data_9MJQ
# 
_entry.id   9MJQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9MJQ         pdb_00009mjq 10.2210/pdb9mjq/pdb 
WWPDB D_1000291132 ?            ?                   
# 
_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                        9MJQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-16 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 swlovell@ku.edu                    Scott    Lovell ? 'principal investigator/group leader' 0000-0002-3215-4472 
3 isabelle.phan@seattlechildrens.org Isabelle Phan   ? 'principal investigator/group leader' 0000-0001-6873-3401 
4 julie.early@seattlechildrens.org   Julie    Early  ? 'principal investigator/group leader' 0000-0003-1224-2747 
5 peter.myler@seattlechildrens.org   Peter    Myler  ? 'principal investigator/group leader' 0000-0002-0056-0513 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Seattle Structural Genomics Center for Infectious Disease'          1 ? 
'Seattle Structural Genomics Center for Infectious Disease (SSGCID)' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of Purine nucleoside phosphorylase from Trichomonas vaginalis (inosine bound)' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ung, A.R.'      1 0000-0002-9906-0710 
primary 'Lovell, S.'     2 0000-0002-3215-4472 
primary 'Liu, L.'        3 0000-0003-0514-281X 
primary 'Battaile, K.P.' 4 0000-0003-0833-3259 
# 
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 'Purine nucleoside phosphorylase, putative' 26643.428 1   ? ? ? ? 
2 non-polymer syn INOSINE                                     268.226   1   ? ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                              35.453    3   ? ? ? ? 
4 water       nat water                                       18.015    197 ? ? ? ? 
# 
_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       
;MAHHHHHHMATPHNSAKVGDFAETVLMCGDPLRAKLIADNYLENAKQVNSVRGMLGFTGTYKGKPLSVMGHGMGIPSISI
YAEELYNVYKVKTIIRVGTCGTVDPNVHVRDVCIVTASGTDSNVNRMRLLGHDFPATANFEVVSALVESAKALNIPTQVG
KAYSTDIFYSKEQGLNEALAQYHFIAVEMESAGLFPIADYYGARAGCICTVSDHIITHESATPEERQTSFQNMIKIALEA
TLKL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAHHHHHHMATPHNSAKVGDFAETVLMCGDPLRAKLIADNYLENAKQVNSVRGMLGFTGTYKGKPLSVMGHGMGIPSISI
YAEELYNVYKVKTIIRVGTCGTVDPNVHVRDVCIVTASGTDSNVNRMRLLGHDFPATANFEVVSALVESAKALNIPTQVG
KAYSTDIFYSKEQGLNEALAQYHFIAVEMESAGLFPIADYYGARAGCICTVSDHIITHESATPEERQTSFQNMIKIALEA
TLKL
;
_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 INOSINE        NOS 
3 'CHLORIDE ION' CL  
4 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   MET n 
1 10  ALA n 
1 11  THR n 
1 12  PRO n 
1 13  HIS n 
1 14  ASN n 
1 15  SER n 
1 16  ALA n 
1 17  LYS n 
1 18  VAL n 
1 19  GLY n 
1 20  ASP n 
1 21  PHE n 
1 22  ALA n 
1 23  GLU n 
1 24  THR n 
1 25  VAL n 
1 26  LEU n 
1 27  MET n 
1 28  CYS n 
1 29  GLY n 
1 30  ASP n 
1 31  PRO n 
1 32  LEU n 
1 33  ARG n 
1 34  ALA n 
1 35  LYS n 
1 36  LEU n 
1 37  ILE n 
1 38  ALA n 
1 39  ASP n 
1 40  ASN n 
1 41  TYR n 
1 42  LEU n 
1 43  GLU n 
1 44  ASN n 
1 45  ALA n 
1 46  LYS n 
1 47  GLN n 
1 48  VAL n 
1 49  ASN n 
1 50  SER n 
1 51  VAL n 
1 52  ARG n 
1 53  GLY n 
1 54  MET n 
1 55  LEU n 
1 56  GLY n 
1 57  PHE n 
1 58  THR n 
1 59  GLY n 
1 60  THR n 
1 61  TYR n 
1 62  LYS n 
1 63  GLY n 
1 64  LYS n 
1 65  PRO n 
1 66  LEU n 
1 67  SER n 
1 68  VAL n 
1 69  MET n 
1 70  GLY n 
1 71  HIS n 
1 72  GLY n 
1 73  MET n 
1 74  GLY n 
1 75  ILE n 
1 76  PRO n 
1 77  SER n 
1 78  ILE n 
1 79  SER n 
1 80  ILE n 
1 81  TYR n 
1 82  ALA n 
1 83  GLU n 
1 84  GLU n 
1 85  LEU n 
1 86  TYR n 
1 87  ASN n 
1 88  VAL n 
1 89  TYR n 
1 90  LYS n 
1 91  VAL n 
1 92  LYS n 
1 93  THR n 
1 94  ILE n 
1 95  ILE n 
1 96  ARG n 
1 97  VAL n 
1 98  GLY n 
1 99  THR n 
1 100 CYS n 
1 101 GLY n 
1 102 THR n 
1 103 VAL n 
1 104 ASP n 
1 105 PRO n 
1 106 ASN n 
1 107 VAL n 
1 108 HIS n 
1 109 VAL n 
1 110 ARG n 
1 111 ASP n 
1 112 VAL n 
1 113 CYS n 
1 114 ILE n 
1 115 VAL n 
1 116 THR n 
1 117 ALA n 
1 118 SER n 
1 119 GLY n 
1 120 THR n 
1 121 ASP n 
1 122 SER n 
1 123 ASN n 
1 124 VAL n 
1 125 ASN n 
1 126 ARG n 
1 127 MET n 
1 128 ARG n 
1 129 LEU n 
1 130 LEU n 
1 131 GLY n 
1 132 HIS n 
1 133 ASP n 
1 134 PHE n 
1 135 PRO n 
1 136 ALA n 
1 137 THR n 
1 138 ALA n 
1 139 ASN n 
1 140 PHE n 
1 141 GLU n 
1 142 VAL n 
1 143 VAL n 
1 144 SER n 
1 145 ALA n 
1 146 LEU n 
1 147 VAL n 
1 148 GLU n 
1 149 SER n 
1 150 ALA n 
1 151 LYS n 
1 152 ALA n 
1 153 LEU n 
1 154 ASN n 
1 155 ILE n 
1 156 PRO n 
1 157 THR n 
1 158 GLN n 
1 159 VAL n 
1 160 GLY n 
1 161 LYS n 
1 162 ALA n 
1 163 TYR n 
1 164 SER n 
1 165 THR n 
1 166 ASP n 
1 167 ILE n 
1 168 PHE n 
1 169 TYR n 
1 170 SER n 
1 171 LYS n 
1 172 GLU n 
1 173 GLN n 
1 174 GLY n 
1 175 LEU n 
1 176 ASN n 
1 177 GLU n 
1 178 ALA n 
1 179 LEU n 
1 180 ALA n 
1 181 GLN n 
1 182 TYR n 
1 183 HIS n 
1 184 PHE n 
1 185 ILE n 
1 186 ALA n 
1 187 VAL n 
1 188 GLU n 
1 189 MET n 
1 190 GLU n 
1 191 SER n 
1 192 ALA n 
1 193 GLY n 
1 194 LEU n 
1 195 PHE n 
1 196 PRO n 
1 197 ILE n 
1 198 ALA n 
1 199 ASP n 
1 200 TYR n 
1 201 TYR n 
1 202 GLY n 
1 203 ALA n 
1 204 ARG n 
1 205 ALA n 
1 206 GLY n 
1 207 CYS n 
1 208 ILE n 
1 209 CYS n 
1 210 THR n 
1 211 VAL n 
1 212 SER n 
1 213 ASP n 
1 214 HIS n 
1 215 ILE n 
1 216 ILE n 
1 217 THR n 
1 218 HIS n 
1 219 GLU n 
1 220 SER n 
1 221 ALA n 
1 222 THR n 
1 223 PRO n 
1 224 GLU n 
1 225 GLU n 
1 226 ARG n 
1 227 GLN n 
1 228 THR n 
1 229 SER n 
1 230 PHE n 
1 231 GLN n 
1 232 ASN n 
1 233 MET n 
1 234 ILE n 
1 235 LYS n 
1 236 ILE n 
1 237 ALA n 
1 238 LEU n 
1 239 GLU n 
1 240 ALA n 
1 241 THR n 
1 242 LEU n 
1 243 LYS n 
1 244 LEU 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                   244 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 TVAG_454490 
_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      'Trichomonas vaginalis G3' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     412133 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       TrvaA.01033.d.B1 
_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 
NOS non-polymer         . INOSINE         ? 'C10 H12 N4 O5'  268.226 
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 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -7  ?   ?   ?   A . n 
A 1 2   ALA 2   -6  ?   ?   ?   A . n 
A 1 3   HIS 3   -5  ?   ?   ?   A . n 
A 1 4   HIS 4   -4  -4  HIS HIS A . n 
A 1 5   HIS 5   -3  -3  HIS HIS A . n 
A 1 6   HIS 6   -2  -2  HIS HIS A . n 
A 1 7   HIS 7   -1  -1  HIS HIS A . n 
A 1 8   HIS 8   0   0   HIS HIS A . n 
A 1 9   MET 9   1   1   MET MET A . n 
A 1 10  ALA 10  2   2   ALA ALA A . n 
A 1 11  THR 11  3   3   THR THR A . n 
A 1 12  PRO 12  4   4   PRO PRO A . n 
A 1 13  HIS 13  5   5   HIS HIS A . n 
A 1 14  ASN 14  6   6   ASN ASN A . n 
A 1 15  SER 15  7   7   SER SER A . n 
A 1 16  ALA 16  8   8   ALA ALA A . n 
A 1 17  LYS 17  9   9   LYS LYS A . n 
A 1 18  VAL 18  10  10  VAL VAL A . n 
A 1 19  GLY 19  11  11  GLY GLY A . n 
A 1 20  ASP 20  12  12  ASP ASP A . n 
A 1 21  PHE 21  13  13  PHE PHE A . n 
A 1 22  ALA 22  14  14  ALA ALA A . n 
A 1 23  GLU 23  15  15  GLU GLU A . n 
A 1 24  THR 24  16  16  THR THR A . n 
A 1 25  VAL 25  17  17  VAL VAL A . n 
A 1 26  LEU 26  18  18  LEU LEU A . n 
A 1 27  MET 27  19  19  MET MET A . n 
A 1 28  CYS 28  20  20  CYS CYS A . n 
A 1 29  GLY 29  21  21  GLY GLY A . n 
A 1 30  ASP 30  22  22  ASP ASP A . n 
A 1 31  PRO 31  23  23  PRO PRO A . n 
A 1 32  LEU 32  24  24  LEU LEU A . n 
A 1 33  ARG 33  25  25  ARG ARG A . n 
A 1 34  ALA 34  26  26  ALA ALA A . n 
A 1 35  LYS 35  27  27  LYS LYS A . n 
A 1 36  LEU 36  28  28  LEU LEU A . n 
A 1 37  ILE 37  29  29  ILE ILE A . n 
A 1 38  ALA 38  30  30  ALA ALA A . n 
A 1 39  ASP 39  31  31  ASP ASP A . n 
A 1 40  ASN 40  32  32  ASN ASN A . n 
A 1 41  TYR 41  33  33  TYR TYR A . n 
A 1 42  LEU 42  34  34  LEU LEU A . n 
A 1 43  GLU 43  35  35  GLU GLU A . n 
A 1 44  ASN 44  36  36  ASN ASN A . n 
A 1 45  ALA 45  37  37  ALA ALA A . n 
A 1 46  LYS 46  38  38  LYS LYS A . n 
A 1 47  GLN 47  39  39  GLN GLN A . n 
A 1 48  VAL 48  40  40  VAL VAL A . n 
A 1 49  ASN 49  41  41  ASN ASN A . n 
A 1 50  SER 50  42  42  SER SER A . n 
A 1 51  VAL 51  43  43  VAL VAL A . n 
A 1 52  ARG 52  44  44  ARG ARG A . n 
A 1 53  GLY 53  45  45  GLY GLY A . n 
A 1 54  MET 54  46  46  MET MET A . n 
A 1 55  LEU 55  47  47  LEU LEU A . n 
A 1 56  GLY 56  48  48  GLY GLY A . n 
A 1 57  PHE 57  49  49  PHE PHE A . n 
A 1 58  THR 58  50  50  THR THR A . n 
A 1 59  GLY 59  51  51  GLY GLY A . n 
A 1 60  THR 60  52  52  THR THR A . n 
A 1 61  TYR 61  53  53  TYR TYR A . n 
A 1 62  LYS 62  54  54  LYS LYS A . n 
A 1 63  GLY 63  55  55  GLY GLY A . n 
A 1 64  LYS 64  56  56  LYS LYS A . n 
A 1 65  PRO 65  57  57  PRO PRO A . n 
A 1 66  LEU 66  58  58  LEU LEU A . n 
A 1 67  SER 67  59  59  SER SER A . n 
A 1 68  VAL 68  60  60  VAL VAL A . n 
A 1 69  MET 69  61  61  MET MET A . n 
A 1 70  GLY 70  62  62  GLY GLY A . n 
A 1 71  HIS 71  63  63  HIS HIS A . n 
A 1 72  GLY 72  64  64  GLY GLY A . n 
A 1 73  MET 73  65  65  MET MET A . n 
A 1 74  GLY 74  66  66  GLY GLY A . n 
A 1 75  ILE 75  67  67  ILE ILE A . n 
A 1 76  PRO 76  68  68  PRO PRO A . n 
A 1 77  SER 77  69  69  SER SER A . n 
A 1 78  ILE 78  70  70  ILE ILE A . n 
A 1 79  SER 79  71  71  SER SER A . n 
A 1 80  ILE 80  72  72  ILE ILE A . n 
A 1 81  TYR 81  73  73  TYR TYR A . n 
A 1 82  ALA 82  74  74  ALA ALA A . n 
A 1 83  GLU 83  75  75  GLU GLU A . n 
A 1 84  GLU 84  76  76  GLU GLU A . n 
A 1 85  LEU 85  77  77  LEU LEU A . n 
A 1 86  TYR 86  78  78  TYR TYR A . n 
A 1 87  ASN 87  79  79  ASN ASN A . n 
A 1 88  VAL 88  80  80  VAL VAL A . n 
A 1 89  TYR 89  81  81  TYR TYR A . n 
A 1 90  LYS 90  82  82  LYS LYS A . n 
A 1 91  VAL 91  83  83  VAL VAL A . n 
A 1 92  LYS 92  84  84  LYS LYS A . n 
A 1 93  THR 93  85  85  THR THR A . n 
A 1 94  ILE 94  86  86  ILE ILE A . n 
A 1 95  ILE 95  87  87  ILE ILE A . n 
A 1 96  ARG 96  88  88  ARG ARG A . n 
A 1 97  VAL 97  89  89  VAL VAL A . n 
A 1 98  GLY 98  90  90  GLY GLY A . n 
A 1 99  THR 99  91  91  THR THR A . n 
A 1 100 CYS 100 92  92  CYS CYS A . n 
A 1 101 GLY 101 93  93  GLY GLY A . n 
A 1 102 THR 102 94  94  THR THR A . n 
A 1 103 VAL 103 95  95  VAL VAL A . n 
A 1 104 ASP 104 96  96  ASP ASP A . n 
A 1 105 PRO 105 97  97  PRO PRO A . n 
A 1 106 ASN 106 98  98  ASN ASN A . n 
A 1 107 VAL 107 99  99  VAL VAL A . n 
A 1 108 HIS 108 100 100 HIS HIS A . n 
A 1 109 VAL 109 101 101 VAL VAL A . n 
A 1 110 ARG 110 102 102 ARG ARG A . n 
A 1 111 ASP 111 103 103 ASP ASP A . n 
A 1 112 VAL 112 104 104 VAL VAL A . n 
A 1 113 CYS 113 105 105 CYS CYS A . n 
A 1 114 ILE 114 106 106 ILE ILE A . n 
A 1 115 VAL 115 107 107 VAL VAL A . n 
A 1 116 THR 116 108 108 THR THR A . n 
A 1 117 ALA 117 109 109 ALA ALA A . n 
A 1 118 SER 118 110 110 SER SER A . n 
A 1 119 GLY 119 111 111 GLY GLY A . n 
A 1 120 THR 120 112 112 THR THR A . n 
A 1 121 ASP 121 113 113 ASP ASP A . n 
A 1 122 SER 122 114 114 SER SER A . n 
A 1 123 ASN 123 115 115 ASN ASN A . n 
A 1 124 VAL 124 116 116 VAL VAL A . n 
A 1 125 ASN 125 117 117 ASN ASN A . n 
A 1 126 ARG 126 118 118 ARG ARG A . n 
A 1 127 MET 127 119 119 MET MET A . n 
A 1 128 ARG 128 120 120 ARG ARG A . n 
A 1 129 LEU 129 121 121 LEU LEU A . n 
A 1 130 LEU 130 122 122 LEU LEU A . n 
A 1 131 GLY 131 123 123 GLY GLY A . n 
A 1 132 HIS 132 124 124 HIS HIS A . n 
A 1 133 ASP 133 125 125 ASP ASP A . n 
A 1 134 PHE 134 126 126 PHE PHE A . n 
A 1 135 PRO 135 127 127 PRO PRO A . n 
A 1 136 ALA 136 128 128 ALA ALA A . n 
A 1 137 THR 137 129 129 THR THR A . n 
A 1 138 ALA 138 130 130 ALA ALA A . n 
A 1 139 ASN 139 131 131 ASN ASN A . n 
A 1 140 PHE 140 132 132 PHE PHE A . n 
A 1 141 GLU 141 133 133 GLU GLU A . n 
A 1 142 VAL 142 134 134 VAL VAL A . n 
A 1 143 VAL 143 135 135 VAL VAL A . n 
A 1 144 SER 144 136 136 SER SER A . n 
A 1 145 ALA 145 137 137 ALA ALA A . n 
A 1 146 LEU 146 138 138 LEU LEU A . n 
A 1 147 VAL 147 139 139 VAL VAL A . n 
A 1 148 GLU 148 140 140 GLU GLU A . n 
A 1 149 SER 149 141 141 SER SER A . n 
A 1 150 ALA 150 142 142 ALA ALA A . n 
A 1 151 LYS 151 143 143 LYS LYS A . n 
A 1 152 ALA 152 144 144 ALA ALA A . n 
A 1 153 LEU 153 145 145 LEU LEU A . n 
A 1 154 ASN 154 146 146 ASN ASN A . n 
A 1 155 ILE 155 147 147 ILE ILE A . n 
A 1 156 PRO 156 148 148 PRO PRO A . n 
A 1 157 THR 157 149 149 THR THR A . n 
A 1 158 GLN 158 150 150 GLN GLN A . n 
A 1 159 VAL 159 151 151 VAL VAL A . n 
A 1 160 GLY 160 152 152 GLY GLY A . n 
A 1 161 LYS 161 153 153 LYS LYS A . n 
A 1 162 ALA 162 154 154 ALA ALA A . n 
A 1 163 TYR 163 155 155 TYR TYR A . n 
A 1 164 SER 164 156 156 SER SER A . n 
A 1 165 THR 165 157 157 THR THR A . n 
A 1 166 ASP 166 158 158 ASP ASP A . n 
A 1 167 ILE 167 159 159 ILE ILE A . n 
A 1 168 PHE 168 160 160 PHE PHE A . n 
A 1 169 TYR 169 161 161 TYR TYR A . n 
A 1 170 SER 170 162 162 SER SER A . n 
A 1 171 LYS 171 163 163 LYS LYS A . n 
A 1 172 GLU 172 164 164 GLU GLU A . n 
A 1 173 GLN 173 165 165 GLN GLN A . n 
A 1 174 GLY 174 166 166 GLY GLY A . n 
A 1 175 LEU 175 167 167 LEU LEU A . n 
A 1 176 ASN 176 168 168 ASN ASN A . n 
A 1 177 GLU 177 169 169 GLU GLU A . n 
A 1 178 ALA 178 170 170 ALA ALA A . n 
A 1 179 LEU 179 171 171 LEU LEU A . n 
A 1 180 ALA 180 172 172 ALA ALA A . n 
A 1 181 GLN 181 173 173 GLN GLN A . n 
A 1 182 TYR 182 174 174 TYR TYR A . n 
A 1 183 HIS 183 175 175 HIS HIS A . n 
A 1 184 PHE 184 176 176 PHE PHE A . n 
A 1 185 ILE 185 177 177 ILE ILE A . n 
A 1 186 ALA 186 178 178 ALA ALA A . n 
A 1 187 VAL 187 179 179 VAL VAL A . n 
A 1 188 GLU 188 180 180 GLU GLU A . n 
A 1 189 MET 189 181 181 MET MET A . n 
A 1 190 GLU 190 182 182 GLU GLU A . n 
A 1 191 SER 191 183 183 SER SER A . n 
A 1 192 ALA 192 184 184 ALA ALA A . n 
A 1 193 GLY 193 185 185 GLY GLY A . n 
A 1 194 LEU 194 186 186 LEU LEU A . n 
A 1 195 PHE 195 187 187 PHE PHE A . n 
A 1 196 PRO 196 188 188 PRO PRO A . n 
A 1 197 ILE 197 189 189 ILE ILE A . n 
A 1 198 ALA 198 190 190 ALA ALA A . n 
A 1 199 ASP 199 191 191 ASP ASP A . n 
A 1 200 TYR 200 192 192 TYR TYR A . n 
A 1 201 TYR 201 193 193 TYR TYR A . n 
A 1 202 GLY 202 194 194 GLY GLY A . n 
A 1 203 ALA 203 195 195 ALA ALA A . n 
A 1 204 ARG 204 196 196 ARG ARG A . n 
A 1 205 ALA 205 197 197 ALA ALA A . n 
A 1 206 GLY 206 198 198 GLY GLY A . n 
A 1 207 CYS 207 199 199 CYS CYS A . n 
A 1 208 ILE 208 200 200 ILE ILE A . n 
A 1 209 CYS 209 201 201 CYS CYS A . n 
A 1 210 THR 210 202 202 THR THR A . n 
A 1 211 VAL 211 203 203 VAL VAL A . n 
A 1 212 SER 212 204 204 SER SER A . n 
A 1 213 ASP 213 205 205 ASP ASP A . n 
A 1 214 HIS 214 206 206 HIS HIS A . n 
A 1 215 ILE 215 207 207 ILE ILE A . n 
A 1 216 ILE 216 208 208 ILE ILE A . n 
A 1 217 THR 217 209 209 THR THR A . n 
A 1 218 HIS 218 210 210 HIS HIS A . n 
A 1 219 GLU 219 211 211 GLU GLU A . n 
A 1 220 SER 220 212 212 SER SER A . n 
A 1 221 ALA 221 213 213 ALA ALA A . n 
A 1 222 THR 222 214 214 THR THR A . n 
A 1 223 PRO 223 215 215 PRO PRO A . n 
A 1 224 GLU 224 216 216 GLU GLU A . n 
A 1 225 GLU 225 217 217 GLU GLU A . n 
A 1 226 ARG 226 218 218 ARG ARG A . n 
A 1 227 GLN 227 219 219 GLN GLN A . n 
A 1 228 THR 228 220 220 THR THR A . n 
A 1 229 SER 229 221 221 SER SER A . n 
A 1 230 PHE 230 222 222 PHE PHE A . n 
A 1 231 GLN 231 223 223 GLN GLN A . n 
A 1 232 ASN 232 224 224 ASN ASN A . n 
A 1 233 MET 233 225 225 MET MET A . n 
A 1 234 ILE 234 226 226 ILE ILE A . n 
A 1 235 LYS 235 227 227 LYS LYS A . n 
A 1 236 ILE 236 228 228 ILE ILE A . n 
A 1 237 ALA 237 229 229 ALA ALA A . n 
A 1 238 LEU 238 230 230 LEU LEU A . n 
A 1 239 GLU 239 231 231 GLU GLU A . n 
A 1 240 ALA 240 232 232 ALA ALA A . n 
A 1 241 THR 241 233 233 THR THR A . n 
A 1 242 LEU 242 234 234 LEU LEU A . n 
A 1 243 LYS 243 235 235 LYS LYS A . n 
A 1 244 LEU 244 236 236 LEU LEU A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NOS 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NOS 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NOS 1   301 301 NOS NOS A . 
C 3 CL  1   302 1   CL  CL  A . 
D 3 CL  1   303 2   CL  CL  A . 
E 3 CL  1   304 3   CL  CL  A . 
F 4 HOH 1   401 113 HOH HOH A . 
F 4 HOH 2   402 66  HOH HOH A . 
F 4 HOH 3   403 101 HOH HOH A . 
F 4 HOH 4   404 88  HOH HOH A . 
F 4 HOH 5   405 193 HOH HOH A . 
F 4 HOH 6   406 159 HOH HOH A . 
F 4 HOH 7   407 90  HOH HOH A . 
F 4 HOH 8   408 163 HOH HOH A . 
F 4 HOH 9   409 161 HOH HOH A . 
F 4 HOH 10  410 59  HOH HOH A . 
F 4 HOH 11  411 137 HOH HOH A . 
F 4 HOH 12  412 173 HOH HOH A . 
F 4 HOH 13  413 108 HOH HOH A . 
F 4 HOH 14  414 95  HOH HOH A . 
F 4 HOH 15  415 180 HOH HOH A . 
F 4 HOH 16  416 105 HOH HOH A . 
F 4 HOH 17  417 54  HOH HOH A . 
F 4 HOH 18  418 157 HOH HOH A . 
F 4 HOH 19  419 107 HOH HOH A . 
F 4 HOH 20  420 120 HOH HOH A . 
F 4 HOH 21  421 175 HOH HOH A . 
F 4 HOH 22  422 154 HOH HOH A . 
F 4 HOH 23  423 99  HOH HOH A . 
F 4 HOH 24  424 92  HOH HOH A . 
F 4 HOH 25  425 1   HOH HOH A . 
F 4 HOH 26  426 47  HOH HOH A . 
F 4 HOH 27  427 30  HOH HOH A . 
F 4 HOH 28  428 33  HOH HOH A . 
F 4 HOH 29  429 114 HOH HOH A . 
F 4 HOH 30  430 15  HOH HOH A . 
F 4 HOH 31  431 17  HOH HOH A . 
F 4 HOH 32  432 135 HOH HOH A . 
F 4 HOH 33  433 156 HOH HOH A . 
F 4 HOH 34  434 98  HOH HOH A . 
F 4 HOH 35  435 49  HOH HOH A . 
F 4 HOH 36  436 56  HOH HOH A . 
F 4 HOH 37  437 103 HOH HOH A . 
F 4 HOH 38  438 65  HOH HOH A . 
F 4 HOH 39  439 153 HOH HOH A . 
F 4 HOH 40  440 19  HOH HOH A . 
F 4 HOH 41  441 40  HOH HOH A . 
F 4 HOH 42  442 58  HOH HOH A . 
F 4 HOH 43  443 11  HOH HOH A . 
F 4 HOH 44  444 69  HOH HOH A . 
F 4 HOH 45  445 6   HOH HOH A . 
F 4 HOH 46  446 9   HOH HOH A . 
F 4 HOH 47  447 186 HOH HOH A . 
F 4 HOH 48  448 71  HOH HOH A . 
F 4 HOH 49  449 121 HOH HOH A . 
F 4 HOH 50  450 110 HOH HOH A . 
F 4 HOH 51  451 41  HOH HOH A . 
F 4 HOH 52  452 31  HOH HOH A . 
F 4 HOH 53  453 20  HOH HOH A . 
F 4 HOH 54  454 151 HOH HOH A . 
F 4 HOH 55  455 38  HOH HOH A . 
F 4 HOH 56  456 196 HOH HOH A . 
F 4 HOH 57  457 36  HOH HOH A . 
F 4 HOH 58  458 76  HOH HOH A . 
F 4 HOH 59  459 35  HOH HOH A . 
F 4 HOH 60  460 8   HOH HOH A . 
F 4 HOH 61  461 34  HOH HOH A . 
F 4 HOH 62  462 189 HOH HOH A . 
F 4 HOH 63  463 60  HOH HOH A . 
F 4 HOH 64  464 55  HOH HOH A . 
F 4 HOH 65  465 5   HOH HOH A . 
F 4 HOH 66  466 136 HOH HOH A . 
F 4 HOH 67  467 64  HOH HOH A . 
F 4 HOH 68  468 171 HOH HOH A . 
F 4 HOH 69  469 43  HOH HOH A . 
F 4 HOH 70  470 117 HOH HOH A . 
F 4 HOH 71  471 44  HOH HOH A . 
F 4 HOH 72  472 104 HOH HOH A . 
F 4 HOH 73  473 13  HOH HOH A . 
F 4 HOH 74  474 61  HOH HOH A . 
F 4 HOH 75  475 188 HOH HOH A . 
F 4 HOH 76  476 96  HOH HOH A . 
F 4 HOH 77  477 79  HOH HOH A . 
F 4 HOH 78  478 87  HOH HOH A . 
F 4 HOH 79  479 149 HOH HOH A . 
F 4 HOH 80  480 14  HOH HOH A . 
F 4 HOH 81  481 93  HOH HOH A . 
F 4 HOH 82  482 42  HOH HOH A . 
F 4 HOH 83  483 25  HOH HOH A . 
F 4 HOH 84  484 46  HOH HOH A . 
F 4 HOH 85  485 84  HOH HOH A . 
F 4 HOH 86  486 24  HOH HOH A . 
F 4 HOH 87  487 75  HOH HOH A . 
F 4 HOH 88  488 50  HOH HOH A . 
F 4 HOH 89  489 32  HOH HOH A . 
F 4 HOH 90  490 37  HOH HOH A . 
F 4 HOH 91  491 129 HOH HOH A . 
F 4 HOH 92  492 68  HOH HOH A . 
F 4 HOH 93  493 23  HOH HOH A . 
F 4 HOH 94  494 138 HOH HOH A . 
F 4 HOH 95  495 115 HOH HOH A . 
F 4 HOH 96  496 26  HOH HOH A . 
F 4 HOH 97  497 77  HOH HOH A . 
F 4 HOH 98  498 45  HOH HOH A . 
F 4 HOH 99  499 109 HOH HOH A . 
F 4 HOH 100 500 72  HOH HOH A . 
F 4 HOH 101 501 57  HOH HOH A . 
F 4 HOH 102 502 194 HOH HOH A . 
F 4 HOH 103 503 29  HOH HOH A . 
F 4 HOH 104 504 63  HOH HOH A . 
F 4 HOH 105 505 12  HOH HOH A . 
F 4 HOH 106 506 27  HOH HOH A . 
F 4 HOH 107 507 125 HOH HOH A . 
F 4 HOH 108 508 83  HOH HOH A . 
F 4 HOH 109 509 81  HOH HOH A . 
F 4 HOH 110 510 21  HOH HOH A . 
F 4 HOH 111 511 4   HOH HOH A . 
F 4 HOH 112 512 16  HOH HOH A . 
F 4 HOH 113 513 48  HOH HOH A . 
F 4 HOH 114 514 150 HOH HOH A . 
F 4 HOH 115 515 80  HOH HOH A . 
F 4 HOH 116 516 39  HOH HOH A . 
F 4 HOH 117 517 168 HOH HOH A . 
F 4 HOH 118 518 28  HOH HOH A . 
F 4 HOH 119 519 127 HOH HOH A . 
F 4 HOH 120 520 131 HOH HOH A . 
F 4 HOH 121 521 124 HOH HOH A . 
F 4 HOH 122 522 91  HOH HOH A . 
F 4 HOH 123 523 106 HOH HOH A . 
F 4 HOH 124 524 74  HOH HOH A . 
F 4 HOH 125 525 139 HOH HOH A . 
F 4 HOH 126 526 183 HOH HOH A . 
F 4 HOH 127 527 82  HOH HOH A . 
F 4 HOH 128 528 73  HOH HOH A . 
F 4 HOH 129 529 52  HOH HOH A . 
F 4 HOH 130 530 126 HOH HOH A . 
F 4 HOH 131 531 51  HOH HOH A . 
F 4 HOH 132 532 2   HOH HOH A . 
F 4 HOH 133 533 172 HOH HOH A . 
F 4 HOH 134 534 116 HOH HOH A . 
F 4 HOH 135 535 102 HOH HOH A . 
F 4 HOH 136 536 152 HOH HOH A . 
F 4 HOH 137 537 97  HOH HOH A . 
F 4 HOH 138 538 133 HOH HOH A . 
F 4 HOH 139 539 122 HOH HOH A . 
F 4 HOH 140 540 78  HOH HOH A . 
F 4 HOH 141 541 119 HOH HOH A . 
F 4 HOH 142 542 165 HOH HOH A . 
F 4 HOH 143 543 100 HOH HOH A . 
F 4 HOH 144 544 166 HOH HOH A . 
F 4 HOH 145 545 169 HOH HOH A . 
F 4 HOH 146 546 155 HOH HOH A . 
F 4 HOH 147 547 167 HOH HOH A . 
F 4 HOH 148 548 176 HOH HOH A . 
F 4 HOH 149 549 70  HOH HOH A . 
F 4 HOH 150 550 130 HOH HOH A . 
F 4 HOH 151 551 85  HOH HOH A . 
F 4 HOH 152 552 184 HOH HOH A . 
F 4 HOH 153 553 140 HOH HOH A . 
F 4 HOH 154 554 112 HOH HOH A . 
F 4 HOH 155 555 147 HOH HOH A . 
F 4 HOH 156 556 89  HOH HOH A . 
F 4 HOH 157 557 191 HOH HOH A . 
F 4 HOH 158 558 181 HOH HOH A . 
F 4 HOH 159 559 7   HOH HOH A . 
F 4 HOH 160 560 170 HOH HOH A . 
F 4 HOH 161 561 146 HOH HOH A . 
F 4 HOH 162 562 142 HOH HOH A . 
F 4 HOH 163 563 178 HOH HOH A . 
F 4 HOH 164 564 132 HOH HOH A . 
F 4 HOH 165 565 94  HOH HOH A . 
F 4 HOH 166 566 144 HOH HOH A . 
F 4 HOH 167 567 160 HOH HOH A . 
F 4 HOH 168 568 158 HOH HOH A . 
F 4 HOH 169 569 195 HOH HOH A . 
F 4 HOH 170 570 145 HOH HOH A . 
F 4 HOH 171 571 190 HOH HOH A . 
F 4 HOH 172 572 174 HOH HOH A . 
F 4 HOH 173 573 179 HOH HOH A . 
F 4 HOH 174 574 197 HOH HOH A . 
F 4 HOH 175 575 182 HOH HOH A . 
F 4 HOH 176 576 111 HOH HOH A . 
F 4 HOH 177 577 192 HOH HOH A . 
F 4 HOH 178 578 10  HOH HOH A . 
F 4 HOH 179 579 164 HOH HOH A . 
F 4 HOH 180 580 187 HOH HOH A . 
F 4 HOH 181 581 123 HOH HOH A . 
F 4 HOH 182 582 67  HOH HOH A . 
F 4 HOH 183 583 118 HOH HOH A . 
F 4 HOH 184 584 134 HOH HOH A . 
F 4 HOH 185 585 3   HOH HOH A . 
F 4 HOH 186 586 18  HOH HOH A . 
F 4 HOH 187 587 162 HOH HOH A . 
F 4 HOH 188 588 141 HOH HOH A . 
F 4 HOH 189 589 128 HOH HOH A . 
F 4 HOH 190 590 185 HOH HOH A . 
F 4 HOH 191 591 143 HOH HOH A . 
F 4 HOH 192 592 148 HOH HOH A . 
F 4 HOH 193 593 86  HOH HOH A . 
F 4 HOH 194 594 177 HOH HOH A . 
F 4 HOH 195 595 22  HOH HOH A . 
F 4 HOH 196 596 62  HOH HOH A . 
F 4 HOH 197 597 53  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A HIS -3 ? CG  ? A HIS 5 CG  
2  1 Y 1 A HIS -3 ? ND1 ? A HIS 5 ND1 
3  1 Y 1 A HIS -3 ? CD2 ? A HIS 5 CD2 
4  1 Y 1 A HIS -3 ? CE1 ? A HIS 5 CE1 
5  1 Y 1 A HIS -3 ? NE2 ? A HIS 5 NE2 
6  1 Y 1 A HIS 0  ? CG  ? A HIS 8 CG  
7  1 Y 1 A HIS 0  ? ND1 ? A HIS 8 ND1 
8  1 Y 1 A HIS 0  ? CD2 ? A HIS 8 CD2 
9  1 Y 1 A HIS 0  ? CE1 ? A HIS 8 CE1 
10 1 Y 1 A HIS 0  ? NE2 ? A HIS 8 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? dev_5533 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MJQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     92.821 
_cell.length_a_esd                 ? 
_cell.length_b                     92.821 
_cell.length_b_esd                 ? 
_cell.length_c                     130.152 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        18 
_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                         9MJQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                155 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'H 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9MJQ 
_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             2.02 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.26 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    
;JCSG+ B5: 40% (v/v) MPD, 8% (w/v) PEG 8000, 100mM sodium cacodylate pH 6.5. TrvaA.01033.d.B1.PW39308 at 17.4 mg/mL. cocrystallized with 2mM inosine. plate 14463 well B5 drop 1  , Puck: PSL0310, Cryo: direct.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-12-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Double Crystal Si 111' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9786 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 19-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9786 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MJQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.20 
_reflns.d_resolution_low                               46.41 
_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                                     64325 
_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                           95.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                16.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.97 
_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                                0.079 
_reflns.pdbx_Rpim_I_all                                0.018 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1068776 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.076 
_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                                    1.20 
_reflns_shell.d_res_low                                     1.22 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           10803 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2372 
_reflns_shell.percent_possible_obs                          67.3 
_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                               4.6 
_reflns_shell.pdbx_chi_squared                              0.96 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.7 
_reflns_shell.pdbx_Rrim_I_all                               0.980 
_reflns_shell.pdbx_Rpim_I_all                               0.445 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.738 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.864 
_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                                 9MJQ 
_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                            1.20 
_refine.ls_d_res_low                             46.41 
_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                     64284 
_refine.ls_number_reflns_R_free                  3165 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.49 
_refine.ls_percent_reflns_R_free                 4.92 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1317 
_refine.ls_R_factor_R_free                       0.1588 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1303 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.27 
_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                            0.11 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.20 
_refine_hist.d_res_low                        46.41 
_refine_hist.number_atoms_solvent             197 
_refine_hist.number_atoms_total               2052 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1833 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         22 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 1943 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.922  ? 2655 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.710 ? 729  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.076  ? 310  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 340  ? 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' 1.20 1.22  . . 95  1826 66.00  . . . . 0.3674 . . . . . . . . . . . 0.3599 
'X-RAY DIFFRACTION' 1.22 1.24  . . 119 2053 76.00  . . . . 0.3287 . . . . . . . . . . . 0.3294 
'X-RAY DIFFRACTION' 1.24 1.26  . . 109 2277 82.00  . . . . 0.2992 . . . . . . . . . . . 0.2817 
'X-RAY DIFFRACTION' 1.26 1.28  . . 143 2401 87.00  . . . . 0.2706 . . . . . . . . . . . 0.2861 
'X-RAY DIFFRACTION' 1.28 1.30  . . 137 2515 92.00  . . . . 0.2498 . . . . . . . . . . . 0.2996 
'X-RAY DIFFRACTION' 1.30 1.33  . . 138 2630 96.00  . . . . 0.2173 . . . . . . . . . . . 0.2234 
'X-RAY DIFFRACTION' 1.33 1.35  . . 139 2725 99.00  . . . . 0.1844 . . . . . . . . . . . 0.2024 
'X-RAY DIFFRACTION' 1.35 1.38  . . 133 2773 100.00 . . . . 0.1632 . . . . . . . . . . . 0.2214 
'X-RAY DIFFRACTION' 1.38 1.42  . . 149 2748 100.00 . . . . 0.1506 . . . . . . . . . . . 0.1968 
'X-RAY DIFFRACTION' 1.42 1.45  . . 133 2766 100.00 . . . . 0.1360 . . . . . . . . . . . 0.1776 
'X-RAY DIFFRACTION' 1.45 1.49  . . 142 2764 100.00 . . . . 0.1254 . . . . . . . . . . . 0.1558 
'X-RAY DIFFRACTION' 1.49 1.53  . . 130 2793 100.00 . . . . 0.1230 . . . . . . . . . . . 0.1372 
'X-RAY DIFFRACTION' 1.53 1.58  . . 129 2766 100.00 . . . . 0.1171 . . . . . . . . . . . 0.1540 
'X-RAY DIFFRACTION' 1.58 1.64  . . 161 2775 100.00 . . . . 0.1063 . . . . . . . . . . . 0.1334 
'X-RAY DIFFRACTION' 1.64 1.71  . . 132 2779 100.00 . . . . 0.0975 . . . . . . . . . . . 0.1470 
'X-RAY DIFFRACTION' 1.71 1.78  . . 139 2795 100.00 . . . . 0.0919 . . . . . . . . . . . 0.1327 
'X-RAY DIFFRACTION' 1.78 1.88  . . 137 2773 100.00 . . . . 0.0936 . . . . . . . . . . . 0.1090 
'X-RAY DIFFRACTION' 1.88 2.00  . . 150 2798 100.00 . . . . 0.0936 . . . . . . . . . . . 0.1221 
'X-RAY DIFFRACTION' 2.00 2.15  . . 143 2787 100.00 . . . . 0.0943 . . . . . . . . . . . 0.1143 
'X-RAY DIFFRACTION' 2.15 2.37  . . 154 2793 100.00 . . . . 0.0986 . . . . . . . . . . . 0.1214 
'X-RAY DIFFRACTION' 2.37 2.71  . . 132 2824 100.00 . . . . 0.1062 . . . . . . . . . . . 0.1194 
'X-RAY DIFFRACTION' 2.71 3.41  . . 135 2863 100.00 . . . . 0.1187 . . . . . . . . . . . 0.1540 
'X-RAY DIFFRACTION' 3.41 46.41 . . 186 2895 100.00 . . . . 0.1404 . . . . . . . . . . . 0.1706 
# 
_struct.entry_id                     9MJQ 
_struct.title                        
'Crystal structure of Purine nucleoside phosphorylase from Trichomonas vaginalis (inosine bound)' 
_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        9MJQ 
_struct_keywords.text            
;SSGCID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, Purine nucleoside phosphorylase, Trichomonas vaginalis, TRANSFERASE
;
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A2EU62_TRIV3 
_struct_ref.pdbx_db_accession          A2EU62 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATPHNSAKVGDFAETVLMCGDPLRAKLIADNYLENAKQVNSVRGMLGFTGTYKGKPLSVMGHGMGIPSISIYAEELYNV
YKVKTIIRVGTCGTVDPNVHVRDVCIVTASGTDSNVNRMRLLGHDFPATANFEVVSALVESAKALNIPTQVGKAYSTDIF
YSKEQGLNEALAQYHFIAVEMESAGLFPIADYYGARAGCICTVSDHIITHESATPEERQTSFQNMIKIALEATLKL
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9MJQ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 9 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 244 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A2EU62 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  236 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       236 
# 
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 9MJQ MET A 1 ? UNP A2EU62 ? ? 'initiating methionine' -7 1 
1 9MJQ ALA A 2 ? UNP A2EU62 ? ? 'expression tag'        -6 2 
1 9MJQ HIS A 3 ? UNP A2EU62 ? ? 'expression tag'        -5 3 
1 9MJQ HIS A 4 ? UNP A2EU62 ? ? 'expression tag'        -4 4 
1 9MJQ HIS A 5 ? UNP A2EU62 ? ? 'expression tag'        -3 5 
1 9MJQ HIS A 6 ? UNP A2EU62 ? ? 'expression tag'        -2 6 
1 9MJQ HIS A 7 ? UNP A2EU62 ? ? 'expression tag'        -1 7 
1 9MJQ HIS A 8 ? UNP A2EU62 ? ? 'expression tag'        0  8 
# 
_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   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
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)' 25900 ? 
1 MORE         -321  ? 
1 'SSA (A^2)'  48100 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4,5,6 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z                  1.0000000000  0.0000000000  0.0000000000 0.0000000000  0.0000000000  
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 2_545  -y,x-y-1,z             -0.5000000000 -0.8660254038 0.0000000000 46.4105000000 0.8660254038  
-0.5000000000 0.0000000000 -80.3853440047 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
3 'crystal symmetry operation' 3_655  -x+y+1,-x,z            -0.5000000000 0.8660254038  0.0000000000 92.8210000000 -0.8660254038 
-0.5000000000 0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
4 'crystal symmetry operation' 10_545 y+2/3,x-2/3,-z+1/3     -0.5000000000 0.8660254038  0.0000000000 92.8210000000 0.8660254038  
0.5000000000  0.0000000000 -53.5902293365 0.0000000000 0.0000000000 -1.0000000000 43.3840000000 
5 'crystal symmetry operation' 11_445 x-y-1/3,-y-2/3,-z+1/3  1.0000000000  0.0000000000  0.0000000000 0.0000000000  0.0000000000  
-1.0000000000 0.0000000000 -53.5902293365 0.0000000000 0.0000000000 -1.0000000000 43.3840000000 
6 'crystal symmetry operation' 12_555 -x+2/3,-x+y+1/3,-z+1/3 -0.5000000000 -0.8660254038 0.0000000000 46.4105000000 -0.8660254038 
0.5000000000  0.0000000000 26.7951146682  0.0000000000 0.0000000000 -1.0000000000 43.3840000000 
# 
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 ASP A 30  ? LEU A 42  ? ASP A 22  LEU A 34  1 ? 13 
HELX_P HELX_P2 AA2 SER A 50  ? MET A 54  ? SER A 42  MET A 46  5 ? 5  
HELX_P HELX_P3 AA3 GLY A 74  ? VAL A 88  ? GLY A 66  VAL A 80  1 ? 15 
HELX_P HELX_P4 AA4 ASN A 125 ? LEU A 129 ? ASN A 117 LEU A 121 5 ? 5  
HELX_P HELX_P5 AA5 ASN A 139 ? LEU A 153 ? ASN A 131 LEU A 145 1 ? 15 
HELX_P HELX_P6 AA6 GLY A 174 ? TYR A 182 ? GLY A 166 TYR A 174 1 ? 9  
HELX_P HELX_P7 AA7 GLU A 190 ? TYR A 201 ? GLU A 182 TYR A 193 1 ? 12 
HELX_P HELX_P8 AA8 THR A 222 ? LEU A 242 ? THR A 214 LEU A 234 1 ? 21 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 43  ? ASN A 49  ? GLU A 35  ASN A 41  
AA1 2 GLY A 56  ? TYR A 61  ? GLY A 48  TYR A 53  
AA1 3 LYS A 64  ? GLY A 70  ? LYS A 56  GLY A 62  
AA1 4 THR A 24  ? CYS A 28  ? THR A 16  CYS A 20  
AA1 5 THR A 93  ? THR A 102 ? THR A 85  THR A 94  
AA1 6 ALA A 186 ? GLU A 188 ? ALA A 178 GLU A 180 
AA1 7 GLN A 158 ? SER A 164 ? GLN A 150 SER A 156 
AA1 8 VAL A 112 ? THR A 120 ? VAL A 104 THR A 112 
AA1 9 ALA A 136 ? THR A 137 ? ALA A 128 THR A 129 
AA2 1 GLU A 43  ? ASN A 49  ? GLU A 35  ASN A 41  
AA2 2 GLY A 56  ? TYR A 61  ? GLY A 48  TYR A 53  
AA2 3 LYS A 64  ? GLY A 70  ? LYS A 56  GLY A 62  
AA2 4 THR A 24  ? CYS A 28  ? THR A 16  CYS A 20  
AA2 5 THR A 93  ? THR A 102 ? THR A 85  THR A 94  
AA2 6 ARG A 204 ? HIS A 214 ? ARG A 196 HIS A 206 
AA2 7 VAL A 112 ? THR A 120 ? VAL A 104 THR A 112 
AA2 8 ALA A 136 ? THR A 137 ? ALA A 128 THR A 129 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLU A 43  ? N GLU A 35  O THR A 60  ? O THR A 52  
AA1 2 3 N GLY A 59  ? N GLY A 51  O LEU A 66  ? O LEU A 58  
AA1 3 4 O SER A 67  ? O SER A 59  N LEU A 26  ? N LEU A 18  
AA1 4 5 N MET A 27  ? N MET A 19  O VAL A 97  ? O VAL A 89  
AA1 5 6 N GLY A 101 ? N GLY A 93  O VAL A 187 ? O VAL A 179 
AA1 6 7 O GLU A 188 ? O GLU A 180 N TYR A 163 ? N TYR A 155 
AA1 7 8 O GLN A 158 ? O GLN A 150 N ILE A 114 ? N ILE A 106 
AA1 8 9 N SER A 118 ? N SER A 110 O ALA A 136 ? O ALA A 128 
AA2 1 2 N GLU A 43  ? N GLU A 35  O THR A 60  ? O THR A 52  
AA2 2 3 N GLY A 59  ? N GLY A 51  O LEU A 66  ? O LEU A 58  
AA2 3 4 O SER A 67  ? O SER A 59  N LEU A 26  ? N LEU A 18  
AA2 4 5 N MET A 27  ? N MET A 19  O VAL A 97  ? O VAL A 89  
AA2 5 6 N CYS A 100 ? N CYS A 92  O SER A 212 ? O SER A 204 
AA2 6 7 O CYS A 209 ? O CYS A 201 N CYS A 113 ? N CYS A 105 
AA2 7 8 N SER A 118 ? N SER A 110 O ALA A 136 ? O ALA A 128 
# 
_pdbx_entry_details.entry_id                   9MJQ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A -3  ? ? -69.65  12.90   
2 1 SER A 42  ? ? -142.37 10.18   
3 1 ARG A 44  ? ? 59.00   18.95   
4 1 ARG A 102 ? ? 85.42   -8.42   
5 1 GLU A 180 ? ? -144.34 -159.22 
6 1 GLU A 182 ? ? -140.80 -37.44  
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Seattle Structural Genomics Center for Infectious Disease' 
_pdbx_SG_project.initial_of_center     SSGCID 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 402 ? F HOH . 
2 1 A HOH 442 ? F HOH . 
3 1 A HOH 460 ? F HOH . 
4 1 A HOH 595 ? F HOH . 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       597 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.46 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET -7 ? A MET 1 
2 1 Y 1 A ALA -6 ? A ALA 2 
3 1 Y 1 A HIS -5 ? A HIS 3 
# 
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 
NOS N9    N  Y N 251 
NOS C4    C  Y N 252 
NOS N3    N  N N 253 
NOS C2    C  N N 254 
NOS N1    N  N N 255 
NOS C6    C  N N 256 
NOS O6    O  N N 257 
NOS C5    C  Y N 258 
NOS N7    N  Y N 259 
NOS C8    C  Y N 260 
NOS "C5'" C  N N 261 
NOS "O5'" O  N N 262 
NOS "C4'" C  N R 263 
NOS "O4'" O  N N 264 
NOS "C1'" C  N R 265 
NOS "C2'" C  N R 266 
NOS "O2'" O  N N 267 
NOS "C3'" C  N S 268 
NOS "O3'" O  N N 269 
NOS H1    H  N N 270 
NOS H2    H  N N 271 
NOS H3    H  N N 272 
NOS H4    H  N N 273 
NOS H5    H  N N 274 
NOS H6    H  N N 275 
NOS H7    H  N N 276 
NOS H8    H  N N 277 
NOS H9    H  N N 278 
NOS H10   H  N N 279 
NOS H11   H  N N 280 
NOS H12   H  N N 281 
PHE N     N  N N 282 
PHE CA    C  N S 283 
PHE C     C  N N 284 
PHE O     O  N N 285 
PHE CB    C  N N 286 
PHE CG    C  Y N 287 
PHE CD1   C  Y N 288 
PHE CD2   C  Y N 289 
PHE CE1   C  Y N 290 
PHE CE2   C  Y N 291 
PHE CZ    C  Y N 292 
PHE OXT   O  N N 293 
PHE H     H  N N 294 
PHE H2    H  N N 295 
PHE HA    H  N N 296 
PHE HB2   H  N N 297 
PHE HB3   H  N N 298 
PHE HD1   H  N N 299 
PHE HD2   H  N N 300 
PHE HE1   H  N N 301 
PHE HE2   H  N N 302 
PHE HZ    H  N N 303 
PHE HXT   H  N N 304 
PRO N     N  N N 305 
PRO CA    C  N S 306 
PRO C     C  N N 307 
PRO O     O  N N 308 
PRO CB    C  N N 309 
PRO CG    C  N N 310 
PRO CD    C  N N 311 
PRO OXT   O  N N 312 
PRO H     H  N N 313 
PRO HA    H  N N 314 
PRO HB2   H  N N 315 
PRO HB3   H  N N 316 
PRO HG2   H  N N 317 
PRO HG3   H  N N 318 
PRO HD2   H  N N 319 
PRO HD3   H  N N 320 
PRO HXT   H  N N 321 
SER N     N  N N 322 
SER CA    C  N S 323 
SER C     C  N N 324 
SER O     O  N N 325 
SER CB    C  N N 326 
SER OG    O  N N 327 
SER OXT   O  N N 328 
SER H     H  N N 329 
SER H2    H  N N 330 
SER HA    H  N N 331 
SER HB2   H  N N 332 
SER HB3   H  N N 333 
SER HG    H  N N 334 
SER HXT   H  N N 335 
THR N     N  N N 336 
THR CA    C  N S 337 
THR C     C  N N 338 
THR O     O  N N 339 
THR CB    C  N R 340 
THR OG1   O  N N 341 
THR CG2   C  N N 342 
THR OXT   O  N N 343 
THR H     H  N N 344 
THR H2    H  N N 345 
THR HA    H  N N 346 
THR HB    H  N N 347 
THR HG1   H  N N 348 
THR HG21  H  N N 349 
THR HG22  H  N N 350 
THR HG23  H  N N 351 
THR HXT   H  N N 352 
TYR N     N  N N 353 
TYR CA    C  N S 354 
TYR C     C  N N 355 
TYR O     O  N N 356 
TYR CB    C  N N 357 
TYR CG    C  Y N 358 
TYR CD1   C  Y N 359 
TYR CD2   C  Y N 360 
TYR CE1   C  Y N 361 
TYR CE2   C  Y N 362 
TYR CZ    C  Y N 363 
TYR OH    O  N N 364 
TYR OXT   O  N N 365 
TYR H     H  N N 366 
TYR H2    H  N N 367 
TYR HA    H  N N 368 
TYR HB2   H  N N 369 
TYR HB3   H  N N 370 
TYR HD1   H  N N 371 
TYR HD2   H  N N 372 
TYR HE1   H  N N 373 
TYR HE2   H  N N 374 
TYR HH    H  N N 375 
TYR HXT   H  N N 376 
VAL N     N  N N 377 
VAL CA    C  N S 378 
VAL C     C  N N 379 
VAL O     O  N N 380 
VAL CB    C  N N 381 
VAL CG1   C  N N 382 
VAL CG2   C  N N 383 
VAL OXT   O  N N 384 
VAL H     H  N N 385 
VAL H2    H  N N 386 
VAL HA    H  N N 387 
VAL HB    H  N N 388 
VAL HG11  H  N N 389 
VAL HG12  H  N N 390 
VAL HG13  H  N N 391 
VAL HG21  H  N N 392 
VAL HG22  H  N N 393 
VAL HG23  H  N N 394 
VAL HXT   H  N N 395 
# 
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 
NOS N1    C2    sing N N 237 
NOS N1    C6    sing N N 238 
NOS C2    N3    doub N N 239 
NOS O6    C6    doub N N 240 
NOS C6    C5    sing N N 241 
NOS N3    C4    sing N N 242 
NOS "O2'" "C2'" sing N N 243 
NOS C5    C4    doub Y N 244 
NOS C5    N7    sing Y N 245 
NOS C4    N9    sing Y N 246 
NOS N7    C8    doub Y N 247 
NOS N9    C8    sing Y N 248 
NOS N9    "C1'" sing N N 249 
NOS "C1'" "C2'" sing N N 250 
NOS "C1'" "O4'" sing N N 251 
NOS "C2'" "C3'" sing N N 252 
NOS "O4'" "C4'" sing N N 253 
NOS "C3'" "O3'" sing N N 254 
NOS "C3'" "C4'" sing N N 255 
NOS "C4'" "C5'" sing N N 256 
NOS "C5'" "O5'" sing N N 257 
NOS C2    H1    sing N N 258 
NOS N1    H2    sing N N 259 
NOS C8    H3    sing N N 260 
NOS "C5'" H4    sing N N 261 
NOS "C5'" H5    sing N N 262 
NOS "O5'" H6    sing N N 263 
NOS "C4'" H7    sing N N 264 
NOS "C1'" H8    sing N N 265 
NOS "C2'" H9    sing N N 266 
NOS "O2'" H10   sing N N 267 
NOS "C3'" H11   sing N N 268 
NOS "O3'" H12   sing N N 269 
PHE N     CA    sing N N 270 
PHE N     H     sing N N 271 
PHE N     H2    sing N N 272 
PHE CA    C     sing N N 273 
PHE CA    CB    sing N N 274 
PHE CA    HA    sing N N 275 
PHE C     O     doub N N 276 
PHE C     OXT   sing N N 277 
PHE CB    CG    sing N N 278 
PHE CB    HB2   sing N N 279 
PHE CB    HB3   sing N N 280 
PHE CG    CD1   doub Y N 281 
PHE CG    CD2   sing Y N 282 
PHE CD1   CE1   sing Y N 283 
PHE CD1   HD1   sing N N 284 
PHE CD2   CE2   doub Y N 285 
PHE CD2   HD2   sing N N 286 
PHE CE1   CZ    doub Y N 287 
PHE CE1   HE1   sing N N 288 
PHE CE2   CZ    sing Y N 289 
PHE CE2   HE2   sing N N 290 
PHE CZ    HZ    sing N N 291 
PHE OXT   HXT   sing N N 292 
PRO N     CA    sing N N 293 
PRO N     CD    sing N N 294 
PRO N     H     sing N N 295 
PRO CA    C     sing N N 296 
PRO CA    CB    sing N N 297 
PRO CA    HA    sing N N 298 
PRO C     O     doub N N 299 
PRO C     OXT   sing N N 300 
PRO CB    CG    sing N N 301 
PRO CB    HB2   sing N N 302 
PRO CB    HB3   sing N N 303 
PRO CG    CD    sing N N 304 
PRO CG    HG2   sing N N 305 
PRO CG    HG3   sing N N 306 
PRO CD    HD2   sing N N 307 
PRO CD    HD3   sing N N 308 
PRO OXT   HXT   sing N N 309 
SER N     CA    sing N N 310 
SER N     H     sing N N 311 
SER N     H2    sing N N 312 
SER CA    C     sing N N 313 
SER CA    CB    sing N N 314 
SER CA    HA    sing N N 315 
SER C     O     doub N N 316 
SER C     OXT   sing N N 317 
SER CB    OG    sing N N 318 
SER CB    HB2   sing N N 319 
SER CB    HB3   sing N N 320 
SER OG    HG    sing N N 321 
SER OXT   HXT   sing N N 322 
THR N     CA    sing N N 323 
THR N     H     sing N N 324 
THR N     H2    sing N N 325 
THR CA    C     sing N N 326 
THR CA    CB    sing N N 327 
THR CA    HA    sing N N 328 
THR C     O     doub N N 329 
THR C     OXT   sing N N 330 
THR CB    OG1   sing N N 331 
THR CB    CG2   sing N N 332 
THR CB    HB    sing N N 333 
THR OG1   HG1   sing N N 334 
THR CG2   HG21  sing N N 335 
THR CG2   HG22  sing N N 336 
THR CG2   HG23  sing N N 337 
THR OXT   HXT   sing N N 338 
TYR N     CA    sing N N 339 
TYR N     H     sing N N 340 
TYR N     H2    sing N N 341 
TYR CA    C     sing N N 342 
TYR CA    CB    sing N N 343 
TYR CA    HA    sing N N 344 
TYR C     O     doub N N 345 
TYR C     OXT   sing N N 346 
TYR CB    CG    sing N N 347 
TYR CB    HB2   sing N N 348 
TYR CB    HB3   sing N N 349 
TYR CG    CD1   doub Y N 350 
TYR CG    CD2   sing Y N 351 
TYR CD1   CE1   sing Y N 352 
TYR CD1   HD1   sing N N 353 
TYR CD2   CE2   doub Y N 354 
TYR CD2   HD2   sing N N 355 
TYR CE1   CZ    doub Y N 356 
TYR CE1   HE1   sing N N 357 
TYR CE2   CZ    sing Y N 358 
TYR CE2   HE2   sing N N 359 
TYR CZ    OH    sing N N 360 
TYR OH    HH    sing N N 361 
TYR OXT   HXT   sing N N 362 
VAL N     CA    sing N N 363 
VAL N     H     sing N N 364 
VAL N     H2    sing N N 365 
VAL CA    C     sing N N 366 
VAL CA    CB    sing N N 367 
VAL CA    HA    sing N N 368 
VAL C     O     doub N N 369 
VAL C     OXT   sing N N 370 
VAL CB    CG1   sing N N 371 
VAL CB    CG2   sing N N 372 
VAL CB    HB    sing N N 373 
VAL CG1   HG11  sing N N 374 
VAL CG1   HG12  sing N N 375 
VAL CG1   HG13  sing N N 376 
VAL CG2   HG21  sing N N 377 
VAL CG2   HG22  sing N N 378 
VAL CG2   HG23  sing N N 379 
VAL OXT   HXT   sing N N 380 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 75N93022C00036 1 
'National Institutes of Health/Office of the Director'                                            'United States' S10OD030394    2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-A2EU62-F1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9MJQ 
_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]   0.010773 
_atom_sites.fract_transf_matrix[1][2]   0.006220 
_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]   0.012440 
_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]   0.007683 
_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     . HIS A 1 4   ? 25.483 17.266  37.761 1.00 53.40 ? -4  HIS A N     1 
ATOM   2    C  CA    . HIS A 1 4   ? 26.783 17.120  38.477 1.00 53.24 ? -4  HIS A CA    1 
ATOM   3    C  C     . HIS A 1 4   ? 27.716 16.222  37.675 1.00 52.64 ? -4  HIS A C     1 
ATOM   4    O  O     . HIS A 1 4   ? 27.279 15.249  37.061 1.00 53.07 ? -4  HIS A O     1 
ATOM   5    C  CB    . HIS A 1 4   ? 26.566 16.529  39.870 1.00 53.49 ? -4  HIS A CB    1 
ATOM   6    C  CG    . HIS A 1 4   ? 27.749 16.670  40.777 1.00 53.62 ? -4  HIS A CG    1 
ATOM   7    N  ND1   . HIS A 1 4   ? 28.352 17.883  41.027 1.00 53.61 ? -4  HIS A ND1   1 
ATOM   8    C  CD2   . HIS A 1 4   ? 28.438 15.751  41.495 1.00 53.72 ? -4  HIS A CD2   1 
ATOM   9    C  CE1   . HIS A 1 4   ? 29.362 17.707  41.860 1.00 53.64 ? -4  HIS A CE1   1 
ATOM   10   N  NE2   . HIS A 1 4   ? 29.436 16.422  42.159 1.00 53.78 ? -4  HIS A NE2   1 
ATOM   11   N  N     . HIS A 1 5   ? 29.002 16.546  37.693 1.00 51.52 ? -3  HIS A N     1 
ATOM   12   C  CA    . HIS A 1 5   ? 29.991 15.811  36.906 1.00 50.13 ? -3  HIS A CA    1 
ATOM   13   C  C     . HIS A 1 5   ? 30.250 14.381  37.416 1.00 48.37 ? -3  HIS A C     1 
ATOM   14   O  O     . HIS A 1 5   ? 31.241 13.797  36.948 1.00 48.87 ? -3  HIS A O     1 
ATOM   15   C  CB    . HIS A 1 5   ? 31.304 16.593  36.862 1.00 50.02 ? -3  HIS A CB    1 
ATOM   16   N  N     . HIS A 1 6   ? 29.471 13.768  38.307 1.00 45.88 ? -2  HIS A N     1 
ATOM   17   C  CA    . HIS A 1 6   ? 29.786 12.419  38.754 1.00 43.36 ? -2  HIS A CA    1 
ATOM   18   C  C     . HIS A 1 6   ? 28.524 11.741  39.267 1.00 40.82 ? -2  HIS A C     1 
ATOM   19   O  O     . HIS A 1 6   ? 27.736 12.344  40.001 1.00 40.24 ? -2  HIS A O     1 
ATOM   20   C  CB    . HIS A 1 6   ? 30.863 12.432  39.846 1.00 43.70 ? -2  HIS A CB    1 
ATOM   21   C  CG    . HIS A 1 6   ? 31.340 11.069  40.241 1.00 44.21 ? -2  HIS A CG    1 
ATOM   22   N  ND1   . HIS A 1 6   ? 31.285 10.608  41.539 1.00 44.66 ? -2  HIS A ND1   1 
ATOM   23   C  CD2   . HIS A 1 6   ? 31.882 10.065  39.509 1.00 44.34 ? -2  HIS A CD2   1 
ATOM   24   C  CE1   . HIS A 1 6   ? 31.773 9.381   41.591 1.00 44.48 ? -2  HIS A CE1   1 
ATOM   25   N  NE2   . HIS A 1 6   ? 32.141 9.027   40.372 1.00 44.49 ? -2  HIS A NE2   1 
ATOM   26   N  N     . HIS A 1 7   ? 28.352 10.482  38.872 1.00 38.67 ? -1  HIS A N     1 
ATOM   27   C  CA    . HIS A 1 7   ? 27.206 9.675   39.255 1.00 37.58 ? -1  HIS A CA    1 
ATOM   28   C  C     . HIS A 1 7   ? 27.692 8.354   39.833 1.00 33.59 ? -1  HIS A C     1 
ATOM   29   O  O     . HIS A 1 7   ? 28.824 7.927   39.600 1.00 32.09 ? -1  HIS A O     1 
ATOM   30   C  CB    . HIS A 1 7   ? 26.287 9.413   38.054 1.00 40.92 ? -1  HIS A CB    1 
ATOM   31   C  CG    . HIS A 1 7   ? 25.443 10.590  37.671 1.00 43.72 ? -1  HIS A CG    1 
ATOM   32   N  ND1   . HIS A 1 7   ? 25.980 11.813  37.331 1.00 45.04 ? -1  HIS A ND1   1 
ATOM   33   C  CD2   . HIS A 1 7   ? 24.099 10.731  37.577 1.00 44.81 ? -1  HIS A CD2   1 
ATOM   34   C  CE1   . HIS A 1 7   ? 25.003 12.657  37.045 1.00 45.64 ? -1  HIS A CE1   1 
ATOM   35   N  NE2   . HIS A 1 7   ? 23.852 12.025  37.188 1.00 45.55 ? -1  HIS A NE2   1 
ATOM   36   N  N     . HIS A 1 8   ? 26.815 7.710   40.598 1.00 31.13 ? 0   HIS A N     1 
ATOM   37   C  CA    . HIS A 1 8   ? 27.126 6.404   41.158 1.00 30.61 ? 0   HIS A CA    1 
ATOM   38   C  C     . HIS A 1 8   ? 27.372 5.406   40.035 1.00 29.94 ? 0   HIS A C     1 
ATOM   39   O  O     . HIS A 1 8   ? 26.712 5.447   38.994 1.00 30.68 ? 0   HIS A O     1 
ATOM   40   C  CB    . HIS A 1 8   ? 25.954 5.929   42.018 1.00 31.53 ? 0   HIS A CB    1 
ATOM   41   N  N     . MET A 1 9   ? 28.350 4.525   40.235 1.00 27.96 ? 1   MET A N     1 
ATOM   42   C  CA    . MET A 1 9   ? 28.695 3.489   39.264 1.00 26.50 ? 1   MET A CA    1 
ATOM   43   C  C     . MET A 1 9   ? 28.604 2.134   39.950 1.00 25.24 ? 1   MET A C     1 
ATOM   44   O  O     . MET A 1 9   ? 29.459 1.796   40.774 1.00 26.75 ? 1   MET A O     1 
ATOM   45   C  CB    . MET A 1 9   ? 30.110 3.710   38.727 1.00 27.07 ? 1   MET A CB    1 
ATOM   46   C  CG    . MET A 1 9   ? 30.268 4.989   37.941 1.00 28.07 ? 1   MET A CG    1 
ATOM   47   S  SD    . MET A 1 9   ? 29.551 4.847   36.303 1.00 29.32 ? 1   MET A SD    1 
ATOM   48   C  CE    . MET A 1 9   ? 30.775 3.821   35.483 1.00 29.07 ? 1   MET A CE    1 
ATOM   49   N  N     . ALA A 1 10  ? 27.582 1.348   39.598 1.00 22.76 ? 2   ALA A N     1 
ATOM   50   C  CA    . ALA A 1 10  ? 27.463 0.009   40.164 1.00 21.89 ? 2   ALA A CA    1 
ATOM   51   C  C     . ALA A 1 10  ? 28.514 -0.929  39.593 1.00 21.03 ? 2   ALA A C     1 
ATOM   52   O  O     . ALA A 1 10  ? 28.902 -1.899  40.252 1.00 22.29 ? 2   ALA A O     1 
ATOM   53   C  CB    . ALA A 1 10  ? 26.070 -0.563  39.901 1.00 22.05 ? 2   ALA A CB    1 
ATOM   54   N  N     . THR A 1 11  ? 28.945 -0.680  38.366 1.00 18.38 ? 3   THR A N     1 
ATOM   55   C  CA    . THR A 1 11  ? 30.031 -1.421  37.743 1.00 17.32 ? 3   THR A CA    1 
ATOM   56   C  C     . THR A 1 11  ? 30.907 -0.414  37.010 1.00 16.92 ? 3   THR A C     1 
ATOM   57   O  O     . THR A 1 11  ? 30.519 0.751   36.852 1.00 17.88 ? 3   THR A O     1 
ATOM   58   C  CB    . THR A 1 11  ? 29.521 -2.439  36.722 1.00 16.52 ? 3   THR A CB    1 
ATOM   59   O  OG1   . THR A 1 11  ? 29.292 -1.766  35.479 1.00 14.59 ? 3   THR A OG1   1 
ATOM   60   C  CG2   . THR A 1 11  ? 28.239 -3.120  37.178 1.00 17.14 ? 3   THR A CG2   1 
ATOM   61   N  N     . PRO A 1 12  ? 32.083 -0.811  36.525 1.00 17.17 ? 4   PRO A N     1 
ATOM   62   C  CA    . PRO A 1 12  ? 32.905 0.140   35.767 1.00 17.17 ? 4   PRO A CA    1 
ATOM   63   C  C     . PRO A 1 12  ? 32.283 0.551   34.451 1.00 16.09 ? 4   PRO A C     1 
ATOM   64   O  O     . PRO A 1 12  ? 32.744 1.524   33.843 1.00 17.85 ? 4   PRO A O     1 
ATOM   65   C  CB    . PRO A 1 12  ? 34.215 -0.623  35.532 1.00 18.11 ? 4   PRO A CB    1 
ATOM   66   C  CG    . PRO A 1 12  ? 34.232 -1.694  36.559 1.00 19.07 ? 4   PRO A CG    1 
ATOM   67   C  CD    . PRO A 1 12  ? 32.788 -2.079  36.762 1.00 18.28 ? 4   PRO A CD    1 
ATOM   68   N  N     . HIS A 1 13  ? 31.250 -0.148  34.000 1.00 14.61 ? 5   HIS A N     1 
ATOM   69   C  CA    . HIS A 1 13  ? 30.726 0.016   32.655 1.00 14.34 ? 5   HIS A CA    1 
ATOM   70   C  C     . HIS A 1 13  ? 29.245 0.372   32.635 1.00 15.19 ? 5   HIS A C     1 
ATOM   71   O  O     . HIS A 1 13  ? 28.663 0.478   31.551 1.00 15.38 ? 5   HIS A O     1 
ATOM   72   C  CB    . HIS A 1 13  ? 30.957 -1.267  31.847 1.00 13.64 ? 5   HIS A CB    1 
ATOM   73   C  CG    . HIS A 1 13  ? 32.348 -1.800  31.964 1.00 12.68 ? 5   HIS A CG    1 
ATOM   74   N  ND1   . HIS A 1 13  ? 32.671 -2.841  32.802 1.00 12.28 ? 5   HIS A ND1   1 
ATOM   75   C  CD2   . HIS A 1 13  ? 33.506 -1.420  31.372 1.00 13.01 ? 5   HIS A CD2   1 
ATOM   76   C  CE1   . HIS A 1 13  ? 33.967 -3.089  32.714 1.00 12.04 ? 5   HIS A CE1   1 
ATOM   77   N  NE2   . HIS A 1 13  ? 34.502 -2.229  31.863 1.00 12.84 ? 5   HIS A NE2   1 
ATOM   78   N  N     . ASN A 1 14  ? 28.618 0.575   33.792 1.00 15.43 ? 6   ASN A N     1 
ATOM   79   C  CA    . ASN A 1 14  ? 27.169 0.736   33.834 1.00 16.43 ? 6   ASN A CA    1 
ATOM   80   C  C     . ASN A 1 14  ? 26.819 1.609   35.028 1.00 17.39 ? 6   ASN A C     1 
ATOM   81   O  O     . ASN A 1 14  ? 27.186 1.288   36.162 1.00 18.90 ? 6   ASN A O     1 
ATOM   82   C  CB    . ASN A 1 14  ? 26.506 -0.642  33.952 1.00 16.39 ? 6   ASN A CB    1 
ATOM   83   C  CG    . ASN A 1 14  ? 25.053 -0.637  33.508 1.00 16.35 ? 6   ASN A CG    1 
ATOM   84   O  OD1   . ASN A 1 14  ? 24.336 0.357   33.672 1.00 16.67 ? 6   ASN A OD1   1 
ATOM   85   N  ND2   . ASN A 1 14  ? 24.613 -1.750  32.943 1.00 16.78 ? 6   ASN A ND2   1 
ATOM   86   N  N     . SER A 1 15  ? 26.117 2.708   34.779 1.00 18.31 ? 7   SER A N     1 
ATOM   87   C  CA    . SER A 1 15  ? 25.718 3.598   35.857 1.00 19.50 ? 7   SER A CA    1 
ATOM   88   C  C     . SER A 1 15  ? 24.353 3.260   36.435 1.00 19.19 ? 7   SER A C     1 
ATOM   89   O  O     . SER A 1 15  ? 23.919 3.923   37.383 1.00 20.61 ? 7   SER A O     1 
ATOM   90   C  CB    . SER A 1 15  ? 25.712 5.052   35.369 1.00 21.80 ? 7   SER A CB    1 
ATOM   91   O  OG    . SER A 1 15  ? 24.755 5.200   34.335 1.00 23.95 ? 7   SER A OG    1 
ATOM   92   N  N     . ALA A 1 16  ? 23.661 2.267   35.884 1.00 18.29 ? 8   ALA A N     1 
ATOM   93   C  CA    . ALA A 1 16  ? 22.359 1.890   36.415 1.00 18.57 ? 8   ALA A CA    1 
ATOM   94   C  C     . ALA A 1 16  ? 22.511 1.394   37.846 1.00 20.82 ? 8   ALA A C     1 
ATOM   95   O  O     . ALA A 1 16  ? 23.505 0.752   38.193 1.00 21.22 ? 8   ALA A O     1 
ATOM   96   C  CB    . ALA A 1 16  ? 21.754 0.784   35.552 1.00 19.00 ? 8   ALA A CB    1 
ATOM   97   N  N     . LYS A 1 17  ? 21.526 1.703   38.685 1.00 23.30 ? 9   LYS A N     1 
ATOM   98   C  CA    . LYS A 1 17  ? 21.483 1.119   40.014 1.00 25.85 ? 9   LYS A CA    1 
ATOM   99   C  C     . LYS A 1 17  ? 20.862 -0.269  39.944 1.00 23.91 ? 9   LYS A C     1 
ATOM   100  O  O     . LYS A 1 17  ? 20.062 -0.575  39.052 1.00 21.33 ? 9   LYS A O     1 
ATOM   101  C  CB    . LYS A 1 17  ? 20.662 1.996   40.964 1.00 30.27 ? 9   LYS A CB    1 
ATOM   102  C  CG    . LYS A 1 17  ? 21.292 3.350   41.294 1.00 34.17 ? 9   LYS A CG    1 
ATOM   103  C  CD    . LYS A 1 17  ? 22.563 3.211   42.123 1.00 36.99 ? 9   LYS A CD    1 
ATOM   104  C  CE    . LYS A 1 17  ? 23.827 3.354   41.264 1.00 38.93 ? 9   LYS A CE    1 
ATOM   105  N  NZ    . LYS A 1 17  ? 25.065 2.909   41.965 1.00 39.85 ? 9   LYS A NZ    1 
ATOM   106  N  N     . VAL A 1 18  ? 21.244 -1.125  40.891 1.00 24.93 ? 10  VAL A N     1 
ATOM   107  C  CA    . VAL A 1 18  ? 20.572 -2.410  41.006 1.00 26.05 ? 10  VAL A CA    1 
ATOM   108  C  C     . VAL A 1 18  ? 19.077 -2.170  41.167 1.00 23.97 ? 10  VAL A C     1 
ATOM   109  O  O     . VAL A 1 18  ? 18.641 -1.309  41.944 1.00 24.17 ? 10  VAL A O     1 
ATOM   110  C  CB    . VAL A 1 18  ? 21.141 -3.231  42.171 1.00 28.70 ? 10  VAL A CB    1 
ATOM   111  C  CG1   . VAL A 1 18  ? 20.473 -4.597  42.202 1.00 29.27 ? 10  VAL A CG1   1 
ATOM   112  C  CG2   . VAL A 1 18  ? 22.669 -3.363  42.049 1.00 29.68 ? 10  VAL A CG2   1 
ATOM   113  N  N     . GLY A 1 19  ? 18.281 -2.931  40.419 1.00 21.90 ? 11  GLY A N     1 
ATOM   114  C  CA    . GLY A 1 19  ? 16.856 -2.731  40.337 1.00 20.91 ? 11  GLY A CA    1 
ATOM   115  C  C     . GLY A 1 19  ? 16.412 -1.961  39.115 1.00 19.16 ? 11  GLY A C     1 
ATOM   116  O  O     . GLY A 1 19  ? 15.219 -1.981  38.786 1.00 20.60 ? 11  GLY A O     1 
ATOM   117  N  N     . ASP A 1 20  ? 17.341 -1.286  38.434 1.00 17.44 ? 12  ASP A N     1 
ATOM   118  C  CA    . ASP A 1 20  ? 17.003 -0.495  37.260 1.00 18.10 ? 12  ASP A CA    1 
ATOM   119  C  C     . ASP A 1 20  ? 16.858 -1.340  36.006 1.00 16.45 ? 12  ASP A C     1 
ATOM   120  O  O     . ASP A 1 20  ? 16.344 -0.834  35.003 1.00 17.06 ? 12  ASP A O     1 
ATOM   121  C  CB    . ASP A 1 20  ? 18.091 0.552   36.973 1.00 20.41 ? 12  ASP A CB    1 
ATOM   122  C  CG    . ASP A 1 20  ? 18.048 1.744   37.910 1.00 22.94 ? 12  ASP A CG    1 
ATOM   123  O  OD1   . ASP A 1 20  ? 17.090 1.884   38.703 1.00 24.29 ? 12  ASP A OD1   1 
ATOM   124  O  OD2   . ASP A 1 20  ? 18.987 2.568   37.816 1.00 24.01 ? 12  ASP A OD2   1 
ATOM   125  N  N     . PHE A 1 21  ? 17.345 -2.585  36.023 1.00 15.59 ? 13  PHE A N     1 
ATOM   126  C  CA    . PHE A 1 21  ? 17.171 -3.517  34.918 1.00 14.36 ? 13  PHE A CA    1 
ATOM   127  C  C     . PHE A 1 21  ? 16.080 -4.514  35.263 1.00 14.18 ? 13  PHE A C     1 
ATOM   128  O  O     . PHE A 1 21  ? 15.992 -4.985  36.402 1.00 15.93 ? 13  PHE A O     1 
ATOM   129  C  CB    . PHE A 1 21  ? 18.471 -4.262  34.587 1.00 15.07 ? 13  PHE A CB    1 
ATOM   130  C  CG    . PHE A 1 21  ? 19.373 -3.484  33.682 1.00 14.51 ? 13  PHE A CG    1 
ATOM   131  C  CD1   . PHE A 1 21  ? 19.239 -3.582  32.305 1.00 15.48 ? 13  PHE A CD1   1 
ATOM   132  C  CD2   . PHE A 1 21  ? 20.313 -2.609  34.198 1.00 15.77 ? 13  PHE A CD2   1 
ATOM   133  C  CE1   . PHE A 1 21  ? 20.032 -2.821  31.463 1.00 16.31 ? 13  PHE A CE1   1 
ATOM   134  C  CE2   . PHE A 1 21  ? 21.107 -1.854  33.359 1.00 15.89 ? 13  PHE A CE2   1 
ATOM   135  C  CZ    . PHE A 1 21  ? 20.969 -1.962  31.994 1.00 15.89 ? 13  PHE A CZ    1 
ATOM   136  N  N     . ALA A 1 22  ? 15.234 -4.811  34.284 1.00 13.77 ? 14  ALA A N     1 
ATOM   137  C  CA    . ALA A 1 22  ? 14.238 -5.854  34.448 1.00 13.89 ? 14  ALA A CA    1 
ATOM   138  C  C     . ALA A 1 22  ? 14.912 -7.226  34.456 1.00 13.58 ? 14  ALA A C     1 
ATOM   139  O  O     . ALA A 1 22  ? 16.076 -7.378  34.079 1.00 14.30 ? 14  ALA A O     1 
ATOM   140  C  CB    . ALA A 1 22  ? 13.221 -5.786  33.312 1.00 14.75 ? 14  ALA A CB    1 
ATOM   141  N  N     . GLU A 1 23  ? 14.146 -8.241  34.870 1.00 13.40 ? 15  GLU A N     1 
ATOM   142  C  CA    . GLU A 1 23  ? 14.676 -9.603  34.896 1.00 14.07 ? 15  GLU A CA    1 
ATOM   143  C  C     . GLU A 1 23  ? 14.887 -10.166 33.505 1.00 13.10 ? 15  GLU A C     1 
ATOM   144  O  O     . GLU A 1 23  ? 15.613 -11.151 33.354 1.00 13.55 ? 15  GLU A O     1 
ATOM   145  C  CB    . GLU A 1 23  ? 13.740 -10.531 35.662 1.00 18.53 ? 15  GLU A CB    1 
ATOM   146  C  CG    . GLU A 1 23  ? 13.745 -10.303 37.155 1.00 23.04 ? 15  GLU A CG    1 
ATOM   147  C  CD    . GLU A 1 23  ? 13.088 -11.428 37.910 1.00 27.20 ? 15  GLU A CD    1 
ATOM   148  O  OE1   . GLU A 1 23  ? 12.070 -11.945 37.412 1.00 27.48 ? 15  GLU A OE1   1 
ATOM   149  O  OE2   . GLU A 1 23  ? 13.596 -11.802 38.992 1.00 29.72 ? 15  GLU A OE2   1 
ATOM   150  N  N     . THR A 1 24  ? 14.265 -9.581  32.493 1.00 12.95 ? 16  THR A N     1 
ATOM   151  C  CA    . THR A 1 24  ? 14.419 -10.004 31.108 1.00 12.29 ? 16  THR A CA    1 
ATOM   152  C  C     . THR A 1 24  ? 15.019 -8.848  30.328 1.00 12.06 ? 16  THR A C     1 
ATOM   153  O  O     . THR A 1 24  ? 14.572 -7.709  30.470 1.00 12.55 ? 16  THR A O     1 
ATOM   154  C  CB    . THR A 1 24  ? 13.057 -10.390 30.511 1.00 14.35 ? 16  THR A CB    1 
ATOM   155  O  OG1   . THR A 1 24  ? 12.374 -11.308 31.377 1.00 15.85 ? 16  THR A OG1   1 
ATOM   156  C  CG2   . THR A 1 24  ? 13.222 -11.016 29.141 1.00 15.36 ? 16  THR A CG2   1 
ATOM   157  N  N     . VAL A 1 25  ? 16.029 -9.148  29.513 1.00 12.21 ? 17  VAL A N     1 
ATOM   158  C  CA    . VAL A 1 25  ? 16.766 -8.134  28.772 1.00 12.42 ? 17  VAL A CA    1 
ATOM   159  C  C     . VAL A 1 25  ? 16.971 -8.608  27.343 1.00 12.26 ? 17  VAL A C     1 
ATOM   160  O  O     . VAL A 1 25  ? 17.395 -9.744  27.118 1.00 12.87 ? 17  VAL A O     1 
ATOM   161  C  CB    . VAL A 1 25  ? 18.135 -7.843  29.421 1.00 12.38 ? 17  VAL A CB    1 
ATOM   162  C  CG1   . VAL A 1 25  ? 18.846 -6.688  28.700 1.00 13.27 ? 17  VAL A CG1   1 
ATOM   163  C  CG2   . VAL A 1 25  ? 18.009 -7.566  30.919 1.00 13.34 ? 17  VAL A CG2   1 
ATOM   164  N  N     . LEU A 1 26  ? 16.701 -7.728  26.381 1.00 11.31 ? 18  LEU A N     1 
ATOM   165  C  CA    . LEU A 1 26  ? 17.151 -7.905  25.008 1.00 11.32 ? 18  LEU A CA    1 
ATOM   166  C  C     . LEU A 1 26  ? 18.447 -7.138  24.836 1.00 11.29 ? 18  LEU A C     1 
ATOM   167  O  O     . LEU A 1 26  ? 18.555 -5.989  25.269 1.00 11.99 ? 18  LEU A O     1 
ATOM   168  C  CB    . LEU A 1 26  ? 16.142 -7.346  24.016 1.00 12.21 ? 18  LEU A CB    1 
ATOM   169  C  CG    . LEU A 1 26  ? 14.720 -7.894  24.089 1.00 13.27 ? 18  LEU A CG    1 
ATOM   170  C  CD1   . LEU A 1 26  ? 13.900 -7.335  22.944 1.00 14.52 ? 18  LEU A CD1   1 
ATOM   171  C  CD2   . LEU A 1 26  ? 14.706 -9.412  24.089 1.00 13.44 ? 18  LEU A CD2   1 
ATOM   172  N  N     . MET A 1 27  ? 19.422 -7.752  24.194 1.00 11.37 ? 19  MET A N     1 
ATOM   173  C  CA    . MET A 1 27  ? 20.663 -7.046  23.899 1.00 11.83 ? 19  MET A CA    1 
ATOM   174  C  C     . MET A 1 27  ? 20.983 -7.146  22.422 1.00 11.81 ? 19  MET A C     1 
ATOM   175  O  O     . MET A 1 27  ? 20.914 -8.222  21.842 1.00 12.57 ? 19  MET A O     1 
ATOM   176  C  CB    . MET A 1 27  ? 21.850 -7.579  24.694 1.00 13.37 ? 19  MET A CB    1 
ATOM   177  C  CG    . MET A 1 27  ? 21.658 -7.521  26.191 1.00 15.40 ? 19  MET A CG    1 
ATOM   178  S  SD    . MET A 1 27  ? 23.149 -7.926  27.085 1.00 19.39 ? 19  MET A SD    1 
ATOM   179  C  CE    . MET A 1 27  ? 23.872 -6.301  27.117 1.00 19.61 ? 19  MET A CE    1 
ATOM   180  N  N     . CYS A 1 28  ? 21.400 -6.034  21.835 1.00 12.80 ? 20  CYS A N     1 
ATOM   181  C  CA    . CYS A 1 28  ? 21.863 -5.989  20.458 1.00 14.04 ? 20  CYS A CA    1 
ATOM   182  C  C     . CYS A 1 28  ? 23.217 -5.298  20.452 1.00 13.47 ? 20  CYS A C     1 
ATOM   183  O  O     . CYS A 1 28  ? 23.559 -4.588  21.391 1.00 14.19 ? 20  CYS A O     1 
ATOM   184  C  CB    . CYS A 1 28  ? 20.867 -5.260  19.558 1.00 15.56 ? 20  CYS A CB    1 
ATOM   185  S  SG    . CYS A 1 28  ? 20.423 -3.586  20.130 1.00 16.44 ? 20  CYS A SG    1 
ATOM   186  N  N     . GLY A 1 29  ? 24.011 -5.501  19.396 1.00 14.14 ? 21  GLY A N     1 
ATOM   187  C  CA    . GLY A 1 29  ? 25.349 -4.935  19.392 1.00 14.57 ? 21  GLY A CA    1 
ATOM   188  C  C     . GLY A 1 29  ? 25.350 -3.420  19.362 1.00 14.06 ? 21  GLY A C     1 
ATOM   189  O  O     . GLY A 1 29  ? 26.165 -2.779  20.032 1.00 14.72 ? 21  GLY A O     1 
ATOM   190  N  N     . ASP A 1 30  ? 24.468 -2.827  18.555 1.00 13.30 ? 22  ASP A N     1 
ATOM   191  C  CA    . ASP A 1 30  ? 24.467 -1.390  18.294 1.00 13.40 ? 22  ASP A CA    1 
ATOM   192  C  C     . ASP A 1 30  ? 23.631 -0.677  19.350 1.00 13.10 ? 22  ASP A C     1 
ATOM   193  O  O     . ASP A 1 30  ? 22.400 -0.855  19.374 1.00 12.93 ? 22  ASP A O     1 
ATOM   194  C  CB    . ASP A 1 30  ? 23.887 -1.140  16.905 1.00 13.91 ? 22  ASP A CB    1 
ATOM   195  C  CG    . ASP A 1 30  ? 23.920 0.318   16.498 1.00 14.52 ? 22  ASP A CG    1 
ATOM   196  O  OD1   . ASP A 1 30  ? 24.260 1.177   17.328 1.00 13.85 ? 22  ASP A OD1   1 
ATOM   197  O  OD2   . ASP A 1 30  ? 23.599 0.610   15.322 1.00 16.35 ? 22  ASP A OD2   1 
ATOM   198  N  N     . PRO A 1 31  ? 24.230 0.160   20.208 1.00 13.41 ? 23  PRO A N     1 
ATOM   199  C  CA    . PRO A 1 31  ? 23.416 0.875   21.204 1.00 13.72 ? 23  PRO A CA    1 
ATOM   200  C  C     . PRO A 1 31  ? 22.387 1.792   20.584 1.00 13.99 ? 23  PRO A C     1 
ATOM   201  O  O     . PRO A 1 31  ? 21.351 2.061   21.205 1.00 14.54 ? 23  PRO A O     1 
ATOM   202  C  CB    . PRO A 1 31  ? 24.455 1.647   22.027 1.00 14.70 ? 23  PRO A CB    1 
ATOM   203  C  CG    . PRO A 1 31  ? 25.607 1.845   21.087 1.00 14.92 ? 23  PRO A CG    1 
ATOM   204  C  CD    . PRO A 1 31  ? 25.650 0.564   20.276 1.00 13.93 ? 23  PRO A CD    1 
ATOM   205  N  N     . LEU A 1 32  ? 22.632 2.278   19.372 1.00 14.54 ? 24  LEU A N     1 
ATOM   206  C  CA    . LEU A 1 32  ? 21.634 3.122   18.730 1.00 15.08 ? 24  LEU A CA    1 
ATOM   207  C  C     . LEU A 1 32  ? 20.418 2.308   18.328 1.00 15.21 ? 24  LEU A C     1 
ATOM   208  O  O     . LEU A 1 32  ? 19.302 2.832   18.293 1.00 15.87 ? 24  LEU A O     1 
ATOM   209  C  CB    . LEU A 1 32  ? 22.242 3.826   17.520 1.00 15.93 ? 24  LEU A CB    1 
ATOM   210  C  CG    . LEU A 1 32  ? 23.516 4.639   17.802 1.00 18.57 ? 24  LEU A CG    1 
ATOM   211  C  CD1   . LEU A 1 32  ? 23.962 5.401   16.564 1.00 19.31 ? 24  LEU A CD1   1 
ATOM   212  C  CD2   . LEU A 1 32  ? 23.312 5.571   18.979 1.00 19.84 ? 24  LEU A CD2   1 
ATOM   213  N  N     . ARG A 1 33  ? 20.617 1.024   18.036 1.00 14.76 ? 25  ARG A N     1 
ATOM   214  C  CA    . ARG A 1 33  ? 19.485 0.149   17.785 1.00 15.49 ? 25  ARG A CA    1 
ATOM   215  C  C     . ARG A 1 33  ? 18.738 -0.165  19.075 1.00 14.92 ? 25  ARG A C     1 
ATOM   216  O  O     . ARG A 1 33  ? 17.511 -0.303  19.061 1.00 14.79 ? 25  ARG A O     1 
ATOM   217  C  CB    . ARG A 1 33  ? 19.980 -1.130  17.107 1.00 16.85 ? 25  ARG A CB    1 
ATOM   218  C  CG    . ARG A 1 33  ? 18.881 -2.136  16.784 1.00 20.76 ? 25  ARG A CG    1 
ATOM   219  C  CD    . ARG A 1 33  ? 18.054 -1.702  15.595 1.00 25.74 ? 25  ARG A CD    1 
ATOM   220  N  NE    . ARG A 1 33  ? 18.780 -1.851  14.340 1.00 29.93 ? 25  ARG A NE    1 
ATOM   221  C  CZ    . ARG A 1 33  ? 18.280 -1.559  13.147 1.00 32.64 ? 25  ARG A CZ    1 
ATOM   222  N  NH1   . ARG A 1 33  ? 17.056 -1.070  13.011 1.00 33.68 ? 25  ARG A NH1   1 
ATOM   223  N  NH2   . ARG A 1 33  ? 19.027 -1.761  12.065 1.00 33.79 ? 25  ARG A NH2   1 
ATOM   224  N  N     . ALA A 1 34  ? 19.451 -0.274  20.199 1.00 14.72 ? 26  ALA A N     1 
ATOM   225  C  CA    . ALA A 1 34  ? 18.770 -0.417  21.480 1.00 15.91 ? 26  ALA A CA    1 
ATOM   226  C  C     . ALA A 1 34  ? 17.832 0.756   21.727 1.00 15.38 ? 26  ALA A C     1 
ATOM   227  O  O     . ALA A 1 34  ? 16.694 0.568   22.183 1.00 15.41 ? 26  ALA A O     1 
ATOM   228  C  CB    . ALA A 1 34  ? 19.780 -0.549  22.615 1.00 15.71 ? 26  ALA A CB    1 
ATOM   229  N  N     . LYS A 1 35  ? 18.289 1.975   21.424 1.00 14.94 ? 27  LYS A N     1 
ATOM   230  C  CA    . LYS A 1 35  ? 17.433 3.146   21.556 1.00 15.50 ? 27  LYS A CA    1 
ATOM   231  C  C     . LYS A 1 35  ? 16.221 3.047   20.639 1.00 15.26 ? 27  LYS A C     1 
ATOM   232  O  O     . LYS A 1 35  ? 15.100 3.351   21.048 1.00 15.49 ? 27  LYS A O     1 
ATOM   233  C  CB    . LYS A 1 35  ? 18.238 4.415   21.265 1.00 17.02 ? 27  LYS A CB    1 
ATOM   234  C  CG    . LYS A 1 35  ? 17.386 5.670   21.350 1.00 18.11 ? 27  LYS A CG    1 
ATOM   235  C  CD    . LYS A 1 35  ? 18.218 6.907   21.071 1.00 20.19 ? 27  LYS A CD    1 
ATOM   236  C  CE    . LYS A 1 35  ? 17.362 8.158   20.953 1.00 22.96 ? 27  LYS A CE    1 
ATOM   237  N  NZ    . LYS A 1 35  ? 16.626 8.370   22.199 1.00 26.22 ? 27  LYS A NZ    1 
ATOM   238  N  N     . LEU A 1 36  ? 16.425 2.642   19.387 1.00 16.01 ? 28  LEU A N     1 
ATOM   239  C  CA    . LEU A 1 36  ? 15.289 2.502   18.484 1.00 16.10 ? 28  LEU A CA    1 
ATOM   240  C  C     . LEU A 1 36  ? 14.278 1.504   19.022 1.00 15.59 ? 28  LEU A C     1 
ATOM   241  O  O     . LEU A 1 36  ? 13.070 1.725   18.927 1.00 16.14 ? 28  LEU A O     1 
ATOM   242  C  CB    . LEU A 1 36  ? 15.770 2.075   17.099 1.00 18.52 ? 28  LEU A CB    1 
ATOM   243  C  CG    . LEU A 1 36  ? 16.392 3.184   16.250 1.00 23.03 ? 28  LEU A CG    1 
ATOM   244  C  CD1   . LEU A 1 36  ? 17.016 2.579   15.000 1.00 24.80 ? 28  LEU A CD1   1 
ATOM   245  C  CD2   . LEU A 1 36  ? 15.346 4.231   15.891 1.00 25.65 ? 28  LEU A CD2   1 
ATOM   246  N  N     . ILE A 1 37  ? 14.753 0.391   19.584 1.00 14.87 ? 29  ILE A N     1 
ATOM   247  C  CA    . ILE A 1 37  ? 13.836 -0.601  20.143 1.00 15.23 ? 29  ILE A CA    1 
ATOM   248  C  C     . ILE A 1 37  ? 13.050 0.004   21.295 1.00 15.56 ? 29  ILE A C     1 
ATOM   249  O  O     . ILE A 1 37  ? 11.820 -0.112  21.363 1.00 16.11 ? 29  ILE A O     1 
ATOM   250  C  CB    . ILE A 1 37  ? 14.603 -1.859  20.587 1.00 15.71 ? 29  ILE A CB    1 
ATOM   251  C  CG1   . ILE A 1 37  ? 15.196 -2.580  19.374 1.00 16.67 ? 29  ILE A CG1   1 
ATOM   252  C  CG2   . ILE A 1 37  ? 13.677 -2.785  21.370 1.00 15.71 ? 29  ILE A CG2   1 
ATOM   253  C  CD1   . ILE A 1 37  ? 16.283 -3.570  19.719 1.00 16.85 ? 29  ILE A CD1   1 
ATOM   254  N  N     . ALA A 1 38  ? 13.750 0.693   22.200 1.00 15.54 ? 30  ALA A N     1 
ATOM   255  C  CA    . ALA A 1 38  ? 13.079 1.276   23.353 1.00 16.33 ? 30  ALA A CA    1 
ATOM   256  C  C     . ALA A 1 38  ? 12.048 2.308   22.918 1.00 17.82 ? 30  ALA A C     1 
ATOM   257  O  O     . ALA A 1 38  ? 10.926 2.324   23.432 1.00 19.06 ? 30  ALA A O     1 
ATOM   258  C  CB    . ALA A 1 38  ? 14.105 1.892   24.306 1.00 17.63 ? 30  ALA A CB    1 
ATOM   259  N  N     . ASP A 1 39  ? 12.405 3.161   21.953 1.00 17.12 ? 31  ASP A N     1 
ATOM   260  C  CA    . ASP A 1 39  ? 11.552 4.270   21.554 1.00 18.80 ? 31  ASP A CA    1 
ATOM   261  C  C     . ASP A 1 39  ? 10.336 3.816   20.770 1.00 18.74 ? 31  ASP A C     1 
ATOM   262  O  O     . ASP A 1 39  ? 9.394  4.595   20.629 1.00 20.69 ? 31  ASP A O     1 
ATOM   263  C  CB    . ASP A 1 39  ? 12.346 5.243   20.677 1.00 20.70 ? 31  ASP A CB    1 
ATOM   264  C  CG    . ASP A 1 39  ? 13.336 6.082   21.466 1.00 23.88 ? 31  ASP A CG    1 
ATOM   265  O  OD1   . ASP A 1 39  ? 13.308 6.060   22.719 1.00 26.66 ? 31  ASP A OD1   1 
ATOM   266  O  OD2   . ASP A 1 39  ? 14.165 6.755   20.827 1.00 24.40 ? 31  ASP A OD2   1 
ATOM   267  N  N     . ASN A 1 40  ? 10.339 2.596   20.238 1.00 17.91 ? 32  ASN A N     1 
ATOM   268  C  CA    . ASN A 1 40  ? 9.247  2.127   19.402 1.00 18.77 ? 32  ASN A CA    1 
ATOM   269  C  C     . ASN A 1 40  ? 8.447  0.974   19.976 1.00 18.32 ? 32  ASN A C     1 
ATOM   270  O  O     . ASN A 1 40  ? 7.318  0.758   19.531 1.00 19.85 ? 32  ASN A O     1 
ATOM   271  C  CB    . ASN A 1 40  ? 9.770  1.739   18.013 1.00 20.71 ? 32  ASN A CB    1 
ATOM   272  C  CG    . ASN A 1 40  ? 10.211 2.951   17.213 1.00 23.47 ? 32  ASN A CG    1 
ATOM   273  O  OD1   . ASN A 1 40  ? 11.386 3.328   17.226 1.00 25.42 ? 32  ASN A OD1   1 
ATOM   274  N  ND2   . ASN A 1 40  ? 9.272  3.570   16.521 1.00 25.34 ? 32  ASN A ND2   1 
ATOM   275  N  N     . TYR A 1 41  ? 8.972  0.245   20.953 1.00 16.35 ? 33  TYR A N     1 
ATOM   276  C  CA    . TYR A 1 41  ? 8.287  -0.939  21.450 1.00 16.45 ? 33  TYR A CA    1 
ATOM   277  C  C     . TYR A 1 41  ? 8.048  -0.953  22.948 1.00 16.44 ? 33  TYR A C     1 
ATOM   278  O  O     . TYR A 1 41  ? 7.207  -1.739  23.400 1.00 17.95 ? 33  TYR A O     1 
ATOM   279  C  CB    . TYR A 1 41  ? 9.048  -2.210  21.053 1.00 15.83 ? 33  TYR A CB    1 
ATOM   280  C  CG    . TYR A 1 41  ? 9.139  -2.404  19.563 1.00 16.50 ? 33  TYR A CG    1 
ATOM   281  C  CD1   . TYR A 1 41  ? 8.121  -3.038  18.863 1.00 17.99 ? 33  TYR A CD1   1 
ATOM   282  C  CD2   . TYR A 1 41  ? 10.235 -1.944  18.851 1.00 17.48 ? 33  TYR A CD2   1 
ATOM   283  C  CE1   . TYR A 1 41  ? 8.210  -3.226  17.482 1.00 18.47 ? 33  TYR A CE1   1 
ATOM   284  C  CE2   . TYR A 1 41  ? 10.325 -2.115  17.479 1.00 18.39 ? 33  TYR A CE2   1 
ATOM   285  C  CZ    . TYR A 1 41  ? 9.314  -2.751  16.804 1.00 19.22 ? 33  TYR A CZ    1 
ATOM   286  O  OH    . TYR A 1 41  ? 9.414  -2.914  15.442 1.00 21.05 ? 33  TYR A OH    1 
ATOM   287  N  N     . LEU A 1 42  ? 8.713  -0.105  23.727 1.00 16.81 ? 34  LEU A N     1 
ATOM   288  C  CA    . LEU A 1 42  ? 8.558  -0.115  25.171 1.00 17.35 ? 34  LEU A CA    1 
ATOM   289  C  C     . LEU A 1 42  ? 7.663  1.030   25.617 1.00 17.67 ? 34  LEU A C     1 
ATOM   290  O  O     . LEU A 1 42  ? 7.650  2.113   25.022 1.00 19.90 ? 34  LEU A O     1 
ATOM   291  C  CB    . LEU A 1 42  ? 9.909  0.020   25.879 1.00 18.56 ? 34  LEU A CB    1 
ATOM   292  C  CG    . LEU A 1 42  ? 10.929 -1.077  25.594 1.00 19.16 ? 34  LEU A CG    1 
ATOM   293  C  CD1   . LEU A 1 42  ? 12.182 -0.832  26.409 1.00 21.50 ? 34  LEU A CD1   1 
ATOM   294  C  CD2   . LEU A 1 42  ? 10.355 -2.449  25.891 1.00 19.80 ? 34  LEU A CD2   1 
ATOM   295  N  N     . GLU A 1 43  ? 6.924  0.778   26.682 1.00 16.47 ? 35  GLU A N     1 
ATOM   296  C  CA    . GLU A 1 43  ? 6.261  1.822   27.442 1.00 15.92 ? 35  GLU A CA    1 
ATOM   297  C  C     . GLU A 1 43  ? 6.955  1.971   28.785 1.00 15.35 ? 35  GLU A C     1 
ATOM   298  O  O     . GLU A 1 43  ? 7.828  1.188   29.148 1.00 15.36 ? 35  GLU A O     1 
ATOM   299  C  CB    . GLU A 1 43  ? 4.776  1.509   27.628 1.00 17.28 ? 35  GLU A CB    1 
ATOM   300  C  CG    . GLU A 1 43  ? 4.030  1.336   26.337 1.00 20.81 ? 35  GLU A CG    1 
ATOM   301  C  CD    . GLU A 1 43  ? 2.533  1.149   26.572 1.00 24.64 ? 35  GLU A CD    1 
ATOM   302  O  OE1   . GLU A 1 43  ? 2.151  0.404   27.508 1.00 27.75 ? 35  GLU A OE1   1 
ATOM   303  O  OE2   . GLU A 1 43  ? 1.733  1.719   25.821 1.00 26.88 ? 35  GLU A OE2   1 
ATOM   304  N  N     . ASN A 1 44  ? 6.603  3.028   29.506 1.00 15.42 ? 36  ASN A N     1 
ATOM   305  C  CA    . ASN A 1 44  ? 7.142  3.247   30.842 1.00 17.10 ? 36  ASN A CA    1 
ATOM   306  C  C     . ASN A 1 44  ? 8.663  3.288   30.817 1.00 17.95 ? 36  ASN A C     1 
ATOM   307  O  O     . ASN A 1 44  ? 9.316  2.859   31.767 1.00 19.68 ? 36  ASN A O     1 
ATOM   308  C  CB    . ASN A 1 44  ? 6.651  2.175   31.814 1.00 18.78 ? 36  ASN A CB    1 
ATOM   309  C  CG    . ASN A 1 44  ? 5.151  2.125   31.893 1.00 19.34 ? 36  ASN A CG    1 
ATOM   310  O  OD1   . ASN A 1 44  ? 4.529  3.052   32.398 1.00 20.10 ? 36  ASN A OD1   1 
ATOM   311  N  ND2   . ASN A 1 44  ? 4.558  1.057   31.384 1.00 19.22 ? 36  ASN A ND2   1 
ATOM   312  N  N     . ALA A 1 45  ? 9.238  3.786   29.724 1.00 16.85 ? 37  ALA A N     1 
ATOM   313  C  CA    . ALA A 1 45  ? 10.651 3.574   29.445 1.00 17.23 ? 37  ALA A CA    1 
ATOM   314  C  C     . ALA A 1 45  ? 11.509 4.699   29.992 1.00 16.53 ? 37  ALA A C     1 
ATOM   315  O  O     . ALA A 1 45  ? 11.134 5.876   29.948 1.00 17.90 ? 37  ALA A O     1 
ATOM   316  C  CB    . ALA A 1 45  ? 10.905 3.435   27.941 1.00 18.44 ? 37  ALA A CB    1 
ATOM   317  N  N     . LYS A 1 46  ? 12.682 4.326   30.487 1.00 16.17 ? 38  LYS A N     1 
ATOM   318  C  CA    . LYS A 1 46  ? 13.691 5.283   30.901 1.00 16.94 ? 38  LYS A CA    1 
ATOM   319  C  C     . LYS A 1 46  ? 15.056 4.775   30.474 1.00 15.19 ? 38  LYS A C     1 
ATOM   320  O  O     . LYS A 1 46  ? 15.303 3.565   30.419 1.00 15.12 ? 38  LYS A O     1 
ATOM   321  C  CB    . LYS A 1 46  ? 13.672 5.542   32.413 1.00 21.35 ? 38  LYS A CB    1 
ATOM   322  C  CG    . LYS A 1 46  ? 14.070 4.388   33.287 1.00 26.98 ? 38  LYS A CG    1 
ATOM   323  C  CD    . LYS A 1 46  ? 13.915 4.727   34.771 1.00 31.21 ? 38  LYS A CD    1 
ATOM   324  C  CE    . LYS A 1 46  ? 14.396 3.575   35.660 1.00 33.83 ? 38  LYS A CE    1 
ATOM   325  N  NZ    . LYS A 1 46  ? 13.316 2.992   36.519 1.00 36.00 ? 38  LYS A NZ    1 
ATOM   326  N  N     . GLN A 1 47  ? 15.936 5.716   30.177 1.00 15.65 ? 39  GLN A N     1 
ATOM   327  C  CA    . GLN A 1 47  ? 17.317 5.378   29.915 1.00 16.06 ? 39  GLN A CA    1 
ATOM   328  C  C     . GLN A 1 47  ? 18.015 5.147   31.243 1.00 16.29 ? 39  GLN A C     1 
ATOM   329  O  O     . GLN A 1 47  ? 17.953 5.986   32.142 1.00 18.77 ? 39  GLN A O     1 
ATOM   330  C  CB    . GLN A 1 47  ? 17.998 6.512   29.157 1.00 17.58 ? 39  GLN A CB    1 
ATOM   331  C  CG    . GLN A 1 47  ? 19.387 6.129   28.708 1.00 19.93 ? 39  GLN A CG    1 
ATOM   332  C  CD    . GLN A 1 47  ? 20.068 7.221   27.931 1.00 23.99 ? 39  GLN A CD    1 
ATOM   333  O  OE1   . GLN A 1 47  ? 21.151 7.659   28.284 1.00 27.55 ? 39  GLN A OE1   1 
ATOM   334  N  NE2   . GLN A 1 47  ? 19.436 7.664   26.861 1.00 25.92 ? 39  GLN A NE2   1 
ATOM   335  N  N     . VAL A 1 48  ? 18.658 3.995   31.375 1.00 14.91 ? 40  VAL A N     1 
ATOM   336  C  CA    . VAL A 1 48  ? 19.300 3.612   32.629 1.00 15.63 ? 40  VAL A CA    1 
ATOM   337  C  C     . VAL A 1 48  ? 20.812 3.553   32.534 1.00 15.98 ? 40  VAL A C     1 
ATOM   338  O  O     . VAL A 1 48  ? 21.477 3.468   33.578 1.00 17.12 ? 40  VAL A O     1 
ATOM   339  C  CB    . VAL A 1 48  ? 18.735 2.282   33.178 1.00 15.72 ? 40  VAL A CB    1 
ATOM   340  C  CG1   . VAL A 1 48  ? 17.265 2.456   33.549 1.00 16.81 ? 40  VAL A CG1   1 
ATOM   341  C  CG2   . VAL A 1 48  ? 18.913 1.126   32.181 1.00 16.17 ? 40  VAL A CG2   1 
ATOM   342  N  N     . ASN A 1 49  ? 21.384 3.592   31.338 1.00 16.12 ? 41  ASN A N     1 
ATOM   343  C  CA    . ASN A 1 49  ? 22.830 3.657   31.218 1.00 15.86 ? 41  ASN A CA    1 
ATOM   344  C  C     . ASN A 1 49  ? 23.222 4.405   29.960 1.00 14.63 ? 41  ASN A C     1 
ATOM   345  O  O     . ASN A 1 49  ? 22.573 4.276   28.923 1.00 15.66 ? 41  ASN A O     1 
ATOM   346  C  CB    . ASN A 1 49  ? 23.457 2.267   31.154 1.00 16.69 ? 41  ASN A CB    1 
ATOM   347  C  CG    . ASN A 1 49  ? 24.969 2.335   31.069 1.00 17.81 ? 41  ASN A CG    1 
ATOM   348  O  OD1   . ASN A 1 49  ? 25.620 2.964   31.896 1.00 17.47 ? 41  ASN A OD1   1 
ATOM   349  N  ND2   . ASN A 1 49  ? 25.527 1.740   30.032 1.00 20.49 ? 41  ASN A ND2   1 
ATOM   350  N  N     . SER A 1 50  ? 24.325 5.145   30.051 1.00 15.72 ? 42  SER A N     1 
ATOM   351  C  CA    . SER A 1 50  ? 24.949 5.723   28.869 1.00 17.33 ? 42  SER A CA    1 
ATOM   352  C  C     . SER A 1 50  ? 26.470 5.694   28.966 1.00 16.29 ? 42  SER A C     1 
ATOM   353  O  O     . SER A 1 50  ? 27.130 6.313   28.129 1.00 16.20 ? 42  SER A O     1 
ATOM   354  C  CB    . SER A 1 50  ? 24.488 7.149   28.611 1.00 21.19 ? 42  SER A CB    1 
ATOM   355  O  OG    . SER A 1 50  ? 24.784 7.928   29.731 1.00 22.83 ? 42  SER A OG    1 
ATOM   356  N  N     . VAL A 1 51  ? 27.048 4.995   29.952 1.00 15.98 ? 43  VAL A N     1 
ATOM   357  C  CA    . VAL A 1 51  ? 28.502 4.902   30.045 1.00 15.47 ? 43  VAL A CA    1 
ATOM   358  C  C     . VAL A 1 51  ? 29.056 4.317   28.755 1.00 14.71 ? 43  VAL A C     1 
ATOM   359  O  O     . VAL A 1 51  ? 28.532 3.333   28.225 1.00 14.85 ? 43  VAL A O     1 
ATOM   360  C  CB    . VAL A 1 51  ? 28.888 4.030   31.251 1.00 16.71 ? 43  VAL A CB    1 
ATOM   361  C  CG1   . VAL A 1 51  ? 30.388 3.725   31.258 1.00 16.63 ? 43  VAL A CG1   1 
ATOM   362  C  CG2   . VAL A 1 51  ? 28.469 4.710   32.545 1.00 18.87 ? 43  VAL A CG2   1 
ATOM   363  N  N     . ARG A 1 52  ? 30.127 4.924   28.244 1.00 14.80 ? 44  ARG A N     1 
ATOM   364  C  CA    . ARG A 1 52  ? 30.777 4.527   26.997 1.00 15.35 ? 44  ARG A CA    1 
ATOM   365  C  C     . ARG A 1 52  ? 29.842 4.584   25.799 1.00 15.15 ? 44  ARG A C     1 
ATOM   366  O  O     . ARG A 1 52  ? 30.140 4.001   24.755 1.00 16.57 ? 44  ARG A O     1 
ATOM   367  C  CB    . ARG A 1 52  ? 31.479 3.163   27.099 1.00 15.87 ? 44  ARG A CB    1 
ATOM   368  C  CG    . ARG A 1 52  ? 32.645 3.176   28.063 1.00 16.30 ? 44  ARG A CG    1 
ATOM   369  C  CD    . ARG A 1 52  ? 33.135 1.764   28.402 1.00 16.69 ? 44  ARG A CD    1 
ATOM   370  N  NE    . ARG A 1 52  ? 34.358 1.774   29.197 1.00 18.18 ? 44  ARG A NE    1 
ATOM   371  C  CZ    . ARG A 1 52  ? 35.580 1.706   28.690 1.00 18.23 ? 44  ARG A CZ    1 
ATOM   372  N  NH1   . ARG A 1 52  ? 35.779 1.596   27.386 1.00 17.38 ? 44  ARG A NH1   1 
ATOM   373  N  NH2   . ARG A 1 52  ? 36.627 1.712   29.512 1.00 20.18 ? 44  ARG A NH2   1 
ATOM   374  N  N     . GLY A 1 53  ? 28.735 5.320   25.916 1.00 14.34 ? 45  GLY A N     1 
ATOM   375  C  CA    . GLY A 1 53  ? 27.733 5.337   24.871 1.00 15.28 ? 45  GLY A CA    1 
ATOM   376  C  C     . GLY A 1 53  ? 26.950 4.053   24.728 1.00 14.52 ? 45  GLY A C     1 
ATOM   377  O  O     . GLY A 1 53  ? 26.207 3.901   23.754 1.00 14.75 ? 45  GLY A O     1 
ATOM   378  N  N     . MET A 1 54  ? 27.078 3.123   25.673 1.00 13.49 ? 46  MET A N     1 
ATOM   379  C  CA    . MET A 1 54  ? 26.420 1.824   25.548 1.00 13.28 ? 46  MET A CA    1 
ATOM   380  C  C     . MET A 1 54  ? 25.022 1.916   26.148 1.00 13.81 ? 46  MET A C     1 
ATOM   381  O  O     . MET A 1 54  ? 24.742 1.462   27.261 1.00 14.30 ? 46  MET A O     1 
ATOM   382  C  CB    . MET A 1 54  ? 27.235 0.715   26.192 1.00 13.71 ? 46  MET A CB    1 
ATOM   383  C  CG    . MET A 1 54  ? 26.813 -0.667  25.709 1.00 13.48 ? 46  MET A CG    1 
ATOM   384  S  SD    . MET A 1 54  ? 26.924 -0.890  23.917 1.00 14.39 ? 46  MET A SD    1 
ATOM   385  C  CE    . MET A 1 54  ? 28.695 -0.923  23.694 1.00 16.58 ? 46  MET A CE    1 
ATOM   386  N  N     . LEU A 1 55  ? 24.134 2.529   25.370 1.00 13.92 ? 47  LEU A N     1 
ATOM   387  C  CA    . LEU A 1 55  ? 22.812 2.899   25.856 1.00 13.67 ? 47  LEU A CA    1 
ATOM   388  C  C     . LEU A 1 55  ? 22.028 1.679   26.317 1.00 12.96 ? 47  LEU A C     1 
ATOM   389  O  O     . LEU A 1 55  ? 21.987 0.647   25.640 1.00 13.16 ? 47  LEU A O     1 
ATOM   390  C  CB    . LEU A 1 55  ? 22.024 3.567   24.734 1.00 14.16 ? 47  LEU A CB    1 
ATOM   391  C  CG    . LEU A 1 55  ? 22.725 4.764   24.093 1.00 15.17 ? 47  LEU A CG    1 
ATOM   392  C  CD1   . LEU A 1 55  ? 21.814 5.368   23.052 1.00 16.21 ? 47  LEU A CD1   1 
ATOM   393  C  CD2   . LEU A 1 55  ? 23.139 5.810   25.124 1.00 16.86 ? 47  LEU A CD2   1 
ATOM   394  N  N     . GLY A 1 56  ? 21.364 1.837   27.453 1.00 12.80 ? 48  GLY A N     1 
ATOM   395  C  CA    . GLY A 1 56  ? 20.446 0.833   27.956 1.00 12.72 ? 48  GLY A CA    1 
ATOM   396  C  C     . GLY A 1 56  ? 19.202 1.505   28.495 1.00 12.30 ? 48  GLY A C     1 
ATOM   397  O  O     . GLY A 1 56  ? 19.245 2.638   28.979 1.00 12.31 ? 48  GLY A O     1 
ATOM   398  N  N     . PHE A 1 57  ? 18.086 0.779   28.414 1.00 12.08 ? 49  PHE A N     1 
ATOM   399  C  CA    . PHE A 1 57  ? 16.755 1.285   28.706 1.00 12.62 ? 49  PHE A CA    1 
ATOM   400  C  C     . PHE A 1 57  ? 15.957 0.215   29.436 1.00 12.23 ? 49  PHE A C     1 
ATOM   401  O  O     . PHE A 1 57  ? 16.142 -0.978  29.200 1.00 12.89 ? 49  PHE A O     1 
ATOM   402  C  CB    . PHE A 1 57  ? 16.018 1.623   27.398 1.00 13.06 ? 49  PHE A CB    1 
ATOM   403  C  CG    . PHE A 1 57  ? 16.746 2.605   26.544 1.00 13.49 ? 49  PHE A CG    1 
ATOM   404  C  CD1   . PHE A 1 57  ? 17.719 2.176   25.658 1.00 13.94 ? 49  PHE A CD1   1 
ATOM   405  C  CD2   . PHE A 1 57  ? 16.498 3.956   26.656 1.00 14.60 ? 49  PHE A CD2   1 
ATOM   406  C  CE1   . PHE A 1 57  ? 18.431 3.076   24.900 1.00 14.64 ? 49  PHE A CE1   1 
ATOM   407  C  CE2   . PHE A 1 57  ? 17.210 4.858   25.894 1.00 14.94 ? 49  PHE A CE2   1 
ATOM   408  C  CZ    . PHE A 1 57  ? 18.173 4.415   25.014 1.00 15.09 ? 49  PHE A CZ    1 
ATOM   409  N  N     . THR A 1 58  ? 15.048 0.649   30.305 1.00 12.58 ? 50  THR A N     1 
ATOM   410  C  CA    . THR A 1 58  ? 14.127 -0.254  30.977 1.00 12.49 ? 50  THR A CA    1 
ATOM   411  C  C     . THR A 1 58  ? 12.722 0.307   30.856 1.00 12.58 ? 50  THR A C     1 
ATOM   412  O  O     . THR A 1 58  ? 12.505 1.498   31.079 1.00 13.45 ? 50  THR A O     1 
ATOM   413  C  CB    . THR A 1 58  ? 14.501 -0.414  32.447 1.00 13.19 ? 50  THR A CB    1 
ATOM   414  O  OG1   . THR A 1 58  ? 15.803 -1.003  32.511 1.00 14.12 ? 50  THR A OG1   1 
ATOM   415  C  CG2   . THR A 1 58  ? 13.511 -1.308  33.178 1.00 14.56 ? 50  THR A CG2   1 
ATOM   416  N  N     . GLY A 1 59  ? 11.772 -0.559  30.514 1.00 12.34 ? 51  GLY A N     1 
ATOM   417  C  CA    . GLY A 1 59  ? 10.375 -0.193  30.469 1.00 12.37 ? 51  GLY A CA    1 
ATOM   418  C  C     . GLY A 1 59  ? 9.541  -1.450  30.541 1.00 12.79 ? 51  GLY A C     1 
ATOM   419  O  O     . GLY A 1 59  ? 9.882  -2.388  31.271 1.00 13.23 ? 51  GLY A O     1 
ATOM   420  N  N     . THR A 1 60  ? 8.459  -1.487  29.776 1.00 13.50 ? 52  THR A N     1 
ATOM   421  C  CA    . THR A 1 60  ? 7.591  -2.647  29.687 1.00 13.21 ? 52  THR A CA    1 
ATOM   422  C  C     . THR A 1 60  ? 7.264  -2.917  28.228 1.00 13.41 ? 52  THR A C     1 
ATOM   423  O  O     . THR A 1 60  ? 7.166  -1.993  27.412 1.00 13.83 ? 52  THR A O     1 
ATOM   424  C  CB    . THR A 1 60  ? 6.274  -2.447  30.467 1.00 14.27 ? 52  THR A CB    1 
ATOM   425  O  OG1   . THR A 1 60  ? 5.605  -1.264  30.016 1.00 14.65 ? 52  THR A OG1   1 
ATOM   426  C  CG2   . THR A 1 60  ? 6.519  -2.345  31.962 1.00 14.76 ? 52  THR A CG2   1 
ATOM   427  N  N     . TYR A 1 61  ? 7.070  -4.195  27.910 1.00 13.36 ? 53  TYR A N     1 
ATOM   428  C  CA    . TYR A 1 61  ? 6.486  -4.602  26.642 1.00 14.03 ? 53  TYR A CA    1 
ATOM   429  C  C     . TYR A 1 61  ? 5.185  -5.313  26.965 1.00 13.79 ? 53  TYR A C     1 
ATOM   430  O  O     . TYR A 1 61  ? 5.181  -6.332  27.667 1.00 14.18 ? 53  TYR A O     1 
ATOM   431  C  CB    . TYR A 1 61  ? 7.403  -5.538  25.852 1.00 14.32 ? 53  TYR A CB    1 
ATOM   432  C  CG    . TYR A 1 61  ? 6.730  -6.052  24.595 1.00 14.05 ? 53  TYR A CG    1 
ATOM   433  C  CD1   . TYR A 1 61  ? 6.495  -5.206  23.518 1.00 14.71 ? 53  TYR A CD1   1 
ATOM   434  C  CD2   . TYR A 1 61  ? 6.290  -7.371  24.503 1.00 14.37 ? 53  TYR A CD2   1 
ATOM   435  C  CE1   . TYR A 1 61  ? 5.848  -5.656  22.383 1.00 14.93 ? 53  TYR A CE1   1 
ATOM   436  C  CE2   . TYR A 1 61  ? 5.650  -7.831  23.375 1.00 14.95 ? 53  TYR A CE2   1 
ATOM   437  C  CZ    . TYR A 1 61  ? 5.437  -6.974  22.316 1.00 15.06 ? 53  TYR A CZ    1 
ATOM   438  O  OH    . TYR A 1 61  ? 4.825  -7.412  21.169 1.00 16.50 ? 53  TYR A OH    1 
ATOM   439  N  N     . LYS A 1 62  ? 4.080  -4.765  26.473 1.00 14.53 ? 54  LYS A N     1 
ATOM   440  C  CA    . LYS A 1 62  ? 2.746  -5.258  26.809 1.00 15.00 ? 54  LYS A CA    1 
ATOM   441  C  C     . LYS A 1 62  ? 2.587  -5.452  28.316 1.00 14.83 ? 54  LYS A C     1 
ATOM   442  O  O     . LYS A 1 62  ? 1.981  -6.419  28.784 1.00 15.44 ? 54  LYS A O     1 
ATOM   443  C  CB    . LYS A 1 62  ? 2.390  -6.519  26.021 1.00 16.33 ? 54  LYS A CB    1 
ATOM   444  C  CG    . LYS A 1 62  ? 2.292  -6.250  24.517 1.00 16.79 ? 54  LYS A CG    1 
ATOM   445  C  CD    . LYS A 1 62  ? 1.803  -7.448  23.745 1.00 17.61 ? 54  LYS A CD    1 
ATOM   446  C  CE    . LYS A 1 62  ? 1.521  -7.113  22.291 1.00 17.90 ? 54  LYS A CE    1 
ATOM   447  N  NZ    . LYS A 1 62  ? 1.068  -8.316  21.533 1.00 19.49 ? 54  LYS A NZ    1 
ATOM   448  N  N     . GLY A 1 63  ? 3.113  -4.495  29.078 1.00 14.93 ? 55  GLY A N     1 
ATOM   449  C  CA    . GLY A 1 63  ? 2.973  -4.452  30.513 1.00 14.69 ? 55  GLY A CA    1 
ATOM   450  C  C     . GLY A 1 63  ? 4.011  -5.211  31.302 1.00 15.46 ? 55  GLY A C     1 
ATOM   451  O  O     . GLY A 1 63  ? 4.092  -5.022  32.523 1.00 17.04 ? 55  GLY A O     1 
ATOM   452  N  N     . LYS A 1 64  ? 4.801  -6.067  30.657 1.00 14.25 ? 56  LYS A N     1 
ATOM   453  C  CA    . LYS A 1 64  ? 5.766  -6.900  31.363 1.00 14.51 ? 56  LYS A CA    1 
ATOM   454  C  C     . LYS A 1 64  ? 7.117  -6.190  31.400 1.00 14.45 ? 56  LYS A C     1 
ATOM   455  O  O     . LYS A 1 64  ? 7.584  -5.718  30.359 1.00 14.31 ? 56  LYS A O     1 
ATOM   456  C  CB    . LYS A 1 64  ? 5.903  -8.236  30.654 1.00 15.64 ? 56  LYS A CB    1 
ATOM   457  C  CG    . LYS A 1 64  ? 6.760  -9.246  31.400 1.00 16.08 ? 56  LYS A CG    1 
ATOM   458  C  CD    . LYS A 1 64  ? 6.705  -10.610 30.704 1.00 16.08 ? 56  LYS A CD    1 
ATOM   459  C  CE    . LYS A 1 64  ? 7.535  -11.670 31.401 1.00 17.32 ? 56  LYS A CE    1 
ATOM   460  N  NZ    . LYS A 1 64  ? 8.996  -11.494 31.186 1.00 18.56 ? 56  LYS A NZ    1 
ATOM   461  N  N     . PRO A 1 65  ? 7.786  -6.101  32.552 1.00 14.73 ? 57  PRO A N     1 
ATOM   462  C  CA    . PRO A 1 65  ? 9.097  -5.430  32.600 1.00 14.65 ? 57  PRO A CA    1 
ATOM   463  C  C     . PRO A 1 65  ? 10.077 -6.013  31.590 1.00 13.31 ? 57  PRO A C     1 
ATOM   464  O  O     . PRO A 1 65  ? 10.215 -7.224  31.453 1.00 14.41 ? 57  PRO A O     1 
ATOM   465  C  CB    . PRO A 1 65  ? 9.561  -5.671  34.040 1.00 16.15 ? 57  PRO A CB    1 
ATOM   466  C  CG    . PRO A 1 65  ? 8.287  -5.853  34.813 1.00 17.37 ? 57  PRO A CG    1 
ATOM   467  C  CD    . PRO A 1 65  ? 7.359  -6.557  33.886 1.00 16.51 ? 57  PRO A CD    1 
ATOM   468  N  N     . LEU A 1 66  ? 10.777 -5.135  30.883 1.00 13.00 ? 58  LEU A N     1 
ATOM   469  C  CA    . LEU A 1 66  ? 11.740 -5.534  29.874 1.00 12.54 ? 58  LEU A CA    1 
ATOM   470  C  C     . LEU A 1 66  ? 12.781 -4.432  29.738 1.00 12.60 ? 58  LEU A C     1 
ATOM   471  O  O     . LEU A 1 66  ? 12.431 -3.258  29.688 1.00 12.73 ? 58  LEU A O     1 
ATOM   472  C  CB    . LEU A 1 66  ? 11.058 -5.761  28.519 1.00 13.38 ? 58  LEU A CB    1 
ATOM   473  C  CG    . LEU A 1 66  ? 11.970 -6.275  27.403 1.00 13.57 ? 58  LEU A CG    1 
ATOM   474  C  CD1   . LEU A 1 66  ? 12.608 -7.607  27.757 1.00 13.52 ? 58  LEU A CD1   1 
ATOM   475  C  CD2   . LEU A 1 66  ? 11.215 -6.378  26.101 1.00 14.37 ? 58  LEU A CD2   1 
ATOM   476  N  N     . SER A 1 67  ? 14.050 -4.816  29.674 1.00 12.06 ? 59  SER A N     1 
ATOM   477  C  CA    . SER A 1 67  ? 15.136 -3.896  29.379 1.00 12.09 ? 59  SER A CA    1 
ATOM   478  C  C     . SER A 1 67  ? 15.711 -4.213  28.009 1.00 11.59 ? 59  SER A C     1 
ATOM   479  O  O     . SER A 1 67  ? 15.594 -5.334  27.506 1.00 11.95 ? 59  SER A O     1 
ATOM   480  C  CB    . SER A 1 67  ? 16.232 -3.961  30.441 1.00 12.89 ? 59  SER A CB    1 
ATOM   481  O  OG    . SER A 1 67  ? 15.739 -3.603  31.720 1.00 13.14 ? 59  SER A OG    1 
ATOM   482  N  N     . VAL A 1 68  ? 16.384 -3.221  27.430 1.00 12.40 ? 60  VAL A N     1 
ATOM   483  C  CA    A VAL A 1 68  ? 17.097 -3.404  26.174 0.52 12.39 ? 60  VAL A CA    1 
ATOM   484  C  CA    B VAL A 1 68  ? 17.066 -3.361  26.145 0.48 12.75 ? 60  VAL A CA    1 
ATOM   485  C  C     . VAL A 1 68  ? 18.375 -2.589  26.241 1.00 12.44 ? 60  VAL A C     1 
ATOM   486  O  O     . VAL A 1 68  ? 18.368 -1.437  26.674 1.00 12.55 ? 60  VAL A O     1 
ATOM   487  C  CB    A VAL A 1 68  ? 16.249 -3.031  24.942 0.52 12.95 ? 60  VAL A CB    1 
ATOM   488  C  CB    B VAL A 1 68  ? 16.195 -2.811  24.996 0.48 14.31 ? 60  VAL A CB    1 
ATOM   489  C  CG1   A VAL A 1 68  ? 15.826 -1.576  25.007 0.52 12.71 ? 60  VAL A CG1   1 
ATOM   490  C  CG1   B VAL A 1 68  ? 16.862 -3.052  23.647 0.48 15.33 ? 60  VAL A CG1   1 
ATOM   491  C  CG2   A VAL A 1 68  ? 17.024 -3.320  23.653 0.52 14.26 ? 60  VAL A CG2   1 
ATOM   492  C  CG2   B VAL A 1 68  ? 14.777 -3.413  25.032 0.48 14.82 ? 60  VAL A CG2   1 
ATOM   493  N  N     . MET A 1 69  ? 19.489 -3.197  25.833 1.00 12.90 ? 61  MET A N     1 
ATOM   494  C  CA    . MET A 1 69  ? 20.766 -2.514  25.933 1.00 13.33 ? 61  MET A CA    1 
ATOM   495  C  C     . MET A 1 69  ? 21.715 -2.995  24.853 1.00 13.07 ? 61  MET A C     1 
ATOM   496  O  O     . MET A 1 69  ? 21.660 -4.145  24.417 1.00 13.56 ? 61  MET A O     1 
ATOM   497  C  CB    . MET A 1 69  ? 21.368 -2.717  27.321 1.00 15.36 ? 61  MET A CB    1 
ATOM   498  C  CG    . MET A 1 69  ? 22.710 -2.062  27.544 1.00 18.06 ? 61  MET A CG    1 
ATOM   499  S  SD    . MET A 1 69  ? 23.224 -2.269  29.244 1.00 21.83 ? 61  MET A SD    1 
ATOM   500  C  CE    . MET A 1 69  ? 24.931 -1.823  29.087 1.00 22.35 ? 61  MET A CE    1 
ATOM   501  N  N     . GLY A 1 70  ? 22.598 -2.100  24.434 1.00 12.61 ? 62  GLY A N     1 
ATOM   502  C  CA    . GLY A 1 70  ? 23.658 -2.505  23.537 1.00 12.98 ? 62  GLY A CA    1 
ATOM   503  C  C     . GLY A 1 70  ? 24.695 -3.376  24.224 1.00 12.83 ? 62  GLY A C     1 
ATOM   504  O  O     . GLY A 1 70  ? 24.902 -3.308  25.442 1.00 13.35 ? 62  GLY A O     1 
ATOM   505  N  N     . HIS A 1 71  ? 25.387 -4.200  23.429 1.00 12.85 ? 63  HIS A N     1 
ATOM   506  C  CA    . HIS A 1 71  ? 26.469 -5.033  23.947 1.00 12.17 ? 63  HIS A CA    1 
ATOM   507  C  C     . HIS A 1 71  ? 27.809 -4.834  23.256 1.00 11.88 ? 63  HIS A C     1 
ATOM   508  O  O     . HIS A 1 71  ? 28.787 -5.433  23.706 1.00 12.61 ? 63  HIS A O     1 
ATOM   509  C  CB    . HIS A 1 71  ? 26.105 -6.540  24.026 1.00 13.07 ? 63  HIS A CB    1 
ATOM   510  C  CG    . HIS A 1 71  ? 25.749 -7.197  22.721 1.00 12.59 ? 63  HIS A CG    1 
ATOM   511  N  ND1   . HIS A 1 71  ? 26.592 -7.233  21.632 1.00 12.28 ? 63  HIS A ND1   1 
ATOM   512  C  CD2   . HIS A 1 71  ? 24.656 -7.923  22.367 1.00 12.39 ? 63  HIS A CD2   1 
ATOM   513  C  CE1   . HIS A 1 71  ? 26.025 -7.926  20.655 1.00 12.61 ? 63  HIS A CE1   1 
ATOM   514  N  NE2   . HIS A 1 71  ? 24.849 -8.358  21.075 1.00 12.40 ? 63  HIS A NE2   1 
ATOM   515  N  N     . GLY A 1 72  ? 27.892 -4.013  22.204 1.00 12.39 ? 64  GLY A N     1 
ATOM   516  C  CA    . GLY A 1 72  ? 29.138 -3.836  21.471 1.00 12.43 ? 64  GLY A CA    1 
ATOM   517  C  C     . GLY A 1 72  ? 29.443 -5.044  20.605 1.00 12.43 ? 64  GLY A C     1 
ATOM   518  O  O     . GLY A 1 72  ? 28.681 -5.990  20.532 1.00 14.73 ? 64  GLY A O     1 
ATOM   519  N  N     . MET A 1 73  ? 30.592 -5.018  19.951 1.00 11.08 ? 65  MET A N     1 
ATOM   520  C  CA    . MET A 1 73  ? 30.967 -6.092  19.041 1.00 10.29 ? 65  MET A CA    1 
ATOM   521  C  C     . MET A 1 73  ? 32.018 -6.993  19.662 1.00 10.18 ? 65  MET A C     1 
ATOM   522  O  O     . MET A 1 73  ? 33.060 -6.521  20.129 1.00 10.81 ? 65  MET A O     1 
ATOM   523  C  CB    . MET A 1 73  ? 31.471 -5.529  17.710 1.00 11.10 ? 65  MET A CB    1 
ATOM   524  C  CG    . MET A 1 73  ? 30.429 -4.662  16.998 1.00 11.23 ? 65  MET A CG    1 
ATOM   525  S  SD    . MET A 1 73  ? 30.809 -4.254  15.310 1.00 12.70 ? 65  MET A SD    1 
ATOM   526  C  CE    . MET A 1 73  ? 32.151 -3.119  15.581 1.00 13.59 ? 65  MET A CE    1 
ATOM   527  N  N     . GLY A 1 74  ? 31.736 -8.285  19.664 1.00 9.87  ? 66  GLY A N     1 
ATOM   528  C  CA    . GLY A 1 74  ? 32.695 -9.304  20.022 1.00 9.71  ? 66  GLY A CA    1 
ATOM   529  C  C     . GLY A 1 74  ? 32.446 -9.916  21.394 1.00 9.49  ? 66  GLY A C     1 
ATOM   530  O  O     . GLY A 1 74  ? 31.830 -9.326  22.290 1.00 10.29 ? 66  GLY A O     1 
ATOM   531  N  N     . ILE A 1 75  ? 32.971 -11.127 21.541 1.00 9.31  ? 67  ILE A N     1 
ATOM   532  C  CA    . ILE A 1 75  ? 32.821 -11.875 22.786 1.00 9.40  ? 67  ILE A CA    1 
ATOM   533  C  C     . ILE A 1 75  ? 33.313 -11.106 24.009 1.00 9.15  ? 67  ILE A C     1 
ATOM   534  O  O     . ILE A 1 75  ? 32.613 -11.093 25.028 1.00 9.53  ? 67  ILE A O     1 
ATOM   535  C  CB    . ILE A 1 75  ? 33.460 -13.270 22.637 1.00 9.11  ? 67  ILE A CB    1 
ATOM   536  C  CG1   . ILE A 1 75  ? 32.526 -14.176 21.826 1.00 9.34  ? 67  ILE A CG1   1 
ATOM   537  C  CG2   . ILE A 1 75  ? 33.798 -13.863 23.987 1.00 10.09 ? 67  ILE A CG2   1 
ATOM   538  C  CD1   . ILE A 1 75  ? 33.155 -15.436 21.303 1.00 10.82 ? 67  ILE A CD1   1 
ATOM   539  N  N     . PRO A 1 76  ? 34.472 -10.457 23.989 1.00 8.82  ? 68  PRO A N     1 
ATOM   540  C  CA    . PRO A 1 76  ? 34.910 -9.782  25.222 1.00 9.64  ? 68  PRO A CA    1 
ATOM   541  C  C     . PRO A 1 76  ? 33.962 -8.672  25.660 1.00 9.28  ? 68  PRO A C     1 
ATOM   542  O  O     . PRO A 1 76  ? 33.767 -8.448  26.864 1.00 10.21 ? 68  PRO A O     1 
ATOM   543  C  CB    . PRO A 1 76  ? 36.311 -9.261  24.858 1.00 9.82  ? 68  PRO A CB    1 
ATOM   544  C  CG    . PRO A 1 76  ? 36.796 -10.223 23.779 1.00 9.53  ? 68  PRO A CG    1 
ATOM   545  C  CD    . PRO A 1 76  ? 35.534 -10.523 22.971 1.00 9.39  ? 68  PRO A CD    1 
ATOM   546  N  N     . SER A 1 77  ? 33.367 -7.964  24.705 1.00 10.06 ? 69  SER A N     1 
ATOM   547  C  CA    . SER A 1 77  ? 32.457 -6.870  25.032 1.00 10.33 ? 69  SER A CA    1 
ATOM   548  C  C     . SER A 1 77  ? 31.146 -7.402  25.612 1.00 10.23 ? 69  SER A C     1 
ATOM   549  O  O     . SER A 1 77  ? 30.724 -6.995  26.699 1.00 10.73 ? 69  SER A O     1 
ATOM   550  C  CB    . SER A 1 77  ? 32.217 -6.050  23.772 1.00 10.84 ? 69  SER A CB    1 
ATOM   551  O  OG    . SER A 1 77  ? 31.424 -4.899  24.038 1.00 11.65 ? 69  SER A OG    1 
ATOM   552  N  N     . ILE A 1 78  ? 30.495 -8.342  24.924 1.00 10.11 ? 70  ILE A N     1 
ATOM   553  C  CA    . ILE A 1 78  ? 29.262 -8.887  25.490 1.00 10.24 ? 70  ILE A CA    1 
ATOM   554  C  C     . ILE A 1 78  ? 29.520 -9.563  26.826 1.00 10.10 ? 70  ILE A C     1 
ATOM   555  O  O     . ILE A 1 78  ? 28.668 -9.538  27.712 1.00 10.48 ? 70  ILE A O     1 
ATOM   556  C  CB    . ILE A 1 78  ? 28.523 -9.800  24.495 1.00 10.56 ? 70  ILE A CB    1 
ATOM   557  C  CG1   . ILE A 1 78  ? 27.114 -10.106 25.014 1.00 10.94 ? 70  ILE A CG1   1 
ATOM   558  C  CG2   . ILE A 1 78  ? 29.275 -11.089 24.263 1.00 11.19 ? 70  ILE A CG2   1 
ATOM   559  C  CD1   . ILE A 1 78  ? 26.214 -10.739 24.004 1.00 11.42 ? 70  ILE A CD1   1 
ATOM   560  N  N     . SER A 1 79  ? 30.697 -10.166 27.005 1.00 10.08 ? 71  SER A N     1 
ATOM   561  C  CA    . SER A 1 79  ? 30.967 -10.848 28.262 1.00 10.58 ? 71  SER A CA    1 
ATOM   562  C  C     . SER A 1 79  ? 30.960 -9.877  29.437 1.00 10.25 ? 71  SER A C     1 
ATOM   563  O  O     . SER A 1 79  ? 30.427 -10.183 30.509 1.00 10.77 ? 71  SER A O     1 
ATOM   564  C  CB    . SER A 1 79  ? 32.314 -11.557 28.183 1.00 10.32 ? 71  SER A CB    1 
ATOM   565  O  OG    . SER A 1 79  ? 32.303 -12.628 27.253 1.00 10.97 ? 71  SER A OG    1 
ATOM   566  N  N     . ILE A 1 80  ? 31.571 -8.707  29.268 1.00 10.33 ? 72  ILE A N     1 
ATOM   567  C  CA    . ILE A 1 80  ? 31.521 -7.687  30.315 1.00 10.16 ? 72  ILE A CA    1 
ATOM   568  C  C     . ILE A 1 80  ? 30.077 -7.352  30.668 1.00 10.26 ? 72  ILE A C     1 
ATOM   569  O  O     . ILE A 1 80  ? 29.673 -7.380  31.838 1.00 10.99 ? 72  ILE A O     1 
ATOM   570  C  CB    . ILE A 1 80  ? 32.299 -6.432  29.875 1.00 10.37 ? 72  ILE A CB    1 
ATOM   571  C  CG1   . ILE A 1 80  ? 33.802 -6.673  29.966 1.00 10.76 ? 72  ILE A CG1   1 
ATOM   572  C  CG2   . ILE A 1 80  ? 31.913 -5.213  30.719 1.00 11.23 ? 72  ILE A CG2   1 
ATOM   573  C  CD1   . ILE A 1 80  ? 34.643 -5.640  29.239 1.00 12.18 ? 72  ILE A CD1   1 
ATOM   574  N  N     . TYR A 1 81  ? 29.291 -6.982  29.665 1.00 10.69 ? 73  TYR A N     1 
ATOM   575  C  CA    . TYR A 1 81  ? 27.963 -6.452  29.943 1.00 11.40 ? 73  TYR A CA    1 
ATOM   576  C  C     . TYR A 1 81  ? 27.046 -7.532  30.493 1.00 11.30 ? 73  TYR A C     1 
ATOM   577  O  O     . TYR A 1 81  ? 26.290 -7.278  31.435 1.00 12.12 ? 73  TYR A O     1 
ATOM   578  C  CB    . TYR A 1 81  ? 27.394 -5.812  28.684 1.00 11.77 ? 73  TYR A CB    1 
ATOM   579  C  CG    . TYR A 1 81  ? 28.099 -4.523  28.315 1.00 12.30 ? 73  TYR A CG    1 
ATOM   580  C  CD1   . TYR A 1 81  ? 28.008 -3.398  29.123 1.00 13.02 ? 73  TYR A CD1   1 
ATOM   581  C  CD2   . TYR A 1 81  ? 28.866 -4.439  27.171 1.00 13.05 ? 73  TYR A CD2   1 
ATOM   582  C  CE1   . TYR A 1 81  ? 28.654 -2.233  28.791 1.00 13.67 ? 73  TYR A CE1   1 
ATOM   583  C  CE2   . TYR A 1 81  ? 29.527 -3.279  26.832 1.00 13.41 ? 73  TYR A CE2   1 
ATOM   584  C  CZ    . TYR A 1 81  ? 29.419 -2.179  27.643 1.00 13.62 ? 73  TYR A CZ    1 
ATOM   585  O  OH    . TYR A 1 81  ? 30.072 -1.019  27.281 1.00 14.33 ? 73  TYR A OH    1 
ATOM   586  N  N     . ALA A 1 82  ? 27.121 -8.748  29.943 1.00 11.05 ? 74  ALA A N     1 
ATOM   587  C  CA    . ALA A 1 82  ? 26.246 -9.827  30.391 1.00 11.58 ? 74  ALA A CA    1 
ATOM   588  C  C     . ALA A 1 82  ? 26.636 -10.332 31.772 1.00 11.20 ? 74  ALA A C     1 
ATOM   589  O  O     . ALA A 1 82  ? 25.766 -10.625 32.596 1.00 11.88 ? 74  ALA A O     1 
ATOM   590  C  CB    . ALA A 1 82  ? 26.258 -10.967 29.381 1.00 12.01 ? 74  ALA A CB    1 
ATOM   591  N  N     . GLU A 1 83  ? 27.937 -10.492 32.033 1.00 10.92 ? 75  GLU A N     1 
ATOM   592  C  CA    . GLU A 1 83  ? 28.365 -10.860 33.378 1.00 11.62 ? 75  GLU A CA    1 
ATOM   593  C  C     . GLU A 1 83  ? 27.768 -9.906  34.406 1.00 11.51 ? 75  GLU A C     1 
ATOM   594  O  O     . GLU A 1 83  ? 27.254 -10.323 35.444 1.00 12.42 ? 75  GLU A O     1 
ATOM   595  C  CB    . GLU A 1 83  ? 29.896 -10.858 33.460 1.00 11.87 ? 75  GLU A CB    1 
ATOM   596  C  CG    . GLU A 1 83  ? 30.442 -11.346 34.799 1.00 13.32 ? 75  GLU A CG    1 
ATOM   597  C  CD    . GLU A 1 83  ? 30.795 -12.821 34.820 1.00 13.84 ? 75  GLU A CD    1 
ATOM   598  O  OE1   . GLU A 1 83  ? 30.912 -13.429 33.748 1.00 14.19 ? 75  GLU A OE1   1 
ATOM   599  O  OE2   . GLU A 1 83  ? 30.976 -13.365 35.919 1.00 14.45 ? 75  GLU A OE2   1 
ATOM   600  N  N     . GLU A 1 84  ? 27.849 -8.606  34.137 1.00 11.20 ? 76  GLU A N     1 
ATOM   601  C  CA    . GLU A 1 84  ? 27.310 -7.623  35.072 1.00 11.67 ? 76  GLU A CA    1 
ATOM   602  C  C     . GLU A 1 84  ? 25.801 -7.742  35.203 1.00 11.32 ? 76  GLU A C     1 
ATOM   603  O  O     . GLU A 1 84  ? 25.264 -7.665  36.311 1.00 12.94 ? 76  GLU A O     1 
ATOM   604  C  CB    . GLU A 1 84  ? 27.711 -6.224  34.606 1.00 11.90 ? 76  GLU A CB    1 
ATOM   605  C  CG    . GLU A 1 84  ? 29.199 -5.989  34.715 1.00 11.97 ? 76  GLU A CG    1 
ATOM   606  C  CD    . GLU A 1 84  ? 29.662 -4.656  34.188 1.00 12.36 ? 76  GLU A CD    1 
ATOM   607  O  OE1   . GLU A 1 84  ? 28.819 -3.851  33.721 1.00 13.12 ? 76  GLU A OE1   1 
ATOM   608  O  OE2   . GLU A 1 84  ? 30.886 -4.409  34.256 1.00 12.41 ? 76  GLU A OE2   1 
ATOM   609  N  N     . LEU A 1 85  ? 25.100 -7.897  34.088 1.00 11.11 ? 77  LEU A N     1 
ATOM   610  C  CA    . LEU A 1 85  ? 23.644 -8.005  34.149 1.00 11.76 ? 77  LEU A CA    1 
ATOM   611  C  C     . LEU A 1 85  ? 23.202 -9.172  35.019 1.00 12.87 ? 77  LEU A C     1 
ATOM   612  O  O     . LEU A 1 85  ? 22.321 -9.021  35.866 1.00 13.16 ? 77  LEU A O     1 
ATOM   613  C  CB    . LEU A 1 85  ? 23.057 -8.102  32.746 1.00 12.36 ? 77  LEU A CB    1 
ATOM   614  C  CG    . LEU A 1 85  ? 23.044 -6.767  31.986 1.00 12.96 ? 77  LEU A CG    1 
ATOM   615  C  CD1   . LEU A 1 85  ? 22.606 -6.999  30.551 1.00 15.72 ? 77  LEU A CD1   1 
ATOM   616  C  CD2   . LEU A 1 85  ? 22.160 -5.701  32.647 1.00 14.03 ? 77  LEU A CD2   1 
ATOM   617  N  N     . TYR A 1 86  ? 23.802 -10.348 34.827 1.00 12.59 ? 78  TYR A N     1 
ATOM   618  C  CA    . TYR A 1 86  ? 23.417 -11.498 35.642 1.00 13.01 ? 78  TYR A CA    1 
ATOM   619  C  C     . TYR A 1 86  ? 23.878 -11.339 37.086 1.00 14.20 ? 78  TYR A C     1 
ATOM   620  O  O     . TYR A 1 86  ? 23.146 -11.667 38.018 1.00 16.71 ? 78  TYR A O     1 
ATOM   621  C  CB    . TYR A 1 86  ? 23.986 -12.791 35.059 1.00 13.21 ? 78  TYR A CB    1 
ATOM   622  C  CG    . TYR A 1 86  ? 23.376 -13.258 33.755 1.00 12.91 ? 78  TYR A CG    1 
ATOM   623  C  CD1   . TYR A 1 86  ? 22.020 -13.542 33.655 1.00 13.13 ? 78  TYR A CD1   1 
ATOM   624  C  CD2   . TYR A 1 86  ? 24.152 -13.452 32.641 1.00 13.38 ? 78  TYR A CD2   1 
ATOM   625  C  CE1   . TYR A 1 86  ? 21.472 -13.993 32.459 1.00 13.72 ? 78  TYR A CE1   1 
ATOM   626  C  CE2   . TYR A 1 86  ? 23.612 -13.896 31.453 1.00 12.79 ? 78  TYR A CE2   1 
ATOM   627  C  CZ    . TYR A 1 86  ? 22.280 -14.179 31.370 1.00 12.59 ? 78  TYR A CZ    1 
ATOM   628  O  OH    . TYR A 1 86  ? 21.786 -14.614 30.170 1.00 13.12 ? 78  TYR A OH    1 
ATOM   629  N  N     . ASN A 1 87  ? 25.089 -10.844 37.300 1.00 14.37 ? 79  ASN A N     1 
ATOM   630  C  CA    . ASN A 1 87  ? 25.658 -10.849 38.641 1.00 15.67 ? 79  ASN A CA    1 
ATOM   631  C  C     . ASN A 1 87  ? 25.177 -9.674  39.481 1.00 16.26 ? 79  ASN A C     1 
ATOM   632  O  O     . ASN A 1 87  ? 24.687 -9.862  40.600 1.00 19.53 ? 79  ASN A O     1 
ATOM   633  C  CB    . ASN A 1 87  ? 27.183 -10.817 38.534 1.00 16.80 ? 79  ASN A CB    1 
ATOM   634  C  CG    . ASN A 1 87  ? 27.857 -10.908 39.871 1.00 20.87 ? 79  ASN A CG    1 
ATOM   635  O  OD1   . ASN A 1 87  ? 27.440 -11.676 40.733 1.00 24.30 ? 79  ASN A OD1   1 
ATOM   636  N  ND2   . ASN A 1 87  ? 28.925 -10.127 40.054 1.00 22.53 ? 79  ASN A ND2   1 
ATOM   637  N  N     . VAL A 1 88  ? 25.351 -8.452  38.981 1.00 15.39 ? 80  VAL A N     1 
ATOM   638  C  CA    . VAL A 1 88  ? 25.022 -7.256  39.748 1.00 15.53 ? 80  VAL A CA    1 
ATOM   639  C  C     . VAL A 1 88  ? 23.540 -6.930  39.634 1.00 14.85 ? 80  VAL A C     1 
ATOM   640  O  O     . VAL A 1 88  ? 22.886 -6.587  40.625 1.00 16.58 ? 80  VAL A O     1 
ATOM   641  C  CB    . VAL A 1 88  ? 25.911 -6.086  39.275 1.00 16.21 ? 80  VAL A CB    1 
ATOM   642  C  CG1   . VAL A 1 88  ? 25.497 -4.771  39.940 1.00 18.55 ? 80  VAL A CG1   1 
ATOM   643  C  CG2   . VAL A 1 88  ? 27.395 -6.412  39.517 1.00 17.62 ? 80  VAL A CG2   1 
ATOM   644  N  N     . TYR A 1 89  ? 22.988 -7.023  38.437 1.00 13.79 ? 81  TYR A N     1 
ATOM   645  C  CA    . TYR A 1 89  ? 21.627 -6.567  38.202 1.00 14.30 ? 81  TYR A CA    1 
ATOM   646  C  C     . TYR A 1 89  ? 20.586 -7.673  38.367 1.00 14.32 ? 81  TYR A C     1 
ATOM   647  O  O     . TYR A 1 89  ? 19.384 -7.388  38.296 1.00 15.16 ? 81  TYR A O     1 
ATOM   648  C  CB    . TYR A 1 89  ? 21.527 -5.880  36.838 1.00 14.08 ? 81  TYR A CB    1 
ATOM   649  C  CG    . TYR A 1 89  ? 22.364 -4.623  36.793 1.00 13.24 ? 81  TYR A CG    1 
ATOM   650  C  CD1   . TYR A 1 89  ? 21.939 -3.452  37.407 1.00 14.88 ? 81  TYR A CD1   1 
ATOM   651  C  CD2   . TYR A 1 89  ? 23.615 -4.613  36.175 1.00 13.69 ? 81  TYR A CD2   1 
ATOM   652  C  CE1   . TYR A 1 89  ? 22.715 -2.317  37.387 1.00 15.46 ? 81  TYR A CE1   1 
ATOM   653  C  CE2   . TYR A 1 89  ? 24.385 -3.468  36.138 1.00 14.26 ? 81  TYR A CE2   1 
ATOM   654  C  CZ    . TYR A 1 89  ? 23.934 -2.327  36.753 1.00 15.22 ? 81  TYR A CZ    1 
ATOM   655  O  OH    . TYR A 1 89  ? 24.708 -1.192  36.718 1.00 16.37 ? 81  TYR A OH    1 
ATOM   656  N  N     . LYS A 1 90  ? 21.015 -8.911  38.624 1.00 14.62 ? 82  LYS A N     1 
ATOM   657  C  CA    . LYS A 1 90  ? 20.116 -10.023 38.964 1.00 14.95 ? 82  LYS A CA    1 
ATOM   658  C  C     . LYS A 1 90  ? 19.164 -10.377 37.827 1.00 14.49 ? 82  LYS A C     1 
ATOM   659  O  O     . LYS A 1 90  ? 18.063 -10.880 38.053 1.00 15.70 ? 82  LYS A O     1 
ATOM   660  C  CB    . LYS A 1 90  ? 19.328 -9.757  40.250 1.00 17.35 ? 82  LYS A CB    1 
ATOM   661  C  CG    . LYS A 1 90  ? 20.165 -9.234  41.403 1.00 22.13 ? 82  LYS A CG    1 
ATOM   662  C  CD    . LYS A 1 90  ? 21.290 -10.164 41.760 1.00 26.26 ? 82  LYS A CD    1 
ATOM   663  C  CE    . LYS A 1 90  ? 22.013 -9.669  43.000 1.00 29.84 ? 82  LYS A CE    1 
ATOM   664  N  NZ    . LYS A 1 90  ? 23.245 -10.443 43.241 1.00 31.95 ? 82  LYS A NZ    1 
ATOM   665  N  N     . VAL A 1 91  ? 19.596 -10.139 36.597 1.00 14.39 ? 83  VAL A N     1 
ATOM   666  C  CA    . VAL A 1 91  ? 18.824 -10.521 35.430 1.00 14.02 ? 83  VAL A CA    1 
ATOM   667  C  C     . VAL A 1 91  ? 18.714 -12.038 35.359 1.00 13.55 ? 83  VAL A C     1 
ATOM   668  O  O     . VAL A 1 91  ? 19.628 -12.772 35.750 1.00 14.56 ? 83  VAL A O     1 
ATOM   669  C  CB    . VAL A 1 91  ? 19.517 -9.917  34.196 1.00 14.35 ? 83  VAL A CB    1 
ATOM   670  C  CG1   . VAL A 1 91  ? 19.009 -10.514 32.888 1.00 16.09 ? 83  VAL A CG1   1 
ATOM   671  C  CG2   . VAL A 1 91  ? 19.337 -8.396  34.222 1.00 13.95 ? 83  VAL A CG2   1 
ATOM   672  N  N     . LYS A 1 92  ? 17.568 -12.511 34.871 1.00 13.12 ? 84  LYS A N     1 
ATOM   673  C  CA    . LYS A 1 92  ? 17.312 -13.936 34.735 1.00 13.19 ? 84  LYS A CA    1 
ATOM   674  C  C     . LYS A 1 92  ? 17.400 -14.441 33.303 1.00 12.96 ? 84  LYS A C     1 
ATOM   675  O  O     . LYS A 1 92  ? 17.801 -15.592 33.099 1.00 13.69 ? 84  LYS A O     1 
ATOM   676  C  CB    . LYS A 1 92  ? 15.942 -14.272 35.335 1.00 15.87 ? 84  LYS A CB    1 
ATOM   677  C  CG    . LYS A 1 92  ? 15.811 -13.914 36.820 1.00 20.67 ? 84  LYS A CG    1 
ATOM   678  C  CD    . LYS A 1 92  ? 16.947 -14.445 37.695 1.00 26.23 ? 84  LYS A CD    1 
ATOM   679  C  CE    . LYS A 1 92  ? 16.899 -15.961 37.874 1.00 30.26 ? 84  LYS A CE    1 
ATOM   680  N  NZ    . LYS A 1 92  ? 18.241 -16.565 38.147 1.00 32.73 ? 84  LYS A NZ    1 
ATOM   681  N  N     . THR A 1 93  ? 17.084 -13.610 32.311 1.00 12.30 ? 85  THR A N     1 
ATOM   682  C  CA    . THR A 1 93  ? 16.984 -14.046 30.924 1.00 12.34 ? 85  THR A CA    1 
ATOM   683  C  C     . THR A 1 93  ? 17.524 -12.944 30.030 1.00 12.39 ? 85  THR A C     1 
ATOM   684  O  O     . THR A 1 93  ? 17.082 -11.797 30.138 1.00 12.96 ? 85  THR A O     1 
ATOM   685  C  CB    . THR A 1 93  ? 15.523 -14.320 30.524 1.00 13.67 ? 85  THR A CB    1 
ATOM   686  O  OG1   . THR A 1 93  ? 14.916 -15.243 31.437 1.00 14.93 ? 85  THR A OG1   1 
ATOM   687  C  CG2   . THR A 1 93  ? 15.459 -14.898 29.111 1.00 15.29 ? 85  THR A CG2   1 
ATOM   688  N  N     . ILE A 1 94  ? 18.471 -13.286 29.160 1.00 12.18 ? 86  ILE A N     1 
ATOM   689  C  CA    . ILE A 1 94  ? 18.948 -12.385 28.119 1.00 12.22 ? 86  ILE A CA    1 
ATOM   690  C  C     . ILE A 1 94  ? 18.723 -13.031 26.764 1.00 11.83 ? 86  ILE A C     1 
ATOM   691  O  O     . ILE A 1 94  ? 19.142 -14.168 26.536 1.00 12.64 ? 86  ILE A O     1 
ATOM   692  C  CB    . ILE A 1 94  ? 20.437 -12.035 28.292 1.00 12.41 ? 86  ILE A CB    1 
ATOM   693  C  CG1   . ILE A 1 94  ? 20.672 -11.352 29.636 1.00 12.94 ? 86  ILE A CG1   1 
ATOM   694  C  CG2   . ILE A 1 94  ? 20.921 -11.179 27.120 1.00 13.27 ? 86  ILE A CG2   1 
ATOM   695  C  CD1   . ILE A 1 94  ? 22.113 -10.971 29.901 1.00 13.85 ? 86  ILE A CD1   1 
ATOM   696  N  N     . ILE A 1 95  ? 18.071 -12.307 25.862 1.00 11.94 ? 87  ILE A N     1 
ATOM   697  C  CA    . ILE A 1 95  ? 17.979 -12.703 24.466 1.00 11.74 ? 87  ILE A CA    1 
ATOM   698  C  C     . ILE A 1 95  ? 18.807 -11.734 23.651 1.00 11.61 ? 87  ILE A C     1 
ATOM   699  O  O     . ILE A 1 95  ? 18.540 -10.528 23.643 1.00 11.50 ? 87  ILE A O     1 
ATOM   700  C  CB    . ILE A 1 95  ? 16.536 -12.770 23.948 1.00 12.74 ? 87  ILE A CB    1 
ATOM   701  C  CG1   . ILE A 1 95  ? 15.681 -13.660 24.848 1.00 14.23 ? 87  ILE A CG1   1 
ATOM   702  C  CG2   . ILE A 1 95  ? 16.547 -13.277 22.504 1.00 14.19 ? 87  ILE A CG2   1 
ATOM   703  C  CD1   . ILE A 1 95  ? 14.198 -13.682 24.456 1.00 14.97 ? 87  ILE A CD1   1 
ATOM   704  N  N     . ARG A 1 96  ? 19.825 -12.253 22.990 1.00 11.80 ? 88  ARG A N     1 
ATOM   705  C  CA    . ARG A 1 96  ? 20.591 -11.476 22.041 1.00 11.88 ? 88  ARG A CA    1 
ATOM   706  C  C     . ARG A 1 96  ? 19.802 -11.377 20.744 1.00 12.00 ? 88  ARG A C     1 
ATOM   707  O  O     . ARG A 1 96  ? 19.296 -12.376 20.231 1.00 12.64 ? 88  ARG A O     1 
ATOM   708  C  CB    . ARG A 1 96  ? 21.954 -12.122 21.807 1.00 13.52 ? 88  ARG A CB    1 
ATOM   709  C  CG    . ARG A 1 96  ? 22.928 -11.126 21.324 1.00 16.15 ? 88  ARG A CG    1 
ATOM   710  C  CD    . ARG A 1 96  ? 24.271 -11.699 21.019 1.00 16.28 ? 88  ARG A CD    1 
ATOM   711  N  NE    . ARG A 1 96  ? 24.346 -12.165 19.647 1.00 17.64 ? 88  ARG A NE    1 
ATOM   712  C  CZ    . ARG A 1 96  ? 24.365 -11.387 18.577 1.00 20.32 ? 88  ARG A CZ    1 
ATOM   713  N  NH1   . ARG A 1 96  ? 24.287 -10.068 18.677 1.00 17.95 ? 88  ARG A NH1   1 
ATOM   714  N  NH2   . ARG A 1 96  ? 24.451 -11.945 17.377 1.00 24.00 ? 88  ARG A NH2   1 
ATOM   715  N  N     . VAL A 1 97  ? 19.704 -10.163 20.230 1.00 12.54 ? 89  VAL A N     1 
ATOM   716  C  CA    A VAL A 1 97  ? 19.000 -9.888  18.990 0.62 13.66 ? 89  VAL A CA    1 
ATOM   717  C  CA    B VAL A 1 97  ? 18.973 -9.831  19.013 0.38 14.46 ? 89  VAL A CA    1 
ATOM   718  C  C     . VAL A 1 97  ? 19.986 -9.196  18.067 1.00 15.12 ? 89  VAL A C     1 
ATOM   719  O  O     . VAL A 1 97  ? 20.643 -8.223  18.443 1.00 17.41 ? 89  VAL A O     1 
ATOM   720  C  CB    A VAL A 1 97  ? 17.719 -9.066  19.223 0.62 13.84 ? 89  VAL A CB    1 
ATOM   721  C  CB    B VAL A 1 97  ? 17.843 -8.845  19.358 0.38 16.14 ? 89  VAL A CB    1 
ATOM   722  C  CG1   A VAL A 1 97  ? 16.806 -9.819  20.176 0.62 14.21 ? 89  VAL A CG1   1 
ATOM   723  C  CG1   B VAL A 1 97  ? 17.359 -8.093  18.148 0.38 17.89 ? 89  VAL A CG1   1 
ATOM   724  C  CG2   A VAL A 1 97  ? 18.030 -7.704  19.782 0.62 14.56 ? 89  VAL A CG2   1 
ATOM   725  C  CG2   B VAL A 1 97  ? 16.702 -9.576  20.055 0.38 16.81 ? 89  VAL A CG2   1 
ATOM   726  N  N     . GLY A 1 98  ? 20.132 -9.725  16.865 1.00 16.14 ? 90  GLY A N     1 
ATOM   727  C  CA    . GLY A 1 98  ? 21.184 -9.159  16.055 1.00 17.98 ? 90  GLY A CA    1 
ATOM   728  C  C     . GLY A 1 98  ? 21.071 -9.520  14.600 1.00 17.02 ? 90  GLY A C     1 
ATOM   729  O  O     . GLY A 1 98  ? 20.040 -10.002 14.138 1.00 15.84 ? 90  GLY A O     1 
ATOM   730  N  N     . THR A 1 99  ? 22.153 -9.247  13.884 1.00 17.05 ? 91  THR A N     1 
ATOM   731  C  CA    . THR A 1 99  ? 22.296 -9.586  12.482 1.00 16.07 ? 91  THR A CA    1 
ATOM   732  C  C     . THR A 1 99  ? 23.426 -10.598 12.337 1.00 14.69 ? 91  THR A C     1 
ATOM   733  O  O     . THR A 1 99  ? 24.252 -10.788 13.241 1.00 14.87 ? 91  THR A O     1 
ATOM   734  C  CB    . THR A 1 99  ? 22.612 -8.340  11.665 1.00 17.22 ? 91  THR A CB    1 
ATOM   735  O  OG1   . THR A 1 99  ? 23.913 -7.862  12.044 1.00 17.15 ? 91  THR A OG1   1 
ATOM   736  C  CG2   . THR A 1 99  ? 21.550 -7.262  11.899 1.00 19.24 ? 91  THR A CG2   1 
ATOM   737  N  N     . CYS A 1 100 ? 23.464 -11.247 11.181 1.00 13.97 ? 92  CYS A N     1 
ATOM   738  C  CA    . CYS A 1 100 ? 24.483 -12.258 10.944 1.00 12.62 ? 92  CYS A CA    1 
ATOM   739  C  C     . CYS A 1 100 ? 24.724 -12.396 9.451  1.00 12.38 ? 92  CYS A C     1 
ATOM   740  O  O     . CYS A 1 100 ? 23.917 -11.972 8.630  1.00 14.13 ? 92  CYS A O     1 
ATOM   741  C  CB    . CYS A 1 100 ? 24.063 -13.613 11.530 1.00 12.46 ? 92  CYS A CB    1 
ATOM   742  S  SG    . CYS A 1 100 ? 22.584 -14.339 10.783 1.00 14.07 ? 92  CYS A SG    1 
ATOM   743  N  N     . GLY A 1 101 ? 25.834 -13.054 9.111  1.00 11.80 ? 93  GLY A N     1 
ATOM   744  C  CA    . GLY A 1 101 ? 26.042 -13.570 7.777  1.00 12.51 ? 93  GLY A CA    1 
ATOM   745  C  C     . GLY A 1 101 ? 25.653 -15.039 7.745  1.00 12.77 ? 93  GLY A C     1 
ATOM   746  O  O     . GLY A 1 101 ? 25.372 -15.640 8.768  1.00 12.93 ? 93  GLY A O     1 
ATOM   747  N  N     . THR A 1 102 ? 25.619 -15.610 6.548  1.00 13.56 ? 94  THR A N     1 
ATOM   748  C  CA    . THR A 1 102 ? 25.441 -17.051 6.429  1.00 14.37 ? 94  THR A CA    1 
ATOM   749  C  C     . THR A 1 102 ? 26.307 -17.584 5.300  1.00 15.13 ? 94  THR A C     1 
ATOM   750  O  O     . THR A 1 102 ? 26.586 -16.881 4.327  1.00 15.52 ? 94  THR A O     1 
ATOM   751  C  CB    . THR A 1 102 ? 23.968 -17.447 6.195  1.00 14.15 ? 94  THR A CB    1 
ATOM   752  O  OG1   . THR A 1 102 ? 23.833 -18.864 6.360  1.00 14.61 ? 94  THR A OG1   1 
ATOM   753  C  CG2   . THR A 1 102 ? 23.513 -17.085 4.805  1.00 14.63 ? 94  THR A CG2   1 
ATOM   754  N  N     . VAL A 1 103 ? 26.723 -18.842 5.444  1.00 15.46 ? 95  VAL A N     1 
ATOM   755  C  CA    . VAL A 1 103 ? 27.339 -19.601 4.359  1.00 16.96 ? 95  VAL A CA    1 
ATOM   756  C  C     . VAL A 1 103 ? 26.498 -20.789 3.931  1.00 17.98 ? 95  VAL A C     1 
ATOM   757  O  O     . VAL A 1 103 ? 26.874 -21.481 2.969  1.00 19.61 ? 95  VAL A O     1 
ATOM   758  C  CB    . VAL A 1 103 ? 28.757 -20.093 4.724  1.00 17.36 ? 95  VAL A CB    1 
ATOM   759  C  CG1   . VAL A 1 103 ? 29.696 -18.946 5.029  1.00 17.41 ? 95  VAL A CG1   1 
ATOM   760  C  CG2   . VAL A 1 103 ? 28.687 -21.058 5.900  1.00 18.13 ? 95  VAL A CG2   1 
ATOM   761  N  N     . ASP A 1 104 ? 25.410 -21.079 4.622  1.00 18.42 ? 96  ASP A N     1 
ATOM   762  C  CA    . ASP A 1 104 ? 24.680 -22.308 4.348  1.00 19.87 ? 96  ASP A CA    1 
ATOM   763  C  C     . ASP A 1 104 ? 23.948 -22.171 3.020  1.00 21.67 ? 96  ASP A C     1 
ATOM   764  O  O     . ASP A 1 104 ? 23.326 -21.133 2.769  1.00 20.99 ? 96  ASP A O     1 
ATOM   765  C  CB    . ASP A 1 104 ? 23.698 -22.602 5.477  1.00 21.04 ? 96  ASP A CB    1 
ATOM   766  C  CG    . ASP A 1 104 ? 23.043 -23.963 5.336  1.00 22.04 ? 96  ASP A CG    1 
ATOM   767  O  OD1   . ASP A 1 104 ? 22.149 -24.096 4.479  1.00 23.66 ? 96  ASP A OD1   1 
ATOM   768  O  OD2   . ASP A 1 104 ? 23.450 -24.911 6.046  1.00 23.55 ? 96  ASP A OD2   1 
ATOM   769  N  N     . PRO A 1 105 ? 24.003 -23.179 2.142  1.00 23.95 ? 97  PRO A N     1 
ATOM   770  C  CA    . PRO A 1 105 ? 23.425 -23.009 0.801  1.00 25.41 ? 97  PRO A CA    1 
ATOM   771  C  C     . PRO A 1 105 ? 21.920 -22.853 0.800  1.00 26.01 ? 97  PRO A C     1 
ATOM   772  O  O     . PRO A 1 105 ? 21.370 -22.370 -0.197 1.00 27.67 ? 97  PRO A O     1 
ATOM   773  C  CB    . PRO A 1 105 ? 23.858 -24.284 0.063  1.00 26.35 ? 97  PRO A CB    1 
ATOM   774  C  CG    . PRO A 1 105 ? 24.079 -25.280 1.132  1.00 26.19 ? 97  PRO A CG    1 
ATOM   775  C  CD    . PRO A 1 105 ? 24.608 -24.510 2.312  1.00 25.31 ? 97  PRO A CD    1 
ATOM   776  N  N     . ASN A 1 106 ? 21.237 -23.226 1.880  1.00 24.71 ? 98  ASN A N     1 
ATOM   777  C  CA    . ASN A 1 106 ? 19.785 -23.138 1.949  1.00 25.19 ? 98  ASN A CA    1 
ATOM   778  C  C     . ASN A 1 106 ? 19.308 -22.092 2.940  1.00 23.75 ? 98  ASN A C     1 
ATOM   779  O  O     . ASN A 1 106 ? 18.122 -22.073 3.288  1.00 24.82 ? 98  ASN A O     1 
ATOM   780  C  CB    . ASN A 1 106 ? 19.183 -24.504 2.263  1.00 27.15 ? 98  ASN A CB    1 
ATOM   781  C  CG    . ASN A 1 106 ? 19.418 -25.493 1.149  1.00 29.72 ? 98  ASN A CG    1 
ATOM   782  O  OD1   . ASN A 1 106 ? 20.188 -26.440 1.294  1.00 31.09 ? 98  ASN A OD1   1 
ATOM   783  N  ND2   . ASN A 1 106 ? 18.775 -25.257 0.013  1.00 30.95 ? 98  ASN A ND2   1 
ATOM   784  N  N     . VAL A 1 107 ? 20.193 -21.208 3.383  1.00 21.99 ? 99  VAL A N     1 
ATOM   785  C  CA    . VAL A 1 107 ? 19.812 -20.042 4.167  1.00 20.82 ? 99  VAL A CA    1 
ATOM   786  C  C     . VAL A 1 107 ? 19.983 -18.815 3.286  1.00 20.68 ? 99  VAL A C     1 
ATOM   787  O  O     . VAL A 1 107 ? 20.926 -18.734 2.492  1.00 20.49 ? 99  VAL A O     1 
ATOM   788  C  CB    . VAL A 1 107 ? 20.636 -19.926 5.462  1.00 20.51 ? 99  VAL A CB    1 
ATOM   789  C  CG1   . VAL A 1 107 ? 20.286 -18.640 6.201  1.00 20.45 ? 99  VAL A CG1   1 
ATOM   790  C  CG2   . VAL A 1 107 ? 20.379 -21.136 6.340  1.00 20.43 ? 99  VAL A CG2   1 
ATOM   791  N  N     . HIS A 1 108 ? 19.058 -17.868 3.412  1.00 21.02 ? 100 HIS A N     1 
ATOM   792  C  CA    . HIS A 1 108 ? 18.974 -16.745 2.495  1.00 21.88 ? 100 HIS A CA    1 
ATOM   793  C  C     . HIS A 1 108 ? 18.959 -15.433 3.255  1.00 20.92 ? 100 HIS A C     1 
ATOM   794  O  O     . HIS A 1 108 ? 18.558 -15.364 4.420  1.00 20.49 ? 100 HIS A O     1 
ATOM   795  C  CB    . HIS A 1 108 ? 17.725 -16.855 1.630  1.00 24.79 ? 100 HIS A CB    1 
ATOM   796  C  CG    . HIS A 1 108 ? 17.688 -18.098 0.809  1.00 27.77 ? 100 HIS A CG    1 
ATOM   797  N  ND1   . HIS A 1 108 ? 18.347 -18.212 -0.396 1.00 29.51 ? 100 HIS A ND1   1 
ATOM   798  C  CD2   . HIS A 1 108 ? 17.097 -19.294 1.031  1.00 29.02 ? 100 HIS A CD2   1 
ATOM   799  C  CE1   . HIS A 1 108 ? 18.152 -19.423 -0.887 1.00 29.85 ? 100 HIS A CE1   1 
ATOM   800  N  NE2   . HIS A 1 108 ? 17.399 -20.099 -0.039 1.00 29.97 ? 100 HIS A NE2   1 
ATOM   801  N  N     . VAL A 1 109 ? 19.424 -14.388 2.575  1.00 21.15 ? 101 VAL A N     1 
ATOM   802  C  CA    . VAL A 1 109 ? 19.321 -13.048 3.124  1.00 20.77 ? 101 VAL A CA    1 
ATOM   803  C  C     . VAL A 1 109 ? 17.868 -12.789 3.509  1.00 21.06 ? 101 VAL A C     1 
ATOM   804  O  O     . VAL A 1 109 ? 16.934 -13.175 2.797  1.00 21.65 ? 101 VAL A O     1 
ATOM   805  C  CB    . VAL A 1 109 ? 19.862 -12.040 2.095  1.00 22.43 ? 101 VAL A CB    1 
ATOM   806  C  CG1   . VAL A 1 109 ? 19.540 -10.637 2.498  1.00 25.09 ? 101 VAL A CG1   1 
ATOM   807  C  CG2   . VAL A 1 109 ? 21.373 -12.215 1.926  1.00 23.02 ? 101 VAL A CG2   1 
ATOM   808  N  N     . ARG A 1 110 ? 17.681 -12.145 4.661  1.00 20.93 ? 102 ARG A N     1 
ATOM   809  C  CA    . ARG A 1 110 ? 16.414 -11.791 5.296  1.00 21.66 ? 102 ARG A CA    1 
ATOM   810  C  C     . ARG A 1 110 ? 15.849 -12.920 6.151  1.00 21.13 ? 102 ARG A C     1 
ATOM   811  O  O     . ARG A 1 110 ? 14.874 -12.699 6.865  1.00 22.65 ? 102 ARG A O     1 
ATOM   812  C  CB    . ARG A 1 110 ? 15.334 -11.302 4.311  1.00 22.79 ? 102 ARG A CB    1 
ATOM   813  C  CG    . ARG A 1 110 ? 15.801 -10.127 3.455  1.00 25.44 ? 102 ARG A CG    1 
ATOM   814  C  CD    . ARG A 1 110 ? 14.749 -9.668  2.455  1.00 30.08 ? 102 ARG A CD    1 
ATOM   815  N  NE    . ARG A 1 110 ? 14.294 -10.749 1.590  1.00 34.15 ? 102 ARG A NE    1 
ATOM   816  C  CZ    . ARG A 1 110 ? 13.095 -11.318 1.652  1.00 37.57 ? 102 ARG A CZ    1 
ATOM   817  N  NH1   . ARG A 1 110 ? 12.189 -10.939 2.540  1.00 39.19 ? 102 ARG A NH1   1 
ATOM   818  N  NH2   . ARG A 1 110 ? 12.796 -12.290 0.795  1.00 38.68 ? 102 ARG A NH2   1 
ATOM   819  N  N     . ASP A 1 111 ? 16.428 -14.116 6.106  1.00 19.51 ? 103 ASP A N     1 
ATOM   820  C  CA    . ASP A 1 111 ? 15.950 -15.189 6.960  1.00 18.51 ? 103 ASP A CA    1 
ATOM   821  C  C     . ASP A 1 111 ? 16.180 -14.839 8.424  1.00 16.74 ? 103 ASP A C     1 
ATOM   822  O  O     . ASP A 1 111 ? 17.126 -14.131 8.780  1.00 17.59 ? 103 ASP A O     1 
ATOM   823  C  CB    . ASP A 1 111 ? 16.691 -16.486 6.654  1.00 19.54 ? 103 ASP A CB    1 
ATOM   824  C  CG    . ASP A 1 111 ? 16.170 -17.198 5.417  1.00 21.55 ? 103 ASP A CG    1 
ATOM   825  O  OD1   . ASP A 1 111 ? 15.200 -16.724 4.793  1.00 22.85 ? 103 ASP A OD1   1 
ATOM   826  O  OD2   . ASP A 1 111 ? 16.733 -18.268 5.094  1.00 22.40 ? 103 ASP A OD2   1 
ATOM   827  N  N     . VAL A 1 112 ? 15.321 -15.377 9.276  1.00 16.50 ? 104 VAL A N     1 
ATOM   828  C  CA    . VAL A 1 112 ? 15.425 -15.231 10.721 1.00 15.90 ? 104 VAL A CA    1 
ATOM   829  C  C     . VAL A 1 112 ? 15.969 -16.543 11.274 1.00 14.99 ? 104 VAL A C     1 
ATOM   830  O  O     . VAL A 1 112 ? 15.399 -17.612 11.029 1.00 16.07 ? 104 VAL A O     1 
ATOM   831  C  CB    . VAL A 1 112 ? 14.050 -14.904 11.334 1.00 17.91 ? 104 VAL A CB    1 
ATOM   832  C  CG1   . VAL A 1 112 ? 14.140 -14.815 12.850 1.00 19.01 ? 104 VAL A CG1   1 
ATOM   833  C  CG2   . VAL A 1 112 ? 13.491 -13.613 10.745 1.00 19.54 ? 104 VAL A CG2   1 
ATOM   834  N  N     . CYS A 1 113 ? 17.059 -16.463 12.027 1.00 13.70 ? 105 CYS A N     1 
ATOM   835  C  CA    . CYS A 1 113 ? 17.743 -17.631 12.563 1.00 12.71 ? 105 CYS A CA    1 
ATOM   836  C  C     . CYS A 1 113 ? 17.606 -17.635 14.079 1.00 12.07 ? 105 CYS A C     1 
ATOM   837  O  O     . CYS A 1 113 ? 17.947 -16.653 14.744 1.00 13.52 ? 105 CYS A O     1 
ATOM   838  C  CB    . CYS A 1 113 ? 19.230 -17.608 12.184 1.00 13.31 ? 105 CYS A CB    1 
ATOM   839  S  SG    . CYS A 1 113 ? 19.544 -17.675 10.425 1.00 16.14 ? 105 CYS A SG    1 
ATOM   840  N  N     . ILE A 1 114 ? 17.126 -18.745 14.618 1.00 11.40 ? 106 ILE A N     1 
ATOM   841  C  CA    . ILE A 1 114 ? 17.039 -18.959 16.056 1.00 10.88 ? 106 ILE A CA    1 
ATOM   842  C  C     . ILE A 1 114 ? 18.159 -19.924 16.417 1.00 11.25 ? 106 ILE A C     1 
ATOM   843  O  O     . ILE A 1 114 ? 18.236 -21.025 15.868 1.00 11.94 ? 106 ILE A O     1 
ATOM   844  C  CB    . ILE A 1 114 ? 15.656 -19.494 16.462 1.00 11.58 ? 106 ILE A CB    1 
ATOM   845  C  CG1   . ILE A 1 114 ? 14.584 -18.429 16.191 1.00 12.62 ? 106 ILE A CG1   1 
ATOM   846  C  CG2   . ILE A 1 114 ? 15.647 -19.885 17.925 1.00 12.12 ? 106 ILE A CG2   1 
ATOM   847  C  CD1   . ILE A 1 114 ? 13.167 -18.928 16.303 1.00 13.47 ? 106 ILE A CD1   1 
ATOM   848  N  N     . VAL A 1 115 ? 19.035 -19.494 17.317 1.00 11.23 ? 107 VAL A N     1 
ATOM   849  C  CA    . VAL A 1 115 ? 20.295 -20.164 17.591 1.00 11.36 ? 107 VAL A CA    1 
ATOM   850  C  C     . VAL A 1 115 ? 20.116 -21.197 18.702 1.00 11.50 ? 107 VAL A C     1 
ATOM   851  O  O     . VAL A 1 115 ? 19.748 -20.863 19.834 1.00 13.24 ? 107 VAL A O     1 
ATOM   852  C  CB    . VAL A 1 115 ? 21.350 -19.117 17.975 1.00 12.37 ? 107 VAL A CB    1 
ATOM   853  C  CG1   . VAL A 1 115 ? 22.657 -19.776 18.348 1.00 12.93 ? 107 VAL A CG1   1 
ATOM   854  C  CG2   . VAL A 1 115 ? 21.553 -18.135 16.837 1.00 12.65 ? 107 VAL A CG2   1 
ATOM   855  N  N     . THR A 1 116 ? 20.463 -22.448 18.410 1.00 11.39 ? 108 THR A N     1 
ATOM   856  C  CA    . THR A 1 116 ? 20.435 -23.487 19.439 1.00 11.95 ? 108 THR A CA    1 
ATOM   857  C  C     . THR A 1 116 ? 21.757 -23.606 20.199 1.00 10.70 ? 108 THR A C     1 
ATOM   858  O  O     . THR A 1 116 ? 21.753 -23.922 21.388 1.00 10.82 ? 108 THR A O     1 
ATOM   859  C  CB    . THR A 1 116 ? 20.115 -24.831 18.792 1.00 13.26 ? 108 THR A CB    1 
ATOM   860  O  OG1   . THR A 1 116 ? 21.023 -25.036 17.707 1.00 14.01 ? 108 THR A OG1   1 
ATOM   861  C  CG2   . THR A 1 116 ? 18.653 -24.872 18.294 1.00 15.74 ? 108 THR A CG2   1 
ATOM   862  N  N     . ALA A 1 117 ? 22.875 -23.319 19.543 1.00 10.96 ? 109 ALA A N     1 
ATOM   863  C  CA    . ALA A 1 117 ? 24.211 -23.351 20.133 1.00 10.33 ? 109 ALA A CA    1 
ATOM   864  C  C     . ALA A 1 117 ? 25.112 -22.583 19.180 1.00 9.79  ? 109 ALA A C     1 
ATOM   865  O  O     . ALA A 1 117 ? 24.782 -22.421 18.007 1.00 10.60 ? 109 ALA A O     1 
ATOM   866  C  CB    . ALA A 1 117 ? 24.732 -24.785 20.300 1.00 11.02 ? 109 ALA A CB    1 
ATOM   867  N  N     . SER A 1 118 ? 26.279 -22.157 19.662 1.00 10.62 ? 110 SER A N     1 
ATOM   868  C  CA    A SER A 1 118 ? 27.184 -21.365 18.836 0.65 10.72 ? 110 SER A CA    1 
ATOM   869  C  CA    B SER A 1 118 ? 27.190 -21.358 18.852 0.35 10.27 ? 110 SER A CA    1 
ATOM   870  C  C     . SER A 1 118 ? 28.612 -21.851 19.014 1.00 10.32 ? 110 SER A C     1 
ATOM   871  O  O     . SER A 1 118 ? 29.108 -21.932 20.139 1.00 12.09 ? 110 SER A O     1 
ATOM   872  C  CB    A SER A 1 118 ? 27.094 -19.867 19.154 0.65 11.93 ? 110 SER A CB    1 
ATOM   873  C  CB    B SER A 1 118 ? 27.138 -19.900 19.283 0.35 10.37 ? 110 SER A CB    1 
ATOM   874  O  OG    A SER A 1 118 ? 27.698 -19.102 18.117 0.65 12.14 ? 110 SER A OG    1 
ATOM   875  O  OG    B SER A 1 118 ? 25.802 -19.478 19.272 0.35 10.14 ? 110 SER A OG    1 
ATOM   876  N  N     . GLY A 1 119 ? 29.271 -22.144 17.891 1.00 9.88  ? 111 GLY A N     1 
ATOM   877  C  CA    . GLY A 1 119 ? 30.686 -22.449 17.893 1.00 9.92  ? 111 GLY A CA    1 
ATOM   878  C  C     . GLY A 1 119 ? 31.495 -21.173 18.012 1.00 9.93  ? 111 GLY A C     1 
ATOM   879  O  O     . GLY A 1 119 ? 30.951 -20.067 18.015 1.00 10.35 ? 111 GLY A O     1 
ATOM   880  N  N     . THR A 1 120 ? 32.812 -21.328 18.111 1.00 9.31  ? 112 THR A N     1 
ATOM   881  C  CA    . THR A 1 120 ? 33.650 -20.144 18.229 1.00 9.73  ? 112 THR A CA    1 
ATOM   882  C  C     . THR A 1 120 ? 35.104 -20.491 17.947 1.00 9.56  ? 112 THR A C     1 
ATOM   883  O  O     . THR A 1 120 ? 35.537 -21.639 18.093 1.00 10.05 ? 112 THR A O     1 
ATOM   884  C  CB    . THR A 1 120 ? 33.499 -19.489 19.612 1.00 10.82 ? 112 THR A CB    1 
ATOM   885  O  OG1   . THR A 1 120 ? 34.209 -18.246 19.628 1.00 10.66 ? 112 THR A OG1   1 
ATOM   886  C  CG2   . THR A 1 120 ? 34.028 -20.353 20.729 1.00 11.04 ? 112 THR A CG2   1 
ATOM   887  N  N     . ASP A 1 121 ? 35.859 -19.455 17.575 1.00 10.30 ? 113 ASP A N     1 
ATOM   888  C  CA    . ASP A 1 121 ? 37.313 -19.493 17.526 1.00 10.73 ? 113 ASP A CA    1 
ATOM   889  C  C     . ASP A 1 121 ? 37.960 -18.814 18.731 1.00 10.75 ? 113 ASP A C     1 
ATOM   890  O  O     . ASP A 1 121 ? 39.191 -18.689 18.783 1.00 11.13 ? 113 ASP A O     1 
ATOM   891  C  CB    . ASP A 1 121 ? 37.823 -18.924 16.198 1.00 10.67 ? 113 ASP A CB    1 
ATOM   892  C  CG    . ASP A 1 121 ? 37.316 -17.530 15.908 1.00 11.04 ? 113 ASP A CG    1 
ATOM   893  O  OD1   . ASP A 1 121 ? 36.819 -16.861 16.833 1.00 10.76 ? 113 ASP A OD1   1 
ATOM   894  O  OD2   . ASP A 1 121 ? 37.424 -17.098 14.737 1.00 11.36 ? 113 ASP A OD2   1 
ATOM   895  N  N     . SER A 1 122 ? 37.164 -18.400 19.710 1.00 10.75 ? 114 SER A N     1 
ATOM   896  C  CA    . SER A 1 122 ? 37.647 -17.847 20.963 1.00 10.79 ? 114 SER A CA    1 
ATOM   897  C  C     . SER A 1 122 ? 38.111 -18.952 21.909 1.00 10.76 ? 114 SER A C     1 
ATOM   898  O  O     . SER A 1 122 ? 37.656 -20.091 21.833 1.00 11.64 ? 114 SER A O     1 
ATOM   899  C  CB    . SER A 1 122 ? 36.524 -17.047 21.629 1.00 10.63 ? 114 SER A CB    1 
ATOM   900  O  OG    . SER A 1 122 ? 36.873 -16.601 22.933 1.00 10.71 ? 114 SER A OG    1 
ATOM   901  N  N     . ASN A 1 123 ? 39.004 -18.600 22.833 1.00 10.92 ? 115 ASN A N     1 
ATOM   902  C  CA    . ASN A 1 123 ? 39.413 -19.525 23.887 1.00 11.99 ? 115 ASN A CA    1 
ATOM   903  C  C     . ASN A 1 123 ? 38.595 -19.426 25.163 1.00 11.49 ? 115 ASN A C     1 
ATOM   904  O  O     . ASN A 1 123 ? 38.884 -20.157 26.120 1.00 11.84 ? 115 ASN A O     1 
ATOM   905  C  CB    . ASN A 1 123 ? 40.880 -19.307 24.275 1.00 13.71 ? 115 ASN A CB    1 
ATOM   906  C  CG    . ASN A 1 123 ? 41.805 -19.920 23.336 1.00 17.16 ? 115 ASN A CG    1 
ATOM   907  O  OD1   . ASN A 1 123 ? 41.585 -21.060 22.886 1.00 18.00 ? 115 ASN A OD1   1 
ATOM   908  N  ND2   . ASN A 1 123 ? 42.898 -19.201 23.037 1.00 17.58 ? 115 ASN A ND2   1 
ATOM   909  N  N     . VAL A 1 124 ? 37.578 -18.564 25.218 1.00 10.32 ? 116 VAL A N     1 
ATOM   910  C  CA    . VAL A 1 124 ? 37.001 -18.277 26.527 1.00 10.67 ? 116 VAL A CA    1 
ATOM   911  C  C     . VAL A 1 124 ? 36.297 -19.481 27.133 1.00 10.15 ? 116 VAL A C     1 
ATOM   912  O  O     . VAL A 1 124 ? 36.194 -19.583 28.365 1.00 11.16 ? 116 VAL A O     1 
ATOM   913  C  CB    . VAL A 1 124 ? 36.067 -17.053 26.502 1.00 10.80 ? 116 VAL A CB    1 
ATOM   914  C  CG1   . VAL A 1 124 ? 36.814 -15.782 26.145 1.00 11.04 ? 116 VAL A CG1   1 
ATOM   915  C  CG2   . VAL A 1 124 ? 34.862 -17.257 25.562 1.00 11.74 ? 116 VAL A CG2   1 
ATOM   916  N  N     . ASN A 1 125 ? 35.764 -20.386 26.314 1.00 10.03 ? 117 ASN A N     1 
ATOM   917  C  CA    . ASN A 1 125 ? 35.035 -21.527 26.848 1.00 10.25 ? 117 ASN A CA    1 
ATOM   918  C  C     . ASN A 1 125 ? 35.958 -22.686 27.177 1.00 10.15 ? 117 ASN A C     1 
ATOM   919  O  O     . ASN A 1 125 ? 35.719 -23.394 28.165 1.00 10.63 ? 117 ASN A O     1 
ATOM   920  C  CB    . ASN A 1 125 ? 33.899 -21.905 25.902 1.00 10.59 ? 117 ASN A CB    1 
ATOM   921  C  CG    . ASN A 1 125 ? 32.905 -20.788 25.777 1.00 10.54 ? 117 ASN A CG    1 
ATOM   922  O  OD1   . ASN A 1 125 ? 32.741 -20.010 26.712 1.00 11.09 ? 117 ASN A OD1   1 
ATOM   923  N  ND2   . ASN A 1 125 ? 32.263 -20.671 24.630 1.00 11.09 ? 117 ASN A ND2   1 
ATOM   924  N  N     . ARG A 1 126 ? 37.052 -22.848 26.431 1.00 9.86  ? 118 ARG A N     1 
ATOM   925  C  CA    . ARG A 1 126 ? 38.076 -23.798 26.851 1.00 10.15 ? 118 ARG A CA    1 
ATOM   926  C  C     . ARG A 1 126 ? 38.589 -23.433 28.232 1.00 10.68 ? 118 ARG A C     1 
ATOM   927  O  O     . ARG A 1 126 ? 38.851 -24.307 29.062 1.00 11.70 ? 118 ARG A O     1 
ATOM   928  C  CB    . ARG A 1 126 ? 39.202 -23.828 25.825 1.00 10.48 ? 118 ARG A CB    1 
ATOM   929  C  CG    . ARG A 1 126 ? 38.774 -24.400 24.496 1.00 10.89 ? 118 ARG A CG    1 
ATOM   930  C  CD    . ARG A 1 126 ? 39.860 -24.430 23.468 1.00 12.34 ? 118 ARG A CD    1 
ATOM   931  N  NE    . ARG A 1 126 ? 39.260 -24.808 22.201 1.00 13.47 ? 118 ARG A NE    1 
ATOM   932  C  CZ    . ARG A 1 126 ? 39.930 -25.115 21.107 1.00 15.80 ? 118 ARG A CZ    1 
ATOM   933  N  NH1   . ARG A 1 126 ? 41.254 -25.081 21.078 1.00 19.23 ? 118 ARG A NH1   1 
ATOM   934  N  NH2   . ARG A 1 126 ? 39.259 -25.486 20.024 1.00 15.14 ? 118 ARG A NH2   1 
ATOM   935  N  N     . MET A 1 127 ? 38.743 -22.135 28.498 1.00 10.80 ? 119 MET A N     1 
ATOM   936  C  CA    A MET A 1 127 ? 39.233 -21.719 29.803 0.50 11.26 ? 119 MET A CA    1 
ATOM   937  C  CA    B MET A 1 127 ? 39.218 -21.679 29.798 0.50 12.02 ? 119 MET A CA    1 
ATOM   938  C  C     . MET A 1 127 ? 38.283 -22.083 30.926 1.00 11.96 ? 119 MET A C     1 
ATOM   939  O  O     . MET A 1 127 ? 38.732 -22.241 32.068 1.00 13.06 ? 119 MET A O     1 
ATOM   940  C  CB    A MET A 1 127 ? 39.484 -20.220 29.799 0.50 12.37 ? 119 MET A CB    1 
ATOM   941  C  CB    B MET A 1 127 ? 39.363 -20.160 29.766 0.50 14.24 ? 119 MET A CB    1 
ATOM   942  C  CG    A MET A 1 127 ? 40.650 -19.838 28.919 0.50 14.08 ? 119 MET A CG    1 
ATOM   943  C  CG    B MET A 1 127 ? 40.542 -19.687 28.939 0.50 17.06 ? 119 MET A CG    1 
ATOM   944  S  SD    A MET A 1 127 ? 42.182 -20.714 29.307 0.50 16.76 ? 119 MET A SD    1 
ATOM   945  S  SD    B MET A 1 127 ? 40.568 -17.902 28.591 0.50 20.06 ? 119 MET A SD    1 
ATOM   946  C  CE    A MET A 1 127 ? 42.455 -20.244 31.007 0.50 18.42 ? 119 MET A CE    1 
ATOM   947  C  CE    B MET A 1 127 ? 39.961 -17.211 30.142 0.50 19.77 ? 119 MET A CE    1 
ATOM   948  N  N     . ARG A 1 128 ? 36.989 -22.250 30.630 1.00 11.21 ? 120 ARG A N     1 
ATOM   949  C  CA    . ARG A 1 128 ? 35.991 -22.567 31.637 1.00 11.40 ? 120 ARG A CA    1 
ATOM   950  C  C     . ARG A 1 128 ? 35.874 -24.059 31.908 1.00 11.62 ? 120 ARG A C     1 
ATOM   951  O  O     . ARG A 1 128 ? 35.316 -24.445 32.945 1.00 12.65 ? 120 ARG A O     1 
ATOM   952  C  CB    . ARG A 1 128 ? 34.621 -22.037 31.195 1.00 11.61 ? 120 ARG A CB    1 
ATOM   953  C  CG    . ARG A 1 128 ? 34.525 -20.540 31.133 1.00 12.18 ? 120 ARG A CG    1 
ATOM   954  C  CD    . ARG A 1 128 ? 33.196 -20.065 30.532 1.00 12.73 ? 120 ARG A CD    1 
ATOM   955  N  NE    . ARG A 1 128 ? 33.010 -18.635 30.793 1.00 13.85 ? 120 ARG A NE    1 
ATOM   956  C  CZ    . ARG A 1 128 ? 32.989 -17.649 29.903 1.00 12.21 ? 120 ARG A CZ    1 
ATOM   957  N  NH1   . ARG A 1 128 ? 33.023 -17.877 28.599 1.00 12.19 ? 120 ARG A NH1   1 
ATOM   958  N  NH2   . ARG A 1 128 ? 32.906 -16.388 30.335 1.00 12.30 ? 120 ARG A NH2   1 
ATOM   959  N  N     . LEU A 1 129 ? 36.364 -24.909 31.009 1.00 11.18 ? 121 LEU A N     1 
ATOM   960  C  CA    . LEU A 1 129 ? 36.159 -26.350 31.137 1.00 11.15 ? 121 LEU A CA    1 
ATOM   961  C  C     . LEU A 1 129 ? 37.454 -27.116 30.944 1.00 11.38 ? 121 LEU A C     1 
ATOM   962  O  O     . LEU A 1 129 ? 37.513 -28.099 30.208 1.00 11.52 ? 121 LEU A O     1 
ATOM   963  C  CB    . LEU A 1 129 ? 35.058 -26.830 30.192 1.00 11.95 ? 121 LEU A CB    1 
ATOM   964  C  CG    . LEU A 1 129 ? 34.478 -28.215 30.477 1.00 13.21 ? 121 LEU A CG    1 
ATOM   965  C  CD1   . LEU A 1 129 ? 33.955 -28.310 31.898 1.00 16.75 ? 121 LEU A CD1   1 
ATOM   966  C  CD2   . LEU A 1 129 ? 33.386 -28.562 29.484 1.00 13.32 ? 121 LEU A CD2   1 
ATOM   967  N  N     . LEU A 1 130 ? 38.512 -26.672 31.626 1.00 11.36 ? 122 LEU A N     1 
ATOM   968  C  CA    . LEU A 1 130 ? 39.764 -27.427 31.740 1.00 11.60 ? 122 LEU A CA    1 
ATOM   969  C  C     . LEU A 1 130 ? 40.381 -27.702 30.374 1.00 11.63 ? 122 LEU A C     1 
ATOM   970  O  O     . LEU A 1 130 ? 41.080 -28.696 30.183 1.00 12.27 ? 122 LEU A O     1 
ATOM   971  C  CB    . LEU A 1 130 ? 39.571 -28.728 32.529 1.00 13.15 ? 122 LEU A CB    1 
ATOM   972  C  CG    . LEU A 1 130 ? 39.290 -28.561 34.021 1.00 15.65 ? 122 LEU A CG    1 
ATOM   973  C  CD1   . LEU A 1 130 ? 37.895 -28.034 34.291 1.00 17.70 ? 122 LEU A CD1   1 
ATOM   974  C  CD2   . LEU A 1 130 ? 39.492 -29.877 34.767 1.00 18.37 ? 122 LEU A CD2   1 
ATOM   975  N  N     . GLY A 1 131 ? 40.140 -26.815 29.416 1.00 10.55 ? 123 GLY A N     1 
ATOM   976  C  CA    . GLY A 1 131 ? 40.699 -26.921 28.091 1.00 10.71 ? 123 GLY A CA    1 
ATOM   977  C  C     . GLY A 1 131 ? 39.898 -27.753 27.122 1.00 10.06 ? 123 GLY A C     1 
ATOM   978  O  O     . GLY A 1 131 ? 40.308 -27.883 25.960 1.00 11.24 ? 123 GLY A O     1 
ATOM   979  N  N     . HIS A 1 132 ? 38.758 -28.283 27.541 1.00 9.90  ? 124 HIS A N     1 
ATOM   980  C  CA    . HIS A 1 132 ? 37.947 -29.178 26.731 1.00 9.93  ? 124 HIS A CA    1 
ATOM   981  C  C     . HIS A 1 132 ? 36.929 -28.390 25.904 1.00 9.97  ? 124 HIS A C     1 
ATOM   982  O  O     . HIS A 1 132 ? 36.945 -27.153 25.870 1.00 10.81 ? 124 HIS A O     1 
ATOM   983  C  CB    . HIS A 1 132 ? 37.287 -30.211 27.634 1.00 10.19 ? 124 HIS A CB    1 
ATOM   984  C  CG    . HIS A 1 132 ? 38.255 -30.946 28.499 1.00 10.50 ? 124 HIS A CG    1 
ATOM   985  N  ND1   . HIS A 1 132 ? 39.369 -31.594 27.996 1.00 11.21 ? 124 HIS A ND1   1 
ATOM   986  C  CD2   . HIS A 1 132 ? 38.283 -31.142 29.838 1.00 10.46 ? 124 HIS A CD2   1 
ATOM   987  C  CE1   . HIS A 1 132 ? 40.034 -32.151 28.991 1.00 12.05 ? 124 HIS A CE1   1 
ATOM   988  N  NE2   . HIS A 1 132 ? 39.399 -31.887 30.118 1.00 11.56 ? 124 HIS A NE2   1 
ATOM   989  N  N     . ASP A 1 133 ? 36.059 -29.118 25.201 1.00 9.28  ? 125 ASP A N     1 
ATOM   990  C  CA    . ASP A 1 133 ? 34.994 -28.538 24.395 1.00 9.50  ? 125 ASP A CA    1 
ATOM   991  C  C     . ASP A 1 133 ? 33.763 -28.332 25.263 1.00 9.49  ? 125 ASP A C     1 
ATOM   992  O  O     . ASP A 1 133 ? 33.127 -29.302 25.712 1.00 9.77  ? 125 ASP A O     1 
ATOM   993  C  CB    . ASP A 1 133 ? 34.601 -29.410 23.206 1.00 10.16 ? 125 ASP A CB    1 
ATOM   994  C  CG    . ASP A 1 133 ? 35.601 -29.399 22.075 1.00 10.63 ? 125 ASP A CG    1 
ATOM   995  O  OD1   . ASP A 1 133 ? 36.699 -28.841 22.240 1.00 14.35 ? 125 ASP A OD1   1 
ATOM   996  O  OD2   . ASP A 1 133 ? 35.272 -29.936 20.992 1.00 9.75  ? 125 ASP A OD2   1 
ATOM   997  N  N     . PHE A 1 134 ? 33.409 -27.072 25.435 1.00 9.43  ? 126 PHE A N     1 
ATOM   998  C  CA    . PHE A 1 134 ? 32.250 -26.627 26.198 1.00 9.81  ? 126 PHE A CA    1 
ATOM   999  C  C     . PHE A 1 134 ? 31.293 -26.005 25.188 1.00 10.20 ? 126 PHE A C     1 
ATOM   1000 O  O     . PHE A 1 134 ? 31.571 -24.908 24.688 1.00 11.43 ? 126 PHE A O     1 
ATOM   1001 C  CB    . PHE A 1 134 ? 32.750 -25.579 27.198 1.00 10.29 ? 126 PHE A CB    1 
ATOM   1002 C  CG    . PHE A 1 134 ? 31.699 -24.955 28.111 1.00 11.11 ? 126 PHE A CG    1 
ATOM   1003 C  CD1   . PHE A 1 134 ? 30.339 -25.012 27.868 1.00 12.08 ? 126 PHE A CD1   1 
ATOM   1004 C  CD2   . PHE A 1 134 ? 32.132 -24.242 29.213 1.00 12.39 ? 126 PHE A CD2   1 
ATOM   1005 C  CE1   . PHE A 1 134 ? 29.434 -24.377 28.730 1.00 12.57 ? 126 PHE A CE1   1 
ATOM   1006 C  CE2   . PHE A 1 134 ? 31.248 -23.598 30.053 1.00 12.76 ? 126 PHE A CE2   1 
ATOM   1007 C  CZ    . PHE A 1 134 ? 29.892 -23.676 29.820 1.00 12.35 ? 126 PHE A CZ    1 
ATOM   1008 N  N     . PRO A 1 135 ? 30.172 -26.645 24.852 1.00 10.13 ? 127 PRO A N     1 
ATOM   1009 C  CA    . PRO A 1 135 ? 29.278 -26.068 23.844 1.00 10.85 ? 127 PRO A CA    1 
ATOM   1010 C  C     . PRO A 1 135 ? 28.528 -24.886 24.429 1.00 10.45 ? 127 PRO A C     1 
ATOM   1011 O  O     . PRO A 1 135 ? 27.898 -25.006 25.482 1.00 10.82 ? 127 PRO A O     1 
ATOM   1012 C  CB    . PRO A 1 135 ? 28.325 -27.224 23.522 1.00 11.50 ? 127 PRO A CB    1 
ATOM   1013 C  CG    . PRO A 1 135 ? 28.256 -28.005 24.787 1.00 10.31 ? 127 PRO A CG    1 
ATOM   1014 C  CD    . PRO A 1 135 ? 29.650 -27.909 25.388 1.00 10.65 ? 127 PRO A CD    1 
ATOM   1015 N  N     . ALA A 1 136 ? 28.625 -23.743 23.759 1.00 10.64 ? 128 ALA A N     1 
ATOM   1016 C  CA    . ALA A 1 136 ? 27.836 -22.584 24.124 1.00 10.12 ? 128 ALA A CA    1 
ATOM   1017 C  C     . ALA A 1 136 ? 26.415 -22.855 23.648 1.00 9.70  ? 128 ALA A C     1 
ATOM   1018 O  O     . ALA A 1 136 ? 26.140 -22.843 22.444 1.00 10.12 ? 128 ALA A O     1 
ATOM   1019 C  CB    . ALA A 1 136 ? 28.422 -21.334 23.473 1.00 10.80 ? 128 ALA A CB    1 
ATOM   1020 N  N     . THR A 1 137 ? 25.513 -23.139 24.579 1.00 10.30 ? 129 THR A N     1 
ATOM   1021 C  CA    . THR A 1 137 ? 24.221 -23.728 24.269 1.00 10.47 ? 129 THR A CA    1 
ATOM   1022 C  C     . THR A 1 137 ? 23.119 -22.812 24.784 1.00 10.18 ? 129 THR A C     1 
ATOM   1023 O  O     . THR A 1 137 ? 23.122 -22.422 25.960 1.00 10.82 ? 129 THR A O     1 
ATOM   1024 C  CB    . THR A 1 137 ? 24.115 -25.120 24.919 1.00 11.11 ? 129 THR A CB    1 
ATOM   1025 O  OG1   . THR A 1 137 ? 25.261 -25.906 24.587 1.00 11.47 ? 129 THR A OG1   1 
ATOM   1026 C  CG2   . THR A 1 137 ? 22.882 -25.834 24.432 1.00 11.65 ? 129 THR A CG2   1 
ATOM   1027 N  N     . ALA A 1 138 ? 22.158 -22.504 23.919 1.00 10.53 ? 130 ALA A N     1 
ATOM   1028 C  CA    . ALA A 1 138 ? 21.018 -21.706 24.332 1.00 11.25 ? 130 ALA A CA    1 
ATOM   1029 C  C     . ALA A 1 138 ? 20.124 -22.523 25.255 1.00 11.47 ? 130 ALA A C     1 
ATOM   1030 O  O     . ALA A 1 138 ? 20.030 -23.749 25.157 1.00 12.19 ? 130 ALA A O     1 
ATOM   1031 C  CB    . ALA A 1 138 ? 20.216 -21.248 23.111 1.00 11.38 ? 130 ALA A CB    1 
ATOM   1032 N  N     . ASN A 1 139 ? 19.429 -21.819 26.139 1.00 11.74 ? 131 ASN A N     1 
ATOM   1033 C  CA    . ASN A 1 139 ? 18.455 -22.452 27.008 1.00 12.37 ? 131 ASN A CA    1 
ATOM   1034 C  C     . ASN A 1 139 ? 17.244 -22.888 26.193 1.00 12.97 ? 131 ASN A C     1 
ATOM   1035 O  O     . ASN A 1 139 ? 16.731 -22.138 25.355 1.00 13.59 ? 131 ASN A O     1 
ATOM   1036 C  CB    . ASN A 1 139 ? 18.036 -21.450 28.083 1.00 13.49 ? 131 ASN A CB    1 
ATOM   1037 C  CG    . ASN A 1 139 ? 16.862 -21.933 28.902 1.00 14.64 ? 131 ASN A CG    1 
ATOM   1038 O  OD1   . ASN A 1 139 ? 15.697 -21.624 28.610 1.00 15.32 ? 131 ASN A OD1   1 
ATOM   1039 N  ND2   . ASN A 1 139 ? 17.162 -22.657 29.955 1.00 17.11 ? 131 ASN A ND2   1 
ATOM   1040 N  N     . PHE A 1 140 ? 16.767 -24.103 26.458 1.00 14.00 ? 132 PHE A N     1 
ATOM   1041 C  CA    . PHE A 1 140 ? 15.709 -24.665 25.629 1.00 14.41 ? 132 PHE A CA    1 
ATOM   1042 C  C     . PHE A 1 140 ? 14.408 -23.876 25.747 1.00 14.52 ? 132 PHE A C     1 
ATOM   1043 O  O     . PHE A 1 140 ? 13.703 -23.704 24.753 1.00 14.98 ? 132 PHE A O     1 
ATOM   1044 C  CB    . PHE A 1 140 ? 15.478 -26.132 25.980 1.00 15.85 ? 132 PHE A CB    1 
ATOM   1045 C  CG    . PHE A 1 140 ? 14.299 -26.727 25.272 1.00 17.70 ? 132 PHE A CG    1 
ATOM   1046 C  CD1   . PHE A 1 140 ? 14.386 -27.104 23.940 1.00 19.37 ? 132 PHE A CD1   1 
ATOM   1047 C  CD2   . PHE A 1 140 ? 13.076 -26.836 25.913 1.00 18.65 ? 132 PHE A CD2   1 
ATOM   1048 C  CE1   . PHE A 1 140 ? 13.289 -27.618 23.279 1.00 20.53 ? 132 PHE A CE1   1 
ATOM   1049 C  CE2   . PHE A 1 140 ? 11.979 -27.367 25.251 1.00 20.22 ? 132 PHE A CE2   1 
ATOM   1050 C  CZ    . PHE A 1 140 ? 12.094 -27.738 23.927 1.00 20.30 ? 132 PHE A CZ    1 
ATOM   1051 N  N     . GLU A 1 141 ? 14.050 -23.428 26.952 1.00 15.08 ? 133 GLU A N     1 
ATOM   1052 C  CA    . GLU A 1 141 ? 12.834 -22.632 27.105 1.00 15.95 ? 133 GLU A CA    1 
ATOM   1053 C  C     . GLU A 1 141 ? 12.905 -21.362 26.266 1.00 14.55 ? 133 GLU A C     1 
ATOM   1054 O  O     . GLU A 1 141 ? 11.895 -20.937 25.693 1.00 14.76 ? 133 GLU A O     1 
ATOM   1055 C  CB    . GLU A 1 141 ? 12.592 -22.288 28.577 1.00 19.41 ? 133 GLU A CB    1 
ATOM   1056 C  CG    . GLU A 1 141 ? 12.215 -23.477 29.460 1.00 24.21 ? 133 GLU A CG    1 
ATOM   1057 C  CD    . GLU A 1 141 ? 11.876 -23.070 30.886 1.00 30.01 ? 133 GLU A CD    1 
ATOM   1058 O  OE1   . GLU A 1 141 ? 12.704 -22.403 31.544 1.00 31.35 ? 133 GLU A OE1   1 
ATOM   1059 O  OE2   . GLU A 1 141 ? 10.772 -23.413 31.353 1.00 33.45 ? 133 GLU A OE2   1 
ATOM   1060 N  N     . VAL A 1 142 ? 14.080 -20.725 26.207 1.00 13.90 ? 134 VAL A N     1 
ATOM   1061 C  CA    . VAL A 1 142 ? 14.238 -19.526 25.381 1.00 13.08 ? 134 VAL A CA    1 
ATOM   1062 C  C     . VAL A 1 142 ? 14.102 -19.870 23.901 1.00 12.51 ? 134 VAL A C     1 
ATOM   1063 O  O     . VAL A 1 142 ? 13.381 -19.197 23.154 1.00 12.97 ? 134 VAL A O     1 
ATOM   1064 C  CB    . VAL A 1 142 ? 15.574 -18.818 25.676 1.00 13.02 ? 134 VAL A CB    1 
ATOM   1065 C  CG1   . VAL A 1 142 ? 15.750 -17.618 24.753 1.00 13.15 ? 134 VAL A CG1   1 
ATOM   1066 C  CG2   . VAL A 1 142 ? 15.648 -18.376 27.125 1.00 13.46 ? 134 VAL A CG2   1 
ATOM   1067 N  N     . VAL A 1 143 ? 14.788 -20.924 23.454 1.00 12.48 ? 135 VAL A N     1 
ATOM   1068 C  CA    . VAL A 1 143 ? 14.671 -21.333 22.058 1.00 12.85 ? 135 VAL A CA    1 
ATOM   1069 C  C     . VAL A 1 143 ? 13.212 -21.596 21.719 1.00 13.01 ? 135 VAL A C     1 
ATOM   1070 O  O     . VAL A 1 143 ? 12.693 -21.121 20.706 1.00 13.67 ? 135 VAL A O     1 
ATOM   1071 C  CB    . VAL A 1 143 ? 15.539 -22.569 21.775 1.00 12.84 ? 135 VAL A CB    1 
ATOM   1072 C  CG1   . VAL A 1 143 ? 15.336 -23.023 20.347 1.00 13.38 ? 135 VAL A CG1   1 
ATOM   1073 C  CG2   . VAL A 1 143 ? 17.009 -22.288 22.041 1.00 12.73 ? 135 VAL A CG2   1 
ATOM   1074 N  N     . SER A 1 144 ? 12.534 -22.365 22.572 1.00 13.74 ? 136 SER A N     1 
ATOM   1075 C  CA    . SER A 1 144 ? 11.147 -22.727 22.312 1.00 14.89 ? 136 SER A CA    1 
ATOM   1076 C  C     . SER A 1 144 ? 10.256 -21.499 22.288 1.00 14.47 ? 136 SER A C     1 
ATOM   1077 O  O     . SER A 1 144 ? 9.347  -21.403 21.458 1.00 14.74 ? 136 SER A O     1 
ATOM   1078 C  CB    . SER A 1 144 ? 10.658 -23.685 23.394 1.00 16.91 ? 136 SER A CB    1 
ATOM   1079 O  OG    . SER A 1 144 ? 9.307  -24.051 23.182 1.00 20.28 ? 136 SER A OG    1 
ATOM   1080 N  N     . ALA A 1 145 ? 10.489 -20.551 23.197 1.00 14.07 ? 137 ALA A N     1 
ATOM   1081 C  CA    . ALA A 1 145 ? 9.664  -19.345 23.206 1.00 14.02 ? 137 ALA A CA    1 
ATOM   1082 C  C     . ALA A 1 145 ? 9.823  -18.577 21.903 1.00 13.99 ? 137 ALA A C     1 
ATOM   1083 O  O     . ALA A 1 145 ? 8.846  -18.052 21.358 1.00 14.58 ? 137 ALA A O     1 
ATOM   1084 C  CB    . ALA A 1 145 ? 10.006 -18.477 24.415 1.00 14.97 ? 137 ALA A CB    1 
ATOM   1085 N  N     . LEU A 1 146 ? 11.053 -18.475 21.398 1.00 13.34 ? 138 LEU A N     1 
ATOM   1086 C  CA    . LEU A 1 146 ? 11.278 -17.815 20.118 1.00 13.21 ? 138 LEU A CA    1 
ATOM   1087 C  C     . LEU A 1 146 ? 10.605 -18.573 18.981 1.00 13.23 ? 138 LEU A C     1 
ATOM   1088 O  O     . LEU A 1 146 ? 9.940  -17.973 18.130 1.00 13.89 ? 138 LEU A O     1 
ATOM   1089 C  CB    . LEU A 1 146 ? 12.780 -17.685 19.875 1.00 13.24 ? 138 LEU A CB    1 
ATOM   1090 C  CG    . LEU A 1 146 ? 13.508 -16.735 20.838 1.00 12.84 ? 138 LEU A CG    1 
ATOM   1091 C  CD1   . LEU A 1 146 ? 15.018 -16.983 20.801 1.00 13.19 ? 138 LEU A CD1   1 
ATOM   1092 C  CD2   . LEU A 1 146 ? 13.234 -15.286 20.492 1.00 13.66 ? 138 LEU A CD2   1 
ATOM   1093 N  N     . VAL A 1 147 ? 10.760 -19.899 18.948 1.00 13.61 ? 139 VAL A N     1 
ATOM   1094 C  CA    . VAL A 1 147 ? 10.154 -20.695 17.879 1.00 14.14 ? 139 VAL A CA    1 
ATOM   1095 C  C     . VAL A 1 147 ? 8.636  -20.540 17.887 1.00 14.89 ? 139 VAL A C     1 
ATOM   1096 O  O     . VAL A 1 147 ? 8.006  -20.347 16.840 1.00 15.50 ? 139 VAL A O     1 
ATOM   1097 C  CB    . VAL A 1 147 ? 10.572 -22.169 18.017 1.00 14.68 ? 139 VAL A CB    1 
ATOM   1098 C  CG1   . VAL A 1 147 ? 9.722  -23.064 17.130 1.00 15.83 ? 139 VAL A CG1   1 
ATOM   1099 C  CG2   . VAL A 1 147 ? 12.046 -22.344 17.675 1.00 14.46 ? 139 VAL A CG2   1 
ATOM   1100 N  N     . GLU A 1 148 ? 8.026  -20.634 19.067 1.00 15.46 ? 140 GLU A N     1 
ATOM   1101 C  CA    . GLU A 1 148 ? 6.573  -20.583 19.153 1.00 16.58 ? 140 GLU A CA    1 
ATOM   1102 C  C     . GLU A 1 148 ? 6.049  -19.195 18.843 1.00 16.53 ? 140 GLU A C     1 
ATOM   1103 O  O     . GLU A 1 148 ? 4.976  -19.051 18.257 1.00 17.05 ? 140 GLU A O     1 
ATOM   1104 C  CB    . GLU A 1 148 ? 6.129  -21.021 20.542 1.00 18.99 ? 140 GLU A CB    1 
ATOM   1105 C  CG    . GLU A 1 148 ? 6.346  -22.497 20.791 1.00 21.00 ? 140 GLU A CG    1 
ATOM   1106 C  CD    . GLU A 1 148 ? 5.704  -23.366 19.712 1.00 23.94 ? 140 GLU A CD    1 
ATOM   1107 O  OE1   . GLU A 1 148 ? 4.486  -23.207 19.485 1.00 25.38 ? 140 GLU A OE1   1 
ATOM   1108 O  OE2   . GLU A 1 148 ? 6.429  -24.164 19.070 1.00 24.73 ? 140 GLU A OE2   1 
ATOM   1109 N  N     . SER A 1 149 ? 6.779  -18.161 19.249 1.00 15.40 ? 141 SER A N     1 
ATOM   1110 C  CA    A SER A 1 149 ? 6.371  -16.801 18.916 0.75 16.15 ? 141 SER A CA    1 
ATOM   1111 C  CA    B SER A 1 149 ? 6.389  -16.796 18.917 0.25 15.76 ? 141 SER A CA    1 
ATOM   1112 C  C     . SER A 1 149 ? 6.402  -16.575 17.409 1.00 16.30 ? 141 SER A C     1 
ATOM   1113 O  O     . SER A 1 149 ? 5.466  -16.001 16.845 1.00 16.91 ? 141 SER A O     1 
ATOM   1114 C  CB    A SER A 1 149 ? 7.248  -15.780 19.643 0.75 16.13 ? 141 SER A CB    1 
ATOM   1115 C  CB    B SER A 1 149 ? 7.331  -15.815 19.612 0.25 15.43 ? 141 SER A CB    1 
ATOM   1116 O  OG    A SER A 1 149 ? 7.093  -15.878 21.054 0.75 16.25 ? 141 SER A OG    1 
ATOM   1117 O  OG    B SER A 1 149 ? 7.290  -14.550 18.986 0.25 15.14 ? 141 SER A OG    1 
ATOM   1118 N  N     . ALA A 1 150 ? 7.464  -17.031 16.734 1.00 16.20 ? 142 ALA A N     1 
ATOM   1119 C  CA    . ALA A 1 150 ? 7.523  -16.900 15.281 1.00 16.87 ? 142 ALA A CA    1 
ATOM   1120 C  C     . ALA A 1 150 ? 6.374  -17.636 14.610 1.00 18.24 ? 142 ALA A C     1 
ATOM   1121 O  O     . ALA A 1 150 ? 5.776  -17.127 13.656 1.00 18.71 ? 142 ALA A O     1 
ATOM   1122 C  CB    . ALA A 1 150 ? 8.862  -17.421 14.761 1.00 17.05 ? 142 ALA A CB    1 
ATOM   1123 N  N     . LYS A 1 151 ? 6.049  -18.835 15.094 1.00 19.11 ? 143 LYS A N     1 
ATOM   1124 C  CA    . LYS A 1 151 ? 4.912  -19.574 14.547 1.00 21.14 ? 143 LYS A CA    1 
ATOM   1125 C  C     . LYS A 1 151 ? 3.617  -18.786 14.685 1.00 22.25 ? 143 LYS A C     1 
ATOM   1126 O  O     . LYS A 1 151 ? 2.821  -18.704 13.741 1.00 23.29 ? 143 LYS A O     1 
ATOM   1127 C  CB    . LYS A 1 151 ? 4.772  -20.913 15.267 1.00 22.37 ? 143 LYS A CB    1 
ATOM   1128 C  CG    . LYS A 1 151 ? 5.807  -21.948 14.892 1.00 24.22 ? 143 LYS A CG    1 
ATOM   1129 C  CD    . LYS A 1 151 ? 5.590  -23.209 15.708 1.00 27.01 ? 143 LYS A CD    1 
ATOM   1130 C  CE    . LYS A 1 151 ? 6.560  -24.305 15.348 1.00 29.21 ? 143 LYS A CE    1 
ATOM   1131 N  NZ    . LYS A 1 151 ? 6.414  -25.442 16.299 1.00 30.55 ? 143 LYS A NZ    1 
ATOM   1132 N  N     . ALA A 1 152 ? 3.377  -18.213 15.865 1.00 21.25 ? 144 ALA A N     1 
ATOM   1133 C  CA    . ALA A 1 152 ? 2.150  -17.453 16.076 1.00 22.22 ? 144 ALA A CA    1 
ATOM   1134 C  C     . ALA A 1 152 ? 2.093  -16.223 15.179 1.00 23.37 ? 144 ALA A C     1 
ATOM   1135 O  O     . ALA A 1 152 ? 1.004  -15.784 14.797 1.00 23.75 ? 144 ALA A O     1 
ATOM   1136 C  CB    . ALA A 1 152 ? 2.034  -17.056 17.548 1.00 22.24 ? 144 ALA A CB    1 
ATOM   1137 N  N     . LEU A 1 153 ? 3.243  -15.664 14.828 1.00 22.75 ? 145 LEU A N     1 
ATOM   1138 C  CA    . LEU A 1 153 ? 3.327  -14.519 13.938 1.00 22.88 ? 145 LEU A CA    1 
ATOM   1139 C  C     . LEU A 1 153 ? 3.408  -14.916 12.471 1.00 24.05 ? 145 LEU A C     1 
ATOM   1140 O  O     . LEU A 1 153 ? 3.457  -14.034 11.612 1.00 25.74 ? 145 LEU A O     1 
ATOM   1141 C  CB    . LEU A 1 153 ? 4.543  -13.658 14.313 1.00 22.36 ? 145 LEU A CB    1 
ATOM   1142 C  CG    . LEU A 1 153 ? 4.506  -13.016 15.713 1.00 22.12 ? 145 LEU A CG    1 
ATOM   1143 C  CD1   . LEU A 1 153 ? 5.896  -12.546 16.154 1.00 21.43 ? 145 LEU A CD1   1 
ATOM   1144 C  CD2   . LEU A 1 153 ? 3.520  -11.860 15.759 1.00 23.70 ? 145 LEU A CD2   1 
ATOM   1145 N  N     . ASN A 1 154 ? 3.413  -16.210 12.162 1.00 24.35 ? 146 ASN A N     1 
ATOM   1146 C  CA    . ASN A 1 154 ? 3.522  -16.683 10.782 1.00 25.64 ? 146 ASN A CA    1 
ATOM   1147 C  C     . ASN A 1 154 ? 4.807  -16.189 10.110 1.00 23.87 ? 146 ASN A C     1 
ATOM   1148 O  O     . ASN A 1 154 ? 4.808  -15.814 8.937  1.00 25.58 ? 146 ASN A O     1 
ATOM   1149 C  CB    . ASN A 1 154 ? 2.283  -16.302 9.964  1.00 30.05 ? 146 ASN A CB    1 
ATOM   1150 C  CG    . ASN A 1 154 ? 2.232  -17.006 8.620  1.00 34.42 ? 146 ASN A CG    1 
ATOM   1151 O  OD1   . ASN A 1 154 ? 2.595  -18.177 8.508  1.00 36.20 ? 146 ASN A OD1   1 
ATOM   1152 N  ND2   . ASN A 1 154 ? 1.795  -16.290 7.593  1.00 36.09 ? 146 ASN A ND2   1 
ATOM   1153 N  N     . ILE A 1 155 ? 5.910  -16.191 10.850 1.00 21.22 ? 147 ILE A N     1 
ATOM   1154 C  CA    . ILE A 1 155 ? 7.217  -15.806 10.325 1.00 20.43 ? 147 ILE A CA    1 
ATOM   1155 C  C     . ILE A 1 155 ? 8.081  -17.062 10.247 1.00 19.87 ? 147 ILE A C     1 
ATOM   1156 O  O     . ILE A 1 155 ? 8.380  -17.659 11.289 1.00 19.16 ? 147 ILE A O     1 
ATOM   1157 C  CB    . ILE A 1 155 ? 7.889  -14.739 11.204 1.00 20.50 ? 147 ILE A CB    1 
ATOM   1158 C  CG1   . ILE A 1 155 ? 7.037  -13.468 11.278 1.00 20.87 ? 147 ILE A CG1   1 
ATOM   1159 C  CG2   . ILE A 1 155 ? 9.269  -14.409 10.652 1.00 21.13 ? 147 ILE A CG2   1 
ATOM   1160 C  CD1   . ILE A 1 155 ? 7.430  -12.555 12.422 1.00 21.59 ? 147 ILE A CD1   1 
ATOM   1161 N  N     . PRO A 1 156 ? 8.508  -17.495 9.058  1.00 21.10 ? 148 PRO A N     1 
ATOM   1162 C  CA    . PRO A 1 156 ? 9.390  -18.668 8.971  1.00 21.72 ? 148 PRO A CA    1 
ATOM   1163 C  C     . PRO A 1 156 ? 10.722 -18.419 9.661  1.00 20.00 ? 148 PRO A C     1 
ATOM   1164 O  O     . PRO A 1 156 ? 11.238 -17.302 9.677  1.00 20.08 ? 148 PRO A O     1 
ATOM   1165 C  CB    . PRO A 1 156 ? 9.589  -18.850 7.460  1.00 23.44 ? 148 PRO A CB    1 
ATOM   1166 C  CG    . PRO A 1 156 ? 8.489  -18.091 6.818  1.00 25.59 ? 148 PRO A CG    1 
ATOM   1167 C  CD    . PRO A 1 156 ? 8.201  -16.945 7.727  1.00 24.05 ? 148 PRO A CD    1 
ATOM   1168 N  N     . THR A 1 157 ? 11.294 -19.486 10.217 1.00 18.53 ? 149 THR A N     1 
ATOM   1169 C  CA    . THR A 1 157 ? 12.587 -19.393 10.883 1.00 17.81 ? 149 THR A CA    1 
ATOM   1170 C  C     . THR A 1 157 ? 13.475 -20.574 10.519 1.00 18.24 ? 149 THR A C     1 
ATOM   1171 O  O     . THR A 1 157 ? 12.997 -21.679 10.253 1.00 20.24 ? 149 THR A O     1 
ATOM   1172 C  CB    . THR A 1 157 ? 12.427 -19.395 12.405 1.00 18.77 ? 149 THR A CB    1 
ATOM   1173 O  OG1   . THR A 1 157 ? 11.761 -20.600 12.807 1.00 20.06 ? 149 THR A OG1   1 
ATOM   1174 C  CG2   . THR A 1 157 ? 11.628 -18.192 12.857 1.00 19.01 ? 149 THR A CG2   1 
ATOM   1175 N  N     . GLN A 1 158 ? 14.777 -20.315 10.528 1.00 17.42 ? 150 GLN A N     1 
ATOM   1176 C  CA    . GLN A 1 158 ? 15.812 -21.334 10.506 1.00 17.50 ? 150 GLN A CA    1 
ATOM   1177 C  C     . GLN A 1 158 ? 16.252 -21.553 11.948 1.00 16.44 ? 150 GLN A C     1 
ATOM   1178 O  O     . GLN A 1 158 ? 16.473 -20.593 12.676 1.00 18.44 ? 150 GLN A O     1 
ATOM   1179 C  CB    . GLN A 1 158 ? 17.002 -20.821 9.695  1.00 19.95 ? 150 GLN A CB    1 
ATOM   1180 C  CG    . GLN A 1 158 ? 16.672 -20.352 8.290  1.00 22.84 ? 150 GLN A CG    1 
ATOM   1181 C  CD    . GLN A 1 158 ? 16.549 -21.493 7.300  1.00 25.78 ? 150 GLN A CD    1 
ATOM   1182 O  OE1   . GLN A 1 158 ? 16.506 -22.665 7.679  1.00 27.13 ? 150 GLN A OE1   1 
ATOM   1183 N  NE2   . GLN A 1 158 ? 16.512 -21.153 6.013  1.00 26.57 ? 150 GLN A NE2   1 
ATOM   1184 N  N     . VAL A 1 159 ? 16.397 -22.800 12.368 1.00 14.43 ? 151 VAL A N     1 
ATOM   1185 C  CA    . VAL A 1 159 ? 16.743 -23.114 13.749 1.00 14.36 ? 151 VAL A CA    1 
ATOM   1186 C  C     . VAL A 1 159 ? 17.999 -23.976 13.714 1.00 14.82 ? 151 VAL A C     1 
ATOM   1187 O  O     . VAL A 1 159 ? 18.006 -25.048 13.095 1.00 17.55 ? 151 VAL A O     1 
ATOM   1188 C  CB    . VAL A 1 159 ? 15.593 -23.856 14.453 1.00 14.68 ? 151 VAL A CB    1 
ATOM   1189 C  CG1   . VAL A 1 159 ? 15.936 -24.151 15.901 1.00 15.16 ? 151 VAL A CG1   1 
ATOM   1190 C  CG2   . VAL A 1 159 ? 14.315 -23.040 14.384 1.00 14.79 ? 151 VAL A CG2   1 
ATOM   1191 N  N     . GLY A 1 160 ? 19.065 -23.523 14.367 1.00 13.24 ? 152 GLY A N     1 
ATOM   1192 C  CA    . GLY A 1 160 ? 20.296 -24.294 14.343 1.00 13.01 ? 152 GLY A CA    1 
ATOM   1193 C  C     . GLY A 1 160 ? 21.485 -23.509 14.869 1.00 12.45 ? 152 GLY A C     1 
ATOM   1194 O  O     . GLY A 1 160 ? 21.342 -22.538 15.611 1.00 12.46 ? 152 GLY A O     1 
ATOM   1195 N  N     . LYS A 1 161 ? 22.663 -23.967 14.472 1.00 11.68 ? 153 LYS A N     1 
ATOM   1196 C  CA    . LYS A 1 161 ? 23.906 -23.505 15.067 1.00 10.80 ? 153 LYS A CA    1 
ATOM   1197 C  C     . LYS A 1 161 ? 24.368 -22.183 14.472 1.00 10.53 ? 153 LYS A C     1 
ATOM   1198 O  O     . LYS A 1 161 ? 24.321 -21.978 13.254 1.00 11.46 ? 153 LYS A O     1 
ATOM   1199 C  CB    . LYS A 1 161 ? 25.036 -24.511 14.813 1.00 10.77 ? 153 LYS A CB    1 
ATOM   1200 C  CG    . LYS A 1 161 ? 24.837 -25.888 15.441 1.00 11.26 ? 153 LYS A CG    1 
ATOM   1201 C  CD    . LYS A 1 161 ? 26.025 -26.821 15.157 1.00 11.90 ? 153 LYS A CD    1 
ATOM   1202 C  CE    . LYS A 1 161 ? 26.285 -27.023 13.668 1.00 11.85 ? 153 LYS A CE    1 
ATOM   1203 N  NZ    . LYS A 1 161 ? 25.176 -27.696 12.943 1.00 11.80 ? 153 LYS A NZ    1 
ATOM   1204 N  N     . ALA A 1 162 ? 24.914 -21.333 15.329 1.00 10.04 ? 154 ALA A N     1 
ATOM   1205 C  CA    . ALA A 1 162 ? 25.680 -20.168 14.913 1.00 9.86  ? 154 ALA A CA    1 
ATOM   1206 C  C     . ALA A 1 162 ? 27.169 -20.430 15.101 1.00 9.78  ? 154 ALA A C     1 
ATOM   1207 O  O     . ALA A 1 162 ? 27.580 -21.410 15.711 1.00 9.65  ? 154 ALA A O     1 
ATOM   1208 C  CB    . ALA A 1 162 ? 25.264 -18.940 15.723 1.00 11.05 ? 154 ALA A CB    1 
ATOM   1209 N  N     . TYR A 1 163 ? 27.975 -19.500 14.595 1.00 9.77  ? 155 TYR A N     1 
ATOM   1210 C  CA    . TYR A 1 163 ? 29.415 -19.485 14.802 1.00 9.49  ? 155 TYR A CA    1 
ATOM   1211 C  C     . TYR A 1 163 ? 29.791 -18.063 15.167 1.00 9.96  ? 155 TYR A C     1 
ATOM   1212 O  O     . TYR A 1 163 ? 29.535 -17.142 14.386 1.00 10.91 ? 155 TYR A O     1 
ATOM   1213 C  CB    . TYR A 1 163 ? 30.146 -19.920 13.538 1.00 10.80 ? 155 TYR A CB    1 
ATOM   1214 C  CG    . TYR A 1 163 ? 31.644 -20.076 13.711 1.00 10.46 ? 155 TYR A CG    1 
ATOM   1215 C  CD1   . TYR A 1 163 ? 32.166 -21.149 14.425 1.00 10.71 ? 155 TYR A CD1   1 
ATOM   1216 C  CD2   . TYR A 1 163 ? 32.541 -19.193 13.126 1.00 10.25 ? 155 TYR A CD2   1 
ATOM   1217 C  CE1   . TYR A 1 163 ? 33.509 -21.326 14.572 1.00 11.20 ? 155 TYR A CE1   1 
ATOM   1218 C  CE2   . TYR A 1 163 ? 33.905 -19.370 13.265 1.00 10.83 ? 155 TYR A CE2   1 
ATOM   1219 C  CZ    . TYR A 1 163 ? 34.380 -20.445 13.987 1.00 11.53 ? 155 TYR A CZ    1 
ATOM   1220 O  OH    . TYR A 1 163 ? 35.727 -20.690 14.146 1.00 12.67 ? 155 TYR A OH    1 
ATOM   1221 N  N     . SER A 1 164 ? 30.374 -17.898 16.354 1.00 9.84  ? 156 SER A N     1 
ATOM   1222 C  CA    . SER A 1 164 ? 30.776 -16.602 16.893 1.00 9.91  ? 156 SER A CA    1 
ATOM   1223 C  C     . SER A 1 164 ? 32.283 -16.465 16.710 1.00 10.24 ? 156 SER A C     1 
ATOM   1224 O  O     . SER A 1 164 ? 33.064 -17.134 17.399 1.00 11.22 ? 156 SER A O     1 
ATOM   1225 C  CB    . SER A 1 164 ? 30.442 -16.522 18.379 1.00 10.64 ? 156 SER A CB    1 
ATOM   1226 O  OG    . SER A 1 164 ? 29.079 -16.777 18.625 1.00 11.03 ? 156 SER A OG    1 
ATOM   1227 N  N     . THR A 1 165 ? 32.699 -15.601 15.791 1.00 10.17 ? 157 THR A N     1 
ATOM   1228 C  CA    . THR A 1 165 ? 34.109 -15.396 15.512 1.00 10.10 ? 157 THR A CA    1 
ATOM   1229 C  C     . THR A 1 165 ? 34.636 -14.125 16.175 1.00 9.86  ? 157 THR A C     1 
ATOM   1230 O  O     . THR A 1 165 ? 33.926 -13.129 16.342 1.00 10.58 ? 157 THR A O     1 
ATOM   1231 C  CB    . THR A 1 165 ? 34.375 -15.361 13.998 1.00 10.80 ? 157 THR A CB    1 
ATOM   1232 O  OG1   . THR A 1 165 ? 35.787 -15.246 13.768 1.00 10.67 ? 157 THR A OG1   1 
ATOM   1233 C  CG2   . THR A 1 165 ? 33.671 -14.207 13.321 1.00 11.31 ? 157 THR A CG2   1 
ATOM   1234 N  N     . ASP A 1 166 ? 35.911 -14.186 16.550 1.00 9.13  ? 158 ASP A N     1 
ATOM   1235 C  CA    . ASP A 1 166 ? 36.658 -13.017 16.993 1.00 10.14 ? 158 ASP A CA    1 
ATOM   1236 C  C     . ASP A 1 166 ? 37.106 -12.129 15.833 1.00 9.61  ? 158 ASP A C     1 
ATOM   1237 O  O     . ASP A 1 166 ? 37.520 -10.990 16.077 1.00 9.66  ? 158 ASP A O     1 
ATOM   1238 C  CB    . ASP A 1 166 ? 37.924 -13.476 17.729 1.00 9.72  ? 158 ASP A CB    1 
ATOM   1239 C  CG    . ASP A 1 166 ? 37.690 -13.887 19.191 1.00 9.51  ? 158 ASP A CG    1 
ATOM   1240 O  OD1   . ASP A 1 166 ? 36.571 -13.738 19.729 1.00 10.71 ? 158 ASP A OD1   1 
ATOM   1241 O  OD2   . ASP A 1 166 ? 38.671 -14.389 19.810 1.00 11.20 ? 158 ASP A OD2   1 
ATOM   1242 N  N     . ILE A 1 167 ? 37.044 -12.614 14.587 1.00 9.74  ? 159 ILE A N     1 
ATOM   1243 C  CA    . ILE A 1 167 ? 37.642 -11.936 13.442 1.00 10.57 ? 159 ILE A CA    1 
ATOM   1244 C  C     . ILE A 1 167 ? 36.568 -11.720 12.385 1.00 10.38 ? 159 ILE A C     1 
ATOM   1245 O  O     . ILE A 1 167 ? 36.259 -12.607 11.587 1.00 10.62 ? 159 ILE A O     1 
ATOM   1246 C  CB    . ILE A 1 167 ? 38.861 -12.682 12.891 1.00 11.54 ? 159 ILE A CB    1 
ATOM   1247 C  CG1   . ILE A 1 167 ? 39.987 -12.654 13.929 1.00 13.61 ? 159 ILE A CG1   1 
ATOM   1248 C  CG2   . ILE A 1 167 ? 39.303 -12.084 11.547 1.00 12.69 ? 159 ILE A CG2   1 
ATOM   1249 C  CD1   . ILE A 1 167 ? 40.593 -11.264 14.175 1.00 14.40 ? 159 ILE A CD1   1 
ATOM   1250 N  N     . PHE A 1 168 ? 36.018 -10.511 12.346 1.00 10.54 ? 160 PHE A N     1 
ATOM   1251 C  CA    . PHE A 1 168 ? 35.086 -10.164 11.285 1.00 11.14 ? 160 PHE A CA    1 
ATOM   1252 C  C     . PHE A 1 168 ? 35.734 -10.321 9.919  1.00 11.45 ? 160 PHE A C     1 
ATOM   1253 O  O     . PHE A 1 168 ? 35.149 -10.910 9.003  1.00 12.79 ? 160 PHE A O     1 
ATOM   1254 C  CB    . PHE A 1 168 ? 34.589 -8.737  11.496 1.00 11.20 ? 160 PHE A CB    1 
ATOM   1255 C  CG    . PHE A 1 168 ? 33.564 -8.290  10.492 1.00 11.47 ? 160 PHE A CG    1 
ATOM   1256 C  CD1   . PHE A 1 168 ? 32.220 -8.518  10.718 1.00 12.55 ? 160 PHE A CD1   1 
ATOM   1257 C  CD2   . PHE A 1 168 ? 33.940 -7.663  9.324  1.00 12.10 ? 160 PHE A CD2   1 
ATOM   1258 C  CE1   . PHE A 1 168 ? 31.264 -8.118  9.796  1.00 13.53 ? 160 PHE A CE1   1 
ATOM   1259 C  CE2   . PHE A 1 168 ? 32.994 -7.251  8.397  1.00 12.31 ? 160 PHE A CE2   1 
ATOM   1260 C  CZ    . PHE A 1 168 ? 31.635 -7.491  8.634  1.00 12.87 ? 160 PHE A CZ    1 
ATOM   1261 N  N     . TYR A 1 169 ? 36.941 -9.780  9.760  1.00 10.72 ? 161 TYR A N     1 
ATOM   1262 C  CA    . TYR A 1 169 ? 37.629 -9.763  8.469  1.00 11.75 ? 161 TYR A CA    1 
ATOM   1263 C  C     . TYR A 1 169 ? 38.459 -11.036 8.308  1.00 12.19 ? 161 TYR A C     1 
ATOM   1264 O  O     . TYR A 1 169 ? 39.689 -11.046 8.370  1.00 12.33 ? 161 TYR A O     1 
ATOM   1265 C  CB    . TYR A 1 169 ? 38.469 -8.500  8.343  1.00 12.00 ? 161 TYR A CB    1 
ATOM   1266 C  CG    . TYR A 1 169 ? 37.598 -7.288  8.127  1.00 12.12 ? 161 TYR A CG    1 
ATOM   1267 C  CD1   . TYR A 1 169 ? 36.916 -7.138  6.934  1.00 13.17 ? 161 TYR A CD1   1 
ATOM   1268 C  CD2   . TYR A 1 169 ? 37.431 -6.314  9.109  1.00 12.28 ? 161 TYR A CD2   1 
ATOM   1269 C  CE1   . TYR A 1 169 ? 36.087 -6.060  6.709  1.00 13.39 ? 161 TYR A CE1   1 
ATOM   1270 C  CE2   . TYR A 1 169 ? 36.600 -5.209  8.891  1.00 12.46 ? 161 TYR A CE2   1 
ATOM   1271 C  CZ    . TYR A 1 169 ? 35.933 -5.103  7.685  1.00 12.63 ? 161 TYR A CZ    1 
ATOM   1272 O  OH    . TYR A 1 169 ? 35.082 -4.053  7.414  1.00 13.06 ? 161 TYR A OH    1 
ATOM   1273 N  N     . SER A 1 170 ? 37.746 -12.137 8.093  1.00 12.27 ? 162 SER A N     1 
ATOM   1274 C  CA    . SER A 1 170 ? 38.381 -13.442 8.008  1.00 13.14 ? 162 SER A CA    1 
ATOM   1275 C  C     . SER A 1 170 ? 39.318 -13.534 6.815  1.00 13.23 ? 162 SER A C     1 
ATOM   1276 O  O     . SER A 1 170 ? 39.005 -13.088 5.708  1.00 15.09 ? 162 SER A O     1 
ATOM   1277 C  CB    . SER A 1 170 ? 37.321 -14.525 7.851  1.00 13.71 ? 162 SER A CB    1 
ATOM   1278 O  OG    . SER A 1 170 ? 37.953 -15.795 7.730  1.00 14.13 ? 162 SER A OG    1 
ATOM   1279 N  N     . LYS A 1 171 ? 40.470 -14.159 7.051  1.00 12.92 ? 163 LYS A N     1 
ATOM   1280 C  CA    . LYS A 1 171 ? 41.431 -14.527 6.022  1.00 13.39 ? 163 LYS A CA    1 
ATOM   1281 C  C     . LYS A 1 171 ? 41.649 -16.034 6.033  1.00 13.39 ? 163 LYS A C     1 
ATOM   1282 O  O     . LYS A 1 171 ? 42.662 -16.524 5.535  1.00 14.19 ? 163 LYS A O     1 
ATOM   1283 C  CB    . LYS A 1 171 ? 42.744 -13.782 6.258  1.00 14.11 ? 163 LYS A CB    1 
ATOM   1284 C  CG    . LYS A 1 171 ? 42.613 -12.266 6.193  1.00 14.69 ? 163 LYS A CG    1 
ATOM   1285 C  CD    . LYS A 1 171 ? 43.844 -11.568 6.785  1.00 15.12 ? 163 LYS A CD    1 
ATOM   1286 C  CE    . LYS A 1 171 ? 43.773 -10.058 6.648  1.00 15.82 ? 163 LYS A CE    1 
ATOM   1287 N  NZ    . LYS A 1 171 ? 42.584 -9.515  7.358  1.00 16.23 ? 163 LYS A NZ    1 
ATOM   1288 N  N     . GLU A 1 172 ? 40.712 -16.779 6.603  1.00 12.75 ? 164 GLU A N     1 
ATOM   1289 C  CA    . GLU A 1 172 ? 40.926 -18.176 6.980  1.00 12.24 ? 164 GLU A CA    1 
ATOM   1290 C  C     . GLU A 1 172 ? 40.432 -19.114 5.887  1.00 13.65 ? 164 GLU A C     1 
ATOM   1291 O  O     . GLU A 1 172 ? 39.233 -19.358 5.748  1.00 14.24 ? 164 GLU A O     1 
ATOM   1292 C  CB    . GLU A 1 172 ? 40.239 -18.446 8.313  1.00 11.88 ? 164 GLU A CB    1 
ATOM   1293 C  CG    . GLU A 1 172 ? 40.535 -19.794 8.867  1.00 12.05 ? 164 GLU A CG    1 
ATOM   1294 C  CD    . GLU A 1 172 ? 39.935 -20.025 10.238 1.00 13.13 ? 164 GLU A CD    1 
ATOM   1295 O  OE1   . GLU A 1 172 ? 39.216 -19.145 10.762 1.00 12.75 ? 164 GLU A OE1   1 
ATOM   1296 O  OE2   . GLU A 1 172 ? 40.193 -21.121 10.775 1.00 15.09 ? 164 GLU A OE2   1 
ATOM   1297 N  N     . GLN A 1 173 ? 41.369 -19.683 5.143  1.00 14.75 ? 165 GLN A N     1 
ATOM   1298 C  CA    . GLN A 1 173 ? 41.016 -20.612 4.082  1.00 16.68 ? 165 GLN A CA    1 
ATOM   1299 C  C     . GLN A 1 173 ? 40.332 -21.852 4.651  1.00 16.07 ? 165 GLN A C     1 
ATOM   1300 O  O     . GLN A 1 173 ? 40.762 -22.426 5.656  1.00 16.65 ? 165 GLN A O     1 
ATOM   1301 C  CB    . GLN A 1 173 ? 42.279 -21.012 3.323  1.00 20.13 ? 165 GLN A CB    1 
ATOM   1302 C  CG    . GLN A 1 173 ? 43.059 -19.844 2.743  1.00 24.51 ? 165 GLN A CG    1 
ATOM   1303 C  CD    . GLN A 1 173 ? 42.484 -19.326 1.441  1.00 29.35 ? 165 GLN A CD    1 
ATOM   1304 O  OE1   . GLN A 1 173 ? 41.429 -19.773 0.987  1.00 32.14 ? 165 GLN A OE1   1 
ATOM   1305 N  NE2   . GLN A 1 173 ? 43.188 -18.383 0.822  1.00 31.72 ? 165 GLN A NE2   1 
ATOM   1306 N  N     . GLY A 1 174 ? 39.248 -22.260 4.007  1.00 15.04 ? 166 GLY A N     1 
ATOM   1307 C  CA    . GLY A 1 174 ? 38.536 -23.458 4.383  1.00 14.82 ? 166 GLY A CA    1 
ATOM   1308 C  C     . GLY A 1 174 ? 37.480 -23.286 5.448  1.00 14.31 ? 166 GLY A C     1 
ATOM   1309 O  O     . GLY A 1 174 ? 36.706 -24.221 5.674  1.00 14.52 ? 166 GLY A O     1 
ATOM   1310 N  N     . LEU A 1 175 ? 37.421 -22.133 6.117  1.00 13.05 ? 167 LEU A N     1 
ATOM   1311 C  CA    . LEU A 1 175 ? 36.453 -21.952 7.190  1.00 12.90 ? 167 LEU A CA    1 
ATOM   1312 C  C     . LEU A 1 175 ? 35.031 -22.010 6.652  1.00 12.58 ? 167 LEU A C     1 
ATOM   1313 O  O     . LEU A 1 175 ? 34.182 -22.727 7.190  1.00 12.28 ? 167 LEU A O     1 
ATOM   1314 C  CB    . LEU A 1 175 ? 36.691 -20.632 7.926  1.00 13.02 ? 167 LEU A CB    1 
ATOM   1315 C  CG    . LEU A 1 175 ? 35.676 -20.310 9.042  1.00 12.98 ? 167 LEU A CG    1 
ATOM   1316 C  CD1   . LEU A 1 175 ? 35.805 -21.259 10.225 1.00 14.56 ? 167 LEU A CD1   1 
ATOM   1317 C  CD2   . LEU A 1 175 ? 35.821 -18.881 9.498  1.00 14.07 ? 167 LEU A CD2   1 
ATOM   1318 N  N     . ASN A 1 176 ? 34.745 -21.253 5.587  1.00 12.79 ? 168 ASN A N     1 
ATOM   1319 C  CA    . ASN A 1 176 ? 33.377 -21.200 5.072  1.00 13.78 ? 168 ASN A CA    1 
ATOM   1320 C  C     . ASN A 1 176 ? 32.908 -22.569 4.607  1.00 13.17 ? 168 ASN A C     1 
ATOM   1321 O  O     . ASN A 1 176 ? 31.741 -22.938 4.803  1.00 12.97 ? 168 ASN A O     1 
ATOM   1322 C  CB    . ASN A 1 176 ? 33.290 -20.196 3.924  1.00 15.06 ? 168 ASN A CB    1 
ATOM   1323 C  CG    . ASN A 1 176 ? 33.423 -18.761 4.399  1.00 15.92 ? 168 ASN A CG    1 
ATOM   1324 O  OD1   . ASN A 1 176 ? 33.174 -18.458 5.567  1.00 16.89 ? 168 ASN A OD1   1 
ATOM   1325 N  ND2   . ASN A 1 176 ? 33.811 -17.871 3.497  1.00 16.93 ? 168 ASN A ND2   1 
ATOM   1326 N  N     . GLU A 1 177 ? 33.814 -23.342 4.012  1.00 13.45 ? 169 GLU A N     1 
ATOM   1327 C  CA    . GLU A 1 177 ? 33.469 -24.668 3.527  1.00 14.54 ? 169 GLU A CA    1 
ATOM   1328 C  C     . GLU A 1 177 ? 33.109 -25.590 4.679  1.00 13.58 ? 169 GLU A C     1 
ATOM   1329 O  O     . GLU A 1 177 ? 32.132 -26.337 4.592  1.00 13.77 ? 169 GLU A O     1 
ATOM   1330 C  CB    . GLU A 1 177 ? 34.638 -25.230 2.723  1.00 17.02 ? 169 GLU A CB    1 
ATOM   1331 C  CG    . GLU A 1 177 ? 34.806 -24.593 1.349  1.00 20.73 ? 169 GLU A CG    1 
ATOM   1332 C  CD    . GLU A 1 177 ? 35.607 -23.290 1.337  1.00 23.56 ? 169 GLU A CD    1 
ATOM   1333 O  OE1   . GLU A 1 177 ? 36.024 -22.770 2.404  1.00 22.02 ? 169 GLU A OE1   1 
ATOM   1334 O  OE2   . GLU A 1 177 ? 35.836 -22.791 0.217  1.00 26.98 ? 169 GLU A OE2   1 
ATOM   1335 N  N     . ALA A 1 178 ? 33.861 -25.531 5.776  1.00 12.93 ? 170 ALA A N     1 
ATOM   1336 C  CA    . ALA A 1 178 ? 33.549 -26.369 6.932  1.00 12.69 ? 170 ALA A CA    1 
ATOM   1337 C  C     . ALA A 1 178 ? 32.249 -25.936 7.598  1.00 11.85 ? 170 ALA A C     1 
ATOM   1338 O  O     . ALA A 1 178 ? 31.418 -26.775 7.958  1.00 12.30 ? 170 ALA A O     1 
ATOM   1339 C  CB    . ALA A 1 178 ? 34.708 -26.356 7.928  1.00 13.54 ? 170 ALA A CB    1 
ATOM   1340 N  N     . LEU A 1 179 ? 32.044 -24.627 7.741  1.00 11.39 ? 171 LEU A N     1 
ATOM   1341 C  CA    . LEU A 1 179 ? 30.808 -24.148 8.334  1.00 11.58 ? 171 LEU A CA    1 
ATOM   1342 C  C     . LEU A 1 179 ? 29.605 -24.600 7.522  1.00 11.13 ? 171 LEU A C     1 
ATOM   1343 O  O     . LEU A 1 179 ? 28.591 -25.023 8.087  1.00 12.30 ? 171 LEU A O     1 
ATOM   1344 C  CB    . LEU A 1 179 ? 30.848 -22.631 8.436  1.00 11.69 ? 171 LEU A CB    1 
ATOM   1345 C  CG    . LEU A 1 179 ? 31.817 -22.038 9.450  1.00 11.58 ? 171 LEU A CG    1 
ATOM   1346 C  CD1   . LEU A 1 179 ? 31.865 -20.520 9.268  1.00 12.44 ? 171 LEU A CD1   1 
ATOM   1347 C  CD2   . LEU A 1 179 ? 31.424 -22.393 10.871 1.00 12.24 ? 171 LEU A CD2   1 
ATOM   1348 N  N     . ALA A 1 180 ? 29.703 -24.534 6.189  1.00 11.66 ? 172 ALA A N     1 
ATOM   1349 C  CA    . ALA A 1 180 ? 28.589 -24.954 5.347  1.00 12.78 ? 172 ALA A CA    1 
ATOM   1350 C  C     . ALA A 1 180 ? 28.388 -26.461 5.411  1.00 13.08 ? 172 ALA A C     1 
ATOM   1351 O  O     . ALA A 1 180 ? 27.252 -26.941 5.423  1.00 13.85 ? 172 ALA A O     1 
ATOM   1352 C  CB    . ALA A 1 180 ? 28.849 -24.530 3.906  1.00 13.52 ? 172 ALA A CB    1 
ATOM   1353 N  N     . GLN A 1 181 ? 29.482 -27.230 5.440  1.00 13.15 ? 173 GLN A N     1 
ATOM   1354 C  CA    . GLN A 1 181 ? 29.366 -28.683 5.441  1.00 14.11 ? 173 GLN A CA    1 
ATOM   1355 C  C     . GLN A 1 181 ? 28.591 -29.173 6.651  1.00 13.47 ? 173 GLN A C     1 
ATOM   1356 O  O     . GLN A 1 181 ? 27.871 -30.177 6.571  1.00 14.68 ? 173 GLN A O     1 
ATOM   1357 C  CB    . GLN A 1 181 ? 30.758 -29.315 5.441  1.00 15.93 ? 173 GLN A CB    1 
ATOM   1358 C  CG    . GLN A 1 181 ? 30.744 -30.837 5.486  1.00 18.74 ? 173 GLN A CG    1 
ATOM   1359 C  CD    . GLN A 1 181 ? 30.127 -31.442 4.257  1.00 23.37 ? 173 GLN A CD    1 
ATOM   1360 O  OE1   . GLN A 1 181 ? 30.746 -31.462 3.199  1.00 26.25 ? 173 GLN A OE1   1 
ATOM   1361 N  NE2   . GLN A 1 181 ? 28.907 -31.978 4.391  1.00 24.54 ? 173 GLN A NE2   1 
ATOM   1362 N  N     . TYR A 1 182 ? 28.741 -28.495 7.782  1.00 12.46 ? 174 TYR A N     1 
ATOM   1363 C  CA    . TYR A 1 182 ? 28.091 -28.897 9.017  1.00 11.97 ? 174 TYR A CA    1 
ATOM   1364 C  C     . TYR A 1 182 ? 26.862 -28.059 9.319  1.00 11.87 ? 174 TYR A C     1 
ATOM   1365 O  O     . TYR A 1 182 ? 26.302 -28.159 10.417 1.00 12.20 ? 174 TYR A O     1 
ATOM   1366 C  CB    . TYR A 1 182 ? 29.098 -28.929 10.166 1.00 12.16 ? 174 TYR A CB    1 
ATOM   1367 C  CG    . TYR A 1 182 ? 30.125 -30.030 9.947  1.00 12.04 ? 174 TYR A CG    1 
ATOM   1368 C  CD1   . TYR A 1 182 ? 29.851 -31.334 10.330 1.00 11.51 ? 174 TYR A CD1   1 
ATOM   1369 C  CD2   . TYR A 1 182 ? 31.341 -29.782 9.317  1.00 12.27 ? 174 TYR A CD2   1 
ATOM   1370 C  CE1   . TYR A 1 182 ? 30.759 -32.347 10.111 1.00 12.02 ? 174 TYR A CE1   1 
ATOM   1371 C  CE2   . TYR A 1 182 ? 32.254 -30.804 9.092  1.00 12.35 ? 174 TYR A CE2   1 
ATOM   1372 C  CZ    . TYR A 1 182 ? 31.950 -32.077 9.501  1.00 11.94 ? 174 TYR A CZ    1 
ATOM   1373 O  OH    . TYR A 1 182 ? 32.821 -33.114 9.290  1.00 12.32 ? 174 TYR A OH    1 
ATOM   1374 N  N     . HIS A 1 183 ? 26.433 -27.243 8.362  1.00 12.57 ? 175 HIS A N     1 
ATOM   1375 C  CA    . HIS A 1 183 ? 25.152 -26.543 8.429  1.00 13.41 ? 175 HIS A CA    1 
ATOM   1376 C  C     . HIS A 1 183 ? 25.073 -25.572 9.597  1.00 12.89 ? 175 HIS A C     1 
ATOM   1377 O  O     . HIS A 1 183 ? 24.038 -25.437 10.251 1.00 14.23 ? 175 HIS A O     1 
ATOM   1378 C  CB    . HIS A 1 183 ? 23.988 -27.525 8.387  1.00 14.31 ? 175 HIS A CB    1 
ATOM   1379 C  CG    . HIS A 1 183 ? 23.972 -28.302 7.123  1.00 15.68 ? 175 HIS A CG    1 
ATOM   1380 N  ND1   . HIS A 1 183 ? 23.675 -27.722 5.908  1.00 19.08 ? 175 HIS A ND1   1 
ATOM   1381 C  CD2   . HIS A 1 183 ? 24.283 -29.590 6.862  1.00 15.89 ? 175 HIS A CD2   1 
ATOM   1382 C  CE1   . HIS A 1 183 ? 23.771 -28.633 4.957  1.00 20.04 ? 175 HIS A CE1   1 
ATOM   1383 N  NE2   . HIS A 1 183 ? 24.139 -29.773 5.510  1.00 17.89 ? 175 HIS A NE2   1 
ATOM   1384 N  N     . PHE A 1 184 ? 26.155 -24.834 9.817  1.00 12.12 ? 176 PHE A N     1 
ATOM   1385 C  CA    . PHE A 1 184 ? 26.053 -23.625 10.618 1.00 11.51 ? 176 PHE A CA    1 
ATOM   1386 C  C     . PHE A 1 184 ? 25.267 -22.594 9.826  1.00 12.09 ? 176 PHE A C     1 
ATOM   1387 O  O     . PHE A 1 184 ? 25.575 -22.328 8.659  1.00 14.13 ? 176 PHE A O     1 
ATOM   1388 C  CB    . PHE A 1 184 ? 27.446 -23.088 10.930 1.00 11.63 ? 176 PHE A CB    1 
ATOM   1389 C  CG    . PHE A 1 184 ? 28.194 -23.905 11.955 1.00 10.21 ? 176 PHE A CG    1 
ATOM   1390 C  CD1   . PHE A 1 184 ? 28.855 -25.074 11.614 1.00 10.67 ? 176 PHE A CD1   1 
ATOM   1391 C  CD2   . PHE A 1 184 ? 28.230 -23.500 13.276 1.00 10.59 ? 176 PHE A CD2   1 
ATOM   1392 C  CE1   . PHE A 1 184 ? 29.540 -25.792 12.572 1.00 9.68  ? 176 PHE A CE1   1 
ATOM   1393 C  CE2   . PHE A 1 184 ? 28.892 -24.223 14.237 1.00 10.69 ? 176 PHE A CE2   1 
ATOM   1394 C  CZ    . PHE A 1 184 ? 29.553 -25.373 13.890 1.00 10.03 ? 176 PHE A CZ    1 
ATOM   1395 N  N     . ILE A 1 185 ? 24.229 -22.035 10.442 1.00 11.96 ? 177 ILE A N     1 
ATOM   1396 C  CA    . ILE A 1 185 ? 23.307 -21.160 9.722  1.00 12.77 ? 177 ILE A CA    1 
ATOM   1397 C  C     . ILE A 1 185 ? 23.617 -19.681 9.876  1.00 13.48 ? 177 ILE A C     1 
ATOM   1398 O  O     . ILE A 1 185 ? 23.151 -18.881 9.047  1.00 14.67 ? 177 ILE A O     1 
ATOM   1399 C  CB    . ILE A 1 185 ? 21.834 -21.443 10.093 1.00 13.68 ? 177 ILE A CB    1 
ATOM   1400 C  CG1   . ILE A 1 185 ? 21.549 -21.166 11.573 1.00 13.89 ? 177 ILE A CG1   1 
ATOM   1401 C  CG2   . ILE A 1 185 ? 21.486 -22.874 9.740  1.00 15.27 ? 177 ILE A CG2   1 
ATOM   1402 C  CD1   . ILE A 1 185 ? 20.056 -21.235 11.944 1.00 15.55 ? 177 ILE A CD1   1 
ATOM   1403 N  N     . ALA A 1 186 ? 24.347 -19.291 10.918 1.00 12.45 ? 178 ALA A N     1 
ATOM   1404 C  CA    . ALA A 1 186 ? 24.572 -17.884 11.217 1.00 12.44 ? 178 ALA A CA    1 
ATOM   1405 C  C     . ALA A 1 186 ? 26.015 -17.656 11.628 1.00 12.85 ? 178 ALA A C     1 
ATOM   1406 O  O     . ALA A 1 186 ? 26.559 -18.419 12.425 1.00 13.47 ? 178 ALA A O     1 
ATOM   1407 C  CB    . ALA A 1 186 ? 23.666 -17.437 12.367 1.00 12.69 ? 178 ALA A CB    1 
ATOM   1408 N  N     . VAL A 1 187 ? 26.627 -16.607 11.087 1.00 11.40 ? 179 VAL A N     1 
ATOM   1409 C  CA    . VAL A 1 187 ? 27.962 -16.172 11.481 1.00 11.45 ? 179 VAL A CA    1 
ATOM   1410 C  C     . VAL A 1 187 ? 27.812 -14.817 12.157 1.00 10.67 ? 179 VAL A C     1 
ATOM   1411 O  O     . VAL A 1 187 ? 27.333 -13.857 11.542 1.00 11.28 ? 179 VAL A O     1 
ATOM   1412 C  CB    . VAL A 1 187 ? 28.908 -16.083 10.274 1.00 13.00 ? 179 VAL A CB    1 
ATOM   1413 C  CG1   . VAL A 1 187 ? 30.303 -15.638 10.724 1.00 13.60 ? 179 VAL A CG1   1 
ATOM   1414 C  CG2   . VAL A 1 187 ? 28.966 -17.414 9.542  1.00 14.49 ? 179 VAL A CG2   1 
ATOM   1415 N  N     . GLU A 1 188 ? 28.214 -14.739 13.420 1.00 10.89 ? 180 GLU A N     1 
ATOM   1416 C  CA    . GLU A 1 188 ? 28.144 -13.502 14.195 1.00 11.09 ? 180 GLU A CA    1 
ATOM   1417 C  C     . GLU A 1 188 ? 29.369 -13.485 15.102 1.00 10.49 ? 180 GLU A C     1 
ATOM   1418 O  O     . GLU A 1 188 ? 30.371 -14.140 14.802 1.00 10.30 ? 180 GLU A O     1 
ATOM   1419 C  CB    . GLU A 1 188 ? 26.750 -13.307 14.821 1.00 12.12 ? 180 GLU A CB    1 
ATOM   1420 C  CG    . GLU A 1 188 ? 26.153 -14.503 15.505 1.00 13.19 ? 180 GLU A CG    1 
ATOM   1421 C  CD    . GLU A 1 188 ? 26.734 -14.760 16.844 1.00 15.66 ? 180 GLU A CD    1 
ATOM   1422 O  OE1   . GLU A 1 188 ? 26.348 -14.116 17.821 1.00 20.44 ? 180 GLU A OE1   1 
ATOM   1423 O  OE2   . GLU A 1 188 ? 27.641 -15.578 16.900 1.00 19.92 ? 180 GLU A OE2   1 
ATOM   1424 N  N     . MET A 1 189 ? 29.334 -12.700 16.194 1.00 10.36 ? 181 MET A N     1 
ATOM   1425 C  CA    . MET A 1 189 ? 30.541 -12.496 16.992 1.00 9.84  ? 181 MET A CA    1 
ATOM   1426 C  C     . MET A 1 189 ? 30.314 -12.543 18.501 1.00 10.78 ? 181 MET A C     1 
ATOM   1427 O  O     . MET A 1 189 ? 31.217 -12.153 19.249 1.00 13.27 ? 181 MET A O     1 
ATOM   1428 C  CB    . MET A 1 189 ? 31.257 -11.184 16.607 1.00 9.99  ? 181 MET A CB    1 
ATOM   1429 C  CG    . MET A 1 189 ? 31.643 -11.139 15.140 1.00 10.57 ? 181 MET A CG    1 
ATOM   1430 S  SD    . MET A 1 189 ? 32.477 -9.615  14.673 1.00 11.82 ? 181 MET A SD    1 
ATOM   1431 C  CE    . MET A 1 189 ? 33.945 -9.694  15.709 1.00 12.62 ? 181 MET A CE    1 
ATOM   1432 N  N     . GLU A 1 190 ? 29.170 -13.032 18.987 1.00 10.37 ? 182 GLU A N     1 
ATOM   1433 C  CA    . GLU A 1 190 ? 28.853 -12.815 20.390 1.00 9.86  ? 182 GLU A CA    1 
ATOM   1434 C  C     . GLU A 1 190 ? 28.198 -13.972 21.138 1.00 10.13 ? 182 GLU A C     1 
ATOM   1435 O  O     . GLU A 1 190 ? 28.464 -14.134 22.337 1.00 10.84 ? 182 GLU A O     1 
ATOM   1436 C  CB    . GLU A 1 190 ? 27.937 -11.587 20.523 1.00 11.26 ? 182 GLU A CB    1 
ATOM   1437 C  CG    . GLU A 1 190 ? 28.584 -10.262 20.178 1.00 11.59 ? 182 GLU A CG    1 
ATOM   1438 C  CD    . GLU A 1 190 ? 28.565 -9.914  18.698 1.00 11.57 ? 182 GLU A CD    1 
ATOM   1439 O  OE1   . GLU A 1 190 ? 27.793 -10.536 17.923 1.00 12.74 ? 182 GLU A OE1   1 
ATOM   1440 O  OE2   . GLU A 1 190 ? 29.313 -8.966  18.323 1.00 11.37 ? 182 GLU A OE2   1 
ATOM   1441 N  N     . SER A 1 191 ? 27.297 -14.739 20.501 1.00 10.67 ? 183 SER A N     1 
ATOM   1442 C  CA    A SER A 1 191 ? 26.470 -15.692 21.241 0.58 11.06 ? 183 SER A CA    1 
ATOM   1443 C  CA    B SER A 1 191 ? 26.471 -15.652 21.284 0.42 10.91 ? 183 SER A CA    1 
ATOM   1444 C  C     . SER A 1 191 ? 27.304 -16.689 22.030 1.00 10.48 ? 183 SER A C     1 
ATOM   1445 O  O     . SER A 1 191 ? 26.927 -17.090 23.140 1.00 10.93 ? 183 SER A O     1 
ATOM   1446 C  CB    A SER A 1 191 ? 25.570 -16.461 20.282 0.58 12.25 ? 183 SER A CB    1 
ATOM   1447 C  CB    B SER A 1 191 ? 25.390 -16.308 20.420 0.42 11.76 ? 183 SER A CB    1 
ATOM   1448 O  OG    A SER A 1 191 ? 24.587 -15.609 19.768 0.58 12.61 ? 183 SER A OG    1 
ATOM   1449 O  OG    B SER A 1 191 ? 25.923 -16.914 19.264 0.42 11.46 ? 183 SER A OG    1 
ATOM   1450 N  N     . ALA A 1 192 ? 28.434 -17.131 21.462 1.00 10.54 ? 184 ALA A N     1 
ATOM   1451 C  CA    . ALA A 1 192 ? 29.242 -18.141 22.141 1.00 11.11 ? 184 ALA A CA    1 
ATOM   1452 C  C     . ALA A 1 192 ? 29.813 -17.632 23.452 1.00 10.89 ? 184 ALA A C     1 
ATOM   1453 O  O     . ALA A 1 192 ? 30.185 -18.436 24.309 1.00 11.24 ? 184 ALA A O     1 
ATOM   1454 C  CB    . ALA A 1 192 ? 30.347 -18.671 21.223 1.00 11.23 ? 184 ALA A CB    1 
ATOM   1455 N  N     . GLY A 1 193 ? 29.919 -16.309 23.623 1.00 10.12 ? 185 GLY A N     1 
ATOM   1456 C  CA    . GLY A 1 193 ? 30.343 -15.780 24.907 1.00 10.85 ? 185 GLY A CA    1 
ATOM   1457 C  C     . GLY A 1 193 ? 29.222 -15.616 25.906 1.00 10.38 ? 185 GLY A C     1 
ATOM   1458 O  O     . GLY A 1 193 ? 29.464 -15.637 27.118 1.00 11.48 ? 185 GLY A O     1 
ATOM   1459 N  N     . LEU A 1 194 ? 27.988 -15.442 25.425 1.00 10.50 ? 186 LEU A N     1 
ATOM   1460 C  CA    . LEU A 1 194 ? 26.848 -15.175 26.297 1.00 10.01 ? 186 LEU A CA    1 
ATOM   1461 C  C     . LEU A 1 194 ? 26.365 -16.439 26.995 1.00 9.87  ? 186 LEU A C     1 
ATOM   1462 O  O     . LEU A 1 194 ? 26.109 -16.435 28.208 1.00 10.42 ? 186 LEU A O     1 
ATOM   1463 C  CB    . LEU A 1 194 ? 25.718 -14.579 25.467 1.00 10.76 ? 186 LEU A CB    1 
ATOM   1464 C  CG    . LEU A 1 194 ? 24.372 -14.392 26.161 1.00 11.06 ? 186 LEU A CG    1 
ATOM   1465 C  CD1   . LEU A 1 194 ? 24.477 -13.429 27.330 1.00 12.13 ? 186 LEU A CD1   1 
ATOM   1466 C  CD2   . LEU A 1 194 ? 23.319 -13.939 25.173 1.00 11.94 ? 186 LEU A CD2   1 
ATOM   1467 N  N     . PHE A 1 195 ? 26.207 -17.531 26.248 1.00 10.13 ? 187 PHE A N     1 
ATOM   1468 C  CA    . PHE A 1 195 ? 25.531 -18.694 26.811 1.00 10.49 ? 187 PHE A CA    1 
ATOM   1469 C  C     . PHE A 1 195 ? 26.268 -19.284 28.009 1.00 10.32 ? 187 PHE A C     1 
ATOM   1470 O  O     . PHE A 1 195 ? 25.601 -19.648 28.992 1.00 10.53 ? 187 PHE A O     1 
ATOM   1471 C  CB    . PHE A 1 195 ? 25.268 -19.744 25.724 1.00 11.26 ? 187 PHE A CB    1 
ATOM   1472 C  CG    . PHE A 1 195 ? 24.435 -19.255 24.544 1.00 10.08 ? 187 PHE A CG    1 
ATOM   1473 C  CD1   . PHE A 1 195 ? 23.563 -18.184 24.650 1.00 12.53 ? 187 PHE A CD1   1 
ATOM   1474 C  CD2   . PHE A 1 195 ? 24.531 -19.875 23.316 1.00 11.07 ? 187 PHE A CD2   1 
ATOM   1475 C  CE1   . PHE A 1 195 ? 22.811 -17.778 23.554 1.00 12.22 ? 187 PHE A CE1   1 
ATOM   1476 C  CE2   . PHE A 1 195 ? 23.781 -19.476 22.236 1.00 11.77 ? 187 PHE A CE2   1 
ATOM   1477 C  CZ    . PHE A 1 195 ? 22.920 -18.433 22.352 1.00 11.65 ? 187 PHE A CZ    1 
ATOM   1478 N  N     . PRO A 1 196 ? 27.600 -19.407 28.014 1.00 10.46 ? 188 PRO A N     1 
ATOM   1479 C  CA    . PRO A 1 196 ? 28.262 -19.965 29.200 1.00 10.63 ? 188 PRO A CA    1 
ATOM   1480 C  C     . PRO A 1 196 ? 28.185 -19.077 30.417 1.00 11.10 ? 188 PRO A C     1 
ATOM   1481 O  O     . PRO A 1 196 ? 28.218 -19.587 31.540 1.00 11.46 ? 188 PRO A O     1 
ATOM   1482 C  CB    . PRO A 1 196 ? 29.700 -20.182 28.725 1.00 10.49 ? 188 PRO A CB    1 
ATOM   1483 C  CG    . PRO A 1 196 ? 29.565 -20.329 27.230 1.00 10.75 ? 188 PRO A CG    1 
ATOM   1484 C  CD    . PRO A 1 196 ? 28.525 -19.318 26.872 1.00 10.88 ? 188 PRO A CD    1 
ATOM   1485 N  N     . ILE A 1 197 ? 28.092 -17.757 30.236 1.00 10.70 ? 189 ILE A N     1 
ATOM   1486 C  CA    . ILE A 1 197 ? 27.900 -16.865 31.375 1.00 10.45 ? 189 ILE A CA    1 
ATOM   1487 C  C     . ILE A 1 197 ? 26.525 -17.086 31.994 1.00 10.12 ? 189 ILE A C     1 
ATOM   1488 O  O     . ILE A 1 197 ? 26.379 -17.150 33.225 1.00 10.80 ? 189 ILE A O     1 
ATOM   1489 C  CB    . ILE A 1 197 ? 28.113 -15.407 30.931 1.00 10.74 ? 189 ILE A CB    1 
ATOM   1490 C  CG1   . ILE A 1 197 ? 29.560 -15.197 30.478 1.00 11.25 ? 189 ILE A CG1   1 
ATOM   1491 C  CG2   . ILE A 1 197 ? 27.750 -14.449 32.046 1.00 11.23 ? 189 ILE A CG2   1 
ATOM   1492 C  CD1   . ILE A 1 197 ? 29.829 -13.808 29.942 1.00 11.90 ? 189 ILE A CD1   1 
ATOM   1493 N  N     . ALA A 1 198 ? 25.490 -17.199 31.164 1.00 10.53 ? 190 ALA A N     1 
ATOM   1494 C  CA    . ALA A 1 198 ? 24.175 -17.549 31.694 1.00 11.13 ? 190 ALA A CA    1 
ATOM   1495 C  C     . ALA A 1 198 ? 24.240 -18.847 32.491 1.00 11.17 ? 190 ALA A C     1 
ATOM   1496 O  O     . ALA A 1 198 ? 23.707 -18.925 33.600 1.00 11.65 ? 190 ALA A O     1 
ATOM   1497 C  CB    . ALA A 1 198 ? 23.169 -17.660 30.556 1.00 11.54 ? 190 ALA A CB    1 
ATOM   1498 N  N     . ASP A 1 199 ? 24.948 -19.858 31.972 1.00 10.88 ? 191 ASP A N     1 
ATOM   1499 C  CA    . ASP A 1 199 ? 25.089 -21.120 32.701 1.00 11.91 ? 191 ASP A CA    1 
ATOM   1500 C  C     . ASP A 1 199 ? 25.724 -20.899 34.070 1.00 12.15 ? 191 ASP A C     1 
ATOM   1501 O  O     . ASP A 1 199 ? 25.269 -21.451 35.075 1.00 13.37 ? 191 ASP A O     1 
ATOM   1502 C  CB    . ASP A 1 199 ? 25.971 -22.101 31.931 1.00 12.80 ? 191 ASP A CB    1 
ATOM   1503 C  CG    . ASP A 1 199 ? 25.333 -22.658 30.686 1.00 13.80 ? 191 ASP A CG    1 
ATOM   1504 O  OD1   . ASP A 1 199 ? 24.097 -22.611 30.551 1.00 15.21 ? 191 ASP A OD1   1 
ATOM   1505 O  OD2   . ASP A 1 199 ? 26.093 -23.203 29.851 1.00 13.83 ? 191 ASP A OD2   1 
ATOM   1506 N  N     . TYR A 1 200 ? 26.814 -20.123 34.115 1.00 11.86 ? 192 TYR A N     1 
ATOM   1507 C  CA    . TYR A 1 200 ? 27.520 -19.888 35.371 1.00 11.93 ? 192 TYR A CA    1 
ATOM   1508 C  C     . TYR A 1 200 ? 26.577 -19.360 36.439 1.00 11.97 ? 192 TYR A C     1 
ATOM   1509 O  O     . TYR A 1 200 ? 26.676 -19.736 37.615 1.00 13.18 ? 192 TYR A O     1 
ATOM   1510 C  CB    . TYR A 1 200 ? 28.650 -18.889 35.129 1.00 12.16 ? 192 TYR A CB    1 
ATOM   1511 C  CG    . TYR A 1 200 ? 29.479 -18.586 36.356 1.00 12.25 ? 192 TYR A CG    1 
ATOM   1512 C  CD1   . TYR A 1 200 ? 30.607 -19.335 36.653 1.00 12.70 ? 192 TYR A CD1   1 
ATOM   1513 C  CD2   . TYR A 1 200 ? 29.167 -17.524 37.198 1.00 12.87 ? 192 TYR A CD2   1 
ATOM   1514 C  CE1   . TYR A 1 200 ? 31.377 -19.061 37.758 1.00 13.61 ? 192 TYR A CE1   1 
ATOM   1515 C  CE2   . TYR A 1 200 ? 29.927 -17.250 38.319 1.00 14.36 ? 192 TYR A CE2   1 
ATOM   1516 C  CZ    . TYR A 1 200 ? 31.039 -18.011 38.584 1.00 14.55 ? 192 TYR A CZ    1 
ATOM   1517 O  OH    . TYR A 1 200 ? 31.808 -17.743 39.692 1.00 17.03 ? 192 TYR A OH    1 
ATOM   1518 N  N     . TYR A 1 201 ? 25.669 -18.470 36.050 1.00 12.39 ? 193 TYR A N     1 
ATOM   1519 C  CA    . TYR A 1 201 ? 24.735 -17.840 36.981 1.00 13.38 ? 193 TYR A CA    1 
ATOM   1520 C  C     . TYR A 1 201 ? 23.428 -18.610 37.148 1.00 14.30 ? 193 TYR A C     1 
ATOM   1521 O  O     . TYR A 1 201 ? 22.537 -18.132 37.850 1.00 15.27 ? 193 TYR A O     1 
ATOM   1522 C  CB    . TYR A 1 201 ? 24.489 -16.373 36.580 1.00 13.07 ? 193 TYR A CB    1 
ATOM   1523 C  CG    . TYR A 1 201 ? 25.710 -15.548 36.865 1.00 12.86 ? 193 TYR A CG    1 
ATOM   1524 C  CD1   . TYR A 1 201 ? 26.025 -15.197 38.168 1.00 14.26 ? 193 TYR A CD1   1 
ATOM   1525 C  CD2   . TYR A 1 201 ? 26.587 -15.178 35.856 1.00 12.86 ? 193 TYR A CD2   1 
ATOM   1526 C  CE1   . TYR A 1 201 ? 27.175 -14.491 38.469 1.00 14.34 ? 193 TYR A CE1   1 
ATOM   1527 C  CE2   . TYR A 1 201 ? 27.739 -14.443 36.147 1.00 13.04 ? 193 TYR A CE2   1 
ATOM   1528 C  CZ    . TYR A 1 201 ? 28.024 -14.113 37.460 1.00 13.85 ? 193 TYR A CZ    1 
ATOM   1529 O  OH    . TYR A 1 201 ? 29.172 -13.408 37.772 1.00 14.59 ? 193 TYR A OH    1 
ATOM   1530 N  N     . GLY A 1 202 ? 23.311 -19.807 36.576 1.00 13.91 ? 194 GLY A N     1 
ATOM   1531 C  CA    . GLY A 1 202 ? 22.058 -20.538 36.694 1.00 14.27 ? 194 GLY A CA    1 
ATOM   1532 C  C     . GLY A 1 202 ? 20.901 -19.826 36.036 1.00 14.53 ? 194 GLY A C     1 
ATOM   1533 O  O     . GLY A 1 202 ? 19.755 -19.954 36.485 1.00 16.16 ? 194 GLY A O     1 
ATOM   1534 N  N     . ALA A 1 203 ? 21.176 -19.087 34.969 1.00 14.02 ? 195 ALA A N     1 
ATOM   1535 C  CA    . ALA A 1 203 ? 20.229 -18.210 34.296 1.00 13.59 ? 195 ALA A CA    1 
ATOM   1536 C  C     . ALA A 1 203 ? 20.060 -18.674 32.847 1.00 14.05 ? 195 ALA A C     1 
ATOM   1537 O  O     . ALA A 1 203 ? 20.605 -19.706 32.429 1.00 14.98 ? 195 ALA A O     1 
ATOM   1538 C  CB    . ALA A 1 203 ? 20.719 -16.765 34.412 1.00 14.85 ? 195 ALA A CB    1 
ATOM   1539 N  N     . ARG A 1 204 ? 19.321 -17.888 32.071 1.00 14.07 ? 196 ARG A N     1 
ATOM   1540 C  CA    . ARG A 1 204 ? 18.889 -18.290 30.744 1.00 14.66 ? 196 ARG A CA    1 
ATOM   1541 C  C     . ARG A 1 204 ? 19.351 -17.296 29.699 1.00 12.97 ? 196 ARG A C     1 
ATOM   1542 O  O     . ARG A 1 204 ? 19.360 -16.084 29.938 1.00 12.62 ? 196 ARG A O     1 
ATOM   1543 C  CB    . ARG A 1 204 ? 17.359 -18.380 30.694 1.00 17.17 ? 196 ARG A CB    1 
ATOM   1544 C  CG    . ARG A 1 204 ? 16.861 -19.450 31.610 1.00 20.51 ? 196 ARG A CG    1 
ATOM   1545 C  CD    . ARG A 1 204 ? 15.432 -19.701 31.391 1.00 23.45 ? 196 ARG A CD    1 
ATOM   1546 N  NE    . ARG A 1 204 ? 14.662 -18.491 31.600 1.00 24.97 ? 196 ARG A NE    1 
ATOM   1547 C  CZ    . ARG A 1 204 ? 13.345 -18.473 31.656 1.00 26.23 ? 196 ARG A CZ    1 
ATOM   1548 N  NH1   . ARG A 1 204 ? 12.635 -19.583 31.532 1.00 26.44 ? 196 ARG A NH1   1 
ATOM   1549 N  NH2   . ARG A 1 204 ? 12.727 -17.315 31.841 1.00 26.23 ? 196 ARG A NH2   1 
ATOM   1550 N  N     . ALA A 1 205 ? 19.663 -17.813 28.515 1.00 12.00 ? 197 ALA A N     1 
ATOM   1551 C  CA    . ALA A 1 205 ? 20.014 -16.978 27.384 1.00 11.73 ? 197 ALA A CA    1 
ATOM   1552 C  C     . ALA A 1 205 ? 19.624 -17.662 26.086 1.00 11.17 ? 197 ALA A C     1 
ATOM   1553 O  O     . ALA A 1 205 ? 19.517 -18.887 26.004 1.00 12.36 ? 197 ALA A O     1 
ATOM   1554 C  CB    . ALA A 1 205 ? 21.507 -16.644 27.362 1.00 12.90 ? 197 ALA A CB    1 
ATOM   1555 N  N     . GLY A 1 206 ? 19.410 -16.845 25.066 1.00 11.32 ? 198 GLY A N     1 
ATOM   1556 C  CA    . GLY A 1 206 ? 19.245 -17.307 23.710 1.00 11.72 ? 198 GLY A CA    1 
ATOM   1557 C  C     . GLY A 1 206 ? 19.641 -16.217 22.741 1.00 10.83 ? 198 GLY A C     1 
ATOM   1558 O  O     . GLY A 1 206 ? 20.095 -15.135 23.130 1.00 11.14 ? 198 GLY A O     1 
ATOM   1559 N  N     . CYS A 1 207 ? 19.481 -16.517 21.455 1.00 11.08 ? 199 CYS A N     1 
ATOM   1560 C  CA    . CYS A 1 207 ? 19.835 -15.561 20.415 1.00 11.59 ? 199 CYS A CA    1 
ATOM   1561 C  C     . CYS A 1 207 ? 18.956 -15.769 19.195 1.00 11.59 ? 199 CYS A C     1 
ATOM   1562 O  O     . CYS A 1 207 ? 18.654 -16.902 18.813 1.00 11.75 ? 199 CYS A O     1 
ATOM   1563 C  CB    . CYS A 1 207 ? 21.305 -15.739 20.015 1.00 11.76 ? 199 CYS A CB    1 
ATOM   1564 S  SG    . CYS A 1 207 ? 21.878 -14.633 18.682 1.00 13.97 ? 199 CYS A SG    1 
ATOM   1565 N  N     . ILE A 1 208 ? 18.536 -14.661 18.601 1.00 11.74 ? 200 ILE A N     1 
ATOM   1566 C  CA    . ILE A 1 208 ? 17.853 -14.652 17.318 1.00 12.13 ? 200 ILE A CA    1 
ATOM   1567 C  C     . ILE A 1 208 ? 18.534 -13.597 16.456 1.00 12.19 ? 200 ILE A C     1 
ATOM   1568 O  O     . ILE A 1 208 ? 18.911 -12.534 16.956 1.00 13.44 ? 200 ILE A O     1 
ATOM   1569 C  CB    . ILE A 1 208 ? 16.339 -14.395 17.517 1.00 12.84 ? 200 ILE A CB    1 
ATOM   1570 C  CG1   . ILE A 1 208 ? 15.585 -14.507 16.194 1.00 13.65 ? 200 ILE A CG1   1 
ATOM   1571 C  CG2   . ILE A 1 208 ? 16.095 -13.047 18.209 1.00 13.50 ? 200 ILE A CG2   1 
ATOM   1572 C  CD1   . ILE A 1 208 ? 14.072 -14.540 16.369 1.00 14.68 ? 200 ILE A CD1   1 
ATOM   1573 N  N     . CYS A 1 209 ? 18.746 -13.903 15.178 1.00 13.21 ? 201 CYS A N     1 
ATOM   1574 C  CA    A CYS A 1 209 ? 19.462 -13.021 14.264 0.62 14.19 ? 201 CYS A CA    1 
ATOM   1575 C  CA    B CYS A 1 209 ? 19.402 -12.954 14.294 0.38 14.26 ? 201 CYS A CA    1 
ATOM   1576 C  C     . CYS A 1 209 ? 18.808 -13.049 12.897 1.00 15.46 ? 201 CYS A C     1 
ATOM   1577 O  O     . CYS A 1 209 ? 18.244 -14.059 12.504 1.00 18.67 ? 201 CYS A O     1 
ATOM   1578 C  CB    A CYS A 1 209 ? 20.891 -13.484 13.988 0.62 16.29 ? 201 CYS A CB    1 
ATOM   1579 C  CB    B CYS A 1 209 ? 20.937 -13.116 14.283 0.38 15.31 ? 201 CYS A CB    1 
ATOM   1580 S  SG    A CYS A 1 209 ? 22.019 -13.321 15.335 0.62 17.58 ? 201 CYS A SG    1 
ATOM   1581 S  SG    B CYS A 1 209 ? 21.553 -14.816 14.287 0.38 15.22 ? 201 CYS A SG    1 
ATOM   1582 N  N     . THR A 1 210 ? 18.922 -11.955 12.155 1.00 15.94 ? 202 THR A N     1 
ATOM   1583 C  CA    A THR A 1 210 ? 18.498 -11.914 10.765 0.63 16.82 ? 202 THR A CA    1 
ATOM   1584 C  CA    B THR A 1 210 ? 18.494 -11.910 10.765 0.37 17.01 ? 202 THR A CA    1 
ATOM   1585 C  C     . THR A 1 210 ? 19.712 -11.863 9.850  1.00 16.12 ? 202 THR A C     1 
ATOM   1586 O  O     . THR A 1 210 ? 20.700 -11.180 10.144 1.00 15.23 ? 202 THR A O     1 
ATOM   1587 C  CB    A THR A 1 210 ? 17.619 -10.696 10.510 0.63 19.52 ? 202 THR A CB    1 
ATOM   1588 C  CB    B THR A 1 210 ? 17.581 -10.703 10.510 0.37 19.79 ? 202 THR A CB    1 
ATOM   1589 O  OG1   A THR A 1 210 ? 18.320 -9.515  10.914 0.63 20.73 ? 202 THR A OG1   1 
ATOM   1590 O  OG1   B THR A 1 210 ? 17.319 -10.580 9.105  0.37 21.48 ? 202 THR A OG1   1 
ATOM   1591 C  CG2   A THR A 1 210 ? 16.336 -10.824 11.287 0.63 20.18 ? 202 THR A CG2   1 
ATOM   1592 C  CG2   B THR A 1 210 ? 18.216 -9.426  11.032 0.37 20.48 ? 202 THR A CG2   1 
ATOM   1593 N  N     . VAL A 1 211 ? 19.624 -12.575 8.734  1.00 15.20 ? 203 VAL A N     1 
ATOM   1594 C  CA    . VAL A 1 211 ? 20.729 -12.677 7.787  1.00 15.76 ? 203 VAL A CA    1 
ATOM   1595 C  C     . VAL A 1 211 ? 20.795 -11.402 6.955  1.00 16.48 ? 203 VAL A C     1 
ATOM   1596 O  O     . VAL A 1 211 ? 19.863 -11.080 6.209  1.00 17.44 ? 203 VAL A O     1 
ATOM   1597 C  CB    . VAL A 1 211 ? 20.559 -13.913 6.892  1.00 15.67 ? 203 VAL A CB    1 
ATOM   1598 C  CG1   . VAL A 1 211 ? 21.726 -14.043 5.932  1.00 16.48 ? 203 VAL A CG1   1 
ATOM   1599 C  CG2   . VAL A 1 211 ? 20.416 -15.173 7.730  1.00 16.14 ? 203 VAL A CG2   1 
ATOM   1600 N  N     . SER A 1 212 ? 21.898 -10.670 7.088  1.00 16.67 ? 204 SER A N     1 
ATOM   1601 C  CA    . SER A 1 212 ? 22.145 -9.472  6.292  1.00 18.67 ? 204 SER A CA    1 
ATOM   1602 C  C     . SER A 1 212 ? 22.877 -9.763  4.995  1.00 18.89 ? 204 SER A C     1 
ATOM   1603 O  O     . SER A 1 212 ? 22.670 -9.062  4.004  1.00 19.79 ? 204 SER A O     1 
ATOM   1604 C  CB    . SER A 1 212 ? 23.025 -8.490  7.070  1.00 21.87 ? 204 SER A CB    1 
ATOM   1605 O  OG    . SER A 1 212 ? 22.361 -7.969  8.198  1.00 24.87 ? 204 SER A OG    1 
ATOM   1606 N  N     . ASP A 1 213 ? 23.736 -10.775 4.984  1.00 18.35 ? 205 ASP A N     1 
ATOM   1607 C  CA    . ASP A 1 213 ? 24.621 -11.016 3.860  1.00 18.15 ? 205 ASP A CA    1 
ATOM   1608 C  C     . ASP A 1 213 ? 24.830 -12.514 3.718  1.00 16.90 ? 205 ASP A C     1 
ATOM   1609 O  O     . ASP A 1 213 ? 24.992 -13.218 4.718  1.00 16.91 ? 205 ASP A O     1 
ATOM   1610 C  CB    . ASP A 1 213 ? 25.988 -10.377 4.122  1.00 20.54 ? 205 ASP A CB    1 
ATOM   1611 C  CG    . ASP A 1 213 ? 25.942 -8.867  4.090  1.00 23.08 ? 205 ASP A CG    1 
ATOM   1612 O  OD1   . ASP A 1 213 ? 25.963 -8.300  2.979  1.00 23.34 ? 205 ASP A OD1   1 
ATOM   1613 O  OD2   . ASP A 1 213 ? 25.871 -8.246  5.174  1.00 24.90 ? 205 ASP A OD2   1 
ATOM   1614 N  N     . HIS A 1 214 ? 24.826 -12.995 2.477  1.00 17.19 ? 206 HIS A N     1 
ATOM   1615 C  CA    . HIS A 1 214 ? 25.281 -14.347 2.180  1.00 17.62 ? 206 HIS A CA    1 
ATOM   1616 C  C     . HIS A 1 214 ? 26.753 -14.275 1.798  1.00 17.61 ? 206 HIS A C     1 
ATOM   1617 O  O     . HIS A 1 214 ? 27.112 -13.681 0.775  1.00 18.75 ? 206 HIS A O     1 
ATOM   1618 C  CB    . HIS A 1 214 ? 24.471 -15.012 1.071  1.00 18.32 ? 206 HIS A CB    1 
ATOM   1619 C  CG    . HIS A 1 214 ? 24.531 -16.503 1.128  1.00 18.09 ? 206 HIS A CG    1 
ATOM   1620 N  ND1   . HIS A 1 214 ? 25.692 -17.208 0.890  1.00 18.80 ? 206 HIS A ND1   1 
ATOM   1621 C  CD2   . HIS A 1 214 ? 23.589 -17.421 1.451  1.00 18.74 ? 206 HIS A CD2   1 
ATOM   1622 C  CE1   . HIS A 1 214 ? 25.456 -18.500 1.047  1.00 19.56 ? 206 HIS A CE1   1 
ATOM   1623 N  NE2   . HIS A 1 214 ? 24.191 -18.654 1.394  1.00 19.59 ? 206 HIS A NE2   1 
ATOM   1624 N  N     . ILE A 1 215 ? 27.599 -14.879 2.631  1.00 17.56 ? 207 ILE A N     1 
ATOM   1625 C  CA    . ILE A 1 215 ? 29.043 -14.778 2.469  1.00 19.06 ? 207 ILE A CA    1 
ATOM   1626 C  C     . ILE A 1 215 ? 29.515 -15.478 1.203  1.00 20.99 ? 207 ILE A C     1 
ATOM   1627 O  O     . ILE A 1 215 ? 30.555 -15.108 0.642  1.00 22.04 ? 207 ILE A O     1 
ATOM   1628 C  CB    . ILE A 1 215 ? 29.707 -15.329 3.744  1.00 19.46 ? 207 ILE A CB    1 
ATOM   1629 C  CG1   . ILE A 1 215 ? 29.402 -14.413 4.928  1.00 19.45 ? 207 ILE A CG1   1 
ATOM   1630 C  CG2   . ILE A 1 215 ? 31.211 -15.482 3.559  1.00 20.01 ? 207 ILE A CG2   1 
ATOM   1631 C  CD1   . ILE A 1 215 ? 29.591 -15.055 6.279  1.00 20.12 ? 207 ILE A CD1   1 
ATOM   1632 N  N     . ILE A 1 216 ? 28.775 -16.479 0.727  1.00 22.54 ? 208 ILE A N     1 
ATOM   1633 C  CA    . ILE A 1 216 ? 29.183 -17.242 -0.453 1.00 24.11 ? 208 ILE A CA    1 
ATOM   1634 C  C     . ILE A 1 216 ? 28.638 -16.629 -1.734 1.00 25.18 ? 208 ILE A C     1 
ATOM   1635 O  O     . ILE A 1 216 ? 29.380 -16.423 -2.696 1.00 26.43 ? 208 ILE A O     1 
ATOM   1636 C  CB    . ILE A 1 216 ? 28.751 -18.718 -0.327 1.00 24.67 ? 208 ILE A CB    1 
ATOM   1637 C  CG1   . ILE A 1 216 ? 29.304 -19.331 0.955  1.00 24.71 ? 208 ILE A CG1   1 
ATOM   1638 C  CG2   . ILE A 1 216 ? 29.211 -19.507 -1.549 1.00 25.71 ? 208 ILE A CG2   1 
ATOM   1639 C  CD1   . ILE A 1 216 ? 30.796 -19.229 1.076  1.00 24.41 ? 208 ILE A CD1   1 
ATOM   1640 N  N     . THR A 1 217 ? 27.329 -16.366 -1.785 1.00 25.61 ? 209 THR A N     1 
ATOM   1641 C  CA    . THR A 1 217 ? 26.712 -15.890 -3.019 1.00 26.99 ? 209 THR A CA    1 
ATOM   1642 C  C     . THR A 1 217 ? 26.875 -14.392 -3.207 1.00 27.60 ? 209 THR A C     1 
ATOM   1643 O  O     . THR A 1 217 ? 26.666 -13.896 -4.319 1.00 28.64 ? 209 THR A O     1 
ATOM   1644 C  CB    . THR A 1 217 ? 25.216 -16.214 -3.041 1.00 27.63 ? 209 THR A CB    1 
ATOM   1645 O  OG1   . THR A 1 217 ? 24.544 -15.418 -2.058 1.00 27.39 ? 209 THR A OG1   1 
ATOM   1646 C  CG2   . THR A 1 217 ? 24.972 -17.681 -2.753 1.00 28.53 ? 209 THR A CG2   1 
ATOM   1647 N  N     . HIS A 1 218 ? 27.228 -13.667 -2.151 1.00 27.07 ? 210 HIS A N     1 
ATOM   1648 C  CA    . HIS A 1 218 ? 27.407 -12.221 -2.127 1.00 27.68 ? 210 HIS A CA    1 
ATOM   1649 C  C     . HIS A 1 218 ? 26.072 -11.476 -2.087 1.00 26.87 ? 210 HIS A C     1 
ATOM   1650 O  O     . HIS A 1 218 ? 26.071 -10.245 -2.155 1.00 27.20 ? 210 HIS A O     1 
ATOM   1651 C  CB    . HIS A 1 218 ? 28.250 -11.688 -3.300 1.00 29.95 ? 210 HIS A CB    1 
ATOM   1652 C  CG    . HIS A 1 218 ? 29.636 -12.258 -3.374 1.00 32.39 ? 210 HIS A CG    1 
ATOM   1653 N  ND1   . HIS A 1 218 ? 30.169 -13.072 -2.396 1.00 33.26 ? 210 HIS A ND1   1 
ATOM   1654 C  CD2   . HIS A 1 218 ? 30.602 -12.118 -4.312 1.00 33.23 ? 210 HIS A CD2   1 
ATOM   1655 C  CE1   . HIS A 1 218 ? 31.403 -13.410 -2.731 1.00 33.54 ? 210 HIS A CE1   1 
ATOM   1656 N  NE2   . HIS A 1 218 ? 31.688 -12.846 -3.891 1.00 33.98 ? 210 HIS A NE2   1 
ATOM   1657 N  N     . GLU A 1 219 ? 24.943 -12.170 -1.986 1.00 25.92 ? 211 GLU A N     1 
ATOM   1658 C  CA    . GLU A 1 219 ? 23.669 -11.487 -1.818 1.00 26.04 ? 211 GLU A CA    1 
ATOM   1659 C  C     . GLU A 1 219 ? 23.693 -10.648 -0.544 1.00 25.18 ? 211 GLU A C     1 
ATOM   1660 O  O     . GLU A 1 219 ? 24.324 -11.007 0.454  1.00 23.98 ? 211 GLU A O     1 
ATOM   1661 C  CB    . GLU A 1 219 ? 22.544 -12.517 -1.753 1.00 28.33 ? 211 GLU A CB    1 
ATOM   1662 C  CG    . GLU A 1 219 ? 22.295 -13.225 -3.083 1.00 30.86 ? 211 GLU A CG    1 
ATOM   1663 C  CD    . GLU A 1 219 ? 21.559 -14.545 -2.930 1.00 33.29 ? 211 GLU A CD    1 
ATOM   1664 O  OE1   . GLU A 1 219 ? 21.976 -15.376 -2.093 1.00 34.25 ? 211 GLU A OE1   1 
ATOM   1665 O  OE2   . GLU A 1 219 ? 20.559 -14.751 -3.652 1.00 35.06 ? 211 GLU A OE2   1 
ATOM   1666 N  N     . SER A 1 220 ? 22.992 -9.519  -0.577 1.00 25.93 ? 212 SER A N     1 
ATOM   1667 C  CA    . SER A 1 220 ? 23.034 -8.573  0.529  1.00 25.91 ? 212 SER A CA    1 
ATOM   1668 C  C     . SER A 1 220 ? 21.687 -7.875  0.628  1.00 25.93 ? 212 SER A C     1 
ATOM   1669 O  O     . SER A 1 220 ? 21.141 -7.432  -0.385 1.00 27.58 ? 212 SER A O     1 
ATOM   1670 C  CB    . SER A 1 220 ? 24.153 -7.549  0.300  1.00 26.86 ? 212 SER A CB    1 
ATOM   1671 O  OG    . SER A 1 220 ? 24.361 -6.725  1.436  1.00 27.61 ? 212 SER A OG    1 
ATOM   1672 N  N     . ALA A 1 221 ? 21.158 -7.790  1.846  1.00 24.60 ? 213 ALA A N     1 
ATOM   1673 C  CA    . ALA A 1 221 ? 19.902 -7.093  2.078  1.00 24.51 ? 213 ALA A CA    1 
ATOM   1674 C  C     . ALA A 1 221 ? 20.111 -5.588  1.960  1.00 24.21 ? 213 ALA A C     1 
ATOM   1675 O  O     . ALA A 1 221 ? 21.099 -5.042  2.454  1.00 24.50 ? 213 ALA A O     1 
ATOM   1676 C  CB    . ALA A 1 221 ? 19.385 -7.427  3.477  1.00 25.17 ? 213 ALA A CB    1 
ATOM   1677 N  N     . THR A 1 222 ? 19.171 -4.915  1.298  1.00 23.67 ? 214 THR A N     1 
ATOM   1678 C  CA    . THR A 1 222 ? 19.208 -3.464  1.206  1.00 23.54 ? 214 THR A CA    1 
ATOM   1679 C  C     . THR A 1 222 ? 18.876 -2.867  2.568  1.00 23.14 ? 214 THR A C     1 
ATOM   1680 O  O     . THR A 1 222 ? 18.401 -3.566  3.465  1.00 22.38 ? 214 THR A O     1 
ATOM   1681 C  CB    . THR A 1 222 ? 18.161 -2.968  0.215  1.00 23.70 ? 214 THR A CB    1 
ATOM   1682 O  OG1   . THR A 1 222 ? 16.862 -3.251  0.744  1.00 23.64 ? 214 THR A OG1   1 
ATOM   1683 C  CG2   . THR A 1 222 ? 18.329 -3.629  -1.155 1.00 24.78 ? 214 THR A CG2   1 
ATOM   1684 N  N     . PRO A 1 223 ? 19.086 -1.565  2.755  1.00 24.03 ? 215 PRO A N     1 
ATOM   1685 C  CA    . PRO A 1 223 ? 18.727 -0.972  4.054  1.00 23.72 ? 215 PRO A CA    1 
ATOM   1686 C  C     . PRO A 1 223 ? 17.267 -1.186  4.424  1.00 23.49 ? 215 PRO A C     1 
ATOM   1687 O  O     . PRO A 1 223 ? 16.960 -1.491  5.582  1.00 24.07 ? 215 PRO A O     1 
ATOM   1688 C  CB    . PRO A 1 223 ? 19.090 0.510   3.877  1.00 24.59 ? 215 PRO A CB    1 
ATOM   1689 C  CG    . PRO A 1 223 ? 20.138 0.515   2.810  1.00 24.95 ? 215 PRO A CG    1 
ATOM   1690 C  CD    . PRO A 1 223 ? 19.776 -0.601  1.875  1.00 24.42 ? 215 PRO A CD    1 
ATOM   1691 N  N     . GLU A 1 224 ? 16.357 -1.057  3.455  1.00 23.69 ? 216 GLU A N     1 
ATOM   1692 C  CA    . GLU A 1 224 ? 14.941 -1.258  3.729  1.00 23.83 ? 216 GLU A CA    1 
ATOM   1693 C  C     . GLU A 1 224 ? 14.653 -2.709  4.080  1.00 22.91 ? 216 GLU A C     1 
ATOM   1694 O  O     . GLU A 1 224 ? 13.877 -2.991  5.001  1.00 23.26 ? 216 GLU A O     1 
ATOM   1695 C  CB    . GLU A 1 224 ? 14.118 -0.818  2.516  1.00 25.18 ? 216 GLU A CB    1 
ATOM   1696 C  CG    . GLU A 1 224 ? 14.143 0.687   2.260  1.00 27.33 ? 216 GLU A CG    1 
ATOM   1697 C  CD    . GLU A 1 224 ? 15.257 1.168   1.336  1.00 27.89 ? 216 GLU A CD    1 
ATOM   1698 O  OE1   . GLU A 1 224 ? 16.312 0.480   1.207  1.00 27.52 ? 216 GLU A OE1   1 
ATOM   1699 O  OE2   . GLU A 1 224 ? 15.053 2.271   0.757  1.00 27.58 ? 216 GLU A OE2   1 
ATOM   1700 N  N     . GLU A 1 225 ? 15.289 -3.646  3.375  1.00 21.58 ? 217 GLU A N     1 
ATOM   1701 C  CA    . GLU A 1 225 ? 15.105 -5.057  3.699  1.00 21.71 ? 217 GLU A CA    1 
ATOM   1702 C  C     . GLU A 1 225 ? 15.627 -5.373  5.093  1.00 21.25 ? 217 GLU A C     1 
ATOM   1703 O  O     . GLU A 1 225 ? 15.018 -6.155  5.831  1.00 21.39 ? 217 GLU A O     1 
ATOM   1704 C  CB    . GLU A 1 225 ? 15.790 -5.919  2.645  1.00 22.42 ? 217 GLU A CB    1 
ATOM   1705 C  CG    . GLU A 1 225 ? 15.055 -5.914  1.332  1.00 23.54 ? 217 GLU A CG    1 
ATOM   1706 C  CD    . GLU A 1 225 ? 15.831 -6.534  0.196  1.00 25.69 ? 217 GLU A CD    1 
ATOM   1707 O  OE1   . GLU A 1 225 ? 17.059 -6.747  0.333  1.00 26.11 ? 217 GLU A OE1   1 
ATOM   1708 O  OE2   . GLU A 1 225 ? 15.192 -6.787  -0.855 1.00 27.57 ? 217 GLU A OE2   1 
ATOM   1709 N  N     . ARG A 1 226 ? 16.749 -4.764  5.478  1.00 22.02 ? 218 ARG A N     1 
ATOM   1710 C  CA    . ARG A 1 226 ? 17.272 -4.983  6.822  1.00 22.56 ? 218 ARG A CA    1 
ATOM   1711 C  C     . ARG A 1 226 ? 16.322 -4.431  7.871  1.00 22.70 ? 218 ARG A C     1 
ATOM   1712 O  O     . ARG A 1 226 ? 16.184 -5.009  8.953  1.00 22.31 ? 218 ARG A O     1 
ATOM   1713 C  CB    . ARG A 1 226 ? 18.645 -4.332  6.955  1.00 24.03 ? 218 ARG A CB    1 
ATOM   1714 C  CG    . ARG A 1 226 ? 19.680 -4.993  6.087  1.00 25.41 ? 218 ARG A CG    1 
ATOM   1715 C  CD    . ARG A 1 226 ? 21.033 -4.340  6.198  1.00 27.02 ? 218 ARG A CD    1 
ATOM   1716 N  NE    . ARG A 1 226 ? 21.902 -4.857  5.149  1.00 27.71 ? 218 ARG A NE    1 
ATOM   1717 C  CZ    . ARG A 1 226 ? 23.184 -5.156  5.300  1.00 27.50 ? 218 ARG A CZ    1 
ATOM   1718 N  NH1   . ARG A 1 226 ? 23.796 -5.020  6.467  1.00 27.20 ? 218 ARG A NH1   1 
ATOM   1719 N  NH2   . ARG A 1 226 ? 23.860 -5.640  4.264  1.00 28.13 ? 218 ARG A NH2   1 
ATOM   1720 N  N     . GLN A 1 227 ? 15.659 -3.313  7.574  1.00 23.70 ? 219 GLN A N     1 
ATOM   1721 C  CA    . GLN A 1 227 ? 14.701 -2.752  8.517  1.00 24.63 ? 219 GLN A CA    1 
ATOM   1722 C  C     . GLN A 1 227 ? 13.513 -3.687  8.695  1.00 23.53 ? 219 GLN A C     1 
ATOM   1723 O  O     . GLN A 1 227 ? 13.078 -3.951  9.821  1.00 23.46 ? 219 GLN A O     1 
ATOM   1724 C  CB    . GLN A 1 227 ? 14.239 -1.378  8.026  1.00 28.03 ? 219 GLN A CB    1 
ATOM   1725 C  CG    . GLN A 1 227 ? 13.281 -0.673  8.970  1.00 32.39 ? 219 GLN A CG    1 
ATOM   1726 C  CD    . GLN A 1 227 ? 13.875 -0.442  10.348 1.00 36.48 ? 219 GLN A CD    1 
ATOM   1727 O  OE1   . GLN A 1 227 ? 15.099 -0.438  10.521 1.00 38.67 ? 219 GLN A OE1   1 
ATOM   1728 N  NE2   . GLN A 1 227 ? 13.009 -0.260  11.343 1.00 37.49 ? 219 GLN A NE2   1 
ATOM   1729 N  N     . THR A 1 228 ? 12.973 -4.196  7.588  1.00 22.26 ? 220 THR A N     1 
ATOM   1730 C  CA    . THR A 1 228 ? 11.844 -5.109  7.670  1.00 22.52 ? 220 THR A CA    1 
ATOM   1731 C  C     . THR A 1 228 ? 12.233 -6.385  8.401  1.00 20.53 ? 220 THR A C     1 
ATOM   1732 O  O     . THR A 1 228 ? 11.470 -6.887  9.235  1.00 19.71 ? 220 THR A O     1 
ATOM   1733 C  CB    . THR A 1 228 ? 11.344 -5.425  6.261  1.00 24.69 ? 220 THR A CB    1 
ATOM   1734 O  OG1   . THR A 1 228 ? 10.885 -4.218  5.637  1.00 26.75 ? 220 THR A OG1   1 
ATOM   1735 C  CG2   . THR A 1 228 ? 10.209 -6.441  6.316  1.00 25.65 ? 220 THR A CG2   1 
ATOM   1736 N  N     . SER A 1 229 ? 13.425 -6.913  8.106  1.00 19.70 ? 221 SER A N     1 
ATOM   1737 C  CA    . SER A 1 229 ? 13.907 -8.113  8.776  1.00 20.54 ? 221 SER A CA    1 
ATOM   1738 C  C     . SER A 1 229 ? 14.020 -7.882  10.268 1.00 19.03 ? 221 SER A C     1 
ATOM   1739 O  O     . SER A 1 229 ? 13.611 -8.727  11.074 1.00 17.87 ? 221 SER A O     1 
ATOM   1740 C  CB    . SER A 1 229 ? 15.290 -8.479  8.237  1.00 24.09 ? 221 SER A CB    1 
ATOM   1741 O  OG    . SER A 1 229 ? 15.206 -9.060  6.954  1.00 27.44 ? 221 SER A OG    1 
ATOM   1742 N  N     . PHE A 1 230 ? 14.583 -6.737  10.651 1.00 19.32 ? 222 PHE A N     1 
ATOM   1743 C  CA    A PHE A 1 230 ? 14.726 -6.449  12.069 0.54 20.05 ? 222 PHE A CA    1 
ATOM   1744 C  CA    B PHE A 1 230 ? 14.720 -6.398  12.064 0.46 20.27 ? 222 PHE A CA    1 
ATOM   1745 C  C     . PHE A 1 230 ? 13.362 -6.305  12.732 1.00 20.65 ? 222 PHE A C     1 
ATOM   1746 O  O     . PHE A 1 230 ? 13.175 -6.766  13.857 1.00 20.32 ? 222 PHE A O     1 
ATOM   1747 C  CB    A PHE A 1 230 ? 15.607 -5.215  12.273 0.54 20.75 ? 222 PHE A CB    1 
ATOM   1748 C  CB    B PHE A 1 230 ? 15.435 -5.056  12.206 0.46 21.45 ? 222 PHE A CB    1 
ATOM   1749 C  CG    A PHE A 1 230 ? 16.487 -5.291  13.498 0.54 20.69 ? 222 PHE A CG    1 
ATOM   1750 C  CG    B PHE A 1 230 ? 15.040 -4.295  13.444 0.46 22.26 ? 222 PHE A CG    1 
ATOM   1751 C  CD1   A PHE A 1 230 ? 15.961 -5.057  14.755 0.54 21.41 ? 222 PHE A CD1   1 
ATOM   1752 C  CD1   B PHE A 1 230 ? 15.586 -4.622  14.673 0.46 22.87 ? 222 PHE A CD1   1 
ATOM   1753 C  CD2   A PHE A 1 230 ? 17.839 -5.592  13.390 0.54 21.52 ? 222 PHE A CD2   1 
ATOM   1754 C  CD2   B PHE A 1 230 ? 14.114 -3.265  13.381 0.46 23.25 ? 222 PHE A CD2   1 
ATOM   1755 C  CE1   A PHE A 1 230 ? 16.755 -5.125  15.881 0.54 22.28 ? 222 PHE A CE1   1 
ATOM   1756 C  CE1   B PHE A 1 230 ? 15.220 -3.933  15.813 0.46 23.29 ? 222 PHE A CE1   1 
ATOM   1757 C  CE2   A PHE A 1 230 ? 18.643 -5.659  14.519 0.54 22.23 ? 222 PHE A CE2   1 
ATOM   1758 C  CE2   B PHE A 1 230 ? 13.750 -2.571  14.516 0.46 23.25 ? 222 PHE A CE2   1 
ATOM   1759 C  CZ    A PHE A 1 230 ? 18.096 -5.426  15.766 0.54 22.01 ? 222 PHE A CZ    1 
ATOM   1760 C  CZ    B PHE A 1 230 ? 14.302 -2.906  15.732 0.46 23.22 ? 222 PHE A CZ    1 
ATOM   1761 N  N     . GLN A 1 231 ? 12.395 -5.688  12.049 1.00 21.18 ? 223 GLN A N     1 
ATOM   1762 C  CA    . GLN A 1 231 ? 11.051 -5.575  12.609 1.00 22.78 ? 223 GLN A CA    1 
ATOM   1763 C  C     . GLN A 1 231 ? 10.450 -6.947  12.885 1.00 21.06 ? 223 GLN A C     1 
ATOM   1764 O  O     . GLN A 1 231 ? 9.858  -7.176  13.947 1.00 21.60 ? 223 GLN A O     1 
ATOM   1765 C  CB    . GLN A 1 231 ? 10.164 -4.782  11.653 1.00 25.76 ? 223 GLN A CB    1 
ATOM   1766 C  CG    . GLN A 1 231 ? 10.523 -3.309  11.613 1.00 27.96 ? 223 GLN A CG    1 
ATOM   1767 C  CD    . GLN A 1 231 ? 9.833  -2.518  10.504 1.00 30.85 ? 223 GLN A CD    1 
ATOM   1768 O  OE1   . GLN A 1 231 ? 10.120 -1.336  10.317 1.00 33.77 ? 223 GLN A OE1   1 
ATOM   1769 N  NE2   . GLN A 1 231 ? 8.927  -3.156  9.771  1.00 31.56 ? 223 GLN A NE2   1 
ATOM   1770 N  N     . ASN A 1 232 ? 10.572 -7.869  11.929 1.00 19.40 ? 224 ASN A N     1 
ATOM   1771 C  CA    . ASN A 1 232 ? 10.077 -9.225  12.134 1.00 19.31 ? 224 ASN A CA    1 
ATOM   1772 C  C     . ASN A 1 232 ? 10.787 -9.882  13.306 1.00 16.48 ? 224 ASN A C     1 
ATOM   1773 O  O     . ASN A 1 232 ? 10.157 -10.459 14.194 1.00 16.36 ? 224 ASN A O     1 
ATOM   1774 C  CB    . ASN A 1 232 ? 10.295 -10.052 10.867 1.00 23.12 ? 224 ASN A CB    1 
ATOM   1775 C  CG    . ASN A 1 232 ? 9.325  -9.702  9.771  1.00 27.71 ? 224 ASN A CG    1 
ATOM   1776 O  OD1   . ASN A 1 232 ? 8.240  -9.205  10.037 1.00 30.15 ? 224 ASN A OD1   1 
ATOM   1777 N  ND2   . ASN A 1 232 ? 9.708  -9.971  8.526  1.00 29.47 ? 224 ASN A ND2   1 
ATOM   1778 N  N     . MET A 1 233 ? 12.110 -9.785  13.333 1.00 16.06 ? 225 MET A N     1 
ATOM   1779 C  CA    A MET A 1 233 ? 12.887 -10.434 14.383 0.59 15.75 ? 225 MET A CA    1 
ATOM   1780 C  CA    B MET A 1 233 ? 12.855 -10.461 14.378 0.41 16.18 ? 225 MET A CA    1 
ATOM   1781 C  C     . MET A 1 233 ? 12.568 -9.855  15.752 1.00 15.22 ? 225 MET A C     1 
ATOM   1782 O  O     . MET A 1 233 ? 12.407 -10.589 16.731 1.00 14.63 ? 225 MET A O     1 
ATOM   1783 C  CB    A MET A 1 233 ? 14.378 -10.264 14.103 0.59 15.91 ? 225 MET A CB    1 
ATOM   1784 C  CB    B MET A 1 233 ? 14.332 -10.426 14.011 0.41 17.22 ? 225 MET A CB    1 
ATOM   1785 C  CG    A MET A 1 233 ? 15.236 -10.555 15.321 0.59 16.11 ? 225 MET A CG    1 
ATOM   1786 C  CG    B MET A 1 233 ? 15.216 -11.111 14.995 0.41 18.25 ? 225 MET A CG    1 
ATOM   1787 S  SD    A MET A 1 233 ? 16.999 -10.451 15.006 0.59 17.57 ? 225 MET A SD    1 
ATOM   1788 S  SD    B MET A 1 233 ? 15.787 -9.917  16.188 0.41 18.28 ? 225 MET A SD    1 
ATOM   1789 C  CE    A MET A 1 233 ? 17.192 -8.678  14.816 0.59 18.33 ? 225 MET A CE    1 
ATOM   1790 C  CE    B MET A 1 233 ? 16.848 -8.931  15.118 0.41 19.14 ? 225 MET A CE    1 
ATOM   1791 N  N     . ILE A 1 234 ? 12.482 -8.530  15.850 1.00 14.82 ? 226 ILE A N     1 
ATOM   1792 C  CA    . ILE A 1 234 ? 12.254 -7.926  17.158 1.00 14.97 ? 226 ILE A CA    1 
ATOM   1793 C  C     . ILE A 1 234 ? 10.868 -8.278  17.678 1.00 14.50 ? 226 ILE A C     1 
ATOM   1794 O  O     . ILE A 1 234 ? 10.675 -8.476  18.883 1.00 14.67 ? 226 ILE A O     1 
ATOM   1795 C  CB    . ILE A 1 234 ? 12.513 -6.404  17.123 1.00 16.26 ? 226 ILE A CB    1 
ATOM   1796 C  CG1   . ILE A 1 234 ? 12.713 -5.900  18.550 1.00 19.03 ? 226 ILE A CG1   1 
ATOM   1797 C  CG2   . ILE A 1 234 ? 11.384 -5.612  16.429 1.00 18.17 ? 226 ILE A CG2   1 
ATOM   1798 C  CD1   . ILE A 1 234 ? 14.049 -6.374  19.164 1.00 21.15 ? 226 ILE A CD1   1 
ATOM   1799 N  N     . LYS A 1 235 ? 9.876  -8.357  16.791 1.00 14.94 ? 227 LYS A N     1 
ATOM   1800 C  CA    . LYS A 1 235 ? 8.550  -8.759  17.235 1.00 15.02 ? 227 LYS A CA    1 
ATOM   1801 C  C     . LYS A 1 235 ? 8.562  -10.182 17.784 1.00 14.61 ? 227 LYS A C     1 
ATOM   1802 O  O     . LYS A 1 235 ? 7.943  -10.456 18.817 1.00 14.07 ? 227 LYS A O     1 
ATOM   1803 C  CB    . LYS A 1 235 ? 7.546  -8.614  16.096 1.00 16.49 ? 227 LYS A CB    1 
ATOM   1804 C  CG    . LYS A 1 235 ? 6.113  -8.762  16.548 1.00 18.52 ? 227 LYS A CG    1 
ATOM   1805 C  CD    . LYS A 1 235 ? 5.694  -7.671  17.538 1.00 20.21 ? 227 LYS A CD    1 
ATOM   1806 C  CE    . LYS A 1 235 ? 4.195  -7.643  17.731 1.00 21.75 ? 227 LYS A CE    1 
ATOM   1807 N  NZ    . LYS A 1 235 ? 3.762  -6.538  18.632 1.00 23.05 ? 227 LYS A NZ    1 
ATOM   1808 N  N     . ILE A 1 236 ? 9.294  -11.089 17.131 1.00 14.12 ? 228 ILE A N     1 
ATOM   1809 C  CA    . ILE A 1 236 ? 9.437  -12.448 17.653 1.00 13.67 ? 228 ILE A CA    1 
ATOM   1810 C  C     . ILE A 1 236 ? 10.064 -12.412 19.042 1.00 12.91 ? 228 ILE A C     1 
ATOM   1811 O  O     . ILE A 1 236 ? 9.584  -13.060 19.980 1.00 13.34 ? 228 ILE A O     1 
ATOM   1812 C  CB    . ILE A 1 236 ? 10.277 -13.311 16.691 1.00 14.36 ? 228 ILE A CB    1 
ATOM   1813 C  CG1   . ILE A 1 236 ? 9.562  -13.526 15.355 1.00 14.86 ? 228 ILE A CG1   1 
ATOM   1814 C  CG2   . ILE A 1 236 ? 10.614 -14.655 17.334 1.00 13.98 ? 228 ILE A CG2   1 
ATOM   1815 C  CD1   . ILE A 1 236 ? 10.489 -14.041 14.266 1.00 15.63 ? 228 ILE A CD1   1 
ATOM   1816 N  N     . ALA A 1 237 ? 11.160 -11.661 19.191 1.00 12.57 ? 229 ALA A N     1 
ATOM   1817 C  CA    . ALA A 1 237 ? 11.849 -11.611 20.474 1.00 13.34 ? 229 ALA A CA    1 
ATOM   1818 C  C     . ALA A 1 237 ? 10.958 -11.027 21.562 1.00 13.08 ? 229 ALA A C     1 
ATOM   1819 O  O     . ALA A 1 237 ? 10.886 -11.558 22.677 1.00 13.23 ? 229 ALA A O     1 
ATOM   1820 C  CB    . ALA A 1 237 ? 13.151 -10.814 20.333 1.00 13.80 ? 229 ALA A CB    1 
ATOM   1821 N  N     . LEU A 1 238 ? 10.271 -9.926  21.252 1.00 12.79 ? 230 LEU A N     1 
ATOM   1822 C  CA    . LEU A 1 238 ? 9.415  -9.264  22.238 1.00 13.29 ? 230 LEU A CA    1 
ATOM   1823 C  C     . LEU A 1 238 ? 8.296  -10.197 22.684 1.00 13.04 ? 230 LEU A C     1 
ATOM   1824 O  O     . LEU A 1 238 ? 8.020  -10.343 23.884 1.00 13.59 ? 230 LEU A O     1 
ATOM   1825 C  CB    . LEU A 1 238 ? 8.836  -7.977  21.650 1.00 14.02 ? 230 LEU A CB    1 
ATOM   1826 C  CG    . LEU A 1 238 ? 9.843  -6.855  21.416 1.00 14.39 ? 230 LEU A CG    1 
ATOM   1827 C  CD1   . LEU A 1 238 ? 9.274  -5.835  20.450 1.00 15.10 ? 230 LEU A CD1   1 
ATOM   1828 C  CD2   . LEU A 1 238 ? 10.184 -6.221  22.739 1.00 15.14 ? 230 LEU A CD2   1 
ATOM   1829 N  N     . GLU A 1 239 ? 7.634  -10.845 21.728 1.00 13.38 ? 231 GLU A N     1 
ATOM   1830 C  CA    . GLU A 1 239 ? 6.573  -11.780 22.087 1.00 14.11 ? 231 GLU A CA    1 
ATOM   1831 C  C     . GLU A 1 239 ? 7.131  -12.942 22.900 1.00 14.16 ? 231 GLU A C     1 
ATOM   1832 O  O     . GLU A 1 239 ? 6.481  -13.422 23.834 1.00 14.97 ? 231 GLU A O     1 
ATOM   1833 C  CB    . GLU A 1 239 ? 5.848  -12.255 20.829 1.00 15.51 ? 231 GLU A CB    1 
ATOM   1834 C  CG    . GLU A 1 239 ? 4.960  -11.184 20.202 1.00 15.59 ? 231 GLU A CG    1 
ATOM   1835 C  CD    . GLU A 1 239 ? 3.769  -10.871 21.070 1.00 17.03 ? 231 GLU A CD    1 
ATOM   1836 O  OE1   . GLU A 1 239 ? 3.080  -11.818 21.480 1.00 18.48 ? 231 GLU A OE1   1 
ATOM   1837 O  OE2   . GLU A 1 239 ? 3.522  -9.692  21.356 1.00 17.94 ? 231 GLU A OE2   1 
ATOM   1838 N  N     . ALA A 1 240 ? 8.347  -13.394 22.583 1.00 13.55 ? 232 ALA A N     1 
ATOM   1839 C  CA    . ALA A 1 240 ? 8.951  -14.482 23.345 1.00 13.71 ? 232 ALA A CA    1 
ATOM   1840 C  C     . ALA A 1 240 ? 9.165  -14.090 24.803 1.00 13.11 ? 232 ALA A C     1 
ATOM   1841 O  O     . ALA A 1 240 ? 9.015  -14.936 25.695 1.00 13.83 ? 232 ALA A O     1 
ATOM   1842 C  CB    . ALA A 1 240 ? 10.262 -14.916 22.696 1.00 14.33 ? 232 ALA A CB    1 
ATOM   1843 N  N     . THR A 1 241 ? 9.486  -12.818 25.076 1.00 13.30 ? 233 THR A N     1 
ATOM   1844 C  CA    . THR A 1 241 ? 9.729  -12.424 26.462 1.00 13.98 ? 233 THR A CA    1 
ATOM   1845 C  C     . THR A 1 241 ? 8.487  -12.604 27.326 1.00 13.76 ? 233 THR A C     1 
ATOM   1846 O  O     . THR A 1 241 ? 8.606  -12.788 28.542 1.00 14.94 ? 233 THR A O     1 
ATOM   1847 C  CB    . THR A 1 241 ? 10.232 -10.977 26.589 1.00 14.91 ? 233 THR A CB    1 
ATOM   1848 O  OG1   . THR A 1 241 ? 9.207  -10.037 26.217 1.00 15.14 ? 233 THR A OG1   1 
ATOM   1849 C  CG2   . THR A 1 241 ? 11.494 -10.759 25.756 1.00 15.39 ? 233 THR A CG2   1 
ATOM   1850 N  N     . LEU A 1 242 ? 7.292  -12.551 26.728 1.00 14.03 ? 234 LEU A N     1 
ATOM   1851 C  CA    . LEU A 1 242 ? 6.064  -12.735 27.497 1.00 15.03 ? 234 LEU A CA    1 
ATOM   1852 C  C     . LEU A 1 242 ? 5.917  -14.159 28.009 1.00 16.76 ? 234 LEU A C     1 
ATOM   1853 O  O     . LEU A 1 242 ? 5.125  -14.404 28.927 1.00 18.03 ? 234 LEU A O     1 
ATOM   1854 C  CB    . LEU A 1 242 ? 4.855  -12.367 26.636 1.00 15.25 ? 234 LEU A CB    1 
ATOM   1855 C  CG    . LEU A 1 242 ? 4.840  -10.925 26.113 1.00 16.23 ? 234 LEU A CG    1 
ATOM   1856 C  CD1   . LEU A 1 242 ? 3.614  -10.655 25.232 1.00 17.89 ? 234 LEU A CD1   1 
ATOM   1857 C  CD2   . LEU A 1 242 ? 4.893  -9.938  27.275 1.00 17.16 ? 234 LEU A CD2   1 
ATOM   1858 N  N     . LYS A 1 243 ? 6.651  -15.097 27.427 1.00 17.35 ? 235 LYS A N     1 
ATOM   1859 C  CA    . LYS A 1 243 ? 6.631  -16.499 27.819 1.00 18.75 ? 235 LYS A CA    1 
ATOM   1860 C  C     . LYS A 1 243 ? 7.763  -16.854 28.777 1.00 19.73 ? 235 LYS A C     1 
ATOM   1861 O  O     . LYS A 1 243 ? 7.899  -18.027 29.147 1.00 21.90 ? 235 LYS A O     1 
ATOM   1862 C  CB    . LYS A 1 243 ? 6.746  -17.363 26.562 1.00 20.45 ? 235 LYS A CB    1 
ATOM   1863 C  CG    . LYS A 1 243 ? 5.695  -17.093 25.486 1.00 23.12 ? 235 LYS A CG    1 
ATOM   1864 C  CD    . LYS A 1 243 ? 6.060  -17.755 24.156 1.00 26.11 ? 235 LYS A CD    1 
ATOM   1865 C  CE    . LYS A 1 243 ? 5.051  -17.418 23.060 1.00 29.30 ? 235 LYS A CE    1 
ATOM   1866 N  NZ    . LYS A 1 243 ? 3.734  -18.081 23.263 1.00 32.52 ? 235 LYS A NZ    1 
ATOM   1867 N  N     . LEU A 1 244 ? 8.570  -15.877 29.181 1.00 20.01 ? 236 LEU A N     1 
ATOM   1868 C  CA    . LEU A 1 244 ? 9.807  -16.127 29.921 1.00 20.85 ? 236 LEU A CA    1 
ATOM   1869 C  C     . LEU A 1 244 ? 9.942  -15.304 31.203 1.00 24.24 ? 236 LEU A C     1 
ATOM   1870 O  O     . LEU A 1 244 ? 10.852 -15.554 32.003 1.00 26.41 ? 236 LEU A O     1 
ATOM   1871 C  CB    . LEU A 1 244 ? 11.001 -15.821 29.015 1.00 19.37 ? 236 LEU A CB    1 
ATOM   1872 C  CG    . LEU A 1 244 ? 11.155 -16.716 27.781 1.00 17.74 ? 236 LEU A CG    1 
ATOM   1873 C  CD1   . LEU A 1 244 ? 12.137 -16.085 26.822 1.00 17.26 ? 236 LEU A CD1   1 
ATOM   1874 C  CD2   . LEU A 1 244 ? 11.596 -18.130 28.146 1.00 17.85 ? 236 LEU A CD2   1 
ATOM   1875 O  OXT   . LEU A 1 244 ? 9.178  -14.378 31.459 1.00 26.03 ? 236 LEU A OXT   1 
HETATM 1876 N  N9    . NOS B 2 .   ? 27.525 -9.633  12.141 1.00 13.47 ? 301 NOS A N9    1 
HETATM 1877 C  C4    . NOS B 2 .   ? 28.608 -10.384 11.753 1.00 13.33 ? 301 NOS A C4    1 
HETATM 1878 N  N3    . NOS B 2 .   ? 29.680 -10.762 12.485 1.00 14.03 ? 301 NOS A N3    1 
HETATM 1879 C  C2    . NOS B 2 .   ? 30.539 -11.481 11.830 1.00 13.54 ? 301 NOS A C2    1 
HETATM 1880 N  N1    . NOS B 2 .   ? 30.407 -11.828 10.532 1.00 13.76 ? 301 NOS A N1    1 
HETATM 1881 C  C6    . NOS B 2 .   ? 29.327 -11.515 9.703  1.00 14.72 ? 301 NOS A C6    1 
HETATM 1882 O  O6    . NOS B 2 .   ? 29.286 -11.901 8.540  1.00 16.65 ? 301 NOS A O6    1 
HETATM 1883 C  C5    . NOS B 2 .   ? 28.389 -10.706 10.419 1.00 13.95 ? 301 NOS A C5    1 
HETATM 1884 N  N7    . NOS B 2 .   ? 27.217 -10.172 9.989  1.00 14.69 ? 301 NOS A N7    1 
HETATM 1885 C  C8    . NOS B 2 .   ? 26.749 -9.562  11.025 1.00 14.45 ? 301 NOS A C8    1 
HETATM 1886 C  "C5'" . NOS B 2 .   ? 29.673 -7.076  12.779 1.00 13.87 ? 301 NOS A "C5'" 1 
HETATM 1887 O  "O5'" . NOS B 2 .   ? 29.269 -6.191  11.747 1.00 14.96 ? 301 NOS A "O5'" 1 
HETATM 1888 C  "C4'" . NOS B 2 .   ? 28.618 -7.197  13.850 1.00 12.88 ? 301 NOS A "C4'" 1 
HETATM 1889 O  "O4'" . NOS B 2 .   ? 27.363 -7.570  13.240 1.00 13.63 ? 301 NOS A "O4'" 1 
HETATM 1890 C  "C1'" . NOS B 2 .   ? 27.155 -8.953  13.402 1.00 13.75 ? 301 NOS A "C1'" 1 
HETATM 1891 C  "C2'" . NOS B 2 .   ? 27.917 -9.381  14.657 1.00 14.66 ? 301 NOS A "C2'" 1 
HETATM 1892 O  "O2'" . NOS B 2 .   ? 27.004 -9.586  15.715 1.00 17.25 ? 301 NOS A "O2'" 1 
HETATM 1893 C  "C3'" . NOS B 2 .   ? 28.900 -8.228  14.931 1.00 13.72 ? 301 NOS A "C3'" 1 
HETATM 1894 O  "O3'" . NOS B 2 .   ? 28.635 -7.662  16.213 1.00 14.30 ? 301 NOS A "O3'" 1 
HETATM 1895 CL CL    . CL  C 3 .   ? 21.819 7.652   32.018 1.00 57.86 ? 302 CL  A CL    1 
HETATM 1896 CL CL    A CL  D 3 .   ? 33.757 -12.296 6.609  0.51 26.13 ? 303 CL  A CL    1 
HETATM 1897 CL CL    B CL  D 3 .   ? 33.524 -11.005 6.260  0.49 51.09 ? 303 CL  A CL    1 
HETATM 1898 CL CL    . CL  E 3 .   ? 22.478 -4.339  16.433 1.00 28.02 ? 304 CL  A CL    1 
HETATM 1899 O  O     . HOH F 4 .   ? 14.483 6.310   18.445 1.00 28.59 ? 401 HOH A O     1 
HETATM 1900 O  O     . HOH F 4 .   ? 0.000  0.000   26.418 0.33 25.10 ? 402 HOH A O     1 
HETATM 1901 O  O     . HOH F 4 .   ? 25.118 6.584   32.319 1.00 26.31 ? 403 HOH A O     1 
HETATM 1902 O  O     . HOH F 4 .   ? 11.456 -22.992 11.710 1.00 29.52 ? 404 HOH A O     1 
HETATM 1903 O  O     . HOH F 4 .   ? 14.895 -23.610 31.613 1.00 39.41 ? 405 HOH A O     1 
HETATM 1904 O  O     . HOH F 4 .   ? 11.708 -13.335 35.296 1.00 43.46 ? 406 HOH A O     1 
HETATM 1905 O  O     . HOH F 4 .   ? 34.086 2.441   31.852 1.00 39.51 ? 407 HOH A O     1 
HETATM 1906 O  O     . HOH F 4 .   ? 24.437 -9.442  15.756 1.00 44.43 ? 408 HOH A O     1 
HETATM 1907 O  O     . HOH F 4 .   ? 21.797 -21.628 31.202 1.00 42.37 ? 409 HOH A O     1 
HETATM 1908 O  O     . HOH F 4 .   ? 1.043  -11.659 23.050 1.00 38.45 ? 410 HOH A O     1 
HETATM 1909 O  O     . HOH F 4 .   ? 28.812 -10.827 6.227  1.00 45.15 ? 411 HOH A O     1 
HETATM 1910 O  O     . HOH F 4 .   ? 16.129 -11.581 39.633 1.00 40.63 ? 412 HOH A O     1 
HETATM 1911 O  O     . HOH F 4 .   ? 14.725 -14.948 2.947  1.00 30.35 ? 413 HOH A O     1 
HETATM 1912 O  O     . HOH F 4 .   ? 44.947 -16.230 4.293  1.00 43.98 ? 414 HOH A O     1 
HETATM 1913 O  O     . HOH F 4 .   ? 18.922 7.979   24.306 1.00 41.83 ? 415 HOH A O     1 
HETATM 1914 O  O     . HOH F 4 .   ? 23.194 -1.177  13.428 1.00 47.33 ? 416 HOH A O     1 
HETATM 1915 O  O     . HOH F 4 .   ? 23.562 -6.456  43.179 1.00 33.48 ? 417 HOH A O     1 
HETATM 1916 O  O     . HOH F 4 .   ? 21.657 -26.678 3.491  1.00 43.76 ? 418 HOH A O     1 
HETATM 1917 O  O     . HOH F 4 .   ? 30.502 -4.017  40.249 1.00 29.92 ? 419 HOH A O     1 
HETATM 1918 O  O     . HOH F 4 .   ? 9.428  -13.040 33.744 1.00 39.46 ? 420 HOH A O     1 
HETATM 1919 O  O     . HOH F 4 .   ? 21.767 -26.828 10.360 1.00 42.00 ? 421 HOH A O     1 
HETATM 1920 O  O     . HOH F 4 .   ? 20.143 -15.105 -0.172 1.00 32.20 ? 422 HOH A O     1 
HETATM 1921 O  O     . HOH F 4 .   ? 24.885 -6.670  9.861  1.00 28.46 ? 423 HOH A O     1 
HETATM 1922 O  O     . HOH F 4 .   ? 34.211 -18.805 40.187 1.00 36.86 ? 424 HOH A O     1 
HETATM 1923 O  O     . HOH F 4 .   ? 29.624 0.905   29.093 1.00 15.87 ? 425 HOH A O     1 
HETATM 1924 O  O     . HOH F 4 .   ? 34.998 -32.742 7.778  1.00 16.58 ? 426 HOH A O     1 
HETATM 1925 O  O     . HOH F 4 .   ? 30.453 -23.861 21.425 1.00 11.77 ? 427 HOH A O     1 
HETATM 1926 O  O     . HOH F 4 .   ? 36.593 -21.619 23.762 1.00 10.66 ? 428 HOH A O     1 
HETATM 1927 O  O     . HOH F 4 .   ? 26.912 -22.279 0.403  1.00 35.44 ? 429 HOH A O     1 
HETATM 1928 O  O     . HOH F 4 .   ? 37.669 -20.674 2.039  1.00 37.30 ? 430 HOH A O     1 
HETATM 1929 O  O     . HOH F 4 .   ? 42.961 -22.438 7.209  1.00 25.36 ? 431 HOH A O     1 
HETATM 1930 O  O     . HOH F 4 .   ? 12.685 5.050   25.138 1.00 38.48 ? 432 HOH A O     1 
HETATM 1931 O  O     . HOH F 4 .   ? 43.207 -29.592 31.581 1.00 36.83 ? 433 HOH A O     1 
HETATM 1932 O  O     . HOH F 4 .   ? 8.021  -5.072  14.602 1.00 27.79 ? 434 HOH A O     1 
HETATM 1933 O  O     . HOH F 4 .   ? 35.728 -23.520 35.451 1.00 16.67 ? 435 HOH A O     1 
HETATM 1934 O  O     . HOH F 4 .   ? 3.652  -12.807 30.535 1.00 24.20 ? 436 HOH A O     1 
HETATM 1935 O  O     . HOH F 4 .   ? 13.250 -16.834 7.933  1.00 38.51 ? 437 HOH A O     1 
HETATM 1936 O  O     . HOH F 4 .   ? 37.292 -18.970 12.766 1.00 13.52 ? 438 HOH A O     1 
HETATM 1937 O  O     . HOH F 4 .   ? 19.741 -8.159  8.847  1.00 32.86 ? 439 HOH A O     1 
HETATM 1938 O  O     . HOH F 4 .   ? 32.167 -15.291 27.715 1.00 12.73 ? 440 HOH A O     1 
HETATM 1939 O  O     . HOH F 4 .   ? 26.565 -22.901 27.203 1.00 14.34 ? 441 HOH A O     1 
HETATM 1940 O  O     . HOH F 4 .   ? 35.139 -7.273  21.692 0.50 21.23 ? 442 HOH A O     1 
HETATM 1941 O  O     . HOH F 4 .   ? 33.939 -16.238 6.919  1.00 23.67 ? 443 HOH A O     1 
HETATM 1942 O  O     . HOH F 4 .   ? 21.118 -13.592 37.861 1.00 24.16 ? 444 HOH A O     1 
HETATM 1943 O  O     . HOH F 4 .   ? 36.927 -13.930 22.470 1.00 11.42 ? 445 HOH A O     1 
HETATM 1944 O  O     . HOH F 4 .   ? 36.480 -15.275 11.144 1.00 14.41 ? 446 HOH A O     1 
HETATM 1945 O  O     . HOH F 4 .   ? 18.959 -21.207 38.757 1.00 41.60 ? 447 HOH A O     1 
HETATM 1946 O  O     . HOH F 4 .   ? 10.639 -9.555  32.780 1.00 21.09 ? 448 HOH A O     1 
HETATM 1947 O  O     . HOH F 4 .   ? 8.522  -20.666 28.977 1.00 45.56 ? 449 HOH A O     1 
HETATM 1948 O  O     . HOH F 4 .   ? 7.995  -8.225  27.839 1.00 28.70 ? 450 HOH A O     1 
HETATM 1949 O  O     . HOH F 4 .   ? 13.162 -13.620 32.762 1.00 20.29 ? 451 HOH A O     1 
HETATM 1950 O  O     . HOH F 4 .   ? 32.663 -23.088 22.961 1.00 10.35 ? 452 HOH A O     1 
HETATM 1951 O  O     . HOH F 4 .   ? 18.099 -18.943 20.882 1.00 13.27 ? 453 HOH A O     1 
HETATM 1952 O  O     . HOH F 4 .   ? 7.730  -20.159 12.207 1.00 25.24 ? 454 HOH A O     1 
HETATM 1953 O  O     . HOH F 4 .   ? 3.967  -1.900  27.911 1.00 18.57 ? 455 HOH A O     1 
HETATM 1954 O  O     . HOH F 4 .   ? 8.706  -26.907 16.656 1.00 45.24 ? 456 HOH A O     1 
HETATM 1955 O  O     . HOH F 4 .   ? 30.590 -16.120 34.190 1.00 17.11 ? 457 HOH A O     1 
HETATM 1956 O  O     . HOH F 4 .   ? 8.794  7.157   29.281 1.00 27.30 ? 458 HOH A O     1 
HETATM 1957 O  O     . HOH F 4 .   ? 43.236 -23.255 22.716 1.00 18.22 ? 459 HOH A O     1 
HETATM 1958 O  O     . HOH F 4 .   ? 40.077 -15.825 21.692 0.50 16.99 ? 460 HOH A O     1 
HETATM 1959 O  O     . HOH F 4 .   ? 37.184 -8.732  14.537 1.00 10.82 ? 461 HOH A O     1 
HETATM 1960 O  O     . HOH F 4 .   ? 22.780 -2.885  2.118  1.00 43.83 ? 462 HOH A O     1 
HETATM 1961 O  O     . HOH F 4 .   ? 26.508 -19.778 8.186  1.00 16.14 ? 463 HOH A O     1 
HETATM 1962 O  O     . HOH F 4 .   ? 26.017 5.745   21.713 1.00 20.74 ? 464 HOH A O     1 
HETATM 1963 O  O     . HOH F 4 .   ? 34.234 -12.335 19.302 1.00 10.47 ? 465 HOH A O     1 
HETATM 1964 O  O     . HOH F 4 .   ? 32.087 -16.926 -2.450 1.00 54.81 ? 466 HOH A O     1 
HETATM 1965 O  O     . HOH F 4 .   ? 20.213 -27.452 16.630 1.00 22.98 ? 467 HOH A O     1 
HETATM 1966 O  O     . HOH F 4 .   ? 11.948 8.279   31.053 1.00 40.04 ? 468 HOH A O     1 
HETATM 1967 O  O     . HOH F 4 .   ? 38.952 -24.564 33.572 1.00 16.06 ? 469 HOH A O     1 
HETATM 1968 O  O     . HOH F 4 .   ? 1.046  -7.485  18.883 1.00 28.27 ? 470 HOH A O     1 
HETATM 1969 O  O     . HOH F 4 .   ? 38.922 -16.387 10.614 1.00 22.88 ? 471 HOH A O     1 
HETATM 1970 O  O     . HOH F 4 .   ? 2.888  -20.833 18.706 1.00 39.19 ? 472 HOH A O     1 
HETATM 1971 O  O     . HOH F 4 .   ? 36.316 -16.830 5.729  1.00 24.15 ? 473 HOH A O     1 
HETATM 1972 O  O     . HOH F 4 .   ? 42.007 -10.636 9.863  1.00 15.90 ? 474 HOH A O     1 
HETATM 1973 O  O     . HOH F 4 .   ? 14.266 8.104   24.356 1.00 45.94 ? 475 HOH A O     1 
HETATM 1974 O  O     . HOH F 4 .   ? 8.820  -24.902 20.303 1.00 30.61 ? 476 HOH A O     1 
HETATM 1975 O  O     . HOH F 4 .   ? 9.320  -21.593 26.546 1.00 27.60 ? 477 HOH A O     1 
HETATM 1976 O  O     . HOH F 4 .   ? -1.460 -8.351  22.717 1.00 36.58 ? 478 HOH A O     1 
HETATM 1977 O  O     . HOH F 4 .   ? 32.592 -17.738 33.406 1.00 16.42 ? 479 HOH A O     1 
HETATM 1978 O  O     . HOH F 4 .   ? 36.735 -19.304 4.490  1.00 17.33 ? 480 HOH A O     1 
HETATM 1979 O  O     . HOH F 4 .   ? 36.126 -2.780  5.150  1.00 30.22 ? 481 HOH A O     1 
HETATM 1980 O  O     . HOH F 4 .   ? 37.606 -26.838 5.244  1.00 20.73 ? 482 HOH A O     1 
HETATM 1981 O  O     . HOH F 4 .   ? 26.400 -4.021  32.318 1.00 14.01 ? 483 HOH A O     1 
HETATM 1982 O  O     A HOH F 4 .   ? 40.601 -9.451  5.379  0.59 14.74 ? 484 HOH A O     1 
HETATM 1983 O  O     B HOH F 4 .   ? 41.099 -8.454  4.423  0.41 19.40 ? 484 HOH A O     1 
HETATM 1984 O  O     . HOH F 4 .   ? 25.069 -32.089 4.232  1.00 35.63 ? 485 HOH A O     1 
HETATM 1985 O  O     . HOH F 4 .   ? 18.319 -8.793  6.748  1.00 25.54 ? 486 HOH A O     1 
HETATM 1986 O  O     . HOH F 4 .   ? 26.389 -27.609 2.828  1.00 35.50 ? 487 HOH A O     1 
HETATM 1987 O  O     . HOH F 4 .   ? 38.359 -22.096 19.986 1.00 17.38 ? 488 HOH A O     1 
HETATM 1988 O  O     . HOH F 4 .   ? 35.264 -25.055 24.781 1.00 9.91  ? 489 HOH A O     1 
HETATM 1989 O  O     . HOH F 4 .   ? 22.703 -26.328 12.794 1.00 16.00 ? 490 HOH A O     1 
HETATM 1990 O  O     . HOH F 4 .   ? 13.233 -8.067  4.739  1.00 32.94 ? 491 HOH A O     1 
HETATM 1991 O  O     . HOH F 4 .   ? 31.143 -27.069 2.038  1.00 26.14 ? 492 HOH A O     1 
HETATM 1992 O  O     . HOH F 4 .   ? 18.028 -25.867 28.287 1.00 20.69 ? 493 HOH A O     1 
HETATM 1993 O  O     . HOH F 4 .   ? 18.927 -0.503  7.374  1.00 48.84 ? 494 HOH A O     1 
HETATM 1994 O  O     . HOH F 4 .   ? 19.912 4.525   35.972 1.00 43.04 ? 495 HOH A O     1 
HETATM 1995 O  O     . HOH F 4 .   ? 18.274 -4.770  38.146 1.00 15.78 ? 496 HOH A O     1 
HETATM 1996 O  O     . HOH F 4 .   ? 15.124 8.439   30.368 1.00 27.98 ? 497 HOH A O     1 
HETATM 1997 O  O     . HOH F 4 .   ? 9.689  -9.277  29.533 1.00 18.00 ? 498 HOH A O     1 
HETATM 1998 O  O     . HOH F 4 .   ? 18.599 -6.050  10.062 1.00 36.77 ? 499 HOH A O     1 
HETATM 1999 O  O     . HOH F 4 .   ? 22.830 -20.340 27.894 1.00 27.59 ? 500 HOH A O     1 
HETATM 2000 O  O     . HOH F 4 .   ? 31.784 6.943   29.423 1.00 19.18 ? 501 HOH A O     1 
HETATM 2001 O  O     . HOH F 4 .   ? 16.594 0.685   41.261 1.00 42.22 ? 502 HOH A O     1 
HETATM 2002 O  O     . HOH F 4 .   ? 38.487 0.833   26.821 1.00 18.59 ? 503 HOH A O     1 
HETATM 2003 O  O     . HOH F 4 .   ? 41.092 -15.003 9.723  1.00 15.32 ? 504 HOH A O     1 
HETATM 2004 O  O     . HOH F 4 .   ? 32.979 -12.821 9.728  1.00 16.40 ? 505 HOH A O     1 
HETATM 2005 O  O     . HOH F 4 .   ? 23.968 -6.574  14.611 1.00 20.02 ? 506 HOH A O     1 
HETATM 2006 O  O     . HOH F 4 .   ? -1.236 -17.585 14.800 1.00 45.86 ? 507 HOH A O     1 
HETATM 2007 O  O     . HOH F 4 .   ? 27.195 -9.764  0.831  1.00 29.24 ? 508 HOH A O     1 
HETATM 2008 O  O     . HOH F 4 .   ? 11.657 -7.592  36.165 1.00 21.33 ? 509 HOH A O     1 
HETATM 2009 O  O     . HOH F 4 .   ? 19.539 -25.206 22.713 1.00 19.81 ? 510 HOH A O     1 
HETATM 2010 O  O     . HOH F 4 .   ? 33.999 1.482   25.117 1.00 17.34 ? 511 HOH A O     1 
HETATM 2011 O  O     . HOH F 4 .   ? 44.060 -19.746 6.185  1.00 27.03 ? 512 HOH A O     1 
HETATM 2012 O  O     . HOH F 4 .   ? 38.040 -10.396 5.297  1.00 21.09 ? 513 HOH A O     1 
HETATM 2013 O  O     . HOH F 4 .   ? 9.302  -20.917 14.299 1.00 22.33 ? 514 HOH A O     1 
HETATM 2014 O  O     . HOH F 4 .   ? 19.054 5.625   17.577 1.00 28.65 ? 515 HOH A O     1 
HETATM 2015 O  O     . HOH F 4 .   ? 33.078 -13.139 31.836 1.00 15.39 ? 516 HOH A O     1 
HETATM 2016 O  O     . HOH F 4 .   ? 21.491 -19.104 -0.334 1.00 43.52 ? 517 HOH A O     1 
HETATM 2017 O  O     . HOH F 4 .   ? 23.474 -7.394  17.249 1.00 34.20 ? 518 HOH A O     1 
HETATM 2018 O  O     . HOH F 4 .   ? 16.415 -17.696 34.561 1.00 39.36 ? 519 HOH A O     1 
HETATM 2019 O  O     . HOH F 4 .   ? 12.403 -11.415 7.721  1.00 42.22 ? 520 HOH A O     1 
HETATM 2020 O  O     . HOH F 4 .   ? 30.561 -15.997 41.674 1.00 45.51 ? 521 HOH A O     1 
HETATM 2021 O  O     . HOH F 4 .   ? 3.674  -14.234 23.641 1.00 36.67 ? 522 HOH A O     1 
HETATM 2022 O  O     . HOH F 4 .   ? 30.347 -13.601 40.450 1.00 41.93 ? 523 HOH A O     1 
HETATM 2023 O  O     A HOH F 4 .   ? 31.039 1.791   23.010 0.76 22.94 ? 524 HOH A O     1 
HETATM 2024 O  O     B HOH F 4 .   ? 29.481 1.791   22.698 0.24 10.99 ? 524 HOH A O     1 
HETATM 2025 O  O     . HOH F 4 .   ? 36.861 1.201   32.420 1.00 41.59 ? 525 HOH A O     1 
HETATM 2026 O  O     . HOH F 4 .   ? 1.678  1.062   30.669 1.00 51.15 ? 526 HOH A O     1 
HETATM 2027 O  O     . HOH F 4 .   ? 42.541 -26.320 18.704 1.00 24.45 ? 527 HOH A O     1 
HETATM 2028 O  O     . HOH F 4 .   ? 20.021 -23.372 30.333 1.00 28.52 ? 528 HOH A O     1 
HETATM 2029 O  O     . HOH F 4 .   ? 38.381 -8.335  11.926 1.00 12.97 ? 529 HOH A O     1 
HETATM 2030 O  O     . HOH F 4 .   ? 41.007 -20.929 33.470 1.00 42.56 ? 530 HOH A O     1 
HETATM 2031 O  O     . HOH F 4 .   ? 20.912 -20.423 29.220 1.00 35.18 ? 531 HOH A O     1 
HETATM 2032 O  O     . HOH F 4 .   ? 32.296 -2.580  20.102 1.00 16.87 ? 532 HOH A O     1 
HETATM 2033 O  O     . HOH F 4 .   ? 26.701 -5.436  5.948  1.00 44.73 ? 533 HOH A O     1 
HETATM 2034 O  O     . HOH F 4 .   ? 22.800 -4.369  9.204  1.00 46.92 ? 534 HOH A O     1 
HETATM 2035 O  O     . HOH F 4 .   ? 26.707 8.506   31.941 1.00 46.70 ? 535 HOH A O     1 
HETATM 2036 O  O     . HOH F 4 .   ? 9.563  -21.918 10.372 1.00 27.64 ? 536 HOH A O     1 
HETATM 2037 O  O     . HOH F 4 .   ? 11.796 -4.538  2.801  1.00 41.69 ? 537 HOH A O     1 
HETATM 2038 O  O     . HOH F 4 .   ? 1.809  -18.900 21.114 1.00 42.18 ? 538 HOH A O     1 
HETATM 2039 O  O     . HOH F 4 .   ? 7.515  -22.031 24.488 1.00 30.88 ? 539 HOH A O     1 
HETATM 2040 O  O     . HOH F 4 .   ? 4.486  -2.106  25.137 1.00 28.91 ? 540 HOH A O     1 
HETATM 2041 O  O     . HOH F 4 .   ? 1.866  -3.519  33.873 1.00 49.81 ? 541 HOH A O     1 
HETATM 2042 O  O     . HOH F 4 .   ? 41.078 -19.440 16.563 1.00 34.06 ? 542 HOH A O     1 
HETATM 2043 O  O     . HOH F 4 .   ? 34.638 -15.030 4.062  1.00 37.05 ? 543 HOH A O     1 
HETATM 2044 O  O     . HOH F 4 .   ? 15.460 -24.999 10.532 1.00 43.68 ? 544 HOH A O     1 
HETATM 2045 O  O     . HOH F 4 .   ? 23.334 0.024   42.790 1.00 46.87 ? 545 HOH A O     1 
HETATM 2046 O  O     . HOH F 4 .   ? 34.413 -19.063 0.754  1.00 39.45 ? 546 HOH A O     1 
HETATM 2047 O  O     . HOH F 4 .   ? 16.442 -7.855  37.628 1.00 42.09 ? 547 HOH A O     1 
HETATM 2048 O  O     . HOH F 4 .   ? 6.032  -15.567 31.606 1.00 42.34 ? 548 HOH A O     1 
HETATM 2049 O  O     . HOH F 4 .   ? 7.960  4.938   27.174 1.00 28.59 ? 549 HOH A O     1 
HETATM 2050 O  O     . HOH F 4 .   ? 9.789  -1.729  34.282 1.00 40.65 ? 550 HOH A O     1 
HETATM 2051 O  O     . HOH F 4 .   ? 30.071 -8.620  37.592 1.00 28.98 ? 551 HOH A O     1 
HETATM 2052 O  O     . HOH F 4 .   ? 16.094 -7.423  -3.764 1.00 46.69 ? 552 HOH A O     1 
HETATM 2053 O  O     . HOH F 4 .   ? 40.113 -31.773 24.969 1.00 28.51 ? 553 HOH A O     1 
HETATM 2054 O  O     . HOH F 4 .   ? 27.945 -6.512  8.917  1.00 43.96 ? 554 HOH A O     1 
HETATM 2055 O  O     . HOH F 4 .   ? 12.220 6.366   16.884 1.00 30.95 ? 555 HOH A O     1 
HETATM 2056 O  O     . HOH F 4 .   ? 9.382  4.803   25.012 1.00 30.38 ? 556 HOH A O     1 
HETATM 2057 O  O     . HOH F 4 .   ? 23.749 -13.262 40.732 1.00 48.17 ? 557 HOH A O     1 
HETATM 2058 O  O     . HOH F 4 .   ? 20.718 -22.534 34.003 1.00 51.23 ? 558 HOH A O     1 
HETATM 2059 O  O     . HOH F 4 .   ? 40.161 -16.242 24.801 1.00 24.10 ? 559 HOH A O     1 
HETATM 2060 O  O     . HOH F 4 .   ? 42.585 -23.130 18.638 1.00 46.45 ? 560 HOH A O     1 
HETATM 2061 O  O     . HOH F 4 .   ? 45.400 -17.383 7.458  1.00 40.66 ? 561 HOH A O     1 
HETATM 2062 O  O     . HOH F 4 .   ? 23.258 -29.700 15.047 1.00 16.89 ? 562 HOH A O     1 
HETATM 2063 O  O     . HOH F 4 .   ? 28.323 8.972   30.049 1.00 47.81 ? 563 HOH A O     1 
HETATM 2064 O  O     . HOH F 4 .   ? 15.394 -25.673 30.041 1.00 47.50 ? 564 HOH A O     1 
HETATM 2065 O  O     . HOH F 4 .   ? 6.471  6.425   30.340 1.00 34.49 ? 565 HOH A O     1 
HETATM 2066 O  O     . HOH F 4 .   ? 12.853 -25.044 11.235 1.00 46.99 ? 566 HOH A O     1 
HETATM 2067 O  O     . HOH F 4 .   ? 43.613 -16.564 8.949  1.00 31.26 ? 567 HOH A O     1 
HETATM 2068 O  O     . HOH F 4 .   ? 9.846  -23.510 13.467 1.00 34.82 ? 568 HOH A O     1 
HETATM 2069 O  O     . HOH F 4 .   ? 25.841 -0.292  43.450 1.00 42.83 ? 569 HOH A O     1 
HETATM 2070 O  O     . HOH F 4 .   ? 13.472 6.411   27.197 1.00 35.85 ? 570 HOH A O     1 
HETATM 2071 O  O     . HOH F 4 .   ? 34.810 -29.099 5.196  1.00 43.64 ? 571 HOH A O     1 
HETATM 2072 O  O     . HOH F 4 .   ? 20.461 -27.716 12.158 1.00 49.24 ? 572 HOH A O     1 
HETATM 2073 O  O     . HOH F 4 .   ? 42.487 -24.445 31.239 1.00 47.27 ? 573 HOH A O     1 
HETATM 2074 O  O     . HOH F 4 .   ? 25.540 -20.934 -1.414 1.00 45.13 ? 574 HOH A O     1 
HETATM 2075 O  O     . HOH F 4 .   ? 11.207 -14.140 6.743  1.00 46.24 ? 575 HOH A O     1 
HETATM 2076 O  O     . HOH F 4 .   ? 9.710  -9.520  35.274 1.00 34.78 ? 576 HOH A O     1 
HETATM 2077 O  O     . HOH F 4 .   ? 22.441 -29.629 10.631 1.00 48.00 ? 577 HOH A O     1 
HETATM 2078 O  O     . HOH F 4 .   ? 33.973 -15.394 9.645  1.00 17.83 ? 578 HOH A O     1 
HETATM 2079 O  O     . HOH F 4 .   ? 46.142 -18.711 5.361  1.00 39.83 ? 579 HOH A O     1 
HETATM 2080 O  O     . HOH F 4 .   ? 33.686 5.188   31.688 1.00 43.48 ? 580 HOH A O     1 
HETATM 2081 O  O     . HOH F 4 .   ? 16.799 7.303   17.440 1.00 34.90 ? 581 HOH A O     1 
HETATM 2082 O  O     . HOH F 4 .   ? 21.149 -28.333 14.396 1.00 29.82 ? 582 HOH A O     1 
HETATM 2083 O  O     . HOH F 4 .   ? 41.833 -24.631 33.923 1.00 45.13 ? 583 HOH A O     1 
HETATM 2084 O  O     . HOH F 4 .   ? 5.579  -20.962 10.573 1.00 49.01 ? 584 HOH A O     1 
HETATM 2085 O  O     . HOH F 4 .   ? 30.772 -0.916  18.385 1.00 20.60 ? 585 HOH A O     1 
HETATM 2086 O  O     . HOH F 4 .   ? 42.387 -31.207 33.548 1.00 27.64 ? 586 HOH A O     1 
HETATM 2087 O  O     . HOH F 4 .   ? 40.130 -6.410  5.210  1.00 46.77 ? 587 HOH A O     1 
HETATM 2088 O  O     . HOH F 4 .   ? 43.020 -13.155 10.727 1.00 17.44 ? 588 HOH A O     1 
HETATM 2089 O  O     . HOH F 4 .   ? 1.094  -13.578 26.741 1.00 49.10 ? 589 HOH A O     1 
HETATM 2090 O  O     . HOH F 4 .   ? 43.051 -13.328 2.166  1.00 39.58 ? 590 HOH A O     1 
HETATM 2091 O  O     . HOH F 4 .   ? 46.600 -13.824 5.143  1.00 21.86 ? 591 HOH A O     1 
HETATM 2092 O  O     . HOH F 4 .   ? 44.887 -14.714 9.402  1.00 19.70 ? 592 HOH A O     1 
HETATM 2093 O  O     . HOH F 4 .   ? 24.315 7.942   21.819 1.00 37.24 ? 593 HOH A O     1 
HETATM 2094 O  O     . HOH F 4 .   ? 43.883 -23.268 26.656 1.00 53.74 ? 594 HOH A O     1 
HETATM 2095 O  O     . HOH F 4 .   ? 17.601 -26.795 21.692 0.50 20.86 ? 595 HOH A O     1 
HETATM 2096 O  O     . HOH F 4 .   ? 38.055 -28.970 7.175  1.00 22.47 ? 596 HOH A O     1 
HETATM 2097 O  O     . HOH F 4 .   ? 43.231 -13.840 13.210 1.00 19.15 ? 597 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     . HIS A 4   ? 0.6367 0.7031 0.6892 -0.0122 0.0460  -0.0398 -4  HIS A N     
2    C  CA    . HIS A 4   ? 0.6337 0.7017 0.6874 -0.0180 0.0493  -0.0337 -4  HIS A CA    
3    C  C     . HIS A 4   ? 0.6269 0.6960 0.6774 -0.0019 0.0672  -0.0270 -4  HIS A C     
4    O  O     . HIS A 4   ? 0.6293 0.7098 0.6774 0.0046  0.0673  -0.0274 -4  HIS A O     
5    C  CB    . HIS A 4   ? 0.6347 0.7029 0.6950 -0.0435 0.0358  -0.0341 -4  HIS A CB    
6    C  CG    . HIS A 4   ? 0.6331 0.7039 0.7002 -0.0675 0.0232  -0.0355 -4  HIS A CG    
7    N  ND1   . HIS A 4   ? 0.6336 0.7009 0.7025 -0.0754 0.0193  -0.0363 -4  HIS A ND1   
8    C  CD2   . HIS A 4   ? 0.6345 0.7044 0.7024 -0.0761 0.0188  -0.0368 -4  HIS A CD2   
9    C  CE1   . HIS A 4   ? 0.6350 0.6986 0.7043 -0.0811 0.0172  -0.0364 -4  HIS A CE1   
10   N  NE2   . HIS A 4   ? 0.6359 0.7035 0.7041 -0.0802 0.0165  -0.0368 -4  HIS A NE2   
11   N  N     . HIS A 5   ? 0.6176 0.6740 0.6659 0.0073  0.0846  -0.0209 -3  HIS A N     
12   C  CA    . HIS A 5   ? 0.6056 0.6458 0.6532 0.0183  0.1000  -0.0155 -3  HIS A CA    
13   C  C     . HIS A 5   ? 0.5921 0.6101 0.6357 0.0292  0.1152  -0.0161 -3  HIS A C     
14   O  O     . HIS A 5   ? 0.6011 0.6178 0.6381 0.0439  0.1146  -0.0160 -3  HIS A O     
15   C  CB    . HIS A 5   ? 0.6018 0.6440 0.6547 0.0088  0.1025  -0.0121 -3  HIS A CB    
16   N  N     . HIS A 6   ? 0.5691 0.5609 0.6134 0.0173  0.1303  -0.0189 -2  HIS A N     
17   C  CA    . HIS A 6   ? 0.5423 0.5159 0.5892 0.0000  0.1463  -0.0230 -2  HIS A CA    
18   C  C     . HIS A 6   ? 0.5143 0.4798 0.5568 -0.0153 0.1519  -0.0406 -2  HIS A C     
19   O  O     . HIS A 6   ? 0.5059 0.4703 0.5529 -0.0290 0.1605  -0.0466 -2  HIS A O     
20   C  CB    . HIS A 6   ? 0.5456 0.5167 0.5983 -0.0010 0.1529  -0.0143 -2  HIS A CB    
21   C  CG    . HIS A 6   ? 0.5506 0.5224 0.6069 0.0092  0.1572  -0.0089 -2  HIS A CG    
22   N  ND1   . HIS A 6   ? 0.5553 0.5312 0.6102 0.0166  0.1563  -0.0106 -2  HIS A ND1   
23   C  CD2   . HIS A 6   ? 0.5542 0.5206 0.6100 0.0184  0.1604  -0.0057 -2  HIS A CD2   
24   C  CE1   . HIS A 6   ? 0.5572 0.5210 0.6119 0.0208  0.1558  -0.0050 -2  HIS A CE1   
25   N  NE2   . HIS A 6   ? 0.5551 0.5227 0.6127 0.0256  0.1590  -0.0038 -2  HIS A NE2   
26   N  N     . HIS A 7   ? 0.4957 0.4462 0.5272 -0.0209 0.1501  -0.0504 -1  HIS A N     
27   C  CA    . HIS A 7   ? 0.4861 0.4401 0.5018 -0.0105 0.1348  -0.0687 -1  HIS A CA    
28   C  C     . HIS A 7   ? 0.4510 0.3579 0.4675 -0.0540 0.1315  -0.0897 -1  HIS A C     
29   O  O     . HIS A 7   ? 0.4299 0.3216 0.4679 -0.0926 0.1284  -0.1048 -1  HIS A O     
30   C  CB    . HIS A 7   ? 0.5163 0.5266 0.5117 0.0432  0.1210  -0.0620 -1  HIS A CB    
31   C  CG    . HIS A 7   ? 0.5439 0.5953 0.5221 0.0874  0.1070  -0.0541 -1  HIS A CG    
32   N  ND1   . HIS A 7   ? 0.5543 0.6292 0.5278 0.1033  0.0998  -0.0529 -1  HIS A ND1   
33   C  CD2   . HIS A 7   ? 0.5554 0.6209 0.5265 0.1043  0.1029  -0.0475 -1  HIS A CD2   
34   C  CE1   . HIS A 7   ? 0.5604 0.6435 0.5301 0.1130  0.0974  -0.0480 -1  HIS A CE1   
35   N  NE2   . HIS A 7   ? 0.5614 0.6395 0.5297 0.1151  0.0984  -0.0465 -1  HIS A NE2   
36   N  N     . HIS A 8   ? 0.4369 0.3099 0.4358 -0.0606 0.1285  -0.0878 0   HIS A N     
37   C  CA    . HIS A 8   ? 0.4382 0.3123 0.4128 -0.0347 0.1087  -0.0889 0   HIS A CA    
38   C  C     . HIS A 8   ? 0.4245 0.3259 0.3873 -0.0224 0.0792  -0.0969 0   HIS A C     
39   O  O     . HIS A 8   ? 0.4077 0.3600 0.3982 -0.0336 0.0725  -0.1129 0   HIS A O     
40   C  CB    . HIS A 8   ? 0.4551 0.3261 0.4169 -0.0299 0.1097  -0.0792 0   HIS A CB    
41   N  N     . MET A 9   ? 0.4202 0.2880 0.3543 -0.0108 0.0558  -0.0840 1   MET A N     
42   C  CA    . MET A 9   ? 0.4110 0.2687 0.3272 0.0132  0.0448  -0.0609 1   MET A CA    
43   C  C     . MET A 9   ? 0.3826 0.2722 0.3041 0.0089  0.0337  -0.0408 1   MET A C     
44   O  O     . MET A 9   ? 0.4092 0.2975 0.3097 -0.0165 0.0139  -0.0312 1   MET A O     
45   C  CB    . MET A 9   ? 0.4350 0.2700 0.3236 0.0328  0.0416  -0.0527 1   MET A CB    
46   C  CG    . MET A 9   ? 0.4595 0.2847 0.3223 0.0359  0.0281  -0.0575 1   MET A CG    
47   S  SD    . MET A 9   ? 0.4762 0.3175 0.3205 0.0457  0.0181  -0.0515 1   MET A SD    
48   C  CE    . MET A 9   ? 0.4774 0.3068 0.3204 0.0561  0.0194  -0.0606 1   MET A CE    
49   N  N     . ALA A 10  ? 0.3340 0.2546 0.2761 0.0143  0.0495  -0.0395 2   ALA A N     
50   C  CA    . ALA A 10  ? 0.3070 0.2690 0.2558 0.0283  0.0447  -0.0275 2   ALA A CA    
51   C  C     . ALA A 10  ? 0.3050 0.2623 0.2318 0.0415  0.0362  -0.0295 2   ALA A C     
52   O  O     . ALA A 10  ? 0.3318 0.2872 0.2279 0.0544  0.0384  -0.0274 2   ALA A O     
53   C  CB    . ALA A 10  ? 0.2882 0.2902 0.2594 0.0245  0.0542  -0.0223 2   ALA A CB    
54   N  N     . THR A 11  ? 0.2663 0.2195 0.2126 0.0132  0.0285  -0.0277 3   THR A N     
55   C  CA    . THR A 11  ? 0.2461 0.2085 0.2033 0.0115  0.0234  -0.0366 3   THR A CA    
56   C  C     . THR A 11  ? 0.2368 0.1937 0.2124 0.0079  0.0249  -0.0461 3   THR A C     
57   O  O     . THR A 11  ? 0.2565 0.1972 0.2257 0.0036  0.0413  -0.0445 3   THR A O     
58   C  CB    . THR A 11  ? 0.2340 0.2047 0.1891 0.0177  0.0161  -0.0290 3   THR A CB    
59   O  OG1   . THR A 11  ? 0.2076 0.1714 0.1752 0.0050  0.0105  -0.0205 3   THR A OG1   
60   C  CG2   . THR A 11  ? 0.2563 0.1996 0.1953 0.0104  0.0173  -0.0332 3   THR A CG2   
61   N  N     . PRO A 12  ? 0.2228 0.2096 0.2202 0.0079  0.0098  -0.0598 4   PRO A N     
62   C  CA    . PRO A 12  ? 0.2068 0.2207 0.2248 -0.0214 0.0162  -0.0520 4   PRO A CA    
63   C  C     . PRO A 12  ? 0.1957 0.1883 0.2274 -0.0174 0.0267  -0.0343 4   PRO A C     
64   O  O     . PRO A 12  ? 0.2383 0.1994 0.2405 -0.0308 0.0293  -0.0399 4   PRO A O     
65   C  CB    . PRO A 12  ? 0.2052 0.2540 0.2290 -0.0112 0.0151  -0.0561 4   PRO A CB    
66   C  CG    . PRO A 12  ? 0.2192 0.2736 0.2317 0.0116  0.0074  -0.0582 4   PRO A CG    
67   C  CD    . PRO A 12  ? 0.2223 0.2463 0.2258 0.0233  0.0024  -0.0614 4   PRO A CD    
68   N  N     . HIS A 13  ? 0.1638 0.1685 0.2228 0.0052  0.0229  -0.0413 5   HIS A N     
69   C  CA    . HIS A 13  ? 0.1587 0.1658 0.2205 0.0063  0.0221  -0.0132 5   HIS A CA    
70   C  C     . HIS A 13  ? 0.1621 0.1710 0.2441 0.0069  0.0250  -0.0033 5   HIS A C     
71   O  O     . HIS A 13  ? 0.1700 0.1705 0.2438 0.0081  0.0177  0.0083  5   HIS A O     
72   C  CB    . HIS A 13  ? 0.1575 0.1635 0.1973 0.0051  0.0219  -0.0105 5   HIS A CB    
73   C  CG    . HIS A 13  ? 0.1487 0.1615 0.1717 0.0078  0.0187  -0.0168 5   HIS A CG    
74   N  ND1   . HIS A 13  ? 0.1514 0.1559 0.1594 -0.0069 0.0220  -0.0180 5   HIS A ND1   
75   C  CD2   . HIS A 13  ? 0.1572 0.1669 0.1701 0.0136  0.0280  -0.0232 5   HIS A CD2   
76   C  CE1   . HIS A 13  ? 0.1367 0.1581 0.1627 -0.0140 0.0204  -0.0237 5   HIS A CE1   
77   N  NE2   . HIS A 13  ? 0.1461 0.1728 0.1689 0.0012  0.0313  -0.0208 5   HIS A NE2   
78   N  N     . ASN A 14  ? 0.1565 0.1647 0.2652 -0.0067 0.0410  -0.0045 6   ASN A N     
79   C  CA    . ASN A 14  ? 0.1662 0.1717 0.2864 0.0115  0.0392  -0.0166 6   ASN A CA    
80   C  C     . ASN A 14  ? 0.1826 0.1675 0.3108 0.0124  0.0404  -0.0233 6   ASN A C     
81   O  O     . ASN A 14  ? 0.2121 0.1953 0.3109 0.0174  0.0490  -0.0147 6   ASN A O     
82   C  CB    . ASN A 14  ? 0.1682 0.1671 0.2873 0.0144  0.0405  -0.0047 6   ASN A CB    
83   C  CG    . ASN A 14  ? 0.1673 0.1603 0.2936 0.0168  0.0343  -0.0023 6   ASN A CG    
84   O  OD1   . ASN A 14  ? 0.1706 0.1663 0.2967 0.0325  0.0491  0.0034  6   ASN A OD1   
85   N  ND2   . ASN A 14  ? 0.1611 0.1766 0.2998 0.0384  0.0184  0.0000  6   ASN A ND2   
86   N  N     . SER A 15  ? 0.1978 0.1599 0.3379 -0.0006 0.0518  -0.0247 7   SER A N     
87   C  CA    . SER A 15  ? 0.2147 0.1711 0.3551 0.0016  0.0590  -0.0351 7   SER A CA    
88   C  C     . SER A 15  ? 0.2059 0.1766 0.3466 -0.0062 0.0641  -0.0480 7   SER A C     
89   O  O     . SER A 15  ? 0.2206 0.2098 0.3529 -0.0049 0.0799  -0.0533 7   SER A O     
90   C  CB    . SER A 15  ? 0.2442 0.2033 0.3808 0.0349  0.0442  -0.0118 7   SER A CB    
91   O  OG    . SER A 15  ? 0.2670 0.2392 0.4038 0.0540  0.0289  0.0174  7   SER A OG    
92   N  N     . ALA A 16  ? 0.1846 0.1822 0.3281 0.0061  0.0583  -0.0513 8   ALA A N     
93   C  CA    . ALA A 16  ? 0.1830 0.2062 0.3163 -0.0100 0.0533  -0.0540 8   ALA A CA    
94   C  C     . ALA A 16  ? 0.2291 0.2521 0.3099 -0.0204 0.0592  -0.0747 8   ALA A C     
95   O  O     . ALA A 16  ? 0.2650 0.2407 0.3007 -0.0103 0.0545  -0.0865 8   ALA A O     
96   C  CB    . ALA A 16  ? 0.1831 0.2252 0.3135 -0.0192 0.0419  -0.0440 8   ALA A CB    
97   N  N     . LYS A 17  ? 0.2702 0.3012 0.3138 -0.0166 0.0472  -0.0848 9   LYS A N     
98   C  CA    . LYS A 17  ? 0.3041 0.3587 0.3195 0.0128  0.0519  -0.0681 9   LYS A CA    
99   C  C     . LYS A 17  ? 0.2660 0.3515 0.2910 0.0270  0.0632  -0.0493 9   LYS A C     
100  O  O     . LYS A 17  ? 0.2276 0.3064 0.2764 0.0056  0.0714  -0.0387 9   LYS A O     
101  C  CB    . LYS A 17  ? 0.3764 0.4234 0.3504 0.0569  0.0443  -0.0727 9   LYS A CB    
102  C  CG    . LYS A 17  ? 0.4220 0.4987 0.3775 0.0821  0.0440  -0.0627 9   LYS A CG    
103  C  CD    . LYS A 17  ? 0.4487 0.5610 0.3957 0.0989  0.0443  -0.0540 9   LYS A CD    
104  C  CE    . LYS A 17  ? 0.4720 0.5991 0.4080 0.1181  0.0474  -0.0516 9   LYS A CE    
105  N  NZ    . LYS A 17  ? 0.4826 0.6186 0.4130 0.1380  0.0563  -0.0471 9   LYS A NZ    
106  N  N     . VAL A 18  ? 0.2679 0.4006 0.2786 0.0540  0.0491  -0.0521 10  VAL A N     
107  C  CA    . VAL A 18  ? 0.3019 0.4139 0.2738 0.1104  0.0306  -0.0480 10  VAL A CA    
108  C  C     . VAL A 18  ? 0.2943 0.3570 0.2594 0.0823  0.0441  -0.0418 10  VAL A C     
109  O  O     . VAL A 18  ? 0.3041 0.3551 0.2590 0.0802  0.0532  -0.0455 10  VAL A O     
110  C  CB    . VAL A 18  ? 0.3309 0.4712 0.2885 0.1423  0.0021  -0.0488 10  VAL A CB    
111  C  CG1   . VAL A 18  ? 0.3409 0.4776 0.2937 0.1599  -0.0072 -0.0463 10  VAL A CG1   
112  C  CG2   . VAL A 18  ? 0.3389 0.4921 0.2966 0.1440  -0.0084 -0.0512 10  VAL A CG2   
113  N  N     . GLY A 19  ? 0.2816 0.3023 0.2483 0.0584  0.0458  -0.0379 11  GLY A N     
114  C  CA    . GLY A 19  ? 0.2643 0.2853 0.2449 0.0227  0.0474  -0.0325 11  GLY A CA    
115  C  C     . GLY A 19  ? 0.2188 0.2639 0.2453 0.0060  0.0501  -0.0244 11  GLY A C     
116  O  O     . GLY A 19  ? 0.2313 0.2946 0.2570 -0.0127 0.0504  -0.0174 11  GLY A O     
117  N  N     . ASP A 20  ? 0.1986 0.2243 0.2398 0.0069  0.0491  -0.0237 12  ASP A N     
118  C  CA    . ASP A 20  ? 0.2058 0.2307 0.2511 0.0079  0.0372  -0.0150 12  ASP A CA    
119  C  C     . ASP A 20  ? 0.1807 0.2006 0.2438 0.0031  0.0099  -0.0142 12  ASP A C     
120  O  O     . ASP A 20  ? 0.2013 0.1955 0.2512 0.0334  -0.0001 -0.0129 12  ASP A O     
121  C  CB    . ASP A 20  ? 0.2563 0.2425 0.2768 0.0096  0.0366  -0.0335 12  ASP A CB    
122  C  CG    . ASP A 20  ? 0.2833 0.2842 0.3041 0.0139  0.0595  -0.0453 12  ASP A CG    
123  O  OD1   . ASP A 20  ? 0.3006 0.3103 0.3119 0.0210  0.0775  -0.0571 12  ASP A OD1   
124  O  OD2   . ASP A 20  ? 0.2943 0.3011 0.3170 -0.0002 0.0589  -0.0524 12  ASP A OD2   
125  N  N     . PHE A 21  ? 0.1628 0.2031 0.2264 0.0097  0.0225  -0.0124 13  PHE A N     
126  C  CA    . PHE A 21  ? 0.1508 0.1843 0.2106 0.0164  0.0248  -0.0100 13  PHE A CA    
127  C  C     . PHE A 21  ? 0.1659 0.1753 0.1974 0.0144  0.0275  0.0061  13  PHE A C     
128  O  O     . PHE A 21  ? 0.2077 0.2057 0.1919 0.0092  0.0163  0.0206  13  PHE A O     
129  C  CB    . PHE A 21  ? 0.1519 0.2100 0.2106 0.0396  0.0235  -0.0090 13  PHE A CB    
130  C  CG    . PHE A 21  ? 0.1413 0.1989 0.2109 0.0286  0.0117  -0.0186 13  PHE A CG    
131  C  CD1   . PHE A 21  ? 0.1486 0.2255 0.2142 0.0332  0.0108  -0.0174 13  PHE A CD1   
132  C  CD2   . PHE A 21  ? 0.1599 0.2193 0.2198 0.0333  0.0178  -0.0347 13  PHE A CD2   
133  C  CE1   . PHE A 21  ? 0.1588 0.2416 0.2195 0.0352  0.0163  -0.0144 13  PHE A CE1   
134  C  CE2   . PHE A 21  ? 0.1677 0.2167 0.2194 0.0282  0.0296  -0.0453 13  PHE A CE2   
135  C  CZ    . PHE A 21  ? 0.1667 0.2182 0.2188 0.0323  0.0304  -0.0218 13  PHE A CZ    
136  N  N     . ALA A 22  ? 0.1648 0.1632 0.1952 0.0157  0.0280  -0.0004 14  ALA A N     
137  C  CA    . ALA A 22  ? 0.1630 0.1669 0.1979 0.0042  0.0280  0.0072  14  ALA A CA    
138  C  C     . ALA A 22  ? 0.1515 0.1728 0.1917 0.0051  0.0352  0.0034  14  ALA A C     
139  O  O     . ALA A 22  ? 0.1507 0.1899 0.2028 0.0077  0.0270  -0.0058 14  ALA A O     
140  C  CB    . ALA A 22  ? 0.1702 0.1836 0.2066 0.0135  0.0152  -0.0058 14  ALA A CB    
141  N  N     . GLU A 23  ? 0.1566 0.1628 0.1899 0.0085  0.0436  0.0106  15  GLU A N     
142  C  CA    . GLU A 23  ? 0.1719 0.1752 0.1874 0.0037  0.0523  0.0293  15  GLU A CA    
143  C  C     . GLU A 23  ? 0.1604 0.1555 0.1817 0.0118  0.0301  0.0289  15  GLU A C     
144  O  O     . GLU A 23  ? 0.1531 0.1681 0.1938 0.0298  0.0180  0.0119  15  GLU A O     
145  C  CB    . GLU A 23  ? 0.2825 0.2180 0.2034 0.0387  0.0525  0.0476  15  GLU A CB    
146  C  CG    . GLU A 23  ? 0.3435 0.3015 0.2305 0.0179  0.0437  0.0552  15  GLU A CG    
147  C  CD    . GLU A 23  ? 0.3830 0.3907 0.2597 -0.0135 0.0407  0.0717  15  GLU A CD    
148  O  OE1   . GLU A 23  ? 0.3759 0.3910 0.2774 -0.0883 0.0535  0.0812  15  GLU A OE1   
149  O  OE2   . GLU A 23  ? 0.4078 0.4531 0.2683 0.0054  0.0417  0.0713  15  GLU A OE2   
150  N  N     . THR A 24  ? 0.1490 0.1629 0.1801 0.0194  0.0198  0.0176  16  THR A N     
151  C  CA    . THR A 24  ? 0.1471 0.1442 0.1756 -0.0044 0.0131  0.0119  16  THR A CA    
152  C  C     . THR A 24  ? 0.1487 0.1398 0.1699 0.0139  0.0181  -0.0042 16  THR A C     
153  O  O     . THR A 24  ? 0.1515 0.1540 0.1714 0.0273  0.0228  0.0071  16  THR A O     
154  C  CB    . THR A 24  ? 0.1819 0.1707 0.1927 -0.0096 0.0050  0.0208  16  THR A CB    
155  O  OG1   . THR A 24  ? 0.2041 0.1926 0.2057 -0.0252 0.0109  0.0416  16  THR A OG1   
156  C  CG2   . THR A 24  ? 0.2028 0.1812 0.1995 0.0181  0.0048  0.0133  16  THR A CG2   
157  N  N     . VAL A 25  ? 0.1567 0.1401 0.1670 0.0282  0.0321  -0.0059 17  VAL A N     
158  C  CA    . VAL A 25  ? 0.1429 0.1574 0.1715 0.0206  0.0302  0.0108  17  VAL A CA    
159  C  C     . VAL A 25  ? 0.1413 0.1480 0.1763 0.0160  0.0222  0.0100  17  VAL A C     
160  O  O     . VAL A 25  ? 0.1756 0.1391 0.1743 0.0375  0.0296  0.0123  17  VAL A O     
161  C  CB    . VAL A 25  ? 0.1402 0.1619 0.1684 0.0214  0.0205  0.0105  17  VAL A CB    
162  C  CG1   . VAL A 25  ? 0.1528 0.1774 0.1739 0.0167  0.0125  0.0089  17  VAL A CG1   
163  C  CG2   . VAL A 25  ? 0.1615 0.1712 0.1741 0.0201  0.0103  0.0081  17  VAL A CG2   
164  N  N     . LEU A 26  ? 0.1216 0.1303 0.1777 0.0048  0.0354  0.0078  18  LEU A N     
165  C  CA    . LEU A 26  ? 0.1267 0.1154 0.1880 0.0098  0.0284  0.0088  18  LEU A CA    
166  C  C     . LEU A 26  ? 0.1267 0.1117 0.1907 0.0026  0.0261  0.0056  18  LEU A C     
167  O  O     . LEU A 26  ? 0.1452 0.1226 0.1878 0.0038  0.0347  -0.0071 18  LEU A O     
168  C  CB    . LEU A 26  ? 0.1334 0.1344 0.1959 0.0141  0.0198  0.0010  18  LEU A CB    
169  C  CG    . LEU A 26  ? 0.1376 0.1701 0.1965 0.0064  0.0092  0.0206  18  LEU A CG    
170  C  CD1   . LEU A 26  ? 0.1551 0.1971 0.1996 0.0232  -0.0063 0.0278  18  LEU A CD1   
171  C  CD2   . LEU A 26  ? 0.1386 0.1685 0.2034 -0.0148 0.0157  0.0141  18  LEU A CD2   
172  N  N     . MET A 27  ? 0.1139 0.1273 0.1908 0.0024  0.0162  0.0005  19  MET A N     
173  C  CA    . MET A 27  ? 0.1266 0.1303 0.1927 -0.0081 0.0190  0.0119  19  MET A CA    
174  C  C     . MET A 27  ? 0.1344 0.1211 0.1934 -0.0081 0.0220  0.0077  19  MET A C     
175  O  O     . MET A 27  ? 0.1573 0.1288 0.1917 -0.0177 0.0221  0.0011  19  MET A O     
176  C  CB    . MET A 27  ? 0.1495 0.1712 0.1875 -0.0078 0.0085  0.0089  19  MET A CB    
177  C  CG    . MET A 27  ? 0.1691 0.2197 0.1965 -0.0328 0.0131  0.0096  19  MET A CG    
178  S  SD    . MET A 27  ? 0.1983 0.3230 0.2154 -0.0384 -0.0044 0.0158  19  MET A SD    
179  C  CE    . MET A 27  ? 0.1907 0.3344 0.2201 -0.0185 0.0087  0.0154  19  MET A CE    
180  N  N     . CYS A 28  ? 0.1658 0.1193 0.2013 -0.0121 0.0263  0.0217  20  CYS A N     
181  C  CA    . CYS A 28  ? 0.1825 0.1294 0.2214 0.0017  0.0221  0.0129  20  CYS A CA    
182  C  C     . CYS A 28  ? 0.1674 0.1289 0.2156 0.0171  0.0317  0.0082  20  CYS A C     
183  O  O     . CYS A 28  ? 0.1553 0.1784 0.2055 0.0104  0.0209  0.0026  20  CYS A O     
184  C  CB    . CYS A 28  ? 0.1840 0.1484 0.2588 -0.0169 0.0033  0.0206  20  CYS A CB    
185  S  SG    . CYS A 28  ? 0.1636 0.1714 0.2895 -0.0080 -0.0010 0.0485  20  CYS A SG    
186  N  N     . GLY A 29  ? 0.1984 0.1213 0.2177 0.0020  0.0297  0.0033  21  GLY A N     
187  C  CA    . GLY A 29  ? 0.2012 0.1302 0.2222 0.0027  0.0352  0.0117  21  GLY A CA    
188  C  C     . GLY A 29  ? 0.1753 0.1376 0.2214 0.0005  0.0332  0.0282  21  GLY A C     
189  O  O     . GLY A 29  ? 0.1736 0.1528 0.2328 0.0112  0.0206  0.0125  21  GLY A O     
190  N  N     . ASP A 30  ? 0.1571 0.1280 0.2201 0.0005  0.0175  0.0134  22  ASP A N     
191  C  CA    . ASP A 30  ? 0.1518 0.1348 0.2227 -0.0017 0.0154  0.0205  22  ASP A CA    
192  C  C     . ASP A 30  ? 0.1417 0.1310 0.2252 0.0034  0.0130  0.0141  22  ASP A C     
193  O  O     . ASP A 30  ? 0.1387 0.1337 0.2188 -0.0079 0.0079  0.0150  22  ASP A O     
194  C  CB    . ASP A 30  ? 0.1619 0.1424 0.2242 -0.0058 0.0090  0.0263  22  ASP A CB    
195  C  CG    . ASP A 30  ? 0.1653 0.1632 0.2233 -0.0021 0.0066  0.0257  22  ASP A CG    
196  O  OD1   . ASP A 30  ? 0.1510 0.1476 0.2278 0.0010  0.0202  0.0190  22  ASP A OD1   
197  O  OD2   . ASP A 30  ? 0.2087 0.1896 0.2230 0.0151  -0.0180 0.0296  22  ASP A OD2   
198  N  N     . PRO A 31  ? 0.1378 0.1411 0.2307 -0.0062 0.0221  0.0169  23  PRO A N     
199  C  CA    . PRO A 31  ? 0.1429 0.1441 0.2343 0.0095  0.0246  0.0088  23  PRO A CA    
200  C  C     . PRO A 31  ? 0.1433 0.1462 0.2419 0.0009  0.0187  0.0180  23  PRO A C     
201  O  O     . PRO A 31  ? 0.1495 0.1586 0.2443 0.0081  0.0233  0.0108  23  PRO A O     
202  C  CB    . PRO A 31  ? 0.1538 0.1684 0.2363 -0.0016 0.0206  0.0103  23  PRO A CB    
203  C  CG    . PRO A 31  ? 0.1554 0.1696 0.2419 0.0066  0.0118  0.0071  23  PRO A CG    
204  C  CD    . PRO A 31  ? 0.1401 0.1511 0.2380 -0.0026 0.0234  0.0172  23  PRO A CD    
205  N  N     . LEU A 32  ? 0.1562 0.1417 0.2546 0.0096  0.0256  0.0288  24  LEU A N     
206  C  CA    . LEU A 32  ? 0.1511 0.1573 0.2647 0.0037  0.0255  0.0331  24  LEU A CA    
207  C  C     . LEU A 32  ? 0.1592 0.1539 0.2648 0.0097  0.0154  0.0286  24  LEU A C     
208  O  O     . LEU A 32  ? 0.1699 0.1602 0.2728 0.0114  0.0175  0.0378  24  LEU A O     
209  C  CB    . LEU A 32  ? 0.1689 0.1629 0.2733 -0.0014 0.0263  0.0498  24  LEU A CB    
210  C  CG    . LEU A 32  ? 0.2166 0.1988 0.2903 0.0001  0.0197  0.0508  24  LEU A CG    
211  C  CD1   . LEU A 32  ? 0.2242 0.2140 0.2957 0.0232  0.0040  0.0603  24  LEU A CD1   
212  C  CD2   . LEU A 32  ? 0.2445 0.2057 0.3037 -0.0243 0.0148  0.0401  24  LEU A CD2   
213  N  N     . ARG A 33  ? 0.1625 0.1352 0.2630 0.0014  0.0169  0.0260  25  ARG A N     
214  C  CA    . ARG A 33  ? 0.1710 0.1476 0.2700 0.0007  0.0142  0.0181  25  ARG A CA    
215  C  C     . ARG A 33  ? 0.1566 0.1510 0.2591 -0.0006 0.0112  0.0184  25  ARG A C     
216  O  O     . ARG A 33  ? 0.1471 0.1669 0.2481 -0.0094 0.0125  0.0207  25  ARG A O     
217  C  CB    . ARG A 33  ? 0.1883 0.1622 0.2895 -0.0080 0.0154  0.0056  25  ARG A CB    
218  C  CG    . ARG A 33  ? 0.2500 0.2296 0.3094 0.0156  0.0112  -0.0084 25  ARG A CG    
219  C  CD    . ARG A 33  ? 0.3210 0.3282 0.3289 0.0722  0.0148  -0.0047 25  ARG A CD    
220  N  NE    . ARG A 33  ? 0.3779 0.4160 0.3434 0.1032  0.0136  -0.0037 25  ARG A NE    
221  C  CZ    . ARG A 33  ? 0.4093 0.4776 0.3534 0.1332  0.0113  -0.0016 25  ARG A CZ    
222  N  NH1   . ARG A 33  ? 0.4249 0.4951 0.3597 0.1407  0.0053  0.0020  25  ARG A NH1   
223  N  NH2   . ARG A 33  ? 0.4220 0.5039 0.3580 0.1380  0.0130  -0.0038 25  ARG A NH2   
224  N  N     . ALA A 34  ? 0.1527 0.1460 0.2607 -0.0201 0.0038  0.0136  26  ALA A N     
225  C  CA    . ALA A 34  ? 0.1743 0.1725 0.2577 -0.0035 0.0032  0.0326  26  ALA A CA    
226  C  C     . ALA A 34  ? 0.1606 0.1730 0.2510 -0.0109 -0.0061 0.0298  26  ALA A C     
227  O  O     . ALA A 34  ? 0.1500 0.1870 0.2486 -0.0092 -0.0053 0.0272  26  ALA A O     
228  C  CB    . ALA A 34  ? 0.1735 0.1602 0.2632 -0.0272 0.0041  0.0379  26  ALA A CB    
229  N  N     . LYS A 35  ? 0.1561 0.1534 0.2580 -0.0008 0.0113  0.0314  27  LYS A N     
230  C  CA    . LYS A 35  ? 0.1607 0.1595 0.2689 -0.0087 0.0121  0.0187  27  LYS A CA    
231  C  C     . LYS A 35  ? 0.1680 0.1539 0.2579 0.0070  0.0140  0.0353  27  LYS A C     
232  O  O     . LYS A 35  ? 0.1599 0.1678 0.2609 0.0031  0.0020  0.0486  27  LYS A O     
233  C  CB    . LYS A 35  ? 0.1814 0.1714 0.2939 -0.0116 0.0047  0.0007  27  LYS A CB    
234  C  CG    . LYS A 35  ? 0.2064 0.1608 0.3207 -0.0114 0.0137  -0.0114 27  LYS A CG    
235  C  CD    . LYS A 35  ? 0.2519 0.1658 0.3494 -0.0117 0.0319  -0.0063 27  LYS A CD    
236  C  CE    . LYS A 35  ? 0.3184 0.1854 0.3685 -0.0006 0.0442  -0.0038 27  LYS A CE    
237  N  NZ    . LYS A 35  ? 0.3750 0.2359 0.3854 0.0364  0.0406  -0.0183 27  LYS A NZ    
238  N  N     . LEU A 36  ? 0.1720 0.1827 0.2537 0.0113  0.0168  0.0369  28  LEU A N     
239  C  CA    . LEU A 36  ? 0.1708 0.1839 0.2570 -0.0027 0.0164  0.0445  28  LEU A CA    
240  C  C     . LEU A 36  ? 0.1571 0.1804 0.2548 0.0023  0.0174  0.0393  28  LEU A C     
241  O  O     . LEU A 36  ? 0.1651 0.1968 0.2513 0.0134  0.0055  0.0523  28  LEU A O     
242  C  CB    . LEU A 36  ? 0.2178 0.2182 0.2676 -0.0102 0.0402  0.0491  28  LEU A CB    
243  C  CG    . LEU A 36  ? 0.2866 0.3049 0.2835 0.0257  0.0411  0.0436  28  LEU A CG    
244  C  CD1   . LEU A 36  ? 0.3177 0.3371 0.2874 0.0447  0.0321  0.0509  28  LEU A CD1   
245  C  CD2   . LEU A 36  ? 0.3367 0.3471 0.2909 0.0707  0.0444  0.0443  28  LEU A CD2   
246  N  N     . ILE A 37  ? 0.1399 0.1657 0.2593 -0.0061 0.0059  0.0400  29  ILE A N     
247  C  CA    . ILE A 37  ? 0.1420 0.1733 0.2635 -0.0124 -0.0049 0.0295  29  ILE A CA    
248  C  C     . ILE A 37  ? 0.1425 0.1849 0.2638 -0.0117 -0.0052 0.0312  29  ILE A C     
249  O  O     . ILE A 37  ? 0.1493 0.1955 0.2672 -0.0026 0.0026  0.0295  29  ILE A O     
250  C  CB    . ILE A 37  ? 0.1561 0.1733 0.2675 -0.0081 -0.0094 0.0214  29  ILE A CB    
251  C  CG1   . ILE A 37  ? 0.1874 0.1757 0.2701 -0.0045 -0.0020 0.0099  29  ILE A CG1   
252  C  CG2   . ILE A 37  ? 0.1639 0.1673 0.2657 -0.0151 -0.0248 0.0213  29  ILE A CG2   
253  C  CD1   . ILE A 37  ? 0.1902 0.1788 0.2713 0.0125  -0.0069 0.0175  29  ILE A CD1   
254  N  N     . ALA A 38  ? 0.1553 0.1720 0.2632 -0.0116 -0.0060 0.0371  30  ALA A N     
255  C  CA    . ALA A 38  ? 0.1586 0.1884 0.2736 -0.0299 0.0127  0.0246  30  ALA A CA    
256  C  C     . ALA A 38  ? 0.1768 0.2129 0.2874 0.0045  0.0218  0.0198  30  ALA A C     
257  O  O     . ALA A 38  ? 0.1822 0.2514 0.2907 0.0182  0.0294  0.0286  30  ALA A O     
258  C  CB    . ALA A 38  ? 0.1789 0.2169 0.2742 -0.0235 0.0178  0.0202  30  ALA A CB    
259  N  N     . ASP A 39  ? 0.1715 0.1781 0.3007 -0.0004 0.0186  0.0063  31  ASP A N     
260  C  CA    . ASP A 39  ? 0.2010 0.1909 0.3223 0.0120  0.0261  0.0098  31  ASP A CA    
261  C  C     . ASP A 39  ? 0.1929 0.1928 0.3264 0.0279  0.0274  0.0132  31  ASP A C     
262  O  O     . ASP A 39  ? 0.1993 0.2406 0.3464 0.0570  0.0220  -0.0109 31  ASP A O     
263  C  CB    . ASP A 39  ? 0.2498 0.1925 0.3444 -0.0146 0.0290  0.0178  31  ASP A CB    
264  C  CG    . ASP A 39  ? 0.3185 0.2264 0.3624 -0.0406 0.0428  0.0255  31  ASP A CG    
265  O  OD1   . ASP A 39  ? 0.3715 0.2664 0.3751 -0.0489 0.0453  -0.0016 31  ASP A OD1   
266  O  OD2   . ASP A 39  ? 0.3121 0.2422 0.3729 -0.0250 0.0383  0.0387  31  ASP A OD2   
267  N  N     . ASN A 40  ? 0.1777 0.1885 0.3144 0.0319  0.0187  0.0407  32  ASN A N     
268  C  CA    . ASN A 40  ? 0.1921 0.2113 0.3098 0.0262  0.0016  0.0561  32  ASN A CA    
269  C  C     . ASN A 40  ? 0.1901 0.2035 0.3025 0.0136  -0.0090 0.0496  32  ASN A C     
270  O  O     . ASN A 40  ? 0.2060 0.2357 0.3126 0.0064  -0.0255 0.0510  32  ASN A O     
271  C  CB    . ASN A 40  ? 0.2079 0.2660 0.3129 0.0231  0.0024  0.0716  32  ASN A CB    
272  C  CG    . ASN A 40  ? 0.2347 0.3362 0.3208 0.0415  -0.0031 0.0832  32  ASN A CG    
273  O  OD1   . ASN A 40  ? 0.2740 0.3604 0.3314 0.0510  0.0017  0.0816  32  ASN A OD1   
274  N  ND2   . ASN A 40  ? 0.2573 0.3832 0.3225 0.0773  -0.0115 0.0904  32  ASN A ND2   
275  N  N     . TYR A 41  ? 0.1742 0.1599 0.2870 -0.0013 -0.0072 0.0363  33  TYR A N     
276  C  CA    . TYR A 41  ? 0.1975 0.1480 0.2796 0.0165  0.0044  0.0239  33  TYR A CA    
277  C  C     . TYR A 41  ? 0.2177 0.1275 0.2794 -0.0078 0.0228  0.0245  33  TYR A C     
278  O  O     . TYR A 41  ? 0.2304 0.1643 0.2873 -0.0116 0.0262  0.0165  33  TYR A O     
279  C  CB    . TYR A 41  ? 0.1844 0.1468 0.2703 0.0106  -0.0056 0.0087  33  TYR A CB    
280  C  CG    . TYR A 41  ? 0.1984 0.1710 0.2577 0.0210  -0.0221 -0.0075 33  TYR A CG    
281  C  CD1   . TYR A 41  ? 0.2348 0.1937 0.2548 0.0277  -0.0166 -0.0181 33  TYR A CD1   
282  C  CD2   . TYR A 41  ? 0.2094 0.2015 0.2534 0.0309  -0.0161 -0.0214 33  TYR A CD2   
283  C  CE1   . TYR A 41  ? 0.2454 0.2047 0.2515 0.0285  -0.0183 -0.0229 33  TYR A CE1   
284  C  CE2   . TYR A 41  ? 0.2273 0.2150 0.2564 0.0357  -0.0142 -0.0328 33  TYR A CE2   
285  C  CZ    . TYR A 41  ? 0.2534 0.2205 0.2562 0.0447  -0.0133 -0.0220 33  TYR A CZ    
286  O  OH    . TYR A 41  ? 0.2780 0.2561 0.2655 0.0275  -0.0041 -0.0071 33  TYR A OH    
287  N  N     . LEU A 42  ? 0.2313 0.1249 0.2826 -0.0014 0.0388  0.0268  34  LEU A N     
288  C  CA    . LEU A 42  ? 0.2285 0.1383 0.2925 0.0052  0.0509  0.0258  34  LEU A CA    
289  C  C     . LEU A 42  ? 0.2444 0.1235 0.3037 0.0124  0.0349  0.0236  34  LEU A C     
290  O  O     . LEU A 42  ? 0.3087 0.1333 0.3140 0.0450  0.0487  0.0433  34  LEU A O     
291  C  CB    . LEU A 42  ? 0.2307 0.1748 0.2997 0.0230  0.0666  0.0430  34  LEU A CB    
292  C  CG    . LEU A 42  ? 0.2420 0.1773 0.3087 0.0190  0.0783  0.0484  34  LEU A CG    
293  C  CD1   . LEU A 42  ? 0.2692 0.2383 0.3095 0.0427  0.0804  0.0514  34  LEU A CD1   
294  C  CD2   . LEU A 42  ? 0.2501 0.1807 0.3216 0.0280  0.0772  0.0549  34  LEU A CD2   
295  N  N     . GLU A 43  ? 0.1957 0.1263 0.3036 0.0054  0.0074  0.0135  35  GLU A N     
296  C  CA    . GLU A 43  ? 0.1668 0.1231 0.3150 0.0152  -0.0065 -0.0146 35  GLU A CA    
297  C  C     . GLU A 43  ? 0.1504 0.1251 0.3077 0.0075  -0.0042 0.0019  35  GLU A C     
298  O  O     . GLU A 43  ? 0.1505 0.1295 0.3036 0.0124  -0.0054 0.0074  35  GLU A O     
299  C  CB    . GLU A 43  ? 0.1718 0.1404 0.3444 0.0066  -0.0320 -0.0382 35  GLU A CB    
300  C  CG    . GLU A 43  ? 0.2254 0.1911 0.3742 0.0159  -0.0434 -0.0428 35  GLU A CG    
301  C  CD    . GLU A 43  ? 0.2537 0.2779 0.4046 0.0050  -0.0428 -0.0298 35  GLU A CD    
302  O  OE1   . GLU A 43  ? 0.2566 0.3779 0.4198 0.0035  -0.0426 -0.0382 35  GLU A OE1   
303  O  OE2   . GLU A 43  ? 0.2970 0.3057 0.4186 0.0110  -0.0303 -0.0250 35  GLU A OE2   
304  N  N     . ASN A 44  ? 0.1380 0.1353 0.3125 0.0151  -0.0124 -0.0057 36  ASN A N     
305  C  CA    . ASN A 44  ? 0.1631 0.1677 0.3187 0.0382  -0.0226 -0.0172 36  ASN A CA    
306  C  C     . ASN A 44  ? 0.1699 0.1797 0.3324 0.0491  -0.0335 -0.0117 36  ASN A C     
307  O  O     . ASN A 44  ? 0.1878 0.2241 0.3356 0.0658  -0.0433 -0.0185 36  ASN A O     
308  C  CB    . ASN A 44  ? 0.1861 0.2126 0.3150 0.0593  -0.0253 -0.0336 36  ASN A CB    
309  C  CG    . ASN A 44  ? 0.2063 0.2153 0.3131 0.0516  -0.0150 -0.0306 36  ASN A CG    
310  O  OD1   . ASN A 44  ? 0.2333 0.2197 0.3108 0.0789  0.0061  -0.0339 36  ASN A OD1   
311  N  ND2   . ASN A 44  ? 0.1876 0.2299 0.3129 0.0244  -0.0084 -0.0267 36  ASN A ND2   
312  N  N     . ALA A 45  ? 0.1566 0.1461 0.3376 0.0123  -0.0367 0.0002  37  ALA A N     
313  C  CA    . ALA A 45  ? 0.1556 0.1660 0.3330 -0.0001 -0.0370 -0.0103 37  ALA A CA    
314  C  C     . ALA A 45  ? 0.1523 0.1410 0.3346 0.0146  -0.0223 -0.0108 37  ALA A C     
315  O  O     . ALA A 45  ? 0.1741 0.1553 0.3506 0.0283  -0.0372 -0.0123 37  ALA A O     
316  C  CB    . ALA A 45  ? 0.1713 0.1974 0.3320 0.0079  -0.0366 -0.0249 37  ALA A CB    
317  N  N     . LYS A 46  ? 0.1272 0.1601 0.3272 0.0079  -0.0118 -0.0189 38  LYS A N     
318  C  CA    . LYS A 46  ? 0.1241 0.1950 0.3245 -0.0021 0.0097  -0.0452 38  LYS A CA    
319  C  C     . LYS A 46  ? 0.1313 0.1338 0.3119 0.0058  0.0016  -0.0404 38  LYS A C     
320  O  O     . LYS A 46  ? 0.1347 0.1347 0.3052 0.0095  0.0069  -0.0246 38  LYS A O     
321  C  CB    . LYS A 46  ? 0.1716 0.3060 0.3338 0.0177  0.0290  -0.0548 38  LYS A CB    
322  C  CG    . LYS A 46  ? 0.2601 0.4185 0.3464 0.0653  0.0491  -0.0449 38  LYS A CG    
323  C  CD    . LYS A 46  ? 0.3234 0.5030 0.3593 0.1135  0.0529  -0.0375 38  LYS A CD    
324  C  CE    . LYS A 46  ? 0.3601 0.5576 0.3678 0.1324  0.0542  -0.0259 38  LYS A CE    
325  N  NZ    . LYS A 46  ? 0.3975 0.5962 0.3742 0.1562  0.0544  -0.0238 38  LYS A NZ    
326  N  N     . GLN A 47  ? 0.1351 0.1432 0.3162 0.0038  0.0064  -0.0264 39  GLN A N     
327  C  CA    . GLN A 47  ? 0.1400 0.1553 0.3149 -0.0009 0.0184  -0.0244 39  GLN A CA    
328  C  C     . GLN A 47  ? 0.1547 0.1675 0.2968 0.0100  0.0104  -0.0430 39  GLN A C     
329  O  O     . GLN A 47  ? 0.2030 0.2081 0.3021 0.0475  -0.0149 -0.0593 39  GLN A O     
330  C  CB    . GLN A 47  ? 0.1518 0.1740 0.3421 -0.0117 0.0345  -0.0018 39  GLN A CB    
331  C  CG    . GLN A 47  ? 0.1726 0.2146 0.3699 -0.0214 0.0392  0.0172  39  GLN A CG    
332  C  CD    . GLN A 47  ? 0.2205 0.2903 0.4007 -0.0436 0.0259  0.0376  39  GLN A CD    
333  O  OE1   . GLN A 47  ? 0.2588 0.3655 0.4225 -0.0580 0.0187  0.0429  39  GLN A OE1   
334  N  NE2   . GLN A 47  ? 0.2778 0.2991 0.4078 -0.0246 0.0297  0.0649  39  GLN A NE2   
335  N  N     . VAL A 48  ? 0.1439 0.1467 0.2758 0.0124  0.0307  -0.0269 40  VAL A N     
336  C  CA    . VAL A 48  ? 0.1578 0.1701 0.2661 0.0050  0.0194  -0.0127 40  VAL A CA    
337  C  C     . VAL A 48  ? 0.1622 0.1847 0.2600 -0.0043 0.0157  -0.0034 40  VAL A C     
338  O  O     . VAL A 48  ? 0.1673 0.2271 0.2559 -0.0080 0.0064  -0.0038 40  VAL A O     
339  C  CB    . VAL A 48  ? 0.1570 0.1730 0.2675 -0.0002 0.0193  -0.0107 40  VAL A CB    
340  C  CG1   . VAL A 48  ? 0.1588 0.2109 0.2690 0.0056  0.0265  -0.0101 40  VAL A CG1   
341  C  CG2   . VAL A 48  ? 0.1653 0.1785 0.2705 0.0126  0.0254  -0.0058 40  VAL A CG2   
342  N  N     . ASN A 49  ? 0.1519 0.1997 0.2611 0.0028  0.0238  -0.0087 41  ASN A N     
343  C  CA    . ASN A 49  ? 0.1286 0.2012 0.2727 -0.0030 0.0298  -0.0129 41  ASN A CA    
344  C  C     . ASN A 49  ? 0.1072 0.1645 0.2844 0.0061  0.0235  -0.0181 41  ASN A C     
345  O  O     . ASN A 49  ? 0.1419 0.1662 0.2868 0.0020  0.0191  -0.0348 41  ASN A O     
346  C  CB    . ASN A 49  ? 0.1447 0.2125 0.2771 -0.0070 0.0267  0.0016  41  ASN A CB    
347  C  CG    . ASN A 49  ? 0.1664 0.2306 0.2797 0.0085  0.0140  -0.0034 41  ASN A CG    
348  O  OD1   . ASN A 49  ? 0.1642 0.2106 0.2891 0.0079  0.0129  0.0145  41  ASN A OD1   
349  N  ND2   . ASN A 49  ? 0.1926 0.3009 0.2850 0.0148  0.0131  -0.0229 41  ASN A ND2   
350  N  N     . SER A 50  ? 0.1335 0.1685 0.2955 0.0029  0.0248  -0.0173 42  SER A N     
351  C  CA    . SER A 50  ? 0.1537 0.1901 0.3148 -0.0118 0.0327  -0.0104 42  SER A CA    
352  C  C     . SER A 50  ? 0.1454 0.1639 0.3097 -0.0082 0.0233  -0.0162 42  SER A C     
353  O  O     . SER A 50  ? 0.1507 0.1502 0.3147 0.0022  0.0210  -0.0101 42  SER A O     
354  C  CB    . SER A 50  ? 0.2116 0.2541 0.3395 0.0067  0.0471  -0.0203 42  SER A CB    
355  O  OG    . SER A 50  ? 0.2771 0.2336 0.3565 0.0177  0.0607  -0.0446 42  SER A OG    
356  N  N     . VAL A 51  ? 0.1443 0.1622 0.3009 -0.0081 0.0146  -0.0232 43  VAL A N     
357  C  CA    . VAL A 51  ? 0.1441 0.1517 0.2920 -0.0118 0.0220  -0.0093 43  VAL A CA    
358  C  C     . VAL A 51  ? 0.1388 0.1382 0.2819 0.0037  0.0353  0.0157  43  VAL A C     
359  O  O     . VAL A 51  ? 0.1591 0.1291 0.2760 -0.0054 0.0339  0.0017  43  VAL A O     
360  C  CB    . VAL A 51  ? 0.1547 0.1881 0.2920 -0.0003 0.0127  -0.0188 43  VAL A CB    
361  C  CG1   . VAL A 51  ? 0.1478 0.1950 0.2888 -0.0002 0.0004  -0.0156 43  VAL A CG1   
362  C  CG2   . VAL A 51  ? 0.1811 0.2389 0.2971 0.0214  0.0120  -0.0241 43  VAL A CG2   
363  N  N     . ARG A 52  ? 0.1371 0.1452 0.2800 0.0020  0.0365  0.0126  44  ARG A N     
364  C  CA    . ARG A 52  ? 0.1553 0.1513 0.2766 0.0098  0.0392  0.0236  44  ARG A CA    
365  C  C     . ARG A 52  ? 0.1490 0.1571 0.2695 -0.0048 0.0473  0.0269  44  ARG A C     
366  O  O     . ARG A 52  ? 0.1607 0.2021 0.2666 0.0040  0.0547  0.0306  44  ARG A O     
367  C  CB    . ARG A 52  ? 0.1566 0.1607 0.2856 0.0149  0.0279  0.0305  44  ARG A CB    
368  C  CG    . ARG A 52  ? 0.1623 0.1623 0.2946 0.0015  0.0181  0.0416  44  ARG A CG    
369  C  CD    . ARG A 52  ? 0.1699 0.1598 0.3046 -0.0096 0.0060  0.0430  44  ARG A CD    
370  N  NE    . ARG A 52  ? 0.2011 0.1739 0.3158 0.0218  0.0083  0.0429  44  ARG A NE    
371  C  CZ    . ARG A 52  ? 0.1924 0.1734 0.3267 0.0237  -0.0049 0.0457  44  ARG A CZ    
372  N  NH1   . ARG A 52  ? 0.1652 0.1625 0.3325 -0.0007 0.0018  0.0554  44  ARG A NH1   
373  N  NH2   . ARG A 52  ? 0.2411 0.1914 0.3344 0.0231  -0.0094 0.0139  44  ARG A NH2   
374  N  N     . GLY A 53  ? 0.1470 0.1320 0.2656 -0.0105 0.0188  0.0091  45  GLY A N     
375  C  CA    . GLY A 53  ? 0.1743 0.1499 0.2564 -0.0016 0.0159  0.0119  45  GLY A CA    
376  C  C     . GLY A 53  ? 0.1582 0.1503 0.2430 -0.0117 0.0196  0.0103  45  GLY A C     
377  O  O     . GLY A 53  ? 0.1704 0.1535 0.2364 0.0018  0.0256  0.0114  45  GLY A O     
378  N  N     . MET A 54  ? 0.1355 0.1420 0.2351 -0.0086 0.0274  0.0028  46  MET A N     
379  C  CA    . MET A 54  ? 0.1355 0.1364 0.2327 -0.0091 0.0298  -0.0007 46  MET A CA    
380  C  C     . MET A 54  ? 0.1480 0.1361 0.2407 -0.0064 0.0394  0.0038  46  MET A C     
381  O  O     . MET A 54  ? 0.1419 0.1496 0.2519 0.0002  0.0354  0.0068  46  MET A O     
382  C  CB    . MET A 54  ? 0.1401 0.1509 0.2298 -0.0117 0.0375  0.0062  46  MET A CB    
383  C  CG    . MET A 54  ? 0.1402 0.1445 0.2273 -0.0163 0.0393  -0.0004 46  MET A CG    
384  S  SD    . MET A 54  ? 0.1598 0.1525 0.2347 0.0013  0.0324  -0.0095 46  MET A SD    
385  C  CE    . MET A 54  ? 0.1766 0.2091 0.2443 -0.0350 0.0427  -0.0334 46  MET A CE    
386  N  N     . LEU A 55  ? 0.1392 0.1509 0.2388 0.0038  0.0342  -0.0027 47  LEU A N     
387  C  CA    . LEU A 55  ? 0.1434 0.1426 0.2335 0.0045  0.0338  -0.0090 47  LEU A CA    
388  C  C     . LEU A 55  ? 0.1405 0.1268 0.2252 -0.0097 0.0337  -0.0154 47  LEU A C     
389  O  O     . LEU A 55  ? 0.1373 0.1373 0.2256 0.0029  0.0255  -0.0192 47  LEU A O     
390  C  CB    . LEU A 55  ? 0.1611 0.1365 0.2404 -0.0034 0.0314  -0.0035 47  LEU A CB    
391  C  CG    . LEU A 55  ? 0.1813 0.1523 0.2427 -0.0181 0.0243  0.0054  47  LEU A CG    
392  C  CD1   . LEU A 55  ? 0.2122 0.1648 0.2389 0.0096  0.0289  0.0324  47  LEU A CD1   
393  C  CD2   . LEU A 55  ? 0.2237 0.1660 0.2509 -0.0123 0.0186  0.0086  47  LEU A CD2   
394  N  N     . GLY A 56  ? 0.1308 0.1381 0.2173 -0.0038 0.0547  -0.0070 48  GLY A N     
395  C  CA    . GLY A 56  ? 0.1274 0.1486 0.2074 -0.0123 0.0364  -0.0097 48  GLY A CA    
396  C  C     . GLY A 56  ? 0.1368 0.1310 0.1995 0.0097  0.0242  -0.0117 48  GLY A C     
397  O  O     . GLY A 56  ? 0.1342 0.1335 0.1999 0.0041  0.0286  -0.0234 48  GLY A O     
398  N  N     . PHE A 57  ? 0.1254 0.1351 0.1984 0.0019  0.0272  -0.0145 49  PHE A N     
399  C  CA    . PHE A 57  ? 0.1281 0.1517 0.1997 0.0011  0.0282  0.0018  49  PHE A CA    
400  C  C     . PHE A 57  ? 0.1228 0.1377 0.2040 0.0031  0.0181  0.0008  49  PHE A C     
401  O  O     . PHE A 57  ? 0.1473 0.1321 0.2103 0.0034  0.0161  -0.0060 49  PHE A O     
402  C  CB    . PHE A 57  ? 0.1314 0.1676 0.1972 0.0009  0.0202  0.0028  49  PHE A CB    
403  C  CG    . PHE A 57  ? 0.1502 0.1582 0.2043 -0.0095 0.0211  0.0065  49  PHE A CG    
404  C  CD1   . PHE A 57  ? 0.1558 0.1681 0.2058 -0.0121 0.0243  0.0035  49  PHE A CD1   
405  C  CD2   . PHE A 57  ? 0.1728 0.1686 0.2132 -0.0020 0.0106  0.0065  49  PHE A CD2   
406  C  CE1   . PHE A 57  ? 0.1659 0.1809 0.2096 -0.0258 0.0141  0.0004  49  PHE A CE1   
407  C  CE2   . PHE A 57  ? 0.1822 0.1697 0.2158 -0.0096 0.0179  0.0206  49  PHE A CE2   
408  C  CZ    . PHE A 57  ? 0.1864 0.1740 0.2128 -0.0293 0.0136  0.0073  49  PHE A CZ    
409  N  N     . THR A 58  ? 0.1248 0.1425 0.2108 0.0115  0.0169  -0.0109 50  THR A N     
410  C  CA    . THR A 58  ? 0.1100 0.1385 0.2262 0.0061  0.0095  -0.0067 50  THR A CA    
411  C  C     . THR A 58  ? 0.1220 0.1179 0.2379 0.0130  0.0087  -0.0012 50  THR A C     
412  O  O     . THR A 58  ? 0.1312 0.1240 0.2558 0.0195  0.0083  -0.0051 50  THR A O     
413  C  CB    . THR A 58  ? 0.1220 0.1462 0.2329 0.0084  0.0207  -0.0055 50  THR A CB    
414  O  OG1   . THR A 58  ? 0.1295 0.1637 0.2434 0.0145  0.0200  0.0006  50  THR A OG1   
415  C  CG2   . THR A 58  ? 0.1391 0.1813 0.2328 0.0235  0.0174  0.0032  50  THR A CG2   
416  N  N     . GLY A 59  ? 0.1182 0.1213 0.2293 0.0119  0.0073  -0.0065 51  GLY A N     
417  C  CA    . GLY A 59  ? 0.1167 0.1245 0.2288 0.0073  0.0036  0.0026  51  GLY A CA    
418  C  C     . GLY A 59  ? 0.1279 0.1273 0.2309 0.0207  0.0107  0.0154  51  GLY A C     
419  O  O     . GLY A 59  ? 0.1268 0.1423 0.2335 0.0122  0.0146  0.0182  51  GLY A O     
420  N  N     . THR A 60  ? 0.1342 0.1401 0.2388 0.0148  0.0005  0.0132  52  THR A N     
421  C  CA    . THR A 60  ? 0.1163 0.1448 0.2409 -0.0122 0.0037  0.0102  52  THR A CA    
422  C  C     . THR A 60  ? 0.1230 0.1372 0.2493 0.0023  0.0027  0.0234  52  THR A C     
423  O  O     . THR A 60  ? 0.1371 0.1355 0.2528 -0.0046 0.0063  0.0191  52  THR A O     
424  C  CB    . THR A 60  ? 0.1355 0.1652 0.2417 0.0020  0.0009  0.0025  52  THR A CB    
425  O  OG1   . THR A 60  ? 0.1460 0.1659 0.2447 0.0116  -0.0048 0.0030  52  THR A OG1   
426  C  CG2   . THR A 60  ? 0.1456 0.1760 0.2393 0.0190  0.0002  -0.0023 52  THR A CG2   
427  N  N     . TYR A 61  ? 0.1293 0.1295 0.2487 0.0111  -0.0050 0.0187  53  TYR A N     
428  C  CA    . TYR A 61  ? 0.1364 0.1337 0.2629 0.0116  -0.0023 0.0174  53  TYR A CA    
429  C  C     . TYR A 61  ? 0.1198 0.1312 0.2727 0.0042  0.0123  0.0188  53  TYR A C     
430  O  O     . TYR A 61  ? 0.1295 0.1351 0.2742 0.0000  0.0122  0.0168  53  TYR A O     
431  C  CB    . TYR A 61  ? 0.1380 0.1413 0.2647 0.0052  0.0099  0.0218  53  TYR A CB    
432  C  CG    . TYR A 61  ? 0.1305 0.1411 0.2620 -0.0121 0.0004  0.0195  53  TYR A CG    
433  C  CD1   . TYR A 61  ? 0.1510 0.1495 0.2584 0.0004  0.0033  0.0253  53  TYR A CD1   
434  C  CD2   . TYR A 61  ? 0.1244 0.1629 0.2585 0.0043  0.0027  0.0083  53  TYR A CD2   
435  C  CE1   . TYR A 61  ? 0.1483 0.1644 0.2547 0.0058  -0.0009 0.0207  53  TYR A CE1   
436  C  CE2   . TYR A 61  ? 0.1381 0.1763 0.2535 0.0115  0.0058  0.0019  53  TYR A CE2   
437  C  CZ    . TYR A 61  ? 0.1342 0.1842 0.2537 0.0108  -0.0129 0.0024  53  TYR A CZ    
438  O  OH    . TYR A 61  ? 0.1470 0.2195 0.2605 0.0186  -0.0051 -0.0084 53  TYR A OH    
439  N  N     . LYS A 62  ? 0.1246 0.1453 0.2821 0.0082  0.0110  0.0166  54  LYS A N     
440  C  CA    . LYS A 62  ? 0.1258 0.1581 0.2861 -0.0126 0.0138  0.0080  54  LYS A CA    
441  C  C     . LYS A 62  ? 0.1181 0.1607 0.2848 -0.0111 0.0125  0.0092  54  LYS A C     
442  O  O     . LYS A 62  ? 0.1212 0.1748 0.2904 -0.0024 0.0182  0.0101  54  LYS A O     
443  C  CB    . LYS A 62  ? 0.1394 0.1833 0.2978 -0.0018 -0.0058 -0.0150 54  LYS A CB    
444  C  CG    . LYS A 62  ? 0.1348 0.1943 0.3090 0.0090  -0.0193 -0.0144 54  LYS A CG    
445  C  CD    . LYS A 62  ? 0.1434 0.2051 0.3207 -0.0012 -0.0176 -0.0183 54  LYS A CD    
446  C  CE    . LYS A 62  ? 0.1487 0.2020 0.3296 0.0019  -0.0066 -0.0200 54  LYS A CE    
447  N  NZ    . LYS A 62  ? 0.1627 0.2400 0.3379 0.0126  -0.0041 -0.0262 54  LYS A NZ    
448  N  N     . GLY A 63  ? 0.1204 0.1680 0.2789 0.0012  0.0130  0.0058  55  GLY A N     
449  C  CA    . GLY A 63  ? 0.1234 0.1612 0.2736 0.0056  0.0157  0.0027  55  GLY A CA    
450  C  C     . GLY A 63  ? 0.1426 0.1681 0.2768 0.0066  0.0238  -0.0025 55  GLY A C     
451  O  O     . GLY A 63  ? 0.1575 0.2036 0.2862 0.0038  0.0333  0.0069  55  GLY A O     
452  N  N     . LYS A 64  ? 0.1194 0.1484 0.2737 0.0003  0.0315  0.0082  56  LYS A N     
453  C  CA    . LYS A 64  ? 0.1331 0.1545 0.2637 0.0083  0.0270  0.0137  56  LYS A CA    
454  C  C     . LYS A 64  ? 0.1355 0.1605 0.2532 0.0095  0.0335  0.0130  56  LYS A C     
455  O  O     . LYS A 64  ? 0.1390 0.1515 0.2533 0.0065  0.0243  0.0161  56  LYS A O     
456  C  CB    . LYS A 64  ? 0.1432 0.1823 0.2686 0.0165  0.0272  0.0083  56  LYS A CB    
457  C  CG    . LYS A 64  ? 0.1555 0.1743 0.2810 0.0219  0.0254  0.0139  56  LYS A CG    
458  C  CD    . LYS A 64  ? 0.1613 0.1605 0.2891 0.0049  0.0296  0.0206  56  LYS A CD    
459  C  CE    . LYS A 64  ? 0.1913 0.1772 0.2894 0.0314  0.0307  0.0315  56  LYS A CE    
460  N  NZ    . LYS A 64  ? 0.2124 0.2018 0.2910 0.0355  0.0270  0.0360  56  LYS A NZ    
461  N  N     . PRO A 65  ? 0.1417 0.1759 0.2420 -0.0054 0.0351  0.0092  57  PRO A N     
462  C  CA    . PRO A 65  ? 0.1362 0.1869 0.2336 0.0012  0.0239  0.0081  57  PRO A CA    
463  C  C     . PRO A 65  ? 0.1245 0.1531 0.2279 0.0020  0.0314  0.0284  57  PRO A C     
464  O  O     . PRO A 65  ? 0.1530 0.1395 0.2552 0.0173  0.0366  0.0259  57  PRO A O     
465  C  CB    . PRO A 65  ? 0.1570 0.2189 0.2379 0.0069  0.0230  0.0004  57  PRO A CB    
466  C  CG    . PRO A 65  ? 0.1744 0.2437 0.2420 0.0128  0.0406  0.0079  57  PRO A CG    
467  C  CD    . PRO A 65  ? 0.1635 0.2219 0.2418 0.0080  0.0482  0.0088  57  PRO A CD    
468  N  N     . LEU A 66  ? 0.1241 0.1536 0.2163 0.0024  0.0226  0.0268  58  LEU A N     
469  C  CA    . LEU A 66  ? 0.1111 0.1521 0.2134 -0.0012 0.0161  0.0238  58  LEU A CA    
470  C  C     . LEU A 66  ? 0.1256 0.1439 0.2093 0.0218  0.0283  0.0178  58  LEU A C     
471  O  O     . LEU A 66  ? 0.1344 0.1278 0.2215 0.0173  0.0368  0.0113  58  LEU A O     
472  C  CB    . LEU A 66  ? 0.1298 0.1541 0.2244 0.0021  0.0071  0.0110  58  LEU A CB    
473  C  CG    . LEU A 66  ? 0.1373 0.1494 0.2291 0.0012  0.0031  0.0091  58  LEU A CG    
474  C  CD1   . LEU A 66  ? 0.1473 0.1368 0.2297 0.0038  0.0084  -0.0077 58  LEU A CD1   
475  C  CD2   . LEU A 66  ? 0.1473 0.1643 0.2344 0.0175  -0.0116 -0.0022 58  LEU A CD2   
476  N  N     . SER A 67  ? 0.1202 0.1369 0.2010 0.0118  0.0419  0.0136  59  SER A N     
477  C  CA    . SER A 67  ? 0.1250 0.1372 0.1970 0.0122  0.0324  0.0060  59  SER A CA    
478  C  C     . SER A 67  ? 0.1152 0.1204 0.2048 -0.0078 0.0218  0.0122  59  SER A C     
479  O  O     . SER A 67  ? 0.1277 0.1255 0.2010 0.0022  0.0152  0.0062  59  SER A O     
480  C  CB    . SER A 67  ? 0.1631 0.1359 0.1907 0.0155  0.0266  -0.0023 59  SER A CB    
481  O  OG    . SER A 67  ? 0.1521 0.1514 0.1959 0.0121  0.0139  0.0072  59  SER A OG    
482  N  N     . VAL A 68  ? 0.1335 0.1247 0.2131 0.0156  0.0242  0.0067  60  VAL A N     
483  C  CA    A VAL A 68  ? 0.1294 0.1299 0.2116 0.0070  0.0264  0.0046  60  VAL A CA    
484  C  CA    B VAL A 68  ? 0.1412 0.1266 0.2165 -0.0055 0.0181  0.0027  60  VAL A CA    
485  C  C     . VAL A 68  ? 0.1349 0.1271 0.2104 0.0043  0.0211  0.0008  60  VAL A C     
486  O  O     . VAL A 68  ? 0.1445 0.1240 0.2084 0.0020  0.0326  -0.0097 60  VAL A O     
487  C  CB    A VAL A 68  ? 0.1342 0.1435 0.2143 0.0129  0.0266  0.0129  60  VAL A CB    
488  C  CB    B VAL A 68  ? 0.1688 0.1457 0.2294 -0.0255 0.0038  0.0061  60  VAL A CB    
489  C  CG1   A VAL A 68  ? 0.1304 0.1418 0.2107 0.0256  0.0447  0.0275  60  VAL A CG1   
490  C  CG1   B VAL A 68  ? 0.1867 0.1618 0.2340 -0.0283 -0.0033 -0.0028 60  VAL A CG1   
491  C  CG2   A VAL A 68  ? 0.1507 0.1723 0.2187 0.0116  0.0113  0.0061  60  VAL A CG2   
492  C  CG2   B VAL A 68  ? 0.1780 0.1526 0.2323 -0.0293 -0.0020 0.0142  60  VAL A CG2   
493  N  N     . MET A 69  ? 0.1390 0.1323 0.2189 0.0070  0.0327  -0.0060 61  MET A N     
494  C  CA    . MET A 69  ? 0.1314 0.1481 0.2272 0.0077  0.0303  -0.0029 61  MET A CA    
495  C  C     . MET A 69  ? 0.1364 0.1316 0.2286 0.0028  0.0269  -0.0083 61  MET A C     
496  O  O     . MET A 69  ? 0.1387 0.1396 0.2368 -0.0053 0.0370  -0.0139 61  MET A O     
497  C  CB    . MET A 69  ? 0.1484 0.1978 0.2375 0.0081  0.0163  -0.0060 61  MET A CB    
498  C  CG    . MET A 69  ? 0.1701 0.2682 0.2478 0.0298  0.0164  -0.0198 61  MET A CG    
499  S  SD    . MET A 69  ? 0.1934 0.3726 0.2633 0.0370  0.0124  -0.0446 61  MET A SD    
500  C  CE    . MET A 69  ? 0.2051 0.3775 0.2667 0.0459  0.0128  -0.0370 61  MET A CE    
501  N  N     . GLY A 70  ? 0.1189 0.1261 0.2341 -0.0078 0.0282  0.0007  62  GLY A N     
502  C  CA    . GLY A 70  ? 0.1241 0.1332 0.2358 0.0149  0.0327  0.0005  62  GLY A CA    
503  C  C     . GLY A 70  ? 0.1260 0.1390 0.2224 0.0009  0.0248  -0.0105 62  GLY A C     
504  O  O     . GLY A 70  ? 0.1295 0.1603 0.2173 0.0048  0.0272  -0.0036 62  GLY A O     
505  N  N     . HIS A 71  ? 0.1410 0.1362 0.2109 0.0174  0.0225  -0.0057 63  HIS A N     
506  C  CA    . HIS A 71  ? 0.1229 0.1333 0.2063 0.0066  0.0220  -0.0002 63  HIS A CA    
507  C  C     . HIS A 71  ? 0.1171 0.1323 0.2019 -0.0007 0.0229  -0.0056 63  HIS A C     
508  O  O     . HIS A 71  ? 0.1108 0.1584 0.2101 0.0079  0.0137  -0.0031 63  HIS A O     
509  C  CB    . HIS A 71  ? 0.1426 0.1507 0.2032 0.0094  0.0187  0.0123  63  HIS A CB    
510  C  CG    . HIS A 71  ? 0.1419 0.1461 0.1904 0.0048  0.0387  0.0173  63  HIS A CG    
511  N  ND1   . HIS A 71  ? 0.1475 0.1298 0.1892 -0.0156 0.0322  0.0108  63  HIS A ND1   
512  C  CD2   . HIS A 71  ? 0.1317 0.1520 0.1873 0.0079  0.0274  0.0093  63  HIS A CD2   
513  C  CE1   . HIS A 71  ? 0.1526 0.1283 0.1984 -0.0077 0.0275  0.0204  63  HIS A CE1   
514  N  NE2   . HIS A 71  ? 0.1461 0.1319 0.1933 0.0057  0.0239  0.0155  63  HIS A NE2   
515  N  N     . GLY A 72  ? 0.1292 0.1412 0.2002 0.0030  0.0337  0.0049  64  GLY A N     
516  C  CA    . GLY A 72  ? 0.1351 0.1357 0.2016 -0.0060 0.0301  0.0045  64  GLY A CA    
517  C  C     . GLY A 72  ? 0.1390 0.1367 0.1964 -0.0125 0.0287  0.0135  64  GLY A C     
518  O  O     . GLY A 72  ? 0.1634 0.1732 0.2230 -0.0380 0.0520  -0.0236 64  GLY A O     
519  N  N     . MET A 73  ? 0.1257 0.1200 0.1751 -0.0062 0.0166  0.0181  65  MET A N     
520  C  CA    . MET A 73  ? 0.1265 0.1074 0.1570 0.0049  -0.0001 0.0135  65  MET A CA    
521  C  C     . MET A 73  ? 0.1233 0.1141 0.1493 -0.0027 -0.0018 0.0173  65  MET A C     
522  O  O     . MET A 73  ? 0.1315 0.1150 0.1643 -0.0068 -0.0179 0.0110  65  MET A O     
523  C  CB    . MET A 73  ? 0.1445 0.1318 0.1454 0.0190  -0.0027 0.0192  65  MET A CB    
524  C  CG    . MET A 73  ? 0.1440 0.1409 0.1417 0.0190  -0.0088 0.0116  65  MET A CG    
525  S  SD    . MET A 73  ? 0.1710 0.1665 0.1451 0.0174  0.0070  0.0324  65  MET A SD    
526  C  CE    . MET A 73  ? 0.2054 0.1488 0.1621 0.0206  0.0254  0.0362  65  MET A CE    
527  N  N     . GLY A 74  ? 0.1340 0.1061 0.1349 -0.0074 -0.0089 0.0145  66  GLY A N     
528  C  CA    . GLY A 74  ? 0.1313 0.1077 0.1299 0.0162  -0.0063 0.0143  66  GLY A CA    
529  C  C     . GLY A 74  ? 0.1093 0.1217 0.1297 0.0006  0.0013  -0.0013 66  GLY A C     
530  O  O     . GLY A 74  ? 0.1361 0.1136 0.1411 0.0047  0.0048  0.0063  66  GLY A O     
531  N  N     . ILE A 75  ? 0.1075 0.1125 0.1339 0.0072  0.0150  0.0139  67  ILE A N     
532  C  CA    . ILE A 75  ? 0.0995 0.1318 0.1258 -0.0001 0.0077  0.0184  67  ILE A CA    
533  C  C     . ILE A 75  ? 0.1011 0.1245 0.1218 0.0078  0.0139  0.0079  67  ILE A C     
534  O  O     . ILE A 75  ? 0.1176 0.1221 0.1223 0.0005  0.0063  0.0123  67  ILE A O     
535  C  CB    . ILE A 75  ? 0.1118 0.1196 0.1147 -0.0054 0.0102  0.0129  67  ILE A CB    
536  C  CG1   . ILE A 75  ? 0.1152 0.1132 0.1265 -0.0119 0.0092  0.0070  67  ILE A CG1   
537  C  CG2   . ILE A 75  ? 0.1450 0.1302 0.1083 0.0021  0.0161  0.0138  67  ILE A CG2   
538  C  CD1   . ILE A 75  ? 0.1435 0.1319 0.1357 0.0096  0.0081  -0.0039 67  ILE A CD1   
539  N  N     . PRO A 76  ? 0.1035 0.1228 0.1088 0.0062  0.0090  0.0126  68  PRO A N     
540  C  CA    . PRO A 76  ? 0.1115 0.1363 0.1183 0.0170  -0.0015 0.0051  68  PRO A CA    
541  C  C     . PRO A 76  ? 0.1124 0.1201 0.1201 0.0040  0.0098  -0.0018 68  PRO A C     
542  O  O     . PRO A 76  ? 0.1378 0.1269 0.1234 0.0107  0.0205  -0.0025 68  PRO A O     
543  C  CB    . PRO A 76  ? 0.1164 0.1309 0.1258 -0.0097 -0.0021 -0.0126 68  PRO A CB    
544  C  CG    . PRO A 76  ? 0.1118 0.1321 0.1182 -0.0064 -0.0017 0.0088  68  PRO A CG    
545  C  CD    . PRO A 76  ? 0.1096 0.1333 0.1140 0.0067  -0.0008 0.0124  68  PRO A CD    
546  N  N     . SER A 77  ? 0.1121 0.1245 0.1458 0.0133  0.0020  0.0087  69  SER A N     
547  C  CA    . SER A 77  ? 0.1063 0.1307 0.1554 0.0085  -0.0040 0.0111  69  SER A CA    
548  C  C     . SER A 77  ? 0.1228 0.1197 0.1461 0.0155  0.0051  -0.0071 69  SER A C     
549  O  O     . SER A 77  ? 0.1322 0.1246 0.1510 0.0005  0.0127  0.0049  69  SER A O     
550  C  CB    . SER A 77  ? 0.1137 0.1318 0.1663 0.0138  -0.0010 0.0264  69  SER A CB    
551  O  OG    . SER A 77  ? 0.1251 0.1317 0.1858 0.0118  0.0215  0.0249  69  SER A OG    
552  N  N     . ILE A 78  ? 0.1239 0.1209 0.1394 0.0029  0.0021  -0.0110 70  ILE A N     
553  C  CA    . ILE A 78  ? 0.1201 0.1316 0.1373 0.0037  0.0080  -0.0078 70  ILE A CA    
554  C  C     . ILE A 78  ? 0.1215 0.1247 0.1376 -0.0062 0.0233  -0.0067 70  ILE A C     
555  O  O     . ILE A 78  ? 0.1315 0.1336 0.1330 0.0007  0.0206  -0.0057 70  ILE A O     
556  C  CB    . ILE A 78  ? 0.1284 0.1288 0.1439 -0.0013 0.0115  -0.0043 70  ILE A CB    
557  C  CG1   . ILE A 78  ? 0.1414 0.1363 0.1381 0.0013  0.0023  -0.0125 70  ILE A CG1   
558  C  CG2   . ILE A 78  ? 0.1280 0.1389 0.1584 0.0043  0.0107  -0.0158 70  ILE A CG2   
559  C  CD1   . ILE A 78  ? 0.1345 0.1585 0.1410 -0.0059 0.0131  -0.0057 70  ILE A CD1   
560  N  N     . SER A 79  ? 0.1172 0.1218 0.1439 0.0006  0.0088  -0.0016 71  SER A N     
561  C  CA    . SER A 79  ? 0.1267 0.1368 0.1385 -0.0023 0.0056  0.0004  71  SER A CA    
562  C  C     . SER A 79  ? 0.1244 0.1320 0.1330 -0.0110 0.0107  0.0106  71  SER A C     
563  O  O     . SER A 79  ? 0.1404 0.1390 0.1297 -0.0038 0.0229  0.0135  71  SER A O     
564  C  CB    . SER A 79  ? 0.1238 0.1200 0.1482 -0.0068 0.0045  -0.0004 71  SER A CB    
565  O  OG    . SER A 79  ? 0.1442 0.1225 0.1500 0.0017  0.0118  0.0065  71  SER A OG    
566  N  N     . ILE A 80  ? 0.1242 0.1343 0.1340 -0.0081 0.0159  -0.0029 72  ILE A N     
567  C  CA    . ILE A 80  ? 0.1251 0.1294 0.1316 0.0049  0.0045  -0.0160 72  ILE A CA    
568  C  C     . ILE A 80  ? 0.1324 0.1192 0.1381 -0.0009 0.0167  -0.0106 72  ILE A C     
569  O  O     . ILE A 80  ? 0.1327 0.1456 0.1395 0.0191  0.0302  -0.0173 72  ILE A O     
570  C  CB    . ILE A 80  ? 0.1304 0.1278 0.1358 0.0166  -0.0036 -0.0044 72  ILE A CB    
571  C  CG1   . ILE A 80  ? 0.1318 0.1336 0.1433 0.0026  -0.0002 -0.0118 72  ILE A CG1   
572  C  CG2   . ILE A 80  ? 0.1487 0.1378 0.1401 -0.0043 0.0106  -0.0107 72  ILE A CG2   
573  C  CD1   . ILE A 80  ? 0.1507 0.1570 0.1551 0.0036  0.0028  -0.0009 72  ILE A CD1   
574  N  N     . TYR A 81  ? 0.1192 0.1341 0.1527 0.0065  0.0039  -0.0125 73  TYR A N     
575  C  CA    . TYR A 81  ? 0.1241 0.1405 0.1688 0.0072  0.0004  -0.0129 73  TYR A CA    
576  C  C     . TYR A 81  ? 0.1242 0.1428 0.1623 0.0144  0.0106  -0.0044 73  TYR A C     
577  O  O     . TYR A 81  ? 0.1277 0.1614 0.1715 0.0173  0.0324  -0.0049 73  TYR A O     
578  C  CB    . TYR A 81  ? 0.1324 0.1321 0.1826 0.0074  -0.0017 -0.0048 73  TYR A CB    
579  C  CG    . TYR A 81  ? 0.1437 0.1294 0.1943 0.0203  0.0170  0.0029  73  TYR A CG    
580  C  CD1   . TYR A 81  ? 0.1642 0.1278 0.2027 0.0204  0.0056  0.0023  73  TYR A CD1   
581  C  CD2   . TYR A 81  ? 0.1391 0.1475 0.2091 0.0085  0.0458  0.0139  73  TYR A CD2   
582  C  CE1   . TYR A 81  ? 0.1634 0.1382 0.2180 0.0240  0.0094  0.0078  73  TYR A CE1   
583  C  CE2   . TYR A 81  ? 0.1378 0.1499 0.2220 0.0102  0.0420  0.0130  73  TYR A CE2   
584  C  CZ    . TYR A 81  ? 0.1481 0.1380 0.2313 0.0025  0.0230  0.0103  73  TYR A CZ    
585  O  OH    . TYR A 81  ? 0.1556 0.1376 0.2514 0.0081  0.0148  0.0020  73  TYR A OH    
586  N  N     . ALA A 82  ? 0.1200 0.1444 0.1557 0.0077  0.0220  -0.0076 74  ALA A N     
587  C  CA    . ALA A 82  ? 0.1344 0.1542 0.1515 0.0024  0.0174  -0.0105 74  ALA A CA    
588  C  C     . ALA A 82  ? 0.1364 0.1438 0.1456 -0.0014 0.0241  -0.0017 74  ALA A C     
589  O  O     . ALA A 82  ? 0.1465 0.1605 0.1442 0.0071  0.0304  0.0065  74  ALA A O     
590  C  CB    . ALA A 82  ? 0.1410 0.1613 0.1541 -0.0069 0.0282  -0.0083 74  ALA A CB    
591  N  N     . GLU A 83  ? 0.1284 0.1440 0.1425 -0.0020 0.0229  0.0116  75  GLU A N     
592  C  CA    . GLU A 83  ? 0.1486 0.1498 0.1432 0.0063  0.0152  -0.0028 75  GLU A CA    
593  C  C     . GLU A 83  ? 0.1525 0.1440 0.1408 0.0066  0.0264  0.0003  75  GLU A C     
594  O  O     . GLU A 83  ? 0.1734 0.1570 0.1416 0.0145  0.0207  0.0024  75  GLU A O     
595  C  CB    . GLU A 83  ? 0.1544 0.1576 0.1390 0.0300  0.0093  0.0050  75  GLU A CB    
596  C  CG    . GLU A 83  ? 0.1672 0.1875 0.1512 0.0181  -0.0031 0.0005  75  GLU A CG    
597  C  CD    . GLU A 83  ? 0.1737 0.1822 0.1699 0.0024  0.0081  0.0190  75  GLU A CD    
598  O  OE1   . GLU A 83  ? 0.1878 0.1664 0.1851 0.0232  0.0037  0.0126  75  GLU A OE1   
599  O  OE2   . GLU A 83  ? 0.1551 0.2170 0.1768 0.0191  0.0226  0.0343  75  GLU A OE2   
600  N  N     . GLU A 84  ? 0.1534 0.1305 0.1414 0.0024  0.0243  -0.0033 76  GLU A N     
601  C  CA    . GLU A 84  ? 0.1418 0.1530 0.1485 -0.0068 0.0165  -0.0146 76  GLU A CA    
602  C  C     . GLU A 84  ? 0.1383 0.1377 0.1540 0.0082  0.0241  0.0003  76  GLU A C     
603  O  O     . GLU A 84  ? 0.1247 0.1894 0.1775 0.0107  0.0347  0.0011  76  GLU A O     
604  C  CB    . GLU A 84  ? 0.1441 0.1511 0.1571 -0.0051 0.0167  -0.0228 76  GLU A CB    
605  C  CG    . GLU A 84  ? 0.1430 0.1606 0.1514 -0.0050 0.0226  -0.0223 76  GLU A CG    
606  C  CD    . GLU A 84  ? 0.1435 0.1614 0.1646 0.0022  0.0213  -0.0162 76  GLU A CD    
607  O  OE1   . GLU A 84  ? 0.1620 0.1528 0.1837 0.0099  0.0055  -0.0111 76  GLU A OE1   
608  O  OE2   . GLU A 84  ? 0.1458 0.1559 0.1698 -0.0047 0.0243  -0.0107 76  GLU A OE2   
609  N  N     . LEU A 85  ? 0.1275 0.1459 0.1488 0.0028  0.0235  -0.0043 77  LEU A N     
610  C  CA    . LEU A 85  ? 0.1273 0.1691 0.1504 0.0102  0.0289  0.0003  77  LEU A CA    
611  C  C     . LEU A 85  ? 0.1423 0.1866 0.1600 0.0152  0.0350  0.0064  77  LEU A C     
612  O  O     . LEU A 85  ? 0.1532 0.1879 0.1588 0.0181  0.0475  0.0115  77  LEU A O     
613  C  CB    . LEU A 85  ? 0.1441 0.1723 0.1532 0.0114  0.0190  -0.0052 77  LEU A CB    
614  C  CG    . LEU A 85  ? 0.1690 0.1689 0.1544 0.0260  0.0075  -0.0054 77  LEU A CG    
615  C  CD1   . LEU A 85  ? 0.2154 0.2203 0.1616 0.0442  0.0002  -0.0061 77  LEU A CD1   
616  C  CD2   . LEU A 85  ? 0.1985 0.1714 0.1633 0.0592  0.0205  0.0109  77  LEU A CD2   
617  N  N     . TYR A 86  ? 0.1370 0.1702 0.1713 0.0150  0.0293  0.0215  78  TYR A N     
618  C  CA    . TYR A 86  ? 0.1379 0.1762 0.1803 0.0132  0.0257  0.0222  78  TYR A CA    
619  C  C     . TYR A 86  ? 0.1496 0.2147 0.1751 0.0195  0.0308  0.0311  78  TYR A C     
620  O  O     . TYR A 86  ? 0.1655 0.2848 0.1846 0.0095  0.0370  0.0447  78  TYR A O     
621  C  CB    . TYR A 86  ? 0.1495 0.1605 0.1920 0.0101  0.0168  0.0126  78  TYR A CB    
622  C  CG    . TYR A 86  ? 0.1458 0.1447 0.2001 0.0034  0.0266  0.0073  78  TYR A CG    
623  C  CD1   . TYR A 86  ? 0.1337 0.1635 0.2019 -0.0014 0.0273  0.0096  78  TYR A CD1   
624  C  CD2   . TYR A 86  ? 0.1429 0.1545 0.2109 0.0086  0.0401  0.0204  78  TYR A CD2   
625  C  CE1   . TYR A 86  ? 0.1371 0.1798 0.2043 0.0035  0.0246  0.0128  78  TYR A CE1   
626  C  CE2   . TYR A 86  ? 0.1234 0.1570 0.2056 0.0187  0.0396  0.0250  78  TYR A CE2   
627  C  CZ    . TYR A 86  ? 0.1429 0.1329 0.2028 0.0046  0.0231  0.0109  78  TYR A CZ    
628  O  OH    . TYR A 86  ? 0.1402 0.1495 0.2086 0.0114  0.0132  0.0111  78  TYR A OH    
629  N  N     . ASN A 87  ? 0.1819 0.1890 0.1753 0.0167  0.0322  0.0148  79  ASN A N     
630  C  CA    . ASN A 87  ? 0.2070 0.2093 0.1792 0.0008  0.0336  0.0113  79  ASN A CA    
631  C  C     . ASN A 87  ? 0.2269 0.2158 0.1752 -0.0186 0.0684  0.0181  79  ASN A C     
632  O  O     . ASN A 87  ? 0.3243 0.2361 0.1817 0.0193  0.1013  0.0284  79  ASN A O     
633  C  CB    . ASN A 87  ? 0.2257 0.2174 0.1952 -0.0242 0.0260  0.0137  79  ASN A CB    
634  C  CG    . ASN A 87  ? 0.3089 0.2622 0.2218 -0.0382 -0.0020 0.0055  79  ASN A CG    
635  O  OD1   . ASN A 87  ? 0.3569 0.3383 0.2281 -0.0048 -0.0010 0.0016  79  ASN A OD1   
636  N  ND2   . ASN A 87  ? 0.3407 0.2756 0.2397 -0.0187 -0.0209 -0.0058 79  ASN A ND2   
637  N  N     . VAL A 88  ? 0.1872 0.2182 0.1795 -0.0009 0.0273  -0.0140 80  VAL A N     
638  C  CA    . VAL A 88  ? 0.1815 0.2223 0.1863 0.0016  0.0052  -0.0238 80  VAL A CA    
639  C  C     . VAL A 88  ? 0.1733 0.2149 0.1760 0.0181  0.0103  -0.0178 80  VAL A C     
640  O  O     . VAL A 88  ? 0.2009 0.2445 0.1844 0.0278  0.0271  -0.0015 80  VAL A O     
641  C  CB    . VAL A 88  ? 0.1898 0.2239 0.2021 -0.0089 0.0025  -0.0313 80  VAL A CB    
642  C  CG1   . VAL A 88  ? 0.2433 0.2501 0.2115 0.0093  0.0030  -0.0434 80  VAL A CG1   
643  C  CG2   . VAL A 88  ? 0.2005 0.2597 0.2095 0.0017  0.0000  -0.0164 80  VAL A CG2   
644  N  N     . TYR A 89  ? 0.1632 0.1925 0.1684 0.0128  0.0065  -0.0143 81  TYR A N     
645  C  CA    . TYR A 89  ? 0.1657 0.2070 0.1708 0.0249  -0.0005 0.0012  81  TYR A CA    
646  C  C     . TYR A 89  ? 0.1618 0.2070 0.1752 0.0161  0.0083  0.0047  81  TYR A C     
647  O  O     . TYR A 89  ? 0.1671 0.2278 0.1811 0.0304  0.0261  0.0135  81  TYR A O     
648  C  CB    . TYR A 89  ? 0.1723 0.1873 0.1754 0.0133  0.0058  0.0069  81  TYR A CB    
649  C  CG    . TYR A 89  ? 0.1645 0.1610 0.1776 -0.0030 0.0098  -0.0077 81  TYR A CG    
650  C  CD1   . TYR A 89  ? 0.2044 0.1829 0.1779 0.0204  0.0159  -0.0068 81  TYR A CD1   
651  C  CD2   . TYR A 89  ? 0.1601 0.1784 0.1819 -0.0139 0.0228  -0.0124 81  TYR A CD2   
652  C  CE1   . TYR A 89  ? 0.2195 0.1845 0.1834 0.0419  0.0241  -0.0138 81  TYR A CE1   
653  C  CE2   . TYR A 89  ? 0.1792 0.1828 0.1798 0.0143  0.0338  -0.0132 81  TYR A CE2   
654  C  CZ    . TYR A 89  ? 0.2128 0.1784 0.1871 0.0185  0.0230  -0.0072 81  TYR A CZ    
655  O  OH    . TYR A 89  ? 0.2325 0.1915 0.1980 0.0009  0.0169  -0.0001 81  TYR A OH    
656  N  N     . LYS A 90  ? 0.1742 0.2035 0.1779 0.0186  0.0186  0.0117  82  LYS A N     
657  C  CA    . LYS A 90  ? 0.1847 0.1995 0.1839 -0.0013 0.0256  0.0142  82  LYS A CA    
658  C  C     . LYS A 90  ? 0.1717 0.1948 0.1838 0.0081  0.0305  0.0228  82  LYS A C     
659  O  O     . LYS A 90  ? 0.1773 0.2367 0.1825 0.0067  0.0374  0.0290  82  LYS A O     
660  C  CB    . LYS A 90  ? 0.2505 0.2164 0.1922 -0.0031 0.0227  0.0117  82  LYS A CB    
661  C  CG    . LYS A 90  ? 0.3298 0.2976 0.2135 0.0209  0.0047  0.0021  82  LYS A CG    
662  C  CD    . LYS A 90  ? 0.3908 0.3686 0.2384 0.0396  -0.0089 -0.0073 82  LYS A CD    
663  C  CE    . LYS A 90  ? 0.4385 0.4302 0.2652 0.0648  -0.0142 -0.0054 82  LYS A CE    
664  N  NZ    . LYS A 90  ? 0.4635 0.4689 0.2817 0.0826  -0.0094 0.0077  82  LYS A NZ    
665  N  N     . VAL A 91  ? 0.1637 0.1985 0.1846 0.0050  0.0386  0.0198  83  VAL A N     
666  C  CA    . VAL A 91  ? 0.1664 0.1797 0.1867 0.0067  0.0203  0.0208  83  VAL A CA    
667  C  C     . VAL A 91  ? 0.1458 0.1871 0.1818 0.0174  0.0235  0.0177  83  VAL A C     
668  O  O     . VAL A 91  ? 0.1646 0.2060 0.1827 0.0297  0.0061  0.0106  83  VAL A O     
669  C  CB    . VAL A 91  ? 0.1831 0.1781 0.1839 -0.0096 -0.0047 0.0131  83  VAL A CB    
670  C  CG1   . VAL A 91  ? 0.2129 0.2101 0.1883 0.0135  -0.0033 0.0150  83  VAL A CG1   
671  C  CG2   . VAL A 91  ? 0.1612 0.1889 0.1798 0.0049  -0.0181 0.0138  83  VAL A CG2   
672  N  N     . LYS A 92  ? 0.1386 0.1769 0.1831 0.0190  0.0241  0.0107  84  LYS A N     
673  C  CA    . LYS A 92  ? 0.1408 0.1643 0.1961 0.0051  0.0344  0.0231  84  LYS A CA    
674  C  C     . LYS A 92  ? 0.1433 0.1621 0.1871 0.0154  0.0227  0.0402  84  LYS A C     
675  O  O     . LYS A 92  ? 0.1743 0.1574 0.1886 0.0221  0.0301  0.0360  84  LYS A O     
676  C  CB    . LYS A 92  ? 0.1920 0.1877 0.2231 0.0054  0.0411  0.0298  84  LYS A CB    
677  C  CG    . LYS A 92  ? 0.2638 0.2614 0.2600 0.0093  0.0429  0.0168  84  LYS A CG    
678  C  CD    . LYS A 92  ? 0.3595 0.3410 0.2960 0.0618  0.0341  0.0146  84  LYS A CD    
679  C  CE    . LYS A 92  ? 0.4217 0.4052 0.3228 0.0983  0.0282  0.0123  84  LYS A CE    
680  N  NZ    . LYS A 92  ? 0.4557 0.4487 0.3393 0.1075  0.0195  0.0143  84  LYS A NZ    
681  N  N     . THR A 93  ? 0.1436 0.1408 0.1830 0.0078  0.0159  0.0251  85  THR A N     
682  C  CA    . THR A 93  ? 0.1399 0.1518 0.1774 0.0022  0.0130  0.0143  85  THR A CA    
683  C  C     . THR A 93  ? 0.1381 0.1540 0.1789 0.0136  0.0161  0.0076  85  THR A C     
684  O  O     . THR A 93  ? 0.1568 0.1475 0.1880 0.0244  0.0241  0.0185  85  THR A O     
685  C  CB    . THR A 93  ? 0.1624 0.1764 0.1805 0.0042  0.0137  0.0255  85  THR A CB    
686  O  OG1   . THR A 93  ? 0.1820 0.1894 0.1959 -0.0069 0.0237  0.0399  85  THR A OG1   
687  C  CG2   . THR A 93  ? 0.1930 0.2060 0.1819 0.0174  -0.0134 0.0074  85  THR A CG2   
688  N  N     . ILE A 94  ? 0.1399 0.1472 0.1755 0.0084  0.0172  0.0030  86  ILE A N     
689  C  CA    . ILE A 94  ? 0.1574 0.1340 0.1729 0.0262  0.0315  0.0069  86  ILE A CA    
690  C  C     . ILE A 94  ? 0.1574 0.1224 0.1695 0.0209  0.0213  0.0043  86  ILE A C     
691  O  O     . ILE A 94  ? 0.1863 0.1288 0.1653 0.0394  0.0263  0.0149  86  ILE A O     
692  C  CB    . ILE A 94  ? 0.1508 0.1437 0.1769 0.0298  0.0360  0.0132  86  ILE A CB    
693  C  CG1   . ILE A 94  ? 0.1531 0.1485 0.1903 0.0200  0.0256  0.0011  86  ILE A CG1   
694  C  CG2   . ILE A 94  ? 0.1805 0.1437 0.1798 0.0244  0.0261  0.0044  86  ILE A CG2   
695  C  CD1   . ILE A 94  ? 0.1631 0.1672 0.1961 0.0085  0.0344  0.0001  86  ILE A CD1   
696  N  N     . ILE A 95  ? 0.1654 0.1178 0.1704 0.0211  0.0205  0.0163  87  ILE A N     
697  C  CA    . ILE A 95  ? 0.1509 0.1219 0.1732 0.0040  0.0250  0.0125  87  ILE A CA    
698  C  C     . ILE A 95  ? 0.1382 0.1279 0.1750 0.0184  0.0163  0.0083  87  ILE A C     
699  O  O     . ILE A 95  ? 0.1516 0.1082 0.1770 0.0084  0.0181  0.0017  87  ILE A O     
700  C  CB    . ILE A 95  ? 0.1553 0.1467 0.1819 -0.0085 0.0204  0.0249  87  ILE A CB    
701  C  CG1   . ILE A 95  ? 0.1690 0.1870 0.1846 -0.0177 0.0258  0.0222  87  ILE A CG1   
702  C  CG2   . ILE A 95  ? 0.1618 0.1775 0.1999 -0.0230 0.0084  0.0109  87  ILE A CG2   
703  C  CD1   . ILE A 95  ? 0.1839 0.1972 0.1878 -0.0175 0.0227  0.0248  87  ILE A CD1   
704  N  N     . ARG A 96  ? 0.1410 0.1191 0.1884 0.0091  0.0154  0.0156  88  ARG A N     
705  C  CA    . ARG A 96  ? 0.1327 0.1200 0.1986 0.0032  0.0047  0.0087  88  ARG A CA    
706  C  C     . ARG A 96  ? 0.1447 0.1219 0.1894 0.0004  0.0075  0.0108  88  ARG A C     
707  O  O     . ARG A 96  ? 0.1630 0.1250 0.1924 -0.0137 -0.0057 0.0126  88  ARG A O     
708  C  CB    . ARG A 96  ? 0.1296 0.1540 0.2300 0.0080  0.0112  0.0123  88  ARG A CB    
709  C  CG    . ARG A 96  ? 0.1402 0.2009 0.2727 0.0274  0.0299  0.0228  88  ARG A CG    
710  C  CD    . ARG A 96  ? 0.1366 0.1927 0.2892 0.0189  0.0247  0.0011  88  ARG A CD    
711  N  NE    . ARG A 96  ? 0.1525 0.2127 0.3052 0.0256  -0.0069 -0.0591 88  ARG A NE    
712  C  CZ    . ARG A 96  ? 0.1703 0.2983 0.3036 0.0555  -0.0150 -0.0749 88  ARG A CZ    
713  N  NH1   . ARG A 96  ? 0.1247 0.2625 0.2949 0.0011  -0.0107 -0.0585 88  ARG A NH1   
714  N  NH2   . ARG A 96  ? 0.2296 0.3694 0.3131 0.1033  -0.0368 -0.0954 88  ARG A NH2   
715  N  N     . VAL A 97  ? 0.1547 0.1278 0.1939 -0.0125 -0.0050 0.0161  89  VAL A N     
716  C  CA    A VAL A 97  ? 0.1785 0.1338 0.2067 -0.0053 -0.0104 0.0069  89  VAL A CA    
717  C  CA    B VAL A 97  ? 0.1894 0.1534 0.2068 -0.0052 -0.0079 0.0105  89  VAL A CA    
718  C  C     . VAL A 97  ? 0.1997 0.1581 0.2166 -0.0224 -0.0014 0.0002  89  VAL A C     
719  O  O     . VAL A 97  ? 0.2641 0.1691 0.2283 -0.0598 0.0168  0.0076  89  VAL A O     
720  C  CB    A VAL A 97  ? 0.1811 0.1321 0.2128 0.0021  -0.0051 0.0118  89  VAL A CB    
721  C  CB    B VAL A 97  ? 0.2151 0.1860 0.2121 0.0142  -0.0047 0.0199  89  VAL A CB    
722  C  CG1   A VAL A 97  ? 0.1660 0.1597 0.2141 -0.0015 0.0044  0.0270  89  VAL A CG1   
723  C  CG1   B VAL A 97  ? 0.2400 0.2219 0.2177 0.0421  -0.0020 0.0252  89  VAL A CG1   
724  C  CG2   A VAL A 97  ? 0.1954 0.1371 0.2209 0.0168  -0.0037 0.0066  89  VAL A CG2   
725  C  CG2   B VAL A 97  ? 0.2188 0.2060 0.2138 0.0163  0.0004  0.0229  89  VAL A CG2   
726  N  N     . GLY A 98  ? 0.1827 0.1942 0.2363 -0.0542 0.0135  -0.0075 90  GLY A N     
727  C  CA    . GLY A 98  ? 0.1994 0.2406 0.2433 -0.0535 0.0196  -0.0088 90  GLY A CA    
728  C  C     . GLY A 98  ? 0.2036 0.1994 0.2438 -0.0275 0.0279  0.0096  90  GLY A C     
729  O  O     . GLY A 98  ? 0.1831 0.1739 0.2447 -0.0249 0.0159  0.0323  90  GLY A O     
730  N  N     . THR A 99  ? 0.2101 0.1921 0.2457 -0.0399 0.0346  -0.0078 91  THR A N     
731  C  CA    . THR A 99  ? 0.1991 0.1662 0.2453 -0.0101 0.0293  0.0122  91  THR A CA    
732  C  C     . THR A 99  ? 0.1813 0.1639 0.2130 -0.0013 0.0112  0.0265  91  THR A C     
733  O  O     . THR A 99  ? 0.1954 0.1611 0.2086 -0.0014 0.0226  0.0244  91  THR A O     
734  C  CB    . THR A 99  ? 0.2032 0.1632 0.2878 -0.0052 0.0309  0.0263  91  THR A CB    
735  O  OG1   . THR A 99  ? 0.1822 0.1561 0.3133 -0.0143 0.0293  0.0281  91  THR A OG1   
736  C  CG2   . THR A 99  ? 0.2426 0.1842 0.3042 0.0380  0.0246  0.0382  91  THR A CG2   
737  N  N     . CYS A 100 ? 0.1882 0.1545 0.1881 0.0116  -0.0092 0.0336  92  CYS A N     
738  C  CA    . CYS A 100 ? 0.1699 0.1412 0.1685 -0.0022 -0.0077 0.0305  92  CYS A CA    
739  C  C     . CYS A 100 ? 0.1624 0.1578 0.1501 0.0059  -0.0136 0.0386  92  CYS A C     
740  O  O     . CYS A 100 ? 0.1800 0.1995 0.1572 0.0292  -0.0170 0.0417  92  CYS A O     
741  C  CB    . CYS A 100 ? 0.1489 0.1558 0.1686 -0.0131 -0.0128 0.0361  92  CYS A CB    
742  S  SG    . CYS A 100 ? 0.1827 0.1696 0.1821 0.0047  -0.0291 0.0370  92  CYS A SG    
743  N  N     . GLY A 101 ? 0.1543 0.1580 0.1362 0.0059  -0.0025 0.0305  93  GLY A N     
744  C  CA    . GLY A 101 ? 0.1706 0.1747 0.1301 -0.0028 0.0053  0.0310  93  GLY A CA    
745  C  C     . GLY A 101 ? 0.1807 0.1745 0.1301 -0.0045 -0.0015 0.0337  93  GLY A C     
746  O  O     . GLY A 101 ? 0.1913 0.1751 0.1248 -0.0027 -0.0239 0.0396  93  GLY A O     
747  N  N     . THR A 102 ? 0.2006 0.1742 0.1404 0.0176  -0.0085 0.0230  94  THR A N     
748  C  CA    . THR A 102 ? 0.2260 0.1744 0.1458 0.0101  -0.0067 0.0281  94  THR A CA    
749  C  C     . THR A 102 ? 0.2313 0.1855 0.1579 0.0228  -0.0066 0.0300  94  THR A C     
750  O  O     . THR A 102 ? 0.2361 0.1969 0.1566 0.0259  -0.0036 0.0333  94  THR A O     
751  C  CB    . THR A 102 ? 0.2276 0.1722 0.1377 -0.0054 -0.0034 0.0337  94  THR A CB    
752  O  OG1   . THR A 102 ? 0.2380 0.1799 0.1372 0.0079  -0.0156 0.0310  94  THR A OG1   
753  C  CG2   . THR A 102 ? 0.2121 0.2048 0.1391 0.0065  0.0001  0.0368  94  THR A CG2   
754  N  N     . VAL A 103 ? 0.2346 0.1805 0.1722 0.0148  -0.0141 0.0234  95  VAL A N     
755  C  CA    . VAL A 103 ? 0.2462 0.2077 0.1905 0.0314  -0.0186 0.0091  95  VAL A CA    
756  C  C     . VAL A 103 ? 0.2598 0.2186 0.2049 0.0198  -0.0116 -0.0032 95  VAL A C     
757  O  O     . VAL A 103 ? 0.2773 0.2654 0.2024 0.0345  -0.0115 -0.0115 95  VAL A O     
758  C  CB    . VAL A 103 ? 0.2472 0.2139 0.1987 0.0511  -0.0261 0.0100  95  VAL A CB    
759  C  CG1   . VAL A 103 ? 0.2362 0.2202 0.2053 0.0452  -0.0234 0.0098  95  VAL A CG1   
760  C  CG2   . VAL A 103 ? 0.2677 0.2199 0.2014 0.0669  -0.0319 0.0092  95  VAL A CG2   
761  N  N     . ASP A 104 ? 0.2774 0.2006 0.2219 -0.0043 -0.0302 -0.0053 96  ASP A N     
762  C  CA    . ASP A 104 ? 0.2892 0.2230 0.2428 -0.0228 -0.0455 -0.0094 96  ASP A CA    
763  C  C     . ASP A 104 ? 0.2949 0.2776 0.2508 -0.0150 -0.0450 -0.0147 96  ASP A C     
764  O  O     . ASP A 104 ? 0.2785 0.2764 0.2425 -0.0216 -0.0478 -0.0109 96  ASP A O     
765  C  CB    . ASP A 104 ? 0.3122 0.2303 0.2570 -0.0310 -0.0680 0.0121  96  ASP A CB    
766  C  CG    . ASP A 104 ? 0.3320 0.2348 0.2705 -0.0298 -0.1026 0.0250  96  ASP A CG    
767  O  OD1   . ASP A 104 ? 0.3540 0.2648 0.2801 -0.0240 -0.0957 0.0174  96  ASP A OD1   
768  O  OD2   . ASP A 104 ? 0.3634 0.2493 0.2821 -0.0303 -0.1023 0.0346  96  ASP A OD2   
769  N  N     . PRO A 105 ? 0.3217 0.3229 0.2654 -0.0042 -0.0504 -0.0271 97  PRO A N     
770  C  CA    . PRO A 105 ? 0.3467 0.3438 0.2750 0.0108  -0.0511 -0.0356 97  PRO A CA    
771  C  C     . PRO A 105 ? 0.3577 0.3479 0.2826 0.0065  -0.0515 -0.0296 97  PRO A C     
772  O  O     . PRO A 105 ? 0.3726 0.3933 0.2854 0.0206  -0.0549 -0.0220 97  PRO A O     
773  C  CB    . PRO A 105 ? 0.3601 0.3643 0.2768 0.0255  -0.0524 -0.0484 97  PRO A CB    
774  C  CG    . PRO A 105 ? 0.3564 0.3594 0.2792 0.0263  -0.0540 -0.0570 97  PRO A CG    
775  C  CD    . PRO A 105 ? 0.3420 0.3471 0.2725 0.0210  -0.0551 -0.0479 97  PRO A CD    
776  N  N     . ASN A 106 ? 0.3494 0.3038 0.2855 -0.0121 -0.0527 -0.0249 98  ASN A N     
777  C  CA    . ASN A 106 ? 0.3474 0.3181 0.2915 -0.0235 -0.0504 -0.0192 98  ASN A CA    
778  C  C     . ASN A 106 ? 0.3136 0.3117 0.2769 -0.0319 -0.0440 -0.0037 98  ASN A C     
779  O  O     . ASN A 106 ? 0.3221 0.3388 0.2822 -0.0295 -0.0420 -0.0026 98  ASN A O     
780  C  CB    . ASN A 106 ? 0.3771 0.3441 0.3102 -0.0137 -0.0536 -0.0354 98  ASN A CB    
781  C  CG    . ASN A 106 ? 0.4080 0.3917 0.3297 0.0047  -0.0587 -0.0509 98  ASN A CG    
782  O  OD1   . ASN A 106 ? 0.4233 0.4106 0.3472 0.0100  -0.0552 -0.0579 98  ASN A OD1   
783  N  ND2   . ASN A 106 ? 0.4183 0.4262 0.3314 0.0152  -0.0552 -0.0487 98  ASN A ND2   
784  N  N     . VAL A 107 ? 0.2915 0.2861 0.2580 -0.0352 -0.0421 0.0026  99  VAL A N     
785  C  CA    . VAL A 107 ? 0.2651 0.2828 0.2433 -0.0317 -0.0309 0.0165  99  VAL A CA    
786  C  C     . VAL A 107 ? 0.2541 0.2962 0.2352 -0.0249 -0.0314 0.0403  99  VAL A C     
787  O  O     . VAL A 107 ? 0.2497 0.2948 0.2339 -0.0298 -0.0216 0.0483  99  VAL A O     
788  C  CB    . VAL A 107 ? 0.2687 0.2735 0.2372 -0.0209 -0.0342 0.0119  99  VAL A CB    
789  C  CG1   . VAL A 107 ? 0.2680 0.2721 0.2369 -0.0263 -0.0358 -0.0011 99  VAL A CG1   
790  C  CG2   . VAL A 107 ? 0.2733 0.2640 0.2388 -0.0295 -0.0382 0.0130  99  VAL A CG2   
791  N  N     . HIS A 108 ? 0.2579 0.3106 0.2303 -0.0135 -0.0294 0.0582  100 HIS A N     
792  C  CA    . HIS A 108 ? 0.2639 0.3349 0.2326 -0.0091 -0.0418 0.0511  100 HIS A CA    
793  C  C     . HIS A 108 ? 0.2271 0.3372 0.2306 -0.0034 -0.0290 0.0746  100 HIS A C     
794  O  O     . HIS A 108 ? 0.2100 0.3429 0.2255 -0.0042 -0.0237 0.0757  100 HIS A O     
795  C  CB    . HIS A 108 ? 0.3147 0.3745 0.2525 -0.0162 -0.0464 0.0238  100 HIS A CB    
796  C  CG    . HIS A 108 ? 0.3721 0.4155 0.2674 -0.0070 -0.0438 0.0020  100 HIS A CG    
797  N  ND1   . HIS A 108 ? 0.4068 0.4348 0.2796 -0.0034 -0.0361 -0.0120 100 HIS A ND1   
798  C  CD2   . HIS A 108 ? 0.4036 0.4261 0.2730 0.0046  -0.0449 -0.0082 100 HIS A CD2   
799  C  CE1   . HIS A 108 ? 0.4210 0.4318 0.2815 -0.0067 -0.0367 -0.0214 100 HIS A CE1   
800  N  NE2   . HIS A 108 ? 0.4243 0.4360 0.2783 0.0050  -0.0402 -0.0154 100 HIS A NE2   
801  N  N     . VAL A 109 ? 0.2293 0.3380 0.2362 0.0076  -0.0160 0.0875  101 VAL A N     
802  C  CA    . VAL A 109 ? 0.2239 0.3207 0.2445 0.0058  -0.0057 0.1139  101 VAL A CA    
803  C  C     . VAL A 109 ? 0.2261 0.3341 0.2400 0.0145  -0.0233 0.1066  101 VAL A C     
804  O  O     . VAL A 109 ? 0.2290 0.3522 0.2414 0.0304  -0.0224 0.1010  101 VAL A O     
805  C  CB    . VAL A 109 ? 0.2380 0.3518 0.2626 0.0114  0.0165  0.1167  101 VAL A CB    
806  C  CG1   . VAL A 109 ? 0.2757 0.3972 0.2805 0.0323  0.0189  0.0940  101 VAL A CG1   
807  C  CG2   . VAL A 109 ? 0.2401 0.3703 0.2642 0.0065  0.0260  0.1222  101 VAL A CG2   
808  N  N     . ARG A 110 ? 0.2309 0.3311 0.2332 0.0067  -0.0325 0.1136  102 ARG A N     
809  C  CA    . ARG A 110 ? 0.2381 0.3464 0.2385 0.0049  -0.0287 0.1147  102 ARG A CA    
810  C  C     . ARG A 110 ? 0.2291 0.3410 0.2326 0.0074  -0.0171 0.1049  102 ARG A C     
811  O  O     . ARG A 110 ? 0.2489 0.3672 0.2443 0.0327  0.0076  0.1093  102 ARG A O     
812  C  CB    . ARG A 110 ? 0.2505 0.3605 0.2551 -0.0096 -0.0399 0.1170  102 ARG A CB    
813  C  CG    . ARG A 110 ? 0.2990 0.3908 0.2767 0.0132  -0.0476 0.1150  102 ARG A CG    
814  C  CD    . ARG A 110 ? 0.3737 0.4661 0.3031 0.0391  -0.0587 0.0866  102 ARG A CD    
815  N  NE    . ARG A 110 ? 0.4254 0.5411 0.3309 0.0611  -0.0563 0.0594  102 ARG A NE    
816  C  CZ    . ARG A 110 ? 0.4650 0.6082 0.3542 0.0862  -0.0461 0.0313  102 ARG A CZ    
817  N  NH1   . ARG A 110 ? 0.4858 0.6403 0.3630 0.1018  -0.0396 0.0207  102 ARG A NH1   
818  N  NH2   . ARG A 110 ? 0.4775 0.6300 0.3623 0.0919  -0.0478 0.0207  102 ARG A NH2   
819  N  N     . ASP A 111 ? 0.2063 0.3223 0.2127 -0.0108 -0.0226 0.0824  103 ASP A N     
820  C  CA    . ASP A 111 ? 0.2017 0.2970 0.2046 -0.0222 -0.0272 0.0597  103 ASP A CA    
821  C  C     . ASP A 111 ? 0.1809 0.2658 0.1894 -0.0280 -0.0181 0.0514  103 ASP A C     
822  O  O     . ASP A 111 ? 0.1989 0.2850 0.1844 -0.0397 -0.0050 0.0435  103 ASP A O     
823  C  CB    . ASP A 111 ? 0.2288 0.2947 0.2187 -0.0247 -0.0251 0.0469  103 ASP A CB    
824  C  CG    . ASP A 111 ? 0.2501 0.3287 0.2402 -0.0279 -0.0263 0.0367  103 ASP A CG    
825  O  OD1   . ASP A 111 ? 0.2576 0.3595 0.2511 -0.0367 -0.0403 0.0294  103 ASP A OD1   
826  O  OD2   . ASP A 111 ? 0.2815 0.3242 0.2455 -0.0270 -0.0139 0.0309  103 ASP A OD2   
827  N  N     . VAL A 112 ? 0.1770 0.2673 0.1826 -0.0029 -0.0168 0.0549  104 VAL A N     
828  C  CA    . VAL A 112 ? 0.1701 0.2543 0.1796 -0.0064 -0.0180 0.0560  104 VAL A CA    
829  C  C     . VAL A 112 ? 0.1723 0.2188 0.1785 -0.0163 -0.0218 0.0500  104 VAL A C     
830  O  O     . VAL A 112 ? 0.1924 0.2285 0.1896 -0.0403 -0.0347 0.0346  104 VAL A O     
831  C  CB    . VAL A 112 ? 0.1836 0.3089 0.1881 0.0311  -0.0076 0.0481  104 VAL A CB    
832  C  CG1   . VAL A 112 ? 0.1807 0.3485 0.1931 0.0387  -0.0029 0.0324  104 VAL A CG1   
833  C  CG2   . VAL A 112 ? 0.2043 0.3412 0.1967 0.0626  -0.0074 0.0449  104 VAL A CG2   
834  N  N     . CYS A 113 ? 0.1623 0.1882 0.1701 -0.0029 -0.0152 0.0457  105 CYS A N     
835  C  CA    . CYS A 113 ? 0.1523 0.1698 0.1609 -0.0119 -0.0067 0.0413  105 CYS A CA    
836  C  C     . CYS A 113 ? 0.1462 0.1534 0.1590 -0.0106 -0.0132 0.0270  105 CYS A C     
837  O  O     . CYS A 113 ? 0.1934 0.1555 0.1646 -0.0174 -0.0179 0.0356  105 CYS A O     
838  C  CB    . CYS A 113 ? 0.1764 0.1675 0.1620 -0.0151 -0.0008 0.0342  105 CYS A CB    
839  S  SG    . CYS A 113 ? 0.2090 0.2227 0.1815 -0.0049 0.0182  0.0319  105 CYS A SG    
840  N  N     . ILE A 114 ? 0.1390 0.1360 0.1582 -0.0076 -0.0124 0.0296  106 ILE A N     
841  C  CA    . ILE A 114 ? 0.1125 0.1407 0.1603 -0.0037 -0.0143 0.0379  106 ILE A CA    
842  C  C     . ILE A 114 ? 0.1279 0.1233 0.1761 0.0041  -0.0112 0.0217  106 ILE A C     
843  O  O     . ILE A 114 ? 0.1373 0.1373 0.1790 0.0040  -0.0027 0.0081  106 ILE A O     
844  C  CB    . ILE A 114 ? 0.1133 0.1580 0.1685 -0.0022 -0.0136 0.0374  106 ILE A CB    
845  C  CG1   . ILE A 114 ? 0.1195 0.1780 0.1820 0.0016  -0.0206 0.0256  106 ILE A CG1   
846  C  CG2   . ILE A 114 ? 0.1250 0.1689 0.1665 0.0116  -0.0237 0.0377  106 ILE A CG2   
847  C  CD1   . ILE A 114 ? 0.1479 0.1716 0.1923 0.0143  -0.0226 0.0119  106 ILE A CD1   
848  N  N     . VAL A 115 ? 0.1239 0.1212 0.1816 0.0073  -0.0080 -0.0028 107 VAL A N     
849  C  CA    . VAL A 115 ? 0.1269 0.1217 0.1831 0.0108  -0.0094 0.0152  107 VAL A CA    
850  C  C     . VAL A 115 ? 0.1208 0.1352 0.1808 0.0026  0.0018  0.0124  107 VAL A C     
851  O  O     . VAL A 115 ? 0.1555 0.1569 0.1906 0.0266  0.0116  0.0043  107 VAL A O     
852  C  CB    . VAL A 115 ? 0.1187 0.1553 0.1961 -0.0030 -0.0055 0.0207  107 VAL A CB    
853  C  CG1   . VAL A 115 ? 0.1215 0.1665 0.2031 0.0055  -0.0106 0.0024  107 VAL A CG1   
854  C  CG2   . VAL A 115 ? 0.1239 0.1499 0.2067 -0.0139 -0.0148 0.0213  107 VAL A CG2   
855  N  N     . THR A 116 ? 0.1201 0.1357 0.1769 -0.0013 0.0035  0.0196  108 THR A N     
856  C  CA    . THR A 116 ? 0.1341 0.1350 0.1851 0.0007  0.0085  0.0327  108 THR A CA    
857  C  C     . THR A 116 ? 0.1195 0.1260 0.1610 0.0005  0.0042  0.0391  108 THR A C     
858  O  O     . THR A 116 ? 0.1028 0.1397 0.1685 0.0003  0.0204  0.0280  108 THR A O     
859  C  CB    . THR A 116 ? 0.1504 0.1340 0.2195 -0.0224 -0.0187 0.0183  108 THR A CB    
860  O  OG1   . THR A 116 ? 0.1769 0.1259 0.2294 0.0027  -0.0488 0.0073  108 THR A OG1   
861  C  CG2   . THR A 116 ? 0.1678 0.1875 0.2427 -0.0246 -0.0314 0.0134  108 THR A CG2   
862  N  N     . ALA A 117 ? 0.1225 0.1449 0.1488 -0.0004 -0.0050 0.0258  109 ALA A N     
863  C  CA    . ALA A 117 ? 0.1129 0.1415 0.1379 0.0028  -0.0063 0.0109  109 ALA A CA    
864  C  C     . ALA A 117 ? 0.1104 0.1381 0.1233 0.0040  -0.0150 0.0169  109 ALA A C     
865  O  O     . ALA A 117 ? 0.1179 0.1660 0.1187 -0.0144 -0.0176 0.0160  109 ALA A O     
866  C  CB    . ALA A 117 ? 0.1350 0.1426 0.1412 0.0092  -0.0035 0.0030  109 ALA A CB    
867  N  N     . SER A 118 ? 0.1138 0.1584 0.1312 0.0023  -0.0015 0.0137  110 SER A N     
868  C  CA    A SER A 118 ? 0.1246 0.1432 0.1392 -0.0035 0.0082  0.0222  110 SER A CA    
869  C  CA    B SER A 118 ? 0.1109 0.1417 0.1374 -0.0081 -0.0001 0.0178  110 SER A CA    
870  C  C     . SER A 118 ? 0.1184 0.1338 0.1398 -0.0063 0.0075  0.0346  110 SER A C     
871  O  O     . SER A 118 ? 0.1238 0.1858 0.1498 0.0008  -0.0147 0.0319  110 SER A O     
872  C  CB    A SER A 118 ? 0.1581 0.1461 0.1489 0.0009  0.0127  0.0193  110 SER A CB    
873  C  CB    B SER A 118 ? 0.1111 0.1400 0.1429 -0.0124 -0.0089 0.0062  110 SER A CB    
874  O  OG    A SER A 118 ? 0.1623 0.1403 0.1586 0.0038  0.0090  0.0220  110 SER A OG    
875  O  OG    B SER A 118 ? 0.1026 0.1332 0.1494 -0.0110 -0.0212 -0.0055 110 SER A OG    
876  N  N     . GLY A 119 ? 0.1119 0.1270 0.1365 -0.0091 0.0033  0.0139  111 GLY A N     
877  C  CA    . GLY A 119 ? 0.1185 0.1232 0.1353 -0.0020 0.0053  0.0203  111 GLY A CA    
878  C  C     . GLY A 119 ? 0.1201 0.1232 0.1341 0.0024  0.0121  0.0106  111 GLY A C     
879  O  O     . GLY A 119 ? 0.1295 0.1202 0.1435 0.0107  0.0149  0.0216  111 GLY A O     
880  N  N     . THR A 120 ? 0.1187 0.1051 0.1298 0.0020  0.0137  0.0069  112 THR A N     
881  C  CA    . THR A 120 ? 0.1180 0.1156 0.1360 -0.0132 0.0180  0.0104  112 THR A CA    
882  C  C     . THR A 120 ? 0.1175 0.1047 0.1410 -0.0056 0.0055  -0.0039 112 THR A C     
883  O  O     . THR A 120 ? 0.1304 0.1076 0.1437 0.0002  0.0177  0.0105  112 THR A O     
884  C  CB    . THR A 120 ? 0.1346 0.1303 0.1461 0.0044  0.0115  0.0056  112 THR A CB    
885  O  OG1   . THR A 120 ? 0.1362 0.1123 0.1566 -0.0071 0.0089  -0.0013 112 THR A OG1   
886  C  CG2   . THR A 120 ? 0.1396 0.1294 0.1504 0.0019  0.0092  0.0042  112 THR A CG2   
887  N  N     . ASP A 121 ? 0.1222 0.1190 0.1501 -0.0095 0.0090  -0.0004 113 ASP A N     
888  C  CA    . ASP A 121 ? 0.1290 0.1297 0.1491 0.0014  0.0139  0.0054  113 ASP A CA    
889  C  C     . ASP A 121 ? 0.1353 0.1219 0.1514 -0.0033 0.0108  -0.0023 113 ASP A C     
890  O  O     . ASP A 121 ? 0.1244 0.1367 0.1618 -0.0107 0.0117  0.0057  113 ASP A O     
891  C  CB    . ASP A 121 ? 0.1363 0.1145 0.1547 0.0159  0.0148  0.0152  113 ASP A CB    
892  C  CG    . ASP A 121 ? 0.1346 0.1331 0.1516 -0.0014 0.0122  0.0186  113 ASP A CG    
893  O  OD1   . ASP A 121 ? 0.1293 0.1242 0.1553 -0.0009 0.0128  0.0100  113 ASP A OD1   
894  O  OD2   . ASP A 121 ? 0.1476 0.1363 0.1477 0.0093  0.0087  0.0190  113 ASP A OD2   
895  N  N     . SER A 122 ? 0.1371 0.1261 0.1454 -0.0141 0.0137  -0.0005 114 SER A N     
896  C  CA    . SER A 122 ? 0.1421 0.1315 0.1363 -0.0029 0.0121  0.0007  114 SER A CA    
897  C  C     . SER A 122 ? 0.1394 0.1306 0.1390 -0.0034 0.0125  0.0125  114 SER A C     
898  O  O     . SER A 122 ? 0.1812 0.1279 0.1333 -0.0296 -0.0004 0.0067  114 SER A O     
899  C  CB    . SER A 122 ? 0.1390 0.1398 0.1250 0.0004  0.0057  -0.0094 114 SER A CB    
900  O  OG    . SER A 122 ? 0.1451 0.1341 0.1277 -0.0085 0.0105  0.0003  114 SER A OG    
901  N  N     . ASN A 123 ? 0.1179 0.1276 0.1695 -0.0053 0.0148  -0.0040 115 ASN A N     
902  C  CA    . ASN A 123 ? 0.1105 0.1396 0.2055 0.0105  -0.0171 -0.0104 115 ASN A CA    
903  C  C     . ASN A 123 ? 0.1299 0.1208 0.1857 0.0009  -0.0254 -0.0006 115 ASN A C     
904  O  O     . ASN A 123 ? 0.1322 0.1326 0.1849 -0.0011 -0.0253 0.0039  115 ASN A O     
905  C  CB    . ASN A 123 ? 0.1276 0.1360 0.2572 0.0078  -0.0237 -0.0205 115 ASN A CB    
906  C  CG    . ASN A 123 ? 0.1648 0.1854 0.3019 -0.0055 -0.0286 -0.0530 115 ASN A CG    
907  O  OD1   . ASN A 123 ? 0.1471 0.2113 0.3254 0.0157  -0.0168 -0.0968 115 ASN A OD1   
908  N  ND2   . ASN A 123 ? 0.1702 0.1924 0.3052 0.0088  -0.0256 -0.0271 115 ASN A ND2   
909  N  N     . VAL A 124 ? 0.1177 0.1115 0.1628 -0.0085 -0.0013 0.0083  116 VAL A N     
910  C  CA    . VAL A 124 ? 0.1288 0.1304 0.1461 -0.0096 0.0169  0.0194  116 VAL A CA    
911  C  C     . VAL A 124 ? 0.1258 0.1202 0.1398 -0.0055 0.0092  0.0048  116 VAL A C     
912  O  O     . VAL A 124 ? 0.1492 0.1372 0.1378 -0.0163 0.0112  0.0095  116 VAL A O     
913  C  CB    . VAL A 124 ? 0.1360 0.1199 0.1544 0.0099  0.0123  0.0011  116 VAL A CB    
914  C  CG1   . VAL A 124 ? 0.1475 0.1136 0.1583 -0.0050 0.0197  0.0019  116 VAL A CG1   
915  C  CG2   . VAL A 124 ? 0.1560 0.1343 0.1557 0.0206  0.0220  -0.0002 116 VAL A CG2   
916  N  N     . ASN A 125 ? 0.1182 0.1239 0.1391 -0.0060 0.0003  0.0186  117 ASN A N     
917  C  CA    . ASN A 125 ? 0.1188 0.1251 0.1455 -0.0097 -0.0002 0.0113  117 ASN A CA    
918  C  C     . ASN A 125 ? 0.1198 0.1249 0.1409 -0.0150 0.0039  0.0108  117 ASN A C     
919  O  O     . ASN A 125 ? 0.1274 0.1358 0.1407 -0.0079 0.0098  0.0167  117 ASN A O     
920  C  CB    . ASN A 125 ? 0.1250 0.1267 0.1506 0.0123  0.0037  0.0090  117 ASN A CB    
921  C  CG    . ASN A 125 ? 0.1226 0.1226 0.1554 -0.0073 -0.0038 0.0014  117 ASN A CG    
922  O  OD1   . ASN A 125 ? 0.1201 0.1358 0.1655 -0.0048 0.0002  -0.0016 117 ASN A OD1   
923  N  ND2   . ASN A 125 ? 0.1364 0.1314 0.1537 0.0163  -0.0085 0.0083  117 ASN A ND2   
924  N  N     . ARG A 126 ? 0.1134 0.1290 0.1323 -0.0050 -0.0039 0.0023  118 ARG A N     
925  C  CA    . ARG A 126 ? 0.1302 0.1186 0.1366 0.0159  0.0015  -0.0037 118 ARG A CA    
926  C  C     . ARG A 126 ? 0.1246 0.1402 0.1412 0.0085  -0.0103 0.0009  118 ARG A C     
927  O  O     . ARG A 126 ? 0.1548 0.1490 0.1409 0.0155  -0.0014 0.0034  118 ARG A O     
928  C  CB    . ARG A 126 ? 0.1252 0.1452 0.1276 0.0141  -0.0087 0.0046  118 ARG A CB    
929  C  CG    . ARG A 126 ? 0.1232 0.1582 0.1322 0.0203  -0.0036 0.0124  118 ARG A CG    
930  C  CD    . ARG A 126 ? 0.1260 0.2052 0.1377 0.0175  -0.0099 0.0120  118 ARG A CD    
931  N  NE    . ARG A 126 ? 0.1398 0.2307 0.1413 0.0347  -0.0168 0.0053  118 ARG A NE    
932  C  CZ    . ARG A 126 ? 0.1444 0.3145 0.1414 0.0634  -0.0070 0.0013  118 ARG A CZ    
933  N  NH1   . ARG A 126 ? 0.1590 0.4217 0.1501 0.0588  0.0104  -0.0114 118 ARG A NH1   
934  N  NH2   . ARG A 126 ? 0.1457 0.2937 0.1357 0.0443  0.0068  0.0146  118 ARG A NH2   
935  N  N     . MET A 127 ? 0.1301 0.1364 0.1438 0.0010  -0.0147 0.0047  119 MET A N     
936  C  CA    A MET A 127 ? 0.1269 0.1486 0.1525 -0.0034 -0.0194 0.0044  119 MET A CA    
937  C  CA    B MET A 127 ? 0.1583 0.1523 0.1462 -0.0180 -0.0214 0.0018  119 MET A CA    
938  C  C     . MET A 127 ? 0.1521 0.1539 0.1484 -0.0059 -0.0223 -0.0025 119 MET A C     
939  O  O     . MET A 127 ? 0.1474 0.1987 0.1500 -0.0182 -0.0246 0.0073  119 MET A O     
940  C  CB    A MET A 127 ? 0.1248 0.1750 0.1703 -0.0138 -0.0082 0.0139  119 MET A CB    
941  C  CB    B MET A 127 ? 0.2157 0.1740 0.1515 -0.0657 -0.0173 0.0026  119 MET A CB    
942  C  CG    A MET A 127 ? 0.1417 0.2012 0.1921 -0.0283 -0.0052 0.0274  119 MET A CG    
943  C  CG    B MET A 127 ? 0.2806 0.2044 0.1630 -0.1115 -0.0224 0.0067  119 MET A CG    
944  S  SD    A MET A 127 ? 0.1813 0.2415 0.2138 -0.0223 -0.0068 0.0438  119 MET A SD    
945  S  SD    B MET A 127 ? 0.3571 0.2347 0.1705 -0.1262 -0.0327 0.0096  119 MET A SD    
946  C  CE    A MET A 127 ? 0.2125 0.2731 0.2142 -0.0082 -0.0069 0.0449  119 MET A CE    
947  C  CE    B MET A 127 ? 0.3789 0.2023 0.1700 -0.1074 -0.0355 0.0191  119 MET A CE    
948  N  N     . ARG A 128 ? 0.1375 0.1466 0.1419 -0.0127 0.0024  0.0072  120 ARG A N     
949  C  CA    . ARG A 128 ? 0.1446 0.1390 0.1494 -0.0017 0.0084  -0.0025 120 ARG A CA    
950  C  C     . ARG A 128 ? 0.1559 0.1423 0.1435 0.0000  0.0092  -0.0002 120 ARG A C     
951  O  O     . ARG A 128 ? 0.1858 0.1600 0.1348 0.0161  0.0113  0.0012  120 ARG A O     
952  C  CB    . ARG A 128 ? 0.1412 0.1468 0.1531 0.0098  0.0169  0.0016  120 ARG A CB    
953  C  CG    . ARG A 128 ? 0.1581 0.1402 0.1647 0.0159  0.0203  -0.0037 120 ARG A CG    
954  C  CD    . ARG A 128 ? 0.1702 0.1466 0.1668 0.0158  0.0185  0.0090  120 ARG A CD    
955  N  NE    . ARG A 128 ? 0.1861 0.1701 0.1700 0.0273  0.0115  0.0103  120 ARG A NE    
956  C  CZ    . ARG A 128 ? 0.1619 0.1457 0.1563 0.0113  -0.0027 -0.0046 120 ARG A CZ    
957  N  NH1   . ARG A 128 ? 0.1594 0.1495 0.1542 0.0136  0.0044  -0.0190 120 ARG A NH1   
958  N  NH2   . ARG A 128 ? 0.1741 0.1371 0.1561 0.0134  0.0029  0.0094  120 ARG A NH2   
959  N  N     . LEU A 129 ? 0.1362 0.1438 0.1446 -0.0028 0.0092  -0.0074 121 LEU A N     
960  C  CA    . LEU A 129 ? 0.1355 0.1342 0.1539 -0.0150 0.0047  0.0091  121 LEU A CA    
961  C  C     . LEU A 129 ? 0.1463 0.1310 0.1550 -0.0063 -0.0074 0.0080  121 LEU A C     
962  O  O     . LEU A 129 ? 0.1478 0.1288 0.1611 0.0012  -0.0009 0.0034  121 LEU A O     
963  C  CB    . LEU A 129 ? 0.1350 0.1501 0.1691 -0.0155 0.0023  0.0097  121 LEU A CB    
964  C  CG    . LEU A 129 ? 0.1594 0.1642 0.1783 -0.0258 0.0011  0.0064  121 LEU A CG    
965  C  CD1   . LEU A 129 ? 0.2252 0.2156 0.1957 -0.0357 0.0052  -0.0061 121 LEU A CD1   
966  C  CD2   . LEU A 129 ? 0.1550 0.1708 0.1803 -0.0161 -0.0053 0.0125  121 LEU A CD2   
967  N  N     . LEU A 130 ? 0.1426 0.1388 0.1502 -0.0020 -0.0113 0.0081  122 LEU A N     
968  C  CA    . LEU A 130 ? 0.1443 0.1465 0.1500 -0.0013 -0.0118 0.0117  122 LEU A CA    
969  C  C     . LEU A 130 ? 0.1470 0.1489 0.1458 0.0057  -0.0104 0.0210  122 LEU A C     
970  O  O     . LEU A 130 ? 0.1596 0.1510 0.1556 0.0189  -0.0083 0.0267  122 LEU A O     
971  C  CB    . LEU A 130 ? 0.1746 0.1658 0.1594 -0.0091 -0.0047 0.0207  122 LEU A CB    
972  C  CG    . LEU A 130 ? 0.2229 0.2023 0.1693 -0.0168 -0.0009 0.0287  122 LEU A CG    
973  C  CD1   . LEU A 130 ? 0.2561 0.2313 0.1851 0.0143  0.0049  0.0362  122 LEU A CD1   
974  C  CD2   . LEU A 130 ? 0.2719 0.2493 0.1768 0.0007  0.0044  0.0390  122 LEU A CD2   
975  N  N     . GLY A 131 ? 0.1308 0.1325 0.1377 -0.0061 -0.0200 0.0094  123 GLY A N     
976  C  CA    . GLY A 131 ? 0.1249 0.1406 0.1412 -0.0250 -0.0051 0.0061  123 GLY A CA    
977  C  C     . GLY A 131 ? 0.1094 0.1316 0.1411 -0.0045 -0.0006 0.0101  123 GLY A C     
978  O  O     . GLY A 131 ? 0.1314 0.1486 0.1470 -0.0097 0.0066  0.0086  123 GLY A O     
979  N  N     . HIS A 132 ? 0.1114 0.1221 0.1425 -0.0009 -0.0109 0.0053  124 HIS A N     
980  C  CA    . HIS A 132 ? 0.1215 0.1158 0.1401 0.0047  -0.0138 -0.0034 124 HIS A CA    
981  C  C     . HIS A 132 ? 0.1191 0.1164 0.1433 0.0111  -0.0085 -0.0049 124 HIS A C     
982  O  O     . HIS A 132 ? 0.1370 0.1142 0.1598 -0.0017 -0.0161 0.0102  124 HIS A O     
983  C  CB    . HIS A 132 ? 0.1329 0.1173 0.1368 -0.0071 -0.0200 0.0178  124 HIS A CB    
984  C  CG    . HIS A 132 ? 0.1423 0.1176 0.1392 -0.0072 -0.0302 0.0214  124 HIS A CG    
985  N  ND1   . HIS A 132 ? 0.1494 0.1298 0.1469 0.0116  -0.0353 0.0102  124 HIS A ND1   
986  C  CD2   . HIS A 132 ? 0.1378 0.1264 0.1332 -0.0144 -0.0398 0.0217  124 HIS A CD2   
987  C  CE1   . HIS A 132 ? 0.1690 0.1433 0.1456 0.0134  -0.0376 0.0030  124 HIS A CE1   
988  N  NE2   . HIS A 132 ? 0.1617 0.1355 0.1420 0.0104  -0.0467 0.0138  124 HIS A NE2   
989  N  N     . ASP A 133 ? 0.1108 0.1118 0.1302 0.0023  -0.0141 -0.0097 125 ASP A N     
990  C  CA    . ASP A 133 ? 0.1120 0.1242 0.1247 0.0048  0.0014  0.0096  125 ASP A CA    
991  C  C     . ASP A 133 ? 0.1163 0.1177 0.1266 -0.0045 -0.0029 0.0140  125 ASP A C     
992  O  O     . ASP A 133 ? 0.1223 0.1155 0.1332 -0.0099 0.0036  0.0118  125 ASP A O     
993  C  CB    . ASP A 133 ? 0.1245 0.1420 0.1196 0.0025  -0.0085 -0.0070 125 ASP A CB    
994  C  CG    . ASP A 133 ? 0.1359 0.1480 0.1199 -0.0165 -0.0050 -0.0186 125 ASP A CG    
995  O  OD1   . ASP A 133 ? 0.1556 0.2554 0.1341 -0.0517 0.0181  -0.0247 125 ASP A OD1   
996  O  OD2   . ASP A 133 ? 0.1287 0.1272 0.1146 0.0107  -0.0043 -0.0014 125 ASP A OD2   
997  N  N     . PHE A 134 ? 0.1191 0.1137 0.1256 0.0039  0.0102  0.0160  126 PHE A N     
998  C  CA    . PHE A 134 ? 0.1157 0.1235 0.1334 0.0117  0.0023  0.0057  126 PHE A CA    
999  C  C     . PHE A 134 ? 0.1164 0.1246 0.1468 0.0018  0.0004  0.0217  126 PHE A C     
1000 O  O     . PHE A 134 ? 0.1313 0.1458 0.1573 -0.0048 -0.0024 0.0394  126 PHE A O     
1001 C  CB    . PHE A 134 ? 0.1322 0.1207 0.1380 0.0062  -0.0032 -0.0091 126 PHE A CB    
1002 C  CG    . PHE A 134 ? 0.1464 0.1280 0.1478 0.0044  -0.0065 -0.0036 126 PHE A CG    
1003 C  CD1   . PHE A 134 ? 0.1566 0.1423 0.1601 0.0135  -0.0025 -0.0220 126 PHE A CD1   
1004 C  CD2   . PHE A 134 ? 0.1640 0.1581 0.1487 0.0268  -0.0123 -0.0220 126 PHE A CD2   
1005 C  CE1   . PHE A 134 ? 0.1590 0.1541 0.1645 -0.0087 0.0144  -0.0047 126 PHE A CE1   
1006 C  CE2   . PHE A 134 ? 0.1749 0.1575 0.1525 0.0155  0.0050  -0.0214 126 PHE A CE2   
1007 C  CZ    . PHE A 134 ? 0.1616 0.1494 0.1582 0.0152  0.0138  -0.0024 126 PHE A CZ    
1008 N  N     . PRO A 135 ? 0.1208 0.1165 0.1476 -0.0033 -0.0071 0.0184  127 PRO A N     
1009 C  CA    . PRO A 135 ? 0.1280 0.1409 0.1435 0.0067  -0.0066 0.0170  127 PRO A CA    
1010 C  C     . PRO A 135 ? 0.1325 0.1281 0.1363 0.0194  0.0104  0.0229  127 PRO A C     
1011 O  O     . PRO A 135 ? 0.1334 0.1407 0.1369 0.0263  0.0166  0.0234  127 PRO A O     
1012 C  CB    . PRO A 135 ? 0.1371 0.1553 0.1447 0.0136  -0.0032 0.0112  127 PRO A CB    
1013 C  CG    . PRO A 135 ? 0.1151 0.1274 0.1493 -0.0068 -0.0045 0.0121  127 PRO A CG    
1014 C  CD    . PRO A 135 ? 0.1301 0.1206 0.1541 -0.0035 -0.0066 0.0135  127 PRO A CD    
1015 N  N     . ALA A 136 ? 0.1276 0.1388 0.1380 0.0039  0.0066  0.0072  128 ALA A N     
1016 C  CA    . ALA A 136 ? 0.1147 0.1310 0.1388 -0.0008 0.0058  -0.0010 128 ALA A CA    
1017 C  C     . ALA A 136 ? 0.1180 0.1168 0.1336 -0.0063 -0.0010 0.0099  128 ALA A C     
1018 O  O     . ALA A 136 ? 0.1237 0.1276 0.1332 -0.0018 -0.0189 0.0106  128 ALA A O     
1019 C  CB    . ALA A 136 ? 0.1264 0.1430 0.1410 -0.0136 0.0028  0.0047  128 ALA A CB    
1020 N  N     . THR A 137 ? 0.1175 0.1309 0.1428 0.0025  0.0030  0.0142  129 THR A N     
1021 C  CA    . THR A 137 ? 0.1230 0.1207 0.1541 0.0008  0.0123  0.0220  129 THR A CA    
1022 C  C     . THR A 137 ? 0.1245 0.1140 0.1481 -0.0081 0.0027  0.0052  129 THR A C     
1023 O  O     . THR A 137 ? 0.1309 0.1351 0.1450 0.0000  0.0083  0.0069  129 THR A O     
1024 C  CB    . THR A 137 ? 0.1158 0.1299 0.1765 0.0096  0.0130  0.0245  129 THR A CB    
1025 O  OG1   . THR A 137 ? 0.1231 0.1279 0.1849 0.0002  0.0031  0.0129  129 THR A OG1   
1026 C  CG2   . THR A 137 ? 0.1382 0.1196 0.1847 -0.0097 0.0166  0.0291  129 THR A CG2   
1027 N  N     . ALA A 138 ? 0.1188 0.1246 0.1568 0.0054  0.0031  0.0217  130 ALA A N     
1028 C  CA    . ALA A 138 ? 0.1262 0.1259 0.1753 0.0175  0.0057  0.0341  130 ALA A CA    
1029 C  C     . ALA A 138 ? 0.1162 0.1295 0.1901 0.0092  0.0119  0.0315  130 ALA A C     
1030 O  O     . ALA A 138 ? 0.1422 0.1174 0.2035 -0.0082 0.0141  0.0138  130 ALA A O     
1031 C  CB    . ALA A 138 ? 0.1357 0.1232 0.1735 0.0072  0.0107  0.0365  130 ALA A CB    
1032 N  N     . ASN A 139 ? 0.1191 0.1211 0.2057 0.0077  0.0193  0.0210  131 ASN A N     
1033 C  CA    . ASN A 139 ? 0.1258 0.1273 0.2170 0.0127  0.0220  0.0273  131 ASN A CA    
1034 C  C     . ASN A 139 ? 0.1152 0.1362 0.2413 0.0068  0.0239  0.0369  131 ASN A C     
1035 O  O     . ASN A 139 ? 0.1277 0.1384 0.2504 0.0109  0.0266  0.0316  131 ASN A O     
1036 C  CB    . ASN A 139 ? 0.1604 0.1435 0.2088 0.0067  0.0131  0.0225  131 ASN A CB    
1037 C  CG    . ASN A 139 ? 0.1588 0.1868 0.2104 0.0063  0.0263  0.0350  131 ASN A CG    
1038 O  OD1   . ASN A 139 ? 0.1647 0.2076 0.2099 0.0230  0.0273  0.0194  131 ASN A OD1   
1039 N  ND2   . ASN A 139 ? 0.2049 0.2270 0.2182 0.0212  0.0322  0.0365  131 ASN A ND2   
1040 N  N     . PHE A 140 ? 0.1356 0.1362 0.2603 -0.0108 0.0200  0.0344  132 PHE A N     
1041 C  CA    . PHE A 140 ? 0.1464 0.1147 0.2863 -0.0064 0.0099  0.0329  132 PHE A CA    
1042 C  C     . PHE A 140 ? 0.1491 0.1195 0.2832 -0.0050 0.0106  0.0451  132 PHE A C     
1043 O  O     . PHE A 140 ? 0.1567 0.1364 0.2760 0.0150  0.0075  0.0543  132 PHE A O     
1044 C  CB    . PHE A 140 ? 0.1628 0.1196 0.3200 -0.0008 0.0024  0.0382  132 PHE A CB    
1045 C  CG    . PHE A 140 ? 0.1912 0.1295 0.3517 -0.0089 -0.0052 0.0386  132 PHE A CG    
1046 C  CD1   . PHE A 140 ? 0.2234 0.1418 0.3709 0.0180  -0.0248 0.0233  132 PHE A CD1   
1047 C  CD2   . PHE A 140 ? 0.1928 0.1454 0.3702 -0.0476 -0.0163 0.0369  132 PHE A CD2   
1048 C  CE1   . PHE A 140 ? 0.2423 0.1593 0.3786 0.0246  -0.0374 0.0139  132 PHE A CE1   
1049 C  CE2   . PHE A 140 ? 0.2198 0.1669 0.3814 -0.0299 -0.0275 0.0021  132 PHE A CE2   
1050 C  CZ    . PHE A 140 ? 0.2355 0.1534 0.3826 -0.0004 -0.0455 -0.0078 132 PHE A CZ    
1051 N  N     . GLU A 141 ? 0.1392 0.1516 0.2822 0.0033  0.0263  0.0588  133 GLU A N     
1052 C  CA    . GLU A 141 ? 0.1457 0.1785 0.2820 0.0305  0.0340  0.0667  133 GLU A CA    
1053 C  C     . GLU A 141 ? 0.1347 0.1570 0.2612 0.0199  0.0262  0.0455  133 GLU A C     
1054 O  O     . GLU A 141 ? 0.1302 0.1638 0.2669 0.0135  0.0223  0.0379  133 GLU A O     
1055 C  CB    . GLU A 141 ? 0.1626 0.2680 0.3068 0.0332  0.0506  0.0973  133 GLU A CB    
1056 C  CG    . GLU A 141 ? 0.2154 0.3667 0.3376 0.0373  0.0601  0.1005  133 GLU A CG    
1057 C  CD    . GLU A 141 ? 0.3032 0.4617 0.3752 0.0350  0.0545  0.0853  133 GLU A CD    
1058 O  OE1   . GLU A 141 ? 0.3247 0.4810 0.3856 0.0251  0.0534  0.0862  133 GLU A OE1   
1059 O  OE2   . GLU A 141 ? 0.3607 0.5163 0.3941 0.0603  0.0555  0.0753  133 GLU A OE2   
1060 N  N     . VAL A 142 ? 0.1357 0.1569 0.2354 0.0254  0.0116  0.0309  134 VAL A N     
1061 C  CA    . VAL A 142 ? 0.1380 0.1355 0.2235 0.0296  0.0138  0.0193  134 VAL A CA    
1062 C  C     . VAL A 142 ? 0.1234 0.1252 0.2266 0.0044  0.0122  0.0196  134 VAL A C     
1063 O  O     . VAL A 142 ? 0.1320 0.1282 0.2326 0.0033  -0.0022 0.0145  134 VAL A O     
1064 C  CB    . VAL A 142 ? 0.1333 0.1452 0.2162 0.0123  0.0122  0.0141  134 VAL A CB    
1065 C  CG1   . VAL A 142 ? 0.1379 0.1451 0.2165 -0.0024 0.0070  0.0189  134 VAL A CG1   
1066 C  CG2   . VAL A 142 ? 0.1399 0.1561 0.2153 0.0116  0.0105  0.0188  134 VAL A CG2   
1067 N  N     . VAL A 143 ? 0.1292 0.1170 0.2280 0.0060  0.0199  0.0113  135 VAL A N     
1068 C  CA    . VAL A 143 ? 0.1276 0.1227 0.2378 0.0120  0.0063  0.0098  135 VAL A CA    
1069 C  C     . VAL A 143 ? 0.1288 0.1146 0.2508 0.0050  0.0002  0.0226  135 VAL A C     
1070 O  O     . VAL A 143 ? 0.1261 0.1335 0.2597 0.0035  -0.0066 0.0150  135 VAL A O     
1071 C  CB    . VAL A 143 ? 0.1181 0.1323 0.2375 0.0119  0.0128  0.0108  135 VAL A CB    
1072 C  CG1   . VAL A 143 ? 0.1217 0.1492 0.2374 0.0219  0.0010  0.0078  135 VAL A CG1   
1073 C  CG2   . VAL A 143 ? 0.1146 0.1358 0.2334 -0.0046 0.0116  0.0089  135 VAL A CG2   
1074 N  N     . SER A 144 ? 0.1349 0.1264 0.2609 -0.0122 0.0042  0.0371  136 SER A N     
1075 C  CA    . SER A 144 ? 0.1274 0.1566 0.2816 -0.0073 0.0044  0.0194  136 SER A CA    
1076 C  C     . SER A 144 ? 0.1220 0.1546 0.2732 -0.0013 0.0044  0.0239  136 SER A C     
1077 O  O     . SER A 144 ? 0.1360 0.1560 0.2682 0.0033  -0.0075 0.0283  136 SER A O     
1078 C  CB    . SER A 144 ? 0.1388 0.1917 0.3119 -0.0514 0.0118  0.0191  136 SER A CB    
1079 O  OG    . SER A 144 ? 0.2026 0.2323 0.3358 -0.0308 0.0151  0.0233  136 SER A OG    
1080 N  N     . ALA A 145 ? 0.1252 0.1374 0.2722 -0.0059 0.0109  0.0260  137 ALA A N     
1081 C  CA    . ALA A 145 ? 0.1216 0.1385 0.2725 0.0040  0.0098  0.0234  137 ALA A CA    
1082 C  C     . ALA A 145 ? 0.1225 0.1436 0.2657 0.0045  0.0097  0.0253  137 ALA A C     
1083 O  O     . ALA A 145 ? 0.1260 0.1571 0.2708 0.0117  0.0082  0.0237  137 ALA A O     
1084 C  CB    . ALA A 145 ? 0.1376 0.1506 0.2806 0.0251  0.0150  0.0219  137 ALA A CB    
1085 N  N     . LEU A 146 ? 0.1225 0.1326 0.2518 0.0028  0.0073  0.0229  138 LEU A N     
1086 C  CA    . LEU A 146 ? 0.1194 0.1429 0.2395 0.0030  0.0026  0.0244  138 LEU A CA    
1087 C  C     . LEU A 146 ? 0.1277 0.1408 0.2342 0.0032  -0.0050 0.0175  138 LEU A C     
1088 O  O     . LEU A 146 ? 0.1384 0.1596 0.2298 0.0032  -0.0193 0.0202  138 LEU A O     
1089 C  CB    . LEU A 146 ? 0.1198 0.1460 0.2371 -0.0053 -0.0057 0.0261  138 LEU A CB    
1090 C  CG    . LEU A 146 ? 0.1252 0.1289 0.2336 -0.0024 -0.0105 0.0285  138 LEU A CG    
1091 C  CD1   . LEU A 146 ? 0.1277 0.1411 0.2324 0.0114  -0.0064 0.0340  138 LEU A CD1   
1092 C  CD2   . LEU A 146 ? 0.1332 0.1518 0.2341 0.0158  -0.0195 0.0328  138 LEU A CD2   
1093 N  N     . VAL A 147 ? 0.1439 0.1363 0.2370 0.0056  -0.0022 0.0170  139 VAL A N     
1094 C  CA    . VAL A 147 ? 0.1451 0.1443 0.2478 -0.0096 -0.0021 0.0167  139 VAL A CA    
1095 C  C     . VAL A 147 ? 0.1411 0.1624 0.2624 -0.0036 -0.0123 0.0140  139 VAL A C     
1096 O  O     . VAL A 147 ? 0.1477 0.1782 0.2630 -0.0010 -0.0213 0.0082  139 VAL A O     
1097 C  CB    . VAL A 147 ? 0.1550 0.1465 0.2563 -0.0130 -0.0140 0.0004  139 VAL A CB    
1098 C  CG1   . VAL A 147 ? 0.1825 0.1566 0.2624 0.0026  -0.0227 -0.0039 139 VAL A CG1   
1099 C  CG2   . VAL A 147 ? 0.1458 0.1476 0.2560 0.0011  -0.0078 -0.0032 139 VAL A CG2   
1100 N  N     . GLU A 148 ? 0.1272 0.1779 0.2822 -0.0118 -0.0050 0.0119  140 GLU A N     
1101 C  CA    . GLU A 148 ? 0.1338 0.1897 0.3065 -0.0206 0.0055  0.0230  140 GLU A CA    
1102 C  C     . GLU A 148 ? 0.1363 0.1916 0.3002 -0.0107 0.0055  0.0233  140 GLU A C     
1103 O  O     . GLU A 148 ? 0.1423 0.1993 0.3062 -0.0085 -0.0177 0.0112  140 GLU A O     
1104 C  CB    . GLU A 148 ? 0.1668 0.2154 0.3395 -0.0078 0.0136  0.0240  140 GLU A CB    
1105 C  CG    . GLU A 148 ? 0.1950 0.2316 0.3714 -0.0181 0.0100  0.0204  140 GLU A CG    
1106 C  CD    . GLU A 148 ? 0.2267 0.2828 0.4002 -0.0053 0.0084  0.0150  140 GLU A CD    
1107 O  OE1   . GLU A 148 ? 0.2363 0.3119 0.4160 -0.0428 0.0018  0.0165  140 GLU A OE1   
1108 O  OE2   . GLU A 148 ? 0.2435 0.2881 0.4081 0.0174  0.0072  0.0083  140 GLU A OE2   
1109 N  N     . SER A 149 ? 0.1425 0.1548 0.2880 -0.0178 -0.0028 0.0237  141 SER A N     
1110 C  CA    A SER A 149 ? 0.1554 0.1738 0.2846 -0.0019 -0.0119 0.0234  141 SER A CA    
1111 C  CA    B SER A 149 ? 0.1570 0.1571 0.2846 0.0072  -0.0104 0.0214  141 SER A CA    
1112 C  C     . SER A 149 ? 0.1581 0.1761 0.2852 0.0049  -0.0187 0.0301  141 SER A C     
1113 O  O     . SER A 149 ? 0.1570 0.1963 0.2890 0.0076  -0.0405 0.0219  141 SER A O     
1114 C  CB    A SER A 149 ? 0.1487 0.1871 0.2770 0.0062  -0.0001 0.0373  141 SER A CB    
1115 C  CB    B SER A 149 ? 0.1651 0.1418 0.2794 0.0360  -0.0054 0.0168  141 SER A CB    
1116 O  OG    A SER A 149 ? 0.1392 0.1986 0.2795 -0.0011 0.0050  0.0510  141 SER A OG    
1117 O  OG    B SER A 149 ? 0.1667 0.1307 0.2779 0.0570  -0.0020 0.0154  141 SER A OG    
1118 N  N     . ALA A 150 ? 0.1539 0.1728 0.2887 -0.0051 -0.0270 0.0197  142 ALA A N     
1119 C  CA    . ALA A 150 ? 0.1615 0.1832 0.2965 0.0042  -0.0417 0.0086  142 ALA A CA    
1120 C  C     . ALA A 150 ? 0.1704 0.2128 0.3100 -0.0025 -0.0476 0.0106  142 ALA A C     
1121 O  O     . ALA A 150 ? 0.1773 0.2223 0.3114 -0.0027 -0.0562 0.0223  142 ALA A O     
1122 C  CB    . ALA A 150 ? 0.1596 0.1921 0.2963 0.0065  -0.0467 0.0066  142 ALA A CB    
1123 N  N     . LYS A 151 ? 0.1748 0.2231 0.3280 -0.0254 -0.0567 -0.0147 143 LYS A N     
1124 C  CA    . LYS A 151 ? 0.1884 0.2625 0.3522 -0.0385 -0.0633 -0.0092 143 LYS A CA    
1125 C  C     . LYS A 151 ? 0.1860 0.3021 0.3573 -0.0313 -0.0559 -0.0035 143 LYS A C     
1126 O  O     . LYS A 151 ? 0.1966 0.3260 0.3621 -0.0316 -0.0631 -0.0095 143 LYS A O     
1127 C  CB    . LYS A 151 ? 0.2173 0.2591 0.3738 -0.0624 -0.0622 -0.0012 143 LYS A CB    
1128 C  CG    . LYS A 151 ? 0.2455 0.2840 0.3909 -0.0622 -0.0588 0.0173  143 LYS A CG    
1129 C  CD    . LYS A 151 ? 0.2931 0.3256 0.4075 -0.0314 -0.0491 0.0340  143 LYS A CD    
1130 C  CE    . LYS A 151 ? 0.3325 0.3584 0.4188 -0.0120 -0.0487 0.0407  143 LYS A CE    
1131 N  NZ    . LYS A 151 ? 0.3710 0.3643 0.4253 0.0065  -0.0440 0.0463  143 LYS A NZ    
1132 N  N     . ALA A 152 ? 0.1622 0.2908 0.3542 -0.0333 -0.0522 0.0038  144 ALA A N     
1133 C  CA    . ALA A 152 ? 0.1610 0.3266 0.3568 -0.0072 -0.0446 0.0130  144 ALA A CA    
1134 C  C     . ALA A 152 ? 0.1729 0.3574 0.3577 0.0272  -0.0445 0.0179  144 ALA A C     
1135 O  O     . ALA A 152 ? 0.1608 0.3837 0.3578 0.0277  -0.0472 0.0190  144 ALA A O     
1136 C  CB    . ALA A 152 ? 0.1578 0.3259 0.3612 -0.0098 -0.0305 0.0207  144 ALA A CB    
1137 N  N     . LEU A 153 ? 0.1608 0.3433 0.3601 0.0124  -0.0405 0.0305  145 LEU A N     
1138 C  CA    . LEU A 153 ? 0.1690 0.3386 0.3618 0.0111  -0.0497 0.0352  145 LEU A CA    
1139 C  C     . LEU A 153 ? 0.1881 0.3650 0.3609 0.0041  -0.0631 0.0334  145 LEU A C     
1140 O  O     . LEU A 153 ? 0.2439 0.3723 0.3616 0.0432  -0.0599 0.0413  145 LEU A O     
1141 C  CB    . LEU A 153 ? 0.1728 0.3105 0.3661 0.0357  -0.0448 0.0363  145 LEU A CB    
1142 C  CG    . LEU A 153 ? 0.1797 0.2910 0.3697 0.0588  -0.0334 0.0336  145 LEU A CG    
1143 C  CD1   . LEU A 153 ? 0.1774 0.2633 0.3733 0.0333  -0.0178 0.0336  145 LEU A CD1   
1144 C  CD2   . LEU A 153 ? 0.1990 0.3246 0.3768 0.0762  -0.0309 0.0316  145 LEU A CD2   
1145 N  N     . ASN A 154 ? 0.1806 0.3894 0.3553 -0.0300 -0.0737 0.0273  146 ASN A N     
1146 C  CA    . ASN A 154 ? 0.2103 0.4160 0.3480 -0.0275 -0.0984 0.0077  146 ASN A CA    
1147 C  C     . ASN A 154 ? 0.2195 0.3650 0.3223 -0.0274 -0.0900 0.0228  146 ASN A C     
1148 O  O     . ASN A 154 ? 0.2404 0.4074 0.3243 -0.0082 -0.0867 0.0223  146 ASN A O     
1149 C  CB    . ASN A 154 ? 0.2751 0.4962 0.3703 0.0175  -0.1109 -0.0103 146 ASN A CB    
1150 C  CG    . ASN A 154 ? 0.3445 0.5648 0.3987 0.0700  -0.0976 -0.0106 146 ASN A CG    
1151 O  OD1   . ASN A 154 ? 0.3782 0.5834 0.4138 0.0770  -0.0868 -0.0173 146 ASN A OD1   
1152 N  ND2   . ASN A 154 ? 0.3679 0.5976 0.4057 0.0790  -0.0988 -0.0112 146 ASN A ND2   
1153 N  N     . ILE A 155 ? 0.2090 0.2978 0.2995 -0.0106 -0.0750 0.0293  147 ILE A N     
1154 C  CA    . ILE A 155 ? 0.2098 0.2812 0.2851 -0.0208 -0.0649 0.0319  147 ILE A CA    
1155 C  C     . ILE A 155 ? 0.1931 0.2873 0.2746 -0.0344 -0.0552 0.0298  147 ILE A C     
1156 O  O     . ILE A 155 ? 0.1908 0.2657 0.2716 -0.0222 -0.0419 0.0430  147 ILE A O     
1157 C  CB    . ILE A 155 ? 0.2231 0.2691 0.2867 -0.0176 -0.0669 0.0359  147 ILE A CB    
1158 C  CG1   . ILE A 155 ? 0.2286 0.2746 0.2899 -0.0006 -0.0750 0.0408  147 ILE A CG1   
1159 C  CG2   . ILE A 155 ? 0.2468 0.2704 0.2856 -0.0290 -0.0615 0.0323  147 ILE A CG2   
1160 C  CD1   . ILE A 155 ? 0.2367 0.2877 0.2957 0.0106  -0.0799 0.0463  147 ILE A CD1   
1161 N  N     . PRO A 156 ? 0.2062 0.3249 0.2707 -0.0145 -0.0503 0.0114  148 PRO A N     
1162 C  CA    . PRO A 156 ? 0.2113 0.3483 0.2658 -0.0129 -0.0395 0.0050  148 PRO A CA    
1163 C  C     . PRO A 156 ? 0.1918 0.3156 0.2525 -0.0398 -0.0316 0.0120  148 PRO A C     
1164 O  O     . PRO A 156 ? 0.1900 0.3236 0.2493 -0.0421 -0.0398 0.0348  148 PRO A O     
1165 C  CB    . PRO A 156 ? 0.2387 0.3799 0.2720 0.0063  -0.0413 -0.0071 148 PRO A CB    
1166 C  CG    . PRO A 156 ? 0.2913 0.4025 0.2787 0.0632  -0.0405 0.0019  148 PRO A CG    
1167 C  CD    . PRO A 156 ? 0.2630 0.3760 0.2747 0.0464  -0.0365 0.0071  148 PRO A CD    
1168 N  N     . THR A 157 ? 0.1760 0.2858 0.2422 -0.0453 -0.0290 -0.0091 149 THR A N     
1169 C  CA    . THR A 157 ? 0.1752 0.2598 0.2417 -0.0477 -0.0259 -0.0120 149 THR A CA    
1170 C  C     . THR A 157 ? 0.1959 0.2501 0.2469 -0.0482 -0.0228 -0.0231 149 THR A C     
1171 O  O     . THR A 157 ? 0.2140 0.2866 0.2684 -0.0380 -0.0167 -0.0437 149 THR A O     
1172 C  CB    . THR A 157 ? 0.1887 0.2799 0.2445 -0.0228 -0.0219 0.0015  149 THR A CB    
1173 O  OG1   . THR A 157 ? 0.1917 0.3175 0.2529 -0.0120 -0.0228 0.0119  149 THR A OG1   
1174 C  CG2   . THR A 157 ? 0.1998 0.2798 0.2427 0.0041  -0.0122 0.0072  149 THR A CG2   
1175 N  N     . GLN A 158 ? 0.1943 0.2346 0.2331 -0.0304 -0.0225 -0.0163 150 GLN A N     
1176 C  CA    . GLN A 158 ? 0.2137 0.2246 0.2264 -0.0470 -0.0172 -0.0040 150 GLN A CA    
1177 C  C     . GLN A 158 ? 0.2130 0.1902 0.2213 -0.0372 -0.0215 -0.0049 150 GLN A C     
1178 O  O     . GLN A 158 ? 0.3026 0.1749 0.2232 -0.0057 -0.0392 0.0001  150 GLN A O     
1179 C  CB    . GLN A 158 ? 0.2478 0.2819 0.2282 -0.0449 -0.0074 0.0150  150 GLN A CB    
1180 C  CG    . GLN A 158 ? 0.3166 0.3134 0.2379 -0.0269 -0.0013 0.0328  150 GLN A CG    
1181 C  CD    . GLN A 158 ? 0.3918 0.3403 0.2473 -0.0001 -0.0150 0.0333  150 GLN A CD    
1182 O  OE1   . GLN A 158 ? 0.4365 0.3404 0.2537 0.0221  -0.0153 0.0232  150 GLN A OE1   
1183 N  NE2   . GLN A 158 ? 0.4039 0.3536 0.2522 -0.0154 -0.0250 0.0388  150 GLN A NE2   
1184 N  N     . VAL A 159 ? 0.1552 0.1684 0.2245 -0.0274 -0.0177 -0.0151 151 VAL A N     
1185 C  CA    . VAL A 159 ? 0.1416 0.1658 0.2383 -0.0101 -0.0044 -0.0131 151 VAL A CA    
1186 C  C     . VAL A 159 ? 0.1339 0.1680 0.2613 -0.0034 -0.0095 -0.0318 151 VAL A C     
1187 O  O     . VAL A 159 ? 0.1653 0.2079 0.2936 0.0071  -0.0270 -0.0739 151 VAL A O     
1188 C  CB    . VAL A 159 ? 0.1415 0.1735 0.2430 -0.0189 -0.0081 0.0026  151 VAL A CB    
1189 C  CG1   . VAL A 159 ? 0.1598 0.1647 0.2514 -0.0329 -0.0146 0.0164  151 VAL A CG1   
1190 C  CG2   . VAL A 159 ? 0.1462 0.1735 0.2422 -0.0055 0.0022  0.0178  151 VAL A CG2   
1191 N  N     . GLY A 160 ? 0.1215 0.1386 0.2430 -0.0186 0.0006  -0.0110 152 GLY A N     
1192 C  CA    . GLY A 160 ? 0.1210 0.1501 0.2233 -0.0113 -0.0015 -0.0018 152 GLY A CA    
1193 C  C     . GLY A 160 ? 0.1334 0.1391 0.2007 0.0057  -0.0086 0.0065  152 GLY A C     
1194 O  O     . GLY A 160 ? 0.1397 0.1387 0.1951 -0.0155 -0.0024 0.0079  152 GLY A O     
1195 N  N     . LYS A 161 ? 0.1314 0.1314 0.1811 0.0039  -0.0028 0.0041  153 LYS A N     
1196 C  CA    . LYS A 161 ? 0.1208 0.1342 0.1552 -0.0043 -0.0104 -0.0011 153 LYS A CA    
1197 C  C     . LYS A 161 ? 0.1285 0.1383 0.1333 -0.0064 -0.0133 0.0229  153 LYS A C     
1198 O  O     . LYS A 161 ? 0.1511 0.1433 0.1410 -0.0043 -0.0067 0.0266  153 LYS A O     
1199 C  CB    . LYS A 161 ? 0.1250 0.1315 0.1528 0.0006  -0.0054 0.0031  153 LYS A CB    
1200 C  CG    . LYS A 161 ? 0.1463 0.1367 0.1450 -0.0020 -0.0007 0.0082  153 LYS A CG    
1201 C  CD    . LYS A 161 ? 0.1525 0.1480 0.1517 0.0074  -0.0062 0.0160  153 LYS A CD    
1202 C  CE    . LYS A 161 ? 0.1448 0.1479 0.1577 0.0103  -0.0003 0.0167  153 LYS A CE    
1203 N  NZ    . LYS A 161 ? 0.1490 0.1398 0.1596 0.0042  0.0137  0.0098  153 LYS A NZ    
1204 N  N     . ALA A 162 ? 0.1183 0.1401 0.1231 -0.0114 -0.0021 0.0196  154 ALA A N     
1205 C  CA    . ALA A 162 ? 0.1273 0.1277 0.1198 0.0013  -0.0044 0.0225  154 ALA A CA    
1206 C  C     . ALA A 162 ? 0.1266 0.1195 0.1257 0.0051  -0.0043 0.0198  154 ALA A C     
1207 O  O     . ALA A 162 ? 0.1267 0.1217 0.1184 0.0056  -0.0096 0.0183  154 ALA A O     
1208 C  CB    . ALA A 162 ? 0.1524 0.1462 0.1213 0.0078  -0.0019 0.0249  154 ALA A CB    
1209 N  N     . TYR A 163 ? 0.1173 0.1238 0.1303 -0.0122 -0.0084 0.0209  155 TYR A N     
1210 C  CA    . TYR A 163 ? 0.1103 0.1207 0.1295 -0.0196 -0.0008 0.0157  155 TYR A CA    
1211 C  C     . TYR A 163 ? 0.1172 0.1260 0.1352 -0.0078 -0.0013 0.0203  155 TYR A C     
1212 O  O     . TYR A 163 ? 0.1459 0.1292 0.1395 -0.0136 -0.0144 0.0321  155 TYR A O     
1213 C  CB    . TYR A 163 ? 0.1439 0.1313 0.1353 -0.0047 0.0001  0.0083  155 TYR A CB    
1214 C  CG    . TYR A 163 ? 0.1378 0.1225 0.1371 0.0091  0.0032  -0.0064 155 TYR A CG    
1215 C  CD1   . TYR A 163 ? 0.1306 0.1259 0.1504 0.0003  0.0214  0.0003  155 TYR A CD1   
1216 C  CD2   . TYR A 163 ? 0.1306 0.1307 0.1284 -0.0042 0.0069  -0.0058 155 TYR A CD2   
1217 C  CE1   . TYR A 163 ? 0.1340 0.1373 0.1545 0.0084  0.0223  -0.0070 155 TYR A CE1   
1218 C  CE2   . TYR A 163 ? 0.1404 0.1332 0.1376 -0.0018 0.0087  -0.0102 155 TYR A CE2   
1219 C  CZ    . TYR A 163 ? 0.1265 0.1558 0.1557 0.0147  0.0138  -0.0009 155 TYR A CZ    
1220 O  OH    . TYR A 163 ? 0.1389 0.1667 0.1759 0.0017  0.0021  -0.0028 155 TYR A OH    
1221 N  N     . SER A 164 ? 0.1193 0.1232 0.1314 0.0000  -0.0129 0.0163  156 SER A N     
1222 C  CA    . SER A 164 ? 0.1232 0.1160 0.1372 -0.0043 -0.0101 0.0196  156 SER A CA    
1223 C  C     . SER A 164 ? 0.1183 0.1176 0.1532 0.0098  -0.0099 0.0187  156 SER A C     
1224 O  O     . SER A 164 ? 0.1165 0.1339 0.1760 0.0028  -0.0110 0.0280  156 SER A O     
1225 C  CB    . SER A 164 ? 0.1392 0.1245 0.1406 -0.0048 -0.0082 0.0051  156 SER A CB    
1226 O  OG    . SER A 164 ? 0.1367 0.1268 0.1556 -0.0077 0.0120  0.0154  156 SER A OG    
1227 N  N     . THR A 165 ? 0.1081 0.1264 0.1518 -0.0012 0.0025  0.0199  157 THR A N     
1228 C  CA    . THR A 165 ? 0.1080 0.1336 0.1421 0.0027  -0.0017 -0.0007 157 THR A CA    
1229 C  C     . THR A 165 ? 0.1135 0.1245 0.1367 0.0052  0.0108  0.0058  157 THR A C     
1230 O  O     . THR A 165 ? 0.1239 0.1291 0.1491 0.0054  0.0016  -0.0002 157 THR A O     
1231 C  CB    . THR A 165 ? 0.1281 0.1357 0.1466 -0.0043 0.0030  0.0061  157 THR A CB    
1232 O  OG1   . THR A 165 ? 0.1262 0.1287 0.1505 -0.0063 0.0143  -0.0045 157 THR A OG1   
1233 C  CG2   . THR A 165 ? 0.1352 0.1510 0.1434 0.0014  0.0029  0.0016  157 THR A CG2   
1234 N  N     . ASP A 166 ? 0.1138 0.1051 0.1280 -0.0101 0.0107  0.0008  158 ASP A N     
1235 C  CA    . ASP A 166 ? 0.1410 0.1292 0.1151 -0.0034 0.0152  0.0105  158 ASP A CA    
1236 C  C     . ASP A 166 ? 0.1211 0.1362 0.1079 -0.0017 0.0011  -0.0005 158 ASP A C     
1237 O  O     . ASP A 166 ? 0.1349 0.1233 0.1088 -0.0154 0.0098  0.0035  158 ASP A O     
1238 C  CB    . ASP A 166 ? 0.1279 0.1274 0.1140 -0.0130 0.0122  0.0146  158 ASP A CB    
1239 C  CG    . ASP A 166 ? 0.1143 0.1191 0.1281 -0.0049 -0.0116 -0.0010 158 ASP A CG    
1240 O  OD1   . ASP A 166 ? 0.1334 0.1323 0.1414 0.0092  -0.0024 0.0051  158 ASP A OD1   
1241 O  OD2   . ASP A 166 ? 0.1375 0.1440 0.1439 0.0149  -0.0170 0.0057  158 ASP A OD2   
1242 N  N     . ILE A 167 ? 0.1292 0.1315 0.1093 0.0025  0.0060  0.0054  159 ILE A N     
1243 C  CA    . ILE A 167 ? 0.1441 0.1386 0.1187 0.0186  0.0085  0.0007  159 ILE A CA    
1244 C  C     . ILE A 167 ? 0.1516 0.1183 0.1245 -0.0015 0.0102  -0.0047 159 ILE A C     
1245 O  O     . ILE A 167 ? 0.1647 0.1242 0.1145 0.0077  0.0040  -0.0092 159 ILE A O     
1246 C  CB    . ILE A 167 ? 0.1432 0.1769 0.1184 0.0212  0.0094  0.0159  159 ILE A CB    
1247 C  CG1   . ILE A 167 ? 0.1526 0.2370 0.1274 0.0295  0.0089  0.0403  159 ILE A CG1   
1248 C  CG2   . ILE A 167 ? 0.1532 0.2024 0.1267 0.0150  0.0264  0.0090  159 ILE A CG2   
1249 C  CD1   . ILE A 167 ? 0.1586 0.2575 0.1311 0.0041  0.0062  0.0427  159 ILE A CD1   
1250 N  N     . PHE A 168 ? 0.1553 0.1133 0.1320 0.0063  0.0010  -0.0035 160 PHE A N     
1251 C  CA    . PHE A 168 ? 0.1478 0.1428 0.1328 0.0047  0.0030  0.0072  160 PHE A CA    
1252 C  C     . PHE A 168 ? 0.1554 0.1372 0.1426 0.0097  0.0025  -0.0067 160 PHE A C     
1253 O  O     . PHE A 168 ? 0.1643 0.1639 0.1579 0.0031  0.0050  0.0086  160 PHE A O     
1254 C  CB    . PHE A 168 ? 0.1493 0.1451 0.1311 0.0038  0.0063  0.0135  160 PHE A CB    
1255 C  CG    . PHE A 168 ? 0.1560 0.1544 0.1255 0.0085  0.0062  0.0375  160 PHE A CG    
1256 C  CD1   . PHE A 168 ? 0.1673 0.1760 0.1337 0.0069  0.0070  0.0492  160 PHE A CD1   
1257 C  CD2   . PHE A 168 ? 0.1644 0.1736 0.1216 0.0023  -0.0161 0.0336  160 PHE A CD2   
1258 C  CE1   . PHE A 168 ? 0.1698 0.2134 0.1308 0.0115  -0.0007 0.0413  160 PHE A CE1   
1259 C  CE2   . PHE A 168 ? 0.1725 0.1751 0.1202 0.0022  -0.0162 0.0559  160 PHE A CE2   
1260 C  CZ    . PHE A 168 ? 0.1698 0.1930 0.1262 0.0066  -0.0146 0.0442  160 PHE A CZ    
1261 N  N     . TYR A 169 ? 0.1449 0.1298 0.1327 0.0047  0.0126  0.0012  161 TYR A N     
1262 C  CA    . TYR A 169 ? 0.1659 0.1452 0.1354 0.0129  0.0144  -0.0003 161 TYR A CA    
1263 C  C     . TYR A 169 ? 0.1624 0.1619 0.1387 0.0040  0.0142  -0.0056 161 TYR A C     
1264 O  O     . TYR A 169 ? 0.1643 0.1691 0.1351 0.0023  0.0078  -0.0133 161 TYR A O     
1265 C  CB    . TYR A 169 ? 0.1662 0.1433 0.1466 0.0066  0.0194  0.0042  161 TYR A CB    
1266 C  CG    . TYR A 169 ? 0.1633 0.1537 0.1435 0.0101  0.0095  0.0044  161 TYR A CG    
1267 C  CD1   . TYR A 169 ? 0.1938 0.1624 0.1442 0.0068  -0.0028 0.0092  161 TYR A CD1   
1268 C  CD2   . TYR A 169 ? 0.1763 0.1420 0.1481 0.0067  0.0035  0.0097  161 TYR A CD2   
1269 C  CE1   . TYR A 169 ? 0.1867 0.1692 0.1527 0.0146  -0.0022 0.0054  161 TYR A CE1   
1270 C  CE2   . TYR A 169 ? 0.1787 0.1366 0.1582 -0.0084 0.0032  0.0107  161 TYR A CE2   
1271 C  CZ    . TYR A 169 ? 0.1743 0.1447 0.1607 0.0081  -0.0068 0.0119  161 TYR A CZ    
1272 O  OH    . TYR A 169 ? 0.1660 0.1534 0.1767 0.0196  -0.0167 0.0148  161 TYR A OH    
1273 N  N     . SER A 170 ? 0.1675 0.1427 0.1560 0.0035  0.0070  -0.0050 162 SER A N     
1274 C  CA    . SER A 170 ? 0.1859 0.1472 0.1661 0.0145  0.0099  -0.0095 162 SER A CA    
1275 C  C     . SER A 170 ? 0.1971 0.1467 0.1589 0.0104  0.0065  -0.0011 162 SER A C     
1276 O  O     . SER A 170 ? 0.2192 0.1865 0.1676 0.0325  -0.0001 0.0061  162 SER A O     
1277 C  CB    . SER A 170 ? 0.1939 0.1417 0.1853 0.0070  0.0080  -0.0042 162 SER A CB    
1278 O  OG    . SER A 170 ? 0.1771 0.1560 0.2038 -0.0070 0.0113  0.0034  162 SER A OG    
1279 N  N     . LYS A 171 ? 0.1844 0.1491 0.1576 0.0009  0.0233  0.0037  163 LYS A N     
1280 C  CA    . LYS A 171 ? 0.1811 0.1512 0.1765 -0.0043 0.0245  -0.0013 163 LYS A CA    
1281 C  C     . LYS A 171 ? 0.1804 0.1554 0.1730 -0.0071 0.0201  -0.0030 163 LYS A C     
1282 O  O     . LYS A 171 ? 0.1987 0.1601 0.1803 -0.0027 0.0425  0.0012  163 LYS A O     
1283 C  CB    . LYS A 171 ? 0.1881 0.1583 0.1896 -0.0036 0.0244  -0.0012 163 LYS A CB    
1284 C  CG    . LYS A 171 ? 0.2079 0.1519 0.1984 -0.0055 0.0367  0.0054  163 LYS A CG    
1285 C  CD    . LYS A 171 ? 0.2143 0.1587 0.2015 -0.0146 0.0460  0.0123  163 LYS A CD    
1286 C  CE    . LYS A 171 ? 0.2338 0.1661 0.2013 -0.0084 0.0446  0.0002  163 LYS A CE    
1287 N  NZ    . LYS A 171 ? 0.2379 0.1700 0.2088 -0.0060 0.0390  0.0048  163 LYS A NZ    
1288 N  N     . GLU A 172 ? 0.1673 0.1532 0.1641 -0.0098 0.0176  0.0029  164 GLU A N     
1289 C  CA    . GLU A 172 ? 0.1576 0.1527 0.1546 -0.0039 0.0222  0.0032  164 GLU A CA    
1290 C  C     . GLU A 172 ? 0.1814 0.1721 0.1650 -0.0025 0.0215  -0.0001 164 GLU A C     
1291 O  O     . GLU A 172 ? 0.1734 0.2087 0.1589 -0.0086 0.0022  -0.0231 164 GLU A O     
1292 C  CB    . GLU A 172 ? 0.1570 0.1412 0.1530 -0.0040 0.0162  -0.0023 164 GLU A CB    
1293 C  CG    . GLU A 172 ? 0.1609 0.1463 0.1509 0.0086  0.0139  -0.0053 164 GLU A CG    
1294 C  CD    . GLU A 172 ? 0.1775 0.1612 0.1602 0.0161  0.0215  0.0090  164 GLU A CD    
1295 O  OE1   . GLU A 172 ? 0.1732 0.1641 0.1472 0.0024  0.0299  0.0070  164 GLU A OE1   
1296 O  OE2   . GLU A 172 ? 0.2082 0.1789 0.1864 0.0274  0.0342  0.0326  164 GLU A OE2   
1297 N  N     . GLN A 173 ? 0.2092 0.1655 0.1857 -0.0257 0.0367  -0.0090 165 GLN A N     
1298 C  CA    . GLN A 173 ? 0.2255 0.2053 0.2030 -0.0417 0.0485  -0.0191 165 GLN A CA    
1299 C  C     . GLN A 173 ? 0.2175 0.1969 0.1960 -0.0334 0.0389  -0.0128 165 GLN A C     
1300 O  O     . GLN A 173 ? 0.2177 0.2098 0.2053 -0.0489 0.0211  -0.0062 165 GLN A O     
1301 C  CB    . GLN A 173 ? 0.2598 0.2703 0.2347 -0.0531 0.0503  -0.0222 165 GLN A CB    
1302 C  CG    . GLN A 173 ? 0.3129 0.3495 0.2687 -0.0570 0.0410  -0.0038 165 GLN A CG    
1303 C  CD    . GLN A 173 ? 0.3786 0.4335 0.3028 -0.0423 0.0250  0.0127  165 GLN A CD    
1304 O  OE1   . GLN A 173 ? 0.4123 0.4931 0.3160 -0.0112 0.0148  0.0172  165 GLN A OE1   
1305 N  NE2   . GLN A 173 ? 0.4152 0.4760 0.3139 -0.0136 0.0243  0.0210  165 GLN A NE2   
1306 N  N     . GLY A 174 ? 0.2164 0.1748 0.1804 -0.0175 0.0407  -0.0135 166 GLY A N     
1307 C  CA    . GLY A 174 ? 0.2251 0.1660 0.1720 -0.0162 0.0335  -0.0139 166 GLY A CA    
1308 C  C     . GLY A 174 ? 0.2039 0.1778 0.1619 -0.0130 0.0192  -0.0121 166 GLY A C     
1309 O  O     . GLY A 174 ? 0.2024 0.1847 0.1648 -0.0199 0.0206  -0.0102 166 GLY A O     
1310 N  N     . LEU A 175 ? 0.1852 0.1720 0.1388 -0.0117 0.0237  0.0023  167 LEU A N     
1311 C  CA    . LEU A 175 ? 0.1827 0.1772 0.1304 0.0050  0.0194  0.0127  167 LEU A CA    
1312 C  C     . LEU A 175 ? 0.1747 0.1731 0.1300 -0.0177 0.0067  0.0045  167 LEU A C     
1313 O  O     . LEU A 175 ? 0.1820 0.1654 0.1191 -0.0118 0.0173  0.0055  167 LEU A O     
1314 C  CB    . LEU A 175 ? 0.1794 0.1829 0.1323 0.0010  0.0163  0.0088  167 LEU A CB    
1315 C  CG    . LEU A 175 ? 0.1846 0.1755 0.1330 -0.0214 0.0152  -0.0101 167 LEU A CG    
1316 C  CD1   . LEU A 175 ? 0.2065 0.2102 0.1367 -0.0005 0.0240  -0.0143 167 LEU A CD1   
1317 C  CD2   . LEU A 175 ? 0.2114 0.1855 0.1375 -0.0176 0.0099  -0.0283 167 LEU A CD2   
1318 N  N     . ASN A 176 ? 0.1713 0.1788 0.1359 -0.0187 0.0042  0.0147  168 ASN A N     
1319 C  CA    . ASN A 176 ? 0.1859 0.1992 0.1385 -0.0020 -0.0121 0.0134  168 ASN A CA    
1320 C  C     . ASN A 176 ? 0.1863 0.1932 0.1212 -0.0168 -0.0058 0.0073  168 ASN A C     
1321 O  O     . ASN A 176 ? 0.1911 0.1792 0.1223 -0.0118 -0.0100 0.0126  168 ASN A O     
1322 C  CB    . ASN A 176 ? 0.1993 0.2097 0.1634 -0.0181 -0.0151 0.0178  168 ASN A CB    
1323 C  CG    . ASN A 176 ? 0.2123 0.2054 0.1871 -0.0107 -0.0231 0.0172  168 ASN A CG    
1324 O  OD1   . ASN A 176 ? 0.2392 0.1934 0.2093 -0.0024 -0.0215 -0.0109 168 ASN A OD1   
1325 N  ND2   . ASN A 176 ? 0.2119 0.2287 0.2025 0.0025  -0.0262 0.0357  168 ASN A ND2   
1326 N  N     . GLU A 177 ? 0.2056 0.1906 0.1148 -0.0390 0.0174  0.0137  169 GLU A N     
1327 C  CA    . GLU A 177 ? 0.2285 0.1985 0.1254 -0.0424 0.0282  0.0030  169 GLU A CA    
1328 C  C     . GLU A 177 ? 0.2091 0.1786 0.1282 -0.0254 0.0218  -0.0159 169 GLU A C     
1329 O  O     . GLU A 177 ? 0.2012 0.1811 0.1409 -0.0338 0.0106  -0.0126 169 GLU A O     
1330 C  CB    . GLU A 177 ? 0.2765 0.2335 0.1368 -0.0426 0.0453  -0.0040 169 GLU A CB    
1331 C  CG    . GLU A 177 ? 0.3222 0.3101 0.1555 -0.0380 0.0543  0.0053  169 GLU A CG    
1332 C  CD    . GLU A 177 ? 0.3574 0.3637 0.1741 -0.0225 0.0583  0.0118  169 GLU A CD    
1333 O  OE1   . GLU A 177 ? 0.3134 0.3446 0.1785 -0.0570 0.0612  0.0100  169 GLU A OE1   
1334 O  OE2   . GLU A 177 ? 0.4152 0.4159 0.1940 0.0084  0.0582  0.0187  169 GLU A OE2   
1335 N  N     . ALA A 178 ? 0.1929 0.1730 0.1255 -0.0093 0.0134  -0.0174 170 ALA A N     
1336 C  CA    . ALA A 178 ? 0.1855 0.1734 0.1232 -0.0174 0.0123  0.0003  170 ALA A CA    
1337 C  C     . ALA A 178 ? 0.1826 0.1477 0.1201 -0.0216 0.0040  0.0031  170 ALA A C     
1338 O  O     . ALA A 178 ? 0.1762 0.1485 0.1426 -0.0213 0.0005  0.0122  170 ALA A O     
1339 C  CB    . ALA A 178 ? 0.1861 0.1883 0.1402 -0.0012 0.0134  0.0091  170 ALA A CB    
1340 N  N     . LEU A 179 ? 0.1723 0.1431 0.1174 -0.0173 0.0015  0.0002  171 LEU A N     
1341 C  CA    . LEU A 179 ? 0.1671 0.1518 0.1210 -0.0098 -0.0020 0.0064  171 LEU A CA    
1342 C  C     . LEU A 179 ? 0.1717 0.1446 0.1064 -0.0056 -0.0035 0.0127  171 LEU A C     
1343 O  O     . LEU A 179 ? 0.1775 0.1734 0.1164 -0.0217 -0.0048 0.0099  171 LEU A O     
1344 C  CB    . LEU A 179 ? 0.1647 0.1498 0.1298 -0.0022 0.0046  0.0031  171 LEU A CB    
1345 C  CG    . LEU A 179 ? 0.1679 0.1367 0.1355 -0.0026 0.0067  -0.0039 171 LEU A CG    
1346 C  CD1   . LEU A 179 ? 0.1821 0.1485 0.1419 -0.0082 -0.0021 0.0010  171 LEU A CD1   
1347 C  CD2   . LEU A 179 ? 0.1703 0.1497 0.1449 0.0124  0.0050  -0.0051 171 LEU A CD2   
1348 N  N     . ALA A 180 ? 0.1715 0.1632 0.1085 0.0021  -0.0057 0.0187  172 ALA A N     
1349 C  CA    . ALA A 180 ? 0.1878 0.1740 0.1237 0.0033  -0.0060 0.0092  172 ALA A CA    
1350 C  C     . ALA A 180 ? 0.1961 0.1709 0.1302 -0.0125 -0.0097 0.0053  172 ALA A C     
1351 O  O     . ALA A 180 ? 0.1937 0.1938 0.1389 -0.0237 -0.0110 0.0190  172 ALA A O     
1352 C  CB    . ALA A 180 ? 0.1935 0.1926 0.1277 -0.0066 0.0041  0.0085  172 ALA A CB    
1353 N  N     . GLN A 181 ? 0.2000 0.1554 0.1444 -0.0111 0.0035  0.0139  173 GLN A N     
1354 C  CA    . GLN A 181 ? 0.2230 0.1574 0.1556 -0.0095 0.0135  0.0066  173 GLN A CA    
1355 C  C     . GLN A 181 ? 0.1944 0.1604 0.1571 -0.0231 0.0032  0.0037  173 GLN A C     
1356 O  O     . GLN A 181 ? 0.2154 0.1742 0.1683 -0.0394 -0.0066 0.0018  173 GLN A O     
1357 C  CB    . GLN A 181 ? 0.2694 0.1577 0.1783 -0.0073 0.0341  -0.0114 173 GLN A CB    
1358 C  CG    . GLN A 181 ? 0.3257 0.1866 0.1999 -0.0141 0.0584  0.0112  173 GLN A CG    
1359 C  CD    . GLN A 181 ? 0.4001 0.2666 0.2211 -0.0082 0.0747  0.0276  173 GLN A CD    
1360 O  OE1   . GLN A 181 ? 0.4493 0.3163 0.2317 0.0016  0.0915  0.0345  173 GLN A OE1   
1361 N  NE2   . GLN A 181 ? 0.4173 0.2837 0.2314 -0.0091 0.0532  0.0137  173 GLN A NE2   
1362 N  N     . TYR A 182 ? 0.1719 0.1522 0.1494 -0.0098 -0.0037 -0.0027 174 TYR A N     
1363 C  CA    . TYR A 182 ? 0.1623 0.1478 0.1448 0.0047  -0.0057 0.0072  174 TYR A CA    
1364 C  C     . TYR A 182 ? 0.1619 0.1369 0.1524 0.0016  -0.0015 0.0131  174 TYR A C     
1365 O  O     . TYR A 182 ? 0.1634 0.1499 0.1501 0.0080  0.0095  0.0139  174 TYR A O     
1366 C  CB    . TYR A 182 ? 0.1619 0.1517 0.1483 -0.0112 -0.0056 0.0053  174 TYR A CB    
1367 C  CG    . TYR A 182 ? 0.1603 0.1531 0.1440 -0.0086 -0.0101 0.0082  174 TYR A CG    
1368 C  CD1   . TYR A 182 ? 0.1440 0.1500 0.1433 -0.0138 -0.0163 0.0107  174 TYR A CD1   
1369 C  CD2   . TYR A 182 ? 0.1816 0.1395 0.1453 0.0018  -0.0100 0.0062  174 TYR A CD2   
1370 C  CE1   . TYR A 182 ? 0.1530 0.1513 0.1526 -0.0038 -0.0088 0.0099  174 TYR A CE1   
1371 C  CE2   . TYR A 182 ? 0.1689 0.1521 0.1481 -0.0115 -0.0038 0.0101  174 TYR A CE2   
1372 C  CZ    . TYR A 182 ? 0.1545 0.1439 0.1554 -0.0096 -0.0089 0.0037  174 TYR A CZ    
1373 O  OH    . TYR A 182 ? 0.1571 0.1425 0.1686 0.0001  -0.0038 -0.0049 174 TYR A OH    
1374 N  N     . HIS A 183 ? 0.1521 0.1632 0.1623 -0.0075 -0.0123 0.0038  175 HIS A N     
1375 C  CA    . HIS A 183 ? 0.1575 0.1775 0.1746 -0.0175 -0.0161 0.0058  175 HIS A CA    
1376 C  C     . HIS A 183 ? 0.1646 0.1548 0.1703 -0.0133 0.0037  0.0182  175 HIS A C     
1377 O  O     . HIS A 183 ? 0.1686 0.1829 0.1891 -0.0229 0.0195  0.0105  175 HIS A O     
1378 C  CB    . HIS A 183 ? 0.1725 0.1894 0.1817 0.0072  -0.0403 0.0007  175 HIS A CB    
1379 C  CG    . HIS A 183 ? 0.2146 0.1960 0.1851 -0.0155 -0.0752 -0.0052 175 HIS A CG    
1380 N  ND1   . HIS A 183 ? 0.2902 0.2401 0.1945 0.0386  -0.0710 -0.0115 175 HIS A ND1   
1381 C  CD2   . HIS A 183 ? 0.2316 0.1851 0.1870 -0.0202 -0.0713 0.0038  175 HIS A CD2   
1382 C  CE1   . HIS A 183 ? 0.3134 0.2469 0.2011 0.0454  -0.0655 -0.0104 175 HIS A CE1   
1383 N  NE2   . HIS A 183 ? 0.2783 0.2067 0.1946 -0.0005 -0.0653 0.0070  175 HIS A NE2   
1384 N  N     . PHE A 184 ? 0.1667 0.1471 0.1468 0.0014  -0.0055 0.0242  176 PHE A N     
1385 C  CA    . PHE A 184 ? 0.1669 0.1314 0.1391 0.0108  -0.0053 0.0223  176 PHE A CA    
1386 C  C     . PHE A 184 ? 0.1789 0.1358 0.1446 -0.0016 -0.0030 0.0377  176 PHE A C     
1387 O  O     . PHE A 184 ? 0.2186 0.1742 0.1441 0.0208  0.0096  0.0463  176 PHE A O     
1388 C  CB    . PHE A 184 ? 0.1650 0.1515 0.1253 0.0070  -0.0024 0.0180  176 PHE A CB    
1389 C  CG    . PHE A 184 ? 0.1499 0.1362 0.1017 -0.0049 0.0112  0.0222  176 PHE A CG    
1390 C  CD1   . PHE A 184 ? 0.1501 0.1584 0.0969 -0.0009 0.0030  0.0121  176 PHE A CD1   
1391 C  CD2   . PHE A 184 ? 0.1554 0.1590 0.0878 -0.0018 0.0028  0.0045  176 PHE A CD2   
1392 C  CE1   . PHE A 184 ? 0.1451 0.1344 0.0883 -0.0090 0.0078  0.0042  176 PHE A CE1   
1393 C  CE2   . PHE A 184 ? 0.1494 0.1648 0.0918 -0.0036 0.0038  -0.0052 176 PHE A CE2   
1394 C  CZ    . PHE A 184 ? 0.1317 0.1573 0.0921 -0.0021 -0.0003 -0.0054 176 PHE A CZ    
1395 N  N     . ILE A 185 ? 0.1558 0.1365 0.1620 0.0030  -0.0154 0.0249  177 ILE A N     
1396 C  CA    . ILE A 185 ? 0.1602 0.1460 0.1791 0.0130  -0.0346 0.0252  177 ILE A CA    
1397 C  C     . ILE A 185 ? 0.1661 0.1685 0.1777 0.0157  -0.0322 0.0269  177 ILE A C     
1398 O  O     . ILE A 185 ? 0.2043 0.1680 0.1852 0.0017  -0.0450 0.0312  177 ILE A O     
1399 C  CB    . ILE A 185 ? 0.1715 0.1487 0.1997 -0.0020 -0.0401 0.0212  177 ILE A CB    
1400 C  CG1   . ILE A 185 ? 0.1629 0.1501 0.2145 -0.0122 -0.0301 0.0105  177 ILE A CG1   
1401 C  CG2   . ILE A 185 ? 0.1942 0.1770 0.2091 0.0013  -0.0339 0.0159  177 ILE A CG2   
1402 C  CD1   . ILE A 185 ? 0.1780 0.1854 0.2275 -0.0051 -0.0255 0.0066  177 ILE A CD1   
1403 N  N     . ALA A 186 ? 0.1434 0.1614 0.1681 0.0051  -0.0304 0.0260  178 ALA A N     
1404 C  CA    . ALA A 186 ? 0.1540 0.1503 0.1684 -0.0098 -0.0202 0.0242  178 ALA A CA    
1405 C  C     . ALA A 186 ? 0.1519 0.1732 0.1631 -0.0082 -0.0223 0.0331  178 ALA A C     
1406 O  O     . ALA A 186 ? 0.1515 0.1810 0.1792 -0.0169 -0.0325 0.0592  178 ALA A O     
1407 C  CB    . ALA A 186 ? 0.1695 0.1431 0.1697 -0.0026 -0.0097 0.0219  178 ALA A CB    
1408 N  N     . VAL A 187 ? 0.1382 0.1542 0.1408 -0.0074 -0.0144 0.0292  179 VAL A N     
1409 C  CA    . VAL A 187 ? 0.1553 0.1362 0.1435 -0.0040 -0.0013 0.0285  179 VAL A CA    
1410 C  C     . VAL A 187 ? 0.1495 0.1176 0.1385 0.0016  -0.0131 0.0241  179 VAL A C     
1411 O  O     . VAL A 187 ? 0.1592 0.1304 0.1389 0.0013  -0.0207 0.0245  179 VAL A O     
1412 C  CB    . VAL A 187 ? 0.1669 0.1658 0.1612 -0.0019 0.0041  0.0198  179 VAL A CB    
1413 C  CG1   . VAL A 187 ? 0.1601 0.1863 0.1702 0.0038  0.0093  0.0200  179 VAL A CG1   
1414 C  CG2   . VAL A 187 ? 0.1889 0.1925 0.1690 0.0122  0.0029  0.0082  179 VAL A CG2   
1415 N  N     . GLU A 188 ? 0.1446 0.1236 0.1457 -0.0113 -0.0233 0.0239  180 GLU A N     
1416 C  CA    . GLU A 188 ? 0.1353 0.1276 0.1583 -0.0096 -0.0177 0.0098  180 GLU A CA    
1417 C  C     . GLU A 188 ? 0.1260 0.1160 0.1564 -0.0214 -0.0038 0.0146  180 GLU A C     
1418 O  O     . GLU A 188 ? 0.1255 0.1237 0.1420 -0.0018 -0.0049 0.0071  180 GLU A O     
1419 C  CB    . GLU A 188 ? 0.1223 0.1610 0.1773 -0.0118 -0.0014 0.0105  180 GLU A CB    
1420 C  CG    . GLU A 188 ? 0.1203 0.1744 0.2065 -0.0202 0.0128  0.0102  180 GLU A CG    
1421 C  CD    . GLU A 188 ? 0.1629 0.1986 0.2335 -0.0116 0.0110  0.0145  180 GLU A CD    
1422 O  OE1   . GLU A 188 ? 0.2135 0.3177 0.2455 0.0655  -0.0179 -0.0033 180 GLU A OE1   
1423 O  OE2   . GLU A 188 ? 0.2316 0.2747 0.2504 0.0582  -0.0288 0.0173  180 GLU A OE2   
1424 N  N     . MET A 189 ? 0.1121 0.1169 0.1646 -0.0049 -0.0023 0.0068  181 MET A N     
1425 C  CA    . MET A 189 ? 0.1127 0.1090 0.1523 -0.0040 0.0009  -0.0023 181 MET A CA    
1426 C  C     . MET A 189 ? 0.1298 0.1277 0.1520 0.0045  0.0000  0.0096  181 MET A C     
1427 O  O     . MET A 189 ? 0.1394 0.2005 0.1643 -0.0305 -0.0170 0.0403  181 MET A O     
1428 C  CB    . MET A 189 ? 0.1187 0.1129 0.1481 -0.0026 0.0040  0.0004  181 MET A CB    
1429 C  CG    . MET A 189 ? 0.1310 0.1123 0.1585 -0.0088 0.0111  0.0140  181 MET A CG    
1430 S  SD    . MET A 189 ? 0.1294 0.1449 0.1748 -0.0151 -0.0057 0.0210  181 MET A SD    
1431 C  CE    . MET A 189 ? 0.1178 0.1803 0.1814 -0.0288 0.0179  0.0368  181 MET A CE    
1432 N  N     . GLU A 190 ? 0.1246 0.1305 0.1388 -0.0028 0.0136  -0.0008 182 GLU A N     
1433 C  CA    . GLU A 190 ? 0.1109 0.1272 0.1364 0.0067  0.0114  0.0008  182 GLU A CA    
1434 C  C     . GLU A 190 ? 0.1099 0.1308 0.1440 0.0049  0.0047  -0.0011 182 GLU A C     
1435 O  O     . GLU A 190 ? 0.1465 0.1274 0.1378 0.0039  -0.0020 0.0023  182 GLU A O     
1436 C  CB    . GLU A 190 ? 0.1445 0.1408 0.1424 0.0207  0.0080  0.0071  182 GLU A CB    
1437 C  CG    . GLU A 190 ? 0.1574 0.1322 0.1508 0.0252  0.0106  0.0165  182 GLU A CG    
1438 C  CD    . GLU A 190 ? 0.1359 0.1383 0.1653 -0.0044 -0.0153 0.0093  182 GLU A CD    
1439 O  OE1   . GLU A 190 ? 0.1448 0.1570 0.1822 -0.0202 -0.0215 0.0229  182 GLU A OE1   
1440 O  OE2   . GLU A 190 ? 0.1313 0.1287 0.1721 -0.0011 -0.0212 0.0037  182 GLU A OE2   
1441 N  N     . SER A 191 ? 0.1214 0.1293 0.1547 0.0026  0.0022  -0.0020 183 SER A N     
1442 C  CA    A SER A 191 ? 0.1193 0.1382 0.1627 0.0012  0.0114  0.0042  183 SER A CA    
1443 C  CA    B SER A 191 ? 0.1212 0.1383 0.1550 -0.0013 0.0131  -0.0020 183 SER A CA    
1444 C  C     . SER A 191 ? 0.1129 0.1259 0.1593 -0.0079 0.0166  0.0052  183 SER A C     
1445 O  O     . SER A 191 ? 0.1248 0.1319 0.1587 -0.0163 0.0179  0.0044  183 SER A O     
1446 C  CB    A SER A 191 ? 0.1091 0.1767 0.1797 0.0020  0.0063  0.0099  183 SER A CB    
1447 C  CB    B SER A 191 ? 0.1197 0.1712 0.1559 -0.0078 0.0139  -0.0063 183 SER A CB    
1448 O  OG    A SER A 191 ? 0.1157 0.1722 0.1912 0.0084  -0.0067 0.0037  183 SER A OG    
1449 O  OG    B SER A 191 ? 0.1236 0.1590 0.1528 -0.0208 0.0078  -0.0176 183 SER A OG    
1450 N  N     . ALA A 192 ? 0.1150 0.1167 0.1687 -0.0069 0.0003  -0.0063 184 ALA A N     
1451 C  CA    . ALA A 192 ? 0.1340 0.1248 0.1635 -0.0054 0.0097  0.0035  184 ALA A CA    
1452 C  C     . ALA A 192 ? 0.1311 0.1290 0.1535 -0.0028 0.0020  0.0125  184 ALA A C     
1453 O  O     . ALA A 192 ? 0.1449 0.1285 0.1537 -0.0045 0.0113  0.0133  184 ALA A O     
1454 C  CB    . ALA A 192 ? 0.1330 0.1275 0.1660 -0.0021 0.0189  0.0053  184 ALA A CB    
1455 N  N     . GLY A 193 ? 0.1233 0.1177 0.1435 -0.0127 -0.0044 0.0088  185 GLY A N     
1456 C  CA    . GLY A 193 ? 0.1275 0.1419 0.1429 0.0024  -0.0025 0.0019  185 GLY A CA    
1457 C  C     . GLY A 193 ? 0.1275 0.1306 0.1364 0.0023  -0.0003 0.0088  185 GLY A C     
1458 O  O     . GLY A 193 ? 0.1245 0.1708 0.1408 0.0013  -0.0016 0.0100  185 GLY A O     
1459 N  N     . LEU A 194 ? 0.1296 0.1370 0.1324 0.0086  0.0143  0.0037  186 LEU A N     
1460 C  CA    . LEU A 194 ? 0.1354 0.1081 0.1368 0.0017  0.0105  -0.0039 186 LEU A CA    
1461 C  C     . LEU A 194 ? 0.1296 0.1128 0.1327 0.0149  0.0162  -0.0027 186 LEU A C     
1462 O  O     . LEU A 194 ? 0.1292 0.1360 0.1306 0.0051  0.0166  0.0097  186 LEU A O     
1463 C  CB    . LEU A 194 ? 0.1423 0.1168 0.1496 -0.0030 0.0087  0.0014  186 LEU A CB    
1464 C  CG    . LEU A 194 ? 0.1369 0.1338 0.1497 0.0072  0.0046  0.0087  186 LEU A CG    
1465 C  CD1   . LEU A 194 ? 0.1428 0.1654 0.1528 0.0225  0.0119  0.0123  186 LEU A CD1   
1466 C  CD2   . LEU A 194 ? 0.1376 0.1575 0.1587 0.0072  0.0034  0.0074  186 LEU A CD2   
1467 N  N     . PHE A 195 ? 0.1293 0.1181 0.1372 0.0125  0.0082  0.0043  187 PHE A N     
1468 C  CA    . PHE A 195 ? 0.1240 0.1267 0.1480 -0.0053 -0.0038 0.0075  187 PHE A CA    
1469 C  C     . PHE A 195 ? 0.1340 0.1216 0.1365 -0.0028 0.0140  0.0168  187 PHE A C     
1470 O  O     . PHE A 195 ? 0.1326 0.1326 0.1351 0.0080  0.0117  0.0160  187 PHE A O     
1471 C  CB    . PHE A 195 ? 0.1465 0.1355 0.1458 0.0014  -0.0119 0.0086  187 PHE A CB    
1472 C  CG    . PHE A 195 ? 0.1200 0.1306 0.1324 -0.0141 -0.0047 0.0113  187 PHE A CG    
1473 C  CD1   . PHE A 195 ? 0.1465 0.1950 0.1347 0.0408  -0.0033 0.0002  187 PHE A CD1   
1474 C  CD2   . PHE A 195 ? 0.1495 0.1387 0.1325 0.0178  -0.0046 0.0178  187 PHE A CD2   
1475 C  CE1   . PHE A 195 ? 0.1418 0.1941 0.1284 0.0247  0.0016  0.0038  187 PHE A CE1   
1476 C  CE2   . PHE A 195 ? 0.1778 0.1409 0.1283 0.0191  0.0024  0.0231  187 PHE A CE2   
1477 C  CZ    . PHE A 195 ? 0.1483 0.1702 0.1241 0.0016  -0.0086 0.0122  187 PHE A CZ    
1478 N  N     . PRO A 196 ? 0.1311 0.1315 0.1348 0.0019  0.0045  0.0223  188 PRO A N     
1479 C  CA    . PRO A 196 ? 0.1297 0.1314 0.1427 0.0034  0.0015  0.0207  188 PRO A CA    
1480 C  C     . PRO A 196 ? 0.1282 0.1426 0.1508 0.0057  0.0114  0.0309  188 PRO A C     
1481 O  O     . PRO A 196 ? 0.1365 0.1299 0.1689 0.0034  0.0122  0.0289  188 PRO A O     
1482 C  CB    . PRO A 196 ? 0.1358 0.1317 0.1313 0.0131  0.0076  0.0060  188 PRO A CB    
1483 C  CG    . PRO A 196 ? 0.1408 0.1400 0.1275 0.0134  0.0002  -0.0038 188 PRO A CG    
1484 C  CD    . PRO A 196 ? 0.1315 0.1509 0.1309 0.0008  0.0082  0.0044  188 PRO A CD    
1485 N  N     . ILE A 197 ? 0.1343 0.1307 0.1414 -0.0003 0.0061  0.0051  189 ILE A N     
1486 C  CA    . ILE A 197 ? 0.1305 0.1371 0.1296 -0.0055 0.0048  0.0082  189 ILE A CA    
1487 C  C     . ILE A 197 ? 0.1425 0.1201 0.1220 0.0053  0.0123  0.0101  189 ILE A C     
1488 O  O     . ILE A 197 ? 0.1555 0.1354 0.1193 0.0089  0.0288  0.0189  189 ILE A O     
1489 C  CB    . ILE A 197 ? 0.1282 0.1482 0.1317 -0.0019 0.0022  0.0038  189 ILE A CB    
1490 C  CG1   . ILE A 197 ? 0.1544 0.1325 0.1404 -0.0033 0.0110  0.0109  189 ILE A CG1   
1491 C  CG2   . ILE A 197 ? 0.1508 0.1482 0.1275 0.0050  0.0048  -0.0041 189 ILE A CG2   
1492 C  CD1   . ILE A 197 ? 0.1738 0.1355 0.1429 -0.0144 0.0178  0.0044  189 ILE A CD1   
1493 N  N     . ALA A 198 ? 0.1400 0.1342 0.1258 0.0085  0.0094  0.0228  190 ALA A N     
1494 C  CA    . ALA A 198 ? 0.1454 0.1409 0.1367 0.0107  0.0235  0.0305  190 ALA A CA    
1495 C  C     . ALA A 198 ? 0.1347 0.1498 0.1398 0.0036  0.0295  0.0264  190 ALA A C     
1496 O  O     . ALA A 198 ? 0.1510 0.1509 0.1407 0.0113  0.0294  0.0244  190 ALA A O     
1497 C  CB    . ALA A 198 ? 0.1646 0.1287 0.1451 0.0213  0.0062  0.0280  190 ALA A CB    
1498 N  N     . ASP A 199 ? 0.1354 0.1239 0.1539 0.0062  0.0085  0.0092  191 ASP A N     
1499 C  CA    . ASP A 199 ? 0.1448 0.1395 0.1680 0.0082  0.0107  0.0224  191 ASP A CA    
1500 C  C     . ASP A 199 ? 0.1502 0.1445 0.1670 0.0081  0.0162  0.0390  191 ASP A C     
1501 O  O     . ASP A 199 ? 0.1723 0.1520 0.1838 0.0084  0.0164  0.0342  191 ASP A O     
1502 C  CB    . ASP A 199 ? 0.1539 0.1564 0.1761 0.0114  0.0173  0.0204  191 ASP A CB    
1503 C  CG    . ASP A 199 ? 0.1689 0.1690 0.1865 0.0102  0.0271  0.0183  191 ASP A CG    
1504 O  OD1   . ASP A 199 ? 0.1799 0.1991 0.1989 0.0007  0.0208  -0.0075 191 ASP A OD1   
1505 O  OD2   . ASP A 199 ? 0.1740 0.1676 0.1839 0.0205  0.0179  0.0156  191 ASP A OD2   
1506 N  N     . TYR A 200 ? 0.1507 0.1497 0.1501 0.0100  -0.0035 0.0316  192 TYR A N     
1507 C  CA    . TYR A 200 ? 0.1762 0.1443 0.1326 0.0203  -0.0001 0.0301  192 TYR A CA    
1508 C  C     . TYR A 200 ? 0.1716 0.1612 0.1221 -0.0013 0.0055  0.0485  192 TYR A C     
1509 O  O     . TYR A 200 ? 0.1806 0.2038 0.1163 0.0124  0.0163  0.0476  192 TYR A O     
1510 C  CB    . TYR A 200 ? 0.1690 0.1629 0.1300 0.0111  0.0067  0.0179  192 TYR A CB    
1511 C  CG    . TYR A 200 ? 0.1670 0.1696 0.1289 0.0233  -0.0128 0.0076  192 TYR A CG    
1512 C  CD1   . TYR A 200 ? 0.1670 0.1755 0.1399 0.0015  -0.0093 0.0001  192 TYR A CD1   
1513 C  CD2   . TYR A 200 ? 0.1655 0.1905 0.1330 0.0059  -0.0157 -0.0072 192 TYR A CD2   
1514 C  CE1   . TYR A 200 ? 0.1805 0.1949 0.1417 0.0066  -0.0152 0.0118  192 TYR A CE1   
1515 C  CE2   . TYR A 200 ? 0.1921 0.2098 0.1438 0.0082  -0.0090 -0.0043 192 TYR A CE2   
1516 C  CZ    . TYR A 200 ? 0.1913 0.2147 0.1469 -0.0195 -0.0221 -0.0108 192 TYR A CZ    
1517 O  OH    . TYR A 200 ? 0.2299 0.2573 0.1601 -0.0112 -0.0204 -0.0099 192 TYR A OH    
1518 N  N     . TYR A 201 ? 0.1648 0.1734 0.1327 0.0211  0.0093  0.0399  193 TYR A N     
1519 C  CA    . TYR A 201 ? 0.1644 0.1937 0.1502 0.0114  0.0286  0.0222  193 TYR A CA    
1520 C  C     . TYR A 201 ? 0.1732 0.2068 0.1632 0.0177  0.0296  0.0282  193 TYR A C     
1521 O  O     . TYR A 201 ? 0.1796 0.2241 0.1764 0.0167  0.0494  0.0238  193 TYR A O     
1522 C  CB    . TYR A 201 ? 0.1603 0.1882 0.1480 0.0225  0.0271  0.0118  193 TYR A CB    
1523 C  CG    . TYR A 201 ? 0.1716 0.1665 0.1504 0.0151  0.0212  0.0004  193 TYR A CG    
1524 C  CD1   . TYR A 201 ? 0.1915 0.1931 0.1570 0.0091  0.0162  -0.0065 193 TYR A CD1   
1525 C  CD2   . TYR A 201 ? 0.1647 0.1719 0.1521 0.0289  0.0202  -0.0065 193 TYR A CD2   
1526 C  CE1   . TYR A 201 ? 0.1814 0.1973 0.1661 0.0089  0.0166  -0.0053 193 TYR A CE1   
1527 C  CE2   . TYR A 201 ? 0.1680 0.1689 0.1585 0.0216  0.0175  -0.0111 193 TYR A CE2   
1528 C  CZ    . TYR A 201 ? 0.1765 0.1876 0.1622 0.0128  0.0202  -0.0068 193 TYR A CZ    
1529 O  OH    . TYR A 201 ? 0.1727 0.2148 0.1668 0.0184  0.0117  -0.0099 193 TYR A OH    
1530 N  N     . GLY A 202 ? 0.1617 0.1982 0.1688 0.0100  0.0265  0.0400  194 GLY A N     
1531 C  CA    . GLY A 202 ? 0.1640 0.1947 0.1834 0.0192  0.0360  0.0429  194 GLY A CA    
1532 C  C     . GLY A 202 ? 0.1578 0.2016 0.1926 -0.0044 0.0316  0.0508  194 GLY A C     
1533 O  O     . GLY A 202 ? 0.1799 0.2241 0.2099 0.0008  0.0524  0.0659  194 GLY A O     
1534 N  N     . ALA A 203 ? 0.1469 0.1972 0.1886 0.0005  0.0182  0.0463  195 ALA A N     
1535 C  CA    . ALA A 203 ? 0.1557 0.1668 0.1940 0.0041  0.0125  0.0296  195 ALA A CA    
1536 C  C     . ALA A 203 ? 0.1548 0.1703 0.2086 0.0085  0.0145  0.0180  195 ALA A C     
1537 O  O     . ALA A 203 ? 0.1745 0.1717 0.2228 0.0150  0.0178  0.0085  195 ALA A O     
1538 C  CB    . ALA A 203 ? 0.1831 0.1811 0.2000 0.0188  0.0063  0.0214  195 ALA A CB    
1539 N  N     . ARG A 204 ? 0.1783 0.1510 0.2054 0.0048  0.0116  0.0258  196 ARG A N     
1540 C  CA    . ARG A 204 ? 0.1807 0.1666 0.2098 0.0032  0.0040  0.0042  196 ARG A CA    
1541 C  C     . ARG A 204 ? 0.1491 0.1471 0.1967 0.0036  0.0229  0.0061  196 ARG A C     
1542 O  O     . ARG A 204 ? 0.1505 0.1289 0.2003 0.0146  0.0239  0.0053  196 ARG A O     
1543 C  CB    . ARG A 204 ? 0.2103 0.2079 0.2343 -0.0369 0.0132  0.0030  196 ARG A CB    
1544 C  CG    . ARG A 204 ? 0.2287 0.2847 0.2659 -0.0415 0.0332  0.0175  196 ARG A CG    
1545 C  CD    . ARG A 204 ? 0.2478 0.3511 0.2920 -0.0225 0.0391  0.0089  196 ARG A CD    
1546 N  NE    . ARG A 204 ? 0.2656 0.3695 0.3137 -0.0364 0.0367  0.0062  196 ARG A NE    
1547 C  CZ    . ARG A 204 ? 0.2797 0.3889 0.3281 -0.0215 0.0297  0.0088  196 ARG A CZ    
1548 N  NH1   . ARG A 204 ? 0.2831 0.3907 0.3307 -0.0439 0.0281  0.0118  196 ARG A NH1   
1549 N  NH2   . ARG A 204 ? 0.2801 0.3825 0.3341 0.0119  0.0305  0.0123  196 ARG A NH2   
1550 N  N     . ALA A 205 ? 0.1303 0.1328 0.1929 0.0117  0.0137  0.0142  197 ALA A N     
1551 C  CA    . ALA A 205 ? 0.1332 0.1279 0.1845 0.0101  0.0264  0.0247  197 ALA A CA    
1552 C  C     . ALA A 205 ? 0.1240 0.1110 0.1894 0.0152  0.0146  0.0123  197 ALA A C     
1553 O  O     . ALA A 205 ? 0.1616 0.1186 0.1894 0.0087  0.0238  0.0138  197 ALA A O     
1554 C  CB    . ALA A 205 ? 0.1483 0.1584 0.1835 0.0145  0.0221  0.0114  197 ALA A CB    
1555 N  N     . GLY A 206 ? 0.1430 0.1058 0.1814 0.0144  0.0083  0.0086  198 GLY A N     
1556 C  CA    . GLY A 206 ? 0.1463 0.1191 0.1798 0.0053  -0.0030 -0.0106 198 GLY A CA    
1557 C  C     . GLY A 206 ? 0.1331 0.1086 0.1698 0.0104  -0.0050 -0.0197 198 GLY A C     
1558 O  O     . GLY A 206 ? 0.1401 0.1144 0.1688 0.0124  0.0037  0.0055  198 GLY A O     
1559 N  N     . CYS A 207 ? 0.1476 0.1049 0.1684 -0.0015 -0.0079 0.0005  199 CYS A N     
1560 C  CA    . CYS A 207 ? 0.1496 0.1207 0.1701 0.0049  -0.0052 0.0161  199 CYS A CA    
1561 C  C     . CYS A 207 ? 0.1491 0.1238 0.1674 -0.0049 -0.0019 0.0107  199 CYS A C     
1562 O  O     . CYS A 207 ? 0.1500 0.1259 0.1705 -0.0053 -0.0044 0.0146  199 CYS A O     
1563 C  CB    . CYS A 207 ? 0.1404 0.1294 0.1771 -0.0081 0.0023  0.0141  199 CYS A CB    
1564 S  SG    . CYS A 207 ? 0.1779 0.1572 0.1955 -0.0111 0.0247  0.0146  199 CYS A SG    
1565 N  N     . ILE A 208 ? 0.1607 0.1238 0.1617 -0.0008 -0.0073 0.0168  200 ILE A N     
1566 C  CA    . ILE A 208 ? 0.1660 0.1343 0.1606 0.0021  -0.0116 0.0189  200 ILE A CA    
1567 C  C     . ILE A 208 ? 0.1619 0.1328 0.1684 -0.0080 -0.0121 0.0206  200 ILE A C     
1568 O  O     . ILE A 208 ? 0.1932 0.1445 0.1729 -0.0020 -0.0089 0.0244  200 ILE A O     
1569 C  CB    . ILE A 208 ? 0.1661 0.1541 0.1676 0.0226  -0.0087 0.0331  200 ILE A CB    
1570 C  CG1   . ILE A 208 ? 0.1509 0.1956 0.1721 0.0143  -0.0036 0.0262  200 ILE A CG1   
1571 C  CG2   . ILE A 208 ? 0.1695 0.1673 0.1762 0.0227  -0.0036 0.0148  200 ILE A CG2   
1572 C  CD1   . ILE A 208 ? 0.1405 0.2374 0.1800 0.0085  -0.0095 0.0121  200 ILE A CD1   
1573 N  N     . CYS A 209 ? 0.1778 0.1446 0.1797 -0.0119 -0.0160 0.0308  201 CYS A N     
1574 C  CA    A CYS A 209 ? 0.1845 0.1688 0.1860 -0.0132 -0.0002 0.0493  201 CYS A CA    
1575 C  CA    B CYS A 209 ? 0.1934 0.1561 0.1922 -0.0071 -0.0035 0.0369  201 CYS A CA    
1576 C  C     . CYS A 209 ? 0.2235 0.1694 0.1943 -0.0129 0.0006  0.0384  201 CYS A C     
1577 O  O     . CYS A 209 ? 0.3097 0.1919 0.2079 -0.0255 -0.0186 0.0241  201 CYS A O     
1578 C  CB    A CYS A 209 ? 0.1794 0.2432 0.1963 0.0050  -0.0004 0.0605  201 CYS A CB    
1579 C  CB    B CYS A 209 ? 0.1947 0.1794 0.2075 0.0169  0.0000  0.0350  201 CYS A CB    
1580 S  SG    A CYS A 209 ? 0.1714 0.2923 0.2043 -0.0216 0.0018  0.0563  201 CYS A SG    
1581 S  SG    B CYS A 209 ? 0.1830 0.1756 0.2199 0.0021  0.0112  0.0404  201 CYS A SG    
1582 N  N     . THR A 210 ? 0.2203 0.1890 0.1964 -0.0060 0.0046  0.0442  202 THR A N     
1583 C  CA    A THR A 210 ? 0.2182 0.2200 0.2011 0.0124  0.0126  0.0507  202 THR A CA    
1584 C  CA    B THR A 210 ? 0.2223 0.2246 0.1996 0.0199  0.0058  0.0483  202 THR A CA    
1585 C  C     . THR A 210 ? 0.2031 0.2100 0.1993 0.0123  0.0053  0.0540  202 THR A C     
1586 O  O     . THR A 210 ? 0.1900 0.1846 0.2040 -0.0013 0.0013  0.0599  202 THR A O     
1587 C  CB    A THR A 210 ? 0.2593 0.2707 0.2117 0.0594  0.0379  0.0649  202 THR A CB    
1588 C  CB    B THR A 210 ? 0.2621 0.2840 0.2057 0.0723  0.0143  0.0541  202 THR A CB    
1589 O  OG1   A THR A 210 ? 0.3035 0.2640 0.2202 0.1174  0.0396  0.0757  202 THR A OG1   
1590 O  OG1   B THR A 210 ? 0.2799 0.3267 0.2095 0.1065  0.0116  0.0513  202 THR A OG1   
1591 C  CG2   A THR A 210 ? 0.2493 0.3016 0.2159 0.0495  0.0498  0.0639  202 THR A CG2   
1592 C  CG2   B THR A 210 ? 0.2802 0.2889 0.2089 0.0894  0.0191  0.0617  202 THR A CG2   
1593 N  N     . VAL A 211 ? 0.1846 0.1967 0.1963 0.0030  0.0130  0.0649  203 VAL A N     
1594 C  CA    . VAL A 211 ? 0.1940 0.2087 0.1962 0.0105  0.0102  0.0768  203 VAL A CA    
1595 C  C     . VAL A 211 ? 0.2000 0.2154 0.2108 0.0293  -0.0001 0.0788  203 VAL A C     
1596 O  O     . VAL A 211 ? 0.2015 0.2418 0.2191 0.0254  -0.0236 0.0878  203 VAL A O     
1597 C  CB    . VAL A 211 ? 0.1972 0.2105 0.1876 0.0039  -0.0009 0.0662  203 VAL A CB    
1598 C  CG1   . VAL A 211 ? 0.2124 0.2252 0.1885 0.0139  0.0097  0.0612  203 VAL A CG1   
1599 C  CG2   . VAL A 211 ? 0.2116 0.2149 0.1868 0.0074  -0.0193 0.0630  203 VAL A CG2   
1600 N  N     . SER A 212 ? 0.2074 0.2057 0.2201 0.0156  0.0204  0.0817  204 SER A N     
1601 C  CA    . SER A 212 ? 0.2587 0.2203 0.2304 0.0185  0.0366  0.0943  204 SER A CA    
1602 C  C     . SER A 212 ? 0.2481 0.2413 0.2284 0.0201  0.0212  0.1008  204 SER A C     
1603 O  O     . SER A 212 ? 0.2479 0.2640 0.2399 0.0141  0.0179  0.1035  204 SER A O     
1604 C  CB    . SER A 212 ? 0.3431 0.2369 0.2511 0.0051  0.0850  0.0810  204 SER A CB    
1605 O  OG    . SER A 212 ? 0.3945 0.2769 0.2734 0.0364  0.0945  0.0628  204 SER A OG    
1606 N  N     . ASP A 213 ? 0.2392 0.2439 0.2143 0.0241  0.0219  0.0967  205 ASP A N     
1607 C  CA    . ASP A 213 ? 0.2304 0.2491 0.2102 -0.0093 0.0110  0.0703  205 ASP A CA    
1608 C  C     . ASP A 213 ? 0.2200 0.2385 0.1837 -0.0023 -0.0074 0.0647  205 ASP A C     
1609 O  O     . ASP A 213 ? 0.2353 0.2379 0.1691 0.0079  -0.0173 0.0570  205 ASP A O     
1610 C  CB    . ASP A 213 ? 0.2618 0.2779 0.2408 -0.0306 0.0132  0.0650  205 ASP A CB    
1611 C  CG    . ASP A 213 ? 0.3152 0.2983 0.2635 -0.0288 0.0172  0.0699  205 ASP A CG    
1612 O  OD1   . ASP A 213 ? 0.3144 0.3018 0.2705 -0.0191 0.0015  0.0870  205 ASP A OD1   
1613 O  OD2   . ASP A 213 ? 0.3639 0.3018 0.2804 -0.0130 0.0247  0.0559  205 ASP A OD2   
1614 N  N     . HIS A 214 ? 0.2176 0.2554 0.1799 0.0092  -0.0139 0.0446  206 HIS A N     
1615 C  CA    . HIS A 214 ? 0.2203 0.2764 0.1729 0.0083  -0.0079 0.0479  206 HIS A CA    
1616 C  C     . HIS A 214 ? 0.2166 0.2796 0.1728 0.0128  -0.0024 0.0526  206 HIS A C     
1617 O  O     . HIS A 214 ? 0.2286 0.3073 0.1765 0.0247  0.0176  0.0628  206 HIS A O     
1618 C  CB    . HIS A 214 ? 0.2353 0.2887 0.1721 0.0215  -0.0084 0.0452  206 HIS A CB    
1619 C  CG    . HIS A 214 ? 0.2363 0.2795 0.1715 0.0182  -0.0070 0.0358  206 HIS A CG    
1620 N  ND1   . HIS A 214 ? 0.2556 0.2850 0.1738 0.0327  0.0023  0.0458  206 HIS A ND1   
1621 C  CD2   . HIS A 214 ? 0.2470 0.2929 0.1722 0.0217  -0.0044 0.0286  206 HIS A CD2   
1622 C  CE1   . HIS A 214 ? 0.2697 0.2959 0.1776 0.0382  -0.0027 0.0272  206 HIS A CE1   
1623 N  NE2   . HIS A 214 ? 0.2707 0.2996 0.1742 0.0277  -0.0048 0.0259  206 HIS A NE2   
1624 N  N     . ILE A 215 ? 0.2190 0.2693 0.1787 0.0212  0.0001  0.0423  207 ILE A N     
1625 C  CA    . ILE A 215 ? 0.2347 0.3008 0.1886 0.0170  0.0114  0.0231  207 ILE A CA    
1626 C  C     . ILE A 215 ? 0.2570 0.3440 0.1966 0.0149  0.0291  0.0266  207 ILE A C     
1627 O  O     . ILE A 215 ? 0.2703 0.3642 0.2028 0.0094  0.0382  0.0365  207 ILE A O     
1628 C  CB    . ILE A 215 ? 0.2371 0.3102 0.1919 0.0341  0.0051  0.0096  207 ILE A CB    
1629 C  CG1   . ILE A 215 ? 0.2542 0.2935 0.1915 0.0449  -0.0089 0.0019  207 ILE A CG1   
1630 C  CG2   . ILE A 215 ? 0.2317 0.3283 0.2002 0.0300  -0.0036 -0.0012 207 ILE A CG2   
1631 C  CD1   . ILE A 215 ? 0.2643 0.3098 0.1904 0.0648  -0.0174 0.0005  207 ILE A CD1   
1632 N  N     . ILE A 216 ? 0.2818 0.3817 0.1928 0.0270  0.0321  0.0147  208 ILE A N     
1633 C  CA    . ILE A 216 ? 0.3055 0.4158 0.1946 0.0358  0.0300  0.0141  208 ILE A CA    
1634 C  C     . ILE A 216 ? 0.3158 0.4451 0.1956 0.0413  0.0297  0.0338  208 ILE A C     
1635 O  O     . ILE A 216 ? 0.3351 0.4685 0.2007 0.0653  0.0338  0.0291  208 ILE A O     
1636 C  CB    . ILE A 216 ? 0.3288 0.4111 0.1976 0.0469  0.0250  -0.0104 208 ILE A CB    
1637 C  CG1   . ILE A 216 ? 0.3366 0.4016 0.2004 0.0593  0.0184  -0.0187 208 ILE A CG1   
1638 C  CG2   . ILE A 216 ? 0.3486 0.4230 0.2053 0.0601  0.0218  -0.0159 208 ILE A CG2   
1639 C  CD1   . ILE A 216 ? 0.3317 0.3964 0.1991 0.0618  0.0141  -0.0262 208 ILE A CD1   
1640 N  N     . THR A 217 ? 0.3123 0.4653 0.1953 0.0387  0.0257  0.0482  209 THR A N     
1641 C  CA    . THR A 217 ? 0.3212 0.4972 0.2069 0.0434  0.0204  0.0573  209 THR A CA    
1642 C  C     . THR A 217 ? 0.3222 0.5055 0.2209 0.0410  0.0224  0.0784  209 THR A C     
1643 O  O     . THR A 217 ? 0.3402 0.5311 0.2169 0.0485  0.0149  0.0727  209 THR A O     
1644 C  CB    . THR A 217 ? 0.3323 0.5132 0.2045 0.0550  0.0152  0.0551  209 THR A CB    
1645 O  OG1   . THR A 217 ? 0.3264 0.5188 0.1956 0.0506  0.0174  0.0628  209 THR A OG1   
1646 C  CG2   . THR A 217 ? 0.3454 0.5280 0.2105 0.0738  0.0115  0.0479  209 THR A CG2   
1647 N  N     . HIS A 218 ? 0.3033 0.4890 0.2362 0.0170  0.0375  0.0942  210 HIS A N     
1648 C  CA    . HIS A 218 ? 0.3094 0.4824 0.2601 0.0140  0.0568  0.1157  210 HIS A CA    
1649 C  C     . HIS A 218 ? 0.3024 0.4587 0.2598 0.0075  0.0523  0.1295  210 HIS A C     
1650 O  O     . HIS A 218 ? 0.3020 0.4728 0.2584 -0.0099 0.0532  0.1233  210 HIS A O     
1651 C  CB    . HIS A 218 ? 0.3341 0.5201 0.2837 0.0350  0.0724  0.1132  210 HIS A CB    
1652 C  CG    . HIS A 218 ? 0.3620 0.5553 0.3134 0.0549  0.0720  0.0973  210 HIS A CG    
1653 N  ND1   . HIS A 218 ? 0.3662 0.5686 0.3288 0.0629  0.0719  0.0852  210 HIS A ND1   
1654 C  CD2   . HIS A 218 ? 0.3678 0.5680 0.3268 0.0655  0.0732  0.0869  210 HIS A CD2   
1655 C  CE1   . HIS A 218 ? 0.3717 0.5718 0.3308 0.0679  0.0759  0.0859  210 HIS A CE1   
1656 N  NE2   . HIS A 218 ? 0.3815 0.5754 0.3342 0.0782  0.0717  0.0831  210 HIS A NE2   
1657 N  N     . GLU A 219 ? 0.2930 0.4292 0.2627 0.0139  0.0464  0.1418  211 GLU A N     
1658 C  CA    . GLU A 219 ? 0.2945 0.4174 0.2773 0.0180  0.0338  0.1446  211 GLU A CA    
1659 C  C     . GLU A 219 ? 0.2938 0.3877 0.2753 0.0305  0.0324  0.1575  211 GLU A C     
1660 O  O     . GLU A 219 ? 0.2911 0.3527 0.2671 0.0267  0.0330  0.1697  211 GLU A O     
1661 C  CB    . GLU A 219 ? 0.3190 0.4593 0.2980 0.0248  0.0177  0.1170  211 GLU A CB    
1662 C  CG    . GLU A 219 ? 0.3447 0.5080 0.3199 0.0297  0.0033  0.0933  211 GLU A CG    
1663 C  CD    . GLU A 219 ? 0.3722 0.5521 0.3406 0.0248  -0.0087 0.0684  211 GLU A CD    
1664 O  OE1   . GLU A 219 ? 0.3851 0.5645 0.3517 0.0220  -0.0097 0.0521  211 GLU A OE1   
1665 O  OE2   . GLU A 219 ? 0.3930 0.5883 0.3509 0.0380  -0.0100 0.0591  211 GLU A OE2   
1666 N  N     . SER A 220 ? 0.3103 0.3937 0.2813 0.0463  0.0378  0.1659  212 SER A N     
1667 C  CA    . SER A 220 ? 0.3090 0.3890 0.2865 0.0530  0.0477  0.1708  212 SER A CA    
1668 C  C     . SER A 220 ? 0.3002 0.3988 0.2864 0.0669  0.0422  0.1733  212 SER A C     
1669 O  O     . SER A 220 ? 0.3173 0.4469 0.2837 0.0919  0.0326  0.1660  212 SER A O     
1670 C  CB    . SER A 220 ? 0.3287 0.3962 0.2957 0.0381  0.0690  0.1640  212 SER A CB    
1671 O  OG    . SER A 220 ? 0.3507 0.3906 0.3078 0.0360  0.0821  0.1555  212 SER A OG    
1672 N  N     . ALA A 221 ? 0.2787 0.3668 0.2893 0.0457  0.0501  0.1761  213 ALA A N     
1673 C  CA    . ALA A 221 ? 0.2860 0.3517 0.2935 0.0423  0.0535  0.1765  213 ALA A CA    
1674 C  C     . ALA A 221 ? 0.2890 0.3340 0.2967 0.0370  0.0382  0.1802  213 ALA A C     
1675 O  O     . ALA A 221 ? 0.2940 0.3377 0.2991 0.0470  0.0295  0.1768  213 ALA A O     
1676 C  CB    . ALA A 221 ? 0.2923 0.3688 0.2952 0.0517  0.0583  0.1702  213 ALA A CB    
1677 N  N     . THR A 222 ? 0.2845 0.3183 0.2966 0.0285  0.0293  0.1818  214 THR A N     
1678 C  CA    . THR A 222 ? 0.2808 0.3072 0.3065 0.0216  0.0180  0.1784  214 THR A CA    
1679 C  C     . THR A 222 ? 0.2756 0.2930 0.3107 -0.0007 0.0148  0.1802  214 THR A C     
1680 O  O     . THR A 222 ? 0.2664 0.2796 0.3044 0.0198  0.0041  0.1738  214 THR A O     
1681 C  CB    . THR A 222 ? 0.2824 0.3096 0.3086 0.0303  0.0151  0.1707  214 THR A CB    
1682 O  OG1   . THR A 222 ? 0.2807 0.3071 0.3104 0.0245  0.0108  0.1694  214 THR A OG1   
1683 C  CG2   . THR A 222 ? 0.3073 0.3211 0.3132 0.0555  0.0177  0.1620  214 THR A CG2   
1684 N  N     . PRO A 223 ? 0.2917 0.3005 0.3210 -0.0009 0.0132  0.1707  215 PRO A N     
1685 C  CA    . PRO A 223 ? 0.2919 0.2846 0.3246 -0.0157 0.0226  0.1687  215 PRO A CA    
1686 C  C     . PRO A 223 ? 0.2947 0.2781 0.3198 0.0089  0.0203  0.1677  215 PRO A C     
1687 O  O     . PRO A 223 ? 0.3146 0.2783 0.3219 0.0184  0.0194  0.1549  215 PRO A O     
1688 C  CB    . PRO A 223 ? 0.3082 0.2950 0.3312 -0.0168 0.0261  0.1622  215 PRO A CB    
1689 C  CG    . PRO A 223 ? 0.3132 0.3016 0.3331 -0.0185 0.0242  0.1611  215 PRO A CG    
1690 C  CD    . PRO A 223 ? 0.3041 0.2946 0.3292 -0.0204 0.0185  0.1612  215 PRO A CD    
1691 N  N     . GLU A 224 ? 0.2995 0.2823 0.3182 0.0244  0.0223  0.1689  216 GLU A N     
1692 C  CA    . GLU A 224 ? 0.3025 0.2903 0.3125 0.0303  0.0106  0.1705  216 GLU A CA    
1693 C  C     . GLU A 224 ? 0.2913 0.2836 0.2956 0.0253  0.0151  0.1662  216 GLU A C     
1694 O  O     . GLU A 224 ? 0.3017 0.2886 0.2935 0.0376  0.0296  0.1679  216 GLU A O     
1695 C  CB    . GLU A 224 ? 0.3244 0.3112 0.3213 0.0373  0.0060  0.1819  216 GLU A CB    
1696 C  CG    . GLU A 224 ? 0.3638 0.3369 0.3378 0.0471  0.0098  0.1792  216 GLU A CG    
1697 C  CD    . GLU A 224 ? 0.3781 0.3350 0.3468 0.0580  0.0106  0.1811  216 GLU A CD    
1698 O  OE1   . GLU A 224 ? 0.3933 0.3056 0.3467 0.0403  0.0191  0.1827  216 GLU A OE1   
1699 O  OE2   . GLU A 224 ? 0.3658 0.3359 0.3463 0.0373  0.0125  0.1962  216 GLU A OE2   
1700 N  N     . GLU A 225 ? 0.2667 0.2681 0.2851 0.0090  0.0081  0.1579  217 GLU A N     
1701 C  CA    . GLU A 225 ? 0.2685 0.2722 0.2841 0.0048  0.0066  0.1626  217 GLU A CA    
1702 C  C     . GLU A 225 ? 0.2632 0.2542 0.2900 0.0056  0.0112  0.1601  217 GLU A C     
1703 O  O     . GLU A 225 ? 0.2655 0.2564 0.2908 0.0190  0.0203  0.1532  217 GLU A O     
1704 C  CB    . GLU A 225 ? 0.2814 0.2890 0.2813 0.0006  0.0018  0.1527  217 GLU A CB    
1705 C  CG    . GLU A 225 ? 0.3058 0.3103 0.2784 0.0014  -0.0093 0.1332  217 GLU A CG    
1706 C  CD    . GLU A 225 ? 0.3389 0.3580 0.2792 0.0101  -0.0166 0.1131  217 GLU A CD    
1707 O  OE1   . GLU A 225 ? 0.3548 0.3619 0.2754 0.0325  -0.0094 0.1223  217 GLU A OE1   
1708 O  OE2   . GLU A 225 ? 0.3586 0.4035 0.2853 0.0131  -0.0252 0.0755  217 GLU A OE2   
1709 N  N     . ARG A 226 ? 0.2769 0.2625 0.2972 0.0225  0.0019  0.1479  218 ARG A N     
1710 C  CA    . ARG A 226 ? 0.2808 0.2720 0.3043 0.0313  0.0001  0.1542  218 ARG A CA    
1711 C  C     . ARG A 226 ? 0.2912 0.2699 0.3012 0.0277  0.0168  0.1571  218 ARG A C     
1712 O  O     . ARG A 226 ? 0.2763 0.2821 0.2892 0.0373  0.0166  0.1638  218 ARG A O     
1713 C  CB    . ARG A 226 ? 0.2787 0.3163 0.3182 0.0262  -0.0058 0.1513  218 ARG A CB    
1714 C  CG    . ARG A 226 ? 0.2833 0.3441 0.3379 0.0115  0.0035  0.1486  218 ARG A CG    
1715 C  CD    . ARG A 226 ? 0.2934 0.3762 0.3572 0.0021  0.0150  0.1380  218 ARG A CD    
1716 N  NE    . ARG A 226 ? 0.3026 0.3793 0.3712 -0.0090 0.0194  0.1381  218 ARG A NE    
1717 C  CZ    . ARG A 226 ? 0.3103 0.3519 0.3826 -0.0246 0.0269  0.1507  218 ARG A CZ    
1718 N  NH1   . ARG A 226 ? 0.3075 0.3371 0.3888 -0.0152 0.0157  0.1409  218 ARG A NH1   
1719 N  NH2   . ARG A 226 ? 0.3277 0.3568 0.3842 -0.0285 0.0368  0.1677  218 ARG A NH2   
1720 N  N     . GLN A 227 ? 0.3210 0.2693 0.3103 0.0398  0.0313  0.1532  219 GLN A N     
1721 C  CA    . GLN A 227 ? 0.3488 0.2669 0.3201 0.0677  0.0480  0.1523  219 GLN A CA    
1722 C  C     . GLN A 227 ? 0.3248 0.2626 0.3068 0.0794  0.0544  0.1474  219 GLN A C     
1723 O  O     . GLN A 227 ? 0.3332 0.2468 0.3114 0.0893  0.0651  0.1351  219 GLN A O     
1724 C  CB    . GLN A 227 ? 0.4047 0.3137 0.3466 0.0922  0.0520  0.1459  219 GLN A CB    
1725 C  CG    . GLN A 227 ? 0.4598 0.3992 0.3716 0.1210  0.0518  0.1235  219 GLN A CG    
1726 C  CD    . GLN A 227 ? 0.5042 0.4841 0.3978 0.1441  0.0539  0.0995  219 GLN A CD    
1727 O  OE1   . GLN A 227 ? 0.5362 0.5229 0.4101 0.1510  0.0555  0.0892  219 GLN A OE1   
1728 N  NE2   . GLN A 227 ? 0.5177 0.5028 0.4039 0.1493  0.0572  0.0922  219 GLN A NE2   
1729 N  N     . THR A 228 ? 0.2887 0.2702 0.2870 0.0636  0.0347  0.1450  220 THR A N     
1730 C  CA    . THR A 228 ? 0.2883 0.2933 0.2741 0.0586  0.0168  0.1297  220 THR A CA    
1731 C  C     . THR A 228 ? 0.2529 0.2750 0.2521 0.0562  0.0116  0.1173  220 THR A C     
1732 O  O     . THR A 228 ? 0.2311 0.2806 0.2373 0.0399  0.0070  0.1029  220 THR A O     
1733 C  CB    . THR A 228 ? 0.3232 0.3321 0.2830 0.0554  0.0042  0.1391  220 THR A CB    
1734 O  OG1   . THR A 228 ? 0.3518 0.3683 0.2961 0.0785  0.0107  0.1400  220 THR A OG1   
1735 C  CG2   . THR A 228 ? 0.3328 0.3537 0.2882 0.0328  0.0015  0.1241  220 THR A CG2   
1736 N  N     . SER A 229 ? 0.2485 0.2561 0.2438 0.0517  0.0168  0.1155  221 SER A N     
1737 C  CA    . SER A 229 ? 0.2751 0.2639 0.2414 0.0746  0.0247  0.1058  221 SER A CA    
1738 C  C     . SER A 229 ? 0.2411 0.2481 0.2338 0.0518  0.0241  0.1056  221 SER A C     
1739 O  O     . SER A 229 ? 0.2125 0.2436 0.2229 0.0414  0.0333  0.1015  221 SER A O     
1740 C  CB    . SER A 229 ? 0.3536 0.3095 0.2523 0.1326  0.0329  0.0958  221 SER A CB    
1741 O  OG    . SER A 229 ? 0.4238 0.3441 0.2746 0.1279  0.0319  0.0796  221 SER A OG    
1742 N  N     . PHE A 230 ? 0.2574 0.2336 0.2429 0.0124  0.0057  0.1027  222 PHE A N     
1743 C  CA    A PHE A 230 ? 0.2810 0.2285 0.2523 0.0015  0.0023  0.0929  222 PHE A CA    
1744 C  CA    B PHE A 230 ? 0.2801 0.2388 0.2513 -0.0090 0.0072  0.0937  222 PHE A CA    
1745 C  C     . PHE A 230 ? 0.2885 0.2424 0.2537 0.0062  0.0075  0.0976  222 PHE A C     
1746 O  O     . PHE A 230 ? 0.2982 0.2265 0.2472 -0.0109 0.0084  0.0989  222 PHE A O     
1747 C  CB    A PHE A 230 ? 0.3014 0.2269 0.2602 -0.0076 -0.0062 0.0741  222 PHE A CB    
1748 C  CB    B PHE A 230 ? 0.2988 0.2589 0.2574 -0.0381 0.0092  0.0770  222 PHE A CB    
1749 C  CG    A PHE A 230 ? 0.3075 0.2122 0.2664 -0.0027 -0.0198 0.0506  222 PHE A CG    
1750 C  CG    B PHE A 230 ? 0.3102 0.2723 0.2634 -0.0446 0.0047  0.0529  222 PHE A CG    
1751 C  CD1   A PHE A 230 ? 0.3207 0.2201 0.2726 -0.0006 -0.0265 0.0386  222 PHE A CD1   
1752 C  CD1   B PHE A 230 ? 0.3163 0.2856 0.2669 -0.0505 0.0038  0.0397  222 PHE A CD1   
1753 C  CD2   A PHE A 230 ? 0.3211 0.2278 0.2688 0.0078  -0.0274 0.0373  222 PHE A CD2   
1754 C  CD2   B PHE A 230 ? 0.3209 0.2970 0.2655 -0.0396 0.0039  0.0416  222 PHE A CD2   
1755 C  CE1   A PHE A 230 ? 0.3376 0.2340 0.2751 0.0105  -0.0254 0.0269  222 PHE A CE1   
1756 C  CE1   B PHE A 230 ? 0.3202 0.2962 0.2687 -0.0469 0.0004  0.0306  222 PHE A CE1   
1757 C  CE2   A PHE A 230 ? 0.3360 0.2352 0.2735 0.0199  -0.0238 0.0254  222 PHE A CE2   
1758 C  CE2   B PHE A 230 ? 0.3185 0.2978 0.2670 -0.0431 0.0019  0.0329  222 PHE A CE2   
1759 C  CZ    A PHE A 230 ? 0.3375 0.2240 0.2749 0.0059  -0.0256 0.0261  222 PHE A CZ    
1760 C  CZ    B PHE A 230 ? 0.3204 0.2937 0.2682 -0.0438 0.0009  0.0328  222 PHE A CZ    
1761 N  N     . GLN A 231 ? 0.2998 0.2433 0.2616 0.0390  0.0125  0.1032  223 GLN A N     
1762 C  CA    . GLN A 231 ? 0.3237 0.2693 0.2726 0.0707  0.0208  0.0957  223 GLN A CA    
1763 C  C     . GLN A 231 ? 0.2830 0.2626 0.2546 0.0504  0.0284  0.0948  223 GLN A C     
1764 O  O     . GLN A 231 ? 0.3026 0.2607 0.2574 0.0706  0.0481  0.0875  223 GLN A O     
1765 C  CB    . GLN A 231 ? 0.3864 0.2931 0.2995 0.0944  0.0120  0.0994  223 GLN A CB    
1766 C  CG    . GLN A 231 ? 0.4349 0.3018 0.3257 0.0970  0.0018  0.0986  223 GLN A CG    
1767 C  CD    . GLN A 231 ? 0.4905 0.3319 0.3496 0.1133  -0.0052 0.0981  223 GLN A CD    
1768 O  OE1   . GLN A 231 ? 0.5295 0.3872 0.3662 0.1239  0.0006  0.0913  223 GLN A OE1   
1769 N  NE2   . GLN A 231 ? 0.5061 0.3365 0.3567 0.1140  -0.0132 0.0920  223 GLN A NE2   
1770 N  N     . ASN A 232 ? 0.2266 0.2722 0.2383 0.0264  0.0043  0.0817  224 ASN A N     
1771 C  CA    . ASN A 232 ? 0.2062 0.2904 0.2372 -0.0117 0.0057  0.0622  224 ASN A CA    
1772 C  C     . ASN A 232 ? 0.1758 0.2260 0.2245 -0.0087 0.0165  0.0657  224 ASN A C     
1773 O  O     . ASN A 232 ? 0.1762 0.2270 0.2183 -0.0016 0.0112  0.0633  224 ASN A O     
1774 C  CB    . ASN A 232 ? 0.2604 0.3680 0.2502 -0.0043 -0.0007 0.0606  224 ASN A CB    
1775 C  CG    . ASN A 232 ? 0.3339 0.4567 0.2624 0.0310  -0.0146 0.0483  224 ASN A CG    
1776 O  OD1   . ASN A 232 ? 0.3564 0.5183 0.2708 0.0666  -0.0434 0.0341  224 ASN A OD1   
1777 N  ND2   . ASN A 232 ? 0.3719 0.4776 0.2702 0.0312  -0.0194 0.0413  224 ASN A ND2   
1778 N  N     . MET A 233 ? 0.1797 0.2062 0.2243 -0.0015 0.0135  0.0516  225 MET A N     
1779 C  CA    A MET A 233 ? 0.1748 0.1930 0.2305 -0.0022 0.0170  0.0467  225 MET A CA    
1780 C  CA    B MET A 233 ? 0.1902 0.1958 0.2288 0.0014  0.0108  0.0482  225 MET A CA    
1781 C  C     . MET A 233 ? 0.1697 0.1880 0.2207 -0.0031 0.0202  0.0503  225 MET A C     
1782 O  O     . MET A 233 ? 0.1541 0.1927 0.2092 -0.0084 0.0201  0.0450  225 MET A O     
1783 C  CB    A MET A 233 ? 0.1683 0.1890 0.2471 -0.0071 0.0187  0.0442  225 MET A CB    
1784 C  CB    B MET A 233 ? 0.2162 0.1961 0.2421 0.0038  -0.0011 0.0461  225 MET A CB    
1785 C  CG    A MET A 233 ? 0.1571 0.1916 0.2636 0.0014  0.0099  0.0505  225 MET A CG    
1786 C  CG    B MET A 233 ? 0.2354 0.2021 0.2558 0.0107  -0.0157 0.0492  225 MET A CG    
1787 S  SD    A MET A 233 ? 0.1554 0.2331 0.2792 0.0353  -0.0006 0.0570  225 MET A SD    
1788 S  SD    B MET A 233 ? 0.2371 0.1915 0.2660 0.0007  -0.0261 0.0511  225 MET A SD    
1789 C  CE    A MET A 233 ? 0.1750 0.2307 0.2907 0.0144  -0.0174 0.0562  225 MET A CE    
1790 C  CE    B MET A 233 ? 0.2390 0.2176 0.2706 -0.0085 -0.0323 0.0576  225 MET A CE    
1791 N  N     . ILE A 234 ? 0.1666 0.1753 0.2210 0.0035  0.0109  0.0389  226 ILE A N     
1792 C  CA    . ILE A 234 ? 0.1765 0.1614 0.2308 0.0024  0.0069  0.0449  226 ILE A CA    
1793 C  C     . ILE A 234 ? 0.1662 0.1550 0.2295 -0.0001 0.0017  0.0564  226 ILE A C     
1794 O  O     . ILE A 234 ? 0.1793 0.1514 0.2266 -0.0139 0.0079  0.0576  226 ILE A O     
1795 C  CB    . ILE A 234 ? 0.2083 0.1634 0.2461 -0.0292 0.0016  0.0329  226 ILE A CB    
1796 C  CG1   . ILE A 234 ? 0.2573 0.2060 0.2599 -0.0362 -0.0079 0.0220  226 ILE A CG1   
1797 C  CG2   . ILE A 234 ? 0.2528 0.1833 0.2544 0.0136  0.0108  0.0389  226 ILE A CG2   
1798 C  CD1   . ILE A 234 ? 0.2974 0.2382 0.2681 -0.0047 -0.0338 0.0181  226 ILE A CD1   
1799 N  N     . LYS A 235 ? 0.1666 0.1715 0.2297 0.0093  0.0052  0.0536  227 LYS A N     
1800 C  CA    . LYS A 235 ? 0.1537 0.1826 0.2343 0.0041  0.0025  0.0342  227 LYS A CA    
1801 C  C     . LYS A 235 ? 0.1471 0.1790 0.2290 0.0127  0.0022  0.0300  227 LYS A C     
1802 O  O     . LYS A 235 ? 0.1382 0.1649 0.2314 0.0180  0.0012  0.0233  227 LYS A O     
1803 C  CB    . LYS A 235 ? 0.1625 0.2192 0.2447 0.0232  0.0035  0.0392  227 LYS A CB    
1804 C  CG    . LYS A 235 ? 0.1868 0.2571 0.2599 0.0155  0.0209  0.0407  227 LYS A CG    
1805 C  CD    . LYS A 235 ? 0.1878 0.3056 0.2743 0.0111  0.0247  0.0361  227 LYS A CD    
1806 C  CE    . LYS A 235 ? 0.2080 0.3303 0.2880 0.0179  0.0202  0.0209  227 LYS A CE    
1807 N  NZ    . LYS A 235 ? 0.2320 0.3470 0.2968 0.0333  0.0054  0.0091  227 LYS A NZ    
1808 N  N     . ILE A 236 ? 0.1406 0.1785 0.2174 0.0102  -0.0104 0.0198  228 ILE A N     
1809 C  CA    . ILE A 236 ? 0.1375 0.1681 0.2135 0.0016  0.0027  0.0157  228 ILE A CA    
1810 C  C     . ILE A 236 ? 0.1288 0.1577 0.2041 -0.0040 0.0121  0.0274  228 ILE A C     
1811 O  O     . ILE A 236 ? 0.1457 0.1608 0.2004 -0.0028 0.0097  0.0285  228 ILE A O     
1812 C  CB    . ILE A 236 ? 0.1567 0.1703 0.2185 -0.0008 0.0046  0.0172  228 ILE A CB    
1813 C  CG1   . ILE A 236 ? 0.1558 0.1811 0.2278 0.0036  -0.0064 0.0185  228 ILE A CG1   
1814 C  CG2   . ILE A 236 ? 0.1539 0.1624 0.2150 -0.0025 0.0159  0.0014  228 ILE A CG2   
1815 C  CD1   . ILE A 236 ? 0.1582 0.1987 0.2368 0.0203  -0.0141 0.0112  228 ILE A CD1   
1816 N  N     . ALA A 237 ? 0.1219 0.1479 0.2076 0.0110  0.0093  0.0381  229 ALA A N     
1817 C  CA    . ALA A 237 ? 0.1339 0.1611 0.2120 0.0153  -0.0007 0.0300  229 ALA A CA    
1818 C  C     . ALA A 237 ? 0.1441 0.1403 0.2124 0.0017  0.0048  0.0281  229 ALA A C     
1819 O  O     . ALA A 237 ? 0.1457 0.1521 0.2048 0.0080  0.0010  0.0284  229 ALA A O     
1820 C  CB    . ALA A 237 ? 0.1293 0.1759 0.2190 0.0002  -0.0029 0.0347  229 ALA A CB    
1821 N  N     . LEU A 238 ? 0.1414 0.1252 0.2193 0.0168  0.0197  0.0234  230 LEU A N     
1822 C  CA    . LEU A 238 ? 0.1460 0.1314 0.2277 0.0155  0.0171  0.0185  230 LEU A CA    
1823 C  C     . LEU A 238 ? 0.1400 0.1336 0.2220 0.0013  0.0188  0.0239  230 LEU A C     
1824 O  O     . LEU A 238 ? 0.1529 0.1397 0.2238 0.0171  0.0249  0.0248  230 LEU A O     
1825 C  CB    . LEU A 238 ? 0.1469 0.1457 0.2401 0.0083  0.0151  0.0180  230 LEU A CB    
1826 C  CG    . LEU A 238 ? 0.1457 0.1511 0.2499 -0.0027 0.0181  0.0166  230 LEU A CG    
1827 C  CD1   . LEU A 238 ? 0.1722 0.1423 0.2591 0.0080  0.0070  0.0235  230 LEU A CD1   
1828 C  CD2   . LEU A 238 ? 0.1431 0.1784 0.2538 -0.0033 0.0222  0.0069  230 LEU A CD2   
1829 N  N     . GLU A 239 ? 0.1394 0.1435 0.2253 0.0136  0.0045  0.0145  231 GLU A N     
1830 C  CA    . GLU A 239 ? 0.1559 0.1444 0.2356 0.0129  0.0025  0.0092  231 GLU A CA    
1831 C  C     . GLU A 239 ? 0.1590 0.1437 0.2353 0.0174  0.0085  0.0106  231 GLU A C     
1832 O  O     . GLU A 239 ? 0.1674 0.1563 0.2451 -0.0133 0.0155  0.0152  231 GLU A O     
1833 C  CB    . GLU A 239 ? 0.1720 0.1632 0.2541 0.0295  -0.0020 0.0125  231 GLU A CB    
1834 C  CG    . GLU A 239 ? 0.1463 0.1744 0.2716 0.0048  -0.0034 -0.0048 231 GLU A CG    
1835 C  CD    . GLU A 239 ? 0.1541 0.1982 0.2948 0.0102  0.0050  -0.0085 231 GLU A CD    
1836 O  OE1   . GLU A 239 ? 0.1609 0.2316 0.3097 0.0066  0.0329  0.0259  231 GLU A OE1   
1837 O  OE2   . GLU A 239 ? 0.1543 0.2227 0.3046 0.0091  0.0050  -0.0310 231 GLU A OE2   
1838 N  N     . ALA A 240 ? 0.1538 0.1304 0.2308 0.0191  0.0057  0.0037  232 ALA A N     
1839 C  CA    . ALA A 240 ? 0.1509 0.1426 0.2274 0.0166  0.0156  0.0150  232 ALA A CA    
1840 C  C     . ALA A 240 ? 0.1445 0.1362 0.2176 0.0114  0.0248  0.0347  232 ALA A C     
1841 O  O     . ALA A 240 ? 0.1450 0.1563 0.2244 0.0136  0.0193  0.0428  232 ALA A O     
1842 C  CB    . ALA A 240 ? 0.1606 0.1530 0.2310 0.0121  0.0238  0.0237  232 ALA A CB    
1843 N  N     . THR A 241 ? 0.1559 0.1340 0.2155 0.0193  0.0245  0.0260  233 THR A N     
1844 C  CA    . THR A 241 ? 0.1596 0.1516 0.2200 0.0192  0.0203  0.0186  233 THR A CA    
1845 C  C     . THR A 241 ? 0.1433 0.1510 0.2285 0.0151  0.0238  0.0285  233 THR A C     
1846 O  O     . THR A 241 ? 0.1664 0.1793 0.2220 0.0292  0.0271  0.0273  233 THR A O     
1847 C  CB    . THR A 241 ? 0.1707 0.1637 0.2321 0.0123  0.0164  0.0109  233 THR A CB    
1848 O  OG1   . THR A 241 ? 0.1820 0.1497 0.2435 0.0125  0.0257  0.0091  233 THR A OG1   
1849 C  CG2   . THR A 241 ? 0.1785 0.1722 0.2339 -0.0072 0.0157  0.0096  233 THR A CG2   
1850 N  N     . LEU A 242 ? 0.1419 0.1496 0.2417 0.0244  0.0300  0.0295  234 LEU A N     
1851 C  CA    . LEU A 242 ? 0.1503 0.1644 0.2563 0.0027  0.0304  0.0307  234 LEU A CA    
1852 C  C     . LEU A 242 ? 0.1768 0.1798 0.2803 0.0108  0.0606  0.0576  234 LEU A C     
1853 O  O     . LEU A 242 ? 0.2029 0.1976 0.2847 0.0320  0.0843  0.0679  234 LEU A O     
1854 C  CB    . LEU A 242 ? 0.1484 0.1707 0.2605 0.0033  0.0267  0.0202  234 LEU A CB    
1855 C  CG    . LEU A 242 ? 0.1596 0.1903 0.2666 0.0206  0.0140  0.0147  234 LEU A CG    
1856 C  CD1   . LEU A 242 ? 0.1584 0.2458 0.2754 0.0196  0.0133  0.0182  234 LEU A CD1   
1857 C  CD2   . LEU A 242 ? 0.2015 0.1818 0.2686 0.0351  0.0091  0.0124  234 LEU A CD2   
1858 N  N     . LYS A 243 ? 0.1946 0.1630 0.3015 0.0273  0.0557  0.0622  235 LYS A N     
1859 C  CA    . LYS A 243 ? 0.2307 0.1590 0.3225 0.0103  0.0556  0.0555  235 LYS A CA    
1860 C  C     . LYS A 243 ? 0.2609 0.1676 0.3213 0.0558  0.0632  0.0538  235 LYS A C     
1861 O  O     . LYS A 243 ? 0.3163 0.1807 0.3351 0.0532  0.0671  0.0659  235 LYS A O     
1862 C  CB    . LYS A 243 ? 0.2466 0.1876 0.3428 -0.0108 0.0553  0.0486  235 LYS A CB    
1863 C  CG    . LYS A 243 ? 0.2721 0.2415 0.3648 -0.0146 0.0525  0.0329  235 LYS A CG    
1864 C  CD    . LYS A 243 ? 0.3059 0.3030 0.3833 -0.0263 0.0462  0.0323  235 LYS A CD    
1865 C  CE    . LYS A 243 ? 0.3434 0.3720 0.3977 -0.0195 0.0558  0.0333  235 LYS A CE    
1866 N  NZ    . LYS A 243 ? 0.3846 0.4417 0.4093 0.0156  0.0554  0.0385  235 LYS A NZ    
1867 N  N     . LEU A 244 ? 0.2442 0.2022 0.3140 0.0642  0.0609  0.0464  236 LEU A N     
1868 C  CA    . LEU A 244 ? 0.2682 0.2168 0.3074 0.0829  0.0323  0.0294  236 LEU A CA    
1869 C  C     . LEU A 244 ? 0.3290 0.2774 0.3145 0.1265  0.0129  0.0254  236 LEU A C     
1870 O  O     . LEU A 244 ? 0.3903 0.2906 0.3227 0.1336  0.0160  0.0163  236 LEU A O     
1871 C  CB    . LEU A 244 ? 0.2371 0.2022 0.2965 0.0570  0.0417  0.0284  236 LEU A CB    
1872 C  CG    . LEU A 244 ? 0.2093 0.1787 0.2861 0.0268  0.0388  0.0362  236 LEU A CG    
1873 C  CD1   . LEU A 244 ? 0.1907 0.1776 0.2875 0.0039  0.0330  0.0414  236 LEU A CD1   
1874 C  CD2   . LEU A 244 ? 0.2100 0.1831 0.2850 0.0347  0.0385  0.0404  236 LEU A CD2   
1875 O  OXT   . LEU A 244 ? 0.3827 0.2914 0.3149 0.1604  0.0091  0.0254  236 LEU A OXT   
1876 N  N9    . NOS B .   ? 0.1734 0.1598 0.1787 -0.0165 -0.0037 0.0433  301 NOS A N9    
1877 C  C4    . NOS B .   ? 0.1854 0.1454 0.1758 -0.0215 -0.0109 0.0305  301 NOS A C4    
1878 N  N3    . NOS B .   ? 0.1882 0.1686 0.1763 -0.0139 -0.0135 0.0214  301 NOS A N3    
1879 C  C2    . NOS B .   ? 0.1994 0.1452 0.1697 -0.0111 -0.0183 -0.0003 301 NOS A C2    
1880 N  N1    . NOS B .   ? 0.1941 0.1619 0.1670 -0.0034 -0.0089 0.0023  301 NOS A N1    
1881 C  C6    . NOS B .   ? 0.2081 0.1834 0.1678 -0.0136 -0.0085 0.0001  301 NOS A C6    
1882 O  O6    . NOS B .   ? 0.2344 0.2234 0.1747 -0.0138 0.0009  -0.0145 301 NOS A O6    
1883 C  C5    . NOS B .   ? 0.1859 0.1684 0.1758 -0.0264 -0.0046 0.0255  301 NOS A C5    
1884 N  N7    . NOS B .   ? 0.1822 0.1926 0.1833 -0.0086 -0.0094 0.0146  301 NOS A N7    
1885 C  C8    . NOS B .   ? 0.1759 0.1887 0.1845 -0.0120 -0.0061 0.0243  301 NOS A C8    
1886 C  "C5'" . NOS B .   ? 0.1742 0.1625 0.1901 -0.0180 0.0113  0.0404  301 NOS A "C5'" 
1887 O  "O5'" . NOS B .   ? 0.1822 0.1922 0.1938 -0.0163 -0.0016 0.0502  301 NOS A "O5'" 
1888 C  "C4'" . NOS B .   ? 0.1518 0.1528 0.1850 -0.0231 0.0088  0.0388  301 NOS A "C4'" 
1889 O  "O4'" . NOS B .   ? 0.1762 0.1531 0.1884 -0.0084 0.0001  0.0314  301 NOS A "O4'" 
1890 C  "C1'" . NOS B .   ? 0.1827 0.1623 0.1776 -0.0200 -0.0059 0.0232  301 NOS A "C1'" 
1891 C  "C2'" . NOS B .   ? 0.1936 0.1820 0.1814 -0.0464 0.0035  0.0280  301 NOS A "C2'" 
1892 O  "O2'" . NOS B .   ? 0.2388 0.2299 0.1868 -0.0842 -0.0057 0.0238  301 NOS A "O2'" 
1893 C  "C3'" . NOS B .   ? 0.1801 0.1596 0.1817 -0.0125 0.0007  0.0329  301 NOS A "C3'" 
1894 O  "O3'" . NOS B .   ? 0.2077 0.1484 0.1872 -0.0102 -0.0248 0.0165  301 NOS A "O3'" 
1895 CL CL    . CL  C .   ? 0.5045 0.7511 0.9430 0.1088  -0.0741 -0.0438 302 CL  A CL    
1896 CL CL    A CL  D .   ? 0.2542 0.3431 0.3957 0.0020  -0.0335 -0.0671 303 CL  A CL    
1897 CL CL    B CL  D .   ? 0.7338 0.8357 0.3716 0.1399  -0.1871 0.1092  303 CL  A CL    
1898 CL CL    . CL  E .   ? 0.3343 0.3320 0.3982 -0.0147 0.0322  0.0445  304 CL  A CL    
1899 O  O     . HOH F .   ? 0.3223 0.2661 0.4979 0.0064  -0.0053 0.0421  401 HOH A O     
1900 O  O     . HOH F .   ? 0.1599 0.1599 0.6338 0.0000  0.0000  0.0000  402 HOH A O     
1901 O  O     . HOH F .   ? 0.2841 0.3099 0.4056 0.0008  -0.0084 -0.1095 403 HOH A O     
1902 O  O     . HOH F .   ? 0.2197 0.3780 0.5238 -0.0359 -0.0270 -0.0314 404 HOH A O     
1903 O  O     . HOH F .   ? 0.4237 0.5701 0.5035 -0.0616 0.1851  0.1533  405 HOH A O     
1904 O  O     . HOH F .   ? 0.3990 0.7799 0.4725 -0.0487 0.0859  0.2888  406 HOH A O     
1905 O  O     . HOH F .   ? 0.6596 0.5060 0.3355 -0.3149 0.1261  -0.1313 407 HOH A O     
1906 O  O     . HOH F .   ? 0.2767 1.0386 0.3729 -0.0067 0.0438  0.0066  408 HOH A O     
1907 O  O     . HOH F .   ? 0.2697 0.5253 0.8149 0.0153  -0.0225 -0.3749 409 HOH A O     
1908 O  O     . HOH F .   ? 0.2531 0.8801 0.3278 -0.1029 0.0341  -0.1630 410 HOH A O     
1909 O  O     . HOH F .   ? 0.6046 0.5489 0.5618 0.2397  0.0557  0.1016  411 HOH A O     
1910 O  O     . HOH F .   ? 0.4241 0.7480 0.3717 -0.1041 0.1592  0.1052  412 HOH A O     
1911 O  O     . HOH F .   ? 0.3988 0.4525 0.3020 -0.0331 -0.0747 0.0625  413 HOH A O     
1912 O  O     . HOH F .   ? 0.6700 0.3432 0.6579 -0.0825 0.3857  -0.1117 414 HOH A O     
1913 O  O     . HOH F .   ? 0.7585 0.4263 0.4044 -0.0894 0.0437  -0.0153 415 HOH A O     
1914 O  O     . HOH F .   ? 0.9530 0.4848 0.3606 0.0251  -0.1928 -0.0906 416 HOH A O     
1915 O  O     . HOH F .   ? 0.5869 0.4373 0.2477 0.1226  0.0617  0.0643  417 HOH A O     
1916 O  O     . HOH F .   ? 0.8861 0.2605 0.5162 -0.0595 -0.2369 0.0441  418 HOH A O     
1917 O  O     . HOH F .   ? 0.4379 0.3564 0.3425 0.1063  -0.0287 -0.0735 419 HOH A O     
1918 O  O     . HOH F .   ? 0.5203 0.6420 0.3369 0.1234  -0.1544 0.0466  420 HOH A O     
1919 O  O     . HOH F .   ? 0.7083 0.4786 0.4088 0.0504  -0.0794 0.0423  421 HOH A O     
1920 O  O     . HOH F .   ? 0.5751 0.4749 0.1734 0.0491  0.0456  0.0732  422 HOH A O     
1921 O  O     . HOH F .   ? 0.2924 0.4126 0.3764 -0.0170 -0.0290 0.1422  423 HOH A O     
1922 O  O     . HOH F .   ? 0.4315 0.6726 0.2965 0.2815  0.0332  -0.0134 424 HOH A O     
1923 O  O     . HOH F .   ? 0.1797 0.1426 0.2809 -0.0007 0.0256  -0.0057 425 HOH A O     
1924 O  O     . HOH F .   ? 0.1860 0.1880 0.2561 -0.0140 0.0148  0.0156  426 HOH A O     
1925 O  O     . HOH F .   ? 0.1328 0.1606 0.1537 -0.0059 -0.0022 0.0076  427 HOH A O     
1926 O  O     . HOH F .   ? 0.1453 0.1372 0.1227 -0.0116 0.0030  0.0135  428 HOH A O     
1927 O  O     . HOH F .   ? 0.6355 0.4722 0.2389 -0.1247 0.0243  -0.1292 429 HOH A O     
1928 O  O     . HOH F .   ? 0.7236 0.4198 0.2740 -0.2844 -0.1124 0.0854  430 HOH A O     
1929 O  O     . HOH F .   ? 0.2542 0.4092 0.3003 0.0413  0.0263  -0.0381 431 HOH A O     
1930 O  O     . HOH F .   ? 0.3708 0.5807 0.5104 0.1348  -0.0303 -0.1244 432 HOH A O     
1931 O  O     . HOH F .   ? 0.2838 0.5820 0.5336 0.0772  -0.0319 0.2710  433 HOH A O     
1932 O  O     . HOH F .   ? 0.3616 0.2736 0.4206 0.0031  -0.0614 0.0194  434 HOH A O     
1933 O  O     . HOH F .   ? 0.2800 0.1924 0.1609 0.0010  -0.0153 -0.0092 435 HOH A O     
1934 O  O     . HOH F .   ? 0.2393 0.2956 0.3848 0.0597  0.0174  0.0010  436 HOH A O     
1935 O  O     . HOH F .   ? 0.4015 0.8006 0.2612 -0.2989 -0.0231 0.0493  437 HOH A O     
1936 O  O     . HOH F .   ? 0.1512 0.1973 0.1652 -0.0079 0.0312  0.0088  438 HOH A O     
1937 O  O     . HOH F .   ? 0.4948 0.4037 0.3498 0.1203  0.1457  0.0943  439 HOH A O     
1938 O  O     . HOH F .   ? 0.1564 0.1465 0.1807 0.0027  0.0001  0.0078  440 HOH A O     
1939 O  O     . HOH F .   ? 0.1805 0.1492 0.2153 -0.0053 -0.0147 0.0103  441 HOH A O     
1940 O  O     . HOH F .   ? 0.2696 0.1734 0.3637 0.0833  -0.1377 -0.0795 442 HOH A O     
1941 O  O     . HOH F .   ? 0.3360 0.2437 0.3197 0.0158  -0.0327 -0.0571 443 HOH A O     
1942 O  O     . HOH F .   ? 0.3106 0.3269 0.2802 0.0145  -0.0485 0.0875  444 HOH A O     
1943 O  O     . HOH F .   ? 0.1178 0.1322 0.1841 -0.0021 0.0081  -0.0022 445 HOH A O     
1944 O  O     . HOH F .   ? 0.2064 0.1528 0.1881 0.0286  0.0040  -0.0021 446 HOH A O     
1945 O  O     . HOH F .   ? 0.6129 0.5498 0.4179 0.1215  0.1661  0.1292  447 HOH A O     
1946 O  O     . HOH F .   ? 0.3284 0.2043 0.2685 0.0605  0.0683  0.0404  448 HOH A O     
1947 O  O     . HOH F .   ? 0.6802 0.2769 0.7741 -0.0614 0.2879  0.0239  449 HOH A O     
1948 O  O     . HOH F .   ? 0.2974 0.3113 0.4817 0.0396  0.0398  0.0796  450 HOH A O     
1949 O  O     . HOH F .   ? 0.2171 0.2421 0.3119 0.0195  0.0608  0.0466  451 HOH A O     
1950 O  O     . HOH F .   ? 0.1307 0.1239 0.1386 0.0016  0.0008  0.0092  452 HOH A O     
1951 O  O     . HOH F .   ? 0.1436 0.1228 0.2378 -0.0081 -0.0015 -0.0037 453 HOH A O     
1952 O  O     . HOH F .   ? 0.2910 0.2606 0.4072 -0.0364 -0.0448 0.0272  454 HOH A O     
1953 O  O     . HOH F .   ? 0.1845 0.1525 0.3685 0.0017  -0.0435 0.0038  455 HOH A O     
1954 O  O     . HOH F .   ? 0.3943 0.3368 0.9877 0.0262  -0.0796 -0.1491 456 HOH A O     
1955 O  O     . HOH F .   ? 0.2342 0.1800 0.2360 0.0332  0.0412  0.0157  457 HOH A O     
1956 O  O     . HOH F .   ? 0.2501 0.1787 0.6085 0.0437  -0.0843 -0.0243 458 HOH A O     
1957 O  O     . HOH F .   ? 0.2014 0.2845 0.2064 0.0500  0.0082  0.0053  459 HOH A O     
1958 O  O     . HOH F .   ? 0.1424 0.1633 0.3400 -0.0181 -0.0028 -0.0016 460 HOH A O     
1959 O  O     . HOH F .   ? 0.1321 0.1322 0.1469 -0.0032 -0.0061 0.0066  461 HOH A O     
1960 O  O     . HOH F .   ? 0.4709 0.3731 0.8216 -0.0532 -0.0131 0.1880  462 HOH A O     
1961 O  O     . HOH F .   ? 0.2201 0.1897 0.2033 0.0029  0.0054  0.0370  463 HOH A O     
1962 O  O     . HOH F .   ? 0.2137 0.2838 0.2904 -0.0331 0.0104  0.0436  464 HOH A O     
1963 O  O     . HOH F .   ? 0.1224 0.1267 0.1488 -0.0017 0.0069  -0.0038 465 HOH A O     
1964 O  O     . HOH F .   ? 0.5108 0.7733 0.7984 0.1897  0.3095  0.2960  466 HOH A O     
1965 O  O     . HOH F .   ? 0.5159 0.1638 0.1932 -0.0722 -0.1241 0.0315  467 HOH A O     
1966 O  O     . HOH F .   ? 0.4098 0.3610 0.7503 0.0881  -0.1783 -0.0571 468 HOH A O     
1967 O  O     . HOH F .   ? 0.2297 0.1854 0.1952 -0.0049 -0.0288 -0.0246 469 HOH A O     
1968 O  O     . HOH F .   ? 0.2323 0.4452 0.3965 -0.0454 -0.0181 0.0885  470 HOH A O     
1969 O  O     . HOH F .   ? 0.3199 0.1625 0.3869 0.0370  0.2072  0.0378  471 HOH A O     
1970 O  O     . HOH F .   ? 0.3045 0.6604 0.5243 -0.2040 -0.0557 0.0987  472 HOH A O     
1971 O  O     . HOH F .   ? 0.3395 0.2613 0.3169 -0.0211 -0.0728 -0.0391 473 HOH A O     
1972 O  O     . HOH F .   ? 0.2248 0.1879 0.1915 -0.0089 0.0330  -0.0017 474 HOH A O     
1973 O  O     . HOH F .   ? 0.5172 0.4913 0.7370 -0.1656 -0.0631 -0.1915 475 HOH A O     
1974 O  O     . HOH F .   ? 0.2181 0.4160 0.5290 -0.0137 0.0376  -0.0920 476 HOH A O     
1975 O  O     . HOH F .   ? 0.1989 0.3427 0.5071 -0.0185 0.0758  0.0881  477 HOH A O     
1976 O  O     . HOH F .   ? 0.2191 0.7572 0.4137 -0.0501 0.0119  -0.2042 478 HOH A O     
1977 O  O     . HOH F .   ? 0.2097 0.1895 0.2247 -0.0093 0.0022  0.0345  479 HOH A O     
1978 O  O     . HOH F .   ? 0.2049 0.2091 0.2445 -0.0160 0.0168  0.0405  480 HOH A O     
1979 O  O     . HOH F .   ? 0.2762 0.3102 0.5619 -0.0182 -0.0361 0.1129  481 HOH A O     
1980 O  O     . HOH F .   ? 0.2941 0.2100 0.2837 -0.0051 0.0678  -0.0253 482 HOH A O     
1981 O  O     . HOH F .   ? 0.1627 0.1754 0.1942 0.0238  0.0136  0.0094  483 HOH A O     
1982 O  O     A HOH F .   ? 0.2353 0.1890 0.1356 -0.0058 0.0349  0.0645  484 HOH A O     
1983 O  O     B HOH F .   ? 0.2528 0.2626 0.2219 0.1073  0.0645  0.0045  484 HOH A O     
1984 O  O     . HOH F .   ? 0.7391 0.3550 0.2597 0.1931  0.0185  0.0534  485 HOH A O     
1985 O  O     . HOH F .   ? 0.2831 0.2705 0.4169 0.0662  0.0774  0.1669  486 HOH A O     
1986 O  O     . HOH F .   ? 0.4263 0.5440 0.3787 -0.0826 -0.1544 0.0050  487 HOH A O     
1987 O  O     . HOH F .   ? 0.3009 0.1895 0.1701 -0.0121 0.0434  -0.0067 488 HOH A O     
1988 O  O     . HOH F .   ? 0.1279 0.1203 0.1283 -0.0094 0.0076  0.0042  489 HOH A O     
1989 O  O     . HOH F .   ? 0.1559 0.1859 0.2660 0.0297  -0.0285 -0.0750 490 HOH A O     
1990 O  O     . HOH F .   ? 0.3919 0.4734 0.3863 0.0956  -0.0244 -0.0037 491 HOH A O     
1991 O  O     . HOH F .   ? 0.3478 0.3795 0.2657 -0.0492 -0.0356 -0.0228 492 HOH A O     
1992 O  O     . HOH F .   ? 0.2814 0.1830 0.3217 0.0183  -0.0726 0.0786  493 HOH A O     
1993 O  O     . HOH F .   ? 0.8890 0.4144 0.5521 0.1985  -0.0804 0.1013  494 HOH A O     
1994 O  O     . HOH F .   ? 0.5333 0.6229 0.4790 0.2559  -0.1850 -0.2334 495 HOH A O     
1995 O  O     . HOH F .   ? 0.1976 0.2201 0.1820 0.0192  0.0415  -0.0030 496 HOH A O     
1996 O  O     . HOH F .   ? 0.3359 0.1577 0.5695 0.0523  -0.0273 -0.0138 497 HOH A O     
1997 O  O     . HOH F .   ? 0.2047 0.1665 0.3126 0.0191  0.0714  0.0249  498 HOH A O     
1998 O  O     . HOH F .   ? 0.6001 0.4990 0.2980 0.2729  0.0271  0.1101  499 HOH A O     
1999 O  O     . HOH F .   ? 0.5849 0.1972 0.2661 -0.0156 0.0516  -0.0081 500 HOH A O     
2000 O  O     . HOH F .   ? 0.2553 0.2384 0.2350 -0.0550 0.0333  -0.0428 501 HOH A O     
2001 O  O     . HOH F .   ? 0.6798 0.5510 0.3732 -0.0949 0.1083  -0.1622 502 HOH A O     
2002 O  O     . HOH F .   ? 0.1885 0.2407 0.2774 0.0212  0.0317  0.0505  503 HOH A O     
2003 O  O     . HOH F .   ? 0.2190 0.1812 0.1819 -0.0084 0.0112  -0.0139 504 HOH A O     
2004 O  O     . HOH F .   ? 0.1702 0.1906 0.2623 -0.0028 -0.0007 -0.0027 505 HOH A O     
2005 O  O     . HOH F .   ? 0.3190 0.2345 0.2073 0.0843  -0.0620 -0.0465 506 HOH A O     
2006 O  O     . HOH F .   ? 0.2497 0.5222 0.9704 -0.0137 -0.0099 -0.1072 507 HOH A O     
2007 O  O     . HOH F .   ? 0.3761 0.4755 0.2594 -0.0525 0.0466  0.0607  508 HOH A O     
2008 O  O     . HOH F .   ? 0.1914 0.3089 0.3101 0.0572  0.0677  0.0476  509 HOH A O     
2009 O  O     . HOH F .   ? 0.1866 0.2214 0.3445 0.0099  0.0180  0.0574  510 HOH A O     
2010 O  O     . HOH F .   ? 0.1528 0.1906 0.3153 -0.0017 0.0227  0.0219  511 HOH A O     
2011 O  O     . HOH F .   ? 0.2307 0.2681 0.5284 0.0323  -0.0045 -0.1030 512 HOH A O     
2012 O  O     . HOH F .   ? 0.3152 0.2682 0.2181 0.0409  0.0264  0.0250  513 HOH A O     
2013 O  O     . HOH F .   ? 0.2101 0.2349 0.4036 -0.0246 -0.0019 -0.0306 514 HOH A O     
2014 O  O     . HOH F .   ? 0.3501 0.2216 0.5167 0.0560  0.0121  0.0365  515 HOH A O     
2015 O  O     . HOH F .   ? 0.2044 0.1991 0.1813 -0.0276 0.0127  0.0208  516 HOH A O     
2016 O  O     . HOH F .   ? 0.4429 0.8225 0.3880 -0.0912 -0.0729 -0.0804 517 HOH A O     
2017 O  O     . HOH F .   ? 0.3103 0.3312 0.6580 -0.0191 -0.1026 -0.2076 518 HOH A O     
2018 O  O     . HOH F .   ? 0.4646 0.3992 0.6318 0.0195  0.3059  0.0209  519 HOH A O     
2019 O  O     . HOH F .   ? 0.6008 0.6486 0.3547 0.2371  -0.0250 0.0929  520 HOH A O     
2020 O  O     . HOH F .   ? 0.7775 0.5416 0.4101 0.0271  -0.0931 -0.1357 521 HOH A O     
2021 O  O     . HOH F .   ? 0.3514 0.4635 0.5783 0.1687  -0.1099 -0.2231 522 HOH A O     
2022 O  O     . HOH F .   ? 0.6089 0.4792 0.5052 0.0722  -0.2614 0.0166  523 HOH A O     
2023 O  O     A HOH F .   ? 0.1646 0.1473 0.5597 0.0060  0.0670  0.0393  524 HOH A O     
2024 O  O     B HOH F .   ? 0.0984 0.0887 0.2306 -0.0160 0.0024  -0.0041 524 HOH A O     
2025 O  O     . HOH F .   ? 0.5290 0.3652 0.6860 -0.1165 -0.0081 -0.0190 525 HOH A O     
2026 O  O     . HOH F .   ? 0.6358 0.5335 0.7741 -0.2551 0.0360  0.0731  526 HOH A O     
2027 O  O     . HOH F .   ? 0.2236 0.4720 0.2332 0.0993  -0.0028 0.0353  527 HOH A O     
2028 O  O     . HOH F .   ? 0.2498 0.2500 0.5837 0.0370  -0.0890 0.0170  528 HOH A O     
2029 O  O     . HOH F .   ? 0.1777 0.1548 0.1604 -0.0076 0.0024  0.0105  529 HOH A O     
2030 O  O     . HOH F .   ? 0.5036 0.6144 0.4991 -0.3260 0.0285  -0.0735 530 HOH A O     
2031 O  O     . HOH F .   ? 0.3716 0.2348 0.7302 0.0416  -0.2736 -0.0734 531 HOH A O     
2032 O  O     . HOH F .   ? 0.1331 0.1177 0.3901 0.0020  0.0471  -0.0049 532 HOH A O     
2033 O  O     . HOH F .   ? 0.2985 0.5007 0.9005 0.0474  -0.1007 0.1580  533 HOH A O     
2034 O  O     . HOH F .   ? 0.6727 0.6068 0.5033 -0.1170 0.0184  0.1956  534 HOH A O     
2035 O  O     . HOH F .   ? 0.8126 0.4832 0.4787 0.0491  -0.0401 0.1284  535 HOH A O     
2036 O  O     . HOH F .   ? 0.2721 0.3710 0.4070 -0.0983 -0.0539 -0.0225 536 HOH A O     
2037 O  O     . HOH F .   ? 0.4591 0.7875 0.3374 0.1255  -0.0122 0.0643  537 HOH A O     
2038 O  O     . HOH F .   ? 0.2384 0.6206 0.7438 0.0722  0.0613  0.1897  538 HOH A O     
2039 O  O     . HOH F .   ? 0.2710 0.4499 0.4524 -0.0197 0.0134  0.0626  539 HOH A O     
2040 O  O     . HOH F .   ? 0.5532 0.1772 0.3679 0.0495  -0.1811 -0.0021 540 HOH A O     
2041 O  O     . HOH F .   ? 0.5948 0.7477 0.5502 0.0398  0.0355  -0.1803 541 HOH A O     
2042 O  O     . HOH F .   ? 0.3527 0.4095 0.5318 -0.1392 -0.0599 0.0082  542 HOH A O     
2043 O  O     . HOH F .   ? 0.3290 0.2482 0.8306 -0.0154 -0.0479 0.0043  543 HOH A O     
2044 O  O     . HOH F .   ? 0.5793 0.4245 0.6558 -0.1187 -0.2916 -0.0716 544 HOH A O     
2045 O  O     . HOH F .   ? 0.5741 0.8313 0.3755 -0.2058 0.0418  -0.1222 545 HOH A O     
2046 O  O     . HOH F .   ? 0.3663 0.7850 0.3475 -0.1216 -0.0185 0.1157  546 HOH A O     
2047 O  O     . HOH F .   ? 0.4885 0.2878 0.8229 -0.0386 -0.3526 0.0711  547 HOH A O     
2048 O  O     . HOH F .   ? 0.4800 0.4807 0.6479 0.1332  0.0900  0.1372  548 HOH A O     
2049 O  O     . HOH F .   ? 0.2129 0.2794 0.5939 -0.0619 -0.1102 0.1467  549 HOH A O     
2050 O  O     . HOH F .   ? 0.3375 0.4807 0.7265 -0.0533 -0.0747 0.1001  550 HOH A O     
2051 O  O     . HOH F .   ? 0.2910 0.3332 0.4768 -0.0563 0.0425  0.0784  551 HOH A O     
2052 O  O     . HOH F .   ? 0.5841 0.6852 0.5045 -0.0326 0.0404  0.1235  552 HOH A O     
2053 O  O     . HOH F .   ? 0.2044 0.2405 0.6384 -0.0072 -0.0577 0.1623  553 HOH A O     
2054 O  O     . HOH F .   ? 0.3712 0.4323 0.8669 -0.0395 -0.2636 0.1431  554 HOH A O     
2055 O  O     . HOH F .   ? 0.5114 0.2964 0.3683 0.0037  0.1506  0.0430  555 HOH A O     
2056 O  O     . HOH F .   ? 0.4170 0.3375 0.3998 -0.0102 -0.0276 0.0926  556 HOH A O     
2057 O  O     . HOH F .   ? 0.7698 0.6565 0.4039 -0.0387 0.1223  0.1869  557 HOH A O     
2058 O  O     . HOH F .   ? 0.9187 0.7213 0.3064 0.2702  0.0105  -0.0704 558 HOH A O     
2059 O  O     . HOH F .   ? 0.1530 0.1587 0.6040 0.0026  0.0163  0.0395  559 HOH A O     
2060 O  O     . HOH F .   ? 0.7769 0.4189 0.5690 -0.0915 -0.3601 0.0719  560 HOH A O     
2061 O  O     . HOH F .   ? 0.2618 0.4494 0.8338 0.0309  0.0113  0.1546  561 HOH A O     
2062 O  O     . HOH F .   ? 0.2824 0.1687 0.1905 -0.0171 -0.0152 -0.0027 562 HOH A O     
2063 O  O     . HOH F .   ? 0.6983 0.5315 0.5869 -0.0599 -0.0520 0.0340  563 HOH A O     
2064 O  O     . HOH F .   ? 0.6997 0.6126 0.4925 -0.2691 0.2487  -0.1867 564 HOH A O     
2065 O  O     . HOH F .   ? 0.2948 0.2195 0.7962 0.0205  -0.1620 -0.0092 565 HOH A O     
2066 O  O     . HOH F .   ? 0.5249 0.5192 0.7413 -0.0903 -0.1083 0.0201  566 HOH A O     
2067 O  O     . HOH F .   ? 0.3464 0.3888 0.4526 0.1681  -0.1937 -0.2205 567 HOH A O     
2068 O  O     . HOH F .   ? 0.5018 0.2827 0.5385 -0.0035 0.0165  -0.0167 568 HOH A O     
2069 O  O     . HOH F .   ? 0.6504 0.5936 0.3835 -0.0816 0.1750  -0.0439 569 HOH A O     
2070 O  O     . HOH F .   ? 0.3573 0.5127 0.4922 0.0010  0.0470  -0.0608 570 HOH A O     
2071 O  O     . HOH F .   ? 0.6661 0.3706 0.6215 0.2257  -0.1612 -0.0848 571 HOH A O     
2072 O  O     . HOH F .   ? 0.3884 0.8027 0.6799 0.0309  0.0543  0.2506  572 HOH A O     
2073 O  O     . HOH F .   ? 0.5719 0.5307 0.6935 -0.2271 -0.1219 0.0566  573 HOH A O     
2074 O  O     . HOH F .   ? 0.7165 0.5464 0.4518 -0.1092 0.0206  -0.0679 574 HOH A O     
2075 O  O     . HOH F .   ? 0.5665 0.4895 0.7009 0.0417  0.2272  0.0684  575 HOH A O     
2076 O  O     . HOH F .   ? 0.3750 0.4889 0.4575 0.0309  0.1159  -0.0077 576 HOH A O     
2077 O  O     . HOH F .   ? 0.8865 0.3057 0.6317 0.1209  0.0885  0.1465  577 HOH A O     
2078 O  O     . HOH F .   ? 0.1879 0.1792 0.3103 0.0165  0.0054  0.0172  578 HOH A O     
2079 O  O     . HOH F .   ? 0.8753 0.3817 0.2565 -0.1597 0.0215  -0.0576 579 HOH A O     
2080 O  O     . HOH F .   ? 0.5787 0.5063 0.5672 -0.2195 -0.0664 0.0352  580 HOH A O     
2081 O  O     . HOH F .   ? 0.2784 0.5350 0.5125 0.0906  0.0767  0.2351  581 HOH A O     
2082 O  O     . HOH F .   ? 0.2642 0.2232 0.6457 0.0365  0.0187  0.0939  582 HOH A O     
2083 O  O     . HOH F .   ? 0.4200 0.6598 0.6350 0.1533  -0.1921 0.0575  583 HOH A O     
2084 O  O     . HOH F .   ? 0.3739 0.6898 0.7985 -0.0797 -0.1847 -0.2186 584 HOH A O     
2085 O  O     . HOH F .   ? 0.1411 0.1582 0.4834 0.0022  0.0170  0.0635  585 HOH A O     
2086 O  O     . HOH F .   ? 0.2950 0.2971 0.4581 -0.0665 -0.0886 0.1059  586 HOH A O     
2087 O  O     . HOH F .   ? 0.3540 0.8003 0.6226 -0.1326 -0.0505 0.3653  587 HOH A O     
2088 O  O     . HOH F .   ? 0.2019 0.1942 0.2665 0.0157  -0.0026 -0.0203 588 HOH A O     
2089 O  O     . HOH F .   ? 0.3669 0.3895 1.1093 0.0131  -0.0331 -0.1276 589 HOH A O     
2090 O  O     . HOH F .   ? 0.5401 0.4313 0.5325 -0.0290 -0.0956 0.0060  590 HOH A O     
2091 O  O     . HOH F .   ? 0.3110 0.2597 0.2600 0.0225  -0.0093 -0.0140 591 HOH A O     
2092 O  O     . HOH F .   ? 0.2157 0.2085 0.3244 -0.0115 0.0305  -0.0100 592 HOH A O     
2093 O  O     . HOH F .   ? 0.4006 0.2583 0.7558 0.0151  0.1829  0.0668  593 HOH A O     
2094 O  O     . HOH F .   ? 0.7421 0.5656 0.7340 0.3280  0.2696  0.2385  594 HOH A O     
2095 O  O     . HOH F .   ? 0.2452 0.3019 0.2456 0.0000  0.0000  -0.0126 595 HOH A O     
2096 O  O     . HOH F .   ? 0.2652 0.2597 0.3289 -0.0242 -0.0070 0.0317  596 HOH A O     
2097 O  O     . HOH F .   ? 0.1642 0.3033 0.2601 0.0552  -0.0095 0.0013  597 HOH A O     
# 
