3255 0.2713 0.0543  0.0131  -0.0416 168 ASN A C   
728  O O   . ASN A 114 ? 0.4532 0.3218 0.2810 0.0493  0.0145  -0.0323 168 ASN A O   
729  C CB  . ASN A 114 ? 0.4057 0.3387 0.2991 0.0228  0.0326  -0.0182 168 ASN A CB  
730  C CG  . ASN A 114 ? 0.4285 0.3489 0.3176 0.0285  0.0435  -0.0110 168 ASN A CG  
731  O OD1 . ASN A 114 ? 0.4438 0.3797 0.3403 0.0740  0.0776  -0.0149 168 ASN A OD1 
732  N ND2 . ASN A 114 ? 0.3961 0.3066 0.3241 0.0337  0.0278  -0.0374 168 ASN A ND2 
733  N N   . ASP A 115 ? 0.3937 0.3238 0.2529 0.0650  -0.0200 -0.0247 169 ASP A N   
734  C CA  . ASP A 115 ? 0.4212 0.3431 0.2469 0.0464  -0.0527 -0.0429 169 ASP A CA  
735  C C   . ASP A 115 ? 0.3957 0.3204 0.2787 0.0283  -0.0516 -0.0350 169 ASP A C   
736  O O   . ASP A 115 ? 0.4230 0.3289 0.3053 0.0231  -0.0842 -0.0008 169 ASP A O   
737  C CB  . ASP A 115 ? 0.4630 0.4022 0.2571 0.0346  -0.1007 -0.0504 169 ASP A CB  
738  C CG  . ASP A 115 ? 0.5412 0.4768 0.3223 0.0061  -0.1018 -0.0977 169 ASP A CG  
739  O OD1 . ASP A 115 ? 0.5649 0.5130 0.3646 0.0187  -0.0878 -0.0654 169 ASP A OD1 
740  O OD2 . ASP A 115 ? 0.6258 0.5108 0.3589 -0.0053 -0.0713 -0.1082 169 ASP A OD2 
741  N N   . THR A 116 ? 0.3859 0.2758 0.2614 0.0200  -0.0365 -0.0415 170 THR A N   
742  C CA  . THR A 116 ? 0.3524 0.2589 0.2665 0.0411  -0.0079 -0.0401 170 THR A CA  
743  C C   . THR A 116 ? 0.3010 0.2309 0.2487 0.0194  -0.0073 -0.0304 170 THR A C   
744  O O   . THR A 116 ? 0.3831 0.2227 0.2348 0.0021  0.0091  -0.0087 170 THR A O   
745  C CB  . THR A 116 ? 0.4286 0.2938 0.3048 0.0330  0.0040  -0.0440 170 THR A CB  
746  O OG1 . THR A 116 ? 0.5098 0.2980 0.3111 0.0240  0.0083  -0.0283 170 THR A OG1 
747  C CG2 . THR A 116 ? 0.4303 0.2929 0.3146 0.0291  0.0125  -0.0435 170 THR A CG2 
748  N N   . TYR A 117 ? 0.3011 0.2524 0.2293 -0.0008 -0.0325 -0.0246 171 TYR A N   
749  C CA  . TYR A 117 ? 0.2649 0.2347 0.2462 -0.0107 -0.0225 -0.0014 171 TYR A CA  
750  C C   . TYR A 117 ? 0.2687 0.2127 0.2706 0.0112  -0.0381 -0.0171 171 TYR A C   
751  O O   . TYR A 117 ? 0.3243 0.2419 0.3083 0.0148  -0.0290 -0.0288 171 TYR A O   
752  C CB  . TYR A 117 ? 0.2365 0.2468 0.2421 0.0027  -0.0063 -0.0004 171 TYR A CB  
753  C CG  . TYR A 117 ? 0.2572 0.2339 0.2224 0.0117  -0.0303 0.0116  171 TYR A CG  
754  C CD1 . TYR A 117 ? 0.3080 0.2266 0.2364 0.0485  -0.0206 0.0037  171 TYR A CD1 
755  C CD2 . TYR A 117 ? 0.2661 0.2418 0.2589 -0.0168 -0.0089 0.0072  171 TYR A CD2 
756  C CE1 . TYR A 117 ? 0.2408 0.2510 0.2331 0.0141  -0.0223 -0.0117 171 TYR A CE1 
757  C CE2 . TYR A 117 ? 0.2551 0.2655 0.2640 0.0050  -0.0370 -0.0001 171 TYR A CE2 
758  C CZ  . TYR A 117 ? 0.2436 0.2551 0.2411 0.0264  -0.0427 -0.0207 171 TYR A CZ  
759  O OH  . TYR A 117 ? 0.3026 0.3042 0.2595 0.0233  -0.0525 -0.0075 171 TYR A OH  
760  N N   . CYS A 118 ? 0.2606 0.2369 0.2572 -0.0432 -0.0280 -0.0076 172 CYS A N   
761  C CA  . CYS A 118 ? 0.2404 0.2287 0.2440 -0.0324 -0.0197 -0.0010 172 CYS A CA  
762  C C   . CYS A 118 ? 0.1943 0.2355 0.2400 0.0058  0.0115  -0.0131 172 CYS A C   
763  O O   . CYS A 118 ? 0.2262 0.2410 0.2565 0.0128  0.0423  -0.0265 172 CYS A O   
764  C CB  . CYS A 118 ? 0.2933 0.2239 0.2452 -0.0433 0.0000  0.0157  172 CYS A CB  
765  S SG  . CYS A 118 ? 0.3077 0.2766 0.2605 -0.0401 0.0060  0.0074  172 CYS A SG  
766  N N   . ASN A 119 ? 0.2221 0.2324 0.2654 0.0325  -0.0038 -0.0184 173 ASN A N   
767  C CA  . ASN A 119 ? 0.2277 0.2367 0.2787 0.0462  -0.0009 -0.0291 173 ASN A CA  
768  C C   . ASN A 119 ? 0.2478 0.2681 0.2775 0.0435  -0.0232 -0.0038 173 ASN A C   
769  O O   . ASN A 119 ? 0.2335 0.2981 0.2839 0.0447  -0.0312 -0.0086 173 ASN A O   
770  C CB  . ASN A 119 ? 0.2544 0.2688 0.3011 0.0224  0.0262  -0.0756 173 ASN A CB  
771  C CG  . ASN A 119 ? 0.2692 0.2948 0.3231 -0.0019 0.0483  -0.0525 173 ASN A CG  
772  O OD1 . ASN A 119 ? 0.2973 0.3263 0.3476 0.0075  0.0225  -0.0521 173 ASN A OD1 
773  N ND2 . ASN A 119 ? 0.3628 0.3128 0.3290 0.0358  0.0261  -0.0428 173 ASN A ND2 
774  N N   . GLY A 120 ? 0.2298 0.2011 0.2660 0.0026  -0.0046 -0.0116 174 GLY A N   
775  C CA  . GLY A 120 ? 0.2317 0.1837 0.2452 -0.0103 0.0058  -0.0097 174 GLY A CA  
776  C C   . GLY A 120 ? 0.2189 0.1798 0.2295 -0.0015 0.0198  -0.0131 174 GLY A C   
777  O O   . GLY A 120 ? 0.2148 0.2060 0.2657 0.0085  0.0181  0.0071  174 GLY A O   
778  N N   . PHE A 121 ? 0.2410 0.1817 0.2439 0.0205  -0.0021 -0.0297 175 PHE A N   
779  C CA  . PHE A 121 ? 0.2141 0.1965 0.2442 0.0088  0.0212  -0.0175 175 PHE A CA  
780  C C   . PHE A 121 ? 0.2002 0.2201 0.2567 0.0227  0.0042  -0.0182 175 PHE A C   
781  O O   . PHE A 121 ? 0.2293 0.1951 0.2496 0.0091  -0.0080 -0.0062 175 PHE A O   
782  C CB  . PHE A 121 ? 0.2251 0.2177 0.2452 0.0568  -0.0163 -0.0043 175 PHE A CB  
783  C CG  . PHE A 121 ? 0.2464 0.2656 0.2436 0.0436  -0.0290 -0.0164 175 PHE A CG  
784  C CD1 . PHE A 121 ? 0.2876 0.2855 0.2461 0.0395  -0.0355 0.0084  175 PHE A CD1 
785  C CD2 . PHE A 121 ? 0.2482 0.2976 0.2344 0.0693  -0.0307 0.0149  175 PHE A CD2 
786  C CE1 . PHE A 121 ? 0.2879 0.3185 0.2587 0.0511  -0.0508 -0.0142 175 PHE A CE1 
787  C CE2 . PHE A 121 ? 0.2996 0.3240 0.2619 0.0557  -0.0540 -0.0082 175 PHE A CE2 
788  C CZ  . PHE A 121 ? 0.3114 0.3054 0.2549 0.0499  -0.0621 -0.0300 175 PHE A CZ  
789  N N   . GLU A 122 ? 0.2202 0.2382 0.2430 0.0218  0.0054  -0.0177 176 GLU A N   
790  C CA  . GLU A 122 ? 0.2144 0.2490 0.2675 0.0669  -0.0263 0.0207  176 GLU A CA  
791  C C   . GLU A 122 ? 0.1816 0.2259 0.2811 0.0169  -0.0150 0.0094  176 GLU A C   
792  O O   . GLU A 122 ? 0.2115 0.2293 0.2826 0.0054  -0.0048 0.0028  176 GLU A O   
793  C CB  . GLU A 122 ? 0.2753 0.3166 0.2813 0.1156  -0.0202 0.0468  176 GLU A CB  
794  C CG  . GLU A 122 ? 0.3961 0.3502 0.3036 0.1000  -0.0381 0.0579  176 GLU A CG  
795  C CD  . GLU A 122 ? 0.4564 0.3470 0.3627 0.0725  -0.0412 0.0406  176 GLU A CD  
796  O OE1 . GLU A 122 ? 0.3683 0.2808 0.3413 0.0792  -0.0286 0.0255  176 GLU A OE1 
797  O OE2 . GLU A 122 ? 0.5127 0.4323 0.4551 0.0520  -0.0399 0.0329  176 GLU A OE2 
798  N N   . GLU A 123 ? 0.1989 0.2490 0.2574 0.0360  -0.0245 -0.0093 177 GLU A N   
799  C CA  . GLU A 123 ? 0.2422 0.2338 0.2591 0.0222  -0.0127 -0.0281 177 GLU A CA  
800  C C   . GLU A 123 ? 0.2267 0.2034 0.2429 0.0166  0.0247  -0.0040 177 GLU A C   
801  O O   . GLU A 123 ? 0.2762 0.2185 0.2479 0.0088  0.0410  0.0136  177 GLU A O   
802  C CB  . GLU A 123 ? 0.3082 0.2813 0.2651 0.0062  0.0296  -0.0526 177 GLU A CB  
803  C CG  . GLU A 123 ? 0.3632 0.3251 0.3243 -0.0175 0.0693  -0.0700 177 GLU A CG  
804  C CD  . GLU A 123 ? 0.3754 0.3956 0.3917 -0.0591 0.1416  -0.0957 177 GLU A CD  
805  O OE1 . GLU A 123 ? 0.4128 0.4309 0.4408 -0.0552 0.1488  -0.1056 177 GLU A OE1 
806  O OE2 . GLU A 123 ? 0.3973 0.4433 0.4067 -0.0712 0.1558  -0.0964 177 GLU A OE2 
807  N N   . VAL A 124 ? 0.2215 0.2253 0.2548 0.0411  0.0006  -0.0064 178 VAL A N   
808  C CA  . VAL A 124 ? 0.2087 0.2195 0.2510 0.0194  0.0212  0.0117  178 VAL A CA  
809  C C   . VAL A 124 ? 0.1750 0.1989 0.2385 0.0210  -0.0105 0.0262  178 VAL A C   
810  O O   . VAL A 124 ? 0.2109 0.2067 0.2487 0.0105  0.0069  0.0280  178 VAL A O   
811  C CB  . VAL A 124 ? 0.1932 0.1977 0.2652 0.0122  0.0049  0.0029  178 VAL A CB  
812  C CG1 . VAL A 124 ? 0.1918 0.2033 0.2918 0.0257  0.0037  -0.0003 178 VAL A CG1 
813  C CG2 . VAL A 124 ? 0.2255 0.2135 0.2717 -0.0018 0.0037  0.0342  178 VAL A CG2 
814  N N   . LEU A 125 ? 0.1629 0.2123 0.2315 0.0053  -0.0043 0.0115  179 LEU A N   
815  C CA  . LEU A 125 ? 0.1571 0.2229 0.2547 0.0034  -0.0001 -0.0146 179 LEU A CA  
816  C C   . LEU A 125 ? 0.1648 0.2160 0.2801 0.0024  0.0113  0.0034  179 LEU A C   
817  O O   . LEU A 125 ? 0.2332 0.2080 0.2783 0.0023  -0.0098 0.0176  179 LEU A O   
818  C CB  . LEU A 125 ? 0.1767 0.2449 0.2825 0.0022  -0.0047 -0.0140 179 LEU A CB  
819  C CG  . LEU A 125 ? 0.2788 0.2305 0.2980 -0.0103 -0.0446 -0.0056 179 LEU A CG  
820  C CD1 . LEU A 125 ? 0.3030 0.2656 0.3106 -0.0027 -0.0767 0.0096  179 LEU A CD1 
821  C CD2 . LEU A 125 ? 0.3065 0.2412 0.3044 -0.0305 -0.0207 0.0014  179 LEU A CD2 
822  N N   . MET A 126 ? 0.1810 0.2480 0.3061 0.0133  0.0289  0.0069  180 MET A N   
823  C CA  . MET A 126 ? 0.2074 0.3265 0.3891 0.0385  0.0450  0.0235  180 MET A CA  
824  C C   . MET A 126 ? 0.1741 0.2995 0.3310 -0.0057 0.0159  -0.0095 180 MET A C   
825  O O   . MET A 126 ? 0.1785 0.3253 0.3442 -0.0003 0.0286  -0.0143 180 MET A O   
826  C CB  . MET A 126 ? 0.3960 0.5452 0.6508 0.1117  0.0680  0.0135  180 MET A CB  
827  C CG  . MET A 126 ? 0.6669 0.8360 0.8579 0.1257  0.0682  0.0065  180 MET A CG  
828  S SD  . MET A 126 ? 0.9771 1.0371 1.0161 0.1431  0.0474  0.0054  180 MET A SD  
829  C CE  . MET A 126 ? 1.0160 1.0857 1.0785 0.1257  0.0405  0.0099  180 MET A CE  
830  N N   . CYS A 127 ? 0.1878 0.2529 0.2741 0.0134  -0.0088 -0.0233 181 CYS A N   
831  C CA  . CYS A 127 ? 0.1859 0.2486 0.2723 0.0220  -0.0108 0.0042  181 CYS A CA  
832  C C   . CYS A 127 ? 0.2371 0.2297 0.2474 0.0212  -0.0056 0.0010  181 CYS A C   
833  O O   . CYS A 127 ? 0.2725 0.2666 0.2311 0.0310  0.0154  0.0330  181 CYS A O   
834  C CB  . CYS A 127 ? 0.2320 0.2435 0.2646 0.0278  -0.0123 -0.0244 181 CYS A CB  
835  S SG  . CYS A 127 ? 0.2931 0.2715 0.2523 0.0018  0.0226  0.0060  181 CYS A SG  
836  N N   . TYR A 128 ? 0.1943 0.2376 0.2431 0.0122  0.0052  -0.0147 182 TYR A N   
837  C CA  . TYR A 128 ? 0.2149 0.2409 0.2588 0.0097  0.0441  -0.0014 182 TYR A CA  
838  C C   . TYR A 128 ? 0.2061 0.2304 0.2848 -0.0109 0.0131  0.0414  182 TYR A C   
839  O O   . TYR A 128 ? 0.2299 0.2323 0.2804 0.0061  0.0284  0.0539  182 TYR A O   
840  C CB  . TYR A 128 ? 0.2467 0.2164 0.2758 0.0288  0.0380  -0.0065 182 TYR A CB  
841  C CG  . TYR A 128 ? 0.2373 0.1708 0.2552 -0.0030 0.0208  0.0253  182 TYR A CG  
842  C CD1 . TYR A 128 ? 0.2190 0.1789 0.2634 0.0423  0.0220  0.0157  182 TYR A CD1 
843  C CD2 . TYR A 128 ? 0.2401 0.2113 0.2605 -0.0025 -0.0347 0.0022  182 TYR A CD2 
844  C CE1 . TYR A 128 ? 0.1944 0.1777 0.2741 0.0110  0.0087  0.0173  182 TYR A CE1 
845  C CE2 . TYR A 128 ? 0.2618 0.1919 0.2566 0.0044  -0.0050 0.0367  182 TYR A CE2 
846  C CZ  . TYR A 128 ? 0.2261 0.1745 0.2589 0.0074  0.0098  0.0219  182 TYR A CZ  
847  O OH  . TYR A 128 ? 0.2072 0.2001 0.2571 0.0077  0.0047  0.0198  182 TYR A OH  
848  N N   . ARG A 129 ? 0.2043 0.2624 0.3157 -0.0051 -0.0174 0.0697  183 ARG A N   
849  C CA  . ARG A 129 ? 0.1955 0.3738 0.3851 -0.0096 -0.0063 0.1259  183 ARG A CA  
850  C C   . ARG A 129 ? 0.2110 0.4070 0.4062 0.0264  0.0418  0.1494  183 ARG A C   
851  O O   . ARG A 129 ? 0.2651 0.4099 0.4244 0.0175  -0.0040 0.1667  183 ARG A O   
852  C CB  . ARG A 129 ? 0.2051 0.4689 0.4849 -0.0379 0.0110  0.1435  183 ARG A CB  
853  C CG  . ARG A 129 ? 0.3675 0.5660 0.5734 0.0042  0.0008  0.1318  183 ARG A CG  
854  C CD  . ARG A 129 ? 0.4723 0.6556 0.6401 0.0319  -0.0152 0.1176  183 ARG A CD  
855  N NE  . ARG A 129 ? 0.5975 0.7205 0.7085 0.0470  -0.0201 0.1129  183 ARG A NE  
856  C CZ  . ARG A 129 ? 0.7088 0.8015 0.7743 0.0318  -0.0155 0.0993  183 ARG A CZ  
857  N NH1 . ARG A 129 ? 0.7591 0.8237 0.7955 0.0253  -0.0023 0.0931  183 ARG A NH1 
858  N NH2 . ARG A 129 ? 0.7395 0.8314 0.8116 0.0352  -0.0266 0.0927  183 ARG A NH2 
859  N N   . GLU A 130 ? 0.2523 0.4316 0.4327 0.0583  0.0677  0.1458  184 GLU A N   
860  C CA  . GLU A 130 ? 0.3439 0.5124 0.4883 0.0897  0.0914  0.1357  184 GLU A CA  
861  C C   . GLU A 130 ? 0.3028 0.4014 0.3954 0.0889  0.1030  0.1081  184 GLU A C   
862  O O   . GLU A 130 ? 0.3433 0.4202 0.3867 0.1117  0.1523  0.1026  184 GLU A O   
863  C CB  . GLU A 130 ? 0.5636 0.7089 0.6655 0.0905  0.1102  0.1259  184 GLU A CB  
864  C CG  . GLU A 130 ? 0.8049 0.9424 0.8749 0.0779  0.1060  0.1109  184 GLU A CG  
865  C CD  . GLU A 130 ? 1.0492 1.1321 1.0504 0.0669  0.0891  0.0912  184 GLU A CD  
866  O OE1 . GLU A 130 ? 1.1354 1.2085 1.1363 0.0654  0.0848  0.0846  184 GLU A OE1 
867  O OE2 . GLU A 130 ? 1.1378 1.2368 1.1416 0.0598  0.0790  0.0848  184 GLU A OE2 
868  N N   . ILE A 131 ? 0.2788 0.3072 0.3316 0.0492  0.0533  0.0573  185 ILE A N   
869  C CA  . ILE A 131 ? 0.2384 0.2883 0.2909 0.0584  0.0595  0.0655  185 ILE A CA  
870  C C   . ILE A 131 ? 0.2570 0.2980 0.2775 0.0518  0.0531  0.0702  185 ILE A C   
871  O O   . ILE A 131 ? 0.2735 0.2975 0.2755 0.0306  0.0598  0.0785  185 ILE A O   
872  C CB  . ILE A 131 ? 0.2880 0.2963 0.3347 0.0310  0.0040  0.0289  185 ILE A CB  
873  C CG1 . ILE A 131 ? 0.3573 0.3559 0.3864 -0.0218 0.0339  0.0263  185 ILE A CG1 
874  C CG2 . ILE A 131 ? 0.2507 0.3295 0.3295 0.0213  -0.0090 0.0288  185 ILE A CG2 
875  C CD1 . ILE A 131 ? 0.4663 0.4080 0.4052 -0.0304 0.0701  0.0320  185 ILE A CD1 
876  N N   . VAL A 132 ? 0.2556 0.2963 0.2715 0.0109  0.0199  0.0775  186 VAL A N   
877  C CA  . VAL A 132 ? 0.2825 0.2974 0.2830 0.0027  0.0127  0.0790  186 VAL A CA  
878  C C   . VAL A 132 ? 0.2558 0.3412 0.3487 -0.0224 0.0057  0.0926  186 VAL A C   
879  O O   . VAL A 132 ? 0.2743 0.3290 0.3374 0.0031  -0.0173 0.0985  186 VAL A O   
880  C CB  . VAL A 132 ? 0.2749 0.2703 0.2876 0.0296  -0.0125 0.0479  186 VAL A CB  
881  C CG1 . VAL A 132 ? 0.2863 0.3205 0.3239 -0.0101 0.0008  0.0342  186 VAL A CG1 
882  C CG2 . VAL A 132 ? 0.3282 0.2755 0.2937 0.0218  -0.0193 0.0476  186 VAL A CG2 
883  N N   . PRO A 133 ? 0.2490 0.3883 0.4188 0.0014  0.0247  0.1472  187 PRO A N   
884  C CA  . PRO A 133 ? 0.2422 0.4071 0.4395 -0.0060 0.0217  0.1798  187 PRO A CA  
885  C C   . PRO A 133 ? 0.2985 0.3989 0.4316 0.0169  0.0743  0.1955  187 PRO A C   
886  O O   . PRO A 133 ? 0.3258 0.4062 0.4794 -0.0195 0.0469  0.2010  187 PRO A O   
887  C CB  . PRO A 133 ? 0.2584 0.4350 0.4613 -0.0119 0.0244  0.1539  187 PRO A CB  
888  C CG  . PRO A 133 ? 0.2363 0.4406 0.4607 -0.0498 0.0206  0.1613  187 PRO A CG  
889  C CD  . PRO A 133 ? 0.2236 0.4051 0.4462 -0.0190 0.0262  0.1657  187 PRO A CD  
890  N N   . GLN A 134 ? 0.2949 0.4266 0.3955 0.0756  0.1016  0.1890  188 GLN A N   
891  C CA  . GLN A 134 ? 0.3308 0.4232 0.4069 0.1049  0.0805  0.1523  188 GLN A CA  
892  C C   . GLN A 134 ? 0.2867 0.3561 0.3513 0.0754  0.0625  0.1304  188 GLN A C   
893  O O   . GLN A 134 ? 0.3632 0.3826 0.3386 0.0780  0.0787  0.1097  188 GLN A O   
894  C CB  . GLN A 134 ? 0.4489 0.5172 0.4599 0.1387  0.0438  0.1309  188 GLN A CB  
895  C CG  . GLN A 134 ? 0.5364 0.6201 0.5317 0.1340  0.0281  0.1118  188 GLN A CG  
896  C CD  . GLN A 134 ? 0.6573 0.7405 0.6098 0.0887  0.0143  0.1059  188 GLN A CD  
897  O OE1 . GLN A 134 ? 0.7204 0.7791 0.6649 0.0660  0.0009  0.1031  188 GLN A OE1 
898  N NE2 . GLN A 134 ? 0.6809 0.7617 0.6203 0.0695  0.0250  0.1146  188 GLN A NE2 
899  N N   . LEU A 135 ? 0.2132 0.3045 0.3380 0.0179  0.0909  0.0587  189 LEU A N   
900  C CA  . LEU A 135 ? 0.2326 0.2669 0.3131 0.0327  0.0697  0.0999  189 LEU A CA  
901  C C   . LEU A 135 ? 0.2124 0.2672 0.3371 -0.0021 0.0329  0.0829  189 LEU A C   
902  O O   . LEU A 135 ? 0.2658 0.2969 0.3462 -0.0026 0.0156  0.0954  189 LEU A O   
903  C CB  . LEU A 135 ? 0.2570 0.2997 0.2928 -0.0068 0.0490  0.0933  189 LEU A CB  
904  C CG  . LEU A 135 ? 0.2625 0.2976 0.2678 0.0010  0.0217  0.0713  189 LEU A CG  
905  C CD1 . LEU A 135 ? 0.2703 0.3223 0.2622 0.0044  0.0593  0.0662  189 LEU A CD1 
906  C CD2 . LEU A 135 ? 0.2544 0.3068 0.2884 0.0098  -0.0002 0.0490  189 LEU A CD2 
907  N N   . ARG A 136 ? 0.2129 0.2687 0.3311 0.0332  0.0526  0.0886  190 ARG A N   
908  C CA  . ARG A 136 ? 0.2453 0.3042 0.3453 0.0252  -0.0036 0.1025  190 ARG A CA  
909  C C   . ARG A 136 ? 0.1918 0.2547 0.2900 -0.0063 0.0037  0.0677  190 ARG A C   
910  O O   . ARG A 136 ? 0.2142 0.2731 0.2538 -0.0224 0.0046  0.0443  190 ARG A O   
911  C CB  . ARG A 136 ? 0.3366 0.4027 0.4160 0.0586  -0.0202 0.1596  190 ARG A CB  
912  C CG  . ARG A 136 ? 0.4976 0.5377 0.5384 0.0726  0.0095  0.1649  190 ARG A CG  
913  C CD  . ARG A 136 ? 0.6425 0.6890 0.6703 0.0360  0.0339  0.1574  190 ARG A CD  
914  N NE  . ARG A 136 ? 0.7672 0.7900 0.7662 0.0102  0.0369  0.1466  190 ARG A NE  
915  C CZ  . ARG A 136 ? 0.8498 0.8958 0.8561 -0.0090 0.0500  0.1354  190 ARG A CZ  
916  N NH1 . ARG A 136 ? 0.8878 0.9071 0.8761 -0.0169 0.0542  0.1381  190 ARG A NH1 
917  N NH2 . ARG A 136 ? 0.8690 0.9120 0.8828 -0.0101 0.0490  0.1298  190 ARG A NH2 
918  N N   . LEU A 137 ? 0.2318 0.2230 0.2902 -0.0150 0.0167  0.0650  191 LEU A N   
919  C CA  . LEU A 137 ? 0.2280 0.2236 0.2718 -0.0134 -0.0187 0.0387  191 LEU A CA  
920  C C   . LEU A 137 ? 0.2270 0.1453 0.2861 -0.0232 -0.0212 0.0604  191 LEU A C   
921  O O   . LEU A 137 ? 0.3138 0.1577 0.3223 -0.0224 -0.0160 0.0774  191 LEU A O   
922  C CB  . LEU A 137 ? 0.2437 0.2528 0.2688 -0.0113 -0.0290 0.0474  191 LEU A CB  
923  C CG  . LEU A 137 ? 0.2600 0.2456 0.2892 -0.0752 -0.0450 0.0453  191 LEU A CG  
924  C CD1 . LEU A 137 ? 0.3079 0.3252 0.3177 -0.0082 -0.0678 0.0093  191 LEU A CD1 
925  C CD2 . LEU A 137 ? 0.2817 0.2505 0.3067 -0.0437 -0.0391 0.0506  191 LEU A CD2 
926  N N   . SER A 138 ? 0.1980 0.1674 0.2667 -0.0164 -0.0138 0.0448  192 SER A N   
927  C CA  . SER A 138 ? 0.2254 0.1777 0.2567 0.0010  -0.0186 0.0336  192 SER A CA  
928  C C   . SER A 138 ? 0.2386 0.1986 0.2337 -0.0151 -0.0390 0.0476  192 SER A C   
929  O O   . SER A 138 ? 0.2614 0.1922 0.2413 -0.0111 -0.0566 0.0424  192 SER A O   
930  C CB  . SER A 138 ? 0.2484 0.1992 0.2747 0.0199  -0.0307 0.0431  192 SER A CB  
931  O OG  . SER A 138 ? 0.2364 0.2309 0.2621 0.0133  -0.0271 0.0581  192 SER A OG  
932  N N   . GLY A 139 ? 0.1953 0.1999 0.2765 -0.0085 0.0078  0.0686  193 GLY A N   
933  C CA  . GLY A 139 ? 0.2103 0.2196 0.2863 0.0134  0.0160  0.0632  193 GLY A CA  
934  C C   . GLY A 139 ? 0.2293 0.2094 0.2798 0.0001  -0.0195 0.0524  193 GLY A C   
935  O O   . GLY A 139 ? 0.2247 0.2352 0.2613 0.0080  -0.0101 0.0461  193 GLY A O   
936  N N   . PRO A 140 ? 0.2176 0.2152 0.2972 -0.0120 -0.0020 0.0297  194 PRO A N   
937  C CA  . PRO A 140 ? 0.2825 0.2018 0.2904 0.0375  0.0153  0.0370  194 PRO A CA  
938  C C   . PRO A 140 ? 0.2618 0.1762 0.2989 0.0033  0.0097  0.0209  194 PRO A C   
939  O O   . PRO A 140 ? 0.2640 0.2051 0.2871 -0.0279 0.0395  0.0300  194 PRO A O   
940  C CB  . PRO A 140 ? 0.3059 0.2697 0.2960 0.0567  -0.0064 0.0373  194 PRO A CB  
941  C CG  . PRO A 140 ? 0.2872 0.3210 0.3325 0.0402  0.0140  -0.0424 194 PRO A CG  
942  C CD  . PRO A 140 ? 0.2339 0.3043 0.2891 -0.0222 0.0187  0.0394  194 PRO A CD  
943  N N   . THR A 141 ? 0.2476 0.2076 0.2859 -0.0114 0.0199  0.0336  195 THR A N   
944  C CA  . THR A 141 ? 0.1670 0.2230 0.2883 0.0058  0.0082  0.0324  195 THR A CA  
945  C C   . THR A 141 ? 0.1806 0.2061 0.2553 0.0232  0.0406  0.0327  195 THR A C   
946  O O   . THR A 141 ? 0.2115 0.2213 0.2571 0.0195  0.0380  0.0270  195 THR A O   
947  C CB  . THR A 141 ? 0.1983 0.2470 0.3043 -0.0123 -0.0351 0.0190  195 THR A CB  
948  O OG1 . THR A 141 ? 0.2101 0.2926 0.3521 -0.0296 -0.0326 -0.0067 195 THR A OG1 
949  C CG2 . THR A 141 ? 0.2673 0.2633 0.3011 0.0372  -0.0493 0.0175  195 THR A CG2 
950  N N   . SER A 142 ? 0.2015 0.1844 0.2499 -0.0062 0.0164  0.0402  196 SER A N   
951  C CA  . SER A 142 ? 0.2137 0.1744 0.2362 0.0147  -0.0211 0.0625  196 SER A CA  
952  C C   . SER A 142 ? 0.2084 0.1763 0.2195 0.0131  0.0272  0.0497  196 SER A C   
953  O O   . SER A 142 ? 0.2266 0.2321 0.2433 0.0172  0.0470  0.0372  196 SER A O   
954  C CB  . SER A 142 ? 0.2127 0.1898 0.2425 -0.0040 -0.0002 0.0349  196 SER A CB  
955  O OG  . SER A 142 ? 0.2089 0.1830 0.2614 0.0109  0.0219  0.0416  196 SER A OG  
956  N N   . PHE A 143 ? 0.1982 0.1804 0.1906 0.0087  -0.0077 0.0445  197 PHE A N   
957  C CA  . PHE A 143 ? 0.2272 0.1682 0.2049 -0.0017 -0.0183 0.0445  197 PHE A CA  
958  C C   . PHE A 143 ? 0.1764 0.1877 0.2140 0.0132  -0.0377 0.0230  197 PHE A C   
959  O O   . PHE A 143 ? 0.1941 0.1634 0.2324 0.0085  -0.0052 0.0120  197 PHE A O   
960  C CB  . PHE A 143 ? 0.2373 0.1694 0.2098 0.0128  -0.0046 0.0209  197 PHE A CB  
961  C CG  . PHE A 143 ? 0.1875 0.1836 0.2380 0.0272  -0.0139 0.0122  197 PHE A CG  
962  C CD1 . PHE A 143 ? 0.1813 0.2176 0.2558 0.0145  0.0025  0.0273  197 PHE A CD1 
963  C CD2 . PHE A 143 ? 0.2029 0.2419 0.2389 -0.0105 -0.0214 -0.0099 197 PHE A CD2 
964  C CE1 . PHE A 143 ? 0.1985 0.2558 0.2365 0.0180  -0.0355 0.0219  197 PHE A CE1 
965  C CE2 . PHE A 143 ? 0.2098 0.2687 0.2495 -0.0095 -0.0336 0.0085  197 PHE A CE2 
966  C CZ  . PHE A 143 ? 0.1981 0.2442 0.2532 0.0134  -0.0307 0.0045  197 PHE A CZ  
967  N N   . ALA A 144 ? 0.1611 0.1857 0.2118 -0.0087 -0.0275 0.0269  198 ALA A N   
968  C CA  . ALA A 144 ? 0.1642 0.1883 0.2156 0.0082  -0.0201 0.0086  198 ALA A CA  
969  C C   . ALA A 144 ? 0.1605 0.2115 0.2359 -0.0222 -0.0113 0.0185  198 ALA A C   
970  O O   . ALA A 144 ? 0.1794 0.2027 0.2436 -0.0066 -0.0078 0.0154  198 ALA A O   
971  C CB  . ALA A 144 ? 0.1672 0.2285 0.2406 0.0602  -0.0180 0.0251  198 ALA A CB  
972  N N   . PRO A 145 ? 0.1735 0.1763 0.2156 -0.0173 0.0020  0.0082  199 PRO A N   
973  C CA  . PRO A 145 ? 0.1985 0.1905 0.2191 -0.0008 -0.0050 0.0490  199 PRO A CA  
974  C C   . PRO A 145 ? 0.1652 0.1769 0.2040 -0.0170 -0.0211 0.0268  199 PRO A C   
975  O O   . PRO A 145 ? 0.1721 0.1797 0.2024 -0.0149 -0.0211 0.0252  199 PRO A O   
976  C CB  . PRO A 145 ? 0.2163 0.1940 0.2453 0.0208  0.0448  0.0630  199 PRO A CB  
977  C CG  . PRO A 145 ? 0.2506 0.2008 0.2431 0.0142  0.0101  0.0217  199 PRO A CG  
978  C CD  . PRO A 145 ? 0.2257 0.2081 0.2272 -0.0352 0.0148  0.0241  199 PRO A CD  
979  N N   . ILE A 146 ? 0.1699 0.1863 0.1964 0.0070  -0.0112 0.0143  200 ILE A N   
980  C CA  . ILE A 146 ? 0.1613 0.2188 0.1820 -0.0247 -0.0209 0.0153  200 ILE A CA  
981  C C   . ILE A 146 ? 0.1529 0.2228 0.1693 -0.0186 -0.0022 -0.0059 200 ILE A C   
982  O O   . ILE A 146 ? 0.1747 0.2020 0.1844 -0.0188 -0.0010 -0.0057 200 ILE A O   
983  C CB  . ILE A 146 ? 0.1685 0.2078 0.1951 -0.0095 -0.0025 -0.0002 200 ILE A CB  
984  C CG1 . ILE A 146 ? 0.1783 0.2056 0.2062 0.0212  0.0077  0.0113  200 ILE A CG1 
985  C CG2 . ILE A 146 ? 0.1703 0.2460 0.2129 0.0038  0.0009  -0.0362 200 ILE A CG2 
986  C CD1 . ILE A 146 ? 0.1970 0.2409 0.2188 0.0499  0.0295  -0.0122 200 ILE A CD1 
987  N N   . ILE A 147 ? 0.1374 0.2009 0.1607 -0.0005 -0.0076 0.0158  201 ILE A N   
988  C CA  . ILE A 147 ? 0.1413 0.2292 0.1873 -0.0048 0.0144  0.0253  201 ILE A CA  
989  C C   . ILE A 147 ? 0.1683 0.2309 0.1767 -0.0232 -0.0065 0.0421  201 ILE A C   
990  O O   . ILE A 147 ? 0.1585 0.2157 0.2106 -0.0181 -0.0181 0.0304  201 ILE A O   
991  C CB  . ILE A 147 ? 0.1128 0.2082 0.2038 -0.0025 0.0150  0.0214  201 ILE A CB  
992  C CG1 . ILE A 147 ? 0.1520 0.2103 0.1987 0.0223  0.0046  0.0092  201 ILE A CG1 
993  C CG2 . ILE A 147 ? 0.1540 0.2320 0.2209 0.0077  0.0290  0.0461  201 ILE A CG2 
994  C CD1 . ILE A 147 ? 0.1965 0.1963 0.2148 0.0365  0.0346  -0.0187 201 ILE A CD1 
995  N N   . GLU A 148 ? 0.1871 0.1925 0.1866 -0.0174 -0.0221 0.0120  202 GLU A N   
996  C CA  . GLU A 148 ? 0.1801 0.2078 0.2089 0.0100  -0.0282 0.0248  202 GLU A CA  
997  C C   . GLU A 148 ? 0.1409 0.1980 0.2114 -0.0025 -0.0183 0.0280  202 GLU A C   
998  O O   . GLU A 148 ? 0.1817 0.1919 0.2208 -0.0221 -0.0094 0.0240  202 GLU A O   
999  C CB  . GLU A 148 ? 0.2046 0.2299 0.2156 0.0178  -0.0447 0.0425  202 GLU A CB  
1000 C CG  . GLU A 148 ? 0.2115 0.2755 0.2631 0.0736  -0.0162 0.0584  202 GLU A CG  
1001 C CD  . GLU A 148 ? 0.3161 0.3784 0.3237 0.1322  0.0208  0.0752  202 GLU A CD  
1002 O OE1 . GLU A 148 ? 0.3586 0.4180 0.3137 0.1228  0.0050  0.0946  202 GLU A OE1 
1003 O OE2 . GLU A 148 ? 0.3967 0.4272 0.3959 0.1732  0.0384  0.0806  202 GLU A OE2 
1004 N N   . ARG A 149 ? 0.1747 0.2037 0.2056 -0.0013 -0.0197 0.0178  203 ARG A N   
1005 C CA  . ARG A 149 ? 0.1762 0.1668 0.2237 0.0001  -0.0018 0.0265  203 ARG A CA  
1006 C C   . ARG A 149 ? 0.1766 0.1690 0.2032 -0.0056 -0.0171 0.0186  203 ARG A C   
1007 O O   . ARG A 149 ? 0.2003 0.1735 0.2070 -0.0171 -0.0041 0.0078  203 ARG A O   
1008 C CB  . ARG A 149 ? 0.1721 0.1686 0.2179 -0.0230 0.0001  0.0202  203 ARG A CB  
1009 C CG  . ARG A 149 ? 0.2343 0.1930 0.1879 0.0027  -0.0036 -0.0238 203 ARG A CG  
1010 C CD  . ARG A 149 ? 0.2895 0.2298 0.2194 0.0698  0.0079  -0.0442 203 ARG A CD  
1011 N NE  . ARG A 149 ? 0.3139 0.2442 0.2201 0.0560  0.0193  -0.0357 203 ARG A NE  
1012 C CZ  . ARG A 149 ? 0.3091 0.2591 0.2486 0.0617  -0.0445 -0.0466 203 ARG A CZ  
1013 N NH1 . ARG A 149 ? 0.2946 0.3183 0.2978 0.0420  -0.0592 -0.0394 203 ARG A NH1 
1014 N NH2 . ARG A 149 ? 0.3129 0.2870 0.2816 0.0639  -0.0376 -0.0383 203 ARG A NH2 
1015 N N   . ALA A 150 ? 0.1780 0.1997 0.1594 0.0004  -0.0101 0.0327  204 ALA A N   
1016 C CA  . ALA A 150 ? 0.1656 0.2347 0.1602 -0.0049 -0.0101 0.0384  204 ALA A CA  
1017 C C   . ALA A 150 ? 0.1644 0.2116 0.1976 0.0039  -0.0094 -0.0005 204 ALA A C   
1018 O O   . ALA A 150 ? 0.2100 0.1939 0.2040 -0.0076 -0.0196 0.0027  204 ALA A O   
1019 C CB  . ALA A 150 ? 0.1821 0.2290 0.1557 -0.0137 -0.0315 0.0387  204 ALA A CB  
1020 N N   . MET A 151 ? 0.1603 0.1946 0.2025 -0.0272 -0.0099 0.0088  205 MET A N   
1021 C CA  . MET A 151 ? 0.1914 0.1988 0.2171 -0.0187 -0.0230 0.0039  205 MET A CA  
1022 C C   . MET A 151 ? 0.2042 0.2155 0.2034 -0.0234 -0.0179 0.0228  205 MET A C   
1023 O O   . MET A 151 ? 0.2434 0.2174 0.2186 -0.0260 -0.0228 0.0289  205 MET A O   
1024 C CB  . MET A 151 ? 0.2068 0.2259 0.2417 0.0097  -0.0066 0.0158  205 MET A CB  
1025 C CG  . MET A 151 ? 0.2715 0.2596 0.2665 0.1067  -0.0264 0.0117  205 MET A CG  
1026 S SD  . MET A 151 ? 0.4710 0.3665 0.3041 0.0838  -0.0146 0.0074  205 MET A SD  
1027 C CE  . MET A 151 ? 0.2942 0.2433 0.3297 -0.0610 0.1295  0.0243  205 MET A CE  
1028 N N   . THR A 152 ? 0.1795 0.2170 0.1930 -0.0165 -0.0093 0.0309  206 THR A N   
1029 C CA  . THR A 152 ? 0.2310 0.2108 0.1954 -0.0372 -0.0078 0.0313  206 THR A CA  
1030 C C   . THR A 152 ? 0.1991 0.1912 0.1988 -0.0544 -0.0301 0.0166  206 THR A C   
1031 O O   . THR A 152 ? 0.2248 0.2114 0.2105 -0.0488 -0.0278 0.0140  206 THR A O   
1032 C CB  . THR A 152 ? 0.2476 0.2337 0.1794 -0.0222 -0.0320 0.0401  206 THR A CB  
1033 O OG1 . THR A 152 ? 0.2675 0.2753 0.2090 -0.0088 -0.0344 0.0499  206 THR A OG1 
1034 C CG2 . THR A 152 ? 0.2759 0.2536 0.1991 -0.0535 -0.0359 -0.0111 206 THR A CG2 
1035 N N   . ILE A 153 ? 0.2022 0.1857 0.1818 -0.0111 -0.0103 -0.0120 207 ILE A N   
1036 C CA  . ILE A 153 ? 0.1891 0.2036 0.1796 -0.0348 -0.0020 0.0098  207 ILE A CA  
1037 C C   . ILE A 153 ? 0.2043 0.1892 0.1844 -0.0371 0.0206  -0.0042 207 ILE A C   
1038 O O   . ILE A 153 ? 0.2704 0.1692 0.2124 -0.0554 0.0257  0.0091  207 ILE A O   
1039 C CB  . ILE A 153 ? 0.1818 0.2047 0.1982 -0.0292 -0.0043 0.0507  207 ILE A CB  
1040 C CG1 . ILE A 153 ? 0.1956 0.2241 0.2043 -0.0314 0.0089  0.0128  207 ILE A CG1 
1041 C CG2 . ILE A 153 ? 0.2028 0.2017 0.2411 0.0020  -0.0316 0.0426  207 ILE A CG2 
1042 C CD1 . ILE A 153 ? 0.1811 0.2470 0.2278 -0.0311 -0.0013 0.0253  207 ILE A CD1 
1043 N N   . VAL A 154 ? 0.1859 0.1984 0.2017 -0.0239 0.0057  -0.0119 208 VAL A N   
1044 C CA  . VAL A 154 ? 0.1981 0.2032 0.1984 -0.0395 0.0178  0.0013  208 VAL A CA  
1045 C C   . VAL A 154 ? 0.2107 0.1884 0.2134 -0.0352 0.0012  0.0224  208 VAL A C   
1046 O O   . VAL A 154 ? 0.2455 0.1794 0.2400 -0.0391 0.0092  0.0178  208 VAL A O   
1047 C CB  . VAL A 154 ? 0.2135 0.2107 0.1855 -0.0243 0.0152  -0.0018 208 VAL A CB  
1048 C CG1 . VAL A 154 ? 0.2864 0.2019 0.1596 -0.0199 0.0334  0.0420  208 VAL A CG1 
1049 C CG2 . VAL A 154 ? 0.2387 0.2201 0.2032 -0.0253 -0.0424 0.0018  208 VAL A CG2 
1050 N N   . GLU A 155 ? 0.1860 0.2280 0.2187 -0.0439 -0.0394 0.0327  209 GLU A N   
1051 C CA  . GLU A 155 ? 0.2166 0.2422 0.2354 -0.0361 -0.0652 0.0185  209 GLU A CA  
1052 C C   . GLU A 155 ? 0.2780 0.2074 0.2372 -0.0506 -0.0354 -0.0033 209 GLU A C   
1053 O O   . GLU A 155 ? 0.2809 0.2235 0.2470 -0.0587 -0.0239 -0.0054 209 GLU A O   
1054 C CB  . GLU A 155 ? 0.2292 0.2726 0.2692 -0.0575 -0.0847 0.0287  209 GLU A CB  
1055 C CG  . GLU A 155 ? 0.2415 0.2866 0.2830 -0.0744 -0.0716 0.0458  209 GLU A CG  
1056 C CD  . GLU A 155 ? 0.2705 0.3443 0.3111 -0.0623 -0.0751 0.0296  209 GLU A CD  
1057 O OE1 . GLU A 155 ? 0.2618 0.3274 0.3504 -0.0974 -0.0666 0.0425  209 GLU A OE1 
1058 O OE2 . GLU A 155 ? 0.2686 0.3864 0.3381 -0.0575 -0.0593 0.0142  209 GLU A OE2 
1059 N N   . GLU A 156 ? 0.2982 0.2128 0.2221 -0.0372 -0.0201 -0.0184 210 GLU A N   
1060 C CA  . GLU A 156 ? 0.3189 0.2404 0.2283 -0.0673 -0.0216 -0.0040 210 GLU A CA  
1061 C C   . GLU A 156 ? 0.3236 0.2299 0.2137 -0.0516 -0.0140 -0.0228 210 GLU A C   
1062 O O   . GLU A 156 ? 0.4085 0.2485 0.2393 -0.0536 -0.0110 -0.0324 210 GLU A O   
1063 C CB  . GLU A 156 ? 0.3745 0.3142 0.2277 -0.0457 0.0169  0.0169  210 GLU A CB  
1064 C CG  . GLU A 156 ? 0.4124 0.3602 0.2402 -0.0207 0.0051  0.0566  210 GLU A CG  
1065 C CD  . GLU A 156 ? 0.4438 0.4161 0.2843 -0.0021 0.0167  0.1011  210 GLU A CD  
1066 O OE1 . GLU A 156 ? 0.4680 0.4585 0.3259 0.0138  0.0287  0.1069  210 GLU A OE1 
1067 O OE2 . GLU A 156 ? 0.4881 0.4605 0.3155 -0.0121 0.0158  0.0959  210 GLU A OE2 
1068 N N   . SER A 157 ? 0.2890 0.2586 0.2102 -0.0316 -0.0043 -0.0019 211 SER A N   
1069 C CA  . SER A 157 ? 0.3089 0.2322 0.2121 -0.0172 -0.0059 -0.0069 211 SER A CA  
1070 C C   . SER A 157 ? 0.3117 0.2186 0.2393 -0.0006 0.0002  -0.0200 211 SER A C   
1071 O O   . SER A 157 ? 0.3434 0.2024 0.2869 -0.0255 -0.0221 -0.0178 211 SER A O   
1072 C CB  . SER A 157 ? 0.2618 0.2249 0.2157 -0.0090 0.0037  -0.0305 211 SER A CB  
1073 O OG  . SER A 157 ? 0.2558 0.2052 0.2222 -0.0431 0.0077  0.0036  211 SER A OG  
1074 N N   . GLY A 158 ? 0.2775 0.2185 0.2394 -0.0449 0.0129  -0.0148 212 GLY A N   
1075 C CA  . GLY A 158 ? 0.2859 0.2176 0.2698 -0.0616 0.0305  -0.0379 212 GLY A CA  
1076 C C   . GLY A 158 ? 0.2746 0.2299 0.2599 -0.0833 0.0292  -0.0108 212 GLY A C   
1077 O O   . GLY A 158 ? 0.3430 0.2711 0.2523 -0.0896 0.0506  0.0236  212 GLY A O   
1078 N N   . GLY A 159 ? 0.2397 0.2310 0.2337 -0.0641 0.0053  0.0016  213 GLY A N   
1079 C CA  . GLY A 159 ? 0.2309 0.2233 0.2368 -0.0314 0.0097  0.0151  213 GLY A CA  
1080 C C   . GLY A 159 ? 0.2312 0.1971 0.2501 -0.0239 0.0102  0.0296  213 GLY A C   
1081 O O   . GLY A 159 ? 0.2555 0.2210 0.2292 -0.0451 0.0220  0.0198  213 GLY A O   
1082 N N   . GLN A 160 ? 0.2344 0.1796 0.2522 -0.0212 0.0128  0.0248  214 GLN A N   
1083 C CA  . GLN A 160 ? 0.2510 0.1898 0.2319 -0.0072 0.0315  -0.0091 214 GLN A CA  
1084 C C   . GLN A 160 ? 0.2159 0.1767 0.2233 -0.0034 0.0122  0.0099  214 GLN A C   
1085 O O   . GLN A 160 ? 0.2176 0.1798 0.2164 -0.0126 0.0048  0.0284  214 GLN A O   
1086 C CB  . GLN A 160 ? 0.3071 0.1891 0.2655 0.0181  0.0315  -0.0158 214 GLN A CB  
1087 C CG  . GLN A 160 ? 0.3699 0.1888 0.2986 0.0557  0.0205  -0.0258 214 GLN A CG  
1088 C CD  . GLN A 160 ? 0.4224 0.3056 0.3594 0.0120  0.0013  -0.0680 214 GLN A CD  
1089 O OE1 . GLN A 160 ? 0.5045 0.3958 0.4052 0.0095  0.0168  -0.0407 214 GLN A OE1 
1090 N NE2 . GLN A 160 ? 0.4598 0.3361 0.4023 0.0064  -0.0117 -0.0873 214 GLN A NE2 
1091 N N   . TYR A 161 ? 0.2135 0.1979 0.1946 -0.0390 0.0020  -0.0015 215 TYR A N   
1092 C CA  . TYR A 161 ? 0.2333 0.1918 0.1723 -0.0460 0.0152  -0.0032 215 TYR A CA  
1093 C C   . TYR A 161 ? 0.2087 0.1779 0.1887 -0.0141 0.0088  0.0239  215 TYR A C   
1094 O O   . TYR A 161 ? 0.2306 0.1840 0.2061 -0.0131 0.0150  0.0244  215 TYR A O   
1095 C CB  . TYR A 161 ? 0.2436 0.1874 0.1753 -0.0296 0.0153  0.0179  215 TYR A CB  
1096 C CG  . TYR A 161 ? 0.2273 0.1903 0.1910 -0.0194 -0.0032 0.0150  215 TYR A CG  
1097 C CD1 . TYR A 161 ? 0.2778 0.1849 0.2128 -0.0256 0.0111  0.0108  215 TYR A CD1 
1098 C CD2 . TYR A 161 ? 0.2236 0.2259 0.1908 -0.0229 -0.0067 0.0195  215 TYR A CD2 
1099 C CE1 . TYR A 161 ? 0.2623 0.2169 0.1915 -0.0322 0.0218  0.0075  215 TYR A CE1 
1100 C CE2 . TYR A 161 ? 0.2592 0.2408 0.1995 -0.0237 -0.0125 0.0229  215 TYR A CE2 
1101 C CZ  . TYR A 161 ? 0.2528 0.2287 0.1794 -0.0534 -0.0085 0.0051  215 TYR A CZ  
1102 O OH  . TYR A 161 ? 0.2960 0.2403 0.2167 -0.0479 -0.0099 -0.0135 215 TYR A OH  
1103 N N   . HIS A 162 ? 0.2066 0.1860 0.1929 -0.0088 0.0026  0.0185  216 HIS A N   
1104 C CA  . HIS A 162 ? 0.2209 0.2078 0.1844 -0.0189 0.0171  0.0052  216 HIS A CA  
1105 C C   . HIS A 162 ? 0.1620 0.1888 0.1803 0.0116  0.0335  0.0106  216 HIS A C   
1106 O O   . HIS A 162 ? 0.1916 0.1990 0.1913 -0.0041 0.0135  0.0114  216 HIS A O   
1107 C CB  . HIS A 162 ? 0.2381 0.1960 0.1678 0.0148  0.0054  0.0171  216 HIS A CB  
1108 C CG  . HIS A 162 ? 0.2087 0.1718 0.1681 0.0040  0.0029  -0.0064 216 HIS A CG  
1109 N ND1 . HIS A 162 ? 0.2417 0.1927 0.1811 -0.0234 -0.0177 0.0072  216 HIS A ND1 
1110 C CD2 . HIS A 162 ? 0.2537 0.1954 0.1770 0.0196  0.0141  -0.0004 216 HIS A CD2 
1111 C CE1 . HIS A 162 ? 0.2547 0.2089 0.1759 0.0015  0.0408  0.0123  216 HIS A CE1 
1112 N NE2 . HIS A 162 ? 0.2795 0.1945 0.1715 0.0148  0.0245  0.0187  216 HIS A NE2 
1113 N N   . VAL A 163 ? 0.1878 0.1672 0.1913 -0.0196 0.0023  0.0193  217 VAL A N   
1114 C CA  . VAL A 163 ? 0.1551 0.2056 0.1746 -0.0098 0.0125  0.0162  217 VAL A CA  
1115 C C   . VAL A 163 ? 0.1428 0.1871 0.1829 0.0065  0.0181  0.0156  217 VAL A C   
1116 O O   . VAL A 163 ? 0.1724 0.2158 0.1934 0.0146  0.0238  0.0165  217 VAL A O   
1117 C CB  . VAL A 163 ? 0.2005 0.2134 0.1742 0.0082  -0.0152 0.0203  217 VAL A CB  
1118 C CG1 . VAL A 163 ? 0.2537 0.2092 0.2175 -0.0203 -0.0171 -0.0298 217 VAL A CG1 
1119 C CG2 . VAL A 163 ? 0.2380 0.2501 0.1674 0.0112  0.0320  0.0459  217 VAL A CG2 
1120 N N   . LEU A 164 ? 0.1732 0.1562 0.1946 0.0030  0.0085  0.0134  218 LEU A N   
1121 C CA  . LEU A 164 ? 0.1699 0.1645 0.1776 -0.0004 -0.0100 0.0193  218 LEU A CA  
1122 C C   . LEU A 164 ? 0.1706 0.1673 0.1798 -0.0106 0.0091  0.0058  218 LEU A C   
1123 O O   . LEU A 164 ? 0.1974 0.1835 0.1845 0.0153  0.0156  -0.0035 218 LEU A O   
1124 C CB  . LEU A 164 ? 0.1920 0.1566 0.1690 0.0017  -0.0004 0.0404  218 LEU A CB  
1125 C CG  . LEU A 164 ? 0.1835 0.1723 0.1603 0.0156  0.0084  0.0254  218 LEU A CG  
1126 C CD1 . LEU A 164 ? 0.2197 0.2021 0.1544 -0.0360 0.0318  -0.0067 218 LEU A CD1 
1127 C CD2 . LEU A 164 ? 0.2141 0.1892 0.1973 0.0476  -0.0069 0.0412  218 LEU A CD2 
1128 N N   . LEU A 165 ? 0.1703 0.1511 0.1916 -0.0295 -0.0146 0.0258  219 LEU A N   
1129 C CA  . LEU A 165 ? 0.1958 0.1463 0.1822 0.0118  -0.0133 0.0277  219 LEU A CA  
1130 C C   . LEU A 165 ? 0.1901 0.1622 0.1974 -0.0054 -0.0037 0.0352  219 LEU A C   
1131 O O   . LEU A 165 ? 0.2232 0.2064 0.2027 0.0125  0.0125  0.0194  219 LEU A O   
1132 C CB  . LEU A 165 ? 0.1756 0.2227 0.1875 0.0207  -0.0247 0.0177  219 LEU A CB  
1133 C CG  . LEU A 165 ? 0.1808 0.2346 0.2464 0.0091  -0.0443 0.0208  219 LEU A CG  
1134 C CD1 . LEU A 165 ? 0.2429 0.2789 0.2984 0.0323  -0.0631 -0.0506 219 LEU A CD1 
1135 C CD2 . LEU A 165 ? 0.1780 0.2623 0.2470 -0.0021 -0.0259 0.0053  219 LEU A CD2 
1136 N N   . ILE A 166 ? 0.1624 0.1632 0.1895 -0.0004 -0.0174 0.0309  220 ILE A N   
1137 C CA  . ILE A 166 ? 0.1613 0.1669 0.2068 -0.0119 -0.0233 0.0079  220 ILE A CA  
1138 C C   . ILE A 166 ? 0.1766 0.1602 0.2043 -0.0234 -0.0292 -0.0098 220 ILE A C   
1139 O O   . ILE A 166 ? 0.2193 0.2409 0.1901 -0.0274 -0.0115 -0.0319 220 ILE A O   
1140 C CB  . ILE A 166 ? 0.1810 0.1724 0.2068 -0.0191 -0.0380 0.0266  220 ILE A CB  
1141 C CG1 . ILE A 166 ? 0.1305 0.2021 0.2088 0.0016  -0.0242 -0.0007 220 ILE A CG1 
1142 C CG2 . ILE A 166 ? 0.1946 0.2084 0.2311 0.0030  -0.0004 0.0433  220 ILE A CG2 
1143 C CD1 . ILE A 166 ? 0.1882 0.2280 0.2422 0.0195  -0.0168 -0.0028 220 ILE A CD1 
1144 N N   . ILE A 167 ? 0.1784 0.1851 0.2176 -0.0395 -0.0182 -0.0057 221 ILE A N   
1145 C CA  . ILE A 167 ? 0.1646 0.1678 0.2277 0.0005  -0.0167 0.0104  221 ILE A CA  
1146 C C   . ILE A 167 ? 0.1683 0.1338 0.2124 -0.0096 -0.0102 0.0060  221 ILE A C   
1147 O O   . ILE A 167 ? 0.2042 0.2018 0.1961 -0.0123 -0.0157 -0.0006 221 ILE A O   
1148 C CB  . ILE A 167 ? 0.1974 0.1924 0.2272 0.0077  -0.0513 0.0359  221 ILE A CB  
1149 C CG1 . ILE A 167 ? 0.2114 0.2197 0.2493 0.0191  -0.0100 -0.0044 221 ILE A CG1 
1150 C CG2 . ILE A 167 ? 0.1912 0.2261 0.2369 -0.0079 -0.0643 0.0324  221 ILE A CG2 
1151 C CD1 . ILE A 167 ? 0.2855 0.2470 0.2803 0.0186  0.0271  0.0230  221 ILE A CD1 
1152 N N   . ALA A 168 ? 0.2045 0.1402 0.2360 -0.0161 -0.0260 0.0091  222 ALA A N   
1153 C CA  . ALA A 168 ? 0.2103 0.1458 0.2592 0.0214  -0.0300 0.0150  222 ALA A CA  
1154 C C   . ALA A 168 ? 0.2133 0.1646 0.2694 -0.0006 -0.0146 -0.0231 222 ALA A C   
1155 O O   . ALA A 168 ? 0.2287 0.1905 0.2809 -0.0051 -0.0430 -0.0111 222 ALA A O   
1156 C CB  . ALA A 168 ? 0.2204 0.2156 0.2742 0.0243  -0.0491 0.0048  222 ALA A CB  
1157 N N   . ASP A 169 ? 0.2727 0.1877 0.3046 0.0005  -0.0459 -0.0052 223 ASP A N   
1158 C CA  . ASP A 169 ? 0.2898 0.2040 0.3345 -0.0088 -0.0657 -0.0190 223 ASP A CA  
1159 C C   . ASP A 169 ? 0.2889 0.2355 0.3806 -0.0183 -0.0897 -0.0315 223 ASP A C   
1160 O O   . ASP A 169 ? 0.3336 0.2400 0.4066 -0.0232 -0.0687 -0.0486 223 ASP A O   
1161 C CB  . ASP A 169 ? 0.2754 0.2702 0.3301 -0.0482 -0.0424 0.0102  223 ASP A CB  
1162 C CG  . ASP A 169 ? 0.3272 0.3078 0.3370 -0.0636 -0.0176 0.0314  223 ASP A CG  
1163 O OD1 . ASP A 169 ? 0.3451 0.3715 0.3611 -0.0516 -0.0236 0.0603  223 ASP A OD1 
1164 O OD2 . ASP A 169 ? 0.3542 0.2872 0.3243 -0.0581 -0.0352 0.0116  223 ASP A OD2 
1165 N N   . GLY A 170 ? 0.3137 0.2045 0.4075 0.0530  -0.0861 -0.0355 224 GLY A N   
1166 C CA  . GLY A 170 ? 0.3109 0.2355 0.4403 0.0188  -0.0804 -0.0417 224 GLY A CA  
1167 C C   . GLY A 170 ? 0.2687 0.2277 0.4570 0.0625  -0.0699 -0.0268 224 GLY A C   
1168 O O   . GLY A 170 ? 0.3210 0.2295 0.4538 0.0331  -0.0690 -0.0235 224 GLY A O   
1169 N N   . GLN A 171 ? 0.2471 0.2802 0.4423 0.0461  -0.0881 0.0203  225 GLN A N   
1170 C CA  . GLN A 171 ? 0.3356 0.3059 0.4495 0.0560  -0.0673 0.0223  225 GLN A CA  
1171 C C   . GLN A 171 ? 0.2697 0.2687 0.3805 -0.0159 -0.0599 -0.0020 225 GLN A C   
1172 O O   . GLN A 171 ? 0.2991 0.2666 0.3652 0.0274  0.0215  0.0186  225 GLN A O   
1173 C CB  . GLN A 171 ? 0.4654 0.4126 0.5329 0.0593  -0.0509 0.0030  225 GLN A CB  
1174 C CG  . GLN A 171 ? 0.6401 0.5336 0.6579 0.0785  -0.0265 0.0080  225 GLN A CG  
1175 C CD  . GLN A 171 ? 0.7612 0.6634 0.7447 0.0481  -0.0131 0.0209  225 GLN A CD  
1176 O OE1 . GLN A 171 ? 0.8463 0.7497 0.8306 0.0213  -0.0063 0.0115  225 GLN A OE1 
1177 N NE2 . GLN A 171 ? 0.7547 0.6547 0.7564 0.0323  -0.0147 0.0212  225 GLN A NE2 
1178 N N   . VAL A 172 ? 0.2965 0.2499 0.3409 0.0134  -0.0044 0.0160  226 VAL A N   
1179 C CA  . VAL A 172 ? 0.3042 0.2255 0.3720 -0.0385 -0.0512 0.0453  226 VAL A CA  
1180 C C   . VAL A 172 ? 0.3099 0.2420 0.3736 0.0173  -0.0466 0.0239  226 VAL A C   
1181 O O   . VAL A 172 ? 0.3409 0.2627 0.3940 0.0202  -0.0432 0.0105  226 VAL A O   
1182 C CB  . VAL A 172 ? 0.3529 0.2479 0.4081 -0.0765 -0.1184 0.0577  226 VAL A CB  
1183 C CG1 . VAL A 172 ? 0.4154 0.3038 0.4361 -0.0762 -0.1255 0.0440  226 VAL A CG1 
1184 C CG2 . VAL A 172 ? 0.3748 0.2618 0.4123 -0.0290 -0.1029 0.0898  226 VAL A CG2 
1185 N N   . THR A 173 ? 0.2664 0.2419 0.3674 0.0445  -0.0313 0.0316  227 THR A N   
1186 C CA  . THR A 173 ? 0.2693 0.2343 0.3569 0.0275  -0.0281 0.0109  227 THR A CA  
1187 C C   . THR A 173 ? 0.2854 0.2208 0.3396 0.0258  0.0009  0.0106  227 THR A C   
1188 O O   . THR A 173 ? 0.2821 0.2450 0.3142 0.0610  0.0051  -0.0041 227 THR A O   
1189 C CB  . THR A 173 ? 0.2538 0.2085 0.3512 0.0562  -0.0125 0.0114  227 THR A CB  
1190 O OG1 . THR A 173 ? 0.2862 0.2276 0.3826 0.0369  0.0424  -0.0104 227 THR A OG1 
1191 C CG2 . THR A 173 ? 0.3671 0.2140 0.3469 0.0604  0.0190  0.0073  227 THR A CG2 
1192 N N   . ARG A 174 ? 0.3441 0.2123 0.3705 0.0268  0.0240  0.0239  228 ARG A N   
1193 C CA  . ARG A 174 ? 0.4018 0.2542 0.4188 0.0708  0.0297  0.0139  228 ARG A CA  
1194 C C   . ARG A 174 ? 0.3451 0.2664 0.4147 0.0525  0.0534  0.0272  228 ARG A C   
1195 O O   . ARG A 174 ? 0.3493 0.2823 0.3967 0.0401  0.0477  0.0368  228 ARG A O   
1196 C CB  . ARG A 174 ? 0.5286 0.3249 0.5052 0.0878  0.0004  0.0111  228 ARG A CB  
1197 C CG  . ARG A 174 ? 0.6787 0.4239 0.6065 0.0674  -0.0159 0.0110  228 ARG A CG  
1198 C CD  . ARG A 174 ? 0.7946 0.5189 0.6890 0.0597  -0.0227 0.0106  228 ARG A CD  
1199 N NE  . ARG A 174 ? 0.8752 0.5973 0.7835 0.0412  -0.0188 0.0223  228 ARG A NE  
1200 C CZ  . ARG A 174 ? 0.9306 0.6518 0.8436 0.0409  -0.0150 0.0259  228 ARG A CZ  
1201 N NH1 . ARG A 174 ? 0.9256 0.6808 0.8498 0.0562  -0.0178 0.0255  228 ARG A NH1 
1202 N NH2 . ARG A 174 ? 0.9678 0.6838 0.8567 0.0202  -0.0095 0.0219  228 ARG A NH2 
1203 N N   . SER A 175 ? 0.3132 0.2745 0.4446 0.0762  0.0050  0.0313  229 SER A N   
1204 C CA  . SER A 175 ? 0.3296 0.3264 0.4840 0.0677  0.0270  0.0417  229 SER A CA  
1205 C C   . SER A 175 ? 0.3684 0.2950 0.5109 0.0591  0.0575  0.0623  229 SER A C   
1206 O O   . SER A 175 ? 0.3651 0.2954 0.5058 0.0133  0.0766  0.0521  229 SER A O   
1207 C CB  . SER A 175 ? 0.3681 0.3956 0.5069 0.0616  0.0364  0.0419  229 SER A CB  
1208 O OG  . SER A 175 ? 0.4591 0.4469 0.5266 0.0098  0.0568  0.0188  229 SER A OG  
1209 N N   . VAL A 176 ? 0.4160 0.3097 0.5448 0.0701  0.0770  0.0474  230 VAL A N   
1210 C CA  . VAL A 176 ? 0.4949 0.3287 0.5976 0.0890  0.0593  0.0545  230 VAL A CA  
1211 C C   . VAL A 176 ? 0.5684 0.3728 0.6689 0.1001  0.0403  0.0317  230 VAL A C   
1212 O O   . VAL A 176 ? 0.5958 0.3804 0.6712 0.0840  0.0511  0.0128  230 VAL A O   
1213 C CB  . VAL A 176 ? 0.5020 0.3494 0.5879 0.0542  0.0425  0.0640  230 VAL A CB  
1214 C CG1 . VAL A 176 ? 0.5103 0.3373 0.5737 0.0341  0.0508  0.0666  230 VAL A CG1 
1215 C CG2 . VAL A 176 ? 0.5270 0.3669 0.5780 0.0368  0.0296  0.0790  230 VAL A CG2 
1216 N N   . ASP A 177 ? 0.6203 0.4062 0.7365 0.1525  0.0390  0.0260  231 ASP A N   
1217 C CA  . ASP A 177 ? 0.7013 0.4765 0.7838 0.1526  0.0349  0.0218  231 ASP A CA  
1218 C C   . ASP A 177 ? 0.7448 0.5281 0.8173 0.1259  0.0389  0.0063  231 ASP A C   
1219 O O   . ASP A 177 ? 0.7356 0.5309 0.8235 0.1049  0.0543  0.0059  231 ASP A O   
1220 C CB  . ASP A 177 ? 0.7669 0.5029 0.7923 0.1635  0.0319  0.0245  231 ASP A CB  
1221 C CG  . ASP A 177 ? 0.8170 0.5574 0.8299 0.1421  0.0246  0.0274  231 ASP A CG  
1222 O OD1 . ASP A 177 ? 0.8387 0.5739 0.8333 0.1307  0.0369  0.0284  231 ASP A OD1 
1223 O OD2 . ASP A 177 ? 0.8438 0.5800 0.8374 0.1427  0.0034  0.0275  231 ASP A OD2 
1224 N N   . THR A 178 ? 0.8044 0.5628 0.8453 0.1086  0.0388  -0.0011 232 THR A N   
1225 C CA  . THR A 178 ? 0.8458 0.6043 0.8774 0.1113  0.0335  -0.0051 232 THR A CA  
1226 C C   . THR A 178 ? 0.8522 0.6224 0.9039 0.1226  0.0413  -0.0151 232 THR A C   
1227 O O   . THR A 178 ? 0.8455 0.6285 0.9062 0.1199  0.0626  -0.0246 232 THR A O   
1228 C CB  . THR A 178 ? 0.8760 0.6232 0.8847 0.0990  0.0298  0.0069  232 THR A CB  
1229 O OG1 . THR A 178 ? 0.8861 0.6268 0.8825 0.0735  0.0356  0.0142  232 THR A OG1 
1230 C CG2 . THR A 178 ? 0.8763 0.6441 0.8877 0.1027  0.0276  0.0059  232 THR A CG2 
1231 N N   . ASP A 179 ? 0.8729 0.6308 0.9346 0.1350  0.0316  -0.0192 233 ASP A N   
1232 C CA  . ASP A 179 ? 0.9113 0.6582 0.9676 0.1397  0.0311  -0.0178 233 ASP A CA  
1233 C C   . ASP A 179 ? 0.9442 0.7139 0.9916 0.1303  0.0255  -0.0113 233 ASP A C   
1234 O O   . ASP A 179 ? 0.9579 0.7258 0.9828 0.1098  0.0262  -0.0082 233 ASP A O   
1235 C CB  . ASP A 179 ? 0.9052 0.6426 0.9673 0.1593  0.0371  -0.0299 233 ASP A CB  
1236 C CG  . ASP A 179 ? 0.9012 0.6323 0.9702 0.1740  0.0387  -0.0340 233 ASP A CG  
1237 O OD1 . ASP A 179 ? 0.8877 0.6372 0.9680 0.1748  0.0447  -0.0491 233 ASP A OD1 
1238 O OD2 . ASP A 179 ? 0.9135 0.6241 0.9710 0.1737  0.0414  -0.0382 233 ASP A OD2 
1239 N N   . ASN A 180 ? 0.9571 0.7531 1.0111 0.1440  0.0208  -0.0061 234 ASN A N   
1240 C CA  . ASN A 180 ? 0.9857 0.7812 1.0311 0.1540  0.0180  0.0062  234 ASN A CA  
1241 C C   . ASN A 180 ? 0.9804 0.7771 1.0282 0.1567  0.0189  0.0056  234 ASN A C   
1242 O O   . ASN A 180 ? 0.9702 0.7780 1.0365 0.1556  0.0249  0.0003  234 ASN A O   
1243 C CB  . ASN A 180 ? 1.0053 0.7996 1.0445 0.1639  0.0151  0.0155  234 ASN A CB  
1244 C CG  . ASN A 180 ? 1.0170 0.8095 1.0679 0.1710  0.0103  0.0228  234 ASN A CG  
1245 O OD1 . ASN A 180 ? 1.0312 0.8155 1.0812 0.1802  0.0039  0.0338  234 ASN A OD1 
1246 N ND2 . ASN A 180 ? 1.0184 0.8047 1.0776 0.1666  0.0111  0.0162  234 ASN A ND2 
1247 N N   . GLY A 181 ? 0.9783 0.7725 1.0069 0.1520  0.0118  0.0166  235 GLY A N   
1248 C CA  . GLY A 181 ? 0.9620 0.7573 0.9855 0.1516  0.0054  0.0240  235 GLY A CA  
1249 C C   . GLY A 181 ? 0.9443 0.7436 0.9665 0.1468  -0.0009 0.0257  235 GLY A C   
1250 O O   . GLY A 181 ? 0.9875 0.7658 0.9813 0.1198  -0.0141 0.0251  235 GLY A O   
1251 N N   . GLY A 182 ? 0.8587 0.7028 0.9203 0.1729  0.0144  0.0238  236 GLY A N   
1252 C CA  . GLY A 182 ? 0.7919 0.6468 0.8760 0.1898  0.0389  0.0228  236 GLY A CA  
1253 C C   . GLY A 182 ? 0.7190 0.5809 0.8291 0.2239  0.0536  0.0134  236 GLY A C   
1254 O O   . GLY A 182 ? 0.7232 0.5700 0.8395 0.2175  0.0545  0.0009  236 GLY A O   
1255 N N   . PHE A 183 ? 0.6478 0.5384 0.7613 0.2147  0.0545  0.0410  237 PHE A N   
1256 C CA  . PHE A 183 ? 0.5795 0.4876 0.6819 0.2241  0.0739  0.0435  237 PHE A CA  
1257 C C   . PHE A 183 ? 0.4895 0.3909 0.6023 0.2282  0.0676  0.0622  237 PHE A C   
1258 O O   . PHE A 183 ? 0.4771 0.4394 0.5940 0.2221  0.0969  0.0503  237 PHE A O   
1259 C CB  . PHE A 183 ? 0.6038 0.5388 0.6831 0.1717  0.0738  0.0337  237 PHE A CB  
1260 C CG  . PHE A 183 ? 0.6573 0.5809 0.6929 0.1272  0.0436  0.0359  237 PHE A CG  
1261 C CD1 . PHE A 183 ? 0.6723 0.6200 0.6930 0.0921  0.0177  0.0479  237 PHE A CD1 
1262 C CD2 . PHE A 183 ? 0.6823 0.5815 0.6980 0.1255  0.0297  0.0334  237 PHE A CD2 
1263 C CE1 . PHE A 183 ? 0.6850 0.6291 0.6974 0.0840  0.0054  0.0461  237 PHE A CE1 
1264 C CE2 . PHE A 183 ? 0.6808 0.6027 0.6962 0.1132  0.0266  0.0326  237 PHE A CE2 
1265 C CZ  . PHE A 183 ? 0.6843 0.6162 0.6954 0.0983  0.0151  0.0393  237 PHE A CZ  
1266 N N   . SER A 184 ? 0.4271 0.2800 0.5361 0.1730  0.0749  0.0593  238 SER A N   
1267 C CA  . SER A 184 ? 0.3608 0.2249 0.4593 0.1112  0.0333  0.0711  238 SER A CA  
1268 C C   . SER A 184 ? 0.3131 0.2199 0.4186 0.0695  -0.0019 0.0786  238 SER A C   
1269 O O   . SER A 184 ? 0.2755 0.2361 0.3940 0.0513  0.0340  0.0749  238 SER A O   
1270 C CB  . SER A 184 ? 0.3605 0.2339 0.4166 0.0764  0.0120  0.0921  238 SER A CB  
1271 O OG  . SER A 184 ? 0.3730 0.2096 0.3660 0.0605  0.0143  0.0794  238 SER A OG  
1272 N N   . PRO A 185 ? 0.3137 0.2441 0.4159 0.0521  -0.0444 0.0830  239 PRO A N   
1273 C CA  . PRO A 185 ? 0.2913 0.2457 0.3983 0.0259  -0.0255 0.0889  239 PRO A CA  
1274 C C   . PRO A 185 ? 0.2523 0.2427 0.3707 0.0107  -0.0016 0.0742  239 PRO A C   
1275 O O   . PRO A 185 ? 0.2680 0.2521 0.3680 0.0029  -0.0015 0.0798  239 PRO A O   
1276 C CB  . PRO A 185 ? 0.3206 0.2571 0.3864 0.0002  -0.0487 0.1010  239 PRO A CB  
1277 C CG  . PRO A 185 ? 0.3741 0.2552 0.3985 -0.0091 -0.0582 0.0821  239 PRO A CG  
1278 C CD  . PRO A 185 ? 0.3544 0.2301 0.4011 0.0084  -0.0648 0.0858  239 PRO A CD  
1279 N N   . GLN A 186 ? 0.2539 0.2413 0.3441 0.0330  -0.0005 0.0874  240 GLN A N   
1280 C CA  . GLN A 186 ? 0.2276 0.2320 0.3033 0.0539  0.0073  0.0884  240 GLN A CA  
1281 C C   . GLN A 186 ? 0.2294 0.2358 0.3028 0.0533  0.0094  0.0811  240 GLN A C   
1282 O O   . GLN A 186 ? 0.2191 0.2336 0.2850 0.0384  0.0019  0.0790  240 GLN A O   
1283 C CB  . GLN A 186 ? 0.2381 0.2405 0.2862 0.0376  0.0160  0.0775  240 GLN A CB  
1284 C CG  . GLN A 186 ? 0.2964 0.2124 0.2831 0.0231  0.0292  0.1029  240 GLN A CG  
1285 C CD  . GLN A 186 ? 0.2824 0.2362 0.2965 0.0262  0.0719  0.0718  240 GLN A CD  
1286 O OE1 . GLN A 186 ? 0.3074 0.2697 0.2912 0.0237  0.0405  0.0547  240 GLN A OE1 
1287 N NE2 . GLN A 186 ? 0.3086 0.2731 0.3083 0.0551  0.0335  0.0670  240 GLN A NE2 
1288 N N   . GLU A 187 ? 0.2766 0.2234 0.3195 0.0587  0.0350  0.0666  241 GLU A N   
1289 C CA  . GLU A 187 ? 0.2819 0.2363 0.3393 0.0648  0.0476  0.0297  241 GLU A CA  
1290 C C   . GLU A 187 ? 0.2477 0.2454 0.3548 0.0782  0.0219  0.0607  241 GLU A C   
1291 O O   . GLU A 187 ? 0.2476 0.2244 0.3494 0.0723  0.0399  0.0655  241 GLU A O   
1292 C CB  . GLU A 187 ? 0.3593 0.1941 0.3608 0.0275  0.0443  -0.0107 241 GLU A CB  
1293 C CG  . GLU A 187 ? 0.4102 0.2347 0.3909 0.0536  0.0399  0.0020  241 GLU A CG  
1294 C CD  . GLU A 187 ? 0.4502 0.2551 0.4393 0.1042  0.0129  0.0003  241 GLU A CD  
1295 O OE1 . GLU A 187 ? 0.5013 0.2774 0.4336 0.1117  0.0232  0.0034  241 GLU A OE1 
1296 O OE2 . GLU A 187 ? 0.4713 0.2922 0.4758 0.0458  -0.0068 -0.0065 241 GLU A OE2 
1297 N N   . GLN A 188 ? 0.2103 0.2837 0.3824 0.0488  0.0254  0.0656  242 GLN A N   
1298 C CA  . GLN A 188 ? 0.2138 0.2607 0.4139 0.0561  0.0192  0.0945  242 GLN A CA  
1299 C C   . GLN A 188 ? 0.2325 0.2371 0.3866 0.0501  0.0313  0.0898  242 GLN A C   
1300 O O   . GLN A 188 ? 0.2614 0.2199 0.3909 0.0638  0.0388  0.0831  242 GLN A O   
1301 C CB  . GLN A 188 ? 0.2350 0.2879 0.4749 0.0564  0.0180  0.1137  242 GLN A CB  
1302 C CG  . GLN A 188 ? 0.2702 0.3384 0.5175 0.0938  0.0512  0.0831  242 GLN A CG  
1303 C CD  . GLN A 188 ? 0.3595 0.3960 0.5533 0.0961  0.1236  0.0740  242 GLN A CD  
1304 O OE1 . GLN A 188 ? 0.4625 0.4200 0.5871 0.1211  0.1304  0.0420  242 GLN A OE1 
1305 N NE2 . GLN A 188 ? 0.3458 0.4145 0.5542 0.0519  0.1328  0.0756  242 GLN A NE2 
1306 N N   . GLN A 189 ? 0.2137 0.2510 0.3674 0.0345  0.0081  0.0999  243 GLN A N   
1307 C CA  . GLN A 189 ? 0.2466 0.2765 0.3492 0.0414  -0.0198 0.1040  243 GLN A CA  
1308 C C   . GLN A 189 ? 0.1990 0.2387 0.3089 0.0301  0.0110  0.0842  243 GLN A C   
1309 O O   . GLN A 189 ? 0.2175 0.2441 0.2937 0.0265  0.0245  0.1059  243 GLN A O   
1310 C CB  . GLN A 189 ? 0.2972 0.3409 0.3565 0.0555  -0.0678 0.1263  243 GLN A CB  
1311 C CG  . GLN A 189 ? 0.3440 0.4244 0.4077 0.0813  -0.1028 0.1663  243 GLN A CG  
1312 C CD  . GLN A 189 ? 0.4227 0.5288 0.4847 0.1091  -0.1323 0.1460  243 GLN A CD  
1313 O OE1 . GLN A 189 ? 0.4850 0.5928 0.5253 0.0880  -0.1420 0.1471  243 GLN A OE1 
1314 N NE2 . GLN A 189 ? 0.4630 0.5817 0.5175 0.0993  -0.1155 0.1225  243 GLN A NE2 
1315 N N   . THR A 190 ? 0.2001 0.2421 0.2955 0.0437  0.0066  0.0551  244 THR A N   
1316 C CA  . THR A 190 ? 0.1687 0.2437 0.2875 0.0604  0.0085  0.0514  244 THR A CA  
1317 C C   . THR A 190 ? 0.1898 0.2235 0.2908 0.0476  0.0407  0.0269  244 THR A C   
1318 O O   . THR A 190 ? 0.2067 0.2146 0.2915 0.0301  0.0172  0.0475  244 THR A O   
1319 C CB  . THR A 190 ? 0.1525 0.2242 0.2694 0.0368  0.0207  0.0294  244 THR A CB  
1320 O OG1 . THR A 190 ? 0.1720 0.2208 0.2727 0.0291  0.0069  0.0247  244 THR A OG1 
1321 C CG2 . THR A 190 ? 0.2564 0.2151 0.2611 0.0441  -0.0061 0.0476  244 THR A CG2 
1322 N N   . ILE A 191 ? 0.1859 0.2400 0.2920 0.0421  0.0627  0.0217  245 ILE A N   
1323 C CA  . ILE A 191 ? 0.1963 0.2384 0.3139 0.0420  0.0546  0.0295  245 ILE A CA  
1324 C C   . ILE A 191 ? 0.1818 0.2518 0.3104 0.0282  0.0287  0.0667  245 ILE A C   
1325 O O   . ILE A 191 ? 0.1888 0.2552 0.3167 0.0257  0.0252  0.0514  245 ILE A O   
1326 C CB  . ILE A 191 ? 0.2424 0.2333 0.3441 0.0225  0.1090  0.0298  245 ILE A CB  
1327 C CG1 . ILE A 191 ? 0.3209 0.2380 0.3413 0.0081  0.1068  0.0287  245 ILE A CG1 
1328 C CG2 . ILE A 191 ? 0.2410 0.2468 0.3660 0.0299  0.1213  0.0258  245 ILE A CG2 
1329 C CD1 . ILE A 191 ? 0.3744 0.2586 0.3403 0.0533  0.1362  0.0131  245 ILE A CD1 
1330 N N   . ASP A 192 ? 0.1752 0.2555 0.3035 0.0287  0.0125  0.0642  246 ASP A N   
1331 C CA  . ASP A 192 ? 0.1919 0.2761 0.3174 0.0334  -0.0094 0.0754  246 ASP A CA  
1332 C C   . ASP A 192 ? 0.1895 0.2561 0.3016 0.0587  0.0134  0.0745  246 ASP A C   
1333 O O   . ASP A 192 ? 0.1954 0.2440 0.3036 0.0319  0.0090  0.0598  246 ASP A O   
1334 C CB  . ASP A 192 ? 0.2350 0.3184 0.3551 0.0695  -0.0340 0.1084  246 ASP A CB  
1335 C CG  . ASP A 192 ? 0.3463 0.4057 0.3990 0.0332  -0.0230 0.0988  246 ASP A CG  
1336 O OD1 . ASP A 192 ? 0.3371 0.4324 0.4221 0.0515  0.0005  0.0661  246 ASP A OD1 
1337 O OD2 . ASP A 192 ? 0.4146 0.4318 0.4473 0.0367  -0.0386 0.1217  246 ASP A OD2 
1338 N N   . ALA A 193 ? 0.1821 0.2438 0.2757 0.0535  -0.0045 0.0650  247 ALA A N   
1339 C CA  . ALA A 193 ? 0.1742 0.2315 0.2701 0.0592  0.0190  0.0664  247 ALA A CA  
1340 C C   . ALA A 193 ? 0.1850 0.2377 0.2500 0.0483  0.0099  0.0388  247 ALA A C   
1341 O O   . ALA A 193 ? 0.1860 0.2091 0.2578 0.0199  -0.0044 0.0529  247 ALA A O   
1342 C CB  . ALA A 193 ? 0.1408 0.2853 0.2508 0.0355  0.0078  0.0487  247 ALA A CB  
1343 N N   . ILE A 194 ? 0.1930 0.2331 0.2332 0.0318  -0.0026 0.0687  248 ILE A N   
1344 C CA  . ILE A 194 ? 0.1773 0.2289 0.2414 0.0370  0.0106  0.0463  248 ILE A CA  
1345 C C   . ILE A 194 ? 0.2007 0.2019 0.2443 0.0697  0.0185  0.0737  248 ILE A C   
1346 O O   . ILE A 194 ? 0.1894 0.2050 0.2623 0.0398  -0.0127 0.0382  248 ILE A O   
1347 C CB  . ILE A 194 ? 0.1810 0.2265 0.2483 0.0003  0.0174  0.0143  248 ILE A CB  
1348 C CG1 . ILE A 194 ? 0.1921 0.2081 0.2647 -0.0118 0.0101  0.0082  248 ILE A CG1 
1349 C CG2 . ILE A 194 ? 0.2133 0.2613 0.2695 0.0069  -0.0025 0.0132  248 ILE A CG2 
1350 C CD1 . ILE A 194 ? 0.1970 0.2144 0.2934 0.0236  0.0167  -0.0274 248 ILE A CD1 
1351 N N   . VAL A 195 ? 0.1909 0.2254 0.2457 0.0232  0.0412  0.0367  249 VAL A N   
1352 C CA  . VAL A 195 ? 0.1893 0.2545 0.2725 0.0386  0.0301  0.0398  249 VAL A CA  
1353 C C   . VAL A 195 ? 0.1876 0.2414 0.2606 0.0040  0.0231  0.0412  249 VAL A C   
1354 O O   . VAL A 195 ? 0.1835 0.2408 0.2681 0.0154  0.0121  0.0392  249 VAL A O   
1355 C CB  . VAL A 195 ? 0.1707 0.2501 0.2932 0.0356  0.0218  0.0221  249 VAL A CB  
1356 C CG1 . VAL A 195 ? 0.1465 0.2657 0.3105 0.0097  0.0173  0.0196  249 VAL A CG1 
1357 C CG2 . VAL A 195 ? 0.2049 0.2704 0.2984 0.0424  0.0314  0.0351  249 VAL A CG2 
1358 N N   . ARG A 196 ? 0.1629 0.2365 0.2788 0.0150  0.0186  0.0294  250 ARG A N   
1359 C CA  . ARG A 196 ? 0.1672 0.2676 0.2923 0.0264  0.0386  0.0434  250 ARG A CA  
1360 C C   . ARG A 196 ? 0.1736 0.2541 0.2762 -0.0222 -0.0066 0.0179  250 ARG A C   
1361 O O   . ARG A 196 ? 0.1802 0.2574 0.2785 -0.0346 0.0008  -0.0080 250 ARG A O   
1362 C CB  . ARG A 196 ? 0.1790 0.3587 0.3573 0.0826  0.0943  0.1205  250 ARG A CB  
1363 C CG  . ARG A 196 ? 0.3270 0.4362 0.3974 0.0674  0.0823  0.1012  250 ARG A CG  
1364 C CD  . ARG A 196 ? 0.4424 0.5489 0.4816 0.0263  -0.0047 0.0521  250 ARG A CD  
1365 N NE  . ARG A 196 ? 0.5633 0.6888 0.5293 0.0052  0.0054  0.0351  250 ARG A NE  
1366 C CZ  . ARG A 196 ? 0.5706 0.6987 0.5832 0.0568  0.0261  0.0583  250 ARG A CZ  
1367 N NH1 . ARG A 196 ? 0.5982 0.6836 0.6101 0.1014  0.0164  0.0922  250 ARG A NH1 
1368 N NH2 . ARG A 196 ? 0.5524 0.6899 0.6180 0.0889  0.0362  0.0539  250 ARG A NH2 
1369 N N   . ALA A 197 ? 0.1485 0.2421 0.2602 0.0110  -0.0124 0.0331  251 ALA A N   
1370 C CA  . ALA A 197 ? 0.1603 0.2279 0.2908 0.0100  0.0103  0.0429  251 ALA A CA  
1371 C C   . ALA A 197 ? 0.1666 0.2243 0.2823 -0.0008 0.0247  0.0482  251 ALA A C   
1372 O O   . ALA A 197 ? 0.1819 0.2131 0.2782 0.0003  0.0040  0.0405  251 ALA A O   
1373 C CB  . ALA A 197 ? 0.1621 0.2096 0.2858 -0.0007 0.0223  0.0551  251 ALA A CB  
1374 N N   . SER A 198 ? 0.1640 0.2183 0.2753 -0.0008 0.0190  0.0398  252 SER A N   
1375 C CA  . SER A 198 ? 0.2090 0.2198 0.2889 0.0222  0.0282  0.0246  252 SER A CA  
1376 C C   . SER A 198 ? 0.1948 0.2671 0.2771 -0.0094 0.0175  0.0228  252 SER A C   
1377 O O   . SER A 198 ? 0.2702 0.2565 0.2768 -0.0143 0.0073  0.0340  252 SER A O   
1378 C CB  . SER A 198 ? 0.2020 0.2555 0.3080 0.0465  0.0350  0.0143  252 SER A CB  
1379 O OG  . SER A 198 ? 0.2201 0.2672 0.2988 0.0299  0.0282  0.0193  252 SER A OG  
1380 N N   . GLU A 199 ? 0.1638 0.2724 0.2782 -0.0038 -0.0036 0.0038  253 GLU A N   
1381 C CA  . GLU A 199 ? 0.1885 0.2692 0.3050 -0.0197 -0.0238 0.0313  253 GLU A CA  
1382 C C   . GLU A 199 ? 0.1867 0.2725 0.2869 0.0016  0.0030  0.0465  253 GLU A C   
1383 O O   . GLU A 199 ? 0.2296 0.2928 0.3052 -0.0229 -0.0019 0.0451  253 GLU A O   
1384 C CB  . GLU A 199 ? 0.1847 0.3238 0.3824 -0.0232 -0.0626 0.0334  253 GLU A CB  
1385 C CG  . GLU A 199 ? 0.2595 0.4379 0.4449 0.0273  -0.0875 0.0314  253 GLU A CG  
1386 C CD  . GLU A 199 ? 0.3865 0.5698 0.5172 0.0504  -0.1249 0.0138  253 GLU A CD  
1387 O OE1 . GLU A 199 ? 0.3816 0.5918 0.5237 0.0079  -0.1544 -0.0127 253 GLU A OE1 
1388 O OE2 . GLU A 199 ? 0.4835 0.6327 0.5785 0.0651  -0.1021 0.0215  253 GLU A OE2 
1389 N N   . TYR A 200 ? 0.1705 0.2647 0.2486 -0.0029 0.0277  0.0469  254 TYR A N   
1390 C CA  . TYR A 200 ? 0.2125 0.2509 0.2131 0.0030  -0.0070 0.0265  254 TYR A CA  
1391 C C   . TYR A 200 ? 0.1926 0.2336 0.1958 -0.0316 0.0014  0.0176  254 TYR A C   
1392 O O   . TYR A 200 ? 0.2119 0.2346 0.2177 -0.0351 0.0090  -0.0084 254 TYR A O   
1393 C CB  . TYR A 200 ? 0.1838 0.2539 0.1982 -0.0100 0.0098  0.0413  254 TYR A CB  
1394 C CG  . TYR A 200 ? 0.2275 0.2479 0.2215 -0.0086 -0.0120 0.0417  254 TYR A CG  
1395 C CD1 . TYR A 200 ? 0.2229 0.2398 0.2250 0.0084  0.0068  0.0876  254 TYR A CD1 
1396 C CD2 . TYR A 200 ? 0.2656 0.2523 0.2222 -0.0211 -0.0007 0.0323  254 TYR A CD2 
1397 C CE1 . TYR A 200 ? 0.2171 0.2465 0.2221 -0.0008 0.0085  0.0758  254 TYR A CE1 
1398 C CE2 . TYR A 200 ? 0.2910 0.2627 0.2230 -0.0157 -0.0342 0.0190  254 TYR A CE2 
1399 C CZ  . TYR A 200 ? 0.2682 0.2819 0.2234 0.0212  -0.0258 0.0335  254 TYR A CZ  
1400 O OH  . TYR A 200 ? 0.3213 0.3204 0.2703 -0.0174 -0.0614 0.0234  254 TYR A OH  
1401 N N   . PRO A 201 ? 0.2133 0.2118 0.2010 -0.0143 -0.0151 0.0150  255 PRO A N   
1402 C CA  . PRO A 201 ? 0.1958 0.2073 0.2081 -0.0388 -0.0175 0.0313  255 PRO A CA  
1403 C C   . PRO A 201 ? 0.1799 0.2145 0.2207 0.0073  0.0087  0.0204  255 PRO A C   
1404 O O   . PRO A 201 ? 0.2027 0.2021 0.2080 -0.0108 0.0208  0.0141  255 PRO A O   
1405 C CB  . PRO A 201 ? 0.2371 0.2144 0.1923 -0.0087 -0.0206 0.0352  255 PRO A CB  
1406 C CG  . PRO A 201 ? 0.2394 0.2294 0.1947 0.0127  -0.0129 0.0331  255 PRO A CG  
1407 C CD  . PRO A 201 ? 0.2384 0.2042 0.2258 0.0072  -0.0140 0.0210  255 PRO A CD  
1408 N N   . LEU A 202 ? 0.1863 0.2018 0.2321 -0.0374 0.0197  0.0181  256 LEU A N   
1409 C CA  . LEU A 202 ? 0.2135 0.2031 0.2049 -0.0093 -0.0163 0.0061  256 LEU A CA  
1410 C C   . LEU A 202 ? 0.1850 0.2105 0.2028 -0.0023 0.0012  0.0009  256 LEU A C   
1411 O O   . LEU A 202 ? 0.1970 0.2244 0.2396 0.0249  0.0224  -0.0159 256 LEU A O   
1412 C CB  . LEU A 202 ? 0.2318 0.1943 0.2011 0.0093  0.0005  0.0094  256 LEU A CB  
1413 C CG  . LEU A 202 ? 0.2264 0.2069 0.2110 0.0056  0.0250  0.0419  256 LEU A CG  
1414 C CD1 . LEU A 202 ? 0.1943 0.2287 0.2198 -0.0015 0.0252  0.0033  256 LEU A CD1 
1415 C CD2 . LEU A 202 ? 0.3096 0.2645 0.1981 0.0145  0.0299  0.0185  256 LEU A CD2 
1416 N N   . SER A 203 ? 0.2065 0.1824 0.2123 -0.0074 -0.0032 0.0027  257 SER A N   
1417 C CA  . SER A 203 ? 0.2187 0.1966 0.1963 0.0102  0.0188  -0.0017 257 SER A CA  
1418 C C   . SER A 203 ? 0.1617 0.1907 0.1933 -0.0113 0.0092  0.0160  257 SER A C   
1419 O O   . SER A 203 ? 0.2165 0.1984 0.2323 0.0099  0.0528  0.0031  257 SER A O   
1420 C CB  . SER A 203 ? 0.2025 0.2213 0.2079 0.0096  -0.0004 0.0182  257 SER A CB  
1421 O OG  . SER A 203 ? 0.2575 0.2692 0.2067 -0.0445 0.0282  0.0226  257 SER A OG  
1422 N N   . ILE A 204 ? 0.1949 0.1989 0.1643 -0.0108 0.0366  0.0125  258 ILE A N   
1423 C CA  . ILE A 204 ? 0.2340 0.1887 0.1685 0.0163  0.0310  0.0027  258 ILE A CA  
1424 C C   . ILE A 204 ? 0.2281 0.2068 0.1540 0.0274  0.0550  -0.0326 258 ILE A C   
1425 O O   . ILE A 204 ? 0.1972 0.2298 0.2022 0.0008  0.0155  -0.0480 258 ILE A O   
1426 C CB  . ILE A 204 ? 0.1909 0.1836 0.2137 -0.0036 0.0096  0.0062  258 ILE A CB  
1427 C CG1 . ILE A 204 ? 0.1707 0.2197 0.2437 0.0030  -0.0073 -0.0055 258 ILE A CG1 
1428 C CG2 . ILE A 204 ? 0.2188 0.2023 0.2467 -0.0194 0.0211  0.0194  258 ILE A CG2 
1429 C CD1 . ILE A 204 ? 0.1767 0.2280 0.2577 -0.0034 -0.0119 0.0154  258 ILE A CD1 
1430 N N   . VAL A 205 ? 0.1923 0.1910 0.1760 -0.0110 0.0078  -0.0135 259 VAL A N   
1431 C CA  . VAL A 205 ? 0.1977 0.2159 0.1957 -0.0138 0.0004  -0.0102 259 VAL A CA  
1432 C C   . VAL A 205 ? 0.1730 0.2089 0.1923 -0.0234 0.0194  0.0016  259 VAL A C   
1433 O O   . VAL A 205 ? 0.2302 0.2120 0.1799 -0.0358 0.0283  -0.0067 259 VAL A O   
1434 C CB  . VAL A 205 ? 0.1748 0.2343 0.2049 -0.0386 -0.0296 0.0336  259 VAL A CB  
1435 C CG1 . VAL A 205 ? 0.2028 0.2688 0.2317 -0.0554 -0.0299 0.0129  259 VAL A CG1 
1436 C CG2 . VAL A 205 ? 0.2079 0.2622 0.2322 -0.0396 -0.0302 0.0242  259 VAL A CG2 
1437 N N   . LEU A 206 ? 0.2023 0.1994 0.2085 -0.0239 -0.0026 -0.0017 260 LEU A N   
1438 C CA  . LEU A 206 ? 0.1787 0.2197 0.2157 0.0024  0.0025  0.0023  260 LEU A CA  
1439 C C   . LEU A 206 ? 0.1984 0.2015 0.2085 0.0070  0.0003  -0.0436 260 LEU A C   
1440 O O   . LEU A 206 ? 0.2418 0.2260 0.1769 -0.0035 0.0106  -0.0508 260 LEU A O   
1441 C CB  . LEU A 206 ? 0.2483 0.2207 0.2138 0.0193  0.0296  0.0289  260 LEU A CB  
1442 C CG  . LEU A 206 ? 0.2821 0.2043 0.2366 0.0332  0.0265  -0.0121 260 LEU A CG  
1443 C CD1 . LEU A 206 ? 0.2832 0.2330 0.2246 0.0565  0.0235  -0.0157 260 LEU A CD1 
1444 C CD2 . LEU A 206 ? 0.2788 0.2200 0.2436 0.0586  0.0200  -0.0068 260 LEU A CD2 
1445 N N   . VAL A 207 ? 0.1943 0.2025 0.2251 0.0042  -0.0428 -0.0010 261 VAL A N   
1446 C CA  . VAL A 207 ? 0.2067 0.2078 0.2302 0.0012  -0.0080 0.0014  261 VAL A CA  
1447 C C   . VAL A 207 ? 0.2104 0.1981 0.2034 -0.0211 -0.0181 -0.0051 261 VAL A C   
1448 O O   . VAL A 207 ? 0.2392 0.2165 0.1948 -0.0091 0.0055  -0.0100 261 VAL A O   
1449 C CB  . VAL A 207 ? 0.1875 0.2018 0.2679 -0.0115 -0.0040 0.0135  261 VAL A CB  
1450 C CG1 . VAL A 207 ? 0.2022 0.2316 0.2569 -0.0099 -0.0228 -0.0051 261 VAL A CG1 
1451 C CG2 . VAL A 207 ? 0.1795 0.1894 0.3012 -0.0202 0.0178  0.0050  261 VAL A CG2 
1452 N N   . GLY A 208 ? 0.2227 0.1941 0.2264 -0.0287 -0.0345 -0.0126 262 GLY A N   
1453 C CA  . GLY A 208 ? 0.2265 0.1949 0.2355 -0.0229 -0.0466 0.0076  262 GLY A CA  
1454 C C   . GLY A 208 ? 0.2383 0.1974 0.2286 -0.0031 -0.0460 -0.0254 262 GLY A C   
1455 O O   . GLY A 208 ? 0.2482 0.2529 0.2212 -0.0084 -0.0591 0.0172  262 GLY A O   
1456 N N   . VAL A 209 ? 0.2203 0.1977 0.2328 -0.0221 0.0002  -0.0268 263 VAL A N   
1457 C CA  . VAL A 209 ? 0.2121 0.2065 0.2411 -0.0121 -0.0348 -0.0216 263 VAL A CA  
1458 C C   . VAL A 209 ? 0.2470 0.2244 0.2657 -0.0701 -0.0466 -0.0043 263 VAL A C   
1459 O O   . VAL A 209 ? 0.2480 0.2316 0.2927 -0.0272 -0.0560 0.0198  263 VAL A O   
1460 C CB  . VAL A 209 ? 0.2489 0.2050 0.2175 -0.0002 -0.0313 0.0028  263 VAL A CB  
1461 C CG1 . VAL A 209 ? 0.2584 0.1957 0.2331 -0.0114 -0.0118 0.0097  263 VAL A CG1 
1462 C CG2 . VAL A 209 ? 0.2587 0.2246 0.1920 -0.0055 -0.0146 0.0134  263 VAL A CG2 
1463 N N   . GLY A 210 ? 0.2568 0.1917 0.2687 -0.0585 -0.0316 -0.0023 264 GLY A N   
1464 C CA  . GLY A 210 ? 0.3011 0.1804 0.3102 -0.0539 -0.0467 -0.0211 264 GLY A CA  
1465 C C   . GLY A 210 ? 0.3326 0.2017 0.3466 -0.0410 -0.0859 -0.0190 264 GLY A C   
1466 O O   . GLY A 210 ? 0.3411 0.2230 0.3469 -0.0346 -0.0750 -0.0391 264 GLY A O   
1467 N N   . ASP A 211 ? 0.3707 0.1704 0.3825 -0.0308 -0.1078 -0.0217 265 ASP A N   
1468 C CA  . ASP A 211 ? 0.4178 0.1981 0.4291 -0.0331 -0.0777 -0.0318 265 ASP A CA  
1469 C C   . ASP A 211 ? 0.4584 0.2723 0.4609 -0.0158 -0.0479 -0.0228 265 ASP A C   
1470 O O   . ASP A 211 ? 0.4894 0.2816 0.4750 -0.0192 -0.0273 -0.0177 265 ASP A O   
1471 C CB  . ASP A 211 ? 0.4469 0.2291 0.4497 -0.0813 -0.0822 -0.0186 265 ASP A CB  
1472 C CG  . ASP A 211 ? 0.4805 0.2410 0.4529 -0.0688 -0.0612 -0.0101 265 ASP A CG  
1473 O OD1 . ASP A 211 ? 0.4963 0.2444 0.4376 -0.0575 -0.0593 -0.0298 265 ASP A OD1 
1474 O OD2 . ASP A 211 ? 0.4643 0.2486 0.4634 -0.0571 -0.0325 0.0010  265 ASP A OD2 
1475 N N   . GLY A 212 ? 0.4192 0.2604 0.4907 0.0428  -0.0586 0.0258  266 GLY A N   
1476 C CA  . GLY A 212 ? 0.4389 0.2667 0.5230 0.0490  -0.0616 0.0281  266 GLY A CA  
1477 C C   . GLY A 212 ? 0.5244 0.2810 0.5437 0.0444  -0.0602 -0.0017 266 GLY A C   
1478 O O   . GLY A 212 ? 0.5369 0.3004 0.5469 0.0450  -0.0613 0.0029  266 GLY A O   
1479 N N   . PRO A 213 ? 0.5517 0.2997 0.5595 0.0704  -0.0513 -0.0131 267 PRO A N   
1480 C CA  . PRO A 213 ? 0.5558 0.3003 0.5726 0.0687  -0.0140 -0.0291 267 PRO A CA  
1481 C C   . PRO A 213 ? 0.5612 0.3683 0.5840 0.0510  -0.0207 -0.0408 267 PRO A C   
1482 O O   . PRO A 213 ? 0.5444 0.3880 0.5861 0.0722  -0.0608 -0.0342 267 PRO A O   
1483 C CB  . PRO A 213 ? 0.5592 0.3085 0.5756 0.0774  -0.0183 -0.0329 267 PRO A CB  
1484 C CG  . PRO A 213 ? 0.5748 0.3040 0.5723 0.0966  -0.0341 -0.0176 267 PRO A CG  
1485 C CD  . PRO A 213 ? 0.5826 0.3020 0.5551 0.0879  -0.0530 -0.0090 267 PRO A CD  
1486 N N   . TRP A 214 ? 0.6064 0.3960 0.5834 0.0331  0.0121  -0.0564 268 TRP A N   
1487 C CA  . TRP A 214 ? 0.6260 0.4035 0.5913 0.0211  0.0399  -0.0553 268 TRP A CA  
1488 C C   . TRP A 214 ? 0.6975 0.4616 0.6567 0.0346  0.0512  -0.0945 268 TRP A C   
1489 O O   . TRP A 214 ? 0.7032 0.4678 0.6691 0.0473  0.0706  -0.1167 268 TRP A O   
1490 C CB  . TRP A 214 ? 0.5780 0.3647 0.5383 0.0218  0.0647  -0.0187 268 TRP A CB  
1491 C CG  . TRP A 214 ? 0.5245 0.3187 0.4865 0.0322  0.0802  0.0421  268 TRP A CG  
1492 C CD1 . TRP A 214 ? 0.4943 0.3150 0.4680 0.0286  0.0774  0.0727  268 TRP A CD1 
1493 C CD2 . TRP A 214 ? 0.4764 0.3001 0.4691 0.0591  0.0904  0.0477  268 TRP A CD2 
1494 N NE1 . TRP A 214 ? 0.4732 0.3116 0.4529 0.0594  0.0832  0.0807  268 TRP A NE1 
1495 C CE2 . TRP A 214 ? 0.4335 0.2851 0.4516 0.0377  0.0920  0.0780  268 TRP A CE2 
1496 C CE3 . TRP A 214 ? 0.4894 0.2802 0.4547 0.0781  0.0987  0.0316  268 TRP A CE3 
1497 C CZ2 . TRP A 214 ? 0.4396 0.2737 0.4580 0.0874  0.0603  0.0918  268 TRP A CZ2 
1498 C CZ3 . TRP A 214 ? 0.4933 0.3110 0.4561 0.0759  0.0735  0.0574  268 TRP A CZ3 
1499 C CH2 . TRP A 214 ? 0.4240 0.2831 0.4515 0.1064  0.0754  0.0699  268 TRP A CH2 
1500 N N   . ASP A 215 ? 0.7544 0.5337 0.7029 0.0420  0.0365  -0.1071 269 ASP A N   
1501 C CA  . ASP A 215 ? 0.8307 0.5985 0.7491 0.0366  0.0152  -0.1120 269 ASP A CA  
1502 C C   . ASP A 215 ? 0.8320 0.6302 0.7789 0.0290  0.0052  -0.1163 269 ASP A C   
1503 O O   . ASP A 215 ? 0.8313 0.6423 0.7836 0.0308  0.0001  -0.1252 269 ASP A O   
1504 C CB  . ASP A 215 ? 0.8925 0.6305 0.7671 0.0380  0.0007  -0.1042 269 ASP A CB  
1505 C CG  . ASP A 215 ? 0.9418 0.6489 0.7873 0.0522  -0.0120 -0.0949 269 ASP A CG  
1506 O OD1 . ASP A 215 ? 0.9630 0.6498 0.7904 0.0731  -0.0148 -0.0925 269 ASP A OD1 
1507 O OD2 . ASP A 215 ? 0.9508 0.6573 0.8010 0.0394  -0.0188 -0.0925 269 ASP A OD2 
1508 N N   . THR A 216 ? 0.8313 0.6389 0.7984 0.0311  -0.0016 -0.1015 270 THR A N   
1509 C CA  . THR A 216 ? 0.8278 0.6367 0.8069 0.0426  0.0076  -0.0892 270 THR A CA  
1510 C C   . THR A 216 ? 0.7960 0.6125 0.8066 0.0517  0.0151  -0.1027 270 THR A C   
1511 O O   . THR A 216 ? 0.7952 0.5733 0.8244 0.0629  0.0221  -0.1109 270 THR A O   
1512 C CB  . THR A 216 ? 0.8562 0.6474 0.8108 0.0447  0.0145  -0.0704 270 THR A CB  
1513 O OG1 . THR A 216 ? 0.8727 0.6639 0.8112 0.0371  0.0185  -0.0590 270 THR A OG1 
1514 C CG2 . THR A 216 ? 0.8626 0.6472 0.8080 0.0318  0.0173  -0.0668 270 THR A CG2 
1515 N N   . MET A 217 ? 0.7788 0.6293 0.7891 0.0631  0.0190  -0.1025 271 MET A N   
1516 C CA  . MET A 217 ? 0.7920 0.6407 0.7718 0.1135  0.0332  -0.1065 271 MET A CA  
1517 C C   . MET A 217 ? 0.7966 0.6495 0.7929 0.1292  0.0396  -0.1276 271 MET A C   
1518 O O   . MET A 217 ? 0.7382 0.6172 0.8008 0.1627  0.0621  -0.1597 271 MET A O   
1519 C CB  . MET A 217 ? 0.7904 0.6428 0.7637 0.1276  0.0390  -0.0845 271 MET A CB  
1520 C CG  . MET A 217 ? 0.7326 0.6608 0.7686 0.1536  0.0610  -0.0798 271 MET A CG  
1521 S SD  . MET A 217 ? 0.7404 0.6921 0.7832 0.2101  0.0785  -0.0749 271 MET A SD  
1522 C CE  . MET A 217 ? 0.7998 0.7097 0.7767 0.1965  0.0731  -0.0837 271 MET A CE  
1523 N N   . ARG A 218 ? 0.8273 0.6811 0.7857 0.1037  0.0181  -0.1169 272 ARG A N   
1524 C CA  . ARG A 218 ? 0.8501 0.7052 0.7834 0.0883  0.0108  -0.1109 272 ARG A CA  
1525 C C   . ARG A 218 ? 0.8115 0.7026 0.7597 0.0883  0.0208  -0.1078 272 ARG A C   
1526 O O   . ARG A 218 ? 0.7929 0.7041 0.7525 0.1157  0.0355  -0.1007 272 ARG A O   
1527 C CB  . ARG A 218 ? 0.9028 0.7358 0.8060 0.0679  0.0032  -0.1064 272 ARG A CB  
1528 C CG  . ARG A 218 ? 0.9557 0.7693 0.8196 0.0491  -0.0039 -0.1040 272 ARG A CG  
1529 C CD  . ARG A 218 ? 0.9984 0.8035 0.8373 0.0406  -0.0074 -0.0956 272 ARG A CD  
1530 N NE  . ARG A 218 ? 1.0266 0.8320 0.8527 0.0485  -0.0082 -0.0951 272 ARG A NE  
1531 C CZ  . ARG A 218 ? 1.0516 0.8509 0.8690 0.0427  -0.0167 -0.0937 272 ARG A CZ  
1532 N NH1 . ARG A 218 ? 1.0506 0.8510 0.8817 0.0616  -0.0219 -0.1101 272 ARG A NH1 
1533 N NH2 . ARG A 218 ? 1.0618 0.8616 0.8661 0.0261  -0.0188 -0.0769 272 ARG A NH2 
1534 N N   . GLN A 219 ? 0.8063 0.6943 0.7552 0.0816  0.0278  -0.1162 273 GLN A N   
1535 C CA  . GLN A 219 ? 0.7914 0.6869 0.7523 0.0918  0.0541  -0.1177 273 GLN A CA  
1536 C C   . GLN A 219 ? 0.6956 0.6447 0.7124 0.0997  0.0784  -0.1323 273 GLN A C   
1537 O O   . GLN A 219 ? 0.6649 0.6253 0.7040 0.1020  0.0838  -0.1509 273 GLN A O   
1538 C CB  . GLN A 219 ? 0.8637 0.7335 0.7877 0.0854  0.0494  -0.0958 273 GLN A CB  
1539 C CG  . GLN A 219 ? 0.9438 0.7705 0.8192 0.0911  0.0390  -0.0800 273 GLN A CG  
1540 C CD  . GLN A 219 ? 1.0102 0.8056 0.8701 0.1055  0.0305  -0.0701 273 GLN A CD  
1541 O OE1 . GLN A 219 ? 1.0715 0.8250 0.8886 0.1024  0.0448  -0.0700 273 GLN A OE1 
1542 N NE2 . GLN A 219 ? 0.9963 0.8180 0.8858 0.1224  0.0151  -0.0642 273 GLN A NE2 
1543 N N   . PHE A 220 ? 0.6313 0.6141 0.6847 0.1015  0.1006  -0.1345 274 PHE A N   
1544 C CA  . PHE A 220 ? 0.5899 0.5914 0.6666 0.0715  0.0889  -0.1086 274 PHE A CA  
1545 C C   . PHE A 220 ? 0.5626 0.5803 0.6578 0.0914  0.1114  -0.0977 274 PHE A C   
1546 O O   . PHE A 220 ? 0.4976 0.5734 0.6543 0.0916  0.1498  -0.0861 274 PHE A O   
1547 C CB  . PHE A 220 ? 0.5981 0.5789 0.6552 0.0525  0.0868  -0.1078 274 PHE A CB  
1548 C CG  . PHE A 220 ? 0.6181 0.5741 0.6501 0.0455  0.0845  -0.1052 274 PHE A CG  
1549 C CD1 . PHE A 220 ? 0.6331 0.5853 0.6420 0.0404  0.0746  -0.1050 274 PHE A CD1 
1550 C CD2 . PHE A 220 ? 0.6041 0.5781 0.6510 0.0290  0.0870  -0.0976 274 PHE A CD2 
1551 C CE1 . PHE A 220 ? 0.6398 0.5788 0.6363 0.0298  0.0624  -0.1146 274 PHE A CE1 
1552 C CE2 . PHE A 220 ? 0.6060 0.5747 0.6447 0.0359  0.0809  -0.1062 274 PHE A CE2 
1553 C CZ  . PHE A 220 ? 0.6212 0.5782 0.6403 0.0372  0.0710  -0.1071 274 PHE A CZ  
1554 N N   . ASP A 221 ? 0.5898 0.5813 0.6548 0.0897  0.0988  -0.0907 275 ASP A N   
1555 C CA  . ASP A 221 ? 0.6413 0.5774 0.6540 0.0733  0.0761  -0.0694 275 ASP A CA  
1556 C C   . ASP A 221 ? 0.6379 0.5685 0.6687 0.0853  0.0804  -0.0701 275 ASP A C   
1557 O O   . ASP A 221 ? 0.6400 0.5599 0.6633 0.0990  0.0894  -0.0730 275 ASP A O   
1558 C CB  . ASP A 221 ? 0.6858 0.5898 0.6393 0.0483  0.0614  -0.0607 275 ASP A CB  
1559 C CG  . ASP A 221 ? 0.7214 0.6192 0.6369 0.0394  0.0616  -0.0487 275 ASP A CG  
1560 O OD1 . ASP A 221 ? 0.7301 0.6246 0.6300 0.0513  0.0586  -0.0471 275 ASP A OD1 
1561 O OD2 . ASP A 221 ? 0.7350 0.6402 0.6482 0.0198  0.0668  -0.0384 275 ASP A OD2 
1562 N N   . ASP A 222 ? 0.6662 0.5705 0.6776 0.0730  0.0676  -0.0768 276 ASP A N   
1563 C CA  . ASP A 222 ? 0.6881 0.5947 0.6779 0.0625  0.0558  -0.0730 276 ASP A CA  
1564 C C   . ASP A 222 ? 0.6617 0.5719 0.6676 0.0607  0.0486  -0.0627 276 ASP A C   
1565 O O   . ASP A 222 ? 0.6726 0.6057 0.6841 0.0846  0.0466  -0.0434 276 ASP A O   
1566 C CB  . ASP A 222 ? 0.7624 0.6467 0.6906 0.0721  0.0565  -0.0783 276 ASP A CB  
1567 C CG  . ASP A 222 ? 0.8205 0.7128 0.7270 0.0772  0.0553  -0.0689 276 ASP A CG  
1568 O OD1 . ASP A 222 ? 0.8319 0.7227 0.7417 0.0768  0.0384  -0.0671 276 ASP A OD1 
1569 O OD2 . ASP A 222 ? 0.8852 0.7364 0.7479 0.0629  0.0620  -0.0637 276 ASP A OD2 
1570 N N   . ASN A 223 ? 0.6085 0.5103 0.6316 0.0568  0.0517  -0.0662 277 ASN A N   
1571 C CA  . ASN A 223 ? 0.5669 0.4602 0.5845 0.0551  0.0434  -0.0540 277 ASN A CA  
1572 C C   . ASN A 223 ? 0.4935 0.4012 0.5398 0.0321  0.0414  -0.0558 277 ASN A C   
1573 O O   . ASN A 223 ? 0.5034 0.3973 0.5360 0.0170  0.0236  -0.0508 277 ASN A O   
1574 C CB  . ASN A 223 ? 0.6211 0.4746 0.5948 0.0651  0.0234  -0.0402 277 ASN A CB  
1575 C CG  . ASN A 223 ? 0.6582 0.5104 0.6126 0.0766  0.0102  -0.0247 277 ASN A CG  
1576 O OD1 . ASN A 223 ? 0.6844 0.5039 0.6165 0.1114  0.0033  -0.0300 277 ASN A OD1 
1577 N ND2 . ASN A 223 ? 0.6717 0.5157 0.6178 0.0651  0.0031  -0.0013 277 ASN A ND2 
1578 N N   . ILE A 224 ? 0.4035 0.3868 0.5029 0.0267  0.0577  -0.0586 278 ILE A N   
1579 C CA  . ILE A 224 ? 0.3367 0.3727 0.4668 0.0411  0.0475  -0.0318 278 ILE A CA  
1580 C C   . ILE A 224 ? 0.3357 0.3742 0.4392 0.0386  0.0639  0.0033  278 ILE A C   
1581 O O   . ILE A 224 ? 0.3839 0.4264 0.4349 0.0312  0.0533  -0.0017 278 ILE A O   
1582 C CB  . ILE A 224 ? 0.2857 0.3690 0.4633 0.0289  0.0208  -0.0422 278 ILE A CB  
1583 C CG1 . ILE A 224 ? 0.2909 0.3921 0.4515 0.0448  0.0036  -0.0477 278 ILE A CG1 
1584 C CG2 . ILE A 224 ? 0.2458 0.3422 0.4654 0.0086  0.0042  -0.0522 278 ILE A CG2 
1585 C CD1 . ILE A 224 ? 0.3343 0.3945 0.4352 0.0233  0.0186  -0.0725 278 ILE A CD1 
1586 N N   . PRO A 225 ? 0.2872 0.3394 0.4207 0.0672  0.0828  0.0070  279 PRO A N   
1587 C CA  . PRO A 225 ? 0.2892 0.3344 0.4150 0.0391  0.0748  0.0245  279 PRO A CA  
1588 C C   . PRO A 225 ? 0.3263 0.3226 0.4131 0.0796  0.0900  0.0066  279 PRO A C   
1589 O O   . PRO A 225 ? 0.3121 0.3302 0.4008 0.0997  0.0849  0.0260  279 PRO A O   
1590 C CB  . PRO A 225 ? 0.2934 0.3480 0.4163 0.0335  0.0498  0.0396  279 PRO A CB  
1591 C CG  . PRO A 225 ? 0.2738 0.3310 0.4229 0.0501  0.0402  0.0388  279 PRO A CG  
1592 C CD  . PRO A 225 ? 0.2759 0.3466 0.4221 0.0448  0.0704  0.0159  279 PRO A CD  
1593 N N   . ALA A 226 ? 0.3817 0.3386 0.4112 0.0343  0.1193  0.0266  280 ALA A N   
1594 C CA  . ALA A 226 ? 0.4142 0.3501 0.4254 0.0262  0.1122  0.0557  280 ALA A CA  
1595 C C   . ALA A 226 ? 0.4384 0.3644 0.4361 0.0257  0.0908  0.0727  280 ALA A C   
1596 O O   . ALA A 226 ? 0.4384 0.3855 0.4543 0.0175  0.0618  0.1022  280 ALA A O   
1597 C CB  . ALA A 226 ? 0.4649 0.3858 0.4259 0.0371  0.1014  0.0591  280 ALA A CB  
1598 N N   . ARG A 227 ? 0.4191 0.3400 0.4249 0.0363  0.0967  0.0672  281 ARG A N   
1599 C CA  . ARG A 227 ? 0.3783 0.3255 0.4212 0.0234  0.0952  0.0419  281 ARG A CA  
1600 C C   . ARG A 227 ? 0.4219 0.3126 0.4298 0.0014  0.0814  0.0393  281 ARG A C   
1601 O O   . ARG A 227 ? 0.4234 0.2925 0.4409 0.0235  0.1090  0.0061  281 ARG A O   
1602 C CB  . ARG A 227 ? 0.2999 0.3159 0.3844 0.0117  0.1015  0.0163  281 ARG A CB  
1603 C CG  . ARG A 227 ? 0.2479 0.3020 0.3421 0.0176  0.0520  -0.0007 281 ARG A CG  
1604 C CD  . ARG A 227 ? 0.2755 0.3096 0.3191 -0.0232 0.0516  0.0202  281 ARG A CD  
1605 N NE  . ARG A 227 ? 0.3596 0.3451 0.3372 -0.0026 0.0308  0.0155  281 ARG A NE  
1606 C CZ  . ARG A 227 ? 0.3676 0.3493 0.3356 0.0117  0.0202  -0.0352 281 ARG A CZ  
1607 N NH1 . ARG A 227 ? 0.3053 0.3312 0.3220 0.0740  0.0506  -0.0318 281 ARG A NH1 
1608 N NH2 . ARG A 227 ? 0.4084 0.3498 0.3713 0.0402  0.0553  -0.0604 281 ARG A NH2 
1609 N N   . ALA A 228 ? 0.4421 0.3279 0.4314 0.0058  0.0226  0.0632  282 ALA A N   
1610 C CA  . ALA A 228 ? 0.4115 0.3553 0.4325 0.0127  0.0264  0.0511  282 ALA A CA  
1611 C C   . ALA A 228 ? 0.3221 0.3300 0.4120 0.0401  0.0813  0.0474  282 ALA A C   
1612 O O   . ALA A 228 ? 0.3378 0.3397 0.4156 0.0407  0.0728  0.0278  282 ALA A O   
1613 C CB  . ALA A 228 ? 0.4403 0.3848 0.4495 -0.0065 -0.0226 0.0394  282 ALA A CB  
1614 N N   . PHE A 229 ? 0.3346 0.3663 0.3978 0.0215  0.1088  0.0608  283 PHE A N   
1615 C CA  . PHE A 229 ? 0.3672 0.4007 0.3607 0.0665  0.1066  0.0634  283 PHE A CA  
1616 C C   . PHE A 229 ? 0.3344 0.4549 0.3607 0.0933  0.1527  0.0764  283 PHE A C   
1617 O O   . PHE A 229 ? 0.3357 0.4733 0.4012 0.1040  0.1015  0.0934  283 PHE A O   
1618 C CB  . PHE A 229 ? 0.3448 0.3607 0.3080 0.0234  0.0864  0.1179  283 PHE A CB  
1619 C CG  . PHE A 229 ? 0.3149 0.3710 0.3073 -0.0059 0.0486  0.0941  283 PHE A CG  
1620 C CD1 . PHE A 229 ? 0.3336 0.3018 0.2761 -0.0486 0.0114  0.0852  283 PHE A CD1 
1621 C CD2 . PHE A 229 ? 0.3065 0.3976 0.2955 0.0032  0.0136  0.1082  283 PHE A CD2 
1622 C CE1 . PHE A 229 ? 0.2644 0.2763 0.2880 -0.0474 -0.0022 0.0701  283 PHE A CE1 
1623 C CE2 . PHE A 229 ? 0.2896 0.3733 0.2843 -0.0176 -0.0030 0.1003  283 PHE A CE2 
1624 C CZ  . PHE A 229 ? 0.2715 0.3160 0.2677 -0.0573 0.0085  0.0867  283 PHE A CZ  
1625 N N   . ASP A 230 ? 0.3756 0.4857 0.3832 0.1241  0.1195  0.0626  284 ASP A N   
1626 C CA  . ASP A 230 ? 0.3931 0.4811 0.3701 0.1212  0.1195  0.0259  284 ASP A CA  
1627 C C   . ASP A 230 ? 0.3026 0.4227 0.3196 0.1404  0.0836  0.0477  284 ASP A C   
1628 O O   . ASP A 230 ? 0.4441 0.4716 0.3105 0.2264  0.0524  0.0603  284 ASP A O   
1629 C CB  . ASP A 230 ? 0.4988 0.5196 0.4411 0.0943  0.1581  -0.0418 284 ASP A CB  
1630 C CG  . ASP A 230 ? 0.5713 0.5885 0.5100 0.0949  0.1710  -0.0954 284 ASP A CG  
1631 O OD1 . ASP A 230 ? 0.5242 0.5685 0.5225 0.1174  0.2216  -0.1324 284 ASP A OD1 
1632 O OD2 . ASP A 230 ? 0.6491 0.6367 0.5782 0.0674  0.1472  -0.0800 284 ASP A OD2 
1633 N N   . ASN A 231 ? 0.2375 0.3025 0.2640 0.0652  0.0789  0.0452  285 ASN A N   
1634 C CA  . ASN A 231 ? 0.1800 0.2624 0.2605 0.0289  0.0167  0.0125  285 ASN A CA  
1635 C C   . ASN A 231 ? 0.1586 0.2384 0.2442 0.0026  0.0199  -0.0208 285 ASN A C   
1636 O O   . ASN A 231 ? 0.2059 0.2747 0.2426 0.0231  0.0458  -0.0103 285 ASN A O   
1637 C CB  . ASN A 231 ? 0.2472 0.2404 0.2297 0.0149  0.0020  0.0489  285 ASN A CB  
1638 C CG  . ASN A 231 ? 0.2153 0.2284 0.2243 0.0050  -0.0026 0.0190  285 ASN A CG  
1639 O OD1 . ASN A 231 ? 0.2940 0.2664 0.2481 0.0508  0.0167  -0.0030 285 ASN A OD1 
1640 N ND2 . ASN A 231 ? 0.2087 0.2519 0.2372 0.0084  0.0111  0.0252  285 ASN A ND2 
1641 N N   . PHE A 232 ? 0.2166 0.2464 0.2639 -0.0086 -0.0054 -0.0197 286 PHE A N   
1642 C CA  . PHE A 232 ? 0.2453 0.2702 0.2793 0.0186  0.0099  -0.0491 286 PHE A CA  
1643 C C   . PHE A 232 ? 0.2458 0.3230 0.2636 -0.0156 0.0067  -0.0646 286 PHE A C   
1644 O O   . PHE A 232 ? 0.3003 0.4185 0.3032 -0.0349 0.0679  -0.1014 286 PHE A O   
1645 C CB  . PHE A 232 ? 0.2758 0.2693 0.3263 0.0158  0.0436  -0.0227 286 PHE A CB  
1646 C CG  . PHE A 232 ? 0.2236 0.2577 0.3766 0.0131  0.0400  -0.0343 286 PHE A CG  
1647 C CD1 . PHE A 232 ? 0.2049 0.2451 0.3963 0.0101  0.0460  -0.0039 286 PHE A CD1 
1648 C CD2 . PHE A 232 ? 0.2829 0.2794 0.4011 0.0185  0.0317  -0.0221 286 PHE A CD2 
1649 C CE1 . PHE A 232 ? 0.2608 0.2553 0.4107 0.0347  0.0743  0.0111  286 PHE A CE1 
1650 C CE2 . PHE A 232 ? 0.3519 0.2930 0.4017 0.0057  0.0608  0.0104  286 PHE A CE2 
1651 C CZ  . PHE A 232 ? 0.3117 0.2862 0.4108 0.0243  0.0946  -0.0012 286 PHE A CZ  
1652 N N   . GLN A 233 ? 0.2607 0.2817 0.2299 -0.0459 -0.0120 -0.0622 287 GLN A N   
1653 C CA  . GLN A 233 ? 0.2902 0.2844 0.2384 -0.0326 0.0260  -0.0576 287 GLN A CA  
1654 C C   . GLN A 233 ? 0.2767 0.2343 0.2170 -0.0382 0.0576  -0.0562 287 GLN A C   
1655 O O   . GLN A 233 ? 0.2755 0.2533 0.2190 -0.0473 0.0461  -0.0540 287 GLN A O   
1656 C CB  . GLN A 233 ? 0.3195 0.3655 0.2641 -0.0677 0.0231  -0.0233 287 GLN A CB  
1657 C CG  . GLN A 233 ? 0.3837 0.4470 0.3222 -0.1077 0.0517  -0.0005 287 GLN A CG  
1658 C CD  . GLN A 233 ? 0.5568 0.4984 0.4148 -0.1107 0.0915  0.0005  287 GLN A CD  
1659 O OE1 . GLN A 233 ? 0.7045 0.5808 0.4233 -0.0817 0.0719  0.0297  287 GLN A OE1 
1660 N NE2 . GLN A 233 ? 0.4382 0.4778 0.4777 -0.1359 0.2091  0.0096  287 GLN A NE2 
1661 N N   . PHE A 234 ? 0.2890 0.2440 0.2568 -0.0458 0.0194  -0.0458 288 PHE A N   
1662 C CA  . PHE A 234 ? 0.2456 0.2274 0.2608 -0.0339 0.0289  -0.0596 288 PHE A CA  
1663 C C   . PHE A 234 ? 0.2795 0.2645 0.2347 -0.0556 0.0230  -0.0525 288 PHE A C   
1664 O O   . PHE A 234 ? 0.3085 0.3497 0.2296 -0.0656 0.0161  -0.0640 288 PHE A O   
1665 C CB  . PHE A 234 ? 0.2355 0.2158 0.3028 -0.0113 0.0504  -0.0346 288 PHE A CB  
1666 C CG  . PHE A 234 ? 0.2762 0.1953 0.3178 -0.0194 0.0313  -0.0515 288 PHE A CG  
1667 C CD1 . PHE A 234 ? 0.2855 0.1980 0.3360 0.0020  0.0360  -0.0086 288 PHE A CD1 
1668 C CD2 . PHE A 234 ? 0.3011 0.2051 0.3307 -0.0315 -0.0030 -0.0557 288 PHE A CD2 
1669 C CE1 . PHE A 234 ? 0.3072 0.1976 0.3504 0.0145  -0.0085 -0.0226 288 PHE A CE1 
1670 C CE2 . PHE A 234 ? 0.3187 0.1999 0.3202 -0.0287 -0.0001 -0.0614 288 PHE A CE2 
1671 C CZ  . PHE A 234 ? 0.2918 0.1967 0.3353 -0.0241 0.0013  -0.0204 288 PHE A CZ  
1672 N N   . VAL A 235 ? 0.2413 0.2362 0.2212 -0.0322 -0.0102 -0.0414 289 VAL A N   
1673 C CA  . VAL A 235 ? 0.2408 0.2386 0.2360 -0.0415 0.0055  -0.0246 289 VAL A CA  
1674 C C   . VAL A 235 ? 0.2497 0.2101 0.2331 -0.0152 -0.0116 -0.0301 289 VAL A C   
1675 O O   . VAL A 235 ? 0.2432 0.2413 0.2076 -0.0085 -0.0094 -0.0134 289 VAL A O   
1676 C CB  . VAL A 235 ? 0.3001 0.2820 0.2391 -0.0193 0.0151  0.0070  289 VAL A CB  
1677 C CG1 . VAL A 235 ? 0.2990 0.2726 0.2771 -0.0167 0.0325  0.0051  289 VAL A CG1 
1678 C CG2 . VAL A 235 ? 0.3011 0.2981 0.2505 0.0107  -0.0303 0.0249  289 VAL A CG2 
1679 N N   . ASN A 236 ? 0.2674 0.2175 0.2652 -0.0293 -0.0476 -0.0694 290 ASN A N   
1680 C CA  . ASN A 236 ? 0.2779 0.2120 0.2769 0.0148  -0.0514 -0.0608 290 ASN A CA  
1681 C C   . ASN A 236 ? 0.2544 0.2433 0.2521 0.0320  -0.0711 -0.0315 290 ASN A C   
1682 O O   . ASN A 236 ? 0.2638 0.2687 0.2503 0.0245  -0.0730 -0.0064 290 ASN A O   
1683 C CB  . ASN A 236 ? 0.3178 0.2069 0.3188 0.0089  -0.0640 -0.0726 290 ASN A CB  
1684 C CG  . ASN A 236 ? 0.3638 0.2122 0.3707 0.0138  -0.0567 -0.0485 290 ASN A CG  
1685 O OD1 . ASN A 236 ? 0.3797 0.2358 0.3594 0.0127  -0.0813 -0.0431 290 ASN A OD1 
1686 N ND2 . ASN A 236 ? 0.4193 0.2523 0.4304 -0.0207 -0.0429 -0.0503 290 ASN A ND2 
1687 N N   . PHE A 237 ? 0.2391 0.2270 0.2322 0.0046  -0.0423 -0.0203 291 PHE A N   
1688 C CA  . PHE A 237 ? 0.2550 0.2325 0.2391 -0.0110 -0.0807 -0.0411 291 PHE A CA  
1689 C C   . PHE A 237 ? 0.2738 0.1964 0.2873 0.0108  -0.0898 -0.0320 291 PHE A C   
1690 O O   . PHE A 237 ? 0.3109 0.2343 0.2893 0.0081  -0.0902 -0.0298 291 PHE A O   
1691 C CB  . PHE A 237 ? 0.2538 0.2508 0.2372 0.0313  -0.0635 -0.0256 291 PHE A CB  
1692 C CG  . PHE A 237 ? 0.2631 0.2520 0.2597 0.0303  -0.0794 -0.0079 291 PHE A CG  
1693 C CD1 . PHE A 237 ? 0.2313 0.2702 0.2716 0.0104  -0.0370 0.0031  291 PHE A CD1 
1694 C CD2 . PHE A 237 ? 0.2573 0.2361 0.2835 0.0577  -0.0926 -0.0278 291 PHE A CD2 
1695 C CE1 . PHE A 237 ? 0.2469 0.2714 0.2858 0.0039  -0.0452 -0.0067 291 PHE A CE1 
1696 C CE2 . PHE A 237 ? 0.2462 0.2285 0.2959 0.0021  -0.0891 -0.0457 291 PHE A CE2 
1697 C CZ  . PHE A 237 ? 0.2417 0.2257 0.2934 -0.0117 -0.0622 -0.0343 291 PHE A CZ  
1698 N N   . THR A 238 ? 0.2683 0.2018 0.3150 -0.0125 -0.0626 -0.0311 292 THR A N   
1699 C CA  . THR A 238 ? 0.3070 0.2104 0.3238 -0.0265 -0.0751 -0.0058 292 THR A CA  
1700 C C   . THR A 238 ? 0.3411 0.2240 0.3351 -0.0243 -0.1126 -0.0240 292 THR A C   
1701 O O   . THR A 238 ? 0.3637 0.2663 0.3626 -0.0374 -0.1481 -0.0082 292 THR A O   
1702 C CB  . THR A 238 ? 0.3522 0.2430 0.3232 -0.0651 -0.0773 -0.0058 292 THR A CB  
1703 O OG1 . THR A 238 ? 0.3618 0.2474 0.3110 -0.0435 -0.0666 -0.0144 292 THR A OG1 
1704 C CG2 . THR A 238 ? 0.3645 0.2633 0.3447 -0.0946 -0.0796 0.0072  292 THR A CG2 
1705 N N   . ASP A 239 ? 0.3812 0.2437 0.3269 0.0191  -0.0939 -0.0390 293 ASP A N   
1706 C CA  . ASP A 239 ? 0.4412 0.3029 0.3420 0.0283  -0.1129 -0.0418 293 ASP A CA  
1707 C C   . ASP A 239 ? 0.4242 0.2588 0.3293 0.0177  -0.0992 -0.0501 293 ASP A C   
1708 O O   . ASP A 239 ? 0.4365 0.3205 0.3456 0.0061  -0.1525 -0.0532 293 ASP A O   
1709 C CB  . ASP A 239 ? 0.5160 0.3446 0.3593 0.0656  -0.1240 -0.0378 293 ASP A CB  
1710 C CG  . ASP A 239 ? 0.5715 0.4177 0.4117 0.0811  -0.1153 -0.0470 293 ASP A CG  
1711 O OD1 . ASP A 239 ? 0.6073 0.3501 0.4335 0.0338  -0.1345 -0.0644 293 ASP A OD1 
1712 O OD2 . ASP A 239 ? 0.6262 0.5246 0.4695 0.1154  -0.1155 -0.0310 293 ASP A OD2 
1713 N N   . ILE A 240 ? 0.3559 0.2400 0.3325 0.0124  -0.0798 -0.0245 294 ILE A N   
1714 C CA  . ILE A 240 ? 0.3297 0.2351 0.3226 -0.0419 -0.0986 -0.0198 294 ILE A CA  
1715 C C   . ILE A 240 ? 0.3665 0.2619 0.2995 -0.0447 -0.1270 -0.0346 294 ILE A C   
1716 O O   . ILE A 240 ? 0.3991 0.2868 0.3049 -0.0233 -0.1595 -0.0350 294 ILE A O   
1717 C CB  . ILE A 240 ? 0.3754 0.2281 0.3040 -0.0343 -0.0843 -0.0274 294 ILE A CB  
1718 C CG1 . ILE A 240 ? 0.4137 0.2510 0.3306 -0.0512 -0.0622 -0.0404 294 ILE A CG1 
1719 C CG2 . ILE A 240 ? 0.3986 0.2031 0.2991 -0.0019 -0.0758 -0.0204 294 ILE A CG2 
1720 C CD1 . ILE A 240 ? 0.3946 0.2606 0.3335 -0.0799 -0.0343 -0.0516 294 ILE A CD1 
1721 N N   . MET A 241 ? 0.3403 0.2818 0.3149 -0.0307 -0.1161 -0.0183 295 MET A N   
1722 C CA  . MET A 241 ? 0.3244 0.3454 0.3384 -0.0233 -0.1030 -0.0093 295 MET A CA  
1723 C C   . MET A 241 ? 0.3255 0.3735 0.4107 -0.0278 -0.0857 0.0082  295 MET A C   
1724 O O   . MET A 241 ? 0.3053 0.4263 0.4523 -0.0324 -0.0948 0.0003  295 MET A O   
1725 C CB  . MET A 241 ? 0.3011 0.3563 0.3199 0.0012  -0.0694 -0.0071 295 MET A CB  
1726 C CG  . MET A 241 ? 0.3298 0.3583 0.3119 0.0458  -0.0947 -0.0093 295 MET A CG  
1727 S SD  . MET A 241 ? 0.3410 0.4199 0.3255 -0.0167 -0.0667 0.0017  295 MET A SD  
1728 C CE  . MET A 241 ? 0.3526 0.4694 0.3511 0.0268  -0.0493 0.0324  295 MET A CE  
1729 N N   . SER A 242 ? 0.3564 0.3169 0.4413 -0.0802 -0.1053 0.0071  296 SER A N   
1730 C CA  . SER A 242 ? 0.4194 0.3255 0.4885 -0.1102 -0.1399 -0.0106 296 SER A CA  
1731 C C   . SER A 242 ? 0.4590 0.3737 0.5087 -0.1483 -0.1937 -0.0254 296 SER A C   
1732 O O   . SER A 242 ? 0.4948 0.4019 0.5370 -0.1216 -0.1971 -0.0099 296 SER A O   
1733 C CB  . SER A 242 ? 0.4649 0.3261 0.5031 -0.0867 -0.1152 -0.0298 296 SER A CB  
1734 O OG  . SER A 242 ? 0.5441 0.3367 0.4958 -0.0754 -0.0986 -0.0356 296 SER A OG  
1735 N N   . LYS A 243 ? 0.4906 0.4352 0.5083 -0.1014 -0.2001 -0.0353 297 LYS A N   
1736 C CA  . LYS A 243 ? 0.5256 0.4856 0.5144 -0.0967 -0.2077 -0.0594 297 LYS A CA  
1737 C C   . LYS A 243 ? 0.5578 0.5339 0.5522 -0.1210 -0.2417 -0.0489 297 LYS A C   
1738 O O   . LYS A 243 ? 0.5268 0.5482 0.5713 -0.1291 -0.2611 -0.0423 297 LYS A O   
1739 C CB  . LYS A 243 ? 0.5523 0.4916 0.4989 -0.0641 -0.1699 -0.0682 297 LYS A CB  
1740 C CG  . LYS A 243 ? 0.5468 0.5039 0.5053 -0.0253 -0.1206 -0.0805 297 LYS A CG  
1741 C CD  . LYS A 243 ? 0.5688 0.5141 0.5107 -0.0042 -0.0701 -0.0881 297 LYS A CD  
1742 C CE  . LYS A 243 ? 0.6049 0.5127 0.5213 -0.0296 -0.0310 -0.0861 297 LYS A CE  
1743 N NZ  . LYS A 243 ? 0.6349 0.5231 0.5314 -0.0354 -0.0053 -0.0725 297 LYS A NZ  
1744 N N   . ASN A 244 ? 0.6112 0.5757 0.5718 -0.1164 -0.2540 -0.0366 298 ASN A N   
1745 C CA  . ASN A 244 ? 0.6545 0.6249 0.5972 -0.1102 -0.2357 -0.0276 298 ASN A CA  
1746 C C   . ASN A 244 ? 0.6423 0.6504 0.5959 -0.0918 -0.2361 -0.0339 298 ASN A C   
1747 O O   . ASN A 244 ? 0.6710 0.6414 0.6021 -0.0662 -0.1914 -0.0196 298 ASN A O   
1748 C CB  . ASN A 244 ? 0.7238 0.6846 0.6306 -0.1191 -0.2159 -0.0251 298 ASN A CB  
1749 C CG  . ASN A 244 ? 0.7919 0.7391 0.6643 -0.1174 -0.1924 -0.0149 298 ASN A CG  
1750 O OD1 . ASN A 244 ? 0.8109 0.7563 0.6790 -0.0977 -0.1772 -0.0090 298 ASN A OD1 
1751 N ND2 . ASN A 244 ? 0.8152 0.7607 0.6651 -0.1297 -0.1873 0.0009  298 ASN A ND2 
1752 N N   . ILE A 245 ? 0.5584 0.6184 0.5832 -0.1383 -0.2783 -0.0504 299 ILE A N   
1753 C CA  . ILE A 245 ? 0.5496 0.6466 0.5768 -0.0993 -0.2639 -0.0360 299 ILE A CA  
1754 C C   . ILE A 245 ? 0.5120 0.6487 0.5470 -0.0830 -0.2691 -0.0251 299 ILE A C   
1755 O O   . ILE A 245 ? 0.5413 0.6552 0.5416 -0.0822 -0.2506 -0.0076 299 ILE A O   
1756 C CB  . ILE A 245 ? 0.6464 0.6691 0.6025 -0.0693 -0.1696 -0.0242 299 ILE A CB  
1757 C CG1 . ILE A 245 ? 0.7017 0.6786 0.6161 -0.0586 -0.1288 -0.0110 299 ILE A CG1 
1758 C CG2 . ILE A 245 ? 0.6671 0.6793 0.6031 -0.0747 -0.1682 -0.0338 299 ILE A CG2 
1759 C CD1 . ILE A 245 ? 0.7336 0.6945 0.6187 -0.0501 -0.1346 -0.0094 299 ILE A CD1 
1760 N N   . ASP A 246 ? 0.4854 0.6237 0.4997 -0.0909 -0.2763 -0.0466 300 ASP A N   
1761 C CA  . ASP A 246 ? 0.4360 0.6112 0.4736 -0.0613 -0.2599 -0.0540 300 ASP A CA  
1762 C C   . ASP A 246 ? 0.3889 0.5914 0.4435 -0.0791 -0.2192 -0.0670 300 ASP A C   
1763 O O   . ASP A 246 ? 0.3562 0.5855 0.4453 -0.0941 -0.1976 -0.0925 300 ASP A O   
1764 C CB  . ASP A 246 ? 0.4503 0.6058 0.4977 -0.0262 -0.2565 -0.0612 300 ASP A CB  
1765 C CG  . ASP A 246 ? 0.4730 0.6263 0.5278 -0.0258 -0.2324 -0.0638 300 ASP A CG  
1766 O OD1 . ASP A 246 ? 0.4845 0.6514 0.5339 -0.0035 -0.2162 -0.0603 300 ASP A OD1 
1767 O OD2 . ASP A 246 ? 0.5240 0.6160 0.5500 0.0121  -0.2084 -0.0483 300 ASP A OD2 
1768 N N   . PRO A 247 ? 0.3242 0.5946 0.4201 -0.0708 -0.1800 -0.0191 301 PRO A N   
1769 C CA  . PRO A 247 ? 0.3168 0.5850 0.4058 -0.0692 -0.1314 -0.0278 301 PRO A CA  
1770 C C   . PRO A 247 ? 0.2856 0.5309 0.3719 -0.0532 -0.1072 -0.0385 301 PRO A C   
1771 O O   . PRO A 247 ? 0.2420 0.5156 0.3648 -0.0564 -0.1074 -0.0632 301 PRO A O   
1772 C CB  . PRO A 247 ? 0.3819 0.6024 0.4221 -0.0702 -0.1098 -0.0262 301 PRO A CB  
1773 C CG  . PRO A 247 ? 0.3817 0.6126 0.4280 -0.0856 -0.0990 -0.0163 301 PRO A CG  
1774 C CD  . PRO A 247 ? 0.3589 0.6098 0.4183 -0.0682 -0.1447 -0.0086 301 PRO A CD  
1775 N N   . ALA A 248 ? 0.2835 0.4859 0.3676 -0.0401 -0.0827 -0.0267 302 ALA A N   
1776 C CA  . ALA A 248 ? 0.3056 0.4673 0.3486 -0.0062 -0.1348 -0.0177 302 ALA A CA  
1777 C C   . ALA A 248 ? 0.3157 0.4191 0.3271 -0.0256 -0.1432 -0.0356 302 ALA A C   
1778 O O   . ALA A 248 ? 0.3122 0.4099 0.3103 0.0162  -0.1164 -0.0449 302 ALA A O   
1779 C CB  . ALA A 248 ? 0.3099 0.5110 0.3769 0.0734  -0.1406 0.0099  302 ALA A CB  
1780 N N   . ARG A 249 ? 0.3570 0.4362 0.3364 -0.0179 -0.1613 -0.0416 303 ARG A N   
1781 C CA  . ARG A 249 ? 0.3949 0.4319 0.3293 -0.0210 -0.1667 -0.0861 303 ARG A CA  
1782 C C   . ARG A 249 ? 0.3579 0.3719 0.3241 -0.0563 -0.1423 -0.0645 303 ARG A C   
1783 O O   . ARG A 249 ? 0.3280 0.3380 0.3197 -0.0426 -0.1230 -0.0708 303 ARG A O   
1784 C CB  . ARG A 249 ? 0.4771 0.5093 0.3618 -0.0450 -0.1830 -0.1203 303 ARG A CB  
1785 C CG  . ARG A 249 ? 0.5865 0.5873 0.4123 -0.0779 -0.1850 -0.1231 303 ARG A CG  
1786 C CD  . ARG A 249 ? 0.6930 0.6588 0.4725 -0.0985 -0.1544 -0.1268 303 ARG A CD  
1787 N NE  . ARG A 249 ? 0.8043 0.7291 0.5564 -0.0930 -0.1281 -0.1045 303 ARG A NE  
1788 C CZ  . ARG A 249 ? 0.8886 0.8096 0.6328 -0.0641 -0.0871 -0.0680 303 ARG A CZ  
1789 N NH1 . ARG A 249 ? 0.9304 0.8372 0.6631 -0.0603 -0.0679 -0.0558 303 ARG A NH1 
1790 N NH2 . ARG A 249 ? 0.9070 0.8364 0.6586 -0.0444 -0.0746 -0.0522 303 ARG A NH2 
1791 N N   . LYS A 250 ? 0.3552 0.3661 0.3271 -0.0475 -0.1395 -0.0407 304 LYS A N   
1792 C CA  . LYS A 250 ? 0.3693 0.3271 0.3542 -0.0730 -0.0874 -0.0125 304 LYS A CA  
1793 C C   . LYS A 250 ? 0.3090 0.2896 0.3250 -0.0340 -0.0660 -0.0005 304 LYS A C   
1794 O O   . LYS A 250 ? 0.2755 0.2685 0.3201 -0.0434 -0.0369 -0.0201 304 LYS A O   
1795 C CB  . LYS A 250 ? 0.4123 0.3831 0.4096 -0.1118 -0.1099 -0.0132 304 LYS A CB  
1796 C CG  . LYS A 250 ? 0.4394 0.4230 0.4599 -0.1226 -0.1075 0.0355  304 LYS A CG  
1797 C CD  . LYS A 250 ? 0.4607 0.4538 0.4901 -0.1493 -0.0792 0.0622  304 LYS A CD  
1798 C CE  . LYS A 250 ? 0.4577 0.4602 0.5253 -0.1373 -0.0758 0.0801  304 LYS A CE  
1799 N NZ  . LYS A 250 ? 0.4607 0.5115 0.5340 -0.0808 -0.0994 0.0802  304 LYS A NZ  
1800 N N   . GLU A 251 ? 0.2680 0.2701 0.3038 -0.0194 -0.1046 0.0136  305 GLU A N   
1801 C CA  . GLU A 251 ? 0.2604 0.2687 0.2850 0.0109  -0.0928 -0.0204 305 GLU A CA  
1802 C C   . GLU A 251 ? 0.2468 0.2518 0.2601 -0.0079 -0.0872 -0.0043 305 GLU A C   
1803 O O   . GLU A 251 ? 0.2475 0.2715 0.2536 0.0022  -0.0843 0.0037  305 GLU A O   
1804 C CB  . GLU A 251 ? 0.2850 0.3318 0.3265 0.0284  -0.0546 -0.0006 305 GLU A CB  
1805 C CG  . GLU A 251 ? 0.3208 0.3783 0.3641 0.0371  0.0127  -0.0005 305 GLU A CG  
1806 C CD  . GLU A 251 ? 0.4120 0.4117 0.4079 -0.0092 0.0590  -0.0006 305 GLU A CD  
1807 O OE1 . GLU A 251 ? 0.4430 0.3985 0.4398 0.0068  0.0639  -0.0263 305 GLU A OE1 
1808 O OE2 . GLU A 251 ? 0.4407 0.4502 0.4230 0.0310  0.0468  0.0183  305 GLU A OE2 
1809 N N   . ALA A 252 ? 0.2632 0.2431 0.2540 0.0268  -0.0735 -0.0210 306 ALA A N   
1810 C CA  . ALA A 252 ? 0.2667 0.2329 0.2410 0.0131  -0.0731 0.0091  306 ALA A CA  
1811 C C   . ALA A 252 ? 0.2410 0.2416 0.2482 -0.0220 -0.0648 0.0255  306 ALA A C   
1812 O O   . ALA A 252 ? 0.2537 0.2559 0.2689 0.0013  -0.0553 0.0258  306 ALA A O   
1813 C CB  . ALA A 252 ? 0.3269 0.2518 0.2595 0.0366  -0.0878 0.0022  306 ALA A CB  
1814 N N   . GLU A 253 ? 0.2689 0.2410 0.2339 -0.0043 -0.0812 0.0161  307 GLU A N   
1815 C CA  . GLU A 253 ? 0.3062 0.2633 0.2574 0.0266  -0.0908 -0.0310 307 GLU A CA  
1816 C C   . GLU A 253 ? 0.2799 0.2391 0.2562 0.0096  -0.0698 -0.0255 307 GLU A C   
1817 O O   . GLU A 253 ? 0.2898 0.2308 0.2737 -0.0025 -0.0484 -0.0243 307 GLU A O   
1818 C CB  . GLU A 253 ? 0.3538 0.2731 0.2927 0.0331  -0.0998 -0.0633 307 GLU A CB  
1819 C CG  . GLU A 253 ? 0.4516 0.3271 0.3298 0.0353  -0.1180 -0.0589 307 GLU A CG  
1820 C CD  . GLU A 253 ? 0.5122 0.3949 0.3789 0.0353  -0.1318 -0.0740 307 GLU A CD  
1821 O OE1 . GLU A 253 ? 0.5510 0.4140 0.3973 0.0186  -0.1464 -0.0723 307 GLU A OE1 
1822 O OE2 . GLU A 253 ? 0.5772 0.4374 0.4188 0.0299  -0.0993 -0.0753 307 GLU A OE2 
1823 N N   . PHE A 254 ? 0.2689 0.2245 0.2404 0.0125  -0.0521 -0.0124 308 PHE A N   
1824 C CA  . PHE A 254 ? 0.2903 0.2138 0.2203 -0.0079 -0.0403 0.0035  308 PHE A CA  
1825 C C   . PHE A 254 ? 0.2453 0.1952 0.2103 0.0007  -0.0501 0.0016  308 PHE A C   
1826 O O   . PHE A 254 ? 0.2442 0.2207 0.2175 0.0015  -0.0488 0.0012  308 PHE A O   
1827 C CB  . PHE A 254 ? 0.2588 0.2190 0.2005 -0.0063 -0.0413 0.0340  308 PHE A CB  
1828 C CG  . PHE A 254 ? 0.2190 0.2046 0.2171 0.0120  -0.0419 0.0300  308 PHE A CG  
1829 C CD1 . PHE A 254 ? 0.2606 0.2367 0.2181 0.0146  -0.0184 0.0585  308 PHE A CD1 
1830 C CD2 . PHE A 254 ? 0.2405 0.2076 0.2435 -0.0191 -0.0276 -0.0008 308 PHE A CD2 
1831 C CE1 . PHE A 254 ? 0.2845 0.2604 0.2117 0.0204  -0.0050 0.0392  308 PHE A CE1 
1832 C CE2 . PHE A 254 ? 0.2505 0.2325 0.2653 -0.0333 -0.0248 0.0170  308 PHE A CE2 
1833 C CZ  . PHE A 254 ? 0.3061 0.2578 0.2419 -0.0100 -0.0198 0.0130  308 PHE A CZ  
1834 N N   . ALA A 255 ? 0.2422 0.1855 0.2040 -0.0026 -0.0606 0.0061  309 ALA A N   
1835 C CA  . ALA A 255 ? 0.2541 0.2006 0.2014 -0.0047 -0.0488 0.0038  309 ALA A CA  
1836 C C   . ALA A 255 ? 0.2118 0.2232 0.1876 0.0068  -0.0596 0.0296  309 ALA A C   
1837 O O   . ALA A 255 ? 0.2091 0.2328 0.2107 0.0088  -0.0360 0.0257  309 ALA A O   
1838 C CB  . ALA A 255 ? 0.2691 0.1951 0.2108 0.0283  -0.0494 0.0022  309 ALA A CB  
1839 N N   . LEU A 256 ? 0.2645 0.2294 0.1947 0.0022  -0.0484 0.0123  310 LEU A N   
1840 C CA  . LEU A 256 ? 0.2744 0.2312 0.2045 0.0473  -0.0518 0.0060  310 LEU A CA  
1841 C C   . LEU A 256 ? 0.2540 0.2369 0.1966 0.0036  -0.0301 -0.0145 310 LEU A C   
1842 O O   . LEU A 256 ? 0.2655 0.2646 0.2070 0.0218  -0.0461 0.0054  310 LEU A O   
1843 C CB  . LEU A 256 ? 0.2958 0.2866 0.2016 0.0284  -0.0428 0.0049  310 LEU A CB  
1844 C CG  . LEU A 256 ? 0.3465 0.3401 0.2307 -0.0071 -0.0259 0.0095  310 LEU A CG  
1845 C CD1 . LEU A 256 ? 0.4029 0.3901 0.2784 -0.0197 -0.0192 0.0108  310 LEU A CD1 
1846 C CD2 . LEU A 256 ? 0.3987 0.3586 0.2272 -0.0045 -0.0354 -0.0237 310 LEU A CD2 
1847 N N   . SER A 257 ? 0.2511 0.2431 0.2100 0.0291  -0.0350 -0.0385 311 SER A N   
1848 C CA  . SER A 257 ? 0.2767 0.2397 0.2386 0.0469  -0.0323 -0.0162 311 SER A CA  
1849 C C   . SER A 257 ? 0.2812 0.2437 0.2311 0.0368  -0.0282 -0.0003 311 SER A C   
1850 O O   . SER A 257 ? 0.2813 0.3161 0.2399 0.0678  -0.0204 -0.0113 311 SER A O   
1851 C CB  . SER A 257 ? 0.3029 0.2684 0.2607 0.0218  -0.0481 -0.0159 311 SER A CB  
1852 O OG  . SER A 257 ? 0.4236 0.3390 0.3039 0.0027  -0.0447 -0.0239 311 SER A OG  
1853 N N   . ALA A 258 ? 0.2595 0.2126 0.2173 0.0101  -0.0401 0.0086  312 ALA A N   
1854 C CA  . ALA A 258 ? 0.2481 0.2252 0.2155 0.0258  -0.0362 0.0190  312 ALA A CA  
1855 C C   . ALA A 258 ? 0.2280 0.2240 0.2055 0.0372  -0.0157 0.0177  312 ALA A C   
1856 O O   . ALA A 258 ? 0.2617 0.2728 0.2251 0.0432  -0.0179 0.0173  312 ALA A O   
1857 C CB  . ALA A 258 ? 0.2455 0.2380 0.2136 0.0604  0.0172  0.0034  312 ALA A CB  
1858 N N   . LEU A 259 ? 0.2215 0.2217 0.1995 -0.0171 -0.0254 0.0066  313 LEU A N   
1859 C CA  . LEU A 259 ? 0.1865 0.2478 0.2055 0.0238  -0.0134 -0.0023 313 LEU A CA  
1860 C C   . LEU A 259 ? 0.2190 0.3108 0.2322 -0.0081 -0.0167 0.0136  313 LEU A C   
1861 O O   . LEU A 259 ? 0.2087 0.3170 0.2408 0.0005  -0.0221 0.0509  313 LEU A O   
1862 C CB  . LEU A 259 ? 0.2196 0.2351 0.1756 0.0158  -0.0252 0.0212  313 LEU A CB  
1863 C CG  . LEU A 259 ? 0.2466 0.2377 0.1618 0.0433  -0.0259 0.0056  313 LEU A CG  
1864 C CD1 . LEU A 259 ? 0.2386 0.2356 0.1960 0.0330  0.0006  0.0253  313 LEU A CD1 
1865 C CD2 . LEU A 259 ? 0.2833 0.3052 0.1476 0.0185  -0.0257 0.0045  313 LEU A CD2 
1866 N N   . MET A 260 ? 0.2499 0.3513 0.2621 -0.0670 0.0025  0.0038  314 MET A N   
1867 C CA  . MET A 260 ? 0.3173 0.4614 0.3532 -0.1198 0.0032  -0.0261 314 MET A CA  
1868 C C   . MET A 260 ? 0.2801 0.4219 0.3139 -0.0796 -0.0310 -0.0464 314 MET A C   
1869 O O   . MET A 260 ? 0.2912 0.4398 0.2845 -0.0419 -0.0335 -0.0017 314 MET A O   
1870 C CB  . MET A 260 ? 0.5111 0.6755 0.5853 -0.1317 0.0045  -0.0702 314 MET A CB  
1871 C CG  . MET A 260 ? 0.7692 0.8974 0.7725 -0.0948 -0.0003 -0.0985 314 MET A CG  
1872 S SD  . MET A 260 ? 1.0547 1.0527 0.9484 -0.0609 0.0004  -0.1209 314 MET A SD  
1873 C CE  . MET A 260 ? 1.0703 1.1589 1.1125 -0.0356 0.0048  -0.1206 314 MET A CE  
1874 N N   . GLU A 261 ? 0.2368 0.3481 0.3057 -0.0560 -0.0234 -0.0835 315 GLU A N   
1875 C CA  . GLU A 261 ? 0.2045 0.3561 0.3129 -0.0529 0.0104  -0.0378 315 GLU A CA  
1876 C C   . GLU A 261 ? 0.1603 0.3187 0.2670 -0.0326 -0.0143 0.0030  315 GLU A C   
1877 O O   . GLU A 261 ? 0.2039 0.2953 0.2837 -0.0070 -0.0051 0.0137  315 GLU A O   
1878 C CB  . GLU A 261 ? 0.3030 0.3884 0.3612 -0.0207 0.0485  -0.0635 315 GLU A CB  
1879 C CG  . GLU A 261 ? 0.4330 0.4674 0.3948 -0.0120 0.0609  -0.0745 315 GLU A CG  
1880 C CD  . GLU A 261 ? 0.5607 0.5487 0.4483 -0.0060 0.0477  -0.1044 315 GLU A CD  
1881 O OE1 . GLU A 261 ? 0.5773 0.5799 0.4630 0.0075  0.0674  -0.1100 315 GLU A OE1 
1882 O OE2 . GLU A 261 ? 0.6299 0.5935 0.4820 0.0026  0.0387  -0.0992 315 GLU A OE2 
1883 N N   . ILE A 262 ? 0.1911 0.2503 0.2115 0.0189  -0.0030 0.0110  316 ILE A N   
1884 C CA  . ILE A 262 ? 0.2332 0.2380 0.2164 0.0242  -0.0052 0.0019  316 ILE A CA  
1885 C C   . ILE A 262 ? 0.2467 0.2536 0.2035 0.0256  -0.0362 0.0130  316 ILE A C   
1886 O O   . ILE A 262 ? 0.2632 0.2450 0.2039 0.0160  -0.0237 0.0055  316 ILE A O   
1887 C CB  . ILE A 262 ? 0.2797 0.2488 0.2466 0.0035  0.0219  0.0194  316 ILE A CB  
1888 C CG1 . ILE A 262 ? 0.2987 0.2804 0.2574 0.0132  -0.0216 0.0504  316 ILE A CG1 
1889 C CG2 . ILE A 262 ? 0.2920 0.2792 0.2718 0.0186  0.0025  -0.0171 316 ILE A CG2 
1890 C CD1 . ILE A 262 ? 0.3271 0.2887 0.2533 -0.0100 -0.0053 0.0341  316 ILE A CD1 
1891 N N   . PRO A 263 ? 0.2128 0.2602 0.2067 0.0124  -0.0126 0.0443  317 PRO A N   
1892 C CA  . PRO A 263 ? 0.2672 0.2609 0.2344 0.0037  -0.0116 0.0846  317 PRO A CA  
1893 C C   . PRO A 263 ? 0.2852 0.2577 0.2367 -0.0156 -0.0040 0.0690  317 PRO A C   
1894 O O   . PRO A 263 ? 0.2458 0.2767 0.2340 -0.0117 -0.0004 0.0621  317 PRO A O   
1895 C CB  . PRO A 263 ? 0.2796 0.2648 0.2509 -0.0229 -0.0092 0.1022  317 PRO A CB  
1896 C CG  . PRO A 263 ? 0.2466 0.2686 0.2598 -0.0136 -0.0270 0.0880  317 PRO A CG  
1897 C CD  . PRO A 263 ? 0.2134 0.2842 0.2441 0.0016  -0.0596 0.0680  317 PRO A CD  
1898 N N   . SER A 264 ? 0.2380 0.2730 0.2189 0.0197  -0.0101 0.0367  318 SER A N   
1899 C CA  . SER A 264 ? 0.2601 0.3553 0.2216 0.0955  0.0111  0.0241  318 SER A CA  
1900 C C   . SER A 264 ? 0.2373 0.2914 0.2253 -0.0107 0.0194  0.0318  318 SER A C   
1901 O O   . SER A 264 ? 0.2482 0.2886 0.2009 -0.0227 -0.0128 0.0185  318 SER A O   
1902 C CB  . SER A 264 ? 0.3262 0.5336 0.2785 0.2217  -0.0232 -0.0476 318 SER A CB  
1903 O OG  . SER A 264 ? 0.5081 0.6288 0.3186 0.1231  -0.0366 -0.0925 318 SER A OG  
1904 N N   . GLN A 265 ? 0.2102 0.2676 0.1978 -0.0310 -0.0076 0.0126  319 GLN A N   
1905 C CA  . GLN A 265 ? 0.1785 0.2555 0.2029 -0.0232 0.0005  0.0351  319 GLN A CA  
1906 C C   . GLN A 265 ? 0.1889 0.2793 0.1857 -0.0137 -0.0323 0.0428  319 GLN A C   
1907 O O   . GLN A 265 ? 0.1955 0.2547 0.1910 -0.0227 -0.0098 0.0359  319 GLN A O   
1908 C CB  . GLN A 265 ? 0.2092 0.2181 0.2265 0.0033  0.0050  0.0080  319 GLN A CB  
1909 C CG  . GLN A 265 ? 0.2430 0.1879 0.2789 0.0207  0.0181  -0.0077 319 GLN A CG  
1910 C CD  . GLN A 265 ? 0.3005 0.2211 0.3208 0.0387  0.0361  -0.0439 319 GLN A CD  
1911 O OE1 . GLN A 265 ? 0.4050 0.2688 0.3057 -0.0494 0.1082  -0.0265 319 GLN A OE1 
1912 N NE2 . GLN A 265 ? 0.4180 0.2656 0.3696 -0.0153 0.0214  -0.0401 319 GLN A NE2 
1913 N N   . TYR A 266 ? 0.2422 0.2455 0.1955 -0.0167 -0.0174 0.0369  320 TYR A N   
1914 C CA  . TYR A 266 ? 0.2308 0.2278 0.2129 -0.0289 -0.0016 0.0289  320 TYR A CA  
1915 C C   . TYR A 266 ? 0.2593 0.2233 0.2154 -0.0062 -0.0070 0.0384  320 TYR A C   
1916 O O   . TYR A 266 ? 0.2254 0.2360 0.2263 -0.0064 0.0091  0.0494  320 TYR A O   
1917 C CB  . TYR A 266 ? 0.2132 0.2138 0.2347 -0.0049 0.0011  0.0256  320 TYR A CB  
1918 C CG  . TYR A 266 ? 0.2313 0.1981 0.2199 -0.0221 -0.0108 0.0296  320 TYR A CG  
1919 C CD1 . TYR A 266 ? 0.2577 0.2300 0.2367 -0.0229 0.0198  0.0278  320 TYR A CD1 
1920 C CD2 . TYR A 266 ? 0.2476 0.2157 0.2262 -0.0082 -0.0096 0.0398  320 TYR A CD2 
1921 C CE1 . TYR A 266 ? 0.2519 0.2293 0.2559 -0.0199 0.0181  0.0520  320 TYR A CE1 
1922 C CE2 . TYR A 266 ? 0.2603 0.2233 0.2341 -0.0215 0.0159  0.0451  320 TYR A CE2 
1923 C CZ  . TYR A 266 ? 0.2542 0.1995 0.2511 -0.0157 0.0066  0.0610  320 TYR A CZ  
1924 O OH  . TYR A 266 ? 0.2904 0.2001 0.3048 -0.0356 -0.0100 0.0400  320 TYR A OH  
1925 N N   . LYS A 267 ? 0.2546 0.2569 0.2117 -0.0198 0.0065  0.0496  321 LYS A N   
1926 C CA  . LYS A 267 ? 0.2777 0.3039 0.2289 -0.0129 0.0009  0.0791  321 LYS A CA  
1927 C C   . LYS A 267 ? 0.2568 0.2747 0.2122 -0.0432 0.0189  0.0587  321 LYS A C   
1928 O O   . LYS A 267 ? 0.2416 0.2839 0.2320 -0.0495 -0.0017 0.0610  321 LYS A O   
1929 C CB  . LYS A 267 ? 0.3211 0.4022 0.3233 0.0229  0.0317  0.0965  321 LYS A CB  
1930 C CG  . LYS A 267 ? 0.5306 0.5987 0.4868 0.0101  0.0289  0.0893  321 LYS A CG  
1931 C CD  . LYS A 267 ? 0.7231 0.7276 0.6424 0.0196  0.0175  0.0970  321 LYS A CD  
1932 C CE  . LYS A 267 ? 0.8471 0.8305 0.7401 0.0328  0.0200  0.0987  321 LYS A CE  
1933 N NZ  . LYS A 267 ? 0.9037 0.8851 0.7940 0.0433  0.0224  0.1011  321 LYS A NZ  
1934 N N   . ALA A 268 ? 0.2520 0.2843 0.1976 0.0054  -0.0101 0.0455  322 ALA A N   
1935 C CA  . ALA A 268 ? 0.2262 0.2833 0.2203 -0.0166 0.0008  0.0271  322 ALA A CA  
1936 C C   . ALA A 268 ? 0.2334 0.2758 0.2259 -0.0182 0.0274  0.0352  322 ALA A C   
1937 O O   . ALA A 268 ? 0.2297 0.2872 0.2455 -0.0329 0.0274  0.0439  322 ALA A O   
1938 C CB  . ALA A 268 ? 0.2380 0.2723 0.2076 -0.0127 0.0044  -0.0046 322 ALA A CB  
1939 N N   . THR A 269 ? 0.2375 0.2380 0.2027 -0.0011 0.0099  0.0262  323 THR A N   
1940 C CA  . THR A 269 ? 0.2304 0.2571 0.1978 -0.0407 0.0031  0.0078  323 THR A CA  
1941 C C   . THR A 269 ? 0.2327 0.2524 0.2031 -0.0449 -0.0164 0.0388  323 THR A C   
1942 O O   . THR A 269 ? 0.2515 0.2544 0.2230 -0.0488 -0.0236 0.0310  323 THR A O   
1943 C CB  . THR A 269 ? 0.2408 0.2720 0.2161 -0.0244 0.0164  0.0269  323 THR A CB  
1944 O OG1 . THR A 269 ? 0.2244 0.2830 0.2328 -0.0106 0.0082  0.0354  323 THR A OG1 
1945 C CG2 . THR A 269 ? 0.2573 0.2695 0.2083 -0.0622 0.0207  0.0092  323 THR A CG2 
1946 N N   . LEU A 270 ? 0.2181 0.2481 0.2305 -0.0317 0.0042  0.0700  324 LEU A N   
1947 C CA  . LEU A 270 ? 0.2383 0.2476 0.2517 -0.0190 -0.0085 0.0625  324 LEU A CA  
1948 C C   . LEU A 270 ? 0.2379 0.2702 0.2404 -0.0387 -0.0135 0.0523  324 LEU A C   
1949 O O   . LEU A 270 ? 0.2393 0.3199 0.2532 -0.0413 0.0080  0.0563  324 LEU A O   
1950 C CB  . LEU A 270 ? 0.2141 0.2659 0.2635 0.0004  -0.0339 0.0617  324 LEU A CB  
1951 C CG  . LEU A 270 ? 0.3000 0.3061 0.2791 0.0351  -0.0424 0.0564  324 LEU A CG  
1952 C CD1 . LEU A 270 ? 0.3517 0.3177 0.3132 0.0618  -0.0626 0.0804  324 LEU A CD1 
1953 C CD2 . LEU A 270 ? 0.2912 0.3103 0.3053 -0.0241 -0.0262 0.0456  324 LEU A CD2 
1954 N N   . GLU A 271 ? 0.2425 0.2783 0.2433 -0.0191 0.0118  0.0689  325 GLU A N   
1955 C CA  . GLU A 271 ? 0.2378 0.3471 0.2544 0.0095  0.0345  0.0499  325 GLU A CA  
1956 C C   . GLU A 271 ? 0.2153 0.3015 0.2636 -0.0162 0.0079  0.0504  325 GLU A C   
1957 O O   . GLU A 271 ? 0.2551 0.3289 0.2827 -0.0098 0.0080  0.0665  325 GLU A O   
1958 C CB  . GLU A 271 ? 0.2714 0.4254 0.2902 -0.0173 0.0460  0.0004  325 GLU A CB  
1959 C CG  . GLU A 271 ? 0.3276 0.5140 0.3858 0.0106  0.1094  -0.0436 325 GLU A CG  
1960 C CD  . GLU A 271 ? 0.4864 0.6282 0.4866 0.0085  0.0921  -0.0370 325 GLU A CD  
1961 O OE1 . GLU A 271 ? 0.5417 0.6494 0.5138 0.0206  0.0895  -0.0475 325 GLU A OE1 
1962 O OE2 . GLU A 271 ? 0.5429 0.6497 0.5210 0.0283  0.0873  -0.0383 325 GLU A OE2 
1963 N N   . LEU A 272 ? 0.2366 0.2739 0.2465 -0.0172 -0.0012 0.0385  326 LEU A N   
1964 C CA  . LEU A 272 ? 0.2211 0.2673 0.2669 0.0109  0.0187  0.0386  326 LEU A CA  
1965 C C   . LEU A 272 ? 0.2508 0.2528 0.2671 -0.0022 0.0232  0.0527  326 LEU A C   
1966 O O   . LEU A 272 ? 0.3048 0.3047 0.2922 0.0291  -0.0082 0.0653  326 LEU A O   
1967 C CB  . LEU A 272 ? 0.2416 0.2534 0.2987 -0.0187 0.0263  0.0605  326 LEU A CB  
1968 C CG  . LEU A 272 ? 0.2219 0.2898 0.3526 -0.0184 0.0461  0.0270  326 LEU A CG  
1969 C CD1 . LEU A 272 ? 0.2864 0.2802 0.3741 -0.0780 0.0198  0.0573  326 LEU A CD1 
1970 C CD2 . LEU A 272 ? 0.2326 0.3435 0.3752 0.0196  0.0527  0.0091  326 LEU A CD2 
1971 N N   . GLY A 273 ? 0.1944 0.2611 0.2681 -0.0196 0.0201  0.0521  327 GLY A N   
1972 C CA  . GLY A 273 ? 0.2224 0.2606 0.2638 -0.0489 0.0347  0.0641  327 GLY A CA  
1973 C C   . GLY A 273 ? 0.2096 0.2641 0.2525 -0.0535 -0.0093 0.0759  327 GLY A C   
1974 O O   . GLY A 273 ? 0.2661 0.3358 0.2881 -0.0741 -0.0338 0.0779  327 GLY A O   
1975 N N   . LEU A 274 ? 0.2202 0.2597 0.2443 -0.0310 0.0364  0.0598  328 LEU A N   
1976 C CA  . LEU A 274 ? 0.2425 0.2253 0.2263 -0.0264 0.0289  0.0537  328 LEU A CA  
1977 C C   . LEU A 274 ? 0.2247 0.2463 0.2175 -0.0352 -0.0141 0.0357  328 LEU A C   
1978 O O   . LEU A 274 ? 0.2922 0.2666 0.2245 -0.0440 0.0159  0.0323  328 LEU A O   
1979 C CB  . LEU A 274 ? 0.2454 0.2421 0.2199 -0.0253 0.0439  0.0534  328 LEU A CB  
1980 C CG  . LEU A 274 ? 0.2436 0.2545 0.2497 -0.0293 0.0325  0.0319  328 LEU A CG  
1981 C CD1 . LEU A 274 ? 0.2501 0.2511 0.2599 -0.0351 0.0218  0.0323  328 LEU A CD1 
1982 C CD2 . LEU A 274 ? 0.2939 0.2934 0.2906 -0.0047 0.0035  0.0411  328 LEU A CD2 
1983 N N   . LEU A 275 ? 0.2173 0.2315 0.2416 -0.0132 -0.0185 0.0250  329 LEU A N   
1984 C CA  . LEU A 275 ? 0.2078 0.2356 0.2683 -0.0150 0.0181  0.0345  329 LEU A CA  
1985 C C   . LEU A 275 ? 0.2656 0.2539 0.2750 -0.0457 0.0297  0.0532  329 LEU A C   
1986 O O   . LEU A 275 ? 0.2942 0.2589 0.2843 -0.0760 0.0407  0.0418  329 LEU A O   
1987 C CB  . LEU A 275 ? 0.2326 0.2461 0.2757 0.0005  0.0232  0.0622  329 LEU A CB  
1988 C CG  . LEU A 275 ? 0.2541 0.2673 0.2656 -0.0071 0.0239  0.0635  329 LEU A CG  
1989 C CD1 . LEU A 275 ? 0.2425 0.3187 0.2704 -0.0634 0.0172  0.0755  329 LEU A CD1 
1990 C CD2 . LEU A 275 ? 0.2991 0.2448 0.2816 -0.0121 -0.0078 0.0611  329 LEU A CD2 
1991 N N   . GLY A 276 ? 0.2962 0.2375 0.2673 -0.0129 0.0405  0.0285  330 GLY A N   
1992 C CA  . GLY A 276 ? 0.3125 0.2385 0.2892 -0.0261 0.0438  0.0298  330 GLY A CA  
1993 C C   . GLY A 276 ? 0.3284 0.2206 0.2829 -0.0606 0.0382  0.0377  330 GLY A C   
1994 O O   . GLY A 276 ? 0.3737 0.2837 0.3166 -0.1148 -0.0177 -0.0039 330 GLY A O   
1995 N N   . GLN A 277 ? 0.3102 0.2810 0.2869 -0.0468 0.0343  0.0370  331 GLN A N   
1996 C CA  . GLN A 277 ? 0.2892 0.3161 0.3143 -0.0774 0.0305  0.0349  331 GLN A CA  
1997 C C   . GLN A 277 ? 0.3126 0.3298 0.3394 -0.0902 -0.0229 0.0465  331 GLN A C   
1998 O O   . GLN A 277 ? 0.3515 0.3849 0.3633 -0.1275 -0.0755 0.0852  331 GLN A O   
1999 C CB  . GLN A 277 ? 0.2785 0.3172 0.3222 -0.0416 0.0338  0.0336  331 GLN A CB  
2000 C CG  . GLN A 277 ? 0.3069 0.3450 0.3210 -0.0648 0.0078  0.0335  331 GLN A CG  
2001 C CD  . GLN A 277 ? 0.3730 0.3376 0.3207 -0.0793 -0.0214 0.0465  331 GLN A CD  
2002 O OE1 . GLN A 277 ? 0.4107 0.3948 0.3417 -0.0713 -0.0309 0.0015  331 GLN A OE1 
2003 N NE2 . GLN A 277 ? 0.4115 0.3369 0.3073 -0.0682 -0.0350 0.0706  331 GLN A NE2 
2004 N N   . ARG A 278 ? 0.2843 0.3444 0.3301 -0.0502 -0.0343 0.0375  332 ARG A N   
2005 C CA  . ARG A 278 ? 0.2853 0.3557 0.3530 -0.0695 -0.0190 0.0194  332 ARG A CA  
2006 C C   . ARG A 278 ? 0.2541 0.3913 0.3760 -0.0741 0.0147  0.0188  332 ARG A C   
2007 O O   . ARG A 278 ? 0.2578 0.4270 0.3954 -0.0652 0.0024  0.0320  332 ARG A O   
2008 C CB  . ARG A 278 ? 0.3499 0.3894 0.3602 -0.0936 -0.0498 0.0001  332 ARG A CB  
2009 C CG  . ARG A 278 ? 0.3926 0.4439 0.3782 -0.0903 -0.0782 -0.0250 332 ARG A CG  
2010 C CD  . ARG A 278 ? 0.4675 0.5157 0.4461 -0.0516 -0.0683 -0.0347 332 ARG A CD  
2011 N NE  . ARG A 278 ? 0.5692 0.5793 0.4787 -0.0660 -0.0721 -0.0370 332 ARG A NE  
2012 C CZ  . ARG A 278 ? 0.6087 0.5814 0.5197 -0.1306 -0.0743 -0.0419 332 ARG A CZ  
2013 N NH1 . ARG A 278 ? 0.6319 0.5750 0.5306 -0.1692 -0.0876 -0.0515 332 ARG A NH1 
2014 N NH2 . ARG A 278 ? 0.6191 0.5888 0.5396 -0.1334 -0.0619 -0.0532 332 ARG A NH2 
2015 N N   . THR A 279 ? 0.2632 0.4060 0.3747 -0.0490 0.0126  0.0138  333 THR A N   
2016 C CA  . THR A 279 ? 0.2882 0.3944 0.3804 -0.0534 0.0124  0.0257  333 THR A CA  
2017 C C   . THR A 279 ? 0.2869 0.4053 0.4014 -0.0717 -0.0030 0.0450  333 THR A C   
2018 O O   . THR A 279 ? 0.2940 0.4436 0.4451 -0.0532 -0.0117 0.0562  333 THR A O   
2019 C CB  . THR A 279 ? 0.3009 0.3898 0.3564 -0.0762 0.0276  0.0217  333 THR A CB  
2020 O OG1 . THR A 279 ? 0.2918 0.3754 0.3466 -0.0781 0.0002  0.0176  333 THR A OG1 
2021 C CG2 . THR A 279 ? 0.3126 0.4156 0.3435 -0.0368 0.0038  0.0037  333 THR A CG2 
2022 N N   . GLY A 280 ? 0.3112 0.3739 0.3747 -0.0548 -0.0714 0.0501  334 GLY A N   
2023 C CA  . GLY A 280 ? 0.3085 0.3883 0.3937 -0.0800 -0.1093 0.0516  334 GLY A CA  
2024 C C   . GLY A 280 ? 0.3457 0.4054 0.4046 -0.0594 -0.0991 0.0508  334 GLY A C   
2025 O O   . GLY A 280 ? 0.3852 0.4390 0.4123 -0.0364 -0.1282 0.0357  334 GLY A O   
2026 N N   . HIS A 281 ? 0.3196 0.4042 0.4100 -0.0607 -0.1000 0.0582  335 HIS A N   
2027 C CA  . HIS A 281 ? 0.3421 0.4180 0.4318 -0.0770 -0.0858 0.0648  335 HIS A CA  
2028 C C   . HIS A 281 ? 0.3242 0.4055 0.4360 -0.0804 -0.0688 0.0364  335 HIS A C   
2029 O O   . HIS A 281 ? 0.3924 0.4058 0.4420 -0.0419 -0.0483 0.0379  335 HIS A O   
2030 C CB  . HIS A 281 ? 0.4049 0.4705 0.4494 -0.0496 -0.0707 0.0697  335 HIS A CB  
2031 C CG  . HIS A 281 ? 0.4335 0.5168 0.4648 -0.0251 -0.0623 0.0648  335 HIS A CG  
2032 N ND1 . HIS A 281 ? 0.4465 0.5578 0.4783 -0.0098 -0.0519 0.0701  335 HIS A ND1 
2033 C CD2 . HIS A 281 ? 0.4273 0.5380 0.4730 -0.0133 -0.0678 0.0658  335 HIS A CD2 
2034 C CE1 . HIS A 281 ? 0.4370 0.5702 0.4768 0.0004  -0.0679 0.0716  335 HIS A CE1 
2035 N NE2 . HIS A 281 ? 0.4448 0.5485 0.4662 0.0007  -0.0747 0.0701  335 HIS A NE2 
2036 N N   . CYS A 282 ? 0.2570 0.3838 0.4151 -0.0210 -0.0625 0.0497  336 CYS A N   
2037 C CA  . CYS A 282 ? 0.2519 0.3659 0.3974 -0.0874 -0.0532 0.0634  336 CYS A CA  
2038 C C   . CYS A 282 ? 0.2881 0.4106 0.3904 -0.0800 -0.0693 0.0654  336 CYS A C   
2039 O O   . CYS A 282 ? 0.3047 0.4057 0.3984 -0.0504 -0.0808 0.0573  336 CYS A O   
2040 C CB  . CYS A 282 ? 0.2923 0.3568 0.3899 -0.0007 -0.0432 0.0483  336 CYS A CB  
2041 S SG  . CYS A 282 ? 0.3523 0.3918 0.4188 -0.0414 -0.0312 0.0404  336 CYS A SG  
2042 N N   . PRO A 283 ? 0.2617 0.4037 0.3858 -0.1109 -0.0688 0.0812  337 PRO A N   
2043 C CA  . PRO A 283 ? 0.3108 0.3831 0.3748 -0.1034 -0.0834 0.1053  337 PRO A CA  
2044 C C   . PRO A 283 ? 0.3300 0.4020 0.3916 -0.0782 -0.0806 0.1012  337 PRO A C   
2045 O O   . PRO A 283 ? 0.3795 0.4126 0.3993 -0.0956 -0.0614 0.1024  337 PRO A O   
2046 C CB  . PRO A 283 ? 0.3136 0.3540 0.3628 -0.1328 -0.1037 0.1241  337 PRO A CB  
2047 C CG  . PRO A 283 ? 0.3023 0.3816 0.3650 -0.1039 -0.0911 0.1371  337 PRO A CG  
2048 C CD  . PRO A 283 ? 0.2409 0.4027 0.3742 -0.1121 -0.0826 0.0890  337 PRO A CD  
2049 N N   . ASP A 284 ? 0.3424 0.3905 0.3828 -0.0932 -0.0864 0.0686  338 ASP A N   
2050 C CA  . ASP A 284 ? 0.3594 0.4350 0.3799 -0.0926 -0.1195 0.0555  338 ASP A CA  
2051 C C   . ASP A 284 ? 0.3016 0.3903 0.3152 -0.0261 -0.1140 0.0639  338 ASP A C   
2052 O O   . ASP A 284 ? 0.3287 0.4342 0.3227 -0.0646 -0.1212 0.0414  338 ASP A O   
2053 C CB  . ASP A 284 ? 0.4568 0.5799 0.5006 -0.1226 -0.1313 0.0569  338 ASP A CB  
2054 C CG  . ASP A 284 ? 0.6585 0.7271 0.6223 -0.1115 -0.1394 0.0218  338 ASP A CG  
2055 O OD1 . ASP A 284 ? 0.7207 0.7449 0.6488 -0.1058 -0.1163 0.0213  338 ASP A OD1 
2056 O OD2 . ASP A 284 ? 0.7304 0.8023 0.7047 -0.1176 -0.1360 0.0106  338 ASP A OD2 
2057 N N   . ARG A 285 ? 0.2491 0.3077 0.2937 -0.0225 -0.0842 0.0393  339 ARG A N   
2058 C CA  . ARG A 285 ? 0.2545 0.2669 0.2760 -0.0220 -0.0829 0.0204  339 ARG A CA  
2059 C C   . ARG A 285 ? 0.2737 0.2598 0.2778 -0.0007 -0.0821 0.0255  339 ARG A C   
2060 O O   . ARG A 285 ? 0.2990 0.2694 0.2892 0.0079  -0.1123 0.0052  339 ARG A O   
2061 C CB  . ARG A 285 ? 0.2456 0.2803 0.3010 -0.0410 -0.0400 -0.0065 339 ARG A CB  
2062 C CG  . ARG A 285 ? 0.2594 0.2764 0.3161 -0.0233 -0.0335 -0.0171 339 ARG A CG  
2063 C CD  . ARG A 285 ? 0.2306 0.2691 0.3170 0.0309  -0.0587 -0.0100 339 ARG A CD  
2064 N NE  . ARG A 285 ? 0.2745 0.2490 0.3241 0.0012  -0.0642 0.0407  339 ARG A NE  
2065 C CZ  . ARG A 285 ? 0.2344 0.3107 0.3274 0.0070  -0.0356 0.0596  339 ARG A CZ  
2066 N NH1 . ARG A 285 ? 0.2589 0.3128 0.3259 -0.0011 -0.0247 0.0682  339 ARG A NH1 
2067 N NH2 . ARG A 285 ? 0.3022 0.3267 0.3509 0.0139  -0.0156 0.0433  339 ARG A NH2 
2068 N N   . ILE A 286 ? 0.2925 0.2897 0.3057 -0.0283 -0.0407 -0.0289 340 ILE A N   
2069 C CA  . ILE A 286 ? 0.3049 0.2986 0.3106 -0.0167 -0.0428 -0.0402 340 ILE A CA  
2070 C C   . ILE A 286 ? 0.2389 0.2558 0.3054 0.0317  -0.0367 -0.0201 340 ILE A C   
2071 O O   . ILE A 286 ? 0.2826 0.2831 0.3758 0.0354  -0.0628 -0.0132 340 ILE A O   
2072 C CB  . ILE A 286 ? 0.3649 0.3583 0.3426 -0.0302 -0.0445 -0.0672 340 ILE A CB  
2073 C CG1 . ILE A 286 ? 0.3986 0.4128 0.3707 -0.0504 -0.0340 -0.0639 340 ILE A CG1 
2074 C CG2 . ILE A 286 ? 0.4127 0.3974 0.3658 -0.0266 -0.0461 -0.0598 340 ILE A CG2 
2075 C CD1 . ILE A 286 ? 0.4582 0.4440 0.3972 -0.0204 -0.0319 -0.0772 340 ILE A CD1 
2076 N N   . ALA A 287 ? 0.2379 0.2270 0.2457 -0.0071 -0.0256 -0.0108 341 ALA A N   
2077 C CA  . ALA A 287 ? 0.2393 0.2434 0.2320 0.0314  -0.0227 -0.0201 341 ALA A CA  
2078 C C   . ALA A 287 ? 0.2638 0.2418 0.2271 -0.0151 -0.0427 -0.0147 341 ALA A C   
2079 O O   . ALA A 287 ? 0.3313 0.2762 0.2676 -0.0439 -0.0108 -0.0417 341 ALA A O   
2080 C CB  . ALA A 287 ? 0.2821 0.2610 0.2398 0.0212  -0.0553 0.0028  341 ALA A CB  
2081 N N   . LEU A 288 ? 0.2567 0.2774 0.2124 0.0022  -0.0216 0.0139  342 LEU A N   
2082 C CA  . LEU A 288 ? 0.2850 0.2693 0.2151 0.0055  0.0062  0.0067  342 LEU A CA  
2083 C C   . LEU A 288 ? 0.3093 0.2872 0.1993 0.0157  0.0067  -0.0246 342 LEU A C   
2084 O O   . LEU A 288 ? 0.2820 0.2745 0.1766 0.0213  0.0239  -0.0076 342 LEU A O   
2085 C CB  . LEU A 288 ? 0.3241 0.2674 0.2312 0.0195  -0.0261 0.0135  342 LEU A CB  
2086 C CG  . LEU A 288 ? 0.3665 0.2567 0.2589 0.0388  -0.0683 0.0251  342 LEU A CG  
2087 C CD1 . LEU A 288 ? 0.3687 0.2876 0.2569 0.0443  -0.0332 0.0179  342 LEU A CD1 
2088 C CD2 . LEU A 288 ? 0.4274 0.3516 0.3202 0.0399  -0.0453 0.0072  342 LEU A CD2 
2089 N N   . PRO A 289 ? 0.3318 0.3554 0.2008 0.0325  0.0313  -0.0312 343 PRO A N   
2090 C CA  . PRO A 289 ? 0.3455 0.3480 0.2043 0.0415  0.0422  -0.0329 343 PRO A CA  
2091 C C   . PRO A 289 ? 0.2864 0.3113 0.2335 0.0545  0.0590  0.0137  343 PRO A C   
2092 O O   . PRO A 289 ? 0.3445 0.3378 0.2234 0.0471  0.0600  0.0192  343 PRO A O   
2093 C CB  . PRO A 289 ? 0.3914 0.4152 0.2104 0.0415  0.0367  -0.0325 343 PRO A CB  
2094 C CG  . PRO A 289 ? 0.4125 0.4387 0.2214 0.0924  0.0387  -0.0319 343 PRO A CG  
2095 C CD  . PRO A 289 ? 0.3671 0.4205 0.2014 0.0720  0.0420  -0.0375 343 PRO A CD  
2096 N N   . PRO A 290 ? 0.3151 0.2396 0.2611 0.0593  0.0372  0.0128  344 PRO A N   
2097 C CA  . PRO A 290 ? 0.3362 0.2940 0.2501 0.0300  0.0666  0.0253  344 PRO A CA  
2098 C C   . PRO A 290 ? 0.3538 0.3242 0.2621 0.0680  0.1659  -0.0095 344 PRO A C   
2099 O O   . PRO A 290 ? 0.4707 0.3900 0.2715 0.0846  0.1844  -0.0002 344 PRO A O   
2100 C CB  . PRO A 290 ? 0.3303 0.3000 0.2734 0.0446  0.0373  0.0249  344 PRO A CB  
2101 C CG  . PRO A 290 ? 0.2802 0.2928 0.2851 0.0522  0.0501  0.0089  344 PRO A CG  
2102 C CD  . PRO A 290 ? 0.2980 0.2791 0.2926 0.0628  0.0583  0.0162  344 PRO A CD  
# 
