data_9FJQ
# 
_entry.id   9FJQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9FJQ         pdb_00009fjq 10.2210/pdb9fjq/pdb 
WWPDB D_1292138261 ?            ?                   
# 
_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       2025-05-14 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FJQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              lena@ibt.lt 
_pdbx_contact_author.name_first         Elena 
_pdbx_contact_author.name_last          Manakova 
_pdbx_contact_author.name_mi            N. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6027-2265 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Manakova, E.N.'   1 0000-0002-6027-2265 
'Grazulis, S.'     2 0000-0002-7928-5218 
'Paketuryte, V.'   3 0000-0003-0919-7826 
'Smirnov, A.'      4 0000-0001-5080-9367 
'Vaskevicius, A.'  5 0009-0006-8202-9748 
'Trumpickaite, G.' 6 0009-0003-2029-5053 
# 
_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                   GE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemistry 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           0947-6539 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            31 
_citation.language                  ? 
_citation.page_first                e202404409 
_citation.page_last                 e202404409 
_citation.title                     'Design of Rigid Compounds to Enhance Selectivity for Carbonic Anhydrase IX.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/chem.202404409 
_citation.pdbx_database_id_PubMed   39905940 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vaskevicius, A.'      1  ?                   
primary 'Trumpickaite, G.'     2  ?                   
primary 'Parafjanovic, E.'     3  ?                   
primary 'Manakova, E.'         4  ?                   
primary 'Mickeviciute, A.'     5  ?                   
primary 'Gedgaudas, M.'        6  ?                   
primary 'Kojis, T.'            7  ?                   
primary 'Paketuryte-Latve, V.' 8  ?                   
primary 'Smirnov, A.'          9  ?                   
primary 'Baranauskiene, L.'    10 ?                   
primary 'Grazulis, S.'         11 ?                   
primary 'Zubriene, A.'         12 ?                   
primary 'Dudutiene, V.'        13 ?                   
primary 'Matulis, D.'          14 0000-0002-6178-6276 
# 
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 'Carbonic anhydrase 2' 29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION' 65.409    1   ?       ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    1   ?       ? ? ? 
4 non-polymer syn 
'5,7,8-tris(fluoranyl)-1,1-bis(oxidanylidene)-4-(phenylmethyl)-2,3-dihydro-1$l^{6},4-benzothiazine-6-sulfonamide' 406.400   1   ? 
? ? ? 
5 water       nat water 18.015    291 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                                                        ZN    
3 'DIMETHYL SULFOXIDE'                                                                                              DMS   
4 '5,7,8-tris(fluoranyl)-1,1-bis(oxidanylidene)-4-(phenylmethyl)-2,3-dihydro-1$l^{6},4-benzothiazine-6-sulfonamide' A1IDL 
5 water                                                                                                             HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS 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                   260 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_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                       pET21a 
_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 
A1IDL non-polymer         . 
'5,7,8-tris(fluoranyl)-1,1-bis(oxidanylidene)-4-(phenylmethyl)-2,3-dihydro-1$l^{6},4-benzothiazine-6-sulfonamide' ? 
'C15 H13 F3 N2 O4 S2' 406.400 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'          89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'      175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'         132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'          133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'        121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S'           78.133  
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'        146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'          147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'          75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'      156.162 
HOH   non-polymer         . WATER ? 'H2 O'                18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'         131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'         131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'      147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'       149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'         165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'          115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'          105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'          119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'       204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'         181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'         117.146 
ZN    non-polymer         . 'ZINC ION' ? 'Zn 2'                65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IDL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IDL 
_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 ZN    1   301 1   ZN    ZN  A . 
C 3 DMS   1   302 1   DMS   DMS A . 
D 4 A1IDL 1   303 1   A1IDL G10 A . 
E 5 HOH   1   401 238 HOH   HOH A . 
E 5 HOH   2   402 195 HOH   HOH A . 
E 5 HOH   3   403 191 HOH   HOH A . 
E 5 HOH   4   404 246 HOH   HOH A . 
E 5 HOH   5   405 190 HOH   HOH A . 
E 5 HOH   6   406 102 HOH   HOH A . 
E 5 HOH   7   407 86  HOH   HOH A . 
E 5 HOH   8   408 198 HOH   HOH A . 
E 5 HOH   9   409 188 HOH   HOH A . 
E 5 HOH   10  410 205 HOH   HOH A . 
E 5 HOH   11  411 287 HOH   HOH A . 
E 5 HOH   12  412 127 HOH   HOH A . 
E 5 HOH   13  413 24  HOH   HOH A . 
E 5 HOH   14  414 197 HOH   HOH A . 
E 5 HOH   15  415 144 HOH   HOH A . 
E 5 HOH   16  416 145 HOH   HOH A . 
E 5 HOH   17  417 109 HOH   HOH A . 
E 5 HOH   18  418 261 HOH   HOH A . 
E 5 HOH   19  419 199 HOH   HOH A . 
E 5 HOH   20  420 210 HOH   HOH A . 
E 5 HOH   21  421 77  HOH   HOH A . 
E 5 HOH   22  422 150 HOH   HOH A . 
E 5 HOH   23  423 118 HOH   HOH A . 
E 5 HOH   24  424 50  HOH   HOH A . 
E 5 HOH   25  425 282 HOH   HOH A . 
E 5 HOH   26  426 69  HOH   HOH A . 
E 5 HOH   27  427 260 HOH   HOH A . 
E 5 HOH   28  428 73  HOH   HOH A . 
E 5 HOH   29  429 180 HOH   HOH A . 
E 5 HOH   30  430 165 HOH   HOH A . 
E 5 HOH   31  431 108 HOH   HOH A . 
E 5 HOH   32  432 82  HOH   HOH A . 
E 5 HOH   33  433 30  HOH   HOH A . 
E 5 HOH   34  434 196 HOH   HOH A . 
E 5 HOH   35  435 6   HOH   HOH A . 
E 5 HOH   36  436 20  HOH   HOH A . 
E 5 HOH   37  437 39  HOH   HOH A . 
E 5 HOH   38  438 259 HOH   HOH A . 
E 5 HOH   39  439 14  HOH   HOH A . 
E 5 HOH   40  440 185 HOH   HOH A . 
E 5 HOH   41  441 42  HOH   HOH A . 
E 5 HOH   42  442 140 HOH   HOH A . 
E 5 HOH   43  443 7   HOH   HOH A . 
E 5 HOH   44  444 57  HOH   HOH A . 
E 5 HOH   45  445 75  HOH   HOH A . 
E 5 HOH   46  446 119 HOH   HOH A . 
E 5 HOH   47  447 79  HOH   HOH A . 
E 5 HOH   48  448 229 HOH   HOH A . 
E 5 HOH   49  449 178 HOH   HOH A . 
E 5 HOH   50  450 206 HOH   HOH A . 
E 5 HOH   51  451 33  HOH   HOH A . 
E 5 HOH   52  452 96  HOH   HOH A . 
E 5 HOH   53  453 87  HOH   HOH A . 
E 5 HOH   54  454 135 HOH   HOH A . 
E 5 HOH   55  455 275 HOH   HOH A . 
E 5 HOH   56  456 158 HOH   HOH A . 
E 5 HOH   57  457 72  HOH   HOH A . 
E 5 HOH   58  458 162 HOH   HOH A . 
E 5 HOH   59  459 136 HOH   HOH A . 
E 5 HOH   60  460 290 HOH   HOH A . 
E 5 HOH   61  461 103 HOH   HOH A . 
E 5 HOH   62  462 277 HOH   HOH A . 
E 5 HOH   63  463 116 HOH   HOH A . 
E 5 HOH   64  464 88  HOH   HOH A . 
E 5 HOH   65  465 211 HOH   HOH A . 
E 5 HOH   66  466 169 HOH   HOH A . 
E 5 HOH   67  467 133 HOH   HOH A . 
E 5 HOH   68  468 67  HOH   HOH A . 
E 5 HOH   69  469 19  HOH   HOH A . 
E 5 HOH   70  470 233 HOH   HOH A . 
E 5 HOH   71  471 43  HOH   HOH A . 
E 5 HOH   72  472 193 HOH   HOH A . 
E 5 HOH   73  473 70  HOH   HOH A . 
E 5 HOH   74  474 23  HOH   HOH A . 
E 5 HOH   75  475 204 HOH   HOH A . 
E 5 HOH   76  476 53  HOH   HOH A . 
E 5 HOH   77  477 141 HOH   HOH A . 
E 5 HOH   78  478 147 HOH   HOH A . 
E 5 HOH   79  479 163 HOH   HOH A . 
E 5 HOH   80  480 271 HOH   HOH A . 
E 5 HOH   81  481 101 HOH   HOH A . 
E 5 HOH   82  482 40  HOH   HOH A . 
E 5 HOH   83  483 241 HOH   HOH A . 
E 5 HOH   84  484 192 HOH   HOH A . 
E 5 HOH   85  485 5   HOH   HOH A . 
E 5 HOH   86  486 8   HOH   HOH A . 
E 5 HOH   87  487 215 HOH   HOH A . 
E 5 HOH   88  488 27  HOH   HOH A . 
E 5 HOH   89  489 4   HOH   HOH A . 
E 5 HOH   90  490 34  HOH   HOH A . 
E 5 HOH   91  491 171 HOH   HOH A . 
E 5 HOH   92  492 155 HOH   HOH A . 
E 5 HOH   93  493 152 HOH   HOH A . 
E 5 HOH   94  494 250 HOH   HOH A . 
E 5 HOH   95  495 160 HOH   HOH A . 
E 5 HOH   96  496 60  HOH   HOH A . 
E 5 HOH   97  497 121 HOH   HOH A . 
E 5 HOH   98  498 92  HOH   HOH A . 
E 5 HOH   99  499 13  HOH   HOH A . 
E 5 HOH   100 500 68  HOH   HOH A . 
E 5 HOH   101 501 81  HOH   HOH A . 
E 5 HOH   102 502 2   HOH   HOH A . 
E 5 HOH   103 503 95  HOH   HOH A . 
E 5 HOH   104 504 237 HOH   HOH A . 
E 5 HOH   105 505 129 HOH   HOH A . 
E 5 HOH   106 506 78  HOH   HOH A . 
E 5 HOH   107 507 16  HOH   HOH A . 
E 5 HOH   108 508 17  HOH   HOH A . 
E 5 HOH   109 509 1   HOH   HOH A . 
E 5 HOH   110 510 76  HOH   HOH A . 
E 5 HOH   111 511 48  HOH   HOH A . 
E 5 HOH   112 512 186 HOH   HOH A . 
E 5 HOH   113 513 83  HOH   HOH A . 
E 5 HOH   114 514 58  HOH   HOH A . 
E 5 HOH   115 515 279 HOH   HOH A . 
E 5 HOH   116 516 11  HOH   HOH A . 
E 5 HOH   117 517 110 HOH   HOH A . 
E 5 HOH   118 518 267 HOH   HOH A . 
E 5 HOH   119 519 3   HOH   HOH A . 
E 5 HOH   120 520 54  HOH   HOH A . 
E 5 HOH   121 521 291 HOH   HOH A . 
E 5 HOH   122 522 80  HOH   HOH A . 
E 5 HOH   123 523 26  HOH   HOH A . 
E 5 HOH   124 524 64  HOH   HOH A . 
E 5 HOH   125 525 107 HOH   HOH A . 
E 5 HOH   126 526 44  HOH   HOH A . 
E 5 HOH   127 527 51  HOH   HOH A . 
E 5 HOH   128 528 156 HOH   HOH A . 
E 5 HOH   129 529 142 HOH   HOH A . 
E 5 HOH   130 530 122 HOH   HOH A . 
E 5 HOH   131 531 139 HOH   HOH A . 
E 5 HOH   132 532 90  HOH   HOH A . 
E 5 HOH   133 533 89  HOH   HOH A . 
E 5 HOH   134 534 55  HOH   HOH A . 
E 5 HOH   135 535 225 HOH   HOH A . 
E 5 HOH   136 536 52  HOH   HOH A . 
E 5 HOH   137 537 106 HOH   HOH A . 
E 5 HOH   138 538 226 HOH   HOH A . 
E 5 HOH   139 539 128 HOH   HOH A . 
E 5 HOH   140 540 49  HOH   HOH A . 
E 5 HOH   141 541 22  HOH   HOH A . 
E 5 HOH   142 542 264 HOH   HOH A . 
E 5 HOH   143 543 9   HOH   HOH A . 
E 5 HOH   144 544 18  HOH   HOH A . 
E 5 HOH   145 545 37  HOH   HOH A . 
E 5 HOH   146 546 214 HOH   HOH A . 
E 5 HOH   147 547 91  HOH   HOH A . 
E 5 HOH   148 548 149 HOH   HOH A . 
E 5 HOH   149 549 230 HOH   HOH A . 
E 5 HOH   150 550 38  HOH   HOH A . 
E 5 HOH   151 551 173 HOH   HOH A . 
E 5 HOH   152 552 269 HOH   HOH A . 
E 5 HOH   153 553 41  HOH   HOH A . 
E 5 HOH   154 554 62  HOH   HOH A . 
E 5 HOH   155 555 284 HOH   HOH A . 
E 5 HOH   156 556 31  HOH   HOH A . 
E 5 HOH   157 557 278 HOH   HOH A . 
E 5 HOH   158 558 28  HOH   HOH A . 
E 5 HOH   159 559 56  HOH   HOH A . 
E 5 HOH   160 560 45  HOH   HOH A . 
E 5 HOH   161 561 46  HOH   HOH A . 
E 5 HOH   162 562 164 HOH   HOH A . 
E 5 HOH   163 563 146 HOH   HOH A . 
E 5 HOH   164 564 12  HOH   HOH A . 
E 5 HOH   165 565 93  HOH   HOH A . 
E 5 HOH   166 566 117 HOH   HOH A . 
E 5 HOH   167 567 220 HOH   HOH A . 
E 5 HOH   168 568 111 HOH   HOH A . 
E 5 HOH   169 569 157 HOH   HOH A . 
E 5 HOH   170 570 71  HOH   HOH A . 
E 5 HOH   171 571 59  HOH   HOH A . 
E 5 HOH   172 572 143 HOH   HOH A . 
E 5 HOH   173 573 25  HOH   HOH A . 
E 5 HOH   174 574 10  HOH   HOH A . 
E 5 HOH   175 575 170 HOH   HOH A . 
E 5 HOH   176 576 132 HOH   HOH A . 
E 5 HOH   177 577 29  HOH   HOH A . 
E 5 HOH   178 578 281 HOH   HOH A . 
E 5 HOH   179 579 184 HOH   HOH A . 
E 5 HOH   180 580 99  HOH   HOH A . 
E 5 HOH   181 581 175 HOH   HOH A . 
E 5 HOH   182 582 120 HOH   HOH A . 
E 5 HOH   183 583 273 HOH   HOH A . 
E 5 HOH   184 584 176 HOH   HOH A . 
E 5 HOH   185 585 138 HOH   HOH A . 
E 5 HOH   186 586 285 HOH   HOH A . 
E 5 HOH   187 587 66  HOH   HOH A . 
E 5 HOH   188 588 21  HOH   HOH A . 
E 5 HOH   189 589 123 HOH   HOH A . 
E 5 HOH   190 590 114 HOH   HOH A . 
E 5 HOH   191 591 97  HOH   HOH A . 
E 5 HOH   192 592 243 HOH   HOH A . 
E 5 HOH   193 593 240 HOH   HOH A . 
E 5 HOH   194 594 94  HOH   HOH A . 
E 5 HOH   195 595 288 HOH   HOH A . 
E 5 HOH   196 596 63  HOH   HOH A . 
E 5 HOH   197 597 130 HOH   HOH A . 
E 5 HOH   198 598 183 HOH   HOH A . 
E 5 HOH   199 599 154 HOH   HOH A . 
E 5 HOH   200 600 276 HOH   HOH A . 
E 5 HOH   201 601 74  HOH   HOH A . 
E 5 HOH   202 602 134 HOH   HOH A . 
E 5 HOH   203 603 218 HOH   HOH A . 
E 5 HOH   204 604 242 HOH   HOH A . 
E 5 HOH   205 605 262 HOH   HOH A . 
E 5 HOH   206 606 112 HOH   HOH A . 
E 5 HOH   207 607 256 HOH   HOH A . 
E 5 HOH   208 608 137 HOH   HOH A . 
E 5 HOH   209 609 131 HOH   HOH A . 
E 5 HOH   210 610 115 HOH   HOH A . 
E 5 HOH   211 611 166 HOH   HOH A . 
E 5 HOH   212 612 216 HOH   HOH A . 
E 5 HOH   213 613 217 HOH   HOH A . 
E 5 HOH   214 614 255 HOH   HOH A . 
E 5 HOH   215 615 35  HOH   HOH A . 
E 5 HOH   216 616 263 HOH   HOH A . 
E 5 HOH   217 617 289 HOH   HOH A . 
E 5 HOH   218 618 253 HOH   HOH A . 
E 5 HOH   219 619 254 HOH   HOH A . 
E 5 HOH   220 620 248 HOH   HOH A . 
E 5 HOH   221 621 36  HOH   HOH A . 
E 5 HOH   222 622 32  HOH   HOH A . 
E 5 HOH   223 623 280 HOH   HOH A . 
E 5 HOH   224 624 266 HOH   HOH A . 
E 5 HOH   225 625 232 HOH   HOH A . 
E 5 HOH   226 626 104 HOH   HOH A . 
E 5 HOH   227 627 126 HOH   HOH A . 
E 5 HOH   228 628 181 HOH   HOH A . 
E 5 HOH   229 629 200 HOH   HOH A . 
E 5 HOH   230 630 177 HOH   HOH A . 
E 5 HOH   231 631 172 HOH   HOH A . 
E 5 HOH   232 632 268 HOH   HOH A . 
E 5 HOH   233 633 239 HOH   HOH A . 
E 5 HOH   234 634 15  HOH   HOH A . 
E 5 HOH   235 635 174 HOH   HOH A . 
E 5 HOH   236 636 207 HOH   HOH A . 
E 5 HOH   237 637 113 HOH   HOH A . 
E 5 HOH   238 638 286 HOH   HOH A . 
E 5 HOH   239 639 222 HOH   HOH A . 
E 5 HOH   240 640 272 HOH   HOH A . 
E 5 HOH   241 641 219 HOH   HOH A . 
E 5 HOH   242 642 213 HOH   HOH A . 
E 5 HOH   243 643 251 HOH   HOH A . 
E 5 HOH   244 644 47  HOH   HOH A . 
E 5 HOH   245 645 84  HOH   HOH A . 
E 5 HOH   246 646 247 HOH   HOH A . 
E 5 HOH   247 647 283 HOH   HOH A . 
E 5 HOH   248 648 236 HOH   HOH A . 
E 5 HOH   249 649 153 HOH   HOH A . 
E 5 HOH   250 650 182 HOH   HOH A . 
E 5 HOH   251 651 270 HOH   HOH A . 
E 5 HOH   252 652 167 HOH   HOH A . 
E 5 HOH   253 653 100 HOH   HOH A . 
E 5 HOH   254 654 65  HOH   HOH A . 
E 5 HOH   255 655 234 HOH   HOH A . 
E 5 HOH   256 656 194 HOH   HOH A . 
E 5 HOH   257 657 274 HOH   HOH A . 
E 5 HOH   258 658 252 HOH   HOH A . 
E 5 HOH   259 659 98  HOH   HOH A . 
E 5 HOH   260 660 224 HOH   HOH A . 
E 5 HOH   261 661 203 HOH   HOH A . 
E 5 HOH   262 662 85  HOH   HOH A . 
E 5 HOH   263 663 201 HOH   HOH A . 
E 5 HOH   264 664 245 HOH   HOH A . 
E 5 HOH   265 665 212 HOH   HOH A . 
E 5 HOH   266 666 187 HOH   HOH A . 
E 5 HOH   267 667 148 HOH   HOH A . 
E 5 HOH   268 668 208 HOH   HOH A . 
E 5 HOH   269 669 249 HOH   HOH A . 
E 5 HOH   270 670 221 HOH   HOH A . 
E 5 HOH   271 671 244 HOH   HOH A . 
E 5 HOH   272 672 209 HOH   HOH A . 
E 5 HOH   273 673 125 HOH   HOH A . 
E 5 HOH   274 674 223 HOH   HOH A . 
E 5 HOH   275 675 257 HOH   HOH A . 
E 5 HOH   276 676 61  HOH   HOH A . 
E 5 HOH   277 677 124 HOH   HOH A . 
E 5 HOH   278 678 258 HOH   HOH A . 
E 5 HOH   279 679 227 HOH   HOH A . 
E 5 HOH   280 680 105 HOH   HOH A . 
E 5 HOH   281 681 168 HOH   HOH A . 
E 5 HOH   282 682 235 HOH   HOH A . 
E 5 HOH   283 683 265 HOH   HOH A . 
E 5 HOH   284 684 189 HOH   HOH A . 
E 5 HOH   285 685 202 HOH   HOH A . 
E 5 HOH   286 686 161 HOH   HOH A . 
E 5 HOH   287 687 179 HOH   HOH A . 
E 5 HOH   288 688 231 HOH   HOH A . 
E 5 HOH   289 689 159 HOH   HOH A . 
E 5 HOH   290 690 151 HOH   HOH A . 
E 5 HOH   291 691 228 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 0 A LYS 9   ? CG A A LYS 9   CG 
2  1 Y 0 A LYS 9   ? CG B A LYS 9   CG 
3  1 Y 0 A LYS 9   ? CD A A LYS 9   CD 
4  1 Y 0 A LYS 9   ? CD B A LYS 9   CD 
5  1 Y 0 A LYS 9   ? CE A A LYS 9   CE 
6  1 Y 0 A LYS 9   ? CE B A LYS 9   CE 
7  1 Y 0 A LYS 9   ? NZ A A LYS 9   NZ 
8  1 Y 0 A LYS 9   ? NZ B A LYS 9   NZ 
9  1 Y 0 A LYS 172 ? CE ? A LYS 171 CE 
10 1 Y 0 A LYS 172 ? NZ ? A LYS 171 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0258                               1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? 'VERSION Jan 10, 2022  BUILT=20220220' 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.4                                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? 11.7.02                                4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.20 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FJQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.188 
_cell.length_a_esd                 ? 
_cell.length_b                     41.323 
_cell.length_b_esd                 ? 
_cell.length_c                     71.913 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9FJQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   9FJQ 
_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             2.06 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.27 
_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              9 
_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    'Bicine pH 9 0.1M, Sodium Malonate pH 7 2M' 
_exptl_crystal_grow.pdbx_pH_range   7-9 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-12-08 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.90500 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.90500 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          11.507 
_reflns.entry_id                                       9FJQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.10 
_reflns.d_resolution_low                               69.72 
_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                                     95773 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       2.8 
_reflns.pdbx_netI_over_sigmaI                          9.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.00 
_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                                0.095 
_reflns.pdbx_Rpim_I_all                                0.036 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.088 
_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                                    1.1 
_reflns_shell.d_res_low                                     1.12 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4478 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.6 
_reflns_shell.pdbx_chi_squared                              1.02 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.085 
_reflns_shell.pdbx_Rpim_I_all                               0.416 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.700 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          92.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.999 
_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]                            -0.79 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.23 
_refine.aniso_B[2][2]                            0.25 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.38 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               20.073 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.979 
_refine.correlation_coeff_Fo_to_Fc_free          0.975 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 9FJQ 
_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                            1.10 
_refine.ls_d_res_low                             40.90 
_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                     86132 
_refine.ls_number_reflns_R_free                  9609 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.13 
_refine.ls_percent_reflns_R_free                 10.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.14804 
_refine.ls_R_factor_R_free                       0.16787 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.14580 
_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                    MASK 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.033 
_refine.pdbx_overall_ESU_R_Free                  0.033 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                            ? 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.10 
_refine_hist.d_res_low                        40.90 
_refine_hist.number_atoms_solvent             291 
_refine_hist.number_atoms_total               2371 
_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        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  0.012  2317 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.820  1.651  3182 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.039  5.000  297  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 33.467 23.982 113  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.534 15.000 378  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 21.682 15.000 7    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.121  0.200  282  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.020  1841 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.912  1.615  1123 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.460  2.443  1428 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.038  1.907  1194 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.005  23.809 3631 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 6.006  3.000  2317 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.100 
_refine_ls_shell.d_res_low                        1.129 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             662 
_refine_ls_shell.number_reflns_R_work             5961 
_refine_ls_shell.percent_reflns_obs               92.01 
_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                  0.235 
_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   20 
_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                  0.245 
# 
_struct.entry_id                     9FJQ 
_struct.title                        
;Structure of human carbonic anhydrase II complexed with 4-benzyl-5,7,8-trifluoro-3,4-dihydro-2H-benzo[b][1,4]thiazine-6-sulfonamide 1,1-dioxide
;
_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        9FJQ 
_struct_keywords.text            'DRUG DESIGN, CARBONIC ANHYDRASE, BENZENESULFONAMIDE, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_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              9FJQ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_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       261 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 220   ? 
1 MORE         1     ? 
1 'SSA (A^2)'  11460 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN    . ZN  ? ? A HIS 94  A ZN    301 1_555 ? ? ? ? ? ? ? 2.001 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN    . ZN  ? ? A HIS 96  A ZN    301 1_555 ? ? ? ? ? ? ? 2.007 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN    . ZN  ? ? A HIS 119 A ZN    301 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 D A1IDL . N10 ? ? A ZN  301 A A1IDL 303 1_555 ? ? ? ? ? ? ? 1.946 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS   96  ? A HIS   96  ? 1_555 103.8 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS   119 ? A HIS   119 ? 1_555 111.3 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS   119 ? A HIS   119 ? 1_555 100.9 ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? D A1IDL .   ? A A1IDL 303 ? 1_555 112.7 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? D A1IDL .   ? A A1IDL 303 ? 1_555 114.7 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? D A1IDL .   ? A A1IDL 303 ? 1_555 112.6 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -2.19 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 11.12 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
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  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
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 ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
_pdbx_entry_details.entry_id                   9FJQ 
_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 ASN A 11  ? ? -149.22 15.45   
2 1 ARG A 27  ? ? -142.73 55.83   
3 1 LYS A 76  ? ? -100.61 -80.10  
4 1 LYS A 111 ? ? 75.42   -5.02   
5 1 PHE A 176 ? ? -150.53 64.19   
6 1 ASN A 244 ? ? -98.94  44.75   
7 1 LYS A 252 ? ? 55.28   -137.58 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1   ? A MET 1   
2 1 Y 1 A SER 2   ? A SER 2   
3 1 Y 1 A LYS 261 ? A LYS 260 
# 
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 
A1IDL C2   C  Y N 1   
A1IDL C3   C  Y N 2   
A1IDL C4   C  Y N 3   
A1IDL C5   C  Y N 4   
A1IDL C6   C  Y N 5   
A1IDL O9   O  N N 6   
A1IDL C16  C  N N 7   
A1IDL C17  C  N N 8   
A1IDL C19  C  Y N 9   
A1IDL C21  C  Y N 10  
A1IDL C24  C  Y N 11  
A1IDL O26  O  N N 12  
A1IDL S15  S  N N 13  
A1IDL O25  O  N N 14  
A1IDL F13  F  N N 15  
A1IDL F12  F  N N 16  
A1IDL S7   S  N N 17  
A1IDL N10  N  N N 18  
A1IDL O8   O  N N 19  
A1IDL N14  N  N N 20  
A1IDL C1   C  Y N 21  
A1IDL F11  F  N N 22  
A1IDL C18  C  N N 23  
A1IDL C20  C  Y N 24  
A1IDL C22  C  Y N 25  
A1IDL C23  C  Y N 26  
A1IDL H1   H  N N 27  
A1IDL H2   H  N N 28  
A1IDL H3   H  N N 29  
A1IDL H4   H  N N 30  
A1IDL H5   H  N N 31  
A1IDL H6   H  N N 32  
A1IDL H7   H  N N 33  
A1IDL H8   H  N N 34  
A1IDL H9   H  N N 35  
A1IDL H10  H  N N 36  
A1IDL H11  H  N N 37  
A1IDL H12  H  N N 38  
A1IDL H13  H  N N 39  
ALA   N    N  N N 40  
ALA   CA   C  N S 41  
ALA   C    C  N N 42  
ALA   O    O  N N 43  
ALA   CB   C  N N 44  
ALA   OXT  O  N N 45  
ALA   H    H  N N 46  
ALA   H2   H  N N 47  
ALA   HA   H  N N 48  
ALA   HB1  H  N N 49  
ALA   HB2  H  N N 50  
ALA   HB3  H  N N 51  
ALA   HXT  H  N N 52  
ARG   N    N  N N 53  
ARG   CA   C  N S 54  
ARG   C    C  N N 55  
ARG   O    O  N N 56  
ARG   CB   C  N N 57  
ARG   CG   C  N N 58  
ARG   CD   C  N N 59  
ARG   NE   N  N N 60  
ARG   CZ   C  N N 61  
ARG   NH1  N  N N 62  
ARG   NH2  N  N N 63  
ARG   OXT  O  N N 64  
ARG   H    H  N N 65  
ARG   H2   H  N N 66  
ARG   HA   H  N N 67  
ARG   HB2  H  N N 68  
ARG   HB3  H  N N 69  
ARG   HG2  H  N N 70  
ARG   HG3  H  N N 71  
ARG   HD2  H  N N 72  
ARG   HD3  H  N N 73  
ARG   HE   H  N N 74  
ARG   HH11 H  N N 75  
ARG   HH12 H  N N 76  
ARG   HH21 H  N N 77  
ARG   HH22 H  N N 78  
ARG   HXT  H  N N 79  
ASN   N    N  N N 80  
ASN   CA   C  N S 81  
ASN   C    C  N N 82  
ASN   O    O  N N 83  
ASN   CB   C  N N 84  
ASN   CG   C  N N 85  
ASN   OD1  O  N N 86  
ASN   ND2  N  N N 87  
ASN   OXT  O  N N 88  
ASN   H    H  N N 89  
ASN   H2   H  N N 90  
ASN   HA   H  N N 91  
ASN   HB2  H  N N 92  
ASN   HB3  H  N N 93  
ASN   HD21 H  N N 94  
ASN   HD22 H  N N 95  
ASN   HXT  H  N N 96  
ASP   N    N  N N 97  
ASP   CA   C  N S 98  
ASP   C    C  N N 99  
ASP   O    O  N N 100 
ASP   CB   C  N N 101 
ASP   CG   C  N N 102 
ASP   OD1  O  N N 103 
ASP   OD2  O  N N 104 
ASP   OXT  O  N N 105 
ASP   H    H  N N 106 
ASP   H2   H  N N 107 
ASP   HA   H  N N 108 
ASP   HB2  H  N N 109 
ASP   HB3  H  N N 110 
ASP   HD2  H  N N 111 
ASP   HXT  H  N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
DMS   S    S  N N 127 
DMS   O    O  N N 128 
DMS   C1   C  N N 129 
DMS   C2   C  N N 130 
DMS   H11  H  N N 131 
DMS   H12  H  N N 132 
DMS   H13  H  N N 133 
DMS   H21  H  N N 134 
DMS   H22  H  N N 135 
DMS   H23  H  N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
HIS   N    N  N N 186 
HIS   CA   C  N S 187 
HIS   C    C  N N 188 
HIS   O    O  N N 189 
HIS   CB   C  N N 190 
HIS   CG   C  Y N 191 
HIS   ND1  N  Y N 192 
HIS   CD2  C  Y N 193 
HIS   CE1  C  Y N 194 
HIS   NE2  N  Y N 195 
HIS   OXT  O  N N 196 
HIS   H    H  N N 197 
HIS   H2   H  N N 198 
HIS   HA   H  N N 199 
HIS   HB2  H  N N 200 
HIS   HB3  H  N N 201 
HIS   HD1  H  N N 202 
HIS   HD2  H  N N 203 
HIS   HE1  H  N N 204 
HIS   HE2  H  N N 205 
HIS   HXT  H  N N 206 
HOH   O    O  N N 207 
HOH   H1   H  N N 208 
HOH   H2   H  N N 209 
ILE   N    N  N N 210 
ILE   CA   C  N S 211 
ILE   C    C  N N 212 
ILE   O    O  N N 213 
ILE   CB   C  N S 214 
ILE   CG1  C  N N 215 
ILE   CG2  C  N N 216 
ILE   CD1  C  N N 217 
ILE   OXT  O  N N 218 
ILE   H    H  N N 219 
ILE   H2   H  N N 220 
ILE   HA   H  N N 221 
ILE   HB   H  N N 222 
ILE   HG12 H  N N 223 
ILE   HG13 H  N N 224 
ILE   HG21 H  N N 225 
ILE   HG22 H  N N 226 
ILE   HG23 H  N N 227 
ILE   HD11 H  N N 228 
ILE   HD12 H  N N 229 
ILE   HD13 H  N N 230 
ILE   HXT  H  N N 231 
LEU   N    N  N N 232 
LEU   CA   C  N S 233 
LEU   C    C  N N 234 
LEU   O    O  N N 235 
LEU   CB   C  N N 236 
LEU   CG   C  N N 237 
LEU   CD1  C  N N 238 
LEU   CD2  C  N N 239 
LEU   OXT  O  N N 240 
LEU   H    H  N N 241 
LEU   H2   H  N N 242 
LEU   HA   H  N N 243 
LEU   HB2  H  N N 244 
LEU   HB3  H  N N 245 
LEU   HG   H  N N 246 
LEU   HD11 H  N N 247 
LEU   HD12 H  N N 248 
LEU   HD13 H  N N 249 
LEU   HD21 H  N N 250 
LEU   HD22 H  N N 251 
LEU   HD23 H  N N 252 
LEU   HXT  H  N N 253 
LYS   N    N  N N 254 
LYS   CA   C  N S 255 
LYS   C    C  N N 256 
LYS   O    O  N N 257 
LYS   CB   C  N N 258 
LYS   CG   C  N N 259 
LYS   CD   C  N N 260 
LYS   CE   C  N N 261 
LYS   NZ   N  N N 262 
LYS   OXT  O  N N 263 
LYS   H    H  N N 264 
LYS   H2   H  N N 265 
LYS   HA   H  N N 266 
LYS   HB2  H  N N 267 
LYS   HB3  H  N N 268 
LYS   HG2  H  N N 269 
LYS   HG3  H  N N 270 
LYS   HD2  H  N N 271 
LYS   HD3  H  N N 272 
LYS   HE2  H  N N 273 
LYS   HE3  H  N N 274 
LYS   HZ1  H  N N 275 
LYS   HZ2  H  N N 276 
LYS   HZ3  H  N N 277 
LYS   HXT  H  N N 278 
MET   N    N  N N 279 
MET   CA   C  N S 280 
MET   C    C  N N 281 
MET   O    O  N N 282 
MET   CB   C  N N 283 
MET   CG   C  N N 284 
MET   SD   S  N N 285 
MET   CE   C  N N 286 
MET   OXT  O  N N 287 
MET   H    H  N N 288 
MET   H2   H  N N 289 
MET   HA   H  N N 290 
MET   HB2  H  N N 291 
MET   HB3  H  N N 292 
MET   HG2  H  N N 293 
MET   HG3  H  N N 294 
MET   HE1  H  N N 295 
MET   HE2  H  N N 296 
MET   HE3  H  N N 297 
MET   HXT  H  N N 298 
PHE   N    N  N N 299 
PHE   CA   C  N S 300 
PHE   C    C  N N 301 
PHE   O    O  N N 302 
PHE   CB   C  N N 303 
PHE   CG   C  Y N 304 
PHE   CD1  C  Y N 305 
PHE   CD2  C  Y N 306 
PHE   CE1  C  Y N 307 
PHE   CE2  C  Y N 308 
PHE   CZ   C  Y N 309 
PHE   OXT  O  N N 310 
PHE   H    H  N N 311 
PHE   H2   H  N N 312 
PHE   HA   H  N N 313 
PHE   HB2  H  N N 314 
PHE   HB3  H  N N 315 
PHE   HD1  H  N N 316 
PHE   HD2  H  N N 317 
PHE   HE1  H  N N 318 
PHE   HE2  H  N N 319 
PHE   HZ   H  N N 320 
PHE   HXT  H  N N 321 
PRO   N    N  N N 322 
PRO   CA   C  N S 323 
PRO   C    C  N N 324 
PRO   O    O  N N 325 
PRO   CB   C  N N 326 
PRO   CG   C  N N 327 
PRO   CD   C  N N 328 
PRO   OXT  O  N N 329 
PRO   H    H  N N 330 
PRO   HA   H  N N 331 
PRO   HB2  H  N N 332 
PRO   HB3  H  N N 333 
PRO   HG2  H  N N 334 
PRO   HG3  H  N N 335 
PRO   HD2  H  N N 336 
PRO   HD3  H  N N 337 
PRO   HXT  H  N N 338 
SER   N    N  N N 339 
SER   CA   C  N S 340 
SER   C    C  N N 341 
SER   O    O  N N 342 
SER   CB   C  N N 343 
SER   OG   O  N N 344 
SER   OXT  O  N N 345 
SER   H    H  N N 346 
SER   H2   H  N N 347 
SER   HA   H  N N 348 
SER   HB2  H  N N 349 
SER   HB3  H  N N 350 
SER   HG   H  N N 351 
SER   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TRP   N    N  N N 370 
TRP   CA   C  N S 371 
TRP   C    C  N N 372 
TRP   O    O  N N 373 
TRP   CB   C  N N 374 
TRP   CG   C  Y N 375 
TRP   CD1  C  Y N 376 
TRP   CD2  C  Y N 377 
TRP   NE1  N  Y N 378 
TRP   CE2  C  Y N 379 
TRP   CE3  C  Y N 380 
TRP   CZ2  C  Y N 381 
TRP   CZ3  C  Y N 382 
TRP   CH2  C  Y N 383 
TRP   OXT  O  N N 384 
TRP   H    H  N N 385 
TRP   H2   H  N N 386 
TRP   HA   H  N N 387 
TRP   HB2  H  N N 388 
TRP   HB3  H  N N 389 
TRP   HD1  H  N N 390 
TRP   HE1  H  N N 391 
TRP   HE3  H  N N 392 
TRP   HZ2  H  N N 393 
TRP   HZ3  H  N N 394 
TRP   HH2  H  N N 395 
TRP   HXT  H  N N 396 
TYR   N    N  N N 397 
TYR   CA   C  N S 398 
TYR   C    C  N N 399 
TYR   O    O  N N 400 
TYR   CB   C  N N 401 
TYR   CG   C  Y N 402 
TYR   CD1  C  Y N 403 
TYR   CD2  C  Y N 404 
TYR   CE1  C  Y N 405 
TYR   CE2  C  Y N 406 
TYR   CZ   C  Y N 407 
TYR   OH   O  N N 408 
TYR   OXT  O  N N 409 
TYR   H    H  N N 410 
TYR   H2   H  N N 411 
TYR   HA   H  N N 412 
TYR   HB2  H  N N 413 
TYR   HB3  H  N N 414 
TYR   HD1  H  N N 415 
TYR   HD2  H  N N 416 
TYR   HE1  H  N N 417 
TYR   HE2  H  N N 418 
TYR   HH   H  N N 419 
TYR   HXT  H  N N 420 
VAL   N    N  N N 421 
VAL   CA   C  N S 422 
VAL   C    C  N N 423 
VAL   O    O  N N 424 
VAL   CB   C  N N 425 
VAL   CG1  C  N N 426 
VAL   CG2  C  N N 427 
VAL   OXT  O  N N 428 
VAL   H    H  N N 429 
VAL   H2   H  N N 430 
VAL   HA   H  N N 431 
VAL   HB   H  N N 432 
VAL   HG11 H  N N 433 
VAL   HG12 H  N N 434 
VAL   HG13 H  N N 435 
VAL   HG21 H  N N 436 
VAL   HG22 H  N N 437 
VAL   HG23 H  N N 438 
VAL   HXT  H  N N 439 
ZN    ZN   ZN N N 440 
# 
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 
A1IDL C22 C21  doub Y N 1   
A1IDL C22 C23  sing Y N 2   
A1IDL C21 C20  sing Y N 3   
A1IDL C23 C19  doub Y N 4   
A1IDL C16 C17  sing N N 5   
A1IDL C16 S15  sing N N 6   
A1IDL C20 C24  doub Y N 7   
A1IDL C17 N14  sing N N 8   
A1IDL C19 C24  sing Y N 9   
A1IDL C19 C18  sing N N 10  
A1IDL C18 N14  sing N N 11  
A1IDL N14 C6   sing N N 12  
A1IDL O26 S15  doub N N 13  
A1IDL S15 O25  doub N N 14  
A1IDL S15 C5   sing N N 15  
A1IDL C6  C5   doub Y N 16  
A1IDL C6  C1   sing Y N 17  
A1IDL C5  C4   sing Y N 18  
A1IDL F11 C1   sing N N 19  
A1IDL C1  C2   doub Y N 20  
A1IDL C4  F13  sing N N 21  
A1IDL C4  C3   doub Y N 22  
A1IDL C2  C3   sing Y N 23  
A1IDL C2  S7   sing N N 24  
A1IDL C3  F12  sing N N 25  
A1IDL N10 S7   sing N N 26  
A1IDL S7  O9   doub N N 27  
A1IDL S7  O8   doub N N 28  
A1IDL C16 H1   sing N N 29  
A1IDL C16 H2   sing N N 30  
A1IDL C17 H3   sing N N 31  
A1IDL C17 H4   sing N N 32  
A1IDL C21 H5   sing N N 33  
A1IDL C24 H6   sing N N 34  
A1IDL N10 H7   sing N N 35  
A1IDL N10 H8   sing N N 36  
A1IDL C18 H9   sing N N 37  
A1IDL C18 H10  sing N N 38  
A1IDL C20 H11  sing N N 39  
A1IDL C22 H12  sing N N 40  
A1IDL C23 H13  sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
DMS   S   O    doub N N 124 
DMS   S   C1   sing N N 125 
DMS   S   C2   sing N N 126 
DMS   C1  H11  sing N N 127 
DMS   C1  H12  sing N N 128 
DMS   C1  H13  sing N N 129 
DMS   C2  H21  sing N N 130 
DMS   C2  H22  sing N N 131 
DMS   C2  H23  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
THR   N   CA   sing N N 340 
THR   N   H    sing N N 341 
THR   N   H2   sing N N 342 
THR   CA  C    sing N N 343 
THR   CA  CB   sing N N 344 
THR   CA  HA   sing N N 345 
THR   C   O    doub N N 346 
THR   C   OXT  sing N N 347 
THR   CB  OG1  sing N N 348 
THR   CB  CG2  sing N N 349 
THR   CB  HB   sing N N 350 
THR   OG1 HG1  sing N N 351 
THR   CG2 HG21 sing N N 352 
THR   CG2 HG22 sing N N 353 
THR   CG2 HG23 sing N N 354 
THR   OXT HXT  sing N N 355 
TRP   N   CA   sing N N 356 
TRP   N   H    sing N N 357 
TRP   N   H2   sing N N 358 
TRP   CA  C    sing N N 359 
TRP   CA  CB   sing N N 360 
TRP   CA  HA   sing N N 361 
TRP   C   O    doub N N 362 
TRP   C   OXT  sing N N 363 
TRP   CB  CG   sing N N 364 
TRP   CB  HB2  sing N N 365 
TRP   CB  HB3  sing N N 366 
TRP   CG  CD1  doub Y N 367 
TRP   CG  CD2  sing Y N 368 
TRP   CD1 NE1  sing Y N 369 
TRP   CD1 HD1  sing N N 370 
TRP   CD2 CE2  doub Y N 371 
TRP   CD2 CE3  sing Y N 372 
TRP   NE1 CE2  sing Y N 373 
TRP   NE1 HE1  sing N N 374 
TRP   CE2 CZ2  sing Y N 375 
TRP   CE3 CZ3  doub Y N 376 
TRP   CE3 HE3  sing N N 377 
TRP   CZ2 CH2  doub Y N 378 
TRP   CZ2 HZ2  sing N N 379 
TRP   CZ3 CH2  sing Y N 380 
TRP   CZ3 HZ3  sing N N 381 
TRP   CH2 HH2  sing N N 382 
TRP   OXT HXT  sing N N 383 
TYR   N   CA   sing N N 384 
TYR   N   H    sing N N 385 
TYR   N   H2   sing N N 386 
TYR   CA  C    sing N N 387 
TYR   CA  CB   sing N N 388 
TYR   CA  HA   sing N N 389 
TYR   C   O    doub N N 390 
TYR   C   OXT  sing N N 391 
TYR   CB  CG   sing N N 392 
TYR   CB  HB2  sing N N 393 
TYR   CB  HB3  sing N N 394 
TYR   CG  CD1  doub Y N 395 
TYR   CG  CD2  sing Y N 396 
TYR   CD1 CE1  sing Y N 397 
TYR   CD1 HD1  sing N N 398 
TYR   CD2 CE2  doub Y N 399 
TYR   CD2 HD2  sing N N 400 
TYR   CE1 CZ   doub Y N 401 
TYR   CE1 HE1  sing N N 402 
TYR   CE2 CZ   sing Y N 403 
TYR   CE2 HE2  sing N N 404 
TYR   CZ  OH   sing N N 405 
TYR   OH  HH   sing N N 406 
TYR   OXT HXT  sing N N 407 
VAL   N   CA   sing N N 408 
VAL   N   H    sing N N 409 
VAL   N   H2   sing N N 410 
VAL   CA  C    sing N N 411 
VAL   CA  CB   sing N N 412 
VAL   CA  HA   sing N N 413 
VAL   C   O    doub N N 414 
VAL   C   OXT  sing N N 415 
VAL   CB  CG1  sing N N 416 
VAL   CB  CG2  sing N N 417 
VAL   CB  HB   sing N N 418 
VAL   CG1 HG11 sing N N 419 
VAL   CG1 HG12 sing N N 420 
VAL   CG1 HG13 sing N N 421 
VAL   CG2 HG21 sing N N 422 
VAL   CG2 HG22 sing N N 423 
VAL   CG2 HG23 sing N N 424 
VAL   OXT HXT  sing N N 425 
# 
_pdbx_audit_support.funding_organization   iNEXT-Discovery 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           871037 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8RJ2 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9FJQ 
_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]   0.023703 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005998 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024200 
_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]   0.014344 
_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  
F  
N  
O  
S  
ZN 
# 
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 3   ? 34.864  1.723   6.531   1.00 27.76  ? 3   HIS   A N   1 
ATOM   2    C  CA  . HIS   A 1 3   ? 34.525  0.759   7.625   1.00 29.41  ? 3   HIS   A CA  1 
ATOM   3    C  C   . HIS   A 1 3   ? 33.450  1.325   8.565   1.00 31.84  ? 3   HIS   A C   1 
ATOM   4    O  O   . HIS   A 1 3   ? 33.735  1.626   9.729   1.00 35.96  ? 3   HIS   A O   1 
ATOM   5    C  CB  . HIS   A 1 3   ? 35.782  0.387   8.423   1.00 29.55  ? 3   HIS   A CB  1 
ATOM   6    C  CG  . HIS   A 1 3   ? 35.548  -0.809  9.284   1.00 31.56  ? 3   HIS   A CG  1 
ATOM   7    N  ND1 . HIS   A 1 3   ? 35.643  -2.103  8.783   1.00 34.36  ? 3   HIS   A ND1 1 
ATOM   8    C  CD2 . HIS   A 1 3   ? 35.242  -0.919  10.600  1.00 31.99  ? 3   HIS   A CD2 1 
ATOM   9    C  CE1 . HIS   A 1 3   ? 35.407  -2.957  9.761   1.00 38.91  ? 3   HIS   A CE1 1 
ATOM   10   N  NE2 . HIS   A 1 3   ? 35.161  -2.257  10.886  1.00 34.20  ? 3   HIS   A NE2 1 
ATOM   11   N  N   . HIS   A 1 4   ? 32.219  1.484   8.055   1.00 38.34  ? 4   HIS   A N   1 
ATOM   12   C  CA  . HIS   A 1 4   ? 31.162  2.066   8.862   1.00 64.98  ? 4   HIS   A CA  1 
ATOM   13   C  C   . HIS   A 1 4   ? 30.466  0.955   9.621   1.00 27.71  ? 4   HIS   A C   1 
ATOM   14   O  O   . HIS   A 1 4   ? 30.608  -0.234  9.318   1.00 24.67  ? 4   HIS   A O   1 
ATOM   15   C  CB  . HIS   A 1 4   ? 30.213  2.932   8.022   1.00 83.49  ? 4   HIS   A CB  1 
ATOM   16   C  CG  . HIS   A 1 4   ? 30.816  4.268   7.721   1.00 119.51 ? 4   HIS   A CG  1 
ATOM   17   N  ND1 . HIS   A 1 4   ? 31.220  5.123   8.739   1.00 110.89 ? 4   HIS   A ND1 1 
ATOM   18   C  CD2 . HIS   A 1 4   ? 31.063  4.891   6.519   1.00 122.67 ? 4   HIS   A CD2 1 
ATOM   19   C  CE1 . HIS   A 1 4   ? 31.735  6.213   8.199   1.00 99.04  ? 4   HIS   A CE1 1 
ATOM   20   N  NE2 . HIS   A 1 4   ? 31.668  6.105   6.841   1.00 112.01 ? 4   HIS   A NE2 1 
ATOM   21   N  N   . TRP   A 1 5   ? 29.666  1.371   10.586  1.00 24.07  ? 5   TRP   A N   1 
ATOM   22   C  CA  . TRP   A 1 5   ? 28.930  0.399   11.380  1.00 19.83  ? 5   TRP   A CA  1 
ATOM   23   C  C   . TRP   A 1 5   ? 27.921  -0.398  10.558  1.00 19.54  ? 5   TRP   A C   1 
ATOM   24   O  O   . TRP   A 1 5   ? 27.381  0.075   9.556   1.00 19.32  ? 5   TRP   A O   1 
ATOM   25   C  CB  . TRP   A 1 5   ? 28.230  1.121   12.539  1.00 19.86  ? 5   TRP   A CB  1 
ATOM   26   C  CG  . TRP   A 1 5   ? 27.022  1.935   12.166  1.00 18.38  ? 5   TRP   A CG  1 
ATOM   27   C  CD1 . TRP   A 1 5   ? 26.959  3.273   11.865  1.00 21.05  ? 5   TRP   A CD1 1 
ATOM   28   C  CD2 . TRP   A 1 5   ? 25.672  1.450   12.144  1.00 17.60  ? 5   TRP   A CD2 1 
ATOM   29   N  NE1 . TRP   A 1 5   ? 25.663  3.647   11.611  1.00 21.97  ? 5   TRP   A NE1 1 
ATOM   30   C  CE2 . TRP   A 1 5   ? 24.854  2.546   11.772  1.00 19.31  ? 5   TRP   A CE2 1 
ATOM   31   C  CE3 . TRP   A 1 5   ? 25.081  0.209   12.391  1.00 17.82  ? 5   TRP   A CE3 1 
ATOM   32   C  CZ2 . TRP   A 1 5   ? 23.467  2.430   11.656  1.00 20.64  ? 5   TRP   A CZ2 1 
ATOM   33   C  CZ3 . TRP   A 1 5   ? 23.714  0.096   12.273  1.00 18.98  ? 5   TRP   A CZ3 1 
ATOM   34   C  CH2 . TRP   A 1 5   ? 22.915  1.191   11.917  1.00 20.10  ? 5   TRP   A CH2 1 
ATOM   35   N  N   . GLY   A 1 6   ? 27.618  -1.593  11.041  1.00 17.08  ? 6   GLY   A N   1 
ATOM   36   C  CA  . GLY   A 1 6   ? 26.563  -2.375  10.425  1.00 17.43  ? 6   GLY   A CA  1 
ATOM   37   C  C   . GLY   A 1 6   ? 26.169  -3.498  11.372  1.00 16.68  ? 6   GLY   A C   1 
ATOM   38   O  O   . GLY   A 1 6   ? 26.225  -3.360  12.595  1.00 16.23  ? 6   GLY   A O   1 
ATOM   39   N  N   . TYR   A 1 7   ? 25.881  -4.655  10.763  1.00 19.39  ? 7   TYR   A N   1 
ATOM   40   C  CA  . TYR   A 1 7   ? 25.419  -5.804  11.535  1.00 19.47  ? 7   TYR   A CA  1 
ATOM   41   C  C   . TYR   A 1 7   ? 26.287  -7.057  11.334  1.00 23.93  ? 7   TYR   A C   1 
ATOM   42   O  O   . TYR   A 1 7   ? 25.887  -8.154  11.730  1.00 33.21  ? 7   TYR   A O   1 
ATOM   43   C  CB  . TYR   A 1 7   ? 23.938  -6.085  11.246  1.00 18.96  ? 7   TYR   A CB  1 
ATOM   44   C  CG  . TYR   A 1 7   ? 23.050  -4.989  11.786  1.00 15.26  ? 7   TYR   A CG  1 
ATOM   45   C  CD1 . TYR   A 1 7   ? 22.655  -5.027  13.117  1.00 14.72  ? 7   TYR   A CD1 1 
ATOM   46   C  CD2 . TYR   A 1 7   ? 22.625  -3.948  10.997  1.00 16.81  ? 7   TYR   A CD2 1 
ATOM   47   C  CE1 . TYR   A 1 7   ? 21.842  -4.019  13.643  1.00 13.18  ? 7   TYR   A CE1 1 
ATOM   48   C  CE2 . TYR   A 1 7   ? 21.814  -2.950  11.499  1.00 15.76  ? 7   TYR   A CE2 1 
ATOM   49   C  CZ  . TYR   A 1 7   ? 21.416  -2.988  12.828  1.00 14.21  ? 7   TYR   A CZ  1 
ATOM   50   O  OH  . TYR   A 1 7   ? 20.604  -1.999  13.286  1.00 15.41  ? 7   TYR   A OH  1 
ATOM   51   N  N   . GLY   A 1 8   ? 27.504  -6.922  10.771  1.00 25.97  ? 8   GLY   A N   1 
ATOM   52   C  CA  . GLY   A 1 8   ? 28.378  -8.092  10.563  1.00 28.62  ? 8   GLY   A CA  1 
ATOM   53   C  C   . GLY   A 1 8   ? 29.398  -8.368  11.677  1.00 27.70  ? 8   GLY   A C   1 
ATOM   54   O  O   . GLY   A 1 8   ? 29.484  -7.653  12.662  1.00 27.47  ? 8   GLY   A O   1 
ATOM   55   N  N   A LYS   A 1 9   ? 29.982  -9.558  11.498  0.50 33.93  ? 9   LYS   A N   1 
ATOM   56   N  N   B LYS   A 1 9   ? 30.382  -9.271  11.507  0.50 21.72  ? 9   LYS   A N   1 
ATOM   57   C  CA  A LYS   A 1 9   ? 31.194  -9.981  12.160  0.50 33.65  ? 9   LYS   A CA  1 
ATOM   58   C  CA  B LYS   A 1 9   ? 31.309  -9.647  12.588  0.50 25.50  ? 9   LYS   A CA  1 
ATOM   59   C  C   A LYS   A 1 9   ? 32.105  -8.768  12.201  0.50 26.52  ? 9   LYS   A C   1 
ATOM   60   C  C   B LYS   A 1 9   ? 32.345  -8.575  12.921  0.50 20.17  ? 9   LYS   A C   1 
ATOM   61   O  O   A LYS   A 1 9   ? 32.678  -8.487  13.250  0.50 32.17  ? 9   LYS   A O   1 
ATOM   62   O  O   B LYS   A 1 9   ? 32.850  -8.532  14.073  0.50 20.37  ? 9   LYS   A O   1 
ATOM   63   C  CB  A LYS   A 1 9   ? 31.850  -11.153 11.417  0.50 30.39  ? 9   LYS   A CB  1 
ATOM   64   C  CB  B LYS   A 1 9   ? 32.245  -10.773 12.145  0.50 23.28  ? 9   LYS   A CB  1 
ATOM   65   C  CG  A LYS   A 1 9   ? 33.019  -11.836 12.116  0.00 10.00  ? 9   LYS   A CG  1 
ATOM   66   C  CG  B LYS   A 1 9   ? 31.578  -12.116 11.886  0.00 10.00  ? 9   LYS   A CG  1 
ATOM   67   C  CD  A LYS   A 1 9   ? 33.551  -13.080 11.437  0.00 10.00  ? 9   LYS   A CD  1 
ATOM   68   C  CD  B LYS   A 1 9   ? 32.371  -12.996 10.944  0.00 10.00  ? 9   LYS   A CD  1 
ATOM   69   C  CE  A LYS   A 1 9   ? 34.762  -13.665 12.131  0.00 10.00  ? 9   LYS   A CE  1 
ATOM   70   C  CE  B LYS   A 1 9   ? 31.514  -14.015 10.223  0.00 10.00  ? 9   LYS   A CE  1 
ATOM   71   N  NZ  A LYS   A 1 9   ? 35.256  -14.880 11.441  0.00 10.00  ? 9   LYS   A NZ  1 
ATOM   72   N  NZ  B LYS   A 1 9   ? 32.022  -15.394 10.415  0.00 10.00  ? 9   LYS   A NZ  1 
ATOM   73   N  N   A HIS   A 1 10  ? 32.188  -8.012  11.095  0.50 17.51  ? 10  HIS   A N   1 
ATOM   74   N  N   B HIS   A 1 10  ? 32.760  -7.830  11.922  0.50 18.31  ? 10  HIS   A N   1 
ATOM   75   C  CA  A HIS   A 1 10  ? 33.300  -7.081  11.137  0.50 20.08  ? 10  HIS   A CA  1 
ATOM   76   C  CA  B HIS   A 1 10  ? 33.768  -6.807  12.047  0.50 17.76  ? 10  HIS   A CA  1 
ATOM   77   C  C   A HIS   A 1 10  ? 33.015  -5.739  11.816  0.50 22.78  ? 10  HIS   A C   1 
ATOM   78   C  C   B HIS   A 1 10  ? 33.072  -5.455  12.161  0.50 20.84  ? 10  HIS   A C   1 
ATOM   79   O  O   A HIS   A 1 10  ? 33.933  -5.102  12.311  0.50 23.43  ? 10  HIS   A O   1 
ATOM   80   O  O   B HIS   A 1 10  ? 33.760  -4.478  12.445  0.50 23.54  ? 10  HIS   A O   1 
ATOM   81   C  CB  A HIS   A 1 10  ? 34.099  -7.078  9.840   0.50 20.11  ? 10  HIS   A CB  1 
ATOM   82   C  CB  B HIS   A 1 10  ? 34.697  -6.855  10.829  0.50 17.65  ? 10  HIS   A CB  1 
ATOM   83   C  CG  A HIS   A 1 10  ? 34.634  -8.441  9.541   0.50 20.13  ? 10  HIS   A CG  1 
ATOM   84   C  CG  B HIS   A 1 10  ? 35.439  -8.145  10.780  0.50 17.28  ? 10  HIS   A CG  1 
ATOM   85   N  ND1 A HIS   A 1 10  ? 35.634  -9.038  10.301  0.50 21.49  ? 10  HIS   A ND1 1 
ATOM   86   N  ND1 B HIS   A 1 10  ? 35.104  -9.174  9.910   0.50 19.56  ? 10  HIS   A ND1 1 
ATOM   87   C  CD2 A HIS   A 1 10  ? 34.294  -9.337  8.588   0.50 19.58  ? 10  HIS   A CD2 1 
ATOM   88   C  CD2 B HIS   A 1 10  ? 36.469  -8.602  11.531  0.50 17.09  ? 10  HIS   A CD2 1 
ATOM   89   C  CE1 A HIS   A 1 10  ? 35.888  -10.239 9.812   0.50 20.33  ? 10  HIS   A CE1 1 
ATOM   90   C  CE1 B HIS   A 1 10  ? 35.916  -10.197 10.113  0.50 19.29  ? 10  HIS   A CE1 1 
ATOM   91   N  NE2 A HIS   A 1 10  ? 35.078  -10.444 8.753   0.50 22.08  ? 10  HIS   A NE2 1 
ATOM   92   N  NE2 B HIS   A 1 10  ? 36.767  -9.863  11.100  0.50 20.23  ? 10  HIS   A NE2 1 
ATOM   93   N  N   . ASN   A 1 11  ? 31.739  -5.366  11.914  1.00 23.25  ? 11  ASN   A N   1 
ATOM   94   C  CA  . ASN   A 1 11  ? 31.238  -4.013  12.132  1.00 21.28  ? 11  ASN   A CA  1 
ATOM   95   C  C   . ASN   A 1 11  ? 29.920  -3.995  12.911  1.00 19.89  ? 11  ASN   A C   1 
ATOM   96   O  O   . ASN   A 1 11  ? 29.309  -2.949  13.052  1.00 19.85  ? 11  ASN   A O   1 
ATOM   97   C  CB  . ASN   A 1 11  ? 31.043  -3.240  10.830  1.00 20.57  ? 11  ASN   A CB  1 
ATOM   98   C  CG  . ASN   A 1 11  ? 29.955  -3.825  9.957   1.00 21.27  ? 11  ASN   A CG  1 
ATOM   99   O  OD1 . ASN   A 1 11  ? 29.376  -4.856  10.290  1.00 24.66  ? 11  ASN   A OD1 1 
ATOM   100  N  ND2 . ASN   A 1 11  ? 29.651  -3.185  8.842   1.00 22.93  ? 11  ASN   A ND2 1 
ATOM   101  N  N   . GLY   A 1 12  ? 29.570  -5.104  13.547  1.00 19.18  ? 12  GLY   A N   1 
ATOM   102  C  CA  . GLY   A 1 12  ? 28.258  -5.217  14.183  1.00 18.45  ? 12  GLY   A CA  1 
ATOM   103  C  C   . GLY   A 1 12  ? 28.270  -4.712  15.607  1.00 16.65  ? 12  GLY   A C   1 
ATOM   104  O  O   . GLY   A 1 12  ? 29.184  -4.025  16.068  1.00 17.49  ? 12  GLY   A O   1 
ATOM   105  N  N   . PRO   A 1 13  ? 27.173  -5.005  16.330  1.00 15.52  ? 13  PRO   A N   1 
ATOM   106  C  CA  . PRO   A 1 13  ? 26.938  -4.445  17.662  1.00 15.82  ? 13  PRO   A CA  1 
ATOM   107  C  C   . PRO   A 1 13  ? 28.097  -4.465  18.642  1.00 15.67  ? 13  PRO   A C   1 
ATOM   108  O  O   . PRO   A 1 13  ? 28.237  -3.499  19.401  1.00 17.66  ? 13  PRO   A O   1 
ATOM   109  C  CB  . PRO   A 1 13  ? 25.749  -5.253  18.193  1.00 17.11  ? 13  PRO   A CB  1 
ATOM   110  C  CG  . PRO   A 1 13  ? 24.959  -5.472  16.919  1.00 16.68  ? 13  PRO   A CG  1 
ATOM   111  C  CD  . PRO   A 1 13  ? 25.996  -5.739  15.842  1.00 16.77  ? 13  PRO   A CD  1 
ATOM   112  N  N   . GLU   A 1 14  ? 28.951  -5.512  18.614  1.00 16.99  ? 14  GLU   A N   1 
ATOM   113  C  CA  . GLU   A 1 14  ? 30.080  -5.606  19.545  1.00 20.08  ? 14  GLU   A CA  1 
ATOM   114  C  C   . GLU   A 1 14  ? 31.165  -4.564  19.246  1.00 17.15  ? 14  GLU   A C   1 
ATOM   115  O  O   . GLU   A 1 14  ? 32.053  -4.350  20.080  1.00 19.57  ? 14  GLU   A O   1 
ATOM   116  C  CB  . GLU   A 1 14  ? 30.730  -7.004  19.511  1.00 27.69  ? 14  GLU   A CB  1 
ATOM   117  C  CG  . GLU   A 1 14  ? 29.819  -8.100  20.012  1.00 35.55  ? 14  GLU   A CG  1 
ATOM   118  C  CD  . GLU   A 1 14  ? 29.660  -8.169  21.523  1.00 45.13  ? 14  GLU   A CD  1 
ATOM   119  O  OE1 . GLU   A 1 14  ? 30.487  -7.573  22.235  1.00 53.52  ? 14  GLU   A OE1 1 
ATOM   120  O  OE2 . GLU   A 1 14  ? 28.727  -8.840  21.989  1.00 50.07  ? 14  GLU   A OE2 1 
ATOM   121  N  N   . HIS   A 1 15  ? 31.108  -3.980  18.049  1.00 16.30  ? 15  HIS   A N   1 
ATOM   122  C  CA  . HIS   A 1 15  ? 32.104  -3.005  17.634  1.00 16.85  ? 15  HIS   A CA  1 
ATOM   123  C  C   . HIS   A 1 15  ? 31.640  -1.556  17.821  1.00 15.10  ? 15  HIS   A C   1 
ATOM   124  O  O   . HIS   A 1 15  ? 32.460  -0.635  17.783  1.00 17.54  ? 15  HIS   A O   1 
ATOM   125  C  CB  . HIS   A 1 15  ? 32.432  -3.178  16.161  1.00 17.78  ? 15  HIS   A CB  1 
ATOM   126  C  CG  . HIS   A 1 15  ? 33.147  -4.441  15.898  1.00 19.78  ? 15  HIS   A CG  1 
ATOM   127  N  ND1 . HIS   A 1 15  ? 34.538  -4.511  15.949  1.00 21.94  ? 15  HIS   A ND1 1 
ATOM   128  C  CD2 . HIS   A 1 15  ? 32.698  -5.672  15.589  1.00 21.45  ? 15  HIS   A CD2 1 
ATOM   129  C  CE1 . HIS   A 1 15  ? 34.912  -5.747  15.671  1.00 26.23  ? 15  HIS   A CE1 1 
ATOM   130  N  NE2 . HIS   A 1 15  ? 33.812  -6.488  15.460  1.00 26.47  ? 15  HIS   A NE2 1 
ATOM   131  N  N   . TRP   A 1 16  ? 30.328  -1.331  17.989  1.00 14.79  ? 16  TRP   A N   1 
ATOM   132  C  CA  . TRP   A 1 16  ? 29.798  0.012   17.871  1.00 14.52  ? 16  TRP   A CA  1 
ATOM   133  C  C   . TRP   A 1 16  ? 30.385  0.980   18.900  1.00 14.69  ? 16  TRP   A C   1 
ATOM   134  O  O   . TRP   A 1 16  ? 30.479  2.178   18.645  1.00 14.97  ? 16  TRP   A O   1 
ATOM   135  C  CB  . TRP   A 1 16  ? 28.266  -0.028  18.008  1.00 14.72  ? 16  TRP   A CB  1 
ATOM   136  C  CG  . TRP   A 1 16  ? 27.577  -0.709  16.865  1.00 13.79  ? 16  TRP   A CG  1 
ATOM   137  C  CD1 . TRP   A 1 16  ? 28.101  -1.124  15.679  1.00 14.84  ? 16  TRP   A CD1 1 
ATOM   138  C  CD2 . TRP   A 1 16  ? 26.171  -1.025  16.826  1.00 13.06  ? 16  TRP   A CD2 1 
ATOM   139  N  NE1 . TRP   A 1 16  ? 27.122  -1.731  14.927  1.00 14.94  ? 16  TRP   A NE1 1 
ATOM   140  C  CE2 . TRP   A 1 16  ? 25.922  -1.646  15.582  1.00 13.81  ? 16  TRP   A CE2 1 
ATOM   141  C  CE3 . TRP   A 1 16  ? 25.121  -0.836  17.724  1.00 13.66  ? 16  TRP   A CE3 1 
ATOM   142  C  CZ2 . TRP   A 1 16  ? 24.656  -2.088  15.207  1.00 14.09  ? 16  TRP   A CZ2 1 
ATOM   143  C  CZ3 . TRP   A 1 16  ? 23.870  -1.279  17.354  1.00 13.42  ? 16  TRP   A CZ3 1 
ATOM   144  C  CH2 . TRP   A 1 16  ? 23.647  -1.895  16.122  1.00 13.68  ? 16  TRP   A CH2 1 
ATOM   145  N  N   . HIS   A 1 17  ? 30.770  0.456   20.064  1.00 15.32  ? 17  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 17  ? 31.254  1.318   21.142  1.00 15.73  ? 17  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 17  ? 32.488  2.124   20.716  1.00 16.86  ? 17  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 17  ? 32.790  3.175   21.299  1.00 17.56  ? 17  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 17  ? 31.556  0.520   22.427  1.00 16.35  ? 17  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 17  ? 32.770  -0.332  22.308  1.00 17.85  ? 17  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 17  ? 33.972  0.076   22.852  1.00 19.41  ? 17  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 17  ? 32.971  -1.499  21.673  1.00 18.94  ? 17  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 17  ? 34.876  -0.832  22.556  1.00 20.58  ? 17  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 17  ? 34.305  -1.819  21.874  1.00 19.66  ? 17  HIS   A NE2 1 
ATOM   155  N  N   . LYS   A 1 18  ? 33.272  1.622   19.750  1.00 17.28  ? 18  LYS   A N   1 
ATOM   156  C  CA  . LYS   A 1 18  ? 34.497  2.338   19.378  1.00 18.48  ? 18  LYS   A CA  1 
ATOM   157  C  C   . LYS   A 1 18  ? 34.170  3.673   18.702  1.00 20.26  ? 18  LYS   A C   1 
ATOM   158  O  O   . LYS   A 1 18  ? 34.857  4.666   18.908  1.00 25.93  ? 18  LYS   A O   1 
ATOM   159  C  CB  . LYS   A 1 18  ? 35.306  1.439   18.460  1.00 19.65  ? 18  LYS   A CB  1 
ATOM   160  C  CG  . LYS   A 1 18  ? 35.885  0.216   19.148  1.00 20.37  ? 18  LYS   A CG  1 
ATOM   161  C  CD  . LYS   A 1 18  ? 36.668  -0.664  18.199  1.00 20.21  ? 18  LYS   A CD  1 
ATOM   162  C  CE  . LYS   A 1 18  ? 35.714  -1.653  17.565  1.00 18.58  ? 18  LYS   A CE  1 
ATOM   163  N  NZ  . LYS   A 1 18  ? 36.388  -2.472  16.529  1.00 20.24  ? 18  LYS   A NZ  1 
ATOM   164  N  N   . ASP   A 1 19  ? 33.128  3.726   17.861  1.00 18.88  ? 19  ASP   A N   1 
ATOM   165  C  CA  . ASP   A 1 19  ? 32.707  4.995   17.270  1.00 19.05  ? 19  ASP   A CA  1 
ATOM   166  C  C   . ASP   A 1 19  ? 31.681  5.727   18.123  1.00 18.49  ? 19  ASP   A C   1 
ATOM   167  O  O   . ASP   A 1 19  ? 31.558  6.941   18.035  1.00 19.69  ? 19  ASP   A O   1 
ATOM   168  C  CB  . ASP   A 1 19  ? 32.133  4.832   15.861  1.00 23.00  ? 19  ASP   A CB  1 
ATOM   169  C  CG  . ASP   A 1 19  ? 33.186  4.716   14.768  1.00 28.81  ? 19  ASP   A CG  1 
ATOM   170  O  OD1 . ASP   A 1 19  ? 34.257  5.306   14.919  1.00 30.36  ? 19  ASP   A OD1 1 
ATOM   171  O  OD2 . ASP   A 1 19  ? 32.918  4.009   13.788  1.00 46.65  ? 19  ASP   A OD2 1 
ATOM   172  N  N   . PHE   A 1 20  ? 30.926  4.983   18.923  1.00 17.13  ? 20  PHE   A N   1 
ATOM   173  C  CA  . PHE   A 1 20  ? 29.814  5.509   19.685  1.00 16.15  ? 20  PHE   A CA  1 
ATOM   174  C  C   . PHE   A 1 20  ? 29.934  5.011   21.123  1.00 15.50  ? 20  PHE   A C   1 
ATOM   175  O  O   . PHE   A 1 20  ? 29.260  4.040   21.504  1.00 15.87  ? 20  PHE   A O   1 
ATOM   176  C  CB  . PHE   A 1 20  ? 28.480  5.081   19.064  1.00 16.82  ? 20  PHE   A CB  1 
ATOM   177  C  CG  . PHE   A 1 20  ? 28.382  5.466   17.611  1.00 17.14  ? 20  PHE   A CG  1 
ATOM   178  C  CD1 . PHE   A 1 20  ? 28.034  6.763   17.246  1.00 19.24  ? 20  PHE   A CD1 1 
ATOM   179  C  CD2 . PHE   A 1 20  ? 28.731  4.556   16.616  1.00 19.39  ? 20  PHE   A CD2 1 
ATOM   180  C  CE1 . PHE   A 1 20  ? 27.982  7.121   15.901  1.00 21.23  ? 20  PHE   A CE1 1 
ATOM   181  C  CE2 . PHE   A 1 20  ? 28.694  4.913   15.278  1.00 21.92  ? 20  PHE   A CE2 1 
ATOM   182  C  CZ  . PHE   A 1 20  ? 28.312  6.190   14.939  1.00 21.32  ? 20  PHE   A CZ  1 
ATOM   183  N  N   . PRO   A 1 21  ? 30.799  5.625   21.965  1.00 16.47  ? 21  PRO   A N   1 
ATOM   184  C  CA  A PRO   A 1 21  ? 31.038  5.075   23.303  0.50 16.90  ? 21  PRO   A CA  1 
ATOM   185  C  CA  B PRO   A 1 21  ? 31.043  5.133   23.319  0.50 17.78  ? 21  PRO   A CA  1 
ATOM   186  C  C   . PRO   A 1 21  ? 29.809  5.040   24.213  1.00 16.64  ? 21  PRO   A C   1 
ATOM   187  O  O   . PRO   A 1 21  ? 29.822  4.307   25.204  1.00 17.21  ? 21  PRO   A O   1 
ATOM   188  C  CB  A PRO   A 1 21  ? 32.136  5.986   23.887  0.50 20.98  ? 21  PRO   A CB  1 
ATOM   189  C  CB  B PRO   A 1 21  ? 32.098  6.121   23.867  0.50 20.45  ? 21  PRO   A CB  1 
ATOM   190  C  CG  A PRO   A 1 21  ? 32.009  7.263   23.081  0.50 20.74  ? 21  PRO   A CG  1 
ATOM   191  C  CG  B PRO   A 1 21  ? 32.862  6.567   22.629  0.50 20.48  ? 21  PRO   A CG  1 
ATOM   192  C  CD  A PRO   A 1 21  ? 31.654  6.791   21.681  0.50 18.84  ? 21  PRO   A CD  1 
ATOM   193  C  CD  B PRO   A 1 21  ? 31.787  6.646   21.562  0.50 18.11  ? 21  PRO   A CD  1 
ATOM   194  N  N   A ILE   A 1 22  ? 28.764  5.774   23.807  0.50 14.71  ? 22  ILE   A N   1 
ATOM   195  N  N   B ILE   A 1 22  ? 28.734  5.793   23.896  0.50 15.60  ? 22  ILE   A N   1 
ATOM   196  C  CA  A ILE   A 1 22  ? 27.507  5.728   24.531  0.50 14.34  ? 22  ILE   A CA  1 
ATOM   197  C  CA  B ILE   A 1 22  ? 27.503  5.668   24.677  0.50 15.61  ? 22  ILE   A CA  1 
ATOM   198  C  C   A ILE   A 1 22  ? 26.878  4.332   24.462  0.50 13.49  ? 22  ILE   A C   1 
ATOM   199  C  C   B ILE   A 1 22  ? 26.941  4.250   24.569  0.50 13.98  ? 22  ILE   A C   1 
ATOM   200  O  O   A ILE   A 1 22  ? 25.954  4.036   25.206  0.50 13.98  ? 22  ILE   A O   1 
ATOM   201  O  O   B ILE   A 1 22  ? 26.055  3.890   25.333  0.50 14.38  ? 22  ILE   A O   1 
ATOM   202  C  CB  A ILE   A 1 22  ? 26.577  6.844   24.050  0.50 14.32  ? 22  ILE   A CB  1 
ATOM   203  C  CB  B ILE   A 1 22  ? 26.426  6.684   24.272  0.50 14.82  ? 22  ILE   A CB  1 
ATOM   204  C  CG1 A ILE   A 1 22  ? 25.481  7.097   25.090  0.50 14.19  ? 22  ILE   A CG1 1 
ATOM   205  C  CG1 B ILE   A 1 22  ? 25.413  6.931   25.397  0.50 18.21  ? 22  ILE   A CG1 1 
ATOM   206  C  CG2 A ILE   A 1 22  ? 26.015  6.534   22.663  0.50 13.14  ? 22  ILE   A CG2 1 
ATOM   207  C  CG2 B ILE   A 1 22  ? 25.712  6.201   23.016  0.50 14.51  ? 22  ILE   A CG2 1 
ATOM   208  C  CD1 A ILE   A 1 22  ? 24.620  8.266   24.786  0.50 15.08  ? 22  ILE   A CD1 1 
ATOM   209  C  CD1 B ILE   A 1 22  ? 25.965  7.735   26.535  0.50 21.05  ? 22  ILE   A CD1 1 
ATOM   210  N  N   . ALA   A 1 23  ? 27.404  3.452   23.592  1.00 14.01  ? 23  ALA   A N   1 
ATOM   211  C  CA  . ALA   A 1 23  ? 26.957  2.067   23.494  1.00 14.52  ? 23  ALA   A CA  1 
ATOM   212  C  C   . ALA   A 1 23  ? 27.043  1.357   24.840  1.00 14.44  ? 23  ALA   A C   1 
ATOM   213  O  O   . ALA   A 1 23  ? 26.350  0.356   25.044  1.00 15.59  ? 23  ALA   A O   1 
ATOM   214  C  CB  . ALA   A 1 23  ? 27.802  1.318   22.490  1.00 15.02  ? 23  ALA   A CB  1 
ATOM   215  N  N   . LYS   A 1 24  ? 27.978  1.805   25.710  1.00 15.82  ? 24  LYS   A N   1 
ATOM   216  C  CA  . LYS   A 1 24  ? 28.158  1.226   27.029  1.00 16.47  ? 24  LYS   A CA  1 
ATOM   217  C  C   . LYS   A 1 24  ? 27.546  2.114   28.115  1.00 17.40  ? 24  LYS   A C   1 
ATOM   218  O  O   . LYS   A 1 24  ? 27.929  2.000   29.285  1.00 19.29  ? 24  LYS   A O   1 
ATOM   219  C  CB  . LYS   A 1 24  ? 29.643  0.949   27.314  1.00 17.92  ? 24  LYS   A CB  1 
ATOM   220  C  CG  . LYS   A 1 24  ? 30.282  -0.095  26.391  1.00 20.71  ? 24  LYS   A CG  1 
ATOM   221  C  CD  . LYS   A 1 24  ? 31.763  -0.252  26.710  1.00 24.98  ? 24  LYS   A CD  1 
ATOM   222  C  CE  . LYS   A 1 24  ? 32.482  -1.264  25.849  1.00 25.97  ? 24  LYS   A CE  1 
ATOM   223  N  NZ  . LYS   A 1 24  ? 32.147  -2.652  26.235  1.00 32.57  ? 24  LYS   A NZ  1 
ATOM   224  N  N   . GLY   A 1 25  ? 26.508  2.901   27.746  1.00 16.68  ? 25  GLY   A N   1 
ATOM   225  C  CA  . GLY   A 1 25  ? 25.922  3.868   28.663  1.00 17.49  ? 25  GLY   A CA  1 
ATOM   226  C  C   . GLY   A 1 25  ? 24.916  3.257   29.642  1.00 16.11  ? 25  GLY   A C   1 
ATOM   227  O  O   . GLY   A 1 25  ? 24.738  2.045   29.750  1.00 16.47  ? 25  GLY   A O   1 
ATOM   228  N  N   . GLU   A 1 26  ? 24.263  4.165   30.382  1.00 16.54  ? 26  GLU   A N   1 
ATOM   229  C  CA  . GLU   A 1 26  ? 23.406  3.795   31.484  1.00 17.09  ? 26  GLU   A CA  1 
ATOM   230  C  C   . GLU   A 1 26  ? 21.971  3.504   31.076  1.00 14.69  ? 26  GLU   A C   1 
ATOM   231  O  O   . GLU   A 1 26  ? 21.209  3.017   31.915  1.00 17.42  ? 26  GLU   A O   1 
ATOM   232  C  CB  . GLU   A 1 26  ? 23.425  4.883   32.562  1.00 22.01  ? 26  GLU   A CB  1 
ATOM   233  C  CG  . GLU   A 1 26  ? 24.812  5.097   33.151  1.00 26.66  ? 26  GLU   A CG  1 
ATOM   234  C  CD  . GLU   A 1 26  ? 25.396  3.831   33.782  1.00 33.60  ? 26  GLU   A CD  1 
ATOM   235  O  OE1 . GLU   A 1 26  ? 24.685  3.189   34.612  1.00 36.60  ? 26  GLU   A OE1 1 
ATOM   236  O  OE2 . GLU   A 1 26  ? 26.547  3.464   33.426  1.00 43.32  ? 26  GLU   A OE2 1 
ATOM   237  N  N   . ARG   A 1 27  ? 21.571  3.830   29.847  1.00 13.97  ? 27  ARG   A N   1 
ATOM   238  C  CA  . ARG   A 1 27  ? 20.186  3.610   29.447  1.00 12.71  ? 27  ARG   A CA  1 
ATOM   239  C  C   . ARG   A 1 27  ? 20.107  3.155   27.988  1.00 11.67  ? 27  ARG   A C   1 
ATOM   240  O  O   . ARG   A 1 27  ? 19.379  3.727   27.170  1.00 12.23  ? 27  ARG   A O   1 
ATOM   241  C  CB  . ARG   A 1 27  ? 19.275  4.802   29.775  1.00 15.31  ? 27  ARG   A CB  1 
ATOM   242  C  CG  . ARG   A 1 27  ? 19.635  6.130   29.160  1.00 15.78  ? 27  ARG   A CG  1 
ATOM   243  C  CD  . ARG   A 1 27  ? 18.653  7.278   29.353  1.00 17.76  ? 27  ARG   A CD  1 
ATOM   244  N  NE  . ARG   A 1 27  ? 17.504  7.204   28.438  1.00 15.80  ? 27  ARG   A NE  1 
ATOM   245  C  CZ  . ARG   A 1 27  ? 16.531  8.106   28.385  1.00 15.33  ? 27  ARG   A CZ  1 
ATOM   246  N  NH1 . ARG   A 1 27  ? 16.560  9.157   29.186  1.00 17.97  ? 27  ARG   A NH1 1 
ATOM   247  N  NH2 . ARG   A 1 27  ? 15.535  7.959   27.531  1.00 16.60  ? 27  ARG   A NH2 1 
ATOM   248  N  N   . GLN   A 1 28  ? 20.826  2.060   27.698  1.00 11.86  ? 28  GLN   A N   1 
ATOM   249  C  CA  . GLN   A 1 28  ? 20.853  1.546   26.329  1.00 11.15  ? 28  GLN   A CA  1 
ATOM   250  C  C   . GLN   A 1 28  ? 19.708  0.577   26.079  1.00 10.69  ? 28  GLN   A C   1 
ATOM   251  O  O   . GLN   A 1 28  ? 19.211  -0.103  26.979  1.00 12.04  ? 28  GLN   A O   1 
ATOM   252  C  CB  . GLN   A 1 28  ? 22.220  0.856   26.088  1.00 12.38  ? 28  GLN   A CB  1 
ATOM   253  C  CG  . GLN   A 1 28  ? 23.335  1.912   25.995  1.00 12.72  ? 28  GLN   A CG  1 
ATOM   254  C  CD  . GLN   A 1 28  ? 23.234  2.707   24.707  1.00 11.61  ? 28  GLN   A CD  1 
ATOM   255  O  OE1 . GLN   A 1 28  ? 23.405  2.149   23.627  1.00 12.40  ? 28  GLN   A OE1 1 
ATOM   256  N  NE2 . GLN   A 1 28  ? 22.887  3.990   24.809  1.00 12.40  ? 28  GLN   A NE2 1 
ATOM   257  N  N   . SER   A 1 29  ? 19.319  0.506   24.802  1.00 10.65  ? 29  SER   A N   1 
ATOM   258  C  CA  . SER   A 1 29  ? 18.268  -0.383  24.328  1.00 11.04  ? 29  SER   A CA  1 
ATOM   259  C  C   . SER   A 1 29  ? 18.803  -1.255  23.216  1.00 10.49  ? 29  SER   A C   1 
ATOM   260  O  O   . SER   A 1 29  ? 19.757  -0.886  22.523  1.00 11.23  ? 29  SER   A O   1 
ATOM   261  C  CB  . SER   A 1 29  ? 17.126  0.480   23.775  1.00 11.20  ? 29  SER   A CB  1 
ATOM   262  O  OG  . SER   A 1 29  ? 16.508  1.205   24.845  1.00 10.56  ? 29  SER   A OG  1 
ATOM   263  N  N   . PRO   A 1 30  ? 18.160  -2.407  22.943  1.00 10.28  ? 30  PRO   A N   1 
ATOM   264  C  CA  . PRO   A 1 30  ? 16.988  -2.945  23.657  1.00 10.38  ? 30  PRO   A CA  1 
ATOM   265  C  C   . PRO   A 1 30  ? 17.397  -3.629  24.962  1.00 10.62  ? 30  PRO   A C   1 
ATOM   266  O  O   . PRO   A 1 30  ? 18.575  -3.650  25.306  1.00 11.13  ? 30  PRO   A O   1 
ATOM   267  C  CB  . PRO   A 1 30  ? 16.466  -3.961  22.656  1.00 10.89  ? 30  PRO   A CB  1 
ATOM   268  C  CG  . PRO   A 1 30  ? 17.738  -4.535  22.049  1.00 10.57  ? 30  PRO   A CG  1 
ATOM   269  C  CD  . PRO   A 1 30  ? 18.639  -3.343  21.904  1.00 10.80  ? 30  PRO   A CD  1 
ATOM   270  N  N   . VAL   A 1 31  ? 16.397  -4.181  25.649  1.00 10.61  ? 31  VAL   A N   1 
ATOM   271  C  CA  . VAL   A 1 31  ? 16.589  -4.929  26.877  1.00 11.08  ? 31  VAL   A CA  1 
ATOM   272  C  C   . VAL   A 1 31  ? 15.708  -6.156  26.830  1.00 11.27  ? 31  VAL   A C   1 
ATOM   273  O  O   . VAL   A 1 31  ? 14.747  -6.213  26.063  1.00 11.85  ? 31  VAL   A O   1 
ATOM   274  C  CB  . VAL   A 1 31  ? 16.273  -4.084  28.131  1.00 11.90  ? 31  VAL   A CB  1 
ATOM   275  C  CG1 . VAL   A 1 31  ? 17.224  -2.890  28.250  1.00 13.09  ? 31  VAL   A CG1 1 
ATOM   276  C  CG2 . VAL   A 1 31  ? 14.800  -3.654  28.179  1.00 12.60  ? 31  VAL   A CG2 1 
ATOM   277  N  N   . ASP   A 1 32  ? 16.033  -7.148  27.676  1.00 11.40  ? 32  ASP   A N   1 
ATOM   278  C  CA  . ASP   A 1 32  ? 15.116  -8.235  27.952  1.00 11.51  ? 32  ASP   A CA  1 
ATOM   279  C  C   . ASP   A 1 32  ? 14.068  -7.712  28.928  1.00 11.60  ? 32  ASP   A C   1 
ATOM   280  O  O   . ASP   A 1 32  ? 14.369  -7.062  29.937  1.00 14.02  ? 32  ASP   A O   1 
ATOM   281  C  CB  . ASP   A 1 32  ? 15.866  -9.408  28.570  1.00 13.58  ? 32  ASP   A CB  1 
ATOM   282  C  CG  . ASP   A 1 32  ? 14.913  -10.557 28.888  1.00 13.98  ? 32  ASP   A CG  1 
ATOM   283  O  OD1 . ASP   A 1 32  ? 14.195  -11.007 27.948  1.00 13.68  ? 32  ASP   A OD1 1 
ATOM   284  O  OD2 . ASP   A 1 32  ? 14.872  -10.981 30.068  1.00 16.39  ? 32  ASP   A OD2 1 
ATOM   285  N  N   . ILE   A 1 33  ? 12.808  -7.993  28.628  1.00 11.85  ? 33  ILE   A N   1 
ATOM   286  C  CA  . ILE   A 1 33  ? 11.686  -7.653  29.505  1.00 12.84  ? 33  ILE   A CA  1 
ATOM   287  C  C   . ILE   A 1 33  ? 11.379  -8.901  30.317  1.00 12.66  ? 33  ILE   A C   1 
ATOM   288  O  O   . ILE   A 1 33  ? 10.796  -9.878  29.828  1.00 14.49  ? 33  ILE   A O   1 
ATOM   289  C  CB  . ILE   A 1 33  ? 10.478  -7.216  28.674  1.00 13.15  ? 33  ILE   A CB  1 
ATOM   290  C  CG1 . ILE   A 1 33  ? 10.856  -6.007  27.824  1.00 13.60  ? 33  ILE   A CG1 1 
ATOM   291  C  CG2 . ILE   A 1 33  ? 9.289   -6.940  29.608  1.00 14.56  ? 33  ILE   A CG2 1 
ATOM   292  C  CD1 . ILE   A 1 33  ? 9.809   -5.653  26.736  1.00 15.60  ? 33  ILE   A CD1 1 
ATOM   293  N  N   A ASP   A 1 34  ? 11.781  -8.848  31.586  0.50 14.18  ? 34  ASP   A N   1 
ATOM   294  N  N   B ASP   A 1 34  ? 11.784  -8.850  31.579  0.50 14.31  ? 34  ASP   A N   1 
ATOM   295  C  CA  A ASP   A 1 34  ? 11.487  -9.895  32.556  0.50 15.08  ? 34  ASP   A CA  1 
ATOM   296  C  CA  B ASP   A 1 34  ? 11.496  -9.930  32.508  0.50 15.02  ? 34  ASP   A CA  1 
ATOM   297  C  C   A ASP   A 1 34  ? 10.077  -9.622  33.079  0.50 14.89  ? 34  ASP   A C   1 
ATOM   298  C  C   B ASP   A 1 34  ? 10.105  -9.653  33.079  0.50 15.21  ? 34  ASP   A C   1 
ATOM   299  O  O   A ASP   A 1 34  ? 9.855   -8.662  33.833  0.50 17.26  ? 34  ASP   A O   1 
ATOM   300  O  O   B ASP   A 1 34  ? 9.923   -8.716  33.868  0.50 18.09  ? 34  ASP   A O   1 
ATOM   301  C  CB  A ASP   A 1 34  ? 12.524  -9.867  33.682  0.50 17.48  ? 34  ASP   A CB  1 
ATOM   302  C  CB  B ASP   A 1 34  ? 12.592  -10.000 33.571  0.50 17.42  ? 34  ASP   A CB  1 
ATOM   303  C  CG  A ASP   A 1 34  ? 12.238  -10.875 34.789  0.50 17.54  ? 34  ASP   A CG  1 
ATOM   304  C  CG  B ASP   A 1 34  ? 12.440  -11.238 34.442  0.50 20.22  ? 34  ASP   A CG  1 
ATOM   305  O  OD1 A ASP   A 1 34  ? 11.079  -11.369 34.875  0.50 18.22  ? 34  ASP   A OD1 1 
ATOM   306  O  OD1 B ASP   A 1 34  ? 12.927  -12.315 34.041  0.50 25.12  ? 34  ASP   A OD1 1 
ATOM   307  O  OD2 A ASP   A 1 34  ? 13.167  -11.143 35.589  0.50 25.49  ? 34  ASP   A OD2 1 
ATOM   308  O  OD2 B ASP   A 1 34  ? 11.808  -11.131 35.510  0.50 21.37  ? 34  ASP   A OD2 1 
ATOM   309  N  N   . THR   A 1 35  ? 9.112   -10.418 32.598  1.00 16.84  ? 35  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 35  ? 7.704   -10.105 32.823  1.00 18.92  ? 35  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 35  ? 7.351   -10.226 34.290  1.00 18.15  ? 35  THR   A C   1 
ATOM   312  O  O   . THR   A 1 35  ? 6.465   -9.528  34.745  1.00 19.86  ? 35  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 35  ? 6.750   -10.974 31.998  1.00 21.12  ? 35  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 35  ? 6.902   -12.324 32.445  1.00 22.31  ? 35  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 35  ? 7.023   -10.844 30.521  1.00 23.81  ? 35  THR   A CG2 1 
ATOM   316  N  N   . HIS   A 1 36  ? 8.069   -11.089 35.024  1.00 19.30  ? 36  HIS   A N   1 
ATOM   317  C  CA  . HIS   A 1 36  ? 7.773   -11.323 36.417  1.00 19.37  ? 36  HIS   A CA  1 
ATOM   318  C  C   . HIS   A 1 36  ? 8.277   -10.159 37.263  1.00 21.16  ? 36  HIS   A C   1 
ATOM   319  O  O   . HIS   A 1 36  ? 7.619   -9.867  38.271  1.00 25.46  ? 36  HIS   A O   1 
ATOM   320  C  CB  . HIS   A 1 36  ? 8.275   -12.741 36.780  1.00 21.61  ? 36  HIS   A CB  1 
ATOM   321  C  CG  . HIS   A 1 36  ? 7.333   -13.815 36.328  1.00 23.36  ? 36  HIS   A CG  1 
ATOM   322  N  ND1 . HIS   A 1 36  ? 6.047   -13.994 36.856  1.00 30.19  ? 36  HIS   A ND1 1 
ATOM   323  C  CD2 . HIS   A 1 36  ? 7.536   -14.832 35.454  1.00 23.45  ? 36  HIS   A CD2 1 
ATOM   324  C  CE1 . HIS   A 1 36  ? 5.502   -15.053 36.288  1.00 33.86  ? 36  HIS   A CE1 1 
ATOM   325  N  NE2 . HIS   A 1 36  ? 6.388   -15.581 35.423  1.00 35.34  ? 36  HIS   A NE2 1 
ATOM   326  N  N   . THR   A 1 37  ? 9.358   -9.463  36.803  1.00 21.27  ? 37  THR   A N   1 
ATOM   327  C  CA  . THR   A 1 37  ? 10.014  -8.353  37.508  1.00 21.03  ? 37  THR   A CA  1 
ATOM   328  C  C   . THR   A 1 37  ? 9.468   -6.967  37.129  1.00 19.32  ? 37  THR   A C   1 
ATOM   329  O  O   . THR   A 1 37  ? 9.578   -5.994  37.892  1.00 22.84  ? 37  THR   A O   1 
ATOM   330  C  CB  . THR   A 1 37  ? 11.536  -8.374  37.294  1.00 29.53  ? 37  THR   A CB  1 
ATOM   331  O  OG1 . THR   A 1 37  ? 12.007  -9.581  37.888  1.00 34.56  ? 37  THR   A OG1 1 
ATOM   332  C  CG2 . THR   A 1 37  ? 12.258  -7.207  37.949  1.00 27.36  ? 37  THR   A CG2 1 
ATOM   333  N  N   . ALA   A 1 38  ? 8.810   -6.874  35.981  1.00 19.27  ? 38  ALA   A N   1 
ATOM   334  C  CA  . ALA   A 1 38  ? 8.215   -5.607  35.563  1.00 17.08  ? 38  ALA   A CA  1 
ATOM   335  C  C   . ALA   A 1 38  ? 7.146   -5.261  36.596  1.00 20.10  ? 38  ALA   A C   1 
ATOM   336  O  O   . ALA   A 1 38  ? 6.460   -6.106  37.125  1.00 24.71  ? 38  ALA   A O   1 
ATOM   337  C  CB  . ALA   A 1 38  ? 7.627   -5.720  34.179  1.00 17.85  ? 38  ALA   A CB  1 
ATOM   338  N  N   . LYS   A 1 39  ? 7.043   -4.003  36.963  1.00 19.55  ? 39  LYS   A N   1 
ATOM   339  C  CA  . LYS   A 1 39  ? 6.096   -3.579  37.982  1.00 22.47  ? 39  LYS   A CA  1 
ATOM   340  C  C   . LYS   A 1 39  ? 4.809   -3.052  37.326  1.00 17.75  ? 39  LYS   A C   1 
ATOM   341  O  O   . LYS   A 1 39  ? 4.863   -2.097  36.561  1.00 17.67  ? 39  LYS   A O   1 
ATOM   342  C  CB  . LYS   A 1 39  ? 6.835   -2.486  38.772  1.00 28.66  ? 39  LYS   A CB  1 
ATOM   343  C  CG  . LYS   A 1 39  ? 6.070   -1.622  39.734  1.00 25.91  ? 39  LYS   A CG  1 
ATOM   344  C  CD  . LYS   A 1 39  ? 5.881   -2.342  41.055  1.00 25.12  ? 39  LYS   A CD  1 
ATOM   345  C  CE  . LYS   A 1 39  ? 5.133   -1.454  42.014  1.00 27.55  ? 39  LYS   A CE  1 
ATOM   346  N  NZ  . LYS   A 1 39  ? 4.846   -2.137  43.288  1.00 32.33  ? 39  LYS   A NZ  1 
ATOM   347  N  N   . TYR   A 1 40  ? 3.637   -3.620  37.650  1.00 20.15  ? 40  TYR   A N   1 
ATOM   348  C  CA  . TYR   A 1 40  ? 2.384   -2.966  37.278  1.00 18.80  ? 40  TYR   A CA  1 
ATOM   349  C  C   . TYR   A 1 40  ? 2.333   -1.574  37.911  1.00 17.10  ? 40  TYR   A C   1 
ATOM   350  O  O   . TYR   A 1 40  ? 2.499   -1.423  39.123  1.00 20.49  ? 40  TYR   A O   1 
ATOM   351  C  CB  . TYR   A 1 40  ? 1.194   -3.812  37.737  1.00 23.88  ? 40  TYR   A CB  1 
ATOM   352  C  CG  . TYR   A 1 40  ? -0.129  -3.117  37.580  1.00 24.33  ? 40  TYR   A CG  1 
ATOM   353  C  CD1 . TYR   A 1 40  ? -0.515  -2.598  36.354  1.00 22.29  ? 40  TYR   A CD1 1 
ATOM   354  C  CD2 . TYR   A 1 40  ? -0.999  -2.952  38.647  1.00 28.34  ? 40  TYR   A CD2 1 
ATOM   355  C  CE1 . TYR   A 1 40  ? -1.735  -1.973  36.169  1.00 27.93  ? 40  TYR   A CE1 1 
ATOM   356  C  CE2 . TYR   A 1 40  ? -2.225  -2.314  38.480  1.00 32.64  ? 40  TYR   A CE2 1 
ATOM   357  C  CZ  . TYR   A 1 40  ? -2.595  -1.819  37.240  1.00 30.93  ? 40  TYR   A CZ  1 
ATOM   358  O  OH  . TYR   A 1 40  ? -3.792  -1.182  37.063  1.00 40.44  ? 40  TYR   A OH  1 
ATOM   359  N  N   . ASP   A 1 41  ? 2.032   -0.560  37.110  1.00 17.63  ? 41  ASP   A N   1 
ATOM   360  C  CA  . ASP   A 1 41  ? 1.923   0.800   37.614  1.00 18.60  ? 41  ASP   A CA  1 
ATOM   361  C  C   . ASP   A 1 41  ? 0.517   1.299   37.333  1.00 24.60  ? 41  ASP   A C   1 
ATOM   362  O  O   . ASP   A 1 41  ? 0.196   1.612   36.181  1.00 21.48  ? 41  ASP   A O   1 
ATOM   363  C  CB  . ASP   A 1 41  ? 2.966   1.697   36.944  1.00 22.18  ? 41  ASP   A CB  1 
ATOM   364  C  CG  . ASP   A 1 41  ? 2.953   3.123   37.470  1.00 25.64  ? 41  ASP   A CG  1 
ATOM   365  O  OD1 . ASP   A 1 41  ? 2.020   3.461   38.233  1.00 29.66  ? 41  ASP   A OD1 1 
ATOM   366  O  OD2 . ASP   A 1 41  ? 3.902   3.875   37.165  1.00 30.93  ? 41  ASP   A OD2 1 
ATOM   367  N  N   . PRO   A 1 42  ? -0.364  1.346   38.355  1.00 28.80  ? 42  PRO   A N   1 
ATOM   368  C  CA  . PRO   A 1 42  ? -1.747  1.747   38.097  1.00 32.46  ? 42  PRO   A CA  1 
ATOM   369  C  C   . PRO   A 1 42  ? -1.911  3.211   37.697  1.00 31.79  ? 42  PRO   A C   1 
ATOM   370  O  O   . PRO   A 1 42  ? -2.984  3.626   37.272  1.00 41.20  ? 42  PRO   A O   1 
ATOM   371  C  CB  . PRO   A 1 42  ? -2.446  1.478   39.440  1.00 39.94  ? 42  PRO   A CB  1 
ATOM   372  C  CG  . PRO   A 1 42  ? -1.334  1.561   40.466  1.00 35.63  ? 42  PRO   A CG  1 
ATOM   373  C  CD  . PRO   A 1 42  ? -0.108  1.000   39.771  1.00 29.48  ? 42  PRO   A CD  1 
ATOM   374  N  N   . SER   A 1 43  ? -0.834  3.999   37.815  1.00 30.03  ? 43  SER   A N   1 
ATOM   375  C  CA  . SER   A 1 43  ? -0.920  5.402   37.427  1.00 34.90  ? 43  SER   A CA  1 
ATOM   376  C  C   . SER   A 1 43  ? -0.641  5.591   35.931  1.00 30.51  ? 43  SER   A C   1 
ATOM   377  O  O   . SER   A 1 43  ? -0.896  6.674   35.394  1.00 36.15  ? 43  SER   A O   1 
ATOM   378  C  CB  . SER   A 1 43  ? -0.020  6.260   38.263  1.00 45.07  ? 43  SER   A CB  1 
ATOM   379  O  OG  . SER   A 1 43  ? 1.328   6.166   37.828  1.00 44.08  ? 43  SER   A OG  1 
ATOM   380  N  N   . LEU   A 1 44  ? -0.133  4.550   35.251  1.00 27.21  ? 44  LEU   A N   1 
ATOM   381  C  CA  . LEU   A 1 44  ? 0.083   4.616   33.808  1.00 21.85  ? 44  LEU   A CA  1 
ATOM   382  C  C   . LEU   A 1 44  ? -1.254  4.765   33.089  1.00 23.34  ? 44  LEU   A C   1 
ATOM   383  O  O   . LEU   A 1 44  ? -2.217  4.093   33.409  1.00 30.03  ? 44  LEU   A O   1 
ATOM   384  C  CB  . LEU   A 1 44  ? 0.795   3.360   33.301  1.00 20.30  ? 44  LEU   A CB  1 
ATOM   385  C  CG  . LEU   A 1 44  ? 2.295   3.327   33.507  1.00 17.80  ? 44  LEU   A CG  1 
ATOM   386  C  CD1 . LEU   A 1 44  ? 2.804   1.959   33.093  1.00 19.66  ? 44  LEU   A CD1 1 
ATOM   387  C  CD2 . LEU   A 1 44  ? 2.995   4.430   32.761  1.00 19.29  ? 44  LEU   A CD2 1 
ATOM   388  N  N   . LYS   A 1 45  ? -1.283  5.587   32.050  1.00 21.74  ? 45  LYS   A N   1 
ATOM   389  C  CA  . LYS   A 1 45  ? -2.542  5.803   31.354  1.00 21.61  ? 45  LYS   A CA  1 
ATOM   390  C  C   . LYS   A 1 45  ? -2.603  4.905   30.135  1.00 18.89  ? 45  LYS   A C   1 
ATOM   391  O  O   . LYS   A 1 45  ? -1.573  4.456   29.640  1.00 19.37  ? 45  LYS   A O   1 
ATOM   392  C  CB  . LYS   A 1 45  ? -2.626  7.256   30.900  1.00 24.43  ? 45  LYS   A CB  1 
ATOM   393  C  CG  . LYS   A 1 45  ? -2.746  8.293   32.005  1.00 29.72  ? 45  LYS   A CG  1 
ATOM   394  C  CD  . LYS   A 1 45  ? -2.194  9.656   31.648  1.00 42.21  ? 45  LYS   A CD  1 
ATOM   395  C  CE  . LYS   A 1 45  ? -3.019  10.430  30.641  1.00 52.75  ? 45  LYS   A CE  1 
ATOM   396  N  NZ  . LYS   A 1 45  ? -4.246  11.002  31.251  1.00 66.63  ? 45  LYS   A NZ  1 
ATOM   397  N  N   . PRO   A 1 46  ? -3.817  4.701   29.578  1.00 18.93  ? 46  PRO   A N   1 
ATOM   398  C  CA  . PRO   A 1 46  ? -3.916  4.040   28.278  1.00 18.76  ? 46  PRO   A CA  1 
ATOM   399  C  C   . PRO   A 1 46  ? -3.104  4.808   27.244  1.00 17.23  ? 46  PRO   A C   1 
ATOM   400  O  O   . PRO   A 1 46  ? -3.034  6.036   27.307  1.00 17.83  ? 46  PRO   A O   1 
ATOM   401  C  CB  . PRO   A 1 46  ? -5.418  4.069   27.948  1.00 20.91  ? 46  PRO   A CB  1 
ATOM   402  C  CG  . PRO   A 1 46  ? -6.090  4.246   29.296  1.00 26.40  ? 46  PRO   A CG  1 
ATOM   403  C  CD  . PRO   A 1 46  ? -5.132  5.067   30.141  1.00 23.18  ? 46  PRO   A CD  1 
ATOM   404  N  N   A LEU   A 1 47  ? -2.561  4.079   26.268  0.50 18.20  ? 47  LEU   A N   1 
ATOM   405  N  N   B LEU   A 1 47  ? -2.440  4.079   26.336  0.50 18.41  ? 47  LEU   A N   1 
ATOM   406  C  CA  A LEU   A 1 47  ? -1.807  4.696   25.196  0.50 16.19  ? 47  LEU   A CA  1 
ATOM   407  C  CA  B LEU   A 1 47  ? -1.860  4.760   25.193  0.50 17.97  ? 47  LEU   A CA  1 
ATOM   408  C  C   A LEU   A 1 47  ? -2.790  5.239   24.152  0.50 16.62  ? 47  LEU   A C   1 
ATOM   409  C  C   B LEU   A 1 47  ? -2.988  5.419   24.416  0.50 18.44  ? 47  LEU   A C   1 
ATOM   410  O  O   A LEU   A 1 47  ? -3.721  4.517   23.772  0.50 15.43  ? 47  LEU   A O   1 
ATOM   411  O  O   B LEU   A 1 47  ? -4.117  4.913   24.373  0.50 18.85  ? 47  LEU   A O   1 
ATOM   412  C  CB  A LEU   A 1 47  ? -0.911  3.600   24.616  0.50 17.27  ? 47  LEU   A CB  1 
ATOM   413  C  CB  B LEU   A 1 47  ? -1.180  3.770   24.246  0.50 20.09  ? 47  LEU   A CB  1 
ATOM   414  C  CG  A LEU   A 1 47  ? 0.049   4.056   23.538  0.50 16.38  ? 47  LEU   A CG  1 
ATOM   415  C  CG  B LEU   A 1 47  ? 0.127   3.167   24.724  0.50 19.09  ? 47  LEU   A CG  1 
ATOM   416  C  CD1 A LEU   A 1 47  ? 1.141   4.895   24.191  0.50 16.02  ? 47  LEU   A CD1 1 
ATOM   417  C  CD1 B LEU   A 1 47  ? 0.640   2.207   23.663  0.50 20.21  ? 47  LEU   A CD1 1 
ATOM   418  C  CD2 A LEU   A 1 47  ? 0.627   2.844   22.808  0.50 16.05  ? 47  LEU   A CD2 1 
ATOM   419  C  CD2 B LEU   A 1 47  ? 1.146   4.261   25.032  0.50 19.05  ? 47  LEU   A CD2 1 
ATOM   420  N  N   . SER   A 1 48  ? -2.625  6.520   23.766  1.00 17.05  ? 48  SER   A N   1 
ATOM   421  C  CA  . SER   A 1 48  ? -3.473  7.176   22.767  1.00 17.60  ? 48  SER   A CA  1 
ATOM   422  C  C   . SER   A 1 48  ? -2.712  7.182   21.443  1.00 16.54  ? 48  SER   A C   1 
ATOM   423  O  O   . SER   A 1 48  ? -1.730  7.906   21.273  1.00 18.37  ? 48  SER   A O   1 
ATOM   424  C  CB  . SER   A 1 48  ? -3.790  8.606   23.190  1.00 19.15  ? 48  SER   A CB  1 
ATOM   425  O  OG  . SER   A 1 48  ? -4.466  9.293   22.154  1.00 23.91  ? 48  SER   A OG  1 
ATOM   426  N  N   . VAL   A 1 49  ? -3.172  6.375   20.504  1.00 18.13  ? 49  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 49  ? -2.594  6.297   19.181  1.00 18.24  ? 49  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 49  ? -3.577  6.934   18.207  1.00 20.19  ? 49  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 49  ? -4.667  6.406   18.013  1.00 24.53  ? 49  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 49  ? -2.353  4.825   18.804  1.00 20.34  ? 49  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 49  ? -1.727  4.742   17.418  1.00 26.36  ? 49  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 49  ? -1.491  4.139   19.858  1.00 21.99  ? 49  VAL   A CG2 1 
ATOM   433  N  N   . SER   A 1 50  ? -3.224  8.072   17.624  1.00 20.20  ? 50  SER   A N   1 
ATOM   434  C  CA  . SER   A 1 50  ? -4.132  8.816   16.774  1.00 21.90  ? 50  SER   A CA  1 
ATOM   435  C  C   . SER   A 1 50  ? -3.485  8.877   15.402  1.00 20.29  ? 50  SER   A C   1 
ATOM   436  O  O   . SER   A 1 50  ? -2.730  9.800   15.113  1.00 21.52  ? 50  SER   A O   1 
ATOM   437  C  CB  . SER   A 1 50  ? -4.465  10.194  17.340  1.00 26.18  ? 50  SER   A CB  1 
ATOM   438  O  OG  . SER   A 1 50  ? -5.176  10.080  18.568  1.00 31.17  ? 50  SER   A OG  1 
ATOM   439  N  N   . TYR   A 1 51  ? -3.771  7.875   14.561  1.00 19.87  ? 51  TYR   A N   1 
ATOM   440  C  CA  . TYR   A 1 51  ? -3.130  7.717   13.265  1.00 19.87  ? 51  TYR   A CA  1 
ATOM   441  C  C   . TYR   A 1 51  ? -4.072  7.940   12.078  1.00 21.24  ? 51  TYR   A C   1 
ATOM   442  O  O   . TYR   A 1 51  ? -3.659  7.762   10.938  1.00 23.18  ? 51  TYR   A O   1 
ATOM   443  C  CB  . TYR   A 1 51  ? -2.495  6.327   13.124  1.00 18.98  ? 51  TYR   A CB  1 
ATOM   444  C  CG  . TYR   A 1 51  ? -1.225  6.051   13.910  1.00 17.34  ? 51  TYR   A CG  1 
ATOM   445  C  CD1 . TYR   A 1 51  ? -0.515  7.037   14.589  1.00 18.78  ? 51  TYR   A CD1 1 
ATOM   446  C  CD2 . TYR   A 1 51  ? -0.729  4.755   13.979  1.00 16.79  ? 51  TYR   A CD2 1 
ATOM   447  C  CE1 . TYR   A 1 51  ? 0.681   6.721   15.249  1.00 15.56  ? 51  TYR   A CE1 1 
ATOM   448  C  CE2 . TYR   A 1 51  ? 0.454   4.426   14.630  1.00 15.73  ? 51  TYR   A CE2 1 
ATOM   449  C  CZ  . TYR   A 1 51  ? 1.154   5.416   15.285  1.00 15.14  ? 51  TYR   A CZ  1 
ATOM   450  O  OH  . TYR   A 1 51  ? 2.317   5.069   15.912  1.00 15.37  ? 51  TYR   A OH  1 
ATOM   451  N  N   . ASP   A 1 52  ? -5.316  8.376   12.320  1.00 24.01  ? 52  ASP   A N   1 
ATOM   452  C  CA  . ASP   A 1 52  ? -6.304  8.523   11.262  1.00 25.27  ? 52  ASP   A CA  1 
ATOM   453  C  C   . ASP   A 1 52  ? -5.887  9.546   10.198  1.00 23.96  ? 52  ASP   A C   1 
ATOM   454  O  O   . ASP   A 1 52  ? -6.321  9.425   9.054   1.00 30.42  ? 52  ASP   A O   1 
ATOM   455  C  CB  . ASP   A 1 52  ? -7.680  8.835   11.852  1.00 34.43  ? 52  ASP   A CB  1 
ATOM   456  C  CG  . ASP   A 1 52  ? -7.624  9.955   12.881  1.00 43.13  ? 52  ASP   A CG  1 
ATOM   457  O  OD1 . ASP   A 1 52  ? -7.037  9.727   13.988  1.00 45.60  ? 52  ASP   A OD1 1 
ATOM   458  O  OD2 . ASP   A 1 52  ? -8.128  11.056  12.561  1.00 50.47  ? 52  ASP   A OD2 1 
ATOM   459  N  N   . GLN   A 1 53  ? -5.080  10.551  10.548  1.00 25.88  ? 53  GLN   A N   1 
ATOM   460  C  CA  . GLN   A 1 53  ? -4.698  11.522  9.527   1.00 27.75  ? 53  GLN   A CA  1 
ATOM   461  C  C   . GLN   A 1 53  ? -3.265  11.320  9.021   1.00 21.72  ? 53  GLN   A C   1 
ATOM   462  O  O   . GLN   A 1 53  ? -2.688  12.223  8.413   1.00 24.05  ? 53  GLN   A O   1 
ATOM   463  C  CB  . GLN   A 1 53  ? -4.944  12.945  10.034  1.00 34.78  ? 53  GLN   A CB  1 
ATOM   464  C  CG  . GLN   A 1 53  ? -6.413  13.231  10.296  1.00 41.05  ? 53  GLN   A CG  1 
ATOM   465  C  CD  . GLN   A 1 53  ? -7.181  13.278  9.000   1.00 49.56  ? 53  GLN   A CD  1 
ATOM   466  O  OE1 . GLN   A 1 53  ? -6.658  13.670  7.953   1.00 54.25  ? 53  GLN   A OE1 1 
ATOM   467  N  NE2 . GLN   A 1 53  ? -8.436  12.872  9.059   1.00 48.24  ? 53  GLN   A NE2 1 
ATOM   468  N  N   . ALA   A 1 54  ? -2.669  10.159  9.290   1.00 22.02  ? 54  ALA   A N   1 
ATOM   469  C  CA  . ALA   A 1 54  ? -1.284  9.943   8.890   1.00 18.37  ? 54  ALA   A CA  1 
ATOM   470  C  C   . ALA   A 1 54  ? -1.144  10.102  7.382   1.00 21.04  ? 54  ALA   A C   1 
ATOM   471  O  O   . ALA   A 1 54  ? -2.022  9.674   6.628   1.00 26.55  ? 54  ALA   A O   1 
ATOM   472  C  CB  . ALA   A 1 54  ? -0.848  8.546   9.308   1.00 20.58  ? 54  ALA   A CB  1 
ATOM   473  N  N   . THR   A 1 55  ? -0.024  10.711  6.983   1.00 18.02  ? 55  THR   A N   1 
ATOM   474  C  CA  . THR   A 1 55  ? 0.318   10.951  5.586   1.00 19.45  ? 55  THR   A CA  1 
ATOM   475  C  C   . THR   A 1 55  ? 1.659   10.291  5.302   1.00 16.53  ? 55  THR   A C   1 
ATOM   476  O  O   . THR   A 1 55  ? 2.690   10.864  5.572   1.00 17.26  ? 55  THR   A O   1 
ATOM   477  C  CB  . THR   A 1 55  ? 0.415   12.453  5.215   1.00 24.16  ? 55  THR   A CB  1 
ATOM   478  O  OG1 . THR   A 1 55  ? -0.832  13.103  5.443   1.00 29.66  ? 55  THR   A OG1 1 
ATOM   479  C  CG2 . THR   A 1 55  ? 0.886   12.658  3.787   1.00 27.67  ? 55  THR   A CG2 1 
ATOM   480  N  N   . SER   A 1 56  ? 1.643   9.048   4.813   1.00 17.22  ? 56  SER   A N   1 
ATOM   481  C  CA  . SER   A 1 56  ? 2.910   8.438   4.427   1.00 16.96  ? 56  SER   A CA  1 
ATOM   482  C  C   . SER   A 1 56  ? 3.385   9.096   3.141   1.00 18.45  ? 56  SER   A C   1 
ATOM   483  O  O   . SER   A 1 56  ? 2.588   9.559   2.340   1.00 20.01  ? 56  SER   A O   1 
ATOM   484  C  CB  . SER   A 1 56  ? 2.843   6.912   4.250   1.00 18.69  ? 56  SER   A CB  1 
ATOM   485  O  OG  . SER   A 1 56  ? 1.932   6.585   3.185   1.00 19.82  ? 56  SER   A OG  1 
ATOM   486  N  N   . LEU   A 1 57  ? 4.706   9.096   2.950   1.00 16.91  ? 57  LEU   A N   1 
ATOM   487  C  CA  . LEU   A 1 57  ? 5.256   9.761   1.783   1.00 19.35  ? 57  LEU   A CA  1 
ATOM   488  C  C   . LEU   A 1 57  ? 6.046   8.779   0.937   1.00 17.55  ? 57  LEU   A C   1 
ATOM   489  O  O   . LEU   A 1 57  ? 5.943   8.796   -0.287  1.00 19.08  ? 57  LEU   A O   1 
ATOM   490  C  CB  . LEU   A 1 57  ? 6.138   10.917  2.240   1.00 22.17  ? 57  LEU   A CB  1 
ATOM   491  C  CG  . LEU   A 1 57  ? 5.409   12.124  2.837   1.00 26.70  ? 57  LEU   A CG  1 
ATOM   492  C  CD1 . LEU   A 1 57  ? 6.420   13.144  3.341   1.00 35.15  ? 57  LEU   A CD1 1 
ATOM   493  C  CD2 . LEU   A 1 57  ? 4.489   12.770  1.805   1.00 33.67  ? 57  LEU   A CD2 1 
ATOM   494  N  N   . ARG   A 1 58  ? 6.896   7.984   1.578   1.00 16.96  ? 58  ARG   A N   1 
ATOM   495  C  CA  . ARG   A 1 58  ? 7.955   7.339   0.833   1.00 17.48  ? 58  ARG   A CA  1 
ATOM   496  C  C   . ARG   A 1 58  ? 8.489   6.174   1.654   1.00 16.21  ? 58  ARG   A C   1 
ATOM   497  O  O   . ARG   A 1 58  ? 8.382   6.160   2.872   1.00 16.98  ? 58  ARG   A O   1 
ATOM   498  C  CB  . ARG   A 1 58  ? 9.094   8.343   0.652   1.00 20.52  ? 58  ARG   A CB  1 
ATOM   499  C  CG  . ARG   A 1 58  ? 10.189  7.884   -0.276  1.00 21.48  ? 58  ARG   A CG  1 
ATOM   500  C  CD  . ARG   A 1 58  ? 11.181  9.010   -0.479  1.00 24.91  ? 58  ARG   A CD  1 
ATOM   501  N  NE  . ARG   A 1 58  ? 12.008  9.110   0.716   1.00 21.53  ? 58  ARG   A NE  1 
ATOM   502  C  CZ  . ARG   A 1 58  ? 13.325  9.281   0.696   1.00 23.69  ? 58  ARG   A CZ  1 
ATOM   503  N  NH1 . ARG   A 1 58  ? 13.966  9.488   -0.440  1.00 24.89  ? 58  ARG   A NH1 1 
ATOM   504  N  NH2 . ARG   A 1 58  ? 13.982  9.305   1.834   1.00 22.31  ? 58  ARG   A NH2 1 
ATOM   505  N  N   . ILE   A 1 59  ? 9.073   5.193   0.960   1.00 15.49  ? 59  ILE   A N   1 
ATOM   506  C  CA  . ILE   A 1 59  ? 9.761   4.080   1.588   1.00 16.15  ? 59  ILE   A CA  1 
ATOM   507  C  C   . ILE   A 1 59  ? 11.196  4.060   1.070   1.00 14.94  ? 59  ILE   A C   1 
ATOM   508  O  O   . ILE   A 1 59  ? 11.426  4.214   -0.138  1.00 17.88  ? 59  ILE   A O   1 
ATOM   509  C  CB  . ILE   A 1 59  ? 9.023   2.752   1.338   1.00 16.13  ? 59  ILE   A CB  1 
ATOM   510  C  CG1 . ILE   A 1 59  ? 9.592   1.621   2.213   1.00 16.33  ? 59  ILE   A CG1 1 
ATOM   511  C  CG2 . ILE   A 1 59  ? 8.985   2.353   -0.147  1.00 18.47  ? 59  ILE   A CG2 1 
ATOM   512  C  CD1 . ILE   A 1 59  ? 8.716   0.361   2.142   1.00 18.42  ? 59  ILE   A CD1 1 
ATOM   513  N  N   . LEU   A 1 60  ? 12.147  3.864   1.997   1.00 15.66  ? 60  LEU   A N   1 
ATOM   514  C  CA  . LEU   A 1 60  ? 13.573  3.998   1.698   1.00 15.62  ? 60  LEU   A CA  1 
ATOM   515  C  C   . LEU   A 1 60  ? 14.332  2.786   2.224   1.00 14.59  ? 60  LEU   A C   1 
ATOM   516  O  O   . LEU   A 1 60  ? 14.176  2.447   3.388   1.00 15.29  ? 60  LEU   A O   1 
ATOM   517  C  CB  . LEU   A 1 60  ? 14.130  5.270   2.380   1.00 18.59  ? 60  LEU   A CB  1 
ATOM   518  C  CG  . LEU   A 1 60  ? 15.656  5.421   2.316   1.00 17.30  ? 60  LEU   A CG  1 
ATOM   519  C  CD1 . LEU   A 1 60  ? 16.161  5.708   0.909   1.00 19.82  ? 60  LEU   A CD1 1 
ATOM   520  C  CD2 . LEU   A 1 60  ? 16.149  6.515   3.270   1.00 20.63  ? 60  LEU   A CD2 1 
ATOM   521  N  N   . ASN   A 1 61  ? 15.199  2.179   1.411   1.00 14.13  ? 61  ASN   A N   1 
ATOM   522  C  CA  . ASN   A 1 61  ? 16.191  1.230   1.882   1.00 14.79  ? 61  ASN   A CA  1 
ATOM   523  C  C   . ASN   A 1 61  ? 17.420  2.049   2.328   1.00 14.26  ? 61  ASN   A C   1 
ATOM   524  O  O   . ASN   A 1 61  ? 18.082  2.655   1.485   1.00 16.67  ? 61  ASN   A O   1 
ATOM   525  C  CB  . ASN   A 1 61  ? 16.539  0.214   0.790   1.00 15.65  ? 61  ASN   A CB  1 
ATOM   526  C  CG  . ASN   A 1 61  ? 17.610  -0.776  1.192   1.00 14.88  ? 61  ASN   A CG  1 
ATOM   527  O  OD1 . ASN   A 1 61  ? 18.475  -0.510  2.070   1.00 15.90  ? 61  ASN   A OD1 1 
ATOM   528  N  ND2 . ASN   A 1 61  ? 17.581  -1.967  0.583   1.00 16.17  ? 61  ASN   A ND2 1 
ATOM   529  N  N   . ASN   A 1 62  ? 17.703  2.076   3.622   1.00 14.93  ? 62  ASN   A N   1 
ATOM   530  C  CA  . ASN   A 1 62  ? 18.761  2.959   4.072   1.00 17.08  ? 62  ASN   A CA  1 
ATOM   531  C  C   . ASN   A 1 62  ? 20.074  2.198   4.256   1.00 17.35  ? 62  ASN   A C   1 
ATOM   532  O  O   . ASN   A 1 62  ? 21.049  2.706   4.841   1.00 20.92  ? 62  ASN   A O   1 
ATOM   533  C  CB  . ASN   A 1 62  ? 18.415  3.682   5.364   1.00 19.83  ? 62  ASN   A CB  1 
ATOM   534  C  CG  . ASN   A 1 62  ? 18.381  2.758   6.552   1.00 19.66  ? 62  ASN   A CG  1 
ATOM   535  O  OD1 . ASN   A 1 62  ? 18.630  1.561   6.509   1.00 18.53  ? 62  ASN   A OD1 1 
ATOM   536  N  ND2 . ASN   A 1 62  ? 18.273  3.375   7.707   1.00 23.87  ? 62  ASN   A ND2 1 
ATOM   537  N  N   . GLY   A 1 63  ? 20.115  0.961   3.758   1.00 16.89  ? 63  GLY   A N   1 
ATOM   538  C  CA  . GLY   A 1 63  ? 21.281  0.118   3.870   1.00 15.86  ? 63  GLY   A CA  1 
ATOM   539  C  C   . GLY   A 1 63  ? 21.335  -0.781  5.109   1.00 16.78  ? 63  GLY   A C   1 
ATOM   540  O  O   . GLY   A 1 63  ? 22.203  -1.641  5.207   1.00 20.24  ? 63  GLY   A O   1 
ATOM   541  N  N   . HIS   A 1 64  ? 20.401  -0.589  6.044   1.00 15.57  ? 64  HIS   A N   1 
ATOM   542  C  CA  . HIS   A 1 64  ? 20.367  -1.387  7.261   1.00 18.95  ? 64  HIS   A CA  1 
ATOM   543  C  C   . HIS   A 1 64  ? 18.983  -2.018  7.425   1.00 16.70  ? 64  HIS   A C   1 
ATOM   544  O  O   . HIS   A 1 64  ? 18.870  -3.146  7.935   1.00 18.54  ? 64  HIS   A O   1 
ATOM   545  C  CB  . HIS   A 1 64  ? 20.666  -0.520  8.497   1.00 23.34  ? 64  HIS   A CB  1 
ATOM   546  C  CG  . HIS   A 1 64  ? 21.932  0.266   8.448   1.00 26.50  ? 64  HIS   A CG  1 
ATOM   547  N  ND1 . HIS   A 1 64  ? 23.160  -0.339  8.600   1.00 26.27  ? 64  HIS   A ND1 1 
ATOM   548  C  CD2 . HIS   A 1 64  ? 22.160  1.586   8.250   1.00 27.76  ? 64  HIS   A CD2 1 
ATOM   549  C  CE1 . HIS   A 1 64  ? 24.114  0.578   8.533   1.00 25.94  ? 64  HIS   A CE1 1 
ATOM   550  N  NE2 . HIS   A 1 64  ? 23.527  1.773   8.320   1.00 25.64  ? 64  HIS   A NE2 1 
ATOM   551  N  N   . ALA   A 1 65  ? 17.926  -1.291  7.059   1.00 14.73  ? 65  ALA   A N   1 
ATOM   552  C  CA  . ALA   A 1 65  ? 16.533  -1.715  7.105   1.00 14.84  ? 65  ALA   A CA  1 
ATOM   553  C  C   . ALA   A 1 65  ? 15.803  -0.906  6.031   1.00 13.76  ? 65  ALA   A C   1 
ATOM   554  O  O   . ALA   A 1 65  ? 16.417  -0.186  5.251   1.00 16.52  ? 65  ALA   A O   1 
ATOM   555  C  CB  . ALA   A 1 65  ? 15.957  -1.478  8.501   1.00 15.26  ? 65  ALA   A CB  1 
ATOM   556  N  N   . PHE   A 1 66  ? 14.490  -0.955  6.033   1.00 15.64  ? 66  PHE   A N   1 
ATOM   557  C  CA  . PHE   A 1 66  ? 13.726  -0.000  5.238   1.00 17.72  ? 66  PHE   A CA  1 
ATOM   558  C  C   . PHE   A 1 66  ? 12.893  0.901   6.146   1.00 16.91  ? 66  PHE   A C   1 
ATOM   559  O  O   . PHE   A 1 66  ? 12.411  0.458   7.206   1.00 16.38  ? 66  PHE   A O   1 
ATOM   560  C  CB  . PHE   A 1 66  ? 12.882  -0.692  4.160   1.00 20.58  ? 66  PHE   A CB  1 
ATOM   561  C  CG  . PHE   A 1 66  ? 11.816  -1.600  4.720   1.00 18.27  ? 66  PHE   A CG  1 
ATOM   562  C  CD1 . PHE   A 1 66  ? 10.576  -1.095  5.069   1.00 18.37  ? 66  PHE   A CD1 1 
ATOM   563  C  CD2 . PHE   A 1 66  ? 12.055  -2.964  4.897   1.00 19.12  ? 66  PHE   A CD2 1 
ATOM   564  C  CE1 . PHE   A 1 66  ? 9.600   -1.910  5.617   1.00 17.79  ? 66  PHE   A CE1 1 
ATOM   565  C  CE2 . PHE   A 1 66  ? 11.071  -3.798  5.436   1.00 19.03  ? 66  PHE   A CE2 1 
ATOM   566  C  CZ  . PHE   A 1 66  ? 9.829   -3.269  5.784   1.00 17.99  ? 66  PHE   A CZ  1 
ATOM   567  N  N   . ASN   A 1 67  ? 12.748  2.167   5.726   1.00 19.83  ? 67  ASN   A N   1 
ATOM   568  C  CA  . ASN   A 1 67  ? 12.031  3.164   6.503   1.00 17.40  ? 67  ASN   A CA  1 
ATOM   569  C  C   . ASN   A 1 67  ? 10.783  3.615   5.732   1.00 14.93  ? 67  ASN   A C   1 
ATOM   570  O  O   . ASN   A 1 67  ? 10.886  3.985   4.566   1.00 16.54  ? 67  ASN   A O   1 
ATOM   571  C  CB  . ASN   A 1 67  ? 12.879  4.411   6.789   1.00 21.95  ? 67  ASN   A CB  1 
ATOM   572  C  CG  . ASN   A 1 67  ? 14.168  4.201   7.559   1.00 25.05  ? 67  ASN   A CG  1 
ATOM   573  O  OD1 . ASN   A 1 67  ? 14.247  3.358   8.474   1.00 17.02  ? 67  ASN   A OD1 1 
ATOM   574  N  ND2 . ASN   A 1 67  ? 15.169  5.034   7.251   1.00 30.20  ? 67  ASN   A ND2 1 
ATOM   575  N  N   . VAL   A 1 68  ? 9.590   3.581   6.345   1.00 14.82  ? 68  VAL   A N   1 
ATOM   576  C  CA  . VAL   A 1 68  ? 8.410   4.227   5.776   1.00 14.91  ? 68  VAL   A CA  1 
ATOM   577  C  C   . VAL   A 1 68  ? 8.284   5.582   6.458   1.00 14.78  ? 68  VAL   A C   1 
ATOM   578  O  O   . VAL   A 1 68  ? 8.180   5.645   7.691   1.00 14.62  ? 68  VAL   A O   1 
ATOM   579  C  CB  . VAL   A 1 68  ? 7.142   3.381   5.957   1.00 15.84  ? 68  VAL   A CB  1 
ATOM   580  C  CG1 . VAL   A 1 68  ? 5.901   4.156   5.511   1.00 17.28  ? 68  VAL   A CG1 1 
ATOM   581  C  CG2 . VAL   A 1 68  ? 7.229   2.074   5.186   1.00 16.62  ? 68  VAL   A CG2 1 
ATOM   582  N  N   . GLU   A 1 69  ? 8.346   6.646   5.675   1.00 15.49  ? 69  GLU   A N   1 
ATOM   583  C  CA  . GLU   A 1 69  ? 8.406   7.995   6.205   1.00 15.52  ? 69  GLU   A CA  1 
ATOM   584  C  C   . GLU   A 1 69  ? 7.050   8.684   6.087   1.00 16.33  ? 69  GLU   A C   1 
ATOM   585  O  O   . GLU   A 1 69  ? 6.312   8.470   5.117   1.00 18.32  ? 69  GLU   A O   1 
ATOM   586  C  CB  . GLU   A 1 69  ? 9.365   8.774   5.332   1.00 18.35  ? 69  GLU   A CB  1 
ATOM   587  C  CG  . GLU   A 1 69  ? 10.750  8.238   5.400   1.00 20.50  ? 69  GLU   A CG  1 
ATOM   588  C  CD  . GLU   A 1 69  ? 11.546  8.709   4.195   1.00 21.58  ? 69  GLU   A CD  1 
ATOM   589  O  OE1 . GLU   A 1 69  ? 10.984  9.403   3.310   1.00 22.77  ? 69  GLU   A OE1 1 
ATOM   590  O  OE2 . GLU   A 1 69  ? 12.699  8.294   4.076   1.00 27.11  ? 69  GLU   A OE2 1 
ATOM   591  N  N   . PHE   A 1 70  ? 6.804   9.586   7.036   1.00 16.09  ? 70  PHE   A N   1 
ATOM   592  C  CA  . PHE   A 1 70  ? 5.553   10.318  7.102   1.00 15.32  ? 70  PHE   A CA  1 
ATOM   593  C  C   . PHE   A 1 70  ? 5.807   11.822  7.089   1.00 16.71  ? 70  PHE   A C   1 
ATOM   594  O  O   . PHE   A 1 70  ? 6.890   12.310  7.436   1.00 18.15  ? 70  PHE   A O   1 
ATOM   595  C  CB  . PHE   A 1 70  ? 4.811   9.971   8.396   1.00 15.93  ? 70  PHE   A CB  1 
ATOM   596  C  CG  . PHE   A 1 70  ? 4.274   8.570   8.343   1.00 14.72  ? 70  PHE   A CG  1 
ATOM   597  C  CD1 . PHE   A 1 70  ? 5.098   7.474   8.584   1.00 15.86  ? 70  PHE   A CD1 1 
ATOM   598  C  CD2 . PHE   A 1 70  ? 2.949   8.320   8.031   1.00 15.40  ? 70  PHE   A CD2 1 
ATOM   599  C  CE1 . PHE   A 1 70  ? 4.626   6.183   8.454   1.00 16.27  ? 70  PHE   A CE1 1 
ATOM   600  C  CE2 . PHE   A 1 70  ? 2.465   7.020   7.908   1.00 16.35  ? 70  PHE   A CE2 1 
ATOM   601  C  CZ  . PHE   A 1 70  ? 3.310   5.960   8.135   1.00 15.94  ? 70  PHE   A CZ  1 
ATOM   602  N  N   . ASP   A 1 71  ? 4.784   12.565  6.666   1.00 19.04  ? 71  ASP   A N   1 
ATOM   603  C  CA  . ASP   A 1 71  ? 4.806   14.006  6.810   1.00 19.92  ? 71  ASP   A CA  1 
ATOM   604  C  C   . ASP   A 1 71  ? 4.606   14.365  8.271   1.00 18.82  ? 71  ASP   A C   1 
ATOM   605  O  O   . ASP   A 1 71  ? 3.540   14.106  8.817   1.00 24.23  ? 71  ASP   A O   1 
ATOM   606  C  CB  . ASP   A 1 71  ? 3.705   14.637  5.955   1.00 22.61  ? 71  ASP   A CB  1 
ATOM   607  C  CG  . ASP   A 1 71  ? 3.506   16.131  6.228   1.00 23.51  ? 71  ASP   A CG  1 
ATOM   608  O  OD1 . ASP   A 1 71  ? 4.421   16.773  6.761   1.00 23.60  ? 71  ASP   A OD1 1 
ATOM   609  O  OD2 . ASP   A 1 71  ? 2.420   16.676  5.929   1.00 31.11  ? 71  ASP   A OD2 1 
ATOM   610  N  N   . ASP   A 1 72  ? 5.654   14.904  8.907   1.00 17.68  ? 72  ASP   A N   1 
ATOM   611  C  CA  . ASP   A 1 72  ? 5.569   15.263  10.321  1.00 18.28  ? 72  ASP   A CA  1 
ATOM   612  C  C   . ASP   A 1 72  ? 5.659   16.790  10.482  1.00 19.80  ? 72  ASP   A C   1 
ATOM   613  O  O   . ASP   A 1 72  ? 6.200   17.251  11.480  1.00 23.66  ? 72  ASP   A O   1 
ATOM   614  C  CB  . ASP   A 1 72  ? 6.702   14.626  11.124  1.00 19.31  ? 72  ASP   A CB  1 
ATOM   615  C  CG  . ASP   A 1 72  ? 8.081   15.099  10.711  1.00 19.34  ? 72  ASP   A CG  1 
ATOM   616  O  OD1 . ASP   A 1 72  ? 8.190   15.712  9.597   1.00 23.29  ? 72  ASP   A OD1 1 
ATOM   617  O  OD2 . ASP   A 1 72  ? 9.018   14.904  11.492  1.00 22.32  ? 72  ASP   A OD2 1 
ATOM   618  N  N   . SER   A 1 73  ? 5.198   17.540  9.482   1.00 20.29  ? 73  SER   A N   1 
ATOM   619  C  CA  . SER   A 1 73  ? 5.239   19.005  9.531   1.00 22.67  ? 73  SER   A CA  1 
ATOM   620  C  C   . SER   A 1 73  ? 3.964   19.618  10.140  1.00 24.26  ? 73  SER   A C   1 
ATOM   621  O  O   . SER   A 1 73  ? 3.853   20.832  10.243  1.00 25.66  ? 73  SER   A O   1 
ATOM   622  C  CB  . SER   A 1 73  ? 5.537   19.521  8.168   1.00 24.80  ? 73  SER   A CB  1 
ATOM   623  O  OG  . SER   A 1 73  ? 4.389   19.413  7.331   1.00 21.16  ? 73  SER   A OG  1 
ATOM   624  N  N   . GLN   A 1 74  ? 3.029   18.780  10.595  1.00 24.66  ? 74  GLN   A N   1 
ATOM   625  C  CA  . GLN   A 1 74  ? 1.863   19.186  11.368  1.00 27.45  ? 74  GLN   A CA  1 
ATOM   626  C  C   . GLN   A 1 74  ? 1.493   18.012  12.247  1.00 27.11  ? 74  GLN   A C   1 
ATOM   627  O  O   . GLN   A 1 74  ? 1.924   16.936  11.897  1.00 23.51  ? 74  GLN   A O   1 
ATOM   628  C  CB  . GLN   A 1 74  ? 0.645   19.337  10.457  1.00 34.28  ? 74  GLN   A CB  1 
ATOM   629  C  CG  . GLN   A 1 74  ? 0.750   20.494  9.499   1.00 33.23  ? 74  GLN   A CG  1 
ATOM   630  C  CD  . GLN   A 1 74  ? -0.585  20.653  8.837   1.00 34.01  ? 74  GLN   A CD  1 
ATOM   631  O  OE1 . GLN   A 1 74  ? -0.794  20.177  7.723   1.00 35.62  ? 74  GLN   A OE1 1 
ATOM   632  N  NE2 . GLN   A 1 74  ? -1.497  21.312  9.537   1.00 39.44  ? 74  GLN   A NE2 1 
ATOM   633  N  N   . ASP   A 1 75  ? 0.660   18.224  13.286  1.00 32.02  ? 75  ASP   A N   1 
ATOM   634  C  CA  . ASP   A 1 75  ? 0.157   17.154  14.138  1.00 32.23  ? 75  ASP   A CA  1 
ATOM   635  C  C   . ASP   A 1 75  ? -0.896  16.393  13.351  1.00 29.72  ? 75  ASP   A C   1 
ATOM   636  O  O   . ASP   A 1 75  ? -2.072  16.757  13.321  1.00 45.16  ? 75  ASP   A O   1 
ATOM   637  C  CB  . ASP   A 1 75  ? -0.405  17.616  15.491  1.00 36.92  ? 75  ASP   A CB  1 
ATOM   638  C  CG  . ASP   A 1 75  ? 0.646   17.928  16.540  1.00 40.76  ? 75  ASP   A CG  1 
ATOM   639  O  OD1 . ASP   A 1 75  ? 1.765   17.396  16.422  1.00 39.09  ? 75  ASP   A OD1 1 
ATOM   640  O  OD2 . ASP   A 1 75  ? 0.326   18.680  17.482  1.00 49.43  ? 75  ASP   A OD2 1 
ATOM   641  N  N   . LYS   A 1 76  ? -0.411  15.385  12.647  1.00 26.70  ? 76  LYS   A N   1 
ATOM   642  C  CA  . LYS   A 1 76  ? -1.285  14.480  11.940  1.00 27.23  ? 76  LYS   A CA  1 
ATOM   643  C  C   . LYS   A 1 76  ? -1.387  13.237  12.815  1.00 31.96  ? 76  LYS   A C   1 
ATOM   644  O  O   . LYS   A 1 76  ? -2.297  13.101  13.639  1.00 40.19  ? 76  LYS   A O   1 
ATOM   645  C  CB  . LYS   A 1 76  ? -0.698  14.287  10.535  1.00 26.11  ? 76  LYS   A CB  1 
ATOM   646  C  CG  . LYS   A 1 76  ? -0.871  15.468  9.594   1.00 32.41  ? 76  LYS   A CG  1 
ATOM   647  C  CD  . LYS   A 1 76  ? -0.245  15.255  8.219   1.00 31.60  ? 76  LYS   A CD  1 
ATOM   648  C  CE  . LYS   A 1 76  ? -0.742  16.264  7.204   1.00 29.84  ? 76  LYS   A CE  1 
ATOM   649  N  NZ  . LYS   A 1 76  ? -0.342  15.951  5.812   1.00 33.40  ? 76  LYS   A NZ  1 
ATOM   650  N  N   . ALA   A 1 77  ? -0.366  12.406  12.716  1.00 27.05  ? 77  ALA   A N   1 
ATOM   651  C  CA  . ALA   A 1 77  ? -0.336  11.115  13.375  1.00 20.57  ? 77  ALA   A CA  1 
ATOM   652  C  C   . ALA   A 1 77  ? 0.461   11.321  14.663  1.00 18.64  ? 77  ALA   A C   1 
ATOM   653  O  O   . ALA   A 1 77  ? 1.644   11.713  14.591  1.00 22.49  ? 77  ALA   A O   1 
ATOM   654  C  CB  . ALA   A 1 77  ? 0.384   10.190  12.436  1.00 24.13  ? 77  ALA   A CB  1 
ATOM   655  N  N   . VAL   A 1 78  ? -0.180  11.112  15.815  1.00 16.83  ? 78  VAL   A N   1 
ATOM   656  C  CA  . VAL   A 1 78  ? 0.472   11.398  17.091  1.00 17.38  ? 78  VAL   A CA  1 
ATOM   657  C  C   . VAL   A 1 78  ? 0.225   10.291  18.099  1.00 16.46  ? 78  VAL   A C   1 
ATOM   658  O  O   . VAL   A 1 78  ? -0.799  9.602   18.097  1.00 19.40  ? 78  VAL   A O   1 
ATOM   659  C  CB  . VAL   A 1 78  ? 0.077   12.752  17.692  1.00 21.01  ? 78  VAL   A CB  1 
ATOM   660  C  CG1 . VAL   A 1 78  ? 0.380   13.940  16.801  1.00 23.23  ? 78  VAL   A CG1 1 
ATOM   661  C  CG2 . VAL   A 1 78  ? -1.362  12.763  18.119  1.00 25.08  ? 78  VAL   A CG2 1 
ATOM   662  N  N   . LEU   A 1 79  ? 1.214   10.159  18.977  1.00 15.53  ? 79  LEU   A N   1 
ATOM   663  C  CA  . LEU   A 1 79  ? 1.144   9.287   20.129  1.00 14.95  ? 79  LEU   A CA  1 
ATOM   664  C  C   . LEU   A 1 79  ? 1.134   10.171  21.368  1.00 15.45  ? 79  LEU   A C   1 
ATOM   665  O  O   . LEU   A 1 79  ? 1.943   11.095  21.490  1.00 16.32  ? 79  LEU   A O   1 
ATOM   666  C  CB  . LEU   A 1 79  ? 2.399   8.383   20.073  1.00 16.19  ? 79  LEU   A CB  1 
ATOM   667  C  CG  . LEU   A 1 79  ? 2.519   7.329   21.153  1.00 16.90  ? 79  LEU   A CG  1 
ATOM   668  C  CD1 . LEU   A 1 79  ? 1.485   6.251   20.899  1.00 22.56  ? 79  LEU   A CD1 1 
ATOM   669  C  CD2 . LEU   A 1 79  ? 3.904   6.693   21.091  1.00 16.98  ? 79  LEU   A CD2 1 
ATOM   670  N  N   . LYS   A 1 80  ? 0.271   9.831   22.302  1.00 17.13  ? 80  LYS   A N   1 
ATOM   671  C  CA  A LYS   A 1 80  ? 0.254   10.534  23.581  0.50 17.48  ? 80  LYS   A CA  1 
ATOM   672  C  CA  B LYS   A 1 80  ? 0.184   10.587  23.575  0.50 17.48  ? 80  LYS   A CA  1 
ATOM   673  C  C   . LYS   A 1 80  ? -0.302  9.585   24.626  1.00 16.51  ? 80  LYS   A C   1 
ATOM   674  O  O   . LYS   A 1 80  ? -0.557  8.420   24.326  1.00 16.80  ? 80  LYS   A O   1 
ATOM   675  C  CB  A LYS   A 1 80  ? -0.517  11.845  23.530  0.50 24.75  ? 80  LYS   A CB  1 
ATOM   676  C  CB  B LYS   A 1 80  ? -0.830  11.738  23.522  0.50 24.75  ? 80  LYS   A CB  1 
ATOM   677  C  CG  A LYS   A 1 80  ? -1.983  11.704  23.190  0.50 25.23  ? 80  LYS   A CG  1 
ATOM   678  C  CG  B LYS   A 1 80  ? -0.723  12.758  22.397  0.50 25.23  ? 80  LYS   A CG  1 
ATOM   679  C  CD  A LYS   A 1 80  ? -2.735  13.014  23.223  0.50 31.20  ? 80  LYS   A CD  1 
ATOM   680  C  CD  B LYS   A 1 80  ? -1.754  13.859  22.523  0.50 31.20  ? 80  LYS   A CD  1 
ATOM   681  C  CE  A LYS   A 1 80  ? -2.706  13.746  21.898  0.50 10.00  ? 80  LYS   A CE  1 
ATOM   682  C  CE  B LYS   A 1 80  ? -2.744  13.898  21.379  0.50 10.00  ? 80  LYS   A CE  1 
ATOM   683  N  NZ  A LYS   A 1 80  ? -3.858  13.377  21.043  0.50 10.00  ? 80  LYS   A NZ  1 
ATOM   684  N  NZ  B LYS   A 1 80  ? -2.805  15.230  20.731  0.50 10.00  ? 80  LYS   A NZ  1 
ATOM   685  N  N   . GLY   A 1 81  ? -0.444  10.085  25.851  1.00 17.66  ? 81  GLY   A N   1 
ATOM   686  C  CA  . GLY   A 1 81  ? -0.884  9.239   26.938  1.00 18.88  ? 81  GLY   A CA  1 
ATOM   687  C  C   . GLY   A 1 81  ? 0.161   8.201   27.295  1.00 17.09  ? 81  GLY   A C   1 
ATOM   688  O  O   . GLY   A 1 81  ? 1.354   8.415   27.112  1.00 18.08  ? 81  GLY   A O   1 
ATOM   689  N  N   . GLY   A 1 82  ? -0.301  7.066   27.798  1.00 20.71  ? 82  GLY   A N   1 
ATOM   690  C  CA  . GLY   A 1 82  ? 0.632   6.060   28.264  1.00 23.06  ? 82  GLY   A CA  1 
ATOM   691  C  C   . GLY   A 1 82  ? 1.517   6.673   29.342  1.00 19.18  ? 82  GLY   A C   1 
ATOM   692  O  O   . GLY   A 1 82  ? 1.028   7.393   30.215  1.00 24.11  ? 82  GLY   A O   1 
ATOM   693  N  N   . PRO   A 1 83  ? 2.857   6.496   29.257  1.00 18.16  ? 83  PRO   A N   1 
ATOM   694  C  CA  . PRO   A 1 83  ? 3.774   7.114   30.204  1.00 19.68  ? 83  PRO   A CA  1 
ATOM   695  C  C   . PRO   A 1 83  ? 4.181   8.534   29.816  1.00 17.88  ? 83  PRO   A C   1 
ATOM   696  O  O   . PRO   A 1 83  ? 5.015   9.119   30.512  1.00 22.14  ? 83  PRO   A O   1 
ATOM   697  C  CB  . PRO   A 1 83  ? 5.039   6.250   30.039  1.00 19.45  ? 83  PRO   A CB  1 
ATOM   698  C  CG  . PRO   A 1 83  ? 5.040   5.886   28.586  1.00 17.63  ? 83  PRO   A CG  1 
ATOM   699  C  CD  . PRO   A 1 83  ? 3.570   5.700   28.242  1.00 17.52  ? 83  PRO   A CD  1 
ATOM   700  N  N   . LEU   A 1 84  ? 3.658   9.044   28.691  1.00 15.88  ? 84  LEU   A N   1 
ATOM   701  C  CA  . LEU   A 1 84  ? 4.196   10.261  28.093  1.00 16.53  ? 84  LEU   A CA  1 
ATOM   702  C  C   . LEU   A 1 84  ? 3.518   11.492  28.669  1.00 17.85  ? 84  LEU   A C   1 
ATOM   703  O  O   . LEU   A 1 84  ? 2.330   11.491  28.974  1.00 21.25  ? 84  LEU   A O   1 
ATOM   704  C  CB  . LEU   A 1 84  ? 3.969   10.223  26.580  1.00 15.06  ? 84  LEU   A CB  1 
ATOM   705  C  CG  . LEU   A 1 84  ? 4.561   8.997   25.873  1.00 14.52  ? 84  LEU   A CG  1 
ATOM   706  C  CD1 . LEU   A 1 84  ? 4.083   8.970   24.430  1.00 15.26  ? 84  LEU   A CD1 1 
ATOM   707  C  CD2 . LEU   A 1 84  ? 6.107   8.994   25.978  1.00 15.50  ? 84  LEU   A CD2 1 
ATOM   708  N  N   A ASP   A 1 85  ? 4.311   12.566  28.721  0.50 19.17  ? 85  ASP   A N   1 
ATOM   709  N  N   B ASP   A 1 85  ? 4.238   12.596  28.744  0.50 18.82  ? 85  ASP   A N   1 
ATOM   710  C  CA  A ASP   A 1 85  ? 3.834   13.929  28.943  0.50 23.13  ? 85  ASP   A CA  1 
ATOM   711  C  CA  B ASP   A 1 85  ? 3.534   13.772  29.228  0.50 20.82  ? 85  ASP   A CA  1 
ATOM   712  C  C   A ASP   A 1 85  ? 3.838   14.663  27.600  0.50 21.53  ? 85  ASP   A C   1 
ATOM   713  C  C   B ASP   A 1 85  ? 3.463   14.818  28.125  0.50 18.73  ? 85  ASP   A C   1 
ATOM   714  O  O   A ASP   A 1 85  ? 4.827   14.594  26.872  0.50 25.38  ? 85  ASP   A O   1 
ATOM   715  O  O   B ASP   A 1 85  ? 3.274   15.984  28.408  0.50 22.39  ? 85  ASP   A O   1 
ATOM   716  C  CB  A ASP   A 1 85  ? 4.694   14.648  29.988  0.50 24.21  ? 85  ASP   A CB  1 
ATOM   717  C  CB  B ASP   A 1 85  ? 4.144   14.274  30.534  0.50 20.32  ? 85  ASP   A CB  1 
ATOM   718  C  CG  A ASP   A 1 85  ? 4.670   14.025  31.385  0.50 27.22  ? 85  ASP   A CG  1 
ATOM   719  C  CG  B ASP   A 1 85  ? 5.579   14.707  30.309  0.50 20.61  ? 85  ASP   A CG  1 
ATOM   720  O  OD1 A ASP   A 1 85  ? 3.686   13.330  31.705  0.50 30.84  ? 85  ASP   A OD1 1 
ATOM   721  O  OD1 B ASP   A 1 85  ? 6.004   14.667  29.134  0.50 24.19  ? 85  ASP   A OD1 1 
ATOM   722  O  OD2 A ASP   A 1 85  ? 5.651   14.246  32.160  0.50 29.23  ? 85  ASP   A OD2 1 
ATOM   723  O  OD2 B ASP   A 1 85  ? 6.264   15.037  31.300  0.50 26.25  ? 85  ASP   A OD2 1 
ATOM   724  N  N   A GLY   A 1 86  ? 2.728   15.331  27.255  0.50 24.05  ? 86  GLY   A N   1 
ATOM   725  N  N   B GLY   A 1 86  ? 3.621   14.406  26.869  0.50 18.36  ? 86  GLY   A N   1 
ATOM   726  C  CA  A GLY   A 1 86  ? 2.663   16.064  25.998  0.50 21.06  ? 86  GLY   A CA  1 
ATOM   727  C  CA  B GLY   A 1 86  ? 3.601   15.344  25.761  0.50 20.34  ? 86  GLY   A CA  1 
ATOM   728  C  C   A GLY   A 1 86  ? 2.412   15.147  24.794  0.50 23.78  ? 86  GLY   A C   1 
ATOM   729  C  C   B GLY   A 1 86  ? 2.963   14.707  24.532  0.50 19.60  ? 86  GLY   A C   1 
ATOM   730  O  O   A GLY   A 1 86  ? 1.689   14.158  24.884  0.50 24.00  ? 86  GLY   A O   1 
ATOM   731  O  O   B GLY   A 1 86  ? 2.495   13.574  24.621  0.50 18.83  ? 86  GLY   A O   1 
ATOM   732  N  N   A THR   A 1 87  ? 3.005   15.474  23.640  0.50 22.89  ? 87  THR   A N   1 
ATOM   733  N  N   B THR   A 1 87  ? 2.918   15.476  23.424  0.50 18.73  ? 87  THR   A N   1 
ATOM   734  C  CA  A THR   A 1 87  ? 2.570   14.807  22.425  0.50 22.34  ? 87  THR   A CA  1 
ATOM   735  C  CA  B THR   A 1 87  ? 2.462   15.018  22.119  0.50 17.88  ? 87  THR   A CA  1 
ATOM   736  C  C   A THR   A 1 87  ? 3.760   14.553  21.514  0.50 16.57  ? 87  THR   A C   1 
ATOM   737  C  C   B THR   A 1 87  ? 3.677   14.664  21.275  0.50 16.06  ? 87  THR   A C   1 
ATOM   738  O  O   A THR   A 1 87  ? 4.696   15.361  21.458  0.50 16.55  ? 87  THR   A O   1 
ATOM   739  O  O   B THR   A 1 87  ? 4.571   15.489  21.053  0.50 16.97  ? 87  THR   A O   1 
ATOM   740  C  CB  A THR   A 1 87  ? 1.474   15.618  21.728  0.50 22.56  ? 87  THR   A CB  1 
ATOM   741  C  CB  B THR   A 1 87  ? 1.698   16.094  21.333  0.50 19.16  ? 87  THR   A CB  1 
ATOM   742  O  OG1 A THR   A 1 87  ? 2.058   16.896  21.481  0.50 23.06  ? 87  THR   A OG1 1 
ATOM   743  O  OG1 B THR   A 1 87  ? 0.524   16.503  22.036  0.50 24.54  ? 87  THR   A OG1 1 
ATOM   744  C  CG2 A THR   A 1 87  ? 0.244   15.791  22.588  0.50 25.08  ? 87  THR   A CG2 1 
ATOM   745  C  CG2 B THR   A 1 87  ? 1.309   15.603  19.957  0.50 20.26  ? 87  THR   A CG2 1 
ATOM   746  N  N   . TYR   A 1 88  ? 3.687   13.419  20.811  1.00 14.79  ? 88  TYR   A N   1 
ATOM   747  C  CA  . TYR   A 1 88  ? 4.779   12.935  20.002  1.00 13.73  ? 88  TYR   A CA  1 
ATOM   748  C  C   . TYR   A 1 88  ? 4.274   12.634  18.605  1.00 13.68  ? 88  TYR   A C   1 
ATOM   749  O  O   . TYR   A 1 88  ? 3.327   11.888  18.417  1.00 17.63  ? 88  TYR   A O   1 
ATOM   750  C  CB  . TYR   A 1 88  ? 5.420   11.698  20.624  1.00 14.16  ? 88  TYR   A CB  1 
ATOM   751  C  CG  . TYR   A 1 88  ? 6.145   11.922  21.921  1.00 13.21  ? 88  TYR   A CG  1 
ATOM   752  C  CD1 . TYR   A 1 88  ? 5.484   12.275  23.107  1.00 14.45  ? 88  TYR   A CD1 1 
ATOM   753  C  CD2 . TYR   A 1 88  ? 7.531   11.752  21.955  1.00 12.66  ? 88  TYR   A CD2 1 
ATOM   754  C  CE1 . TYR   A 1 88  ? 6.203   12.468  24.285  1.00 14.55  ? 88  TYR   A CE1 1 
ATOM   755  C  CE2 . TYR   A 1 88  ? 8.232   11.871  23.136  1.00 12.78  ? 88  TYR   A CE2 1 
ATOM   756  C  CZ  . TYR   A 1 88  ? 7.578   12.227  24.308  1.00 12.93  ? 88  TYR   A CZ  1 
ATOM   757  O  OH  . TYR   A 1 88  ? 8.292   12.343  25.469  1.00 13.63  ? 88  TYR   A OH  1 
ATOM   758  N  N   . ARG   A 1 89  ? 4.951   13.178  17.605  1.00 12.99  ? 89  ARG   A N   1 
ATOM   759  C  CA  . ARG   A 1 89  ? 4.540   13.065  16.216  1.00 13.62  ? 89  ARG   A CA  1 
ATOM   760  C  C   . ARG   A 1 89  ? 5.261   11.933  15.505  1.00 12.03  ? 89  ARG   A C   1 
ATOM   761  O  O   . ARG   A 1 89  ? 6.489   11.817  15.581  1.00 12.62  ? 89  ARG   A O   1 
ATOM   762  C  CB  . ARG   A 1 89  ? 4.912   14.376  15.519  1.00 17.27  ? 89  ARG   A CB  1 
ATOM   763  C  CG  . ARG   A 1 89  ? 4.203   14.554  14.189  1.00 22.16  ? 89  ARG   A CG  1 
ATOM   764  C  CD  . ARG   A 1 89  ? 4.451   15.998  13.744  1.00 23.38  ? 89  ARG   A CD  1 
ATOM   765  N  NE  . ARG   A 1 89  ? 3.830   17.016  14.594  1.00 23.32  ? 89  ARG   A NE  1 
ATOM   766  C  CZ  . ARG   A 1 89  ? 3.953   18.329  14.437  1.00 21.91  ? 89  ARG   A CZ  1 
ATOM   767  N  NH1 . ARG   A 1 89  ? 4.771   18.837  13.532  1.00 24.94  ? 89  ARG   A NH1 1 
ATOM   768  N  NH2 . ARG   A 1 89  ? 3.322   19.177  15.246  1.00 25.63  ? 89  ARG   A NH2 1 
ATOM   769  N  N   . LEU   A 1 90  ? 4.479   11.118  14.782  1.00 13.25  ? 90  LEU   A N   1 
ATOM   770  C  CA  . LEU   A 1 90  ? 5.062   10.034  14.010  1.00 13.11  ? 90  LEU   A CA  1 
ATOM   771  C  C   . LEU   A 1 90  ? 5.887   10.589  12.861  1.00 13.38  ? 90  LEU   A C   1 
ATOM   772  O  O   . LEU   A 1 90  ? 5.396   11.401  12.064  1.00 15.50  ? 90  LEU   A O   1 
ATOM   773  C  CB  . LEU   A 1 90  ? 3.936   9.178   13.431  1.00 14.11  ? 90  LEU   A CB  1 
ATOM   774  C  CG  . LEU   A 1 90  ? 4.352   8.001   12.528  1.00 14.60  ? 90  LEU   A CG  1 
ATOM   775  C  CD1 . LEU   A 1 90  ? 5.096   6.922   13.320  1.00 14.95  ? 90  LEU   A CD1 1 
ATOM   776  C  CD2 . LEU   A 1 90  ? 3.115   7.406   11.877  1.00 16.74  ? 90  LEU   A CD2 1 
ATOM   777  N  N   . ILE   A 1 91  ? 7.136   10.138  12.785  1.00 12.62  ? 91  ILE   A N   1 
ATOM   778  C  CA  . ILE   A 1 91  ? 8.005   10.512  11.674  1.00 13.11  ? 91  ILE   A CA  1 
ATOM   779  C  C   . ILE   A 1 91  ? 8.277   9.355   10.715  1.00 12.18  ? 91  ILE   A C   1 
ATOM   780  O  O   . ILE   A 1 91  ? 8.347   9.550   9.507   1.00 13.26  ? 91  ILE   A O   1 
ATOM   781  C  CB  . ILE   A 1 91  ? 9.324   11.174  12.169  1.00 14.07  ? 91  ILE   A CB  1 
ATOM   782  C  CG1 . ILE   A 1 91  ? 10.205  11.583  10.982  1.00 16.43  ? 91  ILE   A CG1 1 
ATOM   783  C  CG2 . ILE   A 1 91  ? 10.073  10.318  13.180  1.00 14.73  ? 91  ILE   A CG2 1 
ATOM   784  C  CD1 . ILE   A 1 91  ? 11.334  12.540  11.404  1.00 19.71  ? 91  ILE   A CD1 1 
ATOM   785  N  N   . GLN   A 1 92  ? 8.412   8.122   11.244  1.00 12.77  ? 92  GLN   A N   1 
ATOM   786  C  CA  . GLN   A 1 92  ? 8.735   7.000   10.373  1.00 13.07  ? 92  GLN   A CA  1 
ATOM   787  C  C   . GLN   A 1 92  ? 8.483   5.722   11.143  1.00 11.58  ? 92  GLN   A C   1 
ATOM   788  O  O   . GLN   A 1 92  ? 8.408   5.732   12.370  1.00 12.04  ? 92  GLN   A O   1 
ATOM   789  C  CB  . GLN   A 1 92  ? 10.187  7.052   9.856   1.00 13.70  ? 92  GLN   A CB  1 
ATOM   790  C  CG  . GLN   A 1 92  ? 11.255  6.940   10.943  1.00 14.39  ? 92  GLN   A CG  1 
ATOM   791  C  CD  . GLN   A 1 92  ? 11.899  5.583   10.855  1.00 13.86  ? 92  GLN   A CD  1 
ATOM   792  O  OE1 . GLN   A 1 92  ? 11.469  4.618   11.476  1.00 13.60  ? 92  GLN   A OE1 1 
ATOM   793  N  NE2 . GLN   A 1 92  ? 12.897  5.438   9.999   1.00 16.64  ? 92  GLN   A NE2 1 
ATOM   794  N  N   . PHE   A 1 93  ? 8.408   4.612   10.400  1.00 11.80  ? 93  PHE   A N   1 
ATOM   795  C  CA  . PHE   A 1 93  ? 8.545   3.310   11.003  1.00 12.08  ? 93  PHE   A CA  1 
ATOM   796  C  C   . PHE   A 1 93  ? 9.535   2.478   10.204  1.00 11.13  ? 93  PHE   A C   1 
ATOM   797  O  O   . PHE   A 1 93  ? 9.796   2.703   9.032   1.00 12.92  ? 93  PHE   A O   1 
ATOM   798  C  CB  . PHE   A 1 93  ? 7.200   2.597   11.223  1.00 12.32  ? 93  PHE   A CB  1 
ATOM   799  C  CG  . PHE   A 1 93  ? 6.450   2.123   10.011  1.00 12.66  ? 93  PHE   A CG  1 
ATOM   800  C  CD1 . PHE   A 1 93  ? 6.848   0.986   9.319   1.00 13.69  ? 93  PHE   A CD1 1 
ATOM   801  C  CD2 . PHE   A 1 93  ? 5.307   2.800   9.576   1.00 12.98  ? 93  PHE   A CD2 1 
ATOM   802  C  CE1 . PHE   A 1 93  ? 6.158   0.549   8.194   1.00 13.34  ? 93  PHE   A CE1 1 
ATOM   803  C  CE2 . PHE   A 1 93  ? 4.599   2.348   8.473   1.00 14.04  ? 93  PHE   A CE2 1 
ATOM   804  C  CZ  . PHE   A 1 93  ? 5.017   1.246   7.789   1.00 13.93  ? 93  PHE   A CZ  1 
ATOM   805  N  N   . HIS   A 1 94  ? 10.029  1.426   10.881  1.00 11.53  ? 94  HIS   A N   1 
ATOM   806  C  CA  . HIS   A 1 94  ? 10.920  0.452   10.290  1.00 10.91  ? 94  HIS   A CA  1 
ATOM   807  C  C   . HIS   A 1 94  ? 10.808  -0.847  11.073  1.00 10.92  ? 94  HIS   A C   1 
ATOM   808  O  O   . HIS   A 1 94  ? 10.174  -0.866  12.121  1.00 11.05  ? 94  HIS   A O   1 
ATOM   809  C  CB  . HIS   A 1 94  ? 12.386  0.948   10.261  1.00 12.12  ? 94  HIS   A CB  1 
ATOM   810  C  CG  . HIS   A 1 94  ? 12.895  1.184   11.649  1.00 10.89  ? 94  HIS   A CG  1 
ATOM   811  N  ND1 . HIS   A 1 94  ? 12.708  2.360   12.339  1.00 11.01  ? 94  HIS   A ND1 1 
ATOM   812  C  CD2 . HIS   A 1 94  ? 13.504  0.346   12.526  1.00 11.04  ? 94  HIS   A CD2 1 
ATOM   813  C  CE1 . HIS   A 1 94  ? 13.166  2.235   13.559  1.00 10.82  ? 94  HIS   A CE1 1 
ATOM   814  N  NE2 . HIS   A 1 94  ? 13.683  0.985   13.718  1.00 10.96  ? 94  HIS   A NE2 1 
ATOM   815  N  N   . PHE   A 1 95  ? 11.503  -1.888  10.603  1.00 11.23  ? 95  PHE   A N   1 
ATOM   816  C  CA  . PHE   A 1 95  ? 11.531  -3.181  11.272  1.00 11.11  ? 95  PHE   A CA  1 
ATOM   817  C  C   . PHE   A 1 95  ? 12.976  -3.603  11.455  1.00 10.97  ? 95  PHE   A C   1 
ATOM   818  O  O   . PHE   A 1 95  ? 13.883  -3.153  10.762  1.00 12.20  ? 95  PHE   A O   1 
ATOM   819  C  CB  . PHE   A 1 95  ? 10.803  -4.254  10.443  1.00 11.68  ? 95  PHE   A CB  1 
ATOM   820  C  CG  . PHE   A 1 95  ? 9.347   -3.981  10.147  1.00 11.26  ? 95  PHE   A CG  1 
ATOM   821  C  CD1 . PHE   A 1 95  ? 8.980   -3.102  9.137   1.00 12.70  ? 95  PHE   A CD1 1 
ATOM   822  C  CD2 . PHE   A 1 95  ? 8.350   -4.662  10.837  1.00 13.03  ? 95  PHE   A CD2 1 
ATOM   823  C  CE1 . PHE   A 1 95  ? 7.645   -2.916  8.818   1.00 14.02  ? 95  PHE   A CE1 1 
ATOM   824  C  CE2 . PHE   A 1 95  ? 7.021   -4.492  10.500  1.00 13.38  ? 95  PHE   A CE2 1 
ATOM   825  C  CZ  . PHE   A 1 95  ? 6.667   -3.591  9.495   1.00 13.95  ? 95  PHE   A CZ  1 
ATOM   826  N  N   . HIS   A 1 96  ? 13.139  -4.564  12.380  1.00 10.84  ? 96  HIS   A N   1 
ATOM   827  C  CA  . HIS   A 1 96  ? 14.332  -5.382  12.499  1.00 11.04  ? 96  HIS   A CA  1 
ATOM   828  C  C   . HIS   A 1 96  ? 13.865  -6.835  12.394  1.00 10.90  ? 96  HIS   A C   1 
ATOM   829  O  O   . HIS   A 1 96  ? 12.794  -7.173  12.861  1.00 11.18  ? 96  HIS   A O   1 
ATOM   830  C  CB  . HIS   A 1 96  ? 15.051  -5.194  13.853  1.00 11.10  ? 96  HIS   A CB  1 
ATOM   831  C  CG  . HIS   A 1 96  ? 15.307  -3.748  14.152  1.00 10.71  ? 96  HIS   A CG  1 
ATOM   832  N  ND1 . HIS   A 1 96  ? 16.549  -3.177  13.979  1.00 11.52  ? 96  HIS   A ND1 1 
ATOM   833  C  CD2 . HIS   A 1 96  ? 14.500  -2.751  14.602  1.00 10.88  ? 96  HIS   A CD2 1 
ATOM   834  C  CE1 . HIS   A 1 96  ? 16.503  -1.877  14.306  1.00 11.26  ? 96  HIS   A CE1 1 
ATOM   835  N  NE2 . HIS   A 1 96  ? 15.235  -1.585  14.681  1.00 10.91  ? 96  HIS   A NE2 1 
ATOM   836  N  N   . TRP   A 1 97  ? 14.659  -7.692  11.761  1.00 10.67  ? 97  TRP   A N   1 
ATOM   837  C  CA  . TRP   A 1 97  ? 14.243  -9.076  11.560  1.00 11.79  ? 97  TRP   A CA  1 
ATOM   838  C  C   . TRP   A 1 97  ? 15.455  -9.985  11.421  1.00 11.07  ? 97  TRP   A C   1 
ATOM   839  O  O   . TRP   A 1 97  ? 16.618  -9.558  11.350  1.00 11.88  ? 97  TRP   A O   1 
ATOM   840  C  CB  . TRP   A 1 97  ? 13.322  -9.207  10.325  1.00 12.03  ? 97  TRP   A CB  1 
ATOM   841  C  CG  . TRP   A 1 97  ? 13.988  -8.821  9.025   1.00 11.75  ? 97  TRP   A CG  1 
ATOM   842  C  CD1 . TRP   A 1 97  ? 14.688  -9.645  8.187   1.00 12.91  ? 97  TRP   A CD1 1 
ATOM   843  C  CD2 . TRP   A 1 97  ? 14.065  -7.505  8.452   1.00 11.77  ? 97  TRP   A CD2 1 
ATOM   844  N  NE1 . TRP   A 1 97  ? 15.117  -8.934  7.089   1.00 13.43  ? 97  TRP   A NE1 1 
ATOM   845  C  CE2 . TRP   A 1 97  ? 14.765  -7.613  7.229   1.00 12.73  ? 97  TRP   A CE2 1 
ATOM   846  C  CE3 . TRP   A 1 97  ? 13.567  -6.243  8.848   1.00 11.94  ? 97  TRP   A CE3 1 
ATOM   847  C  CZ2 . TRP   A 1 97  ? 14.959  -6.518  6.379   1.00 12.66  ? 97  TRP   A CZ2 1 
ATOM   848  C  CZ3 . TRP   A 1 97  ? 13.807  -5.159  8.031   1.00 13.10  ? 97  TRP   A CZ3 1 
ATOM   849  C  CH2 . TRP   A 1 97  ? 14.472  -5.307  6.806   1.00 13.46  ? 97  TRP   A CH2 1 
ATOM   850  N  N   . GLY   A 1 98  ? 15.150  -11.292 11.458  1.00 12.20  ? 98  GLY   A N   1 
ATOM   851  C  CA  . GLY   A 1 98  ? 16.182  -12.288 11.514  1.00 12.35  ? 98  GLY   A CA  1 
ATOM   852  C  C   . GLY   A 1 98  ? 16.375  -13.024 10.190  1.00 12.33  ? 98  GLY   A C   1 
ATOM   853  O  O   . GLY   A 1 98  ? 15.645  -12.889 9.206   1.00 13.49  ? 98  GLY   A O   1 
ATOM   854  N  N   . SER   A 1 99  ? 17.375  -13.915 10.196  1.00 13.43  ? 99  SER   A N   1 
ATOM   855  C  CA  . SER   A 1 99  ? 17.581  -14.864 9.099   1.00 14.66  ? 99  SER   A CA  1 
ATOM   856  C  C   . SER   A 1 99  ? 16.700  -16.118 9.245   1.00 14.75  ? 99  SER   A C   1 
ATOM   857  O  O   . SER   A 1 99  ? 16.527  -16.859 8.281   1.00 17.27  ? 99  SER   A O   1 
ATOM   858  C  CB  . SER   A 1 99  ? 19.043  -15.231 9.030   1.00 17.06  ? 99  SER   A CB  1 
ATOM   859  O  OG  . SER   A 1 99  ? 19.500  -15.726 10.297  1.00 16.43  ? 99  SER   A OG  1 
ATOM   860  N  N   . LEU   A 1 100 ? 16.155  -16.328 10.454  1.00 14.98  ? 100 LEU   A N   1 
ATOM   861  C  CA  . LEU   A 1 100 ? 15.364  -17.499 10.831  1.00 16.43  ? 100 LEU   A CA  1 
ATOM   862  C  C   . LEU   A 1 100 ? 14.203  -16.988 11.663  1.00 15.11  ? 100 LEU   A C   1 
ATOM   863  O  O   . LEU   A 1 100 ? 14.329  -15.970 12.331  1.00 15.31  ? 100 LEU   A O   1 
ATOM   864  C  CB  . LEU   A 1 100 ? 16.205  -18.416 11.727  1.00 19.39  ? 100 LEU   A CB  1 
ATOM   865  C  CG  . LEU   A 1 100 ? 17.509  -18.901 11.126  1.00 20.27  ? 100 LEU   A CG  1 
ATOM   866  C  CD1 . LEU   A 1 100 ? 18.378  -19.539 12.205  1.00 27.66  ? 100 LEU   A CD1 1 
ATOM   867  C  CD2 . LEU   A 1 100 ? 17.184  -19.902 10.030  1.00 26.30  ? 100 LEU   A CD2 1 
ATOM   868  N  N   . ASP   A 1 101 ? 13.099  -17.729 11.698  1.00 16.04  ? 101 ASP   A N   1 
ATOM   869  C  CA  . ASP   A 1 101 ? 11.904  -17.244 12.377  1.00 16.07  ? 101 ASP   A CA  1 
ATOM   870  C  C   . ASP   A 1 101 ? 12.122  -17.149 13.885  1.00 16.70  ? 101 ASP   A C   1 
ATOM   871  O  O   . ASP   A 1 101 ? 11.396  -16.411 14.561  1.00 19.78  ? 101 ASP   A O   1 
ATOM   872  C  CB  . ASP   A 1 101 ? 10.706  -18.154 12.093  1.00 17.14  ? 101 ASP   A CB  1 
ATOM   873  C  CG  . ASP   A 1 101 ? 10.222  -18.189 10.653  1.00 18.03  ? 101 ASP   A CG  1 
ATOM   874  O  OD1 . ASP   A 1 101 ? 10.590  -17.316 9.848   1.00 19.12  ? 101 ASP   A OD1 1 
ATOM   875  O  OD2 . ASP   A 1 101 ? 9.427   -19.080 10.351  1.00 24.89  ? 101 ASP   A OD2 1 
ATOM   876  N  N   . GLY   A 1 102 ? 13.126  -17.855 14.416  1.00 17.96  ? 102 GLY   A N   1 
ATOM   877  C  CA  . GLY   A 1 102 ? 13.401  -17.831 15.845  1.00 19.64  ? 102 GLY   A CA  1 
ATOM   878  C  C   . GLY   A 1 102 ? 14.265  -16.687 16.369  1.00 17.07  ? 102 GLY   A C   1 
ATOM   879  O  O   . GLY   A 1 102 ? 14.602  -16.674 17.558  1.00 17.87  ? 102 GLY   A O   1 
ATOM   880  N  N   A GLN   A 1 103 ? 14.473  -15.666 15.543  0.50 14.19  ? 103 GLN   A N   1 
ATOM   881  N  N   B GLN   A 1 103 ? 14.663  -15.755 15.491  0.50 15.26  ? 103 GLN   A N   1 
ATOM   882  C  CA  A GLN   A 1 103 ? 15.260  -14.543 16.004  0.50 13.89  ? 103 GLN   A CA  1 
ATOM   883  C  CA  B GLN   A 1 103 ? 15.381  -14.574 15.948  0.50 12.84  ? 103 GLN   A CA  1 
ATOM   884  C  C   A GLN   A 1 103 ? 14.966  -13.390 15.077  0.50 12.05  ? 103 GLN   A C   1 
ATOM   885  C  C   B GLN   A 1 103 ? 14.939  -13.398 15.100  0.50 11.85  ? 103 GLN   A C   1 
ATOM   886  O  O   A GLN   A 1 103 ? 14.535  -13.593 13.946  0.50 13.03  ? 103 GLN   A O   1 
ATOM   887  O  O   B GLN   A 1 103 ? 14.307  -13.581 14.063  0.50 13.07  ? 103 GLN   A O   1 
ATOM   888  C  CB  A GLN   A 1 103 ? 16.747  -14.851 15.898  0.50 14.15  ? 103 GLN   A CB  1 
ATOM   889  C  CB  B GLN   A 1 103 ? 16.904  -14.759 15.993  0.50 14.38  ? 103 GLN   A CB  1 
ATOM   890  C  CG  A GLN   A 1 103 ? 17.163  -15.078 14.447  0.50 13.31  ? 103 GLN   A CG  1 
ATOM   891  C  CG  B GLN   A 1 103 ? 17.531  -15.026 14.621  0.50 14.01  ? 103 GLN   A CG  1 
ATOM   892  C  CD  A GLN   A 1 103 ? 18.485  -15.794 14.384  0.50 13.58  ? 103 GLN   A CD  1 
ATOM   893  C  CD  B GLN   A 1 103 ? 18.941  -15.538 14.791  0.50 15.65  ? 103 GLN   A CD  1 
ATOM   894  O  OE1 A GLN   A 1 103 ? 18.630  -16.888 14.915  0.50 15.45  ? 103 GLN   A OE1 1 
ATOM   895  O  OE1 B GLN   A 1 103 ? 19.213  -16.317 15.686  0.50 20.62  ? 103 GLN   A OE1 1 
ATOM   896  N  NE2 A GLN   A 1 103 ? 19.454  -15.217 13.693  0.50 14.73  ? 103 GLN   A NE2 1 
ATOM   897  N  NE2 B GLN   A 1 103 ? 19.872  -15.086 13.970  0.50 15.92  ? 103 GLN   A NE2 1 
ATOM   898  N  N   . GLY   A 1 104 ? 15.277  -12.188 15.557  1.00 12.09  ? 104 GLY   A N   1 
ATOM   899  C  CA  . GLY   A 1 104 ? 15.020  -10.993 14.784  1.00 11.89  ? 104 GLY   A CA  1 
ATOM   900  C  C   . GLY   A 1 104 ? 14.565  -9.806  15.595  1.00 11.47  ? 104 GLY   A C   1 
ATOM   901  O  O   . GLY   A 1 104 ? 14.825  -8.666  15.238  1.00 11.92  ? 104 GLY   A O   1 
ATOM   902  N  N   . SER   A 1 105 ? 13.865  -10.047 16.717  1.00 11.38  ? 105 SER   A N   1 
ATOM   903  C  CA  . SER   A 1 105 ? 13.484  -8.928  17.554  1.00 10.66  ? 105 SER   A CA  1 
ATOM   904  C  C   . SER   A 1 105 ? 14.684  -8.394  18.332  1.00 10.21  ? 105 SER   A C   1 
ATOM   905  O  O   . SER   A 1 105 ? 15.691  -9.075  18.528  1.00 11.34  ? 105 SER   A O   1 
ATOM   906  C  CB  . SER   A 1 105 ? 12.332  -9.305  18.496  1.00 11.13  ? 105 SER   A CB  1 
ATOM   907  O  OG  . SER   A 1 105 ? 12.681  -10.267 19.472  1.00 11.27  ? 105 SER   A OG  1 
ATOM   908  N  N   . GLU   A 1 106 ? 14.529  -7.138  18.739  1.00 10.54  ? 106 GLU   A N   1 
ATOM   909  C  CA  . GLU   A 1 106 ? 15.550  -6.449  19.542  1.00 10.61  ? 106 GLU   A CA  1 
ATOM   910  C  C   . GLU   A 1 106 ? 15.221  -6.637  21.019  1.00 10.03  ? 106 GLU   A C   1 
ATOM   911  O  O   . GLU   A 1 106 ? 15.991  -7.197  21.788  1.00 11.24  ? 106 GLU   A O   1 
ATOM   912  C  CB  . GLU   A 1 106 ? 15.606  -4.980  19.107  1.00 10.88  ? 106 GLU   A CB  1 
ATOM   913  C  CG  . GLU   A 1 106 ? 16.095  -4.865  17.680  1.00 12.00  ? 106 GLU   A CG  1 
ATOM   914  C  CD  . GLU   A 1 106 ? 16.763  -3.559  17.388  1.00 10.93  ? 106 GLU   A CD  1 
ATOM   915  O  OE1 . GLU   A 1 106 ? 16.137  -2.504  17.641  1.00 11.06  ? 106 GLU   A OE1 1 
ATOM   916  O  OE2 . GLU   A 1 106 ? 17.926  -3.581  16.904  1.00 12.49  ? 106 GLU   A OE2 1 
ATOM   917  N  N   . HIS   A 1 107 ? 14.037  -6.177  21.442  1.00 10.32  ? 107 HIS   A N   1 
ATOM   918  C  CA  . HIS   A 1 107 ? 13.568  -6.565  22.767  1.00 10.57  ? 107 HIS   A CA  1 
ATOM   919  C  C   . HIS   A 1 107 ? 13.267  -8.074  22.771  1.00 10.32  ? 107 HIS   A C   1 
ATOM   920  O  O   . HIS   A 1 107 ? 12.933  -8.664  21.742  1.00 10.75  ? 107 HIS   A O   1 
ATOM   921  C  CB  . HIS   A 1 107 ? 12.315  -5.766  23.139  1.00 10.56  ? 107 HIS   A CB  1 
ATOM   922  C  CG  . HIS   A 1 107 ? 12.629  -4.317  23.318  1.00 9.90   ? 107 HIS   A CG  1 
ATOM   923  N  ND1 . HIS   A 1 107 ? 12.577  -3.410  22.260  1.00 10.48  ? 107 HIS   A ND1 1 
ATOM   924  C  CD2 . HIS   A 1 107 ? 13.128  -3.611  24.378  1.00 10.35  ? 107 HIS   A CD2 1 
ATOM   925  C  CE1 . HIS   A 1 107 ? 12.991  -2.229  22.699  1.00 10.28  ? 107 HIS   A CE1 1 
ATOM   926  N  NE2 . HIS   A 1 107 ? 13.350  -2.311  23.992  1.00 10.30  ? 107 HIS   A NE2 1 
ATOM   927  N  N   . THR   A 1 108 ? 13.389  -8.648  23.976  1.00 11.29  ? 108 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 108 ? 12.991  -10.016 24.219  1.00 11.88  ? 108 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 108 ? 12.035  -10.028 25.404  1.00 11.30  ? 108 THR   A C   1 
ATOM   930  O  O   . THR   A 1 108 ? 12.011  -9.060  26.181  1.00 12.11  ? 108 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 108 ? 14.215  -10.930 24.421  1.00 12.71  ? 108 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 108 ? 15.040  -10.448 25.480  1.00 12.54  ? 108 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 108 ? 15.022  -11.013 23.144  1.00 13.62  ? 108 THR   A CG2 1 
ATOM   934  N  N   . VAL   A 1 109 ? 11.257  -11.108 25.529  1.00 12.21  ? 109 VAL   A N   1 
ATOM   935  C  CA  . VAL   A 1 109 ? 10.289  -11.187 26.618  1.00 12.98  ? 109 VAL   A CA  1 
ATOM   936  C  C   . VAL   A 1 109 ? 10.599  -12.480 27.358  1.00 13.48  ? 109 VAL   A C   1 
ATOM   937  O  O   . VAL   A 1 109 ? 10.460  -13.576 26.782  1.00 13.93  ? 109 VAL   A O   1 
ATOM   938  C  CB  . VAL   A 1 109 ? 8.853   -11.182 26.066  1.00 14.08  ? 109 VAL   A CB  1 
ATOM   939  C  CG1 . VAL   A 1 109 ? 7.857   -11.317 27.201  1.00 15.73  ? 109 VAL   A CG1 1 
ATOM   940  C  CG2 . VAL   A 1 109 ? 8.582   -9.904  25.262  1.00 14.53  ? 109 VAL   A CG2 1 
ATOM   941  N  N   . ASP   A 1 110 ? 11.079  -12.389 28.596  1.00 14.37  ? 110 ASP   A N   1 
ATOM   942  C  CA  . ASP   A 1 110 ? 11.536  -13.594 29.300  1.00 15.28  ? 110 ASP   A CA  1 
ATOM   943  C  C   . ASP   A 1 110 ? 12.490  -14.402 28.412  1.00 14.65  ? 110 ASP   A C   1 
ATOM   944  O  O   . ASP   A 1 110 ? 12.430  -15.632 28.367  1.00 16.63  ? 110 ASP   A O   1 
ATOM   945  C  CB  . ASP   A 1 110 ? 10.326  -14.413 29.753  1.00 18.05  ? 110 ASP   A CB  1 
ATOM   946  C  CG  . ASP   A 1 110 ? 9.502   -13.681 30.788  1.00 18.05  ? 110 ASP   A CG  1 
ATOM   947  O  OD1 . ASP   A 1 110 ? 10.078  -12.826 31.522  1.00 19.15  ? 110 ASP   A OD1 1 
ATOM   948  O  OD2 . ASP   A 1 110 ? 8.305   -13.959 30.835  1.00 22.73  ? 110 ASP   A OD2 1 
ATOM   949  N  N   . LYS   A 1 111 ? 13.392  -13.679 27.735  1.00 14.04  ? 111 LYS   A N   1 
ATOM   950  C  CA  . LYS   A 1 111 ? 14.441  -14.211 26.872  1.00 14.38  ? 111 LYS   A CA  1 
ATOM   951  C  C   . LYS   A 1 111 ? 13.901  -14.698 25.522  1.00 14.76  ? 111 LYS   A C   1 
ATOM   952  O  O   . LYS   A 1 111 ? 14.712  -15.013 24.648  1.00 16.86  ? 111 LYS   A O   1 
ATOM   953  C  CB  . LYS   A 1 111 ? 15.357  -15.264 27.533  1.00 16.83  ? 111 LYS   A CB  1 
ATOM   954  C  CG  . LYS   A 1 111 ? 16.027  -14.740 28.806  1.00 20.44  ? 111 LYS   A CG  1 
ATOM   955  C  CD  . LYS   A 1 111 ? 17.028  -13.629 28.546  1.00 25.76  ? 111 LYS   A CD  1 
ATOM   956  C  CE  . LYS   A 1 111 ? 17.614  -13.042 29.813  1.00 32.26  ? 111 LYS   A CE  1 
ATOM   957  N  NZ  . LYS   A 1 111 ? 18.888  -13.715 30.117  1.00 38.80  ? 111 LYS   A NZ  1 
ATOM   958  N  N   . LYS   A 1 112 ? 12.577  -14.692 25.307  1.00 13.37  ? 112 LYS   A N   1 
ATOM   959  C  CA  . LYS   A 1 112 ? 12.020  -15.081 24.025  1.00 14.50  ? 112 LYS   A CA  1 
ATOM   960  C  C   . LYS   A 1 112 ? 12.329  -14.031 22.955  1.00 13.00  ? 112 LYS   A C   1 
ATOM   961  O  O   . LYS   A 1 112 ? 12.034  -12.853 23.161  1.00 13.39  ? 112 LYS   A O   1 
ATOM   962  C  CB  . LYS   A 1 112 ? 10.494  -15.223 24.136  1.00 16.69  ? 112 LYS   A CB  1 
ATOM   963  C  CG  . LYS   A 1 112 ? 9.817   -15.591 22.819  1.00 18.76  ? 112 LYS   A CG  1 
ATOM   964  C  CD  . LYS   A 1 112 ? 8.293   -15.501 22.884  1.00 21.77  ? 112 LYS   A CD  1 
ATOM   965  C  CE  . LYS   A 1 112 ? 7.724   -15.736 21.508  1.00 25.56  ? 112 LYS   A CE  1 
ATOM   966  N  NZ  . LYS   A 1 112 ? 7.944   -17.120 21.074  1.00 24.68  ? 112 LYS   A NZ  1 
ATOM   967  N  N   . LYS   A 1 113 ? 12.857  -14.496 21.817  1.00 13.91  ? 113 LYS   A N   1 
ATOM   968  C  CA  A LYS   A 1 113 ? 13.046  -13.691 20.622  0.50 13.98  ? 113 LYS   A CA  1 
ATOM   969  C  CA  B LYS   A 1 113 ? 13.033  -13.678 20.631  0.50 14.08  ? 113 LYS   A CA  1 
ATOM   970  C  C   . LYS   A 1 113 ? 11.894  -13.940 19.654  1.00 14.05  ? 113 LYS   A C   1 
ATOM   971  O  O   . LYS   A 1 113 ? 11.499  -15.078 19.407  1.00 15.79  ? 113 LYS   A O   1 
ATOM   972  C  CB  A LYS   A 1 113 ? 14.341  -14.089 19.914  0.50 14.59  ? 113 LYS   A CB  1 
ATOM   973  C  CB  B LYS   A 1 113 ? 14.369  -14.004 19.966  0.50 15.37  ? 113 LYS   A CB  1 
ATOM   974  C  CG  A LYS   A 1 113 ? 15.624  -13.779 20.676  0.50 14.44  ? 113 LYS   A CG  1 
ATOM   975  C  CG  B LYS   A 1 113 ? 15.583  -13.665 20.818  0.50 15.05  ? 113 LYS   A CG  1 
ATOM   976  C  CD  A LYS   A 1 113 ? 16.858  -14.311 19.959  0.50 15.09  ? 113 LYS   A CD  1 
ATOM   977  C  CD  B LYS   A 1 113 ? 16.839  -14.340 20.319  0.50 16.72  ? 113 LYS   A CD  1 
ATOM   978  C  CE  A LYS   A 1 113 ? 18.126  -13.767 20.585  0.50 17.53  ? 113 LYS   A CE  1 
ATOM   979  C  CE  B LYS   A 1 113 ? 18.055  -13.783 21.022  0.50 17.06  ? 113 LYS   A CE  1 
ATOM   980  N  NZ  A LYS   A 1 113 ? 18.546  -14.522 21.790  0.50 19.10  ? 113 LYS   A NZ  1 
ATOM   981  N  NZ  B LYS   A 1 113 ? 19.280  -14.490 20.588  0.50 19.84  ? 113 LYS   A NZ  1 
ATOM   982  N  N   . TYR   A 1 114 ? 11.359  -12.843 19.138  1.00 12.31  ? 114 TYR   A N   1 
ATOM   983  C  CA  . TYR   A 1 114 ? 10.382  -12.888 18.075  1.00 12.29  ? 114 TYR   A CA  1 
ATOM   984  C  C   . TYR   A 1 114 ? 11.052  -12.841 16.696  1.00 12.04  ? 114 TYR   A C   1 
ATOM   985  O  O   . TYR   A 1 114 ? 12.243  -12.556 16.584  1.00 12.67  ? 114 TYR   A O   1 
ATOM   986  C  CB  . TYR   A 1 114 ? 9.322   -11.779 18.237  1.00 12.49  ? 114 TYR   A CB  1 
ATOM   987  C  CG  . TYR   A 1 114 ? 8.385   -12.018 19.392  1.00 12.62  ? 114 TYR   A CG  1 
ATOM   988  C  CD1 . TYR   A 1 114 ? 8.653   -11.620 20.697  1.00 13.93  ? 114 TYR   A CD1 1 
ATOM   989  C  CD2 . TYR   A 1 114 ? 7.192   -12.686 19.145  1.00 14.23  ? 114 TYR   A CD2 1 
ATOM   990  C  CE1 . TYR   A 1 114 ? 7.756   -11.853 21.732  1.00 16.19  ? 114 TYR   A CE1 1 
ATOM   991  C  CE2 . TYR   A 1 114 ? 6.281   -12.928 20.168  1.00 15.79  ? 114 TYR   A CE2 1 
ATOM   992  C  CZ  . TYR   A 1 114 ? 6.560   -12.489 21.452  1.00 17.67  ? 114 TYR   A CZ  1 
ATOM   993  O  OH  . TYR   A 1 114 ? 5.682   -12.701 22.486  1.00 24.05  ? 114 TYR   A OH  1 
ATOM   994  N  N   . ALA   A 1 115 ? 10.283  -13.121 15.642  1.00 12.28  ? 115 ALA   A N   1 
ATOM   995  C  CA  . ALA   A 1 115 ? 10.823  -13.155 14.288  1.00 12.63  ? 115 ALA   A CA  1 
ATOM   996  C  C   . ALA   A 1 115 ? 11.224  -11.756 13.816  1.00 11.82  ? 115 ALA   A C   1 
ATOM   997  O  O   . ALA   A 1 115 ? 12.063  -11.613 12.919  1.00 13.11  ? 115 ALA   A O   1 
ATOM   998  C  CB  . ALA   A 1 115 ? 9.787   -13.747 13.361  1.00 14.14  ? 115 ALA   A CB  1 
ATOM   999  N  N   . ALA   A 1 116 ? 10.585  -10.713 14.349  1.00 11.47  ? 116 ALA   A N   1 
ATOM   1000 C  CA  . ALA   A 1 116 ? 10.855  -9.354  13.894  1.00 11.25  ? 116 ALA   A CA  1 
ATOM   1001 C  C   . ALA   A 1 116 ? 10.262  -8.421  14.924  1.00 10.76  ? 116 ALA   A C   1 
ATOM   1002 O  O   . ALA   A 1 116 ? 9.523   -8.817  15.827  1.00 11.14  ? 116 ALA   A O   1 
ATOM   1003 C  CB  . ALA   A 1 116 ? 10.307  -9.090  12.499  1.00 12.18  ? 116 ALA   A CB  1 
ATOM   1004 N  N   . GLU   A 1 117 ? 10.597  -7.130  14.772  1.00 10.79  ? 117 GLU   A N   1 
ATOM   1005 C  CA  . GLU   A 1 117 ? 10.054  -6.093  15.648  1.00 10.49  ? 117 GLU   A CA  1 
ATOM   1006 C  C   . GLU   A 1 117 ? 9.853   -4.827  14.824  1.00 10.19  ? 117 GLU   A C   1 
ATOM   1007 O  O   . GLU   A 1 117 ? 10.767  -4.421  14.108  1.00 11.68  ? 117 GLU   A O   1 
ATOM   1008 C  CB  . GLU   A 1 117 ? 11.018  -5.850  16.811  1.00 10.78  ? 117 GLU   A CB  1 
ATOM   1009 C  CG  . GLU   A 1 117 ? 10.476  -4.979  17.925  1.00 11.08  ? 117 GLU   A CG  1 
ATOM   1010 C  CD  . GLU   A 1 117 ? 11.381  -4.896  19.133  1.00 10.50  ? 117 GLU   A CD  1 
ATOM   1011 O  OE1 . GLU   A 1 117 ? 12.091  -5.903  19.406  1.00 11.79  ? 117 GLU   A OE1 1 
ATOM   1012 O  OE2 . GLU   A 1 117 ? 11.420  -3.835  19.819  1.00 11.08  ? 117 GLU   A OE2 1 
ATOM   1013 N  N   . LEU   A 1 118 ? 8.660   -4.262  14.917  1.00 10.61  ? 118 LEU   A N   1 
ATOM   1014 C  CA  . LEU   A 1 118 ? 8.283   -3.023  14.271  1.00 10.51  ? 118 LEU   A CA  1 
ATOM   1015 C  C   . LEU   A 1 118 ? 8.526   -1.890  15.262  1.00 10.05  ? 118 LEU   A C   1 
ATOM   1016 O  O   . LEU   A 1 118 ? 8.104   -1.962  16.417  1.00 10.44  ? 118 LEU   A O   1 
ATOM   1017 C  CB  . LEU   A 1 118 ? 6.782   -3.127  13.933  1.00 11.69  ? 118 LEU   A CB  1 
ATOM   1018 C  CG  . LEU   A 1 118 ? 6.055   -1.822  13.559  1.00 11.71  ? 118 LEU   A CG  1 
ATOM   1019 C  CD1 . LEU   A 1 118 ? 6.649   -1.129  12.348  1.00 12.36  ? 118 LEU   A CD1 1 
ATOM   1020 C  CD2 . LEU   A 1 118 ? 4.599   -2.157  13.313  1.00 12.94  ? 118 LEU   A CD2 1 
ATOM   1021 N  N   . HIS   A 1 119 ? 9.151   -0.815  14.764  1.00 9.96   ? 119 HIS   A N   1 
ATOM   1022 C  CA  . HIS   A 1 119 ? 9.404   0.385   15.567  1.00 10.11  ? 119 HIS   A CA  1 
ATOM   1023 C  C   . HIS   A 1 119 ? 8.757   1.574   14.877  1.00 10.15  ? 119 HIS   A C   1 
ATOM   1024 O  O   . HIS   A 1 119 ? 9.140   1.933   13.752  1.00 11.16  ? 119 HIS   A O   1 
ATOM   1025 C  CB  . HIS   A 1 119 ? 10.921  0.644   15.675  1.00 10.34  ? 119 HIS   A CB  1 
ATOM   1026 C  CG  . HIS   A 1 119 ? 11.557  -0.377  16.569  1.00 9.94   ? 119 HIS   A CG  1 
ATOM   1027 N  ND1 . HIS   A 1 119 ? 12.925  -0.621  16.532  1.00 9.90   ? 119 HIS   A ND1 1 
ATOM   1028 C  CD2 . HIS   A 1 119 ? 11.010  -1.147  17.537  1.00 10.57  ? 119 HIS   A CD2 1 
ATOM   1029 C  CE1 . HIS   A 1 119 ? 13.181  -1.531  17.450  1.00 10.00  ? 119 HIS   A CE1 1 
ATOM   1030 N  NE2 . HIS   A 1 119 ? 12.063  -1.878  18.085  1.00 10.60  ? 119 HIS   A NE2 1 
ATOM   1031 N  N   . LEU   A 1 120 ? 7.741   2.160   15.535  1.00 10.46  ? 120 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 120 ? 7.109   3.414   15.107  1.00 11.01  ? 120 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 120 ? 7.723   4.546   15.899  1.00 10.07  ? 120 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 120 ? 7.599   4.578   17.116  1.00 10.30  ? 120 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 120 ? 5.596   3.312   15.301  1.00 11.86  ? 120 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 120 ? 4.928   2.243   14.419  1.00 13.05  ? 120 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 120 ? 4.067   1.326   15.278  1.00 15.79  ? 120 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 120 ? 4.078   2.929   13.359  1.00 15.25  ? 120 LEU   A CD2 1 
ATOM   1039 N  N   . VAL   A 1 121 ? 8.446   5.418   15.195  1.00 10.73  ? 121 VAL   A N   1 
ATOM   1040 C  CA  . VAL   A 1 121 ? 9.257   6.453   15.834  1.00 11.11  ? 121 VAL   A CA  1 
ATOM   1041 C  C   . VAL   A 1 121 ? 8.507   7.775   15.860  1.00 10.79  ? 121 VAL   A C   1 
ATOM   1042 O  O   . VAL   A 1 121 ? 8.054   8.235   14.805  1.00 11.76  ? 121 VAL   A O   1 
ATOM   1043 C  CB  . VAL   A 1 121 ? 10.593  6.606   15.068  1.00 11.53  ? 121 VAL   A CB  1 
ATOM   1044 C  CG1 . VAL   A 1 121 ? 11.457  7.720   15.663  1.00 12.99  ? 121 VAL   A CG1 1 
ATOM   1045 C  CG2 . VAL   A 1 121 ? 11.387  5.295   14.968  1.00 12.31  ? 121 VAL   A CG2 1 
ATOM   1046 N  N   . HIS   A 1 122 ? 8.470   8.379   17.048  1.00 11.06  ? 122 HIS   A N   1 
ATOM   1047 C  CA  . HIS   A 1 122 ? 7.755   9.630   17.241  1.00 11.20  ? 122 HIS   A CA  1 
ATOM   1048 C  C   . HIS   A 1 122 ? 8.648   10.608  18.001  1.00 11.32  ? 122 HIS   A C   1 
ATOM   1049 O  O   . HIS   A 1 122 ? 9.396   10.208  18.886  1.00 12.13  ? 122 HIS   A O   1 
ATOM   1050 C  CB  . HIS   A 1 122 ? 6.467   9.446   18.063  1.00 11.58  ? 122 HIS   A CB  1 
ATOM   1051 C  CG  . HIS   A 1 122 ? 5.589   8.303   17.666  1.00 11.40  ? 122 HIS   A CG  1 
ATOM   1052 N  ND1 . HIS   A 1 122 ? 5.935   6.988   17.912  1.00 11.29  ? 122 HIS   A ND1 1 
ATOM   1053 C  CD2 . HIS   A 1 122 ? 4.379   8.245   17.060  1.00 12.19  ? 122 HIS   A CD2 1 
ATOM   1054 C  CE1 . HIS   A 1 122 ? 4.946   6.208   17.460  1.00 12.37  ? 122 HIS   A CE1 1 
ATOM   1055 N  NE2 . HIS   A 1 122 ? 3.975   6.948   16.918  1.00 12.35  ? 122 HIS   A NE2 1 
ATOM   1056 N  N   . TRP   A 1 123 ? 8.518   11.902  17.692  1.00 11.38  ? 123 TRP   A N   1 
ATOM   1057 C  CA  . TRP   A 1 123 ? 9.316   12.911  18.389  1.00 11.89  ? 123 TRP   A CA  1 
ATOM   1058 C  C   . TRP   A 1 123 ? 8.444   13.903  19.147  1.00 11.32  ? 123 TRP   A C   1 
ATOM   1059 O  O   . TRP   A 1 123 ? 7.341   14.253  18.715  1.00 12.61  ? 123 TRP   A O   1 
ATOM   1060 C  CB  . TRP   A 1 123 ? 10.303  13.650  17.468  1.00 13.84  ? 123 TRP   A CB  1 
ATOM   1061 C  CG  . TRP   A 1 123 ? 9.679   14.286  16.266  1.00 12.96  ? 123 TRP   A CG  1 
ATOM   1062 C  CD1 . TRP   A 1 123 ? 9.436   13.715  15.045  1.00 14.63  ? 123 TRP   A CD1 1 
ATOM   1063 C  CD2 . TRP   A 1 123 ? 9.271   15.654  16.157  1.00 14.03  ? 123 TRP   A CD2 1 
ATOM   1064 N  NE1 . TRP   A 1 123 ? 8.861   14.622  14.205  1.00 14.99  ? 123 TRP   A NE1 1 
ATOM   1065 C  CE2 . TRP   A 1 123 ? 8.774   15.835  14.840  1.00 15.47  ? 123 TRP   A CE2 1 
ATOM   1066 C  CE3 . TRP   A 1 123 ? 9.282   16.755  17.024  1.00 16.00  ? 123 TRP   A CE3 1 
ATOM   1067 C  CZ2 . TRP   A 1 123 ? 8.266   17.043  14.374  1.00 17.22  ? 123 TRP   A CZ2 1 
ATOM   1068 C  CZ3 . TRP   A 1 123 ? 8.812   17.952  16.541  1.00 17.46  ? 123 TRP   A CZ3 1 
ATOM   1069 C  CH2 . TRP   A 1 123 ? 8.322   18.096  15.245  1.00 18.22  ? 123 TRP   A CH2 1 
ATOM   1070 N  N   . ASN   A 1 124 ? 8.980   14.363  20.281  1.00 12.31  ? 124 ASN   A N   1 
ATOM   1071 C  CA  . ASN   A 1 124 ? 8.242   15.249  21.179  1.00 13.16  ? 124 ASN   A CA  1 
ATOM   1072 C  C   . ASN   A 1 124 ? 8.121   16.638  20.570  1.00 13.29  ? 124 ASN   A C   1 
ATOM   1073 O  O   . ASN   A 1 124 ? 9.132   17.316  20.360  1.00 12.86  ? 124 ASN   A O   1 
ATOM   1074 C  CB  . ASN   A 1 124 ? 9.020   15.305  22.487  1.00 13.61  ? 124 ASN   A CB  1 
ATOM   1075 C  CG  . ASN   A 1 124 ? 8.223   15.921  23.604  1.00 14.16  ? 124 ASN   A CG  1 
ATOM   1076 O  OD1 . ASN   A 1 124 ? 7.414   16.819  23.366  1.00 15.31  ? 124 ASN   A OD1 1 
ATOM   1077 N  ND2 . ASN   A 1 124 ? 8.472   15.447  24.816  1.00 15.26  ? 124 ASN   A ND2 1 
ATOM   1078 N  N   . THR   A 1 125 ? 6.880   17.062  20.301  1.00 14.65  ? 125 THR   A N   1 
ATOM   1079 C  CA  . THR   A 1 125 ? 6.690   18.305  19.570  1.00 15.00  ? 125 THR   A CA  1 
ATOM   1080 C  C   . THR   A 1 125 ? 7.177   19.524  20.355  1.00 15.50  ? 125 THR   A C   1 
ATOM   1081 O  O   . THR   A 1 125 ? 7.371   20.580  19.732  1.00 16.66  ? 125 THR   A O   1 
ATOM   1082 C  CB  . THR   A 1 125 ? 5.231   18.450  19.141  1.00 18.06  ? 125 THR   A CB  1 
ATOM   1083 O  OG1 . THR   A 1 125 ? 4.408   18.492  20.311  1.00 22.54  ? 125 THR   A OG1 1 
ATOM   1084 C  CG2 . THR   A 1 125 ? 4.852   17.330  18.191  1.00 21.23  ? 125 THR   A CG2 1 
ATOM   1085 N  N   . LYS   A 1 126 ? 7.429   19.434  21.678  1.00 14.81  ? 127 LYS   A N   1 
ATOM   1086 C  CA  . LYS   A 1 126 ? 7.958   20.596  22.400  1.00 16.05  ? 127 LYS   A CA  1 
ATOM   1087 C  C   . LYS   A 1 126 ? 9.360   20.984  21.920  1.00 15.83  ? 127 LYS   A C   1 
ATOM   1088 O  O   . LYS   A 1 126 ? 9.792   22.091  22.214  1.00 18.77  ? 127 LYS   A O   1 
ATOM   1089 C  CB  . LYS   A 1 126 ? 7.827   20.348  23.891  1.00 18.61  ? 127 LYS   A CB  1 
ATOM   1090 C  CG  . LYS   A 1 126 ? 8.914   19.503  24.501  1.00 17.76  ? 127 LYS   A CG  1 
ATOM   1091 C  CD  . LYS   A 1 126 ? 8.536   19.213  25.918  1.00 21.89  ? 127 LYS   A CD  1 
ATOM   1092 C  CE  . LYS   A 1 126 ? 9.581   18.393  26.607  1.00 24.80  ? 127 LYS   A CE  1 
ATOM   1093 N  NZ  . LYS   A 1 126 ? 9.116   18.010  27.957  1.00 30.49  ? 127 LYS   A NZ  1 
ATOM   1094 N  N   . TYR   A 1 127 ? 10.060  20.075  21.222  1.00 14.40  ? 128 TYR   A N   1 
ATOM   1095 C  CA  . TYR   A 1 127 ? 11.422  20.345  20.765  1.00 14.80  ? 128 TYR   A CA  1 
ATOM   1096 C  C   . TYR   A 1 127 ? 11.460  20.781  19.304  1.00 14.65  ? 128 TYR   A C   1 
ATOM   1097 O  O   . TYR   A 1 127 ? 12.547  21.045  18.775  1.00 15.87  ? 128 TYR   A O   1 
ATOM   1098 C  CB  . TYR   A 1 127 ? 12.342  19.154  21.024  1.00 14.90  ? 128 TYR   A CB  1 
ATOM   1099 C  CG  . TYR   A 1 127 ? 12.429  18.825  22.476  1.00 14.42  ? 128 TYR   A CG  1 
ATOM   1100 C  CD1 . TYR   A 1 127 ? 12.843  19.810  23.387  1.00 15.95  ? 128 TYR   A CD1 1 
ATOM   1101 C  CD2 . TYR   A 1 127 ? 12.116  17.557  22.938  1.00 13.82  ? 128 TYR   A CD2 1 
ATOM   1102 C  CE1 . TYR   A 1 127 ? 12.929  19.487  24.735  1.00 15.84  ? 128 TYR   A CE1 1 
ATOM   1103 C  CE2 . TYR   A 1 127 ? 12.185  17.249  24.284  1.00 13.84  ? 128 TYR   A CE2 1 
ATOM   1104 C  CZ  . TYR   A 1 127 ? 12.612  18.219  25.179  1.00 15.40  ? 128 TYR   A CZ  1 
ATOM   1105 O  OH  . TYR   A 1 127 ? 12.696  18.007  26.517  1.00 17.21  ? 128 TYR   A OH  1 
ATOM   1106 N  N   . GLY   A 1 128 ? 10.293  20.915  18.672  1.00 14.66  ? 129 GLY   A N   1 
ATOM   1107 C  CA  . GLY   A 1 128 ? 10.258  21.615  17.400  1.00 15.40  ? 129 GLY   A CA  1 
ATOM   1108 C  C   . GLY   A 1 128 ? 10.630  20.788  16.162  1.00 15.48  ? 129 GLY   A C   1 
ATOM   1109 O  O   . GLY   A 1 128 ? 10.009  20.945  15.115  1.00 16.85  ? 129 GLY   A O   1 
ATOM   1110 N  N   . ASP   A 1 129 ? 11.716  20.010  16.197  1.00 16.03  ? 130 ASP   A N   1 
ATOM   1111 C  CA  . ASP   A 1 129 ? 12.099  19.136  15.087  1.00 17.58  ? 130 ASP   A CA  1 
ATOM   1112 C  C   . ASP   A 1 129 ? 12.754  17.889  15.651  1.00 16.45  ? 130 ASP   A C   1 
ATOM   1113 O  O   . ASP   A 1 129 ? 13.171  17.849  16.809  1.00 16.18  ? 130 ASP   A O   1 
ATOM   1114 C  CB  . ASP   A 1 129 ? 13.000  19.864  14.056  1.00 19.42  ? 130 ASP   A CB  1 
ATOM   1115 C  CG  . ASP   A 1 129 ? 14.408  20.255  14.509  1.00 26.58  ? 130 ASP   A CG  1 
ATOM   1116 O  OD1 . ASP   A 1 129 ? 15.260  19.407  14.754  1.00 23.66  ? 130 ASP   A OD1 1 
ATOM   1117 O  OD2 . ASP   A 1 129 ? 14.721  21.473  14.542  1.00 27.39  ? 130 ASP   A OD2 1 
ATOM   1118 N  N   . PHE   A 1 130 ? 12.849  16.882  14.804  1.00 15.84  ? 131 PHE   A N   1 
ATOM   1119 C  CA  . PHE   A 1 130 ? 13.395  15.596  15.204  1.00 15.07  ? 131 PHE   A CA  1 
ATOM   1120 C  C   . PHE   A 1 130 ? 14.859  15.746  15.628  1.00 14.69  ? 131 PHE   A C   1 
ATOM   1121 O  O   . PHE   A 1 130 ? 15.292  15.125  16.593  1.00 14.46  ? 131 PHE   A O   1 
ATOM   1122 C  CB  . PHE   A 1 130 ? 13.242  14.625  14.023  1.00 15.22  ? 131 PHE   A CB  1 
ATOM   1123 C  CG  . PHE   A 1 130 ? 13.870  13.286  14.255  1.00 13.95  ? 131 PHE   A CG  1 
ATOM   1124 C  CD1 . PHE   A 1 130 ? 13.165  12.300  14.899  1.00 15.29  ? 131 PHE   A CD1 1 
ATOM   1125 C  CD2 . PHE   A 1 130 ? 15.184  13.043  13.895  1.00 16.94  ? 131 PHE   A CD2 1 
ATOM   1126 C  CE1 . PHE   A 1 130 ? 13.712  11.053  15.087  1.00 16.86  ? 131 PHE   A CE1 1 
ATOM   1127 C  CE2 . PHE   A 1 130 ? 15.751  11.802  14.111  1.00 18.72  ? 131 PHE   A CE2 1 
ATOM   1128 C  CZ  . PHE   A 1 130 ? 15.008  10.809  14.705  1.00 18.13  ? 131 PHE   A CZ  1 
ATOM   1129 N  N   . GLY   A 1 131 ? 15.635  16.545  14.857  1.00 16.32  ? 132 GLY   A N   1 
ATOM   1130 C  CA  . GLY   A 1 131 ? 17.052  16.670  15.171  1.00 17.47  ? 132 GLY   A CA  1 
ATOM   1131 C  C   . GLY   A 1 131 ? 17.297  17.278  16.557  1.00 16.62  ? 132 GLY   A C   1 
ATOM   1132 O  O   . GLY   A 1 131 ? 18.281  16.939  17.232  1.00 18.40  ? 132 GLY   A O   1 
ATOM   1133 N  N   . LYS   A 1 132 ? 16.435  18.215  16.987  1.00 15.77  ? 133 LYS   A N   1 
ATOM   1134 C  CA  . LYS   A 1 132 ? 16.560  18.745  18.349  1.00 15.22  ? 133 LYS   A CA  1 
ATOM   1135 C  C   . LYS   A 1 132 ? 16.076  17.713  19.359  1.00 14.61  ? 133 LYS   A C   1 
ATOM   1136 O  O   . LYS   A 1 132 ? 16.645  17.576  20.438  1.00 15.00  ? 133 LYS   A O   1 
ATOM   1137 C  CB  . LYS   A 1 132 ? 15.717  20.016  18.509  1.00 17.32  ? 133 LYS   A CB  1 
ATOM   1138 C  CG  . LYS   A 1 132 ? 16.158  21.231  17.731  1.00 27.04  ? 133 LYS   A CG  1 
ATOM   1139 C  CD  . LYS   A 1 132 ? 17.590  21.542  17.866  1.00 33.07  ? 133 LYS   A CD  1 
ATOM   1140 C  CE  . LYS   A 1 132 ? 17.866  22.625  16.851  1.00 38.12  ? 133 LYS   A CE  1 
ATOM   1141 N  NZ  . LYS   A 1 132 ? 17.183  22.312  15.568  1.00 42.42  ? 133 LYS   A NZ  1 
ATOM   1142 N  N   . ALA   A 1 133 ? 14.978  17.018  19.027  1.00 13.77  ? 134 ALA   A N   1 
ATOM   1143 C  CA  . ALA   A 1 133 ? 14.422  16.029  19.953  1.00 13.19  ? 134 ALA   A CA  1 
ATOM   1144 C  C   . ALA   A 1 133 ? 15.418  14.946  20.343  1.00 13.22  ? 134 ALA   A C   1 
ATOM   1145 O  O   . ALA   A 1 133 ? 15.451  14.560  21.496  1.00 13.46  ? 134 ALA   A O   1 
ATOM   1146 C  CB  . ALA   A 1 133 ? 13.169  15.409  19.343  1.00 13.79  ? 134 ALA   A CB  1 
ATOM   1147 N  N   . VAL   A 1 134 ? 16.244  14.485  19.410  1.00 13.54  ? 135 VAL   A N   1 
ATOM   1148 C  CA  . VAL   A 1 134 ? 17.132  13.359  19.738  1.00 14.27  ? 135 VAL   A CA  1 
ATOM   1149 C  C   . VAL   A 1 134 ? 18.263  13.778  20.680  1.00 13.79  ? 135 VAL   A C   1 
ATOM   1150 O  O   . VAL   A 1 134 ? 18.949  12.895  21.210  1.00 15.16  ? 135 VAL   A O   1 
ATOM   1151 C  CB  . VAL   A 1 134 ? 17.737  12.676  18.503  1.00 15.43  ? 135 VAL   A CB  1 
ATOM   1152 C  CG1 . VAL   A 1 134 ? 16.661  12.081  17.640  1.00 17.34  ? 135 VAL   A CG1 1 
ATOM   1153 C  CG2 . VAL   A 1 134 ? 18.632  13.599  17.687  1.00 15.97  ? 135 VAL   A CG2 1 
ATOM   1154 N  N   . GLN   A 1 135 ? 18.396  15.093  20.920  1.00 14.65  ? 136 GLN   A N   1 
ATOM   1155 C  CA  . GLN   A 1 135 ? 19.382  15.576  21.889  1.00 16.54  ? 136 GLN   A CA  1 
ATOM   1156 C  C   . GLN   A 1 135 ? 18.815  15.703  23.302  1.00 14.72  ? 136 GLN   A C   1 
ATOM   1157 O  O   . GLN   A 1 135 ? 19.480  16.232  24.191  1.00 16.88  ? 136 GLN   A O   1 
ATOM   1158 C  CB  . GLN   A 1 135 ? 19.933  16.927  21.415  1.00 17.89  ? 136 GLN   A CB  1 
ATOM   1159 C  CG  . GLN   A 1 135 ? 20.554  16.897  20.030  1.00 21.07  ? 136 GLN   A CG  1 
ATOM   1160 C  CD  . GLN   A 1 135 ? 20.998  18.272  19.582  1.00 25.57  ? 136 GLN   A CD  1 
ATOM   1161 O  OE1 . GLN   A 1 135 ? 21.902  18.878  20.179  1.00 32.72  ? 136 GLN   A OE1 1 
ATOM   1162 N  NE2 . GLN   A 1 135 ? 20.395  18.786  18.508  1.00 28.54  ? 136 GLN   A NE2 1 
ATOM   1163 N  N   . GLN   A 1 136 ? 17.578  15.223  23.502  1.00 13.99  ? 137 GLN   A N   1 
ATOM   1164 C  CA  . GLN   A 1 136 ? 16.899  15.404  24.777  1.00 13.36  ? 137 GLN   A CA  1 
ATOM   1165 C  C   . GLN   A 1 136 ? 16.526  14.071  25.383  1.00 12.94  ? 137 GLN   A C   1 
ATOM   1166 O  O   . GLN   A 1 136 ? 16.184  13.129  24.668  1.00 13.20  ? 137 GLN   A O   1 
ATOM   1167 C  CB  . GLN   A 1 136 ? 15.581  16.178  24.646  1.00 14.18  ? 137 GLN   A CB  1 
ATOM   1168 C  CG  . GLN   A 1 136 ? 15.667  17.344  23.710  1.00 17.20  ? 137 GLN   A CG  1 
ATOM   1169 C  CD  . GLN   A 1 136 ? 16.753  18.285  24.107  1.00 15.70  ? 137 GLN   A CD  1 
ATOM   1170 O  OE1 . GLN   A 1 136 ? 16.998  18.524  25.315  1.00 17.37  ? 137 GLN   A OE1 1 
ATOM   1171 N  NE2 . GLN   A 1 136 ? 17.336  18.909  23.070  1.00 19.56  ? 137 GLN   A NE2 1 
ATOM   1172 N  N   . PRO   A 1 137 ? 16.532  13.941  26.728  1.00 13.20  ? 138 PRO   A N   1 
ATOM   1173 C  CA  . PRO   A 1 137 ? 16.271  12.640  27.344  1.00 13.89  ? 138 PRO   A CA  1 
ATOM   1174 C  C   . PRO   A 1 137 ? 14.850  12.132  27.150  1.00 13.64  ? 138 PRO   A C   1 
ATOM   1175 O  O   . PRO   A 1 137 ? 14.608  10.927  27.255  1.00 17.25  ? 138 PRO   A O   1 
ATOM   1176 C  CB  . PRO   A 1 137 ? 16.603  12.823  28.820  1.00 17.34  ? 138 PRO   A CB  1 
ATOM   1177 C  CG  . PRO   A 1 137 ? 16.610  14.307  28.992  1.00 22.92  ? 138 PRO   A CG  1 
ATOM   1178 C  CD  . PRO   A 1 137 ? 17.043  14.934  27.683  1.00 16.62  ? 138 PRO   A CD  1 
ATOM   1179 N  N   . ASP   A 1 138 ? 13.923  13.074  26.873  1.00 13.60  ? 139 ASP   A N   1 
ATOM   1180 C  CA  . ASP   A 1 138 ? 12.530  12.750  26.585  1.00 13.34  ? 139 ASP   A CA  1 
ATOM   1181 C  C   . ASP   A 1 138 ? 12.167  13.187  25.166  1.00 12.28  ? 139 ASP   A C   1 
ATOM   1182 O  O   . ASP   A 1 138 ? 11.040  13.603  24.922  1.00 13.74  ? 139 ASP   A O   1 
ATOM   1183 C  CB  . ASP   A 1 138 ? 11.578  13.366  27.608  1.00 14.99  ? 139 ASP   A CB  1 
ATOM   1184 C  CG  . ASP   A 1 138 ? 11.675  14.865  27.677  1.00 16.23  ? 139 ASP   A CG  1 
ATOM   1185 O  OD1 . ASP   A 1 138 ? 12.618  15.454  27.077  1.00 15.98  ? 139 ASP   A OD1 1 
ATOM   1186 O  OD2 . ASP   A 1 138 ? 10.802  15.461  28.321  1.00 18.17  ? 139 ASP   A OD2 1 
ATOM   1187 N  N   . GLY   A 1 139 ? 13.109  13.063  24.232  1.00 11.59  ? 140 GLY   A N   1 
ATOM   1188 C  CA  . GLY   A 1 139 ? 12.868  13.559  22.891  1.00 12.66  ? 140 GLY   A CA  1 
ATOM   1189 C  C   . GLY   A 1 139 ? 12.013  12.654  22.013  1.00 11.18  ? 140 GLY   A C   1 
ATOM   1190 O  O   . GLY   A 1 139 ? 11.317  13.145  21.142  1.00 11.91  ? 140 GLY   A O   1 
ATOM   1191 N  N   . LEU   A 1 140 ? 12.157  11.334  22.167  1.00 10.95  ? 141 LEU   A N   1 
ATOM   1192 C  CA  . LEU   A 1 140 ? 11.490  10.375  21.284  1.00 10.81  ? 141 LEU   A CA  1 
ATOM   1193 C  C   . LEU   A 1 140 ? 10.633  9.428   22.106  1.00 10.40  ? 141 LEU   A C   1 
ATOM   1194 O  O   . LEU   A 1 140 ? 10.917  9.134   23.266  1.00 10.90  ? 141 LEU   A O   1 
ATOM   1195 C  CB  . LEU   A 1 140 ? 12.490  9.526   20.506  1.00 11.51  ? 141 LEU   A CB  1 
ATOM   1196 C  CG  . LEU   A 1 140 ? 13.333  10.186  19.432  1.00 13.88  ? 141 LEU   A CG  1 
ATOM   1197 C  CD1 . LEU   A 1 140 ? 14.084  9.135   18.626  1.00 12.99  ? 141 LEU   A CD1 1 
ATOM   1198 C  CD2 . LEU   A 1 140 ? 12.713  11.268  18.601  1.00 17.91  ? 141 LEU   A CD2 1 
ATOM   1199 N  N   . ALA   A 1 141 ? 9.587   8.917   21.449  1.00 10.65  ? 142 ALA   A N   1 
ATOM   1200 C  CA  . ALA   A 1 141 ? 8.854   7.772   21.973  1.00 10.93  ? 142 ALA   A CA  1 
ATOM   1201 C  C   . ALA   A 1 141 ? 8.767   6.791   20.832  1.00 10.11  ? 142 ALA   A C   1 
ATOM   1202 O  O   . ALA   A 1 141 ? 8.343   7.135   19.723  1.00 11.42  ? 142 ALA   A O   1 
ATOM   1203 C  CB  . ALA   A 1 141 ? 7.443   8.194   22.379  1.00 12.63  ? 142 ALA   A CB  1 
ATOM   1204 N  N   . VAL   A 1 142 ? 9.280   5.573   21.087  1.00 10.51  ? 143 VAL   A N   1 
ATOM   1205 C  CA  . VAL   A 1 142 ? 9.239   4.531   20.072  1.00 10.32  ? 143 VAL   A CA  1 
ATOM   1206 C  C   . VAL   A 1 142 ? 8.265   3.463   20.555  1.00 10.27  ? 143 VAL   A C   1 
ATOM   1207 O  O   . VAL   A 1 142 ? 8.397   2.949   21.663  1.00 10.61  ? 143 VAL   A O   1 
ATOM   1208 C  CB  . VAL   A 1 142 ? 10.620  3.957   19.686  1.00 10.69  ? 143 VAL   A CB  1 
ATOM   1209 C  CG1 . VAL   A 1 142 ? 10.477  2.920   18.559  1.00 11.64  ? 143 VAL   A CG1 1 
ATOM   1210 C  CG2 . VAL   A 1 142 ? 11.570  5.076   19.265  1.00 12.30  ? 143 VAL   A CG2 1 
ATOM   1211 N  N   . LEU   A 1 143 ? 7.270   3.203   19.690  1.00 10.22  ? 144 LEU   A N   1 
ATOM   1212 C  CA  . LEU   A 1 143 ? 6.309   2.145   19.938  1.00 10.60  ? 144 LEU   A CA  1 
ATOM   1213 C  C   . LEU   A 1 143 ? 6.834   0.885   19.232  1.00 10.23  ? 144 LEU   A C   1 
ATOM   1214 O  O   . LEU   A 1 143 ? 6.979   0.854   18.013  1.00 10.90  ? 144 LEU   A O   1 
ATOM   1215 C  CB  . LEU   A 1 143 ? 4.948   2.621   19.371  1.00 11.96  ? 144 LEU   A CB  1 
ATOM   1216 C  CG  . LEU   A 1 143 ? 3.797   1.617   19.521  1.00 13.18  ? 144 LEU   A CG  1 
ATOM   1217 C  CD1 . LEU   A 1 143 ? 3.534   1.284   20.972  1.00 14.51  ? 144 LEU   A CD1 1 
ATOM   1218 C  CD2 . LEU   A 1 143 ? 2.543   2.184   18.847  1.00 14.94  ? 144 LEU   A CD2 1 
ATOM   1219 N  N   . GLY   A 1 144 ? 7.107   -0.145  20.054  1.00 10.12  ? 145 GLY   A N   1 
ATOM   1220 C  CA  . GLY   A 1 144 ? 7.629   -1.398  19.540  1.00 10.12  ? 145 GLY   A CA  1 
ATOM   1221 C  C   . GLY   A 1 144 ? 6.566   -2.492  19.579  1.00 9.97   ? 145 GLY   A C   1 
ATOM   1222 O  O   . GLY   A 1 144 ? 5.838   -2.624  20.559  1.00 11.20  ? 145 GLY   A O   1 
ATOM   1223 N  N   . ILE   A 1 145 ? 6.499   -3.222  18.476  1.00 10.36  ? 146 ILE   A N   1 
ATOM   1224 C  CA  . ILE   A 1 145 ? 5.497   -4.272  18.280  1.00 10.20  ? 146 ILE   A CA  1 
ATOM   1225 C  C   . ILE   A 1 145 ? 6.212   -5.506  17.763  1.00 10.22  ? 146 ILE   A C   1 
ATOM   1226 O  O   . ILE   A 1 145 ? 6.902   -5.456  16.757  1.00 10.90  ? 146 ILE   A O   1 
ATOM   1227 C  CB  . ILE   A 1 145 ? 4.394   -3.788  17.307  1.00 11.53  ? 146 ILE   A CB  1 
ATOM   1228 C  CG1 . ILE   A 1 145 ? 3.807   -2.458  17.818  1.00 13.61  ? 146 ILE   A CG1 1 
ATOM   1229 C  CG2 . ILE   A 1 145 ? 3.348   -4.899  17.134  1.00 13.41  ? 146 ILE   A CG2 1 
ATOM   1230 C  CD1 . ILE   A 1 145 ? 2.688   -1.883  16.944  1.00 13.20  ? 146 ILE   A CD1 1 
ATOM   1231 N  N   . PHE   A 1 146 ? 6.025   -6.616  18.469  1.00 10.58  ? 147 PHE   A N   1 
ATOM   1232 C  CA  . PHE   A 1 146 ? 6.640   -7.880  18.055  1.00 10.64  ? 147 PHE   A CA  1 
ATOM   1233 C  C   . PHE   A 1 146 ? 5.875   -8.476  16.890  1.00 11.37  ? 147 PHE   A C   1 
ATOM   1234 O  O   . PHE   A 1 146 ? 4.654   -8.375  16.829  1.00 11.87  ? 147 PHE   A O   1 
ATOM   1235 C  CB  . PHE   A 1 146 ? 6.639   -8.842  19.237  1.00 11.39  ? 147 PHE   A CB  1 
ATOM   1236 C  CG  . PHE   A 1 146 ? 7.501   -8.372  20.369  1.00 10.69  ? 147 PHE   A CG  1 
ATOM   1237 C  CD1 . PHE   A 1 146 ? 8.874   -8.208  20.198  1.00 11.24  ? 147 PHE   A CD1 1 
ATOM   1238 C  CD2 . PHE   A 1 146 ? 6.963   -8.125  21.609  1.00 11.61  ? 147 PHE   A CD2 1 
ATOM   1239 C  CE1 . PHE   A 1 146 ? 9.692   -7.820  21.258  1.00 11.48  ? 147 PHE   A CE1 1 
ATOM   1240 C  CE2 . PHE   A 1 146 ? 7.769   -7.741  22.677  1.00 11.71  ? 147 PHE   A CE2 1 
ATOM   1241 C  CZ  . PHE   A 1 146 ? 9.136   -7.595  22.500  1.00 11.70  ? 147 PHE   A CZ  1 
ATOM   1242 N  N   . LEU   A 1 147 ? 6.607   -9.202  16.036  1.00 11.28  ? 148 LEU   A N   1 
ATOM   1243 C  CA  . LEU   A 1 147 ? 6.020   -9.989  14.954  1.00 11.08  ? 148 LEU   A CA  1 
ATOM   1244 C  C   . LEU   A 1 147 ? 6.376   -11.459 15.187  1.00 11.80  ? 148 LEU   A C   1 
ATOM   1245 O  O   . LEU   A 1 147 ? 7.540   -11.823 15.378  1.00 12.58  ? 148 LEU   A O   1 
ATOM   1246 C  CB  . LEU   A 1 147 ? 6.608   -9.620  13.589  1.00 12.01  ? 148 LEU   A CB  1 
ATOM   1247 C  CG  . LEU   A 1 147 ? 6.057   -8.356  12.930  1.00 11.92  ? 148 LEU   A CG  1 
ATOM   1248 C  CD1 . LEU   A 1 147 ? 6.287   -7.096  13.764  1.00 13.88  ? 148 LEU   A CD1 1 
ATOM   1249 C  CD2 . LEU   A 1 147 ? 6.666   -8.174  11.549  1.00 14.20  ? 148 LEU   A CD2 1 
ATOM   1250 N  N   . LYS   A 1 148 ? 5.334   -12.300 15.169  1.00 12.33  ? 149 LYS   A N   1 
ATOM   1251 C  CA  . LYS   A 1 148 ? 5.501   -13.750 15.141  1.00 12.85  ? 149 LYS   A CA  1 
ATOM   1252 C  C   . LYS   A 1 148 ? 5.007   -14.261 13.794  1.00 13.04  ? 149 LYS   A C   1 
ATOM   1253 O  O   . LYS   A 1 148 ? 4.194   -13.627 13.131  1.00 15.00  ? 149 LYS   A O   1 
ATOM   1254 C  CB  . LYS   A 1 148 ? 4.763   -14.413 16.286  1.00 15.79  ? 149 LYS   A CB  1 
ATOM   1255 C  CG  . LYS   A 1 148 ? 3.251   -14.307 16.213  1.00 18.19  ? 149 LYS   A CG  1 
ATOM   1256 C  CD  . LYS   A 1 148 ? 2.619   -14.985 17.431  1.00 22.87  ? 149 LYS   A CD  1 
ATOM   1257 C  CE  . LYS   A 1 148 ? 1.104   -14.994 17.387  1.00 28.01  ? 149 LYS   A CE  1 
ATOM   1258 N  NZ  . LYS   A 1 148 ? 0.518   -15.594 18.618  1.00 37.89  ? 149 LYS   A NZ  1 
ATOM   1259 N  N   . VAL   A 1 149 ? 5.526   -15.412 13.390  1.00 14.23  ? 150 VAL   A N   1 
ATOM   1260 C  CA  . VAL   A 1 149 ? 5.139   -16.008 12.117  1.00 13.96  ? 150 VAL   A CA  1 
ATOM   1261 C  C   . VAL   A 1 149 ? 3.930   -16.923 12.310  1.00 14.90  ? 150 VAL   A C   1 
ATOM   1262 O  O   . VAL   A 1 149 ? 3.964   -17.859 13.101  1.00 16.59  ? 150 VAL   A O   1 
ATOM   1263 C  CB  . VAL   A 1 149 ? 6.340   -16.744 11.499  1.00 14.56  ? 150 VAL   A CB  1 
ATOM   1264 C  CG1 . VAL   A 1 149 ? 5.931   -17.496 10.236  1.00 17.54  ? 150 VAL   A CG1 1 
ATOM   1265 C  CG2 . VAL   A 1 149 ? 7.443   -15.749 11.172  1.00 18.03  ? 150 VAL   A CG2 1 
ATOM   1266 N  N   . GLY   A 1 150 ? 2.876   -16.673 11.548  1.00 14.65  ? 151 GLY   A N   1 
ATOM   1267 C  CA  . GLY   A 1 150 ? 1.659   -17.443 11.617  1.00 16.39  ? 151 GLY   A CA  1 
ATOM   1268 C  C   . GLY   A 1 150 ? 0.774   -17.040 10.465  1.00 15.34  ? 151 GLY   A C   1 
ATOM   1269 O  O   . GLY   A 1 150 ? 1.158   -17.157 9.294   1.00 15.88  ? 151 GLY   A O   1 
ATOM   1270 N  N   A SER   A 1 151 ? -0.427  -16.547 10.789  0.50 16.50  ? 152 SER   A N   1 
ATOM   1271 N  N   B SER   A 1 151 ? -0.405  -16.515 10.817  0.50 16.83  ? 152 SER   A N   1 
ATOM   1272 C  CA  A SER   A 1 151 ? -1.295  -16.011 9.741   0.50 15.99  ? 152 SER   A CA  1 
ATOM   1273 C  CA  B SER   A 1 151 ? -1.269  -15.919 9.804   0.50 16.42  ? 152 SER   A CA  1 
ATOM   1274 C  C   A SER   A 1 151 ? -0.787  -14.663 9.224   0.50 14.28  ? 152 SER   A C   1 
ATOM   1275 C  C   B SER   A 1 151 ? -0.631  -14.680 9.173   0.50 15.01  ? 152 SER   A C   1 
ATOM   1276 O  O   A SER   A 1 151 ? -0.189  -13.889 9.978   0.50 15.00  ? 152 SER   A O   1 
ATOM   1277 O  O   B SER   A 1 151 ? 0.227   -14.019 9.770   0.50 14.02  ? 152 SER   A O   1 
ATOM   1278 C  CB  A SER   A 1 151 ? -2.681  -15.847 10.266  0.50 21.40  ? 152 SER   A CB  1 
ATOM   1279 C  CB  B SER   A 1 151 ? -2.615  -15.597 10.387  0.50 21.12  ? 152 SER   A CB  1 
ATOM   1280 O  OG  A SER   A 1 151 ? -2.714  -14.740 11.148  0.50 22.37  ? 152 SER   A OG  1 
ATOM   1281 O  OG  B SER   A 1 151 ? -3.249  -16.791 10.823  0.50 23.35  ? 152 SER   A OG  1 
ATOM   1282 N  N   . ALA   A 1 152 ? -1.040  -14.375 7.939   1.00 15.86  ? 153 ALA   A N   1 
ATOM   1283 C  CA  . ALA   A 1 152 ? -0.644  -13.108 7.331   1.00 15.03  ? 153 ALA   A CA  1 
ATOM   1284 C  C   . ALA   A 1 152 ? -1.256  -11.910 8.052   1.00 14.91  ? 153 ALA   A C   1 
ATOM   1285 O  O   . ALA   A 1 152 ? -2.359  -11.972 8.598   1.00 17.56  ? 153 ALA   A O   1 
ATOM   1286 C  CB  . ALA   A 1 152 ? -1.010  -13.079 5.857   1.00 19.00  ? 153 ALA   A CB  1 
ATOM   1287 N  N   . LYS   A 1 153 ? -0.544  -10.778 7.962   1.00 15.71  ? 154 LYS   A N   1 
ATOM   1288 C  CA  . LYS   A 1 153 ? -1.072  -9.498  8.417   1.00 15.69  ? 154 LYS   A CA  1 
ATOM   1289 C  C   . LYS   A 1 153 ? -1.503  -8.713  7.184   1.00 15.68  ? 154 LYS   A C   1 
ATOM   1290 O  O   . LYS   A 1 153 ? -0.665  -8.254  6.419   1.00 15.15  ? 154 LYS   A O   1 
ATOM   1291 C  CB  . LYS   A 1 153 ? -0.011  -8.717  9.211   1.00 17.01  ? 154 LYS   A CB  1 
ATOM   1292 C  CG  . LYS   A 1 153 ? -0.524  -7.487  9.944   1.00 18.49  ? 154 LYS   A CG  1 
ATOM   1293 C  CD  . LYS   A 1 153 ? -1.432  -7.838  11.114  1.00 20.21  ? 154 LYS   A CD  1 
ATOM   1294 C  CE  . LYS   A 1 153 ? -1.600  -6.656  12.040  1.00 20.72  ? 154 LYS   A CE  1 
ATOM   1295 N  NZ  . LYS   A 1 153 ? -2.626  -7.026  13.016  1.00 24.36  ? 154 LYS   A NZ  1 
ATOM   1296 N  N   . PRO   A 1 154 ? -2.819  -8.600  6.892   1.00 16.62  ? 155 PRO   A N   1 
ATOM   1297 C  CA  . PRO   A 1 154 ? -3.215  -8.005  5.616   1.00 18.30  ? 155 PRO   A CA  1 
ATOM   1298 C  C   . PRO   A 1 154 ? -2.683  -6.581  5.470   1.00 17.90  ? 155 PRO   A C   1 
ATOM   1299 O  O   . PRO   A 1 154 ? -2.290  -6.178  4.385   1.00 18.64  ? 155 PRO   A O   1 
ATOM   1300 C  CB  . PRO   A 1 154 ? -4.748  -8.056  5.680   1.00 20.61  ? 155 PRO   A CB  1 
ATOM   1301 C  CG  . PRO   A 1 154 ? -5.012  -9.215  6.593   1.00 24.54  ? 155 PRO   A CG  1 
ATOM   1302 C  CD  . PRO   A 1 154 ? -3.949  -9.163  7.666   1.00 19.07  ? 155 PRO   A CD  1 
ATOM   1303 N  N   . GLY   A 1 155 ? -2.624  -5.844  6.585   1.00 16.69  ? 156 GLY   A N   1 
ATOM   1304 C  CA  . GLY   A 1 155 ? -2.221  -4.447  6.567   1.00 18.33  ? 156 GLY   A CA  1 
ATOM   1305 C  C   . GLY   A 1 155 ? -0.730  -4.255  6.318   1.00 17.80  ? 156 GLY   A C   1 
ATOM   1306 O  O   . GLY   A 1 155 ? -0.281  -3.140  6.131   1.00 19.83  ? 156 GLY   A O   1 
ATOM   1307 N  N   . LEU   A 1 156 ? 0.033   -5.341  6.345   1.00 15.68  ? 157 LEU   A N   1 
ATOM   1308 C  CA  . LEU   A 1 156 ? 1.448   -5.330  6.004   1.00 15.18  ? 157 LEU   A CA  1 
ATOM   1309 C  C   . LEU   A 1 156 ? 1.682   -5.536  4.515   1.00 16.04  ? 157 LEU   A C   1 
ATOM   1310 O  O   . LEU   A 1 156 ? 2.785   -5.260  4.036   1.00 15.88  ? 157 LEU   A O   1 
ATOM   1311 C  CB  . LEU   A 1 156 ? 2.200   -6.370  6.846   1.00 15.93  ? 157 LEU   A CB  1 
ATOM   1312 C  CG  . LEU   A 1 156 ? 3.718   -6.498  6.653   1.00 15.57  ? 157 LEU   A CG  1 
ATOM   1313 C  CD1 . LEU   A 1 156 ? 4.456   -5.217  7.044   1.00 16.99  ? 157 LEU   A CD1 1 
ATOM   1314 C  CD2 . LEU   A 1 156 ? 4.280   -7.658  7.482   1.00 16.20  ? 157 LEU   A CD2 1 
ATOM   1315 N  N   . GLN   A 1 157 ? 0.710   -6.109  3.779   1.00 16.08  ? 158 GLN   A N   1 
ATOM   1316 C  CA  . GLN   A 1 157 ? 1.032   -6.585  2.440   1.00 16.47  ? 158 GLN   A CA  1 
ATOM   1317 C  C   . GLN   A 1 157 ? 1.464   -5.450  1.509   1.00 15.64  ? 158 GLN   A C   1 
ATOM   1318 O  O   . GLN   A 1 157 ? 2.329   -5.677  0.670   1.00 16.64  ? 158 GLN   A O   1 
ATOM   1319 C  CB  . GLN   A 1 157 ? -0.124  -7.383  1.842   1.00 18.42  ? 158 GLN   A CB  1 
ATOM   1320 C  CG  . GLN   A 1 157 ? 0.248   -8.131  0.566   1.00 19.60  ? 158 GLN   A CG  1 
ATOM   1321 C  CD  . GLN   A 1 157 ? 1.355   -9.132  0.808   1.00 18.33  ? 158 GLN   A CD  1 
ATOM   1322 O  OE1 . GLN   A 1 157 ? 1.506   -9.710  1.911   1.00 19.48  ? 158 GLN   A OE1 1 
ATOM   1323 N  NE2 . GLN   A 1 157 ? 2.150   -9.368  -0.224  1.00 21.71  ? 158 GLN   A NE2 1 
ATOM   1324 N  N   . LYS   A 1 158 ? 0.887   -4.242  1.635   1.00 17.16  ? 159 LYS   A N   1 
ATOM   1325 C  CA  . LYS   A 1 158 ? 1.323   -3.146  0.789   1.00 16.85  ? 159 LYS   A CA  1 
ATOM   1326 C  C   . LYS   A 1 158 ? 2.813   -2.848  0.952   1.00 16.21  ? 159 LYS   A C   1 
ATOM   1327 O  O   . LYS   A 1 158 ? 3.471   -2.441  0.007   1.00 17.77  ? 159 LYS   A O   1 
ATOM   1328 C  CB  . LYS   A 1 158 ? 0.434   -1.912  0.956   1.00 20.35  ? 159 LYS   A CB  1 
ATOM   1329 C  CG  . LYS   A 1 158 ? -0.929  -2.071  0.289   1.00 24.45  ? 159 LYS   A CG  1 
ATOM   1330 C  CD  . LYS   A 1 158 ? -1.813  -0.837  0.389   1.00 34.75  ? 159 LYS   A CD  1 
ATOM   1331 C  CE  . LYS   A 1 158 ? -3.273  -1.091  0.037   1.00 42.01  ? 159 LYS   A CE  1 
ATOM   1332 N  NZ  . LYS   A 1 158 ? -4.079  0.153   -0.073  1.00 34.18  ? 159 LYS   A NZ  1 
ATOM   1333 N  N   . VAL   A 1 159 ? 3.305   -2.995  2.176   1.00 15.70  ? 160 VAL   A N   1 
ATOM   1334 C  CA  . VAL   A 1 159 ? 4.718   -2.799  2.423   1.00 15.69  ? 160 VAL   A CA  1 
ATOM   1335 C  C   . VAL   A 1 159 ? 5.514   -3.905  1.740   1.00 15.89  ? 160 VAL   A C   1 
ATOM   1336 O  O   . VAL   A 1 159 ? 6.455   -3.650  1.005   1.00 16.82  ? 160 VAL   A O   1 
ATOM   1337 C  CB  . VAL   A 1 159 ? 5.019   -2.773  3.928   1.00 15.71  ? 160 VAL   A CB  1 
ATOM   1338 C  CG1 . VAL   A 1 159 ? 6.536   -2.792  4.191   1.00 18.15  ? 160 VAL   A CG1 1 
ATOM   1339 C  CG2 . VAL   A 1 159 ? 4.326   -1.601  4.610   1.00 19.11  ? 160 VAL   A CG2 1 
ATOM   1340 N  N   A VAL   A 1 160 ? 5.068   -5.154  1.955   0.50 15.26  ? 161 VAL   A N   1 
ATOM   1341 N  N   B VAL   A 1 160 ? 5.167   -5.173  1.965   0.50 15.26  ? 161 VAL   A N   1 
ATOM   1342 C  CA  A VAL   A 1 160 ? 5.745   -6.310  1.399   0.50 15.06  ? 161 VAL   A CA  1 
ATOM   1343 C  CA  B VAL   A 1 160 ? 6.050   -6.161  1.373   0.50 16.40  ? 161 VAL   A CA  1 
ATOM   1344 C  C   A VAL   A 1 160 ? 5.899   -6.181  -0.110  0.50 16.79  ? 161 VAL   A C   1 
ATOM   1345 C  C   B VAL   A 1 160 ? 5.966   -6.137  -0.165  0.50 16.42  ? 161 VAL   A C   1 
ATOM   1346 O  O   A VAL   A 1 160 ? 6.954   -6.490  -0.652  0.50 18.18  ? 161 VAL   A O   1 
ATOM   1347 O  O   B VAL   A 1 160 ? 6.948   -6.464  -0.824  0.50 20.91  ? 161 VAL   A O   1 
ATOM   1348 C  CB  A VAL   A 1 160 ? 5.005   -7.611  1.760   0.50 14.15  ? 161 VAL   A CB  1 
ATOM   1349 C  CB  B VAL   A 1 160 ? 5.823   -7.563  1.978   0.50 18.87  ? 161 VAL   A CB  1 
ATOM   1350 C  CG1 A VAL   A 1 160 ? 5.525   -8.800  0.954   0.50 15.70  ? 161 VAL   A CG1 1 
ATOM   1351 C  CG1 B VAL   A 1 160 ? 6.210   -7.620  3.445   0.50 18.81  ? 161 VAL   A CG1 1 
ATOM   1352 C  CG2 A VAL   A 1 160 ? 5.156   -7.851  3.255   0.50 13.64  ? 161 VAL   A CG2 1 
ATOM   1353 C  CG2 B VAL   A 1 160 ? 4.375   -7.978  1.809   0.50 20.38  ? 161 VAL   A CG2 1 
ATOM   1354 N  N   . ASP   A 1 161 ? 4.837   -5.705  -0.759  1.00 18.48  ? 162 ASP   A N   1 
ATOM   1355 C  CA  . ASP   A 1 161 ? 4.738   -5.752  -2.209  1.00 20.58  ? 162 ASP   A CA  1 
ATOM   1356 C  C   . ASP   A 1 161 ? 5.623   -4.690  -2.863  1.00 21.58  ? 162 ASP   A C   1 
ATOM   1357 O  O   . ASP   A 1 161 ? 5.928   -4.812  -4.047  1.00 26.52  ? 162 ASP   A O   1 
ATOM   1358 C  CB  . ASP   A 1 161 ? 3.281   -5.665  -2.603  1.00 25.41  ? 162 ASP   A CB  1 
ATOM   1359 C  CG  . ASP   A 1 161 ? 2.670   -7.057  -2.561  1.00 24.09  ? 162 ASP   A CG  1 
ATOM   1360 O  OD1 . ASP   A 1 161 ? 3.427   -8.076  -2.730  1.00 27.88  ? 162 ASP   A OD1 1 
ATOM   1361 O  OD2 . ASP   A 1 161 ? 1.490   -7.126  -2.331  1.00 30.88  ? 162 ASP   A OD2 1 
ATOM   1362 N  N   . VAL   A 1 162 ? 6.046   -3.659  -2.124  1.00 19.03  ? 163 VAL   A N   1 
ATOM   1363 C  CA  . VAL   A 1 162 ? 6.851   -2.601  -2.715  1.00 19.69  ? 163 VAL   A CA  1 
ATOM   1364 C  C   . VAL   A 1 162 ? 8.343   -2.921  -2.542  1.00 18.07  ? 163 VAL   A C   1 
ATOM   1365 O  O   . VAL   A 1 162 ? 9.191   -2.247  -3.098  1.00 18.78  ? 163 VAL   A O   1 
ATOM   1366 C  CB  . VAL   A 1 162 ? 6.472   -1.214  -2.149  1.00 23.49  ? 163 VAL   A CB  1 
ATOM   1367 C  CG1 . VAL   A 1 162 ? 7.034   -1.002  -0.767  1.00 22.73  ? 163 VAL   A CG1 1 
ATOM   1368 C  CG2 . VAL   A 1 162 ? 6.829   -0.036  -3.045  1.00 24.04  ? 163 VAL   A CG2 1 
ATOM   1369 N  N   . LEU   A 1 163 ? 8.694   -3.939  -1.737  1.00 18.48  ? 164 LEU   A N   1 
ATOM   1370 C  CA  . LEU   A 1 163 ? 10.093  -4.143  -1.393  1.00 17.46  ? 164 LEU   A CA  1 
ATOM   1371 C  C   . LEU   A 1 163 ? 10.986  -4.445  -2.599  1.00 18.49  ? 164 LEU   A C   1 
ATOM   1372 O  O   . LEU   A 1 163 ? 12.160  -4.077  -2.594  1.00 19.88  ? 164 LEU   A O   1 
ATOM   1373 C  CB  . LEU   A 1 163 ? 10.258  -5.195  -0.302  1.00 17.28  ? 164 LEU   A CB  1 
ATOM   1374 C  CG  . LEU   A 1 163 ? 9.616   -4.867  1.049   1.00 16.58  ? 164 LEU   A CG  1 
ATOM   1375 C  CD1 . LEU   A 1 163 ? 9.844   -6.006  2.044   1.00 17.62  ? 164 LEU   A CD1 1 
ATOM   1376 C  CD2 . LEU   A 1 163 ? 10.163  -3.558  1.621   1.00 18.14  ? 164 LEU   A CD2 1 
ATOM   1377 N  N   . ASP   A 1 164 ? 10.455  -5.130  -3.611  1.00 21.73  ? 165 ASP   A N   1 
ATOM   1378 C  CA  . ASP   A 1 164 ? 11.280  -5.426  -4.774  1.00 24.96  ? 165 ASP   A CA  1 
ATOM   1379 C  C   . ASP   A 1 164 ? 11.729  -4.142  -5.492  1.00 26.00  ? 165 ASP   A C   1 
ATOM   1380 O  O   . ASP   A 1 164 ? 12.661  -4.190  -6.312  1.00 31.78  ? 165 ASP   A O   1 
ATOM   1381 C  CB  . ASP   A 1 164 ? 10.535  -6.354  -5.729  1.00 32.37  ? 165 ASP   A CB  1 
ATOM   1382 C  CG  . ASP   A 1 164 ? 9.505   -5.569  -6.510  1.00 37.16  ? 165 ASP   A CG  1 
ATOM   1383 O  OD1 . ASP   A 1 164 ? 8.626   -4.968  -5.860  1.00 44.86  ? 165 ASP   A OD1 1 
ATOM   1384 O  OD2 . ASP   A 1 164 ? 9.607   -5.541  -7.764  1.00 51.17  ? 165 ASP   A OD2 1 
ATOM   1385 N  N   . SER   A 1 165 ? 11.047  -3.012  -5.234  1.00 21.21  ? 166 SER   A N   1 
ATOM   1386 C  CA  . SER   A 1 165 ? 11.415  -1.757  -5.869  1.00 24.20  ? 166 SER   A CA  1 
ATOM   1387 C  C   . SER   A 1 165 ? 12.493  -1.000  -5.093  1.00 19.52  ? 166 SER   A C   1 
ATOM   1388 O  O   . SER   A 1 165 ? 13.023  0.001   -5.597  1.00 22.31  ? 166 SER   A O   1 
ATOM   1389 C  CB  . SER   A 1 165 ? 10.194  -0.918  -6.166  1.00 32.06  ? 166 SER   A CB  1 
ATOM   1390 O  OG  . SER   A 1 165 ? 9.705   -0.334  -4.978  1.00 27.51  ? 166 SER   A OG  1 
ATOM   1391 N  N   . ILE   A 1 166 ? 12.801  -1.447  -3.870  1.00 17.85  ? 167 ILE   A N   1 
ATOM   1392 C  CA  . ILE   A 1 166 ? 13.826  -0.792  -3.073  1.00 17.49  ? 167 ILE   A CA  1 
ATOM   1393 C  C   . ILE   A 1 166 ? 14.820  -1.845  -2.591  1.00 15.16  ? 167 ILE   A C   1 
ATOM   1394 O  O   . ILE   A 1 166 ? 15.219  -1.868  -1.421  1.00 16.34  ? 167 ILE   A O   1 
ATOM   1395 C  CB  . ILE   A 1 166 ? 13.234  0.022   -1.901  1.00 16.68  ? 167 ILE   A CB  1 
ATOM   1396 C  CG1 . ILE   A 1 166 ? 12.371  -0.851  -0.995  1.00 17.28  ? 167 ILE   A CG1 1 
ATOM   1397 C  CG2 . ILE   A 1 166 ? 12.457  1.221   -2.411  1.00 18.31  ? 167 ILE   A CG2 1 
ATOM   1398 C  CD1 . ILE   A 1 166 ? 12.365  -0.309  0.422   1.00 18.05  ? 167 ILE   A CD1 1 
ATOM   1399 N  N   . LYS   A 1 167 ? 15.224  -2.741  -3.507  1.00 17.65  ? 168 LYS   A N   1 
ATOM   1400 C  CA  . LYS   A 1 167 ? 16.010  -3.892  -3.087  1.00 16.33  ? 168 LYS   A CA  1 
ATOM   1401 C  C   . LYS   A 1 167 ? 17.332  -3.519  -2.418  1.00 16.26  ? 168 LYS   A C   1 
ATOM   1402 O  O   . LYS   A 1 167 ? 17.774  -4.155  -1.460  1.00 15.86  ? 168 LYS   A O   1 
ATOM   1403 C  CB  . LYS   A 1 167 ? 16.304  -4.806  -4.284  1.00 17.86  ? 168 LYS   A CB  1 
ATOM   1404 C  CG  . LYS   A 1 167 ? 17.081  -6.050  -3.898  1.00 20.29  ? 168 LYS   A CG  1 
ATOM   1405 C  CD  . LYS   A 1 167 ? 17.259  -6.924  -5.132  1.00 27.67  ? 168 LYS   A CD  1 
ATOM   1406 C  CE  . LYS   A 1 167 ? 18.050  -8.186  -4.884  1.00 33.84  ? 168 LYS   A CE  1 
ATOM   1407 N  NZ  . LYS   A 1 167 ? 18.200  -8.998  -6.122  1.00 43.73  ? 168 LYS   A NZ  1 
ATOM   1408 N  N   . THR   A 1 168 ? 17.957  -2.462  -2.930  1.00 16.53  ? 169 THR   A N   1 
ATOM   1409 C  CA  . THR   A 1 168 ? 19.323  -2.131  -2.547  1.00 15.96  ? 169 THR   A CA  1 
ATOM   1410 C  C   . THR   A 1 168 ? 19.418  -0.751  -1.871  1.00 14.54  ? 169 THR   A C   1 
ATOM   1411 O  O   . THR   A 1 168 ? 18.519  0.098   -1.960  1.00 16.47  ? 169 THR   A O   1 
ATOM   1412 C  CB  . THR   A 1 168 ? 20.247  -2.188  -3.781  1.00 17.70  ? 169 THR   A CB  1 
ATOM   1413 O  OG1 . THR   A 1 168 ? 19.684  -1.401  -4.819  1.00 19.92  ? 169 THR   A OG1 1 
ATOM   1414 C  CG2 . THR   A 1 168 ? 20.411  -3.615  -4.287  1.00 19.29  ? 169 THR   A CG2 1 
ATOM   1415 N  N   . LYS   A 1 169 ? 20.525  -0.622  -1.136  1.00 17.94  ? 170 LYS   A N   1 
ATOM   1416 C  CA  . LYS   A 1 169 ? 20.823  0.562   -0.340  1.00 17.47  ? 170 LYS   A CA  1 
ATOM   1417 C  C   . LYS   A 1 169 ? 20.668  1.855   -1.140  1.00 17.20  ? 170 LYS   A C   1 
ATOM   1418 O  O   . LYS   A 1 169 ? 21.207  1.996   -2.254  1.00 19.86  ? 170 LYS   A O   1 
ATOM   1419 C  CB  . LYS   A 1 169 ? 22.260  0.457   0.179   1.00 17.53  ? 170 LYS   A CB  1 
ATOM   1420 C  CG  . LYS   A 1 169 ? 22.737  1.628   1.022   1.00 20.57  ? 170 LYS   A CG  1 
ATOM   1421 C  CD  . LYS   A 1 169 ? 24.070  1.423   1.726   1.00 22.76  ? 170 LYS   A CD  1 
ATOM   1422 C  CE  . LYS   A 1 169 ? 24.613  2.683   2.389   1.00 35.01  ? 170 LYS   A CE  1 
ATOM   1423 N  NZ  . LYS   A 1 169 ? 26.070  2.598   2.649   1.00 45.21  ? 170 LYS   A NZ  1 
ATOM   1424 N  N   . GLY   A 1 170 ? 19.874  2.785   -0.597  1.00 18.59  ? 171 GLY   A N   1 
ATOM   1425 C  CA  . GLY   A 1 170 ? 19.699  4.086   -1.234  1.00 19.77  ? 171 GLY   A CA  1 
ATOM   1426 C  C   . GLY   A 1 170 ? 18.516  4.172   -2.203  1.00 20.31  ? 171 GLY   A C   1 
ATOM   1427 O  O   . GLY   A 1 170 ? 18.189  5.291   -2.641  1.00 22.03  ? 171 GLY   A O   1 
ATOM   1428 N  N   . LYS   A 1 171 ? 17.873  3.032   -2.521  1.00 18.55  ? 172 LYS   A N   1 
ATOM   1429 C  CA  . LYS   A 1 171 ? 16.655  3.095   -3.304  1.00 18.74  ? 172 LYS   A CA  1 
ATOM   1430 C  C   . LYS   A 1 171 ? 15.467  3.563   -2.467  1.00 17.32  ? 172 LYS   A C   1 
ATOM   1431 O  O   . LYS   A 1 171 ? 15.274  3.140   -1.328  1.00 16.75  ? 172 LYS   A O   1 
ATOM   1432 C  CB  . LYS   A 1 171 ? 16.401  1.752   -3.967  1.00 19.32  ? 172 LYS   A CB  1 
ATOM   1433 C  CG  . LYS   A 1 171 ? 17.478  1.320   -4.958  1.00 22.52  ? 172 LYS   A CG  1 
ATOM   1434 C  CD  . LYS   A 1 171 ? 17.075  0.273   -6.006  1.00 31.66  ? 172 LYS   A CD  1 
ATOM   1435 C  CE  . LYS   A 1 171 ? 16.255  0.924   -7.172  0.00 10.00  ? 172 LYS   A CE  1 
ATOM   1436 N  NZ  . LYS   A 1 171 ? 15.120  0.129   -7.697  0.00 10.00  ? 172 LYS   A NZ  1 
ATOM   1437 N  N   A SER   A 1 172 ? 14.594  4.339   -3.101  0.50 18.81  ? 173 SER   A N   1 
ATOM   1438 N  N   B SER   A 1 172 ? 14.622  4.394   -3.087  0.50 19.97  ? 173 SER   A N   1 
ATOM   1439 C  CA  A SER   A 1 172 ? 13.406  4.876   -2.462  0.50 19.90  ? 173 SER   A CA  1 
ATOM   1440 C  CA  B SER   A 1 172 ? 13.336  4.721   -2.498  0.50 20.38  ? 173 SER   A CA  1 
ATOM   1441 C  C   A SER   A 1 172 ? 12.243  4.814   -3.456  0.50 18.84  ? 173 SER   A C   1 
ATOM   1442 C  C   B SER   A 1 172 ? 12.196  4.505   -3.487  0.50 18.99  ? 173 SER   A C   1 
ATOM   1443 O  O   A SER   A 1 172 ? 12.479  4.875   -4.685  0.50 20.21  ? 173 SER   A O   1 
ATOM   1444 O  O   B SER   A 1 172 ? 12.352  4.325   -4.719  0.50 19.03  ? 173 SER   A O   1 
ATOM   1445 C  CB  A SER   A 1 172 ? 13.685  6.278   -1.950  0.50 22.48  ? 173 SER   A CB  1 
ATOM   1446 C  CB  B SER   A 1 172 ? 13.288  6.122   -1.914  0.50 16.40  ? 173 SER   A CB  1 
ATOM   1447 O  OG  A SER   A 1 172 ? 14.301  7.099   -2.944  0.50 24.57  ? 173 SER   A OG  1 
ATOM   1448 O  OG  B SER   A 1 172 ? 13.427  7.126   -2.910  0.50 18.41  ? 173 SER   A OG  1 
ATOM   1449 N  N   . ALA   A 1 173 ? 11.001  4.678   -2.953  1.00 20.55  ? 174 ALA   A N   1 
ATOM   1450 C  CA  . ALA   A 1 173 ? 9.817   4.622   -3.804  1.00 20.29  ? 174 ALA   A CA  1 
ATOM   1451 C  C   . ALA   A 1 173 ? 8.706   5.442   -3.152  1.00 19.37  ? 174 ALA   A C   1 
ATOM   1452 O  O   . ALA   A 1 173 ? 8.628   5.491   -1.933  1.00 18.10  ? 174 ALA   A O   1 
ATOM   1453 C  CB  . ALA   A 1 173 ? 9.363   3.198   -4.020  1.00 23.07  ? 174 ALA   A CB  1 
ATOM   1454 N  N   . ASP   A 1 174 ? 7.866   6.084   -3.961  1.00 22.81  ? 175 ASP   A N   1 
ATOM   1455 C  CA  . ASP   A 1 174 ? 6.678   6.746   -3.441  1.00 24.29  ? 175 ASP   A CA  1 
ATOM   1456 C  C   . ASP   A 1 174 ? 5.882   5.720   -2.662  1.00 23.46  ? 175 ASP   A C   1 
ATOM   1457 O  O   . ASP   A 1 174 ? 5.832   4.555   -3.045  1.00 25.25  ? 175 ASP   A O   1 
ATOM   1458 C  CB  . ASP   A 1 174 ? 5.803   7.309   -4.560  1.00 28.37  ? 175 ASP   A CB  1 
ATOM   1459 C  CG  . ASP   A 1 174 ? 6.518   8.379   -5.368  1.00 32.98  ? 175 ASP   A CG  1 
ATOM   1460 O  OD1 . ASP   A 1 174 ? 7.308   9.143   -4.764  1.00 44.30  ? 175 ASP   A OD1 1 
ATOM   1461 O  OD2 . ASP   A 1 174 ? 6.299   8.437   -6.575  1.00 45.06  ? 175 ASP   A OD2 1 
ATOM   1462 N  N   . PHE   A 1 175 ? 5.320   6.169   -1.533  1.00 19.15  ? 176 PHE   A N   1 
ATOM   1463 C  CA  . PHE   A 1 175 ? 4.609   5.268   -0.649  1.00 18.67  ? 176 PHE   A CA  1 
ATOM   1464 C  C   . PHE   A 1 175 ? 3.535   6.060   0.058   1.00 18.88  ? 176 PHE   A C   1 
ATOM   1465 O  O   . PHE   A 1 175 ? 3.619   6.256   1.246   1.00 22.73  ? 176 PHE   A O   1 
ATOM   1466 C  CB  . PHE   A 1 175 ? 5.581   4.482   0.239   1.00 20.94  ? 176 PHE   A CB  1 
ATOM   1467 C  CG  . PHE   A 1 175 ? 4.981   3.203   0.755   1.00 19.98  ? 176 PHE   A CG  1 
ATOM   1468 C  CD1 . PHE   A 1 175 ? 4.739   2.132   -0.088  1.00 20.43  ? 176 PHE   A CD1 1 
ATOM   1469 C  CD2 . PHE   A 1 175 ? 4.610   3.092   2.083   1.00 19.15  ? 176 PHE   A CD2 1 
ATOM   1470 C  CE1 . PHE   A 1 175 ? 4.173   0.959   0.393   1.00 22.33  ? 176 PHE   A CE1 1 
ATOM   1471 C  CE2 . PHE   A 1 175 ? 4.083   1.916   2.594   1.00 20.92  ? 176 PHE   A CE2 1 
ATOM   1472 C  CZ  . PHE   A 1 175 ? 3.844   0.864   1.741   1.00 19.92  ? 176 PHE   A CZ  1 
ATOM   1473 N  N   . THR   A 1 176 ? 2.582   6.563   -0.699  1.00 18.51  ? 177 THR   A N   1 
ATOM   1474 C  CA  . THR   A 1 176 ? 1.542   7.404   -0.139  1.00 17.80  ? 177 THR   A CA  1 
ATOM   1475 C  C   . THR   A 1 176 ? 0.359   6.548   0.263   1.00 15.93  ? 177 THR   A C   1 
ATOM   1476 O  O   . THR   A 1 176 ? 0.173   5.417   -0.232  1.00 17.59  ? 177 THR   A O   1 
ATOM   1477 C  CB  . THR   A 1 176 ? 1.139   8.453   -1.183  1.00 19.92  ? 177 THR   A CB  1 
ATOM   1478 O  OG1 . THR   A 1 176 ? 0.725   7.823   -2.399  1.00 24.55  ? 177 THR   A OG1 1 
ATOM   1479 C  CG2 . THR   A 1 176 ? 2.286   9.388   -1.503  1.00 29.17  ? 177 THR   A CG2 1 
ATOM   1480 N  N   . ASN   A 1 177 ? -0.475  7.122   1.132   1.00 17.12  ? 178 ASN   A N   1 
ATOM   1481 C  CA  . ASN   A 1 177 ? -1.755  6.551   1.523   1.00 17.37  ? 178 ASN   A CA  1 
ATOM   1482 C  C   . ASN   A 1 177 ? -1.603  5.225   2.254   1.00 17.05  ? 178 ASN   A C   1 
ATOM   1483 O  O   . ASN   A 1 177 ? -2.518  4.422   2.195   1.00 21.96  ? 178 ASN   A O   1 
ATOM   1484 C  CB  . ASN   A 1 177 ? -2.693  6.468   0.322   1.00 19.34  ? 178 ASN   A CB  1 
ATOM   1485 C  CG  . ASN   A 1 177 ? -2.872  7.850   -0.262  1.00 18.96  ? 178 ASN   A CG  1 
ATOM   1486 O  OD1 . ASN   A 1 177 ? -3.526  8.712   0.314   1.00 22.03  ? 178 ASN   A OD1 1 
ATOM   1487 N  ND2 . ASN   A 1 177 ? -2.271  8.094   -1.414  1.00 18.11  ? 178 ASN   A ND2 1 
ATOM   1488 N  N   . PHE   A 1 178 ? -0.476  5.009   2.940   1.00 16.44  ? 179 PHE   A N   1 
ATOM   1489 C  CA  . PHE   A 1 178 ? -0.353  3.803   3.736   1.00 17.58  ? 179 PHE   A CA  1 
ATOM   1490 C  C   . PHE   A 1 178 ? -0.880  4.099   5.130   1.00 16.67  ? 179 PHE   A C   1 
ATOM   1491 O  O   . PHE   A 1 178 ? -0.508  5.097   5.745   1.00 17.75  ? 179 PHE   A O   1 
ATOM   1492 C  CB  . PHE   A 1 178 ? 1.104   3.356   3.841   1.00 17.60  ? 179 PHE   A CB  1 
ATOM   1493 C  CG  . PHE   A 1 178 ? 1.206   2.101   4.682   1.00 16.29  ? 179 PHE   A CG  1 
ATOM   1494 C  CD1 . PHE   A 1 178 ? 0.830   0.849   4.174   1.00 17.70  ? 179 PHE   A CD1 1 
ATOM   1495 C  CD2 . PHE   A 1 178 ? 1.607   2.159   6.015   1.00 15.64  ? 179 PHE   A CD2 1 
ATOM   1496 C  CE1 . PHE   A 1 178 ? 0.852   -0.282  4.966   1.00 17.87  ? 179 PHE   A CE1 1 
ATOM   1497 C  CE2 . PHE   A 1 178 ? 1.637   1.011   6.799   1.00 15.23  ? 179 PHE   A CE2 1 
ATOM   1498 C  CZ  . PHE   A 1 178 ? 1.263   -0.200  6.280   1.00 16.27  ? 179 PHE   A CZ  1 
ATOM   1499 N  N   . ASP   A 1 179 ? -1.740  3.222   5.635   1.00 16.97  ? 180 ASP   A N   1 
ATOM   1500 C  CA  . ASP   A 1 179 ? -2.385  3.405   6.921   1.00 16.83  ? 180 ASP   A CA  1 
ATOM   1501 C  C   . ASP   A 1 179 ? -1.715  2.553   7.991   1.00 15.13  ? 180 ASP   A C   1 
ATOM   1502 O  O   . ASP   A 1 179 ? -1.924  1.335   8.041   1.00 16.41  ? 180 ASP   A O   1 
ATOM   1503 C  CB  . ASP   A 1 179 ? -3.867  3.052   6.824   1.00 19.27  ? 180 ASP   A CB  1 
ATOM   1504 C  CG  . ASP   A 1 179 ? -4.674  3.523   8.019   1.00 21.06  ? 180 ASP   A CG  1 
ATOM   1505 O  OD1 . ASP   A 1 179 ? -4.099  3.687   9.123   1.00 18.26  ? 180 ASP   A OD1 1 
ATOM   1506 O  OD2 . ASP   A 1 179 ? -5.882  3.733   7.842   1.00 28.07  ? 180 ASP   A OD2 1 
ATOM   1507 N  N   . PRO   A 1 180 ? -0.903  3.144   8.915   1.00 14.44  ? 181 PRO   A N   1 
ATOM   1508 C  CA  . PRO   A 1 180 ? -0.188  2.320   9.897   1.00 14.70  ? 181 PRO   A CA  1 
ATOM   1509 C  C   . PRO   A 1 180 ? -1.102  1.670   10.927  1.00 14.49  ? 181 PRO   A C   1 
ATOM   1510 O  O   . PRO   A 1 180 ? -0.661  0.810   11.670  1.00 14.51  ? 181 PRO   A O   1 
ATOM   1511 C  CB  . PRO   A 1 180 ? 0.839   3.289   10.483  1.00 16.14  ? 181 PRO   A CB  1 
ATOM   1512 C  CG  . PRO   A 1 180 ? 0.184   4.651   10.332  1.00 16.64  ? 181 PRO   A CG  1 
ATOM   1513 C  CD  . PRO   A 1 180 ? -0.599  4.580   9.029   1.00 15.66  ? 181 PRO   A CD  1 
ATOM   1514 N  N   . ARG   A 1 181 ? -2.381  2.094   10.982  1.00 14.99  ? 182 ARG   A N   1 
ATOM   1515 C  CA  . ARG   A 1 181 ? -3.296  1.412   11.904  1.00 15.73  ? 182 ARG   A CA  1 
ATOM   1516 C  C   . ARG   A 1 181 ? -3.399  -0.068  11.569  1.00 15.08  ? 182 ARG   A C   1 
ATOM   1517 O  O   . ARG   A 1 181 ? -3.750  -0.851  12.455  1.00 17.27  ? 182 ARG   A O   1 
ATOM   1518 C  CB  . ARG   A 1 181 ? -4.675  2.065   11.898  1.00 16.98  ? 182 ARG   A CB  1 
ATOM   1519 C  CG  . ARG   A 1 181 ? -4.650  3.492   12.423  1.00 18.34  ? 182 ARG   A CG  1 
ATOM   1520 C  CD  . ARG   A 1 181 ? -5.991  4.155   12.363  1.00 21.49  ? 182 ARG   A CD  1 
ATOM   1521 N  NE  . ARG   A 1 181 ? -6.331  4.405   10.976  1.00 20.51  ? 182 ARG   A NE  1 
ATOM   1522 C  CZ  . ARG   A 1 181 ? -7.456  5.021   10.618  1.00 24.58  ? 182 ARG   A CZ  1 
ATOM   1523 N  NH1 . ARG   A 1 181 ? -8.297  5.436   11.552  1.00 28.91  ? 182 ARG   A NH1 1 
ATOM   1524 N  NH2 . ARG   A 1 181 ? -7.699  5.244   9.341   1.00 27.01  ? 182 ARG   A NH2 1 
ATOM   1525 N  N   . GLY   A 1 182 ? -3.168  -0.436  10.294  1.00 15.87  ? 183 GLY   A N   1 
ATOM   1526 C  CA  . GLY   A 1 182 ? -3.254  -1.839  9.916   1.00 17.36  ? 183 GLY   A CA  1 
ATOM   1527 C  C   . GLY   A 1 182 ? -2.098  -2.695  10.437  1.00 16.04  ? 183 GLY   A C   1 
ATOM   1528 O  O   . GLY   A 1 182 ? -2.103  -3.893  10.186  1.00 18.50  ? 183 GLY   A O   1 
ATOM   1529 N  N   . LEU   A 1 183 ? -1.134  -2.123  11.181  1.00 15.69  ? 184 LEU   A N   1 
ATOM   1530 C  CA  . LEU   A 1 183 ? -0.008  -2.863  11.727  1.00 15.64  ? 184 LEU   A CA  1 
ATOM   1531 C  C   . LEU   A 1 183 ? -0.158  -3.092  13.225  1.00 14.94  ? 184 LEU   A C   1 
ATOM   1532 O  O   . LEU   A 1 183 ? 0.718   -3.703  13.830  1.00 16.79  ? 184 LEU   A O   1 
ATOM   1533 C  CB  . LEU   A 1 183 ? 1.295   -2.111  11.447  1.00 15.57  ? 184 LEU   A CB  1 
ATOM   1534 C  CG  . LEU   A 1 183 ? 1.617   -1.959  9.960   1.00 17.02  ? 184 LEU   A CG  1 
ATOM   1535 C  CD1 . LEU   A 1 183 ? 2.882   -1.128  9.829   1.00 19.74  ? 184 LEU   A CD1 1 
ATOM   1536 C  CD2 . LEU   A 1 183 ? 1.776   -3.295  9.250   1.00 20.45  ? 184 LEU   A CD2 1 
ATOM   1537 N  N   . LEU   A 1 184 ? -1.260  -2.614  13.829  1.00 15.52  ? 185 LEU   A N   1 
ATOM   1538 C  CA  . LEU   A 1 184 ? -1.390  -2.674  15.270  1.00 14.46  ? 185 LEU   A CA  1 
ATOM   1539 C  C   . LEU   A 1 184 ? -2.103  -3.955  15.706  1.00 17.15  ? 185 LEU   A C   1 
ATOM   1540 O  O   . LEU   A 1 184 ? -2.997  -4.435  15.022  1.00 25.03  ? 185 LEU   A O   1 
ATOM   1541 C  CB  . LEU   A 1 184 ? -2.206  -1.476  15.772  1.00 15.31  ? 185 LEU   A CB  1 
ATOM   1542 C  CG  . LEU   A 1 184 ? -1.630  -0.096  15.416  1.00 14.59  ? 185 LEU   A CG  1 
ATOM   1543 C  CD1 . LEU   A 1 184 ? -2.519  1.029   15.870  1.00 17.18  ? 185 LEU   A CD1 1 
ATOM   1544 C  CD2 . LEU   A 1 184 ? -0.220  0.046   15.956  1.00 17.67  ? 185 LEU   A CD2 1 
ATOM   1545 N  N   . PRO   A 1 185 ? -1.774  -4.528  16.872  1.00 14.49  ? 186 PRO   A N   1 
ATOM   1546 C  CA  . PRO   A 1 185 ? -2.546  -5.632  17.440  1.00 15.38  ? 186 PRO   A CA  1 
ATOM   1547 C  C   . PRO   A 1 185 ? -3.821  -5.070  18.071  1.00 15.72  ? 186 PRO   A C   1 
ATOM   1548 O  O   . PRO   A 1 185 ? -4.026  -3.872  18.128  1.00 17.52  ? 186 PRO   A O   1 
ATOM   1549 C  CB  . PRO   A 1 185 ? -1.563  -6.203  18.479  1.00 14.51  ? 186 PRO   A CB  1 
ATOM   1550 C  CG  . PRO   A 1 185 ? -0.856  -4.951  18.959  1.00 13.30  ? 186 PRO   A CG  1 
ATOM   1551 C  CD  . PRO   A 1 185 ? -0.637  -4.120  17.712  1.00 13.09  ? 186 PRO   A CD  1 
ATOM   1552 N  N   A GLU   A 1 186 ? -4.620  -6.019  18.554  0.50 16.72  ? 187 GLU   A N   1 
ATOM   1553 N  N   B GLU   A 1 186 ? -4.694  -5.933  18.633  0.50 16.23  ? 187 GLU   A N   1 
ATOM   1554 C  CA  A GLU   A 1 186 ? -5.884  -5.720  19.191  0.50 17.74  ? 187 GLU   A CA  1 
ATOM   1555 C  CA  B GLU   A 1 186 ? -5.952  -5.470  19.237  0.50 16.40  ? 187 GLU   A CA  1 
ATOM   1556 C  C   A GLU   A 1 186 ? -5.655  -4.836  20.416  0.50 17.05  ? 187 GLU   A C   1 
ATOM   1557 C  C   B GLU   A 1 186 ? -5.712  -4.746  20.554  0.50 15.69  ? 187 GLU   A C   1 
ATOM   1558 O  O   A GLU   A 1 186 ? -6.209  -3.732  20.457  0.50 18.34  ? 187 GLU   A O   1 
ATOM   1559 O  O   B GLU   A 1 186 ? -6.379  -3.749  20.875  0.50 16.39  ? 187 GLU   A O   1 
ATOM   1560 C  CB  A GLU   A 1 186 ? -6.599  -7.030  19.495  0.50 20.39  ? 187 GLU   A CB  1 
ATOM   1561 C  CB  B GLU   A 1 186 ? -6.841  -6.620  19.701  0.50 17.25  ? 187 GLU   A CB  1 
ATOM   1562 C  CG  A GLU   A 1 186 ? -7.902  -6.793  20.208  0.50 24.24  ? 187 GLU   A CG  1 
ATOM   1563 C  CG  B GLU   A 1 186 ? -7.463  -7.399  18.580  0.50 18.90  ? 187 GLU   A CG  1 
ATOM   1564 C  CD  A GLU   A 1 186 ? -8.550  -8.072  20.700  0.50 25.32  ? 187 GLU   A CD  1 
ATOM   1565 C  CD  B GLU   A 1 186 ? -8.159  -8.675  19.032  0.50 20.82  ? 187 GLU   A CD  1 
ATOM   1566 O  OE1 A GLU   A 1 186 ? -9.083  -8.055  21.829  0.50 29.08  ? 187 GLU   A OE1 1 
ATOM   1567 O  OE1 B GLU   A 1 186 ? -8.056  -9.025  20.241  0.50 21.88  ? 187 GLU   A OE1 1 
ATOM   1568 O  OE2 A GLU   A 1 186 ? -8.512  -9.087  19.954  0.50 26.21  ? 187 GLU   A OE2 1 
ATOM   1569 O  OE2 B GLU   A 1 186 ? -8.816  -9.302  18.195  0.50 24.51  ? 187 GLU   A OE2 1 
ATOM   1570 N  N   . SER   A 1 187 ? -4.804  -5.297  21.360  1.00 15.50  ? 188 SER   A N   1 
ATOM   1571 C  CA  . SER   A 1 187 ? -4.570  -4.678  22.657  1.00 16.27  ? 188 SER   A CA  1 
ATOM   1572 C  C   . SER   A 1 187 ? -3.461  -3.630  22.578  1.00 15.28  ? 188 SER   A C   1 
ATOM   1573 O  O   . SER   A 1 187 ? -2.434  -3.855  21.915  1.00 16.99  ? 188 SER   A O   1 
ATOM   1574 C  CB  . SER   A 1 187 ? -4.179  -5.712  23.670  1.00 16.67  ? 188 SER   A CB  1 
ATOM   1575 O  OG  . SER   A 1 187 ? -3.902  -5.140  24.949  1.00 17.71  ? 188 SER   A OG  1 
ATOM   1576 N  N   . LEU   A 1 188 ? -3.611  -2.557  23.355  1.00 15.92  ? 189 LEU   A N   1 
ATOM   1577 C  CA  . LEU   A 1 188 ? -2.548  -1.573  23.545  1.00 15.73  ? 189 LEU   A CA  1 
ATOM   1578 C  C   . LEU   A 1 188 ? -1.927  -1.692  24.928  1.00 14.90  ? 189 LEU   A C   1 
ATOM   1579 O  O   . LEU   A 1 188 ? -1.268  -0.764  25.368  1.00 16.69  ? 189 LEU   A O   1 
ATOM   1580 C  CB  . LEU   A 1 188 ? -3.058  -0.151  23.262  1.00 16.93  ? 189 LEU   A CB  1 
ATOM   1581 C  CG  . LEU   A 1 188 ? -3.458  0.182   21.825  1.00 18.45  ? 189 LEU   A CG  1 
ATOM   1582 C  CD1 . LEU   A 1 188 ? -4.024  1.586   21.706  1.00 21.38  ? 189 LEU   A CD1 1 
ATOM   1583 C  CD2 . LEU   A 1 188 ? -2.317  -0.032  20.840  1.00 21.02  ? 189 LEU   A CD2 1 
ATOM   1584 N  N   . ASP   A 1 189 ? -2.056  -2.853  25.590  1.00 14.81  ? 190 ASP   A N   1 
ATOM   1585 C  CA  . ASP   A 1 189 ? -1.323  -3.061  26.826  1.00 15.19  ? 190 ASP   A CA  1 
ATOM   1586 C  C   . ASP   A 1 189 ? 0.185   -3.047  26.524  1.00 13.81  ? 190 ASP   A C   1 
ATOM   1587 O  O   . ASP   A 1 189 ? 0.620   -3.550  25.476  1.00 13.40  ? 190 ASP   A O   1 
ATOM   1588 C  CB  . ASP   A 1 189 ? -1.688  -4.399  27.464  1.00 17.25  ? 190 ASP   A CB  1 
ATOM   1589 C  CG  . ASP   A 1 189 ? -3.076  -4.450  28.094  1.00 22.89  ? 190 ASP   A CG  1 
ATOM   1590 O  OD1 . ASP   A 1 189 ? -3.705  -3.385  28.245  1.00 29.42  ? 190 ASP   A OD1 1 
ATOM   1591 O  OD2 . ASP   A 1 189 ? -3.528  -5.558  28.418  1.00 28.61  ? 190 ASP   A OD2 1 
ATOM   1592 N  N   . TYR   A 1 190 ? 0.980   -2.471  27.448  1.00 13.06  ? 191 TYR   A N   1 
ATOM   1593 C  CA  . TYR   A 1 190 ? 2.383   -2.216  27.112  1.00 12.69  ? 191 TYR   A CA  1 
ATOM   1594 C  C   . TYR   A 1 190 ? 3.276   -2.313  28.345  1.00 11.88  ? 191 TYR   A C   1 
ATOM   1595 O  O   . TYR   A 1 190 ? 2.848   -2.172  29.485  1.00 12.88  ? 191 TYR   A O   1 
ATOM   1596 C  CB  . TYR   A 1 190 ? 2.515   -0.833  26.459  1.00 12.48  ? 191 TYR   A CB  1 
ATOM   1597 C  CG  . TYR   A 1 190 ? 2.132   0.320   27.352  1.00 12.38  ? 191 TYR   A CG  1 
ATOM   1598 C  CD1 . TYR   A 1 190 ? 3.034   0.916   28.215  1.00 13.19  ? 191 TYR   A CD1 1 
ATOM   1599 C  CD2 . TYR   A 1 190 ? 0.839   0.825   27.332  1.00 13.64  ? 191 TYR   A CD2 1 
ATOM   1600 C  CE1 . TYR   A 1 190 ? 2.646   1.942   29.074  1.00 14.23  ? 191 TYR   A CE1 1 
ATOM   1601 C  CE2 . TYR   A 1 190 ? 0.437   1.871   28.152  1.00 14.12  ? 191 TYR   A CE2 1 
ATOM   1602 C  CZ  . TYR   A 1 190 ? 1.350   2.450   29.019  1.00 14.28  ? 191 TYR   A CZ  1 
ATOM   1603 O  OH  . TYR   A 1 190 ? 0.999   3.443   29.877  1.00 15.50  ? 191 TYR   A OH  1 
ATOM   1604 N  N   . TRP   A 1 191 ? 4.576   -2.460  28.037  1.00 11.20  ? 192 TRP   A N   1 
ATOM   1605 C  CA  . TRP   A 1 191 ? 5.646   -2.197  28.994  1.00 11.84  ? 192 TRP   A CA  1 
ATOM   1606 C  C   . TRP   A 1 191 ? 6.346   -0.902  28.572  1.00 10.88  ? 192 TRP   A C   1 
ATOM   1607 O  O   . TRP   A 1 191 ? 6.363   -0.546  27.415  1.00 11.94  ? 192 TRP   A O   1 
ATOM   1608 C  CB  . TRP   A 1 191 ? 6.699   -3.323  28.977  1.00 12.07  ? 192 TRP   A CB  1 
ATOM   1609 C  CG  . TRP   A 1 191 ? 6.188   -4.665  29.367  1.00 12.02  ? 192 TRP   A CG  1 
ATOM   1610 C  CD1 . TRP   A 1 191 ? 5.965   -5.108  30.638  1.00 13.04  ? 192 TRP   A CD1 1 
ATOM   1611 C  CD2 . TRP   A 1 191 ? 5.921   -5.782  28.498  1.00 12.47  ? 192 TRP   A CD2 1 
ATOM   1612 N  NE1 . TRP   A 1 191 ? 5.577   -6.431  30.614  1.00 13.99  ? 192 TRP   A NE1 1 
ATOM   1613 C  CE2 . TRP   A 1 191 ? 5.499   -6.850  29.315  1.00 13.08  ? 192 TRP   A CE2 1 
ATOM   1614 C  CE3 . TRP   A 1 191 ? 5.976   -5.970  27.111  1.00 12.77  ? 192 TRP   A CE3 1 
ATOM   1615 C  CZ2 . TRP   A 1 191 ? 5.220   -8.112  28.768  1.00 14.36  ? 192 TRP   A CZ2 1 
ATOM   1616 C  CZ3 . TRP   A 1 191 ? 5.696   -7.212  26.577  1.00 14.21  ? 192 TRP   A CZ3 1 
ATOM   1617 C  CH2 . TRP   A 1 191 ? 5.304   -8.259  27.402  1.00 15.68  ? 192 TRP   A CH2 1 
ATOM   1618 N  N   . THR   A 1 192 ? 6.958   -0.230  29.544  1.00 10.84  ? 193 THR   A N   1 
ATOM   1619 C  CA  . THR   A 1 192 ? 7.684   0.998   29.222  1.00 11.50  ? 193 THR   A CA  1 
ATOM   1620 C  C   . THR   A 1 192 ? 8.927   1.124   30.095  1.00 10.75  ? 193 THR   A C   1 
ATOM   1621 O  O   . THR   A 1 192 ? 8.942   0.751   31.259  1.00 11.81  ? 193 THR   A O   1 
ATOM   1622 C  CB  . THR   A 1 192 ? 6.761   2.224   29.348  1.00 11.63  ? 193 THR   A CB  1 
ATOM   1623 O  OG1 . THR   A 1 192 ? 7.441   3.407   28.935  1.00 11.58  ? 193 THR   A OG1 1 
ATOM   1624 C  CG2 . THR   A 1 192 ? 6.241   2.464   30.743  1.00 13.20  ? 193 THR   A CG2 1 
ATOM   1625 N  N   . TYR   A 1 193 ? 9.964   1.750   29.515  1.00 11.17  ? 194 TYR   A N   1 
ATOM   1626 C  CA  . TYR   A 1 193 ? 11.203  2.022   30.257  1.00 10.98  ? 194 TYR   A CA  1 
ATOM   1627 C  C   . TYR   A 1 193 ? 11.957  3.096   29.476  1.00 10.54  ? 194 TYR   A C   1 
ATOM   1628 O  O   . TYR   A 1 193 ? 11.751  3.272   28.281  1.00 10.79  ? 194 TYR   A O   1 
ATOM   1629 C  CB  . TYR   A 1 193 ? 12.049  0.740   30.454  1.00 11.41  ? 194 TYR   A CB  1 
ATOM   1630 C  CG  . TYR   A 1 193 ? 12.713  0.264   29.191  1.00 11.11  ? 194 TYR   A CG  1 
ATOM   1631 C  CD1 . TYR   A 1 193 ? 12.042  -0.467  28.196  1.00 11.30  ? 194 TYR   A CD1 1 
ATOM   1632 C  CD2 . TYR   A 1 193 ? 14.036  0.623   28.952  1.00 11.44  ? 194 TYR   A CD2 1 
ATOM   1633 C  CE1 . TYR   A 1 193 ? 12.671  -0.796  27.002  1.00 10.77  ? 194 TYR   A CE1 1 
ATOM   1634 C  CE2 . TYR   A 1 193 ? 14.686  0.283   27.772  1.00 11.27  ? 194 TYR   A CE2 1 
ATOM   1635 C  CZ  . TYR   A 1 193 ? 13.989  -0.411  26.790  1.00 10.66  ? 194 TYR   A CZ  1 
ATOM   1636 O  OH  . TYR   A 1 193 ? 14.637  -0.704  25.612  1.00 10.65  ? 194 TYR   A OH  1 
ATOM   1637 N  N   . PRO   A 1 194 ? 12.903  3.796   30.155  1.00 10.91  ? 195 PRO   A N   1 
ATOM   1638 C  CA  . PRO   A 1 194 ? 13.747  4.788   29.466  1.00 11.44  ? 195 PRO   A CA  1 
ATOM   1639 C  C   . PRO   A 1 194 ? 14.950  4.131   28.811  1.00 10.48  ? 195 PRO   A C   1 
ATOM   1640 O  O   . PRO   A 1 194 ? 15.674  3.349   29.462  1.00 11.83  ? 195 PRO   A O   1 
ATOM   1641 C  CB  . PRO   A 1 194 ? 14.192  5.689   30.622  1.00 12.55  ? 195 PRO   A CB  1 
ATOM   1642 C  CG  . PRO   A 1 194 ? 14.248  4.763   31.817  1.00 13.07  ? 195 PRO   A CG  1 
ATOM   1643 C  CD  . PRO   A 1 194 ? 13.066  3.808   31.615  1.00 12.53  ? 195 PRO   A CD  1 
ATOM   1644 N  N   . GLY   A 1 195 ? 15.150  4.447   27.540  1.00 10.79  ? 196 GLY   A N   1 
ATOM   1645 C  CA  . GLY   A 1 195 ? 16.253  3.824   26.814  1.00 11.19  ? 196 GLY   A CA  1 
ATOM   1646 C  C   . GLY   A 1 195 ? 16.828  4.718   25.732  1.00 10.47  ? 196 GLY   A C   1 
ATOM   1647 O  O   . GLY   A 1 195 ? 16.953  5.939   25.872  1.00 10.80  ? 196 GLY   A O   1 
ATOM   1648 N  N   . SER   A 1 196 ? 17.226  4.071   24.642  1.00 10.18  ? 197 SER   A N   1 
ATOM   1649 C  CA  . SER   A 1 196 ? 18.075  4.694   23.627  1.00 10.55  ? 197 SER   A CA  1 
ATOM   1650 C  C   . SER   A 1 196 ? 17.611  4.294   22.237  1.00 10.04  ? 197 SER   A C   1 
ATOM   1651 O  O   . SER   A 1 196 ? 16.852  3.335   22.069  1.00 10.57  ? 197 SER   A O   1 
ATOM   1652 C  CB  . SER   A 1 196 ? 19.535  4.312   23.806  1.00 11.12  ? 197 SER   A CB  1 
ATOM   1653 O  OG  . SER   A 1 196 ? 19.773  2.961   23.391  1.00 10.94  ? 197 SER   A OG  1 
ATOM   1654 N  N   . LEU   A 1 197 ? 18.152  4.976   21.219  1.00 10.32  ? 198 LEU   A N   1 
ATOM   1655 C  CA  . LEU   A 1 197 ? 18.159  4.386   19.877  1.00 10.69  ? 198 LEU   A CA  1 
ATOM   1656 C  C   . LEU   A 1 197 ? 18.861  3.042   19.966  1.00 10.76  ? 198 LEU   A C   1 
ATOM   1657 O  O   . LEU   A 1 197 ? 19.889  2.910   20.654  1.00 11.12  ? 198 LEU   A O   1 
ATOM   1658 C  CB  . LEU   A 1 197 ? 18.934  5.289   18.917  1.00 11.91  ? 198 LEU   A CB  1 
ATOM   1659 C  CG  . LEU   A 1 197 ? 18.503  6.747   18.823  1.00 14.53  ? 198 LEU   A CG  1 
ATOM   1660 C  CD1 . LEU   A 1 197 ? 19.377  7.464   17.818  1.00 16.36  ? 198 LEU   A CD1 1 
ATOM   1661 C  CD2 . LEU   A 1 197 ? 17.066  6.916   18.460  1.00 16.51  ? 198 LEU   A CD2 1 
ATOM   1662 N  N   . THR   A 1 198 ? 18.389  2.057   19.182  1.00 10.58  ? 199 THR   A N   1 
ATOM   1663 C  CA  . THR   A 1 198 ? 19.069  0.772   19.142  1.00 11.05  ? 199 THR   A CA  1 
ATOM   1664 C  C   . THR   A 1 198 ? 20.109  0.715   18.023  1.00 11.45  ? 199 THR   A C   1 
ATOM   1665 O  O   . THR   A 1 198 ? 20.741  -0.327  17.845  1.00 12.25  ? 199 THR   A O   1 
ATOM   1666 C  CB  . THR   A 1 198 ? 18.066  -0.373  18.981  1.00 10.56  ? 199 THR   A CB  1 
ATOM   1667 O  OG1 . THR   A 1 198 ? 17.543  -0.294  17.657  1.00 10.82  ? 199 THR   A OG1 1 
ATOM   1668 C  CG2 . THR   A 1 198 ? 16.998  -0.396  20.049  1.00 11.56  ? 199 THR   A CG2 1 
ATOM   1669 N  N   . THR   A 1 199 ? 20.236  1.796   17.274  1.00 12.22  ? 200 THR   A N   1 
ATOM   1670 C  CA  . THR   A 1 199 ? 21.175  1.899   16.173  1.00 13.10  ? 200 THR   A CA  1 
ATOM   1671 C  C   . THR   A 1 199 ? 22.083  3.084   16.440  1.00 12.69  ? 200 THR   A C   1 
ATOM   1672 O  O   . THR   A 1 199 ? 21.646  4.078   17.020  1.00 13.23  ? 200 THR   A O   1 
ATOM   1673 C  CB  . THR   A 1 199 ? 20.451  2.188   14.864  1.00 14.84  ? 200 THR   A CB  1 
ATOM   1674 O  OG1 . THR   A 1 199 ? 19.645  3.362   14.998  1.00 18.72  ? 200 THR   A OG1 1 
ATOM   1675 C  CG2 . THR   A 1 199 ? 19.586  1.026   14.468  1.00 15.48  ? 200 THR   A CG2 1 
ATOM   1676 N  N   . PRO   A 1 200 ? 23.357  3.071   15.988  1.00 13.33  ? 201 PRO   A N   1 
ATOM   1677 C  CA  . PRO   A 1 200 ? 24.157  4.279   16.063  1.00 13.77  ? 201 PRO   A CA  1 
ATOM   1678 C  C   . PRO   A 1 200 ? 23.347  5.450   15.522  1.00 13.61  ? 201 PRO   A C   1 
ATOM   1679 O  O   . PRO   A 1 200 ? 22.680  5.319   14.492  1.00 15.64  ? 201 PRO   A O   1 
ATOM   1680 C  CB  . PRO   A 1 200 ? 25.347  3.910   15.176  1.00 15.29  ? 201 PRO   A CB  1 
ATOM   1681 C  CG  . PRO   A 1 200 ? 25.520  2.440   15.464  1.00 15.64  ? 201 PRO   A CG  1 
ATOM   1682 C  CD  . PRO   A 1 200 ? 24.090  1.927   15.404  1.00 14.45  ? 201 PRO   A CD  1 
ATOM   1683 N  N   . PRO   A 1 201 ? 23.400  6.630   16.167  1.00 13.73  ? 202 PRO   A N   1 
ATOM   1684 C  CA  . PRO   A 1 201 ? 24.344  6.997   17.234  1.00 14.43  ? 202 PRO   A CA  1 
ATOM   1685 C  C   . PRO   A 1 201 ? 23.965  6.616   18.674  1.00 13.21  ? 202 PRO   A C   1 
ATOM   1686 O  O   . PRO   A 1 201 ? 24.633  7.055   19.615  1.00 14.10  ? 202 PRO   A O   1 
ATOM   1687 C  CB  . PRO   A 1 201 ? 24.434  8.528   17.041  1.00 16.11  ? 202 PRO   A CB  1 
ATOM   1688 C  CG  . PRO   A 1 201 ? 23.044  8.907   16.566  1.00 17.92  ? 202 PRO   A CG  1 
ATOM   1689 C  CD  . PRO   A 1 201 ? 22.687  7.792   15.623  1.00 16.09  ? 202 PRO   A CD  1 
ATOM   1690 N  N   . LEU   A 1 202 ? 22.928  5.779   18.849  1.00 12.21  ? 203 LEU   A N   1 
ATOM   1691 C  CA  . LEU   A 1 202 ? 22.679  5.156   20.145  1.00 11.83  ? 203 LEU   A CA  1 
ATOM   1692 C  C   . LEU   A 1 202 ? 22.291  6.166   21.228  1.00 11.81  ? 203 LEU   A C   1 
ATOM   1693 O  O   . LEU   A 1 202 ? 22.448  5.939   22.429  1.00 12.08  ? 203 LEU   A O   1 
ATOM   1694 C  CB  . LEU   A 1 202 ? 23.850  4.269   20.628  1.00 12.33  ? 203 LEU   A CB  1 
ATOM   1695 C  CG  . LEU   A 1 202 ? 24.183  3.104   19.700  1.00 12.33  ? 203 LEU   A CG  1 
ATOM   1696 C  CD1 . LEU   A 1 202 ? 25.481  2.423   20.114  1.00 14.82  ? 203 LEU   A CD1 1 
ATOM   1697 C  CD2 . LEU   A 1 202 ? 23.047  2.081   19.603  1.00 12.85  ? 203 LEU   A CD2 1 
ATOM   1698 N  N   . LEU   A 1 203 ? 21.713  7.305   20.795  1.00 12.86  ? 204 LEU   A N   1 
ATOM   1699 C  CA  . LEU   A 1 203 ? 21.429  8.406   21.699  1.00 12.73  ? 204 LEU   A CA  1 
ATOM   1700 C  C   . LEU   A 1 203 ? 20.377  8.000   22.728  1.00 11.63  ? 204 LEU   A C   1 
ATOM   1701 O  O   . LEU   A 1 203 ? 19.410  7.271   22.442  1.00 11.80  ? 204 LEU   A O   1 
ATOM   1702 C  CB  . LEU   A 1 203 ? 20.935  9.609   20.913  1.00 13.91  ? 204 LEU   A CB  1 
ATOM   1703 C  CG  . LEU   A 1 203 ? 21.982  10.200  19.963  1.00 15.73  ? 204 LEU   A CG  1 
ATOM   1704 C  CD1 . LEU   A 1 203 ? 21.347  11.257  19.070  1.00 18.18  ? 204 LEU   A CD1 1 
ATOM   1705 C  CD2 . LEU   A 1 203 ? 23.159  10.824  20.718  1.00 23.64  ? 204 LEU   A CD2 1 
ATOM   1706 N  N   . GLU   A 1 204 ? 20.572  8.475   23.963  1.00 12.45  ? 205 GLU   A N   1 
ATOM   1707 C  CA  . GLU   A 1 204 ? 19.744  8.104   25.100  1.00 12.47  ? 205 GLU   A CA  1 
ATOM   1708 C  C   . GLU   A 1 204 ? 18.565  9.070   25.232  1.00 12.23  ? 205 GLU   A C   1 
ATOM   1709 O  O   . GLU   A 1 204 ? 18.452  9.825   26.181  1.00 14.49  ? 205 GLU   A O   1 
ATOM   1710 C  CB  . GLU   A 1 204 ? 20.618  7.960   26.352  1.00 13.71  ? 205 GLU   A CB  1 
ATOM   1711 C  CG  . GLU   A 1 204 ? 21.530  6.752   26.225  1.00 13.91  ? 205 GLU   A CG  1 
ATOM   1712 C  CD  . GLU   A 1 204 ? 22.420  6.465   27.414  1.00 13.87  ? 205 GLU   A CD  1 
ATOM   1713 O  OE1 . GLU   A 1 204 ? 22.753  7.400   28.165  1.00 16.65  ? 205 GLU   A OE1 1 
ATOM   1714 O  OE2 . GLU   A 1 204 ? 22.817  5.288   27.572  1.00 14.35  ? 205 GLU   A OE2 1 
ATOM   1715 N  N   . CYS   A 1 205 ? 17.675  8.998   24.245  1.00 11.72  ? 206 CYS   A N   1 
ATOM   1716 C  CA  . CYS   A 1 205 ? 16.621  9.987   24.053  1.00 11.80  ? 206 CYS   A CA  1 
ATOM   1717 C  C   . CYS   A 1 205 ? 15.237  9.367   23.963  1.00 11.51  ? 206 CYS   A C   1 
ATOM   1718 O  O   . CYS   A 1 205 ? 14.293  10.060  23.611  1.00 13.12  ? 206 CYS   A O   1 
ATOM   1719 C  CB  . CYS   A 1 205 ? 16.882  10.840  22.807  1.00 13.15  ? 206 CYS   A CB  1 
ATOM   1720 S  SG  . CYS   A 1 205 ? 16.957  9.852   21.287  1.00 13.33  ? 206 CYS   A SG  1 
ATOM   1721 N  N   . VAL   A 1 206 ? 15.110  8.049   24.221  1.00 11.20  ? 207 VAL   A N   1 
ATOM   1722 C  CA  . VAL   A 1 206 ? 13.867  7.348   23.875  1.00 10.86  ? 207 VAL   A CA  1 
ATOM   1723 C  C   . VAL   A 1 206 ? 13.114  6.879   25.120  1.00 10.86  ? 207 VAL   A C   1 
ATOM   1724 O  O   . VAL   A 1 206 ? 13.654  6.205   25.991  1.00 12.42  ? 207 VAL   A O   1 
ATOM   1725 C  CB  . VAL   A 1 206 ? 14.158  6.097   23.039  1.00 11.17  ? 207 VAL   A CB  1 
ATOM   1726 C  CG1 . VAL   A 1 206 ? 12.853  5.357   22.688  1.00 11.65  ? 207 VAL   A CG1 1 
ATOM   1727 C  CG2 . VAL   A 1 206 ? 14.890  6.473   21.753  1.00 12.48  ? 207 VAL   A CG2 1 
ATOM   1728 N  N   . THR   A 1 207 ? 11.813  7.203   25.171  1.00 10.49  ? 208 THR   A N   1 
ATOM   1729 C  CA  . THR   A 1 207 ? 10.875  6.459   26.012  1.00 11.31  ? 208 THR   A CA  1 
ATOM   1730 C  C   . THR   A 1 207 ? 10.335  5.293   25.190  1.00 9.94   ? 208 THR   A C   1 
ATOM   1731 O  O   . THR   A 1 207 ? 9.661   5.474   24.176  1.00 10.97  ? 208 THR   A O   1 
ATOM   1732 C  CB  . THR   A 1 207 ? 9.699   7.336   26.482  1.00 11.45  ? 208 THR   A CB  1 
ATOM   1733 O  OG1 . THR   A 1 207 ? 10.207  8.461   27.202  1.00 12.64  ? 208 THR   A OG1 1 
ATOM   1734 C  CG2 . THR   A 1 207 ? 8.749   6.550   27.362  1.00 13.52  ? 208 THR   A CG2 1 
ATOM   1735 N  N   . TRP   A 1 208 ? 10.695  4.065   25.607  1.00 9.98   ? 209 TRP   A N   1 
ATOM   1736 C  CA  . TRP   A 1 208 ? 10.248  2.875   24.897  1.00 9.96   ? 209 TRP   A CA  1 
ATOM   1737 C  C   . TRP   A 1 208 ? 8.866   2.479   25.415  1.00 10.14  ? 209 TRP   A C   1 
ATOM   1738 O  O   . TRP   A 1 208 ? 8.651   2.425   26.620  1.00 10.49  ? 209 TRP   A O   1 
ATOM   1739 C  CB  . TRP   A 1 208 ? 11.255  1.713   25.106  1.00 10.73  ? 209 TRP   A CB  1 
ATOM   1740 C  CG  . TRP   A 1 208 ? 12.377  1.839   24.122  1.00 9.69   ? 209 TRP   A CG  1 
ATOM   1741 C  CD1 . TRP   A 1 208 ? 13.616  2.420   24.294  1.00 10.66  ? 209 TRP   A CD1 1 
ATOM   1742 C  CD2 . TRP   A 1 208 ? 12.302  1.421   22.758  1.00 9.92   ? 209 TRP   A CD2 1 
ATOM   1743 N  NE1 . TRP   A 1 208 ? 14.300  2.385   23.114  1.00 10.74  ? 209 TRP   A NE1 1 
ATOM   1744 C  CE2 . TRP   A 1 208 ? 13.522  1.796   22.133  1.00 10.33  ? 209 TRP   A CE2 1 
ATOM   1745 C  CE3 . TRP   A 1 208 ? 11.326  0.769   21.985  1.00 10.02  ? 209 TRP   A CE3 1 
ATOM   1746 C  CZ2 . TRP   A 1 208 ? 13.773  1.543   20.788  1.00 10.97  ? 209 TRP   A CZ2 1 
ATOM   1747 C  CZ3 . TRP   A 1 208 ? 11.575  0.515   20.666  1.00 10.87  ? 209 TRP   A CZ3 1 
ATOM   1748 C  CH2 . TRP   A 1 208 ? 12.778  0.903   20.077  1.00 11.06  ? 209 TRP   A CH2 1 
ATOM   1749 N  N   . ILE   A 1 209 ? 8.003   2.119   24.469  1.00 9.89   ? 210 ILE   A N   1 
ATOM   1750 C  CA  . ILE   A 1 209 ? 6.685   1.596   24.779  1.00 10.50  ? 210 ILE   A CA  1 
ATOM   1751 C  C   . ILE   A 1 209 ? 6.561   0.338   23.938  1.00 9.44   ? 210 ILE   A C   1 
ATOM   1752 O  O   . ILE   A 1 209 ? 6.501   0.430   22.719  1.00 10.89  ? 210 ILE   A O   1 
ATOM   1753 C  CB  . ILE   A 1 209 ? 5.604   2.647   24.424  1.00 11.19  ? 210 ILE   A CB  1 
ATOM   1754 C  CG1 . ILE   A 1 209 ? 5.811   3.918   25.246  1.00 12.38  ? 210 ILE   A CG1 1 
ATOM   1755 C  CG2 . ILE   A 1 209 ? 4.228   2.019   24.692  1.00 12.94  ? 210 ILE   A CG2 1 
ATOM   1756 C  CD1 . ILE   A 1 209 ? 4.995   5.107   24.731  1.00 13.90  ? 210 ILE   A CD1 1 
ATOM   1757 N  N   . VAL   A 1 210 ? 6.593   -0.834  24.579  1.00 9.91   ? 211 VAL   A N   1 
ATOM   1758 C  CA  . VAL   A 1 210 ? 6.605   -2.126  23.869  1.00 10.31  ? 211 VAL   A CA  1 
ATOM   1759 C  C   . VAL   A 1 210 ? 5.270   -2.815  24.153  1.00 10.32  ? 211 VAL   A C   1 
ATOM   1760 O  O   . VAL   A 1 210 ? 4.930   -3.062  25.290  1.00 11.31  ? 211 VAL   A O   1 
ATOM   1761 C  CB  . VAL   A 1 210 ? 7.804   -2.981  24.321  1.00 10.85  ? 211 VAL   A CB  1 
ATOM   1762 C  CG1 . VAL   A 1 210 ? 7.758   -4.335  23.616  1.00 11.75  ? 211 VAL   A CG1 1 
ATOM   1763 C  CG2 . VAL   A 1 210 ? 9.122   -2.235  24.046  1.00 12.36  ? 211 VAL   A CG2 1 
ATOM   1764 N  N   . LEU   A 1 211 ? 4.539   -3.091  23.070  1.00 10.83  ? 212 LEU   A N   1 
ATOM   1765 C  CA  . LEU   A 1 211 ? 3.223   -3.721  23.252  1.00 11.43  ? 212 LEU   A CA  1 
ATOM   1766 C  C   . LEU   A 1 211 ? 3.382   -5.181  23.645  1.00 11.16  ? 212 LEU   A C   1 
ATOM   1767 O  O   . LEU   A 1 211 ? 4.242   -5.910  23.134  1.00 11.95  ? 212 LEU   A O   1 
ATOM   1768 C  CB  . LEU   A 1 211 ? 2.441   -3.623  21.936  1.00 12.13  ? 212 LEU   A CB  1 
ATOM   1769 C  CG  . LEU   A 1 211 ? 2.057   -2.200  21.529  1.00 12.73  ? 212 LEU   A CG  1 
ATOM   1770 C  CD1 . LEU   A 1 211 ? 1.031   -2.285  20.383  1.00 14.45  ? 212 LEU   A CD1 1 
ATOM   1771 C  CD2 . LEU   A 1 211 ? 1.514   -1.373  22.673  1.00 13.95  ? 212 LEU   A CD2 1 
ATOM   1772 N  N   . LYS   A 1 212 ? 2.507   -5.630  24.562  1.00 12.23  ? 213 LYS   A N   1 
ATOM   1773 C  CA  A LYS   A 1 212 ? 2.411   -7.009  25.034  0.50 13.80  ? 213 LYS   A CA  1 
ATOM   1774 C  CA  B LYS   A 1 212 ? 2.590   -7.026  24.969  0.50 13.13  ? 213 LYS   A CA  1 
ATOM   1775 C  C   . LYS   A 1 212 ? 2.066   -7.975  23.895  1.00 12.65  ? 213 LYS   A C   1 
ATOM   1776 O  O   . LYS   A 1 212 ? 2.576   -9.103  23.809  1.00 15.03  ? 213 LYS   A O   1 
ATOM   1777 C  CB  A LYS   A 1 212 ? 1.340   -6.990  26.139  0.50 15.28  ? 213 LYS   A CB  1 
ATOM   1778 C  CB  B LYS   A 1 212 ? 1.904   -7.301  26.314  0.50 14.28  ? 213 LYS   A CB  1 
ATOM   1779 C  CG  A LYS   A 1 212 ? 0.764   -8.307  26.624  0.50 19.94  ? 213 LYS   A CG  1 
ATOM   1780 C  CG  B LYS   A 1 212 ? 1.753   -8.779  26.657  0.50 18.42  ? 213 LYS   A CG  1 
ATOM   1781 C  CD  A LYS   A 1 212 ? -0.441  -8.058  27.516  0.50 20.32  ? 213 LYS   A CD  1 
ATOM   1782 C  CD  B LYS   A 1 212 ? 0.917   -9.037  27.892  0.50 23.11  ? 213 LYS   A CD  1 
ATOM   1783 C  CE  A LYS   A 1 212 ? -1.777  -7.958  26.807  0.50 26.79  ? 213 LYS   A CE  1 
ATOM   1784 C  CE  B LYS   A 1 212 ? 0.842   -10.497 28.301  0.50 28.71  ? 213 LYS   A CE  1 
ATOM   1785 N  NZ  A LYS   A 1 212 ? -2.933  -8.000  27.742  0.50 28.14  ? 213 LYS   A NZ  1 
ATOM   1786 N  NZ  B LYS   A 1 212 ? 0.123   -10.702 29.581  0.50 37.04  ? 213 LYS   A NZ  1 
ATOM   1787 N  N   . GLU   A 1 213 ? 1.091   -7.570  23.079  1.00 12.57  ? 214 GLU   A N   1 
ATOM   1788 C  CA  . GLU   A 1 213 ? 0.506   -8.477  22.103  1.00 13.14  ? 214 GLU   A CA  1 
ATOM   1789 C  C   . GLU   A 1 213 ? 1.273   -8.384  20.804  1.00 12.19  ? 214 GLU   A C   1 
ATOM   1790 O  O   . GLU   A 1 213 ? 1.345   -7.311  20.212  1.00 12.38  ? 214 GLU   A O   1 
ATOM   1791 C  CB  . GLU   A 1 213 ? -0.957  -8.132  21.845  1.00 14.40  ? 214 GLU   A CB  1 
ATOM   1792 C  CG  . GLU   A 1 213 ? -1.657  -9.098  20.925  1.00 17.31  ? 214 GLU   A CG  1 
ATOM   1793 C  CD  . GLU   A 1 213 ? -3.132  -8.796  20.662  1.00 19.89  ? 214 GLU   A CD  1 
ATOM   1794 O  OE1 . GLU   A 1 213 ? -3.725  -8.006  21.375  1.00 19.86  ? 214 GLU   A OE1 1 
ATOM   1795 O  OE2 . GLU   A 1 213 ? -3.686  -9.438  19.746  1.00 35.55  ? 214 GLU   A OE2 1 
ATOM   1796 N  N   A PRO   A 1 214 ? 1.803   -9.511  20.288  0.50 11.81  ? 215 PRO   A N   1 
ATOM   1797 N  N   B PRO   A 1 214 ? 1.923   -9.474  20.343  0.50 12.07  ? 215 PRO   A N   1 
ATOM   1798 C  CA  A PRO   A 1 214 ? 2.458   -9.469  18.993  0.50 11.59  ? 215 PRO   A CA  1 
ATOM   1799 C  CA  B PRO   A 1 214 ? 2.526   -9.468  19.011  0.50 12.32  ? 215 PRO   A CA  1 
ATOM   1800 C  C   A PRO   A 1 214 ? 1.405   -9.356  17.907  0.50 12.19  ? 215 PRO   A C   1 
ATOM   1801 C  C   B PRO   A 1 214 ? 1.507   -9.516  17.880  0.50 12.06  ? 215 PRO   A C   1 
ATOM   1802 O  O   A PRO   A 1 214 ? 0.215   -9.591  18.163  0.50 12.95  ? 215 PRO   A O   1 
ATOM   1803 O  O   B PRO   A 1 214 ? 0.416   -10.053 18.047  0.50 13.25  ? 215 PRO   A O   1 
ATOM   1804 C  CB  A PRO   A 1 214 ? 3.148   -10.844 18.871  0.50 12.67  ? 215 PRO   A CB  1 
ATOM   1805 C  CB  B PRO   A 1 214 ? 3.325   -10.789 18.971  0.50 13.33  ? 215 PRO   A CB  1 
ATOM   1806 C  CG  A PRO   A 1 214 ? 2.347   -11.766 19.766  0.50 12.81  ? 215 PRO   A CG  1 
ATOM   1807 C  CG  B PRO   A 1 214 ? 3.434   -11.205 20.424  0.50 15.51  ? 215 PRO   A CG  1 
ATOM   1808 C  CD  A PRO   A 1 214 ? 1.734   -10.875 20.838  0.50 13.08  ? 215 PRO   A CD  1 
ATOM   1809 C  CD  B PRO   A 1 214 ? 2.156   -10.732 21.070  0.50 13.28  ? 215 PRO   A CD  1 
ATOM   1810 N  N   . ILE   A 1 215 ? 1.878   -8.996  16.708  1.00 12.66  ? 216 ILE   A N   1 
ATOM   1811 C  CA  . ILE   A 1 215 ? 1.092   -9.251  15.509  1.00 12.94  ? 216 ILE   A CA  1 
ATOM   1812 C  C   . ILE   A 1 215 ? 1.629   -10.512 14.855  1.00 12.57  ? 216 ILE   A C   1 
ATOM   1813 O  O   . ILE   A 1 215 ? 2.796   -10.862 15.000  1.00 14.04  ? 216 ILE   A O   1 
ATOM   1814 C  CB  . ILE   A 1 215 ? 1.083   -8.044  14.553  1.00 13.92  ? 216 ILE   A CB  1 
ATOM   1815 C  CG1 . ILE   A 1 215 ? 2.488   -7.687  14.037  1.00 14.36  ? 216 ILE   A CG1 1 
ATOM   1816 C  CG2 . ILE   A 1 215 ? 0.371   -6.846  15.179  1.00 15.41  ? 216 ILE   A CG2 1 
ATOM   1817 C  CD1 . ILE   A 1 215 ? 2.474   -6.703  12.846  1.00 16.07  ? 216 ILE   A CD1 1 
ATOM   1818 N  N   A SER   A 1 216 ? 0.759   -11.115 14.044  0.50 13.73  ? 217 SER   A N   1 
ATOM   1819 N  N   B SER   A 1 216 ? 0.777   -11.217 14.123  0.50 14.18  ? 217 SER   A N   1 
ATOM   1820 C  CA  A SER   A 1 216 ? 1.090   -12.281 13.241  0.50 12.91  ? 217 SER   A CA  1 
ATOM   1821 C  CA  B SER   A 1 216 ? 1.296   -12.328 13.344  0.50 15.14  ? 217 SER   A CA  1 
ATOM   1822 C  C   A SER   A 1 216 ? 1.355   -11.845 11.810  0.50 13.07  ? 217 SER   A C   1 
ATOM   1823 C  C   B SER   A 1 216 ? 1.357   -11.922 11.886  0.50 13.52  ? 217 SER   A C   1 
ATOM   1824 O  O   A SER   A 1 216 ? 0.583   -11.073 11.238  0.50 15.34  ? 217 SER   A O   1 
ATOM   1825 O  O   B SER   A 1 216 ? 0.428   -11.272 11.393  0.50 13.90  ? 217 SER   A O   1 
ATOM   1826 C  CB  A SER   A 1 216 ? -0.007  -13.330 13.304  0.50 13.49  ? 217 SER   A CB  1 
ATOM   1827 C  CB  B SER   A 1 216 ? 0.463   -13.560 13.506  0.50 19.20  ? 217 SER   A CB  1 
ATOM   1828 O  OG  A SER   A 1 216 ? -0.016  -14.010 14.563  0.50 17.64  ? 217 SER   A OG  1 
ATOM   1829 O  OG  B SER   A 1 216 ? -0.876  -13.278 13.146  0.50 21.67  ? 217 SER   A OG  1 
ATOM   1830 N  N   . VAL   A 1 217 ? 2.452   -12.354 11.241  1.00 13.18  ? 218 VAL   A N   1 
ATOM   1831 C  CA  . VAL   A 1 217 ? 2.709   -12.166 9.826   1.00 13.68  ? 218 VAL   A CA  1 
ATOM   1832 C  C   . VAL   A 1 217 ? 2.969   -13.539 9.236   1.00 13.14  ? 218 VAL   A C   1 
ATOM   1833 O  O   . VAL   A 1 217 ? 3.329   -14.479 9.943   1.00 13.94  ? 218 VAL   A O   1 
ATOM   1834 C  CB  . VAL   A 1 217 ? 3.901   -11.212 9.607   1.00 14.81  ? 218 VAL   A CB  1 
ATOM   1835 C  CG1 . VAL   A 1 217 ? 3.662   -9.876  10.285  1.00 15.23  ? 218 VAL   A CG1 1 
ATOM   1836 C  CG2 . VAL   A 1 217 ? 5.197   -11.844 10.091  1.00 15.71  ? 218 VAL   A CG2 1 
ATOM   1837 N  N   . SER   A 1 218 ? 2.795   -13.672 7.929   1.00 13.41  ? 219 SER   A N   1 
ATOM   1838 C  CA  . SER   A 1 218 ? 2.989   -14.996 7.342   1.00 13.90  ? 219 SER   A CA  1 
ATOM   1839 C  C   . SER   A 1 218 ? 4.470   -15.259 7.051   1.00 14.03  ? 219 SER   A C   1 
ATOM   1840 O  O   . SER   A 1 218 ? 5.284   -14.347 6.942   1.00 14.59  ? 219 SER   A O   1 
ATOM   1841 C  CB  . SER   A 1 218 ? 2.175   -15.171 6.078   1.00 15.01  ? 219 SER   A CB  1 
ATOM   1842 O  OG  . SER   A 1 218 ? 2.664   -14.285 5.091   1.00 15.72  ? 219 SER   A OG  1 
ATOM   1843 N  N   A SER   A 1 219 ? 4.807   -16.542 6.872   0.50 13.58  ? 220 SER   A N   1 
ATOM   1844 N  N   B SER   A 1 219 ? 4.790   -16.542 6.902   0.50 15.19  ? 220 SER   A N   1 
ATOM   1845 C  CA  A SER   A 1 219 ? 6.155   -16.931 6.492   0.50 14.63  ? 220 SER   A CA  1 
ATOM   1846 C  CA  B SER   A 1 219 ? 6.137   -16.903 6.516   0.50 17.56  ? 220 SER   A CA  1 
ATOM   1847 C  C   A SER   A 1 219 ? 6.531   -16.264 5.170   0.50 16.03  ? 220 SER   A C   1 
ATOM   1848 C  C   B SER   A 1 219 ? 6.505   -16.197 5.213   0.50 16.59  ? 220 SER   A C   1 
ATOM   1849 O  O   A SER   A 1 219 ? 7.672   -15.858 4.972   0.50 16.15  ? 220 SER   A O   1 
ATOM   1850 O  O   B SER   A 1 219 ? 7.623   -15.710 5.079   0.50 17.56  ? 220 SER   A O   1 
ATOM   1851 C  CB  A SER   A 1 219 ? 6.267   -18.455 6.460   0.50 15.63  ? 220 SER   A CB  1 
ATOM   1852 C  CB  B SER   A 1 219 ? 6.253   -18.406 6.432   0.50 20.98  ? 220 SER   A CB  1 
ATOM   1853 O  OG  A SER   A 1 219 ? 5.343   -19.012 5.537   0.50 14.61  ? 220 SER   A OG  1 
ATOM   1854 O  OG  B SER   A 1 219 ? 7.590   -18.786 6.163   0.50 24.93  ? 220 SER   A OG  1 
ATOM   1855 N  N   . GLU   A 1 220 ? 5.555   -16.098 4.279   1.00 15.34  ? 221 GLU   A N   1 
ATOM   1856 C  CA  . GLU   A 1 220 ? 5.833   -15.491 2.992   1.00 17.24  ? 221 GLU   A CA  1 
ATOM   1857 C  C   . GLU   A 1 220 ? 6.142   -14.002 3.151   1.00 16.07  ? 221 GLU   A C   1 
ATOM   1858 O  O   . GLU   A 1 220 ? 6.987   -13.441 2.433   1.00 17.82  ? 221 GLU   A O   1 
ATOM   1859 C  CB  . GLU   A 1 220 ? 4.673   -15.628 2.022   1.00 19.59  ? 221 GLU   A CB  1 
ATOM   1860 C  CG  . GLU   A 1 220 ? 4.433   -17.082 1.579   1.00 22.57  ? 221 GLU   A CG  1 
ATOM   1861 C  CD  . GLU   A 1 220 ? 3.603   -17.904 2.548   1.00 23.31  ? 221 GLU   A CD  1 
ATOM   1862 O  OE1 . GLU   A 1 220 ? 3.048   -17.380 3.522   1.00 20.89  ? 221 GLU   A OE1 1 
ATOM   1863 O  OE2 . GLU   A 1 220 ? 3.493   -19.104 2.324   1.00 30.86  ? 221 GLU   A OE2 1 
ATOM   1864 N  N   . GLN   A 1 221 ? 5.448   -13.320 4.072   1.00 14.65  ? 222 GLN   A N   1 
ATOM   1865 C  CA  . GLN   A 1 221 ? 5.706   -11.890 4.273   1.00 14.58  ? 222 GLN   A CA  1 
ATOM   1866 C  C   . GLN   A 1 221 ? 7.135   -11.675 4.806   1.00 14.45  ? 222 GLN   A C   1 
ATOM   1867 O  O   . GLN   A 1 221 ? 7.888   -10.825 4.300   1.00 15.31  ? 222 GLN   A O   1 
ATOM   1868 C  CB  . GLN   A 1 221 ? 4.648   -11.314 5.212   1.00 14.69  ? 222 GLN   A CB  1 
ATOM   1869 C  CG  . GLN   A 1 221 ? 3.298   -11.180 4.533   1.00 14.88  ? 222 GLN   A CG  1 
ATOM   1870 C  CD  . GLN   A 1 221 ? 2.209   -10.638 5.430   1.00 14.26  ? 222 GLN   A CD  1 
ATOM   1871 O  OE1 . GLN   A 1 221 ? 2.089   -11.010 6.602   1.00 14.53  ? 222 GLN   A OE1 1 
ATOM   1872 N  NE2 . GLN   A 1 221 ? 1.373   -9.764  4.870   1.00 15.29  ? 222 GLN   A NE2 1 
ATOM   1873 N  N   . VAL   A 1 222 ? 7.526   -12.431 5.837   1.00 14.70  ? 223 VAL   A N   1 
ATOM   1874 C  CA  . VAL   A 1 222 ? 8.869   -12.256 6.378   1.00 14.81  ? 223 VAL   A CA  1 
ATOM   1875 C  C   . VAL   A 1 222 ? 9.949   -12.715 5.387   1.00 15.56  ? 223 VAL   A C   1 
ATOM   1876 O  O   . VAL   A 1 222 ? 11.033  -12.113 5.338   1.00 16.39  ? 223 VAL   A O   1 
ATOM   1877 C  CB  . VAL   A 1 222 ? 9.029   -12.840 7.803   1.00 17.73  ? 223 VAL   A CB  1 
ATOM   1878 C  CG1 . VAL   A 1 222 ? 9.028   -14.337 7.761   1.00 20.22  ? 223 VAL   A CG1 1 
ATOM   1879 C  CG2 . VAL   A 1 222 ? 10.289  -12.315 8.497   1.00 20.21  ? 223 VAL   A CG2 1 
ATOM   1880 N  N   A LEU   A 1 223 ? 9.684   -13.737 4.571   0.50 16.09  ? 224 LEU   A N   1 
ATOM   1881 N  N   B LEU   A 1 223 ? 9.650   -13.763 4.604   0.50 16.82  ? 224 LEU   A N   1 
ATOM   1882 C  CA  A LEU   A 1 223 ? 10.672  -14.124 3.580   0.50 17.86  ? 224 LEU   A CA  1 
ATOM   1883 C  CA  B LEU   A 1 223 ? 10.539  -14.180 3.536   0.50 18.74  ? 224 LEU   A CA  1 
ATOM   1884 C  C   A LEU   A 1 223 ? 10.968  -12.980 2.614   0.50 16.59  ? 224 LEU   A C   1 
ATOM   1885 C  C   B LEU   A 1 223 ? 10.945  -12.983 2.684   0.50 16.63  ? 224 LEU   A C   1 
ATOM   1886 O  O   A LEU   A 1 223 ? 12.103  -12.843 2.139   0.50 16.90  ? 224 LEU   A O   1 
ATOM   1887 O  O   B LEU   A 1 223 ? 12.130  -12.822 2.367   0.50 18.91  ? 224 LEU   A O   1 
ATOM   1888 C  CB  A LEU   A 1 223 ? 10.148  -15.339 2.815   0.50 20.09  ? 224 LEU   A CB  1 
ATOM   1889 C  CB  B LEU   A 1 223 ? 9.846   -15.229 2.659   0.50 20.41  ? 224 LEU   A CB  1 
ATOM   1890 C  CG  A LEU   A 1 223 ? 10.195  -16.654 3.582   0.50 23.25  ? 224 LEU   A CG  1 
ATOM   1891 C  CG  B LEU   A 1 223 ? 10.709  -15.751 1.510   0.50 23.34  ? 224 LEU   A CG  1 
ATOM   1892 C  CD1 A LEU   A 1 223 ? 9.425   -17.720 2.815   0.50 28.30  ? 224 LEU   A CD1 1 
ATOM   1893 C  CD1 B LEU   A 1 223 ? 11.940  -16.452 2.068   0.50 30.32  ? 224 LEU   A CD1 1 
ATOM   1894 C  CD2 A LEU   A 1 223 ? 11.632  -17.089 3.823   0.50 25.17  ? 224 LEU   A CD2 1 
ATOM   1895 C  CD2 B LEU   A 1 223 ? 9.919   -16.720 0.635   0.50 30.01  ? 224 LEU   A CD2 1 
ATOM   1896 N  N   . LYS   A 1 224 ? 9.965   -12.144 2.314   1.00 16.78  ? 225 LYS   A N   1 
ATOM   1897 C  CA  . LYS   A 1 224 ? 10.214  -11.018 1.419   1.00 17.84  ? 225 LYS   A CA  1 
ATOM   1898 C  C   . LYS   A 1 224 ? 11.095  -9.962  2.088   1.00 15.08  ? 225 LYS   A C   1 
ATOM   1899 O  O   . LYS   A 1 224 ? 11.928  -9.342  1.432   1.00 16.02  ? 225 LYS   A O   1 
ATOM   1900 C  CB  . LYS   A 1 224 ? 8.886   -10.501 0.866   1.00 20.24  ? 225 LYS   A CB  1 
ATOM   1901 C  CG  . LYS   A 1 224 ? 8.303   -11.538 -0.099  1.00 24.31  ? 225 LYS   A CG  1 
ATOM   1902 C  CD  . LYS   A 1 224 ? 6.990   -11.225 -0.761  1.00 27.78  ? 225 LYS   A CD  1 
ATOM   1903 C  CE  . LYS   A 1 224 ? 6.620   -12.325 -1.743  1.00 38.84  ? 225 LYS   A CE  1 
ATOM   1904 N  NZ  . LYS   A 1 224 ? 5.273   -12.177 -2.350  1.00 35.76  ? 225 LYS   A NZ  1 
ATOM   1905 N  N   . PHE   A 1 225 ? 10.981  -9.750  3.410   1.00 14.36  ? 226 PHE   A N   1 
ATOM   1906 C  CA  . PHE   A 1 225 ? 11.931  -8.893  4.095   1.00 14.35  ? 226 PHE   A CA  1 
ATOM   1907 C  C   . PHE   A 1 225 ? 13.355  -9.380  3.860   1.00 14.57  ? 226 PHE   A C   1 
ATOM   1908 O  O   . PHE   A 1 225 ? 14.295  -8.606  3.674   1.00 15.03  ? 226 PHE   A O   1 
ATOM   1909 C  CB  . PHE   A 1 225 ? 11.719  -8.891  5.608   1.00 14.76  ? 226 PHE   A CB  1 
ATOM   1910 C  CG  . PHE   A 1 225 ? 10.518  -8.118  6.090   1.00 14.67  ? 226 PHE   A CG  1 
ATOM   1911 C  CD1 . PHE   A 1 225 ? 9.442   -7.878  5.253   1.00 17.80  ? 226 PHE   A CD1 1 
ATOM   1912 C  CD2 . PHE   A 1 225 ? 10.461  -7.636  7.388   1.00 16.93  ? 226 PHE   A CD2 1 
ATOM   1913 C  CE1 . PHE   A 1 225 ? 8.339   -7.167  5.700   1.00 19.51  ? 226 PHE   A CE1 1 
ATOM   1914 C  CE2 . PHE   A 1 225 ? 9.358   -6.926  7.834   1.00 20.38  ? 226 PHE   A CE2 1 
ATOM   1915 C  CZ  . PHE   A 1 225 ? 8.299   -6.693  6.990   1.00 19.14  ? 226 PHE   A CZ  1 
ATOM   1916 N  N   . ARG   A 1 226 ? 13.530  -10.701 3.942   1.00 14.35  ? 227 ARG   A N   1 
ATOM   1917 C  CA  . ARG   A 1 226 ? 14.854  -11.293 3.878   1.00 15.31  ? 227 ARG   A CA  1 
ATOM   1918 C  C   . ARG   A 1 226 ? 15.458  -11.294 2.469   1.00 16.90  ? 227 ARG   A C   1 
ATOM   1919 O  O   . ARG   A 1 226 ? 16.621  -11.696 2.330   1.00 17.83  ? 227 ARG   A O   1 
ATOM   1920 C  CB  . ARG   A 1 226 ? 14.827  -12.725 4.427   1.00 16.01  ? 227 ARG   A CB  1 
ATOM   1921 C  CG  . ARG   A 1 226 ? 14.345  -12.859 5.863   1.00 15.18  ? 227 ARG   A CG  1 
ATOM   1922 C  CD  . ARG   A 1 226 ? 14.426  -14.290 6.327   1.00 16.92  ? 227 ARG   A CD  1 
ATOM   1923 N  NE  . ARG   A 1 226 ? 13.853  -14.446 7.660   1.00 15.23  ? 227 ARG   A NE  1 
ATOM   1924 C  CZ  . ARG   A 1 226 ? 12.913  -15.300 8.027   1.00 16.96  ? 227 ARG   A CZ  1 
ATOM   1925 N  NH1 . ARG   A 1 226 ? 12.489  -16.220 7.172   1.00 21.70  ? 227 ARG   A NH1 1 
ATOM   1926 N  NH2 . ARG   A 1 226 ? 12.482  -15.297 9.264   1.00 18.09  ? 227 ARG   A NH2 1 
ATOM   1927 N  N   . LYS   A 1 227 ? 14.712  -10.845 1.442   1.00 14.98  ? 228 LYS   A N   1 
ATOM   1928 C  CA  . LYS   A 1 227 ? 15.252  -10.743 0.094   1.00 17.72  ? 228 LYS   A CA  1 
ATOM   1929 C  C   . LYS   A 1 227 ? 15.809  -9.360  -0.188  1.00 16.17  ? 228 LYS   A C   1 
ATOM   1930 O  O   . LYS   A 1 227 ? 16.439  -9.162  -1.234  1.00 18.23  ? 228 LYS   A O   1 
ATOM   1931 C  CB  . LYS   A 1 227 ? 14.139  -11.020 -0.912  1.00 19.44  ? 228 LYS   A CB  1 
ATOM   1932 C  CG  . LYS   A 1 227 ? 13.565  -12.400 -0.796  1.00 22.79  ? 228 LYS   A CG  1 
ATOM   1933 C  CD  . LYS   A 1 227 ? 12.527  -12.630 -1.861  1.00 29.86  ? 228 LYS   A CD  1 
ATOM   1934 C  CE  . LYS   A 1 227 ? 13.128  -12.756 -3.245  1.00 10.00  ? 228 LYS   A CE  1 
ATOM   1935 N  NZ  . LYS   A 1 227 ? 13.929  -13.995 -3.385  1.00 10.00  ? 228 LYS   A NZ  1 
ATOM   1936 N  N   . LEU   A 1 228 ? 15.638  -8.433  0.752   1.00 16.16  ? 229 LEU   A N   1 
ATOM   1937 C  CA  . LEU   A 1 228 ? 16.254  -7.126  0.633   1.00 15.55  ? 229 LEU   A CA  1 
ATOM   1938 C  C   . LEU   A 1 228 ? 17.759  -7.278  0.722   1.00 16.45  ? 229 LEU   A C   1 
ATOM   1939 O  O   . LEU   A 1 228 ? 18.280  -8.304  1.143   1.00 15.61  ? 229 LEU   A O   1 
ATOM   1940 C  CB  . LEU   A 1 228 ? 15.730  -6.188  1.721   1.00 15.50  ? 229 LEU   A CB  1 
ATOM   1941 C  CG  . LEU   A 1 228 ? 14.304  -5.698  1.517   1.00 16.19  ? 229 LEU   A CG  1 
ATOM   1942 C  CD1 . LEU   A 1 228 ? 13.808  -5.075  2.804   1.00 16.84  ? 229 LEU   A CD1 1 
ATOM   1943 C  CD2 . LEU   A 1 228 ? 14.251  -4.671  0.381   1.00 18.88  ? 229 LEU   A CD2 1 
ATOM   1944 N  N   . ASN   A 1 229 ? 18.471  -6.214  0.364   1.00 16.24  ? 230 ASN   A N   1 
ATOM   1945 C  CA  . ASN   A 1 229 ? 19.925  -6.237  0.331   1.00 16.20  ? 230 ASN   A CA  1 
ATOM   1946 C  C   . ASN   A 1 229 ? 20.467  -5.077  1.170   1.00 15.70  ? 230 ASN   A C   1 
ATOM   1947 O  O   . ASN   A 1 229 ? 19.986  -3.927  1.092   1.00 16.88  ? 230 ASN   A O   1 
ATOM   1948 C  CB  . ASN   A 1 229 ? 20.499  -6.030  -1.073  1.00 17.76  ? 230 ASN   A CB  1 
ATOM   1949 C  CG  . ASN   A 1 229 ? 20.398  -7.210  -2.011  1.00 19.22  ? 230 ASN   A CG  1 
ATOM   1950 O  OD1 . ASN   A 1 229 ? 20.855  -7.083  -3.140  1.00 22.91  ? 230 ASN   A OD1 1 
ATOM   1951 N  ND2 . ASN   A 1 229 ? 19.789  -8.330  -1.615  1.00 20.70  ? 230 ASN   A ND2 1 
ATOM   1952 N  N   . PHE   A 1 230 ? 21.543  -5.404  1.911   1.00 16.48  ? 231 PHE   A N   1 
ATOM   1953 C  CA  . PHE   A 1 230 ? 22.279  -4.336  2.593   1.00 16.43  ? 231 PHE   A CA  1 
ATOM   1954 C  C   . PHE   A 1 230 ? 23.174  -3.531  1.650   1.00 17.78  ? 231 PHE   A C   1 
ATOM   1955 O  O   . PHE   A 1 230 ? 23.450  -2.351  1.904   1.00 18.47  ? 231 PHE   A O   1 
ATOM   1956 C  CB  . PHE   A 1 230 ? 23.264  -4.944  3.589   1.00 16.99  ? 231 PHE   A CB  1 
ATOM   1957 C  CG  . PHE   A 1 230 ? 22.731  -5.531  4.876   1.00 16.04  ? 231 PHE   A CG  1 
ATOM   1958 C  CD1 . PHE   A 1 230 ? 21.994  -4.777  5.785   1.00 16.89  ? 231 PHE   A CD1 1 
ATOM   1959 C  CD2 . PHE   A 1 230 ? 23.086  -6.817  5.264   1.00 17.30  ? 231 PHE   A CD2 1 
ATOM   1960 C  CE1 . PHE   A 1 230 ? 21.549  -5.300  6.991   1.00 17.77  ? 231 PHE   A CE1 1 
ATOM   1961 C  CE2 . PHE   A 1 230 ? 22.659  -7.354  6.469   1.00 17.50  ? 231 PHE   A CE2 1 
ATOM   1962 C  CZ  . PHE   A 1 230 ? 21.926  -6.584  7.348   1.00 16.35  ? 231 PHE   A CZ  1 
ATOM   1963 N  N   . ASN   A 1 231 ? 23.659  -4.183  0.595   1.00 17.46  ? 232 ASN   A N   1 
ATOM   1964 C  CA  . ASN   A 1 231 ? 24.509  -3.570  -0.423  1.00 17.69  ? 232 ASN   A CA  1 
ATOM   1965 C  C   . ASN   A 1 231 ? 23.728  -2.639  -1.334  1.00 16.71  ? 232 ASN   A C   1 
ATOM   1966 O  O   . ASN   A 1 231 ? 22.520  -2.701  -1.497  1.00 18.59  ? 232 ASN   A O   1 
ATOM   1967 C  CB  . ASN   A 1 231 ? 25.161  -4.637  -1.288  1.00 20.59  ? 232 ASN   A CB  1 
ATOM   1968 C  CG  . ASN   A 1 231 ? 24.097  -5.533  -1.874  1.00 19.38  ? 232 ASN   A CG  1 
ATOM   1969 O  OD1 . ASN   A 1 231 ? 23.593  -6.419  -1.183  1.00 20.82  ? 232 ASN   A OD1 1 
ATOM   1970 N  ND2 . ASN   A 1 231 ? 23.793  -5.356  -3.161  1.00 21.32  ? 232 ASN   A ND2 1 
ATOM   1971 N  N   . GLY   A 1 232 ? 24.518  -1.755  -1.986  1.00 19.14  ? 233 GLY   A N   1 
ATOM   1972 C  CA  . GLY   A 1 232 ? 23.986  -0.930  -3.060  1.00 19.25  ? 233 GLY   A CA  1 
ATOM   1973 C  C   . GLY   A 1 232 ? 23.964  -1.683  -4.383  1.00 18.18  ? 233 GLY   A C   1 
ATOM   1974 O  O   . GLY   A 1 232 ? 24.579  -2.750  -4.492  1.00 21.53  ? 233 GLY   A O   1 
ATOM   1975 N  N   . GLU   A 1 233 ? 23.192  -1.153  -5.344  1.00 18.87  ? 234 GLU   A N   1 
ATOM   1976 C  CA  . GLU   A 1 233 ? 23.132  -1.724  -6.685  1.00 18.08  ? 234 GLU   A CA  1 
ATOM   1977 C  C   . GLU   A 1 233 ? 24.549  -1.795  -7.267  1.00 20.30  ? 234 GLU   A C   1 
ATOM   1978 O  O   . GLU   A 1 233 ? 25.388  -0.909  -7.090  1.00 21.92  ? 234 GLU   A O   1 
ATOM   1979 C  CB  . GLU   A 1 233 ? 22.201  -0.829  -7.520  1.00 19.34  ? 234 GLU   A CB  1 
ATOM   1980 C  CG  . GLU   A 1 233 ? 21.894  -1.326  -8.920  1.00 21.62  ? 234 GLU   A CG  1 
ATOM   1981 C  CD  . GLU   A 1 233 ? 21.062  -0.369  -9.747  1.00 29.01  ? 234 GLU   A CD  1 
ATOM   1982 O  OE1 . GLU   A 1 233 ? 20.785  0.786   -9.283  1.00 27.12  ? 234 GLU   A OE1 1 
ATOM   1983 O  OE2 . GLU   A 1 233 ? 20.710  -0.767  -10.864 1.00 32.63  ? 234 GLU   A OE2 1 
ATOM   1984 N  N   . GLY   A 1 234 ? 24.822  -2.914  -7.926  1.00 24.69  ? 235 GLY   A N   1 
ATOM   1985 C  CA  . GLY   A 1 234 ? 26.108  -3.075  -8.588  1.00 26.47  ? 235 GLY   A CA  1 
ATOM   1986 C  C   . GLY   A 1 234 ? 27.200  -3.546  -7.630  1.00 27.82  ? 235 GLY   A C   1 
ATOM   1987 O  O   . GLY   A 1 234 ? 28.368  -3.678  -8.006  1.00 35.67  ? 235 GLY   A O   1 
ATOM   1988 N  N   . GLU   A 1 235 ? 26.803  -3.866  -6.395  1.00 25.31  ? 236 GLU   A N   1 
ATOM   1989 C  CA  . GLU   A 1 235 ? 27.734  -4.454  -5.453  1.00 23.97  ? 236 GLU   A CA  1 
ATOM   1990 C  C   . GLU   A 1 235 ? 27.317  -5.898  -5.182  1.00 27.47  ? 236 GLU   A C   1 
ATOM   1991 O  O   . GLU   A 1 235 ? 26.170  -6.302  -5.423  1.00 29.62  ? 236 GLU   A O   1 
ATOM   1992 C  CB  . GLU   A 1 235 ? 27.684  -3.703  -4.115  1.00 26.24  ? 236 GLU   A CB  1 
ATOM   1993 C  CG  . GLU   A 1 235 ? 28.054  -2.234  -4.244  1.00 30.58  ? 236 GLU   A CG  1 
ATOM   1994 C  CD  . GLU   A 1 235 ? 27.878  -1.320  -3.036  1.00 42.28  ? 236 GLU   A CD  1 
ATOM   1995 O  OE1 . GLU   A 1 235 ? 27.279  -1.760  -1.993  1.00 42.27  ? 236 GLU   A OE1 1 
ATOM   1996 O  OE2 . GLU   A 1 235 ? 28.345  -0.160  -3.134  1.00 58.06  ? 236 GLU   A OE2 1 
ATOM   1997 N  N   . PRO   A 1 236 ? 28.210  -6.707  -4.591  1.00 26.26  ? 237 PRO   A N   1 
ATOM   1998 C  CA  . PRO   A 1 236 ? 27.909  -8.107  -4.334  1.00 28.76  ? 237 PRO   A CA  1 
ATOM   1999 C  C   . PRO   A 1 236 ? 26.742  -8.186  -3.355  1.00 23.88  ? 237 PRO   A C   1 
ATOM   2000 O  O   . PRO   A 1 236 ? 26.648  -7.405  -2.403  1.00 23.57  ? 237 PRO   A O   1 
ATOM   2001 C  CB  . PRO   A 1 236 ? 29.202  -8.652  -3.717  1.00 31.99  ? 237 PRO   A CB  1 
ATOM   2002 C  CG  . PRO   A 1 236 ? 30.276  -7.771  -4.302  1.00 35.33  ? 237 PRO   A CG  1 
ATOM   2003 C  CD  . PRO   A 1 236 ? 29.628  -6.402  -4.297  1.00 34.12  ? 237 PRO   A CD  1 
ATOM   2004 N  N   . GLU   A 1 237 ? 25.910  -9.208  -3.543  1.00 25.93  ? 238 GLU   A N   1 
ATOM   2005 C  CA  . GLU   A 1 237 ? 24.701  -9.291  -2.740  1.00 23.11  ? 238 GLU   A CA  1 
ATOM   2006 C  C   . GLU   A 1 237 ? 24.998  -9.730  -1.308  1.00 20.20  ? 238 GLU   A C   1 
ATOM   2007 O  O   . GLU   A 1 237 ? 25.625  -10.748 -1.063  1.00 20.74  ? 238 GLU   A O   1 
ATOM   2008 C  CB  . GLU   A 1 237 ? 23.736  -10.306 -3.344  1.00 24.25  ? 238 GLU   A CB  1 
ATOM   2009 C  CG  . GLU   A 1 237 ? 22.379  -10.221 -2.673  1.00 28.60  ? 238 GLU   A CG  1 
ATOM   2010 C  CD  . GLU   A 1 237 ? 21.306  -10.985 -3.424  1.00 30.68  ? 238 GLU   A CD  1 
ATOM   2011 O  OE1 . GLU   A 1 237 ? 21.664  -11.969 -4.109  1.00 46.77  ? 238 GLU   A OE1 1 
ATOM   2012 O  OE2 . GLU   A 1 237 ? 20.110  -10.583 -3.360  1.00 26.38  ? 238 GLU   A OE2 1 
ATOM   2013 N  N   A GLU   A 1 238 ? 24.520  -8.996  -0.317  0.50 19.90  ? 239 GLU   A N   1 
ATOM   2014 N  N   B GLU   A 1 238 ? 24.424  -8.944  -0.389  0.50 16.50  ? 239 GLU   A N   1 
ATOM   2015 C  CA  A GLU   A 1 238 ? 24.570  -9.477  1.053   0.50 20.88  ? 239 GLU   A CA  1 
ATOM   2016 C  CA  B GLU   A 1 238 ? 24.401  -9.141  1.051   0.50 15.48  ? 239 GLU   A CA  1 
ATOM   2017 C  C   A GLU   A 1 238 ? 23.173  -9.238  1.610   0.50 17.99  ? 239 GLU   A C   1 
ATOM   2018 C  C   B GLU   A 1 238 ? 22.935  -9.137  1.460   0.50 14.28  ? 239 GLU   A C   1 
ATOM   2019 O  O   A GLU   A 1 238 ? 22.776  -8.098  1.798   0.50 18.82  ? 239 GLU   A O   1 
ATOM   2020 O  O   B GLU   A 1 238 ? 22.272  -8.091  1.428   0.50 16.07  ? 239 GLU   A O   1 
ATOM   2021 C  CB  A GLU   A 1 238 ? 25.661  -8.766  1.860   0.50 21.68  ? 239 GLU   A CB  1 
ATOM   2022 C  CB  B GLU   A 1 238 ? 25.159  -8.046  1.807   0.50 15.44  ? 239 GLU   A CB  1 
ATOM   2023 C  CG  A GLU   A 1 238 ? 25.873  -9.263  3.245   0.50 10.00  ? 239 GLU   A CG  1 
ATOM   2024 C  CG  B GLU   A 1 238 ? 26.624  -7.955  1.437   0.50 18.33  ? 239 GLU   A CG  1 
ATOM   2025 C  CD  A GLU   A 1 238 ? 26.296  -10.721 3.283   0.50 10.00  ? 239 GLU   A CD  1 
ATOM   2026 C  CD  B GLU   A 1 238 ? 27.453  -6.886  2.113   0.50 10.00  ? 239 GLU   A CD  1 
ATOM   2027 O  OE1 A GLU   A 1 238 ? 26.494  -11.304 2.199   0.50 10.00  ? 239 GLU   A OE1 1 
ATOM   2028 O  OE1 B GLU   A 1 238 ? 26.847  -6.026  2.774   0.50 10.00  ? 239 GLU   A OE1 1 
ATOM   2029 O  OE2 A GLU   A 1 238 ? 26.425  -11.269 4.395   0.50 10.00  ? 239 GLU   A OE2 1 
ATOM   2030 O  OE2 B GLU   A 1 238 ? 28.690  -6.936  2.023   0.50 10.00  ? 239 GLU   A OE2 1 
ATOM   2031 N  N   . LEU   A 1 239 ? 22.426  -10.324 1.851   1.00 17.55  ? 240 LEU   A N   1 
ATOM   2032 C  CA  . LEU   A 1 239 ? 21.020  -10.296 2.198   1.00 16.19  ? 240 LEU   A CA  1 
ATOM   2033 C  C   . LEU   A 1 239 ? 20.817  -9.507  3.485   1.00 14.61  ? 240 LEU   A C   1 
ATOM   2034 O  O   . LEU   A 1 239 ? 21.572  -9.666  4.453   1.00 16.09  ? 240 LEU   A O   1 
ATOM   2035 C  CB  . LEU   A 1 239 ? 20.481  -11.707 2.389   1.00 17.46  ? 240 LEU   A CB  1 
ATOM   2036 C  CG  . LEU   A 1 239 ? 20.437  -12.539 1.116   1.00 18.13  ? 240 LEU   A CG  1 
ATOM   2037 C  CD1 . LEU   A 1 239 ? 19.885  -13.904 1.432   1.00 24.39  ? 240 LEU   A CD1 1 
ATOM   2038 C  CD2 . LEU   A 1 239 ? 19.595  -11.865 0.039   1.00 18.93  ? 240 LEU   A CD2 1 
ATOM   2039 N  N   . MET   A 1 240 ? 19.788  -8.657  3.484   1.00 14.88  ? 241 MET   A N   1 
ATOM   2040 C  CA  . MET   A 1 240 ? 19.417  -7.869  4.652   1.00 14.95  ? 241 MET   A CA  1 
ATOM   2041 C  C   . MET   A 1 240 ? 18.654  -8.769  5.627   1.00 13.87  ? 241 MET   A C   1 
ATOM   2042 O  O   . MET   A 1 240 ? 17.445  -8.954  5.517   1.00 14.49  ? 241 MET   A O   1 
ATOM   2043 C  CB  . MET   A 1 240 ? 18.545  -6.691  4.204   1.00 15.57  ? 241 MET   A CB  1 
ATOM   2044 C  CG  . MET   A 1 240 ? 18.278  -5.686  5.370   1.00 15.85  ? 241 MET   A CG  1 
ATOM   2045 S  SD  . MET   A 1 240 ? 17.289  -4.308  4.820   1.00 15.90  ? 241 MET   A SD  1 
ATOM   2046 C  CE  . MET   A 1 240 ? 18.576  -3.278  4.097   1.00 17.42  ? 241 MET   A CE  1 
ATOM   2047 N  N   . VAL   A 1 241 ? 19.420  -9.358  6.561   1.00 13.78  ? 242 VAL   A N   1 
ATOM   2048 C  CA  . VAL   A 1 241 ? 18.897  -10.227 7.625   1.00 13.45  ? 242 VAL   A CA  1 
ATOM   2049 C  C   . VAL   A 1 241 ? 19.713  -9.970  8.889   1.00 13.46  ? 242 VAL   A C   1 
ATOM   2050 O  O   . VAL   A 1 241 ? 20.874  -9.564  8.825   1.00 14.00  ? 242 VAL   A O   1 
ATOM   2051 C  CB  . VAL   A 1 241 ? 18.978  -11.733 7.261   1.00 14.15  ? 242 VAL   A CB  1 
ATOM   2052 C  CG1 . VAL   A 1 241 ? 18.046  -12.064 6.091   1.00 15.57  ? 242 VAL   A CG1 1 
ATOM   2053 C  CG2 . VAL   A 1 241 ? 20.411  -12.190 7.003   1.00 15.05  ? 242 VAL   A CG2 1 
ATOM   2054 N  N   . ASP   A 1 242 ? 19.097  -10.256 10.041  1.00 12.88  ? 243 ASP   A N   1 
ATOM   2055 C  CA  . ASP   A 1 242 ? 19.791  -10.127 11.306  1.00 12.54  ? 243 ASP   A CA  1 
ATOM   2056 C  C   . ASP   A 1 242 ? 20.293  -8.705  11.534  1.00 12.25  ? 243 ASP   A C   1 
ATOM   2057 O  O   . ASP   A 1 242 ? 21.434  -8.491  11.965  1.00 14.06  ? 243 ASP   A O   1 
ATOM   2058 C  CB  . ASP   A 1 242 ? 20.864  -11.201 11.510  1.00 12.93  ? 243 ASP   A CB  1 
ATOM   2059 C  CG  . ASP   A 1 242 ? 20.271  -12.586 11.644  1.00 13.46  ? 243 ASP   A CG  1 
ATOM   2060 O  OD1 . ASP   A 1 242 ? 19.211  -12.727 12.312  1.00 13.53  ? 243 ASP   A OD1 1 
ATOM   2061 O  OD2 . ASP   A 1 242 ? 20.828  -13.528 11.044  1.00 15.51  ? 243 ASP   A OD2 1 
ATOM   2062 N  N   . ASN   A 1 243 ? 19.378  -7.757  11.330  1.00 11.77  ? 244 ASN   A N   1 
ATOM   2063 C  CA  . ASN   A 1 243 ? 19.660  -6.333  11.542  1.00 11.67  ? 244 ASN   A CA  1 
ATOM   2064 C  C   . ASN   A 1 243 ? 19.139  -5.866  12.901  1.00 11.44  ? 244 ASN   A C   1 
ATOM   2065 O  O   . ASN   A 1 243 ? 18.542  -4.783  13.009  1.00 12.61  ? 244 ASN   A O   1 
ATOM   2066 C  CB  . ASN   A 1 243 ? 19.120  -5.500  10.388  1.00 12.53  ? 244 ASN   A CB  1 
ATOM   2067 C  CG  . ASN   A 1 243 ? 17.637  -5.674  10.163  1.00 12.13  ? 244 ASN   A CG  1 
ATOM   2068 O  OD1 . ASN   A 1 243 ? 17.000  -6.469  10.847  1.00 13.25  ? 244 ASN   A OD1 1 
ATOM   2069 N  ND2 . ASN   A 1 243 ? 17.100  -4.961  9.188   1.00 15.63  ? 244 ASN   A ND2 1 
ATOM   2070 N  N   . TRP   A 1 244 ? 19.394  -6.675  13.938  1.00 11.65  ? 245 TRP   A N   1 
ATOM   2071 C  CA  . TRP   A 1 244 ? 18.960  -6.407  15.297  1.00 11.16  ? 245 TRP   A CA  1 
ATOM   2072 C  C   . TRP   A 1 244 ? 20.162  -6.304  16.220  1.00 11.56  ? 245 TRP   A C   1 
ATOM   2073 O  O   . TRP   A 1 244 ? 21.151  -7.031  16.101  1.00 12.68  ? 245 TRP   A O   1 
ATOM   2074 C  CB  . TRP   A 1 244 ? 17.978  -7.482  15.787  1.00 11.10  ? 245 TRP   A CB  1 
ATOM   2075 C  CG  . TRP   A 1 244 ? 18.444  -8.904  15.615  1.00 11.34  ? 245 TRP   A CG  1 
ATOM   2076 C  CD1 . TRP   A 1 244 ? 18.350  -9.645  14.460  1.00 11.66  ? 245 TRP   A CD1 1 
ATOM   2077 C  CD2 . TRP   A 1 244 ? 19.007  -9.791  16.600  1.00 11.39  ? 245 TRP   A CD2 1 
ATOM   2078 N  NE1 . TRP   A 1 244 ? 18.837  -10.915 14.636  1.00 11.75  ? 245 TRP   A NE1 1 
ATOM   2079 C  CE2 . TRP   A 1 244 ? 19.245  -11.030 15.946  1.00 11.95  ? 245 TRP   A CE2 1 
ATOM   2080 C  CE3 . TRP   A 1 244 ? 19.271  -9.651  17.966  1.00 12.55  ? 245 TRP   A CE3 1 
ATOM   2081 C  CZ2 . TRP   A 1 244 ? 19.790  -12.115 16.634  1.00 12.97  ? 245 TRP   A CZ2 1 
ATOM   2082 C  CZ3 . TRP   A 1 244 ? 19.794  -10.741 18.633  1.00 14.05  ? 245 TRP   A CZ3 1 
ATOM   2083 C  CH2 . TRP   A 1 244 ? 20.039  -11.965 17.973  1.00 13.57  ? 245 TRP   A CH2 1 
ATOM   2084 N  N   . ARG   A 1 245 ? 20.027  -5.403  17.195  1.00 11.02  ? 246 ARG   A N   1 
ATOM   2085 C  CA  . ARG   A 1 245 ? 20.957  -5.318  18.317  1.00 11.16  ? 246 ARG   A CA  1 
ATOM   2086 C  C   . ARG   A 1 245 ? 20.468  -6.244  19.420  1.00 11.45  ? 246 ARG   A C   1 
ATOM   2087 O  O   . ARG   A 1 245 ? 19.264  -6.229  19.749  1.00 12.35  ? 246 ARG   A O   1 
ATOM   2088 C  CB  . ARG   A 1 245 ? 21.021  -3.873  18.835  1.00 11.45  ? 246 ARG   A CB  1 
ATOM   2089 C  CG  . ARG   A 1 245 ? 22.140  -3.621  19.829  1.00 11.48  ? 246 ARG   A CG  1 
ATOM   2090 C  CD  . ARG   A 1 245 ? 22.036  -2.303  20.516  1.00 11.59  ? 246 ARG   A CD  1 
ATOM   2091 N  NE  . ARG   A 1 245 ? 23.290  -1.990  21.199  1.00 12.81  ? 246 ARG   A NE  1 
ATOM   2092 C  CZ  . ARG   A 1 245 ? 23.497  -0.947  22.012  1.00 12.28  ? 246 ARG   A CZ  1 
ATOM   2093 N  NH1 . ARG   A 1 245 ? 22.497  -0.163  22.399  1.00 13.35  ? 246 ARG   A NH1 1 
ATOM   2094 N  NH2 . ARG   A 1 245 ? 24.744  -0.714  22.430  1.00 13.85  ? 246 ARG   A NH2 1 
ATOM   2095 N  N   . PRO   A 1 246 ? 21.352  -7.047  20.055  1.00 12.40  ? 247 PRO   A N   1 
ATOM   2096 C  CA  . PRO   A 1 246 ? 20.914  -7.869  21.177  1.00 12.53  ? 247 PRO   A CA  1 
ATOM   2097 C  C   . PRO   A 1 246 ? 20.585  -7.037  22.420  1.00 11.96  ? 247 PRO   A C   1 
ATOM   2098 O  O   . PRO   A 1 246 ? 20.938  -5.853  22.560  1.00 12.38  ? 247 PRO   A O   1 
ATOM   2099 C  CB  . PRO   A 1 246 ? 22.150  -8.733  21.485  1.00 16.48  ? 247 PRO   A CB  1 
ATOM   2100 C  CG  . PRO   A 1 246 ? 23.024  -8.624  20.279  1.00 19.63  ? 247 PRO   A CG  1 
ATOM   2101 C  CD  . PRO   A 1 246 ? 22.784  -7.236  19.730  1.00 14.69  ? 247 PRO   A CD  1 
ATOM   2102 N  N   . ALA   A 1 247 ? 19.927  -7.691  23.379  1.00 12.66  ? 248 ALA   A N   1 
ATOM   2103 C  CA  . ALA   A 1 247 ? 19.595  -7.085  24.660  1.00 12.57  ? 248 ALA   A CA  1 
ATOM   2104 C  C   . ALA   A 1 247 ? 20.854  -6.570  25.358  1.00 12.62  ? 248 ALA   A C   1 
ATOM   2105 O  O   . ALA   A 1 247 ? 21.892  -7.249  25.392  1.00 14.37  ? 248 ALA   A O   1 
ATOM   2106 C  CB  . ALA   A 1 247 ? 18.856  -8.103  25.535  1.00 14.78  ? 248 ALA   A CB  1 
ATOM   2107 N  N   . GLN   A 1 248 ? 20.697  -5.368  25.947  1.00 12.46  ? 249 GLN   A N   1 
ATOM   2108 C  CA  . GLN   A 1 248 ? 21.744  -4.684  26.684  1.00 13.01  ? 249 GLN   A CA  1 
ATOM   2109 C  C   . GLN   A 1 248 ? 21.439  -4.698  28.177  1.00 13.16  ? 249 GLN   A C   1 
ATOM   2110 O  O   . GLN   A 1 248 ? 20.293  -4.902  28.610  1.00 14.07  ? 249 GLN   A O   1 
ATOM   2111 C  CB  . GLN   A 1 248 ? 21.813  -3.232  26.182  1.00 13.68  ? 249 GLN   A CB  1 
ATOM   2112 C  CG  . GLN   A 1 248 ? 22.097  -3.168  24.686  1.00 13.72  ? 249 GLN   A CG  1 
ATOM   2113 C  CD  . GLN   A 1 248 ? 23.425  -3.823  24.342  1.00 14.40  ? 249 GLN   A CD  1 
ATOM   2114 O  OE1 . GLN   A 1 248 ? 24.470  -3.485  24.921  1.00 17.35  ? 249 GLN   A OE1 1 
ATOM   2115 N  NE2 . GLN   A 1 248 ? 23.410  -4.744  23.388  1.00 15.35  ? 249 GLN   A NE2 1 
ATOM   2116 N  N   . PRO   A 1 249 ? 22.445  -4.410  29.021  1.00 14.91  ? 250 PRO   A N   1 
ATOM   2117 C  CA  . PRO   A 1 249 ? 22.250  -4.449  30.462  1.00 16.73  ? 250 PRO   A CA  1 
ATOM   2118 C  C   . PRO   A 1 249 ? 21.175  -3.449  30.890  1.00 14.76  ? 250 PRO   A C   1 
ATOM   2119 O  O   . PRO   A 1 249 ? 21.182  -2.271  30.537  1.00 15.25  ? 250 PRO   A O   1 
ATOM   2120 C  CB  . PRO   A 1 249 ? 23.646  -4.042  31.002  1.00 20.88  ? 250 PRO   A CB  1 
ATOM   2121 C  CG  . PRO   A 1 249 ? 24.596  -4.514  29.945  1.00 22.04  ? 250 PRO   A CG  1 
ATOM   2122 C  CD  . PRO   A 1 249 ? 23.866  -4.165  28.659  1.00 18.97  ? 250 PRO   A CD  1 
ATOM   2123 N  N   . LEU   A 1 250 ? 20.298  -3.910  31.791  1.00 15.30  ? 251 LEU   A N   1 
ATOM   2124 C  CA  . LEU   A 1 250 ? 19.235  -3.047  32.293  1.00 14.74  ? 251 LEU   A CA  1 
ATOM   2125 C  C   . LEU   A 1 250 ? 19.772  -1.958  33.219  1.00 13.99  ? 251 LEU   A C   1 
ATOM   2126 O  O   . LEU   A 1 250 ? 19.199  -0.856  33.281  1.00 14.06  ? 251 LEU   A O   1 
ATOM   2127 C  CB  . LEU   A 1 250 ? 18.205  -3.921  33.023  1.00 16.69  ? 251 LEU   A CB  1 
ATOM   2128 C  CG  . LEU   A 1 250 ? 16.906  -3.219  33.435  1.00 16.75  ? 251 LEU   A CG  1 
ATOM   2129 C  CD1 . LEU   A 1 250 ? 16.149  -2.660  32.207  1.00 16.82  ? 251 LEU   A CD1 1 
ATOM   2130 C  CD2 . LEU   A 1 250 ? 16.008  -4.208  34.202  1.00 21.33  ? 251 LEU   A CD2 1 
ATOM   2131 N  N   . LYS   A 1 251 ? 20.845  -2.258  33.958  1.00 15.48  ? 252 LYS   A N   1 
ATOM   2132 C  CA  . LYS   A 1 251 ? 21.467  -1.263  34.847  1.00 16.54  ? 252 LYS   A CA  1 
ATOM   2133 C  C   . LYS   A 1 251 ? 20.422  -0.708  35.813  1.00 16.38  ? 252 LYS   A C   1 
ATOM   2134 O  O   . LYS   A 1 251 ? 19.614  -1.488  36.332  1.00 18.50  ? 252 LYS   A O   1 
ATOM   2135 C  CB  . LYS   A 1 251 ? 22.232  -0.223  34.014  1.00 18.71  ? 252 LYS   A CB  1 
ATOM   2136 C  CG  . LYS   A 1 251 ? 23.374  -0.876  33.249  1.00 22.69  ? 252 LYS   A CG  1 
ATOM   2137 C  CD  . LYS   A 1 251 ? 24.360  0.071   32.616  1.00 22.95  ? 252 LYS   A CD  1 
ATOM   2138 C  CE  . LYS   A 1 251 ? 25.526  -0.665  32.013  1.00 28.85  ? 252 LYS   A CE  1 
ATOM   2139 N  NZ  . LYS   A 1 251 ? 26.379  0.285   31.260  1.00 28.00  ? 252 LYS   A NZ  1 
ATOM   2140 N  N   . ASN   A 1 252 ? 20.432  0.599   36.040  1.00 16.56  ? 253 ASN   A N   1 
ATOM   2141 C  CA  . ASN   A 1 252 ? 19.595  1.109   37.086  1.00 23.14  ? 253 ASN   A CA  1 
ATOM   2142 C  C   . ASN   A 1 252 ? 18.280  1.569   36.463  1.00 23.41  ? 253 ASN   A C   1 
ATOM   2143 O  O   . ASN   A 1 252 ? 18.046  2.812   36.444  1.00 27.58  ? 253 ASN   A O   1 
ATOM   2144 C  CB  . ASN   A 1 252 ? 20.345  2.229   37.803  1.00 28.07  ? 253 ASN   A CB  1 
ATOM   2145 C  CG  . ASN   A 1 252 ? 19.600  2.743   39.020  1.00 31.97  ? 253 ASN   A CG  1 
ATOM   2146 O  OD1 . ASN   A 1 252 ? 19.067  1.967   39.812  1.00 47.25  ? 253 ASN   A OD1 1 
ATOM   2147 N  ND2 . ASN   A 1 252 ? 19.518  4.053   39.154  1.00 32.41  ? 253 ASN   A ND2 1 
ATOM   2148 N  N   . ARG   A 1 253 ? 17.498  0.573   35.896  1.00 19.39  ? 254 ARG   A N   1 
ATOM   2149 C  CA  . ARG   A 1 253 ? 16.184  0.856   35.350  1.00 15.21  ? 254 ARG   A CA  1 
ATOM   2150 C  C   . ARG   A 1 253 ? 15.128  -0.122  35.832  1.00 16.66  ? 254 ARG   A C   1 
ATOM   2151 O  O   . ARG   A 1 253 ? 15.421  -1.294  36.027  1.00 21.63  ? 254 ARG   A O   1 
ATOM   2152 C  CB  . ARG   A 1 253 ? 16.229  0.900   33.841  1.00 13.77  ? 254 ARG   A CB  1 
ATOM   2153 C  CG  . ARG   A 1 253 ? 17.110  2.034   33.330  1.00 14.10  ? 254 ARG   A CG  1 
ATOM   2154 C  CD  . ARG   A 1 253 ? 17.267  2.050   31.826  1.00 13.15  ? 254 ARG   A CD  1 
ATOM   2155 N  NE  . ARG   A 1 253 ? 18.082  0.914   31.375  1.00 12.74  ? 254 ARG   A NE  1 
ATOM   2156 C  CZ  . ARG   A 1 253 ? 18.316  0.642   30.096  1.00 11.59  ? 254 ARG   A CZ  1 
ATOM   2157 N  NH1 . ARG   A 1 253 ? 17.725  1.331   29.133  1.00 11.90  ? 254 ARG   A NH1 1 
ATOM   2158 N  NH2 . ARG   A 1 253 ? 19.147  -0.353  29.767  1.00 12.03  ? 254 ARG   A NH2 1 
ATOM   2159 N  N   . GLN   A 1 254 ? 13.900  0.385   35.887  1.00 16.51  ? 255 GLN   A N   1 
ATOM   2160 C  CA  A GLN   A 1 254 ? 12.703  -0.390  36.164  0.50 18.64  ? 255 GLN   A CA  1 
ATOM   2161 C  CA  B GLN   A 1 254 ? 12.712  -0.407  36.159  0.50 18.42  ? 255 GLN   A CA  1 
ATOM   2162 C  C   . GLN   A 1 254 ? 11.825  -0.366  34.917  1.00 15.71  ? 255 GLN   A C   1 
ATOM   2163 O  O   . GLN   A 1 254 ? 11.582  0.702   34.325  1.00 21.29  ? 255 GLN   A O   1 
ATOM   2164 C  CB  A GLN   A 1 254 ? 11.921  0.213   37.332  0.50 23.36  ? 255 GLN   A CB  1 
ATOM   2165 C  CB  B GLN   A 1 254 ? 11.968  0.121   37.389  0.50 19.50  ? 255 GLN   A CB  1 
ATOM   2166 C  CG  A GLN   A 1 254 ? 10.757  -0.669  37.759  0.50 28.92  ? 255 GLN   A CG  1 
ATOM   2167 C  CG  B GLN   A 1 254 ? 12.701  -0.130  38.703  0.50 18.91  ? 255 GLN   A CG  1 
ATOM   2168 C  CD  A GLN   A 1 254 ? 10.453  -0.645  39.237  0.50 37.60  ? 255 GLN   A CD  1 
ATOM   2169 C  CD  B GLN   A 1 254 ? 11.996  0.515   39.882  0.50 25.51  ? 255 GLN   A CD  1 
ATOM   2170 O  OE1 A GLN   A 1 254 ? 9.301   -0.776  39.649  0.50 35.57  ? 255 GLN   A OE1 1 
ATOM   2171 O  OE1 B GLN   A 1 254 ? 10.981  1.195   39.720  0.50 34.40  ? 255 GLN   A OE1 1 
ATOM   2172 N  NE2 A GLN   A 1 254 ? 11.486  -0.519  40.057  0.50 42.24  ? 255 GLN   A NE2 1 
ATOM   2173 N  NE2 B GLN   A 1 254 ? 12.515  0.318   41.088  0.50 23.67  ? 255 GLN   A NE2 1 
ATOM   2174 N  N   . ILE   A 1 255 ? 11.385  -1.548  34.495  1.00 13.95  ? 256 ILE   A N   1 
ATOM   2175 C  CA  . ILE   A 1 255 ? 10.378  -1.641  33.447  1.00 13.56  ? 256 ILE   A CA  1 
ATOM   2176 C  C   . ILE   A 1 255 ? 9.009   -1.674  34.137  1.00 14.03  ? 256 ILE   A C   1 
ATOM   2177 O  O   . ILE   A 1 255 ? 8.807   -2.440  35.087  1.00 15.59  ? 256 ILE   A O   1 
ATOM   2178 C  CB  . ILE   A 1 255 ? 10.600  -2.903  32.605  1.00 13.41  ? 256 ILE   A CB  1 
ATOM   2179 C  CG1 . ILE   A 1 255 ? 12.031  -2.902  32.032  1.00 14.82  ? 256 ILE   A CG1 1 
ATOM   2180 C  CG2 . ILE   A 1 255 ? 9.523   -3.005  31.535  1.00 14.97  ? 256 ILE   A CG2 1 
ATOM   2181 C  CD1 . ILE   A 1 255 ? 12.371  -4.139  31.249  1.00 16.68  ? 256 ILE   A CD1 1 
ATOM   2182 N  N   . LYS   A 1 256 ? 8.106   -0.821  33.652  1.00 13.19  ? 257 LYS   A N   1 
ATOM   2183 C  CA  . LYS   A 1 256 ? 6.761   -0.720  34.169  1.00 13.45  ? 257 LYS   A CA  1 
ATOM   2184 C  C   . LYS   A 1 256 ? 5.780   -1.356  33.205  1.00 13.57  ? 257 LYS   A C   1 
ATOM   2185 O  O   . LYS   A 1 256 ? 5.957   -1.255  32.007  1.00 15.35  ? 257 LYS   A O   1 
ATOM   2186 C  CB  . LYS   A 1 256 ? 6.429   0.741   34.462  1.00 15.66  ? 257 LYS   A CB  1 
ATOM   2187 C  CG  . LYS   A 1 256 ? 7.325   1.349   35.537  1.00 20.82  ? 257 LYS   A CG  1 
ATOM   2188 C  CD  . LYS   A 1 256 ? 6.932   2.734   35.941  1.00 27.90  ? 257 LYS   A CD  1 
ATOM   2189 C  CE  . LYS   A 1 256 ? 7.670   3.566   36.789  1.00 10.00  ? 257 LYS   A CE  1 
ATOM   2190 N  NZ  . LYS   A 1 256 ? 7.506   2.941   38.123  1.00 10.00  ? 257 LYS   A NZ  1 
ATOM   2191 N  N   . ALA   A 1 257 ? 4.740   -2.006  33.729  1.00 14.13  ? 258 ALA   A N   1 
ATOM   2192 C  CA  . ALA   A 1 257 ? 3.657   -2.605  32.957  1.00 14.69  ? 258 ALA   A CA  1 
ATOM   2193 C  C   . ALA   A 1 257 ? 2.379   -1.778  33.146  1.00 13.57  ? 258 ALA   A C   1 
ATOM   2194 O  O   . ALA   A 1 257 ? 2.043   -1.384  34.259  1.00 15.50  ? 258 ALA   A O   1 
ATOM   2195 C  CB  . ALA   A 1 257 ? 3.460   -4.065  33.347  1.00 16.09  ? 258 ALA   A CB  1 
ATOM   2196 N  N   . SER   A 1 258 ? 1.625   -1.611  32.058  1.00 14.08  ? 259 SER   A N   1 
ATOM   2197 C  CA  . SER   A 1 258 ? 0.343   -0.919  32.093  1.00 15.27  ? 259 SER   A CA  1 
ATOM   2198 C  C   . SER   A 1 258 ? -0.777  -1.862  32.504  1.00 15.48  ? 259 SER   A C   1 
ATOM   2199 O  O   . SER   A 1 258 ? -1.913  -1.402  32.624  1.00 20.36  ? 259 SER   A O   1 
ATOM   2200 C  CB  . SER   A 1 258 ? 0.016   -0.348  30.732  1.00 16.00  ? 259 SER   A CB  1 
ATOM   2201 O  OG  . SER   A 1 258 ? -0.398  -1.351  29.812  1.00 15.93  ? 259 SER   A OG  1 
ATOM   2202 N  N   . PHE   A 1 259 ? -0.468  -3.143  32.725  1.00 15.99  ? 260 PHE   A N   1 
ATOM   2203 C  CA  . PHE   A 1 259 ? -1.431  -4.217  32.906  1.00 18.38  ? 260 PHE   A CA  1 
ATOM   2204 C  C   . PHE   A 1 259 ? -0.898  -5.125  34.013  1.00 20.38  ? 260 PHE   A C   1 
ATOM   2205 O  O   . PHE   A 1 259 ? 0.291   -5.267  34.194  1.00 20.38  ? 260 PHE   A O   1 
ATOM   2206 C  CB  . PHE   A 1 259 ? -1.665  -4.925  31.569  1.00 19.22  ? 260 PHE   A CB  1 
ATOM   2207 C  CG  . PHE   A 1 259 ? -0.417  -5.622  31.081  1.00 17.54  ? 260 PHE   A CG  1 
ATOM   2208 C  CD1 . PHE   A 1 259 ? 0.567   -4.922  30.396  1.00 15.98  ? 260 PHE   A CD1 1 
ATOM   2209 C  CD2 . PHE   A 1 259 ? -0.182  -6.954  31.392  1.00 21.36  ? 260 PHE   A CD2 1 
ATOM   2210 C  CE1 . PHE   A 1 259 ? 1.765   -5.513  30.014  1.00 17.00  ? 260 PHE   A CE1 1 
ATOM   2211 C  CE2 . PHE   A 1 259 ? 0.995   -7.554  30.976  1.00 22.08  ? 260 PHE   A CE2 1 
ATOM   2212 C  CZ  . PHE   A 1 259 ? 1.975   -6.840  30.309  1.00 21.45  ? 260 PHE   A CZ  1 
HETATM 2213 ZN ZN  . ZN    B 2 .   ? 14.414  0.114   15.364  1.00 10.55  ? 301 ZN    A ZN  1 
HETATM 2214 S  S   . DMS   C 3 .   ? 22.410  -9.810  14.932  1.00 18.69  ? 302 DMS   A S   1 
HETATM 2215 O  O   . DMS   C 3 .   ? 23.466  -8.659  14.539  1.00 24.03  ? 302 DMS   A O   1 
HETATM 2216 C  C1  . DMS   C 3 .   ? 22.653  -9.792  16.639  1.00 17.64  ? 302 DMS   A C1  1 
HETATM 2217 C  C2  . DMS   C 3 .   ? 23.139  -11.235 14.540  1.00 19.74  ? 302 DMS   A C2  1 
HETATM 2218 C  C2  . A1IDL D 4 .   ? 15.475  3.915   15.740  1.00 11.85  ? 303 A1IDL A C2  1 
HETATM 2219 C  C3  . A1IDL D 4 .   ? 15.048  5.210   16.023  1.00 13.49  ? 303 A1IDL A C3  1 
HETATM 2220 C  C4  . A1IDL D 4 .   ? 15.199  6.240   15.133  1.00 14.17  ? 303 A1IDL A C4  1 
HETATM 2221 C  C5  . A1IDL D 4 .   ? 15.747  6.039   13.847  1.00 15.04  ? 303 A1IDL A C5  1 
HETATM 2222 C  C6  . A1IDL D 4 .   ? 16.221  4.745   13.518  1.00 14.39  ? 303 A1IDL A C6  1 
HETATM 2223 O  O9  . A1IDL D 4 .   ? 13.668  2.686   16.890  1.00 11.60  ? 303 A1IDL A O9  1 
HETATM 2224 C  C16 . A1IDL D 4 .   ? 16.326  6.641   11.244  1.00 26.47  ? 303 A1IDL A C16 1 
HETATM 2225 C  C17 . A1IDL D 4 .   ? 17.198  5.460   11.355  1.00 28.25  ? 303 A1IDL A C17 1 
HETATM 2226 C  C19 . A1IDL D 4 .   ? 17.225  2.234   11.378  1.00 20.56  ? 303 A1IDL A C19 1 
HETATM 2227 C  C21 . A1IDL D 4 .   ? 19.204  0.332   11.104  1.00 27.75  ? 303 A1IDL A C21 1 
HETATM 2228 C  C24 . A1IDL D 4 .   ? 16.867  0.865   11.454  1.00 18.62  ? 303 A1IDL A C24 1 
HETATM 2229 O  O26 . A1IDL D 4 .   ? 14.327  7.750   12.453  1.00 25.76  ? 303 A1IDL A O26 1 
HETATM 2230 S  S15 . A1IDL D 4 .   ? 15.704  7.358   12.712  1.00 20.82  ? 303 A1IDL A S15 1 
HETATM 2231 O  O25 . A1IDL D 4 .   ? 16.595  8.339   13.236  1.00 22.28  ? 303 A1IDL A O25 1 
HETATM 2232 F  F13 . A1IDL D 4 .   ? 14.775  7.474   15.434  1.00 16.48  ? 303 A1IDL A F13 1 
HETATM 2233 F  F12 . A1IDL D 4 .   ? 14.469  5.478   17.217  1.00 13.72  ? 303 A1IDL A F12 1 
HETATM 2234 S  S7  . A1IDL D 4 .   ? 15.102  2.648   16.887  1.00 11.21  ? 303 A1IDL A S7  1 
HETATM 2235 N  N10 . A1IDL D 4 .   ? 15.635  1.269   16.345  1.00 10.79  ? 303 A1IDL A N10 1 
HETATM 2236 O  O8  . A1IDL D 4 .   ? 15.776  3.015   18.107  1.00 11.59  ? 303 A1IDL A O8  1 
HETATM 2237 N  N14 . A1IDL D 4 .   ? 16.680  4.476   12.244  1.00 16.70  ? 303 A1IDL A N14 1 
HETATM 2238 C  C1  . A1IDL D 4 .   ? 16.059  3.755   14.473  1.00 12.85  ? 303 A1IDL A C1  1 
HETATM 2239 F  F11 . A1IDL D 4 .   ? 16.531  2.542   14.144  1.00 13.62  ? 303 A1IDL A F11 1 
HETATM 2240 C  C18 . A1IDL D 4 .   ? 16.218  3.309   11.491  1.00 21.33  ? 303 A1IDL A C18 1 
HETATM 2241 C  C20 . A1IDL D 4 .   ? 17.870  -0.077  11.293  1.00 24.78  ? 303 A1IDL A C20 1 
HETATM 2242 C  C22 . A1IDL D 4 .   ? 19.537  1.682   11.042  1.00 29.51  ? 303 A1IDL A C22 1 
HETATM 2243 C  C23 . A1IDL D 4 .   ? 18.548  2.646   11.183  1.00 24.37  ? 303 A1IDL A C23 1 
HETATM 2244 O  O   . HOH   E 5 .   ? 33.510  1.273   11.955  1.00 50.72  ? 401 HOH   A O   1 
HETATM 2245 O  O   . HOH   E 5 .   ? -4.548  -8.761  17.750  1.00 29.41  ? 402 HOH   A O   1 
HETATM 2246 O  O   . HOH   E 5 .   ? 3.301   21.036  6.160   1.00 16.31  ? 403 HOH   A O   1 
HETATM 2247 O  O   . HOH   E 5 .   ? 10.691  -4.024  38.280  1.00 26.86  ? 404 HOH   A O   1 
HETATM 2248 O  O   . HOH   E 5 .   ? 9.968   -13.292 34.108  1.00 29.62  ? 405 HOH   A O   1 
HETATM 2249 O  O   . HOH   E 5 .   ? 8.501   14.871  32.129  1.00 42.10  ? 406 HOH   A O   1 
HETATM 2250 O  O   . HOH   E 5 .   ? 0.098   -5.220  -1.847  1.00 42.65  ? 407 HOH   A O   1 
HETATM 2251 O  O   . HOH   E 5 .   ? 11.617  3.428   39.041  1.00 32.85  ? 408 HOH   A O   1 
HETATM 2252 O  O   . HOH   E 5 .   ? 19.860  -15.714 17.945  1.00 43.04  ? 409 HOH   A O   1 
HETATM 2253 O  O   . HOH   E 5 .   ? 23.733  -2.580  7.802   1.00 31.14  ? 410 HOH   A O   1 
HETATM 2254 O  O   . HOH   E 5 .   ? 27.257  -3.609  3.011   1.00 54.35  ? 411 HOH   A O   1 
HETATM 2255 O  O   . HOH   E 5 .   ? 14.138  7.750   6.012   1.00 28.66  ? 412 HOH   A O   1 
HETATM 2256 O  O   . HOH   E 5 .   ? 7.829   -20.558 11.543  1.00 33.70  ? 413 HOH   A O   1 
HETATM 2257 O  O   . HOH   E 5 .   ? 16.173  4.103   37.509  1.00 40.13  ? 414 HOH   A O   1 
HETATM 2258 O  O   . HOH   E 5 .   ? 5.670   -8.488  37.468  1.00 35.54  ? 415 HOH   A O   1 
HETATM 2259 O  O   . HOH   E 5 .   ? 4.628   7.272   -8.059  1.00 36.66  ? 416 HOH   A O   1 
HETATM 2260 O  O   . HOH   E 5 .   ? 12.393  -1.966  7.908   1.00 16.58  ? 417 HOH   A O   1 
HETATM 2261 O  O   . HOH   E 5 .   ? 6.967   -3.114  -6.417  1.00 41.29  ? 418 HOH   A O   1 
HETATM 2262 O  O   . HOH   E 5 .   ? 12.578  2.582   -6.571  1.00 37.75  ? 419 HOH   A O   1 
HETATM 2263 O  O   . HOH   E 5 .   ? 6.928   -6.820  -5.278  1.00 37.82  ? 420 HOH   A O   1 
HETATM 2264 O  O   . HOH   E 5 .   ? 32.315  -5.245  22.472  1.00 33.43  ? 421 HOH   A O   1 
HETATM 2265 O  O   . HOH   E 5 .   ? 25.756  0.904   -5.303  1.00 33.42  ? 422 HOH   A O   1 
HETATM 2266 O  O   . HOH   E 5 .   ? 8.534   20.232  29.132  1.00 36.85  ? 423 HOH   A O   1 
HETATM 2267 O  O   . HOH   E 5 .   ? 6.670   -14.702 28.974  1.00 29.94  ? 424 HOH   A O   1 
HETATM 2268 O  O   . HOH   E 5 .   ? -6.275  -3.615  27.958  1.00 49.63  ? 425 HOH   A O   1 
HETATM 2269 O  O   . HOH   E 5 .   ? 8.687   14.357  29.367  1.00 27.38  ? 426 HOH   A O   1 
HETATM 2270 O  O   . HOH   E 5 .   ? 31.403  -8.955  16.201  1.00 29.22  ? 427 HOH   A O   1 
HETATM 2271 O  O   . HOH   E 5 .   ? 14.264  -18.271 19.592  1.00 19.92  ? 428 HOH   A O   1 
HETATM 2272 O  O   . HOH   E 5 .   ? 1.685   -18.796 5.243   1.00 25.18  ? 429 HOH   A O   1 
HETATM 2273 O  O   . HOH   E 5 .   ? 18.001  -17.758 6.313   1.00 47.98  ? 430 HOH   A O   1 
HETATM 2274 O  O   . HOH   E 5 .   ? 11.946  7.751   29.028  1.00 23.57  ? 431 HOH   A O   1 
HETATM 2275 O  O   . HOH   E 5 .   ? 6.902   16.296  27.272  1.00 28.94  ? 432 HOH   A O   1 
HETATM 2276 O  O   . HOH   E 5 .   ? 0.717   12.574  26.748  1.00 23.18  ? 433 HOH   A O   1 
HETATM 2277 O  O   . HOH   E 5 .   ? 4.553   16.370  33.268  1.00 29.44  ? 434 HOH   A O   1 
HETATM 2278 O  O   . HOH   E 5 .   ? 19.876  -2.123  15.819  1.00 13.29  ? 435 HOH   A O   1 
HETATM 2279 O  O   . HOH   E 5 .   ? -4.788  -3.888  13.163  1.00 37.45  ? 436 HOH   A O   1 
HETATM 2280 O  O   . HOH   E 5 .   ? 14.804  -2.647  -6.412  1.00 31.10  ? 437 HOH   A O   1 
HETATM 2281 O  O   . HOH   E 5 .   ? 6.856   -19.096 3.371   1.00 38.89  ? 438 HOH   A O   1 
HETATM 2282 O  O   . HOH   E 5 .   ? 24.722  6.939   29.878  1.00 22.23  ? 439 HOH   A O   1 
HETATM 2283 O  O   . HOH   E 5 .   ? -0.015  9.776   1.887   1.00 21.43  ? 440 HOH   A O   1 
HETATM 2284 O  O   . HOH   E 5 .   ? 16.332  -10.171 32.132  1.00 25.90  ? 441 HOH   A O   1 
HETATM 2285 O  O   . HOH   E 5 .   ? 20.540  16.033  16.169  1.00 30.19  ? 442 HOH   A O   1 
HETATM 2286 O  O   . HOH   E 5 .   ? 10.433  10.578  25.614  1.00 13.77  ? 443 HOH   A O   1 
HETATM 2287 O  O   . HOH   E 5 .   ? 1.187   -15.053 3.021   1.00 27.31  ? 444 HOH   A O   1 
HETATM 2288 O  O   . HOH   E 5 .   ? 25.378  -0.592  28.951  1.00 30.30  ? 445 HOH   A O   1 
HETATM 2289 O  O   . HOH   E 5 .   ? 4.010   -21.108 4.007   1.00 34.14  ? 446 HOH   A O   1 
HETATM 2290 O  O   . HOH   E 5 .   ? 25.275  -1.566  26.596  1.00 23.30  ? 447 HOH   A O   1 
HETATM 2291 O  O   . HOH   E 5 .   ? -6.280  -5.512  26.108  1.00 49.13  ? 448 HOH   A O   1 
HETATM 2292 O  O   . HOH   E 5 .   ? 10.560  -16.367 17.098  1.00 19.99  ? 449 HOH   A O   1 
HETATM 2293 O  O   . HOH   E 5 .   ? -6.642  4.548   23.574  1.00 39.27  ? 450 HOH   A O   1 
HETATM 2294 O  O   . HOH   E 5 .   ? -3.097  10.540  20.185  1.00 25.21  ? 451 HOH   A O   1 
HETATM 2295 O  O   . HOH   E 5 .   ? 20.966  2.957   34.577  1.00 29.45  ? 452 HOH   A O   1 
HETATM 2296 O  O   . HOH   E 5 .   ? 29.262  -3.783  -10.526 1.00 34.86  ? 453 HOH   A O   1 
HETATM 2297 O  O   . HOH   E 5 .   ? 0.372   10.076  30.126  1.00 32.13  ? 454 HOH   A O   1 
HETATM 2298 O  O   . HOH   E 5 .   ? 11.060  15.719  9.954   1.00 57.26  ? 455 HOH   A O   1 
HETATM 2299 O  O   . HOH   E 5 .   ? 11.075  -10.629 40.180  1.00 29.43  ? 456 HOH   A O   1 
HETATM 2300 O  O   . HOH   E 5 .   ? -4.837  8.012   27.041  1.00 27.32  ? 457 HOH   A O   1 
HETATM 2301 O  O   . HOH   E 5 .   ? 23.148  10.054  27.922  1.00 41.54  ? 458 HOH   A O   1 
HETATM 2302 O  O   . HOH   E 5 .   ? 28.548  -6.072  -1.026  1.00 34.38  ? 459 HOH   A O   1 
HETATM 2303 O  O   . HOH   E 5 .   ? 32.640  1.415   16.037  1.00 38.02  ? 460 HOH   A O   1 
HETATM 2304 O  O   . HOH   E 5 .   ? 4.566   -13.631 32.796  1.00 48.31  ? 461 HOH   A O   1 
HETATM 2305 O  O   . HOH   E 5 .   ? 9.240   11.446  3.021   1.00 50.06  ? 462 HOH   A O   1 
HETATM 2306 O  O   . HOH   E 5 .   ? 8.425   -20.585 8.343   1.00 40.73  ? 463 HOH   A O   1 
HETATM 2307 O  O   . HOH   E 5 .   ? 12.638  -13.574 36.645  1.00 28.91  ? 464 HOH   A O   1 
HETATM 2308 O  O   . HOH   E 5 .   ? -8.312  12.144  6.451   1.00 57.53  ? 465 HOH   A O   1 
HETATM 2309 O  O   . HOH   E 5 .   ? 4.025   -12.305 37.477  1.00 32.01  ? 466 HOH   A O   1 
HETATM 2310 O  O   . HOH   E 5 .   ? 2.440   -19.285 14.826  1.00 32.42  ? 467 HOH   A O   1 
HETATM 2311 O  O   . HOH   E 5 .   ? 23.560  -11.358 5.182   1.00 23.29  ? 468 HOH   A O   1 
HETATM 2312 O  O   . HOH   E 5 .   ? 13.097  -13.584 11.372  1.00 14.46  ? 469 HOH   A O   1 
HETATM 2313 O  O   . HOH   E 5 .   ? 20.143  5.686   13.606  1.00 43.36  ? 470 HOH   A O   1 
HETATM 2314 O  O   . HOH   E 5 .   ? 19.877  10.977  28.183  1.00 31.40  ? 471 HOH   A O   1 
HETATM 2315 O  O   . HOH   E 5 .   ? -5.217  -5.566  30.544  1.00 39.82  ? 472 HOH   A O   1 
HETATM 2316 O  O   . HOH   E 5 .   ? 14.473  -3.467  37.353  1.00 20.54  ? 473 HOH   A O   1 
HETATM 2317 O  O   . HOH   E 5 .   ? 7.071   12.335  27.897  1.00 21.83  ? 474 HOH   A O   1 
HETATM 2318 O  O   . HOH   E 5 .   ? 21.562  9.108   29.913  1.00 32.04  ? 475 HOH   A O   1 
HETATM 2319 O  O   . HOH   E 5 .   ? 14.048  -13.023 31.663  1.00 23.54  ? 476 HOH   A O   1 
HETATM 2320 O  O   . HOH   E 5 .   ? 3.018   -1.007  44.954  1.00 42.31  ? 477 HOH   A O   1 
HETATM 2321 O  O   . HOH   E 5 .   ? 20.776  2.934   -10.953 1.00 31.11  ? 478 HOH   A O   1 
HETATM 2322 O  O   . HOH   E 5 .   ? 8.211   -7.131  -3.142  1.00 31.27  ? 479 HOH   A O   1 
HETATM 2323 O  O   . HOH   E 5 .   ? -0.539  21.252  17.255  1.00 49.75  ? 480 HOH   A O   1 
HETATM 2324 O  O   . HOH   E 5 .   ? 22.885  -13.791 9.279   1.00 22.75  ? 481 HOH   A O   1 
HETATM 2325 O  O   . HOH   E 5 .   ? 21.234  0.838   -4.724  1.00 20.58  ? 482 HOH   A O   1 
HETATM 2326 O  O   . HOH   E 5 .   ? -4.305  2.403   32.947  1.00 62.57  ? 483 HOH   A O   1 
HETATM 2327 O  O   . HOH   E 5 .   ? -4.370  11.360  13.260  1.00 41.78  ? 484 HOH   A O   1 
HETATM 2328 O  O   . HOH   E 5 .   ? 18.525  -6.908  29.182  1.00 15.58  ? 485 HOH   A O   1 
HETATM 2329 O  O   . HOH   E 5 .   ? 17.261  -14.035 24.447  1.00 18.32  ? 486 HOH   A O   1 
HETATM 2330 O  O   . HOH   E 5 .   ? 23.163  -5.055  -8.365  1.00 42.88  ? 487 HOH   A O   1 
HETATM 2331 O  O   . HOH   E 5 .   ? 29.676  -1.974  21.174  1.00 17.43  ? 488 HOH   A O   1 
HETATM 2332 O  O   . HOH   E 5 .   ? 16.492  -11.661 18.063  1.00 12.80  ? 489 HOH   A O   1 
HETATM 2333 O  O   . HOH   E 5 .   ? 6.037   21.987  17.784  1.00 24.90  ? 490 HOH   A O   1 
HETATM 2334 O  O   . HOH   E 5 .   ? 19.023  -2.673  -7.164  1.00 38.61  ? 491 HOH   A O   1 
HETATM 2335 O  O   . HOH   E 5 .   ? 10.491  -17.579 20.144  1.00 27.31  ? 492 HOH   A O   1 
HETATM 2336 O  O   . HOH   E 5 .   ? 2.413   -10.516 -3.496  1.00 31.48  ? 493 HOH   A O   1 
HETATM 2337 O  O   . HOH   E 5 .   ? 1.671   19.318  6.099   1.00 26.93  ? 494 HOH   A O   1 
HETATM 2338 O  O   . HOH   E 5 .   ? 17.942  6.079   8.095   1.00 31.77  ? 495 HOH   A O   1 
HETATM 2339 O  O   . HOH   E 5 .   ? 22.380  -9.950  25.182  1.00 32.34  ? 496 HOH   A O   1 
HETATM 2340 O  O   . HOH   E 5 .   ? -5.433  4.861   20.926  1.00 36.78  ? 497 HOH   A O   1 
HETATM 2341 O  O   . HOH   E 5 .   ? 17.310  -11.150 -2.929  1.00 28.60  ? 498 HOH   A O   1 
HETATM 2342 O  O   . HOH   E 5 .   ? 17.551  -9.300  20.923  1.00 13.36  ? 499 HOH   A O   1 
HETATM 2343 O  O   . HOH   E 5 .   ? -1.783  -3.977  2.802   1.00 24.06  ? 500 HOH   A O   1 
HETATM 2344 O  O   . HOH   E 5 .   ? 36.465  -0.598  14.506  1.00 24.39  ? 501 HOH   A O   1 
HETATM 2345 O  O   . HOH   E 5 .   ? -0.535  -5.191  23.583  1.00 15.56  ? 502 HOH   A O   1 
HETATM 2346 O  O   . HOH   E 5 .   ? 16.777  -6.667  31.224  1.00 22.60  ? 503 HOH   A O   1 
HETATM 2347 O  O   . HOH   E 5 .   ? 24.547  -7.213  26.146  1.00 44.69  ? 504 HOH   A O   1 
HETATM 2348 O  O   . HOH   E 5 .   ? -2.370  -9.152  17.298  1.00 32.63  ? 505 HOH   A O   1 
HETATM 2349 O  O   . HOH   E 5 .   ? 3.603   -14.421 21.899  1.00 32.18  ? 506 HOH   A O   1 
HETATM 2350 O  O   . HOH   E 5 .   ? 26.498  8.953   20.365  1.00 20.91  ? 507 HOH   A O   1 
HETATM 2351 O  O   . HOH   E 5 .   ? 3.139   -18.685 8.114   1.00 17.93  ? 508 HOH   A O   1 
HETATM 2352 O  O   . HOH   E 5 .   ? 4.040   -6.515  20.442  1.00 12.37  ? 509 HOH   A O   1 
HETATM 2353 O  O   . HOH   E 5 .   ? 25.547  -4.855  8.015   1.00 32.07  ? 510 HOH   A O   1 
HETATM 2354 O  O   . HOH   E 5 .   ? 9.842   -17.358 6.933   1.00 31.51  ? 511 HOH   A O   1 
HETATM 2355 O  O   . HOH   E 5 .   ? 5.569   10.903  -2.057  1.00 38.58  ? 512 HOH   A O   1 
HETATM 2356 O  O   . HOH   E 5 .   ? 4.844   17.775  23.808  1.00 22.53  ? 513 HOH   A O   1 
HETATM 2357 O  O   . HOH   E 5 .   ? 2.958   12.572  11.430  1.00 22.42  ? 514 HOH   A O   1 
HETATM 2358 O  O   . HOH   E 5 .   ? 30.398  9.429   18.494  1.00 45.58  ? 515 HOH   A O   1 
HETATM 2359 O  O   . HOH   E 5 .   ? -0.864  7.682   4.776   1.00 20.70  ? 516 HOH   A O   1 
HETATM 2360 O  O   . HOH   E 5 .   ? 1.409   -2.485  41.454  1.00 40.23  ? 517 HOH   A O   1 
HETATM 2361 O  O   . HOH   E 5 .   ? 24.302  4.438   8.084   1.00 44.37  ? 518 HOH   A O   1 
HETATM 2362 O  O   . HOH   E 5 .   ? 17.647  -11.398 25.234  1.00 15.06  ? 519 HOH   A O   1 
HETATM 2363 O  O   . HOH   E 5 .   ? 20.625  12.675  23.427  1.00 25.06  ? 520 HOH   A O   1 
HETATM 2364 O  O   . HOH   E 5 .   ? 29.071  -7.575  16.735  1.00 27.30  ? 521 HOH   A O   1 
HETATM 2365 O  O   . HOH   E 5 .   ? 5.809   21.414  13.230  1.00 21.94  ? 522 HOH   A O   1 
HETATM 2366 O  O   . HOH   E 5 .   ? 34.533  2.198   24.588  1.00 23.58  ? 523 HOH   A O   1 
HETATM 2367 O  O   . HOH   E 5 .   ? 6.331   -16.779 18.812  1.00 23.69  ? 524 HOH   A O   1 
HETATM 2368 O  O   . HOH   E 5 .   ? -5.242  5.487   15.432  1.00 31.30  ? 525 HOH   A O   1 
HETATM 2369 O  O   . HOH   E 5 .   ? 4.946   -10.440 24.468  1.00 20.66  ? 526 HOH   A O   1 
HETATM 2370 O  O   . HOH   E 5 .   ? -2.052  1.341   34.533  1.00 30.78  ? 527 HOH   A O   1 
HETATM 2371 O  O   . HOH   E 5 .   ? 30.630  3.891   12.173  1.00 44.76  ? 528 HOH   A O   1 
HETATM 2372 O  O   . HOH   E 5 .   ? -1.311  21.786  12.294  1.00 47.04  ? 529 HOH   A O   1 
HETATM 2373 O  O   . HOH   E 5 .   ? -3.005  -0.600  29.088  1.00 36.90  ? 530 HOH   A O   1 
HETATM 2374 O  O   . HOH   E 5 .   ? 20.750  -18.707 14.603  1.00 51.98  ? 531 HOH   A O   1 
HETATM 2375 O  O   . HOH   E 5 .   ? 2.606   -1.824  -2.597  1.00 32.69  ? 532 HOH   A O   1 
HETATM 2376 O  O   . HOH   E 5 .   ? 13.683  -6.896  32.661  1.00 19.27  ? 533 HOH   A O   1 
HETATM 2377 O  O   . HOH   E 5 .   ? 8.006   -14.948 26.664  1.00 21.84  ? 534 HOH   A O   1 
HETATM 2378 O  O   . HOH   E 5 .   ? 7.594   1.075   -6.199  1.00 40.54  ? 535 HOH   A O   1 
HETATM 2379 O  O   . HOH   E 5 .   ? -3.852  -5.842  9.147   1.00 21.04  ? 536 HOH   A O   1 
HETATM 2380 O  O   . HOH   E 5 .   ? 3.673   -5.631  39.624  1.00 45.18  ? 537 HOH   A O   1 
HETATM 2381 O  O   . HOH   E 5 .   ? 16.404  -14.109 0.886   1.00 35.92  ? 538 HOH   A O   1 
HETATM 2382 O  O   . HOH   E 5 .   ? 15.203  18.929  27.453  1.00 28.28  ? 539 HOH   A O   1 
HETATM 2383 O  O   . HOH   E 5 .   ? -2.203  -1.166  6.766   1.00 24.27  ? 540 HOH   A O   1 
HETATM 2384 O  O   . HOH   E 5 .   ? 1.769   11.913  8.933   1.00 18.33  ? 541 HOH   A O   1 
HETATM 2385 O  O   . HOH   E 5 .   ? -3.581  14.061  6.463   1.00 41.09  ? 542 HOH   A O   1 
HETATM 2386 O  O   . HOH   E 5 .   ? 25.987  -3.029  21.062  1.00 17.44  ? 543 HOH   A O   1 
HETATM 2387 O  O   . HOH   E 5 .   ? -2.943  1.194   26.554  1.00 18.76  ? 544 HOH   A O   1 
HETATM 2388 O  O   . HOH   E 5 .   ? 7.391   22.048  15.190  1.00 23.41  ? 545 HOH   A O   1 
HETATM 2389 O  O   . HOH   E 5 .   ? 4.474   2.278   -4.075  1.00 52.42  ? 546 HOH   A O   1 
HETATM 2390 O  O   . HOH   E 5 .   ? -5.729  -2.044  25.186  1.00 24.40  ? 547 HOH   A O   1 
HETATM 2391 O  O   . HOH   E 5 .   ? 13.909  -14.988 1.622   1.00 26.18  ? 548 HOH   A O   1 
HETATM 2392 O  O   . HOH   E 5 .   ? -4.535  0.759   35.108  1.00 47.08  ? 549 HOH   A O   1 
HETATM 2393 O  O   . HOH   E 5 .   ? 4.816   -8.032  32.959  1.00 22.64  ? 550 HOH   A O   1 
HETATM 2394 O  O   . HOH   E 5 .   ? -2.641  -16.126 6.348   1.00 41.22  ? 551 HOH   A O   1 
HETATM 2395 O  O   . HOH   E 5 .   ? 29.869  -10.870 8.960   1.00 53.23  ? 552 HOH   A O   1 
HETATM 2396 O  O   . HOH   E 5 .   ? 22.369  10.671  24.328  1.00 22.17  ? 553 HOH   A O   1 
HETATM 2397 O  O   . HOH   E 5 .   ? -1.069  -16.502 13.600  1.00 26.53  ? 554 HOH   A O   1 
HETATM 2398 O  O   . HOH   E 5 .   ? 13.692  7.689   8.400   1.00 47.18  ? 555 HOH   A O   1 
HETATM 2399 O  O   . HOH   E 5 .   ? 32.364  3.245   26.035  1.00 27.59  ? 556 HOH   A O   1 
HETATM 2400 O  O   . HOH   E 5 .   ? 27.425  -0.963  6.871   1.00 44.37  ? 557 HOH   A O   1 
HETATM 2401 O  O   . HOH   E 5 .   ? -2.841  1.134   3.974   1.00 26.81  ? 558 HOH   A O   1 
HETATM 2402 O  O   . HOH   E 5 .   ? 7.776   -16.598 14.760  1.00 21.12  ? 559 HOH   A O   1 
HETATM 2403 O  O   . HOH   E 5 .   ? 12.061  -3.965  35.932  1.00 21.01  ? 560 HOH   A O   1 
HETATM 2404 O  O   . HOH   E 5 .   ? 9.159   4.693   30.878  1.00 21.24  ? 561 HOH   A O   1 
HETATM 2405 O  O   . HOH   E 5 .   ? 26.821  2.712   8.500   1.00 29.26  ? 562 HOH   A O   1 
HETATM 2406 O  O   . HOH   E 5 .   ? 34.123  -1.870  13.651  1.00 34.14  ? 563 HOH   A O   1 
HETATM 2407 O  O   . HOH   E 5 .   ? 22.281  0.367   29.546  1.00 18.85  ? 564 HOH   A O   1 
HETATM 2408 O  O   A HOH   E 5 .   ? 22.875  -4.283  34.392  0.50 19.40  ? 565 HOH   A O   1 
HETATM 2409 O  O   B HOH   E 5 .   ? 21.888  -4.949  34.562  0.50 21.96  ? 565 HOH   A O   1 
HETATM 2410 O  O   A HOH   E 5 .   ? -2.368  -11.334 11.429  0.50 19.08  ? 566 HOH   A O   1 
HETATM 2411 O  O   B HOH   E 5 .   ? -1.444  -12.514 10.998  0.50 17.59  ? 566 HOH   A O   1 
HETATM 2412 O  O   . HOH   E 5 .   ? 23.657  -9.426  9.655   1.00 25.85  ? 567 HOH   A O   1 
HETATM 2413 O  O   . HOH   E 5 .   ? 20.464  -6.709  32.585  1.00 27.55  ? 568 HOH   A O   1 
HETATM 2414 O  O   . HOH   E 5 .   ? 8.198   5.531   -6.814  1.00 30.54  ? 569 HOH   A O   1 
HETATM 2415 O  O   . HOH   E 5 .   ? -0.148  -17.760 6.716   1.00 25.73  ? 570 HOH   A O   1 
HETATM 2416 O  O   . HOH   E 5 .   ? -1.848  -9.727  14.103  1.00 23.47  ? 571 HOH   A O   1 
HETATM 2417 O  O   . HOH   E 5 .   ? 35.024  7.614   19.076  1.00 47.87  ? 572 HOH   A O   1 
HETATM 2418 O  O   . HOH   E 5 .   ? 34.238  -3.865  24.518  1.00 30.86  ? 573 HOH   A O   1 
HETATM 2419 O  O   . HOH   E 5 .   ? 18.949  -10.459 22.914  1.00 13.64  ? 574 HOH   A O   1 
HETATM 2420 O  O   . HOH   E 5 .   ? 4.426   -14.488 -4.018  1.00 52.27  ? 575 HOH   A O   1 
HETATM 2421 O  O   . HOH   E 5 .   ? 2.477   -7.269  34.464  1.00 35.55  ? 576 HOH   A O   1 
HETATM 2422 O  O   . HOH   E 5 .   ? 28.692  7.974   21.802  1.00 19.90  ? 577 HOH   A O   1 
HETATM 2423 O  O   . HOH   E 5 .   ? 23.771  -13.114 -5.875  1.00 59.32  ? 578 HOH   A O   1 
HETATM 2424 O  O   . HOH   E 5 .   ? 15.505  17.882  12.189  1.00 48.68  ? 579 HOH   A O   1 
HETATM 2425 O  O   . HOH   E 5 .   ? 11.686  -8.246  -1.337  1.00 40.27  ? 580 HOH   A O   1 
HETATM 2426 O  O   . HOH   E 5 .   ? 9.820   2.939   33.420  1.00 32.47  ? 581 HOH   A O   1 
HETATM 2427 O  O   . HOH   E 5 .   ? 26.027  -11.206 -5.764  1.00 36.51  ? 582 HOH   A O   1 
HETATM 2428 O  O   . HOH   E 5 .   ? -6.939  -10.144 16.012  1.00 37.40  ? 583 HOH   A O   1 
HETATM 2429 O  O   . HOH   E 5 .   ? 15.676  5.227   -5.769  1.00 38.72  ? 584 HOH   A O   1 
HETATM 2430 O  O   . HOH   E 5 .   ? 13.953  3.317   35.231  1.00 30.86  ? 585 HOH   A O   1 
HETATM 2431 O  O   . HOH   E 5 .   ? 32.328  -2.005  7.601   1.00 43.87  ? 586 HOH   A O   1 
HETATM 2432 O  O   . HOH   E 5 .   ? 12.872  -17.509 21.800  1.00 23.11  ? 587 HOH   A O   1 
HETATM 2433 O  O   . HOH   E 5 .   ? 11.505  -6.161  34.165  1.00 23.22  ? 588 HOH   A O   1 
HETATM 2434 O  O   . HOH   E 5 .   ? 2.358   5.555   -3.537  1.00 41.08  ? 589 HOH   A O   1 
HETATM 2435 O  O   . HOH   E 5 .   ? 9.963   19.620  12.401  1.00 26.19  ? 590 HOH   A O   1 
HETATM 2436 O  O   . HOH   E 5 .   ? 18.206  7.946   -1.198  1.00 37.23  ? 591 HOH   A O   1 
HETATM 2437 O  O   . HOH   E 5 .   ? 1.331   -11.753 24.561  1.00 44.08  ? 592 HOH   A O   1 
HETATM 2438 O  O   . HOH   E 5 .   ? 5.926   -9.429  -3.781  1.00 66.95  ? 593 HOH   A O   1 
HETATM 2439 O  O   . HOH   E 5 .   ? 19.723  20.747  23.395  1.00 37.48  ? 594 HOH   A O   1 
HETATM 2440 O  O   . HOH   E 5 .   ? -3.523  -18.665 8.451   1.00 49.98  ? 595 HOH   A O   1 
HETATM 2441 O  O   . HOH   E 5 .   ? 20.797  -12.478 22.289  1.00 27.33  ? 596 HOH   A O   1 
HETATM 2442 O  O   . HOH   E 5 .   ? -3.865  6.712   8.089   1.00 52.69  ? 597 HOH   A O   1 
HETATM 2443 O  O   . HOH   E 5 .   ? 11.194  16.987  12.246  1.00 26.23  ? 598 HOH   A O   1 
HETATM 2444 O  O   . HOH   E 5 .   ? 10.527  22.768  25.106  1.00 31.90  ? 599 HOH   A O   1 
HETATM 2445 O  O   . HOH   E 5 .   ? 10.004  11.182  7.507   1.00 46.50  ? 600 HOH   A O   1 
HETATM 2446 O  O   . HOH   E 5 .   ? 26.254  -5.339  22.401  1.00 36.96  ? 601 HOH   A O   1 
HETATM 2447 O  O   . HOH   E 5 .   ? 12.116  2.590   43.118  1.00 30.14  ? 602 HOH   A O   1 
HETATM 2448 O  O   . HOH   E 5 .   ? 3.983   -4.948  42.324  1.00 37.30  ? 603 HOH   A O   1 
HETATM 2449 O  O   . HOH   E 5 .   ? -4.756  5.203   34.790  1.00 60.42  ? 604 HOH   A O   1 
HETATM 2450 O  O   . HOH   E 5 .   ? 35.942  -5.027  7.784   1.00 48.25  ? 605 HOH   A O   1 
HETATM 2451 O  O   . HOH   E 5 .   ? 21.445  2.547   -6.804  1.00 32.40  ? 606 HOH   A O   1 
HETATM 2452 O  O   . HOH   E 5 .   ? 7.987   10.043  30.037  1.00 21.27  ? 607 HOH   A O   1 
HETATM 2453 O  O   . HOH   E 5 .   ? 13.168  -3.171  39.809  1.00 35.49  ? 608 HOH   A O   1 
HETATM 2454 O  O   . HOH   E 5 .   ? 14.451  -18.136 24.229  1.00 35.54  ? 609 HOH   A O   1 
HETATM 2455 O  O   . HOH   E 5 .   ? -3.713  -7.636  1.963   1.00 30.36  ? 610 HOH   A O   1 
HETATM 2456 O  O   . HOH   E 5 .   ? 31.297  -0.581  13.961  1.00 33.84  ? 611 HOH   A O   1 
HETATM 2457 O  O   . HOH   E 5 .   ? 22.637  -13.790 15.014  1.00 44.64  ? 612 HOH   A O   1 
HETATM 2458 O  O   . HOH   E 5 .   ? 10.209  -4.121  40.453  1.00 30.38  ? 613 HOH   A O   1 
HETATM 2459 O  O   . HOH   E 5 .   ? 5.695   -18.327 23.112  1.00 53.77  ? 614 HOH   A O   1 
HETATM 2460 O  O   . HOH   E 5 .   ? 19.632  13.232  25.938  1.00 31.46  ? 615 HOH   A O   1 
HETATM 2461 O  O   . HOH   E 5 .   ? 36.403  -8.342  14.690  1.00 47.69  ? 616 HOH   A O   1 
HETATM 2462 O  O   . HOH   E 5 .   ? 15.740  2.077   40.045  1.00 46.80  ? 617 HOH   A O   1 
HETATM 2463 O  O   . HOH   E 5 .   ? 12.804  -19.737 9.017   1.00 36.44  ? 618 HOH   A O   1 
HETATM 2464 O  O   . HOH   E 5 .   ? 28.174  -1.744  -10.752 1.00 35.11  ? 619 HOH   A O   1 
HETATM 2465 O  O   . HOH   E 5 .   ? 20.819  -1.555  39.480  1.00 47.90  ? 620 HOH   A O   1 
HETATM 2466 O  O   . HOH   E 5 .   ? 29.707  -2.931  23.918  1.00 31.11  ? 621 HOH   A O   1 
HETATM 2467 O  O   . HOH   E 5 .   ? 8.185   -15.393 17.038  1.00 20.68  ? 622 HOH   A O   1 
HETATM 2468 O  O   . HOH   E 5 .   ? 25.430  7.024   11.876  1.00 56.45  ? 623 HOH   A O   1 
HETATM 2469 O  O   . HOH   E 5 .   ? 15.594  -11.061 -5.327  1.00 41.26  ? 624 HOH   A O   1 
HETATM 2470 O  O   . HOH   E 5 .   ? 27.508  -6.066  -10.317 1.00 52.48  ? 625 HOH   A O   1 
HETATM 2471 O  O   . HOH   E 5 .   ? 0.151   -18.673 1.667   1.00 38.67  ? 626 HOH   A O   1 
HETATM 2472 O  O   . HOH   E 5 .   ? 13.579  -7.219  -2.509  1.00 36.18  ? 627 HOH   A O   1 
HETATM 2473 O  O   . HOH   E 5 .   ? 12.593  -15.679 34.820  1.00 33.94  ? 628 HOH   A O   1 
HETATM 2474 O  O   . HOH   E 5 .   ? 15.372  10.651  10.768  1.00 42.79  ? 629 HOH   A O   1 
HETATM 2475 O  O   . HOH   E 5 .   ? 3.317   21.885  17.590  1.00 31.32  ? 630 HOH   A O   1 
HETATM 2476 O  O   . HOH   E 5 .   ? 23.508  -2.662  -12.089 1.00 51.50  ? 631 HOH   A O   1 
HETATM 2477 O  O   . HOH   E 5 .   ? -6.338  8.653   29.482  1.00 46.66  ? 632 HOH   A O   1 
HETATM 2478 O  O   . HOH   E 5 .   ? -5.521  -4.387  4.993   1.00 48.31  ? 633 HOH   A O   1 
HETATM 2479 O  O   . HOH   E 5 .   ? -6.975  6.898   25.348  1.00 42.51  ? 634 HOH   A O   1 
HETATM 2480 O  O   . HOH   E 5 .   ? 18.864  -10.370 31.523  1.00 37.84  ? 635 HOH   A O   1 
HETATM 2481 O  O   . HOH   E 5 .   ? 35.704  1.983   15.112  1.00 33.73  ? 636 HOH   A O   1 
HETATM 2482 O  O   . HOH   E 5 .   ? 4.872   18.678  26.568  1.00 35.85  ? 637 HOH   A O   1 
HETATM 2483 O  O   . HOH   E 5 .   ? 32.882  -4.633  7.878   1.00 39.24  ? 638 HOH   A O   1 
HETATM 2484 O  O   . HOH   E 5 .   ? -2.850  -1.524  4.033   1.00 44.84  ? 639 HOH   A O   1 
HETATM 2485 O  O   . HOH   E 5 .   ? -3.584  15.612  16.488  1.00 64.75  ? 640 HOH   A O   1 
HETATM 2486 O  O   . HOH   E 5 .   ? 23.947  -11.497 8.142   1.00 28.47  ? 641 HOH   A O   1 
HETATM 2487 O  O   . HOH   E 5 .   ? -4.087  10.716  26.284  1.00 44.64  ? 642 HOH   A O   1 
HETATM 2488 O  O   . HOH   E 5 .   ? 8.341   12.680  -5.334  1.00 56.51  ? 643 HOH   A O   1 
HETATM 2489 O  O   . HOH   E 5 .   ? 19.486  -11.305 27.333  1.00 30.94  ? 644 HOH   A O   1 
HETATM 2490 O  O   . HOH   E 5 .   ? 20.416  5.157   10.210  1.00 51.06  ? 645 HOH   A O   1 
HETATM 2491 O  O   . HOH   E 5 .   ? 23.359  -1.208  37.553  1.00 45.38  ? 646 HOH   A O   1 
HETATM 2492 O  O   . HOH   E 5 .   ? 13.238  9.780   9.475   1.00 56.54  ? 647 HOH   A O   1 
HETATM 2493 O  O   . HOH   E 5 .   ? 6.525   13.105  35.649  1.00 44.26  ? 648 HOH   A O   1 
HETATM 2494 O  O   . HOH   E 5 .   ? 3.261   -10.316 31.650  1.00 40.24  ? 649 HOH   A O   1 
HETATM 2495 O  O   . HOH   E 5 .   ? 17.117  15.625  11.394  1.00 64.93  ? 650 HOH   A O   1 
HETATM 2496 O  O   . HOH   E 5 .   ? 27.125  -9.004  15.837  1.00 45.49  ? 651 HOH   A O   1 
HETATM 2497 O  O   . HOH   E 5 .   ? 27.481  -3.451  27.423  1.00 39.33  ? 652 HOH   A O   1 
HETATM 2498 O  O   . HOH   E 5 .   ? 10.521  6.921   30.810  1.00 28.38  ? 653 HOH   A O   1 
HETATM 2499 O  O   . HOH   E 5 .   ? 19.208  -15.558 25.540  1.00 35.14  ? 654 HOH   A O   1 
HETATM 2500 O  O   . HOH   E 5 .   ? 21.253  -15.383 -2.128  1.00 56.37  ? 655 HOH   A O   1 
HETATM 2501 O  O   . HOH   E 5 .   ? 4.162   -16.133 20.237  1.00 34.98  ? 656 HOH   A O   1 
HETATM 2502 O  O   . HOH   E 5 .   ? 22.680  -8.010  30.939  1.00 48.93  ? 657 HOH   A O   1 
HETATM 2503 O  O   . HOH   E 5 .   ? -1.389  -10.469 24.850  1.00 40.65  ? 658 HOH   A O   1 
HETATM 2504 O  O   . HOH   E 5 .   ? 36.522  0.701   26.043  1.00 23.55  ? 659 HOH   A O   1 
HETATM 2505 O  O   . HOH   E 5 .   ? 9.292   2.737   -7.714  1.00 52.99  ? 660 HOH   A O   1 
HETATM 2506 O  O   . HOH   E 5 .   ? 29.257  9.916   23.701  1.00 48.93  ? 661 HOH   A O   1 
HETATM 2507 O  O   . HOH   E 5 .   ? 4.178   -12.136 26.351  1.00 28.30  ? 662 HOH   A O   1 
HETATM 2508 O  O   . HOH   E 5 .   ? 22.877  14.303  22.669  1.00 35.89  ? 663 HOH   A O   1 
HETATM 2509 O  O   . HOH   E 5 .   ? 1.108   -13.766 22.353  1.00 39.89  ? 664 HOH   A O   1 
HETATM 2510 O  O   . HOH   E 5 .   ? 1.066   -0.279  43.069  1.00 46.62  ? 665 HOH   A O   1 
HETATM 2511 O  O   . HOH   E 5 .   ? -3.089  -5.209  0.351   1.00 39.70  ? 666 HOH   A O   1 
HETATM 2512 O  O   . HOH   E 5 .   ? 31.262  8.162   13.995  1.00 66.43  ? 667 HOH   A O   1 
HETATM 2513 O  O   . HOH   E 5 .   ? 24.987  -10.905 22.264  1.00 70.04  ? 668 HOH   A O   1 
HETATM 2514 O  O   . HOH   E 5 .   ? 22.288  14.931  18.295  1.00 62.95  ? 669 HOH   A O   1 
HETATM 2515 O  O   . HOH   E 5 .   ? 8.762   15.404  5.093   1.00 45.87  ? 670 HOH   A O   1 
HETATM 2516 O  O   . HOH   E 5 .   ? -0.509  -12.052 23.178  1.00 38.02  ? 671 HOH   A O   1 
HETATM 2517 O  O   . HOH   E 5 .   ? -12.287 -11.053 16.311  1.00 44.52  ? 672 HOH   A O   1 
HETATM 2518 O  O   . HOH   E 5 .   ? 22.426  -15.596 7.113   1.00 34.27  ? 673 HOH   A O   1 
HETATM 2519 O  O   . HOH   E 5 .   ? 9.367   12.549  0.789   1.00 38.18  ? 674 HOH   A O   1 
HETATM 2520 O  O   . HOH   E 5 .   ? 15.615  -7.737  34.465  1.00 52.29  ? 675 HOH   A O   1 
HETATM 2521 O  O   . HOH   E 5 .   ? 19.868  -9.274  29.058  1.00 21.35  ? 676 HOH   A O   1 
HETATM 2522 O  O   . HOH   E 5 .   ? 25.251  6.943   2.285   1.00 40.20  ? 677 HOH   A O   1 
HETATM 2523 O  O   . HOH   E 5 .   ? 9.844   -9.518  -3.055  1.00 48.48  ? 678 HOH   A O   1 
HETATM 2524 O  O   . HOH   E 5 .   ? 6.640   1.900   42.385  1.00 47.48  ? 679 HOH   A O   1 
HETATM 2525 O  O   . HOH   E 5 .   ? 23.237  -12.269 20.749  1.00 42.73  ? 680 HOH   A O   1 
HETATM 2526 O  O   . HOH   E 5 .   ? 33.524  5.995   27.253  1.00 42.07  ? 681 HOH   A O   1 
HETATM 2527 O  O   . HOH   E 5 .   ? 5.842   10.377  34.821  1.00 47.80  ? 682 HOH   A O   1 
HETATM 2528 O  O   . HOH   E 5 .   ? 27.300  7.432   29.292  1.00 46.13  ? 683 HOH   A O   1 
HETATM 2529 O  O   . HOH   E 5 .   ? 7.933   23.689  26.159  1.00 30.71  ? 684 HOH   A O   1 
HETATM 2530 O  O   . HOH   E 5 .   ? 27.553  10.434  18.272  1.00 45.63  ? 685 HOH   A O   1 
HETATM 2531 O  O   . HOH   E 5 .   ? -4.674  -4.998  33.797  1.00 46.22  ? 686 HOH   A O   1 
HETATM 2532 O  O   . HOH   E 5 .   ? 20.486  -5.041  -7.752  1.00 47.42  ? 687 HOH   A O   1 
HETATM 2533 O  O   . HOH   E 5 .   ? 7.160   5.393   33.320  1.00 42.85  ? 688 HOH   A O   1 
HETATM 2534 O  O   . HOH   E 5 .   ? 35.241  0.471   28.500  1.00 31.99  ? 689 HOH   A O   1 
HETATM 2535 O  O   . HOH   E 5 .   ? 24.915  11.717  23.766  1.00 36.49  ? 690 HOH   A O   1 
HETATM 2536 O  O   . HOH   E 5 .   ? 26.212  -4.838  33.394  1.00 60.58  ? 691 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 3   ? 0.2776 0.3731 0.4041 -0.0140 -0.0241 0.0148  3   HIS   A N   
2    C  CA  . HIS   A 3   ? 0.3014 0.4297 0.3863 -0.0168 -0.0373 0.0458  3   HIS   A CA  
3    C  C   . HIS   A 3   ? 0.4345 0.4417 0.3336 0.0258  -0.0270 0.0484  3   HIS   A C   
4    O  O   . HIS   A 3   ? 0.4511 0.5647 0.3504 -0.0290 -0.0548 0.0332  3   HIS   A O   
5    C  CB  . HIS   A 3   ? 0.3407 0.4106 0.3713 -0.0703 -0.0801 0.0842  3   HIS   A CB  
6    C  CG  . HIS   A 3   ? 0.4087 0.3532 0.4372 -0.0851 -0.0287 0.0533  3   HIS   A CG  
7    N  ND1 . HIS   A 3   ? 0.4027 0.3763 0.5266 -0.0480 -0.0706 -0.0149 3   HIS   A ND1 
8    C  CD2 . HIS   A 3   ? 0.3477 0.4237 0.4441 -0.1118 0.0164  0.0608  3   HIS   A CD2 
9    C  CE1 . HIS   A 3   ? 0.5679 0.2978 0.6127 -0.1314 0.0245  -0.0282 3   HIS   A CE1 
10   N  NE2 . HIS   A 3   ? 0.3759 0.4129 0.5107 -0.1346 0.0108  0.0060  3   HIS   A NE2 
11   N  N   . HIS   A 4   ? 0.4782 0.4198 0.5589 -0.1743 -0.1675 0.2437  4   HIS   A N   
12   C  CA  . HIS   A 4   ? 0.8613 0.9875 0.6200 -0.5284 0.4842  -0.0359 4   HIS   A CA  
13   C  C   . HIS   A 4   ? 0.3115 0.3274 0.4139 -0.0588 0.0466  -0.0478 4   HIS   A C   
14   O  O   . HIS   A 4   ? 0.3125 0.3391 0.2858 -0.0324 0.0793  0.0161  4   HIS   A O   
15   C  CB  . HIS   A 4   ? 2.0948 0.6962 0.3812 -0.6506 0.1234  0.0392  4   HIS   A CB  
16   C  CG  . HIS   A 4   ? 2.1124 1.2979 1.1307 -0.5560 0.2811  -0.0913 4   HIS   A CG  
17   N  ND1 . HIS   A 4   ? 1.3818 1.6803 1.1511 -0.3586 0.1666  -0.2506 4   HIS   A ND1 
18   C  CD2 . HIS   A 4   ? 1.9258 1.5468 1.1884 -0.5105 0.2778  0.0177  4   HIS   A CD2 
19   C  CE1 . HIS   A 4   ? 0.5763 1.7541 1.4325 0.5255  -0.1122 -0.0239 4   HIS   A CE1 
20   N  NE2 . HIS   A 4   ? 1.3178 1.5613 1.3766 -0.3546 0.2803  0.1291  4   HIS   A NE2 
21   N  N   . TRP   A 5   ? 0.2837 0.2731 0.3579 -0.0306 0.0600  0.0425  5   TRP   A N   
22   C  CA  . TRP   A 5   ? 0.2309 0.2052 0.3175 -0.0197 0.0614  0.0008  5   TRP   A CA  
23   C  C   . TRP   A 5   ? 0.2645 0.2074 0.2703 0.0027  0.0563  0.0173  5   TRP   A C   
24   O  O   . TRP   A 5   ? 0.2818 0.1942 0.2579 -0.0223 0.0454  0.0140  5   TRP   A O   
25   C  CB  . TRP   A 5   ? 0.2308 0.2149 0.3090 -0.0251 0.0502  -0.0376 5   TRP   A CB  
26   C  CG  . TRP   A 5   ? 0.2605 0.1981 0.2398 -0.0200 0.0525  -0.0004 5   TRP   A CG  
27   C  CD1 . TRP   A 5   ? 0.3346 0.2210 0.2443 -0.0027 0.0453  0.0196  5   TRP   A CD1 
28   C  CD2 . TRP   A 5   ? 0.2391 0.2080 0.2215 0.0263  0.0005  -0.0170 5   TRP   A CD2 
29   N  NE1 . TRP   A 5   ? 0.3608 0.2078 0.2660 0.0083  0.0294  0.0346  5   TRP   A NE1 
30   C  CE2 . TRP   A 5   ? 0.2746 0.2257 0.2333 0.0403  0.0173  0.0000  5   TRP   A CE2 
31   C  CE3 . TRP   A 5   ? 0.2409 0.2354 0.2007 -0.0100 0.0293  -0.0368 5   TRP   A CE3 
32   C  CZ2 . TRP   A 5   ? 0.2888 0.2850 0.2103 0.0095  -0.0175 -0.0024 5   TRP   A CZ2 
33   C  CZ3 . TRP   A 5   ? 0.2513 0.2767 0.1930 0.0252  -0.0058 -0.0422 5   TRP   A CZ3 
34   C  CH2 . TRP   A 5   ? 0.2451 0.2833 0.2353 0.0272  -0.0140 -0.0690 5   TRP   A CH2 
35   N  N   . GLY   A 6   ? 0.2282 0.1980 0.2228 -0.0087 0.0465  -0.0139 6   GLY   A N   
36   C  CA  . GLY   A 6   ? 0.2418 0.1749 0.2456 -0.0278 0.0410  -0.0220 6   GLY   A CA  
37   C  C   . GLY   A 6   ? 0.2026 0.1966 0.2345 0.0088  0.0475  -0.0172 6   GLY   A C   
38   O  O   . GLY   A 6   ? 0.2074 0.1864 0.2230 -0.0021 0.0378  0.0039  6   GLY   A O   
39   N  N   . TYR   A 7   ? 0.2697 0.1659 0.3010 -0.0017 0.0995  -0.0339 7   TYR   A N   
40   C  CA  . TYR   A 7   ? 0.2485 0.1595 0.3318 -0.0134 0.0943  -0.0223 7   TYR   A CA  
41   C  C   . TYR   A 7   ? 0.2791 0.1843 0.4459 0.0023  0.1081  -0.0566 7   TYR   A C   
42   O  O   . TYR   A 7   ? 0.3417 0.2020 0.7180 0.0054  0.2470  -0.0263 7   TYR   A O   
43   C  CB  . TYR   A 7   ? 0.2511 0.1861 0.2833 -0.0022 0.0739  -0.0522 7   TYR   A CB  
44   C  CG  . TYR   A 7   ? 0.2136 0.1615 0.2045 -0.0225 0.0301  -0.0473 7   TYR   A CG  
45   C  CD1 . TYR   A 7   ? 0.1907 0.1725 0.1961 -0.0171 0.0239  -0.0388 7   TYR   A CD1 
46   C  CD2 . TYR   A 7   ? 0.2294 0.1685 0.2407 -0.0035 0.0137  -0.0353 7   TYR   A CD2 
47   C  CE1 . TYR   A 7   ? 0.1754 0.1421 0.1831 -0.0156 -0.0021 -0.0144 7   TYR   A CE1 
48   C  CE2 . TYR   A 7   ? 0.2275 0.1956 0.1756 0.0081  0.0273  0.0030  7   TYR   A CE2 
49   C  CZ  . TYR   A 7   ? 0.1848 0.1736 0.1817 -0.0037 0.0152  0.0131  7   TYR   A CZ  
50   O  OH  . TYR   A 7   ? 0.2221 0.1815 0.1819 0.0188  0.0230  0.0064  7   TYR   A OH  
51   N  N   . GLY   A 8   ? 0.2981 0.1895 0.4993 -0.0027 0.1435  -0.0661 8   GLY   A N   
52   C  CA  . GLY   A 8   ? 0.3201 0.2002 0.5669 0.0060  0.1689  -0.0871 8   GLY   A CA  
53   C  C   . GLY   A 8   ? 0.3835 0.2222 0.4468 0.0131  0.1865  -0.0707 8   GLY   A C   
54   O  O   . GLY   A 8   ? 0.3112 0.2627 0.4697 0.0089  0.1583  -0.0679 8   GLY   A O   
55   N  N   A LYS   A 9   ? 0.4262 0.2197 0.6431 0.0370  0.0932  -0.0384 9   LYS   A N   
56   N  N   B LYS   A 9   ? 0.2521 0.2396 0.3334 -0.0466 0.0951  -0.0951 9   LYS   A N   
57   C  CA  A LYS   A 9   ? 0.4581 0.2298 0.5905 0.0203  0.0436  -0.0368 9   LYS   A CA  
58   C  CA  B LYS   A 9   ? 0.3093 0.2060 0.4537 -0.0284 0.0259  -0.0456 9   LYS   A CA  
59   C  C   A LYS   A 9   ? 0.3203 0.3292 0.3582 -0.0178 0.0981  0.1034  9   LYS   A C   
60   C  C   B LYS   A 9   ? 0.2174 0.2562 0.2929 0.0157  -0.0168 -0.0436 9   LYS   A C   
61   O  O   A LYS   A 9   ? 0.4348 0.3688 0.4189 0.0991  -0.0421 0.0864  9   LYS   A O   
62   O  O   B LYS   A 9   ? 0.2154 0.2938 0.2648 -0.0406 0.0300  -0.0027 9   LYS   A O   
63   C  CB  A LYS   A 9   ? 0.3678 0.2307 0.5560 0.1101  -0.0540 0.0258  9   LYS   A CB  
64   C  CB  B LYS   A 9   ? 0.2303 0.3054 0.3490 -0.0305 -0.0432 -0.1209 9   LYS   A CB  
65   C  CG  A LYS   A 9   ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  9   LYS   A CG  
66   C  CG  B LYS   A 9   ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  9   LYS   A CG  
67   C  CD  A LYS   A 9   ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  9   LYS   A CD  
68   C  CD  B LYS   A 9   ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  9   LYS   A CD  
69   C  CE  A LYS   A 9   ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  9   LYS   A CE  
70   C  CE  B LYS   A 9   ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  9   LYS   A CE  
71   N  NZ  A LYS   A 9   ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  9   LYS   A NZ  
72   N  NZ  B LYS   A 9   ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  9   LYS   A NZ  
73   N  N   A HIS   A 10  ? 0.1947 0.2298 0.2407 0.0322  0.0617  -0.0046 10  HIS   A N   
74   N  N   B HIS   A 10  ? 0.1816 0.2022 0.3119 0.0239  -0.0066 -0.0564 10  HIS   A N   
75   C  CA  A HIS   A 10  ? 0.1740 0.3210 0.2678 0.0001  -0.0185 -0.0857 10  HIS   A CA  
76   C  CA  B HIS   A 10  ? 0.2143 0.2042 0.2562 0.0091  0.0592  -0.0564 10  HIS   A CA  
77   C  C   A HIS   A 10  ? 0.2634 0.2871 0.3152 0.1315  0.0728  0.0085  10  HIS   A C   
78   C  C   B HIS   A 10  ? 0.2461 0.2098 0.3358 0.0287  0.1051  -0.0336 10  HIS   A C   
79   O  O   A HIS   A 10  ? 0.2505 0.3144 0.3252 0.1627  0.0442  0.0111  10  HIS   A O   
80   O  O   B HIS   A 10  ? 0.2579 0.1451 0.4914 0.0550  0.1285  -0.0131 10  HIS   A O   
81   C  CB  A HIS   A 10  ? 0.1456 0.3398 0.2786 0.0469  -0.0093 -0.0971 10  HIS   A CB  
82   C  CB  B HIS   A 10  ? 0.2054 0.2187 0.2465 0.0168  0.0574  -0.0103 10  HIS   A CB  
83   C  CG  A HIS   A 10  ? 0.2147 0.2877 0.2622 0.0153  -0.0320 -0.0710 10  HIS   A CG  
84   C  CG  B HIS   A 10  ? 0.2147 0.2366 0.2051 0.0384  0.0207  -0.0027 10  HIS   A CG  
85   N  ND1 A HIS   A 10  ? 0.2556 0.2745 0.2866 0.0370  -0.0214 -0.0514 10  HIS   A ND1 
86   N  ND1 B HIS   A 10  ? 0.2248 0.2348 0.2836 0.0223  0.0624  -0.0302 10  HIS   A ND1 
87   C  CD2 A HIS   A 10  ? 0.2463 0.2346 0.2630 -0.0034 -0.0085 -0.0568 10  HIS   A CD2 
88   C  CD2 B HIS   A 10  ? 0.2117 0.1876 0.2502 0.0333  0.0140  0.0020  10  HIS   A CD2 
89   C  CE1 A HIS   A 10  ? 0.2176 0.2514 0.3036 -0.0081 0.0292  -0.0494 10  HIS   A CE1 
90   C  CE1 B HIS   A 10  ? 0.2811 0.1599 0.2919 0.0094  0.0632  -0.0374 10  HIS   A CE1 
91   N  NE2 A HIS   A 10  ? 0.1740 0.2892 0.3759 -0.0013 0.0091  -0.0523 10  HIS   A NE2 
92   N  NE2 B HIS   A 10  ? 0.2521 0.2177 0.2988 0.0638  0.0540  -0.0167 10  HIS   A NE2 
93   N  N   . ASN   A 11  ? 0.2365 0.2423 0.4046 0.0569  0.1382  0.0220  11  ASN   A N   
94   C  CA  . ASN   A 11  ? 0.2465 0.2158 0.3462 0.0330  0.1151  0.0171  11  ASN   A CA  
95   C  C   . ASN   A 11  ? 0.2163 0.2085 0.3310 0.0117  0.0883  0.0092  11  ASN   A C   
96   O  O   . ASN   A 11  ? 0.2283 0.2257 0.3001 0.0328  0.0850  0.0234  11  ASN   A O   
97   C  CB  . ASN   A 11  ? 0.2488 0.2014 0.3312 0.0288  0.1022  0.0019  11  ASN   A CB  
98   C  CG  . ASN   A 11  ? 0.2861 0.2304 0.2918 0.0149  0.1194  -0.0354 11  ASN   A CG  
99   O  OD1 . ASN   A 11  ? 0.2718 0.2663 0.3987 -0.0142 0.1076  0.0069  11  ASN   A OD1 
100  N  ND2 . ASN   A 11  ? 0.3106 0.2940 0.2666 -0.0326 0.0820  -0.0265 11  ASN   A ND2 
101  N  N   . GLY   A 12  ? 0.1975 0.2169 0.3144 0.0093  0.0758  0.0204  12  GLY   A N   
102  C  CA  . GLY   A 12  ? 0.2096 0.2404 0.2509 0.0168  0.0763  -0.0097 12  GLY   A CA  
103  C  C   . GLY   A 12  ? 0.1878 0.1881 0.2568 0.0282  0.0452  0.0168  12  GLY   A C   
104  O  O   . GLY   A 12  ? 0.1734 0.1806 0.3107 0.0241  0.0374  0.0203  12  GLY   A O   
105  N  N   . PRO   A 13  ? 0.1805 0.1612 0.2477 0.0046  0.0402  -0.0075 13  PRO   A N   
106  C  CA  . PRO   A 13  ? 0.2028 0.1447 0.2535 -0.0100 0.0337  -0.0311 13  PRO   A CA  
107  C  C   . PRO   A 13  ? 0.2013 0.1455 0.2485 -0.0081 0.0245  0.0005  13  PRO   A C   
108  O  O   . PRO   A 13  ? 0.1923 0.1795 0.2992 -0.0134 0.0305  -0.0300 13  PRO   A O   
109  C  CB  . PRO   A 13  ? 0.2372 0.1902 0.2226 -0.0453 0.0515  -0.0412 13  PRO   A CB  
110  C  CG  . PRO   A 13  ? 0.2362 0.1966 0.2010 -0.0050 0.0461  -0.0233 13  PRO   A CG  
111  C  CD  . PRO   A 13  ? 0.2101 0.1896 0.2373 -0.0033 0.0507  -0.0245 13  PRO   A CD  
112  N  N   . GLU   A 14  ? 0.2233 0.1434 0.2787 0.0053  0.0291  0.0144  14  GLU   A N   
113  C  CA  . GLU   A 14  ? 0.2725 0.1729 0.3176 0.0111  -0.0124 0.0230  14  GLU   A CA  
114  C  C   . GLU   A 14  ? 0.2215 0.1718 0.2585 0.0487  0.0122  -0.0011 14  GLU   A C   
115  O  O   . GLU   A 14  ? 0.2379 0.2070 0.2986 0.0512  -0.0042 0.0324  14  GLU   A O   
116  C  CB  . GLU   A 14  ? 0.3646 0.1685 0.5189 0.0301  -0.0807 0.1053  14  GLU   A CB  
117  C  CG  . GLU   A 14  ? 0.5050 0.2744 0.5712 -0.0867 -0.0370 0.0785  14  GLU   A CG  
118  C  CD  . GLU   A 14  ? 0.6128 0.5213 0.5804 -0.1931 -0.0693 0.2287  14  GLU   A CD  
119  O  OE1 . GLU   A 14  ? 0.5934 0.8494 0.5908 -0.2011 0.0064  0.0039  14  GLU   A OE1 
120  O  OE2 . GLU   A 14  ? 0.5123 0.5344 0.8556 -0.2057 -0.1998 0.3883  14  GLU   A OE2 
121  N  N   . HIS   A 15  ? 0.1835 0.1833 0.2523 0.0199  0.0254  0.0006  15  HIS   A N   
122  C  CA  . HIS   A 15  ? 0.1888 0.1741 0.2774 0.0147  0.0217  -0.0013 15  HIS   A CA  
123  C  C   . HIS   A 15  ? 0.1676 0.1817 0.2240 0.0167  0.0190  0.0009  15  HIS   A C   
124  O  O   . HIS   A 15  ? 0.1520 0.1785 0.3361 0.0155  0.0145  0.0223  15  HIS   A O   
125  C  CB  . HIS   A 15  ? 0.1890 0.1958 0.2906 0.0410  0.0343  -0.0005 15  HIS   A CB  
126  C  CG  . HIS   A 15  ? 0.2330 0.2143 0.3041 0.0597  0.0561  0.0154  15  HIS   A CG  
127  N  ND1 . HIS   A 15  ? 0.2271 0.2925 0.3140 0.0851  0.0139  -0.0417 15  HIS   A ND1 
128  C  CD2 . HIS   A 15  ? 0.2764 0.2204 0.3183 0.0732  0.0450  -0.0100 15  HIS   A CD2 
129  C  CE1 . HIS   A 15  ? 0.3420 0.3244 0.3301 0.1332  0.0381  -0.0290 15  HIS   A CE1 
130  N  NE2 . HIS   A 15  ? 0.3393 0.2978 0.3688 0.1414  0.0728  -0.0277 15  HIS   A NE2 
131  N  N   . TRP   A 16  ? 0.1498 0.1605 0.2518 0.0174  0.0152  0.0085  16  TRP   A N   
132  C  CA  . TRP   A 16  ? 0.1620 0.1504 0.2394 0.0120  -0.0016 -0.0052 16  TRP   A CA  
133  C  C   . TRP   A 16  ? 0.1479 0.1611 0.2492 0.0100  0.0031  -0.0102 16  TRP   A C   
134  O  O   . TRP   A 16  ? 0.1574 0.1527 0.2587 -0.0072 -0.0160 0.0070  16  TRP   A O   
135  C  CB  . TRP   A 16  ? 0.1485 0.1787 0.2322 0.0060  0.0009  -0.0364 16  TRP   A CB  
136  C  CG  . TRP   A 16  ? 0.1676 0.1390 0.2174 -0.0044 0.0030  -0.0164 16  TRP   A CG  
137  C  CD1 . TRP   A 16  ? 0.1867 0.1719 0.2054 0.0068  0.0100  -0.0054 16  TRP   A CD1 
138  C  CD2 . TRP   A 16  ? 0.1518 0.1229 0.2215 0.0100  0.0140  -0.0113 16  TRP   A CD2 
139  N  NE1 . TRP   A 16  ? 0.1842 0.1781 0.2052 0.0119  0.0276  -0.0122 16  TRP   A NE1 
140  C  CE2 . TRP   A 16  ? 0.1644 0.1456 0.2145 -0.0027 0.0199  -0.0071 16  TRP   A CE2 
141  C  CE3 . TRP   A 16  ? 0.1618 0.1323 0.2251 0.0002  0.0087  0.0109  16  TRP   A CE3 
142  C  CZ2 . TRP   A 16  ? 0.1777 0.1522 0.2056 -0.0044 0.0256  -0.0093 16  TRP   A CZ2 
143  C  CZ3 . TRP   A 16  ? 0.1697 0.1323 0.2079 -0.0071 0.0178  -0.0215 16  TRP   A CZ3 
144  C  CH2 . TRP   A 16  ? 0.1843 0.1474 0.1878 0.0039  0.0156  -0.0107 16  TRP   A CH2 
145  N  N   . HIS   A 17  ? 0.1473 0.1832 0.2517 0.0152  -0.0037 -0.0149 17  HIS   A N   
146  C  CA  . HIS   A 17  ? 0.1479 0.1837 0.2662 0.0005  -0.0177 0.0119  17  HIS   A CA  
147  C  C   . HIS   A 17  ? 0.1367 0.1983 0.3057 -0.0055 -0.0255 0.0050  17  HIS   A C   
148  O  O   . HIS   A 17  ? 0.1530 0.2009 0.3134 -0.0229 -0.0205 0.0038  17  HIS   A O   
149  C  CB  . HIS   A 17  ? 0.1516 0.2218 0.2479 0.0166  -0.0110 0.0003  17  HIS   A CB  
150  C  CG  . HIS   A 17  ? 0.1669 0.1931 0.3181 0.0177  -0.0208 0.0473  17  HIS   A CG  
151  N  ND1 . HIS   A 17  ? 0.1849 0.2479 0.3047 0.0105  -0.0167 0.0462  17  HIS   A ND1 
152  C  CD2 . HIS   A 17  ? 0.1963 0.1878 0.3357 0.0348  0.0019  0.0493  17  HIS   A CD2 
153  C  CE1 . HIS   A 17  ? 0.1750 0.2851 0.3220 0.0355  0.0119  0.0480  17  HIS   A CE1 
154  N  NE2 . HIS   A 17  ? 0.1934 0.2452 0.3083 0.0266  -0.0059 0.0807  17  HIS   A NE2 
155  N  N   . LYS   A 18  ? 0.1328 0.1989 0.3248 0.0092  -0.0107 0.0476  18  LYS   A N   
156  C  CA  . LYS   A 18  ? 0.1459 0.2163 0.3399 0.0084  0.0125  0.0563  18  LYS   A CA  
157  C  C   . LYS   A 18  ? 0.1842 0.2018 0.3837 -0.0128 -0.0192 0.0508  18  LYS   A C   
158  O  O   . LYS   A 18  ? 0.2171 0.2606 0.5077 -0.0734 -0.0908 0.1033  18  LYS   A O   
159  C  CB  . LYS   A 18  ? 0.1654 0.2240 0.3570 0.0162  0.0150  0.0541  18  LYS   A CB  
160  C  CG  . LYS   A 18  ? 0.1684 0.2563 0.3491 0.0551  0.0168  0.0512  18  LYS   A CG  
161  C  CD  . LYS   A 18  ? 0.1802 0.2388 0.3490 0.0411  -0.0012 0.0488  18  LYS   A CD  
162  C  CE  . LYS   A 18  ? 0.1713 0.2332 0.3016 0.0378  0.0174  0.0550  18  LYS   A CE  
163  N  NZ  . LYS   A 18  ? 0.1796 0.3041 0.2852 0.0776  0.0317  0.0618  18  LYS   A NZ  
164  N  N   . ASP   A 19  ? 0.1707 0.2341 0.3127 0.0072  -0.0048 0.0553  19  ASP   A N   
165  C  CA  . ASP   A 19  ? 0.1819 0.1919 0.3501 0.0116  -0.0027 0.0325  19  ASP   A CA  
166  C  C   . ASP   A 19  ? 0.1432 0.1708 0.3887 -0.0104 0.0078  0.0381  19  ASP   A C   
167  O  O   . ASP   A 19  ? 0.2044 0.1687 0.3750 -0.0237 0.0317  0.0453  19  ASP   A O   
168  C  CB  . ASP   A 19  ? 0.2020 0.3461 0.3257 0.0416  -0.0094 0.0616  19  ASP   A CB  
169  C  CG  . ASP   A 19  ? 0.2111 0.4899 0.3935 0.0139  0.0200  -0.0375 19  ASP   A CG  
170  O  OD1 . ASP   A 19  ? 0.2883 0.4695 0.3958 -0.0518 0.0539  -0.0148 19  ASP   A OD1 
171  O  OD2 . ASP   A 19  ? 0.5502 0.6927 0.5296 0.0221  0.1229  -0.2453 19  ASP   A OD2 
172  N  N   . PHE   A 20  ? 0.1707 0.1858 0.2942 -0.0158 0.0113  0.0017  20  PHE   A N   
173  C  CA  . PHE   A 20  ? 0.1676 0.1777 0.2683 -0.0305 0.0095  -0.0085 20  PHE   A CA  
174  C  C   . PHE   A 20  ? 0.1540 0.1799 0.2550 -0.0114 0.0132  -0.0137 20  PHE   A C   
175  O  O   . PHE   A 20  ? 0.1707 0.1600 0.2722 -0.0140 -0.0032 0.0094  20  PHE   A O   
176  C  CB  . PHE   A 20  ? 0.1807 0.1892 0.2691 -0.0251 -0.0168 0.0238  20  PHE   A CB  
177  C  CG  . PHE   A 20  ? 0.1571 0.2258 0.2681 -0.0302 -0.0114 0.0351  20  PHE   A CG  
178  C  CD1 . PHE   A 20  ? 0.1804 0.2408 0.3098 -0.0168 -0.0233 0.0737  20  PHE   A CD1 
179  C  CD2 . PHE   A 20  ? 0.1824 0.2688 0.2857 -0.0453 0.0019  0.0025  20  PHE   A CD2 
180  C  CE1 . PHE   A 20  ? 0.2143 0.3134 0.2791 -0.0266 -0.0141 0.0534  20  PHE   A CE1 
181  C  CE2 . PHE   A 20  ? 0.1932 0.3285 0.3111 -0.0389 0.0025  0.0283  20  PHE   A CE2 
182  C  CZ  . PHE   A 20  ? 0.2115 0.3412 0.2573 -0.0238 0.0137  0.0783  20  PHE   A CZ  
183  N  N   . PRO   A 21  ? 0.1470 0.1922 0.2864 -0.0237 -0.0013 -0.0024 21  PRO   A N   
184  C  CA  A PRO   A 21  ? 0.1601 0.2010 0.2809 -0.0318 -0.0334 -0.0038 21  PRO   A CA  
185  C  CA  B PRO   A 21  ? 0.1724 0.2243 0.2790 -0.0282 -0.0298 0.0001  21  PRO   A CA  
186  C  C   . PRO   A 21  ? 0.1826 0.1868 0.2629 -0.0182 -0.0402 -0.0245 21  PRO   A C   
187  O  O   . PRO   A 21  ? 0.1754 0.2057 0.2727 -0.0122 -0.0395 -0.0157 21  PRO   A O   
188  C  CB  A PRO   A 21  ? 0.1700 0.2684 0.3589 -0.0665 -0.0502 0.0010  21  PRO   A CB  
189  C  CB  B PRO   A 21  ? 0.1707 0.2935 0.3128 -0.0707 -0.0406 0.0304  21  PRO   A CB  
190  C  CG  A PRO   A 21  ? 0.1425 0.2337 0.4117 -0.0551 -0.0770 -0.0189 21  PRO   A CG  
191  C  CG  B PRO   A 21  ? 0.1780 0.2690 0.3313 -0.0374 -0.0127 0.0257  21  PRO   A CG  
192  C  CD  A PRO   A 21  ? 0.1676 0.1926 0.3557 -0.0331 -0.0069 0.0021  21  PRO   A CD  
193  C  CD  B PRO   A 21  ? 0.1585 0.1949 0.3346 -0.0341 -0.0055 0.0003  21  PRO   A CD  
194  N  N   A ILE   A 22  ? 0.1586 0.1659 0.2344 -0.0290 -0.0336 -0.0266 22  ILE   A N   
195  N  N   B ILE   A 22  ? 0.1613 0.1571 0.2742 -0.0249 -0.0156 -0.0089 22  ILE   A N   
196  C  CA  A ILE   A 22  ? 0.1812 0.1433 0.2203 -0.0210 -0.0257 -0.0138 22  ILE   A CA  
197  C  CA  B ILE   A 22  ? 0.1706 0.1549 0.2676 -0.0094 -0.0124 0.0115  22  ILE   A CA  
198  C  C   A ILE   A 22  ? 0.1669 0.1300 0.2158 0.0017  -0.0229 -0.0055 22  ILE   A C   
199  C  C   B ILE   A 22  ? 0.1663 0.1602 0.2045 -0.0049 -0.0344 -0.0188 22  ILE   A C   
200  O  O   A ILE   A 22  ? 0.1733 0.1553 0.2025 -0.0119 -0.0284 0.0031  22  ILE   A O   
201  O  O   B ILE   A 22  ? 0.1521 0.1471 0.2470 0.0071  -0.0212 -0.0068 22  ILE   A O   
202  C  CB  A ILE   A 22  ? 0.2016 0.1597 0.1826 -0.0006 -0.0278 -0.0324 22  ILE   A CB  
203  C  CB  B ILE   A 22  ? 0.1611 0.1499 0.2521 -0.0200 -0.0039 0.0183  22  ILE   A CB  
204  C  CG1 A ILE   A 22  ? 0.1896 0.1285 0.2208 -0.0206 -0.0153 -0.0161 22  ILE   A CG1 
205  C  CG1 B ILE   A 22  ? 0.1843 0.2445 0.2631 0.0061  -0.0009 -0.0281 22  ILE   A CG1 
206  C  CG2 A ILE   A 22  ? 0.1761 0.1641 0.1588 -0.0781 0.0055  -0.0134 22  ILE   A CG2 
207  C  CG2 B ILE   A 22  ? 0.1161 0.1876 0.2477 0.0203  -0.0050 0.0026  22  ILE   A CG2 
208  C  CD1 A ILE   A 22  ? 0.1943 0.1280 0.2507 -0.0141 -0.0132 -0.0088 22  ILE   A CD1 
209  C  CD1 B ILE   A 22  ? 0.2408 0.3022 0.2569 -0.0234 0.0108  -0.0490 22  ILE   A CD1 
210  N  N   . ALA   A 23  ? 0.1583 0.1468 0.2274 -0.0116 -0.0177 -0.0147 23  ALA   A N   
211  C  CA  . ALA   A 23  ? 0.1713 0.1465 0.2337 -0.0131 -0.0055 -0.0133 23  ALA   A CA  
212  C  C   . ALA   A 23  ? 0.1521 0.1708 0.2258 0.0067  -0.0168 -0.0129 23  ALA   A C   
213  O  O   . ALA   A 23  ? 0.1741 0.1716 0.2465 -0.0041 -0.0091 -0.0022 23  ALA   A O   
214  C  CB  . ALA   A 23  ? 0.1611 0.1669 0.2426 0.0029  -0.0119 -0.0238 23  ALA   A CB  
215  N  N   . LYS   A 24  ? 0.1825 0.1807 0.2380 0.0122  -0.0414 0.0124  24  LYS   A N   
216  C  CA  . LYS   A 24  ? 0.1678 0.2205 0.2373 0.0060  -0.0326 -0.0078 24  LYS   A CA  
217  C  C   . LYS   A 24  ? 0.2008 0.2159 0.2443 0.0027  -0.0312 -0.0122 24  LYS   A C   
218  O  O   . LYS   A 24  ? 0.2052 0.2666 0.2612 0.0047  -0.0342 -0.0096 24  LYS   A O   
219  C  CB  . LYS   A 24  ? 0.1838 0.2522 0.2449 0.0258  -0.0302 0.0370  24  LYS   A CB  
220  C  CG  . LYS   A 24  ? 0.2086 0.3314 0.2468 0.0362  -0.0111 0.0125  24  LYS   A CG  
221  C  CD  . LYS   A 24  ? 0.2118 0.3274 0.4100 0.0299  -0.0240 0.0378  24  LYS   A CD  
222  C  CE  . LYS   A 24  ? 0.2546 0.3500 0.3820 0.0971  0.0009  0.1015  24  LYS   A CE  
223  N  NZ  . LYS   A 24  ? 0.4430 0.3147 0.4797 0.0763  0.0538  0.0242  24  LYS   A NZ  
224  N  N   . GLY   A 25  ? 0.1831 0.1991 0.2515 0.0091  -0.0127 -0.0113 25  GLY   A N   
225  C  CA  . GLY   A 25  ? 0.1852 0.2040 0.2754 -0.0067 -0.0107 -0.0460 25  GLY   A CA  
226  C  C   . GLY   A 25  ? 0.1910 0.2200 0.2011 0.0000  -0.0425 -0.0328 25  GLY   A C   
227  O  O   . GLY   A 25  ? 0.2011 0.2296 0.1951 0.0060  -0.0299 -0.0009 25  GLY   A O   
228  N  N   . GLU   A 26  ? 0.1967 0.2518 0.1801 0.0115  -0.0532 -0.0513 26  GLU   A N   
229  C  CA  . GLU   A 26  ? 0.2085 0.2509 0.1901 -0.0029 -0.0275 -0.0346 26  GLU   A CA  
230  C  C   . GLU   A 26  ? 0.2079 0.1958 0.1544 0.0120  -0.0269 -0.0272 26  GLU   A C   
231  O  O   . GLU   A 26  ? 0.2506 0.2630 0.1483 -0.0153 -0.0317 -0.0025 26  GLU   A O   
232  C  CB  . GLU   A 26  ? 0.2617 0.3574 0.2171 -0.0638 -0.0613 -0.1158 26  GLU   A CB  
233  C  CG  . GLU   A 26  ? 0.2823 0.4713 0.2594 0.0042  -0.0954 -0.0898 26  GLU   A CG  
234  C  CD  . GLU   A 26  ? 0.3715 0.5498 0.3555 0.0164  -0.1864 -0.0250 26  GLU   A CD  
235  O  OE1 . GLU   A 26  ? 0.4099 0.5352 0.4454 -0.0057 -0.1177 -0.0666 26  GLU   A OE1 
236  O  OE2 . GLU   A 26  ? 0.4052 0.7101 0.5307 0.1362  -0.1942 -0.0249 26  GLU   A OE2 
237  N  N   . ARG   A 27  ? 0.1989 0.1685 0.1632 -0.0087 -0.0411 -0.0114 27  ARG   A N   
238  C  CA  . ARG   A 27  ? 0.1848 0.1514 0.1467 0.0137  -0.0263 -0.0168 27  ARG   A CA  
239  C  C   . ARG   A 27  ? 0.1588 0.1435 0.1411 -0.0023 -0.0133 -0.0117 27  ARG   A C   
240  O  O   . ARG   A 27  ? 0.1752 0.1472 0.1421 0.0024  -0.0251 -0.0122 27  ARG   A O   
241  C  CB  . ARG   A 27  ? 0.2419 0.1641 0.1757 0.0159  -0.0135 -0.0259 27  ARG   A CB  
242  C  CG  . ARG   A 27  ? 0.2255 0.1984 0.1755 -0.0147 -0.0253 -0.0362 27  ARG   A CG  
243  C  CD  . ARG   A 27  ? 0.3157 0.1790 0.1800 0.0199  -0.0469 -0.0270 27  ARG   A CD  
244  N  NE  . ARG   A 27  ? 0.2583 0.1709 0.1713 -0.0030 -0.0046 -0.0117 27  ARG   A NE  
245  C  CZ  . ARG   A 27  ? 0.2560 0.1606 0.1658 0.0153  0.0109  -0.0095 27  ARG   A CZ  
246  N  NH1 . ARG   A 27  ? 0.2504 0.2128 0.2196 0.0175  0.0062  -0.0903 27  ARG   A NH1 
247  N  NH2 . ARG   A 27  ? 0.2476 0.1779 0.2051 -0.0059 -0.0110 -0.0240 27  ARG   A NH2 
248  N  N   . GLN   A 28  ? 0.1624 0.1419 0.1462 -0.0055 -0.0182 -0.0217 28  GLN   A N   
249  C  CA  . GLN   A 28  ? 0.1534 0.1358 0.1345 -0.0066 -0.0158 -0.0228 28  GLN   A CA  
250  C  C   . GLN   A 28  ? 0.1489 0.1349 0.1223 0.0023  -0.0061 -0.0107 28  GLN   A C   
251  O  O   . GLN   A 28  ? 0.1755 0.1584 0.1235 -0.0126 -0.0130 -0.0079 28  GLN   A O   
252  C  CB  . GLN   A 28  ? 0.1533 0.1429 0.1742 -0.0002 -0.0168 -0.0106 28  GLN   A CB  
253  C  CG  . GLN   A 28  ? 0.1613 0.1508 0.1711 -0.0127 -0.0222 -0.0086 28  GLN   A CG  
254  C  CD  . GLN   A 28  ? 0.1533 0.1386 0.1491 -0.0021 -0.0245 -0.0297 28  GLN   A CD  
255  O  OE1 . GLN   A 28  ? 0.1619 0.1439 0.1653 -0.0141 -0.0149 -0.0262 28  GLN   A OE1 
256  N  NE2 . GLN   A 28  ? 0.1588 0.1339 0.1785 -0.0024 -0.0156 -0.0264 28  GLN   A NE2 
257  N  N   . SER   A 29  ? 0.1540 0.1257 0.1249 -0.0003 -0.0102 -0.0156 29  SER   A N   
258  C  CA  . SER   A 29  ? 0.1529 0.1122 0.1542 0.0020  -0.0168 -0.0222 29  SER   A CA  
259  C  C   . SER   A 29  ? 0.1561 0.1038 0.1386 0.0048  -0.0168 -0.0027 29  SER   A C   
260  O  O   . SER   A 29  ? 0.1534 0.1219 0.1512 -0.0019 -0.0030 -0.0091 29  SER   A O   
261  C  CB  . SER   A 29  ? 0.1641 0.1346 0.1267 0.0216  -0.0055 -0.0121 29  SER   A CB  
262  O  OG  . SER   A 29  ? 0.1540 0.1093 0.1379 -0.0032 -0.0032 -0.0097 29  SER   A OG  
263  N  N   . PRO   A 30  ? 0.1521 0.1077 0.1307 0.0006  -0.0086 -0.0061 30  PRO   A N   
264  C  CA  . PRO   A 30  ? 0.1472 0.1213 0.1259 -0.0080 -0.0135 0.0003  30  PRO   A CA  
265  C  C   . PRO   A 30  ? 0.1562 0.1188 0.1285 0.0018  -0.0060 -0.0143 30  PRO   A C   
266  O  O   . PRO   A 30  ? 0.1611 0.1192 0.1426 0.0076  -0.0194 -0.0006 30  PRO   A O   
267  C  CB  . PRO   A 30  ? 0.1655 0.1210 0.1271 0.0066  -0.0144 -0.0154 30  PRO   A CB  
268  C  CG  . PRO   A 30  ? 0.1606 0.1161 0.1249 0.0015  -0.0065 0.0033  30  PRO   A CG  
269  C  CD  . PRO   A 30  ? 0.1812 0.1034 0.1256 0.0004  -0.0050 -0.0179 30  PRO   A CD  
270  N  N   . VAL   A 31  ? 0.1628 0.1100 0.1302 0.0059  0.0040  0.0083  31  VAL   A N   
271  C  CA  . VAL   A 31  ? 0.1910 0.1136 0.1162 0.0016  -0.0122 0.0089  31  VAL   A CA  
272  C  C   . VAL   A 31  ? 0.1861 0.1093 0.1327 0.0188  -0.0114 0.0058  31  VAL   A C   
273  O  O   . VAL   A 31  ? 0.1786 0.1216 0.1500 0.0031  -0.0189 0.0168  31  VAL   A O   
274  C  CB  . VAL   A 31  ? 0.1846 0.1291 0.1384 0.0006  -0.0158 -0.0052 31  VAL   A CB  
275  C  CG1 . VAL   A 31  ? 0.2078 0.1312 0.1583 -0.0135 0.0006  -0.0150 31  VAL   A CG1 
276  C  CG2 . VAL   A 31  ? 0.1805 0.1362 0.1622 0.0122  0.0132  0.0010  31  VAL   A CG2 
277  N  N   . ASP   A 32  ? 0.1804 0.1091 0.1435 0.0152  -0.0121 0.0234  32  ASP   A N   
278  C  CA  . ASP   A 32  ? 0.1837 0.1056 0.1482 0.0131  0.0131  0.0206  32  ASP   A CA  
279  C  C   . ASP   A 32  ? 0.1939 0.1217 0.1251 0.0042  -0.0072 0.0083  32  ASP   A C   
280  O  O   . ASP   A 32  ? 0.1978 0.1768 0.1582 -0.0020 -0.0063 -0.0155 32  ASP   A O   
281  C  CB  . ASP   A 32  ? 0.2286 0.1138 0.1734 0.0083  -0.0156 0.0340  32  ASP   A CB  
282  C  CG  . ASP   A 32  ? 0.2333 0.1316 0.1664 0.0075  -0.0071 0.0454  32  ASP   A CG  
283  O  OD1 . ASP   A 32  ? 0.2232 0.1247 0.1720 0.0037  -0.0120 0.0295  32  ASP   A OD1 
284  O  OD2 . ASP   A 32  ? 0.3037 0.1555 0.1637 -0.0164 -0.0155 0.0392  32  ASP   A OD2 
285  N  N   . ILE   A 33  ? 0.1825 0.1264 0.1412 0.0065  0.0039  0.0186  33  ILE   A N   
286  C  CA  . ILE   A 33  ? 0.2107 0.1284 0.1489 0.0149  -0.0030 0.0240  33  ILE   A CA  
287  C  C   . ILE   A 33  ? 0.2020 0.1291 0.1499 0.0267  0.0107  0.0263  33  ILE   A C   
288  O  O   . ILE   A 33  ? 0.2393 0.1347 0.1767 0.0015  0.0141  0.0258  33  ILE   A O   
289  C  CB  . ILE   A 33  ? 0.2085 0.1243 0.1668 0.0179  0.0069  0.0288  33  ILE   A CB  
290  C  CG1 . ILE   A 33  ? 0.2008 0.1330 0.1828 0.0080  -0.0099 0.0434  33  ILE   A CG1 
291  C  CG2 . ILE   A 33  ? 0.2085 0.1701 0.1745 0.0215  0.0201  0.0225  33  ILE   A CG2 
292  C  CD1 . ILE   A 33  ? 0.1886 0.2017 0.2023 0.0277  -0.0195 0.0374  33  ILE   A CD1 
293  N  N   A ASP   A 34  ? 0.2451 0.1562 0.1374 0.0306  0.0103  0.0337  34  ASP   A N   
294  N  N   B ASP   A 34  ? 0.2516 0.1561 0.1359 0.0306  0.0103  0.0365  34  ASP   A N   
295  C  CA  A ASP   A 34  ? 0.2366 0.1782 0.1580 0.0275  0.0173  0.0536  34  ASP   A CA  
296  C  CA  B ASP   A 34  ? 0.2563 0.1718 0.1427 0.0358  0.0168  0.0509  34  ASP   A CA  
297  C  C   A ASP   A 34  ? 0.2460 0.1691 0.1508 0.0444  0.0253  0.0425  34  ASP   A C   
298  C  C   B ASP   A 34  ? 0.2533 0.1670 0.1575 0.0406  0.0216  0.0510  34  ASP   A C   
299  O  O   A ASP   A 34  ? 0.3061 0.1760 0.1737 0.0613  0.0275  0.0320  34  ASP   A O   
300  O  O   B ASP   A 34  ? 0.3116 0.2031 0.1724 0.0454  0.0351  0.0282  34  ASP   A O   
301  C  CB  A ASP   A 34  ? 0.3122 0.1761 0.1759 0.0429  -0.0186 0.0433  34  ASP   A CB  
302  C  CB  B ASP   A 34  ? 0.3243 0.1870 0.1507 0.0674  -0.0079 0.0438  34  ASP   A CB  
303  C  CG  A ASP   A 34  ? 0.2521 0.2337 0.1807 0.0628  0.0337  0.0539  34  ASP   A CG  
304  C  CG  B ASP   A 34  ? 0.3569 0.2348 0.1767 0.0719  0.0214  0.0784  34  ASP   A CG  
305  O  OD1 A ASP   A 34  ? 0.2636 0.2594 0.1693 0.0463  0.0174  0.0732  34  ASP   A OD1 
306  O  OD1 B ASP   A 34  ? 0.4419 0.2758 0.2366 0.1571  0.0769  0.1285  34  ASP   A OD1 
307  O  OD2 A ASP   A 34  ? 0.3842 0.3271 0.2570 0.0411  -0.0447 0.1889  34  ASP   A OD2 
308  O  OD2 B ASP   A 34  ? 0.3905 0.1975 0.2238 0.0590  0.0637  0.0496  34  ASP   A OD2 
309  N  N   . THR   A 35  ? 0.2505 0.1922 0.1971 0.0297  0.0266  0.0798  35  THR   A N   
310  C  CA  . THR   A 35  ? 0.2490 0.2519 0.2181 0.0401  0.0355  0.0902  35  THR   A CA  
311  C  C   . THR   A 35  ? 0.3031 0.1812 0.2054 0.0561  0.0504  0.0576  35  THR   A C   
312  O  O   . THR   A 35  ? 0.3175 0.2090 0.2279 0.0549  0.0490  0.0326  35  THR   A O   
313  C  CB  . THR   A 35  ? 0.2618 0.2853 0.2555 0.0357  0.0270  0.0867  35  THR   A CB  
314  O  OG1 . THR   A 35  ? 0.3212 0.2644 0.2619 -0.0104 0.0369  0.0795  35  THR   A OG1 
315  C  CG2 . THR   A 35  ? 0.3001 0.3705 0.2339 0.0541  0.0237  0.0837  35  THR   A CG2 
316  N  N   . HIS   A 36  ? 0.3440 0.1941 0.1952 0.0485  0.0639  0.0763  36  HIS   A N   
317  C  CA  . HIS   A 36  ? 0.3430 0.2129 0.1799 0.0550  0.0469  0.0641  36  HIS   A CA  
318  C  C   . HIS   A 36  ? 0.4093 0.2249 0.1694 0.0516  0.0540  0.0546  36  HIS   A C   
319  O  O   . HIS   A 36  ? 0.3699 0.4101 0.1873 0.0934  0.0400  0.0447  36  HIS   A O   
320  C  CB  . HIS   A 36  ? 0.3931 0.2328 0.1953 0.0514  0.0461  0.1011  36  HIS   A CB  
321  C  CG  . HIS   A 36  ? 0.4449 0.2197 0.2229 0.0531  0.0290  0.0639  36  HIS   A CG  
322  N  ND1 . HIS   A 36  ? 0.6145 0.2674 0.2651 0.1274  -0.0942 0.0633  36  HIS   A ND1 
323  C  CD2 . HIS   A 36  ? 0.4674 0.2312 0.1923 -0.0150 -0.0133 0.0127  36  HIS   A CD2 
324  C  CE1 . HIS   A 36  ? 0.7674 0.2255 0.2936 0.0723  -0.0908 0.0359  36  HIS   A CE1 
325  N  NE2 . HIS   A 36  ? 0.6880 0.3074 0.3472 -0.0293 -0.1239 -0.0505 36  HIS   A NE2 
326  N  N   . THR   A 37  ? 0.3951 0.1876 0.2255 0.0784  0.0758  0.0316  37  THR   A N   
327  C  CA  . THR   A 37  ? 0.4029 0.2091 0.1869 0.0960  0.0294  0.0619  37  THR   A CA  
328  C  C   . THR   A 37  ? 0.3296 0.2208 0.1835 0.0951  0.0238  0.0283  37  THR   A C   
329  O  O   . THR   A 37  ? 0.3849 0.2499 0.2330 0.1103  -0.0070 0.0061  37  THR   A O   
330  C  CB  . THR   A 37  ? 0.3961 0.2683 0.4576 0.1296  -0.1283 0.0328  37  THR   A CB  
331  O  OG1 . THR   A 37  ? 0.5655 0.2878 0.4597 0.1588  -0.0352 0.0751  37  THR   A OG1 
332  C  CG2 . THR   A 37  ? 0.4718 0.3592 0.2087 0.0871  -0.0681 0.0476  37  THR   A CG2 
333  N  N   . ALA   A 38  ? 0.3640 0.2201 0.1482 0.1046  0.0331  0.0458  38  ALA   A N   
334  C  CA  . ALA   A 38  ? 0.2999 0.2010 0.1482 0.0833  0.0329  0.0307  38  ALA   A CA  
335  C  C   . ALA   A 38  ? 0.3242 0.2219 0.2176 0.0648  0.0710  0.0380  38  ALA   A C   
336  O  O   . ALA   A 38  ? 0.4114 0.2462 0.2813 0.0630  0.1188  0.0519  38  ALA   A O   
337  C  CB  . ALA   A 38  ? 0.3045 0.1955 0.1782 0.0460  0.0083  0.0226  38  ALA   A CB  
338  N  N   . LYS   A 39  ? 0.3335 0.2386 0.1708 0.1132  0.0061  -0.0013 39  LYS   A N   
339  C  CA  . LYS   A 39  ? 0.3384 0.3492 0.1662 0.1502  -0.0072 -0.0027 39  LYS   A CA  
340  C  C   . LYS   A 39  ? 0.2754 0.2646 0.1342 0.0858  0.0283  0.0132  39  LYS   A C   
341  O  O   . LYS   A 39  ? 0.2561 0.2718 0.1436 0.0638  0.0036  0.0141  39  LYS   A O   
342  C  CB  . LYS   A 39  ? 0.4173 0.4563 0.2154 0.1844  -0.0758 -0.0978 39  LYS   A CB  
343  C  CG  . LYS   A 39  ? 0.3387 0.4370 0.2089 0.1363  0.0006  -0.0013 39  LYS   A CG  
344  C  CD  . LYS   A 39  ? 0.2777 0.3893 0.2875 0.0977  -0.0161 0.0750  39  LYS   A CD  
345  C  CE  . LYS   A 39  ? 0.3441 0.4447 0.2581 0.0765  0.0017  0.0543  39  LYS   A CE  
346  N  NZ  . LYS   A 39  ? 0.2942 0.6009 0.3334 0.1513  0.0413  0.1849  39  LYS   A NZ  
347  N  N   . TYR   A 40  ? 0.3304 0.2728 0.1625 0.0752  0.0377  0.0408  40  TYR   A N   
348  C  CA  . TYR   A 40  ? 0.2846 0.2287 0.2009 0.0114  0.0547  0.0135  40  TYR   A CA  
349  C  C   . TYR   A 40  ? 0.2552 0.2533 0.1412 0.0223  0.0361  0.0160  40  TYR   A C   
350  O  O   . TYR   A 40  ? 0.3037 0.3262 0.1483 0.0771  0.0289  -0.0062 40  TYR   A O   
351  C  CB  . TYR   A 40  ? 0.3267 0.3314 0.2494 -0.0413 0.0845  0.0422  40  TYR   A CB  
352  C  CG  . TYR   A 40  ? 0.3312 0.3769 0.2163 -0.0445 0.0740  0.0497  40  TYR   A CG  
353  C  CD1 . TYR   A 40  ? 0.3127 0.3143 0.2200 -0.0562 0.0279  0.0225  40  TYR   A CD1 
354  C  CD2 . TYR   A 40  ? 0.3640 0.4708 0.2420 0.0498  0.0888  0.0412  40  TYR   A CD2 
355  C  CE1 . TYR   A 40  ? 0.2786 0.5289 0.2539 -0.0248 0.0450  0.0031  40  TYR   A CE1 
356  C  CE2 . TYR   A 40  ? 0.3146 0.6633 0.2624 0.0656  0.0696  0.0261  40  TYR   A CE2 
357  C  CZ  . TYR   A 40  ? 0.2915 0.6202 0.2636 -0.0142 0.0649  0.0367  40  TYR   A CZ  
358  O  OH  . TYR   A 40  ? 0.2799 0.8131 0.4435 0.0709  0.0904  -0.0666 40  TYR   A OH  
359  N  N   . ASP   A 41  ? 0.2628 0.2215 0.1856 0.0504  0.0205  -0.0047 41  ASP   A N   
360  C  CA  . ASP   A 41  ? 0.3066 0.2136 0.1867 0.0546  0.0083  -0.0187 41  ASP   A CA  
361  C  C   . ASP   A 41  ? 0.3363 0.4004 0.1979 0.1185  0.0244  -0.0250 41  ASP   A C   
362  O  O   . ASP   A 41  ? 0.2933 0.2987 0.2240 0.0675  0.0103  -0.0076 41  ASP   A O   
363  C  CB  . ASP   A 41  ? 0.3764 0.2257 0.2406 -0.0012 -0.0258 -0.0074 41  ASP   A CB  
364  C  CG  . ASP   A 41  ? 0.3767 0.2334 0.3640 -0.0069 -0.0331 -0.0294 41  ASP   A CG  
365  O  OD1 . ASP   A 41  ? 0.5056 0.3235 0.2978 0.1465  -0.0694 -0.0884 41  ASP   A OD1 
366  O  OD2 . ASP   A 41  ? 0.4591 0.2800 0.4362 -0.0652 -0.0275 -0.0042 41  ASP   A OD2 
367  N  N   . PRO   A 42  ? 0.4137 0.4823 0.1983 0.1741  0.0497  -0.0020 42  PRO   A N   
368  C  CA  . PRO   A 42  ? 0.3789 0.5618 0.2925 0.1621  0.0908  0.0449  42  PRO   A CA  
369  C  C   . PRO   A 42  ? 0.4028 0.5459 0.2593 0.1887  0.1045  0.0125  42  PRO   A C   
370  O  O   . PRO   A 42  ? 0.4141 0.7288 0.4225 0.2674  0.1061  0.0302  42  PRO   A O   
371  C  CB  . PRO   A 42  ? 0.4814 0.7355 0.3008 0.1565  0.1453  0.0282  42  PRO   A CB  
372  C  CG  . PRO   A 42  ? 0.4554 0.6141 0.2843 0.2157  0.1200  0.0044  42  PRO   A CG  
373  C  CD  . PRO   A 42  ? 0.4526 0.4807 0.1867 0.2033  0.0753  0.0066  42  PRO   A CD  
374  N  N   . SER   A 43  ? 0.4367 0.4421 0.2623 0.2255  0.0682  -0.0171 43  SER   A N   
375  C  CA  . SER   A 43  ? 0.6883 0.3986 0.2391 0.2965  -0.0217 -0.0751 43  SER   A CA  
376  C  C   . SER   A 43  ? 0.6092 0.3342 0.2157 0.2222  -0.0347 -0.0501 43  SER   A C   
377  O  O   . SER   A 43  ? 0.6846 0.3555 0.3333 0.2762  -0.0895 -0.0286 43  SER   A O   
378  C  CB  . SER   A 43  ? 0.8823 0.5957 0.2346 0.1925  -0.0294 -0.1504 43  SER   A CB  
379  O  OG  . SER   A 43  ? 0.8123 0.2559 0.6067 0.0249  -0.0819 -0.1348 43  SER   A OG  
380  N  N   . LEU   A 44  ? 0.4440 0.3599 0.2298 0.1810  -0.0243 -0.0528 44  LEU   A N   
381  C  CA  . LEU   A 44  ? 0.3187 0.2620 0.2494 0.0824  -0.0243 0.0255  44  LEU   A CA  
382  C  C   . LEU   A 44  ? 0.2779 0.3411 0.2679 0.0664  0.0071  0.0104  44  LEU   A C   
383  O  O   . LEU   A 44  ? 0.2604 0.5007 0.3799 0.0453  0.0233  0.1305  44  LEU   A O   
384  C  CB  . LEU   A 44  ? 0.2750 0.2846 0.2117 0.0298  -0.0201 -0.0177 44  LEU   A CB  
385  C  CG  . LEU   A 44  ? 0.2542 0.2167 0.2055 0.0187  -0.0203 0.0249  44  LEU   A CG  
386  C  CD1 . LEU   A 44  ? 0.2420 0.2503 0.2548 0.0303  0.0139  -0.0041 44  LEU   A CD1 
387  C  CD2 . LEU   A 44  ? 0.3019 0.2046 0.2265 -0.0003 -0.0212 0.0178  44  LEU   A CD2 
388  N  N   . LYS   A 45  ? 0.2917 0.2535 0.2810 0.0565  -0.0328 -0.0089 45  LYS   A N   
389  C  CA  . LYS   A 45  ? 0.2758 0.2187 0.3266 0.0171  -0.0219 -0.0403 45  LYS   A CA  
390  C  C   . LYS   A 45  ? 0.2358 0.2065 0.2755 0.0277  0.0012  0.0000  45  LYS   A C   
391  O  O   . LYS   A 45  ? 0.2240 0.2197 0.2921 0.0249  0.0127  -0.0038 45  LYS   A O   
392  C  CB  . LYS   A 45  ? 0.3419 0.2425 0.3440 0.0933  -0.0075 -0.0059 45  LYS   A CB  
393  C  CG  . LYS   A 45  ? 0.4620 0.2750 0.3923 0.1090  -0.0810 -0.0431 45  LYS   A CG  
394  C  CD  . LYS   A 45  ? 0.6047 0.3325 0.6666 0.0537  0.0103  -0.0545 45  LYS   A CD  
395  C  CE  . LYS   A 45  ? 0.8320 0.4594 0.7129 0.2002  -0.0688 -0.1279 45  LYS   A CE  
396  N  NZ  . LYS   A 45  ? 0.9872 0.4097 1.1349 0.1446  0.1943  -0.2174 45  LYS   A NZ  
397  N  N   . PRO   A 46  ? 0.2086 0.2363 0.2743 -0.0127 0.0226  0.0140  46  PRO   A N   
398  C  CA  . PRO   A 46  ? 0.2165 0.2509 0.2454 -0.0105 0.0027  0.0122  46  PRO   A CA  
399  C  C   . PRO   A 46  ? 0.1812 0.1752 0.2981 0.0055  0.0072  0.0154  46  PRO   A C   
400  O  O   . PRO   A 46  ? 0.1907 0.1901 0.2966 -0.0046 -0.0079 0.0044  46  PRO   A O   
401  C  CB  . PRO   A 46  ? 0.2026 0.2782 0.3138 -0.0285 0.0141  0.0096  46  PRO   A CB  
402  C  CG  . PRO   A 46  ? 0.2316 0.4030 0.3685 -0.0362 0.0710  -0.0678 46  PRO   A CG  
403  C  CD  . PRO   A 46  ? 0.2552 0.3028 0.3229 0.0186  0.0495  -0.0771 46  PRO   A CD  
404  N  N   A LEU   A 47  ? 0.1976 0.2352 0.2587 -0.0004 0.0065  0.0218  47  LEU   A N   
405  N  N   B LEU   A 47  ? 0.1821 0.2179 0.2995 0.0363  0.0131  0.0411  47  LEU   A N   
406  C  CA  A LEU   A 47  ? 0.1714 0.2128 0.2310 -0.0223 -0.0092 -0.0073 47  LEU   A CA  
407  C  CA  B LEU   A 47  ? 0.1832 0.1985 0.3009 0.0093  0.0152  0.0284  47  LEU   A CA  
408  C  C   A LEU   A 47  ? 0.1857 0.1975 0.2481 -0.0226 -0.0267 -0.0020 47  LEU   A C   
409  C  C   B LEU   A 47  ? 0.1637 0.2053 0.3316 -0.0013 0.0128  0.0434  47  LEU   A C   
410  O  O   A LEU   A 47  ? 0.1449 0.2229 0.2183 -0.0208 -0.0002 0.0058  47  LEU   A O   
411  O  O   B LEU   A 47  ? 0.1815 0.2420 0.2928 -0.0364 0.0381  0.0027  47  LEU   A O   
412  C  CB  A LEU   A 47  ? 0.1620 0.2335 0.2605 -0.0241 0.0086  -0.0126 47  LEU   A CB  
413  C  CB  B LEU   A 47  ? 0.2420 0.2177 0.3036 0.0433  0.0048  0.0185  47  LEU   A CB  
414  C  CG  A LEU   A 47  ? 0.1971 0.1902 0.2348 -0.0325 0.0100  -0.0269 47  LEU   A CG  
415  C  CG  B LEU   A 47  ? 0.2026 0.2121 0.3107 0.0120  -0.0212 -0.0345 47  LEU   A CG  
416  C  CD1 A LEU   A 47  ? 0.1828 0.1987 0.2273 -0.0234 -0.0305 0.0274  47  LEU   A CD1 
417  C  CD1 B LEU   A 47  ? 0.2020 0.2679 0.2978 0.0282  -0.0173 -0.0508 47  LEU   A CD1 
418  C  CD2 A LEU   A 47  ? 0.2000 0.1990 0.2107 0.0389  -0.0249 0.0151  47  LEU   A CD2 
419  C  CD2 B LEU   A 47  ? 0.2262 0.2381 0.2596 0.0097  -0.0559 -0.0704 47  LEU   A CD2 
420  N  N   . SER   A 48  ? 0.1764 0.2107 0.2606 -0.0182 -0.0026 0.0294  48  SER   A N   
421  C  CA  . SER   A 48  ? 0.2036 0.2175 0.2477 -0.0353 -0.0066 0.0262  48  SER   A CA  
422  C  C   . SER   A 48  ? 0.1756 0.2201 0.2326 -0.0204 -0.0035 0.0031  48  SER   A C   
423  O  O   . SER   A 48  ? 0.2028 0.2337 0.2616 -0.0494 0.0094  -0.0114 48  SER   A O   
424  C  CB  . SER   A 48  ? 0.2133 0.2480 0.2662 0.0054  0.0003  0.0253  48  SER   A CB  
425  O  OG  . SER   A 48  ? 0.3025 0.2692 0.3366 0.0330  -0.0201 0.0644  48  SER   A OG  
426  N  N   . VAL   A 49  ? 0.2332 0.2381 0.2174 -0.0390 -0.0173 0.0190  49  VAL   A N   
427  C  CA  . VAL   A 49  ? 0.2625 0.2030 0.2274 -0.0662 -0.0018 0.0055  49  VAL   A CA  
428  C  C   . VAL   A 49  ? 0.2528 0.2466 0.2678 -0.0700 -0.0238 0.0042  49  VAL   A C   
429  O  O   . VAL   A 49  ? 0.2756 0.3463 0.3101 -0.1347 -0.0567 0.0272  49  VAL   A O   
430  C  CB  . VAL   A 49  ? 0.3039 0.2171 0.2518 -0.0655 0.0208  -0.0055 49  VAL   A CB  
431  C  CG1 . VAL   A 49  ? 0.4428 0.2801 0.2785 -0.0699 0.0644  0.0127  49  VAL   A CG1 
432  C  CG2 . VAL   A 49  ? 0.3062 0.2190 0.3102 -0.0597 0.0088  -0.0036 49  VAL   A CG2 
433  N  N   . SER   A 50  ? 0.2269 0.2855 0.2550 -0.0677 -0.0332 0.0154  50  SER   A N   
434  C  CA  . SER   A 50  ? 0.2282 0.2953 0.3086 -0.0343 -0.0392 0.0109  50  SER   A CA  
435  C  C   . SER   A 50  ? 0.1967 0.3000 0.2742 -0.0334 -0.0650 0.0171  50  SER   A C   
436  O  O   . SER   A 50  ? 0.2262 0.2963 0.2951 -0.0406 -0.0549 0.0284  50  SER   A O   
437  C  CB  . SER   A 50  ? 0.3277 0.3241 0.3429 0.0044  -0.0409 -0.0051 50  SER   A CB  
438  O  OG  . SER   A 50  ? 0.3157 0.4369 0.4318 0.0066  -0.0006 -0.0500 50  SER   A OG  
439  N  N   . TYR   A 51  ? 0.2218 0.2408 0.2922 -0.0370 -0.0506 0.0237  51  TYR   A N   
440  C  CA  . TYR   A 51  ? 0.2236 0.2447 0.2866 -0.0081 -0.0578 0.0469  51  TYR   A CA  
441  C  C   . TYR   A 51  ? 0.2388 0.2425 0.3257 -0.0164 -0.0623 0.0721  51  TYR   A C   
442  O  O   . TYR   A 51  ? 0.2871 0.2795 0.3141 -0.0013 -0.0855 0.0757  51  TYR   A O   
443  C  CB  . TYR   A 51  ? 0.2228 0.2136 0.2847 -0.0361 -0.0850 0.0391  51  TYR   A CB  
444  C  CG  . TYR   A 51  ? 0.2231 0.2140 0.2215 -0.0493 -0.0580 0.0331  51  TYR   A CG  
445  C  CD1 . TYR   A 51  ? 0.2301 0.1875 0.2958 -0.0396 -0.0561 0.0178  51  TYR   A CD1 
446  C  CD2 . TYR   A 51  ? 0.2109 0.2084 0.2185 -0.0321 -0.0099 0.0233  51  TYR   A CD2 
447  C  CE1 . TYR   A 51  ? 0.2118 0.1538 0.2255 -0.0359 -0.0297 0.0230  51  TYR   A CE1 
448  C  CE2 . TYR   A 51  ? 0.2301 0.1681 0.1993 -0.0487 -0.0417 -0.0013 51  TYR   A CE2 
449  C  CZ  . TYR   A 51  ? 0.2134 0.1483 0.2136 -0.0375 -0.0309 0.0006  51  TYR   A CZ  
450  O  OH  . TYR   A 51  ? 0.2076 0.1574 0.2188 -0.0287 -0.0475 0.0076  51  TYR   A OH  
451  N  N   . ASP   A 52  ? 0.2230 0.3540 0.3352 -0.0271 -0.0672 0.0986  52  ASP   A N   
452  C  CA  . ASP   A 52  ? 0.2493 0.3561 0.3549 -0.0467 -0.0842 0.1176  52  ASP   A CA  
453  C  C   . ASP   A 52  ? 0.2645 0.2904 0.3554 -0.0074 -0.0945 0.1008  52  ASP   A C   
454  O  O   . ASP   A 52  ? 0.3792 0.4189 0.3576 0.0212  -0.1199 0.0938  52  ASP   A O   
455  C  CB  . ASP   A 52  ? 0.2310 0.5764 0.5008 -0.0025 -0.0908 0.1646  52  ASP   A CB  
456  C  CG  . ASP   A 52  ? 0.3565 0.5086 0.7737 0.0880  0.0908  0.0798  52  ASP   A CG  
457  O  OD1 . ASP   A 52  ? 0.4123 0.5199 0.8004 0.0346  0.1028  0.1650  52  ASP   A OD1 
458  O  OD2 . ASP   A 52  ? 0.4490 0.5153 0.9534 0.0251  -0.0352 0.2296  52  ASP   A OD2 
459  N  N   . GLN   A 53  ? 0.2451 0.3216 0.4167 -0.0140 -0.0564 0.0807  53  GLN   A N   
460  C  CA  . GLN   A 53  ? 0.2753 0.3164 0.4625 0.0361  -0.0173 0.0903  53  GLN   A CA  
461  C  C   . GLN   A 53  ? 0.2813 0.2357 0.3080 0.0100  -0.0331 0.0450  53  GLN   A C   
462  O  O   . GLN   A 53  ? 0.3009 0.2587 0.3543 -0.0222 -0.0540 0.0647  53  GLN   A O   
463  C  CB  . GLN   A 53  ? 0.3790 0.3479 0.5946 0.1495  -0.0752 0.0682  53  GLN   A CB  
464  C  CG  . GLN   A 53  ? 0.3956 0.4731 0.6912 0.0939  0.0687  0.1112  53  GLN   A CG  
465  C  CD  . GLN   A 53  ? 0.4127 0.6862 0.7841 0.2199  -0.0100 0.1210  53  GLN   A CD  
466  O  OE1 . GLN   A 53  ? 0.4707 0.8169 0.7735 0.2669  -0.0368 0.1323  53  GLN   A OE1 
467  N  NE2 . GLN   A 53  ? 0.5082 0.7892 0.5353 0.0825  -0.0185 0.2194  53  GLN   A NE2 
468  N  N   . ALA   A 54  ? 0.2814 0.2182 0.3370 -0.0273 -0.0871 0.0240  54  ALA   A N   
469  C  CA  . ALA   A 54  ? 0.2792 0.1844 0.2341 -0.0199 -0.0661 -0.0041 54  ALA   A CA  
470  C  C   . ALA   A 54  ? 0.3128 0.2474 0.2393 -0.0332 -0.0537 -0.0252 54  ALA   A C   
471  O  O   . ALA   A 54  ? 0.3513 0.3652 0.2924 -0.0707 -0.0923 -0.0476 54  ALA   A O   
472  C  CB  . ALA   A 54  ? 0.2922 0.1971 0.2927 -0.0163 -0.0491 0.0263  54  ALA   A CB  
473  N  N   . THR   A 55  ? 0.2573 0.1914 0.2359 0.0232  -0.0537 0.0234  55  THR   A N   
474  C  CA  . THR   A 55  ? 0.2911 0.2086 0.2394 0.0381  -0.0498 0.0450  55  THR   A CA  
475  C  C   . THR   A 55  ? 0.2940 0.1662 0.1678 0.0006  -0.0688 0.0307  55  THR   A C   
476  O  O   . THR   A 55  ? 0.2816 0.1465 0.2276 0.0061  -0.0716 0.0331  55  THR   A O   
477  C  CB  . THR   A 55  ? 0.4117 0.2229 0.2833 0.0368  -0.0521 0.0660  55  THR   A CB  
478  O  OG1 . THR   A 55  ? 0.4128 0.2059 0.5083 0.0181  -0.1637 0.0517  55  THR   A OG1 
479  C  CG2 . THR   A 55  ? 0.4564 0.2985 0.2966 0.0961  -0.0385 0.0917  55  THR   A CG2 
480  N  N   . SER   A 56  ? 0.3174 0.1575 0.1793 0.0173  -0.0713 0.0410  56  SER   A N   
481  C  CA  . SER   A 56  ? 0.3288 0.1463 0.1693 0.0032  -0.0787 0.0152  56  SER   A CA  
482  C  C   . SER   A 56  ? 0.3609 0.1474 0.1928 0.0293  -0.0839 0.0308  56  SER   A C   
483  O  O   . SER   A 56  ? 0.3636 0.1923 0.2041 0.0344  -0.0822 0.0515  56  SER   A O   
484  C  CB  . SER   A 56  ? 0.4019 0.1490 0.1592 -0.0383 -0.0925 0.0178  56  SER   A CB  
485  O  OG  . SER   A 56  ? 0.3776 0.1755 0.2001 -0.0346 -0.1095 0.0366  56  SER   A OG  
486  N  N   . LEU   A 57  ? 0.3263 0.1430 0.1731 0.0293  -0.0495 0.0204  57  LEU   A N   
487  C  CA  . LEU   A 57  ? 0.4023 0.1370 0.1961 0.0402  -0.0304 0.0162  57  LEU   A CA  
488  C  C   . LEU   A 57  ? 0.3747 0.1332 0.1590 0.0270  -0.0270 0.0345  57  LEU   A C   
489  O  O   . LEU   A 57  ? 0.3814 0.1845 0.1588 0.0425  -0.0318 0.0378  57  LEU   A O   
490  C  CB  . LEU   A 57  ? 0.4236 0.1655 0.2531 0.0081  -0.0087 0.0175  57  LEU   A CB  
491  C  CG  . LEU   A 57  ? 0.5792 0.1562 0.2789 0.0464  -0.0255 -0.0027 57  LEU   A CG  
492  C  CD1 . LEU   A 57  ? 0.7741 0.1970 0.3646 -0.0902 -0.0258 0.0156  57  LEU   A CD1 
493  C  CD2 . LEU   A 57  ? 0.7008 0.2229 0.3556 0.1383  -0.0444 0.0373  57  LEU   A CD2 
494  N  N   . ARG   A 58  ? 0.2965 0.1529 0.1949 0.0325  -0.0138 0.0220  58  ARG   A N   
495  C  CA  . ARG   A 58  ? 0.2924 0.1958 0.1761 0.0249  -0.0047 0.0784  58  ARG   A CA  
496  C  C   . ARG   A 58  ? 0.3112 0.1496 0.1552 -0.0072 -0.0195 0.0238  58  ARG   A C   
497  O  O   . ARG   A 58  ? 0.3352 0.1716 0.1383 0.0300  -0.0124 0.0249  58  ARG   A O   
498  C  CB  . ARG   A 58  ? 0.3229 0.2081 0.2485 0.0214  -0.0181 0.0441  58  ARG   A CB  
499  C  CG  . ARG   A 58  ? 0.2522 0.2470 0.3168 -0.0179 0.0070  0.1002  58  ARG   A CG  
500  C  CD  . ARG   A 58  ? 0.3632 0.2768 0.3066 -0.0660 -0.0267 0.0998  58  ARG   A CD  
501  N  NE  . ARG   A 58  ? 0.2758 0.2225 0.3197 -0.0217 0.0010  0.0541  58  ARG   A NE  
502  C  CZ  . ARG   A 58  ? 0.2717 0.2544 0.3740 -0.0429 0.0331  0.0949  58  ARG   A CZ  
503  N  NH1 . ARG   A 58  ? 0.3138 0.2852 0.3468 -0.0827 0.0223  0.0527  58  ARG   A NH1 
504  N  NH2 . ARG   A 58  ? 0.2706 0.2194 0.3578 -0.0095 0.0465  0.0674  58  ARG   A NH2 
505  N  N   . ILE   A 59  ? 0.3005 0.1529 0.1350 0.0107  -0.0247 0.0175  59  ILE   A N   
506  C  CA  . ILE   A 59  ? 0.2836 0.1552 0.1749 0.0183  -0.0206 0.0205  59  ILE   A CA  
507  C  C   . ILE   A 59  ? 0.2986 0.1438 0.1252 0.0120  -0.0428 0.0146  59  ILE   A C   
508  O  O   . ILE   A 59  ? 0.3228 0.2328 0.1237 0.0237  -0.0274 0.0266  59  ILE   A O   
509  C  CB  . ILE   A 59  ? 0.3282 0.1537 0.1309 0.0127  -0.0367 0.0217  59  ILE   A CB  
510  C  CG1 . ILE   A 59  ? 0.3142 0.1446 0.1617 0.0040  -0.0440 0.0347  59  ILE   A CG1 
511  C  CG2 . ILE   A 59  ? 0.3937 0.1755 0.1327 0.0163  -0.0653 0.0044  59  ILE   A CG2 
512  C  CD1 . ILE   A 59  ? 0.3744 0.1377 0.1878 -0.0070 -0.0541 0.0078  59  ILE   A CD1 
513  N  N   . LEU   A 60  ? 0.2649 0.1729 0.1570 -0.0142 -0.0370 0.0184  60  LEU   A N   
514  C  CA  . LEU   A 60  ? 0.2739 0.1552 0.1644 -0.0006 -0.0381 0.0316  60  LEU   A CA  
515  C  C   . LEU   A 60  ? 0.2754 0.1463 0.1324 -0.0012 -0.0055 0.0052  60  LEU   A C   
516  O  O   . LEU   A 60  ? 0.2722 0.1713 0.1375 -0.0078 -0.0044 0.0220  60  LEU   A O   
517  C  CB  . LEU   A 60  ? 0.3015 0.1333 0.2715 -0.0062 -0.0391 0.0125  60  LEU   A CB  
518  C  CG  . LEU   A 60  ? 0.3080 0.1492 0.1999 -0.0108 -0.0333 0.0184  60  LEU   A CG  
519  C  CD1 . LEU   A 60  ? 0.3345 0.1844 0.2341 -0.0569 -0.0150 0.0373  60  LEU   A CD1 
520  C  CD2 . LEU   A 60  ? 0.3251 0.1401 0.3187 -0.0390 -0.0333 -0.0179 60  LEU   A CD2 
521  N  N   . ASN   A 61  ? 0.2597 0.1312 0.1461 -0.0108 -0.0006 0.0015  61  ASN   A N   
522  C  CA  . ASN   A 61  ? 0.2481 0.1694 0.1442 -0.0127 -0.0008 -0.0233 61  ASN   A CA  
523  C  C   . ASN   A 61  ? 0.2445 0.1732 0.1243 -0.0265 0.0047  0.0036  61  ASN   A C   
524  O  O   . ASN   A 61  ? 0.3063 0.1735 0.1535 -0.0423 0.0054  0.0392  61  ASN   A O   
525  C  CB  . ASN   A 61  ? 0.2881 0.1612 0.1453 -0.0092 0.0239  0.0002  61  ASN   A CB  
526  C  CG  . ASN   A 61  ? 0.2700 0.1562 0.1391 -0.0245 0.0003  -0.0223 61  ASN   A CG  
527  O  OD1 . ASN   A 61  ? 0.2682 0.1814 0.1544 -0.0258 -0.0022 0.0065  61  ASN   A OD1 
528  N  ND2 . ASN   A 61  ? 0.3015 0.1560 0.1567 -0.0322 0.0281  -0.0216 61  ASN   A ND2 
529  N  N   . ASN   A 62  ? 0.2922 0.1456 0.1294 -0.0414 -0.0042 0.0089  62  ASN   A N   
530  C  CA  . ASN   A 62  ? 0.3125 0.1586 0.1778 -0.0397 -0.0563 0.0136  62  ASN   A CA  
531  C  C   . ASN   A 62  ? 0.2762 0.1854 0.1978 -0.0741 -0.0058 0.0251  62  ASN   A C   
532  O  O   . ASN   A 62  ? 0.3271 0.2477 0.2201 -0.1253 -0.0199 0.0111  62  ASN   A O   
533  C  CB  . ASN   A 62  ? 0.3569 0.1852 0.2111 -0.0370 -0.0722 -0.0206 62  ASN   A CB  
534  C  CG  . ASN   A 62  ? 0.3431 0.2195 0.1845 -0.0565 -0.0144 -0.0344 62  ASN   A CG  
535  O  OD1 . ASN   A 62  ? 0.3449 0.1773 0.1817 -0.0575 0.0398  -0.0043 62  ASN   A OD1 
536  N  ND2 . ASN   A 62  ? 0.4238 0.2613 0.2217 -0.1125 0.0220  -0.0792 62  ASN   A ND2 
537  N  N   . GLY   A 63  ? 0.2714 0.1903 0.1800 -0.0337 0.0198  0.0234  63  GLY   A N   
538  C  CA  . GLY   A 63  ? 0.2552 0.1912 0.1561 -0.0447 0.0237  0.0030  63  GLY   A CA  
539  C  C   . GLY   A 63  ? 0.2756 0.1631 0.1988 -0.0410 0.0083  0.0051  63  GLY   A C   
540  O  O   . GLY   A 63  ? 0.2751 0.2025 0.2913 -0.0247 0.0308  0.0352  63  GLY   A O   
541  N  N   . HIS   A 64  ? 0.2460 0.1842 0.1612 -0.0545 0.0071  0.0106  64  HIS   A N   
542  C  CA  . HIS   A 64  ? 0.2438 0.2743 0.2018 -0.0494 -0.0125 0.0832  64  HIS   A CA  
543  C  C   . HIS   A 64  ? 0.2307 0.2125 0.1914 -0.0359 0.0079  0.0466  64  HIS   A C   
544  O  O   . HIS   A 64  ? 0.2532 0.2189 0.2323 -0.0186 0.0095  0.0776  64  HIS   A O   
545  C  CB  . HIS   A 64  ? 0.3054 0.4108 0.1706 -0.1468 -0.0457 0.0888  64  HIS   A CB  
546  C  CG  . HIS   A 64  ? 0.2933 0.4991 0.2145 -0.1492 0.0171  0.0377  64  HIS   A CG  
547  N  ND1 . HIS   A 64  ? 0.3053 0.4626 0.2304 -0.1207 -0.0140 0.0359  64  HIS   A ND1 
548  C  CD2 . HIS   A 64  ? 0.3424 0.5083 0.2042 -0.2184 0.0337  -0.0442 64  HIS   A CD2 
549  C  CE1 . HIS   A 64  ? 0.2721 0.4333 0.2802 -0.0983 0.0236  -0.0513 64  HIS   A CE1 
550  N  NE2 . HIS   A 64  ? 0.3112 0.4135 0.2495 -0.1027 0.0321  -0.0375 64  HIS   A NE2 
551  N  N   . ALA   A 65  ? 0.2312 0.1713 0.1571 -0.0389 0.0083  0.0065  65  ALA   A N   
552  C  CA  . ALA   A 65  ? 0.2384 0.1860 0.1394 -0.0390 0.0117  0.0184  65  ALA   A CA  
553  C  C   . ALA   A 65  ? 0.2508 0.1591 0.1128 -0.0121 0.0141  0.0040  65  ALA   A C   
554  O  O   . ALA   A 65  ? 0.2702 0.1948 0.1627 -0.0504 0.0067  0.0325  65  ALA   A O   
555  C  CB  . ALA   A 65  ? 0.2593 0.1727 0.1480 -0.0269 0.0092  0.0089  65  ALA   A CB  
556  N  N   . PHE   A 66  ? 0.2362 0.1834 0.1745 0.0111  0.0201  0.0337  66  PHE   A N   
557  C  CA  . PHE   A 66  ? 0.3148 0.2159 0.1425 0.0476  -0.0130 0.0325  66  PHE   A CA  
558  C  C   . PHE   A 66  ? 0.2623 0.2251 0.1550 0.0298  -0.0019 0.0370  66  PHE   A C   
559  O  O   . PHE   A 66  ? 0.2645 0.2187 0.1390 -0.0263 -0.0077 0.0070  66  PHE   A O   
560  C  CB  . PHE   A 66  ? 0.2983 0.3364 0.1471 0.0220  -0.0011 0.0181  66  PHE   A CB  
561  C  CG  . PHE   A 66  ? 0.2818 0.2701 0.1424 0.0210  -0.0380 -0.0332 66  PHE   A CG  
562  C  CD1 . PHE   A 66  ? 0.2726 0.2778 0.1474 0.0298  -0.0376 -0.0184 66  PHE   A CD1 
563  C  CD2 . PHE   A 66  ? 0.2861 0.2745 0.1658 0.0212  -0.0418 -0.0653 66  PHE   A CD2 
564  C  CE1 . PHE   A 66  ? 0.3019 0.1992 0.1747 0.0221  -0.0740 -0.0104 66  PHE   A CE1 
565  C  CE2 . PHE   A 66  ? 0.3273 0.2208 0.1750 0.0192  -0.0578 -0.0456 66  PHE   A CE2 
566  C  CZ  . PHE   A 66  ? 0.2914 0.2033 0.1890 0.0261  -0.0807 -0.0392 66  PHE   A CZ  
567  N  N   . ASN   A 67  ? 0.3187 0.2605 0.1744 0.0994  0.0040  0.0740  67  ASN   A N   
568  C  CA  . ASN   A 67  ? 0.2828 0.2354 0.1430 0.0541  -0.0065 0.0407  67  ASN   A CA  
569  C  C   . ASN   A 67  ? 0.2847 0.1741 0.1083 0.0126  -0.0172 0.0136  67  ASN   A C   
570  O  O   . ASN   A 67  ? 0.2781 0.2251 0.1251 -0.0128 -0.0100 0.0423  67  ASN   A O   
571  C  CB  . ASN   A 67  ? 0.2767 0.3732 0.1841 -0.0627 -0.0221 0.0596  67  ASN   A CB  
572  C  CG  . ASN   A 67  ? 0.2756 0.4889 0.1874 -0.0015 0.0163  0.0858  67  ASN   A CG  
573  O  OD1 . ASN   A 67  ? 0.2613 0.2122 0.1731 0.0006  -0.0207 -0.0058 67  ASN   A OD1 
574  N  ND2 . ASN   A 67  ? 0.4297 0.4565 0.2613 -0.0926 0.0467  -0.0525 67  ASN   A ND2 
575  N  N   . VAL   A 68  ? 0.2764 0.1493 0.1375 0.0317  -0.0105 0.0161  68  VAL   A N   
576  C  CA  . VAL   A 68  ? 0.2848 0.1491 0.1327 0.0458  -0.0245 0.0210  68  VAL   A CA  
577  C  C   . VAL   A 68  ? 0.2858 0.1381 0.1375 0.0175  -0.0310 0.0219  68  VAL   A C   
578  O  O   . VAL   A 68  ? 0.2936 0.1283 0.1336 0.0162  -0.0230 0.0269  68  VAL   A O   
579  C  CB  . VAL   A 68  ? 0.2821 0.1270 0.1929 0.0149  -0.0348 0.0121  68  VAL   A CB  
580  C  CG1 . VAL   A 68  ? 0.2964 0.1987 0.1615 0.0328  -0.0629 -0.0011 68  VAL   A CG1 
581  C  CG2 . VAL   A 68  ? 0.2910 0.1722 0.1682 0.0030  -0.0119 -0.0150 68  VAL   A CG2 
582  N  N   . GLU   A 69  ? 0.3194 0.1330 0.1362 0.0234  -0.0199 0.0218  69  GLU   A N   
583  C  CA  . GLU   A 69  ? 0.3039 0.1295 0.1562 0.0098  -0.0103 0.0109  69  GLU   A CA  
584  C  C   . GLU   A 69  ? 0.3299 0.1304 0.1600 0.0277  -0.0474 0.0347  69  GLU   A C   
585  O  O   . GLU   A 69  ? 0.3674 0.1409 0.1878 0.0287  -0.0829 0.0042  69  GLU   A O   
586  C  CB  . GLU   A 69  ? 0.2928 0.1766 0.2279 0.0198  0.0432  0.0122  69  GLU   A CB  
587  C  CG  . GLU   A 69  ? 0.2556 0.2407 0.2827 -0.0311 0.0330  0.0026  69  GLU   A CG  
588  C  CD  . GLU   A 69  ? 0.2912 0.2226 0.3061 0.0052  0.0413  0.0324  69  GLU   A CD  
589  O  OE1 . GLU   A 69  ? 0.3249 0.2258 0.3144 -0.0040 0.0190  0.0436  69  GLU   A OE1 
590  O  OE2 . GLU   A 69  ? 0.3055 0.2536 0.4710 -0.0035 0.0855  0.0806  69  GLU   A OE2 
591  N  N   . PHE   A 70  ? 0.2908 0.1525 0.1680 0.0157  -0.0236 0.0138  70  PHE   A N   
592  C  CA  . PHE   A 70  ? 0.2559 0.1132 0.2129 0.0111  -0.0518 0.0280  70  PHE   A CA  
593  C  C   . PHE   A 70  ? 0.3075 0.1248 0.2025 0.0105  -0.0394 0.0276  70  PHE   A C   
594  O  O   . PHE   A 70  ? 0.3041 0.1307 0.2548 0.0010  -0.0591 0.0319  70  PHE   A O   
595  C  CB  . PHE   A 70  ? 0.2920 0.1331 0.1801 -0.0024 -0.0469 0.0234  70  PHE   A CB  
596  C  CG  . PHE   A 70  ? 0.2637 0.1220 0.1735 0.0124  -0.0328 0.0339  70  PHE   A CG  
597  C  CD1 . PHE   A 70  ? 0.2922 0.1307 0.1796 0.0281  -0.0109 0.0442  70  PHE   A CD1 
598  C  CD2 . PHE   A 70  ? 0.2719 0.1263 0.1869 0.0100  -0.0617 0.0228  70  PHE   A CD2 
599  C  CE1 . PHE   A 70  ? 0.2869 0.1407 0.1907 0.0286  -0.0225 0.0468  70  PHE   A CE1 
600  C  CE2 . PHE   A 70  ? 0.3317 0.1228 0.1666 0.0204  -0.0458 0.0162  70  PHE   A CE2 
601  C  CZ  . PHE   A 70  ? 0.2999 0.1395 0.1663 0.0089  -0.0222 0.0206  70  PHE   A CZ  
602  N  N   . ASP   A 71  ? 0.3562 0.1154 0.2517 0.0296  -0.0859 0.0286  71  ASP   A N   
603  C  CA  . ASP   A 71  ? 0.3331 0.1054 0.3184 0.0184  -0.0763 0.0555  71  ASP   A CA  
604  C  C   . ASP   A 71  ? 0.2898 0.1044 0.3209 0.0002  -0.0414 0.0281  71  ASP   A C   
605  O  O   . ASP   A 71  ? 0.3064 0.1757 0.4386 -0.0304 -0.0119 0.0094  71  ASP   A O   
606  C  CB  . ASP   A 71  ? 0.3316 0.1298 0.3975 0.0176  -0.1253 0.0405  71  ASP   A CB  
607  C  CG  . ASP   A 71  ? 0.3970 0.1277 0.3685 0.0179  -0.1415 0.0539  71  ASP   A CG  
608  O  OD1 . ASP   A 71  ? 0.3352 0.1462 0.4154 0.0159  -0.0917 0.0534  71  ASP   A OD1 
609  O  OD2 . ASP   A 71  ? 0.4075 0.1820 0.5926 0.0245  -0.1673 0.0449  71  ASP   A OD2 
610  N  N   . ASP   A 72  ? 0.2656 0.1216 0.2843 -0.0127 -0.0375 0.0488  72  ASP   A N   
611  C  CA  . ASP   A 72  ? 0.2888 0.1362 0.2697 -0.0055 -0.0114 0.0405  72  ASP   A CA  
612  C  C   . ASP   A 72  ? 0.2754 0.1461 0.3308 -0.0242 -0.0262 0.0429  72  ASP   A C   
613  O  O   . ASP   A 72  ? 0.4054 0.1326 0.3609 -0.0271 -0.0402 0.0240  72  ASP   A O   
614  C  CB  . ASP   A 72  ? 0.3023 0.1386 0.2928 0.0153  -0.0220 0.0329  72  ASP   A CB  
615  C  CG  . ASP   A 72  ? 0.3079 0.2099 0.2169 0.0328  -0.0160 0.0241  72  ASP   A CG  
616  O  OD1 . ASP   A 72  ? 0.3231 0.3094 0.2525 -0.0118 -0.0516 0.0892  72  ASP   A OD1 
617  O  OD2 . ASP   A 72  ? 0.3173 0.3101 0.2206 -0.0095 -0.0241 0.0573  72  ASP   A OD2 
618  N  N   . SER   A 73  ? 0.2992 0.1340 0.3376 -0.0324 -0.0255 0.0475  73  SER   A N   
619  C  CA  . SER   A 73  ? 0.3446 0.1355 0.3814 -0.0065 -0.0358 0.0418  73  SER   A CA  
620  C  C   . SER   A 73  ? 0.3510 0.1288 0.4418 -0.0055 -0.0312 0.0260  73  SER   A C   
621  O  O   . SER   A 73  ? 0.4452 0.1180 0.4118 -0.0331 -0.0908 0.0218  73  SER   A O   
622  C  CB  . SER   A 73  ? 0.3607 0.1942 0.3874 -0.0265 -0.0530 0.0725  73  SER   A CB  
623  O  OG  . SER   A 73  ? 0.3646 0.1304 0.3088 0.0070  -0.0267 0.0383  73  SER   A OG  
624  N  N   . GLN   A 74  ? 0.3464 0.1680 0.4226 0.0040  -0.0303 0.0473  74  GLN   A N   
625  C  CA  . GLN   A 74  ? 0.3977 0.2264 0.4188 0.0537  -0.0322 0.0040  74  GLN   A CA  
626  C  C   . GLN   A 74  ? 0.4815 0.2531 0.2955 -0.0629 -0.1368 -0.0735 74  GLN   A C   
627  O  O   . GLN   A 74  ? 0.3502 0.2269 0.3162 -0.0773 -0.0748 0.0249  74  GLN   A O   
628  C  CB  . GLN   A 74  ? 0.4560 0.2853 0.5613 0.1339  -0.0922 0.0378  74  GLN   A CB  
629  C  CG  . GLN   A 74  ? 0.3608 0.2954 0.6063 0.0217  -0.0809 0.0284  74  GLN   A CG  
630  C  CD  . GLN   A 74  ? 0.5123 0.3559 0.4238 -0.0121 -0.2090 0.0640  74  GLN   A CD  
631  O  OE1 . GLN   A 74  ? 0.5831 0.3729 0.3975 -0.0179 -0.1443 0.0151  74  GLN   A OE1 
632  N  NE2 . GLN   A 74  ? 0.5984 0.4510 0.4491 -0.1095 -0.0579 0.0555  74  GLN   A NE2 
633  N  N   . ASP   A 75  ? 0.5465 0.3885 0.2818 -0.0083 -0.1197 -0.0855 75  ASP   A N   
634  C  CA  . ASP   A 75  ? 0.4499 0.4349 0.3398 -0.0251 -0.1085 -0.0502 75  ASP   A CA  
635  C  C   . ASP   A 75  ? 0.3826 0.4504 0.2963 0.0359  -0.1390 -0.0063 75  ASP   A C   
636  O  O   . ASP   A 75  ? 0.3770 0.7684 0.5703 0.0285  -0.1237 -0.1257 75  ASP   A O   
637  C  CB  . ASP   A 75  ? 0.6007 0.4631 0.3389 0.2209  -0.1267 0.0231  75  ASP   A CB  
638  C  CG  . ASP   A 75  ? 0.6767 0.5008 0.3711 0.1323  -0.1354 -0.0230 75  ASP   A CG  
639  O  OD1 . ASP   A 75  ? 0.5820 0.5356 0.3674 -0.0195 -0.1137 -0.1645 75  ASP   A OD1 
640  O  OD2 . ASP   A 75  ? 0.8160 0.5956 0.4667 0.2700  0.0665  0.0024  75  ASP   A OD2 
641  N  N   . LYS   A 76  ? 0.3949 0.2892 0.3305 -0.0566 -0.1076 0.0611  76  LYS   A N   
642  C  CA  . LYS   A 76  ? 0.3602 0.2348 0.4395 -0.0355 -0.1144 0.0680  76  LYS   A CA  
643  C  C   . LYS   A 76  ? 0.3621 0.2764 0.5759 0.0187  0.0085  0.1491  76  LYS   A C   
644  O  O   . LYS   A 76  ? 0.4269 0.4671 0.6330 0.0809  0.0563  0.2067  76  LYS   A O   
645  C  CB  . LYS   A 76  ? 0.3845 0.1842 0.4233 -0.0396 -0.1564 0.0761  76  LYS   A CB  
646  C  CG  . LYS   A 76  ? 0.5791 0.2381 0.4144 -0.0277 -0.1242 0.1082  76  LYS   A CG  
647  C  CD  . LYS   A 76  ? 0.5980 0.2391 0.3635 -0.0983 -0.1195 0.0956  76  LYS   A CD  
648  C  CE  . LYS   A 76  ? 0.4981 0.2481 0.3876 0.0524  -0.1599 -0.0044 76  LYS   A CE  
649  N  NZ  . LYS   A 76  ? 0.5191 0.3447 0.4051 0.0395  -0.0968 0.0149  76  LYS   A NZ  
650  N  N   . ALA   A 77  ? 0.3075 0.3035 0.4167 0.0221  -0.1260 0.1086  77  ALA   A N   
651  C  CA  . ALA   A 77  ? 0.2576 0.2532 0.2709 -0.0278 -0.0614 0.0518  77  ALA   A CA  
652  C  C   . ALA   A 77  ? 0.2088 0.2307 0.2688 -0.0155 -0.0528 0.0226  77  ALA   A C   
653  O  O   . ALA   A 77  ? 0.2159 0.3359 0.3027 -0.0413 -0.0326 -0.0184 77  ALA   A O   
654  C  CB  . ALA   A 77  ? 0.3736 0.2640 0.2793 0.0333  -0.1042 0.0267  77  ALA   A CB  
655  N  N   . VAL   A 78  ? 0.2454 0.1628 0.2312 -0.0125 -0.0559 0.0292  78  VAL   A N   
656  C  CA  . VAL   A 78  ? 0.2800 0.1635 0.2170 0.0119  -0.0526 0.0277  78  VAL   A CA  
657  C  C   . VAL   A 78  ? 0.2264 0.1449 0.2541 -0.0150 -0.0350 0.0265  78  VAL   A C   
658  O  O   . VAL   A 78  ? 0.2341 0.2002 0.3030 -0.0387 -0.0787 0.0399  78  VAL   A O   
659  C  CB  . VAL   A 78  ? 0.3400 0.1727 0.2855 0.0480  -0.0106 0.0241  78  VAL   A CB  
660  C  CG1 . VAL   A 78  ? 0.3753 0.1494 0.3579 0.0187  -0.0359 0.0333  78  VAL   A CG1 
661  C  CG2 . VAL   A 78  ? 0.3165 0.2355 0.4011 0.0357  0.0347  0.0201  78  VAL   A CG2 
662  N  N   . LEU   A 79  ? 0.2113 0.1492 0.2294 0.0030  -0.0262 0.0223  79  LEU   A N   
663  C  CA  . LEU   A 79  ? 0.2046 0.1428 0.2208 -0.0183 -0.0216 0.0042  79  LEU   A CA  
664  C  C   . LEU   A 79  ? 0.2111 0.1530 0.2228 -0.0284 -0.0172 -0.0027 79  LEU   A C   
665  O  O   . LEU   A 79  ? 0.2345 0.1606 0.2250 -0.0410 -0.0106 -0.0174 79  LEU   A O   
666  C  CB  . LEU   A 79  ? 0.1962 0.1769 0.2419 -0.0149 -0.0221 0.0311  79  LEU   A CB  
667  C  CG  . LEU   A 79  ? 0.2350 0.1732 0.2341 -0.0009 -0.0302 0.0190  79  LEU   A CG  
668  C  CD1 . LEU   A 79  ? 0.2990 0.1401 0.4179 -0.0215 -0.0239 0.0549  79  LEU   A CD1 
669  C  CD2 . LEU   A 79  ? 0.2219 0.1891 0.2341 0.0050  -0.0147 0.0024  79  LEU   A CD2 
670  N  N   . LYS   A 80  ? 0.2272 0.2002 0.2233 -0.0319 -0.0013 0.0010  80  LYS   A N   
671  C  CA  A LYS   A 80  ? 0.2305 0.1707 0.2629 -0.0214 0.0036  -0.0025 80  LYS   A CA  
672  C  CA  B LYS   A 80  ? 0.2305 0.1707 0.2629 -0.0214 0.0036  -0.0025 80  LYS   A CA  
673  C  C   . LYS   A 80  ? 0.2006 0.1791 0.2474 -0.0043 0.0055  -0.0050 80  LYS   A C   
674  O  O   . LYS   A 80  ? 0.1975 0.1819 0.2588 -0.0289 0.0059  0.0010  80  LYS   A O   
675  C  CB  A LYS   A 80  ? 0.3878 0.2215 0.3309 0.0510  -0.0145 0.0317  80  LYS   A CB  
676  C  CB  B LYS   A 80  ? 0.3878 0.2215 0.3309 0.0510  -0.0145 0.0317  80  LYS   A CB  
677  C  CG  A LYS   A 80  ? 0.3503 0.2461 0.3623 0.0480  0.0238  0.0147  80  LYS   A CG  
678  C  CG  B LYS   A 80  ? 0.3503 0.2461 0.3623 0.0480  0.0238  0.0147  80  LYS   A CG  
679  C  CD  A LYS   A 80  ? 0.3910 0.2799 0.5145 0.0792  -0.0258 0.0381  80  LYS   A CD  
680  C  CD  B LYS   A 80  ? 0.3910 0.2799 0.5145 0.0792  -0.0258 0.0381  80  LYS   A CD  
681  C  CE  A LYS   A 80  ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  80  LYS   A CE  
682  C  CE  B LYS   A 80  ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  80  LYS   A CE  
683  N  NZ  A LYS   A 80  ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  80  LYS   A NZ  
684  N  NZ  B LYS   A 80  ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  80  LYS   A NZ  
685  N  N   . GLY   A 81  ? 0.2220 0.2221 0.2269 -0.0037 0.0201  0.0105  81  GLY   A N   
686  C  CA  . GLY   A 81  ? 0.2358 0.2261 0.2556 0.0131  0.0534  0.0300  81  GLY   A CA  
687  C  C   . GLY   A 81  ? 0.2294 0.2048 0.2149 0.0002  0.0201  0.0131  81  GLY   A C   
688  O  O   . GLY   A 81  ? 0.2152 0.1921 0.2796 -0.0268 0.0179  -0.0189 81  GLY   A O   
689  N  N   . GLY   A 82  ? 0.2386 0.2398 0.3084 -0.0330 0.0284  0.0530  82  GLY   A N   
690  C  CA  . GLY   A 82  ? 0.2637 0.2046 0.4079 -0.0237 0.0150  0.0177  82  GLY   A CA  
691  C  C   . GLY   A 82  ? 0.2458 0.1914 0.2915 0.0372  0.0366  0.0308  82  GLY   A C   
692  O  O   . GLY   A 82  ? 0.2796 0.3420 0.2945 0.0814  0.0456  -0.0003 82  GLY   A O   
693  N  N   . PRO   A 83  ? 0.2389 0.1772 0.2739 0.0376  0.0359  0.0397  83  PRO   A N   
694  C  CA  . PRO   A 83  ? 0.2920 0.2172 0.2386 0.0697  0.0236  0.0042  83  PRO   A CA  
695  C  C   . PRO   A 83  ? 0.2206 0.2280 0.2308 0.0486  -0.0148 -0.0081 83  PRO   A C   
696  O  O   . PRO   A 83  ? 0.2627 0.2981 0.2805 0.0096  -0.0615 0.0030  83  PRO   A O   
697  C  CB  . PRO   A 83  ? 0.2746 0.2208 0.2436 0.0635  0.0104  0.0311  83  PRO   A CB  
698  C  CG  . PRO   A 83  ? 0.2368 0.1938 0.2393 0.0489  0.0274  0.0148  83  PRO   A CG  
699  C  CD  . PRO   A 83  ? 0.2265 0.1552 0.2841 0.0099  0.0507  0.0111  83  PRO   A CD  
700  N  N   . LEU   A 84  ? 0.1953 0.1859 0.2222 0.0155  0.0149  0.0047  84  LEU   A N   
701  C  CA  . LEU   A 84  ? 0.2523 0.1551 0.2208 0.0138  0.0137  -0.0227 84  LEU   A CA  
702  C  C   . LEU   A 84  ? 0.2397 0.1733 0.2652 0.0337  0.0033  -0.0483 84  LEU   A C   
703  O  O   . LEU   A 84  ? 0.2487 0.2104 0.3484 0.0198  0.0339  -0.0868 84  LEU   A O   
704  C  CB  . LEU   A 84  ? 0.2212 0.1423 0.2089 0.0220  0.0171  -0.0170 84  LEU   A CB  
705  C  CG  . LEU   A 84  ? 0.1826 0.1317 0.2375 0.0239  0.0055  -0.0201 84  LEU   A CG  
706  C  CD1 . LEU   A 84  ? 0.1942 0.1556 0.2301 0.0029  -0.0052 -0.0109 84  LEU   A CD1 
707  C  CD2 . LEU   A 84  ? 0.1849 0.1289 0.2749 0.0033  0.0124  -0.0294 84  LEU   A CD2 
708  N  N   A ASP   A 85  ? 0.3310 0.1351 0.2622 0.0195  0.0165  -0.0669 85  ASP   A N   
709  N  N   B ASP   A 85  ? 0.2921 0.1823 0.2407 0.0086  -0.0159 -0.0532 85  ASP   A N   
710  C  CA  A ASP   A 85  ? 0.4030 0.1100 0.3657 -0.0070 0.0508  -0.0690 85  ASP   A CA  
711  C  CA  B ASP   A 85  ? 0.3614 0.1655 0.2640 0.0254  -0.0168 -0.0391 85  ASP   A CA  
712  C  C   A ASP   A 85  ? 0.3591 0.1158 0.3431 0.0168  0.0414  -0.1039 85  ASP   A C   
713  C  C   B ASP   A 85  ? 0.3050 0.1586 0.2479 0.0099  -0.0416 -0.0538 85  ASP   A C   
714  O  O   A ASP   A 85  ? 0.2877 0.2573 0.4192 0.0363  0.0237  -0.1096 85  ASP   A O   
715  O  O   B ASP   A 85  ? 0.4236 0.1702 0.2570 0.0376  -0.0891 -0.0662 85  ASP   A O   
716  C  CB  A ASP   A 85  ? 0.3754 0.1462 0.3984 -0.0311 0.0870  -0.0937 85  ASP   A CB  
717  C  CB  B ASP   A 85  ? 0.2808 0.2037 0.2874 -0.0285 -0.0204 -0.0248 85  ASP   A CB  
718  C  CG  A ASP   A 85  ? 0.3794 0.2255 0.4292 -0.0159 0.0422  -0.0447 85  ASP   A CG  
719  C  CG  B ASP   A 85  ? 0.2812 0.2122 0.2897 -0.0397 -0.0153 -0.0283 85  ASP   A CG  
720  O  OD1 A ASP   A 85  ? 0.3906 0.3925 0.3887 -0.0328 0.1353  -0.0374 85  ASP   A OD1 
721  O  OD1 B ASP   A 85  ? 0.3322 0.2742 0.3126 -0.0477 0.0077  -0.0528 85  ASP   A OD1 
722  O  OD2 A ASP   A 85  ? 0.3344 0.3497 0.4265 -0.0642 0.0741  0.0181  85  ASP   A OD2 
723  O  OD2 B ASP   A 85  ? 0.4175 0.2952 0.2845 -0.0820 -0.0363 -0.0444 85  ASP   A OD2 
724  N  N   A GLY   A 86  ? 0.4347 0.0955 0.3836 -0.0006 -0.0073 -0.0223 86  GLY   A N   
725  N  N   B GLY   A 86  ? 0.3209 0.1137 0.2631 0.0023  0.0023  -0.0596 86  GLY   A N   
726  C  CA  A GLY   A 86  ? 0.2997 0.1873 0.3133 0.0121  0.0628  -0.0397 86  GLY   A CA  
727  C  CA  B GLY   A 86  ? 0.3579 0.1710 0.2438 -0.0184 -0.0018 -0.0458 86  GLY   A CA  
728  C  C   A GLY   A 86  ? 0.3083 0.2629 0.3325 -0.0289 0.0888  -0.0775 86  GLY   A C   
729  C  C   B GLY   A 86  ? 0.3350 0.1754 0.2345 -0.0297 0.0281  -0.0653 86  GLY   A C   
730  O  O   A GLY   A 86  ? 0.2750 0.2570 0.3800 -0.0133 0.0831  -0.0130 86  GLY   A O   
731  O  O   B GLY   A 86  ? 0.2640 0.1905 0.2610 -0.0381 0.0362  -0.0855 86  GLY   A O   
732  N  N   A THR   A 87  ? 0.3345 0.2061 0.3292 0.0325  0.0935  -0.0688 87  THR   A N   
733  N  N   B THR   A 87  ? 0.3050 0.1403 0.2665 -0.0103 -0.0047 -0.0560 87  THR   A N   
734  C  CA  A THR   A 87  ? 0.2718 0.2314 0.3458 0.0337  0.0681  -0.0527 87  THR   A CA  
735  C  CA  B THR   A 87  ? 0.2542 0.1603 0.2647 0.0196  -0.0182 -0.0275 87  THR   A CA  
736  C  C   A THR   A 87  ? 0.2058 0.1509 0.2728 -0.0085 0.0108  -0.0463 87  THR   A C   
737  C  C   B THR   A 87  ? 0.2346 0.1174 0.2582 0.0164  -0.0279 -0.0118 87  THR   A C   
738  O  O   A THR   A 87  ? 0.2269 0.1237 0.2782 -0.0109 0.0149  -0.0176 87  THR   A O   
739  O  O   B THR   A 87  ? 0.2593 0.1058 0.2797 -0.0076 -0.0353 -0.0240 87  THR   A O   
740  C  CB  A THR   A 87  ? 0.2726 0.1947 0.3899 0.0033  0.0565  -0.0381 87  THR   A CB  
741  C  CB  B THR   A 87  ? 0.2529 0.1522 0.3228 0.0483  0.0082  -0.0281 87  THR   A CB  
742  O  OG1 A THR   A 87  ? 0.3150 0.1799 0.3811 0.0272  0.0747  0.0212  87  THR   A OG1 
743  O  OG1 B THR   A 87  ? 0.2761 0.2085 0.4479 0.0553  0.0633  -0.0587 87  THR   A OG1 
744  C  CG2 A THR   A 87  ? 0.3048 0.2335 0.4147 0.0617  0.0883  0.0001  87  THR   A CG2 
745  C  CG2 B THR   A 87  ? 0.2390 0.2023 0.3284 0.0650  -0.0245 -0.0428 87  THR   A CG2 
746  N  N   . TYR   A 88  ? 0.2060 0.1244 0.2315 -0.0012 0.0021  -0.0181 88  TYR   A N   
747  C  CA  . TYR   A 88  ? 0.1839 0.1288 0.2091 0.0029  0.0059  -0.0102 88  TYR   A CA  
748  C  C   . TYR   A 88  ? 0.1860 0.1181 0.2157 0.0038  -0.0323 0.0117  88  TYR   A C   
749  O  O   . TYR   A 88  ? 0.2051 0.2114 0.2533 -0.0436 -0.0348 0.0251  88  TYR   A O   
750  C  CB  . TYR   A 88  ? 0.2197 0.1174 0.2006 0.0140  -0.0081 -0.0170 88  TYR   A CB  
751  C  CG  . TYR   A 88  ? 0.2051 0.1016 0.1953 -0.0049 -0.0037 -0.0128 88  TYR   A CG  
752  C  CD1 . TYR   A 88  ? 0.2231 0.1329 0.1932 0.0119  -0.0042 -0.0141 88  TYR   A CD1 
753  C  CD2 . TYR   A 88  ? 0.1969 0.0862 0.1980 0.0018  -0.0147 -0.0037 88  TYR   A CD2 
754  C  CE1 . TYR   A 88  ? 0.2019 0.1456 0.2054 0.0170  0.0063  -0.0082 88  TYR   A CE1 
755  C  CE2 . TYR   A 88  ? 0.2001 0.1021 0.1834 -0.0027 -0.0029 0.0004  88  TYR   A CE2 
756  C  CZ  . TYR   A 88  ? 0.2020 0.1007 0.1883 0.0006  -0.0029 -0.0186 88  TYR   A CZ  
757  O  OH  . TYR   A 88  ? 0.2100 0.1320 0.1759 0.0015  0.0024  -0.0143 88  TYR   A OH  
758  N  N   . ARG   A 89  ? 0.1897 0.1007 0.2029 0.0142  -0.0168 -0.0075 89  ARG   A N   
759  C  CA  . ARG   A 89  ? 0.2172 0.1025 0.1978 0.0149  -0.0440 0.0039  89  ARG   A CA  
760  C  C   . ARG   A 89  ? 0.2097 0.0959 0.1513 -0.0030 -0.0242 0.0121  89  ARG   A C   
761  O  O   . ARG   A 89  ? 0.1920 0.1176 0.1700 0.0000  -0.0174 0.0137  89  ARG   A O   
762  C  CB  . ARG   A 89  ? 0.2845 0.0867 0.2848 0.0264  -0.0362 0.0108  89  ARG   A CB  
763  C  CG  . ARG   A 89  ? 0.4197 0.1664 0.2560 -0.0059 -0.0446 0.0535  89  ARG   A CG  
764  C  CD  . ARG   A 89  ? 0.3641 0.1734 0.3507 0.0249  -0.0418 0.0610  89  ARG   A CD  
765  N  NE  . ARG   A 89  ? 0.4208 0.1958 0.2693 -0.0155 -0.0542 0.0712  89  ARG   A NE  
766  C  CZ  . ARG   A 89  ? 0.4064 0.1819 0.2441 0.0150  -0.0171 0.0249  89  ARG   A CZ  
767  N  NH1 . ARG   A 89  ? 0.4220 0.1671 0.3585 0.0174  0.0203  0.0924  89  ARG   A NH1 
768  N  NH2 . ARG   A 89  ? 0.4235 0.1864 0.3638 0.0732  -0.0222 0.0201  89  ARG   A NH2 
769  N  N   . LEU   A 90  ? 0.2238 0.1106 0.1689 -0.0096 -0.0363 0.0040  90  LEU   A N   
770  C  CA  . LEU   A 90  ? 0.2229 0.1257 0.1495 -0.0100 -0.0268 0.0036  90  LEU   A CA  
771  C  C   . LEU   A 90  ? 0.2325 0.1409 0.1348 -0.0130 -0.0434 0.0236  90  LEU   A C   
772  O  O   . LEU   A 90  ? 0.2369 0.1745 0.1776 -0.0046 -0.0341 0.0613  90  LEU   A O   
773  C  CB  . LEU   A 90  ? 0.2267 0.1284 0.1812 -0.0197 -0.0422 0.0040  90  LEU   A CB  
774  C  CG  . LEU   A 90  ? 0.2535 0.1544 0.1468 -0.0284 -0.0436 0.0010  90  LEU   A CG  
775  C  CD1 . LEU   A 90  ? 0.2554 0.1358 0.1769 -0.0255 -0.0230 0.0119  90  LEU   A CD1 
776  C  CD2 . LEU   A 90  ? 0.2557 0.1877 0.1925 -0.0541 -0.0455 0.0016  90  LEU   A CD2 
777  N  N   . ILE   A 91  ? 0.2238 0.0971 0.1584 -0.0088 -0.0189 0.0136  91  ILE   A N   
778  C  CA  . ILE   A 91  ? 0.2330 0.0925 0.1724 -0.0087 -0.0119 0.0130  91  ILE   A CA  
779  C  C   . ILE   A 91  ? 0.2290 0.0926 0.1410 -0.0129 -0.0305 0.0187  91  ILE   A C   
780  O  O   . ILE   A 91  ? 0.2584 0.1132 0.1324 -0.0042 -0.0351 0.0302  91  ILE   A O   
781  C  CB  . ILE   A 91  ? 0.2584 0.1239 0.1522 -0.0249 -0.0205 0.0163  91  ILE   A CB  
782  C  CG1 . ILE   A 91  ? 0.2674 0.1687 0.1881 -0.0734 -0.0010 0.0104  91  ILE   A CG1 
783  C  CG2 . ILE   A 91  ? 0.2567 0.1408 0.1621 -0.0106 -0.0135 0.0268  91  ILE   A CG2 
784  C  CD1 . ILE   A 91  ? 0.3027 0.1976 0.2484 -0.0923 -0.0115 -0.0080 91  ILE   A CD1 
785  N  N   . GLN   A 92  ? 0.2371 0.0851 0.1629 -0.0044 -0.0352 0.0147  92  GLN   A N   
786  C  CA  . GLN   A 92  ? 0.2447 0.0797 0.1723 -0.0011 -0.0106 0.0243  92  GLN   A CA  
787  C  C   . GLN   A 92  ? 0.2207 0.0926 0.1268 0.0023  -0.0099 0.0098  92  GLN   A C   
788  O  O   . GLN   A 92  ? 0.2292 0.1027 0.1256 -0.0044 -0.0074 0.0066  92  GLN   A O   
789  C  CB  . GLN   A 92  ? 0.2495 0.1244 0.1465 -0.0147 -0.0227 0.0150  92  GLN   A CB  
790  C  CG  . GLN   A 92  ? 0.2515 0.1092 0.1859 -0.0060 -0.0479 0.0196  92  GLN   A CG  
791  C  CD  . GLN   A 92  ? 0.2574 0.1113 0.1577 -0.0162 -0.0155 0.0243  92  GLN   A CD  
792  O  OE1 . GLN   A 92  ? 0.2373 0.1181 0.1613 -0.0121 -0.0168 0.0229  92  GLN   A OE1 
793  N  NE2 . GLN   A 92  ? 0.2739 0.1612 0.1970 -0.0198 0.0229  0.0201  92  GLN   A NE2 
794  N  N   . PHE   A 93  ? 0.2239 0.0885 0.1361 0.0005  -0.0222 0.0136  93  PHE   A N   
795  C  CA  . PHE   A 93  ? 0.2318 0.0941 0.1332 -0.0050 -0.0209 0.0093  93  PHE   A CA  
796  C  C   . PHE   A 93  ? 0.2151 0.0937 0.1141 -0.0105 -0.0241 0.0206  93  PHE   A C   
797  O  O   . PHE   A 93  ? 0.2663 0.1156 0.1089 0.0005  -0.0259 0.0177  93  PHE   A O   
798  C  CB  . PHE   A 93  ? 0.2272 0.1165 0.1243 -0.0136 -0.0367 0.0251  93  PHE   A CB  
799  C  CG  . PHE   A 93  ? 0.2359 0.1071 0.1380 -0.0035 -0.0379 0.0087  93  PHE   A CG  
800  C  CD1 . PHE   A 93  ? 0.2452 0.1293 0.1456 -0.0013 -0.0378 -0.0068 93  PHE   A CD1 
801  C  CD2 . PHE   A 93  ? 0.2328 0.1275 0.1329 -0.0005 -0.0379 0.0311  93  PHE   A CD2 
802  C  CE1 . PHE   A 93  ? 0.2280 0.1319 0.1470 0.0076  -0.0345 -0.0091 93  PHE   A CE1 
803  C  CE2 . PHE   A 93  ? 0.2638 0.1144 0.1552 0.0135  -0.0571 -0.0013 93  PHE   A CE2 
804  C  CZ  . PHE   A 93  ? 0.2511 0.1234 0.1547 0.0102  -0.0541 0.0038  93  PHE   A CZ  
805  N  N   . HIS   A 94  ? 0.2142 0.0995 0.1244 -0.0015 -0.0206 0.0127  94  HIS   A N   
806  C  CA  . HIS   A 94  ? 0.1966 0.1068 0.1110 -0.0077 -0.0160 0.0092  94  HIS   A CA  
807  C  C   . HIS   A 94  ? 0.2142 0.1080 0.0926 -0.0075 -0.0188 0.0080  94  HIS   A C   
808  O  O   . HIS   A 94  ? 0.2057 0.0994 0.1146 0.0022  -0.0070 0.0136  94  HIS   A O   
809  C  CB  . HIS   A 94  ? 0.2024 0.1346 0.1235 0.0004  -0.0177 0.0162  94  HIS   A CB  
810  C  CG  . HIS   A 94  ? 0.1909 0.1083 0.1144 -0.0160 -0.0049 0.0065  94  HIS   A CG  
811  N  ND1 . HIS   A 94  ? 0.1974 0.1084 0.1124 -0.0181 -0.0111 0.0016  94  HIS   A ND1 
812  C  CD2 . HIS   A 94  ? 0.1879 0.1371 0.0946 -0.0190 -0.0178 0.0187  94  HIS   A CD2 
813  C  CE1 . HIS   A 94  ? 0.2046 0.0935 0.1132 -0.0238 -0.0118 0.0196  94  HIS   A CE1 
814  N  NE2 . HIS   A 94  ? 0.1811 0.1089 0.1266 -0.0162 0.0010  -0.0034 94  HIS   A NE2 
815  N  N   . PHE   A 95  ? 0.1985 0.1023 0.1260 -0.0095 -0.0116 0.0060  95  PHE   A N   
816  C  CA  . PHE   A 95  ? 0.2042 0.0851 0.1327 -0.0116 -0.0162 0.0075  95  PHE   A CA  
817  C  C   . PHE   A 95  ? 0.1898 0.0996 0.1274 -0.0138 -0.0080 -0.0078 95  PHE   A C   
818  O  O   . PHE   A 95  ? 0.1844 0.1274 0.1518 -0.0151 -0.0022 0.0138  95  PHE   A O   
819  C  CB  . PHE   A 95  ? 0.1988 0.1048 0.1401 -0.0024 -0.0157 -0.0032 95  PHE   A CB  
820  C  CG  . PHE   A 95  ? 0.2007 0.1055 0.1215 -0.0151 -0.0238 -0.0136 95  PHE   A CG  
821  C  CD1 . PHE   A 95  ? 0.2190 0.1210 0.1426 -0.0115 -0.0252 -0.0037 95  PHE   A CD1 
822  C  CD2 . PHE   A 95  ? 0.2043 0.1359 0.1547 -0.0292 -0.0239 -0.0178 95  PHE   A CD2 
823  C  CE1 . PHE   A 95  ? 0.2224 0.1434 0.1669 -0.0055 -0.0425 -0.0204 95  PHE   A CE1 
824  C  CE2 . PHE   A 95  ? 0.2041 0.1353 0.1690 -0.0053 -0.0257 -0.0322 95  PHE   A CE2 
825  C  CZ  . PHE   A 95  ? 0.2186 0.1434 0.1679 0.0031  -0.0286 -0.0314 95  PHE   A CZ  
826  N  N   . HIS   A 96  ? 0.1914 0.0930 0.1274 -0.0054 -0.0141 -0.0040 96  HIS   A N   
827  C  CA  . HIS   A 96  ? 0.1932 0.0996 0.1265 -0.0037 -0.0062 -0.0034 96  HIS   A CA  
828  C  C   . HIS   A 96  ? 0.1763 0.1053 0.1327 -0.0138 -0.0010 -0.0058 96  HIS   A C   
829  O  O   . HIS   A 96  ? 0.1865 0.0998 0.1385 -0.0151 0.0072  -0.0144 96  HIS   A O   
830  C  CB  . HIS   A 96  ? 0.1948 0.0953 0.1318 -0.0133 -0.0085 -0.0083 96  HIS   A CB  
831  C  CG  . HIS   A 96  ? 0.1912 0.1090 0.1068 -0.0076 -0.0103 -0.0050 96  HIS   A CG  
832  N  ND1 . HIS   A 96  ? 0.1881 0.1014 0.1483 -0.0098 -0.0097 -0.0050 96  HIS   A ND1 
833  C  CD2 . HIS   A 96  ? 0.1990 0.0849 0.1294 -0.0052 -0.0055 -0.0036 96  HIS   A CD2 
834  C  CE1 . HIS   A 96  ? 0.1891 0.1007 0.1380 0.0004  -0.0066 -0.0079 96  HIS   A CE1 
835  N  NE2 . HIS   A 96  ? 0.1897 0.0996 0.1253 -0.0214 -0.0194 0.0075  96  HIS   A NE2 
836  N  N   . TRP   A 97  ? 0.1849 0.0968 0.1238 -0.0059 0.0037  -0.0059 97  TRP   A N   
837  C  CA  . TRP   A 97  ? 0.2163 0.0995 0.1322 -0.0019 -0.0038 -0.0110 97  TRP   A CA  
838  C  C   . TRP   A 97  ? 0.2007 0.0998 0.1199 -0.0046 -0.0034 -0.0061 97  TRP   A C   
839  O  O   . TRP   A 97  ? 0.1975 0.1095 0.1444 -0.0144 0.0168  -0.0121 97  TRP   A O   
840  C  CB  . TRP   A 97  ? 0.2159 0.1260 0.1153 -0.0242 -0.0068 -0.0133 97  TRP   A CB  
841  C  CG  . TRP   A 97  ? 0.2178 0.1053 0.1235 -0.0160 -0.0053 -0.0130 97  TRP   A CG  
842  C  CD1 . TRP   A 97  ? 0.2381 0.1226 0.1298 -0.0256 0.0097  -0.0238 97  TRP   A CD1 
843  C  CD2 . TRP   A 97  ? 0.2197 0.1185 0.1089 -0.0171 -0.0120 0.0004  97  TRP   A CD2 
844  N  NE1 . TRP   A 97  ? 0.2577 0.1199 0.1327 -0.0210 -0.0001 -0.0172 97  TRP   A NE1 
845  C  CE2 . TRP   A 97  ? 0.2402 0.1177 0.1258 -0.0190 0.0006  -0.0037 97  TRP   A CE2 
846  C  CE3 . TRP   A 97  ? 0.1978 0.1147 0.1412 -0.0122 -0.0164 -0.0070 97  TRP   A CE3 
847  C  CZ2 . TRP   A 97  ? 0.2233 0.1324 0.1251 -0.0190 -0.0128 0.0080  97  TRP   A CZ2 
848  C  CZ3 . TRP   A 97  ? 0.2412 0.1386 0.1179 -0.0287 -0.0082 -0.0011 97  TRP   A CZ3 
849  C  CH2 . TRP   A 97  ? 0.2543 0.1244 0.1329 -0.0245 -0.0104 -0.0055 97  TRP   A CH2 
850  N  N   . GLY   A 98  ? 0.2139 0.0971 0.1525 -0.0067 0.0006  -0.0080 98  GLY   A N   
851  C  CA  . GLY   A 98  ? 0.2154 0.1161 0.1376 -0.0001 0.0042  -0.0102 98  GLY   A CA  
852  C  C   . GLY   A 98  ? 0.2104 0.1138 0.1441 -0.0125 0.0016  -0.0136 98  GLY   A C   
853  O  O   . GLY   A 98  ? 0.2336 0.1102 0.1688 -0.0161 0.0019  -0.0250 98  GLY   A O   
854  N  N   . SER   A 99  ? 0.2236 0.1153 0.1714 -0.0051 0.0179  -0.0260 99  SER   A N   
855  C  CA  . SER   A 99  ? 0.2554 0.1188 0.1829 -0.0110 0.0211  -0.0447 99  SER   A CA  
856  C  C   . SER   A 99  ? 0.2603 0.1034 0.1967 0.0037  -0.0049 -0.0421 99  SER   A C   
857  O  O   . SER   A 99  ? 0.2843 0.1467 0.2250 -0.0131 -0.0062 -0.0577 99  SER   A O   
858  C  CB  . SER   A 99  ? 0.2685 0.1703 0.2091 0.0195  0.0257  -0.0442 99  SER   A CB  
859  O  OG  . SER   A 99  ? 0.2308 0.1365 0.2569 0.0097  0.0254  -0.0320 99  SER   A OG  
860  N  N   . LEU   A 100 ? 0.2316 0.1215 0.2161 0.0005  0.0134  -0.0249 100 LEU   A N   
861  C  CA  . LEU   A 100 ? 0.2552 0.0807 0.2882 0.0042  0.0318  -0.0430 100 LEU   A CA  
862  C  C   . LEU   A 100 ? 0.2414 0.0873 0.2452 -0.0085 0.0157  -0.0195 100 LEU   A C   
863  O  O   . LEU   A 100 ? 0.2524 0.0986 0.2307 -0.0089 0.0134  -0.0272 100 LEU   A O   
864  C  CB  . LEU   A 100 ? 0.2749 0.1763 0.2855 0.0296  0.0514  -0.0043 100 LEU   A CB  
865  C  CG  . LEU   A 100 ? 0.2892 0.2037 0.2774 0.0439  0.0452  -0.0248 100 LEU   A CG  
866  C  CD1 . LEU   A 100 ? 0.3405 0.3552 0.3551 0.1468  0.0155  -0.0312 100 LEU   A CD1 
867  C  CD2 . LEU   A 100 ? 0.3921 0.1998 0.4075 0.0081  0.1265  -0.1188 100 LEU   A CD2 
868  N  N   . ASP   A 101 ? 0.2330 0.0932 0.2831 -0.0033 0.0172  -0.0237 101 ASP   A N   
869  C  CA  . ASP   A 101 ? 0.2474 0.0961 0.2669 -0.0088 0.0302  -0.0021 101 ASP   A CA  
870  C  C   . ASP   A 101 ? 0.2664 0.1093 0.2587 -0.0042 0.0307  0.0064  101 ASP   A C   
871  O  O   . ASP   A 101 ? 0.3388 0.1254 0.2871 0.0242  0.0699  0.0272  101 ASP   A O   
872  C  CB  . ASP   A 101 ? 0.2404 0.1235 0.2871 -0.0048 0.0100  0.0250  101 ASP   A CB  
873  C  CG  . ASP   A 101 ? 0.2492 0.1271 0.3088 -0.0127 0.0190  -0.0037 101 ASP   A CG  
874  O  OD1 . ASP   A 101 ? 0.2785 0.1463 0.3016 -0.0282 0.0307  -0.0105 101 ASP   A OD1 
875  O  OD2 . ASP   A 101 ? 0.3378 0.1784 0.4296 -0.0857 0.0443  -0.0365 101 ASP   A OD2 
876  N  N   . GLY   A 102 ? 0.2883 0.1239 0.2703 -0.0385 0.0046  0.0162  102 GLY   A N   
877  C  CA  . GLY   A 102 ? 0.3278 0.1264 0.2921 -0.0296 0.0154  0.0217  102 GLY   A CA  
878  C  C   . GLY   A 102 ? 0.3102 0.1000 0.2384 -0.0069 0.0125  0.0179  102 GLY   A C   
879  O  O   . GLY   A 102 ? 0.2877 0.1527 0.2384 -0.0179 0.0326  0.0280  102 GLY   A O   
880  N  N   A GLN   A 103 ? 0.2398 0.1199 0.1793 -0.0115 0.0356  -0.0002 103 GLN   A N   
881  N  N   B GLN   A 103 ? 0.2641 0.0792 0.2366 -0.0058 0.0220  0.0048  103 GLN   A N   
882  C  CA  A GLN   A 103 ? 0.2391 0.1047 0.1838 0.0025  0.0084  0.0051  103 GLN   A CA  
883  C  CA  B GLN   A 103 ? 0.2235 0.1181 0.1464 -0.0116 0.0122  0.0036  103 GLN   A CA  
884  C  C   A GLN   A 103 ? 0.2015 0.0955 0.1609 -0.0019 0.0214  -0.0057 103 GLN   A C   
885  C  C   B GLN   A 103 ? 0.1969 0.1005 0.1530 -0.0029 0.0223  -0.0088 103 GLN   A C   
886  O  O   A GLN   A 103 ? 0.2472 0.0858 0.1620 -0.0236 0.0089  0.0081  103 GLN   A O   
887  O  O   B GLN   A 103 ? 0.2190 0.1273 0.1502 0.0046  0.0192  -0.0289 103 GLN   A O   
888  C  CB  A GLN   A 103 ? 0.2424 0.1137 0.1814 -0.0241 0.0231  -0.0334 103 GLN   A CB  
889  C  CB  B GLN   A 103 ? 0.2341 0.1374 0.1747 0.0186  0.0192  0.0329  103 GLN   A CB  
890  C  CG  A GLN   A 103 ? 0.1997 0.1379 0.1681 0.0337  0.0055  0.0030  103 GLN   A CG  
891  C  CG  B GLN   A 103 ? 0.2005 0.1337 0.1982 -0.0148 0.0358  0.0114  103 GLN   A CG  
892  C  CD  A GLN   A 103 ? 0.1949 0.1180 0.2030 0.0171  -0.0057 -0.0052 103 GLN   A CD  
893  C  CD  B GLN   A 103 ? 0.2322 0.1382 0.2240 0.0173  0.0107  0.0190  103 GLN   A CD  
894  O  OE1 A GLN   A 103 ? 0.2311 0.1203 0.2355 0.0197  0.0035  0.0091  103 GLN   A OE1 
895  O  OE1 B GLN   A 103 ? 0.2567 0.2049 0.3219 0.0800  0.0445  0.1058  103 GLN   A OE1 
896  N  NE2 A GLN   A 103 ? 0.1659 0.1359 0.2579 0.0074  0.0122  -0.0347 103 GLN   A NE2 
897  N  NE2 B GLN   A 103 ? 0.1900 0.1571 0.2578 -0.0201 -0.0016 0.0132  103 GLN   A NE2 
898  N  N   . GLY   A 104 ? 0.2049 0.0923 0.1620 0.0021  0.0173  -0.0006 104 GLY   A N   
899  C  CA  . GLY   A 104 ? 0.1971 0.0961 0.1584 0.0029  0.0062  -0.0006 104 GLY   A CA  
900  C  C   . GLY   A 104 ? 0.1923 0.0886 0.1547 -0.0173 -0.0013 -0.0117 104 GLY   A C   
901  O  O   . GLY   A 104 ? 0.1934 0.1032 0.1562 -0.0126 0.0037  -0.0057 104 GLY   A O   
902  N  N   . SER   A 105 ? 0.1778 0.1142 0.1404 0.0010  0.0019  -0.0143 105 SER   A N   
903  C  CA  . SER   A 105 ? 0.1743 0.1028 0.1280 -0.0036 -0.0063 -0.0097 105 SER   A CA  
904  C  C   . SER   A 105 ? 0.1678 0.1009 0.1192 0.0046  0.0049  0.0020  105 SER   A C   
905  O  O   . SER   A 105 ? 0.1817 0.1071 0.1421 0.0091  -0.0070 -0.0061 105 SER   A O   
906  C  CB  . SER   A 105 ? 0.1720 0.1180 0.1328 -0.0088 -0.0033 0.0146  105 SER   A CB  
907  O  OG  . SER   A 105 ? 0.1973 0.0921 0.1386 0.0010  0.0048  0.0081  105 SER   A OG  
908  N  N   . GLU   A 106 ? 0.1861 0.0905 0.1238 -0.0117 0.0002  -0.0015 106 GLU   A N   
909  C  CA  . GLU   A 106 ? 0.1733 0.1116 0.1181 -0.0085 -0.0143 -0.0016 106 GLU   A CA  
910  C  C   . GLU   A 106 ? 0.1694 0.0823 0.1294 -0.0068 -0.0120 0.0069  106 GLU   A C   
911  O  O   . GLU   A 106 ? 0.1794 0.1113 0.1361 0.0000  -0.0138 0.0102  106 GLU   A O   
912  C  CB  . GLU   A 106 ? 0.2009 0.1000 0.1124 -0.0200 -0.0094 0.0047  106 GLU   A CB  
913  C  CG  . GLU   A 106 ? 0.2298 0.0996 0.1266 -0.0137 0.0089  0.0013  106 GLU   A CG  
914  C  CD  . GLU   A 106 ? 0.1796 0.1047 0.1310 -0.0044 -0.0039 -0.0129 106 GLU   A CD  
915  O  OE1 . GLU   A 106 ? 0.1613 0.1058 0.1532 0.0004  -0.0005 -0.0082 106 GLU   A OE1 
916  O  OE2 . GLU   A 106 ? 0.1738 0.1262 0.1744 0.0012  0.0098  -0.0141 106 GLU   A OE2 
917  N  N   . HIS   A 107 ? 0.1626 0.0973 0.1323 0.0099  -0.0027 0.0025  107 HIS   A N   
918  C  CA  . HIS   A 107 ? 0.1837 0.0961 0.1219 0.0089  -0.0027 0.0035  107 HIS   A CA  
919  C  C   . HIS   A 107 ? 0.1667 0.1093 0.1160 0.0055  -0.0035 0.0027  107 HIS   A C   
920  O  O   . HIS   A 107 ? 0.1727 0.1062 0.1296 -0.0044 -0.0106 0.0103  107 HIS   A O   
921  C  CB  . HIS   A 107 ? 0.1675 0.0939 0.1398 0.0038  -0.0058 0.0021  107 HIS   A CB  
922  C  CG  . HIS   A 107 ? 0.1538 0.1081 0.1144 0.0060  -0.0062 -0.0017 107 HIS   A CG  
923  N  ND1 . HIS   A 107 ? 0.1672 0.0915 0.1395 0.0020  -0.0113 0.0039  107 HIS   A ND1 
924  C  CD2 . HIS   A 107 ? 0.1577 0.0901 0.1454 0.0109  -0.0009 -0.0154 107 HIS   A CD2 
925  C  CE1 . HIS   A 107 ? 0.1701 0.1009 0.1197 0.0103  -0.0111 -0.0231 107 HIS   A CE1 
926  N  NE2 . HIS   A 107 ? 0.1632 0.1038 0.1244 0.0097  -0.0077 -0.0018 107 HIS   A NE2 
927  N  N   . THR   A 108 ? 0.1869 0.1023 0.1395 0.0000  -0.0044 0.0174  108 THR   A N   
928  C  CA  . THR   A 108 ? 0.2157 0.0831 0.1526 0.0119  0.0061  0.0205  108 THR   A CA  
929  C  C   . THR   A 108 ? 0.1892 0.1093 0.1309 0.0006  -0.0080 0.0103  108 THR   A C   
930  O  O   . THR   A 108 ? 0.2030 0.1217 0.1354 0.0098  -0.0069 0.0107  108 THR   A O   
931  C  CB  . THR   A 108 ? 0.2165 0.1174 0.1489 0.0179  -0.0125 0.0000  108 THR   A CB  
932  O  OG1 . THR   A 108 ? 0.2098 0.1133 0.1534 0.0190  -0.0099 0.0075  108 THR   A OG1 
933  C  CG2 . THR   A 108 ? 0.2314 0.1312 0.1550 0.0074  0.0055  -0.0005 108 THR   A CG2 
934  N  N   . VAL   A 109 ? 0.2082 0.1079 0.1477 -0.0083 0.0016  0.0270  109 VAL   A N   
935  C  CA  . VAL   A 109 ? 0.2200 0.1221 0.1509 0.0078  0.0086  0.0284  109 VAL   A CA  
936  C  C   . VAL   A 109 ? 0.2260 0.1041 0.1817 -0.0115 0.0165  0.0386  109 VAL   A C   
937  O  O   . VAL   A 109 ? 0.2273 0.1032 0.1989 -0.0104 0.0143  0.0284  109 VAL   A O   
938  C  CB  . VAL   A 109 ? 0.2051 0.1511 0.1786 -0.0048 0.0092  0.0422  109 VAL   A CB  
939  C  CG1 . VAL   A 109 ? 0.2257 0.1654 0.2064 -0.0107 0.0301  0.0356  109 VAL   A CG1 
940  C  CG2 . VAL   A 109 ? 0.2131 0.1393 0.1995 0.0027  -0.0034 0.0352  109 VAL   A CG2 
941  N  N   . ASP   A 110 ? 0.2418 0.1390 0.1652 0.0174  0.0119  0.0473  110 ASP   A N   
942  C  CA  . ASP   A 110 ? 0.2657 0.1269 0.1879 0.0190  0.0201  0.0465  110 ASP   A CA  
943  C  C   . ASP   A 110 ? 0.2776 0.1088 0.1701 0.0009  0.0040  0.0378  110 ASP   A C   
944  O  O   . ASP   A 110 ? 0.3151 0.1190 0.1978 0.0065  0.0013  0.0479  110 ASP   A O   
945  C  CB  . ASP   A 110 ? 0.3180 0.1585 0.2094 0.0096  0.0461  0.0731  110 ASP   A CB  
946  C  CG  . ASP   A 110 ? 0.3243 0.1731 0.1883 0.0209  0.0324  0.0623  110 ASP   A CG  
947  O  OD1 . ASP   A 110 ? 0.3105 0.1835 0.2334 0.0176  0.0463  0.0452  110 ASP   A OD1 
948  O  OD2 . ASP   A 110 ? 0.3244 0.3046 0.2348 -0.0125 0.0620  0.0400  110 ASP   A OD2 
949  N  N   . LYS   A 111 ? 0.2303 0.1216 0.1815 0.0025  -0.0195 0.0339  111 LYS   A N   
950  C  CA  . LYS   A 111 ? 0.2600 0.1131 0.1733 0.0250  -0.0133 0.0243  111 LYS   A CA  
951  C  C   . LYS   A 111 ? 0.2648 0.1229 0.1731 0.0120  -0.0044 0.0280  111 LYS   A C   
952  O  O   . LYS   A 111 ? 0.2631 0.1655 0.2118 0.0121  0.0085  -0.0003 111 LYS   A O   
953  C  CB  . LYS   A 111 ? 0.2924 0.1632 0.1837 0.0609  -0.0162 0.0416  111 LYS   A CB  
954  C  CG  . LYS   A 111 ? 0.3454 0.2269 0.2044 0.1128  -0.0598 0.0302  111 LYS   A CG  
955  C  CD  . LYS   A 111 ? 0.3287 0.3198 0.3304 0.0612  -0.0587 -0.0249 111 LYS   A CD  
956  C  CE  . LYS   A 111 ? 0.4568 0.4251 0.3438 0.0985  -0.1168 -0.0363 111 LYS   A CE  
957  N  NZ  . LYS   A 111 ? 0.4610 0.5128 0.5005 0.1118  -0.1349 0.0309  111 LYS   A NZ  
958  N  N   . LYS   A 112 ? 0.2321 0.1091 0.1669 -0.0005 -0.0059 0.0254  112 LYS   A N   
959  C  CA  . LYS   A 112 ? 0.2564 0.1328 0.1615 0.0082  0.0073  0.0168  112 LYS   A CA  
960  C  C   . LYS   A 112 ? 0.2323 0.1129 0.1488 0.0190  -0.0084 0.0159  112 LYS   A C   
961  O  O   . LYS   A 112 ? 0.2287 0.1102 0.1694 0.0087  0.0061  0.0027  112 LYS   A O   
962  C  CB  . LYS   A 112 ? 0.2577 0.1781 0.1982 -0.0416 -0.0163 0.0293  112 LYS   A CB  
963  C  CG  . LYS   A 112 ? 0.2526 0.2210 0.2391 -0.0047 -0.0276 -0.0450 112 LYS   A CG  
964  C  CD  . LYS   A 112 ? 0.2740 0.2782 0.2749 -0.0251 -0.0116 0.0466  112 LYS   A CD  
965  C  CE  . LYS   A 112 ? 0.3831 0.2328 0.3551 -0.0062 -0.1294 0.0150  112 LYS   A CE  
966  N  NZ  . LYS   A 112 ? 0.3768 0.2409 0.3201 -0.0040 -0.0609 0.0569  112 LYS   A NZ  
967  N  N   . LYS   A 113 ? 0.2542 0.1262 0.1482 0.0315  -0.0031 0.0067  113 LYS   A N   
968  C  CA  A LYS   A 113 ? 0.2438 0.1228 0.1646 0.0310  -0.0031 0.0193  113 LYS   A CA  
969  C  CA  B LYS   A 113 ? 0.2412 0.1327 0.1611 0.0336  -0.0005 0.0198  113 LYS   A CA  
970  C  C   . LYS   A 113 ? 0.2483 0.0953 0.1904 0.0147  0.0027  0.0226  113 LYS   A C   
971  O  O   . LYS   A 113 ? 0.2983 0.0828 0.2188 0.0072  -0.0168 0.0105  113 LYS   A O   
972  C  CB  A LYS   A 113 ? 0.2249 0.1198 0.2097 0.0177  -0.0115 -0.0154 113 LYS   A CB  
973  C  CB  B LYS   A 113 ? 0.2323 0.1381 0.2135 0.0388  -0.0051 -0.0078 113 LYS   A CB  
974  C  CG  A LYS   A 113 ? 0.2240 0.1449 0.1795 0.0147  -0.0010 -0.0011 113 LYS   A CG  
975  C  CG  B LYS   A 113 ? 0.2381 0.1659 0.1676 0.0228  0.0092  -0.0012 113 LYS   A CG  
976  C  CD  A LYS   A 113 ? 0.2537 0.0845 0.2352 0.0370  0.0125  -0.0244 113 LYS   A CD  
977  C  CD  B LYS   A 113 ? 0.2115 0.2337 0.1900 0.0122  0.0163  0.0022  113 LYS   A CD  
978  C  CE  A LYS   A 113 ? 0.2397 0.2253 0.2009 0.0002  0.0254  0.0006  113 LYS   A CE  
979  C  CE  B LYS   A 113 ? 0.2132 0.2183 0.2167 0.0044  -0.0091 0.0403  113 LYS   A CE  
980  N  NZ  A LYS   A 113 ? 0.2345 0.2584 0.2329 0.0397  -0.0260 -0.0151 113 LYS   A NZ  
981  N  NZ  B LYS   A 113 ? 0.2358 0.2289 0.2892 -0.0001 0.0160  0.0043  113 LYS   A NZ  
982  N  N   . TYR   A 114 ? 0.1988 0.0962 0.1729 0.0071  0.0023  0.0091  114 TYR   A N   
983  C  CA  . TYR   A 114 ? 0.1914 0.1031 0.1723 -0.0021 -0.0089 0.0027  114 TYR   A CA  
984  C  C   . TYR   A 114 ? 0.2129 0.0850 0.1594 -0.0006 0.0016  -0.0065 114 TYR   A C   
985  O  O   . TYR   A 114 ? 0.2006 0.1091 0.1717 -0.0035 0.0172  -0.0097 114 TYR   A O   
986  C  CB  . TYR   A 114 ? 0.1967 0.0946 0.1832 0.0046  0.0217  0.0168  114 TYR   A CB  
987  C  CG  . TYR   A 114 ? 0.2002 0.1074 0.1719 -0.0017 0.0012  0.0190  114 TYR   A CG  
988  C  CD1 . TYR   A 114 ? 0.2376 0.1206 0.1712 0.0285  0.0057  0.0111  114 TYR   A CD1 
989  C  CD2 . TYR   A 114 ? 0.1961 0.1158 0.2287 -0.0097 0.0118  0.0315  114 TYR   A CD2 
990  C  CE1 . TYR   A 114 ? 0.2726 0.1635 0.1791 0.0117  0.0204  0.0303  114 TYR   A CE1 
991  C  CE2 . TYR   A 114 ? 0.2062 0.1509 0.2427 0.0039  0.0348  0.0225  114 TYR   A CE2 
992  C  CZ  . TYR   A 114 ? 0.2641 0.1860 0.2214 -0.0006 0.0390  0.0491  114 TYR   A CZ  
993  O  OH  . TYR   A 114 ? 0.3091 0.3264 0.2784 0.0258  0.0913  0.0963  114 TYR   A OH  
994  N  N   . ALA   A 115 ? 0.2197 0.0807 0.1659 -0.0093 -0.0098 -0.0089 115 ALA   A N   
995  C  CA  . ALA   A 115 ? 0.2303 0.0844 0.1650 -0.0130 0.0010  -0.0198 115 ALA   A CA  
996  C  C   . ALA   A 115 ? 0.1870 0.0966 0.1654 0.0017  -0.0034 -0.0066 115 ALA   A C   
997  O  O   . ALA   A 115 ? 0.2029 0.1005 0.1948 -0.0062 0.0172  -0.0197 115 ALA   A O   
998  C  CB  . ALA   A 115 ? 0.2304 0.1165 0.1903 -0.0386 -0.0099 -0.0200 115 ALA   A CB  
999  N  N   . ALA   A 116 ? 0.1856 0.0881 0.1621 -0.0027 0.0027  -0.0071 116 ALA   A N   
1000 C  CA  . ALA   A 116 ? 0.2033 0.0885 0.1357 -0.0136 0.0053  -0.0053 116 ALA   A CA  
1001 C  C   . ALA   A 116 ? 0.1791 0.1040 0.1256 0.0069  -0.0020 0.0018  116 ALA   A C   
1002 O  O   . ALA   A 116 ? 0.1800 0.1057 0.1375 -0.0023 0.0031  -0.0027 116 ALA   A O   
1003 C  CB  . ALA   A 116 ? 0.2077 0.1201 0.1349 -0.0152 -0.0078 -0.0072 116 ALA   A CB  
1004 N  N   . GLU   A 117 ? 0.1796 0.0892 0.1412 0.0035  -0.0133 -0.0053 117 GLU   A N   
1005 C  CA  . GLU   A 117 ? 0.1949 0.0844 0.1190 -0.0008 -0.0107 -0.0050 117 GLU   A CA  
1006 C  C   . GLU   A 117 ? 0.1824 0.0973 0.1073 -0.0048 -0.0078 -0.0031 117 GLU   A C   
1007 O  O   . GLU   A 117 ? 0.1841 0.1151 0.1445 0.0008  0.0038  0.0179  117 GLU   A O   
1008 C  CB  . GLU   A 117 ? 0.1946 0.1041 0.1110 0.0027  -0.0145 -0.0071 117 GLU   A CB  
1009 C  CG  . GLU   A 117 ? 0.1980 0.1071 0.1156 0.0115  -0.0259 -0.0030 117 GLU   A CG  
1010 C  CD  . GLU   A 117 ? 0.1747 0.1077 0.1165 0.0052  -0.0066 -0.0044 117 GLU   A CD  
1011 O  OE1 . GLU   A 117 ? 0.1793 0.1251 0.1437 0.0114  -0.0161 0.0053  117 GLU   A OE1 
1012 O  OE2 . GLU   A 117 ? 0.1957 0.1079 0.1174 -0.0004 -0.0236 0.0031  117 GLU   A OE2 
1013 N  N   . LEU   A 118 ? 0.1900 0.0874 0.1258 0.0023  -0.0174 -0.0079 118 LEU   A N   
1014 C  CA  . LEU   A 118 ? 0.1840 0.0869 0.1284 -0.0057 -0.0172 -0.0016 118 LEU   A CA  
1015 C  C   . LEU   A 118 ? 0.1720 0.0897 0.1201 0.0030  -0.0114 0.0012  118 LEU   A C   
1016 O  O   . LEU   A 118 ? 0.1879 0.0858 0.1226 -0.0041 -0.0131 0.0010  118 LEU   A O   
1017 C  CB  . LEU   A 118 ? 0.1890 0.1061 0.1491 -0.0017 -0.0295 0.0150  118 LEU   A CB  
1018 C  CG  . LEU   A 118 ? 0.1879 0.1183 0.1386 0.0020  -0.0309 0.0201  118 LEU   A CG  
1019 C  CD1 . LEU   A 118 ? 0.2171 0.1119 0.1407 -0.0089 -0.0403 0.0265  118 LEU   A CD1 
1020 C  CD2 . LEU   A 118 ? 0.1835 0.1494 0.1587 -0.0075 -0.0280 0.0124  118 LEU   A CD2 
1021 N  N   . HIS   A 119 ? 0.1797 0.0879 0.1110 -0.0033 -0.0194 0.0021  119 HIS   A N   
1022 C  CA  . HIS   A 119 ? 0.1820 0.0933 0.1089 -0.0047 -0.0193 0.0046  119 HIS   A CA  
1023 C  C   . HIS   A 119 ? 0.1887 0.0864 0.1106 -0.0086 -0.0239 -0.0003 119 HIS   A C   
1024 O  O   . HIS   A 119 ? 0.2007 0.1086 0.1147 -0.0013 -0.0184 0.0115  119 HIS   A O   
1025 C  CB  . HIS   A 119 ? 0.1729 0.0899 0.1302 -0.0041 -0.0137 0.0069  119 HIS   A CB  
1026 C  CG  . HIS   A 119 ? 0.1649 0.0966 0.1160 -0.0091 0.0015  -0.0048 119 HIS   A CG  
1027 N  ND1 . HIS   A 119 ? 0.1625 0.1074 0.1061 -0.0212 0.0048  0.0078  119 HIS   A ND1 
1028 C  CD2 . HIS   A 119 ? 0.1688 0.1084 0.1244 -0.0022 -0.0140 0.0105  119 HIS   A CD2 
1029 C  CE1 . HIS   A 119 ? 0.1722 0.1077 0.0998 -0.0117 -0.0105 0.0036  119 HIS   A CE1 
1030 N  NE2 . HIS   A 119 ? 0.1621 0.1084 0.1322 -0.0041 -0.0121 0.0073  119 HIS   A NE2 
1031 N  N   . LEU   A 120 ? 0.1812 0.0836 0.1326 -0.0037 -0.0249 0.0010  120 LEU   A N   
1032 C  CA  . LEU   A 120 ? 0.1793 0.0854 0.1537 -0.0004 -0.0323 0.0050  120 LEU   A CA  
1033 C  C   . LEU   A 120 ? 0.1775 0.0833 0.1217 0.0096  -0.0197 0.0078  120 LEU   A C   
1034 O  O   . LEU   A 120 ? 0.1749 0.0912 0.1253 -0.0068 -0.0238 0.0035  120 LEU   A O   
1035 C  CB  . LEU   A 120 ? 0.1807 0.0944 0.1753 -0.0023 -0.0301 0.0061  120 LEU   A CB  
1036 C  CG  . LEU   A 120 ? 0.2060 0.1306 0.1593 -0.0237 -0.0487 0.0048  120 LEU   A CG  
1037 C  CD1 . LEU   A 120 ? 0.2824 0.1326 0.1849 -0.0618 -0.0241 0.0085  120 LEU   A CD1 
1038 C  CD2 . LEU   A 120 ? 0.2178 0.1676 0.1939 0.0038  -0.0767 -0.0068 120 LEU   A CD2 
1039 N  N   . VAL   A 121 ? 0.1874 0.0883 0.1318 -0.0057 -0.0113 0.0058  121 VAL   A N   
1040 C  CA  . VAL   A 121 ? 0.2016 0.0809 0.1398 -0.0065 -0.0118 0.0092  121 VAL   A CA  
1041 C  C   . VAL   A 121 ? 0.1776 0.0941 0.1383 -0.0182 -0.0192 0.0085  121 VAL   A C   
1042 O  O   . VAL   A 121 ? 0.1974 0.1068 0.1424 -0.0023 -0.0212 0.0143  121 VAL   A O   
1043 C  CB  . VAL   A 121 ? 0.1986 0.0886 0.1506 -0.0086 -0.0129 0.0006  121 VAL   A CB  
1044 C  CG1 . VAL   A 121 ? 0.2168 0.0977 0.1791 -0.0129 -0.0219 -0.0148 121 VAL   A CG1 
1045 C  CG2 . VAL   A 121 ? 0.2251 0.0979 0.1448 0.0161  -0.0098 0.0042  121 VAL   A CG2 
1046 N  N   . HIS   A 122 ? 0.1873 0.0865 0.1463 -0.0147 -0.0229 -0.0009 122 HIS   A N   
1047 C  CA  . HIS   A 122 ? 0.1926 0.0798 0.1529 -0.0115 -0.0152 0.0054  122 HIS   A CA  
1048 C  C   . HIS   A 122 ? 0.1961 0.0820 0.1520 -0.0046 -0.0136 0.0001  122 HIS   A C   
1049 O  O   . HIS   A 122 ? 0.2007 0.0928 0.1673 -0.0079 -0.0303 0.0079  122 HIS   A O   
1050 C  CB  . HIS   A 122 ? 0.1866 0.0840 0.1693 0.0016  -0.0114 0.0002  122 HIS   A CB  
1051 C  CG  . HIS   A 122 ? 0.1869 0.0901 0.1560 0.0029  -0.0132 0.0094  122 HIS   A CG  
1052 N  ND1 . HIS   A 122 ? 0.1793 0.0872 0.1625 -0.0016 -0.0044 0.0043  122 HIS   A ND1 
1053 C  CD2 . HIS   A 122 ? 0.1861 0.1188 0.1583 -0.0146 -0.0079 0.0037  122 HIS   A CD2 
1054 C  CE1 . HIS   A 122 ? 0.1799 0.1217 0.1684 -0.0033 -0.0172 -0.0057 122 HIS   A CE1 
1055 N  NE2 . HIS   A 122 ? 0.1806 0.1165 0.1720 -0.0122 -0.0189 0.0025  122 HIS   A NE2 
1056 N  N   . TRP   A 123 ? 0.1993 0.0803 0.1527 -0.0062 -0.0157 -0.0027 123 TRP   A N   
1057 C  CA  . TRP   A 123 ? 0.1922 0.0943 0.1652 -0.0089 -0.0054 -0.0133 123 TRP   A CA  
1058 C  C   . TRP   A 123 ? 0.1916 0.0751 0.1632 -0.0089 -0.0141 -0.0044 123 TRP   A C   
1059 O  O   . TRP   A 123 ? 0.1928 0.0944 0.1917 0.0002  -0.0306 -0.0046 123 TRP   A O   
1060 C  CB  . TRP   A 123 ? 0.2136 0.1538 0.1584 -0.0146 -0.0048 0.0104  123 TRP   A CB  
1061 C  CG  . TRP   A 123 ? 0.2168 0.1037 0.1720 -0.0218 0.0025  0.0081  123 TRP   A CG  
1062 C  CD1 . TRP   A 123 ? 0.2555 0.1374 0.1629 -0.0372 -0.0155 0.0152  123 TRP   A CD1 
1063 C  CD2 . TRP   A 123 ? 0.2602 0.0958 0.1771 -0.0243 -0.0016 0.0189  123 TRP   A CD2 
1064 N  NE1 . TRP   A 123 ? 0.2669 0.1002 0.2023 -0.0281 -0.0229 0.0037  123 TRP   A NE1 
1065 C  CE2 . TRP   A 123 ? 0.2861 0.1113 0.1904 -0.0107 -0.0333 0.0076  123 TRP   A CE2 
1066 C  CE3 . TRP   A 123 ? 0.2958 0.0871 0.2251 -0.0427 -0.0174 0.0011  123 TRP   A CE3 
1067 C  CZ2 . TRP   A 123 ? 0.3544 0.0970 0.2028 -0.0212 -0.0232 0.0195  123 TRP   A CZ2 
1068 C  CZ3 . TRP   A 123 ? 0.3506 0.1007 0.2120 -0.0353 -0.0122 0.0173  123 TRP   A CZ3 
1069 C  CH2 . TRP   A 123 ? 0.3634 0.0858 0.2431 -0.0174 -0.0385 0.0075  123 TRP   A CH2 
1070 N  N   . ASN   A 124 ? 0.1940 0.0971 0.1767 -0.0009 -0.0166 -0.0264 124 ASN   A N   
1071 C  CA  . ASN   A 124 ? 0.2327 0.0894 0.1778 0.0085  -0.0122 -0.0252 124 ASN   A CA  
1072 C  C   . ASN   A 124 ? 0.2150 0.0953 0.1945 -0.0025 -0.0100 -0.0131 124 ASN   A C   
1073 O  O   . ASN   A 124 ? 0.2085 0.0982 0.1817 -0.0005 -0.0050 -0.0122 124 ASN   A O   
1074 C  CB  . ASN   A 124 ? 0.2273 0.1172 0.1726 0.0061  -0.0017 -0.0166 124 ASN   A CB  
1075 C  CG  . ASN   A 124 ? 0.2254 0.1232 0.1894 -0.0022 0.0075  -0.0218 124 ASN   A CG  
1076 O  OD1 . ASN   A 124 ? 0.2298 0.1254 0.2265 0.0157  0.0125  -0.0203 124 ASN   A OD1 
1077 N  ND2 . ASN   A 124 ? 0.2926 0.1124 0.1749 -0.0017 0.0067  -0.0273 124 ASN   A ND2 
1078 N  N   . THR   A 125 ? 0.2253 0.0926 0.2386 0.0139  -0.0341 -0.0089 125 THR   A N   
1079 C  CA  . THR   A 125 ? 0.2499 0.0912 0.2287 -0.0042 -0.0200 -0.0066 125 THR   A CA  
1080 C  C   . THR   A 125 ? 0.2429 0.0740 0.2719 0.0131  0.0025  -0.0130 125 THR   A C   
1081 O  O   . THR   A 125 ? 0.2557 0.0989 0.2782 0.0061  -0.0356 -0.0037 125 THR   A O   
1082 C  CB  . THR   A 125 ? 0.2581 0.1496 0.2785 0.0311  -0.0633 -0.0231 125 THR   A CB  
1083 O  OG1 . THR   A 125 ? 0.2771 0.1821 0.3972 0.0632  -0.0167 -0.0331 125 THR   A OG1 
1084 C  CG2 . THR   A 125 ? 0.3049 0.1471 0.3545 -0.0042 -0.1055 -0.0315 125 THR   A CG2 
1085 N  N   . LYS   A 126 ? 0.2518 0.1041 0.2068 0.0044  0.0012  -0.0287 127 LYS   A N   
1086 C  CA  . LYS   A 126 ? 0.2700 0.1195 0.2204 0.0018  -0.0033 -0.0477 127 LYS   A CA  
1087 C  C   . LYS   A 126 ? 0.2627 0.0970 0.2419 0.0048  -0.0133 -0.0271 127 LYS   A C   
1088 O  O   . LYS   A 126 ? 0.3055 0.1088 0.2989 -0.0206 0.0035  -0.0520 127 LYS   A O   
1089 C  CB  . LYS   A 126 ? 0.3177 0.1601 0.2293 -0.0012 -0.0145 -0.0534 127 LYS   A CB  
1090 C  CG  . LYS   A 126 ? 0.2819 0.1693 0.2236 -0.0121 -0.0008 -0.0173 127 LYS   A CG  
1091 C  CD  . LYS   A 126 ? 0.3250 0.2925 0.2143 -0.0372 -0.0369 -0.0139 127 LYS   A CD  
1092 C  CE  . LYS   A 126 ? 0.3257 0.3895 0.2269 0.0041  -0.0414 0.0076  127 LYS   A CE  
1093 N  NZ  . LYS   A 126 ? 0.4960 0.4489 0.2136 0.1535  0.0027  0.0467  127 LYS   A NZ  
1094 N  N   . TYR   A 127 ? 0.2561 0.0968 0.1943 -0.0052 -0.0154 -0.0108 128 TYR   A N   
1095 C  CA  . TYR   A 127 ? 0.2397 0.1292 0.1936 -0.0128 -0.0276 -0.0081 128 TYR   A CA  
1096 C  C   . TYR   A 127 ? 0.2315 0.1138 0.2114 -0.0092 -0.0062 -0.0271 128 TYR   A C   
1097 O  O   . TYR   A 127 ? 0.2531 0.1269 0.2231 -0.0272 0.0050  -0.0212 128 TYR   A O   
1098 C  CB  . TYR   A 127 ? 0.2612 0.1023 0.2024 -0.0041 -0.0092 -0.0178 128 TYR   A CB  
1099 C  CG  . TYR   A 127 ? 0.2411 0.1059 0.2009 -0.0088 -0.0295 -0.0126 128 TYR   A CG  
1100 C  CD1 . TYR   A 127 ? 0.2665 0.1359 0.2037 -0.0329 -0.0139 -0.0177 128 TYR   A CD1 
1101 C  CD2 . TYR   A 127 ? 0.2168 0.1164 0.1920 -0.0102 0.0065  -0.0111 128 TYR   A CD2 
1102 C  CE1 . TYR   A 127 ? 0.2793 0.1357 0.1869 0.0085  -0.0306 -0.0329 128 TYR   A CE1 
1103 C  CE2 . TYR   A 127 ? 0.2240 0.1244 0.1773 0.0100  -0.0081 -0.0275 128 TYR   A CE2 
1104 C  CZ  . TYR   A 127 ? 0.2759 0.1244 0.1848 0.0307  -0.0057 -0.0343 128 TYR   A CZ  
1105 O  OH  . TYR   A 127 ? 0.3114 0.1574 0.1851 0.0175  -0.0035 -0.0424 128 TYR   A OH  
1106 N  N   . GLY   A 128 ? 0.2458 0.1053 0.2060 -0.0102 -0.0083 0.0139  129 GLY   A N   
1107 C  CA  . GLY   A 128 ? 0.2701 0.1144 0.2006 -0.0031 0.0089  -0.0029 129 GLY   A CA  
1108 C  C   . GLY   A 128 ? 0.2836 0.1315 0.1729 -0.0032 -0.0097 0.0166  129 GLY   A C   
1109 O  O   . GLY   A 128 ? 0.3179 0.1153 0.2071 0.0120  -0.0292 0.0122  129 GLY   A O   
1110 N  N   . ASP   A 129 ? 0.3003 0.1132 0.1956 0.0136  -0.0304 -0.0163 130 ASP   A N   
1111 C  CA  . ASP   A 129 ? 0.3466 0.1235 0.1976 0.0381  -0.0069 -0.0104 130 ASP   A CA  
1112 C  C   . ASP   A 129 ? 0.3162 0.1180 0.1909 0.0259  -0.0362 -0.0188 130 ASP   A C   
1113 O  O   . ASP   A 129 ? 0.3226 0.1171 0.1751 0.0223  -0.0286 -0.0164 130 ASP   A O   
1114 C  CB  . ASP   A 129 ? 0.4208 0.1543 0.1626 0.0637  0.0281  0.0362  130 ASP   A CB  
1115 C  CG  . ASP   A 129 ? 0.3786 0.1409 0.4903 0.0801  -0.0034 -0.1292 130 ASP   A CG  
1116 O  OD1 . ASP   A 129 ? 0.4116 0.1953 0.2922 0.0241  -0.0318 0.0333  130 ASP   A OD1 
1117 O  OD2 . ASP   A 129 ? 0.3512 0.1884 0.5011 0.0111  -0.0247 0.0532  130 ASP   A OD2 
1118 N  N   . PHE   A 130 ? 0.3139 0.1124 0.1757 0.0147  -0.0122 -0.0165 131 PHE   A N   
1119 C  CA  . PHE   A 130 ? 0.2740 0.1283 0.1703 0.0257  -0.0294 -0.0096 131 PHE   A CA  
1120 C  C   . PHE   A 130 ? 0.2484 0.1147 0.1951 -0.0070 0.0070  0.0218  131 PHE   A C   
1121 O  O   . PHE   A 130 ? 0.2542 0.1410 0.1543 -0.0321 -0.0037 0.0030  131 PHE   A O   
1122 C  CB  . PHE   A 130 ? 0.2712 0.1195 0.1877 0.0053  -0.0089 -0.0206 131 PHE   A CB  
1123 C  CG  . PHE   A 130 ? 0.2429 0.1150 0.1723 -0.0078 0.0015  -0.0185 131 PHE   A CG  
1124 C  CD1 . PHE   A 130 ? 0.2699 0.1320 0.1789 -0.0414 -0.0053 -0.0074 131 PHE   A CD1 
1125 C  CD2 . PHE   A 130 ? 0.2810 0.1283 0.2343 -0.0091 0.0434  -0.0060 131 PHE   A CD2 
1126 C  CE1 . PHE   A 130 ? 0.2913 0.1328 0.2165 -0.0493 -0.0196 -0.0073 131 PHE   A CE1 
1127 C  CE2 . PHE   A 130 ? 0.3139 0.1462 0.2512 0.0209  0.0096  0.0013  131 PHE   A CE2 
1128 C  CZ  . PHE   A 130 ? 0.3023 0.1443 0.2420 -0.0065 -0.0196 -0.0165 131 PHE   A CZ  
1129 N  N   . GLY   A 131 ? 0.2982 0.1351 0.1868 -0.0270 0.0419  0.0032  132 GLY   A N   
1130 C  CA  . GLY   A 131 ? 0.2809 0.1979 0.1849 -0.0472 0.0337  0.0311  132 GLY   A CA  
1131 C  C   . GLY   A 131 ? 0.2718 0.1611 0.1987 -0.0491 0.0528  0.0088  132 GLY   A C   
1132 O  O   . GLY   A 131 ? 0.2633 0.1649 0.2711 -0.0368 0.0185  -0.0190 132 GLY   A O   
1133 N  N   . LYS   A 132 ? 0.2420 0.1507 0.2066 -0.0497 0.0108  0.0074  133 LYS   A N   
1134 C  CA  . LYS   A 132 ? 0.2538 0.1199 0.2046 -0.0260 -0.0162 0.0176  133 LYS   A CA  
1135 C  C   . LYS   A 132 ? 0.2343 0.1263 0.1944 -0.0319 -0.0168 -0.0011 133 LYS   A C   
1136 O  O   . LYS   A 132 ? 0.2229 0.1577 0.1895 -0.0430 -0.0113 -0.0032 133 LYS   A O   
1137 C  CB  . LYS   A 132 ? 0.2822 0.1333 0.2425 0.0027  -0.0173 0.0208  133 LYS   A CB  
1138 C  CG  . LYS   A 132 ? 0.4073 0.2430 0.3770 -0.0675 -0.0480 0.1148  133 LYS   A CG  
1139 C  CD  . LYS   A 132 ? 0.4001 0.2053 0.6512 -0.0153 0.0434  0.1491  133 LYS   A CD  
1140 C  CE  . LYS   A 132 ? 0.4994 0.3141 0.6347 0.0473  0.1482  0.2002  133 LYS   A CE  
1141 N  NZ  . LYS   A 132 ? 0.5206 0.4210 0.6703 0.0048  -0.0266 0.3037  133 LYS   A NZ  
1142 N  N   . ALA   A 133 ? 0.2194 0.1271 0.1768 -0.0300 -0.0059 0.0008  134 ALA   A N   
1143 C  CA  . ALA   A 133 ? 0.2039 0.1445 0.1527 -0.0229 -0.0046 0.0105  134 ALA   A CA  
1144 C  C   . ALA   A 133 ? 0.2118 0.1263 0.1640 -0.0263 0.0002  0.0055  134 ALA   A C   
1145 O  O   . ALA   A 133 ? 0.1887 0.1630 0.1599 -0.0097 -0.0015 -0.0074 134 ALA   A O   
1146 C  CB  . ALA   A 133 ? 0.2010 0.1465 0.1763 -0.0216 -0.0195 -0.0006 134 ALA   A CB  
1147 N  N   . VAL   A 134 ? 0.2108 0.1341 0.1694 -0.0266 0.0092  0.0024  135 VAL   A N   
1148 C  CA  . VAL   A 134 ? 0.2161 0.1601 0.1661 -0.0146 0.0111  0.0154  135 VAL   A CA  
1149 C  C   . VAL   A 134 ? 0.2006 0.1485 0.1750 -0.0136 0.0160  0.0127  135 VAL   A C   
1150 O  O   . VAL   A 134 ? 0.2158 0.1628 0.1975 0.0079  0.0195  0.0190  135 VAL   A O   
1151 C  CB  . VAL   A 134 ? 0.2395 0.1670 0.1799 -0.0389 0.0258  -0.0060 135 VAL   A CB  
1152 C  CG1 . VAL   A 134 ? 0.2592 0.1988 0.2007 -0.0461 0.0125  -0.0205 135 VAL   A CG1 
1153 C  CG2 . VAL   A 134 ? 0.2507 0.1697 0.1863 -0.0256 0.0395  0.0039  135 VAL   A CG2 
1154 N  N   . GLN   A 135 ? 0.2182 0.1597 0.1787 -0.0307 0.0251  -0.0048 136 GLN   A N   
1155 C  CA  . GLN   A 135 ? 0.2322 0.1870 0.2094 -0.0401 -0.0071 -0.0110 136 GLN   A CA  
1156 C  C   . GLN   A 135 ? 0.2064 0.1540 0.1989 -0.0223 -0.0186 -0.0024 136 GLN   A C   
1157 O  O   . GLN   A 135 ? 0.2107 0.2212 0.2096 -0.0388 -0.0097 -0.0210 136 GLN   A O   
1158 C  CB  . GLN   A 135 ? 0.2318 0.2090 0.2390 -0.0590 0.0149  -0.0021 136 GLN   A CB  
1159 C  CG  . GLN   A 135 ? 0.2780 0.2770 0.2456 -0.0815 0.0318  0.0170  136 GLN   A CG  
1160 C  CD  . GLN   A 135 ? 0.3440 0.3098 0.3177 -0.1076 0.0048  0.0177  136 GLN   A CD  
1161 O  OE1 . GLN   A 135 ? 0.4351 0.3978 0.4104 -0.1973 -0.0468 0.0372  136 GLN   A OE1 
1162 N  NE2 . GLN   A 135 ? 0.2944 0.3854 0.4046 -0.0609 0.0038  0.0442  136 GLN   A NE2 
1163 N  N   . GLN   A 136 ? 0.1992 0.1526 0.1798 -0.0146 -0.0006 -0.0055 137 GLN   A N   
1164 C  CA  . GLN   A 136 ? 0.2146 0.1460 0.1472 -0.0103 -0.0155 -0.0104 137 GLN   A CA  
1165 C  C   . GLN   A 136 ? 0.1996 0.1435 0.1487 0.0114  -0.0102 -0.0218 137 GLN   A C   
1166 O  O   . GLN   A 136 ? 0.2169 0.1461 0.1386 -0.0035 -0.0033 -0.0166 137 GLN   A O   
1167 C  CB  . GLN   A 136 ? 0.2229 0.1169 0.1988 -0.0144 -0.0259 0.0016  137 GLN   A CB  
1168 C  CG  . GLN   A 136 ? 0.2703 0.1543 0.2287 -0.0263 0.0001  0.0209  137 GLN   A CG  
1169 C  CD  . GLN   A 136 ? 0.2540 0.1551 0.1873 -0.0055 -0.0016 0.0006  137 GLN   A CD  
1170 O  OE1 . GLN   A 136 ? 0.2703 0.1712 0.2186 -0.0041 -0.0154 -0.0372 137 GLN   A OE1 
1171 N  NE2 . GLN   A 136 ? 0.3156 0.2121 0.2154 -0.0463 0.0081  0.0156  137 GLN   A NE2 
1172 N  N   . PRO   A 137 ? 0.1961 0.1525 0.1531 -0.0082 -0.0084 -0.0231 138 PRO   A N   
1173 C  CA  . PRO   A 137 ? 0.2175 0.1635 0.1469 0.0057  -0.0163 0.0161  138 PRO   A CA  
1174 C  C   . PRO   A 137 ? 0.2048 0.1712 0.1423 -0.0068 0.0012  0.0022  138 PRO   A C   
1175 O  O   . PRO   A 137 ? 0.2429 0.1610 0.2516 -0.0027 -0.0074 0.0298  138 PRO   A O   
1176 C  CB  . PRO   A 137 ? 0.2779 0.2319 0.1489 0.0051  -0.0207 0.0016  138 PRO   A CB  
1177 C  CG  . PRO   A 137 ? 0.4456 0.2694 0.1559 -0.0694 -0.0592 -0.0106 138 PRO   A CG  
1178 C  CD  . PRO   A 137 ? 0.2414 0.2224 0.1675 -0.0406 -0.0337 -0.0315 138 PRO   A CD  
1179 N  N   . ASP   A 138 ? 0.2035 0.1570 0.1562 0.0000  -0.0069 -0.0175 139 ASP   A N   
1180 C  CA  . ASP   A 138 ? 0.2011 0.1544 0.1512 -0.0078 0.0010  -0.0036 139 ASP   A CA  
1181 C  C   . ASP   A 138 ? 0.1965 0.1181 0.1518 -0.0177 0.0037  -0.0070 139 ASP   A C   
1182 O  O   . ASP   A 138 ? 0.2010 0.1435 0.1775 -0.0003 0.0018  -0.0013 139 ASP   A O   
1183 C  CB  . ASP   A 138 ? 0.2440 0.1788 0.1465 -0.0061 0.0051  -0.0204 139 ASP   A CB  
1184 C  CG  . ASP   A 138 ? 0.2150 0.2011 0.2005 -0.0079 0.0092  -0.0461 139 ASP   A CG  
1185 O  OD1 . ASP   A 138 ? 0.2444 0.1560 0.2069 0.0072  0.0122  -0.0446 139 ASP   A OD1 
1186 O  OD2 . ASP   A 138 ? 0.2584 0.2158 0.2160 0.0201  0.0243  -0.0402 139 ASP   A OD2 
1187 N  N   . GLY   A 139 ? 0.1834 0.1120 0.1450 -0.0054 -0.0048 -0.0143 140 GLY   A N   
1188 C  CA  . GLY   A 139 ? 0.2140 0.1221 0.1448 -0.0194 -0.0259 -0.0077 140 GLY   A CA  
1189 C  C   . GLY   A 139 ? 0.1895 0.0962 0.1391 -0.0137 0.0002  -0.0029 140 GLY   A C   
1190 O  O   . GLY   A 139 ? 0.2060 0.0930 0.1536 -0.0048 -0.0161 0.0000  140 GLY   A O   
1191 N  N   . LEU   A 140 ? 0.1645 0.0969 0.1547 -0.0102 -0.0032 -0.0117 141 LEU   A N   
1192 C  CA  . LEU   A 140 ? 0.1654 0.1004 0.1451 -0.0042 -0.0044 -0.0162 141 LEU   A CA  
1193 C  C   . LEU   A 140 ? 0.1601 0.0974 0.1374 0.0115  -0.0129 -0.0004 141 LEU   A C   
1194 O  O   . LEU   A 140 ? 0.1778 0.0973 0.1390 -0.0057 -0.0141 -0.0001 141 LEU   A O   
1195 C  CB  . LEU   A 140 ? 0.1791 0.0995 0.1586 -0.0006 0.0027  -0.0034 141 LEU   A CB  
1196 C  CG  . LEU   A 140 ? 0.2369 0.1082 0.1823 0.0125  0.0373  0.0100  141 LEU   A CG  
1197 C  CD1 . LEU   A 140 ? 0.1902 0.1417 0.1615 0.0137  0.0175  -0.0118 141 LEU   A CD1 
1198 C  CD2 . LEU   A 140 ? 0.2982 0.1331 0.2491 0.0406  0.0614  0.0484  141 LEU   A CD2 
1199 N  N   . ALA   A 141 ? 0.1601 0.1057 0.1389 0.0010  -0.0086 -0.0006 142 ALA   A N   
1200 C  CA  . ALA   A 141 ? 0.1771 0.0838 0.1544 -0.0074 -0.0006 -0.0077 142 ALA   A CA  
1201 C  C   . ALA   A 141 ? 0.1657 0.1014 0.1169 -0.0086 -0.0100 0.0031  142 ALA   A C   
1202 O  O   . ALA   A 141 ? 0.1907 0.0968 0.1464 -0.0020 -0.0277 0.0057  142 ALA   A O   
1203 C  CB  . ALA   A 141 ? 0.1778 0.1174 0.1845 -0.0111 0.0017  0.0064  142 ALA   A CB  
1204 N  N   . VAL   A 142 ? 0.1694 0.0886 0.1411 -0.0078 -0.0110 0.0034  143 VAL   A N   
1205 C  CA  . VAL   A 142 ? 0.1760 0.0995 0.1165 -0.0019 -0.0109 -0.0009 143 VAL   A CA  
1206 C  C   . VAL   A 142 ? 0.1849 0.0845 0.1207 0.0080  -0.0098 0.0040  143 VAL   A C   
1207 O  O   . VAL   A 142 ? 0.1732 0.1034 0.1264 -0.0020 -0.0150 0.0037  143 VAL   A O   
1208 C  CB  . VAL   A 142 ? 0.1627 0.1165 0.1271 -0.0053 -0.0178 0.0015  143 VAL   A CB  
1209 C  CG1 . VAL   A 142 ? 0.1852 0.1286 0.1283 0.0108  -0.0154 -0.0121 143 VAL   A CG1 
1210 C  CG2 . VAL   A 142 ? 0.1882 0.1514 0.1276 -0.0183 -0.0142 0.0131  143 VAL   A CG2 
1211 N  N   . LEU   A 143 ? 0.1624 0.0932 0.1329 -0.0012 -0.0146 0.0044  144 LEU   A N   
1212 C  CA  . LEU   A 143 ? 0.1615 0.0926 0.1488 -0.0026 -0.0201 -0.0008 144 LEU   A CA  
1213 C  C   . LEU   A 143 ? 0.1661 0.0994 0.1231 -0.0132 -0.0125 0.0063  144 LEU   A C   
1214 O  O   . LEU   A 143 ? 0.1903 0.1032 0.1204 -0.0023 -0.0102 0.0024  144 LEU   A O   
1215 C  CB  . LEU   A 143 ? 0.1777 0.1293 0.1473 -0.0026 -0.0195 0.0203  144 LEU   A CB  
1216 C  CG  . LEU   A 143 ? 0.1764 0.1238 0.2002 -0.0030 -0.0076 0.0116  144 LEU   A CG  
1217 C  CD1 . LEU   A 143 ? 0.1679 0.1847 0.1987 -0.0077 -0.0068 0.0378  144 LEU   A CD1 
1218 C  CD2 . LEU   A 143 ? 0.1814 0.1815 0.2049 0.0038  -0.0341 0.0044  144 LEU   A CD2 
1219 N  N   . GLY   A 144 ? 0.1701 0.0861 0.1283 -0.0080 -0.0168 0.0055  145 GLY   A N   
1220 C  CA  . GLY   A 144 ? 0.1714 0.0856 0.1274 -0.0035 -0.0125 0.0018  145 GLY   A CA  
1221 C  C   . GLY   A 144 ? 0.1694 0.0850 0.1243 -0.0071 -0.0185 0.0025  145 GLY   A C   
1222 O  O   . GLY   A 144 ? 0.1838 0.1084 0.1331 -0.0152 -0.0021 0.0061  145 GLY   A O   
1223 N  N   . ILE   A 145 ? 0.1793 0.0874 0.1270 -0.0072 -0.0179 -0.0053 146 ILE   A N   
1224 C  CA  . ILE   A 145 ? 0.1674 0.0856 0.1346 -0.0086 -0.0212 0.0016  146 ILE   A CA  
1225 C  C   . ILE   A 145 ? 0.1655 0.0784 0.1445 -0.0055 -0.0168 -0.0042 146 ILE   A C   
1226 O  O   . ILE   A 145 ? 0.1745 0.0919 0.1474 -0.0070 0.0001  -0.0009 146 ILE   A O   
1227 C  CB  . ILE   A 145 ? 0.1819 0.1027 0.1533 -0.0012 -0.0244 0.0064  146 ILE   A CB  
1228 C  CG1 . ILE   A 145 ? 0.2168 0.1181 0.1824 0.0358  -0.0480 -0.0075 146 ILE   A CG1 
1229 C  CG2 . ILE   A 145 ? 0.1736 0.1207 0.2154 -0.0038 -0.0293 -0.0042 146 ILE   A CG2 
1230 C  CD1 . ILE   A 145 ? 0.2066 0.1317 0.1634 0.0079  -0.0410 0.0068  146 ILE   A CD1 
1231 N  N   . PHE   A 146 ? 0.1687 0.0921 0.1411 0.0016  -0.0177 0.0037  147 PHE   A N   
1232 C  CA  . PHE   A 146 ? 0.1900 0.0817 0.1326 0.0091  -0.0162 0.0013  147 PHE   A CA  
1233 C  C   . PHE   A 146 ? 0.1867 0.0994 0.1459 0.0029  -0.0118 -0.0041 147 PHE   A C   
1234 O  O   . PHE   A 146 ? 0.1834 0.1104 0.1571 -0.0043 -0.0127 -0.0095 147 PHE   A O   
1235 C  CB  . PHE   A 146 ? 0.1888 0.0985 0.1455 -0.0073 -0.0205 0.0089  147 PHE   A CB  
1236 C  CG  . PHE   A 146 ? 0.1872 0.0833 0.1356 -0.0032 -0.0190 0.0125  147 PHE   A CG  
1237 C  CD1 . PHE   A 146 ? 0.1830 0.0962 0.1478 -0.0004 -0.0167 0.0009  147 PHE   A CD1 
1238 C  CD2 . PHE   A 146 ? 0.2161 0.0804 0.1446 -0.0110 -0.0115 0.0209  147 PHE   A CD2 
1239 C  CE1 . PHE   A 146 ? 0.1860 0.1025 0.1476 0.0027  -0.0161 0.0004  147 PHE   A CE1 
1240 C  CE2 . PHE   A 146 ? 0.1930 0.1000 0.1518 -0.0108 -0.0029 0.0115  147 PHE   A CE2 
1241 C  CZ  . PHE   A 146 ? 0.1812 0.1067 0.1568 -0.0017 -0.0079 0.0294  147 PHE   A CZ  
1242 N  N   . LEU   A 147 ? 0.1943 0.1002 0.1339 -0.0042 -0.0070 -0.0081 148 LEU   A N   
1243 C  CA  . LEU   A 147 ? 0.2118 0.0953 0.1137 -0.0111 -0.0122 -0.0068 148 LEU   A CA  
1244 C  C   . LEU   A 147 ? 0.2036 0.1046 0.1403 -0.0171 -0.0230 0.0004  148 LEU   A C   
1245 O  O   . LEU   A 147 ? 0.2015 0.0998 0.1767 -0.0102 -0.0093 0.0103  148 LEU   A O   
1246 C  CB  . LEU   A 147 ? 0.2200 0.1039 0.1323 -0.0181 -0.0095 -0.0087 148 LEU   A CB  
1247 C  CG  . LEU   A 147 ? 0.2133 0.0998 0.1398 -0.0166 -0.0274 -0.0027 148 LEU   A CG  
1248 C  CD1 . LEU   A 147 ? 0.2684 0.1023 0.1565 -0.0159 -0.0264 0.0013  148 LEU   A CD1 
1249 C  CD2 . LEU   A 147 ? 0.2413 0.1406 0.1575 -0.0135 -0.0196 0.0093  148 LEU   A CD2 
1250 N  N   . LYS   A 148 ? 0.2110 0.0939 0.1634 -0.0260 -0.0247 -0.0089 149 LYS   A N   
1251 C  CA  . LYS   A 148 ? 0.2264 0.0870 0.1747 -0.0196 -0.0201 0.0050  149 LYS   A CA  
1252 C  C   . LYS   A 148 ? 0.2165 0.1102 0.1688 -0.0068 -0.0228 0.0050  149 LYS   A C   
1253 O  O   . LYS   A 148 ? 0.2618 0.1291 0.1789 0.0234  -0.0502 -0.0163 149 LYS   A O   
1254 C  CB  . LYS   A 148 ? 0.2661 0.1588 0.1749 -0.0528 -0.0298 0.0266  149 LYS   A CB  
1255 C  CG  . LYS   A 148 ? 0.2641 0.1685 0.2586 -0.0409 -0.0139 0.0354  149 LYS   A CG  
1256 C  CD  . LYS   A 148 ? 0.3493 0.2092 0.3105 -0.0216 0.0374  0.0522  149 LYS   A CD  
1257 C  CE  . LYS   A 148 ? 0.3570 0.3796 0.3276 0.0034  0.0805  0.0686  149 LYS   A CE  
1258 N  NZ  . LYS   A 148 ? 0.4710 0.5233 0.4454 -0.1217 0.0590  0.2050  149 LYS   A NZ  
1259 N  N   . VAL   A 149 ? 0.2463 0.0912 0.2030 -0.0134 -0.0352 -0.0106 150 VAL   A N   
1260 C  CA  . VAL   A 149 ? 0.2167 0.1241 0.1896 -0.0111 -0.0223 -0.0156 150 VAL   A CA  
1261 C  C   . VAL   A 149 ? 0.2377 0.1101 0.2182 -0.0167 -0.0302 0.0156  150 VAL   A C   
1262 O  O   . VAL   A 149 ? 0.2561 0.1483 0.2260 -0.0196 -0.0307 0.0297  150 VAL   A O   
1263 C  CB  . VAL   A 149 ? 0.2260 0.1266 0.2006 -0.0105 -0.0194 -0.0207 150 VAL   A CB  
1264 C  CG1 . VAL   A 149 ? 0.2883 0.1971 0.1812 0.0009  -0.0370 -0.0319 150 VAL   A CG1 
1265 C  CG2 . VAL   A 149 ? 0.2298 0.1838 0.2713 -0.0250 -0.0105 0.0217  150 VAL   A CG2 
1266 N  N   . GLY   A 150 ? 0.2354 0.1126 0.2086 -0.0290 -0.0359 0.0001  151 GLY   A N   
1267 C  CA  . GLY   A 150 ? 0.2438 0.1735 0.2053 -0.0366 -0.0326 0.0383  151 GLY   A CA  
1268 C  C   . GLY   A 150 ? 0.2551 0.1385 0.1892 -0.0424 -0.0422 0.0140  151 GLY   A C   
1269 O  O   . GLY   A 150 ? 0.2488 0.1427 0.2118 -0.0407 -0.0301 -0.0055 151 GLY   A O   
1270 N  N   A SER   A 151 ? 0.2434 0.1611 0.2226 -0.0414 -0.0388 0.0105  152 SER   A N   
1271 N  N   B SER   A 151 ? 0.2388 0.1465 0.2543 -0.0420 -0.0450 0.0036  152 SER   A N   
1272 C  CA  A SER   A 151 ? 0.2402 0.1591 0.2081 -0.0363 -0.0416 -0.0102 152 SER   A CA  
1273 C  CA  B SER   A 151 ? 0.2451 0.1541 0.2246 -0.0429 -0.0480 -0.0151 152 SER   A CA  
1274 C  C   A SER   A 151 ? 0.2307 0.1342 0.1777 -0.0173 -0.0248 -0.0291 152 SER   A C   
1275 C  C   B SER   A 151 ? 0.2456 0.1350 0.1896 -0.0205 -0.0461 -0.0163 152 SER   A C   
1276 O  O   A SER   A 151 ? 0.2128 0.1608 0.1963 -0.0242 -0.0231 -0.0419 152 SER   A O   
1277 O  O   B SER   A 151 ? 0.2146 0.1486 0.1694 -0.0067 -0.0353 -0.0201 152 SER   A O   
1278 C  CB  A SER   A 151 ? 0.2459 0.2774 0.2897 -0.0427 -0.0162 -0.0063 152 SER   A CB  
1279 C  CB  B SER   A 151 ? 0.2537 0.1870 0.3618 -0.0510 -0.0035 -0.0190 152 SER   A CB  
1280 O  OG  A SER   A 151 ? 0.2912 0.3029 0.2559 -0.0825 -0.0500 -0.0064 152 SER   A OG  
1281 O  OG  B SER   A 151 ? 0.2476 0.2558 0.3838 -0.0367 0.0092  0.0928  152 SER   A OG  
1282 N  N   . ALA   A 152 ? 0.2715 0.1311 0.1999 -0.0322 -0.0614 -0.0122 153 ALA   A N   
1283 C  CA  . ALA   A 152 ? 0.2437 0.1300 0.1974 -0.0044 -0.0373 -0.0051 153 ALA   A CA  
1284 C  C   . ALA   A 152 ? 0.2426 0.1282 0.1958 -0.0038 -0.0469 -0.0006 153 ALA   A C   
1285 O  O   . ALA   A 152 ? 0.2502 0.1477 0.2692 -0.0048 -0.0386 -0.0196 153 ALA   A O   
1286 C  CB  . ALA   A 152 ? 0.3532 0.1659 0.2027 0.0035  -0.0826 -0.0408 153 ALA   A CB  
1287 N  N   . LYS   A 153 ? 0.2886 0.1104 0.1979 -0.0136 -0.0674 0.0069  154 LYS   A N   
1288 C  CA  . LYS   A 153 ? 0.2517 0.1332 0.2111 -0.0117 -0.0370 0.0022  154 LYS   A CA  
1289 C  C   . LYS   A 153 ? 0.2175 0.1614 0.2168 0.0148  -0.0267 -0.0064 154 LYS   A C   
1290 O  O   . LYS   A 153 ? 0.2365 0.1449 0.1944 -0.0054 -0.0478 0.0006  154 LYS   A O   
1291 C  CB  . LYS   A 153 ? 0.2883 0.1469 0.2111 -0.0154 -0.0715 -0.0212 154 LYS   A CB  
1292 C  CG  . LYS   A 153 ? 0.3638 0.1359 0.2029 -0.0048 -0.0745 -0.0133 154 LYS   A CG  
1293 C  CD  . LYS   A 153 ? 0.4146 0.1434 0.2097 -0.0138 -0.0539 0.0130  154 LYS   A CD  
1294 C  CE  . LYS   A 153 ? 0.4023 0.1705 0.2145 0.0163  -0.0531 -0.0009 154 LYS   A CE  
1295 N  NZ  . LYS   A 153 ? 0.4590 0.1937 0.2728 -0.0267 0.0064  -0.0473 154 LYS   A NZ  
1296 N  N   . PRO   A 154 ? 0.2233 0.1766 0.2315 -0.0060 -0.0427 -0.0039 155 PRO   A N   
1297 C  CA  . PRO   A 154 ? 0.2222 0.2041 0.2689 -0.0095 -0.0723 0.0220  155 PRO   A CA  
1298 C  C   . PRO   A 154 ? 0.2527 0.2113 0.2163 0.0119  -0.0629 0.0188  155 PRO   A C   
1299 O  O   . PRO   A 154 ? 0.2727 0.2108 0.2247 -0.0100 -0.0763 0.0467  155 PRO   A O   
1300 C  CB  . PRO   A 154 ? 0.2214 0.2242 0.3376 -0.0159 -0.0666 0.0359  155 PRO   A CB  
1301 C  CG  . PRO   A 154 ? 0.2736 0.3258 0.3331 -0.0383 -0.0792 0.0801  155 PRO   A CG  
1302 C  CD  . PRO   A 154 ? 0.2490 0.2366 0.2390 -0.0085 -0.0256 0.0044  155 PRO   A CD  
1303 N  N   . GLY   A 155 ? 0.2492 0.1543 0.2305 0.0109  -0.0605 0.0094  156 GLY   A N   
1304 C  CA  . GLY   A 155 ? 0.2671 0.1608 0.2685 0.0047  -0.0427 0.0326  156 GLY   A CA  
1305 C  C   . GLY   A 155 ? 0.2861 0.1388 0.2513 -0.0027 -0.0281 0.0500  156 GLY   A C   
1306 O  O   . GLY   A 155 ? 0.2717 0.1582 0.3235 -0.0055 -0.0255 0.0608  156 GLY   A O   
1307 N  N   . LEU   A 156 ? 0.2445 0.1465 0.2046 -0.0100 -0.0468 -0.0050 157 LEU   A N   
1308 C  CA  . LEU   A 156 ? 0.2497 0.1294 0.1975 -0.0181 -0.0644 -0.0052 157 LEU   A CA  
1309 C  C   . LEU   A 156 ? 0.2812 0.1464 0.1819 -0.0026 -0.0762 -0.0055 157 LEU   A C   
1310 O  O   . LEU   A 156 ? 0.2631 0.1483 0.1917 -0.0174 -0.0629 0.0003  157 LEU   A O   
1311 C  CB  . LEU   A 156 ? 0.2641 0.1469 0.1943 -0.0139 -0.0748 0.0083  157 LEU   A CB  
1312 C  CG  . LEU   A 156 ? 0.2452 0.1693 0.1770 -0.0359 -0.0546 0.0075  157 LEU   A CG  
1313 C  CD1 . LEU   A 156 ? 0.2649 0.1624 0.2183 -0.0325 -0.0608 0.0023  157 LEU   A CD1 
1314 C  CD2 . LEU   A 156 ? 0.2449 0.1805 0.1903 0.0027  -0.0554 0.0003  157 LEU   A CD2 
1315 N  N   . GLN   A 157 ? 0.2685 0.1591 0.1833 -0.0189 -0.0659 -0.0026 158 GLN   A N   
1316 C  CA  . GLN   A 157 ? 0.2911 0.1562 0.1786 -0.0400 -0.0725 -0.0055 158 GLN   A CA  
1317 C  C   . GLN   A 157 ? 0.2643 0.1434 0.1864 -0.0271 -0.0709 0.0021  158 GLN   A C   
1318 O  O   . GLN   A 157 ? 0.2782 0.1645 0.1895 -0.0222 -0.0629 0.0050  158 GLN   A O   
1319 C  CB  . GLN   A 157 ? 0.3024 0.2033 0.1942 -0.0719 -0.0710 0.0020  158 GLN   A CB  
1320 C  CG  . GLN   A 157 ? 0.3496 0.1833 0.2118 -0.0324 -0.0826 -0.0040 158 GLN   A CG  
1321 C  CD  . GLN   A 157 ? 0.3470 0.1550 0.1943 -0.0326 -0.0612 -0.0122 158 GLN   A CD  
1322 O  OE1 . GLN   A 157 ? 0.3781 0.1606 0.2014 -0.0199 -0.0610 -0.0098 158 GLN   A OE1 
1323 N  NE2 . GLN   A 157 ? 0.4173 0.2129 0.1946 -0.0508 -0.0521 -0.0464 158 GLN   A NE2 
1324 N  N   . LYS   A 158 ? 0.2940 0.1561 0.2018 -0.0205 -0.0763 0.0175  159 LYS   A N   
1325 C  CA  . LYS   A 158 ? 0.2759 0.1569 0.2073 -0.0143 -0.0719 0.0110  159 LYS   A CA  
1326 C  C   . LYS   A 158 ? 0.2772 0.1438 0.1949 -0.0074 -0.0582 0.0105  159 LYS   A C   
1327 O  O   . LYS   A 158 ? 0.3136 0.1707 0.1908 -0.0347 -0.0491 0.0162  159 LYS   A O   
1328 C  CB  . LYS   A 158 ? 0.3225 0.1639 0.2867 0.0207  -0.0690 0.0719  159 LYS   A CB  
1329 C  CG  . LYS   A 158 ? 0.3292 0.3282 0.2714 0.0594  -0.0632 0.0556  159 LYS   A CG  
1330 C  CD  . LYS   A 158 ? 0.4319 0.4514 0.4370 0.1594  -0.0532 -0.0195 159 LYS   A CD  
1331 C  CE  . LYS   A 158 ? 0.4277 0.5473 0.6210 0.1490  -0.0922 0.0362  159 LYS   A CE  
1332 N  NZ  . LYS   A 158 ? 0.4123 0.4840 0.4024 0.0754  -0.0034 0.0802  159 LYS   A NZ  
1333 N  N   . VAL   A 159 ? 0.2755 0.1361 0.1850 -0.0085 -0.0647 -0.0039 160 VAL   A N   
1334 C  CA  . VAL   A 159 ? 0.2642 0.1546 0.1772 -0.0118 -0.0465 -0.0077 160 VAL   A CA  
1335 C  C   . VAL   A 159 ? 0.2643 0.1441 0.1953 -0.0134 -0.0462 -0.0047 160 VAL   A C   
1336 O  O   . VAL   A 159 ? 0.2693 0.1625 0.2072 -0.0234 -0.0386 -0.0131 160 VAL   A O   
1337 C  CB  . VAL   A 159 ? 0.2746 0.1593 0.1629 0.0027  -0.0271 0.0035  160 VAL   A CB  
1338 C  CG1 . VAL   A 159 ? 0.2733 0.2258 0.1904 -0.0245 -0.0396 0.0372  160 VAL   A CG1 
1339 C  CG2 . VAL   A 159 ? 0.3481 0.1670 0.2109 0.0307  -0.0480 -0.0271 160 VAL   A CG2 
1340 N  N   A VAL   A 160 ? 0.2552 0.1395 0.1851 -0.0201 -0.0506 -0.0193 161 VAL   A N   
1341 N  N   B VAL   A 160 ? 0.2883 0.1199 0.1717 0.0060  -0.0531 -0.0201 161 VAL   A N   
1342 C  CA  A VAL   A 160 ? 0.2398 0.1458 0.1864 -0.0143 -0.0365 0.0153  161 VAL   A CA  
1343 C  CA  B VAL   A 160 ? 0.3334 0.1122 0.1773 -0.0131 -0.0016 -0.0221 161 VAL   A CA  
1344 C  C   A VAL   A 160 ? 0.3028 0.1489 0.1864 -0.0280 -0.0370 -0.0097 161 VAL   A C   
1345 C  C   B VAL   A 160 ? 0.3332 0.1054 0.1854 -0.0212 -0.0401 -0.0252 161 VAL   A C   
1346 O  O   A VAL   A 160 ? 0.3106 0.1885 0.1914 -0.0177 -0.0273 0.0098  161 VAL   A O   
1347 O  O   B VAL   A 160 ? 0.3964 0.1852 0.2128 -0.0605 0.0258  -0.0532 161 VAL   A O   
1348 C  CB  A VAL   A 160 ? 0.2069 0.1467 0.1840 -0.0333 -0.0379 -0.0337 161 VAL   A CB  
1349 C  CB  B VAL   A 160 ? 0.3399 0.1810 0.1960 0.0060  -0.0219 0.0644  161 VAL   A CB  
1350 C  CG1 A VAL   A 160 ? 0.2746 0.1405 0.1816 -0.0236 -0.0353 -0.0369 161 VAL   A CG1 
1351 C  CG1 B VAL   A 160 ? 0.3625 0.1595 0.1926 0.0187  -0.0166 0.0221  161 VAL   A CG1 
1352 C  CG2 A VAL   A 160 ? 0.2080 0.1217 0.1884 -0.0092 -0.0356 0.0084  161 VAL   A CG2 
1353 C  CG2 B VAL   A 160 ? 0.3326 0.1934 0.2484 0.0046  -0.0024 -0.0048 161 VAL   A CG2 
1354 N  N   . ASP   A 161 ? 0.3458 0.1912 0.1652 -0.0392 -0.0644 -0.0067 162 ASP   A N   
1355 C  CA  . ASP   A 161 ? 0.3617 0.2483 0.1720 -0.0562 -0.0512 -0.0062 162 ASP   A CA  
1356 C  C   . ASP   A 161 ? 0.3946 0.2697 0.1557 -0.0822 -0.0605 -0.0113 162 ASP   A C   
1357 O  O   . ASP   A 161 ? 0.5134 0.3202 0.1741 -0.0897 -0.0326 -0.0146 162 ASP   A O   
1358 C  CB  . ASP   A 161 ? 0.4151 0.3442 0.2062 -0.1134 -0.0775 -0.0223 162 ASP   A CB  
1359 C  CG  . ASP   A 161 ? 0.4954 0.2476 0.1725 -0.0354 -0.0017 -0.0408 162 ASP   A CG  
1360 O  OD1 . ASP   A 161 ? 0.4293 0.3173 0.3128 -0.0683 -0.0380 -0.0634 162 ASP   A OD1 
1361 O  OD2 . ASP   A 161 ? 0.4791 0.3285 0.3656 0.0098  -0.0489 0.0053  162 ASP   A OD2 
1362 N  N   . VAL   A 162 ? 0.3440 0.2052 0.1738 -0.0611 -0.0706 0.0184  163 VAL   A N   
1363 C  CA  . VAL   A 162 ? 0.3318 0.2298 0.1866 -0.0453 -0.0513 0.0322  163 VAL   A CA  
1364 C  C   . VAL   A 162 ? 0.3208 0.1908 0.1751 -0.0347 -0.0096 0.0254  163 VAL   A C   
1365 O  O   . VAL   A 162 ? 0.3458 0.2037 0.1641 -0.0409 -0.0111 0.0085  163 VAL   A O   
1366 C  CB  . VAL   A 162 ? 0.4148 0.1948 0.2828 -0.0142 -0.0851 0.0484  163 VAL   A CB  
1367 C  CG1 . VAL   A 162 ? 0.4245 0.1652 0.2740 -0.0210 -0.0730 0.0222  163 VAL   A CG1 
1368 C  CG2 . VAL   A 162 ? 0.4117 0.2739 0.2276 -0.0190 -0.0197 0.0460  163 VAL   A CG2 
1369 N  N   . LEU   A 163 ? 0.3127 0.1864 0.2031 -0.0359 -0.0414 0.0067  164 LEU   A N   
1370 C  CA  . LEU   A 163 ? 0.3168 0.1861 0.1604 -0.0124 0.0013  0.0080  164 LEU   A CA  
1371 C  C   . LEU   A 163 ? 0.3731 0.1911 0.1382 -0.0034 0.0049  -0.0170 164 LEU   A C   
1372 O  O   . LEU   A 163 ? 0.3489 0.2172 0.1893 -0.0064 0.0156  0.0015  164 LEU   A O   
1373 C  CB  . LEU   A 163 ? 0.3200 0.1738 0.1626 -0.0265 0.0004  0.0006  164 LEU   A CB  
1374 C  CG  . LEU   A 163 ? 0.3238 0.1541 0.1521 -0.0046 -0.0065 0.0172  164 LEU   A CG  
1375 C  CD1 . LEU   A 163 ? 0.3147 0.1722 0.1826 -0.0255 -0.0096 0.0381  164 LEU   A CD1 
1376 C  CD2 . LEU   A 163 ? 0.3497 0.1894 0.1503 -0.0113 -0.0332 -0.0023 164 LEU   A CD2 
1377 N  N   . ASP   A 164 ? 0.4716 0.2017 0.1524 -0.0467 0.0065  -0.0474 165 ASP   A N   
1378 C  CA  . ASP   A 164 ? 0.5290 0.2260 0.1935 -0.0719 0.0559  -0.0692 165 ASP   A CA  
1379 C  C   . ASP   A 164 ? 0.5109 0.2944 0.1826 -0.0484 0.0358  -0.0208 165 ASP   A C   
1380 O  O   . ASP   A 164 ? 0.5950 0.3495 0.2629 -0.0605 0.1238  -0.0405 165 ASP   A O   
1381 C  CB  . ASP   A 164 ? 0.6669 0.3743 0.1889 -0.1476 0.0325  -0.0970 165 ASP   A CB  
1382 C  CG  . ASP   A 164 ? 0.6881 0.3957 0.3283 -0.2402 -0.0929 -0.0952 165 ASP   A CG  
1383 O  OD1 . ASP   A 164 ? 0.6619 0.7528 0.2899 -0.1947 -0.0570 -0.0475 165 ASP   A OD1 
1384 O  OD2 . ASP   A 164 ? 0.8417 0.7701 0.3326 -0.2058 0.0060  -0.2025 165 ASP   A OD2 
1385 N  N   . SER   A 165 ? 0.3729 0.2893 0.1436 -0.0569 -0.0347 0.0063  166 SER   A N   
1386 C  CA  . SER   A 165 ? 0.4987 0.2843 0.1366 -0.0835 -0.0508 0.0071  166 SER   A CA  
1387 C  C   . SER   A 165 ? 0.3764 0.2390 0.1264 -0.0485 -0.0048 0.0175  166 SER   A C   
1388 O  O   . SER   A 165 ? 0.4236 0.2449 0.1793 -0.0472 -0.0077 0.0512  166 SER   A O   
1389 C  CB  . SER   A 165 ? 0.5586 0.3841 0.2753 -0.0018 0.0728  0.0603  166 SER   A CB  
1390 O  OG  . SER   A 165 ? 0.4783 0.2646 0.3024 0.0234  -0.0302 0.0300  166 SER   A OG  
1391 N  N   . ILE   A 166 ? 0.3483 0.1990 0.1307 -0.0257 -0.0205 0.0104  167 ILE   A N   
1392 C  CA  . ILE   A 166 ? 0.3159 0.1701 0.1787 -0.0206 -0.0011 -0.0073 167 ILE   A CA  
1393 C  C   . ILE   A 166 ? 0.2803 0.1606 0.1351 -0.0263 0.0022  -0.0134 167 ILE   A C   
1394 O  O   . ILE   A 166 ? 0.2891 0.1870 0.1447 -0.0422 0.0011  -0.0044 167 ILE   A O   
1395 C  CB  . ILE   A 166 ? 0.3223 0.1567 0.1547 -0.0053 0.0051  0.0051  167 ILE   A CB  
1396 C  CG1 . ILE   A 166 ? 0.3025 0.2172 0.1367 -0.0598 -0.0030 -0.0034 167 ILE   A CG1 
1397 C  CG2 . ILE   A 166 ? 0.3031 0.1838 0.2089 -0.0092 -0.0271 0.0255  167 ILE   A CG2 
1398 C  CD1 . ILE   A 166 ? 0.3393 0.2039 0.1425 -0.0387 0.0222  -0.0166 167 ILE   A CD1 
1399 N  N   . LYS   A 167 ? 0.3181 0.1718 0.1807 -0.0129 0.0199  -0.0135 168 LYS   A N   
1400 C  CA  . LYS   A 167 ? 0.2466 0.2044 0.1693 0.0008  0.0134  -0.0361 168 LYS   A CA  
1401 C  C   . LYS   A 167 ? 0.2728 0.1985 0.1464 -0.0276 0.0276  0.0146  168 LYS   A C   
1402 O  O   . LYS   A 167 ? 0.2760 0.1693 0.1574 -0.0390 -0.0036 0.0034  168 LYS   A O   
1403 C  CB  . LYS   A 167 ? 0.3353 0.1737 0.1697 -0.0220 -0.0071 -0.0359 168 LYS   A CB  
1404 C  CG  . LYS   A 167 ? 0.3197 0.2157 0.2357 0.0102  0.0029  -0.0696 168 LYS   A CG  
1405 C  CD  . LYS   A 167 ? 0.4630 0.2903 0.2982 0.0215  -0.0616 -0.1319 168 LYS   A CD  
1406 C  CE  . LYS   A 167 ? 0.4808 0.4238 0.3811 0.1256  -0.0797 -0.1441 168 LYS   A CE  
1407 N  NZ  . LYS   A 167 ? 0.6134 0.5676 0.4806 0.0457  -0.0095 -0.2493 168 LYS   A NZ  
1408 N  N   . THR   A 168 ? 0.2861 0.1791 0.1625 -0.0443 0.0196  0.0165  169 THR   A N   
1409 C  CA  . THR   A 168 ? 0.2825 0.1788 0.1451 -0.0310 0.0228  0.0089  169 THR   A CA  
1410 C  C   . THR   A 168 ? 0.2376 0.1592 0.1557 -0.0164 0.0309  0.0092  169 THR   A C   
1411 O  O   . THR   A 168 ? 0.2744 0.1719 0.1795 -0.0175 0.0122  0.0149  169 THR   A O   
1412 C  CB  . THR   A 168 ? 0.2945 0.2008 0.1772 -0.0211 0.0285  0.0183  169 THR   A CB  
1413 O  OG1 . THR   A 168 ? 0.3260 0.2821 0.1489 -0.0320 0.0353  0.0262  169 THR   A OG1 
1414 C  CG2 . THR   A 168 ? 0.3387 0.2032 0.1909 -0.0139 0.0401  0.0033  169 THR   A CG2 
1415 N  N   . LYS   A 169 ? 0.2950 0.2143 0.1725 -0.0701 0.0297  -0.0035 170 LYS   A N   
1416 C  CA  . LYS   A 169 ? 0.3012 0.1747 0.1877 -0.0431 0.0067  0.0073  170 LYS   A CA  
1417 C  C   . LYS   A 169 ? 0.2696 0.2017 0.1822 -0.0410 0.0334  0.0401  170 LYS   A C   
1418 O  O   . LYS   A 169 ? 0.3274 0.2575 0.1694 -0.0598 0.0340  0.0249  170 LYS   A O   
1419 C  CB  . LYS   A 169 ? 0.2874 0.2022 0.1764 -0.0488 0.0195  0.0011  170 LYS   A CB  
1420 C  CG  . LYS   A 169 ? 0.3496 0.2321 0.1998 -0.0761 -0.0086 -0.0020 170 LYS   A CG  
1421 C  CD  . LYS   A 169 ? 0.3326 0.3102 0.2218 -0.0273 0.0223  -0.0238 170 LYS   A CD  
1422 C  CE  . LYS   A 169 ? 0.4993 0.3948 0.4360 -0.1256 -0.1513 -0.0175 170 LYS   A CE  
1423 N  NZ  . LYS   A 169 ? 0.4984 0.6434 0.5759 0.1153  -0.1021 -0.0601 170 LYS   A NZ  
1424 N  N   . GLY   A 170 ? 0.3156 0.1683 0.2225 -0.0505 0.0157  0.0276  171 GLY   A N   
1425 C  CA  . GLY   A 170 ? 0.3286 0.1776 0.2448 -0.0479 0.0019  0.0636  171 GLY   A CA  
1426 C  C   . GLY   A 170 ? 0.3661 0.1826 0.2230 -0.0381 0.0009  0.0526  171 GLY   A C   
1427 O  O   . GLY   A 170 ? 0.3962 0.1625 0.2782 -0.0489 0.0168  0.0495  171 GLY   A O   
1428 N  N   . LYS   A 171 ? 0.3247 0.1800 0.2001 -0.0385 0.0063  0.0597  172 LYS   A N   
1429 C  CA  . LYS   A 171 ? 0.3398 0.2029 0.1694 -0.0629 0.0095  0.0336  172 LYS   A CA  
1430 C  C   . LYS   A 171 ? 0.3239 0.1867 0.1474 -0.0262 -0.0118 0.0313  172 LYS   A C   
1431 O  O   . LYS   A 171 ? 0.3001 0.1824 0.1540 -0.0017 0.0146  0.0332  172 LYS   A O   
1432 C  CB  . LYS   A 171 ? 0.3261 0.2074 0.2007 -0.0175 0.0220  0.0030  172 LYS   A CB  
1433 C  CG  . LYS   A 171 ? 0.3198 0.2530 0.2830 -0.0276 0.0468  -0.0167 172 LYS   A CG  
1434 C  CD  . LYS   A 171 ? 0.5301 0.2663 0.4065 -0.0599 0.0187  -0.0642 172 LYS   A CD  
1435 C  CE  . LYS   A 171 ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  172 LYS   A CE  
1436 N  NZ  . LYS   A 171 ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  172 LYS   A NZ  
1437 N  N   A SER   A 172 ? 0.4100 0.1860 0.1186 -0.0018 0.0132  0.0762  173 SER   A N   
1438 N  N   B SER   A 172 ? 0.3619 0.1840 0.2129 0.0297  -0.0087 -0.0038 173 SER   A N   
1439 C  CA  A SER   A 172 ? 0.4381 0.1555 0.1625 0.0023  0.0378  -0.0107 173 SER   A CA  
1440 C  CA  B SER   A 172 ? 0.3227 0.2261 0.2257 0.0179  -0.0211 0.0092  173 SER   A CA  
1441 C  C   A SER   A 172 ? 0.4234 0.1488 0.1438 0.0066  0.0245  0.0012  173 SER   A C   
1442 C  C   B SER   A 172 ? 0.3255 0.2477 0.1483 0.0362  -0.0245 0.0732  173 SER   A C   
1443 O  O   A SER   A 172 ? 0.4430 0.1788 0.1462 0.0257  0.0227  0.0122  173 SER   A O   
1444 O  O   B SER   A 172 ? 0.3137 0.2560 0.1535 0.0225  -0.0466 0.0550  173 SER   A O   
1445 C  CB  A SER   A 172 ? 0.5134 0.1470 0.1937 -0.0530 0.0632  0.0122  173 SER   A CB  
1446 C  CB  B SER   A 172 ? 0.2269 0.2190 0.1771 0.0385  -0.0476 0.0301  173 SER   A CB  
1447 O  OG  A SER   A 172 ? 0.4524 0.2279 0.2532 0.0304  0.1036  0.0894  173 SER   A OG  
1448 O  OG  B SER   A 172 ? 0.2420 0.2027 0.2547 0.0339  -0.0010 0.0572  173 SER   A OG  
1449 N  N   . ALA   A 173 ? 0.3602 0.2404 0.1803 0.0706  -0.0367 0.0337  174 ALA   A N   
1450 C  CA  . ALA   A 173 ? 0.3459 0.2531 0.1719 0.0473  -0.0206 0.0536  174 ALA   A CA  
1451 C  C   . ALA   A 173 ? 0.3365 0.2619 0.1376 0.0427  -0.0630 0.0061  174 ALA   A C   
1452 O  O   . ALA   A 173 ? 0.3384 0.2141 0.1351 0.0343  -0.0352 0.0185  174 ALA   A O   
1453 C  CB  . ALA   A 173 ? 0.4562 0.2351 0.1852 0.0757  -0.0445 -0.0074 174 ALA   A CB  
1454 N  N   . ASP   A 174 ? 0.3978 0.3090 0.1597 0.0793  -0.0417 0.0623  175 ASP   A N   
1455 C  CA  . ASP   A 174 ? 0.3861 0.3308 0.2059 0.0829  -0.0521 0.0564  175 ASP   A CA  
1456 C  C   . ASP   A 174 ? 0.4539 0.2355 0.2019 0.0592  -0.0624 -0.0021 175 ASP   A C   
1457 O  O   . ASP   A 174 ? 0.4597 0.2708 0.2287 0.1005  -0.0648 -0.0565 175 ASP   A O   
1458 C  CB  . ASP   A 174 ? 0.3662 0.4803 0.2314 0.1218  -0.0221 0.1280  175 ASP   A CB  
1459 C  CG  . ASP   A 174 ? 0.4228 0.5579 0.2722 0.0391  -0.0811 0.1553  175 ASP   A CG  
1460 O  OD1 . ASP   A 174 ? 0.5551 0.7673 0.3609 -0.0155 -0.2040 0.0511  175 ASP   A OD1 
1461 O  OD2 . ASP   A 174 ? 0.6549 0.7949 0.2623 -0.1125 -0.0518 0.1547  175 ASP   A OD2 
1462 N  N   . PHE   A 175 ? 0.3147 0.2158 0.1971 0.0311  -0.0449 0.0201  176 PHE   A N   
1463 C  CA  . PHE   A 175 ? 0.2999 0.1892 0.2203 0.0143  -0.0744 0.0179  176 PHE   A CA  
1464 C  C   . PHE   A 175 ? 0.3504 0.1544 0.2122 0.0163  -0.0922 0.0111  176 PHE   A C   
1465 O  O   . PHE   A 175 ? 0.3887 0.2685 0.2065 0.0891  -0.1202 -0.0359 176 PHE   A O   
1466 C  CB  . PHE   A 175 ? 0.3722 0.1582 0.2652 0.0285  -0.0942 0.0308  176 PHE   A CB  
1467 C  CG  . PHE   A 175 ? 0.3513 0.1764 0.2312 0.0270  -0.0708 -0.0113 176 PHE   A CG  
1468 C  CD1 . PHE   A 175 ? 0.3521 0.1612 0.2630 0.0076  -0.0335 -0.0176 176 PHE   A CD1 
1469 C  CD2 . PHE   A 175 ? 0.3541 0.1624 0.2111 0.0108  -0.1005 -0.0038 176 PHE   A CD2 
1470 C  CE1 . PHE   A 175 ? 0.4176 0.1936 0.2372 0.0125  -0.0285 0.0239  176 PHE   A CE1 
1471 C  CE2 . PHE   A 175 ? 0.3811 0.1384 0.2752 0.0337  -0.1032 0.0175  176 PHE   A CE2 
1472 C  CZ  . PHE   A 175 ? 0.3759 0.1625 0.2183 0.0294  -0.0630 0.0074  176 PHE   A CZ  
1473 N  N   . THR   A 176 ? 0.3454 0.1901 0.1679 0.0326  -0.0716 0.0326  177 THR   A N   
1474 C  CA  . THR   A 176 ? 0.2995 0.1811 0.1958 0.0194  -0.0275 0.0690  177 THR   A CA  
1475 C  C   . THR   A 176 ? 0.2940 0.1578 0.1534 -0.0050 -0.0615 0.0447  177 THR   A C   
1476 O  O   . THR   A 176 ? 0.3337 0.1745 0.1600 0.0013  -0.0551 0.0212  177 THR   A O   
1477 C  CB  . THR   A 176 ? 0.3389 0.2183 0.1997 -0.0065 -0.0641 0.0840  177 THR   A CB  
1478 O  OG1 . THR   A 176 ? 0.4936 0.2548 0.1843 0.0666  -0.0545 0.0672  177 THR   A OG1 
1479 C  CG2 . THR   A 176 ? 0.3849 0.2840 0.4394 -0.0228 -0.0450 0.1932  177 THR   A CG2 
1480 N  N   . ASN   A 177 ? 0.3048 0.1824 0.1634 0.0133  -0.0500 0.0373  178 ASN   A N   
1481 C  CA  . ASN   A 177 ? 0.3125 0.1830 0.1643 -0.0096 -0.0452 0.0425  178 ASN   A CA  
1482 C  C   . ASN   A 177 ? 0.3129 0.1700 0.1648 -0.0142 -0.0598 0.0302  178 ASN   A C   
1483 O  O   . ASN   A 177 ? 0.3367 0.2046 0.2930 -0.0469 -0.1027 0.0928  178 ASN   A O   
1484 C  CB  . ASN   A 177 ? 0.3395 0.1824 0.2128 0.0009  -0.0857 0.0603  178 ASN   A CB  
1485 C  CG  . ASN   A 177 ? 0.3220 0.1909 0.2074 0.0374  -0.0458 0.0506  178 ASN   A CG  
1486 O  OD1 . ASN   A 177 ? 0.3460 0.2265 0.2647 0.0576  -0.0159 0.0442  178 ASN   A OD1 
1487 N  ND2 . ASN   A 177 ? 0.3236 0.1859 0.1785 -0.0006 -0.0693 0.0519  178 ASN   A ND2 
1488 N  N   . PHE   A 178 ? 0.3388 0.1551 0.1309 -0.0021 -0.0661 0.0225  179 PHE   A N   
1489 C  CA  . PHE   A 178 ? 0.3365 0.1770 0.1544 -0.0234 -0.0653 0.0498  179 PHE   A CA  
1490 C  C   . PHE   A 178 ? 0.3131 0.1557 0.1645 -0.0098 -0.0734 0.0431  179 PHE   A C   
1491 O  O   . PHE   A 178 ? 0.3531 0.1579 0.1634 -0.0168 -0.0634 0.0237  179 PHE   A O   
1492 C  CB  . PHE   A 178 ? 0.3473 0.1656 0.1559 -0.0061 -0.0494 0.0498  179 PHE   A CB  
1493 C  CG  . PHE   A 178 ? 0.3110 0.1427 0.1652 -0.0205 -0.0432 0.0438  179 PHE   A CG  
1494 C  CD1 . PHE   A 178 ? 0.3410 0.1522 0.1791 0.0036  -0.0365 0.0212  179 PHE   A CD1 
1495 C  CD2 . PHE   A 178 ? 0.2579 0.1763 0.1600 0.0002  -0.0355 0.0428  179 PHE   A CD2 
1496 C  CE1 . PHE   A 178 ? 0.3465 0.1522 0.1801 -0.0050 -0.0637 0.0294  179 PHE   A CE1 
1497 C  CE2 . PHE   A 178 ? 0.2546 0.1600 0.1641 -0.0182 -0.0403 0.0378  179 PHE   A CE2 
1498 C  CZ  . PHE   A 178 ? 0.2846 0.1692 0.1645 -0.0086 -0.0287 0.0208  179 PHE   A CZ  
1499 N  N   . ASP   A 179 ? 0.2916 0.1920 0.1613 -0.0075 -0.0579 0.0480  180 ASP   A N   
1500 C  CA  . ASP   A 179 ? 0.2634 0.1890 0.1870 0.0017  -0.0691 0.0412  180 ASP   A CA  
1501 C  C   . ASP   A 179 ? 0.2557 0.1557 0.1636 -0.0096 -0.0436 0.0256  180 ASP   A C   
1502 O  O   . ASP   A 179 ? 0.2685 0.1566 0.1983 -0.0212 -0.0513 0.0231  180 ASP   A O   
1503 C  CB  . ASP   A 179 ? 0.2398 0.2552 0.2369 0.0055  -0.0729 0.0364  180 ASP   A CB  
1504 C  CG  . ASP   A 179 ? 0.2689 0.2921 0.2391 0.0270  -0.0567 0.0310  180 ASP   A CG  
1505 O  OD1 . ASP   A 179 ? 0.2450 0.2122 0.2365 0.0155  -0.0454 0.0406  180 ASP   A OD1 
1506 O  OD2 . ASP   A 179 ? 0.2725 0.4294 0.3646 0.0308  -0.0967 0.0117  180 ASP   A OD2 
1507 N  N   . PRO   A 180 ? 0.2394 0.1452 0.1641 -0.0022 -0.0392 0.0248  181 PRO   A N   
1508 C  CA  . PRO   A 180 ? 0.2351 0.1512 0.1724 0.0026  -0.0399 0.0228  181 PRO   A CA  
1509 C  C   . PRO   A 180 ? 0.2359 0.1555 0.1593 -0.0005 -0.0399 0.0267  181 PRO   A C   
1510 O  O   . PRO   A 180 ? 0.2386 0.1500 0.1627 -0.0106 -0.0339 0.0359  181 PRO   A O   
1511 C  CB  . PRO   A 180 ? 0.2548 0.1585 0.2000 -0.0160 -0.0569 0.0251  181 PRO   A CB  
1512 C  CG  . PRO   A 180 ? 0.2603 0.1638 0.2082 -0.0240 -0.0697 0.0172  181 PRO   A CG  
1513 C  CD  . PRO   A 180 ? 0.2822 0.1436 0.1692 -0.0129 -0.0547 0.0229  181 PRO   A CD  
1514 N  N   . ARG   A 181 ? 0.2213 0.1641 0.1839 -0.0071 -0.0409 0.0198  182 ARG   A N   
1515 C  CA  . ARG   A 181 ? 0.2251 0.1753 0.1971 -0.0185 -0.0197 0.0126  182 ARG   A CA  
1516 C  C   . ARG   A 181 ? 0.2146 0.1694 0.1890 -0.0071 -0.0566 0.0311  182 ARG   A C   
1517 O  O   . ARG   A 181 ? 0.2509 0.1929 0.2122 -0.0166 -0.0372 0.0423  182 ARG   A O   
1518 C  CB  . ARG   A 181 ? 0.2232 0.1705 0.2514 0.0020  -0.0258 0.0306  182 ARG   A CB  
1519 C  CG  . ARG   A 181 ? 0.2483 0.1969 0.2517 -0.0055 -0.0261 -0.0129 182 ARG   A CG  
1520 C  CD  . ARG   A 181 ? 0.2504 0.2646 0.3016 0.0276  0.0185  0.0565  182 ARG   A CD  
1521 N  NE  . ARG   A 181 ? 0.2327 0.2291 0.3175 0.0155  0.0010  0.0828  182 ARG   A NE  
1522 C  CZ  . ARG   A 181 ? 0.2558 0.3455 0.3327 0.0572  0.0533  0.1621  182 ARG   A CZ  
1523 N  NH1 . ARG   A 181 ? 0.2802 0.3814 0.4368 0.0787  0.0880  0.1221  182 ARG   A NH1 
1524 N  NH2 . ARG   A 181 ? 0.2688 0.3977 0.3598 0.0600  0.0140  0.1641  182 ARG   A NH2 
1525 N  N   . GLY   A 182 ? 0.2429 0.1658 0.1944 0.0059  -0.0715 0.0166  183 GLY   A N   
1526 C  CA  . GLY   A 182 ? 0.2839 0.1666 0.2091 0.0039  -0.0778 0.0177  183 GLY   A CA  
1527 C  C   . GLY   A 182 ? 0.2626 0.1482 0.1986 -0.0082 -0.0538 0.0341  183 GLY   A C   
1528 O  O   . GLY   A 182 ? 0.3037 0.1483 0.2509 -0.0148 -0.0792 0.0179  183 GLY   A O   
1529 N  N   . LEU   A 183 ? 0.2490 0.1606 0.1864 0.0032  -0.0577 0.0133  184 LEU   A N   
1530 C  CA  . LEU   A 183 ? 0.2709 0.1409 0.1826 0.0051  -0.0548 0.0225  184 LEU   A CA  
1531 C  C   . LEU   A 183 ? 0.2493 0.1522 0.1661 -0.0079 -0.0701 0.0089  184 LEU   A C   
1532 O  O   . LEU   A 183 ? 0.2558 0.1823 0.2000 0.0113  -0.0397 0.0372  184 LEU   A O   
1533 C  CB  . LEU   A 183 ? 0.2326 0.1824 0.1767 0.0130  -0.0480 0.0232  184 LEU   A CB  
1534 C  CG  . LEU   A 183 ? 0.2836 0.1991 0.1639 0.0207  -0.0424 0.0016  184 LEU   A CG  
1535 C  CD1 . LEU   A 183 ? 0.2509 0.3036 0.1953 0.0227  -0.0541 0.0545  184 LEU   A CD1 
1536 C  CD2 . LEU   A 183 ? 0.3708 0.2229 0.1832 -0.0111 -0.0091 -0.0363 184 LEU   A CD2 
1537 N  N   . LEU   A 184 ? 0.2511 0.1490 0.1895 -0.0047 -0.0403 0.0236  185 LEU   A N   
1538 C  CA  . LEU   A 184 ? 0.2092 0.1544 0.1860 -0.0311 -0.0333 0.0228  185 LEU   A CA  
1539 C  C   . LEU   A 184 ? 0.2666 0.1722 0.2129 -0.0452 -0.0716 0.0501  185 LEU   A C   
1540 O  O   . LEU   A 184 ? 0.3848 0.2433 0.3229 -0.1491 -0.1940 0.1333  185 LEU   A O   
1541 C  CB  . LEU   A 184 ? 0.1946 0.1485 0.2387 -0.0174 -0.0271 0.0161  185 LEU   A CB  
1542 C  CG  . LEU   A 184 ? 0.1790 0.1562 0.2193 0.0033  -0.0321 0.0089  185 LEU   A CG  
1543 C  CD1 . LEU   A 184 ? 0.2247 0.2020 0.2260 0.0331  -0.0257 0.0035  185 LEU   A CD1 
1544 C  CD2 . LEU   A 184 ? 0.1980 0.1919 0.2815 -0.0167 -0.0582 0.0314  185 LEU   A CD2 
1545 N  N   . PRO   A 185 ? 0.2043 0.1441 0.2020 -0.0201 -0.0497 0.0250  186 PRO   A N   
1546 C  CA  . PRO   A 185 ? 0.2025 0.1693 0.2124 -0.0234 -0.0387 0.0452  186 PRO   A CA  
1547 C  C   . PRO   A 185 ? 0.1949 0.1444 0.2577 -0.0259 -0.0605 0.0334  186 PRO   A C   
1548 O  O   . PRO   A 185 ? 0.1668 0.1503 0.3484 -0.0080 -0.0712 0.0412  186 PRO   A O   
1549 C  CB  . PRO   A 185 ? 0.1822 0.1719 0.1972 -0.0100 -0.0233 0.0342  186 PRO   A CB  
1550 C  CG  . PRO   A 185 ? 0.1723 0.1643 0.1685 0.0201  -0.0225 0.0108  186 PRO   A CG  
1551 C  CD  . PRO   A 185 ? 0.1786 0.1611 0.1575 0.0072  -0.0305 0.0106  186 PRO   A CD  
1552 N  N   A GLU   A 186 ? 0.2011 0.1824 0.2516 -0.0458 -0.0530 0.0358  187 GLU   A N   
1553 N  N   B GLU   A 186 ? 0.2125 0.1740 0.2300 -0.0252 -0.0242 0.0314  187 GLU   A N   
1554 C  CA  A GLU   A 186 ? 0.1860 0.2052 0.2827 -0.0452 -0.0567 0.0526  187 GLU   A CA  
1555 C  CA  B GLU   A 186 ? 0.2018 0.1631 0.2584 -0.0307 -0.0194 0.0304  187 GLU   A CA  
1556 C  C   A GLU   A 186 ? 0.1638 0.1939 0.2901 -0.0249 -0.0403 0.0438  187 GLU   A C   
1557 C  C   B GLU   A 186 ? 0.1804 0.1317 0.2840 -0.0098 -0.0364 0.0234  187 GLU   A C   
1558 O  O   A GLU   A 186 ? 0.1638 0.2301 0.3029 0.0102  -0.0172 0.0427  187 GLU   A O   
1559 O  O   B GLU   A 186 ? 0.1967 0.1738 0.2522 0.0250  -0.0111 0.0275  187 GLU   A O   
1560 C  CB  A GLU   A 186 ? 0.2088 0.1895 0.3763 -0.0480 -0.0570 0.0440  187 GLU   A CB  
1561 C  CB  B GLU   A 186 ? 0.2265 0.1338 0.2950 -0.0409 -0.0535 0.0277  187 GLU   A CB  
1562 C  CG  A GLU   A 186 ? 0.2366 0.2240 0.4603 -0.0037 -0.0168 0.0310  187 GLU   A CG  
1563 C  CG  B GLU   A 186 ? 0.2753 0.1434 0.2994 -0.0381 -0.0225 -0.0218 187 GLU   A CG  
1564 C  CD  A GLU   A 186 ? 0.2486 0.2294 0.4838 0.0207  0.0100  0.0637  187 GLU   A CD  
1565 C  CD  B GLU   A 186 ? 0.2075 0.1872 0.3964 -0.0708 -0.0480 -0.0096 187 GLU   A CD  
1566 O  OE1 A GLU   A 186 ? 0.3474 0.2242 0.5334 0.0359  0.1008  0.0938  187 GLU   A OE1 
1567 O  OE1 B GLU   A 186 ? 0.2122 0.2286 0.3905 -0.0526 -0.0027 -0.0236 187 GLU   A OE1 
1568 O  OE2 A GLU   A 186 ? 0.2172 0.2067 0.5718 -0.0479 -0.0350 0.0522  187 GLU   A OE2 
1569 O  OE2 B GLU   A 186 ? 0.2377 0.2603 0.4332 -0.0419 -0.0522 -0.0749 187 GLU   A OE2 
1570 N  N   . SER   A 187 ? 0.1553 0.1729 0.2608 -0.0140 -0.0276 0.0259  188 SER   A N   
1571 C  CA  . SER   A 187 ? 0.1867 0.1740 0.2575 -0.0230 -0.0097 0.0368  188 SER   A CA  
1572 C  C   . SER   A 187 ? 0.1562 0.1983 0.2258 -0.0250 -0.0121 0.0102  188 SER   A C   
1573 O  O   . SER   A 187 ? 0.1752 0.2348 0.2355 -0.0149 -0.0086 -0.0299 188 SER   A O   
1574 C  CB  . SER   A 187 ? 0.2043 0.1995 0.2297 -0.0221 0.0027  0.0391  188 SER   A CB  
1575 O  OG  . SER   A 187 ? 0.2140 0.2087 0.2503 -0.0222 -0.0018 0.0116  188 SER   A OG  
1576 N  N   . LEU   A 188 ? 0.1761 0.1829 0.2456 -0.0320 -0.0240 0.0015  189 LEU   A N   
1577 C  CA  . LEU   A 188 ? 0.1846 0.1618 0.2513 -0.0205 -0.0321 -0.0151 189 LEU   A CA  
1578 C  C   . LEU   A 188 ? 0.1714 0.1606 0.2341 -0.0034 -0.0121 -0.0159 189 LEU   A C   
1579 O  O   . LEU   A 188 ? 0.1941 0.1817 0.2582 -0.0170 -0.0241 -0.0156 189 LEU   A O   
1580 C  CB  . LEU   A 188 ? 0.1944 0.1755 0.2734 -0.0190 -0.0255 0.0141  189 LEU   A CB  
1581 C  CG  . LEU   A 188 ? 0.2075 0.2312 0.2622 0.0044  -0.0108 0.0113  189 LEU   A CG  
1582 C  CD1 . LEU   A 188 ? 0.2507 0.2060 0.3557 -0.0260 -0.0296 0.0701  189 LEU   A CD1 
1583 C  CD2 . LEU   A 188 ? 0.2102 0.3562 0.2322 -0.0135 -0.0168 0.0133  189 LEU   A CD2 
1584 N  N   . ASP   A 189 ? 0.1634 0.1901 0.2093 0.0003  -0.0057 -0.0126 190 ASP   A N   
1585 C  CA  . ASP   A 189 ? 0.1718 0.2064 0.1988 -0.0194 0.0044  -0.0044 190 ASP   A CA  
1586 C  C   . ASP   A 189 ? 0.1794 0.1621 0.1834 -0.0205 0.0051  -0.0120 190 ASP   A C   
1587 O  O   . ASP   A 189 ? 0.1611 0.1654 0.1826 -0.0125 0.0034  -0.0165 190 ASP   A O   
1588 C  CB  . ASP   A 189 ? 0.1925 0.2707 0.1922 -0.0591 0.0008  0.0348  190 ASP   A CB  
1589 C  CG  . ASP   A 189 ? 0.2068 0.4251 0.2380 -0.0822 0.0037  0.0379  190 ASP   A CG  
1590 O  OD1 . ASP   A 189 ? 0.2297 0.5188 0.3692 -0.0848 0.0756  -0.0260 190 ASP   A OD1 
1591 O  OD2 . ASP   A 189 ? 0.2626 0.5128 0.3118 -0.1186 0.0114  0.1333  190 ASP   A OD2 
1592 N  N   . TYR   A 190 ? 0.1663 0.1682 0.1617 -0.0093 0.0058  -0.0001 191 TYR   A N   
1593 C  CA  . TYR   A 190 ? 0.1726 0.1600 0.1497 -0.0283 -0.0080 0.0230  191 TYR   A CA  
1594 C  C   . TYR   A 190 ? 0.1886 0.1333 0.1293 -0.0146 0.0085  0.0130  191 TYR   A C   
1595 O  O   . TYR   A 190 ? 0.1875 0.1618 0.1400 -0.0011 0.0086  0.0003  191 TYR   A O   
1596 C  CB  . TYR   A 190 ? 0.1805 0.1339 0.1597 -0.0081 -0.0064 0.0080  191 TYR   A CB  
1597 C  CG  . TYR   A 190 ? 0.1777 0.1398 0.1529 -0.0129 -0.0031 0.0122  191 TYR   A CG  
1598 C  CD1 . TYR   A 190 ? 0.1987 0.1370 0.1655 -0.0171 0.0013  0.0047  191 TYR   A CD1 
1599 C  CD2 . TYR   A 190 ? 0.1849 0.1729 0.1603 0.0040  0.0096  0.0103  191 TYR   A CD2 
1600 C  CE1 . TYR   A 190 ? 0.2070 0.1415 0.1922 -0.0005 0.0019  0.0052  191 TYR   A CE1 
1601 C  CE2 . TYR   A 190 ? 0.1979 0.1604 0.1781 0.0012  -0.0081 0.0155  191 TYR   A CE2 
1602 C  CZ  . TYR   A 190 ? 0.2081 0.1474 0.1870 -0.0038 0.0055  -0.0111 191 TYR   A CZ  
1603 O  OH  . TYR   A 190 ? 0.2261 0.1623 0.2006 0.0227  0.0013  -0.0119 191 TYR   A OH  
1604 N  N   . TRP   A 191 ? 0.1648 0.1199 0.1409 -0.0081 -0.0037 0.0137  192 TRP   A N   
1605 C  CA  . TRP   A 191 ? 0.1658 0.1377 0.1462 -0.0044 0.0025  0.0078  192 TRP   A CA  
1606 C  C   . TRP   A 191 ? 0.1703 0.1361 0.1068 0.0111  -0.0033 0.0005  192 TRP   A C   
1607 O  O   . TRP   A 191 ? 0.1936 0.1438 0.1164 -0.0168 0.0016  0.0042  192 TRP   A O   
1608 C  CB  . TRP   A 191 ? 0.1675 0.1350 0.1561 -0.0054 0.0068  0.0049  192 TRP   A CB  
1609 C  CG  . TRP   A 191 ? 0.1837 0.1350 0.1381 0.0144  0.0019  0.0159  192 TRP   A CG  
1610 C  CD1 . TRP   A 191 ? 0.1976 0.1394 0.1584 0.0033  0.0078  0.0364  192 TRP   A CD1 
1611 C  CD2 . TRP   A 191 ? 0.1741 0.1445 0.1551 0.0093  -0.0032 0.0142  192 TRP   A CD2 
1612 N  NE1 . TRP   A 191 ? 0.2287 0.1365 0.1665 0.0130  0.0188  0.0380  192 TRP   A NE1 
1613 C  CE2 . TRP   A 191 ? 0.2042 0.1324 0.1604 0.0190  0.0004  0.0168  192 TRP   A CE2 
1614 C  CE3 . TRP   A 191 ? 0.1722 0.1650 0.1480 -0.0026 0.0044  0.0018  192 TRP   A CE3 
1615 C  CZ2 . TRP   A 191 ? 0.2142 0.1098 0.2215 -0.0020 -0.0121 0.0215  192 TRP   A CZ2 
1616 C  CZ3 . TRP   A 191 ? 0.1788 0.1549 0.2062 0.0049  -0.0135 -0.0122 192 TRP   A CZ3 
1617 C  CH2 . TRP   A 191 ? 0.2133 0.1682 0.2142 0.0020  -0.0199 -0.0096 192 TRP   A CH2 
1618 N  N   . THR   A 192 ? 0.1705 0.1216 0.1197 -0.0024 -0.0122 0.0062  193 THR   A N   
1619 C  CA  . THR   A 192 ? 0.1831 0.1309 0.1228 -0.0050 -0.0069 0.0084  193 THR   A CA  
1620 C  C   . THR   A 192 ? 0.1720 0.1280 0.1084 0.0103  0.0013  0.0069  193 THR   A C   
1621 O  O   . THR   A 192 ? 0.1793 0.1559 0.1137 -0.0103 -0.0034 0.0086  193 THR   A O   
1622 C  CB  . THR   A 192 ? 0.1855 0.1216 0.1349 0.0019  0.0133  0.0032  193 THR   A CB  
1623 O  OG1 . THR   A 192 ? 0.1724 0.1213 0.1463 0.0066  -0.0039 -0.0024 193 THR   A OG1 
1624 C  CG2 . THR   A 192 ? 0.2017 0.1531 0.1468 0.0175  0.0146  -0.0097 193 THR   A CG2 
1625 N  N   . TYR   A 193 ? 0.1638 0.1286 0.1320 0.0000  -0.0006 -0.0010 194 TYR   A N   
1626 C  CA  . TYR   A 193 ? 0.1712 0.1293 0.1165 0.0051  -0.0043 0.0059  194 TYR   A CA  
1627 C  C   . TYR   A 193 ? 0.1655 0.1180 0.1170 0.0140  -0.0115 -0.0076 194 TYR   A C   
1628 O  O   . TYR   A 193 ? 0.1612 0.1297 0.1192 0.0006  -0.0098 -0.0049 194 TYR   A O   
1629 C  CB  . TYR   A 193 ? 0.1875 0.1295 0.1165 0.0111  -0.0062 0.0011  194 TYR   A CB  
1630 C  CG  . TYR   A 193 ? 0.1728 0.1253 0.1241 0.0137  -0.0175 0.0009  194 TYR   A CG  
1631 C  CD1 . TYR   A 193 ? 0.1838 0.1313 0.1142 0.0168  -0.0168 0.0092  194 TYR   A CD1 
1632 C  CD2 . TYR   A 193 ? 0.1685 0.1326 0.1336 0.0132  -0.0176 -0.0031 194 TYR   A CD2 
1633 C  CE1 . TYR   A 193 ? 0.1666 0.1090 0.1338 0.0052  -0.0175 0.0006  194 TYR   A CE1 
1634 C  CE2 . TYR   A 193 ? 0.1699 0.1265 0.1319 0.0131  -0.0170 -0.0093 194 TYR   A CE2 
1635 C  CZ  . TYR   A 193 ? 0.1648 0.1110 0.1294 0.0048  -0.0064 0.0055  194 TYR   A CZ  
1636 O  OH  . TYR   A 193 ? 0.1729 0.1016 0.1302 -0.0015 -0.0067 -0.0025 194 TYR   A OH  
1637 N  N   . PRO   A 194 ? 0.1482 0.1467 0.1197 0.0079  -0.0135 -0.0114 195 PRO   A N   
1638 C  CA  . PRO   A 194 ? 0.1634 0.1353 0.1358 0.0034  -0.0100 -0.0222 195 PRO   A CA  
1639 C  C   . PRO   A 194 ? 0.1503 0.1138 0.1339 -0.0022 -0.0096 -0.0054 195 PRO   A C   
1640 O  O   . PRO   A 194 ? 0.1769 0.1370 0.1354 0.0173  -0.0122 -0.0109 195 PRO   A O   
1641 C  CB  . PRO   A 194 ? 0.1875 0.1682 0.1213 0.0011  -0.0077 -0.0203 195 PRO   A CB  
1642 C  CG  . PRO   A 194 ? 0.2069 0.1665 0.1232 -0.0296 -0.0039 -0.0103 195 PRO   A CG  
1643 C  CD  . PRO   A 194 ? 0.1817 0.1720 0.1225 -0.0158 -0.0177 -0.0217 195 PRO   A CD  
1644 N  N   . GLY   A 195 ? 0.1561 0.1276 0.1261 0.0040  -0.0047 -0.0201 196 GLY   A N   
1645 C  CA  . GLY   A 195 ? 0.1620 0.1257 0.1375 0.0055  -0.0046 0.0079  196 GLY   A CA  
1646 C  C   . GLY   A 195 ? 0.1595 0.0966 0.1416 -0.0044 -0.0083 -0.0159 196 GLY   A C   
1647 O  O   . GLY   A 195 ? 0.1657 0.1055 0.1391 -0.0065 -0.0052 -0.0125 196 GLY   A O   
1648 N  N   . SER   A 196 ? 0.1571 0.1079 0.1219 -0.0012 -0.0079 -0.0098 197 SER   A N   
1649 C  CA  . SER   A 196 ? 0.1551 0.1168 0.1288 -0.0098 -0.0050 -0.0148 197 SER   A CA  
1650 C  C   . SER   A 196 ? 0.1364 0.1137 0.1315 0.0001  0.0019  -0.0100 197 SER   A C   
1651 O  O   . SER   A 196 ? 0.1453 0.1104 0.1459 -0.0044 -0.0142 -0.0055 197 SER   A O   
1652 C  CB  . SER   A 196 ? 0.1532 0.1045 0.1649 0.0038  -0.0087 -0.0227 197 SER   A CB  
1653 O  OG  . SER   A 196 ? 0.1452 0.1141 0.1562 0.0013  -0.0024 -0.0043 197 SER   A OG  
1654 N  N   . LEU   A 197 ? 0.1410 0.1198 0.1313 0.0013  0.0061  -0.0049 198 LEU   A N   
1655 C  CA  . LEU   A 197 ? 0.1627 0.1124 0.1310 -0.0091 0.0025  -0.0161 198 LEU   A CA  
1656 C  C   . LEU   A 197 ? 0.1530 0.1124 0.1433 -0.0100 0.0024  -0.0085 198 LEU   A C   
1657 O  O   . LEU   A 197 ? 0.1498 0.1288 0.1438 -0.0044 -0.0031 -0.0205 198 LEU   A O   
1658 C  CB  . LEU   A 197 ? 0.1667 0.1315 0.1544 -0.0022 0.0018  0.0134  198 LEU   A CB  
1659 C  CG  . LEU   A 197 ? 0.2121 0.1425 0.1976 -0.0033 0.0204  0.0381  198 LEU   A CG  
1660 C  CD1 . LEU   A 197 ? 0.2005 0.1570 0.2642 -0.0147 0.0122  0.0749  198 LEU   A CD1 
1661 C  CD2 . LEU   A 197 ? 0.1973 0.1731 0.2570 0.0265  0.0460  0.0605  198 LEU   A CD2 
1662 N  N   . THR   A 198 ? 0.1571 0.1044 0.1404 -0.0044 -0.0041 -0.0127 199 THR   A N   
1663 C  CA  . THR   A 198 ? 0.1639 0.1025 0.1535 -0.0008 -0.0050 -0.0159 199 THR   A CA  
1664 C  C   . THR   A 198 ? 0.1538 0.1332 0.1481 -0.0004 -0.0088 -0.0079 199 THR   A C   
1665 O  O   . THR   A 198 ? 0.1516 0.1482 0.1656 -0.0037 0.0069  -0.0125 199 THR   A O   
1666 C  CB  . THR   A 198 ? 0.1735 0.1122 0.1154 -0.0103 -0.0095 -0.0124 199 THR   A CB  
1667 O  OG1 . THR   A 198 ? 0.1662 0.1124 0.1324 -0.0038 -0.0059 -0.0010 199 THR   A OG1 
1668 C  CG2 . THR   A 198 ? 0.1649 0.1307 0.1434 -0.0022 0.0115  -0.0053 199 THR   A CG2 
1669 N  N   . THR   A 199 ? 0.1667 0.1489 0.1488 -0.0102 0.0011  -0.0053 200 THR   A N   
1670 C  CA  . THR   A 199 ? 0.1980 0.1439 0.1560 -0.0306 0.0122  -0.0208 200 THR   A CA  
1671 C  C   . THR   A 199 ? 0.1867 0.1294 0.1662 -0.0111 0.0140  -0.0142 200 THR   A C   
1672 O  O   . THR   A 199 ? 0.1829 0.1442 0.1755 -0.0250 0.0156  -0.0216 200 THR   A O   
1673 C  CB  . THR   A 199 ? 0.2498 0.1635 0.1506 -0.0381 -0.0025 -0.0171 200 THR   A CB  
1674 O  OG1 . THR   A 199 ? 0.3410 0.1473 0.2228 -0.0154 -0.0635 -0.0005 200 THR   A OG1 
1675 C  CG2 . THR   A 199 ? 0.2557 0.1429 0.1896 -0.0237 -0.0195 -0.0208 200 THR   A CG2 
1676 N  N   . PRO   A 200 ? 0.1842 0.1426 0.1795 -0.0116 0.0245  -0.0067 201 PRO   A N   
1677 C  CA  . PRO   A 200 ? 0.1856 0.1553 0.1824 -0.0240 0.0226  0.0122  201 PRO   A CA  
1678 C  C   . PRO   A 200 ? 0.1902 0.1596 0.1675 -0.0236 0.0022  -0.0133 201 PRO   A C   
1679 O  O   . PRO   A 200 ? 0.2251 0.1859 0.1832 -0.0166 -0.0047 -0.0023 201 PRO   A O   
1680 C  CB  . PRO   A 200 ? 0.1863 0.1870 0.2075 -0.0073 0.0234  -0.0051 201 PRO   A CB  
1681 C  CG  . PRO   A 200 ? 0.1784 0.1967 0.2190 -0.0055 0.0307  -0.0225 201 PRO   A CG  
1682 C  CD  . PRO   A 200 ? 0.1828 0.1757 0.1905 0.0008  0.0195  -0.0279 201 PRO   A CD  
1683 N  N   . PRO   A 201 ? 0.1991 0.1577 0.1650 -0.0377 0.0153  0.0150  202 PRO   A N   
1684 C  CA  . PRO   A 201 ? 0.2206 0.1456 0.1817 -0.0274 0.0082  -0.0082 202 PRO   A CA  
1685 C  C   . PRO   A 201 ? 0.1540 0.1606 0.1874 -0.0015 0.0053  -0.0138 202 PRO   A C   
1686 O  O   . PRO   A 201 ? 0.1808 0.1445 0.2104 -0.0196 -0.0015 -0.0072 202 PRO   A O   
1687 C  CB  . PRO   A 201 ? 0.2351 0.1534 0.2236 -0.0499 0.0258  0.0115  202 PRO   A CB  
1688 C  CG  . PRO   A 201 ? 0.2808 0.1600 0.2401 -0.0199 0.0020  -0.0124 202 PRO   A CG  
1689 C  CD  . PRO   A 201 ? 0.2626 0.1444 0.2044 -0.0159 0.0049  0.0109  202 PRO   A CD  
1690 N  N   . LEU   A 202 ? 0.1723 0.1261 0.1654 -0.0089 0.0077  0.0071  203 LEU   A N   
1691 C  CA  . LEU   A 202 ? 0.1724 0.1316 0.1455 0.0000  -0.0070 -0.0046 203 LEU   A CA  
1692 C  C   . LEU   A 202 ? 0.1605 0.1197 0.1685 -0.0200 0.0011  -0.0077 203 LEU   A C   
1693 O  O   . LEU   A 202 ? 0.1586 0.1389 0.1613 -0.0040 -0.0013 -0.0192 203 LEU   A O   
1694 C  CB  . LEU   A 202 ? 0.1581 0.1316 0.1786 0.0113  -0.0075 -0.0153 203 LEU   A CB  
1695 C  CG  . LEU   A 202 ? 0.1590 0.1285 0.1808 0.0036  0.0025  -0.0195 203 LEU   A CG  
1696 C  CD1 . LEU   A 202 ? 0.1530 0.1791 0.2310 0.0145  -0.0020 -0.0424 203 LEU   A CD1 
1697 C  CD2 . LEU   A 202 ? 0.1655 0.1392 0.1835 -0.0044 0.0016  -0.0149 203 LEU   A CD2 
1698 N  N   . LEU   A 203 ? 0.1658 0.1146 0.2083 -0.0058 0.0042  -0.0083 204 LEU   A N   
1699 C  CA  . LEU   A 203 ? 0.1644 0.1117 0.2075 -0.0115 0.0002  -0.0121 204 LEU   A CA  
1700 C  C   . LEU   A 203 ? 0.1624 0.1045 0.1749 0.0019  -0.0064 -0.0111 204 LEU   A C   
1701 O  O   . LEU   A 203 ? 0.1671 0.1165 0.1648 -0.0117 -0.0055 -0.0207 204 LEU   A O   
1702 C  CB  . LEU   A 203 ? 0.2169 0.1101 0.2014 -0.0130 0.0185  0.0105  204 LEU   A CB  
1703 C  CG  . LEU   A 203 ? 0.2228 0.1523 0.2224 0.0009  0.0379  0.0208  204 LEU   A CG  
1704 C  CD1 . LEU   A 203 ? 0.2523 0.1549 0.2835 0.0283  0.0637  0.0577  204 LEU   A CD1 
1705 C  CD2 . LEU   A 203 ? 0.2238 0.2467 0.4277 -0.0878 0.0357  0.0416  204 LEU   A CD2 
1706 N  N   . GLU   A 204 ? 0.1791 0.1246 0.1694 -0.0152 -0.0120 -0.0140 205 GLU   A N   
1707 C  CA  . GLU   A 204 ? 0.1945 0.1256 0.1536 -0.0013 -0.0243 -0.0331 205 GLU   A CA  
1708 C  C   . GLU   A 204 ? 0.1883 0.1183 0.1580 0.0008  -0.0179 -0.0190 205 GLU   A C   
1709 O  O   . GLU   A 204 ? 0.2129 0.1652 0.1725 0.0108  -0.0331 -0.0430 205 GLU   A O   
1710 C  CB  . GLU   A 204 ? 0.2006 0.1474 0.1727 0.0049  -0.0421 -0.0329 205 GLU   A CB  
1711 C  CG  . GLU   A 204 ? 0.1885 0.1520 0.1879 0.0002  -0.0289 -0.0341 205 GLU   A CG  
1712 C  CD  . GLU   A 204 ? 0.2064 0.1591 0.1615 -0.0103 -0.0268 -0.0305 205 GLU   A CD  
1713 O  OE1 . GLU   A 204 ? 0.2236 0.1845 0.2244 0.0094  -0.0706 -0.0502 205 GLU   A OE1 
1714 O  OE2 . GLU   A 204 ? 0.1779 0.1618 0.2057 -0.0035 -0.0378 -0.0145 205 GLU   A OE2 
1715 N  N   . CYS   A 205 ? 0.1694 0.1110 0.1648 -0.0107 -0.0049 -0.0142 206 CYS   A N   
1716 C  CA  . CYS   A 205 ? 0.1719 0.1301 0.1465 0.0043  -0.0016 -0.0124 206 CYS   A CA  
1717 C  C   . CYS   A 205 ? 0.1750 0.1018 0.1604 -0.0013 -0.0089 -0.0271 206 CYS   A C   
1718 O  O   . CYS   A 205 ? 0.1868 0.1084 0.2033 0.0050  -0.0303 -0.0073 206 CYS   A O   
1719 C  CB  . CYS   A 205 ? 0.1980 0.1494 0.1523 -0.0155 0.0107  -0.0068 206 CYS   A CB  
1720 S  SG  . CYS   A 205 ? 0.2147 0.1289 0.1627 0.0003  -0.0100 -0.0079 206 CYS   A SG  
1721 N  N   . VAL   A 206 ? 0.1736 0.1039 0.1479 -0.0052 -0.0095 0.0000  207 VAL   A N   
1722 C  CA  . VAL   A 206 ? 0.1659 0.0962 0.1504 -0.0044 -0.0064 -0.0009 207 VAL   A CA  
1723 C  C   . VAL   A 206 ? 0.1711 0.0993 0.1421 0.0035  -0.0185 -0.0004 207 VAL   A C   
1724 O  O   . VAL   A 206 ? 0.1744 0.1385 0.1588 -0.0006 -0.0075 0.0217  207 VAL   A O   
1725 C  CB  . VAL   A 206 ? 0.1577 0.1043 0.1623 0.0034  0.0006  -0.0100 207 VAL   A CB  
1726 C  CG1 . VAL   A 206 ? 0.1657 0.1231 0.1539 -0.0062 -0.0273 -0.0053 207 VAL   A CG1 
1727 C  CG2 . VAL   A 206 ? 0.1724 0.1313 0.1705 0.0098  0.0109  -0.0138 207 VAL   A CG2 
1728 N  N   . THR   A 207 ? 0.1625 0.0962 0.1398 -0.0022 -0.0102 -0.0022 208 THR   A N   
1729 C  CA  . THR   A 207 ? 0.1834 0.1007 0.1456 0.0013  -0.0042 0.0024  208 THR   A CA  
1730 C  C   . THR   A 207 ? 0.1585 0.0924 0.1266 -0.0085 -0.0053 -0.0013 208 THR   A C   
1731 O  O   . THR   A 207 ? 0.1713 0.1058 0.1398 0.0003  -0.0230 -0.0008 208 THR   A O   
1732 C  CB  . THR   A 207 ? 0.1791 0.0955 0.1603 -0.0006 0.0043  -0.0078 208 THR   A CB  
1733 O  OG1 . THR   A 207 ? 0.2029 0.1132 0.1641 0.0000  -0.0003 -0.0215 208 THR   A OG1 
1734 C  CG2 . THR   A 207 ? 0.1913 0.1504 0.1720 -0.0197 0.0058  0.0053  208 THR   A CG2 
1735 N  N   . TRP   A 208 ? 0.1531 0.0985 0.1277 0.0000  -0.0078 -0.0019 209 TRP   A N   
1736 C  CA  . TRP   A 208 ? 0.1573 0.0955 0.1256 -0.0006 -0.0110 -0.0051 209 TRP   A CA  
1737 C  C   . TRP   A 208 ? 0.1685 0.1045 0.1120 0.0105  -0.0057 0.0001  209 TRP   A C   
1738 O  O   . TRP   A 208 ? 0.1641 0.1169 0.1174 -0.0059 -0.0041 0.0000  209 TRP   A O   
1739 C  CB  . TRP   A 208 ? 0.1760 0.1110 0.1208 0.0130  -0.0079 0.0040  209 TRP   A CB  
1740 C  CG  . TRP   A 208 ? 0.1441 0.0955 0.1284 0.0102  -0.0063 -0.0096 209 TRP   A CG  
1741 C  CD1 . TRP   A 208 ? 0.1709 0.1081 0.1261 0.0069  -0.0061 -0.0058 209 TRP   A CD1 
1742 C  CD2 . TRP   A 208 ? 0.1559 0.0895 0.1313 0.0013  -0.0070 0.0033  209 TRP   A CD2 
1743 N  NE1 . TRP   A 208 ? 0.1535 0.1127 0.1418 0.0064  -0.0049 -0.0002 209 TRP   A NE1 
1744 C  CE2 . TRP   A 208 ? 0.1587 0.0980 0.1357 0.0049  -0.0122 0.0091  209 TRP   A CE2 
1745 C  CE3 . TRP   A 208 ? 0.1638 0.0910 0.1259 0.0073  -0.0136 0.0033  209 TRP   A CE3 
1746 C  CZ2 . TRP   A 208 ? 0.1861 0.1009 0.1295 0.0163  0.0068  0.0114  209 TRP   A CZ2 
1747 C  CZ3 . TRP   A 208 ? 0.1794 0.1124 0.1214 0.0192  -0.0054 0.0089  209 TRP   A CZ3 
1748 C  CH2 . TRP   A 208 ? 0.1758 0.1012 0.1433 0.0201  -0.0054 -0.0006 209 TRP   A CH2 
1749 N  N   . ILE   A 209 ? 0.1562 0.0994 0.1203 0.0013  -0.0106 0.0030  210 ILE   A N   
1750 C  CA  . ILE   A 209 ? 0.1530 0.0968 0.1493 -0.0026 -0.0041 -0.0129 210 ILE   A CA  
1751 C  C   . ILE   A 209 ? 0.1444 0.0928 0.1215 -0.0084 -0.0062 0.0033  210 ILE   A C   
1752 O  O   . ILE   A 209 ? 0.1923 0.1067 0.1146 0.0034  -0.0119 -0.0013 210 ILE   A O   
1753 C  CB  . ILE   A 209 ? 0.1556 0.1021 0.1674 0.0055  -0.0046 -0.0100 210 ILE   A CB  
1754 C  CG1 . ILE   A 209 ? 0.1646 0.1098 0.1958 0.0206  -0.0059 -0.0144 210 ILE   A CG1 
1755 C  CG2 . ILE   A 209 ? 0.1647 0.1415 0.1855 0.0021  0.0001  0.0089  210 ILE   A CG2 
1756 C  CD1 . ILE   A 209 ? 0.1806 0.1183 0.2293 0.0250  -0.0157 0.0065  210 ILE   A CD1 
1757 N  N   . VAL   A 210 ? 0.1470 0.0864 0.1430 -0.0075 -0.0070 0.0029  211 VAL   A N   
1758 C  CA  . VAL   A 210 ? 0.1620 0.0930 0.1368 -0.0013 -0.0080 -0.0008 211 VAL   A CA  
1759 C  C   . VAL   A 210 ? 0.1751 0.0976 0.1196 0.0096  -0.0049 -0.0008 211 VAL   A C   
1760 O  O   . VAL   A 210 ? 0.1837 0.1243 0.1217 -0.0127 -0.0083 0.0075  211 VAL   A O   
1761 C  CB  . VAL   A 210 ? 0.1624 0.0874 0.1626 0.0022  -0.0092 0.0044  211 VAL   A CB  
1762 C  CG1 . VAL   A 210 ? 0.1857 0.0960 0.1649 0.0171  -0.0043 -0.0038 211 VAL   A CG1 
1763 C  CG2 . VAL   A 210 ? 0.1724 0.1172 0.1801 -0.0093 0.0009  0.0113  211 VAL   A CG2 
1764 N  N   . LEU   A 211 ? 0.1609 0.1183 0.1322 -0.0069 -0.0055 -0.0002 212 LEU   A N   
1765 C  CA  . LEU   A 211 ? 0.1649 0.1270 0.1424 -0.0164 -0.0128 0.0037  212 LEU   A CA  
1766 C  C   . LEU   A 211 ? 0.1647 0.1215 0.1377 -0.0152 -0.0187 -0.0013 212 LEU   A C   
1767 O  O   . LEU   A 211 ? 0.1758 0.1284 0.1500 -0.0119 -0.0073 0.0017  212 LEU   A O   
1768 C  CB  . LEU   A 211 ? 0.1692 0.1324 0.1591 -0.0096 -0.0282 0.0076  212 LEU   A CB  
1769 C  CG  . LEU   A 211 ? 0.1860 0.1316 0.1661 -0.0049 -0.0274 0.0038  212 LEU   A CG  
1770 C  CD1 . LEU   A 211 ? 0.1832 0.1798 0.1861 0.0010  -0.0421 0.0173  212 LEU   A CD1 
1771 C  CD2 . LEU   A 211 ? 0.1962 0.1460 0.1879 0.0044  0.0039  0.0035  212 LEU   A CD2 
1772 N  N   . LYS   A 212 ? 0.1664 0.1458 0.1524 -0.0257 -0.0068 0.0064  213 LYS   A N   
1773 C  CA  A LYS   A 212 ? 0.2226 0.1474 0.1544 -0.0232 -0.0236 0.0225  213 LYS   A CA  
1774 C  CA  B LYS   A 212 ? 0.1911 0.1384 0.1692 -0.0432 -0.0074 0.0252  213 LYS   A CA  
1775 C  C   . LYS   A 212 ? 0.1816 0.1306 0.1684 -0.0226 -0.0051 0.0179  213 LYS   A C   
1776 O  O   . LYS   A 212 ? 0.2068 0.1363 0.2280 -0.0137 -0.0318 0.0212  213 LYS   A O   
1777 C  CB  A LYS   A 212 ? 0.3125 0.1778 0.0901 -0.0340 -0.0167 0.0107  213 LYS   A CB  
1778 C  CB  B LYS   A 212 ? 0.1813 0.1731 0.1882 -0.0298 0.0046  0.0279  213 LYS   A CB  
1779 C  CG  A LYS   A 212 ? 0.3202 0.2235 0.2138 -0.0678 0.0343  0.0256  213 LYS   A CG  
1780 C  CG  B LYS   A 212 ? 0.2688 0.1942 0.2369 -0.0405 -0.0134 0.0674  213 LYS   A CG  
1781 C  CD  A LYS   A 212 ? 0.3292 0.2699 0.1729 -0.0943 0.0359  -0.0137 213 LYS   A CD  
1782 C  CD  B LYS   A 212 ? 0.4080 0.2456 0.2244 -0.1227 0.0034  0.0230  213 LYS   A CD  
1783 C  CE  A LYS   A 212 ? 0.2879 0.2651 0.4648 -0.1254 -0.0103 -0.0496 213 LYS   A CE  
1784 C  CE  B LYS   A 212 ? 0.4856 0.2982 0.3069 -0.1074 0.0006  0.1223  213 LYS   A CE  
1785 N  NZ  A LYS   A 212 ? 0.3217 0.1732 0.5743 -0.0489 0.0584  -0.0383 213 LYS   A NZ  
1786 N  NZ  B LYS   A 212 ? 0.6318 0.3921 0.3836 -0.1436 0.0989  0.0557  213 LYS   A NZ  
1787 N  N   . GLU   A 213 ? 0.1729 0.1463 0.1582 -0.0261 -0.0141 0.0105  214 GLU   A N   
1788 C  CA  . GLU   A 213 ? 0.1875 0.1355 0.1764 -0.0157 -0.0134 0.0085  214 GLU   A CA  
1789 C  C   . GLU   A 213 ? 0.1745 0.1124 0.1761 -0.0135 -0.0212 0.0120  214 GLU   A C   
1790 O  O   . GLU   A 213 ? 0.1849 0.1213 0.1643 -0.0064 -0.0066 0.0163  214 GLU   A O   
1791 C  CB  . GLU   A 213 ? 0.1881 0.1923 0.1668 -0.0300 -0.0089 0.0030  214 GLU   A CB  
1792 C  CG  . GLU   A 213 ? 0.2278 0.1889 0.2409 -0.0436 -0.0268 -0.0173 214 GLU   A CG  
1793 C  CD  . GLU   A 213 ? 0.2242 0.2339 0.2976 -0.0772 -0.0037 -0.0391 214 GLU   A CD  
1794 O  OE1 . GLU   A 213 ? 0.2226 0.1858 0.3460 -0.0234 -0.0489 -0.0003 214 GLU   A OE1 
1795 O  OE2 . GLU   A 213 ? 0.2843 0.6429 0.4234 -0.0773 -0.0540 -0.2231 214 GLU   A OE2 
1796 N  N   A PRO   A 214 ? 0.1754 0.1249 0.1486 -0.0061 -0.0154 0.0078  215 PRO   A N   
1797 N  N   B PRO   A 214 ? 0.2104 0.1025 0.1458 -0.0150 -0.0225 0.0075  215 PRO   A N   
1798 C  CA  A PRO   A 214 ? 0.1951 0.1150 0.1302 0.0026  -0.0157 0.0010  215 PRO   A CA  
1799 C  CA  B PRO   A 214 ? 0.2169 0.1125 0.1388 0.0063  -0.0172 0.0058  215 PRO   A CA  
1800 C  C   A PRO   A 214 ? 0.1912 0.1306 0.1412 -0.0043 -0.0198 -0.0158 215 PRO   A C   
1801 C  C   B PRO   A 214 ? 0.2064 0.0962 0.1555 -0.0117 -0.0206 -0.0040 215 PRO   A C   
1802 O  O   A PRO   A 214 ? 0.1893 0.1480 0.1546 -0.0076 -0.0196 0.0066  215 PRO   A O   
1803 O  O   B PRO   A 214 ? 0.2013 0.1317 0.1705 -0.0324 -0.0319 -0.0051 215 PRO   A O   
1804 C  CB  A PRO   A 214 ? 0.1812 0.1183 0.1817 0.0044  0.0038  -0.0021 215 PRO   A CB  
1805 C  CB  B PRO   A 214 ? 0.2053 0.0906 0.2106 -0.0085 -0.0170 0.0151  215 PRO   A CB  
1806 C  CG  A PRO   A 214 ? 0.1742 0.1263 0.1864 0.0001  -0.0081 0.0083  215 PRO   A CG  
1807 C  CG  B PRO   A 214 ? 0.2401 0.1560 0.1931 0.0215  0.0062  0.0026  215 PRO   A CG  
1808 C  CD  A PRO   A 214 ? 0.1923 0.0971 0.2075 -0.0277 -0.0062 -0.0098 215 PRO   A CD  
1809 C  CD  B PRO   A 214 ? 0.2285 0.1138 0.1620 -0.0016 0.0036  0.0291  215 PRO   A CD  
1810 N  N   . ILE   A 215 ? 0.2064 0.1365 0.1381 0.0048  -0.0190 -0.0039 216 ILE   A N   
1811 C  CA  . ILE   A 215 ? 0.2290 0.1239 0.1389 -0.0058 -0.0266 -0.0166 216 ILE   A CA  
1812 C  C   . ILE   A 215 ? 0.2002 0.1254 0.1520 -0.0167 -0.0043 -0.0139 216 ILE   A C   
1813 O  O   . ILE   A 215 ? 0.1923 0.1235 0.2176 -0.0104 -0.0044 -0.0300 216 ILE   A O   
1814 C  CB  . ILE   A 215 ? 0.2322 0.1240 0.1727 0.0053  -0.0307 -0.0109 216 ILE   A CB  
1815 C  CG1 . ILE   A 215 ? 0.2382 0.1295 0.1781 -0.0079 -0.0234 0.0059  216 ILE   A CG1 
1816 C  CG2 . ILE   A 215 ? 0.2532 0.1465 0.1858 0.0171  -0.0187 -0.0284 216 ILE   A CG2 
1817 C  CD1 . ILE   A 215 ? 0.2893 0.1432 0.1781 0.0201  -0.0210 0.0111  216 ILE   A CD1 
1818 N  N   A SER   A 216 ? 0.2340 0.1018 0.1856 -0.0065 -0.0365 -0.0197 217 SER   A N   
1819 N  N   B SER   A 216 ? 0.2193 0.1521 0.1672 -0.0109 -0.0252 -0.0264 217 SER   A N   
1820 C  CA  A SER   A 216 ? 0.2318 0.1100 0.1486 -0.0185 -0.0384 -0.0212 217 SER   A CA  
1821 C  CA  B SER   A 216 ? 0.2603 0.1366 0.1782 0.0115  -0.0334 -0.0168 217 SER   A CA  
1822 C  C   A SER   A 216 ? 0.2157 0.1315 0.1495 -0.0044 -0.0511 0.0006  217 SER   A C   
1823 C  C   B SER   A 216 ? 0.2207 0.1144 0.1787 -0.0121 -0.0362 -0.0057 217 SER   A C   
1824 O  O   A SER   A 216 ? 0.2420 0.1579 0.1830 0.0044  -0.0615 0.0248  217 SER   A O   
1825 O  O   B SER   A 216 ? 0.2229 0.1207 0.1847 -0.0147 -0.0339 -0.0001 217 SER   A O   
1826 C  CB  A SER   A 216 ? 0.2455 0.0917 0.1754 -0.0183 -0.0305 -0.0242 217 SER   A CB  
1827 C  CB  B SER   A 216 ? 0.2812 0.1867 0.2617 -0.0035 -0.0172 0.0819  217 SER   A CB  
1828 O  OG  A SER   A 216 ? 0.3037 0.1837 0.1829 -0.0344 -0.0290 0.0096  217 SER   A OG  
1829 O  OG  B SER   A 216 ? 0.2717 0.2600 0.2915 -0.0700 -0.0620 -0.0127 217 SER   A OG  
1830 N  N   . VAL   A 217 ? 0.2226 0.1093 0.1685 -0.0137 -0.0337 -0.0027 218 VAL   A N   
1831 C  CA  . VAL   A 217 ? 0.2531 0.1007 0.1659 -0.0234 -0.0281 -0.0057 218 VAL   A CA  
1832 C  C   . VAL   A 217 ? 0.2212 0.0998 0.1780 -0.0239 -0.0209 -0.0029 218 VAL   A C   
1833 O  O   . VAL   A 217 ? 0.2359 0.1048 0.1890 -0.0268 -0.0297 -0.0031 218 VAL   A O   
1834 C  CB  . VAL   A 217 ? 0.2314 0.0988 0.2326 -0.0153 -0.0475 -0.0114 218 VAL   A CB  
1835 C  CG1 . VAL   A 217 ? 0.2669 0.1185 0.1932 -0.0143 -0.0469 -0.0139 218 VAL   A CG1 
1836 C  CG2 . VAL   A 217 ? 0.2249 0.1187 0.2534 -0.0222 -0.0326 -0.0086 218 VAL   A CG2 
1837 N  N   . SER   A 218 ? 0.2366 0.1080 0.1649 -0.0121 -0.0314 -0.0166 219 SER   A N   
1838 C  CA  . SER   A 218 ? 0.2420 0.1068 0.1791 -0.0196 -0.0314 -0.0208 219 SER   A CA  
1839 C  C   . SER   A 218 ? 0.2494 0.1083 0.1753 -0.0177 -0.0380 -0.0054 219 SER   A C   
1840 O  O   . SER   A 218 ? 0.2616 0.1058 0.1870 -0.0252 -0.0399 -0.0072 219 SER   A O   
1841 C  CB  . SER   A 218 ? 0.2621 0.1291 0.1790 -0.0240 -0.0275 -0.0239 219 SER   A CB  
1842 O  OG  . SER   A 218 ? 0.2736 0.1449 0.1789 -0.0227 -0.0296 -0.0111 219 SER   A OG  
1843 N  N   A SER   A 219 ? 0.2269 0.1036 0.1854 -0.0204 -0.0262 -0.0016 220 SER   A N   
1844 N  N   B SER   A 219 ? 0.2559 0.1072 0.2139 -0.0055 -0.0265 0.0037  220 SER   A N   
1845 C  CA  A SER   A 219 ? 0.2481 0.1128 0.1949 -0.0138 -0.0231 -0.0233 220 SER   A CA  
1846 C  CA  B SER   A 219 ? 0.2728 0.1120 0.2824 0.0161  -0.0179 0.0507  220 SER   A CA  
1847 C  C   A SER   A 219 ? 0.2645 0.1120 0.2323 -0.0233 -0.0185 -0.0040 220 SER   A C   
1848 C  C   B SER   A 219 ? 0.2834 0.0939 0.2529 -0.0225 -0.0343 0.0055  220 SER   A C   
1849 O  O   A SER   A 219 ? 0.2546 0.0996 0.2594 -0.0198 -0.0052 -0.0032 220 SER   A O   
1850 O  O   B SER   A 219 ? 0.2568 0.1347 0.2756 -0.0038 0.0146  0.0086  220 SER   A O   
1851 C  CB  A SER   A 219 ? 0.2400 0.1177 0.2363 -0.0144 -0.0190 -0.0093 220 SER   A CB  
1852 C  CB  B SER   A 219 ? 0.3391 0.1131 0.3450 -0.0102 0.0128  0.0592  220 SER   A CB  
1853 O  OG  A SER   A 219 ? 0.2565 0.0727 0.2258 -0.0237 -0.0095 -0.0207 220 SER   A OG  
1854 O  OG  B SER   A 219 ? 0.3176 0.2521 0.3776 -0.0380 0.0102  0.0594  220 SER   A OG  
1855 N  N   . GLU   A 220 ? 0.2596 0.1181 0.2050 -0.0143 -0.0025 -0.0156 221 GLU   A N   
1856 C  CA  . GLU   A 220 ? 0.3037 0.1279 0.2233 -0.0212 -0.0006 -0.0067 221 GLU   A CA  
1857 C  C   . GLU   A 220 ? 0.3036 0.1274 0.1795 -0.0117 -0.0117 0.0039  221 GLU   A C   
1858 O  O   . GLU   A 220 ? 0.3191 0.1417 0.2161 -0.0046 0.0348  -0.0100 221 GLU   A O   
1859 C  CB  . GLU   A 220 ? 0.3592 0.1806 0.2044 -0.0279 -0.0366 -0.0475 221 GLU   A CB  
1860 C  CG  . GLU   A 220 ? 0.4242 0.1852 0.2481 -0.0281 -0.0159 -0.0551 221 GLU   A CG  
1861 C  CD  . GLU   A 220 ? 0.3965 0.1737 0.3156 -0.0731 -0.0179 -0.0671 221 GLU   A CD  
1862 O  OE1 . GLU   A 220 ? 0.3443 0.1632 0.2861 -0.0348 -0.0303 -0.0147 221 GLU   A OE1 
1863 O  OE2 . GLU   A 220 ? 0.5483 0.1954 0.4290 -0.0723 0.0386  -0.0926 221 GLU   A OE2 
1864 N  N   . GLN   A 221 ? 0.2582 0.1104 0.1879 -0.0089 -0.0258 -0.0114 222 GLN   A N   
1865 C  CA  . GLN   A 221 ? 0.2534 0.1125 0.1881 -0.0077 -0.0245 -0.0108 222 GLN   A CA  
1866 C  C   . GLN   A 221 ? 0.2426 0.1259 0.1806 -0.0073 -0.0134 0.0095  222 GLN   A C   
1867 O  O   . GLN   A 221 ? 0.2544 0.1397 0.1878 -0.0218 -0.0069 0.0140  222 GLN   A O   
1868 C  CB  . GLN   A 221 ? 0.2432 0.1504 0.1645 -0.0146 -0.0325 -0.0111 222 GLN   A CB  
1869 C  CG  . GLN   A 221 ? 0.2490 0.1333 0.1830 -0.0171 -0.0386 -0.0043 222 GLN   A CG  
1870 C  CD  . GLN   A 221 ? 0.2389 0.1257 0.1773 -0.0201 -0.0385 -0.0116 222 GLN   A CD  
1871 O  OE1 . GLN   A 221 ? 0.2444 0.1262 0.1813 -0.0049 -0.0282 -0.0136 222 GLN   A OE1 
1872 N  NE2 . GLN   A 221 ? 0.2405 0.1467 0.1936 -0.0040 -0.0403 -0.0099 222 GLN   A NE2 
1873 N  N   . VAL   A 222 ? 0.2456 0.1276 0.1852 -0.0250 -0.0242 0.0204  223 VAL   A N   
1874 C  CA  . VAL   A 222 ? 0.2466 0.1294 0.1868 -0.0133 -0.0197 0.0244  223 VAL   A CA  
1875 C  C   . VAL   A 222 ? 0.2554 0.1449 0.1909 -0.0357 0.0027  0.0152  223 VAL   A C   
1876 O  O   . VAL   A 222 ? 0.2595 0.1612 0.2022 -0.0386 0.0000  0.0179  223 VAL   A O   
1877 C  CB  . VAL   A 222 ? 0.2700 0.1860 0.2177 -0.0322 -0.0118 0.0613  223 VAL   A CB  
1878 C  CG1 . VAL   A 222 ? 0.2737 0.1941 0.3004 -0.0306 -0.0284 0.0916  223 VAL   A CG1 
1879 C  CG2 . VAL   A 222 ? 0.2734 0.2458 0.2488 -0.0124 -0.0545 0.0465  223 VAL   A CG2 
1880 N  N   A LEU   A 223 ? 0.2477 0.1117 0.2519 -0.0253 0.0109  0.0036  224 LEU   A N   
1881 N  N   B LEU   A 223 ? 0.2669 0.1100 0.2623 -0.0005 0.0083  -0.0065 224 LEU   A N   
1882 C  CA  A LEU   A 223 ? 0.2742 0.0982 0.3062 -0.0335 0.0313  -0.0252 224 LEU   A CA  
1883 C  CA  B LEU   A 223 ? 0.2721 0.1516 0.2882 -0.0333 0.0214  -0.0301 224 LEU   A CA  
1884 C  C   A LEU   A 223 ? 0.2539 0.1377 0.2386 -0.0375 0.0091  -0.0230 224 LEU   A C   
1885 C  C   B LEU   A 223 ? 0.2691 0.1588 0.2037 -0.0279 -0.0096 -0.0363 224 LEU   A C   
1886 O  O   A LEU   A 223 ? 0.2555 0.1729 0.2139 -0.0203 0.0279  -0.0133 224 LEU   A O   
1887 O  O   B LEU   A 223 ? 0.2744 0.1811 0.2630 -0.0304 0.0274  -0.0629 224 LEU   A O   
1888 C  CB  A LEU   A 223 ? 0.3122 0.1100 0.3412 -0.0069 0.0236  -0.0646 224 LEU   A CB  
1889 C  CB  B LEU   A 223 ? 0.2822 0.1927 0.3005 -0.0606 0.0275  -0.0478 224 LEU   A CB  
1890 C  CG  A LEU   A 223 ? 0.3825 0.1948 0.3062 -0.0299 0.0855  -0.0026 224 LEU   A CG  
1891 C  CG  B LEU   A 223 ? 0.2935 0.1995 0.3938 -0.0046 0.0195  -0.1274 224 LEU   A CG  
1892 C  CD1 A LEU   A 223 ? 0.4205 0.1401 0.5148 0.0301  -0.0193 -0.0449 224 LEU   A CD1 
1893 C  CD1 B LEU   A 223 ? 0.3601 0.3651 0.4268 0.0390  -0.0195 -0.0805 224 LEU   A CD1 
1894 C  CD2 A LEU   A 223 ? 0.4096 0.1488 0.3978 0.0209  0.1119  -0.0291 224 LEU   A CD2 
1895 C  CD2 B LEU   A 223 ? 0.3805 0.2672 0.4926 -0.0774 -0.0043 -0.1585 224 LEU   A CD2 
1896 N  N   . LYS   A 224 ? 0.2536 0.1697 0.2143 -0.0287 -0.0023 -0.0231 225 LYS   A N   
1897 C  CA  . LYS   A 224 ? 0.2857 0.2015 0.1905 -0.0414 0.0136  -0.0250 225 LYS   A CA  
1898 C  C   . LYS   A 224 ? 0.2492 0.1808 0.1430 -0.0223 -0.0081 0.0117  225 LYS   A C   
1899 O  O   . LYS   A 224 ? 0.2851 0.1725 0.1509 -0.0254 0.0172  0.0012  225 LYS   A O   
1900 C  CB  . LYS   A 224 ? 0.2943 0.2642 0.2104 -0.0434 -0.0232 0.0136  225 LYS   A CB  
1901 C  CG  . LYS   A 224 ? 0.2901 0.3941 0.2393 -0.0570 -0.0386 -0.0364 225 LYS   A CG  
1902 C  CD  . LYS   A 224 ? 0.3496 0.3545 0.3516 -0.0578 -0.0939 -0.0630 225 LYS   A CD  
1903 C  CE  . LYS   A 224 ? 0.4857 0.5353 0.4546 -0.1656 -0.0387 -0.2055 225 LYS   A CE  
1904 N  NZ  . LYS   A 224 ? 0.4856 0.4707 0.4024 -0.1063 0.0578  -0.1699 225 LYS   A NZ  
1905 N  N   . PHE   A 225 ? 0.2493 0.1479 0.1486 -0.0156 -0.0048 -0.0011 226 PHE   A N   
1906 C  CA  . PHE   A 225 ? 0.2518 0.1429 0.1504 -0.0156 0.0075  -0.0040 226 PHE   A CA  
1907 C  C   . PHE   A 225 ? 0.2609 0.1428 0.1499 -0.0316 0.0000  0.0021  226 PHE   A C   
1908 O  O   . PHE   A 225 ? 0.2557 0.1500 0.1652 -0.0335 0.0187  -0.0190 226 PHE   A O   
1909 C  CB  . PHE   A 225 ? 0.2578 0.1480 0.1550 -0.0072 0.0158  0.0085  226 PHE   A CB  
1910 C  CG  . PHE   A 225 ? 0.2492 0.1408 0.1675 -0.0295 0.0043  -0.0350 226 PHE   A CG  
1911 C  CD1 . PHE   A 225 ? 0.2666 0.2125 0.1973 -0.0063 0.0162  0.0044  226 PHE   A CD1 
1912 C  CD2 . PHE   A 225 ? 0.2565 0.2118 0.1747 -0.0231 0.0214  -0.0323 226 PHE   A CD2 
1913 C  CE1 . PHE   A 225 ? 0.2780 0.2563 0.2069 0.0105  0.0147  0.0004  226 PHE   A CE1 
1914 C  CE2 . PHE   A 225 ? 0.2330 0.2882 0.2529 -0.0210 -0.0085 -0.1176 226 PHE   A CE2 
1915 C  CZ  . PHE   A 225 ? 0.2536 0.2280 0.2456 -0.0230 0.0001  -0.0846 226 PHE   A CZ  
1916 N  N   . ARG   A 226 ? 0.2424 0.1496 0.1534 -0.0110 0.0001  -0.0114 227 ARG   A N   
1917 C  CA  . ARG   A 226 ? 0.2590 0.1525 0.1703 -0.0061 0.0021  -0.0122 227 ARG   A CA  
1918 C  C   . ARG   A 226 ? 0.2609 0.1775 0.2037 -0.0346 0.0222  -0.0227 227 ARG   A C   
1919 O  O   . ARG   A 226 ? 0.2677 0.1989 0.2107 -0.0037 0.0361  -0.0287 227 ARG   A O   
1920 C  CB  . ARG   A 226 ? 0.2867 0.1391 0.1824 0.0111  -0.0009 -0.0292 227 ARG   A CB  
1921 C  CG  . ARG   A 226 ? 0.2657 0.1348 0.1764 0.0044  0.0072  -0.0168 227 ARG   A CG  
1922 C  CD  . ARG   A 226 ? 0.3198 0.1455 0.1773 0.0043  0.0016  -0.0187 227 ARG   A CD  
1923 N  NE  . ARG   A 226 ? 0.2757 0.1225 0.1804 -0.0308 -0.0190 -0.0210 227 ARG   A NE  
1924 C  CZ  . ARG   A 226 ? 0.2894 0.1328 0.2221 -0.0301 0.0000  -0.0390 227 ARG   A CZ  
1925 N  NH1 . ARG   A 226 ? 0.2932 0.1826 0.3486 -0.0381 -0.0219 -0.1080 227 ARG   A NH1 
1926 N  NH2 . ARG   A 226 ? 0.2913 0.1617 0.2341 -0.0380 0.0365  -0.0025 227 ARG   A NH2 
1927 N  N   . LYS   A 227 ? 0.2524 0.1599 0.1567 -0.0259 0.0190  -0.0315 228 LYS   A N   
1928 C  CA  . LYS   A 227 ? 0.3016 0.2120 0.1595 -0.0735 0.0370  -0.0494 228 LYS   A CA  
1929 C  C   . LYS   A 227 ? 0.2756 0.2010 0.1376 -0.0559 0.0176  -0.0463 228 LYS   A C   
1930 O  O   . LYS   A 227 ? 0.3194 0.2262 0.1468 -0.0559 0.0319  -0.0435 228 LYS   A O   
1931 C  CB  . LYS   A 227 ? 0.3309 0.2452 0.1626 -0.0773 0.0071  -0.0544 228 LYS   A CB  
1932 C  CG  . LYS   A 227 ? 0.4021 0.2499 0.2139 -0.1076 0.0502  -0.0736 228 LYS   A CG  
1933 C  CD  . LYS   A 227 ? 0.4673 0.4050 0.2621 -0.1882 0.0206  -0.1244 228 LYS   A CD  
1934 C  CE  . LYS   A 227 ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  228 LYS   A CE  
1935 N  NZ  . LYS   A 227 ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  228 LYS   A NZ  
1936 N  N   . LEU   A 228 ? 0.2879 0.1769 0.1490 -0.0576 0.0237  -0.0343 229 LEU   A N   
1937 C  CA  . LEU   A 228 ? 0.2870 0.1749 0.1289 -0.0378 0.0115  -0.0234 229 LEU   A CA  
1938 C  C   . LEU   A 228 ? 0.3183 0.1585 0.1483 -0.0248 0.0303  -0.0131 229 LEU   A C   
1939 O  O   . LEU   A 228 ? 0.2666 0.1755 0.1509 -0.0117 0.0203  -0.0236 229 LEU   A O   
1940 C  CB  . LEU   A 228 ? 0.3033 0.1562 0.1295 -0.0230 0.0223  -0.0098 229 LEU   A CB  
1941 C  CG  . LEU   A 228 ? 0.2727 0.2002 0.1421 -0.0370 0.0047  -0.0083 229 LEU   A CG  
1942 C  CD1 . LEU   A 228 ? 0.2780 0.2073 0.1546 -0.0364 0.0150  -0.0241 229 LEU   A CD1 
1943 C  CD2 . LEU   A 228 ? 0.3493 0.1931 0.1749 0.0013  0.0216  0.0182  229 LEU   A CD2 
1944 N  N   . ASN   A 229 ? 0.2725 0.1911 0.1535 -0.0441 0.0395  -0.0139 230 ASN   A N   
1945 C  CA  . ASN   A 229 ? 0.2638 0.2110 0.1406 -0.0156 0.0370  -0.0394 230 ASN   A CA  
1946 C  C   . ASN   A 229 ? 0.2575 0.1976 0.1412 -0.0103 0.0266  -0.0111 230 ASN   A C   
1947 O  O   . ASN   A 229 ? 0.2625 0.1852 0.1934 -0.0189 0.0102  -0.0003 230 ASN   A O   
1948 C  CB  . ASN   A 229 ? 0.2897 0.2346 0.1504 -0.0434 0.0296  -0.0216 230 ASN   A CB  
1949 C  CG  . ASN   A 229 ? 0.3597 0.2103 0.1601 -0.0244 0.0374  -0.0187 230 ASN   A CG  
1950 O  OD1 . ASN   A 229 ? 0.4350 0.2586 0.1768 -0.0019 0.0577  -0.0374 230 ASN   A OD1 
1951 N  ND2 . ASN   A 229 ? 0.3722 0.2109 0.2035 -0.0362 0.0522  -0.0536 230 ASN   A ND2 
1952 N  N   . PHE   A 230 ? 0.2558 0.1902 0.1801 -0.0556 0.0368  -0.0108 231 PHE   A N   
1953 C  CA  . PHE   A 230 ? 0.2605 0.1919 0.1720 -0.0520 0.0016  0.0032  231 PHE   A CA  
1954 C  C   . PHE   A 230 ? 0.2738 0.2068 0.1951 -0.0599 0.0226  -0.0245 231 PHE   A C   
1955 O  O   . PHE   A 230 ? 0.2933 0.2020 0.2065 -0.0704 0.0299  0.0061  231 PHE   A O   
1956 C  CB  . PHE   A 230 ? 0.2583 0.1890 0.1981 -0.0208 0.0335  0.0016  231 PHE   A CB  
1957 C  CG  . PHE   A 230 ? 0.2384 0.1611 0.2100 -0.0532 0.0278  -0.0115 231 PHE   A CG  
1958 C  CD1 . PHE   A 230 ? 0.2788 0.1987 0.1641 -0.0225 0.0192  -0.0160 231 PHE   A CD1 
1959 C  CD2 . PHE   A 230 ? 0.2989 0.1763 0.1822 -0.0161 0.0298  -0.0230 231 PHE   A CD2 
1960 C  CE1 . PHE   A 230 ? 0.3084 0.1778 0.1891 -0.0561 0.0051  0.0030  231 PHE   A CE1 
1961 C  CE2 . PHE   A 230 ? 0.2712 0.2279 0.1659 -0.0203 -0.0109 -0.0115 231 PHE   A CE2 
1962 C  CZ  . PHE   A 230 ? 0.2452 0.2172 0.1588 -0.0217 -0.0081 0.0114  231 PHE   A CZ  
1963 N  N   . ASN   A 231 ? 0.2861 0.2090 0.1683 -0.0542 0.0436  -0.0143 232 ASN   A N   
1964 C  CA  . ASN   A 231 ? 0.2664 0.2179 0.1879 -0.0451 0.0301  0.0106  232 ASN   A CA  
1965 C  C   . ASN   A 231 ? 0.2441 0.2229 0.1678 -0.0104 0.0345  -0.0133 232 ASN   A C   
1966 O  O   . ASN   A 231 ? 0.2812 0.2275 0.1978 -0.0079 0.0332  0.0057  232 ASN   A O   
1967 C  CB  . ASN   A 231 ? 0.2809 0.2402 0.2612 -0.0232 0.0776  0.0141  232 ASN   A CB  
1968 C  CG  . ASN   A 231 ? 0.2585 0.2460 0.2319 0.0053  0.0458  0.0275  232 ASN   A CG  
1969 O  OD1 . ASN   A 231 ? 0.3341 0.2278 0.2292 -0.0372 0.0827  -0.0322 232 ASN   A OD1 
1970 N  ND2 . ASN   A 231 ? 0.3037 0.2868 0.2196 0.0127  0.0319  -0.0140 232 ASN   A ND2 
1971 N  N   . GLY   A 232 ? 0.3062 0.2114 0.2098 -0.0490 0.0343  0.0131  233 GLY   A N   
1972 C  CA  . GLY   A 232 ? 0.2991 0.2426 0.1896 -0.0300 0.0332  0.0208  233 GLY   A CA  
1973 C  C   . GLY   A 232 ? 0.2466 0.2145 0.2294 -0.0190 0.0030  0.0135  233 GLY   A C   
1974 O  O   . GLY   A 232 ? 0.3519 0.2511 0.2151 0.0178  0.0913  0.0241  233 GLY   A O   
1975 N  N   . GLU   A 233 ? 0.2678 0.2509 0.1982 -0.0207 0.0245  0.0010  234 GLU   A N   
1976 C  CA  . GLU   A 233 ? 0.2610 0.2250 0.2009 -0.0080 0.0109  0.0116  234 GLU   A CA  
1977 C  C   . GLU   A 233 ? 0.2802 0.2746 0.2164 0.0082  0.0269  0.0293  234 GLU   A C   
1978 O  O   . GLU   A 233 ? 0.2758 0.3249 0.2322 -0.0030 0.0394  0.0351  234 GLU   A O   
1979 C  CB  . GLU   A 233 ? 0.3046 0.2262 0.2040 0.0241  0.0064  0.0302  234 GLU   A CB  
1980 C  CG  . GLU   A 233 ? 0.3170 0.2920 0.2122 -0.0483 0.0184  0.0324  234 GLU   A CG  
1981 C  CD  . GLU   A 233 ? 0.4326 0.4140 0.2558 0.0646  0.0105  0.0100  234 GLU   A CD  
1982 O  OE1 . GLU   A 233 ? 0.3787 0.3385 0.3134 0.0419  0.0232  0.0766  234 GLU   A OE1 
1983 O  OE2 . GLU   A 233 ? 0.5450 0.4097 0.2850 -0.0770 -0.0228 0.0010  234 GLU   A OE2 
1984 N  N   . GLY   A 234 ? 0.4044 0.3209 0.2127 0.0594  0.0706  0.0088  235 GLY   A N   
1985 C  CA  . GLY   A 234 ? 0.3974 0.3428 0.2655 0.0792  0.0669  0.0390  235 GLY   A CA  
1986 C  C   . GLY   A 234 ? 0.4485 0.3790 0.2297 0.1166  0.0779  0.0884  235 GLY   A C   
1987 O  O   . GLY   A 234 ? 0.4509 0.6170 0.2874 0.0804  0.1629  0.0335  235 GLY   A O   
1988 N  N   . GLU   A 235 ? 0.3671 0.3358 0.2587 0.0919  0.0795  0.1011  236 GLU   A N   
1989 C  CA  . GLU   A 235 ? 0.3617 0.2967 0.2523 0.0901  0.0798  0.1249  236 GLU   A CA  
1990 C  C   . GLU   A 235 ? 0.3908 0.3149 0.3382 0.1167  0.1088  0.1576  236 GLU   A C   
1991 O  O   . GLU   A 235 ? 0.4060 0.4528 0.2665 0.0944  0.1013  0.0483  236 GLU   A O   
1992 C  CB  . GLU   A 235 ? 0.3727 0.3158 0.3084 0.0543  0.1012  0.0872  236 GLU   A CB  
1993 C  CG  . GLU   A 235 ? 0.3583 0.3231 0.4804 0.0343  0.0949  0.2041  236 GLU   A CG  
1994 C  CD  . GLU   A 235 ? 0.5830 0.4992 0.5244 -0.0738 0.1004  0.1196  236 GLU   A CD  
1995 O  OE1 . GLU   A 235 ? 0.3321 0.5911 0.6827 -0.0761 0.1682  0.1120  236 GLU   A OE1 
1996 O  OE2 . GLU   A 235 ? 0.7519 0.6301 0.8239 -0.2146 0.1613  0.3559  236 GLU   A OE2 
1997 N  N   . PRO   A 236 ? 0.3677 0.3443 0.2857 0.1180  0.1022  0.1568  237 PRO   A N   
1998 C  CA  . PRO   A 236 ? 0.4408 0.3192 0.3327 0.1812  0.1754  0.1838  237 PRO   A CA  
1999 C  C   . PRO   A 236 ? 0.3631 0.3182 0.2260 0.0445  0.1073  0.0505  237 PRO   A C   
2000 O  O   . PRO   A 236 ? 0.3478 0.2713 0.2766 0.0203  0.0987  0.0353  237 PRO   A O   
2001 C  CB  . PRO   A 236 ? 0.3845 0.4305 0.4006 0.1537  0.1692  0.2095  237 PRO   A CB  
2002 C  CG  . PRO   A 236 ? 0.3420 0.5107 0.4895 0.1289  0.1208  0.2764  237 PRO   A CG  
2003 C  CD  . PRO   A 236 ? 0.3565 0.5104 0.4294 0.1430  0.0495  0.1394  237 PRO   A CD  
2004 N  N   . GLU   A 237 ? 0.3464 0.3464 0.2924 0.0502  0.0878  -0.0013 238 GLU   A N   
2005 C  CA  . GLU   A 237 ? 0.3497 0.2988 0.2296 -0.0339 0.0775  -0.0548 238 GLU   A CA  
2006 C  C   . GLU   A 237 ? 0.3097 0.2034 0.2544 -0.0037 0.0804  -0.0383 238 GLU   A C   
2007 O  O   . GLU   A 237 ? 0.3317 0.2247 0.2318 0.0174  0.0584  -0.0196 238 GLU   A O   
2008 C  CB  . GLU   A 237 ? 0.3609 0.2889 0.2716 0.0361  -0.0271 -0.1145 238 GLU   A CB  
2009 C  CG  . GLU   A 237 ? 0.3907 0.3146 0.3815 -0.0182 0.0345  -0.1088 238 GLU   A CG  
2010 C  CD  . GLU   A 237 ? 0.3859 0.4216 0.3581 -0.0708 0.0785  -0.1641 238 GLU   A CD  
2011 O  OE1 . GLU   A 237 ? 0.5886 0.5237 0.6649 0.0137  -0.0656 -0.3534 238 GLU   A OE1 
2012 O  OE2 . GLU   A 237 ? 0.4295 0.3116 0.2612 -0.0602 0.0615  -0.0970 238 GLU   A OE2 
2013 N  N   A GLU   A 238 ? 0.3404 0.2016 0.2142 -0.0822 0.0833  -0.0621 239 GLU   A N   
2014 N  N   B GLU   A 238 ? 0.2491 0.1841 0.1939 -0.0050 0.0461  -0.0150 239 GLU   A N   
2015 C  CA  A GLU   A 238 ? 0.2610 0.3231 0.2090 -0.0735 0.0425  -0.0606 239 GLU   A CA  
2016 C  CA  B GLU   A 238 ? 0.2327 0.1628 0.1925 0.0354  0.0363  -0.0136 239 GLU   A CA  
2017 C  C   A GLU   A 238 ? 0.2608 0.2648 0.1579 -0.0848 0.0533  -0.0514 239 GLU   A C   
2018 C  C   B GLU   A 238 ? 0.2236 0.1571 0.1618 0.0279  0.0479  -0.0193 239 GLU   A C   
2019 O  O   A GLU   A 238 ? 0.2928 0.2473 0.1749 -0.0724 0.0139  -0.0300 239 GLU   A O   
2020 O  O   B GLU   A 238 ? 0.2390 0.1463 0.2254 0.0228  -0.0143 -0.0423 239 GLU   A O   
2021 C  CB  A GLU   A 238 ? 0.2085 0.3420 0.2734 -0.0472 0.0546  -0.1009 239 GLU   A CB  
2022 C  CB  B GLU   A 238 ? 0.2537 0.1485 0.1843 0.0352  0.0206  0.0092  239 GLU   A CB  
2023 C  CG  A GLU   A 238 ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  239 GLU   A CG  
2024 C  CG  B GLU   A 238 ? 0.2626 0.2158 0.2179 0.0132  0.0352  0.0017  239 GLU   A CG  
2025 C  CD  A GLU   A 238 ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  239 GLU   A CD  
2026 C  CD  B GLU   A 238 ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  239 GLU   A CD  
2027 O  OE1 A GLU   A 238 ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  239 GLU   A OE1 
2028 O  OE1 B GLU   A 238 ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  239 GLU   A OE1 
2029 O  OE2 A GLU   A 238 ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  239 GLU   A OE2 
2030 O  OE2 B GLU   A 238 ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  239 GLU   A OE2 
2031 N  N   . LEU   A 239 ? 0.2819 0.2164 0.1685 -0.0383 0.0414  -0.0238 240 LEU   A N   
2032 C  CA  . LEU   A 239 ? 0.2420 0.1868 0.1863 -0.0401 0.0388  -0.0334 240 LEU   A CA  
2033 C  C   . LEU   A 239 ? 0.2481 0.1659 0.1412 -0.0100 0.0304  0.0068  240 LEU   A C   
2034 O  O   . LEU   A 239 ? 0.2391 0.2037 0.1685 -0.0164 0.0427  -0.0080 240 LEU   A O   
2035 C  CB  . LEU   A 239 ? 0.2821 0.1637 0.2177 0.0019  0.0248  -0.0173 240 LEU   A CB  
2036 C  CG  . LEU   A 239 ? 0.2554 0.1830 0.2504 -0.0016 -0.0012 -0.0550 240 LEU   A CG  
2037 C  CD1 . LEU   A 239 ? 0.3661 0.1645 0.3961 0.0152  -0.0159 -0.0380 240 LEU   A CD1 
2038 C  CD2 . LEU   A 239 ? 0.3062 0.1904 0.2226 0.0064  0.0088  -0.0475 240 LEU   A CD2 
2039 N  N   . MET   A 240 ? 0.2436 0.1772 0.1444 0.0057  0.0423  -0.0104 241 MET   A N   
2040 C  CA  . MET   A 240 ? 0.2687 0.1588 0.1404 -0.0087 0.0512  -0.0100 241 MET   A CA  
2041 C  C   . MET   A 240 ? 0.2390 0.1481 0.1399 -0.0251 0.0219  -0.0269 241 MET   A C   
2042 O  O   . MET   A 240 ? 0.2377 0.1669 0.1459 -0.0234 0.0225  -0.0069 241 MET   A O   
2043 C  CB  . MET   A 240 ? 0.2973 0.1492 0.1450 -0.0004 0.0285  -0.0027 241 MET   A CB  
2044 C  CG  . MET   A 240 ? 0.2824 0.1708 0.1489 -0.0302 0.0495  -0.0244 241 MET   A CG  
2045 S  SD  . MET   A 240 ? 0.2842 0.1453 0.1745 -0.0217 0.0271  -0.0018 241 MET   A SD  
2046 C  CE  . MET   A 240 ? 0.3107 0.1243 0.2268 -0.0379 0.0585  0.0122  241 MET   A CE  
2047 N  N   . VAL   A 241 ? 0.2422 0.1358 0.1455 -0.0199 0.0228  -0.0096 242 VAL   A N   
2048 C  CA  . VAL   A 241 ? 0.2450 0.1319 0.1342 -0.0179 0.0201  -0.0166 242 VAL   A CA  
2049 C  C   . VAL   A 241 ? 0.2447 0.1333 0.1333 -0.0118 0.0194  -0.0290 242 VAL   A C   
2050 O  O   . VAL   A 241 ? 0.2136 0.1571 0.1612 -0.0205 0.0265  -0.0161 242 VAL   A O   
2051 C  CB  . VAL   A 241 ? 0.2383 0.1342 0.1652 -0.0190 0.0217  -0.0293 242 VAL   A CB  
2052 C  CG1 . VAL   A 241 ? 0.2793 0.1416 0.1707 -0.0138 -0.0077 -0.0255 242 VAL   A CG1 
2053 C  CG2 . VAL   A 241 ? 0.2461 0.1496 0.1762 -0.0182 0.0317  -0.0225 242 VAL   A CG2 
2054 N  N   . ASP   A 242 ? 0.2498 0.1160 0.1235 -0.0026 0.0144  -0.0147 243 ASP   A N   
2055 C  CA  . ASP   A 242 ? 0.2296 0.1090 0.1377 0.0152  0.0129  -0.0218 243 ASP   A CA  
2056 C  C   . ASP   A 242 ? 0.2103 0.1258 0.1293 -0.0087 0.0178  -0.0214 243 ASP   A C   
2057 O  O   . ASP   A 242 ? 0.2103 0.1264 0.1976 -0.0105 0.0087  -0.0200 243 ASP   A O   
2058 C  CB  . ASP   A 242 ? 0.2143 0.1081 0.1690 -0.0013 0.0113  -0.0094 243 ASP   A CB  
2059 C  CG  . ASP   A 242 ? 0.2258 0.1161 0.1693 0.0001  0.0118  -0.0192 243 ASP   A CG  
2060 O  OD1 . ASP   A 242 ? 0.2149 0.1134 0.1858 0.0093  0.0207  -0.0141 243 ASP   A OD1 
2061 O  OD2 . ASP   A 242 ? 0.2294 0.1349 0.2249 0.0006  0.0353  -0.0434 243 ASP   A OD2 
2062 N  N   . ASN   A 243 ? 0.2110 0.1016 0.1344 -0.0053 0.0283  -0.0181 244 ASN   A N   
2063 C  CA  . ASN   A 243 ? 0.2016 0.0959 0.1458 -0.0042 0.0055  -0.0120 244 ASN   A CA  
2064 C  C   . ASN   A 243 ? 0.1657 0.1386 0.1304 -0.0162 0.0027  -0.0153 244 ASN   A C   
2065 O  O   . ASN   A 243 ? 0.1990 0.1318 0.1483 0.0089  0.0183  0.0012  244 ASN   A O   
2066 C  CB  . ASN   A 243 ? 0.2007 0.1585 0.1168 -0.0236 0.0095  -0.0017 244 ASN   A CB  
2067 C  CG  . ASN   A 243 ? 0.1975 0.1188 0.1445 -0.0251 0.0173  -0.0096 244 ASN   A CG  
2068 O  OD1 . ASN   A 243 ? 0.2070 0.1259 0.1705 -0.0124 0.0078  0.0140  244 ASN   A OD1 
2069 N  ND2 . ASN   A 243 ? 0.2412 0.1807 0.1720 -0.0400 -0.0149 0.0412  244 ASN   A ND2 
2070 N  N   . TRP   A 244 ? 0.1864 0.1243 0.1320 -0.0156 0.0026  -0.0150 245 TRP   A N   
2071 C  CA  . TRP   A 244 ? 0.1813 0.1156 0.1272 -0.0065 0.0017  -0.0185 245 TRP   A CA  
2072 C  C   . TRP   A 244 ? 0.1872 0.1353 0.1165 -0.0031 0.0096  -0.0048 245 TRP   A C   
2073 O  O   . TRP   A 244 ? 0.1794 0.1460 0.1562 0.0115  -0.0004 -0.0201 245 TRP   A O   
2074 C  CB  . TRP   A 244 ? 0.1951 0.0903 0.1362 -0.0015 0.0064  -0.0085 245 TRP   A CB  
2075 C  CG  . TRP   A 244 ? 0.1724 0.1187 0.1398 -0.0008 0.0156  -0.0032 245 TRP   A CG  
2076 C  CD1 . TRP   A 244 ? 0.1864 0.1091 0.1474 0.0022  0.0285  -0.0027 245 TRP   A CD1 
2077 C  CD2 . TRP   A 244 ? 0.1795 0.1056 0.1477 -0.0002 0.0109  -0.0011 245 TRP   A CD2 
2078 N  NE1 . TRP   A 244 ? 0.1807 0.1141 0.1518 -0.0061 0.0067  0.0003  245 TRP   A NE1 
2079 C  CE2 . TRP   A 244 ? 0.1881 0.1131 0.1527 0.0089  0.0108  0.0068  245 TRP   A CE2 
2080 C  CE3 . TRP   A 244 ? 0.1934 0.1382 0.1454 0.0108  0.0074  0.0027  245 TRP   A CE3 
2081 C  CZ2 . TRP   A 244 ? 0.2175 0.1093 0.1661 0.0127  0.0074  0.0121  245 TRP   A CZ2 
2082 C  CZ3 . TRP   A 244 ? 0.2149 0.1249 0.1941 0.0203  0.0147  0.0140  245 TRP   A CZ3 
2083 C  CH2 . TRP   A 244 ? 0.2089 0.1344 0.1722 0.0194  0.0076  0.0127  245 TRP   A CH2 
2084 N  N   . ARG   A 245 ? 0.1722 0.1247 0.1219 -0.0033 0.0005  -0.0147 246 ARG   A N   
2085 C  CA  . ARG   A 245 ? 0.1790 0.1150 0.1298 -0.0027 -0.0004 -0.0086 246 ARG   A CA  
2086 C  C   . ARG   A 245 ? 0.1780 0.1151 0.1418 0.0033  -0.0120 -0.0139 246 ARG   A C   
2087 O  O   . ARG   A 245 ? 0.1799 0.1342 0.1551 -0.0027 -0.0001 -0.0165 246 ARG   A O   
2088 C  CB  . ARG   A 245 ? 0.1709 0.1254 0.1388 -0.0054 -0.0032 -0.0253 246 ARG   A CB  
2089 C  CG  . ARG   A 245 ? 0.1610 0.1206 0.1544 0.0018  -0.0092 -0.0185 246 ARG   A CG  
2090 C  CD  . ARG   A 245 ? 0.1496 0.1287 0.1620 -0.0010 -0.0065 -0.0243 246 ARG   A CD  
2091 N  NE  . ARG   A 245 ? 0.1582 0.1502 0.1782 -0.0239 -0.0098 -0.0258 246 ARG   A NE  
2092 C  CZ  . ARG   A 245 ? 0.1647 0.1546 0.1474 -0.0288 -0.0046 -0.0212 246 ARG   A CZ  
2093 N  NH1 . ARG   A 245 ? 0.1835 0.1492 0.1746 -0.0266 0.0118  -0.0238 246 ARG   A NH1 
2094 N  NH2 . ARG   A 245 ? 0.1718 0.1647 0.1898 -0.0230 -0.0071 -0.0231 246 ARG   A NH2 
2095 N  N   . PRO   A 246 ? 0.1893 0.1282 0.1535 0.0122  0.0027  -0.0002 247 PRO   A N   
2096 C  CA  . PRO   A 246 ? 0.1958 0.1397 0.1406 0.0222  0.0035  0.0128  247 PRO   A CA  
2097 C  C   . PRO   A 246 ? 0.1780 0.1312 0.1453 0.0132  -0.0122 -0.0057 247 PRO   A C   
2098 O  O   . PRO   A 246 ? 0.1815 0.1254 0.1632 0.0044  -0.0113 -0.0024 247 PRO   A O   
2099 C  CB  . PRO   A 246 ? 0.2491 0.1954 0.1817 0.0721  -0.0019 -0.0132 247 PRO   A CB  
2100 C  CG  . PRO   A 246 ? 0.2547 0.2183 0.2728 0.0547  0.0392  0.0769  247 PRO   A CG  
2101 C  CD  . PRO   A 246 ? 0.1893 0.1694 0.1992 0.0413  0.0048  0.0038  247 PRO   A CD  
2102 N  N   . ALA   A 247 ? 0.1909 0.1398 0.1504 0.0154  0.0048  0.0006  248 ALA   A N   
2103 C  CA  . ALA   A 247 ? 0.1993 0.1421 0.1361 0.0037  -0.0035 -0.0054 248 ALA   A CA  
2104 C  C   . ALA   A 247 ? 0.1944 0.1316 0.1534 0.0178  -0.0121 0.0116  248 ALA   A C   
2105 O  O   . ALA   A 247 ? 0.2000 0.1679 0.1781 0.0424  -0.0193 0.0041  248 ALA   A O   
2106 C  CB  . ALA   A 247 ? 0.2319 0.1647 0.1647 -0.0073 0.0145  0.0171  248 ALA   A CB  
2107 N  N   . GLN   A 248 ? 0.1822 0.1306 0.1606 0.0078  -0.0175 0.0127  249 GLN   A N   
2108 C  CA  . GLN   A 248 ? 0.1908 0.1483 0.1553 0.0129  -0.0277 0.0093  249 GLN   A CA  
2109 C  C   . GLN   A 248 ? 0.2068 0.1382 0.1550 0.0315  -0.0304 0.0041  249 GLN   A C   
2110 O  O   . GLN   A 248 ? 0.2050 0.1566 0.1729 0.0174  -0.0136 0.0058  249 GLN   A O   
2111 C  CB  . GLN   A 248 ? 0.2063 0.1414 0.1720 0.0121  -0.0223 0.0049  249 GLN   A CB  
2112 C  CG  . GLN   A 248 ? 0.2037 0.1472 0.1703 -0.0034 -0.0085 -0.0118 249 GLN   A CG  
2113 C  CD  . GLN   A 248 ? 0.1879 0.1742 0.1851 -0.0141 -0.0063 -0.0006 249 GLN   A CD  
2114 O  OE1 . GLN   A 248 ? 0.1905 0.2470 0.2215 -0.0345 -0.0104 -0.0140 249 GLN   A OE1 
2115 N  NE2 . GLN   A 248 ? 0.2262 0.1879 0.1689 0.0050  -0.0050 0.0044  249 GLN   A NE2 
2116 N  N   . PRO   A 249 ? 0.1973 0.2085 0.1609 0.0536  -0.0368 -0.0173 250 PRO   A N   
2117 C  CA  . PRO   A 249 ? 0.2262 0.2600 0.1496 0.0798  -0.0345 -0.0155 250 PRO   A CA  
2118 C  C   . PRO   A 249 ? 0.2161 0.1752 0.1694 0.0407  -0.0366 0.0039  250 PRO   A C   
2119 O  O   . PRO   A 249 ? 0.2080 0.1925 0.1789 0.0340  -0.0287 0.0145  250 PRO   A O   
2120 C  CB  . PRO   A 249 ? 0.2407 0.3534 0.1993 0.0895  -0.0651 -0.0427 250 PRO   A CB  
2121 C  CG  . PRO   A 249 ? 0.2409 0.3991 0.1973 0.0392  -0.0638 -0.0528 250 PRO   A CG  
2122 C  CD  . PRO   A 249 ? 0.1773 0.3280 0.2154 0.0418  -0.0598 -0.0473 250 PRO   A CD  
2123 N  N   . LEU   A 250 ? 0.2449 0.1825 0.1540 0.0464  -0.0229 0.0067  251 LEU   A N   
2124 C  CA  . LEU   A 250 ? 0.2256 0.1676 0.1667 0.0159  -0.0030 0.0003  251 LEU   A CA  
2125 C  C   . LEU   A 250 ? 0.2121 0.1577 0.1615 0.0276  -0.0302 0.0127  251 LEU   A C   
2126 O  O   . LEU   A 250 ? 0.2151 0.1429 0.1763 0.0192  -0.0307 0.0020  251 LEU   A O   
2127 C  CB  . LEU   A 250 ? 0.2565 0.1945 0.1830 0.0103  0.0107  0.0131  251 LEU   A CB  
2128 C  CG  . LEU   A 250 ? 0.2606 0.2213 0.1544 -0.0089 0.0121  0.0111  251 LEU   A CG  
2129 C  CD1 . LEU   A 250 ? 0.2251 0.2355 0.1782 0.0115  -0.0223 -0.0209 251 LEU   A CD1 
2130 C  CD2 . LEU   A 250 ? 0.3581 0.2520 0.2002 -0.0779 0.0077  0.0165  251 LEU   A CD2 
2131 N  N   . LYS   A 251 ? 0.2522 0.2011 0.1348 0.0469  -0.0433 0.0122  252 LYS   A N   
2132 C  CA  . LYS   A 251 ? 0.2526 0.2398 0.1358 0.0441  -0.0268 -0.0209 252 LYS   A CA  
2133 C  C   . LYS   A 251 ? 0.2154 0.2100 0.1967 0.0283  -0.0336 -0.0174 252 LYS   A C   
2134 O  O   . LYS   A 251 ? 0.2746 0.2244 0.2040 0.0046  -0.0067 0.0040  252 LYS   A O   
2135 C  CB  . LYS   A 251 ? 0.2440 0.2707 0.1961 -0.0026 -0.0330 -0.0253 252 LYS   A CB  
2136 C  CG  . LYS   A 251 ? 0.2579 0.3128 0.2914 0.0036  0.0150  -0.0238 252 LYS   A CG  
2137 C  CD  . LYS   A 251 ? 0.2595 0.3321 0.2803 0.0109  0.0058  0.0018  252 LYS   A CD  
2138 C  CE  . LYS   A 251 ? 0.2251 0.3600 0.5111 0.0658  0.0410  0.0807  252 LYS   A CE  
2139 N  NZ  . LYS   A 251 ? 0.2774 0.3467 0.4397 0.0212  0.0256  0.0455  252 LYS   A NZ  
2140 N  N   . ASN   A 252 ? 0.2566 0.2065 0.1662 0.0326  -0.0567 -0.0350 253 ASN   A N   
2141 C  CA  . ASN   A 252 ? 0.2894 0.3872 0.2027 0.0499  -0.0567 -0.0793 253 ASN   A CA  
2142 C  C   . ASN   A 252 ? 0.3246 0.3130 0.2518 0.0941  -0.0718 -0.0547 253 ASN   A C   
2143 O  O   . ASN   A 252 ? 0.3496 0.3089 0.3895 0.0479  0.0025  0.0044  253 ASN   A O   
2144 C  CB  . ASN   A 252 ? 0.3392 0.3777 0.3496 0.0165  -0.0490 -0.1482 253 ASN   A CB  
2145 C  CG  . ASN   A 252 ? 0.4908 0.3856 0.3382 0.0774  -0.0281 -0.1346 253 ASN   A CG  
2146 O  OD1 . ASN   A 252 ? 0.7773 0.6485 0.3695 -0.0226 0.0998  -0.0590 253 ASN   A OD1 
2147 N  ND2 . ASN   A 252 ? 0.4109 0.3877 0.4330 0.0410  -0.0419 -0.1351 253 ASN   A ND2 
2148 N  N   . ARG   A 253 ? 0.2426 0.3549 0.1391 0.0365  -0.0219 0.0418  254 ARG   A N   
2149 C  CA  . ARG   A 253 ? 0.2142 0.2329 0.1307 0.0383  -0.0012 0.0092  254 ARG   A CA  
2150 C  C   . ARG   A 253 ? 0.2698 0.2127 0.1506 0.0414  0.0292  0.0052  254 ARG   A C   
2151 O  O   . ARG   A 253 ? 0.3292 0.2280 0.2645 0.0708  0.0784  0.0677  254 ARG   A O   
2152 C  CB  . ARG   A 253 ? 0.2297 0.1791 0.1143 0.0146  -0.0108 -0.0037 254 ARG   A CB  
2153 C  CG  . ARG   A 253 ? 0.2290 0.1750 0.1317 -0.0011 -0.0201 -0.0064 254 ARG   A CG  
2154 C  CD  . ARG   A 253 ? 0.2145 0.1470 0.1383 0.0139  -0.0166 -0.0262 254 ARG   A CD  
2155 N  NE  . ARG   A 253 ? 0.1958 0.1434 0.1446 0.0210  -0.0185 -0.0009 254 ARG   A NE  
2156 C  CZ  . ARG   A 253 ? 0.1757 0.1451 0.1194 -0.0029 -0.0217 0.0011  254 ARG   A CZ  
2157 N  NH1 . ARG   A 253 ? 0.1577 0.1599 0.1344 -0.0022 -0.0182 0.0067  254 ARG   A NH1 
2158 N  NH2 . ARG   A 253 ? 0.1685 0.1432 0.1454 0.0144  -0.0234 -0.0047 254 ARG   A NH2 
2159 N  N   . GLN   A 254 ? 0.2262 0.2480 0.1532 0.0178  -0.0132 -0.0443 255 GLN   A N   
2160 C  CA  A GLN   A 254 ? 0.2448 0.3182 0.1453 -0.0105 -0.0162 -0.0477 255 GLN   A CA  
2161 C  CA  B GLN   A 254 ? 0.2533 0.2897 0.1567 -0.0042 -0.0278 -0.0181 255 GLN   A CA  
2162 C  C   . GLN   A 254 ? 0.2401 0.1806 0.1763 -0.0021 -0.0381 0.0008  255 GLN   A C   
2163 O  O   . GLN   A 254 ? 0.3284 0.1787 0.3018 0.0115  -0.1036 -0.0108 255 GLN   A O   
2164 C  CB  A GLN   A 254 ? 0.3102 0.3925 0.1850 -0.0611 0.0097  -0.1355 255 GLN   A CB  
2165 C  CB  B GLN   A 254 ? 0.2816 0.2953 0.1639 -0.0178 -0.0110 -0.0198 255 GLN   A CB  
2166 C  CG  A GLN   A 254 ? 0.3133 0.4861 0.2993 -0.0934 0.0662  -0.1512 255 GLN   A CG  
2167 C  CG  B GLN   A 254 ? 0.3421 0.2236 0.1527 -0.0449 -0.0219 -0.0103 255 GLN   A CG  
2168 C  CD  A GLN   A 254 ? 0.6735 0.4795 0.2756 -0.2301 0.0375  -0.1920 255 GLN   A CD  
2169 C  CD  B GLN   A 254 ? 0.4935 0.3096 0.1661 -0.0084 0.0161  -0.0203 255 GLN   A CD  
2170 O  OE1 A GLN   A 254 ? 0.7671 0.3697 0.2146 -0.1813 0.1151  -0.0277 255 GLN   A OE1 
2171 O  OE1 B GLN   A 254 ? 0.5682 0.2779 0.4610 0.0484  0.1066  -0.0177 255 GLN   A OE1 
2172 N  NE2 A GLN   A 254 ? 0.5989 0.4910 0.5149 -0.1238 0.0428  -0.2883 255 GLN   A NE2 
2173 N  NE2 B GLN   A 254 ? 0.4703 0.2370 0.1922 0.0172  -0.0033 -0.0588 255 GLN   A NE2 
2174 N  N   . ILE   A 255 ? 0.2240 0.1707 0.1355 0.0038  -0.0194 -0.0032 256 ILE   A N   
2175 C  CA  . ILE   A 255 ? 0.2046 0.1697 0.1409 0.0044  -0.0119 -0.0015 256 ILE   A CA  
2176 C  C   . ILE   A 255 ? 0.2065 0.1706 0.1561 0.0060  0.0115  0.0245  256 ILE   A C   
2177 O  O   . ILE   A 255 ? 0.2377 0.1770 0.1775 0.0189  0.0098  0.0461  256 ILE   A O   
2178 C  CB  . ILE   A 255 ? 0.2054 0.1676 0.1364 0.0184  -0.0184 -0.0055 256 ILE   A CB  
2179 C  CG1 . ILE   A 255 ? 0.2233 0.1586 0.1813 0.0156  -0.0012 -0.0058 256 ILE   A CG1 
2180 C  CG2 . ILE   A 255 ? 0.2332 0.1826 0.1529 -0.0049 -0.0219 0.0006  256 ILE   A CG2 
2181 C  CD1 . ILE   A 255 ? 0.2524 0.1779 0.2034 -0.0057 0.0085  -0.0298 256 ILE   A CD1 
2182 N  N   . LYS   A 256 ? 0.1888 0.1661 0.1461 -0.0008 -0.0057 0.0125  257 LYS   A N   
2183 C  CA  . LYS   A 256 ? 0.2037 0.1720 0.1351 0.0055  0.0051  0.0254  257 LYS   A CA  
2184 C  C   . LYS   A 256 ? 0.2037 0.1923 0.1194 0.0104  -0.0074 0.0125  257 LYS   A C   
2185 O  O   . LYS   A 256 ? 0.2298 0.2343 0.1192 -0.0368 0.0047  0.0141  257 LYS   A O   
2186 C  CB  . LYS   A 256 ? 0.2328 0.2009 0.1614 0.0196  0.0013  -0.0183 257 LYS   A CB  
2187 C  CG  . LYS   A 256 ? 0.3391 0.2188 0.2333 -0.0183 0.0000  -0.0677 257 LYS   A CG  
2188 C  CD  . LYS   A 256 ? 0.3968 0.2791 0.3841 0.0305  -0.0308 -0.1083 257 LYS   A CD  
2189 C  CE  . LYS   A 256 ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  257 LYS   A CE  
2190 N  NZ  . LYS   A 256 ? 0.1266 0.1266 0.1266 0.0000  0.0000  0.0000  257 LYS   A NZ  
2191 N  N   . ALA   A 257 ? 0.2014 0.1979 0.1377 -0.0001 0.0154  0.0136  258 ALA   A N   
2192 C  CA  . ALA   A 257 ? 0.1921 0.1949 0.1710 0.0052  -0.0017 0.0149  258 ALA   A CA  
2193 C  C   . ALA   A 257 ? 0.2016 0.1811 0.1330 -0.0038 0.0168  0.0100  258 ALA   A C   
2194 O  O   . ALA   A 257 ? 0.2284 0.2200 0.1406 0.0027  0.0256  0.0051  258 ALA   A O   
2195 C  CB  . ALA   A 257 ? 0.2253 0.1811 0.2050 -0.0217 0.0172  -0.0063 258 ALA   A CB  
2196 N  N   . SER   A 258 ? 0.1934 0.1824 0.1591 -0.0009 0.0050  0.0149  259 SER   A N   
2197 C  CA  . SER   A 258 ? 0.1949 0.1889 0.1962 0.0006  0.0043  0.0233  259 SER   A CA  
2198 C  C   . SER   A 258 ? 0.2037 0.1997 0.1846 -0.0008 0.0266  0.0026  259 SER   A C   
2199 O  O   . SER   A 258 ? 0.2083 0.3063 0.2590 0.0285  0.0411  0.0249  259 SER   A O   
2200 C  CB  . SER   A 258 ? 0.2243 0.1882 0.1955 0.0032  -0.0275 0.0158  259 SER   A CB  
2201 O  OG  . SER   A 258 ? 0.2026 0.2291 0.1735 -0.0100 0.0072  -0.0151 259 SER   A OG  
2202 N  N   . PHE   A 259 ? 0.2185 0.1952 0.1937 -0.0201 0.0400  0.0050  260 PHE   A N   
2203 C  CA  . PHE   A 259 ? 0.2440 0.2041 0.2504 -0.0359 0.0560  0.0149  260 PHE   A CA  
2204 C  C   . PHE   A 259 ? 0.2766 0.2441 0.2537 -0.0614 0.0866  0.0474  260 PHE   A C   
2205 O  O   . PHE   A 259 ? 0.2866 0.2438 0.2438 -0.0129 0.0268  0.0421  260 PHE   A O   
2206 C  CB  . PHE   A 259 ? 0.2300 0.2222 0.2778 -0.0247 0.0326  -0.0155 260 PHE   A CB  
2207 C  CG  . PHE   A 259 ? 0.2157 0.2228 0.2278 -0.0168 0.0182  0.0147  260 PHE   A CG  
2208 C  CD1 . PHE   A 259 ? 0.2096 0.2136 0.1839 -0.0245 0.0027  -0.0062 260 PHE   A CD1 
2209 C  CD2 . PHE   A 259 ? 0.2817 0.2303 0.2996 0.0041  0.0121  0.0115  260 PHE   A CD2 
2210 C  CE1 . PHE   A 259 ? 0.2264 0.2080 0.2116 -0.0290 0.0140  -0.0040 260 PHE   A CE1 
2211 C  CE2 . PHE   A 259 ? 0.3034 0.1993 0.3363 0.0190  0.0446  0.0456  260 PHE   A CE2 
2212 C  CZ  . PHE   A 259 ? 0.2820 0.1997 0.3334 -0.0179 0.0303  -0.0199 260 PHE   A CZ  
2213 ZN ZN  . ZN    B .   ? 0.1781 0.0987 0.1240 -0.0065 -0.0110 -0.0027 301 ZN    A ZN  
2214 S  S   . DMS   C .   ? 0.2685 0.2085 0.2329 -0.0111 0.0098  -0.0291 302 DMS   A S   
2215 O  O   . DMS   C .   ? 0.2867 0.2369 0.3896 -0.0342 0.0151  -0.0511 302 DMS   A O   
2216 C  C1  . DMS   C .   ? 0.2384 0.2102 0.2218 0.0207  0.0260  0.0099  302 DMS   A C1  
2217 C  C2  . DMS   C .   ? 0.3472 0.1943 0.2087 -0.0036 0.0396  -0.0735 302 DMS   A C2  
2218 C  C2  . A1IDL D .   ? 0.1991 0.1050 0.1461 -0.0111 -0.0196 0.0034  303 A1IDL A C2  
2219 C  C3  . A1IDL D .   ? 0.2165 0.1081 0.1881 -0.0096 0.0104  0.0076  303 A1IDL A C3  
2220 C  C4  . A1IDL D .   ? 0.2239 0.1083 0.2062 -0.0058 -0.0073 0.0166  303 A1IDL A C4  
2221 C  C5  . A1IDL D .   ? 0.2140 0.1381 0.2192 -0.0105 0.0190  0.0383  303 A1IDL A C5  
2222 C  C6  . A1IDL D .   ? 0.2448 0.1264 0.1754 -0.0209 0.0058  0.0245  303 A1IDL A C6  
2223 O  O9  . A1IDL D .   ? 0.1874 0.1034 0.1500 -0.0151 -0.0221 -0.0061 303 A1IDL A O9  
2224 C  C16 . A1IDL D .   ? 0.4989 0.2699 0.2370 0.0229  0.0512  0.0753  303 A1IDL A C16 
2225 C  C17 . A1IDL D .   ? 0.4999 0.2606 0.3128 0.0114  0.0785  0.1229  303 A1IDL A C17 
2226 C  C19 . A1IDL D .   ? 0.2891 0.2581 0.2340 0.0038  0.0021  0.0041  303 A1IDL A C19 
2227 C  C21 . A1IDL D .   ? 0.3526 0.4689 0.2330 0.0735  0.0097  -0.0783 303 A1IDL A C21 
2228 C  C24 . A1IDL D .   ? 0.2638 0.2619 0.1817 -0.0274 0.0118  -0.0520 303 A1IDL A C24 
2229 O  O26 . A1IDL D .   ? 0.3895 0.2732 0.3161 0.0354  -0.0364 0.1043  303 A1IDL A O26 
2230 S  S15 . A1IDL D .   ? 0.3546 0.1829 0.2537 -0.0078 0.0264  0.0597  303 A1IDL A S15 
2231 O  O25 . A1IDL D .   ? 0.3386 0.1593 0.3488 -0.0372 0.0708  0.0314  303 A1IDL A O25 
2232 F  F13 . A1IDL D .   ? 0.2329 0.1142 0.2789 0.0062  0.0257  0.0198  303 A1IDL A F13 
2233 F  F12 . A1IDL D .   ? 0.2188 0.1047 0.1979 -0.0077 0.0032  -0.0164 303 A1IDL A F12 
2234 S  S7  . A1IDL D .   ? 0.1796 0.1041 0.1421 -0.0060 -0.0182 -0.0084 303 A1IDL A S7  
2235 N  N10 . A1IDL D .   ? 0.1816 0.0796 0.1488 -0.0294 -0.0174 -0.0064 303 A1IDL A N10 
2236 O  O8  . A1IDL D .   ? 0.1870 0.1120 0.1412 0.0072  -0.0108 -0.0140 303 A1IDL A O8  
2237 N  N14 . A1IDL D .   ? 0.2572 0.2037 0.1734 0.0031  0.0190  0.0335  303 A1IDL A N14 
2238 C  C1  . A1IDL D .   ? 0.2183 0.1077 0.1621 -0.0088 -0.0083 0.0173  303 A1IDL A C1  
2239 F  F11 . A1IDL D .   ? 0.2193 0.1330 0.1653 -0.0050 0.0065  -0.0067 303 A1IDL A F11 
2240 C  C18 . A1IDL D .   ? 0.3039 0.2420 0.2644 -0.0059 -0.0429 0.0049  303 A1IDL A C18 
2241 C  C20 . A1IDL D .   ? 0.3799 0.3195 0.2419 0.0432  -0.0476 -0.0770 303 A1IDL A C20 
2242 C  C22 . A1IDL D .   ? 0.3119 0.5139 0.2953 0.0431  -0.0336 0.0102  303 A1IDL A C22 
2243 C  C23 . A1IDL D .   ? 0.2961 0.3804 0.2493 -0.0286 -0.0293 0.0345  303 A1IDL A C23 
2244 O  O   . HOH   E .   ? 0.5122 0.8308 0.5842 -0.1544 0.0548  0.3049  401 HOH   A O   
2245 O  O   . HOH   E .   ? 0.3552 0.2709 0.4914 -0.0398 0.0247  -0.0524 402 HOH   A O   
2246 O  O   . HOH   E .   ? 0.2797 0.1192 0.2207 -0.0084 -0.0387 0.0063  403 HOH   A O   
2247 O  O   . HOH   E .   ? 0.3619 0.3682 0.2904 0.0144  0.0136  0.0431  404 HOH   A O   
2248 O  O   . HOH   E .   ? 0.5166 0.2728 0.3359 0.0744  0.0776  0.0573  405 HOH   A O   
2249 O  O   . HOH   E .   ? 0.6594 0.5122 0.4280 -0.3355 0.2570  -0.2689 406 HOH   A O   
2250 O  O   . HOH   E .   ? 0.6948 0.4164 0.5094 -0.0016 -0.3459 -0.1657 407 HOH   A O   
2251 O  O   . HOH   E .   ? 0.6660 0.3205 0.2617 -0.0228 -0.0379 -0.1026 408 HOH   A O   
2252 O  O   . HOH   E .   ? 0.8725 0.2997 0.4630 0.2488  -0.0982 -0.0652 409 HOH   A O   
2253 O  O   . HOH   E .   ? 0.4009 0.4199 0.3623 -0.1274 -0.0207 0.0430  410 HOH   A O   
2254 O  O   . HOH   E .   ? 0.7128 0.3447 1.0077 -0.0342 0.0604  -0.0308 411 HOH   A O   
2255 O  O   . HOH   E .   ? 0.3893 0.3725 0.3271 -0.0762 0.0163  0.0675  412 HOH   A O   
2256 O  O   . HOH   E .   ? 0.5011 0.2039 0.5754 -0.0796 0.0502  0.0362  413 HOH   A O   
2257 O  O   . HOH   E .   ? 0.4671 0.3049 0.7526 0.0244  0.0778  -0.1869 414 HOH   A O   
2258 O  O   . HOH   E .   ? 0.6069 0.2566 0.4869 0.0093  0.1241  0.0523  415 HOH   A O   
2259 O  O   . HOH   E .   ? 0.4181 0.4159 0.5588 0.1693  -0.1940 -0.0905 416 HOH   A O   
2260 O  O   . HOH   E .   ? 0.2796 0.1868 0.1634 -0.0289 -0.0229 0.0077  417 HOH   A O   
2261 O  O   . HOH   E .   ? 0.5042 0.6359 0.4289 -0.0241 -0.0794 0.1218  418 HOH   A O   
2262 O  O   . HOH   E .   ? 0.9051 0.2567 0.2727 0.0281  0.0583  0.0516  419 HOH   A O   
2263 O  O   . HOH   E .   ? 0.7475 0.4118 0.2778 -0.2531 0.0500  -0.1156 420 HOH   A O   
2264 O  O   . HOH   E .   ? 0.5549 0.3953 0.3198 -0.0401 -0.0773 0.0020  421 HOH   A O   
2265 O  O   . HOH   E .   ? 0.4607 0.4269 0.3820 -0.1481 0.0431  0.0306  422 HOH   A O   
2266 O  O   . HOH   E .   ? 0.5017 0.5227 0.3757 -0.0472 0.0004  0.1429  423 HOH   A O   
2267 O  O   . HOH   E .   ? 0.3428 0.4919 0.3027 -0.1043 0.0302  0.0588  424 HOH   A O   
2268 O  O   . HOH   E .   ? 0.2814 0.8941 0.7101 0.0636  -0.0820 -0.1085 425 HOH   A O   
2269 O  O   . HOH   E .   ? 0.3466 0.3334 0.3602 -0.0998 0.1099  -0.1321 426 HOH   A O   
2270 O  O   . HOH   E .   ? 0.4263 0.2167 0.4673 -0.0122 0.0429  0.0004  427 HOH   A O   
2271 O  O   . HOH   E .   ? 0.3224 0.2080 0.2266 -0.0346 -0.0043 -0.0270 428 HOH   A O   
2272 O  O   . HOH   E .   ? 0.3999 0.2116 0.3450 -0.0828 0.0291  -0.0405 429 HOH   A O   
2273 O  O   . HOH   E .   ? 0.3687 1.0390 0.4153 0.0731  -0.0283 -0.3956 430 HOH   A O   
2274 O  O   . HOH   E .   ? 0.3426 0.2564 0.2965 0.0589  -0.1198 -0.0420 431 HOH   A O   
2275 O  O   . HOH   E .   ? 0.4719 0.3655 0.2623 -0.1492 0.1241  -0.0932 432 HOH   A O   
2276 O  O   . HOH   E .   ? 0.3517 0.1808 0.3483 0.0070  0.0281  -0.0126 433 HOH   A O   
2277 O  O   . HOH   E .   ? 0.5772 0.2384 0.3029 -0.0908 0.0477  -0.0709 434 HOH   A O   
2278 O  O   . HOH   E .   ? 0.2030 0.1533 0.1488 -0.0109 0.0075  -0.0086 435 HOH   A O   
2279 O  O   . HOH   E .   ? 0.3913 0.7027 0.3289 0.1424  -0.0461 0.1203  436 HOH   A O   
2280 O  O   . HOH   E .   ? 0.6141 0.3890 0.1786 0.0027  0.0142  -0.0176 437 HOH   A O   
2281 O  O   . HOH   E .   ? 0.5057 0.3784 0.5937 0.0682  0.0552  0.1636  438 HOH   A O   
2282 O  O   . HOH   E .   ? 0.3100 0.2046 0.3302 0.0087  -0.1344 -0.0547 439 HOH   A O   
2283 O  O   . HOH   E .   ? 0.4198 0.1613 0.2330 0.0097  -0.1254 0.0197  440 HOH   A O   
2284 O  O   . HOH   E .   ? 0.4128 0.3440 0.2273 -0.0370 -0.0998 0.0102  441 HOH   A O   
2285 O  O   . HOH   E .   ? 0.3662 0.3385 0.4424 0.0087  0.1407  0.0854  442 HOH   A O   
2286 O  O   . HOH   E .   ? 0.2256 0.1213 0.1762 -0.0156 0.0033  -0.0151 443 HOH   A O   
2287 O  O   . HOH   E .   ? 0.3770 0.4504 0.2102 -0.1384 -0.1076 0.0447  444 HOH   A O   
2288 O  O   . HOH   E .   ? 0.4564 0.2670 0.4279 -0.0582 0.1350  -0.1036 445 HOH   A O   
2289 O  O   . HOH   E .   ? 0.5171 0.3280 0.4521 -0.0516 -0.1474 0.0389  446 HOH   A O   
2290 O  O   . HOH   E .   ? 0.3648 0.2382 0.2823 -0.0803 -0.0419 -0.0174 447 HOH   A O   
2291 O  O   . HOH   E .   ? 0.3660 0.8758 0.6251 -0.1568 0.1454  -0.3251 448 HOH   A O   
2292 O  O   . HOH   E .   ? 0.3448 0.1333 0.2813 -0.0385 0.0510  -0.0097 449 HOH   A O   
2293 O  O   . HOH   E .   ? 0.3693 0.5326 0.5903 0.1631  0.1630  0.2761  450 HOH   A O   
2294 O  O   . HOH   E .   ? 0.3360 0.2788 0.3431 0.0076  -0.0336 0.0388  451 HOH   A O   
2295 O  O   . HOH   E .   ? 0.7171 0.2436 0.1583 -0.0181 -0.0102 -0.0052 452 HOH   A O   
2296 O  O   . HOH   E .   ? 0.5775 0.4000 0.3468 -0.0098 0.1674  0.0154  453 HOH   A O   
2297 O  O   . HOH   E .   ? 0.4087 0.3917 0.4204 0.0565  0.1318  -0.0675 454 HOH   A O   
2298 O  O   . HOH   E .   ? 0.6208 0.3219 1.2330 -0.1201 0.0430  -0.2310 455 HOH   A O   
2299 O  O   . HOH   E .   ? 0.5080 0.3182 0.2920 0.0458  0.0594  0.0695  456 HOH   A O   
2300 O  O   . HOH   E .   ? 0.2574 0.3119 0.4686 0.0761  -0.0384 -0.0022 457 HOH   A O   
2301 O  O   . HOH   E .   ? 0.7239 0.2069 0.6474 -0.0727 -0.2622 -0.0425 458 HOH   A O   
2302 O  O   . HOH   E .   ? 0.3072 0.4152 0.5838 0.0066  -0.0038 0.1370  459 HOH   A O   
2303 O  O   . HOH   E .   ? 0.4642 0.4052 0.5753 0.1587  0.2095  0.1355  460 HOH   A O   
2304 O  O   . HOH   E .   ? 0.3657 0.9448 0.5252 -0.1453 -0.0211 0.3378  461 HOH   A O   
2305 O  O   . HOH   E .   ? 0.5751 0.3727 0.9544 0.1967  -0.3019 -0.1620 462 HOH   A O   
2306 O  O   . HOH   E .   ? 0.6943 0.3388 0.5144 -0.1151 -0.2980 0.1087  463 HOH   A O   
2307 O  O   . HOH   E .   ? 0.4021 0.2792 0.4173 -0.0403 -0.0800 0.1562  464 HOH   A O   
2308 O  O   . HOH   E .   ? 1.2130 0.5340 0.4388 0.1415  0.2615  0.0143  465 HOH   A O   
2309 O  O   . HOH   E .   ? 0.4557 0.4251 0.3356 -0.0354 -0.0025 0.1242  466 HOH   A O   
2310 O  O   . HOH   E .   ? 0.4663 0.3409 0.4248 -0.0250 0.0089  0.1647  467 HOH   A O   
2311 O  O   . HOH   E .   ? 0.3233 0.2883 0.2735 0.0669  0.0156  -0.0048 468 HOH   A O   
2312 O  O   . HOH   E .   ? 0.2226 0.1339 0.1930 -0.0088 0.0270  -0.0243 469 HOH   A O   
2313 O  O   . HOH   E .   ? 0.4541 0.2985 0.8948 -0.0744 0.0586  0.2043  470 HOH   A O   
2314 O  O   . HOH   E .   ? 0.4192 0.3545 0.4193 0.1253  -0.2024 -0.2200 471 HOH   A O   
2315 O  O   . HOH   E .   ? 0.2936 0.7384 0.4810 -0.0981 0.0982  0.0815  472 HOH   A O   
2316 O  O   . HOH   E .   ? 0.2600 0.2927 0.2276 0.0206  0.0051  0.0330  473 HOH   A O   
2317 O  O   . HOH   E .   ? 0.2949 0.3085 0.2258 -0.0221 0.0593  -0.0414 474 HOH   A O   
2318 O  O   . HOH   E .   ? 0.4007 0.3318 0.4848 0.0145  -0.0397 -0.1602 475 HOH   A O   
2319 O  O   . HOH   E .   ? 0.4405 0.1982 0.2556 -0.0170 0.0460  0.0769  476 HOH   A O   
2320 O  O   . HOH   E .   ? 0.5028 0.5739 0.5307 0.0078  0.0950  -0.1996 477 HOH   A O   
2321 O  O   . HOH   E .   ? 0.3761 0.3143 0.4915 -0.1210 -0.1284 0.1320  478 HOH   A O   
2322 O  O   . HOH   E .   ? 0.5811 0.3617 0.2452 -0.1585 0.0127  -0.0746 479 HOH   A O   
2323 O  O   . HOH   E .   ? 0.7070 0.5545 0.6286 0.2588  0.1801  0.2241  480 HOH   A O   
2324 O  O   . HOH   E .   ? 0.3037 0.2819 0.2789 0.0132  0.0445  -0.0291 481 HOH   A O   
2325 O  O   . HOH   E .   ? 0.3462 0.2351 0.2006 -0.0351 0.0527  0.0284  482 HOH   A O   
2326 O  O   . HOH   E .   ? 0.5046 1.1081 0.7647 -0.1648 0.2074  -0.1411 483 HOH   A O   
2327 O  O   . HOH   E .   ? 0.4450 0.4245 0.7179 -0.0396 -0.2887 0.1512  484 HOH   A O   
2328 O  O   . HOH   E .   ? 0.2127 0.1825 0.1969 0.0088  -0.0507 0.0187  485 HOH   A O   
2329 O  O   . HOH   E .   ? 0.2763 0.1534 0.2662 0.0357  -0.0076 0.0145  486 HOH   A O   
2330 O  O   . HOH   E .   ? 0.7134 0.3799 0.5360 -0.2036 0.1024  -0.0626 487 HOH   A O   
2331 O  O   . HOH   E .   ? 0.2037 0.1786 0.2801 -0.0093 0.0062  0.0121  488 HOH   A O   
2332 O  O   . HOH   E .   ? 0.2017 0.1165 0.1679 0.0153  -0.0046 -0.0067 489 HOH   A O   
2333 O  O   . HOH   E .   ? 0.4272 0.2523 0.2664 -0.0348 -0.0685 0.0008  490 HOH   A O   
2334 O  O   . HOH   E .   ? 0.5962 0.5796 0.2912 -0.2207 -0.0655 -0.0631 491 HOH   A O   
2335 O  O   . HOH   E .   ? 0.4683 0.1605 0.4087 -0.0301 0.0304  -0.0214 492 HOH   A O   
2336 O  O   . HOH   E .   ? 0.5324 0.3917 0.2718 -0.1454 -0.1175 0.0047  493 HOH   A O   
2337 O  O   . HOH   E .   ? 0.3777 0.1995 0.4461 -0.0354 -0.1051 0.0220  494 HOH   A O   
2338 O  O   . HOH   E .   ? 0.5606 0.3260 0.3206 -0.0022 0.0577  -0.0913 495 HOH   A O   
2339 O  O   . HOH   E .   ? 0.5638 0.2558 0.4091 0.1747  -0.1561 -0.0559 496 HOH   A O   
2340 O  O   . HOH   E .   ? 0.4478 0.4264 0.5233 -0.2675 -0.0708 0.1057  497 HOH   A O   
2341 O  O   . HOH   E .   ? 0.5241 0.3145 0.2479 -0.0414 0.1038  -0.0885 498 HOH   A O   
2342 O  O   . HOH   E .   ? 0.2063 0.1379 0.1632 0.0227  -0.0107 0.0047  499 HOH   A O   
2343 O  O   . HOH   E .   ? 0.3283 0.2470 0.3389 0.0220  0.0099  0.0859  500 HOH   A O   
2344 O  O   . HOH   E .   ? 0.2588 0.4099 0.2580 0.0610  -0.0049 0.1049  501 HOH   A O   
2345 O  O   . HOH   E .   ? 0.1710 0.1597 0.2605 -0.0037 -0.0064 -0.0368 502 HOH   A O   
2346 O  O   . HOH   E .   ? 0.2741 0.3564 0.2283 -0.0119 -0.0197 -0.0569 503 HOH   A O   
2347 O  O   . HOH   E .   ? 0.3031 0.3271 1.0680 0.0619  -0.1085 0.1390  504 HOH   A O   
2348 O  O   . HOH   E .   ? 0.3384 0.4745 0.4270 -0.0839 -0.0644 0.0518  505 HOH   A O   
2349 O  O   . HOH   E .   ? 0.3970 0.3713 0.4543 -0.0508 0.0651  0.1377  506 HOH   A O   
2350 O  O   . HOH   E .   ? 0.2524 0.1779 0.3640 -0.0453 -0.0697 0.0163  507 HOH   A O   
2351 O  O   . HOH   E .   ? 0.2825 0.1477 0.2509 -0.0445 -0.0208 -0.0076 508 HOH   A O   
2352 O  O   . HOH   E .   ? 0.1859 0.1240 0.1602 0.0023  0.0152  0.0077  509 HOH   A O   
2353 O  O   . HOH   E .   ? 0.5213 0.3871 0.3102 -0.0332 0.1332  -0.0458 510 HOH   A O   
2354 O  O   . HOH   E .   ? 0.3203 0.2867 0.5903 -0.0391 0.0309  -0.1033 511 HOH   A O   
2355 O  O   . HOH   E .   ? 0.6001 0.4353 0.4304 -0.0079 -0.0559 0.2986  512 HOH   A O   
2356 O  O   . HOH   E .   ? 0.2922 0.1690 0.3949 0.0054  0.0403  -0.0520 513 HOH   A O   
2357 O  O   . HOH   E .   ? 0.3304 0.2468 0.2746 0.0171  -0.0942 -0.0168 514 HOH   A O   
2358 O  O   . HOH   E .   ? 0.4559 0.3638 0.9120 -0.0416 -0.0392 0.0311  515 HOH   A O   
2359 O  O   . HOH   E .   ? 0.3678 0.2017 0.2171 -0.0287 -0.0987 0.0363  516 HOH   A O   
2360 O  O   . HOH   E .   ? 0.5583 0.6840 0.2863 -0.0133 0.1062  0.1591  517 HOH   A O   
2361 O  O   . HOH   E .   ? 0.7172 0.4847 0.4840 -0.2296 0.0405  0.0757  518 HOH   A O   
2362 O  O   . HOH   E .   ? 0.2088 0.1463 0.2172 0.0192  -0.0155 0.0222  519 HOH   A O   
2363 O  O   . HOH   E .   ? 0.3590 0.2149 0.3783 0.0352  -0.0980 -0.0638 520 HOH   A O   
2364 O  O   . HOH   E .   ? 0.3373 0.2456 0.4541 0.0922  -0.0835 -0.1119 521 HOH   A O   
2365 O  O   . HOH   E .   ? 0.3459 0.1713 0.3166 -0.0243 -0.0436 0.0366  522 HOH   A O   
2366 O  O   . HOH   E .   ? 0.2182 0.3320 0.3456 -0.0207 -0.0318 0.0273  523 HOH   A O   
2367 O  O   . HOH   E .   ? 0.3088 0.2958 0.2957 -0.0103 -0.0243 0.0346  524 HOH   A O   
2368 O  O   . HOH   E .   ? 0.3370 0.5090 0.3431 -0.1567 -0.0625 -0.0215 525 HOH   A O   
2369 O  O   . HOH   E .   ? 0.2573 0.2325 0.2950 0.0471  -0.0370 0.0034  526 HOH   A O   
2370 O  O   . HOH   E .   ? 0.3733 0.4362 0.3599 0.0494  -0.0252 0.1023  527 HOH   A O   
2371 O  O   . HOH   E .   ? 0.4200 0.4187 0.8619 -0.1241 0.2764  -0.2346 528 HOH   A O   
2372 O  O   . HOH   E .   ? 0.9858 0.3395 0.4619 -0.2107 0.0425  0.0969  529 HOH   A O   
2373 O  O   . HOH   E .   ? 0.2720 0.7434 0.3867 0.0069  -0.0190 -0.2055 530 HOH   A O   
2374 O  O   . HOH   E .   ? 0.5295 0.5274 0.9179 0.2532  0.0741  0.0158  531 HOH   A O   
2375 O  O   . HOH   E .   ? 0.5306 0.4494 0.2622 -0.0430 -0.1813 0.1076  532 HOH   A O   
2376 O  O   . HOH   E .   ? 0.2810 0.2481 0.2031 -0.0073 -0.0036 -0.0081 533 HOH   A O   
2377 O  O   . HOH   E .   ? 0.2762 0.2240 0.3296 -0.0378 0.0237  -0.0174 534 HOH   A O   
2378 O  O   . HOH   E .   ? 0.7095 0.3744 0.4565 0.0840  0.0266  -0.0879 535 HOH   A O   
2379 O  O   . HOH   E .   ? 0.3291 0.2246 0.2458 0.0130  -0.0408 0.0079  536 HOH   A O   
2380 O  O   . HOH   E .   ? 0.8558 0.4208 0.4401 0.2533  0.3055  0.2362  537 HOH   A O   
2381 O  O   . HOH   E .   ? 0.3868 0.2563 0.7217 -0.0075 0.0665  -0.1518 538 HOH   A O   
2382 O  O   . HOH   E .   ? 0.3004 0.4741 0.2999 -0.0509 -0.0019 -0.0606 539 HOH   A O   
2383 O  O   . HOH   E .   ? 0.3149 0.1992 0.4079 -0.0089 -0.0451 -0.0413 540 HOH   A O   
2384 O  O   . HOH   E .   ? 0.2601 0.1687 0.2678 0.0001  -0.0618 0.0136  541 HOH   A O   
2385 O  O   . HOH   E .   ? 0.5062 0.4711 0.5838 -0.0615 -0.1055 0.2306  542 HOH   A O   
2386 O  O   . HOH   E .   ? 0.1653 0.2427 0.2545 0.0172  0.0074  -0.0412 543 HOH   A O   
2387 O  O   . HOH   E .   ? 0.2401 0.1854 0.2872 0.0030  -0.0131 -0.0114 544 HOH   A O   
2388 O  O   . HOH   E .   ? 0.3912 0.1546 0.3438 0.0190  -0.1002 0.0225  545 HOH   A O   
2389 O  O   . HOH   E .   ? 1.0520 0.3626 0.5771 0.0575  -0.2328 0.0255  546 HOH   A O   
2390 O  O   . HOH   E .   ? 0.2530 0.2653 0.4087 0.0710  0.0440  0.0163  547 HOH   A O   
2391 O  O   . HOH   E .   ? 0.3344 0.2731 0.3872 0.0217  -0.0089 -0.0381 548 HOH   A O   
2392 O  O   . HOH   E .   ? 0.3185 1.0256 0.4447 0.1174  0.0365  -0.0218 549 HOH   A O   
2393 O  O   . HOH   E .   ? 0.3500 0.2212 0.2890 0.0212  0.0302  0.1106  550 HOH   A O   
2394 O  O   . HOH   E .   ? 0.7269 0.3583 0.4809 -0.2463 -0.3153 0.0696  551 HOH   A O   
2395 O  O   . HOH   E .   ? 1.1751 0.4411 0.4062 0.0996  0.0563  -0.1551 552 HOH   A O   
2396 O  O   . HOH   E .   ? 0.2999 0.2020 0.3405 -0.0986 -0.0515 -0.0408 553 HOH   A O   
2397 O  O   . HOH   E .   ? 0.4157 0.2519 0.3403 -0.0394 0.0289  -0.0140 554 HOH   A O   
2398 O  O   . HOH   E .   ? 0.6812 0.5723 0.5393 -0.1872 0.0498  0.3092  555 HOH   A O   
2399 O  O   . HOH   E .   ? 0.2330 0.3840 0.4313 0.0364  -0.0366 0.0693  556 HOH   A O   
2400 O  O   . HOH   E .   ? 0.8499 0.5072 0.3286 0.1967  0.0461  -0.0449 557 HOH   A O   
2401 O  O   . HOH   E .   ? 0.5199 0.2322 0.2666 -0.1062 -0.1307 0.0013  558 HOH   A O   
2402 O  O   . HOH   E .   ? 0.3058 0.2006 0.2960 0.0385  -0.0097 0.0586  559 HOH   A O   
2403 O  O   . HOH   E .   ? 0.3336 0.2442 0.2206 0.0753  -0.0142 0.0577  560 HOH   A O   
2404 O  O   . HOH   E .   ? 0.3110 0.2341 0.2620 -0.0061 -0.0427 -0.0782 561 HOH   A O   
2405 O  O   . HOH   E .   ? 0.4186 0.3486 0.3447 -0.0081 0.0135  -0.0062 562 HOH   A O   
2406 O  O   . HOH   E .   ? 0.2931 0.5544 0.4497 -0.0752 0.0094  0.0551  563 HOH   A O   
2407 O  O   . HOH   E .   ? 0.2113 0.2879 0.2172 -0.0192 -0.0469 0.0787  564 HOH   A O   
2408 O  O   A HOH   E .   ? 0.2506 0.2361 0.2505 0.0480  -0.0359 0.0458  565 HOH   A O   
2409 O  O   B HOH   E .   ? 0.3539 0.2465 0.2337 0.1184  -0.0187 0.0358  565 HOH   A O   
2410 O  O   A HOH   E .   ? 0.2516 0.2314 0.2419 -0.0207 -0.0690 -0.0041 566 HOH   A O   
2411 O  O   B HOH   E .   ? 0.2792 0.1745 0.2145 -0.0242 -0.0743 -0.0275 566 HOH   A O   
2412 O  O   . HOH   E .   ? 0.2751 0.2599 0.4470 0.0002  0.0510  -0.0217 567 HOH   A O   
2413 O  O   . HOH   E .   ? 0.5134 0.1981 0.3353 0.0897  0.0354  0.0857  568 HOH   A O   
2414 O  O   . HOH   E .   ? 0.4297 0.5171 0.2135 0.1129  -0.0377 0.0181  569 HOH   A O   
2415 O  O   . HOH   E .   ? 0.3779 0.2604 0.3394 0.0039  -0.0436 -0.0145 570 HOH   A O   
2416 O  O   . HOH   E .   ? 0.3025 0.2724 0.3167 0.0675  -0.0617 -0.0012 571 HOH   A O   
2417 O  O   . HOH   E .   ? 0.3705 0.3302 1.1179 -0.1260 0.2007  -0.0333 572 HOH   A O   
2418 O  O   . HOH   E .   ? 0.3085 0.3399 0.5243 -0.0136 0.0710  0.0635  573 HOH   A O   
2419 O  O   . HOH   E .   ? 0.2083 0.1263 0.1837 0.0218  -0.0139 0.0016  574 HOH   A O   
2420 O  O   . HOH   E .   ? 0.5954 0.7871 0.6035 -0.2605 0.0933  -0.2186 575 HOH   A O   
2421 O  O   . HOH   E .   ? 0.5290 0.3276 0.4941 0.1059  0.1719  0.1207  576 HOH   A O   
2422 O  O   . HOH   E .   ? 0.1980 0.1858 0.3722 -0.0138 -0.0029 0.0029  577 HOH   A O   
2423 O  O   . HOH   E .   ? 0.8314 0.5234 0.8991 0.3312  -0.3012 -0.1305 578 HOH   A O   
2424 O  O   . HOH   E .   ? 1.0067 0.5261 0.3170 0.3138  0.2196  0.1921  579 HOH   A O   
2425 O  O   . HOH   E .   ? 0.8483 0.3146 0.3670 0.2624  0.0391  0.0185  580 HOH   A O   
2426 O  O   . HOH   E .   ? 0.5681 0.3661 0.2995 -0.1112 0.0973  -0.0373 581 HOH   A O   
2427 O  O   . HOH   E .   ? 0.6749 0.3870 0.3255 0.2609  0.0815  -0.0400 582 HOH   A O   
2428 O  O   . HOH   E .   ? 0.3597 0.3327 0.7288 -0.0148 0.1084  -0.0182 583 HOH   A O   
2429 O  O   . HOH   E .   ? 0.5799 0.6063 0.2849 0.0903  0.0747  0.1996  584 HOH   A O   
2430 O  O   . HOH   E .   ? 0.4084 0.3212 0.4429 0.0867  0.0671  0.1179  585 HOH   A O   
2431 O  O   . HOH   E .   ? 0.3744 0.4410 0.8514 -0.0740 -0.0457 -0.0317 586 HOH   A O   
2432 O  O   . HOH   E .   ? 0.4103 0.1339 0.3339 0.0538  0.0070  -0.0069 587 HOH   A O   
2433 O  O   . HOH   E .   ? 0.3741 0.2283 0.2798 0.0666  0.0398  0.0495  588 HOH   A O   
2434 O  O   . HOH   E .   ? 0.7965 0.4938 0.2703 0.1849  -0.2516 -0.0133 589 HOH   A O   
2435 O  O   . HOH   E .   ? 0.4339 0.1981 0.3631 -0.0304 -0.0763 0.0411  590 HOH   A O   
2436 O  O   . HOH   E .   ? 0.2939 0.1810 0.9395 -0.0187 0.1460  0.0798  591 HOH   A O   
2437 O  O   . HOH   E .   ? 0.5740 0.5102 0.5908 -0.1412 -0.0713 0.1738  592 HOH   A O   
2438 O  O   . HOH   E .   ? 0.6643 0.9979 0.8815 -0.4984 0.2436  -0.5037 593 HOH   A O   
2439 O  O   . HOH   E .   ? 0.4968 0.4331 0.4942 -0.1509 -0.0458 0.0199  594 HOH   A O   
2440 O  O   . HOH   E .   ? 0.7225 0.3938 0.7828 -0.0111 -0.0070 0.0347  595 HOH   A O   
2441 O  O   . HOH   E .   ? 0.3545 0.2371 0.4470 0.0895  -0.0551 -0.0127 596 HOH   A O   
2442 O  O   . HOH   E .   ? 0.6378 0.2868 1.0775 0.0485  -0.3585 -0.1139 597 HOH   A O   
2443 O  O   . HOH   E .   ? 0.4605 0.2957 0.2402 0.1314  -0.0685 0.0040  598 HOH   A O   
2444 O  O   . HOH   E .   ? 0.6510 0.2136 0.3475 0.0379  -0.1029 -0.0158 599 HOH   A O   
2445 O  O   . HOH   E .   ? 0.5367 0.8328 0.3973 -0.3118 0.1700  -0.2816 600 HOH   A O   
2446 O  O   . HOH   E .   ? 0.5975 0.4213 0.3854 0.2164  0.1314  0.1280  601 HOH   A O   
2447 O  O   . HOH   E .   ? 0.4578 0.2919 0.3956 0.0234  -0.0332 0.0000  602 HOH   A O   
2448 O  O   . HOH   E .   ? 0.4797 0.4123 0.5253 0.1232  0.0198  0.1132  603 HOH   A O   
2449 O  O   . HOH   E .   ? 0.4983 1.0547 0.7425 0.3257  0.1287  0.4092  604 HOH   A O   
2450 O  O   . HOH   E .   ? 0.4492 0.8321 0.5518 0.3309  0.0646  0.1538  605 HOH   A O   
2451 O  O   . HOH   E .   ? 0.5608 0.3258 0.3443 0.0065  0.1231  0.1312  606 HOH   A O   
2452 O  O   . HOH   E .   ? 0.2534 0.2348 0.3200 -0.0075 -0.0476 0.0250  607 HOH   A O   
2453 O  O   . HOH   E .   ? 0.5258 0.4255 0.3970 0.1527  0.1824  0.2239  608 HOH   A O   
2454 O  O   . HOH   E .   ? 0.8887 0.1493 0.3123 0.1562  -0.0089 -0.0279 609 HOH   A O   
2455 O  O   . HOH   E .   ? 0.4589 0.3597 0.3350 -0.0548 -0.0639 -0.0397 610 HOH   A O   
2456 O  O   . HOH   E .   ? 0.3385 0.3555 0.5916 -0.0392 0.0159  -0.0110 611 HOH   A O   
2457 O  O   . HOH   E .   ? 0.5107 0.3322 0.8533 0.0681  0.0170  -0.1497 612 HOH   A O   
2458 O  O   . HOH   E .   ? 0.3140 0.3421 0.4982 -0.0087 -0.0574 -0.0080 613 HOH   A O   
2459 O  O   . HOH   E .   ? 0.5701 0.5359 0.9369 0.2796  0.3097  0.3701  614 HOH   A O   
2460 O  O   . HOH   E .   ? 0.2955 0.4193 0.4805 0.0864  0.0100  0.0642  615 HOH   A O   
2461 O  O   . HOH   E .   ? 0.5673 0.2652 0.9796 0.1229  -0.2093 -0.1815 616 HOH   A O   
2462 O  O   . HOH   E .   ? 0.4705 0.5579 0.7496 0.0425  0.0686  0.1377  617 HOH   A O   
2463 O  O   . HOH   E .   ? 0.2565 0.1731 0.9548 -0.0170 0.1582  -0.2570 618 HOH   A O   
2464 O  O   . HOH   E .   ? 0.5713 0.3931 0.3696 -0.0565 0.1225  -0.0225 619 HOH   A O   
2465 O  O   . HOH   E .   ? 0.8268 0.7027 0.2904 0.1993  0.0049  -0.1122 620 HOH   A O   
2466 O  O   . HOH   E .   ? 0.4360 0.3672 0.3790 0.0954  -0.1206 -0.1103 621 HOH   A O   
2467 O  O   . HOH   E .   ? 0.2901 0.1831 0.3126 -0.0141 -0.0449 -0.0147 622 HOH   A O   
2468 O  O   . HOH   E .   ? 0.6301 0.5213 0.9934 -0.0806 -0.0535 -0.0100 623 HOH   A O   
2469 O  O   . HOH   E .   ? 0.5191 0.5236 0.5251 -0.1246 -0.0789 -0.0724 624 HOH   A O   
2470 O  O   . HOH   E .   ? 0.7350 0.8474 0.4116 0.1186  0.0715  -0.2694 625 HOH   A O   
2471 O  O   . HOH   E .   ? 0.4095 0.6653 0.3945 -0.0156 -0.0790 -0.1577 626 HOH   A O   
2472 O  O   . HOH   E .   ? 0.4336 0.5729 0.3683 -0.0414 -0.0038 -0.0242 627 HOH   A O   
2473 O  O   . HOH   E .   ? 0.5890 0.4257 0.2749 -0.0657 0.0239  0.1332  628 HOH   A O   
2474 O  O   . HOH   E .   ? 0.8308 0.2353 0.5596 -0.0577 -0.1438 0.1239  629 HOH   A O   
2475 O  O   . HOH   E .   ? 0.4113 0.4340 0.3447 -0.0388 -0.0116 0.0289  630 HOH   A O   
2476 O  O   . HOH   E .   ? 1.0469 0.4269 0.4829 -0.3328 0.3649  -0.1932 631 HOH   A O   
2477 O  O   . HOH   E .   ? 0.8496 0.4305 0.4929 0.0410  0.0434  -0.0105 632 HOH   A O   
2478 O  O   . HOH   E .   ? 0.4958 0.4892 0.8506 0.0039  -0.0621 0.1224  633 HOH   A O   
2479 O  O   . HOH   E .   ? 0.2843 0.4085 0.9223 -0.0673 -0.2221 0.2189  634 HOH   A O   
2480 O  O   . HOH   E .   ? 0.4927 0.5156 0.4296 0.0548  -0.0091 0.1847  635 HOH   A O   
2481 O  O   . HOH   E .   ? 0.4485 0.4883 0.3448 0.1500  0.0779  0.1483  636 HOH   A O   
2482 O  O   . HOH   E .   ? 0.4373 0.4016 0.5231 0.1291  -0.0582 -0.1453 637 HOH   A O   
2483 O  O   . HOH   E .   ? 0.5075 0.3856 0.5977 -0.0339 0.2234  -0.1007 638 HOH   A O   
2484 O  O   . HOH   E .   ? 0.6596 0.2409 0.8032 0.0447  -0.1856 0.1079  639 HOH   A O   
2485 O  O   . HOH   E .   ? 0.4743 1.2277 0.7580 0.2563  0.0839  0.4643  640 HOH   A O   
2486 O  O   . HOH   E .   ? 0.3726 0.3925 0.3168 -0.1039 0.0147  0.0379  641 HOH   A O   
2487 O  O   . HOH   E .   ? 0.3134 0.6144 0.7684 0.0425  0.0438  0.1444  642 HOH   A O   
2488 O  O   . HOH   E .   ? 0.3140 1.0887 0.7445 -0.1098 -0.0864 0.2682  643 HOH   A O   
2489 O  O   . HOH   E .   ? 0.4959 0.2170 0.4628 0.0833  -0.2520 -0.0370 644 HOH   A O   
2490 O  O   . HOH   E .   ? 0.9177 0.5342 0.4882 0.1782  -0.1368 -0.0439 645 HOH   A O   
2491 O  O   . HOH   E .   ? 0.7221 0.6235 0.3787 -0.0020 -0.2332 -0.0712 646 HOH   A O   
2492 O  O   . HOH   E .   ? 0.7273 0.3153 1.1058 0.1611  0.4282  0.2487  647 HOH   A O   
2493 O  O   . HOH   E .   ? 0.7736 0.3266 0.5815 -0.1186 0.2638  -0.1010 648 HOH   A O   
2494 O  O   . HOH   E .   ? 0.3320 0.2860 0.9111 -0.0024 0.0299  0.1768  649 HOH   A O   
2495 O  O   . HOH   E .   ? 1.1883 0.9094 0.3695 0.4860  0.1351  0.1509  650 HOH   A O   
2496 O  O   . HOH   E .   ? 0.3786 0.4146 0.9353 -0.0480 -0.2244 -0.0376 651 HOH   A O   
2497 O  O   . HOH   E .   ? 0.3935 0.7707 0.3303 -0.0047 -0.0603 0.0285  652 HOH   A O   
2498 O  O   . HOH   E .   ? 0.4228 0.3111 0.3446 -0.0806 -0.1127 -0.0242 653 HOH   A O   
2499 O  O   . HOH   E .   ? 0.4341 0.4105 0.4907 0.1639  -0.0734 -0.0264 654 HOH   A O   
2500 O  O   . HOH   E .   ? 1.2467 0.4311 0.4639 0.2116  -0.1152 -0.2400 655 HOH   A O   
2501 O  O   . HOH   E .   ? 0.4156 0.5280 0.3853 -0.0304 0.0580  -0.0097 656 HOH   A O   
2502 O  O   . HOH   E .   ? 0.5349 0.2610 1.0634 0.1049  0.1340  0.0108  657 HOH   A O   
2503 O  O   . HOH   E .   ? 0.4530 0.4521 0.6394 -0.0726 0.0210  0.0471  658 HOH   A O   
2504 O  O   . HOH   E .   ? 0.3156 0.2799 0.2992 -0.0243 -0.0084 0.0319  659 HOH   A O   
2505 O  O   . HOH   E .   ? 0.9405 0.7251 0.3476 0.1407  -0.0729 0.0704  660 HOH   A O   
2506 O  O   . HOH   E .   ? 0.7702 0.3634 0.7255 -0.1196 -0.3495 -0.0258 661 HOH   A O   
2507 O  O   . HOH   E .   ? 0.4175 0.3302 0.3274 0.0083  0.0403  0.0836  662 HOH   A O   
2508 O  O   . HOH   E .   ? 0.3898 0.3511 0.6227 -0.0797 0.0109  -0.0682 663 HOH   A O   
2509 O  O   . HOH   E .   ? 0.4205 0.4018 0.6932 -0.1261 -0.0651 0.2438  664 HOH   A O   
2510 O  O   . HOH   E .   ? 0.6624 0.7673 0.3418 0.0097  0.0699  -0.1351 665 HOH   A O   
2511 O  O   . HOH   E .   ? 0.5705 0.4694 0.4684 -0.1699 -0.2353 0.1553  666 HOH   A O   
2512 O  O   . HOH   E .   ? 0.3860 0.7340 1.4042 -0.0857 0.1137  0.4899  667 HOH   A O   
2513 O  O   . HOH   E .   ? 0.4600 0.6820 1.5190 0.0167  -0.2174 0.7047  668 HOH   A O   
2514 O  O   . HOH   E .   ? 0.5400 0.4100 1.4418 -0.1641 -0.2141 0.3005  669 HOH   A O   
2515 O  O   . HOH   E .   ? 0.5140 0.5240 0.7048 -0.2007 0.0822  -0.1558 670 HOH   A O   
2516 O  O   . HOH   E .   ? 0.4897 0.5050 0.4497 -0.1354 -0.0137 0.0999  671 HOH   A O   
2517 O  O   . HOH   E .   ? 0.4895 0.4566 0.7454 -0.1333 0.1013  0.0512  672 HOH   A O   
2518 O  O   . HOH   E .   ? 0.6069 0.3287 0.3665 -0.0276 0.1350  -0.1234 673 HOH   A O   
2519 O  O   . HOH   E .   ? 0.4986 0.4528 0.4992 -0.0980 -0.0274 0.0697  674 HOH   A O   
2520 O  O   . HOH   E .   ? 0.5407 0.2980 1.1480 -0.0080 -0.4430 0.0773  675 HOH   A O   
2521 O  O   . HOH   E .   ? 0.3182 0.2172 0.2757 0.0336  -0.0556 0.0113  676 HOH   A O   
2522 O  O   . HOH   E .   ? 0.6547 0.3580 0.5148 0.1238  0.0289  0.1091  677 HOH   A O   
2523 O  O   . HOH   E .   ? 1.0788 0.4289 0.3345 -0.0043 -0.0144 0.0879  678 HOH   A O   
2524 O  O   . HOH   E .   ? 0.6318 0.6576 0.5146 0.0291  -0.0454 -0.2349 679 HOH   A O   
2525 O  O   . HOH   E .   ? 0.5417 0.4156 0.6664 0.1310  0.0336  0.0659  680 HOH   A O   
2526 O  O   . HOH   E .   ? 0.4065 0.7196 0.4725 0.0020  -0.1229 0.0022  681 HOH   A O   
2527 O  O   . HOH   E .   ? 0.8083 0.5394 0.4682 -0.0031 -0.1734 0.0980  682 HOH   A O   
2528 O  O   . HOH   E .   ? 0.3239 0.5603 0.8687 -0.1518 -0.1688 -0.0266 683 HOH   A O   
2529 O  O   . HOH   E .   ? 0.4507 0.1908 0.5255 -0.0380 0.1298  -0.0005 684 HOH   A O   
2530 O  O   . HOH   E .   ? 0.6556 0.4269 0.6513 -0.3010 -0.0445 0.1694  685 HOH   A O   
2531 O  O   . HOH   E .   ? 0.2707 0.8512 0.6344 -0.1150 0.0480  0.1851  686 HOH   A O   
2532 O  O   . HOH   E .   ? 0.7339 0.5881 0.4798 -0.1547 0.0873  -0.1613 687 HOH   A O   
2533 O  O   . HOH   E .   ? 0.8555 0.4718 0.3007 -0.1266 -0.0094 -0.1124 688 HOH   A O   
2534 O  O   . HOH   E .   ? 0.3449 0.4845 0.3862 -0.0412 0.0748  -0.0133 689 HOH   A O   
2535 O  O   . HOH   E .   ? 0.3287 0.4733 0.5843 -0.0309 -0.0753 -0.1074 690 HOH   A O   
2536 O  O   . HOH   E .   ? 0.7325 0.9193 0.6499 -0.0274 -0.3865 0.2777  691 HOH   A O   
# 
